data_7HEF
# 
_entry.id   7HEF 
# 
_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   7HEF         pdb_00007hef 10.2210/pdb7hef/pdb 
WWPDB D_1001407369 ?            ?                   
# 
_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                        7HEF 
_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 '(2S)-2-[(7H-pyrrolo[2,3-d]pyrimidin-4-yl)amino]-3-(1,3-thiazol-2-yl)propan-1-ol' 275.330   1   ? ? ? ? 
4 non-polymer syn 'CHLORIDE ION'                                                                    35.453    1   ? ? ? ? 
5 water       nat water                                                                             18.015    431 ? ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'nsp3, PL2-PRO, Papain-like protease, Papain-like proteinase, PL-PRO' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;SMVNSFSGYLKLTDNVYIKNADIVEEAKKVKPTVVVNAANVYLKHGGGVAGALNKATNNAMQVESDDYIATNGPLKVGGS
CVLSGHNLAKHCLHVVGPNVNKGEDIQLLKSAYENFNQHEVLLAPLLSAGIFGADPIHSLRVCVDTVRTNVYLAVFDKNL
YDKLVSSFL
;
_entity_poly.pdbx_seq_one_letter_code_can   
;SMVNSFSGYLKLTDNVYIKNADIVEEAKKVKPTVVVNAANVYLKHGGGVAGALNKATNNAMQVESDDYIATNGPLKVGGS
CVLSGHNLAKHCLHVVGPNVNKGEDIQLLKSAYENFNQHEVLLAPLLSAGIFGADPIHSLRVCVDTVRTNVYLAVFDKNL
YDKLVSSFL
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'trifluoroacetic acid'                                                            TFA   
3 '(2S)-2-[(7H-pyrrolo[2,3-d]pyrimidin-4-yl)amino]-3-(1,3-thiazol-2-yl)propan-1-ol' A1A9R 
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 
A1A9R non-polymer         . '(2S)-2-[(7H-pyrrolo[2,3-d]pyrimidin-4-yl)amino]-3-(1,3-thiazol-2-yl)propan-1-ol' ? 'C12 H13 N5 O S' 
275.330 
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 A1A9R 1   202 201  A1A9R LA1 A . 
E 4 CL    1   203 1    CL    CL  A . 
F 5 HOH   1   301 196  HOH   HOH A . 
F 5 HOH   2   302 292  HOH   HOH A . 
F 5 HOH   3   303 1289 HOH   HOH A . 
F 5 HOH   4   304 625  HOH   HOH A . 
F 5 HOH   5   305 109  HOH   HOH A . 
F 5 HOH   6   306 493  HOH   HOH A . 
F 5 HOH   7   307 209  HOH   HOH A . 
F 5 HOH   8   308 229  HOH   HOH A . 
F 5 HOH   9   309 1295 HOH   HOH A . 
F 5 HOH   10  310 20   HOH   HOH A . 
F 5 HOH   11  311 1301 HOH   HOH A . 
F 5 HOH   12  312 136  HOH   HOH A . 
F 5 HOH   13  313 18   HOH   HOH A . 
F 5 HOH   14  314 105  HOH   HOH A . 
F 5 HOH   15  315 148  HOH   HOH A . 
F 5 HOH   16  316 192  HOH   HOH A . 
F 5 HOH   17  317 76   HOH   HOH A . 
F 5 HOH   18  318 247  HOH   HOH A . 
F 5 HOH   19  319 409  HOH   HOH A . 
F 5 HOH   20  320 124  HOH   HOH A . 
F 5 HOH   21  321 17   HOH   HOH A . 
F 5 HOH   22  322 236  HOH   HOH A . 
F 5 HOH   23  323 337  HOH   HOH A . 
F 5 HOH   24  324 49   HOH   HOH A . 
F 5 HOH   25  325 195  HOH   HOH A . 
F 5 HOH   26  326 86   HOH   HOH A . 
F 5 HOH   27  327 661  HOH   HOH A . 
F 5 HOH   28  328 15   HOH   HOH A . 
F 5 HOH   29  329 153  HOH   HOH A . 
F 5 HOH   30  330 393  HOH   HOH A . 
F 5 HOH   31  331 1275 HOH   HOH A . 
F 5 HOH   32  332 15   HOH   HOH A . 
F 5 HOH   33  333 1    HOH   HOH A . 
F 5 HOH   34  334 155  HOH   HOH A . 
F 5 HOH   35  335 36   HOH   HOH A . 
F 5 HOH   36  336 281  HOH   HOH A . 
F 5 HOH   37  337 140  HOH   HOH A . 
F 5 HOH   38  338 8    HOH   HOH A . 
F 5 HOH   39  339 151  HOH   HOH A . 
F 5 HOH   40  340 241  HOH   HOH A . 
F 5 HOH   41  341 964  HOH   HOH A . 
F 5 HOH   42  342 164  HOH   HOH A . 
F 5 HOH   43  343 469  HOH   HOH A . 
F 5 HOH   44  344 57   HOH   HOH A . 
F 5 HOH   45  345 33   HOH   HOH A . 
F 5 HOH   46  346 320  HOH   HOH A . 
F 5 HOH   47  347 1290 HOH   HOH A . 
F 5 HOH   48  348 21   HOH   HOH A . 
F 5 HOH   49  349 630  HOH   HOH A . 
F 5 HOH   50  350 225  HOH   HOH A . 
F 5 HOH   51  351 1300 HOH   HOH A . 
F 5 HOH   52  352 42   HOH   HOH A . 
F 5 HOH   53  353 1283 HOH   HOH A . 
F 5 HOH   54  354 93   HOH   HOH A . 
F 5 HOH   55  355 39   HOH   HOH A . 
F 5 HOH   56  356 354  HOH   HOH A . 
F 5 HOH   57  357 74   HOH   HOH A . 
F 5 HOH   58  358 165  HOH   HOH A . 
F 5 HOH   59  359 102  HOH   HOH A . 
F 5 HOH   60  360 92   HOH   HOH A . 
F 5 HOH   61  361 22   HOH   HOH A . 
F 5 HOH   62  362 26   HOH   HOH A . 
F 5 HOH   63  363 169  HOH   HOH A . 
F 5 HOH   64  364 70   HOH   HOH A . 
F 5 HOH   65  365 939  HOH   HOH A . 
F 5 HOH   66  366 4    HOH   HOH A . 
F 5 HOH   67  367 278  HOH   HOH A . 
F 5 HOH   68  368 21   HOH   HOH A . 
F 5 HOH   69  369 66   HOH   HOH A . 
F 5 HOH   70  370 139  HOH   HOH A . 
F 5 HOH   71  371 7    HOH   HOH A . 
F 5 HOH   72  372 2    HOH   HOH A . 
F 5 HOH   73  373 5    HOH   HOH A . 
F 5 HOH   74  374 45   HOH   HOH A . 
F 5 HOH   75  375 17   HOH   HOH A . 
F 5 HOH   76  376 162  HOH   HOH A . 
F 5 HOH   77  377 19   HOH   HOH A . 
F 5 HOH   78  378 396  HOH   HOH A . 
F 5 HOH   79  379 81   HOH   HOH A . 
F 5 HOH   80  380 159  HOH   HOH A . 
F 5 HOH   81  381 138  HOH   HOH A . 
F 5 HOH   82  382 34   HOH   HOH A . 
F 5 HOH   83  383 186  HOH   HOH A . 
F 5 HOH   84  384 461  HOH   HOH A . 
F 5 HOH   85  385 296  HOH   HOH A . 
F 5 HOH   86  386 62   HOH   HOH A . 
F 5 HOH   87  387 56   HOH   HOH A . 
F 5 HOH   88  388 218  HOH   HOH A . 
F 5 HOH   89  389 46   HOH   HOH A . 
F 5 HOH   90  390 13   HOH   HOH A . 
F 5 HOH   91  391 96   HOH   HOH A . 
F 5 HOH   92  392 134  HOH   HOH A . 
F 5 HOH   93  393 366  HOH   HOH A . 
F 5 HOH   94  394 27   HOH   HOH A . 
F 5 HOH   95  395 24   HOH   HOH A . 
F 5 HOH   96  396 154  HOH   HOH A . 
F 5 HOH   97  397 140  HOH   HOH A . 
F 5 HOH   98  398 351  HOH   HOH A . 
F 5 HOH   99  399 35   HOH   HOH A . 
F 5 HOH   100 400 85   HOH   HOH A . 
F 5 HOH   101 401 67   HOH   HOH A . 
F 5 HOH   102 402 116  HOH   HOH A . 
F 5 HOH   103 403 58   HOH   HOH A . 
F 5 HOH   104 404 8    HOH   HOH A . 
F 5 HOH   105 405 1315 HOH   HOH A . 
F 5 HOH   106 406 115  HOH   HOH A . 
F 5 HOH   107 407 199  HOH   HOH A . 
F 5 HOH   108 408 1308 HOH   HOH A . 
F 5 HOH   109 409 83   HOH   HOH A . 
F 5 HOH   110 410 18   HOH   HOH A . 
F 5 HOH   111 411 12   HOH   HOH A . 
F 5 HOH   112 412 381  HOH   HOH A . 
F 5 HOH   113 413 1313 HOH   HOH A . 
F 5 HOH   114 414 1310 HOH   HOH A . 
F 5 HOH   115 415 25   HOH   HOH A . 
F 5 HOH   116 416 303  HOH   HOH A . 
F 5 HOH   117 417 121  HOH   HOH A . 
F 5 HOH   118 418 3    HOH   HOH A . 
F 5 HOH   119 419 11   HOH   HOH A . 
F 5 HOH   120 420 68   HOH   HOH A . 
F 5 HOH   121 421 125  HOH   HOH A . 
F 5 HOH   122 422 123  HOH   HOH A . 
F 5 HOH   123 423 1068 HOH   HOH A . 
F 5 HOH   124 424 6    HOH   HOH A . 
F 5 HOH   125 425 4    HOH   HOH A . 
F 5 HOH   126 426 662  HOH   HOH A . 
F 5 HOH   127 427 78   HOH   HOH A . 
F 5 HOH   128 428 333  HOH   HOH A . 
F 5 HOH   129 429 51   HOH   HOH A . 
F 5 HOH   130 430 582  HOH   HOH A . 
F 5 HOH   131 431 1094 HOH   HOH A . 
F 5 HOH   132 432 53   HOH   HOH A . 
F 5 HOH   133 433 7    HOH   HOH A . 
F 5 HOH   134 434 397  HOH   HOH A . 
F 5 HOH   135 435 122  HOH   HOH A . 
F 5 HOH   136 436 156  HOH   HOH A . 
F 5 HOH   137 437 1279 HOH   HOH A . 
F 5 HOH   138 438 212  HOH   HOH A . 
F 5 HOH   139 439 95   HOH   HOH A . 
F 5 HOH   140 440 19   HOH   HOH A . 
F 5 HOH   141 441 1222 HOH   HOH A . 
F 5 HOH   142 442 405  HOH   HOH A . 
F 5 HOH   143 443 132  HOH   HOH A . 
F 5 HOH   144 444 6    HOH   HOH A . 
F 5 HOH   145 445 1296 HOH   HOH A . 
F 5 HOH   146 446 71   HOH   HOH A . 
F 5 HOH   147 447 40   HOH   HOH A . 
F 5 HOH   148 448 73   HOH   HOH A . 
F 5 HOH   149 449 80   HOH   HOH A . 
F 5 HOH   150 450 1286 HOH   HOH A . 
F 5 HOH   151 451 188  HOH   HOH A . 
F 5 HOH   152 452 1238 HOH   HOH A . 
F 5 HOH   153 453 94   HOH   HOH A . 
F 5 HOH   154 454 1309 HOH   HOH A . 
F 5 HOH   155 455 944  HOH   HOH A . 
F 5 HOH   156 456 16   HOH   HOH A . 
F 5 HOH   157 457 97   HOH   HOH A . 
F 5 HOH   158 458 952  HOH   HOH A . 
F 5 HOH   159 459 104  HOH   HOH A . 
F 5 HOH   160 460 79   HOH   HOH A . 
F 5 HOH   161 461 1189 HOH   HOH A . 
F 5 HOH   162 462 330  HOH   HOH A . 
F 5 HOH   163 463 576  HOH   HOH A . 
F 5 HOH   164 464 16   HOH   HOH A . 
F 5 HOH   165 465 1119 HOH   HOH A . 
F 5 HOH   166 466 107  HOH   HOH A . 
F 5 HOH   167 467 509  HOH   HOH A . 
F 5 HOH   168 468 1134 HOH   HOH A . 
F 5 HOH   169 469 726  HOH   HOH A . 
F 5 HOH   170 470 163  HOH   HOH A . 
F 5 HOH   171 471 408  HOH   HOH A . 
F 5 HOH   172 472 756  HOH   HOH A . 
F 5 HOH   173 473 1276 HOH   HOH A . 
F 5 HOH   174 474 14   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 63   HOH   HOH A . 
F 5 HOH   178 478 319  HOH   HOH A . 
F 5 HOH   179 479 280  HOH   HOH A . 
F 5 HOH   180 480 361  HOH   HOH A . 
F 5 HOH   181 481 370  HOH   HOH A . 
F 5 HOH   182 482 801  HOH   HOH A . 
F 5 HOH   183 483 342  HOH   HOH A . 
F 5 HOH   184 484 1307 HOH   HOH A . 
F 5 HOH   185 485 250  HOH   HOH A . 
F 5 HOH   186 486 23   HOH   HOH A . 
F 5 HOH   187 487 224  HOH   HOH A . 
F 5 HOH   188 488 267  HOH   HOH A . 
F 5 HOH   189 489 1306 HOH   HOH A . 
F 5 HOH   190 490 1287 HOH   HOH A . 
F 5 HOH   191 491 135  HOH   HOH A . 
F 5 HOH   192 492 695  HOH   HOH A . 
F 5 HOH   193 493 919  HOH   HOH A . 
F 5 HOH   194 494 674  HOH   HOH A . 
F 5 HOH   195 495 202  HOH   HOH A . 
F 5 HOH   196 496 9    HOH   HOH A . 
F 5 HOH   197 497 1299 HOH   HOH A . 
F 5 HOH   198 498 711  HOH   HOH A . 
F 5 HOH   199 499 521  HOH   HOH A . 
F 5 HOH   200 500 326  HOH   HOH A . 
F 5 HOH   201 501 309  HOH   HOH A . 
F 5 HOH   202 502 3    HOH   HOH A . 
F 5 HOH   203 503 331  HOH   HOH A . 
F 5 HOH   204 504 318  HOH   HOH A . 
F 5 HOH   205 505 1314 HOH   HOH A . 
F 5 HOH   206 506 315  HOH   HOH A . 
F 5 HOH   207 507 805  HOH   HOH A . 
F 5 HOH   208 508 263  HOH   HOH A . 
F 5 HOH   209 509 941  HOH   HOH A . 
F 5 HOH   210 510 152  HOH   HOH A . 
F 5 HOH   211 511 10   HOH   HOH A . 
F 5 HOH   212 512 208  HOH   HOH A . 
F 5 HOH   213 513 356  HOH   HOH A . 
F 5 HOH   214 514 1284 HOH   HOH A . 
F 5 HOH   215 515 1071 HOH   HOH A . 
F 5 HOH   216 516 180  HOH   HOH A . 
F 5 HOH   217 517 350  HOH   HOH A . 
F 5 HOH   218 518 363  HOH   HOH A . 
F 5 HOH   219 519 2    HOH   HOH A . 
F 5 HOH   220 520 371  HOH   HOH A . 
F 5 HOH   221 521 313  HOH   HOH A . 
F 5 HOH   222 522 185  HOH   HOH A . 
F 5 HOH   223 523 429  HOH   HOH A . 
F 5 HOH   224 524 772  HOH   HOH A . 
F 5 HOH   225 525 70   HOH   HOH A . 
F 5 HOH   226 526 376  HOH   HOH A . 
F 5 HOH   227 527 1074 HOH   HOH A . 
F 5 HOH   228 528 1292 HOH   HOH A . 
F 5 HOH   229 529 346  HOH   HOH A . 
F 5 HOH   230 530 12   HOH   HOH A . 
F 5 HOH   231 531 1078 HOH   HOH A . 
G 5 HOH   1   201 64   HOH   HOH B . 
G 5 HOH   2   202 549  HOH   HOH B . 
G 5 HOH   3   203 531  HOH   HOH B . 
G 5 HOH   4   204 364  HOH   HOH B . 
G 5 HOH   5   205 900  HOH   HOH B . 
G 5 HOH   6   206 398  HOH   HOH B . 
G 5 HOH   7   207 240  HOH   HOH B . 
G 5 HOH   8   208 358  HOH   HOH B . 
G 5 HOH   9   209 353  HOH   HOH B . 
G 5 HOH   10  210 232  HOH   HOH B . 
G 5 HOH   11  211 50   HOH   HOH B . 
G 5 HOH   12  212 343  HOH   HOH B . 
G 5 HOH   13  213 654  HOH   HOH B . 
G 5 HOH   14  214 444  HOH   HOH B . 
G 5 HOH   15  215 1249 HOH   HOH B . 
G 5 HOH   16  216 758  HOH   HOH B . 
G 5 HOH   17  217 120  HOH   HOH B . 
G 5 HOH   18  218 264  HOH   HOH B . 
G 5 HOH   19  219 131  HOH   HOH B . 
G 5 HOH   20  220 452  HOH   HOH B . 
G 5 HOH   21  221 743  HOH   HOH B . 
G 5 HOH   22  222 1140 HOH   HOH B . 
G 5 HOH   23  223 205  HOH   HOH B . 
G 5 HOH   24  224 332  HOH   HOH B . 
G 5 HOH   25  225 1312 HOH   HOH B . 
G 5 HOH   26  226 282  HOH   HOH B . 
G 5 HOH   27  227 172  HOH   HOH B . 
G 5 HOH   28  228 75   HOH   HOH B . 
G 5 HOH   29  229 82   HOH   HOH B . 
G 5 HOH   30  230 54   HOH   HOH B . 
G 5 HOH   31  231 1278 HOH   HOH B . 
G 5 HOH   32  232 60   HOH   HOH B . 
G 5 HOH   33  233 166  HOH   HOH B . 
G 5 HOH   34  234 276  HOH   HOH B . 
G 5 HOH   35  235 69   HOH   HOH B . 
G 5 HOH   36  236 723  HOH   HOH B . 
G 5 HOH   37  237 272  HOH   HOH B . 
G 5 HOH   38  238 128  HOH   HOH B . 
G 5 HOH   39  239 133  HOH   HOH B . 
G 5 HOH   40  240 1    HOH   HOH B . 
G 5 HOH   41  241 300  HOH   HOH B . 
G 5 HOH   42  242 127  HOH   HOH B . 
G 5 HOH   43  243 325  HOH   HOH B . 
G 5 HOH   44  244 181  HOH   HOH B . 
G 5 HOH   45  245 14   HOH   HOH B . 
G 5 HOH   46  246 110  HOH   HOH B . 
G 5 HOH   47  247 129  HOH   HOH B . 
G 5 HOH   48  248 143  HOH   HOH B . 
G 5 HOH   49  249 9    HOH   HOH B . 
G 5 HOH   50  250 30   HOH   HOH B . 
G 5 HOH   51  251 144  HOH   HOH B . 
G 5 HOH   52  252 347  HOH   HOH B . 
G 5 HOH   53  253 52   HOH   HOH B . 
G 5 HOH   54  254 72   HOH   HOH B . 
G 5 HOH   55  255 231  HOH   HOH B . 
G 5 HOH   56  256 391  HOH   HOH B . 
G 5 HOH   57  257 41   HOH   HOH B . 
G 5 HOH   58  258 103  HOH   HOH B . 
G 5 HOH   59  259 150  HOH   HOH B . 
G 5 HOH   60  260 31   HOH   HOH B . 
G 5 HOH   61  261 252  HOH   HOH B . 
G 5 HOH   62  262 47   HOH   HOH B . 
G 5 HOH   63  263 271  HOH   HOH B . 
G 5 HOH   64  264 10   HOH   HOH B . 
G 5 HOH   65  265 59   HOH   HOH B . 
G 5 HOH   66  266 1277 HOH   HOH B . 
G 5 HOH   67  267 11   HOH   HOH B . 
G 5 HOH   68  268 243  HOH   HOH B . 
G 5 HOH   69  269 242  HOH   HOH B . 
G 5 HOH   70  270 77   HOH   HOH B . 
G 5 HOH   71  271 61   HOH   HOH B . 
G 5 HOH   72  272 20   HOH   HOH B . 
G 5 HOH   73  273 84   HOH   HOH B . 
G 5 HOH   74  274 117  HOH   HOH B . 
G 5 HOH   75  275 235  HOH   HOH B . 
G 5 HOH   76  276 287  HOH   HOH B . 
G 5 HOH   77  277 43   HOH   HOH B . 
G 5 HOH   78  278 216  HOH   HOH B . 
G 5 HOH   79  279 147  HOH   HOH B . 
G 5 HOH   80  280 302  HOH   HOH B . 
G 5 HOH   81  281 175  HOH   HOH B . 
G 5 HOH   82  282 416  HOH   HOH B . 
G 5 HOH   83  283 114  HOH   HOH B . 
G 5 HOH   84  284 1305 HOH   HOH B . 
G 5 HOH   85  285 221  HOH   HOH B . 
G 5 HOH   86  286 1106 HOH   HOH B . 
G 5 HOH   87  287 22   HOH   HOH B . 
G 5 HOH   88  288 13   HOH   HOH B . 
G 5 HOH   89  289 106  HOH   HOH B . 
G 5 HOH   90  290 89   HOH   HOH B . 
G 5 HOH   91  291 137  HOH   HOH B . 
G 5 HOH   92  292 387  HOH   HOH B . 
G 5 HOH   93  293 88   HOH   HOH B . 
G 5 HOH   94  294 99   HOH   HOH B . 
G 5 HOH   95  295 1066 HOH   HOH B . 
G 5 HOH   96  296 311  HOH   HOH B . 
G 5 HOH   97  297 1285 HOH   HOH B . 
G 5 HOH   98  298 112  HOH   HOH B . 
G 5 HOH   99  299 299  HOH   HOH B . 
G 5 HOH   100 300 142  HOH   HOH B . 
G 5 HOH   101 301 141  HOH   HOH B . 
G 5 HOH   102 302 32   HOH   HOH B . 
G 5 HOH   103 303 220  HOH   HOH B . 
G 5 HOH   104 304 297  HOH   HOH B . 
G 5 HOH   105 305 316  HOH   HOH B . 
G 5 HOH   106 306 215  HOH   HOH B . 
G 5 HOH   107 307 118  HOH   HOH B . 
G 5 HOH   108 308 38   HOH   HOH B . 
G 5 HOH   109 309 101  HOH   HOH B . 
G 5 HOH   110 310 160  HOH   HOH B . 
G 5 HOH   111 311 635  HOH   HOH B . 
G 5 HOH   112 312 48   HOH   HOH B . 
G 5 HOH   113 313 197  HOH   HOH B . 
G 5 HOH   114 314 170  HOH   HOH B . 
G 5 HOH   115 315 177  HOH   HOH B . 
G 5 HOH   116 316 37   HOH   HOH B . 
G 5 HOH   117 317 1274 HOH   HOH B . 
G 5 HOH   118 318 91   HOH   HOH B . 
G 5 HOH   119 319 28   HOH   HOH B . 
G 5 HOH   120 320 161  HOH   HOH B . 
G 5 HOH   121 321 23   HOH   HOH B . 
G 5 HOH   122 322 44   HOH   HOH B . 
G 5 HOH   123 323 341  HOH   HOH B . 
G 5 HOH   124 324 1291 HOH   HOH B . 
G 5 HOH   125 325 100  HOH   HOH B . 
G 5 HOH   126 326 704  HOH   HOH B . 
G 5 HOH   127 327 29   HOH   HOH B . 
G 5 HOH   128 328 445  HOH   HOH B . 
G 5 HOH   129 329 55   HOH   HOH B . 
G 5 HOH   130 330 1294 HOH   HOH B . 
G 5 HOH   131 331 334  HOH   HOH B . 
G 5 HOH   132 332 182  HOH   HOH B . 
G 5 HOH   133 333 98   HOH   HOH B . 
G 5 HOH   134 334 1126 HOH   HOH B . 
G 5 HOH   135 335 234  HOH   HOH B . 
G 5 HOH   136 336 717  HOH   HOH B . 
G 5 HOH   137 337 207  HOH   HOH B . 
G 5 HOH   138 338 1293 HOH   HOH B . 
G 5 HOH   139 339 65   HOH   HOH B . 
G 5 HOH   140 340 619  HOH   HOH B . 
G 5 HOH   141 341 339  HOH   HOH B . 
G 5 HOH   142 342 960  HOH   HOH B . 
G 5 HOH   143 343 362  HOH   HOH B . 
G 5 HOH   144 344 178  HOH   HOH B . 
G 5 HOH   145 345 90   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   149 349 623  HOH   HOH B . 
G 5 HOH   150 350 335  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   154 354 304  HOH   HOH B . 
G 5 HOH   155 355 290  HOH   HOH B . 
G 5 HOH   156 356 541  HOH   HOH B . 
G 5 HOH   157 357 203  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   164 364 373  HOH   HOH B . 
G 5 HOH   165 365 898  HOH   HOH B . 
G 5 HOH   166 366 1316 HOH   HOH B . 
G 5 HOH   167 367 615  HOH   HOH B . 
G 5 HOH   168 368 667  HOH   HOH B . 
G 5 HOH   169 369 340  HOH   HOH B . 
G 5 HOH   170 370 291  HOH   HOH B . 
G 5 HOH   171 371 1303 HOH   HOH B . 
G 5 HOH   172 372 190  HOH   HOH B . 
G 5 HOH   173 373 431  HOH   HOH B . 
G 5 HOH   174 374 310  HOH   HOH B . 
G 5 HOH   175 375 1173 HOH   HOH B . 
G 5 HOH   176 376 149  HOH   HOH B . 
G 5 HOH   177 377 183  HOH   HOH B . 
G 5 HOH   178 378 1000 HOH   HOH B . 
G 5 HOH   179 379 1163 HOH   HOH B . 
G 5 HOH   180 380 418  HOH   HOH B . 
G 5 HOH   181 381 176  HOH   HOH B . 
G 5 HOH   182 382 1311 HOH   HOH B . 
G 5 HOH   183 383 424  HOH   HOH B . 
G 5 HOH   184 384 491  HOH   HOH B . 
G 5 HOH   185 385 981  HOH   HOH B . 
G 5 HOH   186 386 1298 HOH   HOH B . 
G 5 HOH   187 387 470  HOH   HOH B . 
G 5 HOH   188 388 248  HOH   HOH B . 
G 5 HOH   189 389 265  HOH   HOH B . 
G 5 HOH   190 390 184  HOH   HOH B . 
G 5 HOH   191 391 360  HOH   HOH B . 
G 5 HOH   192 392 410  HOH   HOH B . 
G 5 HOH   193 393 355  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   198 398 321  HOH   HOH B . 
G 5 HOH   199 399 792  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           7HEF 
_cell.length_a           88.749 
_cell.length_b           88.749 
_cell.length_c           39.456 
_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                         7HEF 
_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          7HEF 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_Matthews      2.14 
_exptl_crystal.density_percent_sol   42.55 
_exptl_crystal.density_meas          ? 
_exptl_crystal.description           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.pH              9.5 
_exptl_crystal_grow.temp            292 
_exptl_crystal_grow.pdbx_details    '100 mM CHES, 28% PEG 3000' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp_details    ? 
# 
_diffrn.id                     1 
_diffrn.crystal_id             1 
_diffrn.ambient_temp           100 
_diffrn.ambient_temp_details   ? 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               PIXEL 
_diffrn_detector.type                   'DECTRIS PILATUS3 6M' 
_diffrn_detector.pdbx_collection_date   2023-05-24 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.pdbx_scattering_type             x-ray 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.monochromator                    ? 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.88557 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'ALS BEAMLINE 8.3.1' 
_diffrn_source.pdbx_wavelength_list        0.88557 
_diffrn_source.pdbx_synchrotron_site       ALS 
_diffrn_source.pdbx_synchrotron_beamline   8.3.1 
_diffrn_source.pdbx_wavelength             ? 
# 
_reflns.entry_id                     7HEF 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             44.370 
_reflns.d_resolution_high            1.000 
_reflns.number_obs                   165059 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         99.600 
_reflns.pdbx_Rmerge_I_obs            0.045 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        15.000 
_reflns.B_iso_Wilson_estimate        11.560 
_reflns.pdbx_redundancy              6.400 
_reflns.pdbx_Rrim_I_all              0.049 
_reflns.pdbx_Rpim_I_all              0.019 
_reflns.pdbx_CC_half                 0.999 
_reflns.pdbx_netI_over_av_sigmaI     ? 
_reflns.pdbx_number_measured_all     1049611 
_reflns.pdbx_scaling_rejects         ? 
_reflns.pdbx_chi_squared             ? 
_reflns.Rmerge_F_all                 ? 
_reflns.Rmerge_F_obs                 ? 
_reflns.observed_criterion_F_max     ? 
_reflns.observed_criterion_F_min     ? 
_reflns.observed_criterion_I_max     ? 
_reflns.observed_criterion_I_min     ? 
_reflns.pdbx_d_res_high_opt          ? 
_reflns.pdbx_d_res_low_opt           ? 
_reflns.details                      ? 
# 
loop_
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_ordinal 
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.number_measured_obs 
_reflns_shell.number_measured_all 
_reflns_shell.number_unique_obs 
_reflns_shell.pdbx_rejects 
_reflns_shell.Rmerge_I_obs 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.pdbx_Rsym_value 
_reflns_shell.pdbx_chi_squared 
_reflns_shell.pdbx_redundancy 
_reflns_shell.percent_possible_obs 
_reflns_shell.pdbx_netI_over_sigmaI_obs 
_reflns_shell.number_possible 
_reflns_shell.number_unique_all 
_reflns_shell.Rmerge_F_all 
_reflns_shell.Rmerge_F_obs 
_reflns_shell.Rmerge_I_all 
_reflns_shell.meanI_over_sigI_all 
_reflns_shell.percent_possible_all 
_reflns_shell.pdbx_Rrim_I_all 
_reflns_shell.pdbx_Rpim_I_all 
_reflns_shell.pdbx_CC_half 
1 1 1.000 1.020  ? 33896 7628 ? 1.019 ? ? ? 4.400 ? 1.000  ? ? ? ? ? ? 93.200 1.155 0.532 0.670 
1 2 5.480 44.370 ? 7497  1090 ? 0.025 ? ? ? 6.900 ? 51.600 ? ? ? ? ? ? 99.700 0.027 0.010 0.999 
# 
_refine.entry_id                                 7HEF 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_d_res_high                            1.0000 
_refine.ls_d_res_low                             39.6900 
_refine.pdbx_ls_sigma_F                          1.350 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.ls_percent_reflns_obs                    99.5500 
_refine.ls_number_reflns_obs                     164994 
_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                          0.1416 
_refine.ls_R_factor_R_work                       0.1410 
_refine.ls_wR_factor_R_work                      ? 
_refine.ls_R_factor_R_free                       0.1534 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_percent_reflns_R_free                 4.8200 
_refine.ls_number_reflns_R_free                  7959 
_refine.ls_number_reflns_R_work                  157035 
_refine.ls_R_factor_R_free_error                 ? 
_refine.B_iso_mean                               17.9380 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.overall_SU_R_free                        ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.overall_SU_ML                            0.1000 
_refine.overall_SU_B                             ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.pdbx_solvent_vdw_probe_radii             1.1000 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.B_iso_max                                68.250 
_refine.B_iso_min                                7.360 
_refine.pdbx_overall_phase_error                 16.3800 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_R_factor_R_free_error_details         ? 
# 
_refine_hist.cycle_id                         final 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.d_res_high                       1.0000 
_refine_hist.d_res_low                        39.6900 
_refine_hist.pdbx_number_atoms_ligand         40 
_refine_hist.number_atoms_solvent             431 
_refine_hist.number_atoms_total               3013 
_refine_hist.pdbx_number_residues_total       336 
_refine_hist.pdbx_B_iso_mean_ligand           12.53 
_refine_hist.pdbx_B_iso_mean_solvent          29.83 
_refine_hist.pdbx_number_atoms_protein        2542 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
# 
loop_
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.R_factor_R_free 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.pdbx_refine_id 
1.0000 1.0100  30 92.0000  4845 . 0.3905 0.3593 . 260 0.0000 5105 . 'X-RAY DIFFRACTION' 
1.0100 1.0200  30 96.0000  5015 . 0.3240 0.3386 . 208 0.0000 5223 . 'X-RAY DIFFRACTION' 
1.0200 1.0400  30 100.0000 5250 . 0.2732 0.2835 . 266 0.0000 5516 . 'X-RAY DIFFRACTION' 
1.0400 1.0500  30 100.0000 5174 . 0.2269 0.2190 . 271 0.0000 5445 . 'X-RAY DIFFRACTION' 
1.0500 1.0600  30 100.0000 5201 . 0.1986 0.2207 . 329 0.0000 5530 . 'X-RAY DIFFRACTION' 
1.0600 1.0800  30 100.0000 5224 . 0.1776 0.1889 . 246 0.0000 5470 . 'X-RAY DIFFRACTION' 
1.0800 1.0900  30 100.0000 5247 . 0.1633 0.1766 . 265 0.0000 5512 . 'X-RAY DIFFRACTION' 
1.0900 1.1100  30 100.0000 5234 . 0.1512 0.1605 . 242 0.0000 5476 . 'X-RAY DIFFRACTION' 
1.1100 1.1300  30 100.0000 5241 . 0.1480 0.1620 . 282 0.0000 5523 . 'X-RAY DIFFRACTION' 
1.1300 1.1400  30 100.0000 5210 . 0.1404 0.1680 . 248 0.0000 5458 . 'X-RAY DIFFRACTION' 
1.1400 1.1600  30 100.0000 5261 . 0.1344 0.1558 . 262 0.0000 5523 . 'X-RAY DIFFRACTION' 
1.1600 1.1900  30 100.0000 5257 . 0.1331 0.1651 . 269 0.0000 5526 . 'X-RAY DIFFRACTION' 
1.1900 1.2100  30 100.0000 5143 . 0.1271 0.1602 . 279 0.0000 5422 . 'X-RAY DIFFRACTION' 
1.2100 1.2300  30 100.0000 5362 . 0.1245 0.1511 . 232 0.0000 5594 . 'X-RAY DIFFRACTION' 
1.2300 1.2600  30 100.0000 5179 . 0.1250 0.1400 . 259 0.0000 5438 . 'X-RAY DIFFRACTION' 
1.2600 1.2900  30 100.0000 5262 . 0.1203 0.1415 . 280 0.0000 5542 . 'X-RAY DIFFRACTION' 
1.2900 1.3200  30 100.0000 5214 . 0.1167 0.1305 . 279 0.0000 5493 . 'X-RAY DIFFRACTION' 
1.3200 1.3600  30 100.0000 5229 . 0.1179 0.1375 . 282 0.0000 5511 . 'X-RAY DIFFRACTION' 
1.3600 1.4000  30 100.0000 5277 . 0.1158 0.1441 . 247 0.0000 5524 . 'X-RAY DIFFRACTION' 
1.4000 1.4400  30 100.0000 5228 . 0.1189 0.1305 . 271 0.0000 5499 . 'X-RAY DIFFRACTION' 
1.4400 1.4900  30 100.0000 5286 . 0.1244 0.1309 . 243 0.0000 5529 . 'X-RAY DIFFRACTION' 
1.4900 1.5500  30 100.0000 5230 . 0.1174 0.1291 . 281 0.0000 5511 . 'X-RAY DIFFRACTION' 
1.5500 1.6200  30 100.0000 5286 . 0.1158 0.1322 . 266 0.0000 5552 . 'X-RAY DIFFRACTION' 
1.6200 1.7100  30 100.0000 5268 . 0.1223 0.1397 . 259 0.0000 5527 . 'X-RAY DIFFRACTION' 
1.7100 1.8200  30 100.0000 5290 . 0.1299 0.1394 . 249 0.0000 5539 . 'X-RAY DIFFRACTION' 
1.8200 1.9600  30 100.0000 5266 . 0.1313 0.1287 . 281 0.0000 5547 . 'X-RAY DIFFRACTION' 
1.9600 2.1500  30 100.0000 5271 . 0.1381 0.1376 . 291 0.0000 5562 . 'X-RAY DIFFRACTION' 
2.1500 2.4700  30 100.0000 5289 . 0.1351 0.1439 . 289 0.0000 5578 . 'X-RAY DIFFRACTION' 
2.4700 3.1100  30 100.0000 5324 . 0.1488 0.1657 . 256 0.0000 5580 . 'X-RAY DIFFRACTION' 
3.1100 39.6900 30 100.0000 5472 . 0.1491 0.1656 . 267 0.0000 5739 . 'X-RAY DIFFRACTION' 
# 
_struct.entry_id                  7HEF 
_struct.title                     
'PanDDA analysis group deposition -- Crystal structure of SARS-CoV-2 NSP3 macrodomain in complex with AVI-0003673' 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_details        ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HEF 
_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 7HEF A 3 ? 169 ? P0DTD1 1025 ? 1191 ? 3 169 
2 1 7HEF 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 7HEF SER A 1 ? UNP P0DTD1 ? ? 'expression tag' 1 1 
1 7HEF MET A 2 ? UNP P0DTD1 ? ? 'expression tag' 2 2 
2 7HEF SER B 1 ? UNP P0DTD1 ? ? 'expression tag' 1 3 
2 7HEF 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 ? PHE A 168 ? ASP A 157 PHE A 168 1 ? 12 
HELX_P HELX_P10 AB1 ASP B 22  ? LYS B 31  ? ASP B 22  LYS B 31  1 ? 10 
HELX_P HELX_P11 AB2 GLY B 47  ? THR B 57  ? GLY B 47  THR B 57  1 ? 11 
HELX_P HELX_P12 AB3 ASN B 59  ? GLY B 73  ? ASN B 59  GLY B 73  1 ? 15 
HELX_P HELX_P13 AB4 ASN B 99  ? GLY B 103 ? ASN B 99  GLY B 103 5 ? 5  
HELX_P HELX_P14 AB5 ASP B 105 ? GLN B 107 ? ASP B 105 GLN B 107 5 ? 3  
HELX_P HELX_P15 AB6 LEU B 108 ? ASN B 115 ? LEU B 108 ASN B 115 1 ? 8  
HELX_P HELX_P16 AB7 PHE B 116 ? HIS B 119 ? PHE B 116 HIS B 119 5 ? 4  
HELX_P HELX_P17 AB8 ALA B 129 ? GLY B 133 ? ALA B 129 GLY B 133 5 ? 5  
HELX_P HELX_P18 AB9 ASP B 135 ? VAL B 147 ? ASP B 135 VAL B 147 1 ? 13 
HELX_P HELX_P19 AC1 ASP B 157 ? LEU B 169 ? ASP B 157 LEU B 169 1 ? 13 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 4 ? 
AA2 ? 3 ? 
AA3 ? 4 ? 
AA4 ? 3 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? parallel      
AA1 3 4 ? parallel      
AA2 1 2 ? parallel      
AA2 2 3 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? parallel      
AA3 3 4 ? parallel      
AA4 1 2 ? parallel      
AA4 2 3 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 LEU A 10  ? LYS A 11  ? LEU A 10  LYS A 11  
AA1 2 VAL A 16  ? ASN A 20  ? VAL A 16  ASN A 20  
AA1 3 ASN A 150 ? VAL A 155 ? ASN A 150 VAL A 155 
AA1 4 VAL A 121 ? ALA A 124 ? VAL A 121 ALA A 124 
AA2 1 VAL A 34  ? ALA A 38  ? VAL A 34  ALA A 38  
AA2 2 HIS A 91  ? VAL A 95  ? HIS A 91  VAL A 95  
AA2 3 SER A 80  ? SER A 84  ? SER A 80  SER A 84  
AA3 1 LEU B 10  ? LYS B 11  ? LEU B 10  LYS B 11  
AA3 2 VAL B 16  ? ASN B 20  ? VAL B 16  ASN B 20  
AA3 3 ASN B 150 ? VAL B 155 ? ASN B 150 VAL B 155 
AA3 4 VAL B 121 ? ALA B 124 ? VAL B 121 ALA B 124 
AA4 1 VAL B 34  ? ALA B 38  ? VAL B 34  ALA B 38  
AA4 2 HIS B 91  ? VAL B 95  ? HIS B 91  VAL B 95  
AA4 3 SER B 80  ? SER B 84  ? SER B 80  SER B 84  
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N LEU A 10  ? N LEU A 10  O ILE A 18  ? O ILE A 18  
AA1 2 3 N TYR A 17  ? N TYR A 17  O LEU A 153 ? O LEU A 153 
AA1 3 4 O TYR A 152 ? O TYR A 152 N LEU A 122 ? N LEU A 122 
AA2 1 2 N ASN A 37  ? N ASN A 37  O VAL A 95  ? O VAL A 95  
AA2 2 3 O CYS A 92  ? O CYS A 92  N LEU A 83  ? N LEU A 83  
AA3 1 2 N LEU B 10  ? N LEU B 10  O ILE B 18  ? O ILE B 18  
AA3 2 3 N TYR B 17  ? N TYR B 17  O LEU B 153 ? O LEU B 153 
AA3 3 4 O TYR B 152 ? O TYR B 152 N LEU B 122 ? N LEU B 122 
AA4 1 2 N ASN B 37  ? N ASN B 37  O LEU B 93  ? O LEU B 93  
AA4 2 3 O HIS B 94  ? O HIS B 94  N CYS B 81  ? N CYS B 81  
# 
_pdbx_entry_details.entry_id                   7HEF 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
_pdbx_validate_close_contact.id               1 
_pdbx_validate_close_contact.PDB_model_num    1 
_pdbx_validate_close_contact.auth_atom_id_1   O 
_pdbx_validate_close_contact.auth_asym_id_1   A 
_pdbx_validate_close_contact.auth_comp_id_1   HOH 
_pdbx_validate_close_contact.auth_seq_id_1    344 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   ? 
_pdbx_validate_close_contact.auth_atom_id_2   O 
_pdbx_validate_close_contact.auth_asym_id_2   A 
_pdbx_validate_close_contact.auth_comp_id_2   HOH 
_pdbx_validate_close_contact.auth_seq_id_2    426 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             2.14 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 HIS A 86  ? ? 55.40 -133.14 
2 1 SER A 128 ? B 70.47 -11.01  
3 1 HIS B 86  ? ? 57.40 -127.67 
# 
_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 528 ? 5.93 . 
2 1 O ? A HOH 529 ? 5.97 . 
3 1 O B A HOH 530 ? 6.18 . 
4 1 O ? A HOH 531 ? 7.60 . 
5 1 O ? B HOH 400 ? 6.28 . 
# 
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 
A1A9R N2   N  N N 1   
A1A9R C3   C  N N 2   
A1A9R C6   C  Y N 3   
A1A9R C9   C  Y N 4   
A1A9R C12  C  Y N 5   
A1A9R C1   C  N N 6   
A1A9R C10  C  Y N 7   
A1A9R C11  C  Y N 8   
A1A9R C2   C  N S 9   
A1A9R C4   C  Y N 10  
A1A9R C5   C  Y N 11  
A1A9R C7   C  Y N 12  
A1A9R C8   C  Y N 13  
A1A9R N1   N  Y N 14  
A1A9R N3   N  Y N 15  
A1A9R N4   N  Y N 16  
A1A9R N5   N  Y N 17  
A1A9R O1   O  N N 18  
A1A9R S1   S  Y N 19  
A1A9R H9   H  N N 20  
A1A9R H5   H  N N 21  
A1A9R H6   H  N N 22  
A1A9R H8   H  N N 23  
A1A9R H12  H  N N 24  
A1A9R H4   H  N N 25  
A1A9R H3   H  N N 26  
A1A9R H11  H  N N 27  
A1A9R H1   H  N N 28  
A1A9R H7   H  N N 29  
A1A9R H10  H  N N 30  
A1A9R H13  H  N N 31  
A1A9R H2   H  N N 32  
ALA   N    N  N N 33  
ALA   CA   C  N S 34  
ALA   C    C  N N 35  
ALA   O    O  N N 36  
ALA   CB   C  N N 37  
ALA   OXT  O  N N 38  
ALA   H    H  N N 39  
ALA   H2   H  N N 40  
ALA   HA   H  N N 41  
ALA   HB1  H  N N 42  
ALA   HB2  H  N N 43  
ALA   HB3  H  N N 44  
ALA   HXT  H  N N 45  
ARG   N    N  N N 46  
ARG   CA   C  N S 47  
ARG   C    C  N N 48  
ARG   O    O  N N 49  
ARG   CB   C  N N 50  
ARG   CG   C  N N 51  
ARG   CD   C  N N 52  
ARG   NE   N  N N 53  
ARG   CZ   C  N N 54  
ARG   NH1  N  N N 55  
ARG   NH2  N  N N 56  
ARG   OXT  O  N N 57  
ARG   H    H  N N 58  
ARG   H2   H  N N 59  
ARG   HA   H  N N 60  
ARG   HB2  H  N N 61  
ARG   HB3  H  N N 62  
ARG   HG2  H  N N 63  
ARG   HG3  H  N N 64  
ARG   HD2  H  N N 65  
ARG   HD3  H  N N 66  
ARG   HE   H  N N 67  
ARG   HH11 H  N N 68  
ARG   HH12 H  N N 69  
ARG   HH21 H  N N 70  
ARG   HH22 H  N N 71  
ARG   HXT  H  N N 72  
ASN   N    N  N N 73  
ASN   CA   C  N S 74  
ASN   C    C  N N 75  
ASN   O    O  N N 76  
ASN   CB   C  N N 77  
ASN   CG   C  N N 78  
ASN   OD1  O  N N 79  
ASN   ND2  N  N N 80  
ASN   OXT  O  N N 81  
ASN   H    H  N N 82  
ASN   H2   H  N N 83  
ASN   HA   H  N N 84  
ASN   HB2  H  N N 85  
ASN   HB3  H  N N 86  
ASN   HD21 H  N N 87  
ASN   HD22 H  N N 88  
ASN   HXT  H  N N 89  
ASP   N    N  N N 90  
ASP   CA   C  N S 91  
ASP   C    C  N N 92  
ASP   O    O  N N 93  
ASP   CB   C  N N 94  
ASP   CG   C  N N 95  
ASP   OD1  O  N N 96  
ASP   OD2  O  N N 97  
ASP   OXT  O  N N 98  
ASP   H    H  N N 99  
ASP   H2   H  N N 100 
ASP   HA   H  N N 101 
ASP   HB2  H  N N 102 
ASP   HB3  H  N N 103 
ASP   HD2  H  N N 104 
ASP   HXT  H  N N 105 
CL    CL   CL N N 106 
CYS   N    N  N N 107 
CYS   CA   C  N R 108 
CYS   C    C  N N 109 
CYS   O    O  N N 110 
CYS   CB   C  N N 111 
CYS   SG   S  N N 112 
CYS   OXT  O  N N 113 
CYS   H    H  N N 114 
CYS   H2   H  N N 115 
CYS   HA   H  N N 116 
CYS   HB2  H  N N 117 
CYS   HB3  H  N N 118 
CYS   HG   H  N N 119 
CYS   HXT  H  N N 120 
GLN   N    N  N N 121 
GLN   CA   C  N S 122 
GLN   C    C  N N 123 
GLN   O    O  N N 124 
GLN   CB   C  N N 125 
GLN   CG   C  N N 126 
GLN   CD   C  N N 127 
GLN   OE1  O  N N 128 
GLN   NE2  N  N N 129 
GLN   OXT  O  N N 130 
GLN   H    H  N N 131 
GLN   H2   H  N N 132 
GLN   HA   H  N N 133 
GLN   HB2  H  N N 134 
GLN   HB3  H  N N 135 
GLN   HG2  H  N N 136 
GLN   HG3  H  N N 137 
GLN   HE21 H  N N 138 
GLN   HE22 H  N N 139 
GLN   HXT  H  N N 140 
GLU   N    N  N N 141 
GLU   CA   C  N S 142 
GLU   C    C  N N 143 
GLU   O    O  N N 144 
GLU   CB   C  N N 145 
GLU   CG   C  N N 146 
GLU   CD   C  N N 147 
GLU   OE1  O  N N 148 
GLU   OE2  O  N N 149 
GLU   OXT  O  N N 150 
GLU   H    H  N N 151 
GLU   H2   H  N N 152 
GLU   HA   H  N N 153 
GLU   HB2  H  N N 154 
GLU   HB3  H  N N 155 
GLU   HG2  H  N N 156 
GLU   HG3  H  N N 157 
GLU   HE2  H  N N 158 
GLU   HXT  H  N N 159 
GLY   N    N  N N 160 
GLY   CA   C  N N 161 
GLY   C    C  N N 162 
GLY   O    O  N N 163 
GLY   OXT  O  N N 164 
GLY   H    H  N N 165 
GLY   H2   H  N N 166 
GLY   HA2  H  N N 167 
GLY   HA3  H  N N 168 
GLY   HXT  H  N N 169 
HIS   N    N  N N 170 
HIS   CA   C  N S 171 
HIS   C    C  N N 172 
HIS   O    O  N N 173 
HIS   CB   C  N N 174 
HIS   CG   C  Y N 175 
HIS   ND1  N  Y N 176 
HIS   CD2  C  Y N 177 
HIS   CE1  C  Y N 178 
HIS   NE2  N  Y N 179 
HIS   OXT  O  N N 180 
HIS   H    H  N N 181 
HIS   H2   H  N N 182 
HIS   HA   H  N N 183 
HIS   HB2  H  N N 184 
HIS   HB3  H  N N 185 
HIS   HD1  H  N N 186 
HIS   HD2  H  N N 187 
HIS   HE1  H  N N 188 
HIS   HE2  H  N N 189 
HIS   HXT  H  N N 190 
HOH   O    O  N N 191 
HOH   H1   H  N N 192 
HOH   H2   H  N N 193 
ILE   N    N  N N 194 
ILE   CA   C  N S 195 
ILE   C    C  N N 196 
ILE   O    O  N N 197 
ILE   CB   C  N S 198 
ILE   CG1  C  N N 199 
ILE   CG2  C  N N 200 
ILE   CD1  C  N N 201 
ILE   OXT  O  N N 202 
ILE   H    H  N N 203 
ILE   H2   H  N N 204 
ILE   HA   H  N N 205 
ILE   HB   H  N N 206 
ILE   HG12 H  N N 207 
ILE   HG13 H  N N 208 
ILE   HG21 H  N N 209 
ILE   HG22 H  N N 210 
ILE   HG23 H  N N 211 
ILE   HD11 H  N N 212 
ILE   HD12 H  N N 213 
ILE   HD13 H  N N 214 
ILE   HXT  H  N N 215 
LEU   N    N  N N 216 
LEU   CA   C  N S 217 
LEU   C    C  N N 218 
LEU   O    O  N N 219 
LEU   CB   C  N N 220 
LEU   CG   C  N N 221 
LEU   CD1  C  N N 222 
LEU   CD2  C  N N 223 
LEU   OXT  O  N N 224 
LEU   H    H  N N 225 
LEU   H2   H  N N 226 
LEU   HA   H  N N 227 
LEU   HB2  H  N N 228 
LEU   HB3  H  N N 229 
LEU   HG   H  N N 230 
LEU   HD11 H  N N 231 
LEU   HD12 H  N N 232 
LEU   HD13 H  N N 233 
LEU   HD21 H  N N 234 
LEU   HD22 H  N N 235 
LEU   HD23 H  N N 236 
LEU   HXT  H  N N 237 
LYS   N    N  N N 238 
LYS   CA   C  N S 239 
LYS   C    C  N N 240 
LYS   O    O  N N 241 
LYS   CB   C  N N 242 
LYS   CG   C  N N 243 
LYS   CD   C  N N 244 
LYS   CE   C  N N 245 
LYS   NZ   N  N N 246 
LYS   OXT  O  N N 247 
LYS   H    H  N N 248 
LYS   H2   H  N N 249 
LYS   HA   H  N N 250 
LYS   HB2  H  N N 251 
LYS   HB3  H  N N 252 
LYS   HG2  H  N N 253 
LYS   HG3  H  N N 254 
LYS   HD2  H  N N 255 
LYS   HD3  H  N N 256 
LYS   HE2  H  N N 257 
LYS   HE3  H  N N 258 
LYS   HZ1  H  N N 259 
LYS   HZ2  H  N N 260 
LYS   HZ3  H  N N 261 
LYS   HXT  H  N N 262 
MET   N    N  N N 263 
MET   CA   C  N S 264 
MET   C    C  N N 265 
MET   O    O  N N 266 
MET   CB   C  N N 267 
MET   CG   C  N N 268 
MET   SD   S  N N 269 
MET   CE   C  N N 270 
MET   OXT  O  N N 271 
MET   H    H  N N 272 
MET   H2   H  N N 273 
MET   HA   H  N N 274 
MET   HB2  H  N N 275 
MET   HB3  H  N N 276 
MET   HG2  H  N N 277 
MET   HG3  H  N N 278 
MET   HE1  H  N N 279 
MET   HE2  H  N N 280 
MET   HE3  H  N N 281 
MET   HXT  H  N N 282 
PHE   N    N  N N 283 
PHE   CA   C  N S 284 
PHE   C    C  N N 285 
PHE   O    O  N N 286 
PHE   CB   C  N N 287 
PHE   CG   C  Y N 288 
PHE   CD1  C  Y N 289 
PHE   CD2  C  Y N 290 
PHE   CE1  C  Y N 291 
PHE   CE2  C  Y N 292 
PHE   CZ   C  Y N 293 
PHE   OXT  O  N N 294 
PHE   H    H  N N 295 
PHE   H2   H  N N 296 
PHE   HA   H  N N 297 
PHE   HB2  H  N N 298 
PHE   HB3  H  N N 299 
PHE   HD1  H  N N 300 
PHE   HD2  H  N N 301 
PHE   HE1  H  N N 302 
PHE   HE2  H  N N 303 
PHE   HZ   H  N N 304 
PHE   HXT  H  N N 305 
PRO   N    N  N N 306 
PRO   CA   C  N S 307 
PRO   C    C  N N 308 
PRO   O    O  N N 309 
PRO   CB   C  N N 310 
PRO   CG   C  N N 311 
PRO   CD   C  N N 312 
PRO   OXT  O  N N 313 
PRO   H    H  N N 314 
PRO   HA   H  N N 315 
PRO   HB2  H  N N 316 
PRO   HB3  H  N N 317 
PRO   HG2  H  N N 318 
PRO   HG3  H  N N 319 
PRO   HD2  H  N N 320 
PRO   HD3  H  N N 321 
PRO   HXT  H  N N 322 
SER   N    N  N N 323 
SER   CA   C  N S 324 
SER   C    C  N N 325 
SER   O    O  N N 326 
SER   CB   C  N N 327 
SER   OG   O  N N 328 
SER   OXT  O  N N 329 
SER   H    H  N N 330 
SER   H2   H  N N 331 
SER   HA   H  N N 332 
SER   HB2  H  N N 333 
SER   HB3  H  N N 334 
SER   HG   H  N N 335 
SER   HXT  H  N N 336 
TFA   C1   C  N N 337 
TFA   C2   C  N N 338 
TFA   O    O  N N 339 
TFA   F1   F  N N 340 
TFA   F2   F  N N 341 
TFA   F3   F  N N 342 
TFA   OXT  O  N N 343 
TFA   HXT  H  N N 344 
THR   N    N  N N 345 
THR   CA   C  N S 346 
THR   C    C  N N 347 
THR   O    O  N N 348 
THR   CB   C  N R 349 
THR   OG1  O  N N 350 
THR   CG2  C  N N 351 
THR   OXT  O  N N 352 
THR   H    H  N N 353 
THR   H2   H  N N 354 
THR   HA   H  N N 355 
THR   HB   H  N N 356 
THR   HG1  H  N N 357 
THR   HG21 H  N N 358 
THR   HG22 H  N N 359 
THR   HG23 H  N N 360 
THR   HXT  H  N N 361 
TYR   N    N  N N 362 
TYR   CA   C  N S 363 
TYR   C    C  N N 364 
TYR   O    O  N N 365 
TYR   CB   C  N N 366 
TYR   CG   C  Y N 367 
TYR   CD1  C  Y N 368 
TYR   CD2  C  Y N 369 
TYR   CE1  C  Y N 370 
TYR   CE2  C  Y N 371 
TYR   CZ   C  Y N 372 
TYR   OH   O  N N 373 
TYR   OXT  O  N N 374 
TYR   H    H  N N 375 
TYR   H2   H  N N 376 
TYR   HA   H  N N 377 
TYR   HB2  H  N N 378 
TYR   HB3  H  N N 379 
TYR   HD1  H  N N 380 
TYR   HD2  H  N N 381 
TYR   HE1  H  N N 382 
TYR   HE2  H  N N 383 
TYR   HH   H  N N 384 
TYR   HXT  H  N N 385 
VAL   N    N  N N 386 
VAL   CA   C  N S 387 
VAL   C    C  N N 388 
VAL   O    O  N N 389 
VAL   CB   C  N N 390 
VAL   CG1  C  N N 391 
VAL   CG2  C  N N 392 
VAL   OXT  O  N N 393 
VAL   H    H  N N 394 
VAL   H2   H  N N 395 
VAL   HA   H  N N 396 
VAL   HB   H  N N 397 
VAL   HG11 H  N N 398 
VAL   HG12 H  N N 399 
VAL   HG13 H  N N 400 
VAL   HG21 H  N N 401 
VAL   HG22 H  N N 402 
VAL   HG23 H  N N 403 
VAL   HXT  H  N N 404 
# 
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 
A1A9R N1  C5   sing Y N 1   
A1A9R N1  C4   doub Y N 2   
A1A9R C5  C6   doub Y N 3   
A1A9R C3  C4   sing N N 4   
A1A9R C3  C2   sing N N 5   
A1A9R C4  S1   sing Y N 6   
A1A9R O1  C1   sing N N 7   
A1A9R C6  S1   sing Y N 8   
A1A9R C1  C2   sing N N 9   
A1A9R C2  N2   sing N N 10  
A1A9R N2  C7   sing N N 11  
A1A9R C7  C10  doub Y N 12  
A1A9R C7  N3   sing Y N 13  
A1A9R C11 C10  sing Y N 14  
A1A9R C11 C12  doub Y N 15  
A1A9R C10 C9   sing Y N 16  
A1A9R N3  C8   doub Y N 17  
A1A9R C12 N5   sing Y N 18  
A1A9R C9  N5   sing Y N 19  
A1A9R C9  N4   doub Y N 20  
A1A9R C8  N4   sing Y N 21  
A1A9R N2  H9   sing N N 22  
A1A9R C3  H5   sing N N 23  
A1A9R C3  H6   sing N N 24  
A1A9R C6  H8   sing N N 25  
A1A9R C12 H12  sing N N 26  
A1A9R C1  H4   sing N N 27  
A1A9R C1  H3   sing N N 28  
A1A9R C11 H11  sing N N 29  
A1A9R C2  H1   sing N N 30  
A1A9R C5  H7   sing N N 31  
A1A9R C8  H10  sing N N 32  
A1A9R N5  H13  sing N N 33  
A1A9R O1  H2   sing N N 34  
ALA   N   CA   sing N N 35  
ALA   N   H    sing N N 36  
ALA   N   H2   sing N N 37  
ALA   CA  C    sing N N 38  
ALA   CA  CB   sing N N 39  
ALA   CA  HA   sing N N 40  
ALA   C   O    doub N N 41  
ALA   C   OXT  sing N N 42  
ALA   CB  HB1  sing N N 43  
ALA   CB  HB2  sing N N 44  
ALA   CB  HB3  sing N N 45  
ALA   OXT HXT  sing N N 46  
ARG   N   CA   sing N N 47  
ARG   N   H    sing N N 48  
ARG   N   H2   sing N N 49  
ARG   CA  C    sing N N 50  
ARG   CA  CB   sing N N 51  
ARG   CA  HA   sing N N 52  
ARG   C   O    doub N N 53  
ARG   C   OXT  sing N N 54  
ARG   CB  CG   sing N N 55  
ARG   CB  HB2  sing N N 56  
ARG   CB  HB3  sing N N 57  
ARG   CG  CD   sing N N 58  
ARG   CG  HG2  sing N N 59  
ARG   CG  HG3  sing N N 60  
ARG   CD  NE   sing N N 61  
ARG   CD  HD2  sing N N 62  
ARG   CD  HD3  sing N N 63  
ARG   NE  CZ   sing N N 64  
ARG   NE  HE   sing N N 65  
ARG   CZ  NH1  sing N N 66  
ARG   CZ  NH2  doub N N 67  
ARG   NH1 HH11 sing N N 68  
ARG   NH1 HH12 sing N N 69  
ARG   NH2 HH21 sing N N 70  
ARG   NH2 HH22 sing N N 71  
ARG   OXT HXT  sing N N 72  
ASN   N   CA   sing N N 73  
ASN   N   H    sing N N 74  
ASN   N   H2   sing N N 75  
ASN   CA  C    sing N N 76  
ASN   CA  CB   sing N N 77  
ASN   CA  HA   sing N N 78  
ASN   C   O    doub N N 79  
ASN   C   OXT  sing N N 80  
ASN   CB  CG   sing N N 81  
ASN   CB  HB2  sing N N 82  
ASN   CB  HB3  sing N N 83  
ASN   CG  OD1  doub N N 84  
ASN   CG  ND2  sing N N 85  
ASN   ND2 HD21 sing N N 86  
ASN   ND2 HD22 sing N N 87  
ASN   OXT HXT  sing N N 88  
ASP   N   CA   sing N N 89  
ASP   N   H    sing N N 90  
ASP   N   H2   sing N N 91  
ASP   CA  C    sing N N 92  
ASP   CA  CB   sing N N 93  
ASP   CA  HA   sing N N 94  
ASP   C   O    doub N N 95  
ASP   C   OXT  sing N N 96  
ASP   CB  CG   sing N N 97  
ASP   CB  HB2  sing N N 98  
ASP   CB  HB3  sing N N 99  
ASP   CG  OD1  doub N N 100 
ASP   CG  OD2  sing N N 101 
ASP   OD2 HD2  sing N N 102 
ASP   OXT HXT  sing N N 103 
CYS   N   CA   sing N N 104 
CYS   N   H    sing N N 105 
CYS   N   H2   sing N N 106 
CYS   CA  C    sing N N 107 
CYS   CA  CB   sing N N 108 
CYS   CA  HA   sing N N 109 
CYS   C   O    doub N N 110 
CYS   C   OXT  sing N N 111 
CYS   CB  SG   sing N N 112 
CYS   CB  HB2  sing N N 113 
CYS   CB  HB3  sing N N 114 
CYS   SG  HG   sing N N 115 
CYS   OXT HXT  sing N N 116 
GLN   N   CA   sing N N 117 
GLN   N   H    sing N N 118 
GLN   N   H2   sing N N 119 
GLN   CA  C    sing N N 120 
GLN   CA  CB   sing N N 121 
GLN   CA  HA   sing N N 122 
GLN   C   O    doub N N 123 
GLN   C   OXT  sing N N 124 
GLN   CB  CG   sing N N 125 
GLN   CB  HB2  sing N N 126 
GLN   CB  HB3  sing N N 127 
GLN   CG  CD   sing N N 128 
GLN   CG  HG2  sing N N 129 
GLN   CG  HG3  sing N N 130 
GLN   CD  OE1  doub N N 131 
GLN   CD  NE2  sing N N 132 
GLN   NE2 HE21 sing N N 133 
GLN   NE2 HE22 sing N N 134 
GLN   OXT HXT  sing N N 135 
GLU   N   CA   sing N N 136 
GLU   N   H    sing N N 137 
GLU   N   H2   sing N N 138 
GLU   CA  C    sing N N 139 
GLU   CA  CB   sing N N 140 
GLU   CA  HA   sing N N 141 
GLU   C   O    doub N N 142 
GLU   C   OXT  sing N N 143 
GLU   CB  CG   sing N N 144 
GLU   CB  HB2  sing N N 145 
GLU   CB  HB3  sing N N 146 
GLU   CG  CD   sing N N 147 
GLU   CG  HG2  sing N N 148 
GLU   CG  HG3  sing N N 149 
GLU   CD  OE1  doub N N 150 
GLU   CD  OE2  sing N N 151 
GLU   OE2 HE2  sing N N 152 
GLU   OXT HXT  sing N N 153 
GLY   N   CA   sing N N 154 
GLY   N   H    sing N N 155 
GLY   N   H2   sing N N 156 
GLY   CA  C    sing N N 157 
GLY   CA  HA2  sing N N 158 
GLY   CA  HA3  sing N N 159 
GLY   C   O    doub N N 160 
GLY   C   OXT  sing N N 161 
GLY   OXT HXT  sing N N 162 
HIS   N   CA   sing N N 163 
HIS   N   H    sing N N 164 
HIS   N   H2   sing N N 165 
HIS   CA  C    sing N N 166 
HIS   CA  CB   sing N N 167 
HIS   CA  HA   sing N N 168 
HIS   C   O    doub N N 169 
HIS   C   OXT  sing N N 170 
HIS   CB  CG   sing N N 171 
HIS   CB  HB2  sing N N 172 
HIS   CB  HB3  sing N N 173 
HIS   CG  ND1  sing Y N 174 
HIS   CG  CD2  doub Y N 175 
HIS   ND1 CE1  doub Y N 176 
HIS   ND1 HD1  sing N N 177 
HIS   CD2 NE2  sing Y N 178 
HIS   CD2 HD2  sing N N 179 
HIS   CE1 NE2  sing Y N 180 
HIS   CE1 HE1  sing N N 181 
HIS   NE2 HE2  sing N N 182 
HIS   OXT HXT  sing N N 183 
HOH   O   H1   sing N N 184 
HOH   O   H2   sing N N 185 
ILE   N   CA   sing N N 186 
ILE   N   H    sing N N 187 
ILE   N   H2   sing N N 188 
ILE   CA  C    sing N N 189 
ILE   CA  CB   sing N N 190 
ILE   CA  HA   sing N N 191 
ILE   C   O    doub N N 192 
ILE   C   OXT  sing N N 193 
ILE   CB  CG1  sing N N 194 
ILE   CB  CG2  sing N N 195 
ILE   CB  HB   sing N N 196 
ILE   CG1 CD1  sing N N 197 
ILE   CG1 HG12 sing N N 198 
ILE   CG1 HG13 sing N N 199 
ILE   CG2 HG21 sing N N 200 
ILE   CG2 HG22 sing N N 201 
ILE   CG2 HG23 sing N N 202 
ILE   CD1 HD11 sing N N 203 
ILE   CD1 HD12 sing N N 204 
ILE   CD1 HD13 sing N N 205 
ILE   OXT HXT  sing N N 206 
LEU   N   CA   sing N N 207 
LEU   N   H    sing N N 208 
LEU   N   H2   sing N N 209 
LEU   CA  C    sing N N 210 
LEU   CA  CB   sing N N 211 
LEU   CA  HA   sing N N 212 
LEU   C   O    doub N N 213 
LEU   C   OXT  sing N N 214 
LEU   CB  CG   sing N N 215 
LEU   CB  HB2  sing N N 216 
LEU   CB  HB3  sing N N 217 
LEU   CG  CD1  sing N N 218 
LEU   CG  CD2  sing N N 219 
LEU   CG  HG   sing N N 220 
LEU   CD1 HD11 sing N N 221 
LEU   CD1 HD12 sing N N 222 
LEU   CD1 HD13 sing N N 223 
LEU   CD2 HD21 sing N N 224 
LEU   CD2 HD22 sing N N 225 
LEU   CD2 HD23 sing N N 226 
LEU   OXT HXT  sing N N 227 
LYS   N   CA   sing N N 228 
LYS   N   H    sing N N 229 
LYS   N   H2   sing N N 230 
LYS   CA  C    sing N N 231 
LYS   CA  CB   sing N N 232 
LYS   CA  HA   sing N N 233 
LYS   C   O    doub N N 234 
LYS   C   OXT  sing N N 235 
LYS   CB  CG   sing N N 236 
LYS   CB  HB2  sing N N 237 
LYS   CB  HB3  sing N N 238 
LYS   CG  CD   sing N N 239 
LYS   CG  HG2  sing N N 240 
LYS   CG  HG3  sing N N 241 
LYS   CD  CE   sing N N 242 
LYS   CD  HD2  sing N N 243 
LYS   CD  HD3  sing N N 244 
LYS   CE  NZ   sing N N 245 
LYS   CE  HE2  sing N N 246 
LYS   CE  HE3  sing N N 247 
LYS   NZ  HZ1  sing N N 248 
LYS   NZ  HZ2  sing N N 249 
LYS   NZ  HZ3  sing N N 250 
LYS   OXT HXT  sing N N 251 
MET   N   CA   sing N N 252 
MET   N   H    sing N N 253 
MET   N   H2   sing N N 254 
MET   CA  C    sing N N 255 
MET   CA  CB   sing N N 256 
MET   CA  HA   sing N N 257 
MET   C   O    doub N N 258 
MET   C   OXT  sing N N 259 
MET   CB  CG   sing N N 260 
MET   CB  HB2  sing N N 261 
MET   CB  HB3  sing N N 262 
MET   CG  SD   sing N N 263 
MET   CG  HG2  sing N N 264 
MET   CG  HG3  sing N N 265 
MET   SD  CE   sing N N 266 
MET   CE  HE1  sing N N 267 
MET   CE  HE2  sing N N 268 
MET   CE  HE3  sing N N 269 
MET   OXT HXT  sing N N 270 
PHE   N   CA   sing N N 271 
PHE   N   H    sing N N 272 
PHE   N   H2   sing N N 273 
PHE   CA  C    sing N N 274 
PHE   CA  CB   sing N N 275 
PHE   CA  HA   sing N N 276 
PHE   C   O    doub N N 277 
PHE   C   OXT  sing N N 278 
PHE   CB  CG   sing N N 279 
PHE   CB  HB2  sing N N 280 
PHE   CB  HB3  sing N N 281 
PHE   CG  CD1  doub Y N 282 
PHE   CG  CD2  sing Y N 283 
PHE   CD1 CE1  sing Y N 284 
PHE   CD1 HD1  sing N N 285 
PHE   CD2 CE2  doub Y N 286 
PHE   CD2 HD2  sing N N 287 
PHE   CE1 CZ   doub Y N 288 
PHE   CE1 HE1  sing N N 289 
PHE   CE2 CZ   sing Y N 290 
PHE   CE2 HE2  sing N N 291 
PHE   CZ  HZ   sing N N 292 
PHE   OXT HXT  sing N N 293 
PRO   N   CA   sing N N 294 
PRO   N   CD   sing N N 295 
PRO   N   H    sing N N 296 
PRO   CA  C    sing N N 297 
PRO   CA  CB   sing N N 298 
PRO   CA  HA   sing N N 299 
PRO   C   O    doub N N 300 
PRO   C   OXT  sing N N 301 
PRO   CB  CG   sing N N 302 
PRO   CB  HB2  sing N N 303 
PRO   CB  HB3  sing N N 304 
PRO   CG  CD   sing N N 305 
PRO   CG  HG2  sing N N 306 
PRO   CG  HG3  sing N N 307 
PRO   CD  HD2  sing N N 308 
PRO   CD  HD3  sing N N 309 
PRO   OXT HXT  sing N N 310 
SER   N   CA   sing N N 311 
SER   N   H    sing N N 312 
SER   N   H2   sing N N 313 
SER   CA  C    sing N N 314 
SER   CA  CB   sing N N 315 
SER   CA  HA   sing N N 316 
SER   C   O    doub N N 317 
SER   C   OXT  sing N N 318 
SER   CB  OG   sing N N 319 
SER   CB  HB2  sing N N 320 
SER   CB  HB3  sing N N 321 
SER   OG  HG   sing N N 322 
SER   OXT HXT  sing N N 323 
TFA   C1  C2   sing N N 324 
TFA   C1  O    doub N N 325 
TFA   C1  OXT  sing N N 326 
TFA   C2  F1   sing N N 327 
TFA   C2  F2   sing N N 328 
TFA   C2  F3   sing N N 329 
TFA   OXT HXT  sing N N 330 
THR   N   CA   sing N N 331 
THR   N   H    sing N N 332 
THR   N   H2   sing N N 333 
THR   CA  C    sing N N 334 
THR   CA  CB   sing N N 335 
THR   CA  HA   sing N N 336 
THR   C   O    doub N N 337 
THR   C   OXT  sing N N 338 
THR   CB  OG1  sing N N 339 
THR   CB  CG2  sing N N 340 
THR   CB  HB   sing N N 341 
THR   OG1 HG1  sing N N 342 
THR   CG2 HG21 sing N N 343 
THR   CG2 HG22 sing N N 344 
THR   CG2 HG23 sing N N 345 
THR   OXT HXT  sing N N 346 
TYR   N   CA   sing N N 347 
TYR   N   H    sing N N 348 
TYR   N   H2   sing N N 349 
TYR   CA  C    sing N N 350 
TYR   CA  CB   sing N N 351 
TYR   CA  HA   sing N N 352 
TYR   C   O    doub N N 353 
TYR   C   OXT  sing N N 354 
TYR   CB  CG   sing N N 355 
TYR   CB  HB2  sing N N 356 
TYR   CB  HB3  sing N N 357 
TYR   CG  CD1  doub Y N 358 
TYR   CG  CD2  sing Y N 359 
TYR   CD1 CE1  sing Y N 360 
TYR   CD1 HD1  sing N N 361 
TYR   CD2 CE2  doub Y N 362 
TYR   CD2 HD2  sing N N 363 
TYR   CE1 CZ   doub Y N 364 
TYR   CE1 HE1  sing N N 365 
TYR   CE2 CZ   sing Y N 366 
TYR   CE2 HE2  sing N N 367 
TYR   CZ  OH   sing N N 368 
TYR   OH  HH   sing N N 369 
TYR   OXT HXT  sing N N 370 
VAL   N   CA   sing N N 371 
VAL   N   H    sing N N 372 
VAL   N   H2   sing N N 373 
VAL   CA  C    sing N N 374 
VAL   CA  CB   sing N N 375 
VAL   CA  HA   sing N N 376 
VAL   C   O    doub N N 377 
VAL   C   OXT  sing N N 378 
VAL   CB  CG1  sing N N 379 
VAL   CB  CG2  sing N N 380 
VAL   CB  HB   sing N N 381 
VAL   CG1 HG11 sing N N 382 
VAL   CG1 HG12 sing N N 383 
VAL   CG1 HG13 sing N N 384 
VAL   CG2 HG21 sing N N 385 
VAL   CG2 HG22 sing N N 386 
VAL   CG2 HG23 sing N N 387 
VAL   OXT HXT  sing N N 388 
# 
_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                    7HEF 
_atom_sites.fract_transf_matrix[1][1]   0.011268 
_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]   0.011268 
_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]   0.025345 
_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    A VAL   A 1 3   ? 19.642 -16.125 22.203  0.62 52.90 ?  3   VAL   A N    1 
ATOM   2    N  N    B VAL   A 1 3   ? 19.561 -16.102 22.326  0.38 52.47 ?  3   VAL   A N    1 
ATOM   3    C  CA   A VAL   A 1 3   ? 18.666 -15.058 22.388  0.62 52.53 ?  3   VAL   A CA   1 
ATOM   4    C  CA   B VAL   A 1 3   ? 18.608 -15.010 22.482  0.38 52.15 ?  3   VAL   A CA   1 
ATOM   5    C  C    A VAL   A 1 3   ? 19.305 -13.704 22.099  0.62 51.11 ?  3   VAL   A C    1 
ATOM   6    C  C    B VAL   A 1 3   ? 19.272 -13.678 22.154  0.38 50.90 ?  3   VAL   A C    1 
ATOM   7    O  O    A VAL   A 1 3   ? 20.415 -13.424 22.553  0.62 51.49 ?  3   VAL   A O    1 
ATOM   8    O  O    B VAL   A 1 3   ? 20.371 -13.390 22.630  0.38 51.27 ?  3   VAL   A O    1 
ATOM   9    C  CB   A VAL   A 1 3   ? 18.048 -15.102 23.800  0.62 53.33 ?  3   VAL   A CB   1 
ATOM   10   C  CB   B VAL   A 1 3   ? 18.001 -14.995 23.899  0.38 52.83 ?  3   VAL   A CB   1 
ATOM   11   C  CG1  A VAL   A 1 3   ? 17.013 -13.998 23.966  0.62 53.58 ?  3   VAL   A CG1  1 
ATOM   12   C  CG1  B VAL   A 1 3   ? 17.016 -13.843 24.045  0.38 53.05 ?  3   VAL   A CG1  1 
ATOM   13   C  CG2  A VAL   A 1 3   ? 17.424 -16.466 24.065  0.62 53.59 ?  3   VAL   A CG2  1 
ATOM   14   C  CG2  B VAL   A 1 3   ? 17.323 -16.323 24.203  0.38 53.06 ?  3   VAL   A CG2  1 
ATOM   15   H  HA   A VAL   A 1 3   ? 17.946 -15.180 21.754  0.62 63.03 ?  3   VAL   A HA   1 
ATOM   16   H  HA   B VAL   A 1 3   ? 17.881 -15.137 21.856  0.38 62.56 ?  3   VAL   A HA   1 
ATOM   17   H  HB   A VAL   A 1 3   ? 18.746 -14.960 24.458  0.62 63.98 ?  3   VAL   A HB   1 
ATOM   18   H  HB   B VAL   A 1 3   ? 18.710 -14.866 24.548  0.38 63.38 ?  3   VAL   A HB   1 
ATOM   19   H  HG11 A VAL   A 1 3   ? 16.521 -14.150 24.789  0.62 64.27 ?  3   VAL   A HG11 1 
ATOM   20   H  HG11 B VAL   A 1 3   ? 16.509 -13.964 24.863  0.38 63.64 ?  3   VAL   A HG11 1 
ATOM   21   H  HG12 A VAL   A 1 3   ? 17.466 -13.142 24.006  0.62 64.27 ?  3   VAL   A HG12 1 
ATOM   22   H  HG12 B VAL   A 1 3   ? 17.507 -13.007 24.083  0.38 63.64 ?  3   VAL   A HG12 1 
ATOM   23   H  HG13 A VAL   A 1 3   ? 16.405 -14.020 23.211  0.62 64.27 ?  3   VAL   A HG13 1 
ATOM   24   H  HG13 B VAL   A 1 3   ? 16.417 -13.842 23.282  0.38 63.64 ?  3   VAL   A HG13 1 
ATOM   25   H  HG21 A VAL   A 1 3   ? 16.975 -16.446 24.925  0.62 64.29 ?  3   VAL   A HG21 1 
ATOM   26   H  HG21 B VAL   A 1 3   ? 16.892 -16.266 25.070  0.38 63.65 ?  3   VAL   A HG21 1 
ATOM   27   H  HG22 A VAL   A 1 3   ? 16.785 -16.662 23.362  0.62 64.29 ?  3   VAL   A HG22 1 
ATOM   28   H  HG22 B VAL   A 1 3   ? 16.663 -16.504 23.516  0.38 63.65 ?  3   VAL   A HG22 1 
ATOM   29   H  HG23 A VAL   A 1 3   ? 18.123 -17.138 24.072  0.62 64.29 ?  3   VAL   A HG23 1 
ATOM   30   H  HG23 B VAL   A 1 3   ? 17.992 -17.025 24.212  0.38 63.65 ?  3   VAL   A HG23 1 
ATOM   31   N  N    . ASN   A 1 4   ? 18.602 -12.871 21.334  1.00 48.96 ?  4   ASN   A N    1 
ATOM   32   C  CA   . ASN   A 1 4   ? 19.055 -11.524 21.004  1.00 44.52 ?  4   ASN   A CA   1 
ATOM   33   C  C    . ASN   A 1 4   ? 17.930 -10.533 21.296  1.00 40.22 ?  4   ASN   A C    1 
ATOM   34   O  O    . ASN   A 1 4   ? 16.831 -10.914 21.714  1.00 40.47 ?  4   ASN   A O    1 
ATOM   35   C  CB   . ASN   A 1 4   ? 19.584 -11.426 19.565  1.00 43.99 ?  4   ASN   A CB   1 
ATOM   36   C  CG   . ASN   A 1 4   ? 18.558 -11.831 18.533  1.00 43.39 ?  4   ASN   A CG   1 
ATOM   37   O  OD1  . ASN   A 1 4   ? 17.436 -11.326 18.523  1.00 43.14 ?  4   ASN   A OD1  1 
ATOM   38   N  ND2  . ASN   A 1 4   ? 18.939 -12.753 17.654  1.00 43.23 ?  4   ASN   A ND2  1 
ATOM   39   H  H    A ASN   A 1 4   ? 17.839 -13.072 20.988  0.62 58.73 ?  4   ASN   A H    1 
ATOM   40   H  H    B ASN   A 1 4   ? 17.861 -13.088 20.951  0.38 58.73 ?  4   ASN   A H    1 
ATOM   41   H  HA   . ASN   A 1 4   ? 19.794 -11.303 21.584  1.00 53.41 ?  4   ASN   A HA   1 
ATOM   42   H  HB2  . ASN   A 1 4   ? 19.847 -10.508 19.386  1.00 52.78 ?  4   ASN   A HB2  1 
ATOM   43   H  HB3  . ASN   A 1 4   ? 20.353 -12.011 19.471  1.00 52.78 ?  4   ASN   A HB3  1 
ATOM   44   H  HD21 . ASN   A 1 4   ? 18.394 -13.016 17.044  1.00 51.86 ?  4   ASN   A HD21 1 
ATOM   45   H  HD22 . ASN   A 1 4   ? 19.733 -13.085 17.693  1.00 51.86 ?  4   ASN   A HD22 1 
ATOM   46   N  N    A SER   A 1 5   ? 18.213 -9.247  21.089  0.62 37.69 ?  5   SER   A N    1 
ATOM   47   N  N    B SER   A 1 5   ? 18.207 -9.251  21.053  0.38 37.79 ?  5   SER   A N    1 
ATOM   48   C  CA   A SER   A 1 5   ? 17.294 -8.179  21.463  0.62 34.97 ?  5   SER   A CA   1 
ATOM   49   C  CA   B SER   A 1 5   ? 17.333 -8.161  21.466  0.38 35.14 ?  5   SER   A CA   1 
ATOM   50   C  C    A SER   A 1 5   ? 16.428 -7.698  20.303  0.62 31.66 ?  5   SER   A C    1 
ATOM   51   C  C    B SER   A 1 5   ? 16.459 -7.620  20.338  0.38 31.94 ?  5   SER   A C    1 
ATOM   52   O  O    A SER   A 1 5   ? 15.774 -6.657  20.424  0.62 32.02 ?  5   SER   A O    1 
ATOM   53   O  O    B SER   A 1 5   ? 15.780 -6.607  20.533  0.38 32.22 ?  5   SER   A O    1 
ATOM   54   C  CB   A SER   A 1 5   ? 18.063 -7.004  22.071  0.62 35.61 ?  5   SER   A CB   1 
ATOM   55   C  CB   B SER   A 1 5   ? 18.157 -7.024  22.075  0.38 35.68 ?  5   SER   A CB   1 
ATOM   56   O  OG   A SER   A 1 5   ? 19.023 -6.496  21.161  0.62 35.94 ?  5   SER   A OG   1 
ATOM   57   O  OG   B SER   A 1 5   ? 19.000 -6.429  21.104  0.38 35.93 ?  5   SER   A OG   1 
ATOM   58   H  H    A SER   A 1 5   ? 18.941 -8.969  20.725  0.62 45.21 ?  5   SER   A H    1 
ATOM   59   H  H    B SER   A 1 5   ? 18.912 -8.988  20.637  0.38 45.33 ?  5   SER   A H    1 
ATOM   60   H  HA   A SER   A 1 5   ? 16.703 -8.517  22.153  0.62 41.95 ?  5   SER   A HA   1 
ATOM   61   H  HA   B SER   A 1 5   ? 16.742 -8.490  22.160  0.38 42.16 ?  5   SER   A HA   1 
ATOM   62   H  HB2  A SER   A 1 5   ? 17.435 -6.296  22.289  0.62 42.72 ?  5   SER   A HB2  1 
ATOM   63   H  HB2  B SER   A 1 5   ? 17.553 -6.349  22.426  0.38 42.80 ?  5   SER   A HB2  1 
ATOM   64   H  HB3  A SER   A 1 5   ? 18.513 -7.303  22.878  0.62 42.72 ?  5   SER   A HB3  1 
ATOM   65   H  HB3  B SER   A 1 5   ? 18.706 -7.380  22.792  0.38 42.80 ?  5   SER   A HB3  1 
ATOM   66   H  HG   A SER   A 1 5   ? 19.440 -5.857  21.514  0.62 43.11 ?  5   SER   A HG   1 
ATOM   67   H  HG   B SER   A 1 5   ? 19.443 -5.805  21.452  0.38 43.10 ?  5   SER   A HG   1 
ATOM   68   N  N    A PHE   A 1 6   ? 16.411 -8.421  19.186  0.62 27.54 ?  6   PHE   A N    1 
ATOM   69   N  N    B PHE   A 1 6   ? 16.459 -8.256  19.169  0.38 28.17 ?  6   PHE   A N    1 
ATOM   70   C  CA   A PHE   A 1 6   ? 15.513 -8.073  18.092  0.62 23.60 ?  6   PHE   A CA   1 
ATOM   71   C  CA   B PHE   A 1 6   ? 15.558 -7.839  18.103  0.38 24.46 ?  6   PHE   A CA   1 
ATOM   72   C  C    A PHE   A 1 6   ? 14.082 -8.464  18.446  0.62 23.03 ?  6   PHE   A C    1 
ATOM   73   C  C    B PHE   A 1 6   ? 14.118 -8.120  18.517  0.38 23.39 ?  6   PHE   A C    1 
ATOM   74   O  O    A PHE   A 1 6   ? 13.830 -9.558  18.956  0.62 24.19 ?  6   PHE   A O    1 
ATOM   75   O  O    B PHE   A 1 6   ? 13.787 -9.236  18.927  0.38 23.65 ?  6   PHE   A O    1 
ATOM   76   C  CB   A PHE   A 1 6   ? 15.944 -8.787  16.814  0.62 20.94 ?  6   PHE   A CB   1 
ATOM   77   C  CB   B PHE   A 1 6   ? 15.893 -8.580  16.810  0.38 22.31 ?  6   PHE   A CB   1 
ATOM   78   C  CG   A PHE   A 1 6   ? 17.211 -8.240  16.212  0.62 18.85 ?  6   PHE   A CG   1 
ATOM   79   C  CG   B PHE   A 1 6   ? 17.200 -8.159  16.190  0.38 20.48 ?  6   PHE   A CG   1 
ATOM   80   C  CD1  A PHE   A 1 6   ? 17.199 -7.051  15.500  0.62 18.11 ?  6   PHE   A CD1  1 
ATOM   81   C  CD1  B PHE   A 1 6   ? 17.303 -6.955  15.514  0.38 19.69 ?  6   PHE   A CD1  1 
ATOM   82   C  CD2  A PHE   A 1 6   ? 18.411 -8.916  16.355  0.62 19.27 ?  6   PHE   A CD2  1 
ATOM   83   C  CD2  B PHE   A 1 6   ? 18.320 -8.970  16.276  0.38 20.39 ?  6   PHE   A CD2  1 
ATOM   84   C  CE1  A PHE   A 1 6   ? 18.359 -6.546  14.944  0.62 18.04 ?  6   PHE   A CE1  1 
ATOM   85   C  CE1  B PHE   A 1 6   ? 18.500 -6.564  14.940  0.38 19.47 ?  6   PHE   A CE1  1 
ATOM   86   C  CE2  A PHE   A 1 6   ? 19.571 -8.418  15.800  0.62 19.08 ?  6   PHE   A CE2  1 
ATOM   87   C  CE2  B PHE   A 1 6   ? 19.519 -8.586  15.703  0.38 20.02 ?  6   PHE   A CE2  1 
ATOM   88   C  CZ   A PHE   A 1 6   ? 19.546 -7.230  15.094  0.62 18.26 ?  6   PHE   A CZ   1 
ATOM   89   C  CZ   B PHE   A 1 6   ? 19.609 -7.380  15.034  0.38 19.51 ?  6   PHE   A CZ   1 
ATOM   90   H  H    A PHE   A 1 6   ? 16.908 -9.108  19.040  0.62 33.03 ?  6   PHE   A H    1 
ATOM   91   H  H    B PHE   A 1 6   ? 16.965 -8.923  18.970  0.38 33.78 ?  6   PHE   A H    1 
ATOM   92   H  HA   A PHE   A 1 6   ? 15.542 -7.120  17.940  0.62 28.31 ?  6   PHE   A HA   1 
ATOM   93   H  HA   B PHE   A 1 6   ? 15.653 -6.887  17.950  0.38 29.33 ?  6   PHE   A HA   1 
ATOM   94   H  HB2  A PHE   A 1 6   ? 16.090 -9.727  17.016  0.62 25.12 ?  6   PHE   A HB2  1 
ATOM   95   H  HB2  B PHE   A 1 6   ? 15.947 -9.530  17.000  0.38 26.76 ?  6   PHE   A HB2  1 
ATOM   96   H  HB3  A PHE   A 1 6   ? 15.239 -8.700  16.156  0.62 25.12 ?  6   PHE   A HB3  1 
ATOM   97   H  HB3  B PHE   A 1 6   ? 15.191 -8.413  16.163  0.38 26.76 ?  6   PHE   A HB3  1 
ATOM   98   H  HD1  A PHE   A 1 6   ? 16.398 -6.588  15.398  0.62 21.72 ?  6   PHE   A HD1  1 
ATOM   99   H  HD1  B PHE   A 1 6   ? 16.560 -6.401  15.448  0.38 23.61 ?  6   PHE   A HD1  1 
ATOM   100  H  HD2  A PHE   A 1 6   ? 18.433 -9.718  16.831  0.62 23.11 ?  6   PHE   A HD2  1 
ATOM   101  H  HD2  B PHE   A 1 6   ? 18.267 -9.782  16.726  0.38 24.46 ?  6   PHE   A HD2  1 
ATOM   102  H  HE1  A PHE   A 1 6   ? 18.337 -5.747  14.470  0.62 21.63 ?  6   PHE   A HE1  1 
ATOM   103  H  HE1  B PHE   A 1 6   ? 18.557 -5.753  14.490  0.38 23.34 ?  6   PHE   A HE1  1 
ATOM   104  H  HE2  A PHE   A 1 6   ? 20.372 -8.879  15.904  0.62 22.88 ?  6   PHE   A HE2  1 
ATOM   105  H  HE2  B PHE   A 1 6   ? 20.267 -9.137  15.768  0.38 24.01 ?  6   PHE   A HE2  1 
ATOM   106  H  HZ   A PHE   A 1 6   ? 20.325 -6.892  14.722  0.62 21.89 ?  6   PHE   A HZ   1 
ATOM   107  H  HZ   B PHE   A 1 6   ? 20.414 -7.118  14.648  0.38 23.40 ?  6   PHE   A HZ   1 
ATOM   108  N  N    A SER   A 1 7   ? 13.137 -7.565  18.163  0.62 21.40 ?  7   SER   A N    1 
ATOM   109  N  N    B SER   A 1 7   ? 13.258 -7.108  18.408  0.38 22.22 ?  7   SER   A N    1 
ATOM   110  C  CA   A SER   A 1 7   ? 11.759 -7.710  18.622  0.62 20.69 ?  7   SER   A CA   1 
ATOM   111  C  CA   B SER   A 1 7   ? 11.917 -7.151  18.976  0.38 21.80 ?  7   SER   A CA   1 
ATOM   112  C  C    A SER   A 1 7   ? 10.769 -7.413  17.500  0.62 18.42 ?  7   SER   A C    1 
ATOM   113  C  C    B SER   A 1 7   ? 10.874 -7.110  17.869  0.38 20.53 ?  7   SER   A C    1 
ATOM   114  O  O    A SER   A 1 7   ? 11.001 -6.534  16.666  0.62 18.59 ?  7   SER   A O    1 
ATOM   115  O  O    B SER   A 1 7   ? 10.928 -6.247  16.988  0.38 20.62 ?  7   SER   A O    1 
ATOM   116  C  CB   A SER   A 1 7   ? 11.497 -6.767  19.805  0.62 22.38 ?  7   SER   A CB   1 
ATOM   117  C  CB   B SER   A 1 7   ? 11.703 -5.974  19.933  0.38 22.41 ?  7   SER   A CB   1 
ATOM   118  O  OG   A SER   A 1 7   ? 10.147 -6.830  20.223  0.62 23.71 ?  7   SER   A OG   1 
ATOM   119  O  OG   B SER   A 1 7   ? 10.432 -6.042  20.553  0.38 23.18 ?  7   SER   A OG   1 
ATOM   120  H  H    A SER   A 1 7   ? 13.276 -6.858  17.697  0.62 25.66 ?  7   SER   A H    1 
ATOM   121  H  H    B SER   A 1 7   ? 13.432 -6.372  17.996  0.38 26.65 ?  7   SER   A H    1 
ATOM   122  H  HA   A SER   A 1 7   ? 11.615 -8.621  18.921  0.62 24.82 ?  7   SER   A HA   1 
ATOM   123  H  HA   B SER   A 1 7   ? 11.799 -7.973  19.475  0.38 26.15 ?  7   SER   A HA   1 
ATOM   124  H  HB2  A SER   A 1 7   ? 12.070 -7.026  20.547  0.62 26.84 ?  7   SER   A HB2  1 
ATOM   125  H  HB2  B SER   A 1 7   ? 12.394 -5.994  20.616  0.38 26.88 ?  7   SER   A HB2  1 
ATOM   126  H  HB3  A SER   A 1 7   ? 11.705 -5.858  19.535  0.62 26.84 ?  7   SER   A HB3  1 
ATOM   127  H  HB3  B SER   A 1 7   ? 11.760 -5.145  19.434  0.38 26.88 ?  7   SER   A HB3  1 
ATOM   128  H  HG   A SER   A 1 7   ? 10.022 -6.309  20.869  0.62 28.44 ?  7   SER   A HG   1 
ATOM   129  H  HG   B SER   A 1 7   ? 10.337 -5.395  21.083  0.38 27.80 ?  7   SER   A HG   1 
ATOM   130  N  N    A GLY   A 1 8   ? 9.655  -8.149  17.491  0.62 16.71 ?  8   GLY   A N    1 
ATOM   131  N  N    B GLY   A 1 8   ? 9.928  -8.046  17.919  0.38 19.43 ?  8   GLY   A N    1 
ATOM   132  C  CA   A GLY   A 1 8   ? 8.572  -7.900  16.558  0.62 15.69 ?  8   GLY   A CA   1 
ATOM   133  C  CA   B GLY   A 1 8   ? 8.773  -7.989  17.049  0.38 17.86 ?  8   GLY   A CA   1 
ATOM   134  C  C    A GLY   A 1 8   ? 8.783  -8.416  15.151  0.62 14.54 ?  8   GLY   A C    1 
ATOM   135  C  C    B GLY   A 1 8   ? 8.983  -8.477  15.638  0.38 16.05 ?  8   GLY   A C    1 
ATOM   136  O  O    A GLY   A 1 8   ? 8.048  -8.007  14.244  0.62 14.62 ?  8   GLY   A O    1 
ATOM   137  O  O    B GLY   A 1 8   ? 8.161  -8.173  14.769  0.38 16.15 ?  8   GLY   A O    1 
ATOM   138  H  H    A GLY   A 1 8   ? 9.510  -8.801  18.028  0.62 20.04 ?  8   GLY   A H    1 
ATOM   139  H  H    B GLY   A 1 8   ? 9.938  -8.724  18.448  0.38 23.29 ?  8   GLY   A H    1 
ATOM   140  H  HA2  A GLY   A 1 8   ? 7.762  -8.302  16.918  0.62 18.81 ?  8   GLY   A HA2  1 
ATOM   141  H  HA2  B GLY   A 1 8   ? 8.064  -8.523  17.431  0.38 21.42 ?  8   GLY   A HA2  1 
ATOM   142  H  HA3  A GLY   A 1 8   ? 8.423  -6.942  16.504  0.62 18.81 ?  8   GLY   A HA3  1 
ATOM   143  H  HA3  B GLY   A 1 8   ? 8.467  -7.072  16.995  0.38 21.42 ?  8   GLY   A HA3  1 
ATOM   144  N  N    A TYR   A 1 9   ? 9.760  -9.292  14.932  0.62 13.46 ?  9   TYR   A N    1 
ATOM   145  N  N    B TYR   A 1 9   ? 10.047 -9.227  15.372  0.38 14.27 ?  9   TYR   A N    1 
ATOM   146  C  CA   A TYR   A 1 9   ? 10.030 -9.838  13.608  0.62 12.52 ?  9   TYR   A CA   1 
ATOM   147  C  CA   B TYR   A 1 9   ? 10.269 -9.728  14.024  0.38 13.02 ?  9   TYR   A CA   1 
ATOM   148  C  C    A TYR   A 1 9   ? 9.172  -11.069 13.339  0.62 11.76 ?  9   TYR   A C    1 
ATOM   149  C  C    B TYR   A 1 9   ? 9.431  -10.972 13.753  0.38 12.39 ?  9   TYR   A C    1 
ATOM   150  O  O    A TYR   A 1 9   ? 8.904  -11.874 14.236  0.62 13.37 ?  9   TYR   A O    1 
ATOM   151  O  O    B TYR   A 1 9   ? 9.219  -11.808 14.636  0.38 13.25 ?  9   TYR   A O    1 
ATOM   152  C  CB   A TYR   A 1 9   ? 11.505 -10.235 13.468  0.62 12.80 ?  9   TYR   A CB   1 
ATOM   153  C  CB   B TYR   A 1 9   ? 11.752 -10.022 13.789  0.38 12.88 ?  9   TYR   A CB   1 
ATOM   154  C  CG   A TYR   A 1 9   ? 12.451 -9.069  13.323  0.62 13.15 ?  9   TYR   A CG   1 
ATOM   155  C  CG   B TYR   A 1 9   ? 12.561 -8.769  13.532  0.38 12.54 ?  9   TYR   A CG   1 
ATOM   156  C  CD1  A TYR   A 1 9   ? 12.823 -8.317  14.426  0.62 13.64 ?  9   TYR   A CD1  1 
ATOM   157  C  CD1  B TYR   A 1 9   ? 12.811 -7.864  14.553  0.38 12.94 ?  9   TYR   A CD1  1 
ATOM   158  C  CD2  A TYR   A 1 9   ? 12.960 -8.717  12.081  0.62 13.25 ?  9   TYR   A CD2  1 
ATOM   159  C  CD2  B TYR   A 1 9   ? 13.051 -8.480  12.265  0.38 12.10 ?  9   TYR   A CD2  1 
ATOM   160  C  CE1  A TYR   A 1 9   ? 13.674 -7.239  14.300  0.62 14.23 ?  9   TYR   A CE1  1 
ATOM   161  C  CE1  B TYR   A 1 9   ? 13.533 -6.712  14.325  0.38 12.71 ?  9   TYR   A CE1  1 
ATOM   162  C  CE2  A TYR   A 1 9   ? 13.808 -7.645  11.942  0.62 13.71 ?  9   TYR   A CE2  1 
ATOM   163  C  CE2  B TYR   A 1 9   ? 13.775 -7.327  12.026  0.38 11.99 ?  9   TYR   A CE2  1 
ATOM   164  C  CZ   A TYR   A 1 9   ? 14.161 -6.908  13.053  0.62 14.40 ?  9   TYR   A CZ   1 
ATOM   165  C  CZ   B TYR   A 1 9   ? 14.012 -6.451  13.061  0.38 12.22 ?  9   TYR   A CZ   1 
ATOM   166  O  OH   A TYR   A 1 9   ? 15.007 -5.841  12.911  0.62 15.34 ?  9   TYR   A OH   1 
ATOM   167  O  OH   B TYR   A 1 9   ? 14.730 -5.302  12.825  0.38 12.15 ?  9   TYR   A OH   1 
ATOM   168  H  H    A TYR   A 1 9   ? 10.281 -9.587  15.541  0.62 16.14 ?  9   TYR   A H    1 
ATOM   169  H  H    B TYR   A 1 9   ? 10.657 -9.454  15.946  0.38 17.10 ?  9   TYR   A H    1 
ATOM   170  H  HA   A TYR   A 1 9   ? 9.827  -9.164  12.933  0.62 15.01 ?  9   TYR   A HA   1 
ATOM   171  H  HA   B TYR   A 1 9   ? 10.004 -9.043  13.394  0.38 15.60 ?  9   TYR   A HA   1 
ATOM   172  H  HB2  A TYR   A 1 9   ? 11.767 -10.740 14.250  0.62 15.34 ?  9   TYR   A HB2  1 
ATOM   173  H  HB2  B TYR   A 1 9   ? 12.118 -10.468 14.568  0.38 15.44 ?  9   TYR   A HB2  1 
ATOM   174  H  HB3  A TYR   A 1 9   ? 11.586 -10.784 12.674  0.62 15.34 ?  9   TYR   A HB3  1 
ATOM   175  H  HB3  B TYR   A 1 9   ? 11.831 -10.596 13.010  0.38 15.44 ?  9   TYR   A HB3  1 
ATOM   176  H  HD1  A TYR   A 1 9   ? 12.483 -8.538  15.264  0.62 16.36 ?  9   TYR   A HD1  1 
ATOM   177  H  HD1  B TYR   A 1 9   ? 12.487 -8.039  15.407  0.38 15.51 ?  9   TYR   A HD1  1 
ATOM   178  H  HD2  A TYR   A 1 9   ? 12.718 -9.213  11.328  0.62 15.89 ?  9   TYR   A HD2  1 
ATOM   179  H  HD2  B TYR   A 1 9   ? 12.890 -9.070  11.566  0.38 14.50 ?  9   TYR   A HD2  1 
ATOM   180  H  HE1  A TYR   A 1 9   ? 13.917 -6.746  15.048  0.62 17.06 ?  9   TYR   A HE1  1 
ATOM   181  H  HE1  B TYR   A 1 9   ? 13.697 -6.116  15.020  0.38 15.24 ?  9   TYR   A HE1  1 
ATOM   182  H  HE2  A TYR   A 1 9   ? 14.150 -7.424  11.105  0.62 16.44 ?  9   TYR   A HE2  1 
ATOM   183  H  HE2  B TYR   A 1 9   ? 14.104 -7.143  11.172  0.38 14.37 ?  9   TYR   A HE2  1 
ATOM   184  H  HH   A TYR   A 1 9   ? 15.154 -5.495  13.662  0.62 18.39 ?  9   TYR   A HH   1 
ATOM   185  H  HH   B TYR   A 1 9   ? 14.811 -4.852  13.533  0.38 14.56 ?  9   TYR   A HH   1 
ATOM   186  N  N    A LEU   A 1 10  ? 8.753  -11.209 12.086  0.62 11.49 ?  10  LEU   A N    1 
ATOM   187  N  N    B LEU   A 1 10  ? 8.956  -11.080 12.515  0.38 11.69 ?  10  LEU   A N    1 
ATOM   188  C  CA   A LEU   A 1 10  ? 8.177  -12.453 11.601  0.62 11.21 ?  10  LEU   A CA   1 
ATOM   189  C  CA   B LEU   A 1 10  ? 8.253  -12.262 12.036  0.38 11.65 ?  10  LEU   A CA   1 
ATOM   190  C  C    A LEU   A 1 10  ? 9.306  -13.391 11.182  0.62 11.16 ?  10  LEU   A C    1 
ATOM   191  C  C    B LEU   A 1 10  ? 9.286  -13.248 11.500  0.38 11.07 ?  10  LEU   A C    1 
ATOM   192  O  O    A LEU   A 1 10  ? 10.275 -12.970 10.544  0.62 11.83 ?  10  LEU   A O    1 
ATOM   193  O  O    B LEU   A 1 10  ? 10.081 -12.906 10.617  0.38 11.47 ?  10  LEU   A O    1 
ATOM   194  C  CB   A LEU   A 1 10  ? 7.288  -12.150 10.397  0.62 11.97 ?  10  LEU   A CB   1 
ATOM   195  C  CB   B LEU   A 1 10  ? 7.271  -11.870 10.931  0.38 11.67 ?  10  LEU   A CB   1 
ATOM   196  C  CG   A LEU   A 1 10  ? 6.639  -13.343 9.702   0.62 14.01 ?  10  LEU   A CG   1 
ATOM   197  C  CG   B LEU   A 1 10  ? 6.535  -13.023 10.248  0.38 12.13 ?  10  LEU   A CG   1 
ATOM   198  C  CD1  A LEU   A 1 10  ? 5.642  -14.013 10.622  0.62 15.26 ?  10  LEU   A CD1  1 
ATOM   199  C  CD1  B LEU   A 1 10  ? 5.589  -13.702 11.220  0.38 13.17 ?  10  LEU   A CD1  1 
ATOM   200  C  CD2  A LEU   A 1 10  ? 5.982  -12.911 8.405   0.62 15.07 ?  10  LEU   A CD2  1 
ATOM   201  C  CD2  B LEU   A 1 10  ? 5.788  -12.508 9.033   0.38 13.14 ?  10  LEU   A CD2  1 
ATOM   202  H  H    A LEU   A 1 10  ? 8.791  -10.589 11.485  0.62 13.77 ?  10  LEU   A H    1 
ATOM   203  H  H    B LEU   A 1 10  ? 9.037  -10.460 11.919  0.38 14.01 ?  10  LEU   A H    1 
ATOM   204  H  HA   A LEU   A 1 10  ? 7.638  -12.866 12.302  0.62 13.44 ?  10  LEU   A HA   1 
ATOM   205  H  HA   B LEU   A 1 10  ? 7.756  -12.670 12.767  0.38 13.97 ?  10  LEU   A HA   1 
ATOM   206  H  HB2  A LEU   A 1 10  ? 6.567  -11.568 10.682  0.62 14.35 ?  10  LEU   A HB2  1 
ATOM   207  H  HB2  B LEU   A 1 10  ? 6.593  -11.281 11.309  0.38 13.99 ?  10  LEU   A HB2  1 
ATOM   208  H  HB3  A LEU   A 1 10  ? 7.825  -11.696 9.733   0.62 14.35 ?  10  LEU   A HB3  1 
ATOM   209  H  HB3  B LEU   A 1 10  ? 7.759  -11.391 10.243  0.38 13.99 ?  10  LEU   A HB3  1 
ATOM   210  H  HG   A LEU   A 1 10  ? 7.324  -13.998 9.481   0.62 16.80 ?  10  LEU   A HG   1 
ATOM   211  H  HG   B LEU   A 1 10  ? 7.180  -13.680 9.947   0.38 14.54 ?  10  LEU   A HG   1 
ATOM   212  H  HD11 A LEU   A 1 10  ? 5.285  -14.801 10.186  0.62 18.30 ?  10  LEU   A HD11 1 
ATOM   213  H  HD11 B LEU   A 1 10  ? 5.231  -14.502 10.803  0.38 15.78 ?  10  LEU   A HD11 1 
ATOM   214  H  HD12 A LEU   A 1 10  ? 6.089  -14.263 11.445  0.62 18.30 ?  10  LEU   A HD12 1 
ATOM   215  H  HD12 B LEU   A 1 10  ? 6.072  -13.938 12.026  0.38 15.78 ?  10  LEU   A HD12 1 
ATOM   216  H  HD13 A LEU   A 1 10  ? 4.925  -13.387 10.815  0.62 18.30 ?  10  LEU   A HD13 1 
ATOM   217  H  HD13 B LEU   A 1 10  ? 4.867  -13.091 11.436  0.38 15.78 ?  10  LEU   A HD13 1 
ATOM   218  H  HD21 A LEU   A 1 10  ? 5.576  -13.686 7.985   0.62 18.07 ?  10  LEU   A HD21 1 
ATOM   219  H  HD21 B LEU   A 1 10  ? 5.325  -13.249 8.614   0.38 15.75 ?  10  LEU   A HD21 1 
ATOM   220  H  HD22 A LEU   A 1 10  ? 5.305  -12.249 8.605   0.62 18.07 ?  10  LEU   A HD22 1 
ATOM   221  H  HD22 B LEU   A 1 10  ? 5.149  -11.836 9.319   0.38 15.75 ?  10  LEU   A HD22 1 
ATOM   222  H  HD23 A LEU   A 1 10  ? 6.658  -12.533 7.823   0.62 18.07 ?  10  LEU   A HD23 1 
ATOM   223  H  HD23 B LEU   A 1 10  ? 6.424  -12.119 8.414   0.38 15.75 ?  10  LEU   A HD23 1 
ATOM   224  N  N    A LYS   A 1 11  ? 9.175  -14.668 11.537  0.62 11.56 ?  11  LYS   A N    1 
ATOM   225  N  N    B LYS   A 1 11  ? 9.280  -14.462 12.038  0.38 10.76 ?  11  LYS   A N    1 
ATOM   226  C  CA   A LYS   A 1 11  ? 10.181 -15.673 11.220  0.62 11.48 ?  11  LYS   A CA   1 
ATOM   227  C  CA   B LYS   A 1 11  ? 10.205 -15.487 11.576  0.38 11.07 ?  11  LYS   A CA   1 
ATOM   228  C  C    A LYS   A 1 11  ? 9.837  -16.288 9.871   0.62 11.65 ?  11  LYS   A C    1 
ATOM   229  C  C    B LYS   A 1 11  ? 9.780  -15.997 10.205  0.38 10.23 ?  11  LYS   A C    1 
ATOM   230  O  O    A LYS   A 1 11  ? 8.772  -16.888 9.722   0.62 12.90 ?  11  LYS   A O    1 
ATOM   231  O  O    B LYS   A 1 11  ? 8.637  -16.423 10.017  0.38 10.49 ?  11  LYS   A O    1 
ATOM   232  C  CB   A LYS   A 1 11  ? 10.206 -16.726 12.329  0.62 11.94 ?  11  LYS   A CB   1 
ATOM   233  C  CB   B LYS   A 1 11  ? 10.248 -16.638 12.580  0.38 11.77 ?  11  LYS   A CB   1 
ATOM   234  C  CG   A LYS   A 1 11  ? 11.229 -17.837 12.174  0.62 12.22 ?  11  LYS   A CG   1 
ATOM   235  C  CG   B LYS   A 1 11  ? 11.226 -17.755 12.225  0.38 12.35 ?  11  LYS   A CG   1 
ATOM   236  C  CD   A LYS   A 1 11  ? 11.331 -18.623 13.481  0.62 12.38 ?  11  LYS   A CD   1 
ATOM   237  C  CD   B LYS   A 1 11  ? 11.279 -18.798 13.340  0.38 13.01 ?  11  LYS   A CD   1 
ATOM   238  C  CE   A LYS   A 1 11  ? 12.299 -19.799 13.393  0.62 12.64 ?  11  LYS   A CE   1 
ATOM   239  C  CE   B LYS   A 1 11  ? 12.324 -19.888 13.093  0.38 13.26 ?  11  LYS   A CE   1 
ATOM   240  N  NZ   A LYS   A 1 11  ? 13.674 -19.360 13.035  0.62 13.27 ?  11  LYS   A NZ   1 
ATOM   241  N  NZ   B LYS   A 1 11  ? 13.713 -19.351 13.037  0.38 13.52 ?  11  LYS   A NZ   1 
ATOM   242  H  H    A LYS   A 1 11  ? 8.484  -14.991 11.951  0.62 13.85 ?  11  LYS   A H    1 
ATOM   243  H  H    B LYS   A 1 11  ? 8.750  -14.705 12.669  0.38 12.89 ?  11  LYS   A H    1 
ATOM   244  H  HA   A LYS   A 1 11  ? 11.051 -15.255 11.159  0.62 13.76 ?  11  LYS   A HA   1 
ATOM   245  H  HA   B LYS   A 1 11  ? 11.087 -15.100 11.496  0.38 13.27 ?  11  LYS   A HA   1 
ATOM   246  H  HB2  A LYS   A 1 11  ? 10.397 -16.273 13.167  0.62 14.31 ?  11  LYS   A HB2  1 
ATOM   247  H  HB2  B LYS   A 1 11  ? 10.507 -16.276 13.442  0.38 14.11 ?  11  LYS   A HB2  1 
ATOM   248  H  HB3  A LYS   A 1 11  ? 9.333  -17.139 12.378  0.62 14.31 ?  11  LYS   A HB3  1 
ATOM   249  H  HB3  B LYS   A 1 11  ? 9.361  -17.023 12.641  0.38 14.11 ?  11  LYS   A HB3  1 
ATOM   250  H  HG2  A LYS   A 1 11  ? 10.947 -18.443 11.471  0.62 14.65 ?  11  LYS   A HG2  1 
ATOM   251  H  HG2  B LYS   A 1 11  ? 10.934 -18.193 11.410  0.38 14.80 ?  11  LYS   A HG2  1 
ATOM   252  H  HG3  A LYS   A 1 11  ? 12.097 -17.459 11.975  0.62 14.65 ?  11  LYS   A HG3  1 
ATOM   253  H  HG3  B LYS   A 1 11  ? 12.113 -17.383 12.110  0.38 14.80 ?  11  LYS   A HG3  1 
ATOM   254  H  HD2  A LYS   A 1 11  ? 11.639 -18.033 14.186  0.62 14.84 ?  11  LYS   A HD2  1 
ATOM   255  H  HD2  B LYS   A 1 11  ? 11.498 -18.357 14.175  0.38 15.60 ?  11  LYS   A HD2  1 
ATOM   256  H  HD3  A LYS   A 1 11  ? 10.452 -18.977 13.709  0.62 14.84 ?  11  LYS   A HD3  1 
ATOM   257  H  HD3  B LYS   A 1 11  ? 10.411 -19.228 13.411  0.38 15.60 ?  11  LYS   A HD3  1 
ATOM   258  H  HE2  A LYS   A 1 11  ? 12.339 -20.248 14.254  0.62 15.15 ?  11  LYS   A HE2  1 
ATOM   259  H  HE2  B LYS   A 1 11  ? 12.283 -20.537 13.816  0.38 15.90 ?  11  LYS   A HE2  1 
ATOM   260  H  HE3  A LYS   A 1 11  ? 11.991 -20.417 12.711  0.62 15.15 ?  11  LYS   A HE3  1 
ATOM   261  H  HE3  B LYS   A 1 11  ? 12.136 -20.324 12.247  0.38 15.90 ?  11  LYS   A HE3  1 
ATOM   262  H  HZ1  A LYS   A 1 11  ? 14.200 -20.069 12.927  0.62 15.91 ?  11  LYS   A HZ1  1 
ATOM   263  H  HZ1  B LYS   A 1 11  ? 14.279 -19.995 12.797  0.38 16.21 ?  11  LYS   A HZ1  1 
ATOM   264  H  HZ2  A LYS   A 1 11  ? 13.655 -18.895 12.276  0.62 15.91 ?  11  LYS   A HZ2  1 
ATOM   265  H  HZ2  B LYS   A 1 11  ? 13.759 -18.690 12.443  0.38 16.21 ?  11  LYS   A HZ2  1 
ATOM   266  H  HZ3  A LYS   A 1 11  ? 14.008 -18.848 13.680  0.62 15.91 ?  11  LYS   A HZ3  1 
ATOM   267  H  HZ3  B LYS   A 1 11  ? 13.951 -19.040 13.836  0.38 16.21 ?  11  LYS   A HZ3  1 
ATOM   268  N  N    A LEU   A 1 12  ? 10.718 -16.135 8.885   0.62 11.02 ?  12  LEU   A N    1 
ATOM   269  N  N    B LEU   A 1 12  ? 10.695 -15.946 9.240   0.38 10.74 ?  12  LEU   A N    1 
ATOM   270  C  CA   A LEU   A 1 12  ? 10.464 -16.735 7.578   0.62 10.92 ?  12  LEU   A CA   1 
ATOM   271  C  CA   B LEU   A 1 12  ? 10.428 -16.445 7.895   0.38 11.12 ?  12  LEU   A CA   1 
ATOM   272  C  C    A LEU   A 1 12  ? 11.079 -18.121 7.452   0.62 10.96 ?  12  LEU   A C    1 
ATOM   273  C  C    B LEU   A 1 12  ? 10.981 -17.844 7.652   0.38 11.38 ?  12  LEU   A C    1 
ATOM   274  O  O    A LEU   A 1 12  ? 10.475 -19.010 6.846   0.62 11.29 ?  12  LEU   A O    1 
ATOM   275  O  O    B LEU   A 1 12  ? 10.292 -18.685 7.062   0.38 11.17 ?  12  LEU   A O    1 
ATOM   276  C  CB   A LEU   A 1 12  ? 10.996 -15.845 6.452   0.62 10.96 ?  12  LEU   A CB   1 
ATOM   277  C  CB   B LEU   A 1 12  ? 10.992 -15.481 6.843   0.38 11.42 ?  12  LEU   A CB   1 
ATOM   278  C  CG   A LEU   A 1 12  ? 10.357 -14.469 6.274   0.62 12.19 ?  12  LEU   A CG   1 
ATOM   279  C  CG   B LEU   A 1 12  ? 10.293 -14.124 6.741   0.38 12.07 ?  12  LEU   A CG   1 
ATOM   280  C  CD1  A LEU   A 1 12  ? 11.106 -13.702 5.208   0.62 12.66 ?  12  LEU   A CD1  1 
ATOM   281  C  CD1  B LEU   A 1 12  ? 10.835 -13.341 5.553   0.38 12.58 ?  12  LEU   A CD1  1 
ATOM   282  C  CD2  A LEU   A 1 12  ? 8.877  -14.597 5.915   0.62 12.53 ?  12  LEU   A CD2  1 
ATOM   283  C  CD2  B LEU   A 1 12  ? 8.783  -14.305 6.629   0.38 12.48 ?  12  LEU   A CD2  1 
ATOM   284  H  H    A LEU   A 1 12  ? 11.454 -15.685 8.939   0.62 13.21 ?  12  LEU   A H    1 
ATOM   285  H  H    B LEU   A 1 12  ? 11.480 -15.602 9.340   0.38 12.87 ?  12  LEU   A H    1 
ATOM   286  H  HA   A LEU   A 1 12  ? 9.507  -16.827 7.458   0.62 13.08 ?  12  LEU   A HA   1 
ATOM   287  H  HA   B LEU   A 1 12  ? 9.469  -16.488 7.768   0.38 13.32 ?  12  LEU   A HA   1 
ATOM   288  H  HB2  A LEU   A 1 12  ? 11.941 -15.704 6.599   0.62 13.13 ?  12  LEU   A HB2  1 
ATOM   289  H  HB2  B LEU   A 1 12  ? 11.926 -15.307 7.049   0.38 13.69 ?  12  LEU   A HB2  1 
ATOM   290  H  HB3  A LEU   A 1 12  ? 10.873 -16.323 5.613   0.62 13.13 ?  12  LEU   A HB3  1 
ATOM   291  H  HB3  B LEU   A 1 12  ? 10.928 -15.900 5.972   0.38 13.69 ?  12  LEU   A HB3  1 
ATOM   292  H  HG   A LEU   A 1 12  ? 10.425 -13.978 7.106   0.62 14.62 ?  12  LEU   A HG   1 
ATOM   293  H  HG   B LEU   A 1 12  ? 10.478 -13.609 7.545   0.38 14.46 ?  12  LEU   A HG   1 
ATOM   294  H  HD11 A LEU   A 1 12  ? 10.697 -12.831 5.099   0.62 15.17 ?  12  LEU   A HD11 1 
ATOM   295  H  HD11 B LEU   A 1 12  ? 10.385 -12.481 5.508   0.38 15.08 ?  12  LEU   A HD11 1 
ATOM   296  H  HD12 A LEU   A 1 12  ? 12.032 -13.601 5.485   0.62 15.17 ?  12  LEU   A HD12 1 
ATOM   297  H  HD12 B LEU   A 1 12  ? 11.789 -13.207 5.668   0.38 15.08 ?  12  LEU   A HD12 1 
ATOM   298  H  HD13 A LEU   A 1 12  ? 11.064 -14.197 4.374   0.62 15.17 ?  12  LEU   A HD13 1 
ATOM   299  H  HD13 B LEU   A 1 12  ? 10.667 -13.844 4.741   0.38 15.08 ?  12  LEU   A HD13 1 
ATOM   300  H  HD21 A LEU   A 1 12  ? 8.514  -13.715 5.741   0.62 15.02 ?  12  LEU   A HD21 1 
ATOM   301  H  HD21 B LEU   A 1 12  ? 8.389  -13.485 6.299   0.38 14.96 ?  12  LEU   A HD21 1 
ATOM   302  H  HD22 A LEU   A 1 12  ? 8.789  -15.151 5.121   0.62 15.02 ?  12  LEU   A HD22 1 
ATOM   303  H  HD22 B LEU   A 1 12  ? 8.600  -15.033 6.016   0.38 14.96 ?  12  LEU   A HD22 1 
ATOM   304  H  HD23 A LEU   A 1 12  ? 8.403  -15.009 6.655   0.62 15.02 ?  12  LEU   A HD23 1 
ATOM   305  H  HD23 B LEU   A 1 12  ? 8.426  -14.515 7.508   0.38 14.96 ?  12  LEU   A HD23 1 
ATOM   306  N  N    A THR   A 1 13  ? 12.284 -18.299 7.988   0.62 11.27 ?  13  THR   A N    1 
ATOM   307  N  N    B THR   A 1 13  ? 12.212 -18.111 8.078   0.38 11.76 ?  13  THR   A N    1 
ATOM   308  C  CA   A THR   A 1 13  ? 13.004 -19.564 7.948   0.62 11.66 ?  13  THR   A CA   1 
ATOM   309  C  CA   B THR   A 1 13  ? 12.849 -19.408 7.884   0.38 12.06 ?  13  THR   A CA   1 
ATOM   310  C  C    A THR   A 1 13  ? 13.752 -19.729 9.266   0.62 11.67 ?  13  THR   A C    1 
ATOM   311  C  C    B THR   A 1 13  ? 13.653 -19.736 9.136   0.38 12.30 ?  13  THR   A C    1 
ATOM   312  O  O    A THR   A 1 13  ? 13.644 -18.909 10.182  0.62 12.23 ?  13  THR   A O    1 
ATOM   313  O  O    B THR   A 1 13  ? 13.565 -19.052 10.160  0.38 12.52 ?  13  THR   A O    1 
ATOM   314  C  CB   A THR   A 1 13  ? 13.994 -19.625 6.776   0.62 12.35 ?  13  THR   A CB   1 
ATOM   315  C  CB   B THR   A 1 13  ? 13.774 -19.397 6.661   0.38 12.10 ?  13  THR   A CB   1 
ATOM   316  O  OG1  A THR   A 1 13  ? 15.068 -18.716 7.033   0.62 12.35 ?  13  THR   A OG1  1 
ATOM   317  O  OG1  B THR   A 1 13  ? 14.825 -18.451 6.882   0.38 12.10 ?  13  THR   A OG1  1 
ATOM   318  C  CG2  A THR   A 1 13  ? 13.339 -19.272 5.445   0.62 12.98 ?  13  THR   A CG2  1 
ATOM   319  C  CG2  B THR   A 1 13  ? 13.024 -19.045 5.382   0.38 12.73 ?  13  THR   A CG2  1 
ATOM   320  H  H    A THR   A 1 13  ? 12.722 -17.672 8.380   0.62 13.51 ?  13  THR   A H    1 
ATOM   321  H  H    B THR   A 1 13  ? 12.708 -17.536 8.483   0.38 14.10 ?  13  THR   A H    1 
ATOM   322  H  HA   A THR   A 1 13  ? 12.379 -20.292 7.856   0.62 13.97 ?  13  THR   A HA   1 
ATOM   323  H  HA   B THR   A 1 13  ? 12.171 -20.091 7.759   0.38 14.45 ?  13  THR   A HA   1 
ATOM   324  H  HB   A THR   A 1 13  ? 14.349 -20.528 6.700   0.62 14.81 ?  13  THR   A HB   1 
ATOM   325  H  HB   B THR   A 1 13  ? 14.159 -20.278 6.546   0.38 14.51 ?  13  THR   A HB   1 
ATOM   326  H  HG1  A THR   A 1 13  ? 15.682 -19.109 7.452   0.62 14.80 ?  13  THR   A HG1  1 
ATOM   327  H  HG1  B THR   A 1 13  ? 15.347 -18.439 6.224   0.38 14.50 ?  13  THR   A HG1  1 
ATOM   328  H  HG21 A THR   A 1 13  ? 13.966 -19.416 4.715   0.62 15.56 ?  13  THR   A HG21 1 
ATOM   329  H  HG21 B THR   A 1 13  ? 13.623 -19.119 4.619   0.38 15.26 ?  13  THR   A HG21 1 
ATOM   330  H  HG22 A THR   A 1 13  ? 12.560 -19.831 5.301   0.62 15.56 ?  13  THR   A HG22 1 
ATOM   331  H  HG22 B THR   A 1 13  ? 12.282 -19.656 5.256   0.38 15.26 ?  13  THR   A HG22 1 
ATOM   332  H  HG23 A THR   A 1 13  ? 13.067 -18.343 5.444   0.62 15.56 ?  13  THR   A HG23 1 
ATOM   333  H  HG23 B THR   A 1 13  ? 12.687 -18.140 5.430   0.38 15.26 ?  13  THR   A HG23 1 
ATOM   334  N  N    A ASP   A 1 14  ? 14.558 -20.785 9.338   0.62 11.86 ?  14  ASP   A N    1 
ATOM   335  N  N    B ASP   A 1 14  ? 14.476 -20.781 9.041   0.38 12.72 ?  14  ASP   A N    1 
ATOM   336  C  CA   A ASP   A 1 14  ? 15.385 -21.018 10.512  0.62 12.55 ?  14  ASP   A CA   1 
ATOM   337  C  CA   B ASP   A 1 14  ? 15.346 -21.124 10.158  0.38 12.71 ?  14  ASP   A CA   1 
ATOM   338  C  C    A ASP   A 1 14  ? 16.181 -19.780 10.912  0.62 12.07 ?  14  ASP   A C    1 
ATOM   339  C  C    B ASP   A 1 14  ? 16.236 -19.954 10.557  0.38 11.22 ?  14  ASP   A C    1 
ATOM   340  O  O    A ASP   A 1 14  ? 16.354 -19.510 12.105  0.62 12.76 ?  14  ASP   A O    1 
ATOM   341  O  O    B ASP   A 1 14  ? 16.557 -19.800 11.741  0.38 11.18 ?  14  ASP   A O    1 
ATOM   342  C  CB   A ASP   A 1 14  ? 16.343 -22.169 10.230  0.62 14.80 ?  14  ASP   A CB   1 
ATOM   343  C  CB   B ASP   A 1 14  ? 16.202 -22.342 9.803   0.38 15.03 ?  14  ASP   A CB   1 
ATOM   344  C  CG   A ASP   A 1 14  ? 17.251 -22.450 11.402  0.62 18.63 ?  14  ASP   A CG   1 
ATOM   345  C  CG   B ASP   A 1 14  ? 17.142 -22.742 10.921  0.38 17.29 ?  14  ASP   A CG   1 
ATOM   346  O  OD1  A ASP   A 1 14  ? 16.740 -22.865 12.465  0.62 19.87 ?  14  ASP   A OD1  1 
ATOM   347  O  OD1  B ASP   A 1 14  ? 16.652 -23.207 11.974  0.38 18.23 ?  14  ASP   A OD1  1 
ATOM   348  O  OD2  A ASP   A 1 14  ? 18.468 -22.219 11.265  0.62 21.28 -1 14  ASP   A OD2  1 
ATOM   349  O  OD2  B ASP   A 1 14  ? 18.368 -22.607 10.744  0.38 18.60 -1 14  ASP   A OD2  1 
ATOM   350  H  H    A ASP   A 1 14  ? 14.647 -21.372 8.725   0.62 14.22 ?  14  ASP   A H    1 
ATOM   351  H  H    B ASP   A 1 14  ? 14.551 -21.290 8.350   0.38 15.25 ?  14  ASP   A H    1 
ATOM   352  H  HA   A ASP   A 1 14  ? 14.822 -21.274 11.262  0.62 15.04 ?  14  ASP   A HA   1 
ATOM   353  H  HA   B ASP   A 1 14  ? 14.800 -21.360 10.920  0.38 15.23 ?  14  ASP   A HA   1 
ATOM   354  H  HB2  A ASP   A 1 14  ? 15.822 -22.968 10.019  0.62 17.74 ?  14  ASP   A HB2  1 
ATOM   355  H  HB2  B ASP   A 1 14  ? 15.623 -23.105 9.641   0.38 18.02 ?  14  ASP   A HB2  1 
ATOM   356  H  HB3  A ASP   A 1 14  ? 16.902 -21.941 9.469   0.62 17.74 ?  14  ASP   A HB3  1 
ATOM   357  H  HB3  B ASP   A 1 14  ? 16.725 -22.147 9.010   0.38 18.02 ?  14  ASP   A HB3  1 
ATOM   358  N  N    A ASN   A 1 15  ? 16.678 -19.015 9.933   0.62 11.90 ?  15  ASN   A N    1 
ATOM   359  N  N    B ASN   A 1 15  ? 16.636 -19.111 9.595   0.38 10.39 ?  15  ASN   A N    1 
ATOM   360  C  CA   A ASN   A 1 15  ? 17.651 -17.961 10.207  0.62 12.23 ?  15  ASN   A CA   1 
ATOM   361  C  CA   B ASN   A 1 15  ? 17.650 -18.092 9.855   0.38 10.73 ?  15  ASN   A CA   1 
ATOM   362  C  C    A ASN   A 1 15  ? 17.268 -16.579 9.700   0.62 12.13 ?  15  ASN   A C    1 
ATOM   363  C  C    B ASN   A 1 15  ? 17.303 -16.699 9.328   0.38 11.21 ?  15  ASN   A C    1 
ATOM   364  O  O    A ASN   A 1 15  ? 17.995 -15.629 10.003  0.62 11.44 ?  15  ASN   A O    1 
ATOM   365  O  O    B ASN   A 1 15  ? 18.166 -15.812 9.368   0.38 11.43 ?  15  ASN   A O    1 
ATOM   366  C  CB   A ASN   A 1 15  ? 19.026 -18.312 9.608   0.62 12.20 ?  15  ASN   A CB   1 
ATOM   367  C  CB   B ASN   A 1 15  ? 19.012 -18.538 9.298   0.38 10.44 ?  15  ASN   A CB   1 
ATOM   368  C  CG   A ASN   A 1 15  ? 18.987 -18.454 8.100   0.62 12.39 ?  15  ASN   A CG   1 
ATOM   369  C  CG   B ASN   A 1 15  ? 19.033 -18.571 7.789   0.38 11.13 ?  15  ASN   A CG   1 
ATOM   370  O  OD1  A ASN   A 1 15  ? 18.233 -19.268 7.561   0.62 12.90 ?  15  ASN   A OD1  1 
ATOM   371  O  OD1  B ASN   A 1 15  ? 18.350 -19.382 7.160   0.38 11.38 ?  15  ASN   A OD1  1 
ATOM   372  N  ND2  A ASN   A 1 15  ? 19.779 -17.637 7.404   0.62 12.74 ?  15  ASN   A ND2  1 
ATOM   373  N  ND2  B ASN   A 1 15  ? 19.814 -17.680 7.195   0.38 11.52 ?  15  ASN   A ND2  1 
ATOM   374  H  H    A ASN   A 1 15  ? 16.465 -19.084 9.109   0.62 14.26 ?  15  ASN   A H    1 
ATOM   375  H  H    B ASN   A 1 15  ? 16.336 -19.127 8.788   0.38 12.45 ?  15  ASN   A H    1 
ATOM   376  H  HA   A ASN   A 1 15  ? 17.771 -17.900 11.171  0.62 14.66 ?  15  ASN   A HA   1 
ATOM   377  H  HA   B ASN   A 1 15  ? 17.750 -18.015 10.811  0.38 12.86 ?  15  ASN   A HA   1 
ATOM   378  H  HB2  A ASN   A 1 15  ? 19.656 -17.603 9.831   0.62 14.63 ?  15  ASN   A HB2  1 
ATOM   379  H  HB2  B ASN   A 1 15  ? 19.696 -17.916 9.599   0.38 12.51 ?  15  ASN   A HB2  1 
ATOM   380  H  HB3  A ASN   A 1 15  ? 19.330 -19.151 9.984   0.62 14.63 ?  15  ASN   A HB3  1 
ATOM   381  H  HB3  B ASN   A 1 15  ? 19.219 -19.433 9.624   0.38 12.51 ?  15  ASN   A HB3  1 
ATOM   382  H  HD21 A ASN   A 1 15  ? 19.798 -17.673 6.541   0.62 15.28 ?  15  ASN   A HD21 1 
ATOM   383  H  HD21 B ASN   A 1 15  ? 19.862 -17.654 6.339   0.38 13.80 ?  15  ASN   A HD21 1 
ATOM   384  H  HD22 A ASN   A 1 15  ? 20.286 -17.068 7.811   0.62 15.28 ?  15  ASN   A HD22 1 
ATOM   385  H  HD22 B ASN   A 1 15  ? 20.277 -17.126 7.668   0.38 13.80 ?  15  ASN   A HD22 1 
ATOM   386  N  N    A VAL   A 1 16  ? 16.187 -16.433 8.935   0.62 12.56 ?  16  VAL   A N    1 
ATOM   387  N  N    B VAL   A 1 16  ? 16.075 -16.465 8.863   0.38 11.49 ?  16  VAL   A N    1 
ATOM   388  C  CA   A VAL   A 1 16  ? 15.778 -15.153 8.368   0.62 12.22 ?  16  VAL   A CA   1 
ATOM   389  C  CA   B VAL   A 1 16  ? 15.689 -15.187 8.269   0.38 11.35 ?  16  VAL   A CA   1 
ATOM   390  C  C    A VAL   A 1 16  ? 14.494 -14.680 9.033   0.62 11.93 ?  16  VAL   A C    1 
ATOM   391  C  C    B VAL   A 1 16  ? 14.431 -14.661 8.954   0.38 11.20 ?  16  VAL   A C    1 
ATOM   392  O  O    A VAL   A 1 16  ? 13.514 -15.431 9.144   0.62 12.22 ?  16  VAL   A O    1 
ATOM   393  O  O    B VAL   A 1 16  ? 13.412 -15.360 9.023   0.38 11.05 ?  16  VAL   A O    1 
ATOM   394  C  CB   A VAL   A 1 16  ? 15.619 -15.212 6.840   0.62 12.52 ?  16  VAL   A CB   1 
ATOM   395  C  CB   B VAL   A 1 16  ? 15.476 -15.304 6.748   0.38 12.04 ?  16  VAL   A CB   1 
ATOM   396  C  CG1  A VAL   A 1 16  ? 15.196 -13.837 6.298   0.62 13.19 ?  16  VAL   A CG1  1 
ATOM   397  C  CG1  B VAL   A 1 16  ? 15.023 -13.968 6.172   0.38 12.65 ?  16  VAL   A CG1  1 
ATOM   398  C  CG2  A VAL   A 1 16  ? 16.909 -15.668 6.182   0.62 13.08 ?  16  VAL   A CG2  1 
ATOM   399  C  CG2  B VAL   A 1 16  ? 16.751 -15.782 6.053   0.38 12.43 ?  16  VAL   A CG2  1 
ATOM   400  H  H    A VAL   A 1 16  ? 15.671 -17.084 8.729   0.62 15.06 ?  16  VAL   A H    1 
ATOM   401  H  H    B VAL   A 1 16  ? 15.439 -17.043 8.886   0.38 13.77 ?  16  VAL   A H    1 
ATOM   402  H  HA   A VAL   A 1 16  ? 16.467 -14.497 8.565   0.62 14.65 ?  16  VAL   A HA   1 
ATOM   403  H  HA   B VAL   A 1 16  ? 16.403 -14.547 8.419   0.38 13.61 ?  16  VAL   A HA   1 
ATOM   404  H  HB   A VAL   A 1 16  ? 14.925 -15.850 6.621   0.62 15.01 ?  16  VAL   A HB   1 
ATOM   405  H  HB   B VAL   A 1 16  ? 14.783 -15.957 6.576   0.38 14.43 ?  16  VAL   A HB   1 
ATOM   406  H  HG11 A VAL   A 1 16  ? 15.276 -13.844 5.332   0.62 15.81 ?  16  VAL   A HG11 1 
ATOM   407  H  HG11 B VAL   A 1 16  ? 15.108 -13.999 5.207   0.38 15.16 ?  16  VAL   A HG11 1 
ATOM   408  H  HG12 A VAL   A 1 16  ? 14.273 -13.667 6.549   0.62 15.81 ?  16  VAL   A HG12 1 
ATOM   409  H  HG12 B VAL   A 1 16  ? 14.098 -13.817 6.418   0.38 15.16 ?  16  VAL   A HG12 1 
ATOM   410  H  HG13 A VAL   A 1 16  ? 15.773 -13.156 6.674   0.62 15.81 ?  16  VAL   A HG13 1 
ATOM   411  H  HG13 B VAL   A 1 16  ? 15.585 -13.264 6.531   0.38 15.16 ?  16  VAL   A HG13 1 
ATOM   412  H  HG21 A VAL   A 1 16  ? 16.864 -15.473 5.234   0.62 15.68 ?  16  VAL   A HG21 1 
ATOM   413  H  HG21 B VAL   A 1 16  ? 16.603 -15.792 5.094   0.38 14.90 ?  16  VAL   A HG21 1 
ATOM   414  H  HG22 A VAL   A 1 16  ? 17.652 -15.196 6.584   0.62 15.68 ?  16  VAL   A HG22 1 
ATOM   415  H  HG22 B VAL   A 1 16  ? 17.476 -15.174 6.268   0.38 14.90 ?  16  VAL   A HG22 1 
ATOM   416  H  HG23 A VAL   A 1 16  ? 17.009 -16.621 6.322   0.62 15.68 ?  16  VAL   A HG23 1 
ATOM   417  H  HG23 B VAL   A 1 16  ? 16.966 -16.675 6.363   0.38 14.90 ?  16  VAL   A HG23 1 
ATOM   418  N  N    . TYR   A 1 17  ? 14.503 -13.410 9.424   1.00 11.54 ?  17  TYR   A N    1 
ATOM   419  C  CA   . TYR   A 1 17  ? 13.422 -12.730 10.125  1.00 11.23 ?  17  TYR   A CA   1 
ATOM   420  C  C    . TYR   A 1 17  ? 13.155 -11.400 9.422   1.00 11.60 ?  17  TYR   A C    1 
ATOM   421  O  O    . TYR   A 1 17  ? 14.060 -10.842 8.801   1.00 12.17 ?  17  TYR   A O    1 
ATOM   422  C  CB   . TYR   A 1 17  ? 13.865 -12.465 11.567  1.00 12.21 ?  17  TYR   A CB   1 
ATOM   423  C  CG   . TYR   A 1 17  ? 14.068 -13.729 12.372  1.00 13.13 ?  17  TYR   A CG   1 
ATOM   424  C  CD1  . TYR   A 1 17  ? 15.239 -14.478 12.268  1.00 14.35 ?  17  TYR   A CD1  1 
ATOM   425  C  CD2  . TYR   A 1 17  ? 13.076 -14.186 13.223  1.00 13.56 ?  17  TYR   A CD2  1 
ATOM   426  C  CE1  . TYR   A 1 17  ? 15.407 -15.652 12.996  1.00 14.90 ?  17  TYR   A CE1  1 
ATOM   427  C  CE2  . TYR   A 1 17  ? 13.234 -15.358 13.951  1.00 14.52 ?  17  TYR   A CE2  1 
ATOM   428  C  CZ   . TYR   A 1 17  ? 14.401 -16.089 13.841  1.00 14.81 ?  17  TYR   A CZ   1 
ATOM   429  O  OH   . TYR   A 1 17  ? 14.552 -17.248 14.576  1.00 15.77 ?  17  TYR   A OH   1 
ATOM   430  H  H    A TYR   A 1 17  ? 15.174 -12.886 9.280   0.62 13.83 ?  17  TYR   A H    1 
ATOM   431  H  H    B TYR   A 1 17  ? 15.203 -12.913 9.334   0.38 13.83 ?  17  TYR   A H    1 
ATOM   432  H  HA   . TYR   A 1 17  ? 12.617 -13.275 10.116  1.00 13.45 ?  17  TYR   A HA   1 
ATOM   433  H  HB2  . TYR   A 1 17  ? 14.700 -11.979 11.546  1.00 14.64 ?  17  TYR   A HB2  1 
ATOM   434  H  HB3  . TYR   A 1 17  ? 13.185 -11.939 12.003  1.00 14.64 ?  17  TYR   A HB3  1 
ATOM   435  H  HD1  . TYR   A 1 17  ? 15.919 -14.192 11.692  1.00 17.20 ?  17  TYR   A HD1  1 
ATOM   436  H  HD2  . TYR   A 1 17  ? 12.286 -13.703 13.299  1.00 16.25 ?  17  TYR   A HD2  1 
ATOM   437  H  HE1  . TYR   A 1 17  ? 16.198 -16.142 12.918  1.00 17.86 ?  17  TYR   A HE1  1 
ATOM   438  H  HE2  . TYR   A 1 17  ? 12.558 -15.640 14.520  1.00 17.41 ?  17  TYR   A HE2  1 
ATOM   439  H  HH   . TYR   A 1 17  ? 13.806 -17.472 14.898  1.00 18.91 ?  17  TYR   A HH   1 
ATOM   440  N  N    A ILE   A 1 18  ? 11.905 -10.925 9.455   0.62 11.55 ?  18  ILE   A N    1 
ATOM   441  N  N    B ILE   A 1 18  ? 11.948 -10.843 9.604   0.38 11.01 ?  18  ILE   A N    1 
ATOM   442  C  CA   A ILE   A 1 18  ? 11.518 -9.757  8.667   0.62 11.52 ?  18  ILE   A CA   1 
ATOM   443  C  CA   B ILE   A 1 18  ? 11.557 -9.622  8.897   0.38 10.30 ?  18  ILE   A CA   1 
ATOM   444  C  C    A ILE   A 1 18  ? 10.530 -8.887  9.438   0.62 12.01 ?  18  ILE   A C    1 
ATOM   445  C  C    B ILE   A 1 18  ? 10.645 -8.753  9.759   0.38 9.82  ?  18  ILE   A C    1 
ATOM   446  O  O    A ILE   A 1 18  ? 9.695  -9.384  10.199  0.62 12.19 ?  18  ILE   A O    1 
ATOM   447  O  O    B ILE   A 1 18  ? 9.852  -9.253  10.564  0.38 10.20 ?  18  ILE   A O    1 
ATOM   448  C  CB   A ILE   A 1 18  ? 10.989 -10.182 7.275   0.62 11.20 ?  18  ILE   A CB   1 
ATOM   449  C  CB   B ILE   A 1 18  ? 10.898 -9.972  7.546   0.38 10.07 ?  18  ILE   A CB   1 
ATOM   450  C  CG1  A ILE   A 1 18  ? 10.958 -8.999  6.308   0.62 11.18 ?  18  ILE   A CG1  1 
ATOM   451  C  CG1  B ILE   A 1 18  ? 10.866 -8.762  6.612   0.38 11.09 ?  18  ILE   A CG1  1 
ATOM   452  C  CG2  A ILE   A 1 18  ? 9.631  -10.882 7.383   0.62 11.11 ?  18  ILE   A CG2  1 
ATOM   453  C  CG2  B ILE   A 1 18  ? 9.507  -10.556 7.760   0.38 10.49 ?  18  ILE   A CG2  1 
ATOM   454  C  CD1  A ILE   A 1 18  ? 10.769 -9.430  4.883   0.62 12.04 ?  18  ILE   A CD1  1 
ATOM   455  C  CD1  B ILE   A 1 18  ? 10.478 -9.135  5.202   0.38 12.44 ?  18  ILE   A CD1  1 
ATOM   456  H  H    A ILE   A 1 18  ? 11.268 -11.279 9.913   0.62 13.85 ?  18  ILE   A H    1 
ATOM   457  H  H    B ILE   A 1 18  ? 11.347 -11.158 10.133  0.38 13.19 ?  18  ILE   A H    1 
ATOM   458  H  HA   A ILE   A 1 18  ? 12.316 -9.228  8.514   0.62 13.81 ?  18  ILE   A HA   1 
ATOM   459  H  HA   B ILE   A 1 18  ? 12.359 -9.109  8.717   0.38 12.34 ?  18  ILE   A HA   1 
ATOM   460  H  HB   A ILE   A 1 18  ? 11.615 -10.832 6.909   0.62 13.42 ?  18  ILE   A HB   1 
ATOM   461  H  HB   B ILE   A 1 18  ? 11.446 -10.647 7.134   0.38 12.07 ?  18  ILE   A HB   1 
ATOM   462  H  HG12 A ILE   A 1 18  ? 10.231 -8.410  6.547   0.62 13.40 ?  18  ILE   A HG12 1 
ATOM   463  H  HG12 B ILE   A 1 18  ? 10.223 -8.116  6.941   0.38 13.29 ?  18  ILE   A HG12 1 
ATOM   464  H  HG13 A ILE   A 1 18  ? 11.806 -8.523  6.363   0.62 13.40 ?  18  ILE   A HG13 1 
ATOM   465  H  HG13 B ILE   A 1 18  ? 11.752 -8.357  6.582   0.38 13.29 ?  18  ILE   A HG13 1 
ATOM   466  H  HG21 A ILE   A 1 18  ? 9.410  -11.280 6.522   0.62 13.31 ?  18  ILE   A HG21 1 
ATOM   467  H  HG21 B ILE   A 1 18  ? 9.206  -10.951 6.927   0.38 12.57 ?  18  ILE   A HG21 1 
ATOM   468  H  HG22 A ILE   A 1 18  ? 9.684  -11.573 8.059   0.62 13.31 ?  18  ILE   A HG22 1 
ATOM   469  H  HG22 B ILE   A 1 18  ? 9.550  -11.234 8.451   0.38 12.57 ?  18  ILE   A HG22 1 
ATOM   470  H  HG23 A ILE   A 1 18  ? 8.956  -10.229 7.624   0.62 13.31 ?  18  ILE   A HG23 1 
ATOM   471  H  HG23 B ILE   A 1 18  ? 8.898  -9.849  8.029   0.38 12.57 ?  18  ILE   A HG23 1 
ATOM   472  H  HD11 A ILE   A 1 18  ? 10.830 -8.648  4.308   0.62 14.43 ?  18  ILE   A HD11 1 
ATOM   473  H  HD11 B ILE   A 1 18  ? 10.667 -8.392  4.609   0.38 14.91 ?  18  ILE   A HD11 1 
ATOM   474  H  HD12 A ILE   A 1 18  ? 11.455 -10.069 4.649   0.62 14.43 ?  18  ILE   A HD12 1 
ATOM   475  H  HD12 B ILE   A 1 18  ? 10.994 -9.912  4.929   0.38 14.91 ?  18  ILE   A HD12 1 
ATOM   476  H  HD13 A ILE   A 1 18  ? 9.890  -9.834  4.793   0.62 14.43 ?  18  ILE   A HD13 1 
ATOM   477  H  HD13 B ILE   A 1 18  ? 9.532  -9.345  5.181   0.38 14.91 ?  18  ILE   A HD13 1 
ATOM   478  N  N    A LYS   A 1 19  ? 10.622 -7.574  9.220   0.62 12.37 ?  19  LYS   A N    1 
ATOM   479  N  N    B LYS   A 1 19  ? 10.743 -7.434  9.555   0.38 9.83  ?  19  LYS   A N    1 
ATOM   480  C  CA   A LYS   A 1 19  ? 9.816  -6.607  9.955   0.62 13.01 ?  19  LYS   A CA   1 
ATOM   481  C  CA   B LYS   A 1 19  ? 9.939  -6.469  10.293  0.38 11.10 ?  19  LYS   A CA   1 
ATOM   482  C  C    A LYS   A 1 19  ? 9.639  -5.358  9.108   0.62 12.82 ?  19  LYS   A C    1 
ATOM   483  C  C    B LYS   A 1 19  ? 9.744  -5.223  9.438   0.38 11.20 ?  19  LYS   A C    1 
ATOM   484  O  O    A LYS   A 1 19  ? 10.521 -5.002  8.322   0.62 12.11 ?  19  LYS   A O    1 
ATOM   485  O  O    B LYS   A 1 19  ? 10.669 -4.799  8.742   0.38 11.01 ?  19  LYS   A O    1 
ATOM   486  C  CB   A LYS   A 1 19  ? 10.538 -6.220  11.252  0.62 14.39 ?  19  LYS   A CB   1 
ATOM   487  C  CB   B LYS   A 1 19  ? 10.634 -6.097  11.609  0.38 12.30 ?  19  LYS   A CB   1 
ATOM   488  C  CG   A LYS   A 1 19  ? 9.814  -5.258  12.193  0.62 15.90 ?  19  LYS   A CG   1 
ATOM   489  C  CG   B LYS   A 1 19  ? 9.832  -5.196  12.511  0.38 13.64 ?  19  LYS   A CG   1 
ATOM   490  C  CD   A LYS   A 1 19  ? 10.698 -5.013  13.420  0.62 17.14 ?  19  LYS   A CD   1 
ATOM   491  C  CD   B LYS   A 1 19  ? 10.644 -4.825  13.725  0.38 15.31 ?  19  LYS   A CD   1 
ATOM   492  C  CE   A LYS   A 1 19  ? 10.079 -4.083  14.453  0.62 18.09 ?  19  LYS   A CE   1 
ATOM   493  C  CE   B LYS   A 1 19  ? 9.850  -3.949  14.661  0.38 16.40 ?  19  LYS   A CE   1 
ATOM   494  N  NZ   A LYS   A 1 19  ? 11.005 -3.893  15.616  0.62 18.06 ?  19  LYS   A NZ   1 
ATOM   495  N  NZ   B LYS   A 1 19  ? 10.698 -3.484  15.780  0.38 16.80 ?  19  LYS   A NZ   1 
ATOM   496  H  H    A LYS   A 1 19  ? 11.151 -7.224  8.640   0.62 14.83 ?  19  LYS   A H    1 
ATOM   497  H  H    B LYS   A 1 19  ? 11.281 -7.058  8.983   0.38 11.78 ?  19  LYS   A H    1 
ATOM   498  H  HA   A LYS   A 1 19  ? 8.946  -6.991  10.163  0.62 15.60 ?  19  LYS   A HA   1 
ATOM   499  H  HA   B LYS   A 1 19  ? 9.072  -6.846  10.500  0.38 13.30 ?  19  LYS   A HA   1 
ATOM   500  H  HB2  A LYS   A 1 19  ? 10.709 -7.033  11.750  0.62 17.25 ?  19  LYS   A HB2  1 
ATOM   501  H  HB2  B LYS   A 1 19  ? 10.813 -6.912  12.111  0.38 14.74 ?  19  LYS   A HB2  1 
ATOM   502  H  HB3  A LYS   A 1 19  ? 11.378 -5.808  11.009  0.62 17.25 ?  19  LYS   A HB3  1 
ATOM   503  H  HB3  B LYS   A 1 19  ? 11.470 -5.646  11.416  0.38 14.74 ?  19  LYS   A HB3  1 
ATOM   504  H  HG2  A LYS   A 1 19  ? 9.659  -4.410  11.746  0.62 19.06 ?  19  LYS   A HG2  1 
ATOM   505  H  HG2  B LYS   A 1 19  ? 9.602  -4.383  12.039  0.38 16.36 ?  19  LYS   A HG2  1 
ATOM   506  H  HG3  A LYS   A 1 19  ? 8.974  -5.649  12.486  0.62 19.06 ?  19  LYS   A HG3  1 
ATOM   507  H  HG3  B LYS   A 1 19  ? 9.033  -5.660  12.807  0.38 16.36 ?  19  LYS   A HG3  1 
ATOM   508  H  HD2  A LYS   A 1 19  ? 10.871 -5.862  13.857  0.62 20.55 ?  19  LYS   A HD2  1 
ATOM   509  H  HD2  B LYS   A 1 19  ? 10.897 -5.634  14.201  0.38 18.36 ?  19  LYS   A HD2  1 
ATOM   510  H  HD3  A LYS   A 1 19  ? 11.534 -4.616  13.131  0.62 20.55 ?  19  LYS   A HD3  1 
ATOM   511  H  HD3  B LYS   A 1 19  ? 11.437 -4.340  13.445  0.38 18.36 ?  19  LYS   A HD3  1 
ATOM   512  H  HE2  A LYS   A 1 19  ? 9.914  -3.214  14.053  0.62 21.69 ?  19  LYS   A HE2  1 
ATOM   513  H  HE2  B LYS   A 1 19  ? 9.526  -3.175  14.175  0.38 19.67 ?  19  LYS   A HE2  1 
ATOM   514  H  HE3  A LYS   A 1 19  ? 9.251  -4.465  14.785  0.62 21.69 ?  19  LYS   A HE3  1 
ATOM   515  H  HE3  B LYS   A 1 19  ? 9.108  -4.458  15.024  0.38 19.67 ?  19  LYS   A HE3  1 
ATOM   516  H  HZ1  A LYS   A 1 19  ? 10.642 -3.339  16.211  0.62 21.66 ?  19  LYS   A HZ1  1 
ATOM   517  H  HZ1  B LYS   A 1 19  ? 10.223 -2.969  16.325  0.38 20.15 ?  19  LYS   A HZ1  1 
ATOM   518  H  HZ2  A LYS   A 1 19  ? 11.163 -4.676  16.010  0.62 21.66 ?  19  LYS   A HZ2  1 
ATOM   519  H  HZ2  B LYS   A 1 19  ? 11.007 -4.184  16.235  0.38 20.15 ?  19  LYS   A HZ2  1 
ATOM   520  H  HZ3  A LYS   A 1 19  ? 11.777 -3.550  15.337  0.62 21.66 ?  19  LYS   A HZ3  1 
ATOM   521  H  HZ3  B LYS   A 1 19  ? 11.387 -3.018  15.464  0.38 20.15 ?  19  LYS   A HZ3  1 
ATOM   522  N  N    A ASN   A 1 20  ? 8.497  -4.689  9.276   0.62 13.71 ?  20  ASN   A N    1 
ATOM   523  N  N    B ASN   A 1 20  ? 8.539  -4.646  9.482   0.38 11.88 ?  20  ASN   A N    1 
ATOM   524  C  CA   A ASN   A 1 20  ? 8.318  -3.346  8.731   0.62 14.89 ?  20  ASN   A CA   1 
ATOM   525  C  CA   B ASN   A 1 20  ? 8.244  -3.375  8.810   0.38 12.78 ?  20  ASN   A CA   1 
ATOM   526  C  C    A ASN   A 1 20  ? 8.967  -2.367  9.700   0.62 15.29 ?  20  ASN   A C    1 
ATOM   527  C  C    B ASN   A 1 20  ? 8.821  -2.248  9.657   0.38 13.50 ?  20  ASN   A C    1 
ATOM   528  O  O    A ASN   A 1 20  ? 8.486  -2.183  10.823  0.62 15.46 ?  20  ASN   A O    1 
ATOM   529  O  O    B ASN   A 1 20  ? 8.176  -1.744  10.580  0.38 14.10 ?  20  ASN   A O    1 
ATOM   530  C  CB   A ASN   A 1 20  ? 6.835  -3.041  8.524   0.62 15.93 ?  20  ASN   A CB   1 
ATOM   531  C  CB   B ASN   A 1 20  ? 6.737  -3.204  8.630   0.38 13.18 ?  20  ASN   A CB   1 
ATOM   532  C  CG   A ASN   A 1 20  ? 6.571  -1.570  8.219   0.62 17.09 ?  20  ASN   A CG   1 
ATOM   533  C  CG   B ASN   A 1 20  ? 6.354  -1.888  7.932   0.38 13.40 ?  20  ASN   A CG   1 
ATOM   534  O  OD1  A ASN   A 1 20  ? 5.686  -0.959  8.811   0.62 19.19 ?  20  ASN   A OD1  1 
ATOM   535  O  OD1  B ASN   A 1 20  ? 5.231  -1.398  8.091   0.38 13.20 ?  20  ASN   A OD1  1 
ATOM   536  N  ND2  A ASN   A 1 20  ? 7.344  -1.000  7.301   0.62 17.00 ?  20  ASN   A ND2  1 
ATOM   537  N  ND2  B ASN   A 1 20  ? 7.273  -1.323  7.157   0.38 14.38 ?  20  ASN   A ND2  1 
ATOM   538  H  H    A ASN   A 1 20  ? 7.810  -5.000  9.698   0.62 16.44 ?  20  ASN   A H    1 
ATOM   539  H  H    B ASN   A 1 20  ? 7.862  -4.992  9.882   0.38 14.24 ?  20  ASN   A H    1 
ATOM   540  H  HA   A ASN   A 1 20  ? 8.766  -3.287  7.879   0.62 17.86 ?  20  ASN   A HA   1 
ATOM   541  H  HA   B ASN   A 1 20  ? 8.670  -3.366  7.938   0.38 15.32 ?  20  ASN   A HA   1 
ATOM   542  H  HB2  A ASN   A 1 20  ? 6.507  -3.567  7.776   0.62 19.10 ?  20  ASN   A HB2  1 
ATOM   543  H  HB2  B ASN   A 1 20  ? 6.394  -3.936  8.102   0.38 15.80 ?  20  ASN   A HB2  1 
ATOM   544  H  HB3  A ASN   A 1 20  ? 6.347  -3.274  9.329   0.62 19.10 ?  20  ASN   A HB3  1 
ATOM   545  H  HB3  B ASN   A 1 20  ? 6.315  -3.208  9.506   0.38 15.80 ?  20  ASN   A HB3  1 
ATOM   546  H  HD21 A ASN   A 1 20  ? 7.229  -0.176  7.097   0.62 20.38 ?  20  ASN   A HD21 1 
ATOM   547  H  HD21 B ASN   A 1 20  ? 7.095  -0.589  6.751   0.38 17.24 ?  20  ASN   A HD21 1 
ATOM   548  H  HD22 A ASN   A 1 20  ? 7.959  -1.461  6.909   0.62 20.38 ?  20  ASN   A HD22 1 
ATOM   549  H  HD22 B ASN   A 1 20  ? 8.046  -1.687  7.060   0.38 17.24 ?  20  ASN   A HD22 1 
ATOM   550  N  N    A ALA   A 1 21  ? 10.079 -1.766  9.287   0.62 15.32 ?  21  ALA   A N    1 
ATOM   551  N  N    B ALA   A 1 21  ? 10.048 -1.839  9.334   0.38 13.47 ?  21  ALA   A N    1 
ATOM   552  C  CA   A ALA   A 1 21  ? 10.803 -0.889  10.193  0.62 15.67 ?  21  ALA   A CA   1 
ATOM   553  C  CA   B ALA   A 1 21  ? 10.711 -0.793  10.098  0.38 13.72 ?  21  ALA   A CA   1 
ATOM   554  C  C    A ALA   A 1 21  ? 11.754 -0.004  9.408   0.62 15.25 ?  21  ALA   A C    1 
ATOM   555  C  C    B ALA   A 1 21  ? 11.792 -0.143  9.249   0.38 12.79 ?  21  ALA   A C    1 
ATOM   556  O  O    A ALA   A 1 21  ? 12.198 -0.356  8.312   0.62 15.37 ?  21  ALA   A O    1 
ATOM   557  O  O    B ALA   A 1 21  ? 12.306 -0.743  8.301   0.38 12.84 ?  21  ALA   A O    1 
ATOM   558  C  CB   A ALA   A 1 21  ? 11.584 -1.695  11.232  0.62 16.33 ?  21  ALA   A CB   1 
ATOM   559  C  CB   B ALA   A 1 21  ? 11.322 -1.341  11.393  0.38 14.51 ?  21  ALA   A CB   1 
ATOM   560  H  H    A ALA   A 1 21  ? 10.430 -1.858  8.507   0.62 18.37 ?  21  ALA   A H    1 
ATOM   561  H  H    B ALA   A 1 21  ? 10.514 -2.149  8.677   0.38 16.15 ?  21  ALA   A H    1 
ATOM   562  H  HA   A ALA   A 1 21  ? 10.167 -0.322  10.658  0.62 18.78 ?  21  ALA   A HA   1 
ATOM   563  H  HA   B ALA   A 1 21  ? 10.061 -0.115  10.335  0.38 16.45 ?  21  ALA   A HA   1 
ATOM   564  H  HB1  A ALA   A 1 21  ? 12.007 -1.078  11.845  0.62 19.58 ?  21  ALA   A HB1  1 
ATOM   565  H  HB1  B ALA   A 1 21  ? 11.749 -0.614  11.873  0.38 17.39 ?  21  ALA   A HB1  1 
ATOM   566  H  HB2  A ALA   A 1 21  ? 10.964 -2.268  11.715  0.62 19.58 ?  21  ALA   A HB2  1 
ATOM   567  H  HB2  B ALA   A 1 21  ? 10.617 -1.727  11.938  0.38 17.39 ?  21  ALA   A HB2  1 
ATOM   568  H  HB3  A ALA   A 1 21  ? 12.248 -2.233  10.780  0.62 19.58 ?  21  ALA   A HB3  1 
ATOM   569  H  HB3  B ALA   A 1 21  ? 11.977 -2.022  11.172  0.38 17.39 ?  21  ALA   A HB3  1 
ATOM   570  N  N    A ASP   A 1 22  ? 12.037 1.159   9.987   0.62 15.49 ?  22  ASP   A N    1 
ATOM   571  N  N    B ASP   A 1 22  ? 12.099 1.106   9.592   0.38 12.43 ?  22  ASP   A N    1 
ATOM   572  C  CA   A ASP   A 1 22  ? 13.082 2.049   9.506   0.62 15.79 ?  22  ASP   A CA   1 
ATOM   573  C  CA   B ASP   A 1 22  ? 13.256 1.808   9.053   0.38 12.20 ?  22  ASP   A CA   1 
ATOM   574  C  C    A ASP   A 1 22  ? 14.406 1.569   10.088  0.62 14.44 ?  22  ASP   A C    1 
ATOM   575  C  C    B ASP   A 1 22  ? 14.517 1.223   9.683   0.38 11.14 ?  22  ASP   A C    1 
ATOM   576  O  O    A ASP   A 1 22  ? 14.590 1.581   11.309  0.62 14.84 ?  22  ASP   A O    1 
ATOM   577  O  O    B ASP   A 1 22  ? 14.634 1.177   10.912  0.38 11.27 ?  22  ASP   A O    1 
ATOM   578  C  CB   A ASP   A 1 22  ? 12.767 3.470   9.969   0.62 17.63 ?  22  ASP   A CB   1 
ATOM   579  C  CB   B ASP   A 1 22  ? 13.123 3.285   9.422   0.38 13.45 ?  22  ASP   A CB   1 
ATOM   580  C  CG   A ASP   A 1 22  ? 13.806 4.487   9.520   0.62 19.60 ?  22  ASP   A CG   1 
ATOM   581  C  CG   B ASP   A 1 22  ? 14.110 4.172   8.695   0.38 13.67 ?  22  ASP   A CG   1 
ATOM   582  O  OD1  A ASP   A 1 22  ? 14.870 4.093   8.995   0.62 20.02 ?  22  ASP   A OD1  1 
ATOM   583  O  OD1  B ASP   A 1 22  ? 15.194 3.682   8.311   0.38 12.64 ?  22  ASP   A OD1  1 
ATOM   584  O  OD2  A ASP   A 1 22  ? 13.554 5.697   9.697   0.62 20.97 -1 22  ASP   A OD2  1 
ATOM   585  O  OD2  B ASP   A 1 22  ? 13.805 5.370   8.520   0.38 15.01 -1 22  ASP   A OD2  1 
ATOM   586  H  H    A ASP   A 1 22  ? 11.612 1.462   10.670  0.62 18.58 ?  22  ASP   A H    1 
ATOM   587  H  H    B ASP   A 1 22  ? 11.626 1.581   10.133  0.38 14.90 ?  22  ASP   A H    1 
ATOM   588  H  HA   A ASP   A 1 22  ? 13.127 2.025   8.536   0.62 18.93 ?  22  ASP   A HA   1 
ATOM   589  H  HA   B ASP   A 1 22  ? 13.293 1.710   8.085   0.38 14.62 ?  22  ASP   A HA   1 
ATOM   590  H  HB2  A ASP   A 1 22  ? 11.905 3.733   9.609   0.62 21.14 ?  22  ASP   A HB2  1 
ATOM   591  H  HB2  B ASP   A 1 22  ? 12.229 3.586   9.205   0.38 16.12 ?  22  ASP   A HB2  1 
ATOM   592  H  HB3  A ASP   A 1 22  ? 12.734 3.479   10.939  0.62 21.14 ?  22  ASP   A HB3  1 
ATOM   593  H  HB3  B ASP   A 1 22  ? 13.282 3.382   10.376  0.38 16.12 ?  22  ASP   A HB3  1 
ATOM   594  N  N    A ILE   A 1 23  ? 15.318 1.129   9.216   0.62 13.70 ?  23  ILE   A N    1 
ATOM   595  N  N    B ILE   A 1 23  ? 15.458 0.767   8.848   0.38 11.02 ?  23  ILE   A N    1 
ATOM   596  C  CA   A ILE   A 1 23  ? 16.570 0.526   9.672   0.62 13.18 ?  23  ILE   A CA   1 
ATOM   597  C  CA   B ILE   A 1 23  ? 16.691 0.175   9.368   0.38 10.73 ?  23  ILE   A CA   1 
ATOM   598  C  C    A ILE   A 1 23  ? 17.367 1.492   10.536  0.62 12.97 ?  23  ILE   A C    1 
ATOM   599  C  C    B ILE   A 1 23  ? 17.414 1.149   10.286  0.38 11.57 ?  23  ILE   A C    1 
ATOM   600  O  O    A ILE   A 1 23  ? 18.104 1.068   11.437  0.62 13.27 ?  23  ILE   A O    1 
ATOM   601  O  O    B ILE   A 1 23  ? 18.065 0.737   11.255  0.38 11.86 ?  23  ILE   A O    1 
ATOM   602  C  CB   A ILE   A 1 23  ? 17.379 0.006   8.465   0.62 12.78 ?  23  ILE   A CB   1 
ATOM   603  C  CB   B ILE   A 1 23  ? 17.602 -0.344  8.230   0.38 10.30 ?  23  ILE   A CB   1 
ATOM   604  C  CG1  A ILE   A 1 23  ? 18.518 -0.904  8.931   0.62 12.85 ?  23  ILE   A CG1  1 
ATOM   605  C  CG1  B ILE   A 1 23  ? 18.678 -1.275  8.803   0.38 10.34 ?  23  ILE   A CG1  1 
ATOM   606  C  CG2  A ILE   A 1 23  ? 17.898 1.166   7.617   0.62 12.79 ?  23  ILE   A CG2  1 
ATOM   607  C  CG2  B ILE   A 1 23  ? 18.244 0.814   7.459   0.38 9.86  ?  23  ILE   A CG2  1 
ATOM   608  C  CD1  A ILE   A 1 23  ? 19.214 -1.614  7.796   0.62 12.92 ?  23  ILE   A CD1  1 
ATOM   609  C  CD1  B ILE   A 1 23  ? 19.550 -1.950  7.756   0.38 10.59 ?  23  ILE   A CD1  1 
ATOM   610  H  H    A ILE   A 1 23  ? 15.229 1.166   8.364   0.62 16.43 ?  23  ILE   A H    1 
ATOM   611  H  H    B ILE   A 1 23  ? 15.405 0.785   7.996   0.38 13.21 ?  23  ILE   A H    1 
ATOM   612  H  HA   A ILE   A 1 23  ? 16.356 -0.243  10.221  0.62 15.80 ?  23  ILE   A HA   1 
ATOM   613  H  HA   B ILE   A 1 23  ? 16.447 -0.595  9.900   0.38 12.85 ?  23  ILE   A HA   1 
ATOM   614  H  HB   A ILE   A 1 23  ? 16.787 -0.523  7.910   0.62 15.32 ?  23  ILE   A HB   1 
ATOM   615  H  HB   B ILE   A 1 23  ? 17.061 -0.857  7.609   0.38 12.34 ?  23  ILE   A HB   1 
ATOM   616  H  HG12 A ILE   A 1 23  ? 19.181 -0.368  9.396   0.62 15.40 ?  23  ILE   A HG12 1 
ATOM   617  H  HG12 B ILE   A 1 23  ? 19.262 -0.760  9.381   0.38 12.39 ?  23  ILE   A HG12 1 
ATOM   618  H  HG13 A ILE   A 1 23  ? 18.159 -1.578  9.528   0.62 15.40 ?  23  ILE   A HG13 1 
ATOM   619  H  HG13 B ILE   A 1 23  ? 18.244 -1.975  9.316   0.38 12.39 ?  23  ILE   A HG13 1 
ATOM   620  H  HG21 A ILE   A 1 23  ? 18.240 0.819   6.777   0.62 15.33 ?  23  ILE   A HG21 1 
ATOM   621  H  HG21 B ILE   A 1 23  ? 18.646 0.468   6.642   0.38 11.82 ?  23  ILE   A HG21 1 
ATOM   622  H  HG22 A ILE   A 1 23  ? 17.165 1.781   7.443   0.62 15.33 ?  23  ILE   A HG22 1 
ATOM   623  H  HG22 B ILE   A 1 23  ? 17.561 1.463   7.238   0.38 11.82 ?  23  ILE   A HG22 1 
ATOM   624  H  HG23 A ILE   A 1 23  ? 18.604 1.624   8.098   0.62 15.33 ?  23  ILE   A HG23 1 
ATOM   625  H  HG23 B ILE   A 1 23  ? 18.928 1.225   8.010   0.38 11.82 ?  23  ILE   A HG23 1 
ATOM   626  H  HD11 A ILE   A 1 23  ? 19.867 -2.230  8.163   0.62 15.49 ?  23  ILE   A HD11 1 
ATOM   627  H  HD11 B ILE   A 1 23  ? 20.149 -2.574  8.199   0.38 12.69 ?  23  ILE   A HD11 1 
ATOM   628  H  HD12 A ILE   A 1 23  ? 18.554 -2.101  7.278   0.62 15.49 ?  23  ILE   A HD12 1 
ATOM   629  H  HD12 B ILE   A 1 23  ? 18.982 -2.426  7.131   0.38 12.69 ?  23  ILE   A HD12 1 
ATOM   630  H  HD13 A ILE   A 1 23  ? 19.656 -0.958  7.235   0.62 15.49 ?  23  ILE   A HD13 1 
ATOM   631  H  HD13 B ILE   A 1 23  ? 20.065 -1.275  7.289   0.38 12.69 ?  23  ILE   A HD13 1 
ATOM   632  N  N    A VAL   A 1 24  ? 17.239 2.796   10.286  0.62 13.67 ?  24  VAL   A N    1 
ATOM   633  N  N    B VAL   A 1 24  ? 17.308 2.450   10.006  0.38 12.42 ?  24  VAL   A N    1 
ATOM   634  C  CA   A VAL   A 1 24  ? 17.909 3.782   11.130  0.62 14.86 ?  24  VAL   A CA   1 
ATOM   635  C  CA   B VAL   A 1 24  ? 17.948 3.452   10.853  0.38 13.41 ?  24  VAL   A CA   1 
ATOM   636  C  C    A VAL   A 1 24  ? 17.387 3.695   12.556  0.62 15.40 ?  24  VAL   A C    1 
ATOM   637  C  C    B VAL   A 1 24  ? 17.329 3.450   12.244  0.38 14.11 ?  24  VAL   A C    1 
ATOM   638  O  O    A VAL   A 1 24  ? 18.160 3.605   13.520  0.62 15.52 ?  24  VAL   A O    1 
ATOM   639  O  O    B VAL   A 1 24  ? 18.038 3.506   13.256  0.38 14.96 ?  24  VAL   A O    1 
ATOM   640  C  CB   A VAL   A 1 24  ? 17.726 5.196   10.551  0.62 15.72 ?  24  VAL   A CB   1 
ATOM   641  C  CB   B VAL   A 1 24  ? 17.866 4.837   10.184  0.38 14.30 ?  24  VAL   A CB   1 
ATOM   642  C  CG1  A VAL   A 1 24  ? 18.229 6.248   11.537  0.62 16.45 ?  24  VAL   A CG1  1 
ATOM   643  C  CG1  B VAL   A 1 24  ? 18.511 5.891   11.063  0.38 15.55 ?  24  VAL   A CG1  1 
ATOM   644  C  CG2  A VAL   A 1 24  ? 18.432 5.319   9.209   0.62 16.33 ?  24  VAL   A CG2  1 
ATOM   645  C  CG2  B VAL   A 1 24  ? 18.519 4.796   8.809   0.38 14.28 ?  24  VAL   A CG2  1 
ATOM   646  H  H    A VAL   A 1 24  ? 16.775 3.129   9.642   0.62 16.38 ?  24  VAL   A H    1 
ATOM   647  H  H    B VAL   A 1 24  ? 16.868 2.773   9.342   0.38 14.89 ?  24  VAL   A H    1 
ATOM   648  H  HA   A VAL   A 1 24  ? 18.856 3.588   11.147  0.62 17.82 ?  24  VAL   A HA   1 
ATOM   649  H  HA   B VAL   A 1 24  ? 18.883 3.225   10.947  0.38 16.07 ?  24  VAL   A HA   1 
ATOM   650  H  HB   A VAL   A 1 24  ? 16.781 5.356   10.401  0.62 18.85 ?  24  VAL   A HB   1 
ATOM   651  H  HB   B VAL   A 1 24  ? 16.933 5.074   10.063  0.38 17.14 ?  24  VAL   A HB   1 
ATOM   652  H  HG11 A VAL   A 1 24  ? 18.362 7.083   11.063  0.62 19.73 ?  24  VAL   A HG11 1 
ATOM   653  H  HG11 B VAL   A 1 24  ? 18.617 6.704   10.549  0.38 18.65 ?  24  VAL   A HG11 1 
ATOM   654  H  HG12 A VAL   A 1 24  ? 17.570 6.367   12.237  0.62 19.73 ?  24  VAL   A HG12 1 
ATOM   655  H  HG12 B VAL   A 1 24  ? 17.938 6.056   11.829  0.38 18.65 ?  24  VAL   A HG12 1 
ATOM   656  H  HG13 A VAL   A 1 24  ? 19.069 5.946   11.916  0.62 19.73 ?  24  VAL   A HG13 1 
ATOM   657  H  HG13 B VAL   A 1 24  ? 19.376 5.567   11.357  0.38 18.65 ?  24  VAL   A HG13 1 
ATOM   658  H  HG21 A VAL   A 1 24  ? 18.196 6.170   8.806   0.62 19.58 ?  24  VAL   A HG21 1 
ATOM   659  H  HG21 B VAL   A 1 24  ? 18.572 5.697   8.459   0.38 17.12 ?  24  VAL   A HG21 1 
ATOM   660  H  HG22 A VAL   A 1 24  ? 19.390 5.277   9.352   0.62 19.58 ?  24  VAL   A HG22 1 
ATOM   661  H  HG22 B VAL   A 1 24  ? 19.410 4.420   8.897   0.38 17.12 ?  24  VAL   A HG22 1 
ATOM   662  H  HG23 A VAL   A 1 24  ? 18.149 4.592   8.632   0.62 19.58 ?  24  VAL   A HG23 1 
ATOM   663  H  HG23 B VAL   A 1 24  ? 17.984 4.240   8.220   0.38 17.12 ?  24  VAL   A HG23 1 
ATOM   664  N  N    A GLU   A 1 25  ? 16.062 3.726   12.711  0.62 16.25 ?  25  GLU   A N    1 
ATOM   665  N  N    B GLU   A 1 25  ? 15.998 3.374   12.319  0.38 14.29 ?  25  GLU   A N    1 
ATOM   666  C  CA   A GLU   A 1 25  ? 15.475 3.667   14.043  0.62 17.52 ?  25  GLU   A CA   1 
ATOM   667  C  CA   B GLU   A 1 25  ? 15.336 3.334   13.620  0.38 15.26 ?  25  GLU   A CA   1 
ATOM   668  C  C    A GLU   A 1 25  ? 15.708 2.312   14.694  0.62 16.37 ?  25  GLU   A C    1 
ATOM   669  C  C    B GLU   A 1 25  ? 15.613 2.019   14.342  0.38 15.30 ?  25  GLU   A C    1 
ATOM   670  O  O    A GLU   A 1 25  ? 15.906 2.236   15.912  0.62 16.52 ?  25  GLU   A O    1 
ATOM   671  O  O    B GLU   A 1 25  ? 15.832 2.009   15.558  0.38 15.70 ?  25  GLU   A O    1 
ATOM   672  C  CB   A GLU   A 1 25  ? 13.983 4.005   13.973  0.62 20.27 ?  25  GLU   A CB   1 
ATOM   673  C  CB   B GLU   A 1 25  ? 13.834 3.580   13.457  0.38 16.84 ?  25  GLU   A CB   1 
ATOM   674  C  CG   A GLU   A 1 25  ? 13.713 5.467   13.638  0.62 23.30 ?  25  GLU   A CG   1 
ATOM   675  C  CG   B GLU   A 1 25  ? 13.505 4.953   12.884  0.38 19.29 ?  25  GLU   A CG   1 
ATOM   676  C  CD   A GLU   A 1 25  ? 14.506 6.433   14.506  0.62 25.83 ?  25  GLU   A CD   1 
ATOM   677  C  CD   B GLU   A 1 25  ? 14.015 6.082   13.753  0.38 21.49 ?  25  GLU   A CD   1 
ATOM   678  O  OE1  A GLU   A 1 25  ? 14.615 6.193   15.728  0.62 26.56 ?  25  GLU   A OE1  1 
ATOM   679  O  OE1  B GLU   A 1 25  ? 14.002 5.930   14.993  0.38 22.52 ?  25  GLU   A OE1  1 
ATOM   680  O  OE2  A GLU   A 1 25  ? 15.038 7.421   13.960  0.62 27.11 -1 25  GLU   A OE2  1 
ATOM   681  O  OE2  B GLU   A 1 25  ? 14.437 7.116   13.195  0.38 22.31 -1 25  GLU   A OE2  1 
ATOM   682  H  H    A GLU   A 1 25  ? 15.490 3.789   12.068  0.62 19.48 ?  25  GLU   A H    1 
ATOM   683  H  H    B GLU   A 1 25  ? 15.466 3.345   11.642  0.38 17.14 ?  25  GLU   A H    1 
ATOM   684  H  HA   A GLU   A 1 25  ? 15.906 4.330   14.600  0.62 21.01 ?  25  GLU   A HA   1 
ATOM   685  H  HA   B GLU   A 1 25  ? 15.692 4.046   14.168  0.38 18.30 ?  25  GLU   A HA   1 
ATOM   686  H  HB2  A GLU   A 1 25  ? 13.564 3.465   13.279  0.62 24.31 ?  25  GLU   A HB2  1 
ATOM   687  H  HB2  B GLU   A 1 25  ? 13.466 2.915   12.855  0.38 20.19 ?  25  GLU   A HB2  1 
ATOM   688  H  HB3  A GLU   A 1 25  ? 13.569 3.817   14.829  0.62 24.31 ?  25  GLU   A HB3  1 
ATOM   689  H  HB3  B GLU   A 1 25  ? 13.407 3.513   14.325  0.38 20.19 ?  25  GLU   A HB3  1 
ATOM   690  H  HG2  A GLU   A 1 25  ? 13.968 5.630   12.719  0.62 27.94 ?  25  GLU   A HG2  1 
ATOM   691  H  HG2  B GLU   A 1 25  ? 13.920 5.042   12.012  0.38 23.13 ?  25  GLU   A HG2  1 
ATOM   692  H  HG3  A GLU   A 1 25  ? 12.767 5.648   13.762  0.62 27.94 ?  25  GLU   A HG3  1 
ATOM   693  H  HG3  B GLU   A 1 25  ? 12.543 5.045   12.806  0.38 23.13 ?  25  GLU   A HG3  1 
ATOM   694  N  N    A GLU   A 1 26  ? 15.704 1.239   13.901  0.62 15.80 ?  26  GLU   A N    1 
ATOM   695  N  N    B GLU   A 1 26  ? 15.616 0.900   13.612  0.38 15.06 ?  26  GLU   A N    1 
ATOM   696  C  CA   A GLU   A 1 26  ? 15.982 -0.087  14.444  0.62 15.40 ?  26  GLU   A CA   1 
ATOM   697  C  CA   B GLU   A 1 26  ? 16.004 -0.369  14.223  0.38 15.45 ?  26  GLU   A CA   1 
ATOM   698  C  C    A GLU   A 1 26  ? 17.399 -0.167  14.999  0.62 14.59 ?  26  GLU   A C    1 
ATOM   699  C  C    B GLU   A 1 26  ? 17.431 -0.308  14.749  0.38 14.92 ?  26  GLU   A C    1 
ATOM   700  O  O    A GLU   A 1 26  ? 17.614 -0.631  16.123  0.62 14.60 ?  26  GLU   A O    1 
ATOM   701  O  O    B GLU   A 1 26  ? 17.741 -0.880  15.800  0.38 14.85 ?  26  GLU   A O    1 
ATOM   702  C  CB   A GLU   A 1 26  ? 15.776 -1.148  13.361  0.62 16.63 ?  26  GLU   A CB   1 
ATOM   703  C  CB   B GLU   A 1 26  ? 15.871 -1.508  13.212  0.38 16.27 ?  26  GLU   A CB   1 
ATOM   704  C  CG   A GLU   A 1 26  ? 14.357 -1.639  13.202  0.62 19.51 ?  26  GLU   A CG   1 
ATOM   705  C  CG   B GLU   A 1 26  ? 14.450 -1.953  12.958  0.38 17.20 ?  26  GLU   A CG   1 
ATOM   706  C  CD   A GLU   A 1 26  ? 13.887 -2.487  14.373  0.62 21.21 ?  26  GLU   A CD   1 
ATOM   707  C  CD   B GLU   A 1 26  ? 13.766 -2.460  14.203  0.38 17.58 ?  26  GLU   A CD   1 
ATOM   708  O  OE1  A GLU   A 1 26  ? 14.328 -3.654  14.515  0.62 21.22 ?  26  GLU   A OE1  1 
ATOM   709  O  OE1  B GLU   A 1 26  ? 14.347 -3.327  14.891  0.38 17.91 ?  26  GLU   A OE1  1 
ATOM   710  O  OE2  A GLU   A 1 26  ? 13.072 -1.976  15.157  0.62 22.29 -1 26  GLU   A OE2  1 
ATOM   711  O  OE2  B GLU   A 1 26  ? 12.655 -1.975  14.496  0.38 16.77 -1 26  GLU   A OE2  1 
ATOM   712  H  H    A GLU   A 1 26  ? 15.547 1.262   13.056  0.62 18.95 ?  26  GLU   A H    1 
ATOM   713  H  H    B GLU   A 1 26  ? 15.400 0.848   12.781  0.38 18.05 ?  26  GLU   A H    1 
ATOM   714  H  HA   A GLU   A 1 26  ? 15.363 -0.261  15.165  0.62 18.46 ?  26  GLU   A HA   1 
ATOM   715  H  HA   B GLU   A 1 26  ? 15.416 -0.556  14.972  0.38 18.53 ?  26  GLU   A HA   1 
ATOM   716  H  HB2  A GLU   A 1 26  ? 16.053 -0.773  12.507  0.62 19.94 ?  26  GLU   A HB2  1 
ATOM   717  H  HB2  B GLU   A 1 26  ? 16.242 -1.217  12.362  0.38 19.51 ?  26  GLU   A HB2  1 
ATOM   718  H  HB3  A GLU   A 1 26  ? 16.330 -1.910  13.575  0.62 19.94 ?  26  GLU   A HB3  1 
ATOM   719  H  HB3  B GLU   A 1 26  ? 16.370 -2.276  13.537  0.38 19.51 ?  26  GLU   A HB3  1 
ATOM   720  H  HG2  A GLU   A 1 26  ? 13.772 -0.868  13.124  0.62 23.40 ?  26  GLU   A HG2  1 
ATOM   721  H  HG2  B GLU   A 1 26  ? 13.937 -1.203  12.632  0.38 20.62 ?  26  GLU   A HG2  1 
ATOM   722  H  HG3  A GLU   A 1 26  ? 14.299 -2.180  12.401  0.62 23.40 ?  26  GLU   A HG3  1 
ATOM   723  H  HG3  B GLU   A 1 26  ? 14.452 -2.671  12.310  0.38 20.62 ?  26  GLU   A HG3  1 
ATOM   724  N  N    A ALA   A 1 27  ? 18.389 0.274   14.215  0.62 14.10 ?  27  ALA   A N    1 
ATOM   725  N  N    B ALA   A 1 27  ? 18.319 0.373   14.024  0.38 14.08 ?  27  ALA   A N    1 
ATOM   726  C  CA   A ALA   A 1 27  ? 19.776 0.197   14.667  0.62 14.16 ?  27  ALA   A CA   1 
ATOM   727  C  CA   B ALA   A 1 27  ? 19.703 0.486   14.471  0.38 13.71 ?  27  ALA   A CA   1 
ATOM   728  C  C    A ALA   A 1 27  ? 19.985 1.005   15.942  0.62 15.22 ?  27  ALA   A C    1 
ATOM   729  C  C    B ALA   A 1 27  ? 19.801 1.330   15.736  0.38 14.22 ?  27  ALA   A C    1 
ATOM   730  O  O    A ALA   A 1 27  ? 20.686 0.563   16.861  0.62 15.73 ?  27  ALA   A O    1 
ATOM   731  O  O    B ALA   A 1 27  ? 20.419 0.918   16.725  0.38 14.29 ?  27  ALA   A O    1 
ATOM   732  C  CB   A ALA   A 1 27  ? 20.722 0.670   13.560  0.62 13.60 ?  27  ALA   A CB   1 
ATOM   733  C  CB   B ALA   A 1 27  ? 20.560 1.084   13.356  0.38 13.11 ?  27  ALA   A CB   1 
ATOM   734  H  H    A ALA   A 1 27  ? 18.285 0.608   13.428  0.62 16.91 ?  27  ALA   A H    1 
ATOM   735  H  H    B ALA   A 1 27  ? 18.142 0.770   13.281  0.38 16.88 ?  27  ALA   A H    1 
ATOM   736  H  HA   A ALA   A 1 27  ? 19.988 -0.729  14.859  0.62 16.97 ?  27  ALA   A HA   1 
ATOM   737  H  HA   B ALA   A 1 27  ? 20.039 -0.398  14.669  0.38 16.44 ?  27  ALA   A HA   1 
ATOM   738  H  HB1  A ALA   A 1 27  ? 21.638 0.607   13.880  0.62 16.30 ?  27  ALA   A HB1  1 
ATOM   739  H  HB1  B ALA   A 1 27  ? 21.477 1.135   13.661  0.38 15.71 ?  27  ALA   A HB1  1 
ATOM   740  H  HB2  A ALA   A 1 27  ? 20.610 0.098   12.781  0.62 16.30 ?  27  ALA   A HB2  1 
ATOM   741  H  HB2  B ALA   A 1 27  ? 20.499 0.517   12.572  0.38 15.71 ?  27  ALA   A HB2  1 
ATOM   742  H  HB3  A ALA   A 1 27  ? 20.513 1.586   13.330  0.62 16.30 ?  27  ALA   A HB3  1 
ATOM   743  H  HB3  B ALA   A 1 27  ? 20.230 1.974   13.146  0.38 15.71 ?  27  ALA   A HB3  1 
ATOM   744  N  N    A LYS   A 1 28  ? 19.375 2.189   16.026  0.62 16.93 ?  28  LYS   A N    1 
ATOM   745  N  N    B LYS   A 1 28  ? 19.186 2.514   15.724  0.38 15.41 ?  28  LYS   A N    1 
ATOM   746  C  CA   A LYS   A 1 28  ? 19.521 3.005   17.226  0.62 19.45 ?  28  LYS   A CA   1 
ATOM   747  C  CA   B LYS   A 1 28  ? 19.274 3.407   16.874  0.38 17.13 ?  28  LYS   A CA   1 
ATOM   748  C  C    A LYS   A 1 28  ? 18.974 2.295   18.457  0.62 20.15 ?  28  LYS   A C    1 
ATOM   749  C  C    B LYS   A 1 28  ? 18.699 2.770   18.130  0.38 17.69 ?  28  LYS   A C    1 
ATOM   750  O  O    A LYS   A 1 28  ? 19.534 2.435   19.550  0.62 21.23 ?  28  LYS   A O    1 
ATOM   751  O  O    B LYS   A 1 28  ? 19.192 3.024   19.236  0.38 18.03 ?  28  LYS   A O    1 
ATOM   752  C  CB   A LYS   A 1 28  ? 18.857 4.371   17.029  0.62 21.60 ?  28  LYS   A CB   1 
ATOM   753  C  CB   B LYS   A 1 28  ? 18.565 4.728   16.569  0.38 18.94 ?  28  LYS   A CB   1 
ATOM   754  C  CG   A LYS   A 1 28  ? 19.687 5.326   16.180  0.62 23.59 ?  28  LYS   A CG   1 
ATOM   755  C  CG   B LYS   A 1 28  ? 19.265 5.565   15.512  0.38 20.96 ?  28  LYS   A CG   1 
ATOM   756  C  CD   A LYS   A 1 28  ? 19.205 6.764   16.281  0.62 25.78 ?  28  LYS   A CD   1 
ATOM   757  C  CD   B LYS   A 1 28  ? 18.701 6.976   15.439  0.38 23.03 ?  28  LYS   A CD   1 
ATOM   758  C  CE   A LYS   A 1 28  ? 17.923 6.974   15.504  0.62 27.38 ?  28  LYS   A CE   1 
ATOM   759  C  CE   B LYS   A 1 28  ? 17.248 6.986   14.998  0.38 24.65 ?  28  LYS   A CE   1 
ATOM   760  N  NZ   A LYS   A 1 28  ? 17.555 8.415   15.445  0.62 28.47 ?  28  LYS   A NZ   1 
ATOM   761  N  NZ   B LYS   A 1 28  ? 16.707 8.371   14.935  0.38 25.33 ?  28  LYS   A NZ   1 
ATOM   762  H  H    A LYS   A 1 28  ? 18.885 2.531   15.416  0.62 20.29 ?  28  LYS   A H    1 
ATOM   763  H  H    B LYS   A 1 28  ? 18.718 2.820   15.072  0.38 18.48 ?  28  LYS   A H    1 
ATOM   764  H  HA   A LYS   A 1 28  ? 20.463 3.158   17.388  0.62 23.32 ?  28  LYS   A HA   1 
ATOM   765  H  HA   B LYS   A 1 28  ? 20.202 3.605   17.049  0.38 20.54 ?  28  LYS   A HA   1 
ATOM   766  H  HB2  A LYS   A 1 28  ? 18.005 4.247   16.586  0.62 25.90 ?  28  LYS   A HB2  1 
ATOM   767  H  HB2  B LYS   A 1 28  ? 17.669 4.536   16.248  0.38 22.71 ?  28  LYS   A HB2  1 
ATOM   768  H  HB3  A LYS   A 1 28  ? 18.723 4.786   17.895  0.62 25.90 ?  28  LYS   A HB3  1 
ATOM   769  H  HB3  B LYS   A 1 28  ? 18.517 5.257   17.380  0.38 22.71 ?  28  LYS   A HB3  1 
ATOM   770  H  HG2  A LYS   A 1 28  ? 20.609 5.299   16.479  0.62 28.30 ?  28  LYS   A HG2  1 
ATOM   771  H  HG2  B LYS   A 1 28  ? 20.208 5.626   15.728  0.38 25.13 ?  28  LYS   A HG2  1 
ATOM   772  H  HG3  A LYS   A 1 28  ? 19.630 5.056   15.251  0.62 28.30 ?  28  LYS   A HG3  1 
ATOM   773  H  HG3  B LYS   A 1 28  ? 19.147 5.148   14.644  0.38 25.13 ?  28  LYS   A HG3  1 
ATOM   774  H  HD2  A LYS   A 1 28  ? 19.036 6.982   17.211  0.62 30.92 ?  28  LYS   A HD2  1 
ATOM   775  H  HD2  B LYS   A 1 28  ? 18.754 7.386   16.317  0.38 27.62 ?  28  LYS   A HD2  1 
ATOM   776  H  HD3  A LYS   A 1 28  ? 19.882 7.356   15.916  0.62 30.92 ?  28  LYS   A HD3  1 
ATOM   777  H  HD3  B LYS   A 1 28  ? 19.216 7.493   14.798  0.38 27.62 ?  28  LYS   A HD3  1 
ATOM   778  H  HE2  A LYS   A 1 28  ? 18.042 6.653   14.596  0.62 32.84 ?  28  LYS   A HE2  1 
ATOM   779  H  HE2  B LYS   A 1 28  ? 17.180 6.591   14.114  0.38 29.57 ?  28  LYS   A HE2  1 
ATOM   780  H  HE3  A LYS   A 1 28  ? 17.202 6.493   15.940  0.62 32.84 ?  28  LYS   A HE3  1 
ATOM   781  H  HE3  B LYS   A 1 28  ? 16.715 6.483   15.633  0.38 29.57 ?  28  LYS   A HE3  1 
ATOM   782  H  HZ1  A LYS   A 1 28  ? 16.800 8.518   14.985  0.62 34.15 ?  28  LYS   A HZ1  1 
ATOM   783  H  HZ1  B LYS   A 1 28  ? 15.856 8.354   14.675  0.38 30.38 ?  28  LYS   A HZ1  1 
ATOM   784  H  HZ2  A LYS   A 1 28  ? 17.438 8.734   16.268  0.62 34.15 ?  28  LYS   A HZ2  1 
ATOM   785  H  HZ2  B LYS   A 1 28  ? 16.757 8.754   15.737  0.38 30.38 ?  28  LYS   A HZ2  1 
ATOM   786  H  HZ3  A LYS   A 1 28  ? 18.202 8.879   15.046  0.62 34.15 ?  28  LYS   A HZ3  1 
ATOM   787  H  HZ3  B LYS   A 1 28  ? 17.177 8.856   14.354  0.38 30.38 ?  28  LYS   A HZ3  1 
ATOM   788  N  N    A LYS   A 1 29  ? 17.905 1.513   18.300  0.62 20.69 ?  29  LYS   A N    1 
ATOM   789  N  N    B LYS   A 1 29  ? 17.668 1.938   17.982  0.38 18.43 ?  29  LYS   A N    1 
ATOM   790  C  CA   A LYS   A 1 29  ? 17.313 0.811   19.435  0.62 22.32 ?  29  LYS   A CA   1 
ATOM   791  C  CA   B LYS   A 1 29  ? 17.039 1.301   19.133  0.38 19.88 ?  29  LYS   A CA   1 
ATOM   792  C  C    A LYS   A 1 29  ? 18.128 -0.422  19.816  0.62 21.45 ?  29  LYS   A C    1 
ATOM   793  C  C    B LYS   A 1 29  ? 17.813 0.066   19.575  0.38 19.34 ?  29  LYS   A C    1 
ATOM   794  O  O    A LYS   A 1 29  ? 18.418 -0.646  20.998  0.62 22.21 ?  29  LYS   A O    1 
ATOM   795  O  O    B LYS   A 1 29  ? 18.085 -0.108  20.768  0.38 19.78 ?  29  LYS   A O    1 
ATOM   796  C  CB   A LYS   A 1 29  ? 15.873 0.411   19.097  0.62 25.10 ?  29  LYS   A CB   1 
ATOM   797  C  CB   B LYS   A 1 29  ? 15.595 0.936   18.785  0.38 22.09 ?  29  LYS   A CB   1 
ATOM   798  C  CG   A LYS   A 1 29  ? 15.120 -0.268  20.236  0.62 27.95 ?  29  LYS   A CG   1 
ATOM   799  C  CG   B LYS   A 1 29  ? 14.852 0.169   19.864  0.38 24.47 ?  29  LYS   A CG   1 
ATOM   800  C  CD   A LYS   A 1 29  ? 14.771 0.718   21.341  0.62 30.51 ?  29  LYS   A CD   1 
ATOM   801  C  CD   B LYS   A 1 29  ? 14.674 0.998   21.119  0.38 26.60 ?  29  LYS   A CD   1 
ATOM   802  C  CE   A LYS   A 1 29  ? 13.911 0.068   22.415  0.62 32.13 ?  29  LYS   A CE   1 
ATOM   803  C  CE   B LYS   A 1 29  ? 13.322 0.725   21.752  0.38 27.99 ?  29  LYS   A CE   1 
ATOM   804  N  NZ   A LYS   A 1 29  ? 13.492 1.047   23.455  0.62 33.24 ?  29  LYS   A NZ   1 
ATOM   805  N  NZ   B LYS   A 1 29  ? 13.305 1.064   23.199  0.38 28.91 ?  29  LYS   A NZ   1 
ATOM   806  H  H    A LYS   A 1 29  ? 17.510 1.369   17.549  0.62 24.81 ?  29  LYS   A H    1 
ATOM   807  H  H    B LYS   A 1 29  ? 17.315 1.725   17.228  0.38 22.10 ?  29  LYS   A H    1 
ATOM   808  H  HA   A LYS   A 1 29  ? 17.285 1.406   20.199  0.62 26.77 ?  29  LYS   A HA   1 
ATOM   809  H  HA   B LYS   A 1 29  ? 17.021 1.922   19.875  0.38 23.84 ?  29  LYS   A HA   1 
ATOM   810  H  HB2  A LYS   A 1 29  ? 15.375 1.208   18.855  0.62 30.11 ?  29  LYS   A HB2  1 
ATOM   811  H  HB2  B LYS   A 1 29  ? 15.101 1.754   18.619  0.38 26.49 ?  29  LYS   A HB2  1 
ATOM   812  H  HB3  A LYS   A 1 29  ? 15.886 -0.205  18.349  0.62 30.11 ?  29  LYS   A HB3  1 
ATOM   813  H  HB3  B LYS   A 1 29  ? 15.596 0.387   17.987  0.38 26.49 ?  29  LYS   A HB3  1 
ATOM   814  H  HG2  A LYS   A 1 29  ? 14.293 -0.642  19.894  0.62 33.53 ?  29  LYS   A HG2  1 
ATOM   815  H  HG2  B LYS   A 1 29  ? 13.972 -0.067  19.533  0.38 29.34 ?  29  LYS   A HG2  1 
ATOM   816  H  HG3  A LYS   A 1 29  ? 15.669 -0.971  20.619  0.62 33.53 ?  29  LYS   A HG3  1 
ATOM   817  H  HG3  B LYS   A 1 29  ? 15.345 -0.635  20.095  0.38 29.34 ?  29  LYS   A HG3  1 
ATOM   818  H  HD2  A LYS   A 1 29  ? 15.588 1.036   21.757  0.62 36.60 ?  29  LYS   A HD2  1 
ATOM   819  H  HD2  B LYS   A 1 29  ? 15.366 0.766   21.759  0.38 31.90 ?  29  LYS   A HD2  1 
ATOM   820  H  HD3  A LYS   A 1 29  ? 14.275 1.461   20.962  0.62 36.60 ?  29  LYS   A HD3  1 
ATOM   821  H  HD3  B LYS   A 1 29  ? 14.725 1.940   20.893  0.38 31.90 ?  29  LYS   A HD3  1 
ATOM   822  H  HE2  A LYS   A 1 29  ? 13.111 -0.300  22.005  0.62 38.53 ?  29  LYS   A HE2  1 
ATOM   823  H  HE2  B LYS   A 1 29  ? 12.649 1.264   21.305  0.38 33.57 ?  29  LYS   A HE2  1 
ATOM   824  H  HE3  A LYS   A 1 29  ? 14.418 -0.637  22.848  0.62 38.53 ?  29  LYS   A HE3  1 
ATOM   825  H  HE3  B LYS   A 1 29  ? 13.111 -0.217  21.657  0.38 33.57 ?  29  LYS   A HE3  1 
ATOM   826  H  HZ1  A LYS   A 1 29  ? 12.990 0.642   24.070  0.62 39.88 ?  29  LYS   A HZ1  1 
ATOM   827  H  HZ1  B LYS   A 1 29  ? 12.501 0.893   23.540  0.38 34.67 ?  29  LYS   A HZ1  1 
ATOM   828  H  HZ2  A LYS   A 1 29  ? 14.208 1.396   23.851  0.62 39.88 ?  29  LYS   A HZ2  1 
ATOM   829  H  HZ2  B LYS   A 1 29  ? 13.912 0.577   23.631  0.38 34.67 ?  29  LYS   A HZ2  1 
ATOM   830  H  HZ3  A LYS   A 1 29  ? 13.018 1.703   23.083  0.62 39.88 ?  29  LYS   A HZ3  1 
ATOM   831  H  HZ3  B LYS   A 1 29  ? 13.491 1.926   23.311  0.38 34.67 ?  29  LYS   A HZ3  1 
ATOM   832  N  N    A VAL   A 1 30  ? 18.489 -1.242  18.829  0.62 20.13 ?  30  VAL   A N    1 
ATOM   833  N  N    B VAL   A 1 30  ? 18.176 -0.801  18.626  0.38 18.93 ?  30  VAL   A N    1 
ATOM   834  C  CA   A VAL   A 1 30  ? 19.141 -2.518  19.111  0.62 19.32 ?  30  VAL   A CA   1 
ATOM   835  C  CA   B VAL   A 1 30  ? 18.796 -2.076  18.979  0.38 18.97 ?  30  VAL   A CA   1 
ATOM   836  C  C    A VAL   A 1 30  ? 20.642 -2.356  19.332  0.62 17.90 ?  30  VAL   A C    1 
ATOM   837  C  C    B VAL   A 1 30  ? 20.293 -1.919  19.223  0.38 18.67 ?  30  VAL   A C    1 
ATOM   838  O  O    A VAL   A 1 30  ? 21.237 -3.099  20.122  0.62 18.08 ?  30  VAL   A O    1 
ATOM   839  O  O    B VAL   A 1 30  ? 20.861 -2.577  20.102  0.38 18.57 ?  30  VAL   A O    1 
ATOM   840  C  CB   A VAL   A 1 30  ? 18.838 -3.511  17.974  0.62 20.08 ?  30  VAL   A CB   1 
ATOM   841  C  CB   B VAL   A 1 30  ? 18.500 -3.128  17.893  0.38 19.13 ?  30  VAL   A CB   1 
ATOM   842  C  CG1  A VAL   A 1 30  ? 19.638 -4.798  18.148  0.62 20.44 ?  30  VAL   A CG1  1 
ATOM   843  C  CG1  B VAL   A 1 30  ? 19.214 -4.436  18.204  0.38 19.45 ?  30  VAL   A CG1  1 
ATOM   844  C  CG2  A VAL   A 1 30  ? 17.347 -3.812  17.911  0.62 20.85 ?  30  VAL   A CG2  1 
ATOM   845  C  CG2  B VAL   A 1 30  ? 17.000 -3.354  17.762  0.38 19.20 ?  30  VAL   A CG2  1 
ATOM   846  H  H    A VAL   A 1 30  ? 18.347 -1.093  17.996  0.62 24.14 ?  30  VAL   A H    1 
ATOM   847  H  H    B VAL   A 1 30  ? 18.063 -0.678  17.777  0.38 22.70 ?  30  VAL   A H    1 
ATOM   848  H  HA   A VAL   A 1 30  ? 18.759 -2.886  19.923  0.62 23.17 ?  30  VAL   A HA   1 
ATOM   849  H  HA   B VAL   A 1 30  ? 18.393 -2.390  19.799  0.38 22.75 ?  30  VAL   A HA   1 
ATOM   850  H  HB   A VAL   A 1 30  ? 19.096 -3.114  17.128  0.62 24.08 ?  30  VAL   A HB   1 
ATOM   851  H  HB   B VAL   A 1 30  ? 18.829 -2.806  17.039  0.38 22.94 ?  30  VAL   A HB   1 
ATOM   852  H  HG11 A VAL   A 1 30  ? 19.259 -5.482  17.572  0.62 24.51 ?  30  VAL   A HG11 1 
ATOM   853  H  HG11 B VAL   A 1 30  ? 18.847 -5.136  17.642  0.38 23.32 ?  30  VAL   A HG11 1 
ATOM   854  H  HG12 A VAL   A 1 30  ? 20.560 -4.634  17.902  0.62 24.51 ?  30  VAL   A HG12 1 
ATOM   855  H  HG12 B VAL   A 1 30  ? 20.161 -4.331  18.024  0.38 23.32 ?  30  VAL   A HG12 1 
ATOM   856  H  HG13 A VAL   A 1 30  ? 19.582 -5.080  19.074  0.62 24.51 ?  30  VAL   A HG13 1 
ATOM   857  H  HG13 B VAL   A 1 30  ? 19.075 -4.655  19.138  0.38 23.32 ?  30  VAL   A HG13 1 
ATOM   858  H  HG21 A VAL   A 1 30  ? 17.184 -4.463  17.210  0.62 25.00 ?  30  VAL   A HG21 1 
ATOM   859  H  HG21 B VAL   A 1 30  ? 16.841 -4.055  17.109  0.38 23.03 ?  30  VAL   A HG21 1 
ATOM   860  H  HG22 A VAL   A 1 30  ? 17.060 -4.170  18.766  0.62 25.00 ?  30  VAL   A HG22 1 
ATOM   861  H  HG22 B VAL   A 1 30  ? 16.645 -3.620  18.625  0.38 23.03 ?  30  VAL   A HG22 1 
ATOM   862  H  HG23 A VAL   A 1 30  ? 16.867 -2.992  17.718  0.62 25.00 ?  30  VAL   A HG23 1 
ATOM   863  H  HG23 B VAL   A 1 30  ? 16.580 -2.530  17.471  0.38 23.03 ?  30  VAL   A HG23 1 
ATOM   864  N  N    A LYS   A 1 31  ? 21.275 -1.399  18.662  0.62 16.92 ?  31  LYS   A N    1 
ATOM   865  N  N    B LYS   A 1 31  ? 20.949 -1.051  18.457  0.38 18.83 ?  31  LYS   A N    1 
ATOM   866  C  CA   A LYS   A 1 31  ? 22.729 -1.295  18.610  0.62 17.38 ?  31  LYS   A CA   1 
ATOM   867  C  CA   B LYS   A 1 31  ? 22.405 -0.957  18.423  0.38 19.13 ?  31  LYS   A CA   1 
ATOM   868  C  C    A LYS   A 1 31  ? 23.333 -2.653  18.244  0.62 15.70 ?  31  LYS   A C    1 
ATOM   869  C  C    B LYS   A 1 31  ? 23.014 -2.340  18.238  0.38 18.16 ?  31  LYS   A C    1 
ATOM   870  O  O    A LYS   A 1 31  ? 24.118 -3.221  19.011  0.62 16.46 ?  31  LYS   A O    1 
ATOM   871  O  O    B LYS   A 1 31  ? 23.704 -2.846  19.134  0.38 18.73 ?  31  LYS   A O    1 
ATOM   872  C  CB   A LYS   A 1 31  ? 23.312 -0.767  19.914  0.62 21.10 ?  31  LYS   A CB   1 
ATOM   873  C  CB   B LYS   A 1 31  ? 22.960 -0.268  19.668  0.38 20.57 ?  31  LYS   A CB   1 
ATOM   874  C  CG   A LYS   A 1 31  ? 22.623 0.485   20.436  0.62 25.87 ?  31  LYS   A CG   1 
ATOM   875  C  CG   B LYS   A 1 31  ? 22.617 1.204   19.721  0.38 22.48 ?  31  LYS   A CG   1 
ATOM   876  C  CD   A LYS   A 1 31  ? 23.625 1.560   20.835  0.62 29.61 ?  31  LYS   A CD   1 
ATOM   877  C  CD   B LYS   A 1 31  ? 23.111 1.849   21.000  0.38 23.84 ?  31  LYS   A CD   1 
ATOM   878  C  CE   A LYS   A 1 31  ? 22.987 2.616   21.731  0.62 32.01 ?  31  LYS   A CE   1 
ATOM   879  C  CE   B LYS   A 1 31  ? 22.143 2.919   21.466  0.38 24.77 ?  31  LYS   A CE   1 
ATOM   880  N  NZ   A LYS   A 1 31  ? 21.810 3.282   21.101  0.62 33.35 ?  31  LYS   A NZ   1 
ATOM   881  N  NZ   B LYS   A 1 31  ? 20.783 2.350   21.686  0.38 25.05 ?  31  LYS   A NZ   1 
ATOM   882  H  H    A LYS   A 1 31  ? 20.872 -0.782  18.221  0.62 20.29 ?  31  LYS   A H    1 
ATOM   883  H  H    B LYS   A 1 31  ? 20.559 -0.487  17.938  0.38 22.58 ?  31  LYS   A H    1 
ATOM   884  H  HA   A LYS   A 1 31  ? 22.964 -0.670  17.912  0.62 20.84 ?  31  LYS   A HA   1 
ATOM   885  H  HA   B LYS   A 1 31  ? 22.648 -0.413  17.670  0.38 22.94 ?  31  LYS   A HA   1 
ATOM   886  H  HB2  A LYS   A 1 31  ? 23.236 -1.456  20.589  0.62 25.30 ?  31  LYS   A HB2  1 
ATOM   887  H  HB2  B LYS   A 1 31  ? 22.596 -0.690  20.459  0.38 24.66 ?  31  LYS   A HB2  1 
ATOM   888  H  HB3  A LYS   A 1 31  ? 24.248 -0.552  19.768  0.62 25.30 ?  31  LYS   A HB3  1 
ATOM   889  H  HB3  B LYS   A 1 31  ? 23.928 -0.347  19.662  0.38 24.66 ?  31  LYS   A HB3  1 
ATOM   890  H  HG2  A LYS   A 1 31  ? 22.050 0.848   19.743  0.62 31.02 ?  31  LYS   A HG2  1 
ATOM   891  H  HG2  B LYS   A 1 31  ? 23.040 1.656   18.975  0.38 26.96 ?  31  LYS   A HG2  1 
ATOM   892  H  HG3  A LYS   A 1 31  ? 22.098 0.256   21.219  0.62 31.02 ?  31  LYS   A HG3  1 
ATOM   893  H  HG3  B LYS   A 1 31  ? 21.655 1.306   19.664  0.38 26.96 ?  31  LYS   A HG3  1 
ATOM   894  H  HD2  A LYS   A 1 31  ? 24.358 1.152   21.322  0.62 35.52 ?  31  LYS   A HD2  1 
ATOM   895  H  HD2  B LYS   A 1 31  ? 23.186 1.175   21.694  0.38 28.60 ?  31  LYS   A HD2  1 
ATOM   896  H  HD3  A LYS   A 1 31  ? 23.958 2.001   20.036  0.62 35.52 ?  31  LYS   A HD3  1 
ATOM   897  H  HD3  B LYS   A 1 31  ? 23.976 2.263   20.838  0.38 28.60 ?  31  LYS   A HD3  1 
ATOM   898  H  HE2  A LYS   A 1 31  ? 22.687 2.194   22.551  0.62 38.39 ?  31  LYS   A HE2  1 
ATOM   899  H  HE2  B LYS   A 1 31  ? 22.457 3.293   22.303  0.38 29.71 ?  31  LYS   A HE2  1 
ATOM   900  H  HE3  A LYS   A 1 31  ? 23.644 3.301   21.932  0.62 38.39 ?  31  LYS   A HE3  1 
ATOM   901  H  HE3  B LYS   A 1 31  ? 22.080 3.611   20.789  0.38 29.71 ?  31  LYS   A HE3  1 
ATOM   902  H  HZ1  A LYS   A 1 31  ? 21.474 3.893   21.656  0.62 40.00 ?  31  LYS   A HZ1  1 
ATOM   903  H  HZ1  B LYS   A 1 31  ? 20.314 2.885   22.216  0.38 30.05 ?  31  LYS   A HZ1  1 
ATOM   904  H  HZ2  A LYS   A 1 31  ? 22.055 3.681   20.345  0.62 40.00 ?  31  LYS   A HZ2  1 
ATOM   905  H  HZ2  B LYS   A 1 31  ? 20.357 2.266   20.908  0.38 30.05 ?  31  LYS   A HZ2  1 
ATOM   906  H  HZ3  A LYS   A 1 31  ? 21.181 2.679   20.920  0.62 40.00 ?  31  LYS   A HZ3  1 
ATOM   907  H  HZ3  B LYS   A 1 31  ? 20.848 1.547   22.067  0.38 30.05 ?  31  LYS   A HZ3  1 
ATOM   908  N  N    A PRO   A 1 32  ? 22.976 -3.198  17.084  0.62 14.20 ?  32  PRO   A N    1 
ATOM   909  N  N    B PRO   A 1 32  ? 22.797 -2.971  17.087  0.38 16.67 ?  32  PRO   A N    1 
ATOM   910  C  CA   A PRO   A 1 32  ? 23.443 -4.536  16.717  0.62 14.68 ?  32  PRO   A CA   1 
ATOM   911  C  CA   B PRO   A 1 32  ? 23.279 -4.339  16.888  0.38 16.14 ?  32  PRO   A CA   1 
ATOM   912  C  C    A PRO   A 1 32  ? 24.943 -4.554  16.503  0.62 14.86 ?  32  PRO   A C    1 
ATOM   913  C  C    B PRO   A 1 32  ? 24.785 -4.370  16.689  0.38 15.49 ?  32  PRO   A C    1 
ATOM   914  O  O    A PRO   A 1 32  ? 25.577 -3.532  16.227  0.62 14.56 ?  32  PRO   A O    1 
ATOM   915  O  O    B PRO   A 1 32  ? 25.463 -3.345  16.603  0.38 15.67 ?  32  PRO   A O    1 
ATOM   916  C  CB   A PRO   A 1 32  ? 22.717 -4.802  15.395  0.62 14.94 ?  32  PRO   A CB   1 
ATOM   917  C  CB   B PRO   A 1 32  ? 22.551 -4.770  15.613  0.38 16.30 ?  32  PRO   A CB   1 
ATOM   918  C  CG   A PRO   A 1 32  ? 22.563 -3.434  14.800  0.62 13.82 ?  32  PRO   A CG   1 
ATOM   919  C  CG   B PRO   A 1 32  ? 22.437 -3.505  14.836  0.38 16.16 ?  32  PRO   A CG   1 
ATOM   920  C  CD   A PRO   A 1 32  ? 22.247 -2.555  15.979  0.62 13.52 ?  32  PRO   A CD   1 
ATOM   921  C  CD   B PRO   A 1 32  ? 22.162 -2.438  15.869  0.38 16.31 ?  32  PRO   A CD   1 
ATOM   922  H  HA   A PRO   A 1 32  ? 23.184 -5.195  17.383  0.62 17.60 ?  32  PRO   A HA   1 
ATOM   923  H  HA   B PRO   A 1 32  ? 23.028 -4.913  17.625  0.38 19.35 ?  32  PRO   A HA   1 
ATOM   924  H  HB2  A PRO   A 1 32  ? 23.263 -5.373  14.827  0.62 17.91 ?  32  PRO   A HB2  1 
ATOM   925  H  HB2  B PRO   A 1 32  ? 23.075 -5.429  15.131  0.38 19.55 ?  32  PRO   A HB2  1 
ATOM   926  H  HB3  A PRO   A 1 32  ? 21.853 -5.211  15.566  0.62 17.91 ?  32  PRO   A HB3  1 
ATOM   927  H  HB3  B PRO   A 1 32  ? 21.671 -5.119  15.832  0.38 19.55 ?  32  PRO   A HB3  1 
ATOM   928  H  HG2  A PRO   A 1 32  ? 23.393 -3.170  14.375  0.62 16.57 ?  32  PRO   A HG2  1 
ATOM   929  H  HG2  B PRO   A 1 32  ? 23.274 -3.335  14.373  0.38 19.38 ?  32  PRO   A HG2  1 
ATOM   930  H  HG3  A PRO   A 1 32  ? 21.832 -3.440  14.161  0.62 16.57 ?  32  PRO   A HG3  1 
ATOM   931  H  HG3  B PRO   A 1 32  ? 21.705 -3.575  14.203  0.38 19.38 ?  32  PRO   A HG3  1 
ATOM   932  H  HD2  A PRO   A 1 32  ? 22.584 -1.660  15.817  0.62 16.20 ?  32  PRO   A HD2  1 
ATOM   933  H  HD2  B PRO   A 1 32  ? 22.577 -1.603  15.603  0.38 19.56 ?  32  PRO   A HD2  1 
ATOM   934  H  HD3  A PRO   A 1 32  ? 21.295 -2.556  16.148  0.62 16.20 ?  32  PRO   A HD3  1 
ATOM   935  H  HD3  B PRO   A 1 32  ? 21.209 -2.339  16.002  0.38 19.56 ?  32  PRO   A HD3  1 
ATOM   936  N  N    A THR   A 1 33  ? 25.508 -5.757  16.600  0.62 15.33 ?  33  THR   A N    1 
ATOM   937  N  N    B THR   A 1 33  ? 25.306 -5.594  16.615  0.38 15.10 ?  33  THR   A N    1 
ATOM   938  C  CA   A THR   A 1 33  ? 26.918 -5.919  16.280  0.62 15.68 ?  33  THR   A CA   1 
ATOM   939  C  CA   B THR   A 1 33  ? 26.722 -5.785  16.322  0.38 14.68 ?  33  THR   A CA   1 
ATOM   940  C  C    A THR   A 1 33  ? 27.202 -5.486  14.848  0.62 14.26 ?  33  THR   A C    1 
ATOM   941  C  C    B THR   A 1 33  ? 27.057 -5.315  14.910  0.38 13.86 ?  33  THR   A C    1 
ATOM   942  O  O    A THR   A 1 33  ? 28.260 -4.904  14.569  0.62 13.76 ?  33  THR   A O    1 
ATOM   943  O  O    B THR   A 1 33  ? 28.028 -4.577  14.703  0.38 13.92 ?  33  THR   A O    1 
ATOM   944  C  CB   A THR   A 1 33  ? 27.345 -7.369  16.512  0.62 17.59 ?  33  THR   A CB   1 
ATOM   945  C  CB   B THR   A 1 33  ? 27.079 -7.261  16.498  0.38 15.83 ?  33  THR   A CB   1 
ATOM   946  O  OG1  A THR   A 1 33  ? 27.125 -7.722  17.882  0.62 19.04 ?  33  THR   A OG1  1 
ATOM   947  O  OG1  B THR   A 1 33  ? 26.704 -7.685  17.814  0.38 16.46 ?  33  THR   A OG1  1 
ATOM   948  C  CG2  A THR   A 1 33  ? 28.816 -7.557  16.189  0.62 18.58 ?  33  THR   A CG2  1 
ATOM   949  C  CG2  B THR   A 1 33  ? 28.569 -7.481  16.295  0.38 16.45 ?  33  THR   A CG2  1 
ATOM   950  H  H    A THR   A 1 33  ? 25.105 -6.479  16.832  0.62 18.38 ?  33  THR   A H    1 
ATOM   951  H  H    B THR   A 1 33  ? 24.867 -6.322  16.742  0.38 18.10 ?  33  THR   A H    1 
ATOM   952  H  HA   A THR   A 1 33  ? 27.445 -5.356  16.870  0.62 18.80 ?  33  THR   A HA   1 
ATOM   953  H  HA   B THR   A 1 33  ? 27.250 -5.270  16.952  0.38 17.60 ?  33  THR   A HA   1 
ATOM   954  H  HB   A THR   A 1 33  ? 26.821 -7.954  15.940  0.62 21.10 ?  33  THR   A HB   1 
ATOM   955  H  HB   B THR   A 1 33  ? 26.596 -7.793  15.842  0.38 18.98 ?  33  THR   A HB   1 
ATOM   956  H  HG1  A THR   A 1 33  ? 27.569 -7.218  18.386  0.62 22.84 ?  33  THR   A HG1  1 
ATOM   957  H  HG1  B THR   A 1 33  ? 27.128 -7.240  18.391  0.38 19.74 ?  33  THR   A HG1  1 
ATOM   958  H  HG21 A THR   A 1 33  ? 29.117 -8.416  16.524  0.62 22.28 ?  33  THR   A HG21 1 
ATOM   959  H  HG21 B THR   A 1 33  ? 28.809 -8.385  16.552  0.38 19.72 ?  33  THR   A HG21 1 
ATOM   960  H  HG22 A THR   A 1 33  ? 28.954 -7.526  15.232  0.62 22.28 ?  33  THR   A HG22 1 
ATOM   961  H  HG22 B THR   A 1 33  ? 28.802 -7.349  15.362  0.38 19.72 ?  33  THR   A HG22 1 
ATOM   962  H  HG23 A THR   A 1 33  ? 29.337 -6.856  16.611  0.62 22.28 ?  33  THR   A HG23 1 
ATOM   963  H  HG23 B THR   A 1 33  ? 29.072 -6.855  16.838  0.38 19.72 ?  33  THR   A HG23 1 
ATOM   964  N  N    . VAL   A 1 34  ? 26.266 -5.741  13.929  1.00 13.21 ?  34  VAL   A N    1 
ATOM   965  C  CA   . VAL   A 1 34  ? 26.465 -5.416  12.521  1.00 11.95 ?  34  VAL   A CA   1 
ATOM   966  C  C    . VAL   A 1 34  ? 25.172 -4.855  11.946  1.00 11.21 ?  34  VAL   A C    1 
ATOM   967  O  O    . VAL   A 1 34  ? 24.131 -5.524  11.986  1.00 12.24 ?  34  VAL   A O    1 
ATOM   968  C  CB   . VAL   A 1 34  ? 26.908 -6.634  11.688  1.00 12.85 ?  34  VAL   A CB   1 
ATOM   969  C  CG1  . VAL   A 1 34  ? 27.084 -6.234  10.233  1.00 12.99 ?  34  VAL   A CG1  1 
ATOM   970  C  CG2  . VAL   A 1 34  ? 28.192 -7.245  12.236  1.00 14.08 ?  34  VAL   A CG2  1 
ATOM   971  H  H    A VAL   A 1 34  ? 25.504 -6.099  14.105  0.62 15.84 ?  34  VAL   A H    1 
ATOM   972  H  H    B VAL   A 1 34  ? 25.583 -6.244  14.064  0.38 15.84 ?  34  VAL   A H    1 
ATOM   973  H  HA   . VAL   A 1 34  ? 27.149 -4.732  12.440  1.00 14.33 ?  34  VAL   A HA   1 
ATOM   974  H  HB   . VAL   A 1 34  ? 26.213 -7.311  11.737  1.00 15.40 ?  34  VAL   A HB   1 
ATOM   975  H  HG11 . VAL   A 1 34  ? 27.589 -6.925  9.780   1.00 15.57 ?  34  VAL   A HG11 1 
ATOM   976  H  HG12 . VAL   A 1 34  ? 26.209 -6.142  9.823   1.00 15.57 ?  34  VAL   A HG12 1 
ATOM   977  H  HG13 . VAL   A 1 34  ? 27.561 -5.393  10.195  1.00 15.57 ?  34  VAL   A HG13 1 
ATOM   978  H  HG21 . VAL   A 1 34  ? 28.467 -7.974  11.655  1.00 16.88 ?  34  VAL   A HG21 1 
ATOM   979  H  HG22 . VAL   A 1 34  ? 28.882 -6.565  12.262  1.00 16.88 ?  34  VAL   A HG22 1 
ATOM   980  H  HG23 . VAL   A 1 34  ? 28.028 -7.585  13.131  1.00 16.88 ?  34  VAL   A HG23 1 
ATOM   981  N  N    . VAL   A 1 35  ? 25.245 -3.650  11.381  1.00 10.53 ?  35  VAL   A N    1 
ATOM   982  C  CA   . VAL   A 1 35  ? 24.213 -3.135  10.491  1.00 10.30 ?  35  VAL   A CA   1 
ATOM   983  C  C    . VAL   A 1 35  ? 24.766 -3.146  9.073   1.00 9.76  ?  35  VAL   A C    1 
ATOM   984  O  O    . VAL   A 1 35  ? 25.912 -2.745  8.842   1.00 10.62 ?  35  VAL   A O    1 
ATOM   985  C  CB   . VAL   A 1 35  ? 23.688 -1.739  10.897  1.00 11.05 ?  35  VAL   A CB   1 
ATOM   986  C  CG1  . VAL   A 1 35  ? 24.760 -0.646  10.762  1.00 11.90 ?  35  VAL   A CG1  1 
ATOM   987  C  CG2  . VAL   A 1 35  ? 22.458 -1.388  10.068  1.00 11.56 ?  35  VAL   A CG2  1 
ATOM   988  H  H    . VAL   A 1 35  ? 25.892 -3.097  11.502  1.00 12.62 ?  35  VAL   A H    1 
ATOM   989  H  HA   . VAL   A 1 35  ? 23.453 -3.743  10.512  1.00 12.34 ?  35  VAL   A HA   1 
ATOM   990  H  HB   . VAL   A 1 35  ? 23.406 -1.767  11.824  1.00 13.24 ?  35  VAL   A HB   1 
ATOM   991  H  HG11 . VAL   A 1 35  ? 24.414 0.187   11.127  1.00 14.26 ?  35  VAL   A HG11 1 
ATOM   992  H  HG12 . VAL   A 1 35  ? 25.550 -0.916  11.253  1.00 14.26 ?  35  VAL   A HG12 1 
ATOM   993  H  HG13 . VAL   A 1 35  ? 24.979 -0.524  9.823   1.00 14.26 ?  35  VAL   A HG13 1 
ATOM   994  H  HG21 . VAL   A 1 35  ? 22.091 -0.547  10.375  1.00 13.86 ?  35  VAL   A HG21 1 
ATOM   995  H  HG22 . VAL   A 1 35  ? 22.715 -1.312  9.131   1.00 13.86 ?  35  VAL   A HG22 1 
ATOM   996  H  HG23 . VAL   A 1 35  ? 21.795 -2.093  10.164  1.00 13.86 ?  35  VAL   A HG23 1 
ATOM   997  N  N    . VAL   A 1 36  ? 23.954 -3.611  8.124   1.00 9.24  ?  36  VAL   A N    1 
ATOM   998  C  CA   . VAL   A 1 36  ? 24.329 -3.629  6.720   1.00 8.80  ?  36  VAL   A CA   1 
ATOM   999  C  C    . VAL   A 1 36  ? 23.872 -2.341  6.048   1.00 9.05  ?  36  VAL   A C    1 
ATOM   1000 O  O    . VAL   A 1 36  ? 22.707 -1.940  6.169   1.00 9.87  ?  36  VAL   A O    1 
ATOM   1001 C  CB   . VAL   A 1 36  ? 23.724 -4.847  6.005   1.00 9.16  ?  36  VAL   A CB   1 
ATOM   1002 C  CG1  . VAL   A 1 36  ? 23.989 -4.776  4.521   1.00 9.85  ?  36  VAL   A CG1  1 
ATOM   1003 C  CG2  . VAL   A 1 36  ? 24.262 -6.134  6.594   1.00 10.16 ?  36  VAL   A CG2  1 
ATOM   1004 H  H    . VAL   A 1 36  ? 23.166 -3.939  8.277   1.00 11.08 ?  36  VAL   A H    1 
ATOM   1005 H  HA   . VAL   A 1 36  ? 25.298 -3.687  6.650   1.00 10.54 ?  36  VAL   A HA   1 
ATOM   1006 H  HB   . VAL   A 1 36  ? 22.765 -4.836  6.133   1.00 10.97 ?  36  VAL   A HB   1 
ATOM   1007 H  HG11 . VAL   A 1 36  ? 23.854 -5.652  4.130   1.00 11.81 ?  36  VAL   A HG11 1 
ATOM   1008 H  HG12 . VAL   A 1 36  ? 23.375 -4.138  4.113   1.00 11.81 ?  36  VAL   A HG12 1 
ATOM   1009 H  HG13 . VAL   A 1 36  ? 24.905 -4.487  4.372   1.00 11.81 ?  36  VAL   A HG13 1 
ATOM   1010 H  HG21 . VAL   A 1 36  ? 23.881 -6.887  6.113   1.00 12.17 ?  36  VAL   A HG21 1 
ATOM   1011 H  HG22 . VAL   A 1 36  ? 25.229 -6.144  6.507   1.00 12.17 ?  36  VAL   A HG22 1 
ATOM   1012 H  HG23 . VAL   A 1 36  ? 24.014 -6.183  7.530   1.00 12.17 ?  36  VAL   A HG23 1 
ATOM   1013 N  N    . ASN   A 1 37  ? 24.797 -1.702  5.324   1.00 8.85  ?  37  ASN   A N    1 
ATOM   1014 C  CA   . ASN   A 1 37  ? 24.472 -0.587  4.451   1.00 8.67  ?  37  ASN   A CA   1 
ATOM   1015 C  C    . ASN   A 1 37  ? 24.337 -1.070  3.017   1.00 8.68  ?  37  ASN   A C    1 
ATOM   1016 O  O    . ASN   A 1 37  ? 25.119 -1.908  2.548   1.00 9.51  ?  37  ASN   A O    1 
ATOM   1017 C  CB   . ASN   A 1 37  ? 25.551 0.491   4.529   1.00 9.31  ?  37  ASN   A CB   1 
ATOM   1018 C  CG   . ASN   A 1 37  ? 25.228 1.684   3.672   1.00 9.39  ?  37  ASN   A CG   1 
ATOM   1019 O  OD1  . ASN   A 1 37  ? 24.057 2.016   3.475   1.00 10.02 ?  37  ASN   A OD1  1 
ATOM   1020 N  ND2  . ASN   A 1 37  ? 26.262 2.330   3.147   1.00 9.69  ?  37  ASN   A ND2  1 
ATOM   1021 H  H    . ASN   A 1 37  ? 25.635 -1.896  5.336   1.00 10.60 ?  37  ASN   A H    1 
ATOM   1022 H  HA   . ASN   A 1 37  ? 23.629 -0.193  4.725   1.00 10.39 ?  37  ASN   A HA   1 
ATOM   1023 H  HB2  . ASN   A 1 37  ? 25.633 0.793   5.449   1.00 11.16 ?  37  ASN   A HB2  1 
ATOM   1024 H  HB3  . ASN   A 1 37  ? 26.397 0.118   4.227   1.00 11.16 ?  37  ASN   A HB3  1 
ATOM   1025 H  HD21 . ASN   A 1 37  ? 26.128 3.020   2.648   1.00 11.62 ?  37  ASN   A HD21 1 
ATOM   1026 H  HD22 . ASN   A 1 37  ? 27.061 2.073   3.306   1.00 11.62 ?  37  ASN   A HD22 1 
ATOM   1027 N  N    A ALA   A 1 38  ? 23.319 -0.537  2.337   0.62 8.96  ?  38  ALA   A N    1 
ATOM   1028 N  N    B ALA   A 1 38  ? 23.331 -0.542  2.313   0.38 9.08  ?  38  ALA   A N    1 
ATOM   1029 C  CA   A ALA   A 1 38  ? 23.127 -0.684  0.896   0.62 9.23  ?  38  ALA   A CA   1 
ATOM   1030 C  CA   B ALA   A 1 38  ? 23.170 -0.796  0.879   0.38 9.63  ?  38  ALA   A CA   1 
ATOM   1031 C  C    A ALA   A 1 38  ? 24.042 0.322   0.196   0.62 9.19  ?  38  ALA   A C    1 
ATOM   1032 C  C    B ALA   A 1 38  ? 24.011 0.227   0.113   0.38 9.33  ?  38  ALA   A C    1 
ATOM   1033 O  O    A ALA   A 1 38  ? 23.639 1.428   -0.178  0.62 9.05  ?  38  ALA   A O    1 
ATOM   1034 O  O    B ALA   A 1 38  ? 23.526 1.241   -0.400  0.38 9.50  ?  38  ALA   A O    1 
ATOM   1035 C  CB   A ALA   A 1 38  ? 21.665 -0.441  0.541   0.62 9.98  ?  38  ALA   A CB   1 
ATOM   1036 C  CB   B ALA   A 1 38  ? 21.699 -0.758  0.485   0.38 10.52 ?  38  ALA   A CB   1 
ATOM   1037 H  H    A ALA   A 1 38  ? 22.710 -0.055  2.708   0.62 10.74 ?  38  ALA   A H    1 
ATOM   1038 H  H    B ALA   A 1 38  ? 22.725 -0.030  2.649   0.38 10.88 ?  38  ALA   A H    1 
ATOM   1039 H  HA   A ALA   A 1 38  ? 23.377 -1.577  0.620   0.62 11.06 ?  38  ALA   A HA   1 
ATOM   1040 H  HA   B ALA   A 1 38  ? 23.514 -1.684  0.679   0.38 11.54 ?  38  ALA   A HA   1 
ATOM   1041 H  HB1  A ALA   A 1 38  ? 21.550 -0.546  -0.415  0.62 11.96 ?  38  ALA   A HB1  1 
ATOM   1042 H  HB1  B ALA   A 1 38  ? 21.628 -0.917  -0.468  0.38 12.61 ?  38  ALA   A HB1  1 
ATOM   1043 H  HB2  A ALA   A 1 38  ? 21.116 -1.087  1.015   0.62 11.96 ?  38  ALA   A HB2  1 
ATOM   1044 H  HB2  B ALA   A 1 38  ? 21.222 -1.449  0.973   0.38 12.61 ?  38  ALA   A HB2  1 
ATOM   1045 H  HB3  A ALA   A 1 38  ? 21.419 0.459   0.809   0.62 11.96 ?  38  ALA   A HB3  1 
ATOM   1046 H  HB3  B ALA   A 1 38  ? 21.338 0.113   0.704   0.38 12.61 ?  38  ALA   A HB3  1 
ATOM   1047 N  N    . ALA   A 1 39  ? 25.305 -0.067  0.040   1.00 9.51  ?  39  ALA   A N    1 
ATOM   1048 C  CA   . ALA   A 1 39  ? 26.331 0.833   -0.460  1.00 9.64  ?  39  ALA   A CA   1 
ATOM   1049 C  C    . ALA   A 1 39  ? 26.458 0.768   -1.977  1.00 9.56  ?  39  ALA   A C    1 
ATOM   1050 O  O    . ALA   A 1 39  ? 25.981 -0.159  -2.633  1.00 10.03 ?  39  ALA   A O    1 
ATOM   1051 C  CB   . ALA   A 1 39  ? 27.673 0.464   0.180   1.00 10.64 ?  39  ALA   A CB   1 
ATOM   1052 H  H    A ALA   A 1 39  ? 25.591 -0.859  0.225   0.62 11.39 ?  39  ALA   A H    1 
ATOM   1053 H  H    B ALA   A 1 39  ? 25.626 -0.828  0.291   0.38 11.39 ?  39  ALA   A H    1 
ATOM   1054 H  HA   . ALA   A 1 39  ? 26.104 1.743   -0.208  1.00 11.56 ?  39  ALA   A HA   1 
ATOM   1055 H  HB1  . ALA   A 1 39  ? 28.351 1.072   -0.153  1.00 12.75 ?  39  ALA   A HB1  1 
ATOM   1056 H  HB2  . ALA   A 1 39  ? 27.593 0.560   1.147   1.00 12.75 ?  39  ALA   A HB2  1 
ATOM   1057 H  HB3  . ALA   A 1 39  ? 27.892 -0.445  -0.047  1.00 12.75 ?  39  ALA   A HB3  1 
ATOM   1058 N  N    A ASN   A 1 40  ? 27.176 1.756   -2.519  0.62 9.95  ?  40  ASN   A N    1 
ATOM   1059 N  N    B ASN   A 1 40  ? 27.073 1.796   -2.550  0.38 9.81  ?  40  ASN   A N    1 
ATOM   1060 C  CA   A ASN   A 1 40  ? 27.740 1.707   -3.860  0.62 9.67  ?  40  ASN   A CA   1 
ATOM   1061 C  CA   B ASN   A 1 40  ? 27.507 1.750   -3.938  0.38 9.86  ?  40  ASN   A CA   1 
ATOM   1062 C  C    A ASN   A 1 40  ? 29.261 1.606   -3.767  0.62 8.72  ?  40  ASN   A C    1 
ATOM   1063 C  C    B ASN   A 1 40  ? 29.029 1.628   -3.967  0.38 9.49  ?  40  ASN   A C    1 
ATOM   1064 O  O    A ASN   A 1 40  ? 29.847 1.718   -2.687  0.62 8.98  ?  40  ASN   A O    1 
ATOM   1065 O  O    B ASN   A 1 40  ? 29.696 1.723   -2.935  0.38 9.84  ?  40  ASN   A O    1 
ATOM   1066 C  CB   A ASN   A 1 40  ? 27.280 2.892   -4.731  0.62 10.48 ?  40  ASN   A CB   1 
ATOM   1067 C  CB   B ASN   A 1 40  ? 27.004 2.971   -4.725  0.38 10.51 ?  40  ASN   A CB   1 
ATOM   1068 C  CG   A ASN   A 1 40  ? 27.629 4.251   -4.140  0.62 11.16 ?  40  ASN   A CG   1 
ATOM   1069 C  CG   B ASN   A 1 40  ? 27.470 4.284   -4.132  0.38 11.54 ?  40  ASN   A CG   1 
ATOM   1070 O  OD1  A ASN   A 1 40  ? 28.776 4.506   -3.762  0.62 11.68 ?  40  ASN   A OD1  1 
ATOM   1071 O  OD1  B ASN   A 1 40  ? 28.666 4.583   -4.115  0.38 11.79 ?  40  ASN   A OD1  1 
ATOM   1072 N  ND2  A ASN   A 1 40  ? 26.630 5.137   -4.067  0.62 11.85 ?  40  ASN   A ND2  1 
ATOM   1073 N  ND2  B ASN   A 1 40  ? 26.522 5.084   -3.652  0.38 12.40 ?  40  ASN   A ND2  1 
ATOM   1074 H  H    A ASN   A 1 40  ? 27.366 2.480   -2.102  0.62 11.92 ?  40  ASN   A H    1 
ATOM   1075 H  H    B ASN   A 1 40  ? 27.244 2.537   -2.152  0.38 11.75 ?  40  ASN   A H    1 
ATOM   1076 H  HA   A ASN   A 1 40  ? 27.442 0.898   -4.289  0.62 11.58 ?  40  ASN   A HA   1 
ATOM   1077 H  HA   B ASN   A 1 40  ? 27.129 0.954   -4.360  0.38 11.81 ?  40  ASN   A HA   1 
ATOM   1078 H  HB2  A ASN   A 1 40  ? 27.704 2.821   -5.602  0.62 12.56 ?  40  ASN   A HB2  1 
ATOM   1079 H  HB2  B ASN   A 1 40  ? 27.331 2.916   -5.634  0.38 12.60 ?  40  ASN   A HB2  1 
ATOM   1080 H  HB3  A ASN   A 1 40  ? 26.320 2.846   -4.825  0.62 12.56 ?  40  ASN   A HB3  1 
ATOM   1081 H  HB3  B ASN   A 1 40  ? 26.028 2.967   -4.725  0.38 12.60 ?  40  ASN   A HB3  1 
ATOM   1082 H  HD21 A ASN   A 1 40  ? 26.775 5.925   -3.748  0.62 14.20 ?  40  ASN   A HD21 1 
ATOM   1083 H  HD21 B ASN   A 1 40  ? 26.739 5.841   -3.304  0.38 14.86 ?  40  ASN   A HD21 1 
ATOM   1084 H  HD22 A ASN   A 1 40  ? 25.844 4.920   -4.332  0.62 14.20 ?  40  ASN   A HD22 1 
ATOM   1085 H  HD22 B ASN   A 1 40  ? 25.696 4.850   -3.687  0.38 14.86 ?  40  ASN   A HD22 1 
ATOM   1086 N  N    A VAL   A 1 41  ? 29.899 1.359   -4.916  0.62 8.91  ?  41  VAL   A N    1 
ATOM   1087 N  N    B VAL   A 1 41  ? 29.582 1.390   -5.159  0.38 9.66  ?  41  VAL   A N    1 
ATOM   1088 C  CA   A VAL   A 1 41  ? 31.330 1.054   -4.929  0.62 9.41  ?  41  VAL   A CA   1 
ATOM   1089 C  CA   B VAL   A 1 41  ? 31.006 1.070   -5.252  0.38 10.11 ?  41  VAL   A CA   1 
ATOM   1090 C  C    A VAL   A 1 41  ? 32.180 2.213   -4.440  0.62 9.16  ?  41  VAL   A C    1 
ATOM   1091 C  C    B VAL   A 1 41  ? 31.893 2.211   -4.769  0.38 10.14 ?  41  VAL   A C    1 
ATOM   1092 O  O    A VAL   A 1 41  ? 33.309 1.995   -3.985  0.62 9.56  ?  41  VAL   A O    1 
ATOM   1093 O  O    B VAL   A 1 41  ? 33.058 1.981   -4.424  0.38 9.92  ?  41  VAL   A O    1 
ATOM   1094 C  CB   A VAL   A 1 41  ? 31.827 0.552   -6.309  0.62 9.39  ?  41  VAL   A CB   1 
ATOM   1095 C  CB   B VAL   A 1 41  ? 31.412 0.638   -6.678  0.38 11.05 ?  41  VAL   A CB   1 
ATOM   1096 C  CG1  A VAL   A 1 41  ? 31.145 -0.759  -6.695  0.62 10.24 ?  41  VAL   A CG1  1 
ATOM   1097 C  CG1  B VAL   A 1 41  ? 30.736 -0.672  -7.056  0.38 11.72 ?  41  VAL   A CG1  1 
ATOM   1098 C  CG2  A VAL   A 1 41  ? 31.673 1.611   -7.404  0.62 9.74  ?  41  VAL   A CG2  1 
ATOM   1099 C  CG2  B VAL   A 1 41  ? 31.104 1.734   -7.691  0.38 11.39 ?  41  VAL   A CG2  1 
ATOM   1100 H  H    A VAL   A 1 41  ? 29.537 1.359   -5.689  0.62 10.68 ?  41  VAL   A H    1 
ATOM   1101 H  H    B VAL   A 1 41  ? 29.160 1.407   -5.908  0.38 11.58 ?  41  VAL   A H    1 
ATOM   1102 H  HA   A VAL   A 1 41  ? 31.493 0.330   -4.310  0.62 11.28 ?  41  VAL   A HA   1 
ATOM   1103 H  HA   B VAL   A 1 41  ? 31.172 0.307   -4.672  0.38 12.12 ?  41  VAL   A HA   1 
ATOM   1104 H  HB   A VAL   A 1 41  ? 32.775 0.359   -6.243  0.62 11.25 ?  41  VAL   A HB   1 
ATOM   1105 H  HB   B VAL   A 1 41  ? 32.367 0.484   -6.689  0.38 13.24 ?  41  VAL   A HB   1 
ATOM   1106 H  HG11 A VAL   A 1 41  ? 31.482 -1.062  -7.554  0.62 12.27 ?  41  VAL   A HG11 1 
ATOM   1107 H  HG11 B VAL   A 1 41  ? 30.949 -0.883  -7.977  0.38 14.04 ?  41  VAL   A HG11 1 
ATOM   1108 H  HG12 A VAL   A 1 41  ? 31.332 -1.429  -6.015  0.62 12.27 ?  41  VAL   A HG12 1 
ATOM   1109 H  HG12 B VAL   A 1 41  ? 31.064 -1.378  -6.472  0.38 14.04 ?  41  VAL   A HG12 1 
ATOM   1110 H  HG13 A VAL   A 1 41  ? 30.184 -0.616  -6.754  0.62 12.27 ?  41  VAL   A HG13 1 
ATOM   1111 H  HG13 B VAL   A 1 41  ? 29.777 -0.582  -6.950  0.38 14.04 ?  41  VAL   A HG13 1 
ATOM   1112 H  HG21 A VAL   A 1 41  ? 31.924 1.217   -8.260  0.62 11.67 ?  41  VAL   A HG21 1 
ATOM   1113 H  HG21 B VAL   A 1 41  ? 31.383 1.433   -8.570  0.38 13.66 ?  41  VAL   A HG21 1 
ATOM   1114 H  HG22 A VAL   A 1 41  ? 30.754 1.904   -7.434  0.62 11.67 ?  41  VAL   A HG22 1 
ATOM   1115 H  HG22 B VAL   A 1 41  ? 30.149 1.908   -7.691  0.38 13.66 ?  41  VAL   A HG22 1 
ATOM   1116 H  HG23 A VAL   A 1 41  ? 32.259 2.356   -7.204  0.62 11.67 ?  41  VAL   A HG23 1 
ATOM   1117 H  HG23 B VAL   A 1 41  ? 31.588 2.535   -7.446  0.38 13.66 ?  41  VAL   A HG23 1 
ATOM   1118 N  N    A TYR   A 1 42  ? 31.679 3.445   -4.541  0.62 9.44  ?  42  TYR   A N    1 
ATOM   1119 N  N    B TYR   A 1 42  ? 31.382 3.443   -4.761  0.38 10.42 ?  42  TYR   A N    1 
ATOM   1120 C  CA   A TYR   A 1 42  ? 32.413 4.634   -4.124  0.62 9.76  ?  42  TYR   A CA   1 
ATOM   1121 C  CA   B TYR   A 1 42  ? 32.150 4.610   -4.344  0.38 10.34 ?  42  TYR   A CA   1 
ATOM   1122 C  C    A TYR   A 1 42  ? 32.135 5.010   -2.679  0.62 9.79  ?  42  TYR   A C    1 
ATOM   1123 C  C    B TYR   A 1 42  ? 31.929 4.990   -2.888  0.38 9.77  ?  42  TYR   A C    1 
ATOM   1124 O  O    A TYR   A 1 42  ? 32.691 6.000   -2.186  0.62 10.42 ?  42  TYR   A O    1 
ATOM   1125 O  O    B TYR   A 1 42  ? 32.512 5.977   -2.423  0.38 10.46 ?  42  TYR   A O    1 
ATOM   1126 C  CB   A TYR   A 1 42  ? 32.075 5.817   -5.050  0.62 10.06 ?  42  TYR   A CB   1 
ATOM   1127 C  CB   B TYR   A 1 42  ? 31.806 5.808   -5.232  0.38 11.03 ?  42  TYR   A CB   1 
ATOM   1128 C  CG   A TYR   A 1 42  ? 32.267 5.488   -6.517  0.62 10.65 ?  42  TYR   A CG   1 
ATOM   1129 C  CG   B TYR   A 1 42  ? 31.991 5.519   -6.696  0.38 11.74 ?  42  TYR   A CG   1 
ATOM   1130 C  CD1  A TYR   A 1 42  ? 33.538 5.289   -7.040  0.62 11.80 ?  42  TYR   A CD1  1 
ATOM   1131 C  CD1  B TYR   A 1 42  ? 33.255 5.316   -7.224  0.38 11.97 ?  42  TYR   A CD1  1 
ATOM   1132 C  CD2  A TYR   A 1 42  ? 31.182 5.347   -7.374  0.62 12.30 ?  42  TYR   A CD2  1 
ATOM   1133 C  CD2  B TYR   A 1 42  ? 30.903 5.437   -7.551  0.38 12.92 ?  42  TYR   A CD2  1 
ATOM   1134 C  CE1  A TYR   A 1 42  ? 33.723 4.967   -8.374  0.62 12.46 ?  42  TYR   A CE1  1 
ATOM   1135 C  CE1  B TYR   A 1 42  ? 33.431 5.039   -8.563  0.38 12.28 ?  42  TYR   A CE1  1 
ATOM   1136 C  CE2  A TYR   A 1 42  ? 31.362 5.036   -8.713  0.62 13.49 ?  42  TYR   A CE2  1 
ATOM   1137 C  CE2  B TYR   A 1 42  ? 31.068 5.169   -8.889  0.38 13.62 ?  42  TYR   A CE2  1 
ATOM   1138 C  CZ   A TYR   A 1 42  ? 32.636 4.845   -9.206  0.62 13.35 ?  42  TYR   A CZ   1 
ATOM   1139 C  CZ   B TYR   A 1 42  ? 32.332 4.968   -9.393  0.38 13.02 ?  42  TYR   A CZ   1 
ATOM   1140 O  OH   A TYR   A 1 42  ? 32.821 4.527   -10.532 0.62 14.85 ?  42  TYR   A OH   1 
ATOM   1141 O  OH   B TYR   A 1 42  ? 32.493 4.700   -10.730 0.38 13.79 ?  42  TYR   A OH   1 
ATOM   1142 H  H    A TYR   A 1 42  ? 30.899 3.618   -4.847  0.62 11.31 ?  42  TYR   A H    1 
ATOM   1143 H  H    B TYR   A 1 42  ? 30.576 3.628   -5.010  0.38 12.49 ?  42  TYR   A H    1 
ATOM   1144 H  HA   A TYR   A 1 42  ? 33.366 4.468   -4.206  0.62 11.69 ?  42  TYR   A HA   1 
ATOM   1145 H  HA   B TYR   A 1 42  ? 33.090 4.417   -4.462  0.38 12.40 ?  42  TYR   A HA   1 
ATOM   1146 H  HB2  A TYR   A 1 42  ? 31.149 6.070   -4.920  0.62 12.06 ?  42  TYR   A HB2  1 
ATOM   1147 H  HB2  B TYR   A 1 42  ? 30.877 6.052   -5.087  0.38 13.22 ?  42  TYR   A HB2  1 
ATOM   1148 H  HB3  A TYR   A 1 42  ? 32.656 6.568   -4.837  0.62 12.06 ?  42  TYR   A HB3  1 
ATOM   1149 H  HB3  B TYR   A 1 42  ? 32.384 6.550   -4.995  0.38 13.22 ?  42  TYR   A HB3  1 
ATOM   1150 H  HD1  A TYR   A 1 42  ? 34.281 5.369   -6.485  0.62 14.15 ?  42  TYR   A HD1  1 
ATOM   1151 H  HD1  B TYR   A 1 42  ? 33.997 5.361   -6.660  0.38 14.35 ?  42  TYR   A HD1  1 
ATOM   1152 H  HD2  A TYR   A 1 42  ? 30.322 5.478   -7.046  0.62 14.74 ?  42  TYR   A HD2  1 
ATOM   1153 H  HD2  B TYR   A 1 42  ? 30.046 5.572   -7.212  0.38 15.48 ?  42  TYR   A HD2  1 
ATOM   1154 H  HE1  A TYR   A 1 42  ? 34.582 4.843   -8.712  0.62 14.94 ?  42  TYR   A HE1  1 
ATOM   1155 H  HE1  B TYR   A 1 42  ? 34.289 4.905   -8.900  0.38 14.73 ?  42  TYR   A HE1  1 
ATOM   1156 H  HE2  A TYR   A 1 42  ? 30.622 4.952   -9.278  0.62 16.17 ?  42  TYR   A HE2  1 
ATOM   1157 H  HE2  B TYR   A 1 42  ? 30.331 5.118   -9.449  0.38 16.32 ?  42  TYR   A HE2  1 
ATOM   1158 H  HH   A TYR   A 1 42  ? 33.638 4.422   -10.695 0.62 17.81 ?  42  TYR   A HH   1 
ATOM   1159 H  HH   B TYR   A 1 42  ? 31.750 4.687   -11.111 0.38 16.53 ?  42  TYR   A HH   1 
ATOM   1160 N  N    A LEU   A 1 43  ? 31.279 4.249   -1.999  0.62 9.92  ?  43  LEU   A N    1 
ATOM   1161 N  N    B LEU   A 1 43  ? 31.096 4.240   -2.165  0.38 9.55  ?  43  LEU   A N    1 
ATOM   1162 C  CA   A LEU   A 1 43  ? 30.819 4.583   -0.656  0.62 9.65  ?  43  LEU   A CA   1 
ATOM   1163 C  CA   B LEU   A 1 43  ? 30.678 4.593   -0.807  0.38 9.59  ?  43  LEU   A CA   1 
ATOM   1164 C  C    A LEU   A 1 43  ? 30.342 6.031   -0.570  0.62 9.94  ?  43  LEU   A C    1 
ATOM   1165 C  C    B LEU   A 1 43  ? 30.201 6.042   -0.721  0.38 9.85  ?  43  LEU   A C    1 
ATOM   1166 O  O    A LEU   A 1 43  ? 30.608 6.738   0.406   0.62 10.90 ?  43  LEU   A O    1 
ATOM   1167 O  O    B LEU   A 1 43  ? 30.464 6.750   0.253   0.38 10.21 ?  43  LEU   A O    1 
ATOM   1168 C  CB   A LEU   A 1 43  ? 31.864 4.276   0.416   0.62 10.04 ?  43  LEU   A CB   1 
ATOM   1169 C  CB   B LEU   A 1 43  ? 31.751 4.291   0.242   0.38 9.82  ?  43  LEU   A CB   1 
ATOM   1170 C  CG   A LEU   A 1 43  ? 32.384 2.837   0.488   0.62 10.38 ?  43  LEU   A CG   1 
ATOM   1171 C  CG   B LEU   A 1 43  ? 32.207 2.835   0.390   0.38 10.19 ?  43  LEU   A CG   1 
ATOM   1172 C  CD1  A LEU   A 1 43  ? 33.455 2.729   1.559   0.62 11.11 ?  43  LEU   A CD1  1 
ATOM   1173 C  CD1  B LEU   A 1 43  ? 33.217 2.718   1.522   0.38 10.62 ?  43  LEU   A CD1  1 
ATOM   1174 C  CD2  A LEU   A 1 43  ? 31.266 1.845   0.757   0.62 10.77 ?  43  LEU   A CD2  1 
ATOM   1175 C  CD2  B LEU   A 1 43  ? 31.026 1.895   0.618   0.38 10.46 ?  43  LEU   A CD2  1 
ATOM   1176 H  H    A LEU   A 1 43  ? 30.948 3.511   -2.299  0.62 11.89 ?  43  LEU   A H    1 
ATOM   1177 H  H    B LEU   A 1 43  ? 30.751 3.502   -2.443  0.38 11.44 ?  43  LEU   A H    1 
ATOM   1178 H  HA   A LEU   A 1 43  ? 30.050 4.027   -0.462  0.62 11.56 ?  43  LEU   A HA   1 
ATOM   1179 H  HA   B LEU   A 1 43  ? 29.913 4.041   -0.585  0.38 11.49 ?  43  LEU   A HA   1 
ATOM   1180 H  HB2  A LEU   A 1 43  ? 32.629 4.855   0.270   0.62 12.03 ?  43  LEU   A HB2  1 
ATOM   1181 H  HB2  B LEU   A 1 43  ? 32.536 4.817   0.032   0.38 11.77 ?  43  LEU   A HB2  1 
ATOM   1182 H  HB3  A LEU   A 1 43  ? 31.471 4.479   1.281   0.62 12.03 ?  43  LEU   A HB3  1 
ATOM   1183 H  HB3  B LEU   A 1 43  ? 31.406 4.567   1.109   0.38 11.77 ?  43  LEU   A HB3  1 
ATOM   1184 H  HG   A LEU   A 1 43  ? 32.792 2.607   -0.363  0.62 12.44 ?  43  LEU   A HG   1 
ATOM   1185 H  HG   B LEU   A 1 43  ? 32.648 2.563   -0.429  0.38 12.21 ?  43  LEU   A HG   1 
ATOM   1186 H  HD11 A LEU   A 1 43  ? 33.777 1.816   1.593   0.62 13.32 ?  43  LEU   A HD11 1 
ATOM   1187 H  HD11 B LEU   A 1 43  ? 33.498 1.793   1.601   0.38 12.73 ?  43  LEU   A HD11 1 
ATOM   1188 H  HD12 A LEU   A 1 43  ? 34.184 3.330   1.338   0.62 13.32 ?  43  LEU   A HD12 1 
ATOM   1189 H  HD12 B LEU   A 1 43  ? 33.983 3.280   1.322   0.38 12.73 ?  43  LEU   A HD12 1 
ATOM   1190 H  HD13 A LEU   A 1 43  ? 33.070 2.977   2.414   0.62 13.32 ?  43  LEU   A HD13 1 
ATOM   1191 H  HD13 B LEU   A 1 43  ? 32.801 3.009   2.349   0.38 12.73 ?  43  LEU   A HD13 1 
ATOM   1192 H  HD21 A LEU   A 1 43  ? 31.650 0.961   0.867   0.62 12.91 ?  43  LEU   A HD21 1 
ATOM   1193 H  HD21 B LEU   A 1 43  ? 31.364 1.012   0.837   0.38 12.53 ?  43  LEU   A HD21 1 
ATOM   1194 H  HD22 A LEU   A 1 43  ? 30.803 2.108   1.567   0.62 12.91 ?  43  LEU   A HD22 1 
ATOM   1195 H  HD22 B LEU   A 1 43  ? 30.489 2.235   1.350   0.38 12.53 ?  43  LEU   A HD22 1 
ATOM   1196 H  HD23 A LEU   A 1 43  ? 30.654 1.851   0.006   0.62 12.91 ?  43  LEU   A HD23 1 
ATOM   1197 H  HD23 B LEU   A 1 43  ? 30.496 1.855   -0.192  0.38 12.53 ?  43  LEU   A HD23 1 
ATOM   1198 N  N    A LYS   A 1 44  ? 29.617 6.472   -1.603  0.62 9.70  ?  44  LYS   A N    1 
ATOM   1199 N  N    B LYS   A 1 44  ? 29.470 6.477   -1.745  0.38 9.93  ?  44  LYS   A N    1 
ATOM   1200 C  CA   A LYS   A 1 44  ? 28.967 7.779   -1.608  0.62 10.39 ?  44  LYS   A CA   1 
ATOM   1201 C  CA   B LYS   A 1 44  ? 28.829 7.792   -1.750  0.38 10.29 ?  44  LYS   A CA   1 
ATOM   1202 C  C    A LYS   A 1 44  ? 27.530 7.580   -1.140  0.62 9.86  ?  44  LYS   A C    1 
ATOM   1203 C  C    B LYS   A 1 44  ? 27.431 7.629   -1.175  0.38 9.37  ?  44  LYS   A C    1 
ATOM   1204 O  O    A LYS   A 1 44  ? 26.694 7.037   -1.870  0.62 10.84 ?  44  LYS   A O    1 
ATOM   1205 O  O    B LYS   A 1 44  ? 26.511 7.180   -1.864  0.38 9.79  ?  44  LYS   A O    1 
ATOM   1206 C  CB   A LYS   A 1 44  ? 29.038 8.429   -2.985  0.62 12.02 ?  44  LYS   A CB   1 
ATOM   1207 C  CB   B LYS   A 1 44  ? 28.790 8.360   -3.164  0.38 12.59 ?  44  LYS   A CB   1 
ATOM   1208 C  CG   A LYS   A 1 44  ? 30.444 8.854   -3.394  0.62 14.97 ?  44  LYS   A CG   1 
ATOM   1209 C  CG   B LYS   A 1 44  ? 30.113 8.945   -3.638  0.38 15.59 ?  44  LYS   A CG   1 
ATOM   1210 C  CD   A LYS   A 1 44  ? 31.083 9.831   -2.407  0.62 19.66 ?  44  LYS   A CD   1 
ATOM   1211 C  CD   B LYS   A 1 44  ? 30.875 9.582   -2.486  0.38 19.15 ?  44  LYS   A CD   1 
ATOM   1212 C  CE   A LYS   A 1 44  ? 32.442 10.297  -2.899  0.62 22.44 ?  44  LYS   A CE   1 
ATOM   1213 C  CE   B LYS   A 1 44  ? 31.893 10.593  -2.959  0.38 20.95 ?  44  LYS   A CE   1 
ATOM   1214 N  NZ   A LYS   A 1 44  ? 33.262 10.862  -1.797  0.62 23.77 ?  44  LYS   A NZ   1 
ATOM   1215 N  NZ   B LYS   A 1 44  ? 32.752 11.045  -1.833  0.38 22.30 ?  44  LYS   A NZ   1 
ATOM   1216 H  H    A LYS   A 1 44  ? 29.490 6.020   -2.330  0.62 11.62 ?  44  LYS   A H    1 
ATOM   1217 H  H    B LYS   A 1 44  ? 29.331 6.023   -2.462  0.38 11.90 ?  44  LYS   A H    1 
ATOM   1218 H  HA   A LYS   A 1 44  ? 29.407 8.352   -0.965  0.62 12.46 ?  44  LYS   A HA   1 
ATOM   1219 H  HA   B LYS   A 1 44  ? 29.298 8.380   -1.143  0.38 12.33 ?  44  LYS   A HA   1 
ATOM   1220 H  HB2  A LYS   A 1 44  ? 28.714 7.805   -3.646  0.62 14.40 ?  44  LYS   A HB2  1 
ATOM   1221 H  HB2  B LYS   A 1 44  ? 28.546 7.649   -3.782  0.38 15.10 ?  44  LYS   A HB2  1 
ATOM   1222 H  HB3  A LYS   A 1 44  ? 28.482 9.226   -2.980  0.62 14.40 ?  44  LYS   A HB3  1 
ATOM   1223 H  HB3  B LYS   A 1 44  ? 28.125 9.065   -3.203  0.38 15.10 ?  44  LYS   A HB3  1 
ATOM   1224 H  HG2  A LYS   A 1 44  ? 31.012 8.069   -3.446  0.62 17.95 ?  44  LYS   A HG2  1 
ATOM   1225 H  HG2  B LYS   A 1 44  ? 30.660 8.241   -4.020  0.38 18.69 ?  44  LYS   A HG2  1 
ATOM   1226 H  HG3  A LYS   A 1 44  ? 30.406 9.293   -4.259  0.62 17.95 ?  44  LYS   A HG3  1 
ATOM   1227 H  HG3  B LYS   A 1 44  ? 29.941 9.634   -4.303  0.38 18.69 ?  44  LYS   A HG3  1 
ATOM   1228 H  HD2  A LYS   A 1 44  ? 30.504 10.600  -2.300  0.62 23.57 ?  44  LYS   A HD2  1 
ATOM   1229 H  HD2  B LYS   A 1 44  ? 30.249 10.050  -1.909  0.38 22.97 ?  44  LYS   A HD2  1 
ATOM   1230 H  HD3  A LYS   A 1 44  ? 31.209 9.382   -1.553  0.62 23.57 ?  44  LYS   A HD3  1 
ATOM   1231 H  HD3  B LYS   A 1 44  ? 31.336 8.883   -1.983  0.38 22.97 ?  44  LYS   A HD3  1 
ATOM   1232 H  HE2  A LYS   A 1 44  ? 32.920 9.544   -3.278  0.62 26.91 ?  44  LYS   A HE2  1 
ATOM   1233 H  HE2  B LYS   A 1 44  ? 32.458 10.188  -3.634  0.38 25.12 ?  44  LYS   A HE2  1 
ATOM   1234 H  HE3  A LYS   A 1 44  ? 32.314 10.986  -3.570  0.62 26.91 ?  44  LYS   A HE3  1 
ATOM   1235 H  HE3  B LYS   A 1 44  ? 31.430 11.365  -3.320  0.38 25.12 ?  44  LYS   A HE3  1 
ATOM   1236 H  HZ1  A LYS   A 1 44  ? 34.047 11.132  -2.112  0.62 28.51 ?  44  LYS   A HZ1  1 
ATOM   1237 H  HZ1  B LYS   A 1 44  ? 33.345 11.640  -2.123  0.38 26.74 ?  44  LYS   A HZ1  1 
ATOM   1238 H  HZ2  A LYS   A 1 44  ? 32.841 11.562  -1.435  0.62 28.51 ?  44  LYS   A HZ2  1 
ATOM   1239 H  HZ2  B LYS   A 1 44  ? 32.252 11.419  -1.199  0.38 26.74 ?  44  LYS   A HZ2  1 
ATOM   1240 H  HZ3  A LYS   A 1 44  ? 33.392 10.249  -1.169  0.62 28.51 ?  44  LYS   A HZ3  1 
ATOM   1241 H  HZ3  B LYS   A 1 44  ? 33.186 10.350  -1.484  0.38 26.74 ?  44  LYS   A HZ3  1 
ATOM   1242 N  N    . HIS   A 1 45  ? 27.266 7.980   0.098   1.00 9.41  ?  45  HIS   A N    1 
ATOM   1243 C  CA   . HIS   A 1 45  ? 26.031 7.652   0.802   1.00 9.57  ?  45  HIS   A CA   1 
ATOM   1244 C  C    . HIS   A 1 45  ? 25.013 8.779   0.637   1.00 10.28 ?  45  HIS   A C    1 
ATOM   1245 O  O    . HIS   A 1 45  ? 24.738 9.552   1.550   1.00 11.90 ?  45  HIS   A O    1 
ATOM   1246 C  CB   . HIS   A 1 45  ? 26.336 7.407   2.266   1.00 9.59  ?  45  HIS   A CB   1 
ATOM   1247 C  CG   . HIS   A 1 45  ? 27.442 6.433   2.496   1.00 9.29  ?  45  HIS   A CG   1 
ATOM   1248 N  ND1  . HIS   A 1 45  ? 27.434 5.144   1.999   1.00 9.66  ?  45  HIS   A ND1  1 
ATOM   1249 C  CD2  . HIS   A 1 45  ? 28.603 6.581   3.177   1.00 9.64  ?  45  HIS   A CD2  1 
ATOM   1250 C  CE1  . HIS   A 1 45  ? 28.556 4.549   2.372   1.00 9.40  ?  45  HIS   A CE1  1 
ATOM   1251 N  NE2  . HIS   A 1 45  ? 29.281 5.396   3.084   1.00 9.72  ?  45  HIS   A NE2  1 
ATOM   1252 H  H    A HIS   A 1 45  ? 27.804 8.462   0.567   0.62 11.27 ?  45  HIS   A H    1 
ATOM   1253 H  H    B HIS   A 1 45  ? 27.844 8.406   0.573   0.38 11.27 ?  45  HIS   A H    1 
ATOM   1254 H  HA   . HIS   A 1 45  ? 25.649 6.841   0.426   1.00 11.46 ?  45  HIS   A HA   1 
ATOM   1255 H  HB2  . HIS   A 1 45  ? 26.582 8.251   2.677   1.00 11.49 ?  45  HIS   A HB2  1 
ATOM   1256 H  HB3  . HIS   A 1 45  ? 25.534 7.059   2.695   1.00 11.49 ?  45  HIS   A HB3  1 
ATOM   1257 H  HD2  . HIS   A 1 45  ? 28.895 7.351   3.617   1.00 11.55 ?  45  HIS   A HD2  1 
ATOM   1258 H  HE1  . HIS   A 1 45  ? 28.785 3.669   2.183   1.00 11.26 ?  45  HIS   A HE1  1 
ATOM   1259 H  HE2  . HIS   A 1 45  ? 30.046 5.226   3.439   1.00 11.65 ?  45  HIS   A HE2  1 
ATOM   1260 N  N    A GLY   A 1 46  ? 24.426 8.835   -0.553  0.62 11.17 ?  46  GLY   A N    1 
ATOM   1261 N  N    B GLY   A 1 46  ? 24.427 8.868   -0.549  0.38 10.70 ?  46  GLY   A N    1 
ATOM   1262 C  CA   A GLY   A 1 46  ? 23.608 9.970   -0.931  0.62 12.09 ?  46  GLY   A CA   1 
ATOM   1263 C  CA   B GLY   A 1 46  ? 23.597 10.027  -0.835  0.38 10.98 ?  46  GLY   A CA   1 
ATOM   1264 C  C    A GLY   A 1 46  ? 22.119 9.826   -0.694  0.62 11.91 ?  46  GLY   A C    1 
ATOM   1265 C  C    B GLY   A 1 46  ? 22.136 9.916   -0.435  0.38 10.45 ?  46  GLY   A C    1 
ATOM   1266 O  O    A GLY   A 1 46  ? 21.443 10.815  -0.383  0.62 12.81 ?  46  GLY   A O    1 
ATOM   1267 O  O    B GLY   A 1 46  ? 21.523 10.911  -0.031  0.38 11.10 ?  46  GLY   A O    1 
ATOM   1268 H  H    A GLY   A 1 46  ? 24.477 8.221   -1.153  0.62 13.39 ?  46  GLY   A H    1 
ATOM   1269 H  H    B GLY   A 1 46  ? 24.476 8.290   -1.183  0.38 12.83 ?  46  GLY   A H    1 
ATOM   1270 H  HA2  A GLY   A 1 46  ? 23.909 10.752  -0.443  0.62 14.50 ?  46  GLY   A HA2  1 
ATOM   1271 H  HA2  B GLY   A 1 46  ? 23.966 10.800  -0.367  0.38 13.16 ?  46  GLY   A HA2  1 
ATOM   1272 H  HA3  A GLY   A 1 46  ? 23.726 10.141  -1.876  0.62 14.50 ?  46  GLY   A HA3  1 
ATOM   1273 H  HA3  B GLY   A 1 46  ? 23.635 10.216  -1.782  0.38 13.16 ?  46  GLY   A HA3  1 
ATOM   1274 N  N    A GLY   A 1 47  ? 21.587 8.617   -0.860  0.62 11.58 ?  47  GLY   A N    1 
ATOM   1275 N  N    B GLY   A 1 47  ? 21.563 8.725   -0.549  0.38 10.18 ?  47  GLY   A N    1 
ATOM   1276 C  CA   A GLY   A 1 47  ? 20.157 8.407   -0.803  0.62 11.29 ?  47  GLY   A CA   1 
ATOM   1277 C  CA   B GLY   A 1 47  ? 20.145 8.542   -0.325  0.38 9.91  ?  47  GLY   A CA   1 
ATOM   1278 C  C    A GLY   A 1 47  ? 19.844 6.980   -0.410  0.62 10.80 ?  47  GLY   A C    1 
ATOM   1279 C  C    B GLY   A 1 47  ? 19.818 7.092   -0.033  0.38 9.76  ?  47  GLY   A C    1 
ATOM   1280 O  O    A GLY   A 1 47  ? 20.742 6.160   -0.206  0.62 11.10 ?  47  GLY   A O    1 
ATOM   1281 O  O    B GLY   A 1 47  ? 20.708 6.249   0.108   0.38 9.60  ?  47  GLY   A O    1 
ATOM   1282 H  H    A GLY   A 1 47  ? 22.041 7.893   -0.995  0.62 13.88 ?  47  GLY   A H    1 
ATOM   1283 H  H    B GLY   A 1 47  ? 21.984 8.008   -0.743  0.38 12.20 ?  47  GLY   A H    1 
ATOM   1284 H  HA2  A GLY   A 1 47  ? 19.755 9.010   -0.158  0.62 13.54 ?  47  GLY   A HA2  1 
ATOM   1285 H  HA2  B GLY   A 1 47  ? 19.853 9.083   0.427   0.38 11.87 ?  47  GLY   A HA2  1 
ATOM   1286 H  HA3  A GLY   A 1 47  ? 19.769 8.576   -1.676  0.62 13.54 ?  47  GLY   A HA3  1 
ATOM   1287 H  HA3  B GLY   A 1 47  ? 19.649 8.823   -1.114  0.38 11.87 ?  47  GLY   A HA3  1 
ATOM   1288 N  N    A GLY   A 1 48  ? 18.553 6.676   -0.314  0.62 10.72 ?  48  GLY   A N    1 
ATOM   1289 N  N    B GLY   A 1 48  ? 18.520 6.810   0.063   0.38 10.42 ?  48  GLY   A N    1 
ATOM   1290 C  CA   A GLY   A 1 48  ? 18.167 5.353   0.116   0.62 11.58 ?  48  GLY   A CA   1 
ATOM   1291 C  CA   B GLY   A 1 48  ? 18.091 5.461   0.389   0.38 10.28 ?  48  GLY   A CA   1 
ATOM   1292 C  C    A GLY   A 1 48  ? 18.658 5.071   1.521   0.62 10.62 ?  48  GLY   A C    1 
ATOM   1293 C  C    B GLY   A 1 48  ? 18.621 5.031   1.740   0.38 9.97  ?  48  GLY   A C    1 
ATOM   1294 O  O    A GLY   A 1 48  ? 18.880 5.979   2.329   0.62 10.72 ?  48  GLY   A O    1 
ATOM   1295 O  O    B GLY   A 1 48  ? 18.735 5.831   2.675   0.38 10.33 ?  48  GLY   A O    1 
ATOM   1296 H  H    A GLY   A 1 48  ? 17.896 7.209   -0.478  0.62 12.85 ?  48  GLY   A H    1 
ATOM   1297 H  H    B GLY   A 1 48  ? 17.874 7.369   -0.052  0.38 12.48 ?  48  GLY   A H    1 
ATOM   1298 H  HA2  A GLY   A 1 48  ? 17.206 5.260   0.099   0.62 13.88 ?  48  GLY   A HA2  1 
ATOM   1299 H  HA2  B GLY   A 1 48  ? 17.123 5.416   0.402   0.38 12.32 ?  48  GLY   A HA2  1 
ATOM   1300 H  HA3  A GLY   A 1 48  ? 18.560 4.690   -0.473  0.62 13.88 ?  48  GLY   A HA3  1 
ATOM   1301 H  HA3  B GLY   A 1 48  ? 18.423 4.842   -0.281  0.38 12.32 ?  48  GLY   A HA3  1 
ATOM   1302 N  N    A VAL   A 1 49  ? 18.833 3.780   1.818   0.62 10.43 ?  49  VAL   A N    1 
ATOM   1303 N  N    B VAL   A 1 49  ? 18.950 3.742   1.848   0.38 9.65  ?  49  VAL   A N    1 
ATOM   1304 C  CA   A VAL   A 1 49  ? 19.353 3.364   3.118   0.62 10.50 ?  49  VAL   A CA   1 
ATOM   1305 C  CA   B VAL   A 1 49  ? 19.536 3.218   3.079   0.38 9.43  ?  49  VAL   A CA   1 
ATOM   1306 C  C    A VAL   A 1 49  ? 20.663 4.071   3.437   0.62 9.73  ?  49  VAL   A C    1 
ATOM   1307 C  C    B VAL   A 1 49  ? 20.799 3.988   3.437   0.38 8.51  ?  49  VAL   A C    1 
ATOM   1308 O  O    A VAL   A 1 49  ? 20.880 4.510   4.571   0.62 10.18 ?  49  VAL   A O    1 
ATOM   1309 O  O    B VAL   A 1 49  ? 20.996 4.387   4.590   0.38 8.58  ?  49  VAL   A O    1 
ATOM   1310 C  CB   A VAL   A 1 49  ? 19.519 1.832   3.148   0.62 11.15 ?  49  VAL   A CB   1 
ATOM   1311 C  CB   B VAL   A 1 49  ? 19.832 1.714   2.938   0.38 9.23  ?  49  VAL   A CB   1 
ATOM   1312 C  CG1  A VAL   A 1 49  ? 20.335 1.391   4.361   0.62 10.85 ?  49  VAL   A CG1  1 
ATOM   1313 C  CG1  B VAL   A 1 49  ? 20.713 1.244   4.093   0.38 8.87  ?  49  VAL   A CG1  1 
ATOM   1314 C  CG2  A VAL   A 1 49  ? 18.157 1.147   3.133   0.62 12.86 ?  49  VAL   A CG2  1 
ATOM   1315 C  CG2  B VAL   A 1 49  ? 18.544 0.905   2.871   0.38 9.23  ?  49  VAL   A CG2  1 
ATOM   1316 H  H    A VAL   A 1 49  ? 18.646 3.125   1.292   0.62 12.50 ?  49  VAL   A H    1 
ATOM   1317 H  H    B VAL   A 1 49  ? 18.846 3.158   1.229   0.38 11.56 ?  49  VAL   A H    1 
ATOM   1318 H  HA   A VAL   A 1 49  ? 18.716 3.598   3.810   0.62 12.58 ?  49  VAL   A HA   1 
ATOM   1319 H  HA   B VAL   A 1 49  ? 18.904 3.327   3.808   0.38 11.31 ?  49  VAL   A HA   1 
ATOM   1320 H  HB   A VAL   A 1 49  ? 20.004 1.552   2.354   0.62 13.37 ?  49  VAL   A HB   1 
ATOM   1321 H  HB   B VAL   A 1 49  ? 20.318 1.565   2.112   0.38 11.06 ?  49  VAL   A HB   1 
ATOM   1322 H  HG11 A VAL   A 1 49  ? 20.195 0.443   4.508   0.62 13.01 ?  49  VAL   A HG11 1 
ATOM   1323 H  HG11 B VAL   A 1 49  ? 20.638 0.282   4.180   0.38 10.62 ?  49  VAL   A HG11 1 
ATOM   1324 H  HG12 A VAL   A 1 49  ? 21.276 1.563   4.196   0.62 13.01 ?  49  VAL   A HG12 1 
ATOM   1325 H  HG12 B VAL   A 1 49  ? 21.639 1.483   3.909   0.38 10.62 ?  49  VAL   A HG12 1 
ATOM   1326 H  HG13 A VAL   A 1 49  ? 20.038 1.891   5.139   0.62 13.01 ?  49  VAL   A HG13 1 
ATOM   1327 H  HG13 B VAL   A 1 49  ? 20.419 1.672   4.913   0.38 10.62 ?  49  VAL   A HG13 1 
ATOM   1328 H  HG21 A VAL   A 1 49  ? 18.287 0.187   3.153   0.62 15.42 ?  49  VAL   A HG21 1 
ATOM   1329 H  HG21 B VAL   A 1 49  ? 18.763 -0.034  2.765   0.38 11.06 ?  49  VAL   A HG21 1 
ATOM   1330 H  HG22 A VAL   A 1 49  ? 17.656 1.431   3.914   0.62 15.42 ?  49  VAL   A HG22 1 
ATOM   1331 H  HG22 B VAL   A 1 49  ? 18.046 1.037   3.695   0.38 11.06 ?  49  VAL   A HG22 1 
ATOM   1332 H  HG23 A VAL   A 1 49  ? 17.688 1.404   2.325   0.62 15.42 ?  49  VAL   A HG23 1 
ATOM   1333 H  HG23 B VAL   A 1 49  ? 18.018 1.210   2.115   0.38 11.06 ?  49  VAL   A HG23 1 
ATOM   1334 N  N    A ALA   A 1 50  ? 21.571 4.147   2.461   0.62 9.55  ?  50  ALA   A N    1 
ATOM   1335 N  N    B ALA   A 1 50  ? 21.692 4.165   2.463   0.38 8.43  ?  50  ALA   A N    1 
ATOM   1336 C  CA   A ALA   A 1 50  ? 22.896 4.705   2.721   0.62 9.35  ?  50  ALA   A CA   1 
ATOM   1337 C  CA   B ALA   A 1 50  ? 22.996 4.753   2.755   0.38 8.54  ?  50  ALA   A CA   1 
ATOM   1338 C  C    A ALA   A 1 50  ? 22.809 6.163   3.146   0.62 9.24  ?  50  ALA   A C    1 
ATOM   1339 C  C    B ALA   A 1 50  ? 22.864 6.207   3.179   0.38 8.77  ?  50  ALA   A C    1 
ATOM   1340 O  O    A ALA   A 1 50  ? 23.450 6.578   4.117   0.62 9.56  ?  50  ALA   A O    1 
ATOM   1341 O  O    B ALA   A 1 50  ? 23.472 6.634   4.167   0.38 8.97  ?  50  ALA   A O    1 
ATOM   1342 C  CB   A ALA   A 1 50  ? 23.768 4.574   1.477   0.62 9.42  ?  50  ALA   A CB   1 
ATOM   1343 C  CB   B ALA   A 1 50  ? 23.909 4.630   1.538   0.38 8.39  ?  50  ALA   A CB   1 
ATOM   1344 H  H    A ALA   A 1 50  ? 21.444 3.886   1.652   0.62 11.45 ?  50  ALA   A H    1 
ATOM   1345 H  H    B ALA   A 1 50  ? 21.563 3.954   1.639   0.38 10.10 ?  50  ALA   A H    1 
ATOM   1346 H  HA   A ALA   A 1 50  ? 23.317 4.211   3.442   0.62 11.20 ?  50  ALA   A HA   1 
ATOM   1347 H  HA   B ALA   A 1 50  ? 23.402 4.266   3.487   0.38 10.23 ?  50  ALA   A HA   1 
ATOM   1348 H  HB1  A ALA   A 1 50  ? 24.644 4.950   1.666   0.62 11.29 ?  50  ALA   A HB1  1 
ATOM   1349 H  HB1  B ALA   A 1 50  ? 24.767 5.029   1.749   0.38 10.05 ?  50  ALA   A HB1  1 
ATOM   1350 H  HB2  A ALA   A 1 50  ? 23.852 3.639   1.246   0.62 11.29 ?  50  ALA   A HB2  1 
ATOM   1351 H  HB2  B ALA   A 1 50  ? 24.023 3.693   1.319   0.38 10.05 ?  50  ALA   A HB2  1 
ATOM   1352 H  HB3  A ALA   A 1 50  ? 23.352 5.063   0.749   0.62 11.29 ?  50  ALA   A HB3  1 
ATOM   1353 H  HB3  B ALA   A 1 50  ? 23.502 5.097   0.790   0.38 10.05 ?  50  ALA   A HB3  1 
ATOM   1354 N  N    A GLY   A 1 51  ? 22.029 6.961   2.420   0.62 9.37  ?  51  GLY   A N    1 
ATOM   1355 N  N    B GLY   A 1 51  ? 22.078 6.989   2.440   0.38 9.13  ?  51  GLY   A N    1 
ATOM   1356 C  CA   A GLY   A 1 51  ? 21.878 8.353   2.803   0.62 9.89  ?  51  GLY   A CA   1 
ATOM   1357 C  CA   B GLY   A 1 51  ? 21.887 8.377   2.820   0.38 9.59  ?  51  GLY   A CA   1 
ATOM   1358 C  C    A GLY   A 1 51  ? 21.270 8.502   4.183   0.62 9.64  ?  51  GLY   A C    1 
ATOM   1359 C  C    B GLY   A 1 51  ? 21.259 8.516   4.192   0.38 9.62  ?  51  GLY   A C    1 
ATOM   1360 O  O    A GLY   A 1 51  ? 21.657 9.386   4.953   0.62 10.30 ?  51  GLY   A O    1 
ATOM   1361 O  O    B GLY   A 1 51  ? 21.624 9.405   4.966   0.38 10.01 ?  51  GLY   A O    1 
ATOM   1362 H  H    A GLY   A 1 51  ? 21.597 6.721   1.715   0.62 11.22 ?  51  GLY   A H    1 
ATOM   1363 H  H    B GLY   A 1 51  ? 21.663 6.742   1.727   0.38 10.94 ?  51  GLY   A H    1 
ATOM   1364 H  HA2  A GLY   A 1 51  ? 22.744 8.784   2.800   0.62 11.86 ?  51  GLY   A HA2  1 
ATOM   1365 H  HA2  B GLY   A 1 51  ? 22.743 8.827   2.827   0.38 11.49 ?  51  GLY   A HA2  1 
ATOM   1366 H  HA3  A GLY   A 1 51  ? 21.305 8.799   2.162   0.62 11.86 ?  51  GLY   A HA3  1 
ATOM   1367 H  HA3  B GLY   A 1 51  ? 21.312 8.810   2.172   0.38 11.49 ?  51  GLY   A HA3  1 
ATOM   1368 N  N    . ALA   A 1 52  ? 20.300 7.641   4.510   1.00 9.83  ?  52  ALA   A N    1 
ATOM   1369 C  CA   . ALA   A 1 52  ? 19.645 7.698   5.812   1.00 10.59 ?  52  ALA   A CA   1 
ATOM   1370 C  C    . ALA   A 1 52  ? 20.591 7.289   6.941   1.00 9.81  ?  52  ALA   A C    1 
ATOM   1371 O  O    . ALA   A 1 52  ? 20.659 7.958   7.976   1.00 10.70 ?  52  ALA   A O    1 
ATOM   1372 C  CB   . ALA   A 1 52  ? 18.380 6.841   5.792   1.00 12.19 ?  52  ALA   A CB   1 
ATOM   1373 H  H    A ALA   A 1 52  ? 20.011 7.011   3.995   0.62 11.78 ?  52  ALA   A H    1 
ATOM   1374 H  H    B ALA   A 1 52  ? 20.022 7.005   3.996   0.38 11.78 ?  52  ALA   A H    1 
ATOM   1375 H  HA   . ALA   A 1 52  ? 19.374 8.608   5.978   1.00 12.69 ?  52  ALA   A HA   1 
ATOM   1376 H  HB1  . ALA   A 1 52  ? 17.928 6.923   6.649   1.00 14.61 ?  52  ALA   A HB1  1 
ATOM   1377 H  HB2  . ALA   A 1 52  ? 17.795 7.159   5.084   1.00 14.61 ?  52  ALA   A HB2  1 
ATOM   1378 H  HB3  . ALA   A 1 52  ? 18.618 5.916   5.631   1.00 14.61 ?  52  ALA   A HB3  1 
ATOM   1379 N  N    A LEU   A 1 53  ? 21.326 6.188   6.769   0.62 9.43  ?  53  LEU   A N    1 
ATOM   1380 N  N    B LEU   A 1 53  ? 21.322 6.183   6.764   0.38 9.52  ?  53  LEU   A N    1 
ATOM   1381 C  CA   A LEU   A 1 53  ? 22.291 5.798   7.796   0.62 9.88  ?  53  LEU   A CA   1 
ATOM   1382 C  CA   B LEU   A 1 53  ? 22.304 5.782   7.770   0.38 9.74  ?  53  LEU   A CA   1 
ATOM   1383 C  C    A LEU   A 1 53  ? 23.354 6.872   7.974   0.62 9.45  ?  53  LEU   A C    1 
ATOM   1384 C  C    B LEU   A 1 53  ? 23.325 6.888   7.992   0.38 9.66  ?  53  LEU   A C    1 
ATOM   1385 O  O    A LEU   A 1 53  ? 23.704 7.231   9.102   0.62 10.35 ?  53  LEU   A O    1 
ATOM   1386 O  O    B LEU   A 1 53  ? 23.613 7.265   9.134   0.38 10.46 ?  53  LEU   A O    1 
ATOM   1387 C  CB   A LEU   A 1 53  ? 22.950 4.461   7.448   0.62 10.50 ?  53  LEU   A CB   1 
ATOM   1388 C  CB   B LEU   A 1 53  ? 23.016 4.487   7.356   0.38 9.77  ?  53  LEU   A CB   1 
ATOM   1389 C  CG   A LEU   A 1 53  ? 22.032 3.237   7.475   0.62 10.89 ?  53  LEU   A CG   1 
ATOM   1390 C  CG   B LEU   A 1 53  ? 22.314 3.129   7.485   0.38 9.44  ?  53  LEU   A CG   1 
ATOM   1391 C  CD1  A LEU   A 1 53  ? 22.760 2.025   6.926   0.62 11.18 ?  53  LEU   A CD1  1 
ATOM   1392 C  CD1  B LEU   A 1 53  ? 23.167 2.051   6.825   0.38 9.73  ?  53  LEU   A CD1  1 
ATOM   1393 C  CD2  A LEU   A 1 53  ? 21.525 2.966   8.884   0.62 11.49 ?  53  LEU   A CD2  1 
ATOM   1394 C  CD2  B LEU   A 1 53  ? 22.031 2.755   8.936   0.38 9.44  ?  53  LEU   A CD2  1 
ATOM   1395 H  H    A LEU   A 1 53  ? 21.288 5.663   6.089   0.62 11.30 ?  53  LEU   A H    1 
ATOM   1396 H  H    B LEU   A 1 53  ? 21.273 5.659   6.083   0.38 11.41 ?  53  LEU   A H    1 
ATOM   1397 H  HA   A LEU   A 1 53  ? 21.828 5.689   8.642   0.62 11.84 ?  53  LEU   A HA   1 
ATOM   1398 H  HA   B LEU   A 1 53  ? 21.851 5.621   8.611   0.38 11.67 ?  53  LEU   A HA   1 
ATOM   1399 H  HB2  A LEU   A 1 53  ? 23.322 4.522   6.553   0.62 12.59 ?  53  LEU   A HB2  1 
ATOM   1400 H  HB2  B LEU   A 1 53  ? 23.259 4.574   6.424   0.38 11.71 ?  53  LEU   A HB2  1 
ATOM   1401 H  HB3  A LEU   A 1 53  ? 23.668 4.294   8.082   0.62 12.59 ?  53  LEU   A HB3  1 
ATOM   1402 H  HB3  B LEU   A 1 53  ? 23.826 4.419   7.884   0.38 11.71 ?  53  LEU   A HB3  1 
ATOM   1403 H  HG   A LEU   A 1 53  ? 21.261 3.409   6.907   0.62 13.05 ?  53  LEU   A HG   1 
ATOM   1404 H  HG   B LEU   A 1 53  ? 21.468 3.158   7.016   0.38 11.31 ?  53  LEU   A HG   1 
ATOM   1405 H  HD11 A LEU   A 1 53  ? 22.163 1.262   6.951   0.62 13.40 ?  53  LEU   A HD11 1 
ATOM   1406 H  HD11 B LEU   A 1 53  ? 22.722 1.193   6.916   0.38 11.66 ?  53  LEU   A HD11 1 
ATOM   1407 H  HD12 A LEU   A 1 53  ? 23.029 2.208   6.013   0.62 13.40 ?  53  LEU   A HD12 1 
ATOM   1408 H  HD12 B LEU   A 1 53  ? 23.277 2.268   5.886   0.38 11.66 ?  53  LEU   A HD12 1 
ATOM   1409 H  HD13 A LEU   A 1 53  ? 23.541 1.855   7.475   0.62 13.40 ?  53  LEU   A HD13 1 
ATOM   1410 H  HD13 B LEU   A 1 53  ? 24.033 2.021   7.262   0.38 11.66 ?  53  LEU   A HD13 1 
ATOM   1411 H  HD21 A LEU   A 1 53  ? 21.025 2.136   8.885   0.62 13.77 ?  53  LEU   A HD21 1 
ATOM   1412 H  HD21 B LEU   A 1 53  ? 21.582 1.895   8.963   0.38 11.31 ?  53  LEU   A HD21 1 
ATOM   1413 H  HD22 A LEU   A 1 53  ? 22.284 2.898   9.482   0.62 13.77 ?  53  LEU   A HD22 1 
ATOM   1414 H  HD22 B LEU   A 1 53  ? 22.871 2.703   9.420   0.38 11.31 ?  53  LEU   A HD22 1 
ATOM   1415 H  HD23 A LEU   A 1 53  ? 20.951 3.698   9.162   0.62 13.77 ?  53  LEU   A HD23 1 
ATOM   1416 H  HD23 B LEU   A 1 53  ? 21.464 3.436   9.330   0.38 11.31 ?  53  LEU   A HD23 1 
ATOM   1417 N  N    A ASN   A 1 54  ? 23.876 7.398   6.870   0.62 9.34  ?  54  ASN   A N    1 
ATOM   1418 N  N    B ASN   A 1 54  ? 23.877 7.431   6.907   0.38 9.33  ?  54  ASN   A N    1 
ATOM   1419 C  CA   A ASN   A 1 54  ? 24.928 8.398   6.986   0.62 9.56  ?  54  ASN   A CA   1 
ATOM   1420 C  CA   B ASN   A 1 54  ? 24.919 8.439   7.056   0.38 8.99  ?  54  ASN   A CA   1 
ATOM   1421 C  C    A ASN   A 1 54  ? 24.417 9.659   7.678   0.62 10.00 ?  54  ASN   A C    1 
ATOM   1422 C  C    B ASN   A 1 54  ? 24.394 9.659   7.803   0.38 9.04  ?  54  ASN   A C    1 
ATOM   1423 O  O    A ASN   A 1 54  ? 25.122 10.248  8.505   0.62 10.48 ?  54  ASN   A O    1 
ATOM   1424 O  O    B ASN   A 1 54  ? 25.038 10.154  8.736   0.38 8.65  ?  54  ASN   A O    1 
ATOM   1425 C  CB   A ASN   A 1 54  ? 25.502 8.722   5.619   0.62 9.78  ?  54  ASN   A CB   1 
ATOM   1426 C  CB   B ASN   A 1 54  ? 25.483 8.837   5.698   0.38 8.82  ?  54  ASN   A CB   1 
ATOM   1427 C  CG   A ASN   A 1 54  ? 26.549 9.790   5.707   0.62 9.98  ?  54  ASN   A CG   1 
ATOM   1428 C  CG   B ASN   A 1 54  ? 26.465 9.973   5.817   0.38 8.41  ?  54  ASN   A CG   1 
ATOM   1429 O  OD1  A ASN   A 1 54  ? 27.551 9.625   6.408   0.62 10.41 ?  54  ASN   A OD1  1 
ATOM   1430 O  OD1  B ASN   A 1 54  ? 27.488 9.848   6.498   0.38 8.25  ?  54  ASN   A OD1  1 
ATOM   1431 N  ND2  A ASN   A 1 54  ? 26.323 10.907  5.033   0.62 10.51 ?  54  ASN   A ND2  1 
ATOM   1432 N  ND2  B ASN   A 1 54  ? 26.154 11.100  5.183   0.38 9.02  ?  54  ASN   A ND2  1 
ATOM   1433 H  H    A ASN   A 1 54  ? 23.641 7.189   6.070   0.62 11.20 ?  54  ASN   A H    1 
ATOM   1434 H  H    B ASN   A 1 54  ? 23.663 7.240   6.095   0.38 11.18 ?  54  ASN   A H    1 
ATOM   1435 H  HA   A ASN   A 1 54  ? 25.636 8.027   7.532   0.62 11.45 ?  54  ASN   A HA   1 
ATOM   1436 H  HA   B ASN   A 1 54  ? 25.639 8.065   7.579   0.38 10.78 ?  54  ASN   A HA   1 
ATOM   1437 H  HB2  A ASN   A 1 54  ? 25.914 7.919   5.254   0.62 11.72 ?  54  ASN   A HB2  1 
ATOM   1438 H  HB2  B ASN   A 1 54  ? 25.949 8.075   5.316   0.38 10.57 ?  54  ASN   A HB2  1 
ATOM   1439 H  HB3  A ASN   A 1 54  ? 24.792 9.028   5.039   0.62 11.72 ?  54  ASN   A HB3  1 
ATOM   1440 H  HB3  B ASN   A 1 54  ? 24.758 9.111   5.118   0.38 10.57 ?  54  ASN   A HB3  1 
ATOM   1441 H  HD21 A ASN   A 1 54  ? 26.891 11.547  5.066   0.62 12.59 ?  54  ASN   A HD21 1 
ATOM   1442 H  HD21 B ASN   A 1 54  ? 26.676 11.781  5.233   0.38 10.80 ?  54  ASN   A HD21 1 
ATOM   1443 H  HD22 A ASN   A 1 54  ? 25.606 10.985  4.564   0.62 12.59 ?  54  ASN   A HD22 1 
ATOM   1444 H  HD22 B ASN   A 1 54  ? 25.429 11.149  4.719   0.38 10.80 ?  54  ASN   A HD22 1 
ATOM   1445 N  N    A LYS   A 1 55  ? 23.190 10.084  7.360   0.62 10.14 ?  55  LYS   A N    1 
ATOM   1446 N  N    B LYS   A 1 55  ? 23.212 10.151  7.415   0.38 9.42  ?  55  LYS   A N    1 
ATOM   1447 C  CA   A LYS   A 1 55  ? 22.601 11.237  8.033   0.62 10.61 ?  55  LYS   A CA   1 
ATOM   1448 C  CA   B LYS   A 1 55  ? 22.636 11.307  8.091   0.38 10.53 ?  55  LYS   A CA   1 
ATOM   1449 C  C    A LYS   A 1 55  ? 22.537 11.023  9.541   0.62 10.75 ?  55  LYS   A C    1 
ATOM   1450 C  C    B LYS   A 1 55  ? 22.494 11.052  9.585   0.38 10.82 ?  55  LYS   A C    1 
ATOM   1451 O  O    A LYS   A 1 55  ? 22.858 11.927  10.321  0.62 11.41 ?  55  LYS   A O    1 
ATOM   1452 O  O    B LYS   A 1 55  ? 22.712 11.956  10.401  0.38 11.23 ?  55  LYS   A O    1 
ATOM   1453 C  CB   A LYS   A 1 55  ? 21.211 11.503  7.451   0.62 11.08 ?  55  LYS   A CB   1 
ATOM   1454 C  CB   B LYS   A 1 55  ? 21.288 11.660  7.459   0.38 11.46 ?  55  LYS   A CB   1 
ATOM   1455 C  CG   A LYS   A 1 55  ? 20.484 12.702  8.031   0.62 12.47 ?  55  LYS   A CG   1 
ATOM   1456 C  CG   B LYS   A 1 55  ? 20.543 12.794  8.152   0.38 12.85 ?  55  LYS   A CG   1 
ATOM   1457 C  CD   A LYS   A 1 55  ? 19.133 12.877  7.333   0.62 13.86 ?  55  LYS   A CD   1 
ATOM   1458 C  CD   B LYS   A 1 55  ? 19.216 13.088  7.457   0.38 14.32 ?  55  LYS   A CD   1 
ATOM   1459 C  CE   A LYS   A 1 55  ? 18.294 13.995  7.940   0.62 15.44 ?  55  LYS   A CE   1 
ATOM   1460 C  CE   B LYS   A 1 55  ? 18.337 14.024  8.282   0.38 15.84 ?  55  LYS   A CE   1 
ATOM   1461 N  NZ   A LYS   A 1 55  ? 16.957 14.079  7.290   0.62 16.32 ?  55  LYS   A NZ   1 
ATOM   1462 N  NZ   B LYS   A 1 55  ? 16.984 14.196  7.683   0.38 16.56 ?  55  LYS   A NZ   1 
ATOM   1463 H  H    A LYS   A 1 55  ? 22.676 9.715   6.774   0.62 12.15 ?  55  LYS   A H    1 
ATOM   1464 H  H    B LYS   A 1 55  ? 22.723 9.829   6.781   0.38 11.29 ?  55  LYS   A H    1 
ATOM   1465 H  HA   A LYS   A 1 55  ? 23.148 12.014  7.862   0.62 12.72 ?  55  LYS   A HA   1 
ATOM   1466 H  HA   B LYS   A 1 55  ? 23.225 12.066  7.972   0.38 12.62 ?  55  LYS   A HA   1 
ATOM   1467 H  HB2  A LYS   A 1 55  ? 21.295 11.653  6.496   0.62 13.28 ?  55  LYS   A HB2  1 
ATOM   1468 H  HB2  B LYS   A 1 55  ? 21.436 11.932  6.538   0.38 13.73 ?  55  LYS   A HB2  1 
ATOM   1469 H  HB3  A LYS   A 1 55  ? 20.650 10.725  7.606   0.62 13.28 ?  55  LYS   A HB3  1 
ATOM   1470 H  HB3  B LYS   A 1 55  ? 20.715 10.880  7.480   0.38 13.73 ?  55  LYS   A HB3  1 
ATOM   1471 H  HG2  A LYS   A 1 55  ? 20.321 12.563  8.977   0.62 14.95 ?  55  LYS   A HG2  1 
ATOM   1472 H  HG2  B LYS   A 1 55  ? 20.350 12.545  9.069   0.38 15.41 ?  55  LYS   A HG2  1 
ATOM   1473 H  HG3  A LYS   A 1 55  ? 21.008 13.504  7.887   0.62 14.95 ?  55  LYS   A HG3  1 
ATOM   1474 H  HG3  B LYS   A 1 55  ? 21.083 13.599  8.128   0.38 15.41 ?  55  LYS   A HG3  1 
ATOM   1475 H  HD2  A LYS   A 1 55  ? 19.284 13.089  6.398   0.62 16.61 ?  55  LYS   A HD2  1 
ATOM   1476 H  HD2  B LYS   A 1 55  ? 19.391 13.511  6.601   0.38 17.16 ?  55  LYS   A HD2  1 
ATOM   1477 H  HD3  A LYS   A 1 55  ? 18.629 12.050  7.407   0.62 16.61 ?  55  LYS   A HD3  1 
ATOM   1478 H  HD3  B LYS   A 1 55  ? 18.734 12.256  7.325   0.38 17.16 ?  55  LYS   A HD3  1 
ATOM   1479 H  HE2  A LYS   A 1 55  ? 18.165 13.821  8.886   0.62 18.52 ?  55  LYS   A HE2  1 
ATOM   1480 H  HE2  B LYS   A 1 55  ? 18.229 13.654  9.173   0.38 19.00 ?  55  LYS   A HE2  1 
ATOM   1481 H  HE3  A LYS   A 1 55  ? 18.751 14.842  7.814   0.62 18.52 ?  55  LYS   A HE3  1 
ATOM   1482 H  HE3  B LYS   A 1 55  ? 18.760 14.895  8.332   0.38 19.00 ?  55  LYS   A HE3  1 
ATOM   1483 H  HZ1  A LYS   A 1 55  ? 16.347 14.336  7.884   0.62 19.57 ?  55  LYS   A HZ1  1 
ATOM   1484 H  HZ1  B LYS   A 1 55  ? 16.493 14.738  8.191   0.38 19.85 ?  55  LYS   A HZ1  1 
ATOM   1485 H  HZ2  A LYS   A 1 55  ? 16.978 14.671  6.625   0.62 19.57 ?  55  LYS   A HZ2  1 
ATOM   1486 H  HZ2  B LYS   A 1 55  ? 17.054 14.548  6.868   0.38 19.85 ?  55  LYS   A HZ2  1 
ATOM   1487 H  HZ3  A LYS   A 1 55  ? 16.725 13.283  6.965   0.62 19.57 ?  55  LYS   A HZ3  1 
ATOM   1488 H  HZ3  B LYS   A 1 55  ? 16.574 13.408  7.623   0.38 19.85 ?  55  LYS   A HZ3  1 
ATOM   1489 N  N    . ALA   A 1 56  ? 22.134 9.822   9.968   1.00 10.89 ?  56  ALA   A N    1 
ATOM   1490 C  CA   . ALA   A 1 56  ? 22.012 9.506   11.386  1.00 11.53 ?  56  ALA   A CA   1 
ATOM   1491 C  C    . ALA   A 1 56  ? 23.353 9.533   12.108  1.00 11.04 ?  56  ALA   A C    1 
ATOM   1492 O  O    . ALA   A 1 56  ? 23.375 9.717   13.324  1.00 12.75 ?  56  ALA   A O    1 
ATOM   1493 C  CB   . ALA   A 1 56  ? 21.319 8.152   11.572  1.00 12.82 ?  56  ALA   A CB   1 
ATOM   1494 H  H    A ALA   A 1 56  ? 21.928 9.174   9.447   0.62 13.05 ?  56  ALA   A H    1 
ATOM   1495 H  H    B ALA   A 1 56  ? 21.955 9.175   9.435   0.38 13.05 ?  56  ALA   A H    1 
ATOM   1496 H  HA   . ALA   A 1 56  ? 21.455 10.172  11.804  1.00 13.81 ?  56  ALA   A HA   1 
ATOM   1497 H  HB1  . ALA   A 1 56  ? 21.252 7.958   12.524  1.00 15.37 ?  56  ALA   A HB1  1 
ATOM   1498 H  HB2  . ALA   A 1 56  ? 20.432 8.195   11.184  1.00 15.37 ?  56  ALA   A HB2  1 
ATOM   1499 H  HB3  . ALA   A 1 56  ? 21.839 7.460   11.134  1.00 15.37 ?  56  ALA   A HB3  1 
ATOM   1500 N  N    . THR   A 1 57  ? 24.465 9.347   11.389  1.00 10.66 ?  57  THR   A N    1 
ATOM   1501 C  CA   . THR   A 1 57  ? 25.808 9.473   11.961  1.00 10.85 ?  57  THR   A CA   1 
ATOM   1502 C  C    . THR   A 1 57  ? 26.361 10.891  11.879  1.00 11.34 ?  57  THR   A C    1 
ATOM   1503 O  O    . THR   A 1 57  ? 27.545 11.098  12.169  1.00 12.01 ?  57  THR   A O    1 
ATOM   1504 C  CB   . THR   A 1 57  ? 26.819 8.522   11.292  1.00 10.80 ?  57  THR   A CB   1 
ATOM   1505 O  OG1  . THR   A 1 57  ? 27.202 9.015   9.991   1.00 10.65 ?  57  THR   A OG1  1 
ATOM   1506 C  CG2  . THR   A 1 57  ? 26.291 7.100   11.199  1.00 11.05 ?  57  THR   A CG2  1 
ATOM   1507 H  H    . THR   A 1 57  ? 24.469 9.127   10.558  1.00 12.77 ?  57  THR   A H    1 
ATOM   1508 H  HA   . THR   A 1 57  ? 25.764 9.220   12.904  1.00 13.00 ?  57  THR   A HA   1 
ATOM   1509 H  HB   . THR   A 1 57  ? 27.616 8.491   11.848  1.00 12.95 ?  57  THR   A HB   1 
ATOM   1510 H  HG1  . THR   A 1 57  ? 26.519 9.088   9.505   1.00 12.77 ?  57  THR   A HG1  1 
ATOM   1511 H  HG21 . THR   A 1 57  ? 26.966 6.515   10.814  1.00 13.25 ?  57  THR   A HG21 1 
ATOM   1512 H  HG22 . THR   A 1 57  ? 26.058 6.768   12.082  1.00 13.25 ?  57  THR   A HG22 1 
ATOM   1513 H  HG23 . THR   A 1 57  ? 25.500 7.070   10.638  1.00 13.25 ?  57  THR   A HG23 1 
ATOM   1514 N  N    . ASN   A 1 58  ? 25.551 11.867  11.472  1.00 11.55 ?  58  ASN   A N    1 
ATOM   1515 C  CA   . ASN   A 1 58  ? 26.022 13.245  11.378  1.00 12.62 ?  58  ASN   A CA   1 
ATOM   1516 C  C    . ASN   A 1 58  ? 27.166 13.364  10.367  1.00 11.49 ?  58  ASN   A C    1 
ATOM   1517 O  O    . ASN   A 1 58  ? 28.066 14.194  10.521  1.00 11.99 ?  58  ASN   A O    1 
ATOM   1518 C  CB   . ASN   A 1 58  ? 26.396 13.776  12.777  1.00 15.57 ?  58  ASN   A CB   1 
ATOM   1519 C  CG   . ASN   A 1 58  ? 26.841 15.220  12.781  1.00 19.33 ?  58  ASN   A CG   1 
ATOM   1520 O  OD1  . ASN   A 1 58  ? 26.226 16.065  12.142  1.00 21.05 ?  58  ASN   A OD1  1 
ATOM   1521 N  ND2  . ASN   A 1 58  ? 27.908 15.516  13.531  1.00 20.49 ?  58  ASN   A ND2  1 
ATOM   1522 H  H    . ASN   A 1 58  ? 24.725 11.748  11.241  1.00 13.84 ?  58  ASN   A H    1 
ATOM   1523 H  HA   . ASN   A 1 58  ? 25.290 13.785  11.051  1.00 15.13 ?  58  ASN   A HA   1 
ATOM   1524 H  HB2  . ASN   A 1 58  ? 25.615 13.701  13.360  1.00 18.67 ?  58  ASN   A HB2  1 
ATOM   1525 H  HB3  . ASN   A 1 58  ? 27.119 13.247  13.140  1.00 18.67 ?  58  ASN   A HB3  1 
ATOM   1526 H  HD21 . ASN   A 1 58  ? 28.198 16.325  13.573  1.00 24.57 ?  58  ASN   A HD21 1 
ATOM   1527 H  HD22 . ASN   A 1 58  ? 28.309 14.893  13.967  1.00 24.57 ?  58  ASN   A HD22 1 
ATOM   1528 N  N    . ASN   A 1 59  ? 27.144 12.538  9.319   1.00 10.51 ?  59  ASN   A N    1 
ATOM   1529 C  CA   . ASN   A 1 59  ? 28.123 12.512  8.225   1.00 10.43 ?  59  ASN   A CA   1 
ATOM   1530 C  C    . ASN   A 1 59  ? 29.440 11.830  8.612   1.00 10.14 ?  59  ASN   A C    1 
ATOM   1531 O  O    . ASN   A 1 59  ? 30.359 11.783  7.780   1.00 10.63 ?  59  ASN   A O    1 
ATOM   1532 C  CB   . ASN   A 1 59  ? 28.403 13.898  7.615   1.00 10.58 ?  59  ASN   A CB   1 
ATOM   1533 C  CG   . ASN   A 1 59  ? 28.776 13.823  6.148   1.00 10.87 ?  59  ASN   A CG   1 
ATOM   1534 O  OD1  . ASN   A 1 59  ? 28.068 13.203  5.349   1.00 11.20 ?  59  ASN   A OD1  1 
ATOM   1535 N  ND2  . ASN   A 1 59  ? 29.861 14.492  5.771   1.00 11.44 ?  59  ASN   A ND2  1 
ATOM   1536 H  H    . ASN   A 1 59  ? 26.527 11.947  9.209   1.00 12.59 ?  59  ASN   A H    1 
ATOM   1537 H  HA   . ASN   A 1 59  ? 27.742 11.982  7.516   1.00 12.50 ?  59  ASN   A HA   1 
ATOM   1538 H  HB2  . ASN   A 1 59  ? 27.608 14.450  7.689   1.00 12.67 ?  59  ASN   A HB2  1 
ATOM   1539 H  HB3  . ASN   A 1 59  ? 29.142 14.317  8.081   1.00 12.67 ?  59  ASN   A HB3  1 
ATOM   1540 H  HD21 . ASN   A 1 59  ? 30.114 14.484  4.947   1.00 13.71 ?  59  ASN   A HD21 1 
ATOM   1541 H  HD22 . ASN   A 1 59  ? 30.331 14.919  6.354   1.00 13.71 ?  59  ASN   A HD22 1 
ATOM   1542 N  N    . ALA   A 1 60  ? 29.566 11.286  9.824   1.00 9.99  ?  60  ALA   A N    1 
ATOM   1543 C  CA   . ALA   A 1 60  ? 30.797 10.593  10.184  1.00 10.36 ?  60  ALA   A CA   1 
ATOM   1544 C  C    . ALA   A 1 60  ? 31.018 9.357   9.321   1.00 10.34 ?  60  ALA   A C    1 
ATOM   1545 O  O    . ALA   A 1 60  ? 32.163 9.031   8.989   1.00 10.93 ?  60  ALA   A O    1 
ATOM   1546 C  CB   . ALA   A 1 60  ? 30.789 10.239  11.669  1.00 11.26 ?  60  ALA   A CB   1 
ATOM   1547 H  H    . ALA   A 1 60  ? 28.970 11.307  10.445  1.00 11.97 ?  60  ALA   A H    1 
ATOM   1548 H  HA   . ALA   A 1 60  ? 31.548 11.193  10.034  1.00 12.42 ?  60  ALA   A HA   1 
ATOM   1549 H  HB1  . ALA   A 1 60  ? 31.615 9.781   11.891  1.00 13.50 ?  60  ALA   A HB1  1 
ATOM   1550 H  HB2  . ALA   A 1 60  ? 30.718 11.058  12.187  1.00 13.50 ?  60  ALA   A HB2  1 
ATOM   1551 H  HB3  . ALA   A 1 60  ? 30.031 9.666   11.852  1.00 13.50 ?  60  ALA   A HB3  1 
ATOM   1552 N  N    . MET   A 1 61  ? 29.944 8.670   8.936   1.00 9.98  ?  61  MET   A N    1 
ATOM   1553 C  CA   . MET   A 1 61  ? 30.082 7.534   8.033   1.00 9.80  ?  61  MET   A CA   1 
ATOM   1554 C  C    . MET   A 1 61  ? 30.713 7.955   6.708   1.00 9.84  ?  61  MET   A C    1 
ATOM   1555 O  O    . MET   A 1 61  ? 31.608 7.272   6.194   1.00 10.21 ?  61  MET   A O    1 
ATOM   1556 C  CB   . MET   A 1 61  ? 28.719 6.871   7.822   1.00 9.69  ?  61  MET   A CB   1 
ATOM   1557 C  CG   . MET   A 1 61  ? 28.731 5.708   6.850   1.00 10.59 ?  61  MET   A CG   1 
ATOM   1558 S  SD   . MET   A 1 61  ? 27.106 4.953   6.644   1.00 11.38 ?  61  MET   A SD   1 
ATOM   1559 C  CE   . MET   A 1 61  ? 26.973 4.067   8.202   1.00 12.73 ?  61  MET   A CE   1 
ATOM   1560 H  H    . MET   A 1 61  ? 29.138 8.845   9.177   1.00 11.96 ?  61  MET   A H    1 
ATOM   1561 H  HA   . MET   A 1 61  ? 30.660 6.880   8.453   1.00 11.74 ?  61  MET   A HA   1 
ATOM   1562 H  HB2  . MET   A 1 61  ? 28.404 6.537   8.678   1.00 11.61 ?  61  MET   A HB2  1 
ATOM   1563 H  HB3  . MET   A 1 61  ? 28.098 7.533   7.484   1.00 11.61 ?  61  MET   A HB3  1 
ATOM   1564 H  HG2  . MET   A 1 61  ? 29.016 6.018   5.980   1.00 12.70 ?  61  MET   A HG2  1 
ATOM   1565 H  HG3  . MET   A 1 61  ? 29.332 5.023   7.178   1.00 12.70 ?  61  MET   A HG3  1 
ATOM   1566 H  HE1  . MET   A 1 61  ? 26.133 3.581   8.224   1.00 15.26 ?  61  MET   A HE1  1 
ATOM   1567 H  HE2  . MET   A 1 61  ? 27.716 3.452   8.281   1.00 15.26 ?  61  MET   A HE2  1 
ATOM   1568 H  HE3  . MET   A 1 61  ? 26.997 4.709   8.934   1.00 15.26 ?  61  MET   A HE3  1 
ATOM   1569 N  N    . GLN   A 1 62  ? 30.274 9.086   6.149   1.00 9.72  ?  62  GLN   A N    1 
ATOM   1570 C  CA   . GLN   A 1 62  ? 30.836 9.552   4.886   1.00 9.86  ?  62  GLN   A CA   1 
ATOM   1571 C  C    . GLN   A 1 62  ? 32.308 9.928   5.033   1.00 9.64  ?  62  GLN   A C    1 
ATOM   1572 O  O    . GLN   A 1 62  ? 33.120 9.611   4.158   1.00 10.22 ?  62  GLN   A O    1 
ATOM   1573 C  CB   . GLN   A 1 62  ? 30.039 10.736  4.348   1.00 10.09 ?  62  GLN   A CB   1 
ATOM   1574 C  CG   . GLN   A 1 62  ? 30.427 11.092  2.927   1.00 10.10 ?  62  GLN   A CG   1 
ATOM   1575 C  CD   . GLN   A 1 62  ? 30.093 9.963   1.983   1.00 10.34 ?  62  GLN   A CD   1 
ATOM   1576 O  OE1  . GLN   A 1 62  ? 28.910 9.659   1.774   1.00 10.78 ?  62  GLN   A OE1  1 
ATOM   1577 N  NE2  . GLN   A 1 62  ? 31.112 9.286   1.457   1.00 10.79 ?  62  GLN   A NE2  1 
ATOM   1578 H  H    . GLN   A 1 62  ? 29.657 9.584   6.477   1.00 11.65 ?  62  GLN   A H    1 
ATOM   1579 H  HA   . GLN   A 1 62  ? 30.780 8.831   4.241   1.00 11.82 ?  62  GLN   A HA   1 
ATOM   1580 H  HB2  . GLN   A 1 62  ? 29.093 10.516  4.356   1.00 12.09 ?  62  GLN   A HB2  1 
ATOM   1581 H  HB3  . GLN   A 1 62  ? 30.202 11.512  4.909   1.00 12.09 ?  62  GLN   A HB3  1 
ATOM   1582 H  HG2  . GLN   A 1 62  ? 29.934 11.878  2.645   1.00 12.10 ?  62  GLN   A HG2  1 
ATOM   1583 H  HG3  . GLN   A 1 62  ? 31.382 11.259  2.882   1.00 12.10 ?  62  GLN   A HG3  1 
ATOM   1584 H  HE21 . GLN   A 1 62  ? 31.921 9.511   1.643   1.00 12.93 ?  62  GLN   A HE21 1 
ATOM   1585 H  HE22 . GLN   A 1 62  ? 30.960 8.627   0.927   1.00 12.93 ?  62  GLN   A HE22 1 
ATOM   1586 N  N    . VAL   A 1 63  ? 32.671 10.612  6.124   1.00 10.19 ?  63  VAL   A N    1 
ATOM   1587 C  CA   . VAL   A 1 63  ? 34.066 11.004  6.335   1.00 11.25 ?  63  VAL   A CA   1 
ATOM   1588 C  C    . VAL   A 1 63  ? 34.960 9.769   6.400   1.00 10.48 ?  63  VAL   A C    1 
ATOM   1589 O  O    . VAL   A 1 63  ? 36.011 9.700   5.748   1.00 11.35 ?  63  VAL   A O    1 
ATOM   1590 C  CB   . VAL   A 1 63  ? 34.181 11.878  7.598   1.00 12.88 ?  63  VAL   A CB   1 
ATOM   1591 C  CG1  . VAL   A 1 63  ? 35.626 12.114  7.957   1.00 14.69 ?  63  VAL   A CG1  1 
ATOM   1592 C  CG2  . VAL   A 1 63  ? 33.459 13.208  7.380   1.00 13.36 ?  63  VAL   A CG2  1 
ATOM   1593 H  H    . VAL   A 1 63  ? 32.129 10.862  6.751   1.00 12.22 ?  63  VAL   A H    1 
ATOM   1594 H  HA   . VAL   A 1 63  ? 34.350 11.540  5.581   1.00 13.48 ?  63  VAL   A HA   1 
ATOM   1595 H  HB   . VAL   A 1 63  ? 33.759 11.420  8.343   1.00 15.44 ?  63  VAL   A HB   1 
ATOM   1596 H  HG11 . VAL   A 1 63  ? 35.676 12.846  8.589   1.00 17.61 ?  63  VAL   A HG11 1 
ATOM   1597 H  HG12 . VAL   A 1 63  ? 35.993 11.309  8.352   1.00 17.61 ?  63  VAL   A HG12 1 
ATOM   1598 H  HG13 . VAL   A 1 63  ? 36.116 12.342  7.149   1.00 17.61 ?  63  VAL   A HG13 1 
ATOM   1599 H  HG21 . VAL   A 1 63  ? 33.553 13.753  8.177   1.00 16.02 ?  63  VAL   A HG21 1 
ATOM   1600 H  HG22 . VAL   A 1 63  ? 33.859 13.663  6.621   1.00 16.02 ?  63  VAL   A HG22 1 
ATOM   1601 H  HG23 . VAL   A 1 63  ? 32.522 13.035  7.206   1.00 16.02 ?  63  VAL   A HG23 1 
ATOM   1602 N  N    . GLU   A 1 64  ? 34.537 8.764   7.171   1.00 10.41 ?  64  GLU   A N    1 
ATOM   1603 C  CA   . GLU   A 1 64  ? 35.294 7.523   7.271   1.00 10.83 ?  64  GLU   A CA   1 
ATOM   1604 C  C    . GLU   A 1 64  ? 35.386 6.829   5.918   1.00 10.29 ?  64  GLU   A C    1 
ATOM   1605 O  O    . GLU   A 1 64  ? 36.438 6.289   5.543   1.00 10.93 ?  64  GLU   A O    1 
ATOM   1606 C  CB   . GLU   A 1 64  ? 34.605 6.617   8.292   1.00 10.98 ?  64  GLU   A CB   1 
ATOM   1607 C  CG   . GLU   A 1 64  ? 35.256 5.271   8.448   1.00 11.85 ?  64  GLU   A CG   1 
ATOM   1608 C  CD   . GLU   A 1 64  ? 34.374 4.278   9.171   1.00 12.25 ?  64  GLU   A CD   1 
ATOM   1609 O  OE1  . GLU   A 1 64  ? 33.134 4.376   9.032   1.00 13.20 ?  64  GLU   A OE1  1 
ATOM   1610 O  OE2  . GLU   A 1 64  ? 34.923 3.388   9.861   1.00 12.70 -1 64  GLU   A OE2  1 
ATOM   1611 H  H    . GLU   A 1 64  ? 33.816 8.775   7.641   1.00 12.47 ?  64  GLU   A H    1 
ATOM   1612 H  HA   . GLU   A 1 64  ? 36.196 7.719   7.586   1.00 12.98 ?  64  GLU   A HA   1 
ATOM   1613 H  HB2  . GLU   A 1 64  ? 34.627 7.059   9.161   1.00 13.16 ?  64  GLU   A HB2  1 
ATOM   1614 H  HB3  . GLU   A 1 64  ? 33.690 6.486   8.015   1.00 13.16 ?  64  GLU   A HB3  1 
ATOM   1615 H  HG2  . GLU   A 1 64  ? 35.458 4.905   7.571   1.00 14.20 ?  64  GLU   A HG2  1 
ATOM   1616 H  HG3  . GLU   A 1 64  ? 36.073 5.375   8.956   1.00 14.20 ?  64  GLU   A HG3  1 
ATOM   1617 N  N    . SER   A 1 65  ? 34.270 6.817   5.183   1.00 9.92  ?  65  SER   A N    1 
ATOM   1618 C  CA   . SER   A 1 65  ? 34.218 6.161   3.881   1.00 9.87  ?  65  SER   A CA   1 
ATOM   1619 C  C    . SER   A 1 65  ? 35.142 6.828   2.873   1.00 10.19 ?  65  SER   A C    1 
ATOM   1620 O  O    . SER   A 1 65  ? 35.780 6.147   2.060   1.00 11.18 ?  65  SER   A O    1 
ATOM   1621 C  CB   . SER   A 1 65  ? 32.784 6.168   3.349   1.00 9.88  ?  65  SER   A CB   1 
ATOM   1622 O  OG   . SER   A 1 65  ? 31.931 5.357   4.153   1.00 10.55 ?  65  SER   A OG   1 
ATOM   1623 H  H    . SER   A 1 65  ? 33.531 7.191   5.420   1.00 11.88 ?  65  SER   A H    1 
ATOM   1624 H  HA   . SER   A 1 65  ? 34.502 5.242   3.979   1.00 11.83 ?  65  SER   A HA   1 
ATOM   1625 H  HB2  . SER   A 1 65  ? 32.446 7.076   3.352   1.00 11.84 ?  65  SER   A HB2  1 
ATOM   1626 H  HB3  . SER   A 1 65  ? 32.785 5.819   2.444   1.00 11.84 ?  65  SER   A HB3  1 
ATOM   1627 H  HG   . SER   A 1 65  ? 31.930 5.650   4.947   1.00 12.64 ?  65  SER   A HG   1 
ATOM   1628 N  N    . ASP   A 1 66  ? 35.224 8.160   2.897   1.00 10.28 ?  66  ASP   A N    1 
ATOM   1629 C  CA   . ASP   A 1 66  ? 36.084 8.856   1.945   1.00 11.26 ?  66  ASP   A CA   1 
ATOM   1630 C  C    . ASP   A 1 66  ? 37.547 8.499   2.178   1.00 11.13 ?  66  ASP   A C    1 
ATOM   1631 O  O    . ASP   A 1 66  ? 38.313 8.320   1.224   1.00 12.27 ?  66  ASP   A O    1 
ATOM   1632 C  CB   . ASP   A 1 66  ? 35.866 10.363  2.053   1.00 12.46 ?  66  ASP   A CB   1 
ATOM   1633 C  CG   . ASP   A 1 66  ? 34.532 10.825  1.457   1.00 14.37 ?  66  ASP   A CG   1 
ATOM   1634 O  OD1  . ASP   A 1 66  ? 33.822 10.028  0.807   1.00 14.38 ?  66  ASP   A OD1  1 
ATOM   1635 O  OD2  . ASP   A 1 66  ? 34.229 12.026  1.612   1.00 17.36 -1 66  ASP   A OD2  1 
ATOM   1636 H  H    . ASP   A 1 66  ? 34.789 8.674   3.433   1.00 12.32 ?  66  ASP   A H    1 
ATOM   1637 H  HA   . ASP   A 1 66  ? 35.847 8.586   1.043   1.00 13.49 ?  66  ASP   A HA   1 
ATOM   1638 H  HB2  . ASP   A 1 66  ? 35.878 10.618  2.989   1.00 14.94 ?  66  ASP   A HB2  1 
ATOM   1639 H  HB3  . ASP   A 1 66  ? 36.584 10.820  1.580   1.00 14.94 ?  66  ASP   A HB3  1 
ATOM   1640 N  N    . ASP   A 1 67  ? 37.946 8.367   3.443   1.00 11.19 ?  67  ASP   A N    1 
ATOM   1641 C  CA   . ASP   A 1 67  ? 39.301 7.916   3.739   1.00 12.18 ?  67  ASP   A CA   1 
ATOM   1642 C  C    . ASP   A 1 67  ? 39.518 6.480   3.274   1.00 12.21 ?  67  ASP   A C    1 
ATOM   1643 O  O    . ASP   A 1 67  ? 40.574 6.155   2.719   1.00 12.69 ?  67  ASP   A O    1 
ATOM   1644 C  CB   . ASP   A 1 67  ? 39.575 8.054   5.233   1.00 13.61 ?  67  ASP   A CB   1 
ATOM   1645 C  CG   . ASP   A 1 67  ? 40.860 7.390   5.653   1.00 14.71 ?  67  ASP   A CG   1 
ATOM   1646 O  OD1  . ASP   A 1 67  ? 41.936 8.020   5.511   1.00 17.25 ?  67  ASP   A OD1  1 
ATOM   1647 O  OD2  . ASP   A 1 67  ? 40.805 6.229   6.123   1.00 14.44 -1 67  ASP   A OD2  1 
ATOM   1648 H  H    . ASP   A 1 67  ? 37.460 8.530   4.130   1.00 13.41 ?  67  ASP   A H    1 
ATOM   1649 H  HA   . ASP   A 1 67  ? 39.932 8.480   3.260   1.00 14.60 ?  67  ASP   A HA   1 
ATOM   1650 H  HB2  . ASP   A 1 67  ? 39.635 8.990   5.453   1.00 16.31 ?  67  ASP   A HB2  1 
ATOM   1651 H  HB3  . ASP   A 1 67  ? 38.852 7.633   5.721   1.00 16.31 ?  67  ASP   A HB3  1 
ATOM   1652 N  N    . TYR   A 1 68  ? 38.521 5.609   3.476   1.00 11.59 ?  68  TYR   A N    1 
ATOM   1653 C  CA   . TYR   A 1 68  ? 38.632 4.230   3.003   1.00 11.72 ?  68  TYR   A CA   1 
ATOM   1654 C  C    . TYR   A 1 68  ? 38.872 4.179   1.495   1.00 11.69 ?  68  TYR   A C    1 
ATOM   1655 O  O    . TYR   A 1 68  ? 39.745 3.437   1.020   1.00 12.20 ?  68  TYR   A O    1 
ATOM   1656 C  CB   . TYR   A 1 68  ? 37.378 3.416   3.386   1.00 12.19 ?  68  TYR   A CB   1 
ATOM   1657 C  CG   . TYR   A 1 68  ? 37.401 2.024   2.760   1.00 13.43 ?  68  TYR   A CG   1 
ATOM   1658 C  CD1  . TYR   A 1 68  ? 36.944 1.829   1.460   1.00 14.68 ?  68  TYR   A CD1  1 
ATOM   1659 C  CD2  . TYR   A 1 68  ? 37.937 0.935   3.433   1.00 14.90 ?  68  TYR   A CD2  1 
ATOM   1660 C  CE1  . TYR   A 1 68  ? 37.014 0.610   0.846   1.00 15.99 ?  68  TYR   A CE1  1 
ATOM   1661 C  CE2  . TYR   A 1 68  ? 38.008 -0.325  2.816   1.00 15.37 ?  68  TYR   A CE2  1 
ATOM   1662 C  CZ   . TYR   A 1 68  ? 37.546 -0.460  1.524   1.00 15.81 ?  68  TYR   A CZ   1 
ATOM   1663 O  OH   . TYR   A 1 68  ? 37.627 -1.668  0.892   1.00 17.12 ?  68  TYR   A OH   1 
ATOM   1664 H  H    . TYR   A 1 68  ? 37.781 5.793   3.875   1.00 13.89 ?  68  TYR   A H    1 
ATOM   1665 H  HA   . TYR   A 1 68  ? 39.392 3.816   3.437   1.00 14.04 ?  68  TYR   A HA   1 
ATOM   1666 H  HB2  . TYR   A 1 68  ? 37.345 3.312   4.349   1.00 14.61 ?  68  TYR   A HB2  1 
ATOM   1667 H  HB3  . TYR   A 1 68  ? 36.586 3.878   3.069   1.00 14.61 ?  68  TYR   A HB3  1 
ATOM   1668 H  HD1  . TYR   A 1 68  ? 36.598 2.556   0.988   1.00 17.60 ?  68  TYR   A HD1  1 
ATOM   1669 H  HD2  . TYR   A 1 68  ? 38.269 1.049   4.293   1.00 17.87 ?  68  TYR   A HD2  1 
ATOM   1670 H  HE1  . TYR   A 1 68  ? 36.696 0.505   -0.020  1.00 19.17 ?  68  TYR   A HE1  1 
ATOM   1671 H  HE2  . TYR   A 1 68  ? 38.369 -1.051  3.261   1.00 18.43 ?  68  TYR   A HE2  1 
ATOM   1672 H  HH   . TYR   A 1 68  ? 37.956 -2.239  1.418   1.00 20.53 ?  68  TYR   A HH   1 
ATOM   1673 N  N    . ILE   A 1 69  ? 38.086 4.940   0.721   1.00 11.08 ?  69  ILE   A N    1 
ATOM   1674 C  CA   . ILE   A 1 69  ? 38.224 4.926   -0.735  1.00 11.33 ?  69  ILE   A CA   1 
ATOM   1675 C  C    . ILE   A 1 69  ? 39.561 5.529   -1.161  1.00 11.30 ?  69  ILE   A C    1 
ATOM   1676 O  O    . ILE   A 1 69  ? 40.213 5.036   -2.090  1.00 11.73 ?  69  ILE   A O    1 
ATOM   1677 C  CB   . ILE   A 1 69  ? 37.034 5.642   -1.403  1.00 12.03 ?  69  ILE   A CB   1 
ATOM   1678 C  CG1  . ILE   A 1 69  ? 35.715 4.920   -1.122  1.00 12.59 ?  69  ILE   A CG1  1 
ATOM   1679 C  CG2  . ILE   A 1 69  ? 37.276 5.823   -2.909  1.00 13.58 ?  69  ILE   A CG2  1 
ATOM   1680 C  CD1  . ILE   A 1 69  ? 35.554 3.622   -1.873  1.00 13.24 ?  69  ILE   A CD1  1 
ATOM   1681 H  H    . ILE   A 1 69  ? 37.479 5.471   1.017   1.00 13.28 ?  69  ILE   A H    1 
ATOM   1682 H  HA   . ILE   A 1 69  ? 38.219 4.002   -1.030  1.00 13.58 ?  69  ILE   A HA   1 
ATOM   1683 H  HB   . ILE   A 1 69  ? 36.973 6.523   -1.012  1.00 14.42 ?  69  ILE   A HB   1 
ATOM   1684 H  HG12 . ILE   A 1 69  ? 35.667 4.719   -0.172  1.00 15.10 ?  69  ILE   A HG12 1 
ATOM   1685 H  HG13 . ILE   A 1 69  ? 34.985 5.502   -1.372  1.00 15.10 ?  69  ILE   A HG13 1 
ATOM   1686 H  HG21 . ILE   A 1 69  ? 36.435 6.043   -3.339  1.00 16.28 ?  69  ILE   A HG21 1 
ATOM   1687 H  HG22 . ILE   A 1 69  ? 37.911 6.549   -3.045  1.00 16.28 ?  69  ILE   A HG22 1 
ATOM   1688 H  HG23 . ILE   A 1 69  ? 37.632 5.001   -3.279  1.00 16.28 ?  69  ILE   A HG23 1 
ATOM   1689 H  HD11 . ILE   A 1 69  ? 34.748 3.182   -1.565  1.00 15.87 ?  69  ILE   A HD11 1 
ATOM   1690 H  HD12 . ILE   A 1 69  ? 35.485 3.812   -2.822  1.00 15.87 ?  69  ILE   A HD12 1 
ATOM   1691 H  HD13 . ILE   A 1 69  ? 36.324 3.057   -1.703  1.00 15.87 ?  69  ILE   A HD13 1 
ATOM   1692 N  N    . ALA   A 1 70  ? 39.985 6.607   -0.502  1.00 11.72 ?  70  ALA   A N    1 
ATOM   1693 C  CA   . ALA   A 1 70  ? 41.268 7.211   -0.851  1.00 12.73 ?  70  ALA   A CA   1 
ATOM   1694 C  C    . ALA   A 1 70  ? 42.414 6.224   -0.682  1.00 13.04 ?  70  ALA   A C    1 
ATOM   1695 O  O    . ALA   A 1 70  ? 43.382 6.258   -1.446  1.00 14.82 ?  70  ALA   A O    1 
ATOM   1696 C  CB   . ALA   A 1 70  ? 41.513 8.459   -0.002  1.00 13.46 ?  70  ALA   A CB   1 
ATOM   1697 H  H    . ALA   A 1 70  ? 39.555 7.000   0.130   1.00 14.05 ?  70  ALA   A H    1 
ATOM   1698 H  HA   . ALA   A 1 70  ? 41.238 7.491   -1.780  1.00 15.26 ?  70  ALA   A HA   1 
ATOM   1699 H  HB1  . ALA   A 1 70  ? 42.375 8.844   -0.250  1.00 16.13 ?  70  ALA   A HB1  1 
ATOM   1700 H  HB2  . ALA   A 1 70  ? 40.810 9.104   -0.163  1.00 16.13 ?  70  ALA   A HB2  1 
ATOM   1701 H  HB3  . ALA   A 1 70  ? 41.529 8.209   0.935   1.00 16.13 ?  70  ALA   A HB3  1 
ATOM   1702 N  N    . THR   A 1 71  ? 42.310 5.326   0.296   1.00 12.53 ?  71  THR   A N    1 
ATOM   1703 C  CA   . THR   A 1 71  ? 43.359 4.344   0.551   1.00 14.11 ?  71  THR   A CA   1 
ATOM   1704 C  C    . THR   A 1 71  ? 43.235 3.118   -0.344  1.00 14.25 ?  71  THR   A C    1 
ATOM   1705 O  O    . THR   A 1 71  ? 44.247 2.601   -0.836  1.00 16.11 ?  71  THR   A O    1 
ATOM   1706 C  CB   . THR   A 1 71  ? 43.277 3.900   2.008   1.00 16.04 ?  71  THR   A CB   1 
ATOM   1707 O  OG1  . THR   A 1 71  ? 43.519 5.028   2.856   1.00 17.28 ?  71  THR   A OG1  1 
ATOM   1708 C  CG2  . THR   A 1 71  ? 44.277 2.791   2.308   1.00 17.51 ?  71  THR   A CG2  1 
ATOM   1709 H  H    . THR   A 1 71  ? 41.634 5.262   0.822   1.00 15.02 ?  71  THR   A H    1 
ATOM   1710 H  HA   . THR   A 1 71  ? 44.225 4.751   0.395   1.00 16.91 ?  71  THR   A HA   1 
ATOM   1711 H  HB   . THR   A 1 71  ? 42.384 3.551   2.175   1.00 19.23 ?  71  THR   A HB   1 
ATOM   1712 H  HG1  . THR   A 1 71  ? 42.932 5.613   2.714   1.00 20.72 ?  71  THR   A HG1  1 
ATOM   1713 H  HG21 . THR   A 1 71  ? 44.396 2.711   3.266   1.00 21.00 ?  71  THR   A HG21 1 
ATOM   1714 H  HG22 . THR   A 1 71  ? 43.961 1.944   1.958   1.00 21.00 ?  71  THR   A HG22 1 
ATOM   1715 H  HG23 . THR   A 1 71  ? 45.134 3.001   1.902   1.00 21.00 ?  71  THR   A HG23 1 
ATOM   1716 N  N    . ASN   A 1 72  ? 42.010 2.620   -0.538  1.00 13.13 ?  72  ASN   A N    1 
ATOM   1717 C  CA   . ASN   A 1 72  ? 41.786 1.296   -1.101  1.00 13.46 ?  72  ASN   A CA   1 
ATOM   1718 C  C    . ASN   A 1 72  ? 41.159 1.285   -2.483  1.00 13.46 ?  72  ASN   A C    1 
ATOM   1719 O  O    . ASN   A 1 72  ? 41.169 0.231   -3.133  1.00 14.78 ?  72  ASN   A O    1 
ATOM   1720 C  CB   . ASN   A 1 72  ? 40.902 0.473   -0.159  1.00 14.16 ?  72  ASN   A CB   1 
ATOM   1721 C  CG   . ASN   A 1 72  ? 41.517 0.320   1.204   1.00 15.29 ?  72  ASN   A CG   1 
ATOM   1722 O  OD1  . ASN   A 1 72  ? 41.061 0.919   2.179   1.00 17.04 ?  72  ASN   A OD1  1 
ATOM   1723 N  ND2  . ASN   A 1 72  ? 42.570 -0.465  1.281   1.00 15.98 ?  72  ASN   A ND2  1 
ATOM   1724 H  H    . ASN   A 1 72  ? 41.280 3.042   -0.349  1.00 15.74 ?  72  ASN   A H    1 
ATOM   1725 H  HA   . ASN   A 1 72  ? 42.644 0.850   -1.174  1.00 16.13 ?  72  ASN   A HA   1 
ATOM   1726 H  HB2  . ASN   A 1 72  ? 40.047 0.911   -0.064  1.00 16.97 ?  72  ASN   A HB2  1 
ATOM   1727 H  HB3  . ASN   A 1 72  ? 40.785 -0.415  -0.541  1.00 16.97 ?  72  ASN   A HB3  1 
ATOM   1728 H  HD21 . ASN   A 1 72  ? 42.967 -0.578  2.037   1.00 19.16 ?  72  ASN   A HD21 1 
ATOM   1729 H  HD22 . ASN   A 1 72  ? 42.872 -0.859  0.578   1.00 19.16 ?  72  ASN   A HD22 1 
ATOM   1730 N  N    . GLY   A 1 73  ? 40.605 2.399   -2.943  1.00 12.98 ?  73  GLY   A N    1 
ATOM   1731 C  CA   . GLY   A 1 73  ? 39.880 2.409   -4.187  1.00 12.66 ?  73  GLY   A CA   1 
ATOM   1732 C  C    . GLY   A 1 73  ? 38.487 1.833   -4.015  1.00 12.16 ?  73  GLY   A C    1 
ATOM   1733 O  O    . GLY   A 1 73  ? 38.103 1.371   -2.933  1.00 12.71 ?  73  GLY   A O    1 
ATOM   1734 H  H    . GLY   A 1 73  ? 40.643 3.169   -2.553  1.00 15.56 ?  73  GLY   A H    1 
ATOM   1735 H  HA2  . GLY   A 1 73  ? 39.805 3.325   -4.510  1.00 15.18 ?  73  GLY   A HA2  1 
ATOM   1736 H  HA3  . GLY   A 1 73  ? 40.356 1.887   -4.850  1.00 15.18 ?  73  GLY   A HA3  1 
ATOM   1737 N  N    . PRO   A 1 74  ? 37.708 1.858   -5.095  1.00 12.78 ?  74  PRO   A N    1 
ATOM   1738 C  CA   . PRO   A 1 74  ? 36.311 1.427   -5.021  1.00 12.67 ?  74  PRO   A CA   1 
ATOM   1739 C  C    . PRO   A 1 74  ? 36.158 -0.054  -4.704  1.00 12.29 ?  74  PRO   A C    1 
ATOM   1740 O  O    . PRO   A 1 74  ? 37.027 -0.886  -4.991  1.00 12.92 ?  74  PRO   A O    1 
ATOM   1741 C  CB   . PRO   A 1 74  ? 35.776 1.731   -6.426  1.00 14.18 ?  74  PRO   A CB   1 
ATOM   1742 C  CG   . PRO   A 1 74  ? 36.737 2.702   -7.026  1.00 16.86 ?  74  PRO   A CG   1 
ATOM   1743 C  CD   . PRO   A 1 74  ? 38.063 2.368   -6.429  1.00 14.68 ?  74  PRO   A CD   1 
ATOM   1744 H  HA   . PRO   A 1 74  ? 35.826 1.953   -4.365  1.00 15.19 ?  74  PRO   A HA   1 
ATOM   1745 H  HB2  . PRO   A 1 74  ? 35.744 0.912   -6.942  1.00 17.00 ?  74  PRO   A HB2  1 
ATOM   1746 H  HB3  . PRO   A 1 74  ? 34.892 2.125   -6.354  1.00 17.00 ?  74  PRO   A HB3  1 
ATOM   1747 H  HG2  . PRO   A 1 74  ? 36.761 2.586   -7.988  1.00 20.21 ?  74  PRO   A HG2  1 
ATOM   1748 H  HG3  . PRO   A 1 74  ? 36.481 3.606   -6.794  1.00 20.21 ?  74  PRO   A HG3  1 
ATOM   1749 H  HD2  . PRO   A 1 74  ? 38.512 1.677   -6.948  1.00 17.60 ?  74  PRO   A HD2  1 
ATOM   1750 H  HD3  . PRO   A 1 74  ? 38.613 3.169   -6.365  1.00 17.60 ?  74  PRO   A HD3  1 
ATOM   1751 N  N    . LEU   A 1 75  ? 35.012 -0.375  -4.114  1.00 11.50 ?  75  LEU   A N    1 
ATOM   1752 C  CA   . LEU   A 1 75  ? 34.611 -1.763  -3.961  1.00 11.10 ?  75  LEU   A CA   1 
ATOM   1753 C  C    . LEU   A 1 75  ? 34.223 -2.339  -5.319  1.00 11.53 ?  75  LEU   A C    1 
ATOM   1754 O  O    . LEU   A 1 75  ? 34.101 -1.625  -6.319  1.00 12.98 ?  75  LEU   A O    1 
ATOM   1755 C  CB   . LEU   A 1 75  ? 33.423 -1.882  -3.006  1.00 11.01 ?  75  LEU   A CB   1 
ATOM   1756 C  CG   . LEU   A 1 75  ? 33.633 -1.451  -1.558  1.00 12.71 ?  75  LEU   A CG   1 
ATOM   1757 C  CD1  . LEU   A 1 75  ? 32.341 -1.641  -0.771  1.00 14.55 ?  75  LEU   A CD1  1 
ATOM   1758 C  CD2  . LEU   A 1 75  ? 34.766 -2.173  -0.895  1.00 15.70 ?  75  LEU   A CD2  1 
ATOM   1759 H  H    . LEU   A 1 75  ? 34.447 0.197   -3.803  1.00 13.78 ?  75  LEU   A H    1 
ATOM   1760 H  HA   . LEU   A 1 75  ? 35.352 -2.274  -3.609  1.00 13.31 ?  75  LEU   A HA   1 
ATOM   1761 H  HB2  . LEU   A 1 75  ? 32.697 -1.346  -3.361  1.00 13.19 ?  75  LEU   A HB2  1 
ATOM   1762 H  HB3  . LEU   A 1 75  ? 33.149 -2.814  -2.990  1.00 13.19 ?  75  LEU   A HB3  1 
ATOM   1763 H  HG   . LEU   A 1 75  ? 33.850 -0.505  -1.547  1.00 15.23 ?  75  LEU   A HG   1 
ATOM   1764 H  HD11 . LEU   A 1 75  ? 32.488 -1.361  0.145   1.00 17.44 ?  75  LEU   A HD11 1 
ATOM   1765 H  HD12 . LEU   A 1 75  ? 31.649 -1.095  -1.178  1.00 17.44 ?  75  LEU   A HD12 1 
ATOM   1766 H  HD13 . LEU   A 1 75  ? 32.090 -2.574  -0.800  1.00 17.44 ?  75  LEU   A HD13 1 
ATOM   1767 H  HD21 . LEU   A 1 75  ? 34.816 -1.899  0.035   1.00 18.82 ?  75  LEU   A HD21 1 
ATOM   1768 H  HD22 . LEU   A 1 75  ? 34.614 -3.126  -0.953  1.00 18.82 ?  75  LEU   A HD22 1 
ATOM   1769 H  HD23 . LEU   A 1 75  ? 35.598 -1.943  -1.347  1.00 18.82 ?  75  LEU   A HD23 1 
ATOM   1770 N  N    . LYS   A 1 76  ? 34.041 -3.658  -5.337  1.00 11.92 ?  76  LYS   A N    1 
ATOM   1771 C  CA   . LYS   A 1 76  ? 33.445 -4.381  -6.454  1.00 12.48 ?  76  LYS   A CA   1 
ATOM   1772 C  C    . LYS   A 1 76  ? 31.932 -4.462  -6.265  1.00 10.91 ?  76  LYS   A C    1 
ATOM   1773 O  O    . LYS   A 1 76  ? 31.446 -4.583  -5.144  1.00 11.10 ?  76  LYS   A O    1 
ATOM   1774 C  CB   . LYS   A 1 76  ? 33.988 -5.821  -6.496  1.00 14.14 ?  76  LYS   A CB   1 
ATOM   1775 C  CG   . LYS   A 1 76  ? 35.498 -5.936  -6.687  1.00 15.49 ?  76  LYS   A CG   1 
ATOM   1776 C  CD   . LYS   A 1 76  ? 36.009 -7.343  -6.479  1.00 16.77 ?  76  LYS   A CD   1 
ATOM   1777 C  CE   . LYS   A 1 76  ? 37.508 -7.399  -6.665  1.00 19.32 ?  76  LYS   A CE   1 
ATOM   1778 N  NZ   . LYS   A 1 76  ? 38.035 -8.756  -6.447  1.00 20.39 ?  76  LYS   A NZ   1 
ATOM   1779 H  H    . LYS   A 1 76  ? 34.272 -4.174  -4.687  1.00 14.29 ?  76  LYS   A H    1 
ATOM   1780 H  HA   . LYS   A 1 76  ? 33.648 -3.936  -7.293  1.00 14.96 ?  76  LYS   A HA   1 
ATOM   1781 H  HB2  . LYS   A 1 76  ? 33.763 -6.257  -5.661  1.00 16.95 ?  76  LYS   A HB2  1 
ATOM   1782 H  HB3  . LYS   A 1 76  ? 33.562 -6.285  -7.234  1.00 16.95 ?  76  LYS   A HB3  1 
ATOM   1783 H  HG2  . LYS   A 1 76  ? 35.720 -5.664  -7.592  1.00 18.57 ?  76  LYS   A HG2  1 
ATOM   1784 H  HG3  . LYS   A 1 76  ? 35.940 -5.356  -6.048  1.00 18.57 ?  76  LYS   A HG3  1 
ATOM   1785 H  HD2  . LYS   A 1 76  ? 35.798 -7.634  -5.577  1.00 20.10 ?  76  LYS   A HD2  1 
ATOM   1786 H  HD3  . LYS   A 1 76  ? 35.595 -7.937  -7.128  1.00 20.10 ?  76  LYS   A HD3  1 
ATOM   1787 H  HE2  . LYS   A 1 76  ? 37.725 -7.130  -7.571  1.00 23.17 ?  76  LYS   A HE2  1 
ATOM   1788 H  HE3  . LYS   A 1 76  ? 37.928 -6.804  -6.026  1.00 23.17 ?  76  LYS   A HE3  1 
ATOM   1789 H  HZ1  . LYS   A 1 76  ? 38.916 -8.768  -6.562  1.00 24.45 ?  76  LYS   A HZ1  1 
ATOM   1790 H  HZ2  . LYS   A 1 76  ? 37.847 -9.031  -5.619  1.00 24.45 ?  76  LYS   A HZ2  1 
ATOM   1791 H  HZ3  . LYS   A 1 76  ? 37.662 -9.328  -7.025  1.00 24.45 ?  76  LYS   A HZ3  1 
ATOM   1792 N  N    . VAL   A 1 77  ? 31.185 -4.432  -7.372  1.00 11.48 ?  77  VAL   A N    1 
ATOM   1793 C  CA   . VAL   A 1 77  ? 29.779 -4.823  -7.289  1.00 11.27 ?  77  VAL   A CA   1 
ATOM   1794 C  C    . VAL   A 1 77  ? 29.717 -6.277  -6.839  1.00 11.00 ?  77  VAL   A C    1 
ATOM   1795 O  O    . VAL   A 1 77  ? 30.372 -7.149  -7.417  1.00 11.62 ?  77  VAL   A O    1 
ATOM   1796 C  CB   . VAL   A 1 77  ? 29.057 -4.609  -8.628  1.00 12.55 ?  77  VAL   A CB   1 
ATOM   1797 C  CG1  . VAL   A 1 77  ? 27.596 -5.046  -8.512  1.00 13.40 ?  77  VAL   A CG1  1 
ATOM   1798 C  CG2  . VAL   A 1 77  ? 29.139 -3.157  -9.060  1.00 13.75 ?  77  VAL   A CG2  1 
ATOM   1799 H  H    . VAL   A 1 77  ? 31.467 -4.194  -8.151  1.00 13.76 ?  77  VAL   A H    1 
ATOM   1800 H  HA   . VAL   A 1 77  ? 29.343 -4.281  -6.617  1.00 13.51 ?  77  VAL   A HA   1 
ATOM   1801 H  HB   . VAL   A 1 77  ? 29.484 -5.151  -9.310  1.00 15.05 ?  77  VAL   A HB   1 
ATOM   1802 H  HG11 . VAL   A 1 77  ? 27.125 -4.773  -9.311  1.00 16.06 ?  77  VAL   A HG11 1 
ATOM   1803 H  HG12 . VAL   A 1 77  ? 27.562 -6.010  -8.417  1.00 16.06 ?  77  VAL   A HG12 1 
ATOM   1804 H  HG13 . VAL   A 1 77  ? 27.205 -4.621  -7.732  1.00 16.06 ?  77  VAL   A HG13 1 
ATOM   1805 H  HG21 . VAL   A 1 77  ? 28.631 -3.047  -9.880  1.00 16.48 ?  77  VAL   A HG21 1 
ATOM   1806 H  HG22 . VAL   A 1 77  ? 28.764 -2.601  -8.361  1.00 16.48 ?  77  VAL   A HG22 1 
ATOM   1807 H  HG23 . VAL   A 1 77  ? 30.067 -2.923  -9.210  1.00 16.48 ?  77  VAL   A HG23 1 
ATOM   1808 N  N    . GLY   A 1 78  ? 28.932 -6.543  -5.795  1.00 10.79 ?  78  GLY   A N    1 
ATOM   1809 C  CA   . GLY   A 1 78  ? 28.914 -7.833  -5.134  1.00 11.13 ?  78  GLY   A CA   1 
ATOM   1810 C  C    . GLY   A 1 78  ? 29.823 -7.915  -3.929  1.00 10.48 ?  78  GLY   A C    1 
ATOM   1811 O  O    . GLY   A 1 78  ? 29.759 -8.907  -3.188  1.00 10.96 ?  78  GLY   A O    1 
ATOM   1812 H  H    . GLY   A 1 78  ? 28.386 -5.971  -5.451  1.00 12.93 ?  78  GLY   A H    1 
ATOM   1813 H  HA2  . GLY   A 1 78  ? 28.009 -8.028  -4.849  1.00 13.34 ?  78  GLY   A HA2  1 
ATOM   1814 H  HA3  . GLY   A 1 78  ? 29.185 -8.516  -5.769  1.00 13.34 ?  78  GLY   A HA3  1 
ATOM   1815 N  N    . GLY   A 1 79  ? 30.675 -6.908  -3.713  1.00 10.68 ?  79  GLY   A N    1 
ATOM   1816 C  CA   . GLY   A 1 79  ? 31.637 -6.923  -2.635  1.00 10.92 ?  79  GLY   A CA   1 
ATOM   1817 C  C    . GLY   A 1 79  ? 31.193 -6.122  -1.422  1.00 10.32 ?  79  GLY   A C    1 
ATOM   1818 O  O    . GLY   A 1 79  ? 30.077 -5.609  -1.341  1.00 10.75 ?  79  GLY   A O    1 
ATOM   1819 H  H    . GLY   A 1 79  ? 30.710 -6.195  -4.194  1.00 12.80 ?  79  GLY   A H    1 
ATOM   1820 H  HA2  . GLY   A 1 79  ? 31.788 -7.846  -2.358  1.00 13.09 ?  79  GLY   A HA2  1 
ATOM   1821 H  HA3  . GLY   A 1 79  ? 32.479 -6.565  -2.952  1.00 13.09 ?  79  GLY   A HA3  1 
ATOM   1822 N  N    . SER   A 1 80  ? 32.103 -6.033  -0.454  1.00 10.85 ?  80  SER   A N    1 
ATOM   1823 C  CA   . SER   A 1 80  ? 31.786 -5.402  0.818   1.00 10.57 ?  80  SER   A CA   1 
ATOM   1824 C  C    . SER   A 1 80  ? 33.059 -4.953  1.519   1.00 10.31 ?  80  SER   A C    1 
ATOM   1825 O  O    . SER   A 1 80  ? 34.170 -5.386  1.194   1.00 11.98 ?  80  SER   A O    1 
ATOM   1826 C  CB   . SER   A 1 80  ? 31.031 -6.366  1.738   1.00 11.60 ?  80  SER   A CB   1 
ATOM   1827 O  OG   . SER   A 1 80  ? 31.864 -7.414  2.216   1.00 13.32 ?  80  SER   A OG   1 
ATOM   1828 H  H    . SER   A 1 80  ? 32.912 -6.318  -0.515  1.00 13.01 ?  80  SER   A H    1 
ATOM   1829 H  HA   . SER   A 1 80  ? 31.233 -4.619  0.644   1.00 12.67 ?  80  SER   A HA   1 
ATOM   1830 H  HB2  . SER   A 1 80  ? 30.690 -5.863  2.495   1.00 13.90 ?  80  SER   A HB2  1 
ATOM   1831 H  HB3  . SER   A 1 80  ? 30.290 -6.747  1.240   1.00 13.90 ?  80  SER   A HB3  1 
ATOM   1832 H  HG   . SER   A 1 80  ? 32.159 -7.854  1.562   1.00 15.96 ?  80  SER   A HG   1 
ATOM   1833 N  N    . CYS   A 1 81  ? 32.867 -4.105  2.527   1.00 10.17 ?  81  CYS   A N    1 
ATOM   1834 C  CA   . CYS   A 1 81  ? 33.918 -3.817  3.489   1.00 10.39 ?  81  CYS   A CA   1 
ATOM   1835 C  C    . CYS   A 1 81  ? 33.275 -3.576  4.846   1.00 10.06 ?  81  CYS   A C    1 
ATOM   1836 O  O    . CYS   A 1 81  ? 32.110 -3.173  4.933   1.00 11.25 ?  81  CYS   A O    1 
ATOM   1837 C  CB   . CYS   A 1 81  ? 34.790 -2.626  3.062   1.00 11.07 ?  81  CYS   A CB   1 
ATOM   1838 S  SG   . CYS   A 1 81  ? 33.894 -1.049  3.080   1.00 11.27 ?  81  CYS   A SG   1 
ATOM   1839 H  H    . CYS   A 1 81  ? 32.130 -3.685  2.678   1.00 12.18 ?  81  CYS   A H    1 
ATOM   1840 H  HA   . CYS   A 1 81  ? 34.495 -4.592  3.562   1.00 12.45 ?  81  CYS   A HA   1 
ATOM   1841 H  HB2  . CYS   A 1 81  ? 35.547 -2.557  3.670   1.00 13.26 ?  81  CYS   A HB2  1 
ATOM   1842 H  HB3  . CYS   A 1 81  ? 35.117 -2.783  2.157   1.00 13.26 ?  81  CYS   A HB3  1 
ATOM   1843 H  HG   . CYS   A 1 81  ? 34.640 -0.173  2.738   1.00 13.50 ?  81  CYS   A HG   1 
ATOM   1844 N  N    . VAL   A 1 82  ? 34.040 -3.839  5.902   1.00 10.55 ?  82  VAL   A N    1 
ATOM   1845 C  CA   . VAL   A 1 82  ? 33.610 -3.592  7.271   1.00 10.82 ?  82  VAL   A CA   1 
ATOM   1846 C  C    . VAL   A 1 82  ? 34.212 -2.275  7.734   1.00 11.08 ?  82  VAL   A C    1 
ATOM   1847 O  O    . VAL   A 1 82  ? 35.437 -2.104  7.720   1.00 11.86 ?  82  VAL   A O    1 
ATOM   1848 C  CB   . VAL   A 1 82  ? 34.035 -4.728  8.214   1.00 12.51 ?  82  VAL   A CB   1 
ATOM   1849 C  CG1  . VAL   A 1 82  ? 33.588 -4.421  9.637   1.00 14.09 ?  82  VAL   A CG1  1 
ATOM   1850 C  CG2  . VAL   A 1 82  ? 33.480 -6.061  7.744   1.00 13.56 ?  82  VAL   A CG2  1 
ATOM   1851 H  H    . VAL   A 1 82  ? 34.833 -4.181  5.848   1.00 12.65 ?  82  VAL   A H    1 
ATOM   1852 H  HA   . VAL   A 1 82  ? 32.642 -3.514  7.295   1.00 12.97 ?  82  VAL   A HA   1 
ATOM   1853 H  HB   . VAL   A 1 82  ? 35.000 -4.785  8.216   1.00 14.99 ?  82  VAL   A HB   1 
ATOM   1854 H  HG11 . VAL   A 1 82  ? 33.669 -5.225  10.172  1.00 16.90 ?  82  VAL   A HG11 1 
ATOM   1855 H  HG12 . VAL   A 1 82  ? 34.149 -3.721  10.007  1.00 16.90 ?  82  VAL   A HG12 1 
ATOM   1856 H  HG13 . VAL   A 1 82  ? 32.661 -4.127  9.623   1.00 16.90 ?  82  VAL   A HG13 1 
ATOM   1857 H  HG21 . VAL   A 1 82  ? 33.725 -6.746  8.384   1.00 16.26 ?  82  VAL   A HG21 1 
ATOM   1858 H  HG22 . VAL   A 1 82  ? 32.514 -5.997  7.680   1.00 16.26 ?  82  VAL   A HG22 1 
ATOM   1859 H  HG23 . VAL   A 1 82  ? 33.857 -6.269  6.875   1.00 16.26 ?  82  VAL   A HG23 1 
ATOM   1860 N  N    . LEU   A 1 83  ? 33.356 -1.353  8.160   1.00 10.71 ?  83  LEU   A N    1 
ATOM   1861 C  CA   . LEU   A 1 83  ? 33.775 -0.085  8.731   1.00 10.58 ?  83  LEU   A CA   1 
ATOM   1862 C  C    . LEU   A 1 83  ? 33.056 0.099   10.063  1.00 10.76 ?  83  LEU   A C    1 
ATOM   1863 O  O    . LEU   A 1 83  ? 32.334 -0.788  10.532  1.00 11.33 ?  83  LEU   A O    1 
ATOM   1864 C  CB   . LEU   A 1 83  ? 33.532 1.070   7.746   1.00 11.15 ?  83  LEU   A CB   1 
ATOM   1865 C  CG   . LEU   A 1 83  ? 34.437 1.061   6.507   1.00 11.90 ?  83  LEU   A CG   1 
ATOM   1866 C  CD1  . LEU   A 1 83  ? 33.999 2.111   5.504   1.00 12.74 ?  83  LEU   A CD1  1 
ATOM   1867 C  CD2  . LEU   A 1 83  ? 35.901 1.278   6.902   1.00 12.58 ?  83  LEU   A CD2  1 
ATOM   1868 H  H    . LEU   A 1 83  ? 32.500 -1.444  8.123   1.00 12.84 ?  83  LEU   A H    1 
ATOM   1869 H  HA   . LEU   A 1 83  ? 34.720 -0.116  8.913   1.00 12.68 ?  83  LEU   A HA   1 
ATOM   1870 H  HB2  . LEU   A 1 83  ? 32.617 1.035   7.433   1.00 13.36 ?  83  LEU   A HB2  1 
ATOM   1871 H  HB3  . LEU   A 1 83  ? 33.686 1.912   8.205   1.00 13.36 ?  83  LEU   A HB3  1 
ATOM   1872 H  HG   . LEU   A 1 83  ? 34.373 0.195   6.076   1.00 14.26 ?  83  LEU   A HG   1 
ATOM   1873 H  HD11 . LEU   A 1 83  ? 34.591 2.074   4.732   1.00 15.27 ?  83  LEU   A HD11 1 
ATOM   1874 H  HD12 . LEU   A 1 83  ? 33.090 1.923   5.230   1.00 15.27 ?  83  LEU   A HD12 1 
ATOM   1875 H  HD13 . LEU   A 1 83  ? 34.052 2.984   5.917   1.00 15.27 ?  83  LEU   A HD13 1 
ATOM   1876 H  HD21 . LEU   A 1 83  ? 36.432 1.431   6.101   1.00 15.08 ?  83  LEU   A HD21 1 
ATOM   1877 H  HD22 . LEU   A 1 83  ? 35.965 2.049   7.488   1.00 15.08 ?  83  LEU   A HD22 1 
ATOM   1878 H  HD23 . LEU   A 1 83  ? 36.230 0.488   7.363   1.00 15.08 ?  83  LEU   A HD23 1 
ATOM   1879 N  N    . SER   A 1 84  ? 33.274 1.251   10.690  1.00 11.35 ?  84  SER   A N    1 
ATOM   1880 C  CA   . SER   A 1 84  ? 32.632 1.516   11.968  1.00 11.32 ?  84  SER   A CA   1 
ATOM   1881 C  C    . SER   A 1 84  ? 31.114 1.599   11.822  1.00 11.39 ?  84  SER   A C    1 
ATOM   1882 O  O    . SER   A 1 84  ? 30.587 2.067   10.810  1.00 11.54 ?  84  SER   A O    1 
ATOM   1883 C  CB   . SER   A 1 84  ? 33.131 2.843   12.529  1.00 12.31 ?  84  SER   A CB   1 
ATOM   1884 O  OG   . SER   A 1 84  ? 32.502 3.119   13.767  1.00 13.39 ?  84  SER   A OG   1 
ATOM   1885 H  H    . SER   A 1 84  ? 33.780 1.889   10.395  1.00 13.60 ?  84  SER   A H    1 
ATOM   1886 H  HA   . SER   A 1 84  ? 32.856 0.810   12.590  1.00 13.57 ?  84  SER   A HA   1 
ATOM   1887 H  HB2  . SER   A 1 84  ? 34.091 2.794   12.659  1.00 14.76 ?  84  SER   A HB2  1 
ATOM   1888 H  HB3  . SER   A 1 84  ? 32.921 3.553   11.895  1.00 14.76 ?  84  SER   A HB3  1 
ATOM   1889 H  HG   . SER   A 1 84  ? 32.777 3.854   14.069  1.00 16.05 ?  84  SER   A HG   1 
ATOM   1890 N  N    . GLY   A 1 85  ? 30.405 1.183   12.873  1.00 12.30 ?  85  GLY   A N    1 
ATOM   1891 C  CA   . GLY   A 1 85  ? 28.982 1.423   12.974  1.00 12.67 ?  85  GLY   A CA   1 
ATOM   1892 C  C    . GLY   A 1 85  ? 28.615 2.747   13.609  1.00 12.17 ?  85  GLY   A C    1 
ATOM   1893 O  O    . GLY   A 1 85  ? 27.425 3.068   13.722  1.00 13.09 ?  85  GLY   A O    1 
ATOM   1894 H  H    . GLY   A 1 85  ? 30.743 0.763   13.549  1.00 14.75 ?  85  GLY   A H    1 
ATOM   1895 H  HA2  . GLY   A 1 85  ? 28.598 1.395   12.086  1.00 15.19 ?  85  GLY   A HA2  1 
ATOM   1896 H  HA3  . GLY   A 1 85  ? 28.580 0.718   13.500  1.00 15.19 ?  85  GLY   A HA3  1 
ATOM   1897 N  N    . HIS   A 1 86  ? 29.606 3.522   14.040  1.00 11.97 ?  86  HIS   A N    1 
ATOM   1898 C  CA   . HIS   A 1 86  ? 29.390 4.862   14.598  1.00 12.53 ?  86  HIS   A CA   1 
ATOM   1899 C  C    . HIS   A 1 86  ? 28.405 4.746   15.754  1.00 13.18 ?  86  HIS   A C    1 
ATOM   1900 O  O    . HIS   A 1 86  ? 28.592 3.874   16.617  1.00 14.37 ?  86  HIS   A O    1 
ATOM   1901 C  CB   . HIS   A 1 86  ? 29.012 5.832   13.486  1.00 12.78 ?  86  HIS   A CB   1 
ATOM   1902 C  CG   . HIS   A 1 86  ? 30.072 5.929   12.451  1.00 12.61 ?  86  HIS   A CG   1 
ATOM   1903 N  ND1  . HIS   A 1 86  ? 31.164 6.759   12.588  1.00 13.62 ?  86  HIS   A ND1  1 
ATOM   1904 C  CD2  . HIS   A 1 86  ? 30.257 5.239   11.303  1.00 12.23 ?  86  HIS   A CD2  1 
ATOM   1905 C  CE1  . HIS   A 1 86  ? 31.965 6.586   11.553  1.00 13.24 ?  86  HIS   A CE1  1 
ATOM   1906 N  NE2  . HIS   A 1 86  ? 31.443 5.666   10.764  1.00 12.66 ?  86  HIS   A NE2  1 
ATOM   1907 H  H    . HIS   A 1 86  ? 30.431 3.296   14.026  1.00 14.35 ?  86  HIS   A H    1 
ATOM   1908 H  HA   . HIS   A 1 86  ? 30.228 5.178   14.965  1.00 15.02 ?  86  HIS   A HA   1 
ATOM   1909 H  HB2  . HIS   A 1 86  ? 28.194 5.531   13.055  1.00 15.32 ?  86  HIS   A HB2  1 
ATOM   1910 H  HB3  . HIS   A 1 86  ? 28.879 6.721   13.858  1.00 15.32 ?  86  HIS   A HB3  1 
ATOM   1911 H  HD2  . HIS   A 1 86  ? 29.692 4.584   10.947  1.00 14.65 ?  86  HIS   A HD2  1 
ATOM   1912 H  HE1  . HIS   A 1 86  ? 32.760 7.042   11.390  1.00 15.88 ?  86  HIS   A HE1  1 
ATOM   1913 H  HE2  . HIS   A 1 86  ? 31.781 5.391   10.013  1.00 15.17 ?  86  HIS   A HE2  1 
ATOM   1914 N  N    . ASN   A 1 87  ? 27.393 5.599   15.824  1.00 14.09 ?  87  ASN   A N    1 
ATOM   1915 C  CA   . ASN   A 1 87  ? 26.419 5.594   16.897  1.00 15.34 ?  87  ASN   A CA   1 
ATOM   1916 C  C    . ASN   A 1 87  ? 25.291 4.602   16.667  1.00 16.28 ?  87  ASN   A C    1 
ATOM   1917 O  O    . ASN   A 1 87  ? 24.378 4.539   17.492  1.00 18.69 ?  87  ASN   A O    1 
ATOM   1918 C  CB   . ASN   A 1 87  ? 25.832 7.005   17.055  1.00 16.12 ?  87  ASN   A CB   1 
ATOM   1919 C  CG   . ASN   A 1 87  ? 25.320 7.577   15.740  1.00 17.04 ?  87  ASN   A CG   1 
ATOM   1920 O  OD1  . ASN   A 1 87  ? 25.958 7.446   14.701  1.00 17.31 ?  87  ASN   A OD1  1 
ATOM   1921 N  ND2  . ASN   A 1 87  ? 24.163 8.211   15.784  1.00 18.18 ?  87  ASN   A ND2  1 
ATOM   1922 H  H    . ASN   A 1 87  ? 27.246 6.214   15.240  1.00 16.90 ?  87  ASN   A H    1 
ATOM   1923 H  HA   . ASN   A 1 87  ? 26.857 5.353   17.734  1.00 18.40 ?  87  ASN   A HA   1 
ATOM   1924 H  HB2  . ASN   A 1 87  ? 25.089 6.970   17.683  1.00 19.32 ?  87  ASN   A HB2  1 
ATOM   1925 H  HB3  . ASN   A 1 87  ? 26.521 7.596   17.392  1.00 19.32 ?  87  ASN   A HB3  1 
ATOM   1926 H  HD21 . ASN   A 1 87  ? 23.833 8.542   15.065  1.00 21.80 ?  87  ASN   A HD21 1 
ATOM   1927 H  HD22 . ASN   A 1 87  ? 23.746 8.293   16.531  1.00 21.80 ?  87  ASN   A HD22 1 
ATOM   1928 N  N    . LEU   A 1 88  ? 25.336 3.824   15.589  1.00 14.75 ?  88  LEU   A N    1 
ATOM   1929 C  CA   . LEU   A 1 88  ? 24.222 2.966   15.199  1.00 14.63 ?  88  LEU   A CA   1 
ATOM   1930 C  C    . LEU   A 1 88  ? 24.433 1.488   15.499  1.00 14.47 ?  88  LEU   A C    1 
ATOM   1931 O  O    . LEU   A 1 88  ? 23.451 0.761   15.674  1.00 15.62 ?  88  LEU   A O    1 
ATOM   1932 C  CB   . LEU   A 1 88  ? 23.966 3.124   13.700  1.00 15.03 ?  88  LEU   A CB   1 
ATOM   1933 C  CG   . LEU   A 1 88  ? 23.675 4.547   13.225  1.00 16.67 ?  88  LEU   A CG   1 
ATOM   1934 C  CD1  . LEU   A 1 88  ? 23.513 4.568   11.720  1.00 17.17 ?  88  LEU   A CD1  1 
ATOM   1935 C  CD2  . LEU   A 1 88  ? 22.437 5.113   13.910  1.00 18.42 ?  88  LEU   A CD2  1 
ATOM   1936 H  H    . LEU   A 1 88  ? 26.017 3.772   15.070  1.00 17.69 ?  88  LEU   A H    1 
ATOM   1937 H  HA   . LEU   A 1 88  ? 23.427 3.256   15.671  1.00 17.54 ?  88  LEU   A HA   1 
ATOM   1938 H  HB2  . LEU   A 1 88  ? 24.743 2.813   13.216  1.00 18.02 ?  88  LEU   A HB2  1 
ATOM   1939 H  HB3  . LEU   A 1 88  ? 23.196 2.581   13.462  1.00 18.02 ?  88  LEU   A HB3  1 
ATOM   1940 H  HG   . LEU   A 1 88  ? 24.426 5.117   13.451  1.00 19.99 ?  88  LEU   A HG   1 
ATOM   1941 H  HD11 . LEU   A 1 88  ? 23.344 5.480   11.429  1.00 20.59 ?  88  LEU   A HD11 1 
ATOM   1942 H  HD12 . LEU   A 1 88  ? 24.327 4.238   11.309  1.00 20.59 ?  88  LEU   A HD12 1 
ATOM   1943 H  HD13 . LEU   A 1 88  ? 22.765 4.001   11.473  1.00 20.59 ?  88  LEU   A HD13 1 
ATOM   1944 H  HD21 . LEU   A 1 88  ? 22.213 5.963   13.501  1.00 22.09 ?  88  LEU   A HD21 1 
ATOM   1945 H  HD22 . LEU   A 1 88  ? 21.706 4.488   13.801  1.00 22.09 ?  88  LEU   A HD22 1 
ATOM   1946 H  HD23 . LEU   A 1 88  ? 22.631 5.239   14.851  1.00 22.09 ?  88  LEU   A HD23 1 
ATOM   1947 N  N    . ALA   A 1 89  ? 25.680 1.033   15.547  1.00 13.89 ?  89  ALA   A N    1 
ATOM   1948 C  CA   . ALA   A 1 89  ? 26.015 -0.380  15.644  1.00 13.55 ?  89  ALA   A CA   1 
ATOM   1949 C  C    . ALA   A 1 89  ? 27.498 -0.456  15.961  1.00 14.25 ?  89  ALA   A C    1 
ATOM   1950 O  O    . ALA   A 1 89  ? 28.217 0.535   15.838  1.00 14.89 ?  89  ALA   A O    1 
ATOM   1951 C  CB   . ALA   A 1 89  ? 25.736 -1.088  14.322  1.00 13.03 ?  89  ALA   A CB   1 
ATOM   1952 H  H    . ALA   A 1 89  ? 26.370 1.544   15.514  1.00 16.65 ?  89  ALA   A H    1 
ATOM   1953 H  HA   . ALA   A 1 89  ? 25.503 -0.798  16.356  1.00 16.24 ?  89  ALA   A HA   1 
ATOM   1954 H  HB1  . ALA   A 1 89  ? 25.990 -2.023  14.405  1.00 15.62 ?  89  ALA   A HB1  1 
ATOM   1955 H  HB2  . ALA   A 1 89  ? 24.785 -1.027  14.119  1.00 15.62 ?  89  ALA   A HB2  1 
ATOM   1956 H  HB3  . ALA   A 1 89  ? 26.251 -0.668  13.619  1.00 15.62 ?  89  ALA   A HB3  1 
ATOM   1957 N  N    . LYS   A 1 90  ? 27.969 -1.637  16.354  1.00 14.81 ?  90  LYS   A N    1 
ATOM   1958 C  CA   . LYS   A 1 90  ? 29.414 -1.795  16.499  1.00 15.23 ?  90  LYS   A CA   1 
ATOM   1959 C  C    . LYS   A 1 90  ? 30.116 -1.608  15.156  1.00 14.37 ?  90  LYS   A C    1 
ATOM   1960 O  O    . LYS   A 1 90  ? 31.051 -0.799  15.026  1.00 15.61 ?  90  LYS   A O    1 
ATOM   1961 C  CB   . LYS   A 1 90  ? 29.748 -3.155  17.113  1.00 17.52 ?  90  LYS   A CB   1 
ATOM   1962 C  CG   . LYS   A 1 90  ? 31.221 -3.299  17.455  1.00 21.78 ?  90  LYS   A CG   1 
ATOM   1963 C  CD   . LYS   A 1 90  ? 31.476 -4.558  18.263  1.00 26.01 ?  90  LYS   A CD   1 
ATOM   1964 C  CE   . LYS   A 1 90  ? 32.880 -4.580  18.844  1.00 29.49 ?  90  LYS   A CE   1 
ATOM   1965 N  NZ   . LYS   A 1 90  ? 33.915 -4.930  17.834  1.00 31.48 ?  90  LYS   A NZ   1 
ATOM   1966 H  H    . LYS   A 1 90  ? 27.491 -2.324  16.546  1.00 17.76 ?  90  LYS   A H    1 
ATOM   1967 H  HA   . LYS   A 1 90  ? 29.742 -1.111  17.098  1.00 18.26 ?  90  LYS   A HA   1 
ATOM   1968 H  HB2  . LYS   A 1 90  ? 29.236 -3.268  17.932  1.00 21.01 ?  90  LYS   A HB2  1 
ATOM   1969 H  HB3  . LYS   A 1 90  ? 29.516 -3.856  16.483  1.00 21.01 ?  90  LYS   A HB3  1 
ATOM   1970 H  HG2  . LYS   A 1 90  ? 31.738 -3.351  16.636  1.00 26.12 ?  90  LYS   A HG2  1 
ATOM   1971 H  HG3  . LYS   A 1 90  ? 31.504 -2.534  17.983  1.00 26.12 ?  90  LYS   A HG3  1 
ATOM   1972 H  HD2  . LYS   A 1 90  ? 30.843 -4.604  18.998  1.00 31.20 ?  90  LYS   A HD2  1 
ATOM   1973 H  HD3  . LYS   A 1 90  ? 31.375 -5.335  17.688  1.00 31.20 ?  90  LYS   A HD3  1 
ATOM   1974 H  HE2  . LYS   A 1 90  ? 33.091 -3.701  19.196  1.00 35.37 ?  90  LYS   A HE2  1 
ATOM   1975 H  HE3  . LYS   A 1 90  ? 32.920 -5.239  19.555  1.00 35.37 ?  90  LYS   A HE3  1 
ATOM   1976 H  HZ1  . LYS   A 1 90  ? 34.717 -4.972  18.220  1.00 37.76 ?  90  LYS   A HZ1  1 
ATOM   1977 H  HZ2  . LYS   A 1 90  ? 33.729 -5.721  17.470  1.00 37.76 ?  90  LYS   A HZ2  1 
ATOM   1978 H  HZ3  . LYS   A 1 90  ? 33.935 -4.314  17.193  1.00 37.76 ?  90  LYS   A HZ3  1 
ATOM   1979 N  N    . HIS   A 1 91  ? 29.645 -2.327  14.135  1.00 12.78 ?  91  HIS   A N    1 
ATOM   1980 C  CA   . HIS   A 1 91  ? 30.223 -2.317  12.805  1.00 12.13 ?  91  HIS   A CA   1 
ATOM   1981 C  C    . HIS   A 1 91  ? 29.141 -2.042  11.779  1.00 10.99 ?  91  HIS   A C    1 
ATOM   1982 O  O    . HIS   A 1 91  ? 27.975 -2.399  11.970  1.00 11.81 ?  91  HIS   A O    1 
ATOM   1983 C  CB   . HIS   A 1 91  ? 30.815 -3.690  12.451  1.00 14.68 ?  91  HIS   A CB   1 
ATOM   1984 C  CG   . HIS   A 1 91  ? 31.779 -4.217  13.464  1.00 18.80 ?  91  HIS   A CG   1 
ATOM   1985 N  ND1  . HIS   A 1 91  ? 33.066 -3.740  13.582  1.00 20.87 ?  91  HIS   A ND1  1 
ATOM   1986 C  CD2  . HIS   A 1 91  ? 31.653 -5.192  14.396  1.00 20.76 ?  91  HIS   A CD2  1 
ATOM   1987 C  CE1  . HIS   A 1 91  ? 33.690 -4.395  14.546  1.00 21.68 ?  91  HIS   A CE1  1 
ATOM   1988 N  NE2  . HIS   A 1 91  ? 32.855 -5.283  15.056  1.00 22.09 ?  91  HIS   A NE2  1 
ATOM   1989 H  H    . HIS   A 1 91  ? 28.959 -2.860  14.201  1.00 15.32 ?  91  HIS   A H    1 
ATOM   1990 H  HA   . HIS   A 1 91  ? 30.910 -1.643  12.742  1.00 14.54 ?  91  HIS   A HA   1 
ATOM   1991 H  HB2  . HIS   A 1 91  ? 30.093 -4.334  12.369  1.00 17.60 ?  91  HIS   A HB2  1 
ATOM   1992 H  HB3  . HIS   A 1 91  ? 31.284 -3.617  11.604  1.00 17.60 ?  91  HIS   A HB3  1 
ATOM   1993 H  HD1  . HIS   A 1 91  ? 33.412 -3.114  13.099  1.00 25.03 ?  91  HIS   A HD1  1 
ATOM   1994 H  HD2  . HIS   A 1 91  ? 30.898 -5.703  14.560  1.00 24.90 ?  91  HIS   A HD2  1 
ATOM   1995 H  HE1  . HIS   A 1 91  ? 34.570 -4.249  14.818  1.00 26.00 ?  91  HIS   A HE1  1 
ATOM   1996 N  N    . CYS   A 1 92  ? 29.552 -1.446  10.666  1.00 10.79 ?  92  CYS   A N    1 
ATOM   1997 C  CA   . CYS   A 1 92  ? 28.723 -1.365  9.471   1.00 10.58 ?  92  CYS   A CA   1 
ATOM   1998 C  C    . CYS   A 1 92  ? 29.372 -2.193  8.369   1.00 10.29 ?  92  CYS   A C    1 
ATOM   1999 O  O    . CYS   A 1 92  ? 30.530 -1.948  8.003   1.00 10.87 ?  92  CYS   A O    1 
ATOM   2000 C  CB   . CYS   A 1 92  ? 28.524 0.078   9.003   1.00 10.87 ?  92  CYS   A CB   1 
ATOM   2001 S  SG   . CYS   A 1 92  ? 27.501 0.177   7.496   1.00 10.63 ?  92  CYS   A SG   1 
ATOM   2002 H  H    . CYS   A 1 92  ? 30.325 -1.078  10.573  1.00 12.93 ?  92  CYS   A H    1 
ATOM   2003 H  HA   . CYS   A 1 92  ? 27.852 -1.743  9.659   1.00 12.68 ?  92  CYS   A HA   1 
ATOM   2004 H  HB2  . CYS   A 1 92  ? 28.075 0.583   9.702   1.00 13.03 ?  92  CYS   A HB2  1 
ATOM   2005 H  HB3  . CYS   A 1 92  ? 29.385 0.476   8.807   1.00 13.03 ?  92  CYS   A HB3  1 
ATOM   2006 H  HG   . CYS   A 1 92  ? 27.364 1.329   7.191   1.00 12.74 ?  92  CYS   A HG   1 
ATOM   2007 N  N    . LEU   A 1 93  ? 28.633 -3.181  7.865   1.00 9.88  ?  93  LEU   A N    1 
ATOM   2008 C  CA   . LEU   A 1 93  ? 29.038 -3.942  6.689   1.00 9.48  ?  93  LEU   A CA   1 
ATOM   2009 C  C    . LEU   A 1 93  ? 28.442 -3.255  5.464   1.00 9.15  ?  93  LEU   A C    1 
ATOM   2010 O  O    . LEU   A 1 93  ? 27.228 -3.311  5.235   1.00 9.39  ?  93  LEU   A O    1 
ATOM   2011 C  CB   . LEU   A 1 93  ? 28.554 -5.386  6.799   1.00 10.11 ?  93  LEU   A CB   1 
ATOM   2012 C  CG   . LEU   A 1 93  ? 28.940 -6.289  5.631   1.00 10.42 ?  93  LEU   A CG   1 
ATOM   2013 C  CD1  . LEU   A 1 93  ? 30.441 -6.554  5.619   1.00 11.55 ?  93  LEU   A CD1  1 
ATOM   2014 C  CD2  . LEU   A 1 93  ? 28.162 -7.610  5.675   1.00 11.17 ?  93  LEU   A CD2  1 
ATOM   2015 H  H    . LEU   A 1 93  ? 27.879 -3.428  8.197   1.00 11.84 ?  93  LEU   A H    1 
ATOM   2016 H  HA   . LEU   A 1 93  ? 30.003 -3.937  6.617   1.00 11.36 ?  93  LEU   A HA   1 
ATOM   2017 H  HB2  . LEU   A 1 93  ? 28.929 -5.774  7.609   1.00 12.11 ?  93  LEU   A HB2  1 
ATOM   2018 H  HB3  . LEU   A 1 93  ? 27.588 -5.386  6.860   1.00 12.11 ?  93  LEU   A HB3  1 
ATOM   2019 H  HG   . LEU   A 1 93  ? 28.724 -5.848  4.803   1.00 12.49 ?  93  LEU   A HG   1 
ATOM   2020 H  HD11 . LEU   A 1 93  ? 30.655 -7.174  4.903   1.00 13.84 ?  93  LEU   A HD11 1 
ATOM   2021 H  HD12 . LEU   A 1 93  ? 30.916 -5.720  5.487   1.00 13.84 ?  93  LEU   A HD12 1 
ATOM   2022 H  HD13 . LEU   A 1 93  ? 30.705 -6.948  6.475   1.00 13.84 ?  93  LEU   A HD13 1 
ATOM   2023 H  HD21 . LEU   A 1 93  ? 28.434 -8.164  4.920   1.00 13.39 ?  93  LEU   A HD21 1 
ATOM   2024 H  HD22 . LEU   A 1 93  ? 28.357 -8.072  6.505   1.00 13.39 ?  93  LEU   A HD22 1 
ATOM   2025 H  HD23 . LEU   A 1 93  ? 27.214 -7.419  5.615   1.00 13.39 ?  93  LEU   A HD23 1 
ATOM   2026 N  N    . HIS   A 1 94  ? 29.297 -2.566  4.705   1.00 9.07  ?  94  HIS   A N    1 
ATOM   2027 C  CA   . HIS   A 1 94  ? 28.874 -1.892  3.482   1.00 9.09  ?  94  HIS   A CA   1 
ATOM   2028 C  C    . HIS   A 1 94  ? 28.888 -2.920  2.366   1.00 9.20  ?  94  HIS   A C    1 
ATOM   2029 O  O    . HIS   A 1 94  ? 29.953 -3.441  2.029   1.00 10.68 ?  94  HIS   A O    1 
ATOM   2030 C  CB   . HIS   A 1 94  ? 29.843 -0.755  3.155   1.00 9.40  ?  94  HIS   A CB   1 
ATOM   2031 C  CG   . HIS   A 1 94  ? 29.827 0.343   4.164   1.00 9.24  ?  94  HIS   A CG   1 
ATOM   2032 N  ND1  . HIS   A 1 94  ? 28.955 1.410   4.097   1.00 9.50  ?  94  HIS   A ND1  1 
ATOM   2033 C  CD2  . HIS   A 1 94  ? 30.559 0.511   5.288   1.00 10.18 ?  94  HIS   A CD2  1 
ATOM   2034 C  CE1  . HIS   A 1 94  ? 29.161 2.187   5.144   1.00 9.60  ?  94  HIS   A CE1  1 
ATOM   2035 N  NE2  . HIS   A 1 94  ? 30.136 1.671   5.874   1.00 10.05 ?  94  HIS   A NE2  1 
ATOM   2036 H  H    . HIS   A 1 94  ? 30.134 -2.468  4.881   1.00 10.87 ?  94  HIS   A H    1 
ATOM   2037 H  HA   . HIS   A 1 94  ? 27.975 -1.533  3.583   1.00 10.89 ?  94  HIS   A HA   1 
ATOM   2038 H  HB2  . HIS   A 1 94  ? 30.739 -1.111  3.116   1.00 11.27 ?  94  HIS   A HB2  1 
ATOM   2039 H  HB3  . HIS   A 1 94  ? 29.596 -0.373  2.297   1.00 11.27 ?  94  HIS   A HB3  1 
ATOM   2040 H  HD2  . HIS   A 1 94  ? 31.230 -0.045  5.599   1.00 12.20 ?  94  HIS   A HD2  1 
ATOM   2041 H  HE1  . HIS   A 1 94  ? 28.698 2.977   5.325   1.00 11.50 ?  94  HIS   A HE1  1 
ATOM   2042 H  HE2  . HIS   A 1 94  ? 30.440 2.015   6.599   1.00 12.05 ?  94  HIS   A HE2  1 
ATOM   2043 N  N    . VAL   A 1 95  ? 27.718 -3.245  1.819   1.00 8.81  ?  95  VAL   A N    1 
ATOM   2044 C  CA   . VAL   A 1 95  ? 27.577 -4.283  0.799   1.00 9.15  ?  95  VAL   A CA   1 
ATOM   2045 C  C    . VAL   A 1 95  ? 27.031 -3.656  -0.469  1.00 8.66  ?  95  VAL   A C    1 
ATOM   2046 O  O    . VAL   A 1 95  ? 26.024 -2.939  -0.421  1.00 9.42  ?  95  VAL   A O    1 
ATOM   2047 C  CB   . VAL   A 1 95  ? 26.660 -5.430  1.254   1.00 9.75  ?  95  VAL   A CB   1 
ATOM   2048 C  CG1  . VAL   A 1 95  ? 26.565 -6.469  0.153   1.00 10.23 ?  95  VAL   A CG1  1 
ATOM   2049 C  CG2  . VAL   A 1 95  ? 27.160 -6.041  2.544   1.00 9.97  ?  95  VAL   A CG2  1 
ATOM   2050 H  H    . VAL   A 1 95  ? 26.968 -2.874  2.033   1.00 10.55 ?  95  VAL   A H    1 
ATOM   2051 H  HA   . VAL   A 1 95  ? 28.448 -4.654  0.603   1.00 10.96 ?  95  VAL   A HA   1 
ATOM   2052 H  HB   . VAL   A 1 95  ? 25.770 -5.084  1.416   1.00 11.69 ?  95  VAL   A HB   1 
ATOM   2053 H  HG11 . VAL   A 1 95  ? 26.200 -7.291  0.519   1.00 12.26 ?  95  VAL   A HG11 1 
ATOM   2054 H  HG12 . VAL   A 1 95  ? 25.987 -6.140  -0.553  1.00 12.26 ?  95  VAL   A HG12 1 
ATOM   2055 H  HG13 . VAL   A 1 95  ? 27.455 -6.640  -0.202  1.00 12.26 ?  95  VAL   A HG13 1 
ATOM   2056 H  HG21 . VAL   A 1 95  ? 26.610 -6.808  2.767   1.00 11.95 ?  95  VAL   A HG21 1 
ATOM   2057 H  HG22 . VAL   A 1 95  ? 28.083 -6.322  2.423   1.00 11.95 ?  95  VAL   A HG22 1 
ATOM   2058 H  HG23 . VAL   A 1 95  ? 27.107 -5.378  3.249   1.00 11.95 ?  95  VAL   A HG23 1 
ATOM   2059 N  N    . VAL   A 1 96  ? 27.663 -3.945  -1.602  1.00 8.66  ?  96  VAL   A N    1 
ATOM   2060 C  CA   . VAL   A 1 96  ? 27.250 -3.398  -2.886  1.00 9.53  ?  96  VAL   A CA   1 
ATOM   2061 C  C    . VAL   A 1 96  ? 26.449 -4.447  -3.650  1.00 9.77  ?  96  VAL   A C    1 
ATOM   2062 O  O    . VAL   A 1 96  ? 27.009 -5.400  -4.200  1.00 10.72 ?  96  VAL   A O    1 
ATOM   2063 C  CB   . VAL   A 1 96  ? 28.438 -2.918  -3.719  1.00 9.93  ?  96  VAL   A CB   1 
ATOM   2064 C  CG1  . VAL   A 1 96  ? 27.932 -2.292  -4.996  1.00 10.14 ?  96  VAL   A CG1  1 
ATOM   2065 C  CG2  . VAL   A 1 96  ? 29.295 -1.933  -2.934  1.00 10.80 ?  96  VAL   A CG2  1 
ATOM   2066 H  H    . VAL   A 1 96  ? 28.359 -4.458  -1.647  1.00 10.38 ?  96  VAL   A H    1 
ATOM   2067 H  HA   . VAL   A 1 96  ? 26.675 -2.637  -2.728  1.00 11.42 ?  96  VAL   A HA   1 
ATOM   2068 H  HB   . VAL   A 1 96  ? 28.992 -3.677  -3.953  1.00 11.91 ?  96  VAL   A HB   1 
ATOM   2069 H  HG11 . VAL   A 1 96  ? 28.666 -1.808  -5.414  1.00 12.16 ?  96  VAL   A HG11 1 
ATOM   2070 H  HG12 . VAL   A 1 96  ? 27.619 -2.987  -5.589  1.00 12.16 ?  96  VAL   A HG12 1 
ATOM   2071 H  HG13 . VAL   A 1 96  ? 27.215 -1.677  -4.784  1.00 12.16 ?  96  VAL   A HG13 1 
ATOM   2072 H  HG21 . VAL   A 1 96  ? 29.999 -1.594  -3.506  1.00 12.94 ?  96  VAL   A HG21 1 
ATOM   2073 H  HG22 . VAL   A 1 96  ? 28.736 -1.198  -2.628  1.00 12.94 ?  96  VAL   A HG22 1 
ATOM   2074 H  HG23 . VAL   A 1 96  ? 29.682 -2.388  -2.167  1.00 12.94 ?  96  VAL   A HG23 1 
ATOM   2075 N  N    A GLY   A 1 97  ? 25.131 -4.291  -3.667  0.62 10.01 ?  97  GLY   A N    1 
ATOM   2076 N  N    B GLY   A 1 97  ? 25.134 -4.266  -3.727  0.38 9.69  ?  97  GLY   A N    1 
ATOM   2077 C  CA   A GLY   A 1 97  ? 24.306 -5.041  -4.575  0.62 10.48 ?  97  GLY   A CA   1 
ATOM   2078 C  CA   B GLY   A 1 97  ? 24.327 -5.058  -4.622  0.38 9.91  ?  97  GLY   A CA   1 
ATOM   2079 C  C    A GLY   A 1 97  ? 24.304 -4.366  -5.930  0.62 10.39 ?  97  GLY   A C    1 
ATOM   2080 C  C    B GLY   A 1 97  ? 24.304 -4.452  -6.013  0.38 10.21 ?  97  GLY   A C    1 
ATOM   2081 O  O    A GLY   A 1 97  ? 24.630 -3.179  -6.052  0.62 11.08 ?  97  GLY   A O    1 
ATOM   2082 O  O    B GLY   A 1 97  ? 24.479 -3.240  -6.184  0.38 10.76 ?  97  GLY   A O    1 
ATOM   2083 H  H    A GLY   A 1 97  ? 24.696 -3.749  -3.153  0.62 11.99 ?  97  GLY   A H    1 
ATOM   2084 H  H    B GLY   A 1 97  ? 24.690 -3.691  -3.261  0.38 11.62 ?  97  GLY   A H    1 
ATOM   2085 H  HA2  A GLY   A 1 97  ? 24.658 -5.940  -4.662  0.62 12.56 ?  97  GLY   A HA2  1 
ATOM   2086 H  HA2  B GLY   A 1 97  ? 24.688 -5.960  -4.660  0.38 11.87 ?  97  GLY   A HA2  1 
ATOM   2087 H  HA3  A GLY   A 1 97  ? 23.398 -5.092  -4.229  0.62 12.56 ?  97  GLY   A HA3  1 
ATOM   2088 H  HA3  B GLY   A 1 97  ? 23.418 -5.105  -4.287  0.38 11.87 ?  97  GLY   A HA3  1 
ATOM   2089 N  N    A PRO   A 1 98  ? 23.943 -5.102  -6.976  0.62 9.86  ?  98  PRO   A N    1 
ATOM   2090 N  N    B PRO   A 1 98  ? 24.083 -5.276  -7.036  0.38 10.65 ?  98  PRO   A N    1 
ATOM   2091 C  CA   A PRO   A 1 98  ? 23.831 -4.477  -8.296  0.62 10.90 ?  98  PRO   A CA   1 
ATOM   2092 C  CA   B PRO   A 1 98  ? 24.013 -4.738  -8.400  0.38 11.64 ?  98  PRO   A CA   1 
ATOM   2093 C  C    A PRO   A 1 98  ? 22.722 -3.435  -8.327  0.62 10.58 ?  98  PRO   A C    1 
ATOM   2094 C  C    B PRO   A 1 98  ? 22.865 -3.748  -8.549  0.38 12.02 ?  98  PRO   A C    1 
ATOM   2095 O  O    A PRO   A 1 98  ? 21.649 -3.617  -7.749  0.62 10.52 ?  98  PRO   A O    1 
ATOM   2096 O  O    B PRO   A 1 98  ? 21.790 -3.917  -7.970  0.38 12.65 ?  98  PRO   A O    1 
ATOM   2097 C  CB   A PRO   A 1 98  ? 23.524 -5.659  -9.224  0.62 11.02 ?  98  PRO   A CB   1 
ATOM   2098 C  CB   B PRO   A 1 98  ? 23.800 -5.987  -9.263  0.38 11.27 ?  98  PRO   A CB   1 
ATOM   2099 C  CG   A PRO   A 1 98  ? 22.913 -6.700  -8.332  0.62 10.82 ?  98  PRO   A CG   1 
ATOM   2100 C  CG   B PRO   A 1 98  ? 23.186 -6.989  -8.334  0.38 11.68 ?  98  PRO   A CG   1 
ATOM   2101 C  CD   A PRO   A 1 98  ? 23.616 -6.539  -7.005  0.62 10.17 ?  98  PRO   A CD   1 
ATOM   2102 C  CD   B PRO   A 1 98  ? 23.838 -6.729  -7.003  0.38 10.94 ?  98  PRO   A CD   1 
ATOM   2103 H  HA   A PRO   A 1 98  ? 24.669 -4.070  -8.544  0.62 13.06 ?  98  PRO   A HA   1 
ATOM   2104 H  HA   B PRO   A 1 98  ? 24.850 -4.311  -8.639  0.38 13.95 ?  98  PRO   A HA   1 
ATOM   2105 H  HB2  A PRO   A 1 98  ? 22.893 -5.384  -9.907  0.62 13.21 ?  98  PRO   A HB2  1 
ATOM   2106 H  HB2  B PRO   A 1 98  ? 23.198 -5.780  -9.994  0.38 13.50 ?  98  PRO   A HB2  1 
ATOM   2107 H  HB3  A PRO   A 1 98  ? 24.345 -5.985  -9.620  0.62 13.21 ?  98  PRO   A HB3  1 
ATOM   2108 H  HB3  B PRO   A 1 98  ? 24.653 -6.307  -9.596  0.38 13.50 ?  98  PRO   A HB3  1 
ATOM   2109 H  HG2  A PRO   A 1 98  ? 21.964 -6.537  -8.240  0.62 12.97 ?  98  PRO   A HG2  1 
ATOM   2110 H  HG2  B PRO   A 1 98  ? 22.228 -6.842  -8.282  0.38 13.99 ?  98  PRO   A HG2  1 
ATOM   2111 H  HG3  A PRO   A 1 98  ? 23.079 -7.582  -8.701  0.62 12.97 ?  98  PRO   A HG3  1 
ATOM   2112 H  HG3  B PRO   A 1 98  ? 23.379 -7.887  -8.647  0.38 13.99 ?  98  PRO   A HG3  1 
ATOM   2113 H  HD2  A PRO   A 1 98  ? 23.017 -6.778  -6.273  0.62 12.19 ?  98  PRO   A HD2  1 
ATOM   2114 H  HD2  B PRO   A 1 98  ? 23.234 -6.962  -6.278  0.38 13.12 ?  98  PRO   A HD2  1 
ATOM   2115 H  HD3  A PRO   A 1 98  ? 24.430 -7.067  -6.979  0.62 12.19 ?  98  PRO   A HD3  1 
ATOM   2116 H  HD3  B PRO   A 1 98  ? 24.677 -7.218  -6.934  0.38 13.12 ?  98  PRO   A HD3  1 
ATOM   2117 N  N    A ASN   A 1 99  ? 23.003 -2.322  -8.996  0.62 11.63 ?  99  ASN   A N    1 
ATOM   2118 N  N    B ASN   A 1 99  ? 23.105 -2.702  -9.334  0.38 11.93 ?  99  ASN   A N    1 
ATOM   2119 C  CA   A ASN   A 1 99  ? 22.027 -1.263  -9.227  0.62 12.87 ?  99  ASN   A CA   1 
ATOM   2120 C  CA   B ASN   A 1 99  ? 22.103 -1.679  -9.611  0.38 12.98 ?  99  ASN   A CA   1 
ATOM   2121 C  C    A ASN   A 1 99  ? 21.489 -1.425  -10.645 0.62 13.88 ?  99  ASN   A C    1 
ATOM   2122 C  C    B ASN   A 1 99  ? 21.444 -1.995  -10.947 0.38 14.24 ?  99  ASN   A C    1 
ATOM   2123 O  O    A ASN   A 1 99  ? 22.188 -1.137  -11.625 0.62 14.87 ?  99  ASN   A O    1 
ATOM   2124 O  O    B ASN   A 1 99  ? 22.070 -1.863  -12.005 0.38 14.17 ?  99  ASN   A O    1 
ATOM   2125 C  CB   A ASN   A 1 99  ? 22.663 0.111   -9.028  0.62 13.23 ?  99  ASN   A CB   1 
ATOM   2126 C  CB   B ASN   A 1 99  ? 22.742 -0.296  -9.634  0.38 13.54 ?  99  ASN   A CB   1 
ATOM   2127 C  CG   A ASN   A 1 99  ? 21.640 1.237   -9.022  0.62 13.06 ?  99  ASN   A CG   1 
ATOM   2128 C  CG   B ASN   A 1 99  ? 21.731 0.809   -9.862  0.38 14.42 ?  99  ASN   A CG   1 
ATOM   2129 O  OD1  A ASN   A 1 99  ? 20.646 1.189   -9.750  0.62 13.21 ?  99  ASN   A OD1  1 
ATOM   2130 O  OD1  B ASN   A 1 99  ? 20.849 0.689   -10.706 0.38 14.85 ?  99  ASN   A OD1  1 
ATOM   2131 N  ND2  A ASN   A 1 99  ? 21.887 2.264   -8.210  0.62 12.92 ?  99  ASN   A ND2  1 
ATOM   2132 N  ND2  B ASN   A 1 99  ? 21.846 1.887   -9.097  0.38 15.10 ?  99  ASN   A ND2  1 
ATOM   2133 H  H    A ASN   A 1 99  ? 23.780 -2.149  -9.313  0.62 13.94 ?  99  ASN   A H    1 
ATOM   2134 H  H    B ASN   A 1 99  ? 23.862 -2.557  -9.715  0.38 14.30 ?  99  ASN   A H    1 
ATOM   2135 H  HA   A ASN   A 1 99  ? 21.289 -1.361  -8.595  0.62 15.43 ?  99  ASN   A HA   1 
ATOM   2136 H  HA   B ASN   A 1 99  ? 21.421 -1.701  -8.919  0.38 15.56 ?  99  ASN   A HA   1 
ATOM   2137 H  HB2  A ASN   A 1 99  ? 23.135 0.124   -8.183  0.62 15.86 ?  99  ASN   A HB2  1 
ATOM   2138 H  HB2  B ASN   A 1 99  ? 23.166 -0.145  -8.780  0.38 16.24 ?  99  ASN   A HB2  1 
ATOM   2139 H  HB3  A ASN   A 1 99  ? 23.282 0.271   -9.758  0.62 15.86 ?  99  ASN   A HB3  1 
ATOM   2140 H  HB3  B ASN   A 1 99  ? 23.392 -0.264  -10.350 0.38 16.24 ?  99  ASN   A HB3  1 
ATOM   2141 H  HD21 A ASN   A 1 99  ? 21.337 2.923   -8.171  0.62 15.48 ?  99  ASN   A HD21 1 
ATOM   2142 H  HD21 B ASN   A 1 99  ? 21.293 2.539   -9.184  0.38 18.10 ?  99  ASN   A HD21 1 
ATOM   2143 H  HD22 A ASN   A 1 99  ? 22.596 2.265   -7.723  0.62 15.48 ?  99  ASN   A HD22 1 
ATOM   2144 H  HD22 B ASN   A 1 99  ? 22.471 1.928   -8.510  0.38 18.10 ?  99  ASN   A HD22 1 
ATOM   2145 N  N    A VAL   A 1 100 ? 20.248 -1.906  -10.746 0.62 15.26 ?  100 VAL   A N    1 
ATOM   2146 N  N    B VAL   A 1 100 ? 20.172 -2.397  -10.883 0.38 16.17 ?  100 VAL   A N    1 
ATOM   2147 C  CA   A VAL   A 1 100 ? 19.635 -2.138  -12.049 0.62 17.31 ?  100 VAL   A CA   1 
ATOM   2148 C  CA   B VAL   A 1 100 ? 19.419 -2.766  -12.078 0.38 17.75 ?  100 VAL   A CA   1 
ATOM   2149 C  C    A VAL   A 1 100 ? 19.490 -0.832  -12.813 0.62 17.67 ?  100 VAL   A C    1 
ATOM   2150 C  C    B VAL   A 1 100 ? 19.410 -1.623  -13.081 0.38 17.59 ?  100 VAL   A C    1 
ATOM   2151 O  O    A VAL   A 1 100 ? 19.547 -0.817  -14.048 0.62 18.06 ?  100 VAL   A O    1 
ATOM   2152 O  O    B VAL   A 1 100 ? 19.525 -1.838  -14.295 0.38 17.49 ?  100 VAL   A O    1 
ATOM   2153 C  CB   A VAL   A 1 100 ? 18.291 -2.878  -11.886 0.62 19.32 ?  100 VAL   A CB   1 
ATOM   2154 C  CB   B VAL   A 1 100 ? 17.992 -3.193  -11.676 0.38 19.58 ?  100 VAL   A CB   1 
ATOM   2155 C  CG1  A VAL   A 1 100 ? 17.630 -3.119  -13.239 0.62 20.21 ?  100 VAL   A CG1  1 
ATOM   2156 C  CG1  B VAL   A 1 100 ? 16.984 -2.832  -12.761 0.38 20.23 ?  100 VAL   A CG1  1 
ATOM   2157 C  CG2  A VAL   A 1 100 ? 18.508 -4.196  -11.160 0.62 19.75 ?  100 VAL   A CG2  1 
ATOM   2158 C  CG2  B VAL   A 1 100 ? 17.953 -4.680  -11.376 0.38 20.46 ?  100 VAL   A CG2  1 
ATOM   2159 H  H    A VAL   A 1 100 ? 19.740 -2.109  -10.074 0.62 18.30 ?  100 VAL   A H    1 
ATOM   2160 H  H    B VAL   A 1 100 ? 19.720 -2.456  -10.154 0.38 19.38 ?  100 VAL   A H    1 
ATOM   2161 H  HA   A VAL   A 1 100 ? 20.218 -2.711  -12.566 0.62 20.76 ?  100 VAL   A HA   1 
ATOM   2162 H  HA   B VAL   A 1 100 ? 19.844 -3.524  -12.501 0.38 21.28 ?  100 VAL   A HA   1 
ATOM   2163 H  HB   A VAL   A 1 100 ? 17.690 -2.337  -11.352 0.62 23.17 ?  100 VAL   A HB   1 
ATOM   2164 H  HB   B VAL   A 1 100 ? 17.738 -2.720  -10.867 0.38 23.48 ?  100 VAL   A HB   1 
ATOM   2165 H  HG11 A VAL   A 1 100 ? 16.872 -3.714  -13.119 0.62 24.23 ?  100 VAL   A HG11 1 
ATOM   2166 H  HG11 B VAL   A 1 100 ? 16.149 -3.285  -12.567 0.38 24.26 ?  100 VAL   A HG11 1 
ATOM   2167 H  HG12 A VAL   A 1 100 ? 17.328 -2.272  -13.602 0.62 24.23 ?  100 VAL   A HG12 1 
ATOM   2168 H  HG12 B VAL   A 1 100 ? 16.838 -1.872  -12.759 0.38 24.26 ?  100 VAL   A HG12 1 
ATOM   2169 H  HG13 A VAL   A 1 100 ? 18.275 -3.527  -13.839 0.62 24.23 ?  100 VAL   A HG13 1 
ATOM   2170 H  HG13 B VAL   A 1 100 ? 17.320 -3.123  -13.621 0.38 24.26 ?  100 VAL   A HG13 1 
ATOM   2171 H  HG21 A VAL   A 1 100 ? 17.677 -4.697  -11.157 0.62 23.69 ?  100 VAL   A HG21 1 
ATOM   2172 H  HG21 B VAL   A 1 100 ? 17.055 -4.922  -11.101 0.38 24.54 ?  100 VAL   A HG21 1 
ATOM   2173 H  HG22 A VAL   A 1 100 ? 19.196 -4.701  -11.622 0.62 23.69 ?  100 VAL   A HG22 1 
ATOM   2174 H  HG22 B VAL   A 1 100 ? 18.199 -5.169  -12.176 0.38 24.54 ?  100 VAL   A HG22 1 
ATOM   2175 H  HG23 A VAL   A 1 100 ? 18.787 -4.014  -10.249 0.62 23.69 ?  100 VAL   A HG23 1 
ATOM   2176 H  HG23 B VAL   A 1 100 ? 18.581 -4.873  -10.663 0.38 24.54 ?  100 VAL   A HG23 1 
ATOM   2177 N  N    A ASN   A 1 101 ? 19.307 0.283   -12.106 0.62 18.74 ?  101 ASN   A N    1 
ATOM   2178 N  N    B ASN   A 1 101 ? 19.261 -0.391  -12.595 0.38 17.78 ?  101 ASN   A N    1 
ATOM   2179 C  CA   A ASN   A 1 101 ? 19.221 1.569   -12.785 0.62 19.91 ?  101 ASN   A CA   1 
ATOM   2180 C  CA   B ASN   A 1 101 ? 19.174 0.755   -13.491 0.38 18.36 ?  101 ASN   A CA   1 
ATOM   2181 C  C    A ASN   A 1 101 ? 20.565 2.030   -13.348 0.62 22.15 ?  101 ASN   A C    1 
ATOM   2182 C  C    B ASN   A 1 101 ? 20.497 1.034   -14.190 0.38 19.12 ?  101 ASN   A C    1 
ATOM   2183 O  O    A ASN   A 1 101 ? 20.606 3.074   -14.008 0.62 23.45 ?  101 ASN   A O    1 
ATOM   2184 O  O    B ASN   A 1 101 ? 20.503 1.662   -15.255 0.38 19.46 ?  101 ASN   A O    1 
ATOM   2185 C  CB   A ASN   A 1 101 ? 18.592 2.606   -11.851 0.62 19.23 ?  101 ASN   A CB   1 
ATOM   2186 C  CB   B ASN   A 1 101 ? 18.735 1.992   -12.709 0.38 18.17 ?  101 ASN   A CB   1 
ATOM   2187 C  CG   A ASN   A 1 101 ? 17.207 2.185   -11.371 0.62 18.92 ?  101 ASN   A CG   1 
ATOM   2188 C  CG   B ASN   A 1 101 ? 17.523 1.730   -11.830 0.38 18.60 ?  101 ASN   A CG   1 
ATOM   2189 O  OD1  A ASN   A 1 101 ? 16.390 1.699   -12.155 0.62 19.28 ?  101 ASN   A OD1  1 
ATOM   2190 O  OD1  B ASN   A 1 101 ? 16.538 1.133   -12.266 0.38 19.08 ?  101 ASN   A OD1  1 
ATOM   2191 N  ND2  A ASN   A 1 101 ? 16.946 2.350   -10.080 0.62 18.84 ?  101 ASN   A ND2  1 
ATOM   2192 N  ND2  B ASN   A 1 101 ? 17.597 2.167   -10.581 0.38 18.64 ?  101 ASN   A ND2  1 
ATOM   2193 H  H    A ASN   A 1 101 ? 19.221 0.319   -11.252 0.62 22.47 ?  101 ASN   A H    1 
ATOM   2194 H  H    B ASN   A 1 101 ? 19.218 -0.191  -11.758 0.38 21.31 ?  101 ASN   A H    1 
ATOM   2195 H  HA   A ASN   A 1 101 ? 18.624 1.469   -13.539 0.62 23.88 ?  101 ASN   A HA   1 
ATOM   2196 H  HA   B ASN   A 1 101 ? 18.502 0.578   -14.169 0.38 22.01 ?  101 ASN   A HA   1 
ATOM   2197 H  HB2  A ASN   A 1 101 ? 19.159 2.725   -11.076 0.62 23.05 ?  101 ASN   A HB2  1 
ATOM   2198 H  HB2  B ASN   A 1 101 ? 19.464 2.282   -12.138 0.38 21.78 ?  101 ASN   A HB2  1 
ATOM   2199 H  HB3  A ASN   A 1 101 ? 18.503 3.448   -12.331 0.62 23.05 ?  101 ASN   A HB3  1 
ATOM   2200 H  HB3  B ASN   A 1 101 ? 18.505 2.700   -13.335 0.38 21.78 ?  101 ASN   A HB3  1 
ATOM   2201 H  HD21 A ASN   A 1 101 ? 16.178 2.121   -9.766  0.62 22.59 ?  101 ASN   A HD21 1 
ATOM   2202 H  HD21 B ASN   A 1 101 ? 16.937 2.042   -10.045 0.38 22.35 ?  101 ASN   A HD21 1 
ATOM   2203 H  HD22 A ASN   A 1 101 ? 17.540 2.689   -9.563  0.62 22.59 ?  101 ASN   A HD22 1 
ATOM   2204 H  HD22 B ASN   A 1 101 ? 18.301 2.580   -10.310 0.38 22.35 ?  101 ASN   A HD22 1 
ATOM   2205 N  N    A LYS   A 1 102 ? 21.645 1.271   -13.121 0.62 23.53 ?  102 LYS   A N    1 
ATOM   2206 N  N    B LYS   A 1 102 ? 21.611 0.598   -13.605 0.38 20.42 ?  102 LYS   A N    1 
ATOM   2207 C  CA   A LYS   A 1 102 ? 22.929 1.476   -13.785 0.62 24.58 ?  102 LYS   A CA   1 
ATOM   2208 C  CA   B LYS   A 1 102 ? 22.925 0.718   -14.221 0.38 21.33 ?  102 LYS   A CA   1 
ATOM   2209 C  C    A LYS   A 1 102 ? 23.249 0.389   -14.803 0.62 24.89 ?  102 LYS   A C    1 
ATOM   2210 C  C    B LYS   A 1 102 ? 23.249 -0.447  -15.150 0.38 20.85 ?  102 LYS   A C    1 
ATOM   2211 O  O    A LYS   A 1 102 ? 24.308 0.450   -15.434 0.62 25.34 ?  102 LYS   A O    1 
ATOM   2212 O  O    B LYS   A 1 102 ? 24.369 -0.514  -15.666 0.38 20.48 ?  102 LYS   A O    1 
ATOM   2213 C  CB   A LYS   A 1 102 ? 24.067 1.538   -12.757 0.62 26.07 ?  102 LYS   A CB   1 
ATOM   2214 C  CB   B LYS   A 1 102 ? 24.016 0.787   -13.144 0.38 22.76 ?  102 LYS   A CB   1 
ATOM   2215 C  CG   A LYS   A 1 102 ? 23.963 2.674   -11.760 0.62 27.33 ?  102 LYS   A CG   1 
ATOM   2216 C  CG   B LYS   A 1 102 ? 23.943 1.984   -12.207 0.38 23.82 ?  102 LYS   A CG   1 
ATOM   2217 C  CD   A LYS   A 1 102 ? 25.140 2.645   -10.797 0.62 28.71 ?  102 LYS   A CD   1 
ATOM   2218 C  CD   B LYS   A 1 102 ? 25.086 1.938   -11.191 0.38 24.90 ?  102 LYS   A CD   1 
ATOM   2219 C  CE   A LYS   A 1 102 ? 25.033 3.732   -9.744  0.62 29.82 ?  102 LYS   A CE   1 
ATOM   2220 C  CE   B LYS   A 1 102 ? 24.856 2.884   -10.021 0.38 25.78 ?  102 LYS   A CE   1 
ATOM   2221 N  NZ   A LYS   A 1 102 ? 26.130 3.630   -8.740  0.62 30.27 ?  102 LYS   A NZ   1 
ATOM   2222 N  NZ   B LYS   A 1 102 ? 24.785 2.157   -8.717  0.38 26.14 ?  102 LYS   A NZ   1 
ATOM   2223 H  H    A LYS   A 1 102 ? 21.658 0.607   -12.573 0.62 28.22 ?  102 LYS   A H    1 
ATOM   2224 H  H    B LYS   A 1 102 ? 21.626 0.227   -12.826 0.38 24.49 ?  102 LYS   A H    1 
ATOM   2225 H  HA   A LYS   A 1 102 ? 22.914 2.312   -14.263 0.62 29.48 ?  102 LYS   A HA   1 
ATOM   2226 H  HA   B LYS   A 1 102 ? 22.955 1.543   -14.729 0.38 25.58 ?  102 LYS   A HA   1 
ATOM   2227 H  HB2  A LYS   A 1 102 ? 24.079 0.708   -12.254 0.62 31.27 ?  102 LYS   A HB2  1 
ATOM   2228 H  HB2  B LYS   A 1 102 ? 23.956 -0.012  -12.597 0.38 27.30 ?  102 LYS   A HB2  1 
ATOM   2229 H  HB3  A LYS   A 1 102 ? 24.909 1.641   -13.230 0.62 31.27 ?  102 LYS   A HB3  1 
ATOM   2230 H  HB3  B LYS   A 1 102 ? 24.879 0.815   -13.584 0.38 27.30 ?  102 LYS   A HB3  1 
ATOM   2231 H  HG2  A LYS   A 1 102 ? 23.972 3.520   -12.234 0.62 32.78 ?  102 LYS   A HG2  1 
ATOM   2232 H  HG2  B LYS   A 1 102 ? 24.027 2.801   -12.721 0.38 28.57 ?  102 LYS   A HG2  1 
ATOM   2233 H  HG3  A LYS   A 1 102 ? 23.144 2.579   -11.249 0.62 32.78 ?  102 LYS   A HG3  1 
ATOM   2234 H  HG3  B LYS   A 1 102 ? 23.100 1.974   -11.729 0.38 28.57 ?  102 LYS   A HG3  1 
ATOM   2235 H  HD2  A LYS   A 1 102 ? 25.162 1.786   -10.346 0.62 34.44 ?  102 LYS   A HD2  1 
ATOM   2236 H  HD2  B LYS   A 1 102 ? 25.167 1.036   -10.842 0.38 29.86 ?  102 LYS   A HD2  1 
ATOM   2237 H  HD3  A LYS   A 1 102 ? 25.962 2.783   -11.294 0.62 34.44 ?  102 LYS   A HD3  1 
ATOM   2238 H  HD3  B LYS   A 1 102 ? 25.910 2.198   -11.632 0.38 29.86 ?  102 LYS   A HD3  1 
ATOM   2239 H  HE2  A LYS   A 1 102 ? 25.093 4.600   -10.175 0.62 35.77 ?  102 LYS   A HE2  1 
ATOM   2240 H  HE2  B LYS   A 1 102 ? 25.591 3.515   -9.974  0.38 30.92 ?  102 LYS   A HE2  1 
ATOM   2241 H  HE3  A LYS   A 1 102 ? 24.185 3.645   -9.281  0.62 35.77 ?  102 LYS   A HE3  1 
ATOM   2242 H  HE3  B LYS   A 1 102 ? 24.019 3.356   -10.151 0.38 30.92 ?  102 LYS   A HE3  1 
ATOM   2243 H  HZ1  A LYS   A 1 102 ? 26.048 4.275   -8.134  0.62 36.31 ?  102 LYS   A HZ1  1 
ATOM   2244 H  HZ1  B LYS   A 1 102 ? 24.266 2.602   -8.146  0.38 31.35 ?  102 LYS   A HZ1  1 
ATOM   2245 H  HZ2  A LYS   A 1 102 ? 26.093 2.840   -8.330  0.62 36.31 ?  102 LYS   A HZ2  1 
ATOM   2246 H  HZ2  B LYS   A 1 102 ? 24.446 1.345   -8.841  0.38 31.35 ?  102 LYS   A HZ2  1 
ATOM   2247 H  HZ3  A LYS   A 1 102 ? 26.919 3.709   -9.144  0.62 36.31 ?  102 LYS   A HZ3  1 
ATOM   2248 H  HZ3  B LYS   A 1 102 ? 25.598 2.076   -8.369  0.38 31.35 ?  102 LYS   A HZ3  1 
ATOM   2249 N  N    A GLY   A 1 103 ? 22.376 -0.604  -14.971 0.62 25.58 ?  103 GLY   A N    1 
ATOM   2250 N  N    B GLY   A 1 103 ? 22.318 -1.377  -15.353 0.38 20.72 ?  103 GLY   A N    1 
ATOM   2251 C  CA   A GLY   A 1 103 ? 22.625 -1.682  -15.910 0.62 25.72 ?  103 GLY   A CA   1 
ATOM   2252 C  CA   B GLY   A 1 103 ? 22.591 -2.535  -16.180 0.38 20.20 ?  103 GLY   A CA   1 
ATOM   2253 C  C    A GLY   A 1 103 ? 23.510 -2.791  -15.386 0.62 25.87 ?  103 GLY   A C    1 
ATOM   2254 C  C    B GLY   A 1 103 ? 23.459 -3.592  -15.533 0.38 19.02 ?  103 GLY   A C    1 
ATOM   2255 O  O    A GLY   A 1 103 ? 24.175 -3.466  -16.179 0.62 26.59 ?  103 GLY   A O    1 
ATOM   2256 O  O    B GLY   A 1 103 ? 23.900 -4.518  -16.223 0.38 19.02 ?  103 GLY   A O    1 
ATOM   2257 H  H    A GLY   A 1 103 ? 21.635 -0.681  -14.548 0.62 30.68 ?  103 GLY   A H    1 
ATOM   2258 H  H    B GLY   A 1 103 ? 21.523 -1.355  -15.018 0.38 24.85 ?  103 GLY   A H    1 
ATOM   2259 H  HA2  A GLY   A 1 103 ? 21.771 -2.061  -16.194 0.62 30.84 ?  103 GLY   A HA2  1 
ATOM   2260 H  HA2  B GLY   A 1 103 ? 21.753 -2.952  -16.420 0.38 24.22 ?  103 GLY   A HA2  1 
ATOM   2261 H  HA3  A GLY   A 1 103 ? 23.064 -1.326  -16.694 0.62 30.84 ?  103 GLY   A HA3  1 
ATOM   2262 H  HA3  B GLY   A 1 103 ? 23.022 -2.234  -17.000 0.38 24.22 ?  103 GLY   A HA3  1 
ATOM   2263 N  N    A GLU   A 1 104 ? 23.546 -3.001  -14.073 0.62 24.70 ?  104 GLU   A N    1 
ATOM   2264 N  N    B GLU   A 1 104 ? 23.708 -3.494  -14.230 0.38 17.93 ?  104 GLU   A N    1 
ATOM   2265 C  CA   A GLU   A 1 104 ? 24.417 -4.000  -13.468 0.62 23.34 ?  104 GLU   A CA   1 
ATOM   2266 C  CA   B GLU   A 1 104 ? 24.595 -4.435  -13.560 0.38 16.71 ?  104 GLU   A CA   1 
ATOM   2267 C  C    A GLU   A 1 104 ? 23.726 -5.358  -13.370 0.62 23.58 ?  104 GLU   A C    1 
ATOM   2268 C  C    B GLU   A 1 104 ? 23.906 -5.786  -13.376 0.38 16.49 ?  104 GLU   A C    1 
ATOM   2269 O  O    A GLU   A 1 104 ? 22.498 -5.454  -13.281 0.62 23.92 ?  104 GLU   A O    1 
ATOM   2270 O  O    B GLU   A 1 104 ? 22.697 -5.863  -13.135 0.38 17.06 ?  104 GLU   A O    1 
ATOM   2271 C  CB   A GLU   A 1 104 ? 24.902 -3.508  -12.100 0.62 21.55 ?  104 GLU   A CB   1 
ATOM   2272 C  CB   B GLU   A 1 104 ? 25.061 -3.843  -12.227 0.38 16.32 ?  104 GLU   A CB   1 
ATOM   2273 C  CG   A GLU   A 1 104 ? 25.860 -2.319  -12.251 0.62 20.52 ?  104 GLU   A CG   1 
ATOM   2274 C  CG   B GLU   A 1 104 ? 25.785 -2.505  -12.415 0.38 16.83 ?  104 GLU   A CG   1 
ATOM   2275 C  CD   A GLU   A 1 104 ? 26.205 -1.579  -10.963 0.62 19.39 ?  104 GLU   A CD   1 
ATOM   2276 C  CD   B GLU   A 1 104 ? 26.166 -1.806  -11.119 0.38 16.95 ?  104 GLU   A CD   1 
ATOM   2277 O  OE1  A GLU   A 1 104 ? 25.607 -1.854  -9.905  0.62 17.58 ?  104 GLU   A OE1  1 
ATOM   2278 O  OE1  B GLU   A 1 104 ? 25.683 -2.201  -10.040 0.38 16.91 ?  104 GLU   A OE1  1 
ATOM   2279 O  OE2  A GLU   A 1 104 ? 27.093 -0.694  -11.028 0.62 20.39 -1 104 GLU   A OE2  1 
ATOM   2280 O  OE2  B GLU   A 1 104 ? 26.949 -0.833  -11.194 0.38 17.42 -1 104 GLU   A OE2  1 
ATOM   2281 H  H    A GLU   A 1 104 ? 23.080 -2.563  -13.502 0.62 29.62 ?  104 GLU   A H    1 
ATOM   2282 H  H    B GLU   A 1 104 ? 23.374 -2.891  -13.716 0.38 21.50 ?  104 GLU   A H    1 
ATOM   2283 H  HA   A GLU   A 1 104 ? 25.194 -4.115  -14.032 0.62 27.99 ?  104 GLU   A HA   1 
ATOM   2284 H  HA   B GLU   A 1 104 ? 25.382 -4.571  -14.111 0.38 20.03 ?  104 GLU   A HA   1 
ATOM   2285 H  HB2  A GLU   A 1 104 ? 24.136 -3.226  -11.576 0.62 25.85 ?  104 GLU   A HB2  1 
ATOM   2286 H  HB2  B GLU   A 1 104 ? 24.294 -3.691  -11.657 0.38 19.57 ?  104 GLU   A HB2  1 
ATOM   2287 H  HB3  A GLU   A 1 104 ? 25.370 -4.229  -11.651 0.62 25.85 ?  104 GLU   A HB3  1 
ATOM   2288 H  HB3  B GLU   A 1 104 ? 25.680 -4.459  -11.804 0.38 19.57 ?  104 GLU   A HB3  1 
ATOM   2289 H  HG2  A GLU   A 1 104 ? 26.691 -2.648  -12.619 0.62 24.60 ?  104 GLU   A HG2  1 
ATOM   2290 H  HG2  B GLU   A 1 104 ? 26.600 -2.656  -12.918 0.38 20.18 ?  104 GLU   A HG2  1 
ATOM   2291 H  HG3  A GLU   A 1 104 ? 25.458 -1.684  -12.864 0.62 24.60 ?  104 GLU   A HG3  1 
ATOM   2292 H  HG3  B GLU   A 1 104 ? 25.206 -1.900  -12.907 0.38 20.18 ?  104 GLU   A HG3  1 
ATOM   2293 N  N    A ASP   A 1 105 ? 24.543 -6.413  -13.387 0.62 24.07 ?  105 ASP   A N    1 
ATOM   2294 N  N    B ASP   A 1 105 ? 24.696 -6.855  -13.497 0.38 16.74 ?  105 ASP   A N    1 
ATOM   2295 C  CA   A ASP   A 1 105 ? 24.055 -7.780  -13.538 0.62 24.87 ?  105 ASP   A CA   1 
ATOM   2296 C  CA   B ASP   A 1 105 ? 24.177 -8.219  -13.578 0.38 17.61 ?  105 ASP   A CA   1 
ATOM   2297 C  C    A ASP   A 1 105 ? 23.366 -8.244  -12.258 0.62 22.66 ?  105 ASP   A C    1 
ATOM   2298 C  C    B ASP   A 1 105 ? 23.456 -8.616  -12.294 0.38 16.53 ?  105 ASP   A C    1 
ATOM   2299 O  O    A ASP   A 1 105 ? 24.008 -8.370  -11.211 0.62 21.16 ?  105 ASP   A O    1 
ATOM   2300 O  O    B ASP   A 1 105 ? 24.038 -8.591  -11.207 0.38 15.17 ?  105 ASP   A O    1 
ATOM   2301 C  CB   A ASP   A 1 105 ? 25.236 -8.692  -13.870 0.62 27.50 ?  105 ASP   A CB   1 
ATOM   2302 C  CB   B ASP   A 1 105 ? 25.354 -9.162  -13.838 0.38 19.63 ?  105 ASP   A CB   1 
ATOM   2303 C  CG   A ASP   A 1 105 ? 24.813 -10.111 -14.167 0.62 29.79 ?  105 ASP   A CG   1 
ATOM   2304 C  CG   B ASP   A 1 105 ? 24.959 -10.627 -13.839 0.38 21.26 ?  105 ASP   A CG   1 
ATOM   2305 O  OD1  A ASP   A 1 105 ? 23.593 -10.360 -14.252 0.62 30.36 ?  105 ASP   A OD1  1 
ATOM   2306 O  OD1  B ASP   A 1 105 ? 23.753 -10.932 -13.926 0.38 21.27 ?  105 ASP   A OD1  1 
ATOM   2307 O  OD2  A ASP   A 1 105 ? 25.704 -10.974 -14.321 0.62 31.00 -1 105 ASP   A OD2  1 
ATOM   2308 O  OD2  B ASP   A 1 105 ? 25.873 -11.479 -13.745 0.38 22.75 -1 105 ASP   A OD2  1 
ATOM   2309 H  H    A ASP   A 1 105 ? 25.400 -6.365  -13.308 0.62 28.87 ?  105 ASP   A H    1 
ATOM   2310 H  H    B ASP   A 1 105 ? 25.553 -6.806  -13.544 0.38 20.07 ?  105 ASP   A H    1 
ATOM   2311 H  HA   A ASP   A 1 105 ? 23.419 -7.831  -14.266 0.62 29.82 ?  105 ASP   A HA   1 
ATOM   2312 H  HA   B ASP   A 1 105 ? 23.554 -8.280  -14.319 0.38 21.11 ?  105 ASP   A HA   1 
ATOM   2313 H  HB2  A ASP   A 1 105 ? 25.690 -8.353  -14.660 0.62 32.98 ?  105 ASP   A HB2  1 
ATOM   2314 H  HB2  B ASP   A 1 105 ? 25.748 -8.937  -14.697 0.38 23.55 ?  105 ASP   A HB2  1 
ATOM   2315 H  HB3  A ASP   A 1 105 ? 25.852 -8.710  -13.120 0.62 32.98 ?  105 ASP   A HB3  1 
ATOM   2316 H  HB3  B ASP   A 1 105 ? 26.004 -9.051  -13.134 0.38 23.55 ?  105 ASP   A HB3  1 
ATOM   2317 N  N    A ILE   A 1 106 ? 22.062 -8.519  -12.346 0.62 22.13 ?  106 ILE   A N    1 
ATOM   2318 N  N    B ILE   A 1 106 ? 22.192 -9.024  -12.431 0.38 17.23 ?  106 ILE   A N    1 
ATOM   2319 C  CA   A ILE   A 1 106 ? 21.299 -8.940  -11.176 0.62 21.12 ?  106 ILE   A CA   1 
ATOM   2320 C  CA   B ILE   A 1 106 ? 21.392 -9.377  -11.261 0.38 17.88 ?  106 ILE   A CA   1 
ATOM   2321 C  C    A ILE   A 1 106 ? 21.828 -10.239 -10.592 0.62 19.84 ?  106 ILE   A C    1 
ATOM   2322 C  C    B ILE   A 1 106 ? 21.967 -10.591 -10.545 0.38 17.56 ?  106 ILE   A C    1 
ATOM   2323 O  O    A ILE   A 1 106 ? 21.624 -10.507 -9.403  0.62 19.13 ?  106 ILE   A O    1 
ATOM   2324 O  O    B ILE   A 1 106 ? 21.776 -10.752 -9.333  0.38 17.64 ?  106 ILE   A O    1 
ATOM   2325 C  CB   A ILE   A 1 106 ? 19.791 -9.030  -11.508 0.62 21.88 ?  106 ILE   A CB   1 
ATOM   2326 C  CB   B ILE   A 1 106 ? 19.918 -9.582  -11.667 0.38 19.10 ?  106 ILE   A CB   1 
ATOM   2327 C  CG1  A ILE   A 1 106 ? 18.959 -9.123  -10.226 0.62 22.19 ?  106 ILE   A CG1  1 
ATOM   2328 C  CG1  B ILE   A 1 106 ? 19.017 -9.639  -10.433 0.38 19.43 ?  106 ILE   A CG1  1 
ATOM   2329 C  CG2  A ILE   A 1 106 ? 19.509 -10.225 -12.409 0.62 22.17 ?  106 ILE   A CG2  1 
ATOM   2330 C  CG2  B ILE   A 1 106 ? 19.759 -10.861 -12.461 0.38 19.54 ?  106 ILE   A CG2  1 
ATOM   2331 C  CD1  A ILE   A 1 106 ? 19.118 -7.932  -9.303  0.62 22.42 ?  106 ILE   A CD1  1 
ATOM   2332 C  CD1  B ILE   A 1 106 ? 18.998 -8.365  -9.630  0.38 19.56 ?  106 ILE   A CD1  1 
ATOM   2333 H  H    A ILE   A 1 106 ? 21.603 -8.463  -13.067 0.62 26.53 ?  106 ILE   A H    1 
ATOM   2334 H  H    B ILE   A 1 106 ? 21.788 -9.109  -13.182 0.38 20.66 ?  106 ILE   A H    1 
ATOM   2335 H  HA   A ILE   A 1 106 ? 21.409 -8.267  -10.496 0.62 25.32 ?  106 ILE   A HA   1 
ATOM   2336 H  HA   B ILE   A 1 106 ? 21.429 -8.640  -10.638 0.38 21.44 ?  106 ILE   A HA   1 
ATOM   2337 H  HB   A ILE   A 1 106 ? 19.535 -8.226  -11.982 0.62 26.24 ?  106 ILE   A HB   1 
ATOM   2338 H  HB   B ILE   A 1 106 ? 19.642 -8.835  -12.222 0.38 22.90 ?  106 ILE   A HB   1 
ATOM   2339 H  HG12 A ILE   A 1 106 ? 18.021 -9.186  -10.468 0.62 26.62 ?  106 ILE   A HG12 1 
ATOM   2340 H  HG12 B ILE   A 1 106 ? 18.108 -9.820  -10.721 0.38 23.30 ?  106 ILE   A HG12 1 
ATOM   2341 H  HG13 A ILE   A 1 106 ? 19.223 -9.917  -9.736  0.62 26.62 ?  106 ILE   A HG13 1 
ATOM   2342 H  HG13 B ILE   A 1 106 ? 19.324 -10.352 -9.853  0.38 23.30 ?  106 ILE   A HG13 1 
ATOM   2343 H  HG21 A ILE   A 1 106 ? 18.613 -10.142 -12.770 0.62 26.58 ?  106 ILE   A HG21 1 
ATOM   2344 H  HG21 B ILE   A 1 106 ? 18.892 -10.855 -12.893 0.38 23.43 ?  106 ILE   A HG21 1 
ATOM   2345 H  HG22 A ILE   A 1 106 ? 20.157 -10.234 -13.131 0.62 26.58 ?  106 ILE   A HG22 1 
ATOM   2346 H  HG22 B ILE   A 1 106 ? 20.462 -10.908 -13.126 0.38 23.43 ?  106 ILE   A HG22 1 
ATOM   2347 H  HG23 A ILE   A 1 106 ? 19.582 -11.040 -11.889 0.62 26.58 ?  106 ILE   A HG23 1 
ATOM   2348 H  HG23 B ILE   A 1 106 ? 19.823 -11.617 -11.856 0.38 23.43 ?  106 ILE   A HG23 1 
ATOM   2349 H  HD11 A ILE   A 1 106 ? 18.380 -7.921  -8.677  0.62 26.89 ?  106 ILE   A HD11 1 
ATOM   2350 H  HD11 B ILE   A 1 106 ? 18.243 -8.389  -9.024  0.38 23.46 ?  106 ILE   A HD11 1 
ATOM   2351 H  HD12 A ILE   A 1 106 ? 19.958 -8.013  -8.825  0.62 26.89 ?  106 ILE   A HD12 1 
ATOM   2352 H  HD12 B ILE   A 1 106 ? 19.824 -8.296  -9.126  0.38 23.46 ?  106 ILE   A HD12 1 
ATOM   2353 H  HD13 A ILE   A 1 106 ? 19.115 -7.121  -9.835  0.62 26.89 ?  106 ILE   A HD13 1 
ATOM   2354 H  HD13 B ILE   A 1 106 ? 18.914 -7.613  -10.236 0.38 23.46 ?  106 ILE   A HD13 1 
ATOM   2355 N  N    A GLN   A 1 107 ? 22.519 -11.053 -11.398 0.62 20.61 ?  107 GLN   A N    1 
ATOM   2356 N  N    B GLN   A 1 107 ? 22.681 -11.461 -11.269 0.38 17.67 ?  107 GLN   A N    1 
ATOM   2357 C  CA   A GLN   A 1 107 ? 23.133 -12.274 -10.889 0.62 22.33 ?  107 GLN   A CA   1 
ATOM   2358 C  CA   B GLN   A 1 107 ? 23.307 -12.614 -10.630 0.38 18.84 ?  107 GLN   A CA   1 
ATOM   2359 C  C    A GLN   A 1 107 ? 24.115 -11.988 -9.763  0.62 20.10 ?  107 GLN   A C    1 
ATOM   2360 C  C    B GLN   A 1 107 ? 24.286 -12.191 -9.543  0.38 16.96 ?  107 GLN   A C    1 
ATOM   2361 O  O    A GLN   A 1 107 ? 24.349 -12.860 -8.920  0.62 21.68 ?  107 GLN   A O    1 
ATOM   2362 O  O    B GLN   A 1 107 ? 24.543 -12.963 -8.610  0.38 17.05 ?  107 GLN   A O    1 
ATOM   2363 C  CB   A GLN   A 1 107 ? 23.844 -13.020 -12.026 0.62 26.43 ?  107 GLN   A CB   1 
ATOM   2364 C  CB   B GLN   A 1 107 ? 24.005 -13.478 -11.684 0.38 21.80 ?  107 GLN   A CB   1 
ATOM   2365 C  CG   A GLN   A 1 107 ? 22.971 -13.293 -13.244 0.62 30.70 ?  107 GLN   A CG   1 
ATOM   2366 C  CG   B GLN   A 1 107 ? 23.066 -13.987 -12.769 0.38 24.64 ?  107 GLN   A CG   1 
ATOM   2367 C  CD   A GLN   A 1 107 ? 21.714 -14.064 -12.899 0.62 34.11 ?  107 GLN   A CD   1 
ATOM   2368 C  CD   B GLN   A 1 107 ? 21.927 -14.816 -12.207 0.38 27.09 ?  107 GLN   A CD   1 
ATOM   2369 O  OE1  A GLN   A 1 107 ? 21.771 -15.115 -12.262 0.62 35.47 ?  107 GLN   A OE1  1 
ATOM   2370 O  OE1  B GLN   A 1 107 ? 22.140 -15.705 -11.382 0.38 27.90 ?  107 GLN   A OE1  1 
ATOM   2371 N  NE2  A GLN   A 1 107 ? 20.567 -13.539 -13.312 0.62 35.20 ?  107 GLN   A NE2  1 
ATOM   2372 N  NE2  B GLN   A 1 107 ? 20.707 -14.521 -12.645 0.38 27.81 ?  107 GLN   A NE2  1 
ATOM   2373 H  H    A GLN   A 1 107 ? 22.649 -10.917 -12.234 0.62 24.72 ?  107 GLN   A H    1 
ATOM   2374 H  H    B GLN   A 1 107 ? 22.819 -11.404 -12.118 0.38 21.19 ?  107 GLN   A H    1 
ATOM   2375 H  HA   A GLN   A 1 107 ? 22.447 -12.860 -10.539 0.62 26.78 ?  107 GLN   A HA   1 
ATOM   2376 H  HA   B GLN   A 1 107 ? 22.620 -13.154 -10.218 0.38 22.59 ?  107 GLN   A HA   1 
ATOM   2377 H  HB2  A GLN   A 1 107 ? 24.602 -12.492 -12.325 0.62 31.70 ?  107 GLN   A HB2  1 
ATOM   2378 H  HB2  B GLN   A 1 107 ? 24.699 -12.956 -12.116 0.38 26.15 ?  107 GLN   A HB2  1 
ATOM   2379 H  HB3  A GLN   A 1 107 ? 24.156 -13.879 -11.697 0.62 31.70 ?  107 GLN   A HB3  1 
ATOM   2380 H  HB3  B GLN   A 1 107 ? 24.398 -14.252 -11.250 0.38 26.15 ?  107 GLN   A HB3  1 
ATOM   2381 H  HG2  A GLN   A 1 107 ? 22.703 -12.451 -13.641 0.62 36.82 ?  107 GLN   A HG2  1 
ATOM   2382 H  HG2  B GLN   A 1 107 ? 22.685 -13.229 -13.239 0.38 29.56 ?  107 GLN   A HG2  1 
ATOM   2383 H  HG3  A GLN   A 1 107 ? 23.478 -13.815 -13.888 0.62 36.82 ?  107 GLN   A HG3  1 
ATOM   2384 H  HG3  B GLN   A 1 107 ? 23.566 -14.544 -13.386 0.38 29.56 ?  107 GLN   A HG3  1 
ATOM   2385 H  HE21 A GLN   A 1 107 ? 20.566 -12.802 -13.754 0.62 42.22 ?  107 GLN   A HE21 1 
ATOM   2386 H  HE21 B GLN   A 1 107 ? 20.596 -13.891 -13.220 0.38 33.36 ?  107 GLN   A HE21 1 
ATOM   2387 H  HE22 A GLN   A 1 107 ? 19.826 -13.940 -13.140 0.62 42.22 ?  107 GLN   A HE22 1 
ATOM   2388 H  HE22 B GLN   A 1 107 ? 20.027 -14.961 -12.354 0.38 33.36 ?  107 GLN   A HE22 1 
ATOM   2389 N  N    A LEU   A 1 108 ? 24.676 -10.777 -9.712  0.62 16.31 ?  108 LEU   A N    1 
ATOM   2390 N  N    B LEU   A 1 108 ? 24.820 -10.973 -9.635  0.38 15.46 ?  108 LEU   A N    1 
ATOM   2391 C  CA   A LEU   A 1 108 ? 25.624 -10.427 -8.662  0.62 14.57 ?  108 LEU   A CA   1 
ATOM   2392 C  CA   B LEU   A 1 108 ? 25.685 -10.434 -8.596  0.38 14.39 ?  108 LEU   A CA   1 
ATOM   2393 C  C    A LEU   A 1 108 ? 24.954 -10.250 -7.307  0.62 12.90 ?  108 LEU   A C    1 
ATOM   2394 C  C    B LEU   A 1 108 ? 24.959 -10.237 -7.273  0.38 13.07 ?  108 LEU   A C    1 
ATOM   2395 O  O    A LEU   A 1 108 ? 25.656 -10.098 -6.304  0.62 12.99 ?  108 LEU   A O    1 
ATOM   2396 O  O    B LEU   A 1 108 ? 25.626 -10.047 -6.251  0.38 13.20 ?  108 LEU   A O    1 
ATOM   2397 C  CB   A LEU   A 1 108 ? 26.410 -9.168  -9.047  0.62 14.52 ?  108 LEU   A CB   1 
ATOM   2398 C  CB   B LEU   A 1 108 ? 26.308 -9.113  -9.066  0.38 14.56 ?  108 LEU   A CB   1 
ATOM   2399 C  CG   A LEU   A 1 108 ? 27.395 -9.399  -10.198 0.62 16.06 ?  108 LEU   A CG   1 
ATOM   2400 C  CG   B LEU   A 1 108 ? 27.305 -9.253  -10.219 0.38 15.45 ?  108 LEU   A CG   1 
ATOM   2401 C  CD1  A LEU   A 1 108 ? 27.969 -8.084  -10.709 0.62 16.55 ?  108 LEU   A CD1  1 
ATOM   2402 C  CD1  B LEU   A 1 108 ? 27.637 -7.898  -10.832 0.38 15.76 ?  108 LEU   A CD1  1 
ATOM   2403 C  CD2  A LEU   A 1 108 ? 28.522 -10.336 -9.775  0.62 17.65 ?  108 LEU   A CD2  1 
ATOM   2404 C  CD2  B LEU   A 1 108 ? 28.573 -9.941  -9.737  0.38 16.24 ?  108 LEU   A CD2  1 
ATOM   2405 H  H    A LEU   A 1 108 ? 24.519 -10.151 -10.272 0.62 19.56 ?  108 LEU   A H    1 
ATOM   2406 H  H    B LEU   A 1 108 ? 24.698 -10.444 -10.297 0.38 18.54 ?  108 LEU   A H    1 
ATOM   2407 H  HA   A LEU   A 1 108 ? 26.259 -11.150 -8.567  0.62 17.46 ?  108 LEU   A HA   1 
ATOM   2408 H  HA   B LEU   A 1 108 ? 26.406 -11.059 -8.436  0.38 17.25 ?  108 LEU   A HA   1 
ATOM   2409 H  HB2  A LEU   A 1 108 ? 25.785 -8.478  -9.325  0.62 17.41 ?  108 LEU   A HB2  1 
ATOM   2410 H  HB2  B LEU   A 1 108 ? 25.600 -8.520  -9.362  0.38 17.45 ?  108 LEU   A HB2  1 
ATOM   2411 H  HB3  A LEU   A 1 108 ? 26.915 -8.864  -8.278  0.62 17.41 ?  108 LEU   A HB3  1 
ATOM   2412 H  HB3  B LEU   A 1 108 ? 26.780 -8.711  -8.321  0.38 17.45 ?  108 LEU   A HB3  1 
ATOM   2413 H  HG   A LEU   A 1 108 ? 26.924 -9.820  -10.933 0.62 19.26 ?  108 LEU   A HG   1 
ATOM   2414 H  HG   B LEU   A 1 108 ? 26.912 -9.806  -10.914 0.38 18.53 ?  108 LEU   A HG   1 
ATOM   2415 H  HD11 A LEU   A 1 108 ? 28.580 -8.268  -11.443 0.62 19.85 ?  108 LEU   A HD11 1 
ATOM   2416 H  HD11 B LEU   A 1 108 ? 28.207 -8.033  -11.609 0.38 18.90 ?  108 LEU   A HD11 1 
ATOM   2417 H  HD12 A LEU   A 1 108 ? 27.242 -7.521  -11.022 0.62 19.85 ?  108 LEU   A HD12 1 
ATOM   2418 H  HD12 B LEU   A 1 108 ? 26.814 -7.462  -11.100 0.38 18.90 ?  108 LEU   A HD12 1 
ATOM   2419 H  HD13 A LEU   A 1 108 ? 28.443 -7.641  -9.989  0.62 19.85 ?  108 LEU   A HD13 1 
ATOM   2420 H  HD13 B LEU   A 1 108 ? 28.102 -7.358  -10.174 0.38 18.90 ?  108 LEU   A HD13 1 
ATOM   2421 H  HD21 A LEU   A 1 108 ? 29.227 -10.299 -10.440 0.62 21.16 ?  108 LEU   A HD21 1 
ATOM   2422 H  HD21 B LEU   A 1 108 ? 29.238 -9.910  -10.442 0.38 19.47 ?  108 LEU   A HD21 1 
ATOM   2423 H  HD22 A LEU   A 1 108 ? 28.863 -10.047 -8.914  0.62 21.16 ?  108 LEU   A HD22 1 
ATOM   2424 H  HD22 B LEU   A 1 108 ? 28.901 -9.482  -8.950  0.38 19.47 ?  108 LEU   A HD22 1 
ATOM   2425 H  HD23 A LEU   A 1 108 ? 28.174 -11.237 -9.708  0.62 21.16 ?  108 LEU   A HD23 1 
ATOM   2426 H  HD23 B LEU   A 1 108 ? 28.367 -10.865 -9.519  0.38 19.47 ?  108 LEU   A HD23 1 
ATOM   2427 N  N    . LEU   A 1 109 ? 23.624 -10.284 -7.252  1.00 12.21 ?  109 LEU   A N    1 
ATOM   2428 C  CA   . LEU   A 1 109 ? 22.931 -10.152 -5.978  1.00 11.53 ?  109 LEU   A CA   1 
ATOM   2429 C  C    . LEU   A 1 109 ? 23.265 -11.310 -5.041  1.00 10.74 ?  109 LEU   A C    1 
ATOM   2430 O  O    . LEU   A 1 109 ? 23.397 -11.119 -3.827  1.00 11.34 ?  109 LEU   A O    1 
ATOM   2431 C  CB   . LEU   A 1 109 ? 21.429 -10.054 -6.226  1.00 12.51 ?  109 LEU   A CB   1 
ATOM   2432 C  CG   . LEU   A 1 109 ? 20.548 -9.779  -5.013  1.00 12.52 ?  109 LEU   A CG   1 
ATOM   2433 C  CD1  . LEU   A 1 109 ? 21.013 -8.533  -4.286  1.00 12.82 ?  109 LEU   A CD1  1 
ATOM   2434 C  CD2  . LEU   A 1 109 ? 19.089 -9.630  -5.438  1.00 13.51 ?  109 LEU   A CD2  1 
ATOM   2435 H  H    A LEU   A 1 109 ? 23.103 -10.376 -7.931  0.62 14.63 ?  109 LEU   A H    1 
ATOM   2436 H  H    B LEU   A 1 109 ? 23.113 -10.386 -7.937  0.38 14.63 ?  109 LEU   A H    1 
ATOM   2437 H  HA   . LEU   A 1 109 ? 23.221 -9.329  -5.551  1.00 13.82 ?  109 LEU   A HA   1 
ATOM   2438 H  HB2  . LEU   A 1 109 ? 21.274 -9.335  -6.860  1.00 14.99 ?  109 LEU   A HB2  1 
ATOM   2439 H  HB3  . LEU   A 1 109 ? 21.132 -10.891 -6.611  1.00 14.99 ?  109 LEU   A HB3  1 
ATOM   2440 H  HG   . LEU   A 1 109 ? 20.606 -10.524 -4.399  1.00 15.01 ?  109 LEU   A HG   1 
ATOM   2441 H  HD11 . LEU   A 1 109 ? 20.331 -8.254  -3.659  1.00 15.37 ?  109 LEU   A HD11 1 
ATOM   2442 H  HD12 . LEU   A 1 109 ? 21.839 -8.726  -3.817  1.00 15.37 ?  109 LEU   A HD12 1 
ATOM   2443 H  HD13 . LEU   A 1 109 ? 21.165 -7.825  -4.939  1.00 15.37 ?  109 LEU   A HD13 1 
ATOM   2444 H  HD21 . LEU   A 1 109 ? 18.559 -9.368  -4.669  1.00 16.20 ?  109 LEU   A HD21 1 
ATOM   2445 H  HD22 . LEU   A 1 109 ? 19.027 -8.950  -6.128  1.00 16.20 ?  109 LEU   A HD22 1 
ATOM   2446 H  HD23 . LEU   A 1 109 ? 18.772 -10.480 -5.784  1.00 16.20 ?  109 LEU   A HD23 1 
ATOM   2447 N  N    . LYS   A 1 110 ? 23.409 -12.522 -5.581  1.00 10.94 ?  110 LYS   A N    1 
ATOM   2448 C  CA   . LYS   A 1 110 ? 23.782 -13.644 -4.727  1.00 10.96 ?  110 LYS   A CA   1 
ATOM   2449 C  C    . LYS   A 1 110 ? 25.166 -13.426 -4.122  1.00 10.44 ?  110 LYS   A C    1 
ATOM   2450 O  O    . LYS   A 1 110 ? 25.360 -13.624 -2.919  1.00 10.76 ?  110 LYS   A O    1 
ATOM   2451 C  CB   . LYS   A 1 110 ? 23.701 -14.964 -5.497  1.00 11.98 ?  110 LYS   A CB   1 
ATOM   2452 C  CG   . LYS   A 1 110 ? 23.921 -16.179 -4.596  1.00 12.20 ?  110 LYS   A CG   1 
ATOM   2453 C  CD   . LYS   A 1 110 ? 23.665 -17.505 -5.301  1.00 12.75 ?  110 LYS   A CD   1 
ATOM   2454 C  CE   . LYS   A 1 110 ? 23.775 -18.686 -4.342  1.00 13.32 ?  110 LYS   A CE   1 
ATOM   2455 N  NZ   . LYS   A 1 110 ? 22.596 -18.806 -3.452  1.00 13.92 ?  110 LYS   A NZ   1 
ATOM   2456 H  H    . LYS   A 1 110 ? 23.304 -12.715 -6.412  1.00 13.11 ?  110 LYS   A H    1 
ATOM   2457 H  HA   . LYS   A 1 110 ? 23.146 -13.697 -3.994  1.00 13.13 ?  110 LYS   A HA   1 
ATOM   2458 H  HB2  . LYS   A 1 110 ? 22.821 -15.047 -5.900  1.00 14.36 ?  110 LYS   A HB2  1 
ATOM   2459 H  HB3  . LYS   A 1 110 ? 24.384 -14.976 -6.184  1.00 14.36 ?  110 LYS   A HB3  1 
ATOM   2460 H  HG2  . LYS   A 1 110 ? 24.837 -16.182 -4.281  1.00 14.62 ?  110 LYS   A HG2  1 
ATOM   2461 H  HG3  . LYS   A 1 110 ? 23.312 -16.129 -3.841  1.00 14.62 ?  110 LYS   A HG3  1 
ATOM   2462 H  HD2  . LYS   A 1 110 ? 22.778 -17.506 -5.677  1.00 15.29 ?  110 LYS   A HD2  1 
ATOM   2463 H  HD3  . LYS   A 1 110 ? 24.332 -17.626 -5.998  1.00 15.29 ?  110 LYS   A HD3  1 
ATOM   2464 H  HE2  . LYS   A 1 110 ? 23.851 -19.509 -4.852  1.00 15.96 ?  110 LYS   A HE2  1 
ATOM   2465 H  HE3  . LYS   A 1 110 ? 24.563 -18.575 -3.781  1.00 15.96 ?  110 LYS   A HE3  1 
ATOM   2466 H  HZ1  . LYS   A 1 110 ? 22.690 -19.500 -2.908  1.00 16.68 ?  110 LYS   A HZ1  1 
ATOM   2467 H  HZ2  . LYS   A 1 110 ? 22.508 -18.064 -2.965  1.00 16.68 ?  110 LYS   A HZ2  1 
ATOM   2468 H  HZ3  . LYS   A 1 110 ? 21.859 -18.915 -3.941  1.00 16.68 ?  110 LYS   A HZ3  1 
ATOM   2469 N  N    . SER   A 1 111 ? 26.127 -12.986 -4.937  1.00 10.54 ?  111 SER   A N    1 
ATOM   2470 C  CA   . SER   A 1 111 ? 27.461 -12.686 -4.421  1.00 10.70 ?  111 SER   A CA   1 
ATOM   2471 C  C    . SER   A 1 111 ? 27.401 -11.632 -3.320  1.00 10.45 ?  111 SER   A C    1 
ATOM   2472 O  O    . SER   A 1 111 ? 28.097 -11.733 -2.304  1.00 10.90 ?  111 SER   A O    1 
ATOM   2473 C  CB   . SER   A 1 111 ? 28.350 -12.202 -5.562  1.00 12.22 ?  111 SER   A CB   1 
ATOM   2474 O  OG   . SER   A 1 111 ? 28.435 -13.183 -6.582  1.00 14.09 ?  111 SER   A OG   1 
ATOM   2475 H  H    . SER   A 1 111 ? 26.024 -12.850 -5.780  1.00 12.63 ?  111 SER   A H    1 
ATOM   2476 H  HA   . SER   A 1 111 ? 27.847 -13.496 -4.053  1.00 12.83 ?  111 SER   A HA   1 
ATOM   2477 H  HB2  . SER   A 1 111 ? 27.965 -11.395 -5.941  1.00 14.65 ?  111 SER   A HB2  1 
ATOM   2478 H  HB3  . SER   A 1 111 ? 29.234 -12.016 -5.215  1.00 14.65 ?  111 SER   A HB3  1 
ATOM   2479 H  HG   . SER   A 1 111 ? 28.942 -12.904 -7.204  1.00 16.89 ?  111 SER   A HG   1 
ATOM   2480 N  N    . ALA   A 1 112 ? 26.553 -10.617 -3.499  1.00 10.57 ?  112 ALA   A N    1 
ATOM   2481 C  CA   . ALA   A 1 112 ? 26.408 -9.581  -2.480  1.00 10.60 ?  112 ALA   A CA   1 
ATOM   2482 C  C    . ALA   A 1 112 ? 25.926 -10.176 -1.158  1.00 10.28 ?  112 ALA   A C    1 
ATOM   2483 O  O    . ALA   A 1 112 ? 26.481 -9.889  -0.092  1.00 10.60 ?  112 ALA   A O    1 
ATOM   2484 C  CB   . ALA   A 1 112 ? 25.452 -8.493  -2.976  1.00 11.12 ?  112 ALA   A CB   1 
ATOM   2485 H  H    . ALA   A 1 112 ? 26.056 -10.505 -4.191  1.00 12.67 ?  112 ALA   A H    1 
ATOM   2486 H  HA   . ALA   A 1 112 ? 27.273 -9.165  -2.326  1.00 12.71 ?  112 ALA   A HA   1 
ATOM   2487 H  HB1  . ALA   A 1 112 ? 25.379 -7.798  -2.293  1.00 13.33 ?  112 ALA   A HB1  1 
ATOM   2488 H  HB2  . ALA   A 1 112 ? 25.805 -8.102  -3.792  1.00 13.33 ?  112 ALA   A HB2  1 
ATOM   2489 H  HB3  . ALA   A 1 112 ? 24.582 -8.879  -3.142  1.00 13.33 ?  112 ALA   A HB3  1 
ATOM   2490 N  N    . TYR   A 1 113 ? 24.884 -11.008 -1.206  1.00 10.17 ?  113 TYR   A N    1 
ATOM   2491 C  CA   . TYR   A 1 113 ? 24.376 -11.618 0.020   1.00 10.22 ?  113 TYR   A CA   1 
ATOM   2492 C  C    . TYR   A 1 113 ? 25.380 -12.572 0.665   1.00 9.82  ?  113 TYR   A C    1 
ATOM   2493 O  O    . TYR   A 1 113 ? 25.342 -12.751 1.885   1.00 10.67 ?  113 TYR   A O    1 
ATOM   2494 C  CB   . TYR   A 1 113 ? 23.047 -12.332 -0.247  1.00 10.79 ?  113 TYR   A CB   1 
ATOM   2495 C  CG   . TYR   A 1 113 ? 21.839 -11.424 -0.161  1.00 10.31 ?  113 TYR   A CG   1 
ATOM   2496 C  CD1  . TYR   A 1 113 ? 21.490 -10.813 1.041   1.00 10.56 ?  113 TYR   A CD1  1 
ATOM   2497 C  CD2  . TYR   A 1 113 ? 21.033 -11.201 -1.268  1.00 10.49 ?  113 TYR   A CD2  1 
ATOM   2498 C  CE1  . TYR   A 1 113 ? 20.373 -10.005 1.135   1.00 10.64 ?  113 TYR   A CE1  1 
ATOM   2499 C  CE2  . TYR   A 1 113 ? 19.895 -10.391 -1.182  1.00 10.80 ?  113 TYR   A CE2  1 
ATOM   2500 C  CZ   . TYR   A 1 113 ? 19.578 -9.798  0.026   1.00 10.79 ?  113 TYR   A CZ   1 
ATOM   2501 O  OH   . TYR   A 1 113 ? 18.459 -8.996  0.149   1.00 11.36 ?  113 TYR   A OH   1 
ATOM   2502 H  H    . TYR   A 1 113 ? 24.468 -11.229 -1.924  1.00 12.19 ?  113 TYR   A H    1 
ATOM   2503 H  HA   . TYR   A 1 113 ? 24.203 -10.911 0.658   1.00 12.24 ?  113 TYR   A HA   1 
ATOM   2504 H  HB2  . TYR   A 1 113 ? 23.066 -12.708 -1.143  1.00 12.93 ?  113 TYR   A HB2  1 
ATOM   2505 H  HB3  . TYR   A 1 113 ? 22.934 -13.038 0.403   1.00 12.93 ?  113 TYR   A HB3  1 
ATOM   2506 H  HD1  . TYR   A 1 113 ? 22.020 -10.957 1.795   1.00 12.65 ?  113 TYR   A HD1  1 
ATOM   2507 H  HD2  . TYR   A 1 113 ? 21.239 -11.610 -2.077  1.00 12.57 ?  113 TYR   A HD2  1 
ATOM   2508 H  HE1  . TYR   A 1 113 ? 20.154 -9.605  1.945   1.00 12.75 ?  113 TYR   A HE1  1 
ATOM   2509 H  HE2  . TYR   A 1 113 ? 19.350 -10.244 -1.928  1.00 12.94 ?  113 TYR   A HE2  1 
ATOM   2510 H  HH   . TYR   A 1 113 ? 18.063 -8.951  -0.595  1.00 13.61 ?  113 TYR   A HH   1 
ATOM   2511 N  N    . GLU   A 1 114 ? 26.277 -13.193 -0.118  1.00 10.03 ?  114 GLU   A N    1 
ATOM   2512 C  CA   . GLU   A 1 114 ? 27.270 -14.090 0.475   1.00 10.36 ?  114 GLU   A CA   1 
ATOM   2513 C  C    . GLU   A 1 114 ? 28.118 -13.381 1.522   1.00 10.53 ?  114 GLU   A C    1 
ATOM   2514 O  O    . GLU   A 1 114 ? 28.591 -14.015 2.473   1.00 10.84 ?  114 GLU   A O    1 
ATOM   2515 C  CB   . GLU   A 1 114 ? 28.141 -14.728 -0.617  1.00 10.38 ?  114 GLU   A CB   1 
ATOM   2516 C  CG   . GLU   A 1 114 ? 27.376 -15.790 -1.391  1.00 10.87 ?  114 GLU   A CG   1 
ATOM   2517 C  CD   . GLU   A 1 114 ? 28.080 -16.320 -2.631  1.00 11.34 ?  114 GLU   A CD   1 
ATOM   2518 O  OE1  . GLU   A 1 114 ? 29.034 -15.685 -3.137  1.00 11.65 ?  114 GLU   A OE1  1 
ATOM   2519 O  OE2  . GLU   A 1 114 ? 27.634 -17.381 -3.117  1.00 12.57 -1 114 GLU   A OE2  1 
ATOM   2520 H  H    . GLU   A 1 114 ? 26.331 -13.106 -0.982  1.00 12.02 ?  114 GLU   A H    1 
ATOM   2521 H  HA   . GLU   A 1 114 ? 26.801 -14.807 0.917   1.00 12.42 ?  114 GLU   A HA   1 
ATOM   2522 H  HB2  . GLU   A 1 114 ? 28.424 -14.045 -1.249  1.00 12.44 ?  114 GLU   A HB2  1 
ATOM   2523 H  HB3  . GLU   A 1 114 ? 28.910 -15.150 -0.212  1.00 12.44 ?  114 GLU   A HB3  1 
ATOM   2524 H  HG2  . GLU   A 1 114 ? 27.212 -16.543 -0.804  1.00 13.02 ?  114 GLU   A HG2  1 
ATOM   2525 H  HG3  . GLU   A 1 114 ? 26.525 -15.413 -1.677  1.00 13.02 ?  114 GLU   A HG3  1 
ATOM   2526 N  N    . ASN   A 1 115 ? 28.298 -12.063 1.394   1.00 10.25 ?  115 ASN   A N    1 
ATOM   2527 C  CA   . ASN   A 1 115 ? 29.075 -11.341 2.400   1.00 10.66 ?  115 ASN   A CA   1 
ATOM   2528 C  C    . ASN   A 1 115 ? 28.462 -11.469 3.788   1.00 9.98  ?  115 ASN   A C    1 
ATOM   2529 O  O    . ASN   A 1 115 ? 29.174 -11.399 4.796   1.00 10.83 ?  115 ASN   A O    1 
ATOM   2530 C  CB   . ASN   A 1 115 ? 29.194 -9.866  2.024   1.00 10.70 ?  115 ASN   A CB   1 
ATOM   2531 C  CG   . ASN   A 1 115 ? 29.987 -9.655  0.755   1.00 11.41 ?  115 ASN   A CG   1 
ATOM   2532 O  OD1  . ASN   A 1 115 ? 31.207 -9.771  0.757   1.00 14.94 ?  115 ASN   A OD1  1 
ATOM   2533 N  ND2  . ASN   A 1 115 ? 29.304 -9.343  -0.332  1.00 11.04 ?  115 ASN   A ND2  1 
ATOM   2534 H  H    . ASN   A 1 115 ? 27.991 -11.573 0.751   1.00 12.29 ?  115 ASN   A H    1 
ATOM   2535 H  HA   . ASN   A 1 115 ? 29.969 -11.710 2.434   1.00 12.77 ?  115 ASN   A HA   1 
ATOM   2536 H  HB2  . ASN   A 1 115 ? 28.306 -9.495  1.897   1.00 12.83 ?  115 ASN   A HB2  1 
ATOM   2537 H  HB3  . ASN   A 1 115 ? 29.646 -9.391  2.746   1.00 12.83 ?  115 ASN   A HB3  1 
ATOM   2538 H  HD21 . ASN   A 1 115 ? 29.712 -9.215  -1.075  1.00 13.23 ?  115 ASN   A HD21 1 
ATOM   2539 H  HD22 . ASN   A 1 115 ? 28.444 -9.290  -0.298  1.00 13.23 ?  115 ASN   A HD22 1 
ATOM   2540 N  N    . PHE   A 1 116 ? 27.137 -11.640 3.865   1.00 10.15 ?  116 PHE   A N    1 
ATOM   2541 C  CA   . PHE   A 1 116 ? 26.485 -11.725 5.168   1.00 10.19 ?  116 PHE   A CA   1 
ATOM   2542 C  C    . PHE   A 1 116 ? 26.952 -12.956 5.943   1.00 10.60 ?  116 PHE   A C    1 
ATOM   2543 O  O    . PHE   A 1 116 ? 26.879 -12.974 7.171   1.00 11.05 ?  116 PHE   A O    1 
ATOM   2544 C  CB   . PHE   A 1 116 ? 24.956 -11.846 5.035   1.00 10.31 ?  116 PHE   A CB   1 
ATOM   2545 C  CG   . PHE   A 1 116 ? 24.206 -10.602 4.563   1.00 10.15 ?  116 PHE   A CG   1 
ATOM   2546 C  CD1  . PHE   A 1 116 ? 24.780 -9.584  3.809   1.00 10.43 ?  116 PHE   A CD1  1 
ATOM   2547 C  CD2  . PHE   A 1 116 ? 22.853 -10.495 4.877   1.00 10.82 ?  116 PHE   A CD2  1 
ATOM   2548 C  CE1  . PHE   A 1 116 ? 24.010 -8.505  3.386   1.00 10.63 ?  116 PHE   A CE1  1 
ATOM   2549 C  CE2  . PHE   A 1 116 ? 22.092 -9.422  4.465   1.00 10.80 ?  116 PHE   A CE2  1 
ATOM   2550 C  CZ   . PHE   A 1 116 ? 22.659 -8.432  3.717   1.00 10.25 ?  116 PHE   A CZ   1 
ATOM   2551 H  H    . PHE   A 1 116 ? 26.602 -11.704 3.188   1.00 12.16 ?  116 PHE   A H    1 
ATOM   2552 H  HA   . PHE   A 1 116 ? 26.690 -10.931 5.686   1.00 12.21 ?  116 PHE   A HA   1 
ATOM   2553 H  HB2  . PHE   A 1 116 ? 24.766 -12.556 4.401   1.00 12.35 ?  116 PHE   A HB2  1 
ATOM   2554 H  HB3  . PHE   A 1 116 ? 24.599 -12.088 5.902   1.00 12.35 ?  116 PHE   A HB3  1 
ATOM   2555 H  HD1  . PHE   A 1 116 ? 25.676 -9.643  3.575   1.00 12.50 ?  116 PHE   A HD1  1 
ATOM   2556 H  HD2  . PHE   A 1 116 ? 22.447 -11.175 5.376   1.00 12.97 ?  116 PHE   A HD2  1 
ATOM   2557 H  HE1  . PHE   A 1 116 ? 24.402 -7.829  2.885   1.00 12.74 ?  116 PHE   A HE1  1 
ATOM   2558 H  HE2  . PHE   A 1 116 ? 21.188 -9.383  4.695   1.00 12.94 ?  116 PHE   A HE2  1 
ATOM   2559 H  HZ   . PHE   A 1 116 ? 22.149 -7.703  3.450   1.00 12.29 ?  116 PHE   A HZ   1 
ATOM   2560 N  N    . ASN   A 1 117 ? 27.399 -14.006 5.244   1.00 10.90 ?  117 ASN   A N    1 
ATOM   2561 C  CA   . ASN   A 1 117 ? 27.762 -15.252 5.918   1.00 11.05 ?  117 ASN   A CA   1 
ATOM   2562 C  C    . ASN   A 1 117 ? 29.025 -15.134 6.752   1.00 11.57 ?  117 ASN   A C    1 
ATOM   2563 O  O    . ASN   A 1 117 ? 29.326 -16.056 7.520   1.00 12.43 ?  117 ASN   A O    1 
ATOM   2564 C  CB   . ASN   A 1 117 ? 27.874 -16.381 4.901   1.00 11.29 ?  117 ASN   A CB   1 
ATOM   2565 C  CG   . ASN   A 1 117 ? 26.521 -16.757 4.359   1.00 11.08 ?  117 ASN   A CG   1 
ATOM   2566 O  OD1  . ASN   A 1 117 ? 25.547 -16.780 5.105   1.00 12.12 ?  117 ASN   A OD1  1 
ATOM   2567 N  ND2  . ASN   A 1 117 ? 26.439 -17.016 3.071   1.00 10.99 ?  117 ASN   A ND2  1 
ATOM   2568 H  H    . ASN   A 1 117 ? 27.482 -14.026 4.384   1.00 13.06 ?  117 ASN   A H    1 
ATOM   2569 H  HA   . ASN   A 1 117 ? 27.038 -15.482 6.523   1.00 13.25 ?  117 ASN   A HA   1 
ATOM   2570 H  HB2  . ASN   A 1 117 ? 28.429 -16.095 4.160   1.00 13.53 ?  117 ASN   A HB2  1 
ATOM   2571 H  HB3  . ASN   A 1 117 ? 28.255 -17.161 5.331   1.00 13.53 ?  117 ASN   A HB3  1 
ATOM   2572 H  HD21 . ASN   A 1 117 ? 25.682 -17.228 2.730   1.00 13.17 ?  117 ASN   A HD21 1 
ATOM   2573 H  HD22 . ASN   A 1 117 ? 27.143 -16.981 2.583   1.00 13.17 ?  117 ASN   A HD22 1 
ATOM   2574 N  N    . GLN   A 1 118 ? 29.754 -14.024 6.633   1.00 11.49 ?  118 GLN   A N    1 
ATOM   2575 C  CA   . GLN   A 1 118 ? 30.931 -13.788 7.456   1.00 12.21 ?  118 GLN   A CA   1 
ATOM   2576 C  C    . GLN   A 1 118 ? 30.588 -13.207 8.823   1.00 12.28 ?  118 GLN   A C    1 
ATOM   2577 O  O    . GLN   A 1 118 ? 31.506 -12.919 9.603   1.00 13.83 ?  118 GLN   A O    1 
ATOM   2578 C  CB   . GLN   A 1 118 ? 31.924 -12.886 6.717   1.00 12.30 ?  118 GLN   A CB   1 
ATOM   2579 C  CG   . GLN   A 1 118 ? 32.397 -13.461 5.393   1.00 12.56 ?  118 GLN   A CG   1 
ATOM   2580 C  CD   . GLN   A 1 118 ? 33.229 -14.726 5.569   1.00 12.78 ?  118 GLN   A CD   1 
ATOM   2581 O  OE1  . GLN   A 1 118 ? 34.092 -14.797 6.453   1.00 13.47 ?  118 GLN   A OE1  1 
ATOM   2582 N  NE2  . GLN   A 1 118 ? 32.980 -15.721 4.719   1.00 12.85 ?  118 GLN   A NE2  1 
ATOM   2583 H  H    . GLN   A 1 118 ? 29.573 -13.382 6.083   1.00 13.77 ?  118 GLN   A H    1 
ATOM   2584 H  HA   . GLN   A 1 118 ? 31.363 -14.644 7.605   1.00 14.63 ?  118 GLN   A HA   1 
ATOM   2585 H  HB2  . GLN   A 1 118 ? 31.501 -12.034 6.540   1.00 14.74 ?  118 GLN   A HB2  1 
ATOM   2586 H  HB3  . GLN   A 1 118 ? 32.703 -12.758 7.282   1.00 14.74 ?  118 GLN   A HB3  1 
ATOM   2587 H  HG2  . GLN   A 1 118 ? 31.626 -13.678 4.844   1.00 15.06 ?  118 GLN   A HG2  1 
ATOM   2588 H  HG3  . GLN   A 1 118 ? 32.949 -12.804 4.940   1.00 15.06 ?  118 GLN   A HG3  1 
ATOM   2589 H  HE21 . GLN   A 1 118 ? 32.364 -15.629 4.113   1.00 15.41 ?  118 GLN   A HE21 1 
ATOM   2590 H  HE22 . GLN   A 1 118 ? 33.414 -16.457 4.770   1.00 15.41 ?  118 GLN   A HE22 1 
ATOM   2591 N  N    . HIS   A 1 119 ? 29.297 -13.049 9.131   1.00 11.79 ?  119 HIS   A N    1 
ATOM   2592 C  CA   . HIS   A 1 119 ? 28.839 -12.438 10.374  1.00 12.22 ?  119 HIS   A CA   1 
ATOM   2593 C  C    . HIS   A 1 119 ? 27.698 -13.257 10.950  1.00 12.39 ?  119 HIS   A C    1 
ATOM   2594 O  O    . HIS   A 1 119 ? 26.757 -13.605 10.232  1.00 12.84 ?  119 HIS   A O    1 
ATOM   2595 C  CB   . HIS   A 1 119 ? 28.385 -11.007 10.093  1.00 12.88 ?  119 HIS   A CB   1 
ATOM   2596 C  CG   . HIS   A 1 119 ? 29.469 -10.194 9.482   1.00 14.17 ?  119 HIS   A CG   1 
ATOM   2597 N  ND1  . HIS   A 1 119 ? 30.435 -9.574  10.240  1.00 16.33 ?  119 HIS   A ND1  1 
ATOM   2598 C  CD2  . HIS   A 1 119 ? 29.815 -10.003 8.189   1.00 15.23 ?  119 HIS   A CD2  1 
ATOM   2599 C  CE1  . HIS   A 1 119 ? 31.306 -8.991  9.435   1.00 16.52 ?  119 HIS   A CE1  1 
ATOM   2600 N  NE2  . HIS   A 1 119 ? 30.961 -9.247  8.186   1.00 16.54 ?  119 HIS   A NE2  1 
ATOM   2601 H  H    . HIS   A 1 119 ? 28.647 -13.304 8.623   1.00 14.13 ?  119 HIS   A H    1 
ATOM   2602 H  HA   . HIS   A 1 119 ? 29.569 -12.422 11.016  1.00 14.65 ?  119 HIS   A HA   1 
ATOM   2603 H  HB2  . HIS   A 1 119 ? 27.633 -11.034 9.479   1.00 15.44 ?  119 HIS   A HB2  1 
ATOM   2604 H  HB3  . HIS   A 1 119 ? 28.122 -10.594 10.928  1.00 15.44 ?  119 HIS   A HB3  1 
ATOM   2605 H  HD2  . HIS   A 1 119 ? 29.361 -10.327 7.440   1.00 18.26 ?  119 HIS   A HD2  1 
ATOM   2606 H  HE1  . HIS   A 1 119 ? 32.040 -8.489  9.701   1.00 19.81 ?  119 HIS   A HE1  1 
ATOM   2607 H  HE2  . HIS   A 1 119 ? 31.368 -8.960  7.483   1.00 19.83 ?  119 HIS   A HE2  1 
ATOM   2608 N  N    . GLU   A 1 120 ? 27.775 -13.551 12.249  1.00 13.41 ?  120 GLU   A N    1 
ATOM   2609 C  CA   . GLU   A 1 120 ? 26.816 -14.477 12.850  1.00 15.29 ?  120 GLU   A CA   1 
ATOM   2610 C  C    . GLU   A 1 120 ? 25.401 -13.911 12.902  1.00 13.71 ?  120 GLU   A C    1 
ATOM   2611 O  O    . GLU   A 1 120 ? 24.428 -14.676 12.791  1.00 13.79 ?  120 GLU   A O    1 
ATOM   2612 C  CB   . GLU   A 1 120 ? 27.285 -14.875 14.252  1.00 19.90 ?  120 GLU   A CB   1 
ATOM   2613 C  CG   . GLU   A 1 120 ? 28.478 -15.817 14.259  1.00 26.51 ?  120 GLU   A CG   1 
ATOM   2614 C  CD   . GLU   A 1 120 ? 28.645 -16.532 15.584  1.00 32.78 ?  120 GLU   A CD   1 
ATOM   2615 O  OE1  . GLU   A 1 120 ? 28.208 -15.982 16.617  1.00 34.55 ?  120 GLU   A OE1  1 
ATOM   2616 O  OE2  . GLU   A 1 120 ? 29.210 -17.647 15.591  1.00 35.87 -1 120 GLU   A OE2  1 
ATOM   2617 H  H    . GLU   A 1 120 ? 28.367 -13.235 12.794  1.00 16.08 ?  120 GLU   A H    1 
ATOM   2618 H  HA   . GLU   A 1 120 ? 26.793 -15.285 12.321  1.00 18.33 ?  120 GLU   A HA   1 
ATOM   2619 H  HB2  . GLU   A 1 120 ? 27.543 -14.080 14.746  1.00 23.86 ?  120 GLU   A HB2  1 
ATOM   2620 H  HB3  . GLU   A 1 120 ? 26.558 -15.324 14.717  1.00 23.86 ?  120 GLU   A HB3  1 
ATOM   2621 H  HG2  . GLU   A 1 120 ? 28.363 -16.484 13.564  1.00 31.80 ?  120 GLU   A HG2  1 
ATOM   2622 H  HG3  . GLU   A 1 120 ? 29.289 -15.311 14.109  1.00 31.80 ?  120 GLU   A HG3  1 
ATOM   2623 N  N    . VAL   A 1 121 ? 25.270 -12.598 13.107  1.00 13.21 ?  121 VAL   A N    1 
ATOM   2624 C  CA   . VAL   A 1 121 ? 23.976 -11.929 13.225  1.00 13.00 ?  121 VAL   A CA   1 
ATOM   2625 C  C    . VAL   A 1 121 ? 24.086 -10.550 12.583  1.00 11.92 ?  121 VAL   A C    1 
ATOM   2626 O  O    . VAL   A 1 121 ? 25.051 -9.821  12.831  1.00 12.68 ?  121 VAL   A O    1 
ATOM   2627 C  CB   . VAL   A 1 121 ? 23.538 -11.778 14.701  1.00 16.09 ?  121 VAL   A CB   1 
ATOM   2628 C  CG1  . VAL   A 1 121 ? 22.145 -11.173 14.787  1.00 16.33 ?  121 VAL   A CG1  1 
ATOM   2629 C  CG2  . VAL   A 1 121 ? 23.575 -13.104 15.442  1.00 18.63 ?  121 VAL   A CG2  1 
ATOM   2630 H  H    . VAL   A 1 121 ? 25.937 -12.057 13.187  1.00 15.84 ?  121 VAL   A H    1 
ATOM   2631 H  HA   . VAL   A 1 121 ? 23.302 -12.444 12.756  1.00 15.58 ?  121 VAL   A HA   1 
ATOM   2632 H  HB   . VAL   A 1 121 ? 24.146 -11.175 15.152  1.00 19.30 ?  121 VAL   A HB   1 
ATOM   2633 H  HG11 . VAL   A 1 121 ? 21.831 -11.224 15.705  1.00 19.58 ?  121 VAL   A HG11 1 
ATOM   2634 H  HG12 . VAL   A 1 121 ? 22.181 -10.246 14.504  1.00 19.58 ?  121 VAL   A HG12 1 
ATOM   2635 H  HG13 . VAL   A 1 121 ? 21.545 -11.673 14.209  1.00 19.58 ?  121 VAL   A HG13 1 
ATOM   2636 H  HG21 . VAL   A 1 121 ? 23.218 -12.976 16.341  1.00 22.34 ?  121 VAL   A HG21 1 
ATOM   2637 H  HG22 . VAL   A 1 121 ? 23.027 -13.750 14.966  1.00 22.34 ?  121 VAL   A HG22 1 
ATOM   2638 H  HG23 . VAL   A 1 121 ? 24.488 -13.415 15.493  1.00 22.34 ?  121 VAL   A HG23 1 
ATOM   2639 N  N    . LEU   A 1 122 ? 23.081 -10.169 11.788  1.00 11.33 ?  122 LEU   A N    1 
ATOM   2640 C  CA   . LEU   A 1 122 ? 23.082 -8.877  11.105  1.00 10.85 ?  122 LEU   A CA   1 
ATOM   2641 C  C    . LEU   A 1 122 ? 21.680 -8.287  11.085  1.00 10.95 ?  122 LEU   A C    1 
ATOM   2642 O  O    . LEU   A 1 122 ? 20.691 -9.009  10.951  1.00 11.85 ?  122 LEU   A O    1 
ATOM   2643 C  CB   . LEU   A 1 122 ? 23.498 -8.989  9.632   1.00 12.17 ?  122 LEU   A CB   1 
ATOM   2644 C  CG   . LEU   A 1 122 ? 24.717 -9.837  9.295   1.00 12.39 ?  122 LEU   A CG   1 
ATOM   2645 C  CD1  . LEU   A 1 122 ? 24.332 -11.289 9.061   1.00 13.51 ?  122 LEU   A CD1  1 
ATOM   2646 C  CD2  . LEU   A 1 122 ? 25.423 -9.267  8.084   1.00 12.35 ?  122 LEU   A CD2  1 
ATOM   2647 H  H    . LEU   A 1 122 ? 22.379 -10.643 11.627  1.00 13.58 ?  122 LEU   A H    1 
ATOM   2648 H  HA   . LEU   A 1 122 ? 23.681 -8.260  11.557  1.00 13.01 ?  122 LEU   A HA   1 
ATOM   2649 H  HB2  . LEU   A 1 122 ? 22.759 -9.364  9.137   1.00 14.58 ?  122 LEU   A HB2  1 
ATOM   2650 H  HB3  . LEU   A 1 122 ? 23.687 -8.098  9.303   1.00 14.58 ?  122 LEU   A HB3  1 
ATOM   2651 H  HG   . LEU   A 1 122 ? 25.347 -9.817  10.033  1.00 14.85 ?  122 LEU   A HG   1 
ATOM   2652 H  HD11 . LEU   A 1 122 ? 25.122 -11.800 8.819   1.00 16.19 ?  122 LEU   A HD11 1 
ATOM   2653 H  HD12 . LEU   A 1 122 ? 23.946 -11.648 9.876   1.00 16.19 ?  122 LEU   A HD12 1 
ATOM   2654 H  HD13 . LEU   A 1 122 ? 23.681 -11.332 8.342   1.00 16.19 ?  122 LEU   A HD13 1 
ATOM   2655 H  HD21 . LEU   A 1 122 ? 26.174 -9.837  7.844   1.00 14.80 ?  122 LEU   A HD21 1 
ATOM   2656 H  HD22 . LEU   A 1 122 ? 24.799 -9.218  7.343   1.00 14.80 ?  122 LEU   A HD22 1 
ATOM   2657 H  HD23 . LEU   A 1 122 ? 25.749 -8.375  8.297   1.00 14.80 ?  122 LEU   A HD23 1 
ATOM   2658 N  N    . LEU   A 1 123 ? 21.617 -6.955  11.174  1.00 10.74 ?  123 LEU   A N    1 
ATOM   2659 C  CA   . LEU   A 1 123 ? 20.450 -6.158  10.803  1.00 10.55 ?  123 LEU   A CA   1 
ATOM   2660 C  C    . LEU   A 1 123 ? 20.698 -5.647  9.391   1.00 9.98  ?  123 LEU   A C    1 
ATOM   2661 O  O    . LEU   A 1 123 ? 21.755 -5.062  9.134   1.00 10.68 ?  123 LEU   A O    1 
ATOM   2662 C  CB   . LEU   A 1 123 ? 20.331 -4.973  11.765  1.00 10.92 ?  123 LEU   A CB   1 
ATOM   2663 C  CG   . LEU   A 1 123 ? 19.283 -3.917  11.420  1.00 11.91 ?  123 LEU   A CG   1 
ATOM   2664 C  CD1  . LEU   A 1 123 ? 17.883 -4.509  11.427  1.00 12.50 ?  123 LEU   A CD1  1 
ATOM   2665 C  CD2  . LEU   A 1 123 ? 19.386 -2.735  12.382  1.00 12.73 ?  123 LEU   A CD2  1 
ATOM   2666 H  H    . LEU   A 1 123 ? 22.271 -6.469  11.456  1.00 12.87 ?  123 LEU   A H    1 
ATOM   2667 H  HA   . LEU   A 1 123 ? 19.638 -6.695  10.835  1.00 12.64 ?  123 LEU   A HA   1 
ATOM   2668 H  HB2  . LEU   A 1 123 ? 20.107 -5.312  12.647  1.00 13.09 ?  123 LEU   A HB2  1 
ATOM   2669 H  HB3  . LEU   A 1 123 ? 21.184 -4.521  11.801  1.00 13.09 ?  123 LEU   A HB3  1 
ATOM   2670 H  HG   . LEU   A 1 123 ? 19.450 -3.577  10.527  1.00 14.28 ?  123 LEU   A HG   1 
ATOM   2671 H  HD11 . LEU   A 1 123 ? 17.235 -3.810  11.255  1.00 14.98 ?  123 LEU   A HD11 1 
ATOM   2672 H  HD12 . LEU   A 1 123 ? 17.823 -5.193  10.741  1.00 14.98 ?  123 LEU   A HD12 1 
ATOM   2673 H  HD13 . LEU   A 1 123 ? 17.712 -4.907  12.300  1.00 14.98 ?  123 LEU   A HD13 1 
ATOM   2674 H  HD21 . LEU   A 1 123 ? 18.711 -2.076  12.152  1.00 15.25 ?  123 LEU   A HD21 1 
ATOM   2675 H  HD22 . LEU   A 1 123 ? 19.232 -3.055  13.290  1.00 15.25 ?  123 LEU   A HD22 1 
ATOM   2676 H  HD23 . LEU   A 1 123 ? 20.268 -2.347  12.315  1.00 15.25 ?  123 LEU   A HD23 1 
ATOM   2677 N  N    A ALA   A 1 124 ? 19.726 -5.811  8.495   0.62 9.35  ?  124 ALA   A N    1 
ATOM   2678 N  N    B ALA   A 1 124 ? 19.765 -5.905  8.469   0.38 10.18 ?  124 ALA   A N    1 
ATOM   2679 C  CA   A ALA   A 1 124 ? 20.006 -5.523  7.098   0.62 8.94  ?  124 ALA   A CA   1 
ATOM   2680 C  CA   B ALA   A 1 124 ? 20.066 -5.696  7.058   0.38 10.52 ?  124 ALA   A CA   1 
ATOM   2681 C  C    A ALA   A 1 124 ? 18.758 -5.049  6.372   0.62 9.00  ?  124 ALA   A C    1 
ATOM   2682 C  C    B ALA   A 1 124 ? 18.850 -5.233  6.267   0.38 10.01 ?  124 ALA   A C    1 
ATOM   2683 O  O    A ALA   A 1 124 ? 17.630 -5.368  6.775   0.62 9.67  ?  124 ALA   A O    1 
ATOM   2684 O  O    B ALA   A 1 124 ? 17.712 -5.578  6.612   0.38 10.24 ?  124 ALA   A O    1 
ATOM   2685 C  CB   A ALA   A 1 124 ? 20.572 -6.756  6.383   0.62 9.52  ?  124 ALA   A CB   1 
ATOM   2686 C  CB   B ALA   A 1 124 ? 20.649 -6.965  6.414   0.38 11.01 ?  124 ALA   A CB   1 
ATOM   2687 H  H    A ALA   A 1 124 ? 18.924 -6.080  8.671   0.62 11.20 ?  124 ALA   A H    1 
ATOM   2688 H  H    B ALA   A 1 124 ? 18.971 -6.202  8.633   0.38 12.20 ?  124 ALA   A H    1 
ATOM   2689 H  HA   A ALA   A 1 124 ? 20.667 -4.815  7.065   0.62 10.71 ?  124 ALA   A HA   1 
ATOM   2690 H  HA   B ALA   A 1 124 ? 20.735 -5.009  6.998   0.38 12.61 ?  124 ALA   A HA   1 
ATOM   2691 H  HB1  A ALA   A 1 124 ? 20.750 -6.532  5.456   0.62 11.41 ?  124 ALA   A HB1  1 
ATOM   2692 H  HB1  B ALA   A 1 124 ? 20.839 -6.789  5.477   0.38 13.20 ?  124 ALA   A HB1  1 
ATOM   2693 H  HB2  A ALA   A 1 124 ? 21.399 -7.021  6.821   0.62 11.41 ?  124 ALA   A HB2  1 
ATOM   2694 H  HB2  B ALA   A 1 124 ? 21.474 -7.204  6.873   0.38 13.20 ?  124 ALA   A HB2  1 
ATOM   2695 H  HB3  A ALA   A 1 124 ? 19.928 -7.478  6.433   0.62 11.41 ?  124 ALA   A HB3  1 
ATOM   2696 H  HB3  B ALA   A 1 124 ? 20.011 -7.690  6.490   0.38 13.20 ?  124 ALA   A HB3  1 
ATOM   2697 N  N    A PRO   A 1 125 ? 18.934 -4.308  5.280   0.62 9.41  ?  125 PRO   A N    1 
ATOM   2698 N  N    B PRO   A 1 125 ? 19.065 -4.482  5.187   0.38 8.62  ?  125 PRO   A N    1 
ATOM   2699 C  CA   A PRO   A 1 125 ? 17.873 -4.092  4.298   0.62 10.32 ?  125 PRO   A CA   1 
ATOM   2700 C  CA   B PRO   A 1 125 ? 17.982 -4.115  4.276   0.38 8.91  ?  125 PRO   A CA   1 
ATOM   2701 C  C    A PRO   A 1 125 ? 17.935 -5.170  3.219   0.62 10.04 ?  125 PRO   A C    1 
ATOM   2702 C  C    B PRO   A 1 125 ? 17.934 -5.120  3.128   0.38 9.45  ?  125 PRO   A C    1 
ATOM   2703 O  O    A PRO   A 1 125 ? 18.896 -5.939  3.124   0.62 10.39 ?  125 PRO   A O    1 
ATOM   2704 O  O    B PRO   A 1 125 ? 18.814 -5.972  2.981   0.38 9.98  ?  125 PRO   A O    1 
ATOM   2705 C  CB   A PRO   A 1 125 ? 18.290 -2.744  3.694   0.62 10.88 ?  125 PRO   A CB   1 
ATOM   2706 C  CB   B PRO   A 1 125 ? 18.466 -2.757  3.755   0.38 8.17  ?  125 PRO   A CB   1 
ATOM   2707 C  CG   A PRO   A 1 125 ? 19.796 -2.873  3.627   0.62 11.19 ?  125 PRO   A CG   1 
ATOM   2708 C  CG   B PRO   A 1 125 ? 19.962 -2.976  3.610   0.38 7.94  ?  125 PRO   A CG   1 
ATOM   2709 C  CD   A PRO   A 1 125 ? 20.177 -3.601  4.901   0.62 10.30 ?  125 PRO   A CD   1 
ATOM   2710 C  CD   B PRO   A 1 125 ? 20.358 -3.932  4.724   0.38 7.36  ?  125 PRO   A CD   1 
ATOM   2711 H  HA   A PRO   A 1 125 ? 16.994 -4.049  4.700   0.62 12.37 ?  125 PRO   A HA   1 
ATOM   2712 H  HA   B PRO   A 1 125 ? 17.137 -4.032  4.745   0.38 10.67 ?  125 PRO   A HA   1 
ATOM   2713 H  HB2  A PRO   A 1 125 ? 17.903 -2.638  2.811   0.62 13.04 ?  125 PRO   A HB2  1 
ATOM   2714 H  HB2  B PRO   A 1 125 ? 18.050 -2.566  2.898   0.38 9.79  ?  125 PRO   A HB2  1 
ATOM   2715 H  HB3  A PRO   A 1 125 ? 18.022 -2.021  4.284   0.62 13.04 ?  125 PRO   A HB3  1 
ATOM   2716 H  HB3  B PRO   A 1 125 ? 18.267 -2.060  4.403   0.38 9.79  ?  125 PRO   A HB3  1 
ATOM   2717 H  HG2  A PRO   A 1 125 ? 20.052 -3.395  2.848   0.62 13.41 ?  125 PRO   A HG2  1 
ATOM   2718 H  HG2  B PRO   A 1 125 ? 20.150 -3.369  2.743   0.38 9.52  ?  125 PRO   A HG2  1 
ATOM   2719 H  HG3  A PRO   A 1 125 ? 20.204 -1.993  3.598   0.62 13.41 ?  125 PRO   A HG3  1 
ATOM   2720 H  HG3  B PRO   A 1 125 ? 20.426 -2.131  3.708   0.38 9.52  ?  125 PRO   A HG3  1 
ATOM   2721 H  HD2  A PRO   A 1 125 ? 20.894 -4.229  4.735   0.62 12.34 ?  125 PRO   A HD2  1 
ATOM   2722 H  HD2  B PRO   A 1 125 ? 20.936 -4.636  4.373   0.38 8.81  ?  125 PRO   A HD2  1 
ATOM   2723 H  HD3  A PRO   A 1 125 ? 20.420 -2.960  5.594   0.62 12.34 ?  125 PRO   A HD3  1 
ATOM   2724 H  HD3  B PRO   A 1 125 ? 20.797 -3.446  5.440   0.38 8.81  ?  125 PRO   A HD3  1 
ATOM   2725 N  N    A LEU   A 1 126 ? 16.898 -5.195  2.383   0.62 9.65  ?  126 LEU   A N    1 
ATOM   2726 N  N    B LEU   A 1 126 ? 16.905 -4.991  2.290   0.38 9.86  ?  126 LEU   A N    1 
ATOM   2727 C  CA   A LEU   A 1 126 ? 16.928 -6.018  1.180   0.62 10.33 ?  126 LEU   A CA   1 
ATOM   2728 C  CA   B LEU   A 1 126 ? 16.832 -5.810  1.084   0.38 9.87  ?  126 LEU   A CA   1 
ATOM   2729 C  C    A LEU   A 1 126 ? 17.864 -5.392  0.152   0.62 10.21 ?  126 LEU   A C    1 
ATOM   2730 C  C    B LEU   A 1 126 ? 17.758 -5.219  0.027   0.38 9.40  ?  126 LEU   A C    1 
ATOM   2731 O  O    A LEU   A 1 126 ? 17.674 -4.246  -0.274  0.62 11.08 ?  126 LEU   A O    1 
ATOM   2732 O  O    B LEU   A 1 126 ? 17.467 -4.167  -0.556  0.38 9.87  ?  126 LEU   A O    1 
ATOM   2733 C  CB   A LEU   A 1 126 ? 15.523 -6.187  0.610   0.62 10.64 ?  126 LEU   A CB   1 
ATOM   2734 C  CB   B LEU   A 1 126 ? 15.400 -5.888  0.572   0.38 10.12 ?  126 LEU   A CB   1 
ATOM   2735 C  CG   A LEU   A 1 126 ? 14.637 -7.173  1.373   0.62 11.42 ?  126 LEU   A CG   1 
ATOM   2736 C  CG   B LEU   A 1 126 ? 14.476 -6.753  1.422   0.38 10.37 ?  126 LEU   A CG   1 
ATOM   2737 C  CD1  A LEU   A 1 126 ? 13.209 -7.098  0.872   0.62 12.89 ?  126 LEU   A CD1  1 
ATOM   2738 C  CD1  B LEU   A 1 126 ? 13.056 -6.618  0.909   0.38 10.80 ?  126 LEU   A CD1  1 
ATOM   2739 C  CD2  A LEU   A 1 126 ? 15.163 -8.599  1.241   0.62 11.38 ?  126 LEU   A CD2  1 
ATOM   2740 C  CD2  B LEU   A 1 126 ? 14.909 -8.215  1.422   0.38 10.39 ?  126 LEU   A CD2  1 
ATOM   2741 H  H    A LEU   A 1 126 ? 16.175 -4.738  2.479   0.62 11.56 ?  126 LEU   A H    1 
ATOM   2742 H  H    B LEU   A 1 126 ? 16.234 -4.444  2.384   0.38 11.82 ?  126 LEU   A H    1 
ATOM   2743 H  HA   A LEU   A 1 126 ? 17.276 -6.890  1.398   0.62 12.39 ?  126 LEU   A HA   1 
ATOM   2744 H  HA   B LEU   A 1 126 ? 17.137 -6.709  1.293   0.38 11.83 ?  126 LEU   A HA   1 
ATOM   2745 H  HB2  A LEU   A 1 126 ? 15.076 -5.325  0.623   0.62 12.75 ?  126 LEU   A HB2  1 
ATOM   2746 H  HB2  B LEU   A 1 126 ? 15.031 -4.991  0.551   0.38 12.13 ?  126 LEU   A HB2  1 
ATOM   2747 H  HB3  A LEU   A 1 126 ? 15.590 -6.503  -0.305  0.62 12.75 ?  126 LEU   A HB3  1 
ATOM   2748 H  HB3  B LEU   A 1 126 ? 15.412 -6.259  -0.323  0.38 12.13 ?  126 LEU   A HB3  1 
ATOM   2749 H  HG   A LEU   A 1 126 ? 14.634 -6.942  2.315   0.62 13.69 ?  126 LEU   A HG   1 
ATOM   2750 H  HG   B LEU   A 1 126 ? 14.493 -6.433  2.339   0.38 12.43 ?  126 LEU   A HG   1 
ATOM   2751 H  HD11 A LEU   A 1 126 ? 12.663 -7.729  1.372   0.62 15.45 ?  126 LEU   A HD11 1 
ATOM   2752 H  HD11 B LEU   A 1 126 ? 12.470 -7.168  1.452   0.38 12.95 ?  126 LEU   A HD11 1 
ATOM   2753 H  HD12 A LEU   A 1 126 ? 12.874 -6.198  1.004   0.62 15.45 ?  126 LEU   A HD12 1 
ATOM   2754 H  HD12 B LEU   A 1 126 ? 12.786 -5.689  0.965   0.38 12.95 ?  126 LEU   A HD12 1 
ATOM   2755 H  HD13 A LEU   A 1 126 ? 13.192 -7.325  -0.071  0.62 15.45 ?  126 LEU   A HD13 1 
ATOM   2756 H  HD13 B LEU   A 1 126 ? 13.026 -6.917  -0.015  0.38 12.95 ?  126 LEU   A HD13 1 
ATOM   2757 H  HD21 A LEU   A 1 126 ? 14.499 -9.217  1.579   0.62 13.64 ?  126 LEU   A HD21 1 
ATOM   2758 H  HD21 B LEU   A 1 126 ? 14.199 -8.754  1.802   0.38 12.45 ?  126 LEU   A HD21 1 
ATOM   2759 H  HD22 A LEU   A 1 126 ? 15.341 -8.782  0.304   0.62 13.64 ?  126 LEU   A HD22 1 
ATOM   2760 H  HD22 B LEU   A 1 126 ? 15.082 -8.490  0.508   0.38 12.45 ?  126 LEU   A HD22 1 
ATOM   2761 H  HD23 A LEU   A 1 126 ? 15.984 -8.680  1.753   0.62 13.64 ?  126 LEU   A HD23 1 
ATOM   2762 H  HD23 B LEU   A 1 126 ? 15.715 -8.306  1.954   0.38 12.45 ?  126 LEU   A HD23 1 
ATOM   2763 N  N    A LEU   A 1 127 ? 18.889 -6.145  -0.234  0.62 10.54 ?  127 LEU   A N    1 
ATOM   2764 N  N    B LEU   A 1 127 ? 18.875 -5.891  -0.226  0.38 9.23  ?  127 LEU   A N    1 
ATOM   2765 C  CA   A LEU   A 1 127 ? 19.885 -5.640  -1.165  0.62 10.02 ?  127 LEU   A CA   1 
ATOM   2766 C  CA   B LEU   A 1 127 ? 19.855 -5.368  -1.165  0.38 9.79  ?  127 LEU   A CA   1 
ATOM   2767 C  C    A LEU   A 1 127 ? 19.274 -5.456  -2.544  0.62 9.45  ?  127 LEU   A C    1 
ATOM   2768 C  C    B LEU   A 1 127 ? 19.305 -5.350  -2.590  0.38 10.33 ?  127 LEU   A C    1 
ATOM   2769 O  O    A LEU   A 1 127 ? 18.447 -6.256  -2.997  0.62 9.81  ?  127 LEU   A O    1 
ATOM   2770 O  O    B LEU   A 1 127 ? 18.472 -6.175  -2.979  0.38 10.71 ?  127 LEU   A O    1 
ATOM   2771 C  CB   A LEU   A 1 127 ? 21.065 -6.606  -1.254  0.62 10.42 ?  127 LEU   A CB   1 
ATOM   2772 C  CB   B LEU   A 1 127 ? 21.137 -6.199  -1.115  0.38 10.40 ?  127 LEU   A CB   1 
ATOM   2773 C  CG   A LEU   A 1 127 ? 21.863 -6.813  0.033   0.62 10.51 ?  127 LEU   A CG   1 
ATOM   2774 C  CG   B LEU   A 1 127 ? 21.927 -6.156  0.198   0.38 10.93 ?  127 LEU   A CG   1 
ATOM   2775 C  CD1  A LEU   A 1 127 ? 22.959 -7.824  -0.225  0.62 10.83 ?  127 LEU   A CD1  1 
ATOM   2776 C  CD1  B LEU   A 1 127 ? 23.069 -7.152  0.158   0.38 11.67 ?  127 LEU   A CD1  1 
ATOM   2777 C  CD2  A LEU   A 1 127 ? 22.464 -5.515  0.535   0.62 10.92 ?  127 LEU   A CD2  1 
ATOM   2778 C  CD2  B LEU   A 1 127 ? 22.459 -4.750  0.484   0.38 11.02 ?  127 LEU   A CD2  1 
ATOM   2779 H  H    A LEU   A 1 127 ? 19.033 -6.951  0.029   0.62 12.63 ?  127 LEU   A H    1 
ATOM   2780 H  H    B LEU   A 1 127 ? 19.093 -6.641  0.144   0.38 11.05 ?  127 LEU   A H    1 
ATOM   2781 H  HA   A LEU   A 1 127 ? 20.215 -4.782  -0.859  0.62 12.00 ?  127 LEU   A HA   1 
ATOM   2782 H  HA   B LEU   A 1 127 ? 20.077 -4.456  -0.908  0.38 11.73 ?  127 LEU   A HA   1 
ATOM   2783 H  HB2  A LEU   A 1 127 ? 20.730 -7.476  -1.526  0.62 12.48 ?  127 LEU   A HB2  1 
ATOM   2784 H  HB2  B LEU   A 1 127 ? 20.902 -7.125  -1.282  0.38 12.46 ?  127 LEU   A HB2  1 
ATOM   2785 H  HB3  A LEU   A 1 127 ? 21.684 -6.278  -1.926  0.62 12.48 ?  127 LEU   A HB3  1 
ATOM   2786 H  HB3  B LEU   A 1 127 ? 21.725 -5.884  -1.818  0.38 12.46 ?  127 LEU   A HB3  1 
ATOM   2787 H  HG   A LEU   A 1 127 ? 21.277 -7.164  0.725   0.62 12.59 ?  127 LEU   A HG   1 
ATOM   2788 H  HG   B LEU   A 1 127 ? 21.340 -6.407  0.929   0.38 13.10 ?  127 LEU   A HG   1 
ATOM   2789 H  HD11 A LEU   A 1 127 ? 23.452 -7.975  0.599   0.62 12.98 ?  127 LEU   A HD11 1 
ATOM   2790 H  HD11 B LEU   A 1 127 ? 23.584 -7.075  0.977   0.38 13.99 ?  127 LEU   A HD11 1 
ATOM   2791 H  HD12 A LEU   A 1 127 ? 22.560 -8.653  -0.528  0.62 12.98 ?  127 LEU   A HD12 1 
ATOM   2792 H  HD12 B LEU   A 1 127 ? 22.704 -8.048  0.081   0.38 13.99 ?  127 LEU   A HD12 1 
ATOM   2793 H  HD13 A LEU   A 1 127 ? 23.556 -7.475  -0.906  0.62 12.98 ?  127 LEU   A HD13 1 
ATOM   2794 H  HD13 B LEU   A 1 127 ? 23.632 -6.957  -0.606  0.38 13.99 ?  127 LEU   A HD13 1 
ATOM   2795 H  HD21 A LEU   A 1 127 ? 23.054 -5.707  1.279   0.62 13.09 ?  127 LEU   A HD21 1 
ATOM   2796 H  HD21 B LEU   A 1 127 ? 23.033 -4.783  1.267   0.38 13.21 ?  127 LEU   A HD21 1 
ATOM   2797 H  HD22 A LEU   A 1 127 ? 22.967 -5.104  -0.188  0.62 13.09 ?  127 LEU   A HD22 1 
ATOM   2798 H  HD22 B LEU   A 1 127 ? 22.968 -4.445  -0.284  0.38 13.21 ?  127 LEU   A HD22 1 
ATOM   2799 H  HD23 A LEU   A 1 127 ? 21.752 -4.923  0.818   0.62 13.09 ?  127 LEU   A HD23 1 
ATOM   2800 H  HD23 B LEU   A 1 127 ? 21.713 -4.156  0.645   0.38 13.21 ?  127 LEU   A HD23 1 
ATOM   2801 N  N    A SER   A 1 128 ? 19.697 -4.389  -3.213  0.62 9.35  ?  128 SER   A N    1 
ATOM   2802 N  N    B SER   A 1 128 ? 19.793 -4.381  -3.364  0.38 10.54 ?  128 SER   A N    1 
ATOM   2803 C  CA   A SER   A 1 128 ? 19.298 -4.007  -4.558  0.62 9.44  ?  128 SER   A CA   1 
ATOM   2804 C  CA   B SER   A 1 128 ? 19.463 -4.172  -4.771  0.38 10.53 ?  128 SER   A CA   1 
ATOM   2805 C  C    A SER   A 1 128 ? 17.840 -3.572  -4.658  0.62 9.70  ?  128 SER   A C    1 
ATOM   2806 C  C    B SER   A 1 128 ? 18.045 -3.670  -5.032  0.38 10.39 ?  128 SER   A C    1 
ATOM   2807 O  O    A SER   A 1 128 ? 17.383 -3.277  -5.762  0.62 10.66 ?  128 SER   A O    1 
ATOM   2808 O  O    B SER   A 1 128 ? 17.740 -3.265  -6.157  0.38 10.39 ?  128 SER   A O    1 
ATOM   2809 C  CB   A SER   A 1 128 ? 19.639 -5.063  -5.620  0.62 9.44  ?  128 SER   A CB   1 
ATOM   2810 C  CB   B SER   A 1 128 ? 19.776 -5.407  -5.621  0.38 10.95 ?  128 SER   A CB   1 
ATOM   2811 O  OG   A SER   A 1 128 ? 21.044 -5.264  -5.681  0.62 9.99  ?  128 SER   A OG   1 
ATOM   2812 O  OG   B SER   A 1 128 ? 21.177 -5.559  -5.787  0.38 11.20 ?  128 SER   A OG   1 
ATOM   2813 H  H    A SER   A 1 128 ? 20.266 -3.828  -2.878  0.62 11.21 ?  128 SER   A H    1 
ATOM   2814 H  H    B SER   A 1 128 ? 20.369 -3.814  -3.075  0.38 12.63 ?  128 SER   A H    1 
ATOM   2815 H  HA   A SER   A 1 128 ? 19.818 -3.227  -4.790  0.62 11.31 ?  128 SER   A HA   1 
ATOM   2816 H  HA   B SER   A 1 128 ? 20.047 -3.475  -5.089  0.38 12.62 ?  128 SER   A HA   1 
ATOM   2817 H  HB2  A SER   A 1 128 ? 19.205 -5.897  -5.392  0.62 11.31 ?  128 SER   A HB2  1 
ATOM   2818 H  HB2  B SER   A 1 128 ? 19.419 -6.195  -5.191  0.38 13.13 ?  128 SER   A HB2  1 
ATOM   2819 H  HB3  A SER   A 1 128 ? 19.326 -4.750  -6.487  0.62 11.31 ?  128 SER   A HB3  1 
ATOM   2820 H  HB3  B SER   A 1 128 ? 19.372 -5.292  -6.498  0.38 13.13 ?  128 SER   A HB3  1 
ATOM   2821 H  HG   A SER   A 1 128 ? 21.427 -4.540  -5.872  0.62 11.98 ?  128 SER   A HG   1 
ATOM   2822 H  HG   B SER   A 1 128 ? 21.493 -4.866  -6.148  0.38 13.42 ?  128 SER   A HG   1 
ATOM   2823 N  N    A ALA   A 1 129 ? 17.110 -3.500  -3.545  0.62 9.71  ?  129 ALA   A N    1 
ATOM   2824 N  N    B ALA   A 1 129 ? 17.178 -3.680  -4.023  0.38 10.66 ?  129 ALA   A N    1 
ATOM   2825 C  CA   A ALA   A 1 129 ? 15.735 -3.022  -3.547  0.62 9.79  ?  129 ALA   A CA   1 
ATOM   2826 C  CA   B ALA   A 1 129 ? 15.831 -3.152  -4.180  0.38 11.09 ?  129 ALA   A CA   1 
ATOM   2827 C  C    A ALA   A 1 129 ? 15.725 -1.495  -3.476  0.62 9.34  ?  129 ALA   A C    1 
ATOM   2828 C  C    B ALA   A 1 129 ? 15.839 -1.640  -3.938  0.38 11.69 ?  129 ALA   A C    1 
ATOM   2829 O  O    A ALA   A 1 129 ? 16.765 -0.832  -3.547  0.62 9.88  ?  129 ALA   A O    1 
ATOM   2830 O  O    B ALA   A 1 129 ? 16.894 -1.000  -3.898  0.38 12.07 ?  129 ALA   A O    1 
ATOM   2831 C  CB   A ALA   A 1 129 ? 14.943 -3.680  -2.415  0.62 10.91 ?  129 ALA   A CB   1 
ATOM   2832 C  CB   B ALA   A 1 129 ? 14.852 -3.937  -3.307  0.38 11.58 ?  129 ALA   A CB   1 
ATOM   2833 H  H    A ALA   A 1 129 ? 17.397 -3.729  -2.763  0.62 11.63 ?  129 ALA   A H    1 
ATOM   2834 H  H    B ALA   A 1 129 ? 17.342 -4.001  -3.238  0.38 12.77 ?  129 ALA   A H    1 
ATOM   2835 H  HA   A ALA   A 1 129 ? 15.319 -3.276  -4.377  0.62 11.73 ?  129 ALA   A HA   1 
ATOM   2836 H  HA   B ALA   A 1 129 ? 15.562 -3.287  -5.098  0.38 13.30 ?  129 ALA   A HA   1 
ATOM   2837 H  HB1  A ALA   A 1 129 ? 14.030 -3.354  -2.433  0.62 13.08 ?  129 ALA   A HB1  1 
ATOM   2838 H  HB1  B ALA   A 1 129 ? 13.962 -3.574  -3.431  0.38 13.88 ?  129 ALA   A HB1  1 
ATOM   2839 H  HB2  A ALA   A 1 129 ? 14.954 -4.641  -2.540  0.62 13.08 ?  129 ALA   A HB2  1 
ATOM   2840 H  HB2  B ALA   A 1 129 ? 14.867 -4.871  -3.583  0.38 13.88 ?  129 ALA   A HB2  1 
ATOM   2841 H  HB3  A ALA   A 1 129 ? 15.355 -3.455  -1.562  0.62 13.08 ?  129 ALA   A HB3  1 
ATOM   2842 H  HB3  B ALA   A 1 129 ? 15.120 -3.862  -2.382  0.38 13.88 ?  129 ALA   A HB3  1 
ATOM   2843 N  N    A GLY   A 1 130 ? 14.534 -0.921  -3.342  0.62 10.01 ?  130 GLY   A N    1 
ATOM   2844 N  N    B GLY   A 1 130 ? 14.656 -1.050  -3.794  0.38 11.60 ?  130 GLY   A N    1 
ATOM   2845 C  CA   A GLY   A 1 130 ? 14.427 0.526   -3.293  0.62 10.63 ?  130 GLY   A CA   1 
ATOM   2846 C  CA   B GLY   A 1 130 ? 14.582 0.393   -3.643  0.38 12.16 ?  130 GLY   A CA   1 
ATOM   2847 C  C    A GLY   A 1 130 ? 15.018 1.145   -4.541  0.62 10.53 ?  130 GLY   A C    1 
ATOM   2848 C  C    B GLY   A 1 130 ? 15.205 1.106   -4.822  0.38 12.19 ?  130 GLY   A C    1 
ATOM   2849 O  O    A GLY   A 1 130 ? 14.773 0.691   -5.664  0.62 10.84 ?  130 GLY   A O    1 
ATOM   2850 O  O    B GLY   A 1 130 ? 15.016 0.727   -5.983  0.38 12.18 ?  130 GLY   A O    1 
ATOM   2851 H  H    A GLY   A 1 130 ? 13.784 -1.343  -3.279  0.62 12.00 ?  130 GLY   A H    1 
ATOM   2852 H  H    B GLY   A 1 130 ? 13.900 -1.459  -3.775  0.38 13.90 ?  130 GLY   A H    1 
ATOM   2853 H  HA2  A GLY   A 1 130 ? 13.490 0.782   -3.218  0.62 12.74 ?  130 GLY   A HA2  1 
ATOM   2854 H  HA2  B GLY   A 1 130 ? 13.655 0.674   -3.547  0.38 14.58 ?  130 GLY   A HA2  1 
ATOM   2855 H  HA3  A GLY   A 1 130 ? 14.903 0.865   -2.524  0.62 12.74 ?  130 GLY   A HA3  1 
ATOM   2856 H  HA3  B GLY   A 1 130 ? 15.076 0.666   -2.861  0.38 14.58 ?  130 GLY   A HA3  1 
ATOM   2857 N  N    A ILE   A 1 131 ? 15.818 2.199   -4.347  0.62 11.23 ?  131 ILE   A N    1 
ATOM   2858 N  N    B ILE   A 1 131 ? 15.976 2.154   -4.519  0.38 12.19 ?  131 ILE   A N    1 
ATOM   2859 C  CA   A ILE   A 1 131 ? 16.346 2.971   -5.469  0.62 11.34 ?  131 ILE   A CA   1 
ATOM   2860 C  CA   B ILE   A 1 131 ? 16.593 2.971   -5.554  0.38 12.01 ?  131 ILE   A CA   1 
ATOM   2861 C  C    A ILE   A 1 131 ? 17.392 2.223   -6.286  0.62 11.32 ?  131 ILE   A C    1 
ATOM   2862 C  C    B ILE   A 1 131 ? 17.578 2.195   -6.418  0.38 12.01 ?  131 ILE   A C    1 
ATOM   2863 O  O    A ILE   A 1 131 ? 17.816 2.737   -7.328  0.62 12.32 ?  131 ILE   A O    1 
ATOM   2864 O  O    B ILE   A 1 131 ? 17.945 2.676   -7.497  0.38 12.89 ?  131 ILE   A O    1 
ATOM   2865 C  CB   A ILE   A 1 131 ? 16.872 4.356   -5.032  0.62 12.43 ?  131 ILE   A CB   1 
ATOM   2866 C  CB   B ILE   A 1 131 ? 17.230 4.255   -4.966  0.38 12.54 ?  131 ILE   A CB   1 
ATOM   2867 C  CG1  A ILE   A 1 131 ? 18.126 4.224   -4.159  0.62 13.62 ?  131 ILE   A CG1  1 
ATOM   2868 C  CG1  B ILE   A 1 131 ? 18.412 3.927   -4.045  0.38 13.10 ?  131 ILE   A CG1  1 
ATOM   2869 C  CG2  A ILE   A 1 131 ? 15.772 5.138   -4.320  0.62 12.85 ?  131 ILE   A CG2  1 
ATOM   2870 C  CG2  B ILE   A 1 131 ? 16.185 5.078   -4.220  0.38 12.77 ?  131 ILE   A CG2  1 
ATOM   2871 C  CD1  A ILE   A 1 131 ? 18.758 5.563   -3.787  0.62 14.43 ?  131 ILE   A CD1  1 
ATOM   2872 C  CD1  B ILE   A 1 131 ? 19.056 5.166   -3.410  0.38 13.61 ?  131 ILE   A CD1  1 
ATOM   2873 H  H    A ILE   A 1 131 ? 16.047 2.492   -3.573  0.62 13.46 ?  131 ILE   A H    1 
ATOM   2874 H  H    B ILE   A 1 131 ? 16.142 2.416   -3.715  0.38 14.61 ?  131 ILE   A H    1 
ATOM   2875 H  HA   A ILE   A 1 131 ? 15.608 3.143   -6.071  0.62 13.60 ?  131 ILE   A HA   1 
ATOM   2876 H  HA   B ILE   A 1 131 ? 15.890 3.259   -6.150  0.38 14.40 ?  131 ILE   A HA   1 
ATOM   2877 H  HB   A ILE   A 1 131 ? 17.113 4.846   -5.829  0.62 14.90 ?  131 ILE   A HB   1 
ATOM   2878 H  HB   B ILE   A 1 131 ? 17.558 4.788   -5.706  0.38 15.03 ?  131 ILE   A HB   1 
ATOM   2879 H  HG12 A ILE   A 1 131 ? 17.891 3.767   -3.337  0.62 16.33 ?  131 ILE   A HG12 1 
ATOM   2880 H  HG12 B ILE   A 1 131 ? 18.104 3.356   -3.328  0.38 15.70 ?  131 ILE   A HG12 1 
ATOM   2881 H  HG13 A ILE   A 1 131 ? 18.794 3.710   -4.641  0.62 16.33 ?  131 ILE   A HG13 1 
ATOM   2882 H  HG13 B ILE   A 1 131 ? 19.098 3.477   -4.560  0.38 15.70 ?  131 ILE   A HG13 1 
ATOM   2883 H  HG21 A ILE   A 1 131 ? 16.078 6.043   -4.160  0.62 15.40 ?  131 ILE   A HG21 1 
ATOM   2884 H  HG21 B ILE   A 1 131 ? 16.539 5.965   -4.051  0.38 15.31 ?  131 ILE   A HG21 1 
ATOM   2885 H  HG22 A ILE   A 1 131 ? 14.982 5.151   -4.884  0.62 15.40 ?  131 ILE   A HG22 1 
ATOM   2886 H  HG22 B ILE   A 1 131 ? 15.384 5.141   -4.764  0.38 15.31 ?  131 ILE   A HG22 1 
ATOM   2887 H  HG23 A ILE   A 1 131 ? 15.567 4.702   -3.477  0.62 15.40 ?  131 ILE   A HG23 1 
ATOM   2888 H  HG23 B ILE   A 1 131 ? 15.977 4.638   -3.380  0.38 15.31 ?  131 ILE   A HG23 1 
ATOM   2889 H  HD11 A ILE   A 1 131 ? 19.603 5.400   -3.339  0.62 17.30 ?  131 ILE   A HD11 1 
ATOM   2890 H  HD11 B ILE   A 1 131 ? 19.883 4.907   -2.974  0.38 16.32 ?  131 ILE   A HD11 1 
ATOM   2891 H  HD12 A ILE   A 1 131 ? 18.908 6.078   -4.596  0.62 17.30 ?  131 ILE   A HD12 1 
ATOM   2892 H  HD12 B ILE   A 1 131 ? 19.240 5.822   -4.102  0.38 16.32 ?  131 ILE   A HD12 1 
ATOM   2893 H  HD13 A ILE   A 1 131 ? 18.158 6.044   -3.196  0.62 17.30 ?  131 ILE   A HD13 1 
ATOM   2894 H  HD13 B ILE   A 1 131 ? 18.444 5.545   -2.756  0.38 16.32 ?  131 ILE   A HD13 1 
ATOM   2895 N  N    A PHE   A 1 132 ? 17.813 1.023   -5.856  0.62 11.25 ?  132 PHE   A N    1 
ATOM   2896 N  N    B PHE   A 1 132 ? 17.998 0.996   -5.992  0.38 11.62 ?  132 PHE   A N    1 
ATOM   2897 C  CA   A PHE   A 1 132 ? 18.678 0.187   -6.683  0.62 11.01 ?  132 PHE   A CA   1 
ATOM   2898 C  CA   B PHE   A 1 132 ? 18.910 0.194   -6.802  0.38 11.71 ?  132 PHE   A CA   1 
ATOM   2899 C  C    A PHE   A 1 132 ? 17.910 -0.571  -7.767  0.62 11.24 ?  132 PHE   A C    1 
ATOM   2900 C  C    B PHE   A 1 132 ? 18.206 -0.550  -7.938  0.38 12.70 ?  132 PHE   A C    1 
ATOM   2901 O  O    A PHE   A 1 132 ? 18.536 -1.212  -8.617  0.62 11.97 ?  132 PHE   A O    1 
ATOM   2902 O  O    B PHE   A 1 132 ? 18.890 -1.084  -8.819  0.38 13.68 ?  132 PHE   A O    1 
ATOM   2903 C  CB   A PHE   A 1 132 ? 19.476 -0.797  -5.818  0.62 11.29 ?  132 PHE   A CB   1 
ATOM   2904 C  CB   B PHE   A 1 132 ? 19.713 -0.781  -5.929  0.38 10.88 ?  132 PHE   A CB   1 
ATOM   2905 C  CG   A PHE   A 1 132 ? 20.720 -0.212  -5.175  0.62 11.42 ?  132 PHE   A CG   1 
ATOM   2906 C  CG   B PHE   A 1 132 ? 20.889 -0.150  -5.214  0.38 10.35 ?  132 PHE   A CG   1 
ATOM   2907 C  CD1  A PHE   A 1 132 ? 20.637 0.840   -4.277  0.62 12.45 ?  132 PHE   A CD1  1 
ATOM   2908 C  CD1  B PHE   A 1 132 ? 20.697 0.770   -4.194  0.38 11.27 ?  132 PHE   A CD1  1 
ATOM   2909 C  CD2  A PHE   A 1 132 ? 21.968 -0.765  -5.428  0.62 11.88 ?  132 PHE   A CD2  1 
ATOM   2910 C  CD2  B PHE   A 1 132 ? 22.188 -0.506  -5.543  0.38 10.34 ?  132 PHE   A CD2  1 
ATOM   2911 C  CE1  A PHE   A 1 132 ? 21.780 1.350   -3.672  0.62 12.59 ?  132 PHE   A CE1  1 
ATOM   2912 C  CE1  B PHE   A 1 132 ? 21.781 1.335   -3.531  0.38 11.42 ?  132 PHE   A CE1  1 
ATOM   2913 C  CE2  A PHE   A 1 132 ? 23.112 -0.263  -4.822  0.62 12.09 ?  132 PHE   A CE2  1 
ATOM   2914 C  CE2  B PHE   A 1 132 ? 23.274 0.052   -4.882  0.38 10.90 ?  132 PHE   A CE2  1 
ATOM   2915 C  CZ   A PHE   A 1 132 ? 23.012 0.796   -3.943  0.62 12.12 ?  132 PHE   A CZ   1 
ATOM   2916 C  CZ   B PHE   A 1 132 ? 23.066 0.974   -3.876  0.38 11.18 ?  132 PHE   A CZ   1 
ATOM   2917 H  H    A PHE   A 1 132 ? 17.606 0.676   -5.093  0.62 13.48 ?  132 PHE   A H    1 
ATOM   2918 H  H    B PHE   A 1 132 ? 17.766 0.625   -5.246  0.38 13.93 ?  132 PHE   A H    1 
ATOM   2919 H  HA   A PHE   A 1 132 ? 19.315 0.761   -7.125  0.62 13.19 ?  132 PHE   A HA   1 
ATOM   2920 H  HA   B PHE   A 1 132 ? 19.552 0.796   -7.202  0.38 14.04 ?  132 PHE   A HA   1 
ATOM   2921 H  HB2  A PHE   A 1 132 ? 18.907 -1.118  -5.101  0.62 13.53 ?  132 PHE   A HB2  1 
ATOM   2922 H  HB2  B PHE   A 1 132 ? 19.130 -1.155  -5.252  0.38 13.04 ?  132 PHE   A HB2  1 
ATOM   2923 H  HB3  A PHE   A 1 132 ? 19.757 -1.543  -6.370  0.62 13.53 ?  132 PHE   A HB3  1 
ATOM   2924 H  HB3  B PHE   A 1 132 ? 20.063 -1.492  -6.491  0.38 13.04 ?  132 PHE   A HB3  1 
ATOM   2925 H  HD1  A PHE   A 1 132 ? 19.812 1.216   -4.083  0.62 14.93 ?  132 PHE   A HD1  1 
ATOM   2926 H  HD1  B PHE   A 1 132 ? 19.836 1.018   -3.952  0.38 13.51 ?  132 PHE   A HD1  1 
ATOM   2927 H  HD2  A PHE   A 1 132 ? 22.044 -1.483  -6.018  0.62 14.24 ?  132 PHE   A HD2  1 
ATOM   2928 H  HD2  B PHE   A 1 132 ? 22.337 -1.127  -6.221  0.38 12.39 ?  132 PHE   A HD2  1 
ATOM   2929 H  HE1  A PHE   A 1 132 ? 21.717 2.061   -3.076  0.62 15.09 ?  132 PHE   A HE1  1 
ATOM   2930 H  HE1  B PHE   A 1 132 ? 21.642 1.955   -2.851  0.38 13.69 ?  132 PHE   A HE1  1 
ATOM   2931 H  HE2  A PHE   A 1 132 ? 23.944 -0.637  -5.011  0.62 14.49 ?  132 PHE   A HE2  1 
ATOM   2932 H  HE2  B PHE   A 1 132 ? 24.141 -0.191  -5.121  0.38 13.07 ?  132 PHE   A HE2  1 
ATOM   2933 H  HZ   A PHE   A 1 132 ? 23.778 1.140   -3.539  0.62 14.53 ?  132 PHE   A HZ   1 
ATOM   2934 H  HZ   B PHE   A 1 132 ? 23.794 1.352   -3.436  0.38 13.40 ?  132 PHE   A HZ   1 
ATOM   2935 N  N    A GLY   A 1 133 ? 16.578 -0.537  -7.749  0.62 11.14 ?  133 GLY   A N    1 
ATOM   2936 N  N    B GLY   A 1 133 ? 16.871 -0.612  -7.940  0.38 12.72 ?  133 GLY   A N    1 
ATOM   2937 C  CA   A GLY   A 1 133 ? 15.786 -0.915  -8.905  0.62 12.15 ?  133 GLY   A CA   1 
ATOM   2938 C  CA   B GLY   A 1 133 ? 16.107 -0.984  -9.115  0.38 12.75 ?  133 GLY   A CA   1 
ATOM   2939 C  C    A GLY   A 1 133 ? 15.527 -2.390  -9.136  0.62 13.06 ?  133 GLY   A C    1 
ATOM   2940 C  C    B GLY   A 1 133 ? 15.440 -2.348  -9.082  0.38 12.68 ?  133 GLY   A C    1 
ATOM   2941 O  O    A GLY   A 1 133 ? 14.951 -2.729  -10.176 0.62 13.83 ?  133 GLY   A O    1 
ATOM   2942 O  O    B GLY   A 1 133 ? 14.508 -2.573  -9.866  0.38 12.78 ?  133 GLY   A O    1 
ATOM   2943 H  H    A GLY   A 1 133 ? 16.112 -0.298  -7.071  0.62 13.35 ?  133 GLY   A H    1 
ATOM   2944 H  H    B GLY   A 1 133 ? 16.385 -0.440  -7.250  0.38 15.24 ?  133 GLY   A H    1 
ATOM   2945 H  HA2  A GLY   A 1 133 ? 14.921 -0.483  -8.832  0.62 14.57 ?  133 GLY   A HA2  1 
ATOM   2946 H  HA2  B GLY   A 1 133 ? 15.409 -0.329  -9.254  0.38 15.28 ?  133 GLY   A HA2  1 
ATOM   2947 H  HA3  A GLY   A 1 133 ? 16.220 -0.570  -9.700  0.62 14.57 ?  133 GLY   A HA3  1 
ATOM   2948 H  HA3  B GLY   A 1 133 ? 16.693 -0.956  -9.888  0.38 15.28 ?  133 GLY   A HA3  1 
ATOM   2949 N  N    A ALA   A 1 134 ? 15.924 -3.282  -8.229  0.62 13.12 ?  134 ALA   A N    1 
ATOM   2950 N  N    B ALA   A 1 134 ? 15.873 -3.264  -8.220  0.38 12.53 ?  134 ALA   A N    1 
ATOM   2951 C  CA   A ALA   A 1 134 ? 15.615 -4.694  -8.404  0.62 13.59 ?  134 ALA   A CA   1 
ATOM   2952 C  CA   B ALA   A 1 134 ? 15.393 -4.636  -8.304  0.38 12.68 ?  134 ALA   A CA   1 
ATOM   2953 C  C    A ALA   A 1 134 ? 14.250 -5.018  -7.795  0.62 13.49 ?  134 ALA   A C    1 
ATOM   2954 C  C    B ALA   A 1 134 ? 14.103 -4.835  -7.512  0.38 12.38 ?  134 ALA   A C    1 
ATOM   2955 O  O    A ALA   A 1 134 ? 13.674 -4.236  -7.037  0.62 14.39 ?  134 ALA   A O    1 
ATOM   2956 O  O    B ALA   A 1 134 ? 13.741 -4.037  -6.644  0.38 12.42 ?  134 ALA   A O    1 
ATOM   2957 C  CB   A ALA   A 1 134 ? 16.710 -5.572  -7.798  0.62 14.39 ?  134 ALA   A CB   1 
ATOM   2958 C  CB   B ALA   A 1 134 ? 16.455 -5.620  -7.818  0.38 12.97 ?  134 ALA   A CB   1 
ATOM   2959 H  H    A ALA   A 1 134 ? 16.375 -3.093  -7.517  0.62 15.73 ?  134 ALA   A H    1 
ATOM   2960 H  H    B ALA   A 1 134 ? 16.434 -3.111  -7.584  0.38 15.02 ?  134 ALA   A H    1 
ATOM   2961 H  HA   A ALA   A 1 134 ? 15.577 -4.887  -9.353  0.62 16.29 ?  134 ALA   A HA   1 
ATOM   2962 H  HA   B ALA   A 1 134 ? 15.202 -4.836  -9.232  0.38 15.20 ?  134 ALA   A HA   1 
ATOM   2963 H  HB1  A ALA   A 1 134 ? 16.487 -6.502  -7.958  0.62 17.25 ?  134 ALA   A HB1  1 
ATOM   2964 H  HB1  B ALA   A 1 134 ? 16.101 -6.519  -7.894  0.38 15.55 ?  134 ALA   A HB1  1 
ATOM   2965 H  HB2  A ALA   A 1 134 ? 17.558 -5.358  -8.221  0.62 17.25 ?  134 ALA   A HB2  1 
ATOM   2966 H  HB2  B ALA   A 1 134 ? 17.243 -5.525  -8.374  0.38 15.55 ?  134 ALA   A HB2  1 
ATOM   2967 H  HB3  A ALA   A 1 134 ? 16.763 -5.400  -6.847  0.62 17.25 ?  134 ALA   A HB3  1 
ATOM   2968 H  HB3  B ALA   A 1 134 ? 16.669 -5.421  -6.896  0.38 15.55 ?  134 ALA   A HB3  1 
ATOM   2969 N  N    A ASP   A 1 135 ? 13.731 -6.190  -8.146  0.62 13.42 ?  135 ASP   A N    1 
ATOM   2970 N  N    B ASP   A 1 135 ? 13.413 -5.926  -7.836  0.38 12.64 ?  135 ASP   A N    1 
ATOM   2971 C  CA   A ASP   A 1 135 ? 12.462 -6.662  -7.592  0.62 13.92 ?  135 ASP   A CA   1 
ATOM   2972 C  CA   B ASP   A 1 135 ? 12.178 -6.309  -7.157  0.38 13.03 ?  135 ASP   A CA   1 
ATOM   2973 C  C    A ASP   A 1 135 ? 12.685 -7.101  -6.151  0.62 13.55 ?  135 ASP   A C    1 
ATOM   2974 C  C    B ASP   A 1 135 ? 12.504 -6.807  -5.753  0.38 12.14 ?  135 ASP   A C    1 
ATOM   2975 O  O    A ASP   A 1 135 ? 13.475 -8.023  -5.912  0.62 13.47 ?  135 ASP   A O    1 
ATOM   2976 O  O    B ASP   A 1 135 ? 13.254 -7.783  -5.613  0.38 12.09 ?  135 ASP   A O    1 
ATOM   2977 C  CB   A ASP   A 1 135 ? 11.960 -7.839  -8.425  0.62 15.86 ?  135 ASP   A CB   1 
ATOM   2978 C  CB   B ASP   A 1 135 ? 11.513 -7.423  -7.962  0.38 14.04 ?  135 ASP   A CB   1 
ATOM   2979 C  CG   A ASP   A 1 135 ? 10.649 -8.439  -7.901  0.62 17.97 ?  135 ASP   A CG   1 
ATOM   2980 C  CG   B ASP   A 1 135 ? 10.108 -7.752  -7.477  0.38 15.45 ?  135 ASP   A CG   1 
ATOM   2981 O  OD1  A ASP   A 1 135 ? 10.122 -7.991  -6.861  0.62 18.29 ?  135 ASP   A OD1  1 
ATOM   2982 O  OD1  B ASP   A 1 135 ? 9.779  -7.429  -6.315  0.38 15.47 ?  135 ASP   A OD1  1 
ATOM   2983 O  OD2  A ASP   A 1 135 ? 10.137 -9.373  -8.553  0.62 20.01 -1 135 ASP   A OD2  1 
ATOM   2984 O  OD2  B ASP   A 1 135 ? 9.341  -8.355  -8.259  0.38 16.73 -1 135 ASP   A OD2  1 
ATOM   2985 H  H    A ASP   A 1 135 ? 14.095 -6.732  -8.704  0.62 16.08 ?  135 ASP   A H    1 
ATOM   2986 H  H    B ASP   A 1 135 ? 13.639 -6.469  -8.459  0.38 15.15 ?  135 ASP   A H    1 
ATOM   2987 H  HA   A ASP   A 1 135 ? 11.809 -5.947  -7.630  0.62 16.69 ?  135 ASP   A HA   1 
ATOM   2988 H  HA   B ASP   A 1 135 ? 11.572 -5.547  -7.120  0.38 15.62 ?  135 ASP   A HA   1 
ATOM   2989 H  HB2  A ASP   A 1 135 ? 11.799 -7.536  -9.329  0.62 19.02 ?  135 ASP   A HB2  1 
ATOM   2990 H  HB2  B ASP   A 1 135 ? 11.474 -7.154  -8.894  0.38 16.83 ?  135 ASP   A HB2  1 
ATOM   2991 H  HB3  A ASP   A 1 135 ? 12.637 -8.533  -8.422  0.62 19.02 ?  135 ASP   A HB3  1 
ATOM   2992 H  HB3  B ASP   A 1 135 ? 12.040 -8.229  -7.871  0.38 16.83 ?  135 ASP   A HB3  1 
ATOM   2993 N  N    A PRO   A 1 136 ? 12.025 -6.483  -5.169  0.62 13.19 ?  136 PRO   A N    1 
ATOM   2994 N  N    B PRO   A 1 136 ? 11.979 -6.180  -4.696  0.38 11.38 ?  136 PRO   A N    1 
ATOM   2995 C  CA   A PRO   A 1 136 ? 12.250 -6.890  -3.772  0.62 13.27 ?  136 PRO   A CA   1 
ATOM   2996 C  CA   B PRO   A 1 136 ? 12.268 -6.669  -3.337  0.38 11.60 ?  136 PRO   A CA   1 
ATOM   2997 C  C    A PRO   A 1 136 ? 11.828 -8.318  -3.464  0.62 12.53 ?  136 PRO   A C    1 
ATOM   2998 C  C    B PRO   A 1 136 ? 11.837 -8.105  -3.094  0.38 11.32 ?  136 PRO   A C    1 
ATOM   2999 O  O    A PRO   A 1 136 ? 12.442 -8.952  -2.600  0.62 12.35 ?  136 PRO   A O    1 
ATOM   3000 O  O    B PRO   A 1 136 ? 12.426 -8.779  -2.240  0.38 10.91 ?  136 PRO   A O    1 
ATOM   3001 C  CB   A PRO   A 1 136 ? 11.447 -5.856  -2.970  0.62 14.15 ?  136 PRO   A CB   1 
ATOM   3002 C  CB   B PRO   A 1 136 ? 11.511 -5.675  -2.439  0.38 12.17 ?  136 PRO   A CB   1 
ATOM   3003 C  CG   A PRO   A 1 136 ? 10.417 -5.343  -3.933  0.62 14.70 ?  136 PRO   A CG   1 
ATOM   3004 C  CG   B PRO   A 1 136 ? 10.458 -5.085  -3.322  0.38 12.44 ?  136 PRO   A CG   1 
ATOM   3005 C  CD   A PRO   A 1 136 ? 11.058 -5.378  -5.282  0.62 14.18 ?  136 PRO   A CD   1 
ATOM   3006 C  CD   B PRO   A 1 136 ? 11.105 -4.995  -4.673  0.38 11.69 ?  136 PRO   A CD   1 
ATOM   3007 H  HA   A PRO   A 1 136 ? 13.193 -6.793  -3.550  0.62 15.90 ?  136 PRO   A HA   1 
ATOM   3008 H  HA   B PRO   A 1 136 ? 13.218 -6.587  -3.152  0.38 13.91 ?  136 PRO   A HA   1 
ATOM   3009 H  HB2  A PRO   A 1 136 ? 11.028 -6.290  -2.209  0.62 16.96 ?  136 PRO   A HB2  1 
ATOM   3010 H  HB2  B PRO   A 1 136 ? 11.111 -6.142  -1.690  0.38 14.58 ?  136 PRO   A HB2  1 
ATOM   3011 H  HB3  A PRO   A 1 136 ? 12.038 -5.144  -2.676  0.62 16.96 ?  136 PRO   A HB3  1 
ATOM   3012 H  HB3  B PRO   A 1 136 ? 12.119 -4.985  -2.130  0.38 14.58 ?  136 PRO   A HB3  1 
ATOM   3013 H  HG2  A PRO   A 1 136 ? 9.640  -5.918  -3.910  0.62 17.63 ?  136 PRO   A HG2  1 
ATOM   3014 H  HG2  B PRO   A 1 136 ? 9.686  -5.673  -3.350  0.38 14.91 ?  136 PRO   A HG2  1 
ATOM   3015 H  HG3  A PRO   A 1 136 ? 10.181 -4.434  -3.695  0.62 17.63 ?  136 PRO   A HG3  1 
ATOM   3016 H  HG3  B PRO   A 1 136 ? 10.209 -4.205  -3.001  0.38 14.91 ?  136 PRO   A HG3  1 
ATOM   3017 H  HD2  A PRO   A 1 136 ? 10.394 -5.580  -5.962  0.62 17.00 ?  136 PRO   A HD2  1 
ATOM   3018 H  HD2  B PRO   A 1 136 ? 10.430 -5.051  -5.370  0.38 14.02 ?  136 PRO   A HD2  1 
ATOM   3019 H  HD3  A PRO   A 1 136 ? 11.515 -4.544  -5.467  0.62 17.00 ?  136 PRO   A HD3  1 
ATOM   3020 H  HD3  B PRO   A 1 136 ? 11.628 -4.180  -4.749  0.38 14.02 ?  136 PRO   A HD3  1 
ATOM   3021 N  N    A ILE   A 1 137 ? 10.788 -8.840  -4.120  0.62 12.70 ?  137 ILE   A N    1 
ATOM   3022 N  N    B ILE   A 1 137 ? 10.816 -8.590  -3.803  0.38 11.76 ?  137 ILE   A N    1 
ATOM   3023 C  CA   A ILE   A 1 137 ? 10.428 -10.242 -3.924  0.62 13.08 ?  137 ILE   A CA   1 
ATOM   3024 C  CA   B ILE   A 1 137 ? 10.404 -9.985  -3.655  0.38 12.38 ?  137 ILE   A CA   1 
ATOM   3025 C  C    A ILE   A 1 137 ? 11.598 -11.134 -4.313  0.62 12.58 ?  137 ILE   A C    1 
ATOM   3026 C  C    B ILE   A 1 137 ? 11.541 -10.916 -4.070  0.38 12.00 ?  137 ILE   A C    1 
ATOM   3027 O  O    A ILE   A 1 137 ? 11.912 -12.116 -3.629  0.62 13.01 ?  137 ILE   A O    1 
ATOM   3028 O  O    B ILE   A 1 137 ? 11.852 -11.897 -3.383  0.38 11.78 ?  137 ILE   A O    1 
ATOM   3029 C  CB   A ILE   A 1 137 ? 9.148  -10.589 -4.708  0.62 14.45 ?  137 ILE   A CB   1 
ATOM   3030 C  CB   B ILE   A 1 137 ? 9.126  -10.255 -4.470  0.38 13.54 ?  137 ILE   A CB   1 
ATOM   3031 C  CG1  A ILE   A 1 137 ? 7.949  -9.817  -4.146  0.62 15.85 ?  137 ILE   A CG1  1 
ATOM   3032 C  CG1  B ILE   A 1 137 ? 8.006  -9.283  -4.078  0.38 15.09 ?  137 ILE   A CG1  1 
ATOM   3033 C  CG2  A ILE   A 1 137 ? 8.895  -12.093 -4.669  0.62 14.99 ?  137 ILE   A CG2  1 
ATOM   3034 C  CG2  B ILE   A 1 137 ? 8.679  -11.703 -4.294  0.38 13.58 ?  137 ILE   A CG2  1 
ATOM   3035 C  CD1  A ILE   A 1 137 ? 6.691  -9.938  -4.977  0.62 17.13 ?  137 ILE   A CD1  1 
ATOM   3036 C  CD1  B ILE   A 1 137 ? 6.861  -9.278  -5.054  0.38 16.16 ?  137 ILE   A CD1  1 
ATOM   3037 H  H    A ILE   A 1 137 ? 10.289 -8.412  -4.670  0.62 15.22 ?  137 ILE   A H    1 
ATOM   3038 H  H    B ILE   A 1 137 ? 10.351 -8.129  -4.363  0.38 14.09 ?  137 ILE   A H    1 
ATOM   3039 H  HA   A ILE   A 1 137 ? 10.251 -10.393 -2.985  0.62 15.68 ?  137 ILE   A HA   1 
ATOM   3040 H  HA   B ILE   A 1 137 ? 10.201 -10.151 -2.720  0.38 14.85 ?  137 ILE   A HA   1 
ATOM   3041 H  HB   A ILE   A 1 137 ? 9.273  -10.326 -5.631  0.62 17.33 ?  137 ILE   A HB   1 
ATOM   3042 H  HB   B ILE   A 1 137 ? 9.331  -10.112 -5.404  0.38 16.23 ?  137 ILE   A HB   1 
ATOM   3043 H  HG12 A ILE   A 1 137 ? 7.755  -10.152 -3.257  0.62 19.01 ?  137 ILE   A HG12 1 
ATOM   3044 H  HG12 B ILE   A 1 137 ? 7.657  -9.535  -3.210  0.38 18.09 ?  137 ILE   A HG12 1 
ATOM   3045 H  HG13 A ILE   A 1 137 ? 8.186  -8.876  -4.097  0.62 19.01 ?  137 ILE   A HG13 1 
ATOM   3046 H  HG13 B ILE   A 1 137 ? 8.358  -8.378  -4.039  0.38 18.09 ?  137 ILE   A HG13 1 
ATOM   3047 H  HG21 A ILE   A 1 137 ? 7.970  -12.279 -4.895  0.62 17.98 ?  137 ILE   A HG21 1 
ATOM   3048 H  HG21 B ILE   A 1 137 ? 7.801  -11.815 -4.691  0.38 16.27 ?  137 ILE   A HG21 1 
ATOM   3049 H  HG22 A ILE   A 1 137 ? 9.479  -12.527 -5.311  0.62 17.98 ?  137 ILE   A HG22 1 
ATOM   3050 H  HG22 B ILE   A 1 137 ? 9.316  -12.286 -4.736  0.38 16.27 ?  137 ILE   A HG22 1 
ATOM   3051 H  HG23 A ILE   A 1 137 ? 9.083  -12.421 -3.776  0.62 17.98 ?  137 ILE   A HG23 1 
ATOM   3052 H  HG23 B ILE   A 1 137 ? 8.642  -11.910 -3.347  0.38 16.27 ?  137 ILE   A HG23 1 
ATOM   3053 H  HD11 A ILE   A 1 137 ? 5.944  -10.113 -4.387  0.62 20.54 ?  137 ILE   A HD11 1 
ATOM   3054 H  HD11 B ILE   A 1 137 ? 6.544  -8.369  -5.162  0.38 19.37 ?  137 ILE   A HD11 1 
ATOM   3055 H  HD12 A ILE   A 1 137 ? 6.557  -9.104  -5.450  0.62 20.54 ?  137 ILE   A HD12 1 
ATOM   3056 H  HD12 B ILE   A 1 137 ? 7.173  -9.622  -5.907  0.38 19.37 ?  137 ILE   A HD12 1 
ATOM   3057 H  HD13 A ILE   A 1 137 ? 6.792  -10.661 -5.613  0.62 20.54 ?  137 ILE   A HD13 1 
ATOM   3058 H  HD13 B ILE   A 1 137 ? 6.152  -9.844  -4.711  0.38 19.37 ?  137 ILE   A HD13 1 
ATOM   3059 N  N    A HIS   A 1 138 ? 12.272 -10.790 -5.410  0.62 12.82 ?  138 HIS   A N    1 
ATOM   3060 N  N    B HIS   A 1 138 ? 12.178 -10.615 -5.205  0.38 12.13 ?  138 HIS   A N    1 
ATOM   3061 C  CA   A HIS   A 1 138 ? 13.473 -11.518 -5.793  0.62 13.14 ?  138 HIS   A CA   1 
ATOM   3062 C  CA   B HIS   A 1 138 ? 13.300 -11.421 -5.677  0.38 12.29 ?  138 HIS   A CA   1 
ATOM   3063 C  C    A HIS   A 1 138 ? 14.588 -11.344 -4.765  0.62 12.54 ?  138 HIS   A C    1 
ATOM   3064 C  C    B HIS   A 1 138 ? 14.482 -11.331 -4.722  0.38 12.14 ?  138 HIS   A C    1 
ATOM   3065 O  O    A HIS   A 1 138 ? 15.271 -12.314 -4.417  0.62 12.64 ?  138 HIS   A O    1 
ATOM   3066 O  O    B HIS   A 1 138 ? 15.113 -12.345 -4.399  0.38 12.34 ?  138 HIS   A O    1 
ATOM   3067 C  CB   A HIS   A 1 138 ? 13.930 -11.090 -7.184  0.62 14.29 ?  138 HIS   A CB   1 
ATOM   3068 C  CB   B HIS   A 1 138 ? 13.699 -10.961 -7.081  0.38 12.53 ?  138 HIS   A CB   1 
ATOM   3069 C  CG   A HIS   A 1 138 ? 15.156 -11.807 -7.648  0.62 14.95 ?  138 HIS   A CG   1 
ATOM   3070 C  CG   B HIS   A 1 138 ? 14.993 -11.541 -7.566  0.38 12.93 ?  138 HIS   A CG   1 
ATOM   3071 N  ND1  A HIS   A 1 138 ? 15.193 -13.173 -7.831  0.62 16.09 ?  138 HIS   A ND1  1 
ATOM   3072 N  ND1  B HIS   A 1 138 ? 15.129 -12.863 -7.928  0.38 13.94 ?  138 HIS   A ND1  1 
ATOM   3073 C  CD2  A HIS   A 1 138 ? 16.398 -11.353 -7.933  0.62 14.91 ?  138 HIS   A CD2  1 
ATOM   3074 C  CD2  B HIS   A 1 138 ? 16.210 -10.975 -7.748  0.38 12.73 ?  138 HIS   A CD2  1 
ATOM   3075 C  CE1  A HIS   A 1 138 ? 16.401 -13.527 -8.229  0.62 16.38 ?  138 HIS   A CE1  1 
ATOM   3076 C  CE1  B HIS   A 1 138 ? 16.373 -13.087 -8.313  0.38 13.89 ?  138 HIS   A CE1  1 
ATOM   3077 N  NE2  A HIS   A 1 138 ? 17.153 -12.442 -8.297  0.62 15.39 ?  138 HIS   A NE2  1 
ATOM   3078 N  NE2  B HIS   A 1 138 ? 17.051 -11.958 -8.212  0.38 13.22 ?  138 HIS   A NE2  1 
ATOM   3079 H  H    A HIS   A 1 138 ? 12.053 -10.147 -5.944  0.62 15.37 ?  138 HIS   A H    1 
ATOM   3080 H  H    B HIS   A 1 138 ? 11.981 -9.944  -5.711  0.38 14.54 ?  138 HIS   A H    1 
ATOM   3081 H  HA   A HIS   A 1 138 ? 13.256 -12.459 -5.840  0.62 15.75 ?  138 HIS   A HA   1 
ATOM   3082 H  HA   B HIS   A 1 138 ? 13.021 -12.345 -5.729  0.38 14.74 ?  138 HIS   A HA   1 
ATOM   3083 H  HB2  A HIS   A 1 138 ? 13.215 -11.274 -7.821  0.62 17.13 ?  138 HIS   A HB2  1 
ATOM   3084 H  HB2  B HIS   A 1 138 ? 13.003 -11.229 -7.706  0.38 15.01 ?  138 HIS   A HB2  1 
ATOM   3085 H  HB3  A HIS   A 1 138 ? 14.120 -10.139 -7.177  0.62 17.13 ?  138 HIS   A HB3  1 
ATOM   3086 H  HB3  B HIS   A 1 138 ? 13.786 -9.996  -7.084  0.38 15.01 ?  138 HIS   A HB3  1 
ATOM   3087 H  HD1  A HIS   A 1 138 ? 14.526 -13.707 -7.716  0.62 19.30 ?  138 HIS   A HD1  1 
ATOM   3088 H  HD1  B HIS   A 1 138 ? 14.502 -13.451 -7.908  0.38 16.72 ?  138 HIS   A HD1  1 
ATOM   3089 H  HD2  A HIS   A 1 138 ? 16.681 -10.468 -7.894  0.62 17.87 ?  138 HIS   A HD2  1 
ATOM   3090 H  HD2  B HIS   A 1 138 ? 16.433 -10.087 -7.586  0.38 15.26 ?  138 HIS   A HD2  1 
ATOM   3091 H  HE1  A HIS   A 1 138 ? 16.675 -14.391 -8.421  0.62 19.64 ?  138 HIS   A HE1  1 
ATOM   3092 H  HE1  B HIS   A 1 138 ? 16.714 -13.902 -8.601  0.38 16.65 ?  138 HIS   A HE1  1 
ATOM   3093 N  N    . SER   A 1 139 ? 14.792 -10.123 -4.262  1.00 12.06 ?  139 SER   A N    1 
ATOM   3094 C  CA   . SER   A 1 139 ? 15.867 -9.932  -3.299  1.00 11.79 ?  139 SER   A CA   1 
ATOM   3095 C  C    . SER   A 1 139 ? 15.651 -10.771 -2.046  1.00 11.16 ?  139 SER   A C    1 
ATOM   3096 O  O    . SER   A 1 139 ? 16.603 -11.359 -1.516  1.00 11.35 ?  139 SER   A O    1 
ATOM   3097 C  CB   . SER   A 1 139 ? 15.992 -8.453  -2.947  1.00 12.00 ?  139 SER   A CB   1 
ATOM   3098 O  OG   . SER   A 1 139 ? 17.071 -8.271  -2.046  1.00 12.20 ?  139 SER   A OG   1 
ATOM   3099 H  H    A SER   A 1 139 ? 14.340 -9.416  -4.456  0.62 14.46 ?  139 SER   A H    1 
ATOM   3100 H  H    B SER   A 1 139 ? 14.387 -9.398  -4.487  0.38 14.46 ?  139 SER   A H    1 
ATOM   3101 H  HA   . SER   A 1 139 ? 16.702 -10.212 -3.703  1.00 14.13 ?  139 SER   A HA   1 
ATOM   3102 H  HB2  . SER   A 1 139 ? 16.156 -7.942  -3.756  1.00 14.39 ?  139 SER   A HB2  1 
ATOM   3103 H  HB3  . SER   A 1 139 ? 15.169 -8.153  -2.525  1.00 14.39 ?  139 SER   A HB3  1 
ATOM   3104 H  HG   . SER   A 1 139 ? 17.148 -7.456  -1.849  1.00 14.63 ?  139 SER   A HG   1 
ATOM   3105 N  N    . LEU   A 1 140 ? 14.411 -10.833 -1.553  1.00 11.21 ?  140 LEU   A N    1 
ATOM   3106 C  CA   . LEU   A 1 140 ? 14.133 -11.650 -0.378  1.00 11.12 ?  140 LEU   A CA   1 
ATOM   3107 C  C    . LEU   A 1 140 ? 14.407 -13.122 -0.659  1.00 11.14 ?  140 LEU   A C    1 
ATOM   3108 O  O    . LEU   A 1 140 ? 14.970 -13.833 0.185   1.00 12.02 ?  140 LEU   A O    1 
ATOM   3109 C  CB   . LEU   A 1 140 ? 12.690 -11.432 0.070   1.00 11.67 ?  140 LEU   A CB   1 
ATOM   3110 C  CG   . LEU   A 1 140 ? 12.220 -12.294 1.243   1.00 12.07 ?  140 LEU   A CG   1 
ATOM   3111 C  CD1  . LEU   A 1 140 ? 13.111 -12.130 2.464   1.00 12.62 ?  140 LEU   A CD1  1 
ATOM   3112 C  CD2  . LEU   A 1 140 ? 10.766 -11.971 1.591   1.00 12.79 ?  140 LEU   A CD2  1 
ATOM   3113 H  H    . LEU   A 1 140 ? 13.732 -10.408 -1.867  1.00 13.44 ?  140 LEU   A H    1 
ATOM   3114 H  HA   . LEU   A 1 140 ? 14.712 -11.374 0.346   1.00 13.33 ?  140 LEU   A HA   1 
ATOM   3115 H  HB2  . LEU   A 1 140 ? 12.582 -10.511 0.333   1.00 13.99 ?  140 LEU   A HB2  1 
ATOM   3116 H  HB3  . LEU   A 1 140 ? 12.103 -11.631 -0.678  1.00 13.99 ?  140 LEU   A HB3  1 
ATOM   3117 H  HG   . LEU   A 1 140 ? 12.245 -13.230 0.983   1.00 14.47 ?  140 LEU   A HG   1 
ATOM   3118 H  HD11 . LEU   A 1 140 ? 12.727 -12.622 3.209   1.00 15.12 ?  140 LEU   A HD11 1 
ATOM   3119 H  HD12 . LEU   A 1 140 ? 13.992 -12.488 2.258   1.00 15.12 ?  140 LEU   A HD12 1 
ATOM   3120 H  HD13 . LEU   A 1 140 ? 13.178 -11.192 2.685   1.00 15.12 ?  140 LEU   A HD13 1 
ATOM   3121 H  HD21 . LEU   A 1 140 ? 10.470 -12.560 2.311   1.00 15.33 ?  140 LEU   A HD21 1 
ATOM   3122 H  HD22 . LEU   A 1 140 ? 10.702 -11.049 1.880   1.00 15.33 ?  140 LEU   A HD22 1 
ATOM   3123 H  HD23 . LEU   A 1 140 ? 10.209 -12.114 0.809   1.00 15.33 ?  140 LEU   A HD23 1 
ATOM   3124 N  N    . ARG   A 1 141 ? 14.012 -13.598 -1.842  1.00 11.70 ?  141 ARG   A N    1 
ATOM   3125 C  CA   . ARG   A 1 141 ? 14.252 -14.990 -2.204  1.00 12.68 ?  141 ARG   A CA   1 
ATOM   3126 C  C    . ARG   A 1 141 ? 15.748 -15.298 -2.228  1.00 12.16 ?  141 ARG   A C    1 
ATOM   3127 O  O    . ARG   A 1 141 ? 16.201 -16.315 -1.685  1.00 12.42 ?  141 ARG   A O    1 
ATOM   3128 C  CB   . ARG   A 1 141 ? 13.621 -15.263 -3.571  1.00 14.56 ?  141 ARG   A CB   1 
ATOM   3129 C  CG   . ARG   A 1 141 ? 13.611 -16.714 -3.998  1.00 17.45 ?  141 ARG   A CG   1 
ATOM   3130 C  CD   . ARG   A 1 141 ? 12.581 -17.471 -3.232  1.00 20.18 ?  141 ARG   A CD   1 
ATOM   3131 N  NE   . ARG   A 1 141 ? 13.198 -18.278 -2.197  1.00 21.01 ?  141 ARG   A NE   1 
ATOM   3132 C  CZ   . ARG   A 1 141 ? 12.533 -18.857 -1.206  1.00 21.71 ?  141 ARG   A CZ   1 
ATOM   3133 N  NH1  . ARG   A 1 141 ? 11.251 -18.606 -0.992  1.00 20.83 ?  141 ARG   A NH1  1 
ATOM   3134 N  NH2  . ARG   A 1 141 ? 13.176 -19.700 -0.401  1.00 22.89 ?  141 ARG   A NH2  1 
ATOM   3135 H  H    . ARG   A 1 141 ? 13.609 -13.138 -2.449  1.00 14.02 ?  141 ARG   A H    1 
ATOM   3136 H  HA   . ARG   A 1 141 ? 13.833 -15.570 -1.553  1.00 15.20 ?  141 ARG   A HA   1 
ATOM   3137 H  HB2  . ARG   A 1 141 ? 12.705 -14.949 -3.559  1.00 17.45 ?  141 ARG   A HB2  1 
ATOM   3138 H  HB3  . ARG   A 1 141 ? 14.121 -14.769 -4.241  1.00 17.45 ?  141 ARG   A HB3  1 
ATOM   3139 H  HG2  . ARG   A 1 141 ? 13.399 -16.775 -4.944  1.00 20.92 ?  141 ARG   A HG2  1 
ATOM   3140 H  HG3  . ARG   A 1 141 ? 14.481 -17.115 -3.825  1.00 20.92 ?  141 ARG   A HG3  1 
ATOM   3141 H  HD2  . ARG   A 1 141 ? 11.970 -16.850 -2.801  1.00 24.20 ?  141 ARG   A HD2  1 
ATOM   3142 H  HD3  . ARG   A 1 141 ? 12.089 -18.055 -3.835  1.00 24.20 ?  141 ARG   A HD3  1 
ATOM   3143 H  HE   . ARG   A 1 141 ? 14.024 -18.490 -2.295  1.00 25.20 ?  141 ARG   A HE   1 
ATOM   3144 H  HH11 . ARG   A 1 141 ? 10.819 -18.075 -1.512  1.00 24.98 ?  141 ARG   A HH11 1 
ATOM   3145 H  HH12 . ARG   A 1 141 ? 10.839 -18.992 -0.339  1.00 24.98 ?  141 ARG   A HH12 1 
ATOM   3146 H  HH21 . ARG   A 1 141 ? 14.007 -19.869 -0.529  1.00 27.46 ?  141 ARG   A HH21 1 
ATOM   3147 H  HH22 . ARG   A 1 141 ? 12.757 -20.073 0.255   1.00 27.46 ?  141 ARG   A HH22 1 
ATOM   3148 N  N    . VAL   A 1 142 ? 16.536 -14.432 -2.867  1.00 11.50 ?  142 VAL   A N    1 
ATOM   3149 C  CA   . VAL   A 1 142 ? 17.982 -14.641 -2.904  1.00 11.53 ?  142 VAL   A CA   1 
ATOM   3150 C  C    . VAL   A 1 142 ? 18.557 -14.619 -1.494  1.00 11.04 ?  142 VAL   A C    1 
ATOM   3151 O  O    . VAL   A 1 142 ? 19.425 -15.430 -1.153  1.00 11.79 ?  142 VAL   A O    1 
ATOM   3152 C  CB   . VAL   A 1 142 ? 18.671 -13.621 -3.829  1.00 12.02 ?  142 VAL   A CB   1 
ATOM   3153 C  CG1  . VAL   A 1 142 ? 20.181 -13.837 -3.806  1.00 12.07 ?  142 VAL   A CG1  1 
ATOM   3154 C  CG2  . VAL   A 1 142 ? 18.158 -13.753 -5.249  1.00 13.20 ?  142 VAL   A CG2  1 
ATOM   3155 H  H    . VAL   A 1 142 ? 16.268 -13.717 -3.273  1.00 13.78 ?  142 VAL   A H    1 
ATOM   3156 H  HA   . VAL   A 1 142 ? 18.156 -15.514 -3.276  1.00 13.82 ?  142 VAL   A HA   1 
ATOM   3157 H  HB   . VAL   A 1 142 ? 18.493 -12.714 -3.520  1.00 14.40 ?  142 VAL   A HB   1 
ATOM   3158 H  HG11 . VAL   A 1 142 ? 20.586 -13.349 -4.543  1.00 14.47 ?  142 VAL   A HG11 1 
ATOM   3159 H  HG12 . VAL   A 1 142 ? 20.541 -13.509 -2.964  1.00 14.47 ?  142 VAL   A HG12 1 
ATOM   3160 H  HG13 . VAL   A 1 142 ? 20.366 -14.783 -3.898  1.00 14.47 ?  142 VAL   A HG13 1 
ATOM   3161 H  HG21 . VAL   A 1 142 ? 18.623 -13.113 -5.813  1.00 15.82 ?  142 VAL   A HG21 1 
ATOM   3162 H  HG22 . VAL   A 1 142 ? 18.338 -14.655 -5.557  1.00 15.82 ?  142 VAL   A HG22 1 
ATOM   3163 H  HG23 . VAL   A 1 142 ? 17.210 -13.578 -5.255  1.00 15.82 ?  142 VAL   A HG23 1 
ATOM   3164 N  N    . CYS   A 1 143 ? 18.092 -13.694 -0.655  1.00 10.77 ?  143 CYS   A N    1 
ATOM   3165 C  CA   . CYS   A 1 143 ? 18.555 -13.653 0.729   1.00 11.13 ?  143 CYS   A CA   1 
ATOM   3166 C  C    . CYS   A 1 143 ? 18.325 -14.996 1.420   1.00 11.21 ?  143 CYS   A C    1 
ATOM   3167 O  O    . CYS   A 1 143 ? 19.243 -15.583 1.999   1.00 11.40 ?  143 CYS   A O    1 
ATOM   3168 C  CB   . CYS   A 1 143 ? 17.828 -12.538 1.475   1.00 11.82 ?  143 CYS   A CB   1 
ATOM   3169 S  SG   . CYS   A 1 143 ? 18.336 -12.357 3.195   1.00 11.99 ?  143 CYS   A SG   1 
ATOM   3170 H  H    . CYS   A 1 143 ? 17.520 -13.089 -0.863  1.00 12.91 ?  143 CYS   A H    1 
ATOM   3171 H  HA   . CYS   A 1 143 ? 19.505 -13.464 0.742   1.00 13.34 ?  143 CYS   A HA   1 
ATOM   3172 H  HB2  . CYS   A 1 143 ? 17.998 -11.697 1.028   1.00 14.17 ?  143 CYS   A HB2  1 
ATOM   3173 H  HB3  . CYS   A 1 143 ? 16.874 -12.727 1.460   1.00 14.17 ?  143 CYS   A HB3  1 
ATOM   3174 H  HG   . CYS   A 1 143 ? 17.732 -11.448 3.676   1.00 14.37 ?  143 CYS   A HG   1 
ATOM   3175 N  N    . VAL   A 1 144 ? 17.094 -15.499 1.361   1.00 11.72 ?  144 VAL   A N    1 
ATOM   3176 C  CA   . VAL   A 1 144 ? 16.753 -16.732 2.057   1.00 12.70 ?  144 VAL   A CA   1 
ATOM   3177 C  C    . VAL   A 1 144 ? 17.569 -17.900 1.529   1.00 12.33 ?  144 VAL   A C    1 
ATOM   3178 O  O    . VAL   A 1 144 ? 17.937 -18.810 2.285   1.00 13.05 ?  144 VAL   A O    1 
ATOM   3179 C  CB   . VAL   A 1 144 ? 15.237 -16.971 1.926   1.00 15.54 ?  144 VAL   A CB   1 
ATOM   3180 C  CG1  . VAL   A 1 144 ? 14.871 -18.400 2.246   1.00 17.39 ?  144 VAL   A CG1  1 
ATOM   3181 C  CG2  . VAL   A 1 144 ? 14.483 -15.975 2.813   1.00 15.60 ?  144 VAL   A CG2  1 
ATOM   3182 H  H    . VAL   A 1 144 ? 16.439 -15.141 0.923   1.00 14.05 ?  144 VAL   A H    1 
ATOM   3183 H  HA   . VAL   A 1 144 ? 16.950 -16.626 2.995   1.00 15.23 ?  144 VAL   A HA   1 
ATOM   3184 H  HB   . VAL   A 1 144 ? 14.968 -16.795 1.005   1.00 18.63 ?  144 VAL   A HB   1 
ATOM   3185 H  HG11 . VAL   A 1 144 ? 13.914 -18.450 2.418   1.00 20.85 ?  144 VAL   A HG11 1 
ATOM   3186 H  HG12 . VAL   A 1 144 ? 15.094 -18.965 1.491   1.00 20.85 ?  144 VAL   A HG12 1 
ATOM   3187 H  HG13 . VAL   A 1 144 ? 15.359 -18.681 3.033   1.00 20.85 ?  144 VAL   A HG13 1 
ATOM   3188 H  HG21 . VAL   A 1 144 ? 13.525 -16.123 2.723   1.00 18.71 ?  144 VAL   A HG21 1 
ATOM   3189 H  HG22 . VAL   A 1 144 ? 14.749 -16.103 3.736   1.00 18.71 ?  144 VAL   A HG22 1 
ATOM   3190 H  HG23 . VAL   A 1 144 ? 14.696 -15.067 2.533   1.00 18.71 ?  144 VAL   A HG23 1 
ATOM   3191 N  N    . ASP   A 1 145 ? 17.835 -17.916 0.227   1.00 12.37 ?  145 ASP   A N    1 
ATOM   3192 C  CA   . ASP   A 1 145 ? 18.545 -19.020 -0.407  1.00 13.22 ?  145 ASP   A CA   1 
ATOM   3193 C  C    . ASP   A 1 145 ? 20.065 -18.874 -0.366  1.00 13.04 ?  145 ASP   A C    1 
ATOM   3194 O  O    . ASP   A 1 145 ? 20.772 -19.764 -0.856  1.00 14.96 ?  145 ASP   A O    1 
ATOM   3195 C  CB   . ASP   A 1 145 ? 18.090 -19.158 -1.864  1.00 14.71 ?  145 ASP   A CB   1 
ATOM   3196 C  CG   . ASP   A 1 145 ? 16.640 -19.605 -1.992  1.00 16.71 ?  145 ASP   A CG   1 
ATOM   3197 O  OD1  . ASP   A 1 145 ? 16.075 -20.159 -1.022  1.00 17.13 ?  145 ASP   A OD1  1 
ATOM   3198 O  OD2  . ASP   A 1 145 ? 16.065 -19.394 -3.078  1.00 18.13 -1 145 ASP   A OD2  1 
ATOM   3199 H  H    . ASP   A 1 145 ? 17.602 -17.294 -0.321  1.00 14.82 ?  145 ASP   A H    1 
ATOM   3200 H  HA   . ASP   A 1 145 ? 18.309 -19.843 0.053   1.00 15.84 ?  145 ASP   A HA   1 
ATOM   3201 H  HB2  . ASP   A 1 145 ? 18.188 -18.299 -2.305  1.00 17.64 ?  145 ASP   A HB2  1 
ATOM   3202 H  HB3  . ASP   A 1 145 ? 18.645 -19.821 -2.303  1.00 17.64 ?  145 ASP   A HB3  1 
ATOM   3203 N  N    . THR   A 1 146 ? 20.589 -17.788 0.191   1.00 11.63 ?  146 THR   A N    1 
ATOM   3204 C  CA   . THR   A 1 146 ? 22.029 -17.544 0.211   1.00 11.15 ?  146 THR   A CA   1 
ATOM   3205 C  C    . THR   A 1 146 ? 22.587 -17.358 1.609   1.00 11.14 ?  146 THR   A C    1 
ATOM   3206 O  O    . THR   A 1 146 ? 23.663 -17.892 1.918   1.00 12.39 ?  146 THR   A O    1 
ATOM   3207 C  CB   . THR   A 1 146 ? 22.353 -16.294 -0.630  1.00 11.25 ?  146 THR   A CB   1 
ATOM   3208 O  OG1  . THR   A 1 146 ? 21.833 -16.460 -1.949  1.00 11.77 ?  146 THR   A OG1  1 
ATOM   3209 C  CG2  . THR   A 1 146 ? 23.852 -16.065 -0.718  1.00 11.90 ?  146 THR   A CG2  1 
ATOM   3210 H  H    . THR   A 1 146 ? 20.125 -17.160 0.558   1.00 13.94 ?  146 THR   A H    1 
ATOM   3211 H  HA   . THR   A 1 146 ? 22.485 -18.299 -0.186  1.00 13.36 ?  146 THR   A HA   1 
ATOM   3212 H  HB   . THR   A 1 146 ? 21.953 -15.512 -0.219  1.00 13.49 ?  146 THR   A HB   1 
ATOM   3213 H  HG1  . THR   A 1 146 ? 20.997 -16.540 -1.918  1.00 14.11 ?  146 THR   A HG1  1 
ATOM   3214 H  HG21 . THR   A 1 146 ? 24.042 -15.397 -1.395  1.00 14.26 ?  146 THR   A HG21 1 
ATOM   3215 H  HG22 . THR   A 1 146 ? 24.193 -15.755 0.135   1.00 14.26 ?  146 THR   A HG22 1 
ATOM   3216 H  HG23 . THR   A 1 146 ? 24.297 -16.892 -0.958  1.00 14.26 ?  146 THR   A HG23 1 
ATOM   3217 N  N    . VAL   A 1 147 ? 21.909 -16.578 2.443   1.00 11.14 ?  147 VAL   A N    1 
ATOM   3218 C  CA   . VAL   A 1 147 ? 22.399 -16.280 3.781   1.00 11.21 ?  147 VAL   A CA   1 
ATOM   3219 C  C    . VAL   A 1 147 ? 22.074 -17.449 4.698   1.00 11.85 ?  147 VAL   A C    1 
ATOM   3220 O  O    . VAL   A 1 147 ? 20.931 -17.926 4.740   1.00 12.48 ?  147 VAL   A O    1 
ATOM   3221 C  CB   . VAL   A 1 147 ? 21.782 -14.972 4.301   1.00 11.46 ?  147 VAL   A CB   1 
ATOM   3222 C  CG1  . VAL   A 1 147 ? 22.306 -14.656 5.678   1.00 12.44 ?  147 VAL   A CG1  1 
ATOM   3223 C  CG2  . VAL   A 1 147 ? 22.036 -13.822 3.332   1.00 11.72 ?  147 VAL   A CG2  1 
ATOM   3224 H  H    . VAL   A 1 147 ? 21.146 -16.217 2.260   1.00 13.35 ?  147 VAL   A H    1 
ATOM   3225 H  HA   . VAL   A 1 147 ? 23.359 -16.173 3.751   1.00 13.44 ?  147 VAL   A HA   1 
ATOM   3226 H  HB   . VAL   A 1 147 ? 20.823 -15.085 4.376   1.00 13.74 ?  147 VAL   A HB   1 
ATOM   3227 H  HG11 . VAL   A 1 147 ? 22.055 -13.751 5.913   1.00 14.92 ?  147 VAL   A HG11 1 
ATOM   3228 H  HG12 . VAL   A 1 147 ? 21.915 -15.280 6.315   1.00 14.92 ?  147 VAL   A HG12 1 
ATOM   3229 H  HG13 . VAL   A 1 147 ? 23.270 -14.746 5.678   1.00 14.92 ?  147 VAL   A HG13 1 
ATOM   3230 H  HG21 . VAL   A 1 147 ? 21.701 -13.001 3.727   1.00 14.05 ?  147 VAL   A HG21 1 
ATOM   3231 H  HG22 . VAL   A 1 147 ? 22.986 -13.752 3.172   1.00 14.05 ?  147 VAL   A HG22 1 
ATOM   3232 H  HG23 . VAL   A 1 147 ? 21.568 -14.005 2.503   1.00 14.05 ?  147 VAL   A HG23 1 
ATOM   3233 N  N    . ARG   A 1 148 ? 23.090 -17.915 5.425   1.00 11.93 ?  148 ARG   A N    1 
ATOM   3234 C  CA   . ARG   A 1 148 ? 22.959 -18.993 6.390   1.00 12.29 ?  148 ARG   A CA   1 
ATOM   3235 C  C    . ARG   A 1 148 ? 23.082 -18.521 7.826   1.00 12.64 ?  148 ARG   A C    1 
ATOM   3236 O  O    . ARG   A 1 148 ? 22.663 -19.243 8.739   1.00 14.32 ?  148 ARG   A O    1 
ATOM   3237 C  CB   . ARG   A 1 148 ? 23.996 -20.089 6.112   1.00 12.95 ?  148 ARG   A CB   1 
ATOM   3238 C  CG   . ARG   A 1 148 ? 23.836 -20.737 4.751   1.00 14.29 ?  148 ARG   A CG   1 
ATOM   3239 C  CD   . ARG   A 1 148 ? 24.918 -21.774 4.466   1.00 15.27 ?  148 ARG   A CD   1 
ATOM   3240 N  NE   . ARG   A 1 148 ? 26.256 -21.191 4.488   1.00 15.11 ?  148 ARG   A NE   1 
ATOM   3241 C  CZ   . ARG   A 1 148 ? 26.771 -20.461 3.506   1.00 14.49 ?  148 ARG   A CZ   1 
ATOM   3242 N  NH1  . ARG   A 1 148 ? 26.096 -20.227 2.391   1.00 14.79 ?  148 ARG   A NH1  1 
ATOM   3243 N  NH2  . ARG   A 1 148 ? 27.988 -19.930 3.655   1.00 14.95 ?  148 ARG   A NH2  1 
ATOM   3244 H  H    . ARG   A 1 148 ? 23.893 -17.606 5.364   1.00 14.29 ?  148 ARG   A H    1 
ATOM   3245 H  HA   . ARG   A 1 148 ? 22.086 -19.390 6.289   1.00 14.73 ?  148 ARG   A HA   1 
ATOM   3246 H  HB2  . ARG   A 1 148 ? 24.886 -19.711 6.154   1.00 15.53 ?  148 ARG   A HB2  1 
ATOM   3247 H  HB3  . ARG   A 1 148 ? 23.902 -20.791 6.777   1.00 15.53 ?  148 ARG   A HB3  1 
ATOM   3248 H  HG2  . ARG   A 1 148 ? 22.973 -21.173 4.710   1.00 17.14 ?  148 ARG   A HG2  1 
ATOM   3249 H  HG3  . ARG   A 1 148 ? 23.892 -20.045 4.070   1.00 17.14 ?  148 ARG   A HG3  1 
ATOM   3250 H  HD2  . ARG   A 1 148 ? 24.879 -22.467 5.142   1.00 18.31 ?  148 ARG   A HD2  1 
ATOM   3251 H  HD3  . ARG   A 1 148 ? 24.765 -22.157 3.586   1.00 18.31 ?  148 ARG   A HD3  1 
ATOM   3252 H  HE   . ARG   A 1 148 ? 26.743 -21.328 5.178   1.00 18.11 ?  148 ARG   A HE   1 
ATOM   3253 H  HH11 . ARG   A 1 148 ? 25.309 -20.552 2.283   1.00 17.73 ?  148 ARG   A HH11 1 
ATOM   3254 H  HH12 . ARG   A 1 148 ? 26.447 -19.742 1.768   1.00 17.73 ?  148 ARG   A HH12 1 
ATOM   3255 H  HH21 . ARG   A 1 148 ? 28.432 -20.066 4.378   1.00 17.92 ?  148 ARG   A HH21 1 
ATOM   3256 H  HH22 . ARG   A 1 148 ? 28.331 -19.446 3.028   1.00 17.92 ?  148 ARG   A HH22 1 
ATOM   3257 N  N    . THR   A 1 149 ? 23.629 -17.328 8.041   1.00 12.46 ?  149 THR   A N    1 
ATOM   3258 C  CA   . THR   A 1 149 ? 23.706 -16.729 9.358   1.00 12.59 ?  149 THR   A CA   1 
ATOM   3259 C  C    . THR   A 1 149 ? 22.383 -16.026 9.657   1.00 12.22 ?  149 THR   A C    1 
ATOM   3260 O  O    . THR   A 1 149 ? 21.454 -16.020 8.840   1.00 12.89 ?  149 THR   A O    1 
ATOM   3261 C  CB   . THR   A 1 149 ? 24.914 -15.800 9.420   1.00 13.16 ?  149 THR   A CB   1 
ATOM   3262 O  OG1  . THR   A 1 149 ? 24.791 -14.866 8.347   1.00 13.13 ?  149 THR   A OG1  1 
ATOM   3263 C  CG2  . THR   A 1 149 ? 26.219 -16.599 9.287   1.00 13.65 ?  149 THR   A CG2  1 
ATOM   3264 H  H    . THR   A 1 149 ? 23.974 -16.837 7.420   1.00 14.93 ?  149 THR   A H    1 
ATOM   3265 H  HA   . THR   A 1 149 ? 23.825 -17.428 10.016  1.00 15.09 ?  149 THR   A HA   1 
ATOM   3266 H  HB   . THR   A 1 149 ? 24.912 -15.328 10.265  1.00 15.77 ?  149 THR   A HB   1 
ATOM   3267 H  HG1  . THR   A 1 149 ? 25.446 -14.337 8.348   1.00 15.74 ?  149 THR   A HG1  1 
ATOM   3268 H  HG21 . THR   A 1 149 ? 26.980 -16.002 9.346   1.00 16.36 ?  149 THR   A HG21 1 
ATOM   3269 H  HG22 . THR   A 1 149 ? 26.280 -17.259 9.996   1.00 16.36 ?  149 THR   A HG22 1 
ATOM   3270 H  HG23 . THR   A 1 149 ? 26.246 -17.058 8.431   1.00 16.36 ?  149 THR   A HG23 1 
ATOM   3271 N  N    . ASN   A 1 150 ? 22.257 -15.486 10.862  1.00 12.47 ?  150 ASN   A N    1 
ATOM   3272 C  CA   . ASN   A 1 150 ? 20.976 -14.966 11.332  1.00 12.84 ?  150 ASN   A CA   1 
ATOM   3273 C  C    . ASN   A 1 150 ? 20.800 -13.530 10.866  1.00 12.17 ?  150 ASN   A C    1 
ATOM   3274 O  O    . ASN   A 1 150 ? 21.557 -12.641 11.273  1.00 13.49 ?  150 ASN   A O    1 
ATOM   3275 C  CB   . ASN   A 1 150 ? 20.907 -15.059 12.851  1.00 15.38 ?  150 ASN   A CB   1 
ATOM   3276 C  CG   . ASN   A 1 150 ? 20.810 -16.485 13.327  1.00 19.30 ?  150 ASN   A CG   1 
ATOM   3277 O  OD1  . ASN   A 1 150 ? 20.227 -17.327 12.647  1.00 20.47 ?  150 ASN   A OD1  1 
ATOM   3278 N  ND2  . ASN   A 1 150 ? 21.396 -16.775 14.485  1.00 21.56 ?  150 ASN   A ND2  1 
ATOM   3279 H  H    . ASN   A 1 150 ? 22.897 -15.415 11.431  1.00 14.95 ?  150 ASN   A H    1 
ATOM   3280 H  HA   . ASN   A 1 150 ? 20.254 -15.502 10.963  1.00 15.40 ?  150 ASN   A HA   1 
ATOM   3281 H  HB2  . ASN   A 1 150 ? 21.709 -14.669 13.232  1.00 18.44 ?  150 ASN   A HB2  1 
ATOM   3282 H  HB3  . ASN   A 1 150 ? 20.122 -14.586 13.168  1.00 18.44 ?  150 ASN   A HB3  1 
ATOM   3283 H  HD21 . ASN   A 1 150 ? 21.372 -17.579 14.799  1.00 25.85 ?  150 ASN   A HD21 1 
ATOM   3284 H  HD22 . ASN   A 1 150 ? 21.799 -16.158 14.932  1.00 25.85 ?  150 ASN   A HD22 1 
ATOM   3285 N  N    . VAL   A 1 151 ? 19.802 -13.299 10.020  1.00 11.68 ?  151 VAL   A N    1 
ATOM   3286 C  CA   . VAL   A 1 151 ? 19.593 -11.992 9.413   1.00 11.56 ?  151 VAL   A CA   1 
ATOM   3287 C  C    . VAL   A 1 151 ? 18.204 -11.477 9.771   1.00 11.55 ?  151 VAL   A C    1 
ATOM   3288 O  O    . VAL   A 1 151 ? 17.195 -12.189 9.627   1.00 12.91 ?  151 VAL   A O    1 
ATOM   3289 C  CB   . VAL   A 1 151 ? 19.886 -11.998 7.897   1.00 13.02 ?  151 VAL   A CB   1 
ATOM   3290 C  CG1  . VAL   A 1 151 ? 19.062 -13.027 7.160   1.00 14.10 ?  151 VAL   A CG1  1 
ATOM   3291 C  CG2  . VAL   A 1 151 ? 19.701 -10.604 7.300   1.00 13.18 ?  151 VAL   A CG2  1 
ATOM   3292 H  H    . VAL   A 1 151 ? 19.224 -13.892 9.778   1.00 14.00 ?  151 VAL   A H    1 
ATOM   3293 H  HA   . VAL   A 1 151 ? 20.232 -11.378 9.804   1.00 13.85 ?  151 VAL   A HA   1 
ATOM   3294 H  HB   . VAL   A 1 151 ? 20.819 -12.240 7.766   1.00 15.61 ?  151 VAL   A HB   1 
ATOM   3295 H  HG11 . VAL   A 1 151 ? 19.249 -12.973 6.208   1.00 16.91 ?  151 VAL   A HG11 1 
ATOM   3296 H  HG12 . VAL   A 1 151 ? 19.298 -13.916 7.486   1.00 16.91 ?  151 VAL   A HG12 1 
ATOM   3297 H  HG13 . VAL   A 1 151 ? 18.121 -12.862 7.321   1.00 16.91 ?  151 VAL   A HG13 1 
ATOM   3298 H  HG21 . VAL   A 1 151 ? 20.013 -10.611 6.377   1.00 15.80 ?  151 VAL   A HG21 1 
ATOM   3299 H  HG22 . VAL   A 1 151 ? 18.761 -10.369 7.324   1.00 15.80 ?  151 VAL   A HG22 1 
ATOM   3300 H  HG23 . VAL   A 1 151 ? 20.219 -9.968  7.815   1.00 15.80 ?  151 VAL   A HG23 1 
ATOM   3301 N  N    . TYR   A 1 152 ? 18.188 -10.230 10.250  1.00 11.80 ?  152 TYR   A N    1 
ATOM   3302 C  CA   . TYR   A 1 152 ? 16.994 -9.500  10.638  1.00 11.42 ?  152 TYR   A CA   1 
ATOM   3303 C  C    . TYR   A 1 152 ? 16.797 -8.400  9.604   1.00 10.98 ?  152 TYR   A C    1 
ATOM   3304 O  O    . TYR   A 1 152 ? 17.579 -7.443  9.545   1.00 11.33 ?  152 TYR   A O    1 
ATOM   3305 C  CB   . TYR   A 1 152 ? 17.180 -8.949  12.049  1.00 12.22 ?  152 TYR   A CB   1 
ATOM   3306 C  CG   . TYR   A 1 152 ? 17.124 -10.067 13.051  1.00 13.01 ?  152 TYR   A CG   1 
ATOM   3307 C  CD1  . TYR   A 1 152 ? 18.244 -10.832 13.336  1.00 14.35 ?  152 TYR   A CD1  1 
ATOM   3308 C  CD2  . TYR   A 1 152 ? 15.934 -10.406 13.673  1.00 13.72 ?  152 TYR   A CD2  1 
ATOM   3309 C  CE1  . TYR   A 1 152 ? 18.189 -11.885 14.223  1.00 15.85 ?  152 TYR   A CE1  1 
ATOM   3310 C  CE2  . TYR   A 1 152 ? 15.865 -11.467 14.570  1.00 15.29 ?  152 TYR   A CE2  1 
ATOM   3311 C  CZ   . TYR   A 1 152 ? 17.001 -12.200 14.840  1.00 15.93 ?  152 TYR   A CZ   1 
ATOM   3312 O  OH   . TYR   A 1 152 ? 16.949 -13.258 15.721  1.00 18.27 ?  152 TYR   A OH   1 
ATOM   3313 H  H    . TYR   A 1 152 ? 18.908 -9.758  10.353  1.00 14.15 ?  152 TYR   A H    1 
ATOM   3314 H  HA   . TYR   A 1 152 ? 16.226 -10.092 10.627  1.00 13.69 ?  152 TYR   A HA   1 
ATOM   3315 H  HB2  . TYR   A 1 152 ? 18.052 -8.527  12.117  1.00 14.65 ?  152 TYR   A HB2  1 
ATOM   3316 H  HB3  . TYR   A 1 152 ? 16.479 -8.317  12.249  1.00 14.65 ?  152 TYR   A HB3  1 
ATOM   3317 H  HD1  . TYR   A 1 152 ? 19.046 -10.626 12.916  1.00 17.20 ?  152 TYR   A HD1  1 
ATOM   3318 H  HD2  . TYR   A 1 152 ? 15.161 -9.910  13.484  1.00 16.45 ?  152 TYR   A HD2  1 
ATOM   3319 H  HE1  . TYR   A 1 152 ? 18.951 -12.378 14.403  1.00 19.00 ?  152 TYR   A HE1  1 
ATOM   3320 H  HE2  . TYR   A 1 152 ? 15.056 -11.671 14.982  1.00 18.33 ?  152 TYR   A HE2  1 
ATOM   3321 H  HH   . TYR   A 1 152 ? 16.169 -13.330 16.030  1.00 21.91 ?  152 TYR   A HH   1 
ATOM   3322 N  N    . LEU   A 1 153 ? 15.781 -8.562  8.762   1.00 11.11 ?  153 LEU   A N    1 
ATOM   3323 C  CA   . LEU   A 1 153 ? 15.529 -7.669  7.643   1.00 11.13 ?  153 LEU   A CA   1 
ATOM   3324 C  C    . LEU   A 1 153 ? 14.535 -6.590  8.038   1.00 11.33 ?  153 LEU   A C    1 
ATOM   3325 O  O    . LEU   A 1 153 ? 13.426 -6.892  8.493   1.00 12.28 ?  153 LEU   A O    1 
ATOM   3326 C  CB   . LEU   A 1 153 ? 14.971 -8.454  6.458   1.00 11.26 ?  153 LEU   A CB   1 
ATOM   3327 C  CG   . LEU   A 1 153 ? 15.910 -9.470  5.808   1.00 11.42 ?  153 LEU   A CG   1 
ATOM   3328 C  CD1  . LEU   A 1 153 ? 15.127 -10.369 4.862   1.00 11.82 ?  153 LEU   A CD1  1 
ATOM   3329 C  CD2  . LEU   A 1 153 ? 17.028 -8.757  5.053   1.00 11.92 ?  153 LEU   A CD2  1 
ATOM   3330 H  H    . LEU   A 1 153 ? 15.202 -9.200  8.827   1.00 13.32 ?  153 LEU   A H    1 
ATOM   3331 H  HA   . LEU   A 1 153 ? 16.358 -7.252  7.377   1.00 13.34 ?  153 LEU   A HA   1 
ATOM   3332 H  HB2  . LEU   A 1 153 ? 14.188 -8.941  6.761   1.00 13.50 ?  153 LEU   A HB2  1 
ATOM   3333 H  HB3  . LEU   A 1 153 ? 14.711 -7.822  5.771   1.00 13.50 ?  153 LEU   A HB3  1 
ATOM   3334 H  HG   . LEU   A 1 153 ? 16.319 -10.022 6.501   1.00 13.69 ?  153 LEU   A HG   1 
ATOM   3335 H  HD11 . LEU   A 1 153 ? 15.710 -11.068 4.533   1.00 14.16 ?  153 LEU   A HD11 1 
ATOM   3336 H  HD12 . LEU   A 1 153 ? 14.384 -10.760 5.349   1.00 14.16 ?  153 LEU   A HD12 1 
ATOM   3337 H  HD13 . LEU   A 1 153 ? 14.795 -9.834  4.126   1.00 14.16 ?  153 LEU   A HD13 1 
ATOM   3338 H  HD21 . LEU   A 1 153 ? 17.607 -9.423  4.654   1.00 14.29 ?  153 LEU   A HD21 1 
ATOM   3339 H  HD22 . LEU   A 1 153 ? 16.628 -8.206  4.364   1.00 14.29 ?  153 LEU   A HD22 1 
ATOM   3340 H  HD23 . LEU   A 1 153 ? 17.528 -8.209  5.673   1.00 14.29 ?  153 LEU   A HD23 1 
ATOM   3341 N  N    A ALA   A 1 154 ? 14.922 -5.337  7.834   0.62 11.31 ?  154 ALA   A N    1 
ATOM   3342 N  N    B ALA   A 1 154 ? 14.938 -5.333  7.869   0.38 11.22 ?  154 ALA   A N    1 
ATOM   3343 C  CA   A ALA   A 1 154 ? 14.041 -4.191  8.015   0.62 11.63 ?  154 ALA   A CA   1 
ATOM   3344 C  CA   B ALA   A 1 154 ? 14.109 -4.173  8.178   0.38 11.45 ?  154 ALA   A CA   1 
ATOM   3345 C  C    A ALA   A 1 154 ? 13.569 -3.720  6.645   0.62 11.12 ?  154 ALA   A C    1 
ATOM   3346 C  C    B ALA   A 1 154 ? 13.590 -3.613  6.858   0.38 10.77 ?  154 ALA   A C    1 
ATOM   3347 O  O    A ALA   A 1 154 ? 14.388 -3.389  5.782   0.62 11.73 ?  154 ALA   A O    1 
ATOM   3348 O  O    B ALA   A 1 154 ? 14.365 -3.108  6.042   0.38 10.62 ?  154 ALA   A O    1 
ATOM   3349 C  CB   A ALA   A 1 154 ? 14.778 -3.061  8.731   0.62 12.39 ?  154 ALA   A CB   1 
ATOM   3350 C  CB   B ALA   A 1 154 ? 14.921 -3.126  8.940   0.38 12.00 ?  154 ALA   A CB   1 
ATOM   3351 H  H    A ALA   A 1 154 ? 15.718 -5.117  7.579   0.62 13.56 ?  154 ALA   A H    1 
ATOM   3352 H  H    B ALA   A 1 154 ? 15.711 -5.117  7.553   0.38 13.45 ?  154 ALA   A H    1 
ATOM   3353 H  HA   A ALA   A 1 154 ? 13.270 -4.450  8.544   0.62 13.94 ?  154 ALA   A HA   1 
ATOM   3354 H  HA   B ALA   A 1 154 ? 13.354 -4.440  8.725   0.38 13.73 ?  154 ALA   A HA   1 
ATOM   3355 H  HB1  A ALA   A 1 154 ? 14.171 -2.311  8.841   0.62 14.85 ?  154 ALA   A HB1  1 
ATOM   3356 H  HB1  B ALA   A 1 154 ? 14.353 -2.363  9.139   0.38 14.39 ?  154 ALA   A HB1  1 
ATOM   3357 H  HB2  A ALA   A 1 154 ? 15.075 -3.375  9.599   0.62 14.85 ?  154 ALA   A HB2  1 
ATOM   3358 H  HB2  B ALA   A 1 154 ? 15.248 -3.516  9.767   0.38 14.39 ?  154 ALA   A HB2  1 
ATOM   3359 H  HB3  A ALA   A 1 154 ? 15.541 -2.792  8.196   0.62 14.85 ?  154 ALA   A HB3  1 
ATOM   3360 H  HB3  B ALA   A 1 154 ? 15.671 -2.842  8.392   0.38 14.39 ?  154 ALA   A HB3  1 
ATOM   3361 N  N    A VAL   A 1 155 ? 12.252 -3.690  6.457   0.32 9.62  ?  155 VAL   A N    1 
ATOM   3362 N  N    B VAL   A 1 155 ? 12.278 -3.708  6.657   0.38 9.76  ?  155 VAL   A N    1 
ATOM   3363 C  CA   A VAL   A 1 155 ? 11.617 -3.221  5.232   0.32 11.56 ?  155 VAL   A CA   1 
ATOM   3364 C  CA   B VAL   A 1 155 ? 11.612 -3.271  5.436   0.38 10.88 ?  155 VAL   A CA   1 
ATOM   3365 C  CA   T VAL   A 1 155 ? 11.588 -3.302  5.227   0.30 14.27 ?  155 VAL   A CA   1 
ATOM   3366 C  C    A VAL   A 1 155 ? 10.866 -1.939  5.573   0.32 12.31 ?  155 VAL   A C    1 
ATOM   3367 C  C    B VAL   A 1 155 ? 10.983 -1.912  5.696   0.38 11.55 ?  155 VAL   A C    1 
ATOM   3368 C  C    T VAL   A 1 155 ? 10.932 -1.953  5.533   0.30 14.01 ?  155 VAL   A C    1 
ATOM   3369 O  O    A VAL   A 1 155 ? 9.820  -1.983  6.233   0.32 12.27 ?  155 VAL   A O    1 
ATOM   3370 O  O    B VAL   A 1 155 ? 10.190 -1.760  6.634   0.38 10.95 ?  155 VAL   A O    1 
ATOM   3371 O  O    T VAL   A 1 155 ? 9.989  -1.874  6.321   0.30 13.82 ?  155 VAL   A O    1 
ATOM   3372 C  CB   A VAL   A 1 155 ? 10.680 -4.285  4.644   0.32 11.99 ?  155 VAL   A CB   1 
ATOM   3373 C  CB   B VAL   A 1 155 ? 10.544 -4.289  5.001   0.38 11.06 ?  155 VAL   A CB   1 
ATOM   3374 C  CB   T VAL   A 1 155 ? 10.586 -4.347  4.700   0.30 14.16 ?  155 VAL   A CB   1 
ATOM   3375 C  CG1  A VAL   A 1 155 ? 10.028 -3.781  3.368   0.32 12.70 ?  155 VAL   A CG1  1 
ATOM   3376 C  CG1  B VAL   A 1 155 ? 9.794  -3.793  3.768   0.38 11.77 ?  155 VAL   A CG1  1 
ATOM   3377 C  CG1  T VAL   A 1 155 ? 9.886  -3.836  3.455   0.30 14.52 ?  155 VAL   A CG1  1 
ATOM   3378 C  CG2  A VAL   A 1 155 ? 11.453 -5.571  4.378   0.32 12.45 ?  155 VAL   A CG2  1 
ATOM   3379 C  CG2  B VAL   A 1 155 ? 11.180 -5.640  4.738   0.38 11.34 ?  155 VAL   A CG2  1 
ATOM   3380 C  CG2  T VAL   A 1 155 ? 11.300 -5.662  4.406   0.30 14.27 ?  155 VAL   A CG2  1 
ATOM   3381 H  H    A VAL   A 1 155 ? 11.686 -3.962  7.050   0.32 11.53 ?  155 VAL   A H    1 
ATOM   3382 H  H    B VAL   A 1 155 ? 11.734 -4.027  7.240   0.38 11.70 ?  155 VAL   A H    1 
ATOM   3383 H  HA   A VAL   A 1 155 ? 12.297 -3.012  4.576   0.32 13.85 ?  155 VAL   A HA   1 
ATOM   3384 H  HA   B VAL   A 1 155 ? 12.262 -3.178  4.724   0.38 13.04 ?  155 VAL   A HA   1 
ATOM   3385 H  HB   A VAL   A 1 155 ? 9.977  -4.482  5.286   0.32 14.38 ?  155 VAL   A HB   1 
ATOM   3386 H  HB   B VAL   A 1 155 ? 9.900  -4.394  5.721   0.38 13.25 ?  155 VAL   A HB   1 
ATOM   3387 H  HB   T VAL   A 1 155 ? 9.916  -4.513  5.381   0.30 16.97 ?  155 VAL   A HB   1 
ATOM   3388 H  HG11 A VAL   A 1 155 ? 9.556  -4.515  2.946   0.32 15.22 ?  155 VAL   A HG11 1 
ATOM   3389 H  HG11 B VAL   A 1 155 ? 9.275  -4.524  3.402   0.38 14.11 ?  155 VAL   A HG11 1 
ATOM   3390 H  HG11 T VAL   A 1 155 ? 9.374  -4.560  3.065   0.30 17.40 ?  155 VAL   A HG11 1 
ATOM   3391 H  HG12 A VAL   A 1 155 ? 9.405  -3.071  3.588   0.32 15.22 ?  155 VAL   A HG12 1 
ATOM   3392 H  HG12 B VAL   A 1 155 ? 9.207  -3.065  4.022   0.38 14.11 ?  155 VAL   A HG12 1 
ATOM   3393 H  HG12 T VAL   A 1 155 ? 9.298  -3.106  3.700   0.30 17.40 ?  155 VAL   A HG12 1 
ATOM   3394 H  HG13 A VAL   A 1 155 ? 10.718 -3.446  2.775   0.32 15.22 ?  155 VAL   A HG13 1 
ATOM   3395 H  HG13 B VAL   A 1 155 ? 10.439 -3.484  3.111   0.38 14.11 ?  155 VAL   A HG13 1 
ATOM   3396 H  HG13 T VAL   A 1 155 ? 10.555 -3.526  2.824   0.30 17.40 ?  155 VAL   A HG13 1 
ATOM   3397 H  HG21 A VAL   A 1 155 ? 10.870 -6.206  3.938   0.32 14.93 ?  155 VAL   A HG21 1 
ATOM   3398 H  HG21 B VAL   A 1 155 ? 10.526 -6.216  4.321   0.38 13.59 ?  155 VAL   A HG21 1 
ATOM   3399 H  HG21 T VAL   A 1 155 ? 10.653 -6.307  4.080   0.30 17.11 ?  155 VAL   A HG21 1 
ATOM   3400 H  HG22 A VAL   A 1 155 ? 12.213 -5.369  3.809   0.32 14.93 ?  155 VAL   A HG22 1 
ATOM   3401 H  HG22 B VAL   A 1 155 ? 11.942 -5.518  4.148   0.38 13.59 ?  155 VAL   A HG22 1 
ATOM   3402 H  HG22 T VAL   A 1 155 ? 11.982 -5.508  3.732   0.30 17.11 ?  155 VAL   A HG22 1 
ATOM   3403 H  HG23 A VAL   A 1 155 ? 11.763 -5.936  5.223   0.32 14.93 ?  155 VAL   A HG23 1 
ATOM   3404 H  HG23 B VAL   A 1 155 ? 11.475 -6.020  5.581   0.38 13.59 ?  155 VAL   A HG23 1 
ATOM   3405 H  HG23 T VAL   A 1 155 ? 11.711 -5.989  5.222   0.30 17.11 ?  155 VAL   A HG23 1 
ATOM   3406 N  N    A PHE   A 1 156 ? 11.399 -0.796  5.125   0.32 13.04 ?  156 PHE   A N    1 
ATOM   3407 N  N    B PHE   A 1 156 ? 11.321 -0.931  4.857   0.38 12.35 ?  156 PHE   A N    1 
ATOM   3408 N  N    T PHE   A 1 156 ? 11.446 -0.899  4.890   0.30 14.10 ?  156 PHE   A N    1 
ATOM   3409 C  CA   A PHE   A 1 156 ? 10.846 0.506   5.506   0.32 14.22 ?  156 PHE   A CA   1 
ATOM   3410 C  CA   B PHE   A 1 156 ? 10.859 0.441   5.062   0.38 13.12 ?  156 PHE   A CA   1 
ATOM   3411 C  CA   T PHE   A 1 156 ? 11.028 0.469   5.198   0.30 14.49 ?  156 PHE   A CA   1 
ATOM   3412 C  C    A PHE   A 1 156 ? 9.379  0.643   5.104   0.32 14.15 ?  156 PHE   A C    1 
ATOM   3413 C  C    B PHE   A 1 156 ? 9.398  0.615   4.662   0.38 13.96 ?  156 PHE   A C    1 
ATOM   3414 C  C    T PHE   A 1 156 ? 9.570  0.710   4.830   0.30 14.83 ?  156 PHE   A C    1 
ATOM   3415 O  O    A PHE   A 1 156 ? 8.545  1.098   5.899   0.32 14.31 ?  156 PHE   A O    1 
ATOM   3416 O  O    B PHE   A 1 156 ? 8.621  1.254   5.384   0.38 14.51 ?  156 PHE   A O    1 
ATOM   3417 O  O    T PHE   A 1 156 ? 8.832  1.362   5.580   0.30 15.20 ?  156 PHE   A O    1 
ATOM   3418 C  CB   A PHE   A 1 156 ? 11.688 1.625   4.881   0.32 15.49 ?  156 PHE   A CB   1 
ATOM   3419 C  CB   B PHE   A 1 156 ? 11.748 1.385   4.245   0.38 12.64 ?  156 PHE   A CB   1 
ATOM   3420 C  CB   T PHE   A 1 156 ? 11.938 1.443   4.443   0.30 14.23 ?  156 PHE   A CB   1 
ATOM   3421 C  CG   A PHE   A 1 156 ? 11.170 3.011   5.170   0.32 16.65 ?  156 PHE   A CG   1 
ATOM   3422 C  CG   B PHE   A 1 156 ? 11.460 2.855   4.453   0.38 12.89 ?  156 PHE   A CG   1 
ATOM   3423 C  CG   T PHE   A 1 156 ? 11.564 2.899   4.602   0.30 14.54 ?  156 PHE   A CG   1 
ATOM   3424 C  CD1  A PHE   A 1 156 ? 11.078 3.465   6.473   0.32 17.35 ?  156 PHE   A CD1  1 
ATOM   3425 C  CD1  B PHE   A 1 156 ? 12.142 3.577   5.425   0.38 13.82 ?  156 PHE   A CD1  1 
ATOM   3426 C  CD1  T PHE   A 1 156 ? 11.891 3.592   5.760   0.30 15.16 ?  156 PHE   A CD1  1 
ATOM   3427 C  CD2  A PHE   A 1 156 ? 10.787 3.863   4.141   0.32 17.39 ?  156 PHE   A CD2  1 
ATOM   3428 C  CD2  B PHE   A 1 156 ? 10.545 3.520   3.651   0.38 14.13 ?  156 PHE   A CD2  1 
ATOM   3429 C  CD2  T PHE   A 1 156 ? 10.923 3.582   3.578   0.30 15.02 ?  156 PHE   A CD2  1 
ATOM   3430 C  CE1  A PHE   A 1 156 ? 10.608 4.734   6.751   0.32 17.76 ?  156 PHE   A CE1  1 
ATOM   3431 C  CE1  B PHE   A 1 156 ? 11.897 4.928   5.611   0.38 14.68 ?  156 PHE   A CE1  1 
ATOM   3432 C  CE1  T PHE   A 1 156 ? 11.563 4.930   5.903   0.30 15.76 ?  156 PHE   A CE1  1 
ATOM   3433 C  CE2  A PHE   A 1 156 ? 10.312 5.137   4.413   0.32 17.92 ?  156 PHE   A CE2  1 
ATOM   3434 C  CE2  B PHE   A 1 156 ? 10.293 4.870   3.835   0.38 15.27 ?  156 PHE   A CE2  1 
ATOM   3435 C  CE2  T PHE   A 1 156 ? 10.596 4.922   3.716   0.30 15.63 ?  156 PHE   A CE2  1 
ATOM   3436 C  CZ   A PHE   A 1 156 ? 10.227 5.572   5.720   0.32 18.06 ?  156 PHE   A CZ   1 
ATOM   3437 C  CZ   B PHE   A 1 156 ? 10.976 5.575   4.814   0.38 15.35 ?  156 PHE   A CZ   1 
ATOM   3438 C  CZ   T PHE   A 1 156 ? 10.917 5.595   4.880   0.30 16.04 ?  156 PHE   A CZ   1 
ATOM   3439 H  H    A PHE   A 1 156 ? 12.082 -0.748  4.605   0.32 15.63 ?  156 PHE   A H    1 
ATOM   3440 H  H    B PHE   A 1 156 ? 11.806 -1.040  4.153   0.38 14.81 ?  156 PHE   A H    1 
ATOM   3441 H  H    T PHE   A 1 156 ? 12.034 -0.953  4.267   0.30 16.90 ?  156 PHE   A H    1 
ATOM   3442 H  HA   A PHE   A 1 156 ? 10.900 0.608   6.468   0.32 17.05 ?  156 PHE   A HA   1 
ATOM   3443 H  HA   B PHE   A 1 156 ? 10.950 0.666   5.999   0.38 15.73 ?  156 PHE   A HA   1 
ATOM   3444 H  HA   T PHE   A 1 156 ? 11.131 0.631   6.147   0.30 17.37 ?  156 PHE   A HA   1 
ATOM   3445 H  HB2  A PHE   A 1 156 ? 12.595 1.574   5.229   0.32 18.57 ?  156 PHE   A HB2  1 
ATOM   3446 H  HB2  B PHE   A 1 156 ? 12.672 1.225   4.491   0.38 15.15 ?  156 PHE   A HB2  1 
ATOM   3447 H  HB2  T PHE   A 1 156 ? 12.845 1.334   4.767   0.30 17.06 ?  156 PHE   A HB2  1 
ATOM   3448 H  HB3  A PHE   A 1 156 ? 11.702 1.512   3.918   0.32 18.57 ?  156 PHE   A HB3  1 
ATOM   3449 H  HB3  B PHE   A 1 156 ? 11.623 1.187   3.303   0.38 15.15 ?  156 PHE   A HB3  1 
ATOM   3450 H  HB3  T PHE   A 1 156 ? 11.902 1.232   3.496   0.30 17.06 ?  156 PHE   A HB3  1 
ATOM   3451 H  HD1  A PHE   A 1 156 ? 11.335 2.908   7.172   0.32 20.81 ?  156 PHE   A HD1  1 
ATOM   3452 H  HD1  B PHE   A 1 156 ? 12.764 3.138   5.967   0.38 16.56 ?  156 PHE   A HD1  1 
ATOM   3453 H  HD1  T PHE   A 1 156 ? 12.325 3.148   6.453   0.30 18.18 ?  156 PHE   A HD1  1 
ATOM   3454 H  HD2  A PHE   A 1 156 ? 10.846 3.574   3.259   0.32 20.85 ?  156 PHE   A HD2  1 
ATOM   3455 H  HD2  B PHE   A 1 156 ? 10.086 3.050   2.994   0.38 16.94 ?  156 PHE   A HD2  1 
ATOM   3456 H  HD2  T PHE   A 1 156 ? 10.703 3.134   2.793   0.30 18.01 ?  156 PHE   A HD2  1 
ATOM   3457 H  HE1  A PHE   A 1 156 ? 10.550 5.025   7.633   0.32 21.30 ?  156 PHE   A HE1  1 
ATOM   3458 H  HE1  B PHE   A 1 156 ? 12.355 5.393   6.274   0.38 17.60 ?  156 PHE   A HE1  1 
ATOM   3459 H  HE1  T PHE   A 1 156 ? 11.781 5.379   6.689   0.30 18.90 ?  156 PHE   A HE1  1 
ATOM   3460 H  HE2  A PHE   A 1 156 ? 10.059 5.697   3.716   0.32 21.48 ?  156 PHE   A HE2  1 
ATOM   3461 H  HE2  B PHE   A 1 156 ? 9.674  5.302   3.298   0.38 18.31 ?  156 PHE   A HE2  1 
ATOM   3462 H  HE2  T PHE   A 1 156 ? 10.158 5.368   3.028   0.30 18.74 ?  156 PHE   A HE2  1 
ATOM   3463 H  HZ   A PHE   A 1 156 ? 9.909  6.426   5.909   0.32 21.66 ?  156 PHE   A HZ   1 
ATOM   3464 H  HZ   B PHE   A 1 156 ? 10.808 6.478   4.940   0.38 18.41 ?  156 PHE   A HZ   1 
ATOM   3465 H  HZ   T PHE   A 1 156 ? 10.696 6.492   4.977   0.30 19.23 ?  156 PHE   A HZ   1 
ATOM   3466 N  N    A ASP   A 1 157 ? 9.046  0.268   3.872   0.32 14.40 ?  157 ASP   A N    1 
ATOM   3467 N  N    B ASP   A 1 157 ? 9.009  0.052   3.524   0.38 14.77 ?  157 ASP   A N    1 
ATOM   3468 N  N    T ASP   A 1 157 ? 9.141  0.199   3.682   0.30 14.94 ?  157 ASP   A N    1 
ATOM   3469 C  CA   A ASP   A 1 157 ? 7.721  0.526   3.315   0.32 15.54 ?  157 ASP   A CA   1 
ATOM   3470 C  CA   B ASP   A 1 157 ? 7.716  0.332   2.915   0.38 15.80 ?  157 ASP   A CA   1 
ATOM   3471 C  CA   T ASP   A 1 157 ? 7.836  0.505   3.114   0.30 15.67 ?  157 ASP   A CA   1 
ATOM   3472 C  C    A ASP   A 1 157 ? 6.728  -0.519  3.820   0.32 16.02 ?  157 ASP   A C    1 
ATOM   3473 C  C    B ASP   A 1 157 ? 6.675  -0.670  3.408   0.38 15.67 ?  157 ASP   A C    1 
ATOM   3474 C  C    T ASP   A 1 157 ? 6.801  -0.476  3.657   0.30 16.55 ?  157 ASP   A C    1 
ATOM   3475 O  O    A ASP   A 1 157 ? 6.904  -1.717  3.573   0.32 15.59 ?  157 ASP   A O    1 
ATOM   3476 O  O    B ASP   A 1 157 ? 6.812  -1.876  3.179   0.38 14.71 ?  157 ASP   A O    1 
ATOM   3477 O  O    T ASP   A 1 157 ? 6.920  -1.688  3.445   0.30 16.08 ?  157 ASP   A O    1 
ATOM   3478 C  CB   A ASP   A 1 157 ? 7.806  0.491   1.791   0.32 16.44 ?  157 ASP   A CB   1 
ATOM   3479 C  CB   B ASP   A 1 157 ? 7.868  0.268   1.397   0.38 16.99 ?  157 ASP   A CB   1 
ATOM   3480 C  CB   T ASP   A 1 157 ? 7.942  0.384   1.597   0.30 15.70 ?  157 ASP   A CB   1 
ATOM   3481 C  CG   A ASP   A 1 157 ? 6.507  0.902   1.122   0.32 17.68 ?  157 ASP   A CG   1 
ATOM   3482 C  CG   B ASP   A 1 157 ? 6.659  0.785   0.671   0.38 18.05 ?  157 ASP   A CG   1 
ATOM   3483 C  CG   T ASP   A 1 157 ? 6.785  1.021   0.879   0.30 15.69 ?  157 ASP   A CG   1 
ATOM   3484 O  OD1  A ASP   A 1 157 ? 6.133  2.088   1.216   0.32 18.46 ?  157 ASP   A OD1  1 
ATOM   3485 O  OD1  B ASP   A 1 157 ? 5.570  0.204   0.862   0.38 18.48 ?  157 ASP   A OD1  1 
ATOM   3486 O  OD1  T ASP   A 1 157 ? 5.712  0.387   0.825   0.30 16.22 ?  157 ASP   A OD1  1 
ATOM   3487 O  OD2  A ASP   A 1 157 ? 5.854  0.034   0.503   0.32 17.87 -1 157 ASP   A OD2  1 
ATOM   3488 O  OD2  B ASP   A 1 157 ? 6.796  1.775   -0.080  0.38 18.38 -1 157 ASP   A OD2  1 
ATOM   3489 O  OD2  T ASP   A 1 157 ? 6.941  2.158   0.383   0.30 15.20 -1 157 ASP   A OD2  1 
ATOM   3490 H  H    A ASP   A 1 157 ? 9.577  -0.149  3.337   0.32 17.26 ?  157 ASP   A H    1 
ATOM   3491 H  H    B ASP   A 1 157 ? 9.485  -0.513  3.078   0.38 17.71 ?  157 ASP   A H    1 
ATOM   3492 H  H    T ASP   A 1 157 ? 9.603  -0.342  3.198   0.30 17.92 ?  157 ASP   A H    1 
ATOM   3493 H  HA   A ASP   A 1 157 ? 7.418  1.406   3.590   0.32 18.63 ?  157 ASP   A HA   1 
ATOM   3494 H  HA   B ASP   A 1 157 ? 7.426  1.217   3.164   0.38 18.95 ?  157 ASP   A HA   1 
ATOM   3495 H  HA   T ASP   A 1 157 ? 7.572  1.412   3.341   0.30 18.79 ?  157 ASP   A HA   1 
ATOM   3496 H  HB2  A ASP   A 1 157 ? 8.534  1.073   1.504   0.32 19.71 ?  157 ASP   A HB2  1 
ATOM   3497 H  HB2  B ASP   A 1 157 ? 8.640  0.797   1.138   0.38 20.37 ?  157 ASP   A HB2  1 
ATOM   3498 H  HB2  T ASP   A 1 157 ? 8.758  0.807   1.300   0.30 18.82 ?  157 ASP   A HB2  1 
ATOM   3499 H  HB3  A ASP   A 1 157 ? 7.989  -0.417  1.507   0.32 19.71 ?  157 ASP   A HB3  1 
ATOM   3500 H  HB3  B ASP   A 1 157 ? 7.998  -0.656  1.136   0.38 20.37 ?  157 ASP   A HB3  1 
ATOM   3501 H  HB3  T ASP   A 1 157 ? 7.963  -0.559  1.369   0.30 18.82 ?  157 ASP   A HB3  1 
ATOM   3502 N  N    A LYS   A 1 158 ? 5.677  -0.069  4.514   0.32 17.45 ?  158 LYS   A N    1 
ATOM   3503 N  N    B LYS   A 1 158 ? 5.631  -0.163  4.074   0.38 16.86 ?  158 LYS   A N    1 
ATOM   3504 N  N    T LYS   A 1 158 ? 5.781  0.045   4.346   0.30 18.14 ?  158 LYS   A N    1 
ATOM   3505 C  CA   A LYS   A 1 158 ? 4.717  -1.012  5.085   0.32 18.74 ?  158 LYS   A CA   1 
ATOM   3506 C  CA   B LYS   A 1 158 ? 4.615  -1.032  4.665   0.38 17.92 ?  158 LYS   A CA   1 
ATOM   3507 C  CA   T LYS   A 1 158 ? 4.796  -0.837  4.969   0.30 19.70 ?  158 LYS   A CA   1 
ATOM   3508 C  C    A LYS   A 1 158 ? 3.952  -1.755  3.997   0.32 18.20 ?  158 LYS   A C    1 
ATOM   3509 C  C    B LYS   A 1 158 ? 3.903  -1.860  3.601   0.38 17.21 ?  158 LYS   A C    1 
ATOM   3510 C  C    T LYS   A 1 158 ? 4.028  -1.637  3.924   0.30 19.58 ?  158 LYS   A C    1 
ATOM   3511 O  O    A LYS   A 1 158 ? 3.744  -2.970  4.098   0.32 18.49 ?  158 LYS   A O    1 
ATOM   3512 O  O    B LYS   A 1 158 ? 3.677  -3.061  3.784   0.38 16.89 ?  158 LYS   A O    1 
ATOM   3513 O  O    T LYS   A 1 158 ? 3.794  -2.838  4.101   0.30 19.73 ?  158 LYS   A O    1 
ATOM   3514 C  CB   A LYS   A 1 158 ? 3.753  -0.291  6.029   0.32 20.30 ?  158 LYS   A CB   1 
ATOM   3515 C  CB   B LYS   A 1 158 ? 3.615  -0.182  5.456   0.38 19.88 ?  158 LYS   A CB   1 
ATOM   3516 C  CB   T LYS   A 1 158 ? 3.833  -0.038  5.851   0.30 21.42 ?  158 LYS   A CB   1 
ATOM   3517 C  CG   A LYS   A 1 158 ? 2.522  -1.107  6.441   0.32 21.74 ?  158 LYS   A CG   1 
ATOM   3518 C  CG   B LYS   A 1 158 ? 2.330  -0.893  5.873   0.38 22.12 ?  158 LYS   A CG   1 
ATOM   3519 C  CG   T LYS   A 1 158 ? 2.615  -0.833  6.325   0.30 22.99 ?  158 LYS   A CG   1 
ATOM   3520 C  CD   A LYS   A 1 158 ? 2.878  -2.373  7.220   0.32 23.11 ?  158 LYS   A CD   1 
ATOM   3521 C  CD   B LYS   A 1 158 ? 2.589  -2.075  6.792   0.38 24.23 ?  158 LYS   A CD   1 
ATOM   3522 C  CD   T LYS   A 1 158 ? 3.002  -2.056  7.154   0.30 24.55 ?  158 LYS   A CD   1 
ATOM   3523 C  CE   A LYS   A 1 158 ? 1.621  -3.033  7.779   0.32 23.78 ?  158 LYS   A CE   1 
ATOM   3524 C  CE   B LYS   A 1 158 ? 1.296  -2.629  7.368   0.38 25.31 ?  158 LYS   A CE   1 
ATOM   3525 C  CE   T LYS   A 1 158 ? 1.766  -2.861  7.552   0.30 25.55 ?  158 LYS   A CE   1 
ATOM   3526 N  NZ   A LYS   A 1 158 ? 1.867  -4.391  8.344   0.32 24.10 ?  158 LYS   A NZ   1 
ATOM   3527 N  NZ   B LYS   A 1 158 ? 1.519  -3.842  8.209   0.38 25.83 ?  158 LYS   A NZ   1 
ATOM   3528 N  NZ   T LYS   A 1 158 ? 2.091  -4.082  8.346   0.30 26.10 ?  158 LYS   A NZ   1 
ATOM   3529 H  H    A LYS   A 1 158 ? 5.505  0.759   4.659   0.32 20.92 ?  158 LYS   A H    1 
ATOM   3530 H  H    B LYS   A 1 158 ? 5.495  0.670   4.196   0.38 20.21 ?  158 LYS   A H    1 
ATOM   3531 H  H    T LYS   A 1 158 ? 5.639  0.885   4.459   0.30 21.76 ?  158 LYS   A H    1 
ATOM   3532 H  HA   A LYS   A 1 158 ? 5.200  -1.670  5.607   0.32 22.47 ?  158 LYS   A HA   1 
ATOM   3533 H  HA   B LYS   A 1 158 ? 5.039  -1.646  5.287   0.38 21.48 ?  158 LYS   A HA   1 
ATOM   3534 H  HA   T LYS   A 1 158 ? 5.262  -1.466  5.539   0.30 23.62 ?  158 LYS   A HA   1 
ATOM   3535 H  HB2  A LYS   A 1 158 ? 4.231  -0.058  6.841   0.32 24.34 ?  158 LYS   A HB2  1 
ATOM   3536 H  HB2  B LYS   A 1 158 ? 4.049  0.128   6.269   0.38 23.84 ?  158 LYS   A HB2  1 
ATOM   3537 H  HB2  T LYS   A 1 158 ? 4.311  0.264   6.641   0.30 25.68 ?  158 LYS   A HB2  1 
ATOM   3538 H  HB3  A LYS   A 1 158 ? 3.437  0.515   5.594   0.32 24.34 ?  158 LYS   A HB3  1 
ATOM   3539 H  HB3  B LYS   A 1 158 ? 3.362  0.580   4.915   0.38 23.84 ?  158 LYS   A HB3  1 
ATOM   3540 H  HB3  T LYS   A 1 158 ? 3.510  0.727   5.352   0.30 25.68 ?  158 LYS   A HB3  1 
ATOM   3541 H  HG2  A LYS   A 1 158 ? 1.964  -0.558  7.012   0.32 26.07 ?  158 LYS   A HG2  1 
ATOM   3542 H  HG2  B LYS   A 1 158 ? 1.769  -0.265  6.354   0.38 26.53 ?  158 LYS   A HG2  1 
ATOM   3543 H  HG2  T LYS   A 1 158 ? 2.066  -0.262  6.883   0.30 27.57 ?  158 LYS   A HG2  1 
ATOM   3544 H  HG3  A LYS   A 1 158 ? 2.018  -1.367  5.652   0.32 26.07 ?  158 LYS   A HG3  1 
ATOM   3545 H  HG3  B LYS   A 1 158 ? 1.863  -1.214  5.087   0.38 26.53 ?  158 LYS   A HG3  1 
ATOM   3546 H  HG3  T LYS   A 1 158 ? 2.098  -1.134  5.560   0.30 27.57 ?  158 LYS   A HG3  1 
ATOM   3547 H  HD2  A LYS   A 1 158 ? 3.317  -3.004  6.631   0.32 27.72 ?  158 LYS   A HD2  1 
ATOM   3548 H  HD2  B LYS   A 1 158 ? 3.038  -2.782  6.299   0.38 29.06 ?  158 LYS   A HD2  1 
ATOM   3549 H  HD2  T LYS   A 1 158 ? 3.583  -2.632  6.634   0.30 29.45 ?  158 LYS   A HD2  1 
ATOM   3550 H  HD3  A LYS   A 1 158 ? 3.458  -2.141  7.962   0.32 27.72 ?  158 LYS   A HD3  1 
ATOM   3551 H  HD3  B LYS   A 1 158 ? 3.132  -1.784  7.537   0.38 29.06 ?  158 LYS   A HD3  1 
ATOM   3552 H  HD3  T LYS   A 1 158 ? 3.450  -1.767  7.964   0.30 29.45 ?  158 LYS   A HD3  1 
ATOM   3553 H  HE2  A LYS   A 1 158 ? 1.255  -2.476  8.484   0.32 28.52 ?  158 LYS   A HE2  1 
ATOM   3554 H  HE2  B LYS   A 1 158 ? 0.883  -1.948  7.923   0.38 30.36 ?  158 LYS   A HE2  1 
ATOM   3555 H  HE2  T LYS   A 1 158 ? 1.183  -2.302  8.089   0.30 30.65 ?  158 LYS   A HE2  1 
ATOM   3556 H  HE3  A LYS   A 1 158 ? 0.973  -3.123  7.065   0.32 28.52 ?  158 LYS   A HE3  1 
ATOM   3557 H  HE3  B LYS   A 1 158 ? 0.705  -2.870  6.640   0.38 30.36 ?  158 LYS   A HE3  1 
ATOM   3558 H  HE3  T LYS   A 1 158 ? 1.302  -3.145  6.749   0.30 30.65 ?  158 LYS   A HE3  1 
ATOM   3559 H  HZ1  A LYS   A 1 158 ? 1.107  -4.732  8.657   0.32 28.91 ?  158 LYS   A HZ1  1 
ATOM   3560 H  HZ1  B LYS   A 1 158 ? 0.740  -4.157  8.499   0.38 30.98 ?  158 LYS   A HZ1  1 
ATOM   3561 H  HZ1  T LYS   A 1 158 ? 1.343  -4.519  8.556   0.30 31.30 ?  158 LYS   A HZ1  1 
ATOM   3562 H  HZ2  A LYS   A 1 158 ? 2.187  -4.929  7.711   0.32 28.91 ?  158 LYS   A HZ2  1 
ATOM   3563 H  HZ2  B LYS   A 1 158 ? 1.927  -4.471  7.731   0.38 30.98 ?  158 LYS   A HZ2  1 
ATOM   3564 H  HZ2  T LYS   A 1 158 ? 2.617  -4.622  7.873   0.30 31.30 ?  158 LYS   A HZ2  1 
ATOM   3565 H  HZ3  A LYS   A 1 158 ? 2.458  -4.343  9.008   0.32 28.91 ?  158 LYS   A HZ3  1 
ATOM   3566 H  HZ3  B LYS   A 1 158 ? 2.029  -3.637  8.910   0.38 30.98 ?  158 LYS   A HZ3  1 
ATOM   3567 H  HZ3  T LYS   A 1 158 ? 2.511  -3.854  9.097   0.30 31.30 ?  158 LYS   A HZ3  1 
ATOM   3568 N  N    A ASN   A 1 159 ? 3.517  -1.048  2.953   0.32 17.70 ?  159 ASN   A N    1 
ATOM   3569 N  N    B ASN   A 1 159 ? 3.548  -1.238  2.477   0.38 17.74 ?  159 ASN   A N    1 
ATOM   3570 N  N    T ASN   A 1 159 ? 3.617  -0.994  2.839   0.30 19.68 ?  159 ASN   A N    1 
ATOM   3571 C  CA   A ASN   A 1 159 ? 2.838  -1.729  1.858   0.32 17.27 ?  159 ASN   A CA   1 
ATOM   3572 C  CA   B ASN   A 1 159 ? 2.843  -1.970  1.432   0.38 18.20 ?  159 ASN   A CA   1 
ATOM   3573 C  CA   T ASN   A 1 159 ? 2.889  -1.699  1.792   0.30 19.84 ?  159 ASN   A CA   1 
ATOM   3574 C  C    A ASN   A 1 159 ? 3.736  -2.795  1.240   0.32 16.07 ?  159 ASN   A C    1 
ATOM   3575 C  C    B ASN   A 1 159 ? 3.710  -3.091  0.858   0.38 17.12 ?  159 ASN   A C    1 
ATOM   3576 C  C    T ASN   A 1 159 ? 3.736  -2.797  1.150   0.30 19.68 ?  159 ASN   A C    1 
ATOM   3577 O  O    A ASN   A 1 159 ? 3.288  -3.916  0.975   0.32 15.94 ?  159 ASN   A O    1 
ATOM   3578 O  O    B ASN   A 1 159 ? 3.223  -4.202  0.616   0.38 17.51 ?  159 ASN   A O    1 
ATOM   3579 O  O    T ASN   A 1 159 ? 3.226  -3.868  0.829   0.30 19.67 ?  159 ASN   A O    1 
ATOM   3580 C  CB   A ASN   A 1 159 ? 2.353  -0.718  0.818   0.32 18.36 ?  159 ASN   A CB   1 
ATOM   3581 C  CB   B ASN   A 1 159 ? 2.358  -0.986  0.361   0.38 20.19 ?  159 ASN   A CB   1 
ATOM   3582 C  CB   T ASN   A 1 159 ? 2.369  -0.720  0.735   0.30 20.53 ?  159 ASN   A CB   1 
ATOM   3583 C  CG   A ASN   A 1 159 ? 1.125  0.046   1.283   0.32 19.79 ?  159 ASN   A CG   1 
ATOM   3584 C  CG   B ASN   A 1 159 ? 1.257  -0.068  0.875   0.38 22.30 ?  159 ASN   A CG   1 
ATOM   3585 C  CG   T ASN   A 1 159 ? 1.166  0.070   1.218   0.30 21.48 ?  159 ASN   A CG   1 
ATOM   3586 O  OD1  A ASN   A 1 159 ? 0.303  -0.487  2.026   0.32 20.69 ?  159 ASN   A OD1  1 
ATOM   3587 O  OD1  B ASN   A 1 159 ? 0.287  -0.532  1.472   0.38 23.23 ?  159 ASN   A OD1  1 
ATOM   3588 O  OD1  T ASN   A 1 159 ? 0.384  -0.416  2.035   0.30 22.06 ?  159 ASN   A OD1  1 
ATOM   3589 N  ND2  A ASN   A 1 159 ? 0.997  1.295   0.849   0.32 20.28 ?  159 ASN   A ND2  1 
ATOM   3590 N  ND2  B ASN   A 1 159 ? 1.406  1.239   0.655   0.38 23.28 ?  159 ASN   A ND2  1 
ATOM   3591 N  ND2  T ASN   A 1 159 ? 1.011  1.289   0.716   0.30 21.85 ?  159 ASN   A ND2  1 
ATOM   3592 H  H    A ASN   A 1 159 ? 3.603  -0.200  2.858   0.32 21.23 ?  159 ASN   A H    1 
ATOM   3593 H  H    B ASN   A 1 159 ? 3.713  -0.417  2.300   0.38 21.27 ?  159 ASN   A H    1 
ATOM   3594 H  H    T ASN   A 1 159 ? 3.737  -0.155  2.692   0.30 23.60 ?  159 ASN   A H    1 
ATOM   3595 H  HA   A ASN   A 1 159 ? 2.056  -2.182  2.209   0.32 20.71 ?  159 ASN   A HA   1 
ATOM   3596 H  HA   B ASN   A 1 159 ? 2.056  -2.380  1.820   0.38 21.82 ?  159 ASN   A HA   1 
ATOM   3597 H  HA   T ASN   A 1 159 ? 2.122  -2.132  2.191   0.30 23.79 ?  159 ASN   A HA   1 
ATOM   3598 H  HB2  A ASN   A 1 159 ? 3.054  -0.074  0.645   0.32 22.02 ?  159 ASN   A HB2  1 
ATOM   3599 H  HB2  B ASN   A 1 159 ? 3.096  -0.426  0.079   0.38 24.21 ?  159 ASN   A HB2  1 
ATOM   3600 H  HB2  T ASN   A 1 159 ? 3.069  -0.090  0.511   0.30 24.62 ?  159 ASN   A HB2  1 
ATOM   3601 H  HB3  A ASN   A 1 159 ? 2.122  -1.187  -0.002  0.32 22.02 ?  159 ASN   A HB3  1 
ATOM   3602 H  HB3  B ASN   A 1 159 ? 2.000  -1.477  -0.391  0.38 24.21 ?  159 ASN   A HB3  1 
ATOM   3603 H  HB3  T ASN   A 1 159 ? 2.106  -1.220  -0.056  0.30 24.62 ?  159 ASN   A HB3  1 
ATOM   3604 H  HD21 A ASN   A 1 159 ? 0.319  1.764   1.084   0.32 24.32 ?  159 ASN   A HD21 1 
ATOM   3605 H  HD21 B ASN   A 1 159 ? 0.808  1.798   0.932   0.38 27.91 ?  159 ASN   A HD21 1 
ATOM   3606 H  HD21 T ASN   A 1 159 ? 0.344  1.772   0.958   0.30 26.20 ?  159 ASN   A HD21 1 
ATOM   3607 H  HD22 A ASN   A 1 159 ? 1.597  1.634   0.336   0.32 24.32 ?  159 ASN   A HD22 1 
ATOM   3608 H  HD22 B ASN   A 1 159 ? 2.098  1.528   0.238   0.38 27.91 ?  159 ASN   A HD22 1 
ATOM   3609 H  HD22 T ASN   A 1 159 ? 1.583  1.593   0.151   0.30 26.20 ?  159 ASN   A HD22 1 
ATOM   3610 N  N    A LEU   A 1 160 ? 5.016  -2.483  1.039   0.32 14.86 ?  160 LEU   A N    1 
ATOM   3611 N  N    B LEU   A 1 160 ? 5.008  -2.839  0.680   0.38 15.75 ?  160 LEU   A N    1 
ATOM   3612 N  N    T LEU   A 1 160 ? 5.029  -2.545  0.980   0.30 19.50 ?  160 LEU   A N    1 
ATOM   3613 C  CA   A LEU   A 1 160 ? 5.918  -3.500  0.510   0.32 13.69 ?  160 LEU   A CA   1 
ATOM   3614 C  CA   B LEU   A 1 160 ? 5.900  -3.890  0.196   0.38 15.01 ?  160 LEU   A CA   1 
ATOM   3615 C  CA   T LEU   A 1 160 ? 5.902  -3.524  0.343   0.30 19.47 ?  160 LEU   A CA   1 
ATOM   3616 C  C    A LEU   A 1 160 ? 6.081  -4.652  1.491   0.32 12.97 ?  160 LEU   A C    1 
ATOM   3617 C  C    B LEU   A 1 160 ? 6.081  -4.983  1.246   0.38 13.86 ?  160 LEU   A C    1 
ATOM   3618 O  O    A LEU   A 1 160 ? 6.099  -5.820  1.086   0.32 12.54 ?  160 LEU   A O    1 
ATOM   3619 O  O    B LEU   A 1 160 ? 6.087  -6.173  0.915   0.38 13.75 ?  160 LEU   A O    1 
ATOM   3620 C  CB   A LEU   A 1 160 ? 7.275  -2.895  0.157   0.32 13.05 ?  160 LEU   A CB   1 
ATOM   3621 C  CB   B LEU   A 1 160 ? 7.251  -3.291  -0.199  0.38 15.60 ?  160 LEU   A CB   1 
ATOM   3622 C  CB   T LEU   A 1 160 ? 7.347  -3.031  0.330   0.30 19.46 ?  160 LEU   A CB   1 
ATOM   3623 C  CG   A LEU   A 1 160 ? 8.291  -3.949  -0.297  0.32 12.65 ?  160 LEU   A CG   1 
ATOM   3624 C  CG   B LEU   A 1 160 ? 7.303  -2.355  -1.411  0.38 17.22 ?  160 LEU   A CG   1 
ATOM   3625 C  CG   T LEU   A 1 160 ? 8.226  -3.540  -0.813  0.30 19.48 ?  160 LEU   A CG   1 
ATOM   3626 C  CD1  A LEU   A 1 160 ? 7.801  -4.683  -1.531  0.32 13.50 ?  160 LEU   A CD1  1 
ATOM   3627 C  CD1  B LEU   A 1 160 ? 8.666  -1.685  -1.528  0.38 17.81 ?  160 LEU   A CD1  1 
ATOM   3628 C  CD1  T LEU   A 1 160 ? 9.688  -3.451  -0.429  0.30 19.19 ?  160 LEU   A CD1  1 
ATOM   3629 C  CD2  A LEU   A 1 160 ? 9.623  -3.288  -0.575  0.32 12.82 ?  160 LEU   A CD2  1 
ATOM   3630 C  CD2  B LEU   A 1 160 ? 6.983  -3.126  -2.680  0.38 17.54 ?  160 LEU   A CD2  1 
ATOM   3631 C  CD2  T LEU   A 1 160 ? 7.859  -4.956  -1.214  0.30 19.27 ?  160 LEU   A CD2  1 
ATOM   3632 H  H    A LEU   A 1 160 ? 5.375  -1.716  1.205   0.32 17.81 ?  160 LEU   A H    1 
ATOM   3633 H  H    B LEU   A 1 160 ? 5.390  -2.089  0.844   0.38 18.88 ?  160 LEU   A H    1 
ATOM   3634 H  H    T LEU   A 1 160 ? 5.426  -1.819  1.228   0.30 23.39 ?  160 LEU   A H    1 
ATOM   3635 H  HA   A LEU   A 1 160 ? 5.536  -3.853  -0.302  0.32 16.42 ?  160 LEU   A HA   1 
ATOM   3636 H  HA   B LEU   A 1 160 ? 5.508  -4.294  -0.596  0.38 17.99 ?  160 LEU   A HA   1 
ATOM   3637 H  HB2  A LEU   A 1 160 ? 7.165  -2.247  -0.563  0.32 15.64 ?  160 LEU   A HB2  1 
ATOM   3638 H  HB2  B LEU   A 1 160 ? 7.585  -2.790  0.559   0.38 18.70 ?  160 LEU   A HB2  1 
ATOM   3639 H  HB2  T LEU   A 1 160 ? 7.324  -2.069  0.246   0.30 23.33 ?  160 LEU   A HB2  1 
ATOM   3640 H  HB3  A LEU   A 1 160 ? 7.640  -2.453  0.941   0.32 15.64 ?  160 LEU   A HB3  1 
ATOM   3641 H  HB3  B LEU   A 1 160 ? 7.856  -4.024  -0.387  0.38 18.70 ?  160 LEU   A HB3  1 
ATOM   3642 H  HB3  T LEU   A 1 160 ? 7.772  -3.277  1.171   0.30 23.33 ?  160 LEU   A HB3  1 
ATOM   3643 H  HG   A LEU   A 1 160 ? 8.428  -4.594  0.410   0.32 15.16 ?  160 LEU   A HG   1 
ATOM   3644 H  HG   B LEU   A 1 160 ? 6.639  -1.659  -1.303  0.38 20.64 ?  160 LEU   A HG   1 
ATOM   3645 H  HG   T LEU   A 1 160 ? 8.090  -2.966  -1.585  0.30 23.36 ?  160 LEU   A HG   1 
ATOM   3646 H  HD11 A LEU   A 1 160 ? 8.523  -5.225  -1.880  0.32 16.18 ?  160 LEU   A HD11 1 
ATOM   3647 H  HD11 B LEU   A 1 160 ? 8.591  -0.916  -2.114  0.38 21.35 ?  160 LEU   A HD11 1 
ATOM   3648 H  HD11 T LEU   A 1 160 ? 10.228 -3.742  -1.180  0.30 23.02 ?  160 LEU   A HD11 1 
ATOM   3649 H  HD12 A LEU   A 1 160 ? 7.051  -5.249  -1.285  0.32 16.18 ?  160 LEU   A HD12 1 
ATOM   3650 H  HD12 B LEU   A 1 160 ? 8.961  -1.403  -0.648  0.38 21.35 ?  160 LEU   A HD12 1 
ATOM   3651 H  HD12 T LEU   A 1 160 ? 9.900  -2.532  -0.204  0.30 23.02 ?  160 LEU   A HD12 1 
ATOM   3652 H  HD13 A LEU   A 1 160 ? 7.521  -4.033  -2.195  0.32 16.18 ?  160 LEU   A HD13 1 
ATOM   3653 H  HD13 B LEU   A 1 160 ? 9.299  -2.322  -1.895  0.38 21.35 ?  160 LEU   A HD13 1 
ATOM   3654 H  HD13 T LEU   A 1 160 ? 9.846  -4.025  0.337   0.30 23.02 ?  160 LEU   A HD13 1 
ATOM   3655 H  HD21 A LEU   A 1 160 ? 10.258 -3.966  -0.858  0.32 15.37 ?  160 LEU   A HD21 1 
ATOM   3656 H  HD21 B LEU   A 1 160 ? 7.099  -2.540  -3.444  0.38 21.03 ?  160 LEU   A HD21 1 
ATOM   3657 H  HD21 T LEU   A 1 160 ? 8.556  -5.309  -1.788  0.30 23.11 ?  160 LEU   A HD21 1 
ATOM   3658 H  HD22 A LEU   A 1 160 ? 9.511  -2.628  -1.279  0.32 15.37 ?  160 LEU   A HD22 1 
ATOM   3659 H  HD22 B LEU   A 1 160 ? 7.588  -3.883  -2.750  0.38 21.03 ?  160 LEU   A HD22 1 
ATOM   3660 H  HD22 T LEU   A 1 160 ? 7.779  -5.498  -0.416  0.30 23.11 ?  160 LEU   A HD22 1 
ATOM   3661 H  HD23 A LEU   A 1 160 ? 9.940  -2.856  0.234   0.32 15.37 ?  160 LEU   A HD23 1 
ATOM   3662 H  HD23 B LEU   A 1 160 ? 6.067  -3.439  -2.637  0.38 21.03 ?  160 LEU   A HD23 1 
ATOM   3663 H  HD23 T LEU   A 1 160 ? 7.014  -4.940  -1.691  0.30 23.11 ?  160 LEU   A HD23 1 
ATOM   3664 N  N    A TYR   A 1 161 ? 6.212  -4.346  2.783   0.62 14.30 ?  161 TYR   A N    1 
ATOM   3665 N  N    B TYR   A 1 161 ? 6.243  -4.598  2.515   0.38 13.80 ?  161 TYR   A N    1 
ATOM   3666 C  CA   A TYR   A 1 161 ? 6.341  -5.403  3.779   0.62 14.52 ?  161 TYR   A CA   1 
ATOM   3667 C  CA   B TYR   A 1 161 ? 6.338  -5.578  3.596   0.38 13.75 ?  161 TYR   A CA   1 
ATOM   3668 C  C    A TYR   A 1 161 ? 5.191  -6.398  3.682   0.62 15.39 ?  161 TYR   A C    1 
ATOM   3669 C  C    B TYR   A 1 161 ? 5.138  -6.517  3.586   0.38 14.27 ?  161 TYR   A C    1 
ATOM   3670 O  O    A TYR   A 1 161 ? 5.403  -7.616  3.661   0.62 15.12 ?  161 TYR   A O    1 
ATOM   3671 O  O    B TYR   A 1 161 ? 5.288  -7.742  3.658   0.38 13.78 ?  161 TYR   A O    1 
ATOM   3672 C  CB   A TYR   A 1 161 ? 6.411  -4.804  5.182   0.62 14.62 ?  161 TYR   A CB   1 
ATOM   3673 C  CB   B TYR   A 1 161 ? 6.445  -4.862  4.949   0.38 13.73 ?  161 TYR   A CB   1 
ATOM   3674 C  CG   A TYR   A 1 161 ? 6.318  -5.858  6.247   0.62 14.26 ?  161 TYR   A CG   1 
ATOM   3675 C  CG   B TYR   A 1 161 ? 6.355  -5.782  6.159   0.38 13.50 ?  161 TYR   A CG   1 
ATOM   3676 C  CD1  A TYR   A 1 161 ? 7.435  -6.585  6.621   0.62 14.27 ?  161 TYR   A CD1  1 
ATOM   3677 C  CD1  B TYR   A 1 161 ? 7.473  -6.465  6.624   0.38 13.49 ?  161 TYR   A CD1  1 
ATOM   3678 C  CD2  A TYR   A 1 161 ? 5.109  -6.145  6.863   0.62 14.20 ?  161 TYR   A CD2  1 
ATOM   3679 C  CD2  B TYR   A 1 161 ? 5.155  -5.955  6.844   0.38 13.44 ?  161 TYR   A CD2  1 
ATOM   3680 C  CE1  A TYR   A 1 161 ? 7.351  -7.558  7.580   0.62 13.76 ?  161 TYR   A CE1  1 
ATOM   3681 C  CE1  B TYR   A 1 161 ? 7.394  -7.308  7.726   0.38 13.38 ?  161 TYR   A CE1  1 
ATOM   3682 C  CE2  A TYR   A 1 161 ? 5.014  -7.117  7.823   0.62 14.03 ?  161 TYR   A CE2  1 
ATOM   3683 C  CE2  B TYR   A 1 161 ? 5.069  -6.796  7.949   0.38 13.44 ?  161 TYR   A CE2  1 
ATOM   3684 C  CZ   A TYR   A 1 161 ? 6.142  -7.823  8.178   0.62 13.65 ?  161 TYR   A CZ   1 
ATOM   3685 C  CZ   B TYR   A 1 161 ? 6.193  -7.469  8.384   0.38 13.57 ?  161 TYR   A CZ   1 
ATOM   3686 O  OH   A TYR   A 1 161 ? 6.078  -8.795  9.143   0.62 13.89 ?  161 TYR   A OH   1 
ATOM   3687 O  OH   B TYR   A 1 161 ? 6.124  -8.310  9.478   0.38 14.31 ?  161 TYR   A OH   1 
ATOM   3688 H  H    A TYR   A 1 161 ? 6.227  -3.543  3.104   0.62 17.14 ?  161 TYR   A H    1 
ATOM   3689 H  H    B TYR   A 1 161 ? 6.299  -3.782  2.766   0.38 16.54 ?  161 TYR   A H    1 
ATOM   3690 H  HA   A TYR   A 1 161 ? 7.161  -5.885  3.620   0.62 17.40 ?  161 TYR   A HA   1 
ATOM   3691 H  HA   B TYR   A 1 161 ? 7.140  -6.110  3.471   0.38 16.48 ?  161 TYR   A HA   1 
ATOM   3692 H  HB2  A TYR   A 1 161 ? 7.262  -4.343  5.289   0.62 17.53 ?  161 TYR   A HB2  1 
ATOM   3693 H  HB2  B TYR   A 1 161 ? 7.301  -4.404  4.988   0.38 16.46 ?  161 TYR   A HB2  1 
ATOM   3694 H  HB3  A TYR   A 1 161 ? 5.679  -4.181  5.307   0.62 17.53 ?  161 TYR   A HB3  1 
ATOM   3695 H  HB3  B TYR   A 1 161 ? 5.727  -4.214  5.013   0.38 16.46 ?  161 TYR   A HB3  1 
ATOM   3696 H  HD1  A TYR   A 1 161 ? 8.253  -6.413  6.215   0.62 17.11 ?  161 TYR   A HD1  1 
ATOM   3697 H  HD1  B TYR   A 1 161 ? 8.286  -6.364  6.186   0.38 16.17 ?  161 TYR   A HD1  1 
ATOM   3698 H  HD2  A TYR   A 1 161 ? 4.346  -5.671  6.620   0.62 17.03 ?  161 TYR   A HD2  1 
ATOM   3699 H  HD2  B TYR   A 1 161 ? 4.395  -5.505  6.556   0.38 16.11 ?  161 TYR   A HD2  1 
ATOM   3700 H  HE1  A TYR   A 1 161 ? 8.106  -8.043  7.822   0.62 16.50 ?  161 TYR   A HE1  1 
ATOM   3701 H  HE1  B TYR   A 1 161 ? 8.152  -7.761  8.027   0.38 16.04 ?  161 TYR   A HE1  1 
ATOM   3702 H  HE2  A TYR   A 1 161 ? 4.193  -7.299  8.226   0.62 16.82 ?  161 TYR   A HE2  1 
ATOM   3703 H  HE2  B TYR   A 1 161 ? 4.257  -6.901  8.397   0.38 16.11 ?  161 TYR   A HE2  1 
ATOM   3704 H  HH   A TYR   A 1 161 ? 5.284  -8.870  9.423   0.62 16.65 ?  161 TYR   A HH   1 
ATOM   3705 H  HH   B TYR   A 1 161 ? 5.338  -8.319  9.794   0.38 17.15 ?  161 TYR   A HH   1 
ATOM   3706 N  N    A ASP   A 1 162 ? 3.955  -5.895  3.628   0.62 16.41 ?  162 ASP   A N    1 
ATOM   3707 N  N    B ASP   A 1 162 ? 3.931  -5.952  3.500   0.38 15.19 ?  162 ASP   A N    1 
ATOM   3708 C  CA   A ASP   A 1 162 ? 2.804  -6.794  3.563   0.62 17.39 ?  162 ASP   A CA   1 
ATOM   3709 C  CA   B ASP   A 1 162 ? 2.726  -6.776  3.453   0.38 16.12 ?  162 ASP   A CA   1 
ATOM   3710 C  C    A ASP   A 1 162 ? 2.858  -7.663  2.313   0.62 17.54 ?  162 ASP   A C    1 
ATOM   3711 C  C    B ASP   A 1 162 ? 2.782  -7.758  2.288   0.38 16.33 ?  162 ASP   A C    1 
ATOM   3712 O  O    A ASP   A 1 162 ? 2.477  -8.839  2.346   0.62 17.95 ?  162 ASP   A O    1 
ATOM   3713 O  O    B ASP   A 1 162 ? 2.453  -8.940  2.443   0.38 16.51 ?  162 ASP   A O    1 
ATOM   3714 C  CB   A ASP   A 1 162 ? 1.499  -5.998  3.596   0.62 18.48 ?  162 ASP   A CB   1 
ATOM   3715 C  CB   B ASP   A 1 162 ? 1.481  -5.888  3.339   0.38 17.08 ?  162 ASP   A CB   1 
ATOM   3716 C  CG   A ASP   A 1 162 ? 1.164  -5.462  4.973   0.62 19.55 ?  162 ASP   A CG   1 
ATOM   3717 C  CG   B ASP   A 1 162 ? 1.233  -5.039  4.583   0.38 17.67 ?  162 ASP   A CG   1 
ATOM   3718 O  OD1  A ASP   A 1 162 ? 1.818  -5.863  5.959   0.62 20.27 ?  162 ASP   A OD1  1 
ATOM   3719 O  OD1  B ASP   A 1 162 ? 1.747  -5.387  5.666   0.38 18.27 ?  162 ASP   A OD1  1 
ATOM   3720 O  OD2  A ASP   A 1 162 ? 0.226  -4.639  5.059   0.62 19.89 -1 162 ASP   A OD2  1 
ATOM   3721 O  OD2  B ASP   A 1 162 ? 0.496  -4.030  4.480   0.38 18.02 -1 162 ASP   A OD2  1 
ATOM   3722 H  H    A ASP   A 1 162 ? 3.755  -5.053  3.624   0.62 19.68 ?  162 ASP   A H    1 
ATOM   3723 H  H    B ASP   A 1 162 ? 3.787  -5.107  3.467   0.38 18.22 ?  162 ASP   A H    1 
ATOM   3724 H  HA   A ASP   A 1 162 ? 2.814  -7.379  4.334   0.62 20.86 ?  162 ASP   A HA   1 
ATOM   3725 H  HA   B ASP   A 1 162 ? 2.658  -7.288  4.270   0.38 19.32 ?  162 ASP   A HA   1 
ATOM   3726 H  HB2  A ASP   A 1 162 ? 1.569  -5.241  2.998   0.62 22.16 ?  162 ASP   A HB2  1 
ATOM   3727 H  HB2  B ASP   A 1 162 ? 1.584  -5.291  2.581   0.38 20.48 ?  162 ASP   A HB2  1 
ATOM   3728 H  HB3  A ASP   A 1 162 ? 0.766  -6.573  3.325   0.62 22.16 ?  162 ASP   A HB3  1 
ATOM   3729 H  HB3  B ASP   A 1 162 ? 0.702  -6.450  3.215   0.38 20.48 ?  162 ASP   A HB3  1 
ATOM   3730 N  N    A LYS   A 1 163 ? 3.325  -7.100  1.198   0.62 18.00 ?  163 LYS   A N    1 
ATOM   3731 N  N    B LYS   A 1 163 ? 3.200  -7.282  1.113   0.38 16.84 ?  163 LYS   A N    1 
ATOM   3732 C  CA   A LYS   A 1 163 ? 3.402  -7.872  -0.039  0.62 18.53 ?  163 LYS   A CA   1 
ATOM   3733 C  CA   B LYS   A 1 163 ? 3.332  -8.154  -0.049  0.38 17.93 ?  163 LYS   A CA   1 
ATOM   3734 C  C    A LYS   A 1 163 ? 4.452  -8.978  0.041   0.62 17.76 ?  163 LYS   A C    1 
ATOM   3735 C  C    B LYS   A 1 163 ? 4.487  -9.130  0.131   0.38 17.17 ?  163 LYS   A C    1 
ATOM   3736 O  O    A LYS   A 1 163 ? 4.259  -10.059 -0.524  0.62 18.07 ?  163 LYS   A O    1 
ATOM   3737 O  O    B LYS   A 1 163 ? 4.383  -10.304 -0.243  0.38 17.61 ?  163 LYS   A O    1 
ATOM   3738 C  CB   A LYS   A 1 163 ? 3.682  -6.946  -1.223  0.62 20.96 ?  163 LYS   A CB   1 
ATOM   3739 C  CB   B LYS   A 1 163 ? 3.536  -7.282  -1.286  0.38 20.32 ?  163 LYS   A CB   1 
ATOM   3740 C  CG   A LYS   A 1 163 ? 3.754  -7.673  -2.555  0.62 23.58 ?  163 LYS   A CG   1 
ATOM   3741 C  CG   B LYS   A 1 163 ? 3.547  -7.992  -2.620  0.38 22.77 ?  163 LYS   A CG   1 
ATOM   3742 C  CD   A LYS   A 1 163 ? 4.167  -6.744  -3.679  0.62 26.19 ?  163 LYS   A CD   1 
ATOM   3743 C  CD   B LYS   A 1 163 ? 3.572  -6.942  -3.720  0.38 25.00 ?  163 LYS   A CD   1 
ATOM   3744 C  CE   A LYS   A 1 163 ? 4.099  -7.445  -5.025  0.62 28.33 ?  163 LYS   A CE   1 
ATOM   3745 C  CE   B LYS   A 1 163 ? 3.831  -7.536  -5.087  0.38 26.69 ?  163 LYS   A CE   1 
ATOM   3746 N  NZ   A LYS   A 1 163 ? 4.698  -6.625  -6.113  0.62 29.65 ?  163 LYS   A NZ   1 
ATOM   3747 N  NZ   B LYS   A 1 163 ? 4.593  -6.588  -5.949  0.38 27.60 ?  163 LYS   A NZ   1 
ATOM   3748 H  H    A LYS   A 1 163 ? 3.592  -6.281  1.135   0.62 21.58 ?  163 LYS   A H    1 
ATOM   3749 H  H    B LYS   A 1 163 ? 3.424  -6.464  0.964   0.38 20.19 ?  163 LYS   A H    1 
ATOM   3750 H  HA   A LYS   A 1 163 ? 2.541  -8.290  -0.189  0.62 22.22 ?  163 LYS   A HA   1 
ATOM   3751 H  HA   B LYS   A 1 163 ? 2.517  -8.664  -0.168  0.38 21.50 ?  163 LYS   A HA   1 
ATOM   3752 H  HB2  A LYS   A 1 163 ? 2.969  -6.287  -1.281  0.62 25.13 ?  163 LYS   A HB2  1 
ATOM   3753 H  HB2  B LYS   A 1 163 ? 2.820  -6.629  -1.320  0.38 24.37 ?  163 LYS   A HB2  1 
ATOM   3754 H  HB3  A LYS   A 1 163 ? 4.529  -6.500  -1.079  0.62 25.13 ?  163 LYS   A HB3  1 
ATOM   3755 H  HB3  B LYS   A 1 163 ? 4.386  -6.824  -1.202  0.38 24.37 ?  163 LYS   A HB3  1 
ATOM   3756 H  HG2  A LYS   A 1 163 ? 4.408  -8.386  -2.500  0.62 28.28 ?  163 LYS   A HG2  1 
ATOM   3757 H  HG2  B LYS   A 1 163 ? 4.344  -8.543  -2.696  0.38 27.31 ?  163 LYS   A HG2  1 
ATOM   3758 H  HG3  A LYS   A 1 163 ? 2.879  -8.038  -2.765  0.62 28.28 ?  163 LYS   A HG3  1 
ATOM   3759 H  HG3  B LYS   A 1 163 ? 2.745  -8.529  -2.718  0.38 27.31 ?  163 LYS   A HG3  1 
ATOM   3760 H  HD2  A LYS   A 1 163 ? 3.565  -5.983  -3.702  0.62 31.41 ?  163 LYS   A HD2  1 
ATOM   3761 H  HD2  B LYS   A 1 163 ? 2.713  -6.490  -3.745  0.38 29.99 ?  163 LYS   A HD2  1 
ATOM   3762 H  HD3  A LYS   A 1 163 ? 5.078  -6.450  -3.532  0.62 31.41 ?  163 LYS   A HD3  1 
ATOM   3763 H  HD3  B LYS   A 1 163 ? 4.277  -6.301  -3.530  0.38 29.99 ?  163 LYS   A HD3  1 
ATOM   3764 H  HE2  A LYS   A 1 163 ? 4.580  -8.285  -4.972  0.62 33.98 ?  163 LYS   A HE2  1 
ATOM   3765 H  HE2  B LYS   A 1 163 ? 4.345  -8.351  -4.991  0.38 32.01 ?  163 LYS   A HE2  1 
ATOM   3766 H  HE3  A LYS   A 1 163 ? 3.170  -7.611  -5.250  0.62 33.98 ?  163 LYS   A HE3  1 
ATOM   3767 H  HE3  B LYS   A 1 163 ? 2.984  -7.722  -5.518  0.38 32.01 ?  163 LYS   A HE3  1 
ATOM   3768 H  HZ1  A LYS   A 1 163 ? 4.645  -7.060  -6.887  0.62 35.57 ?  163 LYS   A HZ1  1 
ATOM   3769 H  HZ1  B LYS   A 1 163 ? 4.738  -6.951  -6.748  0.38 33.10 ?  163 LYS   A HZ1  1 
ATOM   3770 H  HZ2  A LYS   A 1 163 ? 4.262  -5.852  -6.184  0.62 35.57 ?  163 LYS   A HZ2  1 
ATOM   3771 H  HZ2  B LYS   A 1 163 ? 4.132  -5.833  -6.054  0.38 33.10 ?  163 LYS   A HZ2  1 
ATOM   3772 H  HZ3  A LYS   A 1 163 ? 5.553  -6.459  -5.931  0.62 35.57 ?  163 LYS   A HZ3  1 
ATOM   3773 H  HZ3  B LYS   A 1 163 ? 5.377  -6.395  -5.572  0.38 33.10 ?  163 LYS   A HZ3  1 
ATOM   3774 N  N    A LEU   A 1 164 ? 5.581  -8.725  0.714   0.62 16.19 ?  164 LEU   A N    1 
ATOM   3775 N  N    B LEU   A 1 164 ? 5.596  -8.659  0.704   0.38 15.72 ?  164 LEU   A N    1 
ATOM   3776 C  CA   A LEU   A 1 164 ? 6.642  -9.732  0.777   0.62 15.29 ?  164 LEU   A CA   1 
ATOM   3777 C  CA   B LEU   A 1 164 ? 6.716  -9.547  1.005   0.38 14.52 ?  164 LEU   A CA   1 
ATOM   3778 C  C    A LEU   A 1 164 ? 6.219  -10.924 1.623   0.62 14.61 ?  164 LEU   A C    1 
ATOM   3779 C  C    B LEU   A 1 164 ? 6.284  -10.677 1.929   0.38 14.12 ?  164 LEU   A C    1 
ATOM   3780 O  O    A LEU   A 1 164 ? 6.508  -12.075 1.275   0.62 14.73 ?  164 LEU   A O    1 
ATOM   3781 O  O    B LEU   A 1 164 ? 6.663  -11.837 1.724   0.38 14.38 ?  164 LEU   A O    1 
ATOM   3782 C  CB   A LEU   A 1 164 ? 7.915  -9.118  1.355   0.62 14.85 ?  164 LEU   A CB   1 
ATOM   3783 C  CB   B LEU   A 1 164 ? 7.854  -8.746  1.637   0.38 13.67 ?  164 LEU   A CB   1 
ATOM   3784 C  CG   A LEU   A 1 164 ? 8.610  -8.073  0.483   0.62 15.00 ?  164 LEU   A CG   1 
ATOM   3785 C  CG   B LEU   A 1 164 ? 8.712  -7.909  0.686   0.38 13.33 ?  164 LEU   A CG   1 
ATOM   3786 C  CD1  A LEU   A 1 164 ? 9.573  -7.225  1.305   0.62 14.91 ?  164 LEU   A CD1  1 
ATOM   3787 C  CD1  B LEU   A 1 164 ? 9.505  -6.873  1.473   0.38 13.17 ?  164 LEU   A CD1  1 
ATOM   3788 C  CD2  A LEU   A 1 164 ? 9.346  -8.738  -0.666  0.62 15.13 ?  164 LEU   A CD2  1 
ATOM   3789 C  CD2  B LEU   A 1 164 ? 9.650  -8.786  -0.143  0.38 12.68 ?  164 LEU   A CD2  1 
ATOM   3790 H  H    A LEU   A 1 164 ? 5.758  -7.994  1.138   0.62 19.41 ?  164 LEU   A H    1 
ATOM   3791 H  H    B LEU   A 1 164 ? 5.719  -7.837  0.928   0.38 18.84 ?  164 LEU   A H    1 
ATOM   3792 H  HA   A LEU   A 1 164 ? 6.835  -10.049 -0.118  0.62 18.33 ?  164 LEU   A HA   1 
ATOM   3793 H  HA   B LEU   A 1 164 ? 7.045  -9.935  0.182   0.38 17.41 ?  164 LEU   A HA   1 
ATOM   3794 H  HB2  A LEU   A 1 164 ? 7.698  -8.695  2.196   0.62 17.80 ?  164 LEU   A HB2  1 
ATOM   3795 H  HB2  B LEU   A 1 164 ? 7.475  -8.133  2.288   0.38 16.38 ?  164 LEU   A HB2  1 
ATOM   3796 H  HB3  A LEU   A 1 164 ? 8.556  -9.834  1.508   0.62 17.80 ?  164 LEU   A HB3  1 
ATOM   3797 H  HB3  B LEU   A 1 164 ? 8.450  -9.362  2.087   0.38 16.38 ?  164 LEU   A HB3  1 
ATOM   3798 H  HG   A LEU   A 1 164 ? 7.941  -7.483  0.109   0.62 17.98 ?  164 LEU   A HG   1 
ATOM   3799 H  HG   B LEU   A 1 164 ? 8.132  -7.431  0.073   0.38 15.97 ?  164 LEU   A HG   1 
ATOM   3800 H  HD11 A LEU   A 1 164 ? 9.998  -6.577  0.724   0.62 17.87 ?  164 LEU   A HD11 1 
ATOM   3801 H  HD11 B LEU   A 1 164 ? 10.065 -6.369  0.863   0.38 15.79 ?  164 LEU   A HD11 1 
ATOM   3802 H  HD12 A LEU   A 1 164 ? 9.075  -6.768  2.003   0.62 17.87 ?  164 LEU   A HD12 1 
ATOM   3803 H  HD12 B LEU   A 1 164 ? 8.883  -6.275  1.921   0.38 15.79 ?  164 LEU   A HD12 1 
ATOM   3804 H  HD13 A LEU   A 1 164 ? 10.243 -7.803  1.704   0.62 17.87 ?  164 LEU   A HD13 1 
ATOM   3805 H  HD13 B LEU   A 1 164 ? 10.055 -7.328  2.130   0.38 15.79 ?  164 LEU   A HD13 1 
ATOM   3806 H  HD21 A LEU   A 1 164 ? 9.791  -8.053  -1.193  0.62 18.14 ?  164 LEU   A HD21 1 
ATOM   3807 H  HD21 B LEU   A 1 164 ? 10.180 -8.219  -0.727  0.38 15.20 ?  164 LEU   A HD21 1 
ATOM   3808 H  HD22 A LEU   A 1 164 ? 10.002 -9.356  -0.309  0.62 18.14 ?  164 LEU   A HD22 1 
ATOM   3809 H  HD22 B LEU   A 1 164 ? 10.233 -9.279  0.454   0.38 15.20 ?  164 LEU   A HD22 1 
ATOM   3810 H  HD23 A LEU   A 1 164 ? 8.707  -9.214  -1.217  0.62 18.14 ?  164 LEU   A HD23 1 
ATOM   3811 H  HD23 B LEU   A 1 164 ? 9.120  -9.401  -0.673  0.38 15.20 ?  164 LEU   A HD23 1 
ATOM   3812 N  N    A VAL   A 1 165 ? 5.564  -10.659 2.752   0.62 14.19 ?  165 VAL   A N    1 
ATOM   3813 N  N    B VAL   A 1 165 ? 5.500  -10.357 2.960   0.38 13.42 ?  165 VAL   A N    1 
ATOM   3814 C  CA   A VAL   A 1 165 ? 5.071  -11.730 3.611   0.62 14.09 ?  165 VAL   A CA   1 
ATOM   3815 C  CA   B VAL   A 1 165 ? 5.023  -11.392 3.871   0.38 13.81 ?  165 VAL   A CA   1 
ATOM   3816 C  C    A VAL   A 1 165 ? 4.018  -12.547 2.875   0.62 14.44 ?  165 VAL   A C    1 
ATOM   3817 C  C    B VAL   A 1 165 ? 4.047  -12.327 3.163   0.38 13.92 ?  165 VAL   A C    1 
ATOM   3818 O  O    A VAL   A 1 165 ? 4.113  -13.776 2.775   0.62 13.88 ?  165 VAL   A O    1 
ATOM   3819 O  O    B VAL   A 1 165 ? 4.142  -13.555 3.283   0.38 13.92 ?  165 VAL   A O    1 
ATOM   3820 C  CB   A VAL   A 1 165 ? 4.514  -11.129 4.915   0.62 14.49 ?  165 VAL   A CB   1 
ATOM   3821 C  CB   B VAL   A 1 165 ? 4.411  -10.766 5.138   0.38 14.46 ?  165 VAL   A CB   1 
ATOM   3822 C  CG1  A VAL   A 1 165 ? 3.772  -12.179 5.731   0.62 14.39 ?  165 VAL   A CG1  1 
ATOM   3823 C  CG1  B VAL   A 1 165 ? 3.669  -11.820 5.948   0.38 14.48 ?  165 VAL   A CG1  1 
ATOM   3824 C  CG2  A VAL   A 1 165 ? 5.632  -10.486 5.724   0.62 15.04 ?  165 VAL   A CG2  1 
ATOM   3825 C  CG2  B VAL   A 1 165 ? 5.495  -10.113 5.983   0.38 14.74 ?  165 VAL   A CG2  1 
ATOM   3826 H  H    A VAL   A 1 165 ? 5.393  -9.877  3.045   0.62 17.01 ?  165 VAL   A H    1 
ATOM   3827 H  H    B VAL   A 1 165 ? 5.247  -9.553  3.157   0.38 16.09 ?  165 VAL   A H    1 
ATOM   3828 H  HA   A VAL   A 1 165 ? 5.803  -12.326 3.844   0.62 16.89 ?  165 VAL   A HA   1 
ATOM   3829 H  HA   B VAL   A 1 165 ? 5.782  -11.921 4.152   0.38 16.56 ?  165 VAL   A HA   1 
ATOM   3830 H  HB   A VAL   A 1 165 ? 3.879  -10.434 4.687   0.62 17.37 ?  165 VAL   A HB   1 
ATOM   3831 H  HB   B VAL   A 1 165 ? 3.777  -10.076 4.884   0.38 17.34 ?  165 VAL   A HB   1 
ATOM   3832 H  HG11 A VAL   A 1 165 ? 3.653  -11.847 6.635   0.62 17.25 ?  165 VAL   A HG11 1 
ATOM   3833 H  HG11 B VAL   A 1 165 ? 3.536  -11.489 6.851   0.38 17.36 ?  165 VAL   A HG11 1 
ATOM   3834 H  HG12 A VAL   A 1 165 ? 2.904  -12.341 5.326   0.62 17.25 ?  165 VAL   A HG12 1 
ATOM   3835 H  HG12 B VAL   A 1 165 ? 2.811  -11.994 5.532   0.38 17.36 ?  165 VAL   A HG12 1 
ATOM   3836 H  HG13 A VAL   A 1 165 ? 4.291  -12.996 5.745   0.62 17.25 ?  165 VAL   A HG13 1 
ATOM   3837 H  HG13 B VAL   A 1 165 ? 4.200  -12.631 5.972   0.38 17.36 ?  165 VAL   A HG13 1 
ATOM   3838 H  HG21 A VAL   A 1 165 ? 5.262  -10.132 6.548   0.62 18.03 ?  165 VAL   A HG21 1 
ATOM   3839 H  HG21 B VAL   A 1 165 ? 5.089  -9.716  6.770   0.38 17.68 ?  165 VAL   A HG21 1 
ATOM   3840 H  HG22 A VAL   A 1 165 ? 6.305  -11.155 5.923   0.62 18.03 ?  165 VAL   A HG22 1 
ATOM   3841 H  HG22 B VAL   A 1 165 ? 6.138  -10.789 6.249   0.38 17.68 ?  165 VAL   A HG22 1 
ATOM   3842 H  HG23 A VAL   A 1 165 ? 6.024  -9.767  5.202   0.62 18.03 ?  165 VAL   A HG23 1 
ATOM   3843 H  HG23 B VAL   A 1 165 ? 5.936  -9.426  5.458   0.38 17.68 ?  165 VAL   A HG23 1 
ATOM   3844 N  N    A SER   A 1 166 ? 3.005  -11.868 2.336   0.62 15.64 ?  166 SER   A N    1 
ATOM   3845 N  N    B SER   A 1 166 ? 3.100  -11.768 2.406   0.38 14.35 ?  166 SER   A N    1 
ATOM   3846 C  CA   A SER   A 1 166 ? 1.885  -12.561 1.709   0.62 16.45 ?  166 SER   A CA   1 
ATOM   3847 C  CA   B SER   A 1 166 ? 1.992  -12.591 1.925   0.38 14.67 ?  166 SER   A CA   1 
ATOM   3848 C  C    A SER   A 1 166 ? 2.319  -13.337 0.480   0.62 16.71 ?  166 SER   A C    1 
ATOM   3849 C  C    B SER   A 1 166 ? 2.430  -13.621 0.882   0.38 14.65 ?  166 SER   A C    1 
ATOM   3850 O  O    A SER   A 1 166 ? 1.653  -14.307 0.097   0.62 17.62 ?  166 SER   A O    1 
ATOM   3851 O  O    B SER   A 1 166 ? 1.852  -14.712 0.816   0.38 14.74 ?  166 SER   A O    1 
ATOM   3852 C  CB   A SER   A 1 166 ? 0.803  -11.559 1.306   0.62 17.37 ?  166 SER   A CB   1 
ATOM   3853 C  CB   B SER   A 1 166 ? 0.834  -11.714 1.425   0.38 15.62 ?  166 SER   A CB   1 
ATOM   3854 O  OG   A SER   A 1 166 ? 0.188  -10.976 2.439   0.62 18.42 ?  166 SER   A OG   1 
ATOM   3855 O  OG   B SER   A 1 166 ? 1.188  -10.935 0.297   0.38 16.35 ?  166 SER   A OG   1 
ATOM   3856 H  H    A SER   A 1 166 ? 2.946  -11.019 2.321   0.62 18.75 ?  166 SER   A H    1 
ATOM   3857 H  H    B SER   A 1 166 ? 3.069  -10.935 2.173   0.38 17.20 ?  166 SER   A H    1 
ATOM   3858 H  HA   A SER   A 1 166 ? 1.497  -13.191 2.340   0.62 19.72 ?  166 SER   A HA   1 
ATOM   3859 H  HA   B SER   A 1 166 ? 1.649  -13.087 2.681   0.38 17.58 ?  166 SER   A HA   1 
ATOM   3860 H  HB2  A SER   A 1 166 ? 1.206  -10.863 0.766   0.62 20.83 ?  166 SER   A HB2  1 
ATOM   3861 H  HB2  B SER   A 1 166 ? 0.093  -12.288 1.175   0.38 18.72 ?  166 SER   A HB2  1 
ATOM   3862 H  HB3  A SER   A 1 166 ? 0.120  -12.021 0.793   0.62 20.83 ?  166 SER   A HB3  1 
ATOM   3863 H  HB3  B SER   A 1 166 ? 0.555  -11.122 2.146   0.38 18.72 ?  166 SER   A HB3  1 
ATOM   3864 H  HG   A SER   A 1 166 ? -0.391 -10.421 2.199   0.62 22.09 ?  166 SER   A HG   1 
ATOM   3865 H  HG   B SER   A 1 166 ? 0.539  -10.457 0.060   0.38 19.61 ?  166 SER   A HG   1 
ATOM   3866 N  N    A SER   A 1 167 ? 3.404  -12.919 -0.168  0.62 15.86 ?  167 SER   A N    1 
ATOM   3867 N  N    B SER   A 1 167 ? 3.465  -13.327 0.091   0.38 15.08 ?  167 SER   A N    1 
ATOM   3868 C  CA   A SER   A 1 167 ? 3.900  -13.611 -1.347  0.62 16.48 ?  167 SER   A CA   1 
ATOM   3869 C  CA   B SER   A 1 167 ? 3.821  -14.154 -1.056  0.38 15.59 ?  167 SER   A CA   1 
ATOM   3870 C  C    A SER   A 1 167 ? 5.035  -14.575 -1.038  0.62 17.03 ?  167 SER   A C    1 
ATOM   3871 C  C    B SER   A 1 167 ? 4.999  -15.090 -0.786  0.38 15.86 ?  167 SER   A C    1 
ATOM   3872 O  O    A SER   A 1 167 ? 5.515  -15.249 -1.954  0.62 18.30 ?  167 SER   A O    1 
ATOM   3873 O  O    B SER   A 1 167 ? 5.619  -15.578 -1.736  0.38 17.00 ?  167 SER   A O    1 
ATOM   3874 C  CB   A SER   A 1 167 ? 4.351  -12.604 -2.414  0.62 16.65 ?  167 SER   A CB   1 
ATOM   3875 C  CB   B SER   A 1 167 ? 4.123  -13.274 -2.272  0.38 16.24 ?  167 SER   A CB   1 
ATOM   3876 O  OG   A SER   A 1 167 ? 5.399  -11.781 -1.929  0.62 17.02 ?  167 SER   A OG   1 
ATOM   3877 O  OG   B SER   A 1 167 ? 5.347  -12.572 -2.119  0.38 16.73 ?  167 SER   A OG   1 
ATOM   3878 H  H    A SER   A 1 167 ? 3.862  -12.221 0.055   0.62 19.02 ?  167 SER   A H    1 
ATOM   3879 H  H    B SER   A 1 167 ? 3.984  -12.655 0.212   0.38 18.09 ?  167 SER   A H    1 
ATOM   3880 H  HA   A SER   A 1 167 ? 3.172  -14.120 -1.728  0.62 19.76 ?  167 SER   A HA   1 
ATOM   3881 H  HA   B SER   A 1 167 ? 3.060  -14.712 -1.281  0.38 18.69 ?  167 SER   A HA   1 
ATOM   3882 H  HB2  A SER   A 1 167 ? 4.668  -13.090 -3.191  0.62 19.96 ?  167 SER   A HB2  1 
ATOM   3883 H  HB2  B SER   A 1 167 ? 4.177  -13.838 -3.060  0.38 19.48 ?  167 SER   A HB2  1 
ATOM   3884 H  HB3  A SER   A 1 167 ? 3.591  -12.047 -2.667  0.62 19.96 ?  167 SER   A HB3  1 
ATOM   3885 H  HB3  B SER   A 1 167 ? 3.404  -12.631 -2.376  0.38 19.48 ?  167 SER   A HB3  1 
ATOM   3886 H  HG   A SER   A 1 167 ? 5.125  -11.348 -1.259  0.62 20.41 ?  167 SER   A HG   1 
ATOM   3887 H  HG   B SER   A 1 167 ? 5.313  -12.086 -1.437  0.38 20.07 ?  167 SER   A HG   1 
ATOM   3888 N  N    A PHE   A 1 168 ? 5.474  -14.667 0.218   0.62 16.19 ?  168 PHE   A N    1 
ATOM   3889 N  N    B PHE   A 1 168 ? 5.296  -15.387 0.478   0.38 15.27 ?  168 PHE   A N    1 
ATOM   3890 C  CA   A PHE   A 1 168 ? 6.649  -15.473 0.523   0.62 17.01 ?  168 PHE   A CA   1 
ATOM   3891 C  CA   B PHE   A 1 168 ? 6.566  -16.028 0.798   0.38 15.36 ?  168 PHE   A CA   1 
ATOM   3892 C  C    A PHE   A 1 168 ? 6.338  -16.956 0.403   0.62 18.61 ?  168 PHE   A C    1 
ATOM   3893 C  C    B PHE   A 1 168 ? 6.533  -17.549 0.677   0.38 16.01 ?  168 PHE   A C    1 
ATOM   3894 O  O    A PHE   A 1 168 ? 5.331  -17.440 0.930   0.62 20.01 ?  168 PHE   A O    1 
ATOM   3895 O  O    B PHE   A 1 168 ? 7.401  -18.132 0.020   0.38 15.51 ?  168 PHE   A O    1 
ATOM   3896 C  CB   A PHE   A 1 168 ? 7.180  -15.193 1.925   0.62 16.30 ?  168 PHE   A CB   1 
ATOM   3897 C  CB   B PHE   A 1 168 ? 7.023  -15.637 2.203   0.38 15.49 ?  168 PHE   A CB   1 
ATOM   3898 C  CG   A PHE   A 1 168 ? 8.425  -15.974 2.238   0.62 15.45 ?  168 PHE   A CG   1 
ATOM   3899 C  CG   B PHE   A 1 168 ? 8.365  -16.195 2.564   0.38 15.65 ?  168 PHE   A CG   1 
ATOM   3900 C  CD1  A PHE   A 1 168 ? 9.612  -15.665 1.601   0.62 15.21 ?  168 PHE   A CD1  1 
ATOM   3901 C  CD1  B PHE   A 1 168 ? 9.515  -15.665 2.009   0.38 15.99 ?  168 PHE   A CD1  1 
ATOM   3902 C  CD2  A PHE   A 1 168 ? 8.410  -17.041 3.125   0.62 15.27 ?  168 PHE   A CD2  1 
ATOM   3903 C  CD2  B PHE   A 1 168 ? 8.481  -17.259 3.443   0.38 15.74 ?  168 PHE   A CD2  1 
ATOM   3904 C  CE1  A PHE   A 1 168 ? 10.763 -16.385 1.856   0.62 14.77 ?  168 PHE   A CE1  1 
ATOM   3905 C  CE1  B PHE   A 1 168 ? 10.754 -16.177 2.328   0.38 16.15 ?  168 PHE   A CE1  1 
ATOM   3906 C  CE2  A PHE   A 1 168 ? 9.568  -17.760 3.387   0.62 15.28 ?  168 PHE   A CE2  1 
ATOM   3907 C  CE2  B PHE   A 1 168 ? 9.723  -17.773 3.769   0.38 16.05 ?  168 PHE   A CE2  1 
ATOM   3908 C  CZ   A PHE   A 1 168 ? 10.743 -17.428 2.750   0.62 14.83 ?  168 PHE   A CZ   1 
ATOM   3909 C  CZ   B PHE   A 1 168 ? 10.859 -17.231 3.208   0.38 16.20 ?  168 PHE   A CZ   1 
ATOM   3910 H  H    A PHE   A 1 168 ? 5.117  -14.270 0.898   0.62 19.41 ?  168 PHE   A H    1 
ATOM   3911 H  H    B PHE   A 1 168 ? 4.785  -15.245 1.155   0.38 18.30 ?  168 PHE   A H    1 
ATOM   3912 H  HA   A PHE   A 1 168 ? 7.348  -15.254 -0.112  0.62 20.39 ?  168 PHE   A HA   1 
ATOM   3913 H  HA   B PHE   A 1 168 ? 7.237  -15.706 0.175   0.38 18.42 ?  168 PHE   A HA   1 
ATOM   3914 H  HB2  A PHE   A 1 168 ? 7.389  -14.249 2.005   0.62 19.55 ?  168 PHE   A HB2  1 
ATOM   3915 H  HB2  B PHE   A 1 168 ? 7.082  -14.672 2.254   0.38 18.57 ?  168 PHE   A HB2  1 
ATOM   3916 H  HB3  A PHE   A 1 168 ? 6.500  -15.436 2.575   0.62 19.55 ?  168 PHE   A HB3  1 
ATOM   3917 H  HB3  B PHE   A 1 168 ? 6.382  -15.969 2.847   0.38 18.57 ?  168 PHE   A HB3  1 
ATOM   3918 H  HD1  A PHE   A 1 168 ? 9.638  -14.959 0.995   0.62 18.23 ?  168 PHE   A HD1  1 
ATOM   3919 H  HD1  B PHE   A 1 168 ? 9.452  -14.953 1.413   0.38 19.18 ?  168 PHE   A HD1  1 
ATOM   3920 H  HD2  A PHE   A 1 168 ? 7.621  -17.267 3.560   0.62 18.30 ?  168 PHE   A HD2  1 
ATOM   3921 H  HD2  B PHE   A 1 168 ? 7.716  -17.628 3.823   0.38 18.88 ?  168 PHE   A HD2  1 
ATOM   3922 H  HE1  A PHE   A 1 168 ? 11.559 -16.160 1.427   0.62 17.71 ?  168 PHE   A HE1  1 
ATOM   3923 H  HE1  B PHE   A 1 168 ? 11.522 -15.808 1.951   0.38 19.36 ?  168 PHE   A HE1  1 
ATOM   3924 H  HE2  A PHE   A 1 168 ? 9.550  -18.469 3.990   0.62 18.32 ?  168 PHE   A HE2  1 
ATOM   3925 H  HE2  B PHE   A 1 168 ? 9.789  -18.486 4.363   0.38 19.24 ?  168 PHE   A HE2  1 
ATOM   3926 H  HZ   A PHE   A 1 168 ? 11.522 -17.912 2.921   0.62 17.78 ?  168 PHE   A HZ   1 
ATOM   3927 H  HZ   B PHE   A 1 168 ? 11.695 -17.575 3.426   0.38 19.43 ?  168 PHE   A HZ   1 
ATOM   3928 N  N    A LEU   A 1 169 ? 7.230  -17.687 -0.255  0.62 19.94 ?  169 LEU   A N    1 
ATOM   3929 N  N    B LEU   A 1 169 ? 5.587  -18.210 1.336   0.38 17.73 ?  169 LEU   A N    1 
ATOM   3930 C  CA   A LEU   A 1 169 ? 7.043  -19.120 -0.411  0.62 21.45 ?  169 LEU   A CA   1 
ATOM   3931 C  CA   B LEU   A 1 169 ? 5.585  -19.673 1.367   0.38 19.88 ?  169 LEU   A CA   1 
ATOM   3932 C  C    A LEU   A 1 169 ? 7.882  -19.884 0.611   0.62 21.04 ?  169 LEU   A C    1 
ATOM   3933 C  C    B LEU   A 1 169 ? 4.922  -20.286 0.135   0.38 21.24 ?  169 LEU   A C    1 
ATOM   3934 O  O    A LEU   A 1 169 ? 7.316  -20.430 1.560   0.62 21.59 ?  169 LEU   A O    1 
ATOM   3935 O  O    B LEU   A 1 169 ? 3.982  -19.737 -0.439  0.38 21.48 ?  169 LEU   A O    1 
ATOM   3936 C  CB   A LEU   A 1 169 ? 7.366  -19.558 -1.843  0.62 22.70 ?  169 LEU   A CB   1 
ATOM   3937 C  CB   B LEU   A 1 169 ? 4.911  -20.191 2.643   0.38 20.45 ?  169 LEU   A CB   1 
ATOM   3938 C  CG   A LEU   A 1 169 ? 7.059  -21.019 -2.192  0.62 23.76 ?  169 LEU   A CG   1 
ATOM   3939 C  CG   B LEU   A 1 169 ? 4.750  -21.710 2.764   0.38 21.07 ?  169 LEU   A CG   1 
ATOM   3940 C  CD1  A LEU   A 1 169 ? 5.633  -21.393 -1.811  0.62 24.23 ?  169 LEU   A CD1  1 
ATOM   3941 C  CD1  B LEU   A 1 169 ? 6.053  -22.450 2.504   0.38 21.72 ?  169 LEU   A CD1  1 
ATOM   3942 C  CD2  A LEU   A 1 169 ? 7.295  -21.280 -3.673  0.62 24.04 ?  169 LEU   A CD2  1 
ATOM   3943 C  CD2  B LEU   A 1 169 ? 4.195  -22.069 4.139   0.38 21.24 ?  169 LEU   A CD2  1 
ATOM   3944 O  OXT  A LEU   A 1 169 ? 9.113  -19.967 0.541   0.62 20.14 -1 169 LEU   A OXT  1 
ATOM   3945 O  OXT  B LEU   A 1 169 ? 5.322  -21.362 -0.311  0.38 22.24 -1 169 LEU   A OXT  1 
ATOM   3946 H  H    A LEU   A 1 169 ? 7.954  -17.377 -0.610  0.62 23.91 ?  169 LEU   A H    1 
ATOM   3947 H  H    B LEU   A 1 169 ? 4.955  -17.838 1.781   0.38 21.26 ?  169 LEU   A H    1 
ATOM   3948 H  HA   A LEU   A 1 169 ? 6.119  -19.334 -0.233  0.62 25.73 ?  169 LEU   A HA   1 
ATOM   3949 H  HA   B LEU   A 1 169 ? 6.507  -19.972 1.380   0.38 23.84 ?  169 LEU   A HA   1 
ATOM   3950 H  HB2  A LEU   A 1 169 ? 6.849  -19.005 -2.451  0.62 27.23 ?  169 LEU   A HB2  1 
ATOM   3951 H  HB2  B LEU   A 1 169 ? 5.434  -19.895 3.404   0.38 24.52 ?  169 LEU   A HB2  1 
ATOM   3952 H  HB3  A LEU   A 1 169 ? 8.309  -19.418 -2.004  0.62 27.23 ?  169 LEU   A HB3  1 
ATOM   3953 H  HB3  B LEU   A 1 169 ? 4.024  -19.810 2.695   0.38 24.52 ?  169 LEU   A HB3  1 
ATOM   3954 H  HG   A LEU   A 1 169 ? 7.658  -21.595 -1.693  0.62 28.50 ?  169 LEU   A HG   1 
ATOM   3955 H  HG   B LEU   A 1 169 ? 4.105  -22.007 2.106   0.38 25.26 ?  169 LEU   A HG   1 
ATOM   3956 H  HD11 A LEU   A 1 169 ? 5.413  -22.252 -2.206  0.62 29.06 ?  169 LEU   A HD11 1 
ATOM   3957 H  HD11 B LEU   A 1 169 ? 5.862  -23.397 2.439   0.38 26.04 ?  169 LEU   A HD11 1 
ATOM   3958 H  HD12 A LEU   A 1 169 ? 5.566  -21.449 -0.845  0.62 29.06 ?  169 LEU   A HD12 1 
ATOM   3959 H  HD12 B LEU   A 1 169 ? 6.446  -22.138 1.675   0.38 26.04 ?  169 LEU   A HD12 1 
ATOM   3960 H  HD13 A LEU   A 1 169 ? 5.026  -20.713 -2.147  0.62 29.06 ?  169 LEU   A HD13 1 
ATOM   3961 H  HD13 B LEU   A 1 169 ? 6.654  -22.287 3.242   0.38 26.04 ?  169 LEU   A HD13 1 
ATOM   3962 H  HD21 A LEU   A 1 169 ? 7.100  -22.211 -3.866  0.62 28.83 ?  169 LEU   A HD21 1 
ATOM   3963 H  HD21 B LEU   A 1 169 ? 4.098  -23.032 4.198   0.38 25.47 ?  169 LEU   A HD21 1 
ATOM   3964 H  HD22 A LEU   A 1 169 ? 6.709  -20.706 -4.192  0.62 28.83 ?  169 LEU   A HD22 1 
ATOM   3965 H  HD22 B LEU   A 1 169 ? 4.812  -21.757 4.820   0.38 25.47 ?  169 LEU   A HD22 1 
ATOM   3966 H  HD23 A LEU   A 1 169 ? 8.221  -21.085 -3.884  0.62 28.83 ?  169 LEU   A HD23 1 
ATOM   3967 H  HD23 B LEU   A 1 169 ? 3.332  -21.641 4.254   0.38 25.47 ?  169 LEU   A HD23 1 
ATOM   3968 N  N    A SER   B 1 1   ? 50.776 -9.241  -23.705 0.62 28.09 ?  1   SER   B N    1 
ATOM   3969 N  N    B SER   B 1 1   ? 50.774 -9.256  -23.679 0.38 26.27 ?  1   SER   B N    1 
ATOM   3970 C  CA   A SER   B 1 1   ? 51.281 -10.293 -22.802 0.62 28.02 ?  1   SER   B CA   1 
ATOM   3971 C  CA   B SER   B 1 1   ? 51.239 -10.254 -22.694 0.38 26.15 ?  1   SER   B CA   1 
ATOM   3972 C  C    A SER   B 1 1   ? 50.213 -11.351 -22.559 0.62 26.89 ?  1   SER   B C    1 
ATOM   3973 C  C    B SER   B 1 1   ? 50.172 -11.313 -22.461 0.38 24.96 ?  1   SER   B C    1 
ATOM   3974 O  O    A SER   B 1 1   ? 49.020 -11.149 -22.827 0.62 26.88 ?  1   SER   B O    1 
ATOM   3975 O  O    B SER   B 1 1   ? 48.997 -11.134 -22.802 0.38 24.89 ?  1   SER   B O    1 
ATOM   3976 C  CB   A SER   B 1 1   ? 51.733 -9.694  -21.472 0.62 28.73 ?  1   SER   B CB   1 
ATOM   3977 C  CB   B SER   B 1 1   ? 51.592 -9.580  -21.372 0.38 26.91 ?  1   SER   B CB   1 
ATOM   3978 O  OG   A SER   B 1 1   ? 50.620 -9.391  -20.653 0.62 30.31 ?  1   SER   B OG   1 
ATOM   3979 O  OG   B SER   B 1 1   ? 50.419 -9.268  -20.642 0.38 28.07 ?  1   SER   B OG   1 
ATOM   3980 H  H1   A SER   B 1 1   ? 50.702 -9.575  -24.524 0.62 33.70 ?  1   SER   B H1   1 
ATOM   3981 H  H1   B SER   B 1 1   ? 50.740 -9.636  -24.481 0.38 31.51 ?  1   SER   B H1   1 
ATOM   3982 H  H2   A SER   B 1 1   ? 49.984 -8.968  -23.415 0.62 33.70 ?  1   SER   B H2   1 
ATOM   3983 H  H2   B SER   B 1 1   ? 49.969 -8.972  -23.443 0.38 31.51 ?  1   SER   B H2   1 
ATOM   3984 H  H3   A SER   B 1 1   ? 51.350 -8.563  -23.706 0.62 33.70 ?  1   SER   B H3   1 
ATOM   3985 H  H3   B SER   B 1 1   ? 51.345 -8.577  -23.692 0.38 31.51 ?  1   SER   B H3   1 
ATOM   3986 H  HA   A SER   B 1 1   ? 52.044 -10.714 -23.224 0.62 33.60 ?  1   SER   B HA   1 
ATOM   3987 H  HA   B SER   B 1 1   ? 52.033 -10.680 -23.045 0.38 31.36 ?  1   SER   B HA   1 
ATOM   3988 H  HB2  A SER   B 1 1   ? 52.293 -10.341 -21.017 0.62 34.46 ?  1   SER   B HB2  1 
ATOM   3989 H  HB2  B SER   B 1 1   ? 52.149 -10.185 -20.857 0.38 32.28 ?  1   SER   B HB2  1 
ATOM   3990 H  HB3  A SER   B 1 1   ? 52.235 -8.881  -21.643 0.62 34.46 ?  1   SER   B HB3  1 
ATOM   3991 H  HB3  B SER   B 1 1   ? 52.074 -8.758  -21.553 0.38 32.28 ?  1   SER   B HB3  1 
ATOM   3992 H  HG   A SER   B 1 1   ? 50.868 -8.919  -20.003 0.62 36.35 ?  1   SER   B HG   1 
ATOM   3993 H  HG   B SER   B 1 1   ? 50.596 -8.691  -20.059 0.38 33.67 ?  1   SER   B HG   1 
ATOM   3994 N  N    A MET   B 1 2   ? 50.665 -12.482 -22.038 0.62 25.99 ?  2   MET   B N    1 
ATOM   3995 N  N    B MET   B 1 2   ? 50.600 -12.416 -21.864 0.38 23.86 ?  2   MET   B N    1 
ATOM   3996 C  CA   A MET   B 1 2   ? 49.839 -13.668 -21.869 0.62 25.62 ?  2   MET   B CA   1 
ATOM   3997 C  CA   B MET   B 1 2   ? 49.774 -13.602 -21.691 0.38 23.02 ?  2   MET   B CA   1 
ATOM   3998 C  C    A MET   B 1 2   ? 49.590 -13.867 -20.382 0.62 23.11 ?  2   MET   B C    1 
ATOM   3999 C  C    B MET   B 1 2   ? 49.496 -13.780 -20.205 0.38 21.43 ?  2   MET   B C    1 
ATOM   4000 O  O    A MET   B 1 2   ? 50.527 -14.112 -19.617 0.62 23.13 ?  2   MET   B O    1 
ATOM   4001 O  O    B MET   B 1 2   ? 50.398 -14.127 -19.436 0.38 21.65 ?  2   MET   B O    1 
ATOM   4002 C  CB   A MET   B 1 2   ? 50.555 -14.869 -22.473 0.62 29.04 ?  2   MET   B CB   1 
ATOM   4003 C  CB   B MET   B 1 2   ? 50.521 -14.803 -22.249 0.38 24.65 ?  2   MET   B CB   1 
ATOM   4004 C  CG   A MET   B 1 2   ? 49.698 -16.115 -22.600 0.62 32.34 ?  2   MET   B CG   1 
ATOM   4005 C  CG   B MET   B 1 2   ? 49.641 -15.945 -22.732 0.38 26.00 ?  2   MET   B CG   1 
ATOM   4006 S  SD   A MET   B 1 2   ? 50.532 -17.389 -23.563 0.62 35.43 ?  2   MET   B SD   1 
ATOM   4007 S  SD   B MET   B 1 2   ? 50.552 -17.031 -23.837 0.38 27.36 ?  2   MET   B SD   1 
ATOM   4008 C  CE   A MET   B 1 2   ? 51.096 -16.390 -24.938 0.62 35.70 ?  2   MET   B CE   1 
ATOM   4009 C  CE   B MET   B 1 2   ? 51.510 -15.838 -24.738 0.38 27.53 ?  2   MET   B CE   1 
ATOM   4010 H  H    A MET   B 1 2   ? 51.477 -12.594 -21.768 0.62 31.18 ?  2   MET   B H    1 
ATOM   4011 H  H    B MET   B 1 2   ? 51.398 -12.513 -21.550 0.38 28.62 ?  2   MET   B H    1 
ATOM   4012 H  HA   A MET   B 1 2   ? 48.998 -13.554 -22.332 0.62 30.72 ?  2   MET   B HA   1 
ATOM   4013 H  HA   B MET   B 1 2   ? 48.947 -13.508 -22.188 0.38 27.61 ?  2   MET   B HA   1 
ATOM   4014 H  HB2  A MET   B 1 2   ? 50.855 -14.598 -23.351 0.62 34.83 ?  2   MET   B HB2  1 
ATOM   4015 H  HB2  B MET   B 1 2   ? 51.053 -14.452 -22.972 0.38 29.57 ?  2   MET   B HB2  1 
ATOM   4016 H  HB3  A MET   B 1 2   ? 51.318 -15.104 -21.925 0.62 34.83 ?  2   MET   B HB3  1 
ATOM   4017 H  HB3  B MET   B 1 2   ? 51.104 -15.176 -21.578 0.38 29.57 ?  2   MET   B HB3  1 
ATOM   4018 H  HG2  A MET   B 1 2   ? 49.517 -16.468 -21.713 0.62 38.79 ?  2   MET   B HG2  1 
ATOM   4019 H  HG2  B MET   B 1 2   ? 49.338 -16.467 -21.965 0.38 31.18 ?  2   MET   B HG2  1 
ATOM   4020 H  HG3  A MET   B 1 2   ? 48.867 -15.891 -23.049 0.62 38.79 ?  2   MET   B HG3  1 
ATOM   4021 H  HG3  B MET   B 1 2   ? 48.879 -15.603 -23.219 0.38 31.18 ?  2   MET   B HG3  1 
ATOM   4022 H  HE1  A MET   B 1 2   ? 51.266 -16.965 -25.688 0.62 42.82 ?  2   MET   B HE1  1 
ATOM   4023 H  HE1  B MET   B 1 2   ? 51.785 -16.261 -25.538 0.38 33.01 ?  2   MET   B HE1  1 
ATOM   4024 H  HE2  A MET   B 1 2   ? 50.402 -15.743 -25.161 0.62 42.82 ?  2   MET   B HE2  1 
ATOM   4025 H  HE2  B MET   B 1 2   ? 50.949 -15.068 -24.938 0.38 33.01 ?  2   MET   B HE2  1 
ATOM   4026 H  HE3  A MET   B 1 2   ? 51.910 -15.918 -24.685 0.62 42.82 ?  2   MET   B HE3  1 
ATOM   4027 H  HE3  B MET   B 1 2   ? 52.285 -15.570 -24.209 0.38 33.01 ?  2   MET   B HE3  1 
ATOM   4028 N  N    A VAL   B 1 3   ? 48.331 -13.747 -19.973 0.62 20.72 ?  3   VAL   B N    1 
ATOM   4029 N  N    B VAL   B 1 3   ? 48.257 -13.529 -19.804 0.38 19.71 ?  3   VAL   B N    1 
ATOM   4030 C  CA   A VAL   B 1 3   ? 47.924 -13.985 -18.596 0.62 19.73 ?  3   VAL   B CA   1 
ATOM   4031 C  CA   B VAL   B 1 3   ? 47.813 -13.786 -18.441 0.38 18.82 ?  3   VAL   B CA   1 
ATOM   4032 C  C    A VAL   B 1 3   ? 46.682 -14.864 -18.606 0.62 17.72 ?  3   VAL   B C    1 
ATOM   4033 C  C    B VAL   B 1 3   ? 46.561 -14.648 -18.482 0.38 17.42 ?  3   VAL   B C    1 
ATOM   4034 O  O    A VAL   B 1 3   ? 45.983 -14.985 -19.616 0.62 17.73 ?  3   VAL   B O    1 
ATOM   4035 O  O    B VAL   B 1 3   ? 45.747 -14.559 -19.407 0.38 17.68 ?  3   VAL   B O    1 
ATOM   4036 C  CB   A VAL   B 1 3   ? 47.653 -12.674 -17.828 0.62 21.04 ?  3   VAL   B CB   1 
ATOM   4037 C  CB   B VAL   B 1 3   ? 47.553 -12.491 -17.640 0.38 19.53 ?  3   VAL   B CB   1 
ATOM   4038 C  CG1  A VAL   B 1 3   ? 48.926 -11.829 -17.737 0.62 21.44 ?  3   VAL   B CG1  1 
ATOM   4039 C  CG1  B VAL   B 1 3   ? 48.831 -11.671 -17.515 0.38 19.77 ?  3   VAL   B CG1  1 
ATOM   4040 C  CG2  A VAL   B 1 3   ? 46.525 -11.895 -18.490 0.62 21.75 ?  3   VAL   B CG2  1 
ATOM   4041 C  CG2  B VAL   B 1 3   ? 46.441 -11.682 -18.284 0.38 19.89 ?  3   VAL   B CG2  1 
ATOM   4042 H  H    A VAL   B 1 3   ? 47.683 -13.529 -20.492 0.62 24.85 ?  3   VAL   B H    1 
ATOM   4043 H  H    B VAL   B 1 3   ? 47.651 -13.203 -20.319 0.38 23.64 ?  3   VAL   B H    1 
ATOM   4044 H  HA   A VAL   B 1 3   ? 48.633 -14.466 -18.135 0.62 23.66 ?  3   VAL   B HA   1 
ATOM   4045 H  HA   B VAL   B 1 3   ? 48.502 -14.287 -17.981 0.38 22.57 ?  3   VAL   B HA   1 
ATOM   4046 H  HB   A VAL   B 1 3   ? 47.377 -12.897 -16.925 0.62 25.24 ?  3   VAL   B HB   1 
ATOM   4047 H  HB   B VAL   B 1 3   ? 47.267 -12.735 -16.747 0.38 23.42 ?  3   VAL   B HB   1 
ATOM   4048 H  HG11 A VAL   B 1 3   ? 48.729 -11.021 -17.239 0.62 25.71 ?  3   VAL   B HG11 1 
ATOM   4049 H  HG11 B VAL   B 1 3   ? 48.643 -10.874 -16.996 0.38 23.70 ?  3   VAL   B HG11 1 
ATOM   4050 H  HG12 A VAL   B 1 3   ? 49.612 -12.342 -17.279 0.62 25.71 ?  3   VAL   B HG12 1 
ATOM   4051 H  HG12 B VAL   B 1 3   ? 49.506 -12.206 -17.067 0.38 23.70 ?  3   VAL   B HG12 1 
ATOM   4052 H  HG13 A VAL   B 1 3   ? 49.220 -11.606 -18.632 0.62 25.71 ?  3   VAL   B HG13 1 
ATOM   4053 H  HG13 B VAL   B 1 3   ? 49.137 -11.426 -18.401 0.38 23.70 ?  3   VAL   B HG13 1 
ATOM   4054 H  HG21 A VAL   B 1 3   ? 46.469 -11.019 -18.083 0.62 26.09 ?  3   VAL   B HG21 1 
ATOM   4055 H  HG21 B VAL   B 1 3   ? 46.399 -10.814 -17.859 0.38 23.86 ?  3   VAL   B HG21 1 
ATOM   4056 H  HG22 A VAL   B 1 3   ? 46.713 -11.811 -19.437 0.62 26.09 ?  3   VAL   B HG22 1 
ATOM   4057 H  HG22 B VAL   B 1 3   ? 46.631 -11.582 -19.230 0.38 23.86 ?  3   VAL   B HG22 1 
ATOM   4058 H  HG23 A VAL   B 1 3   ? 45.690 -12.375 -18.361 0.62 26.09 ?  3   VAL   B HG23 1 
ATOM   4059 H  HG23 B VAL   B 1 3   ? 45.599 -12.151 -18.164 0.38 23.86 ?  3   VAL   B HG23 1 
ATOM   4060 N  N    . ASN   B 1 4   ? 46.412 -15.487 -17.460 1.00 16.26 ?  4   ASN   B N    1 
ATOM   4061 C  CA   . ASN   B 1 4   ? 45.274 -16.397 -17.339 1.00 15.09 ?  4   ASN   B CA   1 
ATOM   4062 C  C    . ASN   B 1 4   ? 45.223 -17.367 -18.517 1.00 15.57 ?  4   ASN   B C    1 
ATOM   4063 O  O    . ASN   B 1 4   ? 44.166 -17.622 -19.087 1.00 16.30 ?  4   ASN   B O    1 
ATOM   4064 C  CB   . ASN   B 1 4   ? 43.952 -15.637 -17.175 1.00 14.68 ?  4   ASN   B CB   1 
ATOM   4065 C  CG   . ASN   B 1 4   ? 43.907 -14.824 -15.895 1.00 13.97 ?  4   ASN   B CG   1 
ATOM   4066 O  OD1  . ASN   B 1 4   ? 44.194 -15.336 -14.817 1.00 13.62 ?  4   ASN   B OD1  1 
ATOM   4067 N  ND2  . ASN   B 1 4   ? 43.571 -13.544 -16.011 1.00 15.02 ?  4   ASN   B ND2  1 
ATOM   4068 H  H    A ASN   B 1 4   ? 46.874 -15.400 -16.743 0.62 19.50 ?  4   ASN   B H    1 
ATOM   4069 H  H    B ASN   B 1 4   ? 46.973 -15.549 -16.814 0.38 19.50 ?  4   ASN   B H    1 
ATOM   4070 H  HA   . ASN   B 1 4   ? 45.402 -16.927 -16.539 1.00 18.10 ?  4   ASN   B HA   1 
ATOM   4071 H  HB2  . ASN   B 1 4   ? 43.837 -15.030 -17.921 1.00 17.60 ?  4   ASN   B HB2  1 
ATOM   4072 H  HB3  . ASN   B 1 4   ? 43.221 -16.277 -17.153 1.00 17.60 ?  4   ASN   B HB3  1 
ATOM   4073 H  HD21 . ASN   B 1 4   ? 43.539 -13.041 -15.310 1.00 18.01 ?  4   ASN   B HD21 1 
ATOM   4074 H  HD22 . ASN   B 1 4   ? 43.386 -13.214 -16.782 1.00 18.01 ?  4   ASN   B HD22 1 
ATOM   4075 N  N    . SER   B 1 5   ? 46.384 -17.901 -18.895 1.00 16.45 ?  5   SER   B N    1 
ATOM   4076 C  CA   . SER   B 1 5   ? 46.485 -18.819 -20.030 1.00 18.69 ?  5   SER   B CA   1 
ATOM   4077 C  C    . SER   B 1 5   ? 46.463 -20.254 -19.511 1.00 20.25 ?  5   SER   B C    1 
ATOM   4078 O  O    . SER   B 1 5   ? 47.469 -20.953 -19.467 1.00 22.55 ?  5   SER   B O    1 
ATOM   4079 C  CB   . SER   B 1 5   ? 47.748 -18.527 -20.839 1.00 20.00 ?  5   SER   B CB   1 
ATOM   4080 O  OG   . SER   B 1 5   ? 48.908 -18.653 -20.033 1.00 22.68 ?  5   SER   B OG   1 
ATOM   4081 H  H    . SER   B 1 5   ? 47.136 -17.755 -18.502 1.00 19.72 ?  5   SER   B H    1 
ATOM   4082 H  HA   . SER   B 1 5   ? 45.723 -18.694 -20.613 1.00 22.41 ?  5   SER   B HA   1 
ATOM   4083 H  HB2  . SER   B 1 5   ? 47.804 -19.151 -21.583 1.00 23.98 ?  5   SER   B HB2  1 
ATOM   4084 H  HB3  . SER   B 1 5   ? 47.693 -17.620 -21.179 1.00 23.98 ?  5   SER   B HB3  1 
ATOM   4085 H  HG   . SER   B 1 5   ? 48.977 -19.441 -19.753 1.00 27.20 ?  5   SER   B HG   1 
ATOM   4086 N  N    . PHE   B 1 6   ? 45.275 -20.668 -19.085 1.00 20.56 ?  6   PHE   B N    1 
ATOM   4087 C  CA   . PHE   B 1 6   ? 45.072 -22.011 -18.564 1.00 20.06 ?  6   PHE   B CA   1 
ATOM   4088 C  C    . PHE   B 1 6   ? 44.983 -22.991 -19.724 1.00 23.37 ?  6   PHE   B C    1 
ATOM   4089 O  O    . PHE   B 1 6   ? 44.295 -22.725 -20.714 1.00 25.32 ?  6   PHE   B O    1 
ATOM   4090 C  CB   . PHE   B 1 6   ? 43.782 -22.058 -17.748 1.00 18.25 ?  6   PHE   B CB   1 
ATOM   4091 C  CG   . PHE   B 1 6   ? 43.809 -21.200 -16.516 1.00 16.06 ?  6   PHE   B CG   1 
ATOM   4092 C  CD1  . PHE   B 1 6   ? 44.320 -21.692 -15.329 1.00 15.24 ?  6   PHE   B CD1  1 
ATOM   4093 C  CD2  . PHE   B 1 6   ? 43.328 -19.901 -16.546 1.00 15.75 ?  6   PHE   B CD2  1 
ATOM   4094 C  CE1  . PHE   B 1 6   ? 44.334 -20.908 -14.185 1.00 14.60 ?  6   PHE   B CE1  1 
ATOM   4095 C  CE2  . PHE   B 1 6   ? 43.350 -19.107 -15.411 1.00 16.29 ?  6   PHE   B CE2  1 
ATOM   4096 C  CZ   . PHE   B 1 6   ? 43.858 -19.604 -14.233 1.00 15.28 ?  6   PHE   B CZ   1 
ATOM   4097 H  H    . PHE   B 1 6   ? 44.564 -20.186 -19.092 1.00 24.66 ?  6   PHE   B H    1 
ATOM   4098 H  HA   . PHE   B 1 6   ? 45.816 -22.264 -17.997 1.00 24.06 ?  6   PHE   B HA   1 
ATOM   4099 H  HB2  . PHE   B 1 6   ? 43.048 -21.755 -18.307 1.00 21.88 ?  6   PHE   B HB2  1 
ATOM   4100 H  HB3  . PHE   B 1 6   ? 43.621 -22.975 -17.470 1.00 21.88 ?  6   PHE   B HB3  1 
ATOM   4101 H  HD1  . PHE   B 1 6   ? 44.647 -22.564 -15.295 1.00 18.27 ?  6   PHE   B HD1  1 
ATOM   4102 H  HD2  . PHE   B 1 6   ? 42.982 -19.561 -17.337 1.00 18.89 ?  6   PHE   B HD2  1 
ATOM   4103 H  HE1  . PHE   B 1 6   ? 44.690 -21.245 -13.391 1.00 17.51 ?  6   PHE   B HE1  1 
ATOM   4104 H  HE2  . PHE   B 1 6   ? 43.021 -18.239 -15.447 1.00 19.53 ?  6   PHE   B HE2  1 
ATOM   4105 H  HZ   . PHE   B 1 6   ? 43.873 -19.076 -13.469 1.00 18.32 ?  6   PHE   B HZ   1 
ATOM   4106 N  N    . SER   B 1 7   ? 45.689 -24.116 -19.606 1.00 24.15 ?  7   SER   B N    1 
ATOM   4107 C  CA   . SER   B 1 7   ? 45.756 -25.104 -20.673 1.00 26.67 ?  7   SER   B CA   1 
ATOM   4108 C  C    . SER   B 1 7   ? 45.693 -26.507 -20.090 1.00 26.03 ?  7   SER   B C    1 
ATOM   4109 O  O    . SER   B 1 7   ? 46.295 -26.787 -19.048 1.00 27.11 ?  7   SER   B O    1 
ATOM   4110 C  CB   . SER   B 1 7   ? 47.049 -24.944 -21.486 1.00 29.20 ?  7   SER   B CB   1 
ATOM   4111 O  OG   . SER   B 1 7   ? 47.026 -25.761 -22.642 1.00 30.98 ?  7   SER   B OG   1 
ATOM   4112 H  H    . SER   B 1 7   ? 46.150 -24.324 -18.907 1.00 28.96 ?  7   SER   B H    1 
ATOM   4113 H  HA   . SER   B 1 7   ? 45.005 -24.989 -21.267 1.00 31.98 ?  7   SER   B HA   1 
ATOM   4114 H  HB2  . SER   B 1 7   ? 47.136 -24.019 -21.762 1.00 35.03 ?  7   SER   B HB2  1 
ATOM   4115 H  HB3  . SER   B 1 7   ? 47.806 -25.197 -20.933 1.00 35.03 ?  7   SER   B HB3  1 
ATOM   4116 H  HG   . SER   B 1 7   ? 47.740 -25.671 -23.074 1.00 37.16 ?  7   SER   B HG   1 
ATOM   4117 N  N    . GLY   B 1 8   ? 44.970 -27.389 -20.777 1.00 25.78 ?  8   GLY   B N    1 
ATOM   4118 C  CA   . GLY   B 1 8   ? 44.928 -28.783 -20.398 1.00 25.18 ?  8   GLY   B CA   1 
ATOM   4119 C  C    . GLY   B 1 8   ? 43.991 -29.107 -19.263 1.00 23.65 ?  8   GLY   B C    1 
ATOM   4120 O  O    . GLY   B 1 8   ? 44.125 -30.177 -18.654 1.00 25.17 ?  8   GLY   B O    1 
ATOM   4121 H  H    . GLY   B 1 8   ? 44.501 -27.194 -21.469 1.00 30.91 ?  8   GLY   B H    1 
ATOM   4122 H  HA2  . GLY   B 1 8   ? 44.659 -29.308 -21.167 1.00 30.20 ?  8   GLY   B HA2  1 
ATOM   4123 H  HA3  . GLY   B 1 8   ? 45.815 -29.066 -20.133 1.00 30.20 ?  8   GLY   B HA3  1 
ATOM   4124 N  N    . TYR   B 1 9   ? 43.027 -28.239 -18.968 1.00 21.94 ?  9   TYR   B N    1 
ATOM   4125 C  CA   . TYR   B 1 9   ? 42.072 -28.525 -17.911 1.00 19.84 ?  9   TYR   B CA   1 
ATOM   4126 C  C    . TYR   B 1 9   ? 40.897 -29.326 -18.437 1.00 19.23 ?  9   TYR   B C    1 
ATOM   4127 O  O    . TYR   B 1 9   ? 40.486 -29.194 -19.593 1.00 21.24 ?  9   TYR   B O    1 
ATOM   4128 C  CB   . TYR   B 1 9   ? 41.548 -27.248 -17.262 1.00 19.03 ?  9   TYR   B CB   1 
ATOM   4129 C  CG   . TYR   B 1 9   ? 42.575 -26.608 -16.362 1.00 18.50 ?  9   TYR   B CG   1 
ATOM   4130 C  CD1  . TYR   B 1 9   ? 43.644 -25.905 -16.895 1.00 18.72 ?  9   TYR   B CD1  1 
ATOM   4131 C  CD2  . TYR   B 1 9   ? 42.496 -26.735 -14.983 1.00 17.72 ?  9   TYR   B CD2  1 
ATOM   4132 C  CE1  . TYR   B 1 9   ? 44.598 -25.337 -16.079 1.00 18.75 ?  9   TYR   B CE1  1 
ATOM   4133 C  CE2  . TYR   B 1 9   ? 43.447 -26.166 -14.156 1.00 17.84 ?  9   TYR   B CE2  1 
ATOM   4134 C  CZ   . TYR   B 1 9   ? 44.499 -25.467 -14.710 1.00 18.59 ?  9   TYR   B CZ   1 
ATOM   4135 O  OH   . TYR   B 1 9   ? 45.452 -24.907 -13.894 1.00 19.39 ?  9   TYR   B OH   1 
ATOM   4136 H  H    . TYR   B 1 9   ? 42.891 -27.495 -19.376 1.00 26.32 ?  9   TYR   B H    1 
ATOM   4137 H  HA   . TYR   B 1 9   ? 42.501 -29.053 -17.226 1.00 23.79 ?  9   TYR   B HA   1 
ATOM   4138 H  HB2  . TYR   B 1 9   ? 41.298 -26.608 -17.948 1.00 22.82 ?  9   TYR   B HB2  1 
ATOM   4139 H  HB3  . TYR   B 1 9   ? 40.779 -27.477 -16.721 1.00 22.82 ?  9   TYR   B HB3  1 
ATOM   4140 H  HD1  . TYR   B 1 9   ? 43.712 -25.816 -17.819 1.00 22.45 ?  9   TYR   B HD1  1 
ATOM   4141 H  HD2  . TYR   B 1 9   ? 41.786 -27.214 -14.608 1.00 21.25 ?  9   TYR   B HD2  1 
ATOM   4142 H  HE1  . TYR   B 1 9   ? 45.301 -24.867 -16.452 1.00 22.48 ?  9   TYR   B HE1  1 
ATOM   4143 H  HE2  . TYR   B 1 9   ? 43.372 -26.266 -13.234 1.00 21.39 ?  9   TYR   B HE2  1 
ATOM   4144 H  HH   . TYR   B 1 9   ? 46.022 -24.515 -14.361 1.00 23.26 ?  9   TYR   B HH   1 
ATOM   4145 N  N    . LEU   B 1 10  ? 40.364 -30.167 -17.558 1.00 17.61 ?  10  LEU   B N    1 
ATOM   4146 C  CA   . LEU   B 1 10  ? 39.157 -30.926 -17.822 1.00 17.56 ?  10  LEU   B CA   1 
ATOM   4147 C  C    . LEU   B 1 10  ? 37.973 -30.156 -17.254 1.00 16.99 ?  10  LEU   B C    1 
ATOM   4148 O  O    . LEU   B 1 10  ? 37.993 -29.739 -16.090 1.00 16.93 ?  10  LEU   B O    1 
ATOM   4149 C  CB   . LEU   B 1 10  ? 39.266 -32.291 -17.144 1.00 18.34 ?  10  LEU   B CB   1 
ATOM   4150 C  CG   . LEU   B 1 10  ? 38.136 -33.265 -17.456 1.00 20.13 ?  10  LEU   B CG   1 
ATOM   4151 C  CD1  . LEU   B 1 10  ? 38.260 -33.789 -18.879 1.00 21.41 ?  10  LEU   B CD1  1 
ATOM   4152 C  CD2  . LEU   B 1 10  ? 38.112 -34.407 -16.452 1.00 21.28 ?  10  LEU   B CD2  1 
ATOM   4153 H  H    . LEU   B 1 10  ? 40.687 -30.314 -16.770 1.00 21.11 ?  10  LEU   B H    1 
ATOM   4154 H  HA   . LEU   B 1 10  ? 39.031 -31.052 -18.772 1.00 21.06 ?  10  LEU   B HA   1 
ATOM   4155 H  HB2  . LEU   B 1 10  ? 40.096 -32.710 -17.425 1.00 21.99 ?  10  LEU   B HB2  1 
ATOM   4156 H  HB3  . LEU   B 1 10  ? 39.280 -32.163 -16.181 1.00 21.99 ?  10  LEU   B HB3  1 
ATOM   4157 H  HG   . LEU   B 1 10  ? 37.289 -32.799 -17.386 1.00 24.14 ?  10  LEU   B HG   1 
ATOM   4158 H  HD11 . LEU   B 1 10  ? 37.560 -34.441 -19.037 1.00 25.67 ?  10  LEU   B HD11 1 
ATOM   4159 H  HD12 . LEU   B 1 10  ? 38.165 -33.046 -19.495 1.00 25.67 ?  10  LEU   B HD12 1 
ATOM   4160 H  HD13 . LEU   B 1 10  ? 39.129 -34.202 -18.988 1.00 25.67 ?  10  LEU   B HD13 1 
ATOM   4161 H  HD21 . LEU   B 1 10  ? 37.388 -35.010 -16.679 1.00 25.52 ?  10  LEU   B HD21 1 
ATOM   4162 H  HD22 . LEU   B 1 10  ? 38.959 -34.873 -16.486 1.00 25.52 ?  10  LEU   B HD22 1 
ATOM   4163 H  HD23 . LEU   B 1 10  ? 37.971 -34.038 -15.565 1.00 25.52 ?  10  LEU   B HD23 1 
ATOM   4164 N  N    . LYS   B 1 11  ? 36.946 -29.969 -18.075 1.00 18.13 ?  11  LYS   B N    1 
ATOM   4165 C  CA   . LYS   B 1 11  ? 35.754 -29.252 -17.652 1.00 20.12 ?  11  LYS   B CA   1 
ATOM   4166 C  C    . LYS   B 1 11  ? 34.885 -30.182 -16.812 1.00 19.23 ?  11  LYS   B C    1 
ATOM   4167 O  O    . LYS   B 1 11  ? 34.511 -31.270 -17.266 1.00 21.10 ?  11  LYS   B O    1 
ATOM   4168 C  CB   . LYS   B 1 11  ? 35.002 -28.776 -18.895 1.00 23.98 ?  11  LYS   B CB   1 
ATOM   4169 C  CG   . LYS   B 1 11  ? 33.850 -27.824 -18.639 1.00 27.56 ?  11  LYS   B CG   1 
ATOM   4170 C  CD   . LYS   B 1 11  ? 33.127 -27.515 -19.944 1.00 30.45 ?  11  LYS   B CD   1 
ATOM   4171 C  CE   . LYS   B 1 11  ? 32.109 -26.403 -19.777 1.00 32.55 ?  11  LYS   B CE   1 
ATOM   4172 N  NZ   . LYS   B 1 11  ? 32.763 -25.088 -19.546 1.00 33.71 ?  11  LYS   B NZ   1 
ATOM   4173 H  H    . LYS   B 1 11  ? 36.910 -30.258 -18.886 1.00 21.74 ?  11  LYS   B H    1 
ATOM   4174 H  HA   . LYS   B 1 11  ? 36.002 -28.482 -17.118 1.00 24.13 ?  11  LYS   B HA   1 
ATOM   4175 H  HB2  . LYS   B 1 11  ? 35.631 -28.318 -19.476 1.00 28.76 ?  11  LYS   B HB2  1 
ATOM   4176 H  HB3  . LYS   B 1 11  ? 34.643 -29.550 -19.354 1.00 28.76 ?  11  LYS   B HB3  1 
ATOM   4177 H  HG2  . LYS   B 1 11  ? 33.218 -28.234 -18.028 1.00 33.06 ?  11  LYS   B HG2  1 
ATOM   4178 H  HG3  . LYS   B 1 11  ? 34.189 -26.992 -18.272 1.00 33.06 ?  11  LYS   B HG3  1 
ATOM   4179 H  HD2  . LYS   B 1 11  ? 33.776 -27.236 -20.610 1.00 36.52 ?  11  LYS   B HD2  1 
ATOM   4180 H  HD3  . LYS   B 1 11  ? 32.662 -28.312 -20.246 1.00 36.52 ?  11  LYS   B HD3  1 
ATOM   4181 H  HE2  . LYS   B 1 11  ? 31.572 -26.340 -20.582 1.00 39.04 ?  11  LYS   B HE2  1 
ATOM   4182 H  HE3  . LYS   B 1 11  ? 31.546 -26.607 -19.014 1.00 39.04 ?  11  LYS   B HE3  1 
ATOM   4183 H  HZ1  . LYS   B 1 11  ? 32.146 -24.452 -19.470 1.00 40.43 ?  11  LYS   B HZ1  1 
ATOM   4184 H  HZ2  . LYS   B 1 11  ? 33.246 -25.116 -18.800 1.00 40.43 ?  11  LYS   B HZ2  1 
ATOM   4185 H  HZ3  . LYS   B 1 11  ? 33.298 -24.892 -20.230 1.00 40.43 ?  11  LYS   B HZ3  1 
ATOM   4186 N  N    . LEU   B 1 12  ? 34.566 -29.761 -15.587 1.00 17.60 ?  12  LEU   B N    1 
ATOM   4187 C  CA   . LEU   B 1 12  ? 33.608 -30.471 -14.746 1.00 17.06 ?  12  LEU   B CA   1 
ATOM   4188 C  C    . LEU   B 1 12  ? 32.217 -29.865 -14.841 1.00 17.01 ?  12  LEU   B C    1 
ATOM   4189 O  O    . LEU   B 1 12  ? 31.232 -30.584 -15.017 1.00 17.45 ?  12  LEU   B O    1 
ATOM   4190 C  CB   . LEU   B 1 12  ? 34.067 -30.493 -13.283 1.00 16.57 ?  12  LEU   B CB   1 
ATOM   4191 C  CG   . LEU   B 1 12  ? 35.413 -31.165 -13.015 1.00 16.47 ?  12  LEU   B CG   1 
ATOM   4192 C  CD1  . LEU   B 1 12  ? 35.775 -31.126 -11.538 1.00 16.88 ?  12  LEU   B CD1  1 
ATOM   4193 C  CD2  . LEU   B 1 12  ? 35.412 -32.601 -13.535 1.00 17.10 ?  12  LEU   B CD2  1 
ATOM   4194 H  H    . LEU   B 1 12  ? 34.889 -29.053 -15.220 1.00 21.11 ?  12  LEU   B H    1 
ATOM   4195 H  HA   . LEU   B 1 12  ? 33.538 -31.386 -15.052 1.00 20.46 ?  12  LEU   B HA   1 
ATOM   4196 H  HB2  . LEU   B 1 12  ? 34.129 -29.579 -12.968 1.00 19.86 ?  12  LEU   B HB2  1 
ATOM   4197 H  HB3  . LEU   B 1 12  ? 33.395 -30.967 -12.762 1.00 19.86 ?  12  LEU   B HB3  1 
ATOM   4198 H  HG   . LEU   B 1 12  ? 36.098 -30.681 -13.496 1.00 19.75 ?  12  LEU   B HG   1 
ATOM   4199 H  HD11 . LEU   B 1 12  ? 36.639 -31.559 -11.414 1.00 20.24 ?  12  LEU   B HD11 1 
ATOM   4200 H  HD12 . LEU   B 1 12  ? 35.829 -30.202 -11.248 1.00 20.24 ?  12  LEU   B HD12 1 
ATOM   4201 H  HD13 . LEU   B 1 12  ? 35.097 -31.595 -11.029 1.00 20.24 ?  12  LEU   B HD13 1 
ATOM   4202 H  HD21 . LEU   B 1 12  ? 36.211 -33.050 -13.220 1.00 20.50 ?  12  LEU   B HD21 1 
ATOM   4203 H  HD22 . LEU   B 1 12  ? 34.622 -33.056 -13.203 1.00 20.50 ?  12  LEU   B HD22 1 
ATOM   4204 H  HD23 . LEU   B 1 12  ? 35.401 -32.584 -14.505 1.00 20.50 ?  12  LEU   B HD23 1 
ATOM   4205 N  N    . THR   B 1 13  ? 32.129 -28.547 -14.728 1.00 16.90 ?  13  THR   B N    1 
ATOM   4206 C  CA   . THR   B 1 13  ? 30.903 -27.796 -14.927 1.00 17.00 ?  13  THR   B CA   1 
ATOM   4207 C  C    . THR   B 1 13  ? 31.235 -26.602 -15.814 1.00 18.93 ?  13  THR   B C    1 
ATOM   4208 O  O    . THR   B 1 13  ? 32.379 -26.415 -16.242 1.00 19.74 ?  13  THR   B O    1 
ATOM   4209 C  CB   . THR   B 1 13  ? 30.311 -27.317 -13.596 1.00 16.51 ?  13  THR   B CB   1 
ATOM   4210 O  OG1  . THR   B 1 13  ? 31.159 -26.298 -13.050 1.00 16.32 ?  13  THR   B OG1  1 
ATOM   4211 C  CG2  . THR   B 1 13  ? 30.184 -28.476 -12.605 1.00 16.82 ?  13  THR   B CG2  1 
ATOM   4212 H  H    . THR   B 1 13  ? 32.797 -28.043 -14.528 1.00 20.27 ?  13  THR   B H    1 
ATOM   4213 H  HA   . THR   B 1 13  ? 30.244 -28.347 -15.373 1.00 20.38 ?  13  THR   B HA   1 
ATOM   4214 H  HB   . THR   B 1 13  ? 29.422 -26.949 -13.748 1.00 19.80 ?  13  THR   B HB   1 
ATOM   4215 H  HG1  . THR   B 1 13  ? 30.855 -25.533 -13.243 1.00 19.57 ?  13  THR   B HG1  1 
ATOM   4216 H  HG21 . THR   B 1 13  ? 29.692 -28.194 -11.817 1.00 20.16 ?  13  THR   B HG21 1 
ATOM   4217 H  HG22 . THR   B 1 13  ? 29.709 -29.216 -13.020 1.00 20.16 ?  13  THR   B HG22 1 
ATOM   4218 H  HG23 . THR   B 1 13  ? 31.063 -28.782 -12.335 1.00 20.16 ?  13  THR   B HG23 1 
ATOM   4219 N  N    A ASP   B 1 14  ? 30.224 -25.775 -16.076 0.62 19.93 ?  14  ASP   B N    1 
ATOM   4220 N  N    B ASP   B 1 14  ? 30.229 -25.764 -16.071 0.38 19.63 ?  14  ASP   B N    1 
ATOM   4221 C  CA   A ASP   B 1 14  ? 30.438 -24.617 -16.934 0.62 21.31 ?  14  ASP   B CA   1 
ATOM   4222 C  CA   B ASP   B 1 14  ? 30.431 -24.610 -16.940 0.38 20.47 ?  14  ASP   B CA   1 
ATOM   4223 C  C    A ASP   B 1 14  ? 31.541 -23.711 -16.399 0.62 19.35 ?  14  ASP   B C    1 
ATOM   4224 C  C    B ASP   B 1 14  ? 31.409 -23.595 -16.369 0.38 18.76 ?  14  ASP   B C    1 
ATOM   4225 O  O    A ASP   B 1 14  ? 32.228 -23.047 -17.186 0.62 20.12 ?  14  ASP   B O    1 
ATOM   4226 O  O    B ASP   B 1 14  ? 31.834 -22.698 -17.106 0.38 19.01 ?  14  ASP   B O    1 
ATOM   4227 C  CB   A ASP   B 1 14  ? 29.132 -23.841 -17.106 0.62 24.97 ?  14  ASP   B CB   1 
ATOM   4228 C  CB   B ASP   B 1 14  ? 29.105 -23.903 -17.213 0.38 23.20 ?  14  ASP   B CB   1 
ATOM   4229 C  CG   A ASP   B 1 14  ? 28.150 -24.542 -18.020 0.62 28.36 ?  14  ASP   B CG   1 
ATOM   4230 C  CG   B ASP   B 1 14  ? 28.236 -24.659 -18.196 0.38 25.64 ?  14  ASP   B CG   1 
ATOM   4231 O  OD1  A ASP   B 1 14  ? 28.508 -25.575 -18.630 0.62 29.57 ?  14  ASP   B OD1  1 
ATOM   4232 O  OD1  B ASP   B 1 14  ? 28.796 -25.312 -19.103 0.38 26.52 ?  14  ASP   B OD1  1 
ATOM   4233 O  OD2  A ASP   B 1 14  ? 27.005 -24.058 -18.117 0.62 29.63 -1 14  ASP   B OD2  1 
ATOM   4234 O  OD2  B ASP   B 1 14  ? 26.996 -24.609 -18.063 0.38 26.46 -1 14  ASP   B OD2  1 
ATOM   4235 H  H    A ASP   B 1 14  ? 29.426 -25.851 -15.764 0.62 23.90 ?  14  ASP   B H    1 
ATOM   4236 H  H    B ASP   B 1 14  ? 29.434 -25.834 -15.750 0.38 23.53 ?  14  ASP   B H    1 
ATOM   4237 H  HA   A ASP   B 1 14  ? 30.719 -24.917 -17.807 0.62 25.56 ?  14  ASP   B HA   1 
ATOM   4238 H  HA   B ASP   B 1 14  ? 30.778 -24.921 -17.790 0.38 24.55 ?  14  ASP   B HA   1 
ATOM   4239 H  HB2  A ASP   B 1 14  ? 28.690 -23.754 -16.251 0.62 29.95 ?  14  ASP   B HB2  1 
ATOM   4240 H  HB2  B ASP   B 1 14  ? 28.617 -23.817 -16.379 0.38 27.82 ?  14  ASP   B HB2  1 
ATOM   4241 H  HB3  A ASP   B 1 14  ? 29.320 -22.966 -17.479 0.62 29.95 ?  14  ASP   B HB3  1 
ATOM   4242 H  HB3  B ASP   B 1 14  ? 29.290 -23.018 -17.576 0.38 27.82 ?  14  ASP   B HB3  1 
ATOM   4243 N  N    . ASN   B 1 15  ? 31.745 -23.684 -15.080 1.00 17.18 ?  15  ASN   B N    1 
ATOM   4244 C  CA   . ASN   B 1 15  ? 32.710 -22.768 -14.475 1.00 15.06 ?  15  ASN   B CA   1 
ATOM   4245 C  C    . ASN   B 1 15  ? 33.806 -23.430 -13.645 1.00 13.80 ?  15  ASN   B C    1 
ATOM   4246 O  O    . ASN   B 1 15  ? 34.660 -22.710 -13.117 1.00 14.01 ?  15  ASN   B O    1 
ATOM   4247 C  CB   . ASN   B 1 15  ? 31.999 -21.717 -13.606 1.00 15.09 ?  15  ASN   B CB   1 
ATOM   4248 C  CG   . ASN   B 1 15  ? 31.387 -22.322 -12.363 1.00 14.65 ?  15  ASN   B CG   1 
ATOM   4249 O  OD1  . ASN   B 1 15  ? 30.447 -23.121 -12.450 1.00 16.16 ?  15  ASN   B OD1  1 
ATOM   4250 N  ND2  . ASN   B 1 15  ? 31.913 -21.969 -11.203 1.00 13.81 ?  15  ASN   B ND2  1 
ATOM   4251 H  H    A ASN   B 1 15  ? 31.339 -24.194 -14.515 0.62 20.60 ?  15  ASN   B H    1 
ATOM   4252 H  H    B ASN   B 1 15  ? 31.394 -24.243 -14.527 0.38 20.60 ?  15  ASN   B H    1 
ATOM   4253 H  HA   . ASN   B 1 15  ? 33.154 -22.282 -15.178 1.00 18.05 ?  15  ASN   B HA   1 
ATOM   4254 H  HB2  . ASN   B 1 15  ? 32.647 -21.039 -13.329 1.00 18.09 ?  15  ASN   B HB2  1 
ATOM   4255 H  HB3  . ASN   B 1 15  ? 31.290 -21.293 -14.118 1.00 18.09 ?  15  ASN   B HB3  1 
ATOM   4256 H  HD21 . ASN   B 1 15  ? 31.596 -22.284 -10.465 1.00 16.55 ?  15  ASN   B HD21 1 
ATOM   4257 H  HD22 . ASN   B 1 15  ? 32.576 -21.412 -11.171 1.00 16.55 ?  15  ASN   B HD22 1 
ATOM   4258 N  N    . VAL   B 1 16  ? 33.815 -24.754 -13.503 1.00 13.59 ?  16  VAL   B N    1 
ATOM   4259 C  CA   . VAL   B 1 16  ? 34.813 -25.447 -12.691 1.00 13.31 ?  16  VAL   B CA   1 
ATOM   4260 C  C    . VAL   B 1 16  ? 35.612 -26.382 -13.586 1.00 13.59 ?  16  VAL   B C    1 
ATOM   4261 O  O    . VAL   B 1 16  ? 35.040 -27.266 -14.243 1.00 14.49 ?  16  VAL   B O    1 
ATOM   4262 C  CB   . VAL   B 1 16  ? 34.186 -26.216 -11.519 1.00 13.73 ?  16  VAL   B CB   1 
ATOM   4263 C  CG1  . VAL   B 1 16  ? 35.273 -26.953 -10.740 1.00 13.74 ?  16  VAL   B CG1  1 
ATOM   4264 C  CG2  . VAL   B 1 16  ? 33.403 -25.266 -10.610 1.00 14.31 ?  16  VAL   B CG2  1 
ATOM   4265 H  H    . VAL   B 1 16  ? 33.236 -25.281 -13.868 1.00 16.29 ?  16  VAL   B H    1 
ATOM   4266 H  HA   . VAL   B 1 16  ? 35.422 -24.788 -12.319 1.00 15.96 ?  16  VAL   B HA   1 
ATOM   4267 H  HB   . VAL   B 1 16  ? 33.566 -26.877 -11.869 1.00 16.46 ?  16  VAL   B HB   1 
ATOM   4268 H  HG11 . VAL   B 1 16  ? 34.908 -27.238 -9.887  1.00 16.47 ?  16  VAL   B HG11 1 
ATOM   4269 H  HG12 . VAL   B 1 16  ? 35.562 -27.725 -11.249 1.00 16.47 ?  16  VAL   B HG12 1 
ATOM   4270 H  HG13 . VAL   B 1 16  ? 36.018 -26.349 -10.595 1.00 16.47 ?  16  VAL   B HG13 1 
ATOM   4271 H  HG21 . VAL   B 1 16  ? 33.052 -25.770 -9.856  1.00 17.15 ?  16  VAL   B HG21 1 
ATOM   4272 H  HG22 . VAL   B 1 16  ? 33.996 -24.570 -10.294 1.00 17.15 ?  16  VAL   B HG22 1 
ATOM   4273 H  HG23 . VAL   B 1 16  ? 32.670 -24.878 -11.114 1.00 17.15 ?  16  VAL   B HG23 1 
ATOM   4274 N  N    . TYR   B 1 17  ? 36.935 -26.214 -13.559 1.00 14.09 ?  17  TYR   B N    1 
ATOM   4275 C  CA   . TYR   B 1 17  ? 37.886 -26.957 -14.372 1.00 14.23 ?  17  TYR   B CA   1 
ATOM   4276 C  C    . TYR   B 1 17  ? 38.935 -27.568 -13.454 1.00 13.32 ?  17  TYR   B C    1 
ATOM   4277 O  O    . TYR   B 1 17  ? 39.208 -27.038 -12.375 1.00 13.54 ?  17  TYR   B O    1 
ATOM   4278 C  CB   . TYR   B 1 17  ? 38.597 -26.021 -15.356 1.00 16.65 ?  17  TYR   B CB   1 
ATOM   4279 C  CG   . TYR   B 1 17  ? 37.672 -25.255 -16.268 1.00 19.05 ?  17  TYR   B CG   1 
ATOM   4280 C  CD1  . TYR   B 1 17  ? 37.070 -24.073 -15.854 1.00 20.64 ?  17  TYR   B CD1  1 
ATOM   4281 C  CD2  . TYR   B 1 17  ? 37.398 -25.718 -17.547 1.00 20.81 ?  17  TYR   B CD2  1 
ATOM   4282 C  CE1  . TYR   B 1 17  ? 36.220 -23.370 -16.693 1.00 22.13 ?  17  TYR   B CE1  1 
ATOM   4283 C  CE2  . TYR   B 1 17  ? 36.557 -25.023 -18.394 1.00 22.31 ?  17  TYR   B CE2  1 
ATOM   4284 C  CZ   . TYR   B 1 17  ? 35.967 -23.851 -17.960 1.00 23.16 ?  17  TYR   B CZ   1 
ATOM   4285 O  OH   . TYR   B 1 17  ? 35.127 -23.158 -18.800 1.00 24.69 ?  17  TYR   B OH   1 
ATOM   4286 H  H    . TYR   B 1 17  ? 37.326 -25.636 -13.048 1.00 16.89 ?  17  TYR   B H    1 
ATOM   4287 H  HA   . TYR   B 1 17  ? 37.426 -27.662 -14.864 1.00 17.06 ?  17  TYR   B HA   1 
ATOM   4288 H  HB2  . TYR   B 1 17  ? 39.123 -25.380 -14.855 1.00 19.97 ?  17  TYR   B HB2  1 
ATOM   4289 H  HB3  . TYR   B 1 17  ? 39.175 -26.554 -15.918 1.00 19.97 ?  17  TYR   B HB3  1 
ATOM   4290 H  HD1  . TYR   B 1 17  ? 37.243 -23.749 -14.999 1.00 24.75 ?  17  TYR   B HD1  1 
ATOM   4291 H  HD2  . TYR   B 1 17  ? 37.791 -26.506 -17.843 1.00 24.95 ?  17  TYR   B HD2  1 
ATOM   4292 H  HE1  . TYR   B 1 17  ? 35.826 -22.577 -16.405 1.00 26.54 ?  17  TYR   B HE1  1 
ATOM   4293 H  HE2  . TYR   B 1 17  ? 36.381 -25.344 -19.250 1.00 26.75 ?  17  TYR   B HE2  1 
ATOM   4294 H  HH   . TYR   B 1 17  ? 35.061 -23.552 -19.538 1.00 29.61 ?  17  TYR   B HH   1 
ATOM   4295 N  N    . ILE   B 1 18  ? 39.544 -28.676 -13.885 1.00 13.37 ?  18  ILE   B N    1 
ATOM   4296 C  CA   . ILE   B 1 18  ? 40.473 -29.400 -13.023 1.00 13.53 ?  18  ILE   B CA   1 
ATOM   4297 C  C    . ILE   B 1 18  ? 41.633 -29.953 -13.842 1.00 13.81 ?  18  ILE   B C    1 
ATOM   4298 O  O    . ILE   B 1 18  ? 41.472 -30.345 -15.003 1.00 15.15 ?  18  ILE   B O    1 
ATOM   4299 C  CB   . ILE   B 1 18  ? 39.722 -30.498 -12.218 1.00 14.10 ?  18  ILE   B CB   1 
ATOM   4300 C  CG1  . ILE   B 1 18  ? 40.582 -31.031 -11.068 1.00 14.61 ?  18  ILE   B CG1  1 
ATOM   4301 C  CG2  . ILE   B 1 18  ? 39.226 -31.618 -13.139 1.00 14.37 ?  18  ILE   B CG2  1 
ATOM   4302 C  CD1  . ILE   B 1 18  ? 39.786 -31.847 -10.055 1.00 15.87 ?  18  ILE   B CD1  1 
ATOM   4303 H  H    . ILE   B 1 18  ? 39.434 -29.025 -14.661 1.00 16.03 ?  18  ILE   B H    1 
ATOM   4304 H  HA   . ILE   B 1 18  ? 40.837 -28.781 -12.374 1.00 16.21 ?  18  ILE   B HA   1 
ATOM   4305 H  HB   . ILE   B 1 18  ? 38.937 -30.089 -11.819 1.00 16.90 ?  18  ILE   B HB   1 
ATOM   4306 H  HG12 . ILE   B 1 18  ? 41.277 -31.597 -11.428 1.00 17.51 ?  18  ILE   B HG12 1 
ATOM   4307 H  HG13 . ILE   B 1 18  ? 40.974 -30.277 -10.597 1.00 17.51 ?  18  ILE   B HG13 1 
ATOM   4308 H  HG21 . ILE   B 1 18  ? 38.635 -32.203 -12.634 1.00 17.23 ?  18  ILE   B HG21 1 
ATOM   4309 H  HG22 . ILE   B 1 18  ? 38.740 -31.220 -13.878 1.00 17.23 ?  18  ILE   B HG22 1 
ATOM   4310 H  HG23 . ILE   B 1 18  ? 39.985 -32.117 -13.468 1.00 17.23 ?  18  ILE   B HG23 1 
ATOM   4311 H  HD11 . ILE   B 1 18  ? 40.377 -32.116 -9.333  1.00 19.03 ?  18  ILE   B HD11 1 
ATOM   4312 H  HD12 . ILE   B 1 18  ? 39.064 -31.301 -9.703  1.00 19.03 ?  18  ILE   B HD12 1 
ATOM   4313 H  HD13 . ILE   B 1 18  ? 39.424 -32.631 -10.495 1.00 19.03 ?  18  ILE   B HD13 1 
ATOM   4314 N  N    . LYS   B 1 19  ? 42.811 -29.995 -13.218 1.00 14.12 ?  19  LYS   B N    1 
ATOM   4315 C  CA   . LYS   B 1 19  ? 44.021 -30.461 -13.878 1.00 15.15 ?  19  LYS   B CA   1 
ATOM   4316 C  C    . LYS   B 1 19  ? 44.928 -31.139 -12.862 1.00 14.72 ?  19  LYS   B C    1 
ATOM   4317 O  O    . LYS   B 1 19  ? 45.019 -30.708 -11.709 1.00 14.25 ?  19  LYS   B O    1 
ATOM   4318 C  CB   . LYS   B 1 19  ? 44.783 -29.293 -14.517 1.00 16.69 ?  19  LYS   B CB   1 
ATOM   4319 C  CG   . LYS   B 1 19  ? 45.964 -29.700 -15.379 1.00 18.42 ?  19  LYS   B CG   1 
ATOM   4320 C  CD   . LYS   B 1 19  ? 46.709 -28.471 -15.888 1.00 20.15 ?  19  LYS   B CD   1 
ATOM   4321 C  CE   . LYS   B 1 19  ? 47.874 -28.853 -16.779 1.00 22.10 ?  19  LYS   B CE   1 
ATOM   4322 N  NZ   . LYS   B 1 19  ? 48.631 -27.668 -17.255 1.00 22.98 ?  19  LYS   B NZ   1 
ATOM   4323 H  H    . LYS   B 1 19  ? 42.924 -29.749 -12.400 1.00 16.93 ?  19  LYS   B H    1 
ATOM   4324 H  HA   . LYS   B 1 19  ? 43.784 -31.100 -14.566 1.00 18.16 ?  19  LYS   B HA   1 
ATOM   4325 H  HB2  . LYS   B 1 19  ? 44.167 -28.799 -15.077 1.00 20.01 ?  19  LYS   B HB2  1 
ATOM   4326 H  HB3  . LYS   B 1 19  ? 45.113 -28.715 -13.807 1.00 20.01 ?  19  LYS   B HB3  1 
ATOM   4327 H  HG2  . LYS   B 1 19  ? 46.570 -30.241 -14.853 1.00 22.08 ?  19  LYS   B HG2  1 
ATOM   4328 H  HG3  . LYS   B 1 19  ? 45.633 -30.205 -16.142 1.00 22.08 ?  19  LYS   B HG3  1 
ATOM   4329 H  HD2  . LYS   B 1 19  ? 46.098 -27.917 -16.400 1.00 24.16 ?  19  LYS   B HD2  1 
ATOM   4330 H  HD3  . LYS   B 1 19  ? 47.053 -27.973 -15.128 1.00 24.16 ?  19  LYS   B HD3  1 
ATOM   4331 H  HE2  . LYS   B 1 19  ? 48.481 -29.422 -16.279 1.00 26.51 ?  19  LYS   B HE2  1 
ATOM   4332 H  HE3  . LYS   B 1 19  ? 47.535 -29.329 -17.554 1.00 26.51 ?  19  LYS   B HE3  1 
ATOM   4333 H  HZ1  . LYS   B 1 19  ? 49.290 -27.924 -17.796 1.00 27.56 ?  19  LYS   B HZ1  1 
ATOM   4334 H  HZ2  . LYS   B 1 19  ? 48.090 -27.118 -17.700 1.00 27.56 ?  19  LYS   B HZ2  1 
ATOM   4335 H  HZ3  . LYS   B 1 19  ? 48.980 -27.231 -16.562 1.00 27.56 ?  19  LYS   B HZ3  1 
ATOM   4336 N  N    . ASN   B 1 20  ? 45.607 -32.192 -13.300 1.00 15.98 ?  20  ASN   B N    1 
ATOM   4337 C  CA   . ASN   B 1 20  ? 46.642 -32.825 -12.491 1.00 17.07 ?  20  ASN   B CA   1 
ATOM   4338 C  C    . ASN   B 1 20  ? 47.908 -31.997 -12.680 1.00 17.42 ?  20  ASN   B C    1 
ATOM   4339 O  O    . ASN   B 1 20  ? 48.551 -32.068 -13.731 1.00 19.35 ?  20  ASN   B O    1 
ATOM   4340 C  CB   . ASN   B 1 20  ? 46.825 -34.267 -12.955 1.00 18.96 ?  20  ASN   B CB   1 
ATOM   4341 C  CG   . ASN   B 1 20  ? 47.978 -34.982 -12.269 1.00 20.51 ?  20  ASN   B CG   1 
ATOM   4342 O  OD1  . ASN   B 1 20  ? 48.633 -35.836 -12.874 1.00 22.74 ?  20  ASN   B OD1  1 
ATOM   4343 N  ND2  . ASN   B 1 20  ? 48.223 -34.660 -11.008 1.00 20.11 ?  20  ASN   B ND2  1 
ATOM   4344 H  H    . ASN   B 1 20  ? 45.484 -32.564 -14.065 1.00 19.16 ?  20  ASN   B H    1 
ATOM   4345 H  HA   . ASN   B 1 20  ? 46.375 -32.819 -11.556 1.00 20.47 ?  20  ASN   B HA   1 
ATOM   4346 H  HB2  . ASN   B 1 20  ? 46.007 -34.760 -12.770 1.00 22.73 ?  20  ASN   B HB2  1 
ATOM   4347 H  HB3  . ASN   B 1 20  ? 46.992 -34.262 -13.911 1.00 22.73 ?  20  ASN   B HB3  1 
ATOM   4348 H  HD21 . ASN   B 1 20  ? 48.868 -35.039 -10.589 1.00 24.11 ?  20  ASN   B HD21 1 
ATOM   4349 H  HD22 . ASN   B 1 20  ? 47.747 -34.062 -10.611 1.00 24.11 ?  20  ASN   B HD22 1 
ATOM   4350 N  N    . ALA   B 1 21  ? 48.266 -31.198 -11.673 1.00 17.11 ?  21  ALA   B N    1 
ATOM   4351 C  CA   . ALA   B 1 21  ? 49.375 -30.268 -11.824 1.00 17.67 ?  21  ALA   B CA   1 
ATOM   4352 C  C    . ALA   B 1 21  ? 49.842 -29.782 -10.460 1.00 16.63 ?  21  ALA   B C    1 
ATOM   4353 O  O    . ALA   B 1 21  ? 49.104 -29.816 -9.471  1.00 16.28 ?  21  ALA   B O    1 
ATOM   4354 C  CB   . ALA   B 1 21  ? 48.973 -29.081 -12.697 1.00 18.88 ?  21  ALA   B CB   1 
ATOM   4355 H  H    . ALA   B 1 21  ? 47.881 -31.184 -10.897 1.00 20.51 ?  21  ALA   B H    1 
ATOM   4356 H  HA   . ALA   B 1 21  ? 50.111 -30.731 -12.251 1.00 21.19 ?  21  ALA   B HA   1 
ATOM   4357 H  HB1  . ALA   B 1 21  ? 49.758 -28.543 -12.854 1.00 22.64 ?  21  ALA   B HB1  1 
ATOM   4358 H  HB2  . ALA   B 1 21  ? 48.623 -29.419 -13.534 1.00 22.64 ?  21  ALA   B HB2  1 
ATOM   4359 H  HB3  . ALA   B 1 21  ? 48.293 -28.569 -12.234 1.00 22.64 ?  21  ALA   B HB3  1 
ATOM   4360 N  N    . ASP   B 1 22  ? 51.100 -29.337 -10.440 1.00 15.97 ?  22  ASP   B N    1 
ATOM   4361 C  CA   . ASP   B 1 22  ? 51.713 -28.642 -9.312  1.00 15.48 ?  22  ASP   B CA   1 
ATOM   4362 C  C    . ASP   B 1 22  ? 51.305 -27.172 -9.392  1.00 13.91 ?  22  ASP   B C    1 
ATOM   4363 O  O    . ASP   B 1 22  ? 51.611 -26.499 -10.379 1.00 14.22 ?  22  ASP   B O    1 
ATOM   4364 C  CB   . ASP   B 1 22  ? 53.232 -28.816 -9.465  1.00 16.89 ?  22  ASP   B CB   1 
ATOM   4365 C  CG   . ASP   B 1 22  ? 54.058 -28.063 -8.427  1.00 18.44 ?  22  ASP   B CG   1 
ATOM   4366 O  OD1  . ASP   B 1 22  ? 53.688 -26.953 -8.009  1.00 18.52 ?  22  ASP   B OD1  1 
ATOM   4367 O  OD2  . ASP   B 1 22  ? 55.139 -28.578 -8.059  1.00 20.93 -1 22  ASP   B OD2  1 
ATOM   4368 H  H    . ASP   B 1 22  ? 51.641 -29.434 -11.105 1.00 19.15 ?  22  ASP   B H    1 
ATOM   4369 H  HA   . ASP   B 1 22  ? 51.421 -29.027 -8.470  1.00 18.56 ?  22  ASP   B HA   1 
ATOM   4370 H  HB2  . ASP   B 1 22  ? 53.455 -29.754 -9.388  1.00 20.25 ?  22  ASP   B HB2  1 
ATOM   4371 H  HB3  . ASP   B 1 22  ? 53.499 -28.482 -10.336 1.00 20.25 ?  22  ASP   B HB3  1 
ATOM   4372 N  N    . ILE   B 1 23  ? 50.597 -26.681 -8.368  1.00 12.90 ?  23  ILE   B N    1 
ATOM   4373 C  CA   . ILE   B 1 23  ? 50.004 -25.341 -8.433  1.00 12.29 ?  23  ILE   B CA   1 
ATOM   4374 C  C    . ILE   B 1 23  ? 51.060 -24.251 -8.571  1.00 12.03 ?  23  ILE   B C    1 
ATOM   4375 O  O    . ILE   B 1 23  ? 50.795 -23.209 -9.175  1.00 11.81 ?  23  ILE   B O    1 
ATOM   4376 C  CB   . ILE   B 1 23  ? 49.067 -25.093 -7.236  1.00 13.01 ?  23  ILE   B CB   1 
ATOM   4377 C  CG1  . ILE   B 1 23  ? 48.235 -23.828 -7.443  1.00 13.37 ?  23  ILE   B CG1  1 
ATOM   4378 C  CG2  . ILE   B 1 23  ? 49.834 -25.054 -5.927  1.00 13.83 ?  23  ILE   B CG2  1 
ATOM   4379 C  CD1  . ILE   B 1 23  ? 47.115 -23.680 -6.430  1.00 14.11 ?  23  ILE   B CD1  1 
ATOM   4380 H  H    . ILE   B 1 23  ? 50.448 -27.108 -7.637  1.00 15.46 ?  23  ILE   B H    1 
ATOM   4381 H  HA   . ILE   B 1 23  ? 49.456 -25.303 -9.230  1.00 14.74 ?  23  ILE   B HA   1 
ATOM   4382 H  HB   . ILE   B 1 23  ? 48.451 -25.842 -7.188  1.00 15.59 ?  23  ILE   B HB   1 
ATOM   4383 H  HG12 . ILE   B 1 23  ? 48.816 -23.052 -7.364  1.00 16.03 ?  23  ILE   B HG12 1 
ATOM   4384 H  HG13 . ILE   B 1 23  ? 47.840 -23.851 -8.331  1.00 16.03 ?  23  ILE   B HG13 1 
ATOM   4385 H  HG21 . ILE   B 1 23  ? 49.203 -25.056 -5.192  1.00 16.58 ?  23  ILE   B HG21 1 
ATOM   4386 H  HG22 . ILE   B 1 23  ? 50.408 -25.833 -5.875  1.00 16.58 ?  23  ILE   B HG22 1 
ATOM   4387 H  HG23 . ILE   B 1 23  ? 50.371 -24.246 -5.903  1.00 16.58 ?  23  ILE   B HG23 1 
ATOM   4388 H  HD11 . ILE   B 1 23  ? 46.572 -22.916 -6.670  1.00 16.91 ?  23  ILE   B HD11 1 
ATOM   4389 H  HD12 . ILE   B 1 23  ? 46.575 -24.488 -6.444  1.00 16.91 ?  23  ILE   B HD12 1 
ATOM   4390 H  HD13 . ILE   B 1 23  ? 47.500 -23.556 -5.551  1.00 16.91 ?  23  ILE   B HD13 1 
ATOM   4391 N  N    . VAL   B 1 24  ? 52.252 -24.455 -8.007  1.00 12.29 ?  24  VAL   B N    1 
ATOM   4392 C  CA   . VAL   B 1 24  ? 53.328 -23.478 -8.176  1.00 13.11 ?  24  VAL   B CA   1 
ATOM   4393 C  C    . VAL   B 1 24  ? 53.781 -23.434 -9.629  1.00 13.12 ?  24  VAL   B C    1 
ATOM   4394 O  O    . VAL   B 1 24  ? 53.934 -22.358 -10.222 1.00 13.82 ?  24  VAL   B O    1 
ATOM   4395 C  CB   . VAL   B 1 24  ? 54.507 -23.796 -7.236  1.00 13.96 ?  24  VAL   B CB   1 
ATOM   4396 C  CG1  . VAL   B 1 24  ? 55.716 -22.919 -7.572  1.00 14.78 ?  24  VAL   B CG1  1 
ATOM   4397 C  CG2  . VAL   B 1 24  ? 54.105 -23.621 -5.795  1.00 14.81 ?  24  VAL   B CG2  1 
ATOM   4398 H  H    . VAL   B 1 24  ? 52.461 -25.139 -7.529  1.00 14.73 ?  24  VAL   B H    1 
ATOM   4399 H  HA   . VAL   B 1 24  ? 52.998 -22.601 -7.943  1.00 15.72 ?  24  VAL   B HA   1 
ATOM   4400 H  HB   . VAL   B 1 24  ? 54.771 -24.726 -7.357  1.00 16.73 ?  24  VAL   B HB   1 
ATOM   4401 H  HG11 . VAL   B 1 24  ? 56.317 -22.906 -6.810  1.00 17.71 ?  24  VAL   B HG11 1 
ATOM   4402 H  HG12 . VAL   B 1 24  ? 56.172 -23.290 -8.343  1.00 17.71 ?  24  VAL   B HG12 1 
ATOM   4403 H  HG13 . VAL   B 1 24  ? 55.407 -22.021 -7.763  1.00 17.71 ?  24  VAL   B HG13 1 
ATOM   4404 H  HG21 . VAL   B 1 24  ? 54.841 -23.888 -5.224  1.00 17.76 ?  24  VAL   B HG21 1 
ATOM   4405 H  HG22 . VAL   B 1 24  ? 53.889 -22.688 -5.643  1.00 17.76 ?  24  VAL   B HG22 1 
ATOM   4406 H  HG23 . VAL   B 1 24  ? 53.328 -24.175 -5.614  1.00 17.76 ?  24  VAL   B HG23 1 
ATOM   4407 N  N    . GLU   B 1 25  ? 54.047 -24.605 -10.213 1.00 13.90 ?  25  GLU   B N    1 
ATOM   4408 C  CA   . GLU   B 1 25  ? 54.445 -24.640 -11.615 1.00 15.40 ?  25  GLU   B CA   1 
ATOM   4409 C  C    . GLU   B 1 25  ? 53.339 -24.092 -12.504 1.00 14.53 ?  25  GLU   B C    1 
ATOM   4410 O  O    . GLU   B 1 25  ? 53.608 -23.368 -13.472 1.00 15.37 ?  25  GLU   B O    1 
ATOM   4411 C  CB   . GLU   B 1 25  ? 54.830 -26.062 -12.015 1.00 19.04 ?  25  GLU   B CB   1 
ATOM   4412 C  CG   . GLU   B 1 25  ? 56.120 -26.527 -11.356 1.00 24.66 ?  25  GLU   B CG   1 
ATOM   4413 C  CD   . GLU   B 1 25  ? 57.247 -25.507 -11.452 1.00 29.42 ?  25  GLU   B CD   1 
ATOM   4414 O  OE1  . GLU   B 1 25  ? 57.631 -25.144 -12.584 1.00 31.14 ?  25  GLU   B OE1  1 
ATOM   4415 O  OE2  . GLU   B 1 25  ? 57.746 -25.053 -10.394 1.00 30.97 -1 25  GLU   B OE2  1 
ATOM   4416 H  H    . GLU   B 1 25  ? 54.010 -25.376 -9.825  1.00 16.66 ?  25  GLU   B H    1 
ATOM   4417 H  HA   . GLU   B 1 25  ? 55.210 -24.062 -11.736 1.00 18.46 ?  25  GLU   B HA   1 
ATOM   4418 H  HB2  . GLU   B 1 25  ? 54.122 -26.672 -11.745 1.00 22.84 ?  25  GLU   B HB2  1 
ATOM   4419 H  HB3  . GLU   B 1 25  ? 54.950 -26.101 -12.977 1.00 22.84 ?  25  GLU   B HB3  1 
ATOM   4420 H  HG2  . GLU   B 1 25  ? 55.956 -26.685 -10.419 1.00 29.58 ?  25  GLU   B HG2  1 
ATOM   4421 H  HG3  . GLU   B 1 25  ? 56.420 -27.338 -11.793 1.00 29.58 ?  25  GLU   B HG3  1 
ATOM   4422 N  N    . GLU   B 1 26  ? 52.087 -24.418 -12.180 1.00 13.74 ?  26  GLU   B N    1 
ATOM   4423 C  CA   . GLU   B 1 26  ? 50.958 -23.888 -12.937 1.00 14.17 ?  26  GLU   B CA   1 
ATOM   4424 C  C    . GLU   B 1 26  ? 50.912 -22.369 -12.859 1.00 13.39 ?  26  GLU   B C    1 
ATOM   4425 O  O    . GLU   B 1 26  ? 50.719 -21.691 -13.873 1.00 14.63 ?  26  GLU   B O    1 
ATOM   4426 C  CB   . GLU   B 1 26  ? 49.649 -24.469 -12.401 1.00 16.20 ?  26  GLU   B CB   1 
ATOM   4427 C  CG   . GLU   B 1 26  ? 49.174 -25.733 -13.089 1.00 20.03 ?  26  GLU   B CG   1 
ATOM   4428 C  CD   . GLU   B 1 26  ? 48.934 -25.567 -14.589 1.00 21.56 ?  26  GLU   B CD   1 
ATOM   4429 O  OE1  . GLU   B 1 26  ? 47.962 -24.909 -15.016 1.00 21.87 ?  26  GLU   B OE1  1 
ATOM   4430 O  OE2  . GLU   B 1 26  ? 49.731 -26.124 -15.350 1.00 23.50 -1 26  GLU   B OE2  1 
ATOM   4431 H  H    . GLU   B 1 26  ? 51.865 -24.947 -11.532 1.00 16.47 ?  26  GLU   B H    1 
ATOM   4432 H  HA   . GLU   B 1 26  ? 51.050 -24.144 -13.864 1.00 16.98 ?  26  GLU   B HA   1 
ATOM   4433 H  HB2  . GLU   B 1 26  ? 49.764 -24.675 -11.457 1.00 19.42 ?  26  GLU   B HB2  1 
ATOM   4434 H  HB3  . GLU   B 1 26  ? 48.953 -23.800 -12.499 1.00 19.42 ?  26  GLU   B HB3  1 
ATOM   4435 H  HG2  . GLU   B 1 26  ? 49.855 -26.406 -12.983 1.00 24.02 ?  26  GLU   B HG2  1 
ATOM   4436 H  HG3  . GLU   B 1 26  ? 48.345 -26.018 -12.673 1.00 24.02 ?  26  GLU   B HG3  1 
ATOM   4437 N  N    . ALA   B 1 27  ? 51.054 -21.817 -11.655 1.00 12.53 ?  27  ALA   B N    1 
ATOM   4438 C  CA   . ALA   B 1 27  ? 51.011 -20.368 -11.508 1.00 12.85 ?  27  ALA   B CA   1 
ATOM   4439 C  C    . ALA   B 1 27  ? 52.084 -19.698 -12.360 1.00 13.72 ?  27  ALA   B C    1 
ATOM   4440 O  O    . ALA   B 1 27  ? 51.824 -18.689 -13.033 1.00 14.41 ?  27  ALA   B O    1 
ATOM   4441 C  CB   . ALA   B 1 27  ? 51.159 -19.990 -10.035 1.00 12.83 ?  27  ALA   B CB   1 
ATOM   4442 H  H    . ALA   B 1 27  ? 51.169 -22.252 -10.919 1.00 15.02 ?  27  ALA   B H    1 
ATOM   4443 H  HA   . ALA   B 1 27  ? 50.150 -20.046 -11.811 1.00 15.40 ?  27  ALA   B HA   1 
ATOM   4444 H  HB1  . ALA   B 1 27  ? 51.121 -19.024 -9.951  1.00 15.38 ?  27  ALA   B HB1  1 
ATOM   4445 H  HB2  . ALA   B 1 27  ? 50.429 -20.391 -9.533  1.00 15.38 ?  27  ALA   B HB2  1 
ATOM   4446 H  HB3  . ALA   B 1 27  ? 52.006 -20.319 -9.705  1.00 15.38 ?  27  ALA   B HB3  1 
ATOM   4447 N  N    . LYS   B 1 28  ? 53.296 -20.251 -12.357 1.00 15.30 ?  28  LYS   B N    1 
ATOM   4448 C  CA   . LYS   B 1 28  ? 54.372 -19.639 -13.130 1.00 17.29 ?  28  LYS   B CA   1 
ATOM   4449 C  C    . LYS   B 1 28  ? 54.111 -19.719 -14.630 1.00 18.08 ?  28  LYS   B C    1 
ATOM   4450 O  O    . LYS   B 1 28  ? 54.511 -18.815 -15.375 1.00 19.32 ?  28  LYS   B O    1 
ATOM   4451 C  CB   . LYS   B 1 28  ? 55.725 -20.247 -12.746 1.00 20.12 ?  28  LYS   B CB   1 
ATOM   4452 C  CG   . LYS   B 1 28  ? 56.129 -19.914 -11.313 1.00 23.28 ?  28  LYS   B CG   1 
ATOM   4453 C  CD   . LYS   B 1 28  ? 57.559 -20.312 -10.983 1.00 27.56 ?  28  LYS   B CD   1 
ATOM   4454 C  CE   . LYS   B 1 28  ? 57.678 -21.787 -10.695 1.00 30.80 ?  28  LYS   B CE   1 
ATOM   4455 N  NZ   . LYS   B 1 28  ? 59.035 -22.128 -10.187 1.00 31.93 ?  28  LYS   B NZ   1 
ATOM   4456 H  H    . LYS   B 1 28  ? 53.520 -20.960 -11.922 1.00 18.34 ?  28  LYS   B H    1 
ATOM   4457 H  HA   . LYS   B 1 28  ? 54.412 -18.698 -12.902 1.00 20.73 ?  28  LYS   B HA   1 
ATOM   4458 H  HB2  . LYS   B 1 28  ? 55.678 -21.212 -12.823 1.00 24.13 ?  28  LYS   B HB2  1 
ATOM   4459 H  HB3  . LYS   B 1 28  ? 56.413 -19.899 -13.336 1.00 24.13 ?  28  LYS   B HB3  1 
ATOM   4460 H  HG2  . LYS   B 1 28  ? 56.043 -18.956 -11.181 1.00 27.92 ?  28  LYS   B HG2  1 
ATOM   4461 H  HG3  . LYS   B 1 28  ? 55.538 -20.385 -10.706 1.00 27.92 ?  28  LYS   B HG3  1 
ATOM   4462 H  HD2  . LYS   B 1 28  ? 58.129 -20.100 -11.739 1.00 33.06 ?  28  LYS   B HD2  1 
ATOM   4463 H  HD3  . LYS   B 1 28  ? 57.849 -19.821 -10.198 1.00 33.06 ?  28  LYS   B HD3  1 
ATOM   4464 H  HE2  . LYS   B 1 28  ? 57.027 -22.034 -10.019 1.00 36.94 ?  28  LYS   B HE2  1 
ATOM   4465 H  HE3  . LYS   B 1 28  ? 57.521 -22.286 -11.511 1.00 36.94 ?  28  LYS   B HE3  1 
ATOM   4466 H  HZ1  . LYS   B 1 28  ? 59.088 -23.000 -10.022 1.00 38.30 ?  28  LYS   B HZ1  1 
ATOM   4467 H  HZ2  . LYS   B 1 28  ? 59.649 -21.909 -10.793 1.00 38.30 ?  28  LYS   B HZ2  1 
ATOM   4468 H  HZ3  . LYS   B 1 28  ? 59.199 -21.680 -9.435  1.00 38.30 ?  28  LYS   B HZ3  1 
ATOM   4469 N  N    . LYS   B 1 29  ? 53.416 -20.764 -15.086 1.00 18.92 ?  29  LYS   B N    1 
ATOM   4470 C  CA   . LYS   B 1 29  ? 53.129 -20.907 -16.511 1.00 21.51 ?  29  LYS   B CA   1 
ATOM   4471 C  C    . LYS   B 1 29  ? 51.894 -20.116 -16.935 1.00 20.76 ?  29  LYS   B C    1 
ATOM   4472 O  O    . LYS   B 1 29  ? 51.905 -19.472 -17.990 1.00 21.96 ?  29  LYS   B O    1 
ATOM   4473 C  CB   . LYS   B 1 29  ? 52.959 -22.386 -16.864 1.00 25.60 ?  29  LYS   B CB   1 
ATOM   4474 C  CG   . LYS   B 1 29  ? 52.888 -22.655 -18.359 1.00 29.59 ?  29  LYS   B CG   1 
ATOM   4475 C  CD   . LYS   B 1 29  ? 53.122 -24.125 -18.678 1.00 32.82 ?  29  LYS   B CD   1 
ATOM   4476 C  CE   . LYS   B 1 29  ? 51.988 -25.000 -18.174 1.00 34.99 ?  29  LYS   B CE   1 
ATOM   4477 N  NZ   . LYS   B 1 29  ? 52.236 -26.444 -18.453 1.00 36.24 ?  29  LYS   B NZ   1 
ATOM   4478 H  H    . LYS   B 1 29  ? 53.104 -21.400 -14.592 1.00 22.69 ?  29  LYS   B H    1 
ATOM   4479 H  HA   . LYS   B 1 29  ? 53.877 -20.566 -17.013 1.00 25.80 ?  29  LYS   B HA   1 
ATOM   4480 H  HB2  . LYS   B 1 29  ? 53.718 -22.878 -16.512 1.00 30.71 ?  29  LYS   B HB2  1 
ATOM   4481 H  HB3  . LYS   B 1 29  ? 52.140 -22.714 -16.465 1.00 30.71 ?  29  LYS   B HB3  1 
ATOM   4482 H  HG2  . LYS   B 1 29  ? 52.008 -22.409 -18.686 1.00 35.49 ?  29  LYS   B HG2  1 
ATOM   4483 H  HG3  . LYS   B 1 29  ? 53.570 -22.133 -18.810 1.00 35.49 ?  29  LYS   B HG3  1 
ATOM   4484 H  HD2  . LYS   B 1 29  ? 53.186 -24.237 -19.640 1.00 39.36 ?  29  LYS   B HD2  1 
ATOM   4485 H  HD3  . LYS   B 1 29  ? 53.944 -24.419 -18.253 1.00 39.36 ?  29  LYS   B HD3  1 
ATOM   4486 H  HE2  . LYS   B 1 29  ? 51.900 -24.889 -17.215 1.00 41.98 ?  29  LYS   B HE2  1 
ATOM   4487 H  HE3  . LYS   B 1 29  ? 51.165 -24.742 -18.618 1.00 41.98 ?  29  LYS   B HE3  1 
ATOM   4488 H  HZ1  . LYS   B 1 29  ? 51.558 -26.934 -18.148 1.00 43.47 ?  29  LYS   B HZ1  1 
ATOM   4489 H  HZ2  . LYS   B 1 29  ? 52.316 -26.576 -19.330 1.00 43.47 ?  29  LYS   B HZ2  1 
ATOM   4490 H  HZ3  . LYS   B 1 29  ? 52.986 -26.708 -18.052 1.00 43.47 ?  29  LYS   B HZ3  1 
ATOM   4491 N  N    . VAL   B 1 30  ? 50.827 -20.161 -16.131 1.00 19.02 ?  30  VAL   B N    1 
ATOM   4492 C  CA   . VAL   B 1 30  ? 49.532 -19.579 -16.500 1.00 19.08 ?  30  VAL   B CA   1 
ATOM   4493 C  C    . VAL   B 1 30  ? 49.528 -18.067 -16.345 1.00 18.12 ?  30  VAL   B C    1 
ATOM   4494 O  O    . VAL   B 1 30  ? 48.781 -17.361 -17.043 1.00 19.09 ?  30  VAL   B O    1 
ATOM   4495 C  CB   . VAL   B 1 30  ? 48.435 -20.207 -15.617 1.00 20.36 ?  30  VAL   B CB   1 
ATOM   4496 C  CG1  . VAL   B 1 30  ? 47.141 -19.400 -15.675 1.00 20.76 ?  30  VAL   B CG1  1 
ATOM   4497 C  CG2  . VAL   B 1 30  ? 48.198 -21.657 -16.009 1.00 21.25 ?  30  VAL   B CG2  1 
ATOM   4498 H  H    . VAL   B 1 30  ? 50.819 -20.545 -15.353 1.00 22.81 ?  30  VAL   B H    1 
ATOM   4499 H  HA   . VAL   B 1 30  ? 49.333 -19.801 -17.422 1.00 22.88 ?  30  VAL   B HA   1 
ATOM   4500 H  HB   . VAL   B 1 30  ? 48.736 -20.206 -14.695 1.00 24.41 ?  30  VAL   B HB   1 
ATOM   4501 H  HG11 . VAL   B 1 30  ? 46.404 -19.983 -15.431 1.00 24.89 ?  30  VAL   B HG11 1 
ATOM   4502 H  HG12 . VAL   B 1 30  ? 47.194 -18.664 -15.047 1.00 24.89 ?  30  VAL   B HG12 1 
ATOM   4503 H  HG13 . VAL   B 1 30  ? 47.007 -19.073 -16.573 1.00 24.89 ?  30  VAL   B HG13 1 
ATOM   4504 H  HG21 . VAL   B 1 30  ? 47.511 -22.034 -15.431 1.00 25.49 ?  30  VAL   B HG21 1 
ATOM   4505 H  HG22 . VAL   B 1 30  ? 47.899 -21.690 -16.933 1.00 25.49 ?  30  VAL   B HG22 1 
ATOM   4506 H  HG23 . VAL   B 1 30  ? 49.022 -22.152 -15.908 1.00 25.49 ?  30  VAL   B HG23 1 
ATOM   4507 N  N    . LYS   B 1 31  ? 50.312 -17.564 -15.408 1.00 17.68 ?  31  LYS   B N    1 
ATOM   4508 C  CA   . LYS   B 1 31  ? 50.337 -16.157 -15.043 1.00 18.08 ?  31  LYS   B CA   1 
ATOM   4509 C  C    . LYS   B 1 31  ? 48.935 -15.684 -14.658 1.00 15.76 ?  31  LYS   B C    1 
ATOM   4510 O  O    . LYS   B 1 31  ? 48.394 -14.764 -15.283 1.00 16.88 ?  31  LYS   B O    1 
ATOM   4511 C  CB   . LYS   B 1 31  ? 50.975 -15.340 -16.173 1.00 21.40 ?  31  LYS   B CB   1 
ATOM   4512 C  CG   . LYS   B 1 31  ? 52.403 -15.797 -16.495 1.00 24.58 ?  31  LYS   B CG   1 
ATOM   4513 C  CD   . LYS   B 1 31  ? 52.996 -15.031 -17.663 1.00 27.74 ?  31  LYS   B CD   1 
ATOM   4514 C  CE   . LYS   B 1 31  ? 54.481 -15.290 -17.809 1.00 30.03 ?  31  LYS   B CE   1 
ATOM   4515 N  NZ   . LYS   B 1 31  ? 55.208 -14.889 -16.576 1.00 31.42 ?  31  LYS   B NZ   1 
ATOM   4516 H  H    . LYS   B 1 31  ? 50.862 -18.048 -14.960 1.00 21.20 ?  31  LYS   B H    1 
ATOM   4517 H  HA   . LYS   B 1 31  ? 50.892 -16.069 -14.266 1.00 21.68 ?  31  LYS   B HA   1 
ATOM   4518 H  HB2  . LYS   B 1 31  ? 50.445 -15.436 -16.981 1.00 25.66 ?  31  LYS   B HB2  1 
ATOM   4519 H  HB3  . LYS   B 1 31  ? 51.013 -14.413 -15.904 1.00 25.66 ?  31  LYS   B HB3  1 
ATOM   4520 H  HG2  . LYS   B 1 31  ? 52.956 -15.655 -15.711 1.00 29.47 ?  31  LYS   B HG2  1 
ATOM   4521 H  HG3  . LYS   B 1 31  ? 52.389 -16.743 -16.723 1.00 29.47 ?  31  LYS   B HG3  1 
ATOM   4522 H  HD2  . LYS   B 1 31  ? 52.553 -15.313 -18.477 1.00 33.28 ?  31  LYS   B HD2  1 
ATOM   4523 H  HD3  . LYS   B 1 31  ? 52.861 -14.085 -17.514 1.00 33.28 ?  31  LYS   B HD3  1 
ATOM   4524 H  HE2  . LYS   B 1 31  ? 54.636 -16.237 -17.962 1.00 36.01 ?  31  LYS   B HE2  1 
ATOM   4525 H  HE3  . LYS   B 1 31  ? 54.828 -14.769 -18.551 1.00 36.01 ?  31  LYS   B HE3  1 
ATOM   4526 H  HZ1  . LYS   B 1 31  ? 56.085 -14.905 -16.720 1.00 37.68 ?  31  LYS   B HZ1  1 
ATOM   4527 H  HZ2  . LYS   B 1 31  ? 54.967 -14.067 -16.337 1.00 37.68 ?  31  LYS   B HZ2  1 
ATOM   4528 H  HZ3  . LYS   B 1 31  ? 55.014 -15.451 -15.913 1.00 37.68 ?  31  LYS   B HZ3  1 
ATOM   4529 N  N    . PRO   B 1 32  ? 48.325 -16.280 -13.627 1.00 13.52 ?  32  PRO   B N    1 
ATOM   4530 C  CA   . PRO   B 1 32  ? 46.948 -15.924 -13.268 1.00 12.66 ?  32  PRO   B CA   1 
ATOM   4531 C  C    . PRO   B 1 32  ? 46.870 -14.580 -12.563 1.00 13.05 ?  32  PRO   B C    1 
ATOM   4532 O  O    . PRO   B 1 32  ? 47.794 -14.155 -11.862 1.00 14.20 ?  32  PRO   B O    1 
ATOM   4533 C  CB   . PRO   B 1 32  ? 46.550 -17.043 -12.297 1.00 12.83 ?  32  PRO   B CB   1 
ATOM   4534 C  CG   . PRO   B 1 32  ? 47.857 -17.381 -11.617 1.00 13.12 ?  32  PRO   B CG   1 
ATOM   4535 C  CD   . PRO   B 1 32  ? 48.902 -17.266 -12.690 1.00 13.67 ?  32  PRO   B CD   1 
ATOM   4536 H  HA   . PRO   B 1 32  ? 46.367 -15.936 -14.048 1.00 15.17 ?  32  PRO   B HA   1 
ATOM   4537 H  HB2  . PRO   B 1 32  ? 45.898 -16.709 -11.658 1.00 15.38 ?  32  PRO   B HB2  1 
ATOM   4538 H  HB3  . PRO   B 1 32  ? 46.203 -17.802 -12.787 1.00 15.38 ?  32  PRO   B HB3  1 
ATOM   4539 H  HG2  . PRO   B 1 32  ? 48.032 -16.742 -10.903 1.00 15.73 ?  32  PRO   B HG2  1 
ATOM   4540 H  HG3  . PRO   B 1 32  ? 47.826 -18.283 -11.267 1.00 15.73 ?  32  PRO   B HG3  1 
ATOM   4541 H  HD2  . PRO   B 1 32  ? 49.729 -16.928 -12.317 1.00 16.39 ?  32  PRO   B HD2  1 
ATOM   4542 H  HD3  . PRO   B 1 32  ? 49.023 -18.118 -13.126 1.00 16.39 ?  32  PRO   B HD3  1 
ATOM   4543 N  N    . THR   B 1 33  ? 45.723 -13.920 -12.738 1.00 12.67 ?  33  THR   B N    1 
ATOM   4544 C  CA   . THR   B 1 33  ? 45.424 -12.747 -11.925 1.00 12.78 ?  33  THR   B CA   1 
ATOM   4545 C  C    . THR   B 1 33  ? 45.381 -13.105 -10.445 1.00 12.47 ?  33  THR   B C    1 
ATOM   4546 O  O    . THR   B 1 33  ? 45.854 -12.329 -9.602  1.00 13.63 ?  33  THR   B O    1 
ATOM   4547 C  CB   . THR   B 1 33  ? 44.106 -12.113 -12.371 1.00 13.40 ?  33  THR   B CB   1 
ATOM   4548 O  OG1  . THR   B 1 33  ? 44.153 -11.848 -13.777 1.00 13.50 ?  33  THR   B OG1  1 
ATOM   4549 C  CG2  . THR   B 1 33  ? 43.843 -10.821 -11.611 1.00 14.80 ?  33  THR   B CG2  1 
ATOM   4550 H  H    . THR   B 1 33  ? 45.109 -14.127 -13.312 1.00 15.19 ?  33  THR   B H    1 
ATOM   4551 H  HA   . THR   B 1 33  ? 46.123 -12.089 -12.051 1.00 15.32 ?  33  THR   B HA   1 
ATOM   4552 H  HB   . THR   B 1 33  ? 43.372 -12.727 -12.186 1.00 16.06 ?  33  THR   B HB   1 
ATOM   4553 H  HG1  . THR   B 1 33  ? 43.430 -11.485 -14.025 1.00 16.18 ?  33  THR   B HG1  1 
ATOM   4554 H  HG21 . THR   B 1 33  ? 43.087 -10.356 -11.997 1.00 17.74 ?  33  THR   B HG21 1 
ATOM   4555 H  HG22 . THR   B 1 33  ? 43.650 -11.015 -10.678 1.00 17.74 ?  33  THR   B HG22 1 
ATOM   4556 H  HG23 . THR   B 1 33  ? 44.625 -10.248 -11.657 1.00 17.74 ?  33  THR   B HG23 1 
ATOM   4557 N  N    . VAL   B 1 34  ? 44.829 -14.275 -10.106 1.00 11.76 ?  34  VAL   B N    1 
ATOM   4558 C  CA   . VAL   B 1 34  ? 44.639 -14.671 -8.715  1.00 10.97 ?  34  VAL   B CA   1 
ATOM   4559 C  C    . VAL   B 1 34  ? 45.066 -16.118 -8.552  1.00 10.36 ?  34  VAL   B C    1 
ATOM   4560 O  O    . VAL   B 1 34  ? 44.543 -17.004 -9.237  1.00 11.10 ?  34  VAL   B O    1 
ATOM   4561 C  CB   . VAL   B 1 34  ? 43.170 -14.532 -8.266  1.00 12.21 ?  34  VAL   B CB   1 
ATOM   4562 C  CG1  . VAL   B 1 34  ? 43.009 -14.988 -6.822  1.00 12.44 ?  34  VAL   B CG1  1 
ATOM   4563 C  CG2  . VAL   B 1 34  ? 42.670 -13.107 -8.452  1.00 13.23 ?  34  VAL   B CG2  1 
ATOM   4564 H  H    . VAL   B 1 34  ? 44.560 -14.867 -10.675 1.00 14.10 ?  34  VAL   B H    1 
ATOM   4565 H  HA   . VAL   B 1 34  ? 45.195 -14.118 -8.141  1.00 13.15 ?  34  VAL   B HA   1 
ATOM   4566 H  HB   . VAL   B 1 34  ? 42.624 -15.109 -8.822  1.00 14.64 ?  34  VAL   B HB   1 
ATOM   4567 H  HG11 . VAL   B 1 34  ? 42.156 -14.674 -6.484  1.00 14.91 ?  34  VAL   B HG11 1 
ATOM   4568 H  HG12 . VAL   B 1 34  ? 43.033 -15.961 -6.789  1.00 14.91 ?  34  VAL   B HG12 1 
ATOM   4569 H  HG13 . VAL   B 1 34  ? 43.730 -14.623 -6.288  1.00 14.91 ?  34  VAL   B HG13 1 
ATOM   4570 H  HG21 . VAL   B 1 34  ? 41.752 -13.050 -8.140  1.00 15.86 ?  34  VAL   B HG21 1 
ATOM   4571 H  HG22 . VAL   B 1 34  ? 43.231 -12.503 -7.944  1.00 15.86 ?  34  VAL   B HG22 1 
ATOM   4572 H  HG23 . VAL   B 1 34  ? 42.708 -12.877 -9.397  1.00 15.86 ?  34  VAL   B HG23 1 
ATOM   4573 N  N    . VAL   B 1 35  ? 45.973 -16.368 -7.609  1.00 9.88  ?  35  VAL   B N    1 
ATOM   4574 C  CA   . VAL   B 1 35  ? 46.208 -17.712 -7.089  1.00 9.72  ?  35  VAL   B CA   1 
ATOM   4575 C  C    . VAL   B 1 35  ? 45.671 -17.767 -5.667  1.00 9.25  ?  35  VAL   B C    1 
ATOM   4576 O  O    . VAL   B 1 35  ? 45.888 -16.842 -4.877  1.00 9.88  ?  35  VAL   B O    1 
ATOM   4577 C  CB   . VAL   B 1 35  ? 47.690 -18.134 -7.178  1.00 10.22 ?  35  VAL   B CB   1 
ATOM   4578 C  CG1  . VAL   B 1 35  ? 48.591 -17.292 -6.263  1.00 11.28 ?  35  VAL   B CG1  1 
ATOM   4579 C  CG2  . VAL   B 1 35  ? 47.838 -19.626 -6.859  1.00 11.01 ?  35  VAL   B CG2  1 
ATOM   4580 H  H    . VAL   B 1 35  ? 46.472 -15.765 -7.250  1.00 11.83 ?  35  VAL   B H    1 
ATOM   4581 H  HA   . VAL   B 1 35  ? 45.691 -18.340 -7.617  1.00 11.64 ?  35  VAL   B HA   1 
ATOM   4582 H  HB   . VAL   B 1 35  ? 47.991 -18.006 -8.092  1.00 12.25 ?  35  VAL   B HB   1 
ATOM   4583 H  HG11 . VAL   B 1 35  ? 49.512 -17.518 -6.443  1.00 13.51 ?  35  VAL   B HG11 1 
ATOM   4584 H  HG12 . VAL   B 1 35  ? 48.426 -16.358 -6.445  1.00 13.51 ?  35  VAL   B HG12 1 
ATOM   4585 H  HG13 . VAL   B 1 35  ? 48.369 -17.497 -5.339  1.00 13.51 ?  35  VAL   B HG13 1 
ATOM   4586 H  HG21 . VAL   B 1 35  ? 48.762 -19.889 -6.967  1.00 13.19 ?  35  VAL   B HG21 1 
ATOM   4587 H  HG22 . VAL   B 1 35  ? 47.552 -19.788 -5.943  1.00 13.19 ?  35  VAL   B HG22 1 
ATOM   4588 H  HG23 . VAL   B 1 35  ? 47.276 -20.144 -7.467  1.00 13.19 ?  35  VAL   B HG23 1 
ATOM   4589 N  N    . VAL   B 1 36  ? 44.943 -18.840 -5.351  1.00 9.46  ?  36  VAL   B N    1 
ATOM   4590 C  CA   . VAL   B 1 36  ? 44.402 -19.047 -4.018  1.00 9.07  ?  36  VAL   B CA   1 
ATOM   4591 C  C    . VAL   B 1 36  ? 45.414 -19.808 -3.166  1.00 8.90  ?  36  VAL   B C    1 
ATOM   4592 O  O    . VAL   B 1 36  ? 45.958 -20.839 -3.588  1.00 10.09 ?  36  VAL   B O    1 
ATOM   4593 C  CB   . VAL   B 1 36  ? 43.066 -19.808 -4.092  1.00 9.59  ?  36  VAL   B CB   1 
ATOM   4594 C  CG1  . VAL   B 1 36  ? 42.560 -20.166 -2.708  1.00 10.18 ?  36  VAL   B CG1  1 
ATOM   4595 C  CG2  . VAL   B 1 36  ? 42.035 -18.976 -4.838  1.00 10.09 ?  36  VAL   B CG2  1 
ATOM   4596 H  H    . VAL   B 1 36  ? 44.751 -19.472 -5.901  1.00 11.33 ?  36  VAL   B H    1 
ATOM   4597 H  HA   . VAL   B 1 36  ? 44.235 -18.189 -3.598  1.00 10.86 ?  36  VAL   B HA   1 
ATOM   4598 H  HB   . VAL   B 1 36  ? 43.196 -20.632 -4.582  1.00 11.49 ?  36  VAL   B HB   1 
ATOM   4599 H  HG11 . VAL   B 1 36  ? 41.620 -20.405 -2.766  1.00 12.20 ?  36  VAL   B HG11 1 
ATOM   4600 H  HG12 . VAL   B 1 36  ? 43.069 -20.910 -2.360  1.00 12.20 ?  36  VAL   B HG12 1 
ATOM   4601 H  HG13 . VAL   B 1 36  ? 42.661 -19.392 -2.125  1.00 12.20 ?  36  VAL   B HG13 1 
ATOM   4602 H  HG21 . VAL   B 1 36  ? 41.191 -19.452 -4.856  1.00 12.10 ?  36  VAL   B HG21 1 
ATOM   4603 H  HG22 . VAL   B 1 36  ? 41.924 -18.124 -4.383  1.00 12.10 ?  36  VAL   B HG22 1 
ATOM   4604 H  HG23 . VAL   B 1 36  ? 42.347 -18.823 -5.746  1.00 12.10 ?  36  VAL   B HG23 1 
ATOM   4605 N  N    . ASN   B 1 37  ? 45.631 -19.318 -1.951  1.00 9.02  ?  37  ASN   B N    1 
ATOM   4606 C  CA   . ASN   B 1 37  ? 46.388 -20.039 -0.943  1.00 9.59  ?  37  ASN   B CA   1 
ATOM   4607 C  C    . ASN   B 1 37  ? 45.440 -20.712 0.041   1.00 9.69  ?  37  ASN   B C    1 
ATOM   4608 O  O    . ASN   B 1 37  ? 44.427 -20.134 0.451   1.00 10.19 ?  37  ASN   B O    1 
ATOM   4609 C  CB   . ASN   B 1 37  ? 47.316 -19.093 -0.183  1.00 9.48  ?  37  ASN   B CB   1 
ATOM   4610 C  CG   . ASN   B 1 37  ? 48.169 -19.810 0.825   1.00 10.10 ?  37  ASN   B CG   1 
ATOM   4611 O  OD1  . ASN   B 1 37  ? 48.509 -20.990 0.645   1.00 10.90 ?  37  ASN   B OD1  1 
ATOM   4612 N  ND2  . ASN   B 1 37  ? 48.521 -19.107 1.902   1.00 10.21 ?  37  ASN   B ND2  1 
ATOM   4613 H  H    . ASN   B 1 37  ? 45.350 -18.548 -1.681  1.00 10.81 ?  37  ASN   B H    1 
ATOM   4614 H  HA   . ASN   B 1 37  ? 46.921 -20.730 -1.363  1.00 11.49 ?  37  ASN   B HA   1 
ATOM   4615 H  HB2  . ASN   B 1 37  ? 47.910 -18.665 -0.815  1.00 11.36 ?  37  ASN   B HB2  1 
ATOM   4616 H  HB3  . ASN   B 1 37  ? 46.788 -18.435 0.288   1.00 11.36 ?  37  ASN   B HB3  1 
ATOM   4617 H  HD21 . ASN   B 1 37  ? 49.015 -19.469 2.510   1.00 12.24 ?  37  ASN   B HD21 1 
ATOM   4618 H  HD22 . ASN   B 1 37  ? 48.271 -18.297 1.990   1.00 12.24 ?  37  ASN   B HD22 1 
ATOM   4619 N  N    . ALA   B 1 38  ? 45.790 -21.949 0.410   1.00 9.66  ?  38  ALA   B N    1 
ATOM   4620 C  CA   . ALA   B 1 38  ? 45.141 -22.692 1.492   1.00 10.24 ?  38  ALA   B CA   1 
ATOM   4621 C  C    . ALA   B 1 38  ? 45.726 -22.204 2.817   1.00 9.98  ?  38  ALA   B C    1 
ATOM   4622 O  O    . ALA   B 1 38  ? 46.630 -22.810 3.402   1.00 10.84 ?  38  ALA   B O    1 
ATOM   4623 C  CB   . ALA   B 1 38  ? 45.362 -24.187 1.302   1.00 11.35 ?  38  ALA   B CB   1 
ATOM   4624 H  H    . ALA   B 1 38  ? 46.428 -22.392 0.042   1.00 11.58 ?  38  ALA   B H    1 
ATOM   4625 H  HA   . ALA   B 1 38  ? 44.186 -22.518 1.489   1.00 12.27 ?  38  ALA   B HA   1 
ATOM   4626 H  HB1  . ALA   B 1 38  ? 44.919 -24.670 2.028   1.00 13.60 ?  38  ALA   B HB1  1 
ATOM   4627 H  HB2  . ALA   B 1 38  ? 44.975 -24.462 0.454   1.00 13.60 ?  38  ALA   B HB2  1 
ATOM   4628 H  HB3  . ALA   B 1 38  ? 46.308 -24.378 1.314   1.00 13.60 ?  38  ALA   B HB3  1 
ATOM   4629 N  N    . ALA   B 1 39  ? 45.211 -21.062 3.277   1.00 9.89  ?  39  ALA   B N    1 
ATOM   4630 C  CA   . ALA   B 1 39  ? 45.761 -20.325 4.402   1.00 10.17 ?  39  ALA   B CA   1 
ATOM   4631 C  C    . ALA   B 1 39  ? 45.144 -20.773 5.725   1.00 10.00 ?  39  ALA   B C    1 
ATOM   4632 O  O    . ALA   B 1 39  ? 44.115 -21.452 5.772   1.00 11.33 ?  39  ALA   B O    1 
ATOM   4633 C  CB   . ALA   B 1 39  ? 45.508 -18.826 4.208   1.00 10.90 ?  39  ALA   B CB   1 
ATOM   4634 H  H    . ALA   B 1 39  ? 44.518 -20.689 2.930   1.00 11.85 ?  39  ALA   B H    1 
ATOM   4635 H  HA   . ALA   B 1 39  ? 46.716 -20.470 4.445   1.00 12.19 ?  39  ALA   B HA   1 
ATOM   4636 H  HB1  . ALA   B 1 39  ? 45.876 -18.340 4.962   1.00 13.07 ?  39  ALA   B HB1  1 
ATOM   4637 H  HB2  . ALA   B 1 39  ? 45.939 -18.534 3.387   1.00 13.07 ?  39  ALA   B HB2  1 
ATOM   4638 H  HB3  . ALA   B 1 39  ? 44.551 -18.667 4.149   1.00 13.07 ?  39  ALA   B HB3  1 
ATOM   4639 N  N    . ASN   B 1 40  ? 45.784 -20.356 6.812   1.00 10.74 ?  40  ASN   B N    1 
ATOM   4640 C  CA   . ASN   B 1 40  ? 45.224 -20.404 8.152   1.00 11.54 ?  40  ASN   B CA   1 
ATOM   4641 C  C    . ASN   B 1 40  ? 45.044 -18.978 8.677   1.00 11.53 ?  40  ASN   B C    1 
ATOM   4642 O  O    . ASN   B 1 40  ? 45.448 -17.997 8.043   1.00 11.31 ?  40  ASN   B O    1 
ATOM   4643 C  CB   . ASN   B 1 40  ? 46.076 -21.280 9.087   1.00 12.46 ?  40  ASN   B CB   1 
ATOM   4644 C  CG   . ASN   B 1 40  ? 47.531 -20.872 9.112   1.00 13.83 ?  40  ASN   B CG   1 
ATOM   4645 O  OD1  . ASN   B 1 40  ? 47.848 -19.690 9.172   1.00 15.61 ?  40  ASN   B OD1  1 
ATOM   4646 N  ND2  . ASN   B 1 40  ? 48.424 -21.847 9.072   1.00 13.67 ?  40  ASN   B ND2  1 
ATOM   4647 H  H    . ASN   B 1 40  ? 46.582 -20.033 6.792   1.00 12.87 ?  40  ASN   B H    1 
ATOM   4648 H  HA   . ASN   B 1 40  ? 44.342 -20.800 8.103   1.00 13.84 ?  40  ASN   B HA   1 
ATOM   4649 H  HB2  . ASN   B 1 40  ? 45.724 -21.206 9.989   1.00 14.94 ?  40  ASN   B HB2  1 
ATOM   4650 H  HB3  . ASN   B 1 40  ? 46.022 -22.199 8.784   1.00 14.94 ?  40  ASN   B HB3  1 
ATOM   4651 H  HD21 . ASN   B 1 40  ? 49.262 -21.662 9.086   1.00 16.38 ?  40  ASN   B HD21 1 
ATOM   4652 H  HD22 . ASN   B 1 40  ? 48.163 -22.666 9.029   1.00 16.38 ?  40  ASN   B HD22 1 
ATOM   4653 N  N    . VAL   B 1 41  ? 44.396 -18.857 9.837   1.00 11.80 ?  41  VAL   B N    1 
ATOM   4654 C  CA   . VAL   B 1 41  ? 43.935 -17.540 10.285  1.00 12.33 ?  41  VAL   B CA   1 
ATOM   4655 C  C    . VAL   B 1 41  ? 45.083 -16.585 10.581  1.00 12.33 ?  41  VAL   B C    1 
ATOM   4656 O  O    . VAL   B 1 41  ? 44.903 -15.365 10.494  1.00 12.68 ?  41  VAL   B O    1 
ATOM   4657 C  CB   . VAL   B 1 41  ? 42.958 -17.619 11.474  1.00 14.13 ?  41  VAL   B CB   1 
ATOM   4658 C  CG1  . VAL   B 1 41  ? 41.658 -18.294 11.063  1.00 14.51 ?  41  VAL   B CG1  1 
ATOM   4659 C  CG2  . VAL   B 1 41  ? 43.605 -18.309 12.665  1.00 15.16 ?  41  VAL   B CG2  1 
ATOM   4660 H  H    . VAL   B 1 41  ? 44.217 -19.503 10.369  1.00 14.15 ?  41  VAL   B H    1 
ATOM   4661 H  HA   . VAL   B 1 41  ? 43.439 -17.145 9.554   1.00 14.78 ?  41  VAL   B HA   1 
ATOM   4662 H  HB   . VAL   B 1 41  ? 42.736 -16.715 11.749  1.00 16.94 ?  41  VAL   B HB   1 
ATOM   4663 H  HG11 . VAL   B 1 41  ? 41.050 -18.295 11.819  1.00 17.39 ?  41  VAL   B HG11 1 
ATOM   4664 H  HG12 . VAL   B 1 41  ? 41.267 -17.802 10.324  1.00 17.39 ?  41  VAL   B HG12 1 
ATOM   4665 H  HG13 . VAL   B 1 41  ? 41.850 -19.205 10.791  1.00 17.39 ?  41  VAL   B HG13 1 
ATOM   4666 H  HG21 . VAL   B 1 41  ? 42.970 -18.339 13.395  1.00 18.17 ?  41  VAL   B HG21 1 
ATOM   4667 H  HG22 . VAL   B 1 41  ? 43.858 -19.210 12.408  1.00 18.17 ?  41  VAL   B HG22 1 
ATOM   4668 H  HG23 . VAL   B 1 41  ? 44.392 -17.808 12.929  1.00 18.17 ?  41  VAL   B HG23 1 
ATOM   4669 N  N    . TYR   B 1 42  ? 46.255 -17.097 10.961  1.00 12.49 ?  42  TYR   B N    1 
ATOM   4670 C  CA   . TYR   B 1 42  ? 47.406 -16.248 11.233  1.00 12.91 ?  42  TYR   B CA   1 
ATOM   4671 C  C    . TYR   B 1 42  ? 48.370 -16.171 10.050  1.00 12.34 ?  42  TYR   B C    1 
ATOM   4672 O  O    . TYR   B 1 42  ? 49.463 -15.606 10.183  1.00 13.36 ?  42  TYR   B O    1 
ATOM   4673 C  CB   . TYR   B 1 42  ? 48.093 -16.657 12.544  1.00 14.67 ?  42  TYR   B CB   1 
ATOM   4674 C  CG   . TYR   B 1 42  ? 47.491 -15.963 13.766  1.00 14.90 ?  42  TYR   B CG   1 
ATOM   4675 C  CD1  . TYR   B 1 42  ? 47.709 -14.606 13.984  1.00 14.34 ?  42  TYR   B CD1  1 
ATOM   4676 C  CD2  . TYR   B 1 42  ? 46.706 -16.651 14.682  1.00 16.57 ?  42  TYR   B CD2  1 
ATOM   4677 C  CE1  . TYR   B 1 42  ? 47.171 -13.956 15.074  1.00 15.48 ?  42  TYR   B CE1  1 
ATOM   4678 C  CE2  . TYR   B 1 42  ? 46.166 -16.004 15.787  1.00 17.27 ?  42  TYR   B CE2  1 
ATOM   4679 C  CZ   . TYR   B 1 42  ? 46.403 -14.653 15.975  1.00 17.36 ?  42  TYR   B CZ   1 
ATOM   4680 O  OH   . TYR   B 1 42  ? 45.881 -13.986 17.065  1.00 20.01 ?  42  TYR   B OH   1 
ATOM   4681 H  H    . TYR   B 1 42  ? 46.406 -17.942 11.059  1.00 14.97 ?  42  TYR   B H    1 
ATOM   4682 H  HA   . TYR   B 1 42  ? 47.078 -15.351 11.367  1.00 15.48 ?  42  TYR   B HA   1 
ATOM   4683 H  HB2  . TYR   B 1 42  ? 48.000 -17.616 12.663  1.00 17.58 ?  42  TYR   B HB2  1 
ATOM   4684 H  HB3  . TYR   B 1 42  ? 49.032 -16.420 12.492  1.00 17.58 ?  42  TYR   B HB3  1 
ATOM   4685 H  HD1  . TYR   B 1 42  ? 48.230 -14.131 13.371  1.00 17.19 ?  42  TYR   B HD1  1 
ATOM   4686 H  HD2  . TYR   B 1 42  ? 46.545 -17.563 14.552  1.00 19.86 ?  42  TYR   B HD2  1 
ATOM   4687 H  HE1  . TYR   B 1 42  ? 47.331 -13.051 15.197  1.00 18.56 ?  42  TYR   B HE1  1 
ATOM   4688 H  HE2  . TYR   B 1 42  ? 45.640 -16.480 16.389  1.00 20.71 ?  42  TYR   B HE2  1 
ATOM   4689 H  HH   . TYR   B 1 42  ? 46.108 -13.181 17.036  1.00 24.00 ?  42  TYR   B HH   1 
ATOM   4690 N  N    . LEU   B 1 43  ? 47.972 -16.690 8.889   1.00 11.20 ?  43  LEU   B N    1 
ATOM   4691 C  CA   . LEU   B 1 43  ? 48.782 -16.617 7.677   1.00 11.20 ?  43  LEU   B CA   1 
ATOM   4692 C  C    . LEU   B 1 43  ? 50.196 -17.124 7.931   1.00 11.56 ?  43  LEU   B C    1 
ATOM   4693 O  O    . LEU   B 1 43  ? 51.177 -16.534 7.477   1.00 12.26 ?  43  LEU   B O    1 
ATOM   4694 C  CB   . LEU   B 1 43  ? 48.801 -15.212 7.070   1.00 11.61 ?  43  LEU   B CB   1 
ATOM   4695 C  CG   . LEU   B 1 43  ? 47.446 -14.597 6.702   1.00 11.69 ?  43  LEU   B CG   1 
ATOM   4696 C  CD1  . LEU   B 1 43  ? 47.651 -13.201 6.106   1.00 13.01 ?  43  LEU   B CD1  1 
ATOM   4697 C  CD2  . LEU   B 1 43  ? 46.675 -15.492 5.742   1.00 11.99 ?  43  LEU   B CD2  1 
ATOM   4698 H  H    . LEU   B 1 43  ? 47.226 -17.104 8.776   1.00 13.42 ?  43  LEU   B H    1 
ATOM   4699 H  HA   . LEU   B 1 43  ? 48.385 -17.209 7.014   1.00 13.42 ?  43  LEU   B HA   1 
ATOM   4700 H  HB2  . LEU   B 1 43  ? 49.226 -14.618 7.705   1.00 13.92 ?  43  LEU   B HB2  1 
ATOM   4701 H  HB3  . LEU   B 1 43  ? 49.329 -15.246 6.257   1.00 13.92 ?  43  LEU   B HB3  1 
ATOM   4702 H  HG   . LEU   B 1 43  ? 46.919 -14.498 7.509   1.00 14.02 ?  43  LEU   B HG   1 
ATOM   4703 H  HD11 . LEU   B 1 43  ? 46.787 -12.822 5.880   1.00 15.60 ?  43  LEU   B HD11 1 
ATOM   4704 H  HD12 . LEU   B 1 43  ? 48.096 -12.637 6.761   1.00 15.60 ?  43  LEU   B HD12 1 
ATOM   4705 H  HD13 . LEU   B 1 43  ? 48.199 -13.272 5.309   1.00 15.60 ?  43  LEU   B HD13 1 
ATOM   4706 H  HD21 . LEU   B 1 43  ? 45.878 -15.025 5.449   1.00 14.38 ?  43  LEU   B HD21 1 
ATOM   4707 H  HD22 . LEU   B 1 43  ? 47.239 -15.699 4.982   1.00 14.38 ?  43  LEU   B HD22 1 
ATOM   4708 H  HD23 . LEU   B 1 43  ? 46.428 -16.309 6.205   1.00 14.38 ?  43  LEU   B HD23 1 
ATOM   4709 N  N    . LYS   B 1 44  ? 50.294 -18.246 8.647   1.00 11.53 ?  44  LYS   B N    1 
ATOM   4710 C  CA   . LYS   B 1 44  ? 51.561 -18.925 8.888   1.00 12.17 ?  44  LYS   B CA   1 
ATOM   4711 C  C    . LYS   B 1 44  ? 51.678 -20.044 7.863   1.00 11.78 ?  44  LYS   B C    1 
ATOM   4712 O  O    . LYS   B 1 44  ? 50.981 -21.058 7.953   1.00 12.91 ?  44  LYS   B O    1 
ATOM   4713 C  CB   . LYS   B 1 44  ? 51.623 -19.439 10.324  1.00 14.01 ?  44  LYS   B CB   1 
ATOM   4714 C  CG   . LYS   B 1 44  ? 51.807 -18.325 11.343  1.00 16.71 ?  44  LYS   B CG   1 
ATOM   4715 C  CD   . LYS   B 1 44  ? 52.992 -17.447 10.930  1.00 19.95 ?  44  LYS   B CD   1 
ATOM   4716 C  CE   . LYS   B 1 44  ? 53.525 -16.592 12.048  1.00 22.96 ?  44  LYS   B CE   1 
ATOM   4717 N  NZ   . LYS   B 1 44  ? 54.713 -15.803 11.640  1.00 24.31 ?  44  LYS   B NZ   1 
ATOM   4718 H  H    . LYS   B 1 44  ? 49.620 -18.636 9.015   1.00 13.82 ?  44  LYS   B H    1 
ATOM   4719 H  HA   . LYS   B 1 44  ? 52.291 -18.312 8.720   1.00 14.58 ?  44  LYS   B HA   1 
ATOM   4720 H  HB2  . LYS   B 1 44  ? 50.789 -19.895 10.533  1.00 16.80 ?  44  LYS   B HB2  1 
ATOM   4721 H  HB3  . LYS   B 1 44  ? 52.366 -20.051 10.412  1.00 16.80 ?  44  LYS   B HB3  1 
ATOM   4722 H  HG2  . LYS   B 1 44  ? 51.008 -17.781 11.381  1.00 20.03 ?  44  LYS   B HG2  1 
ATOM   4723 H  HG3  . LYS   B 1 44  ? 51.998 -18.715 12.215  1.00 20.03 ?  44  LYS   B HG3  1 
ATOM   4724 H  HD2  . LYS   B 1 44  ? 53.707 -18.023 10.605  1.00 23.92 ?  44  LYS   B HD2  1 
ATOM   4725 H  HD3  . LYS   B 1 44  ? 52.700 -16.853 10.219  1.00 23.92 ?  44  LYS   B HD3  1 
ATOM   4726 H  HE2  . LYS   B 1 44  ? 52.841 -15.957 12.281  1.00 27.54 ?  44  LYS   B HE2  1 
ATOM   4727 H  HE3  . LYS   B 1 44  ? 53.757 -17.153 12.808  1.00 27.54 ?  44  LYS   B HE3  1 
ATOM   4728 H  HZ1  . LYS   B 1 44  ? 54.996 -15.308 12.323  1.00 29.16 ?  44  LYS   B HZ1  1 
ATOM   4729 H  HZ2  . LYS   B 1 44  ? 55.368 -16.345 11.382  1.00 29.16 ?  44  LYS   B HZ2  1 
ATOM   4730 H  HZ3  . LYS   B 1 44  ? 54.500 -15.264 10.962  1.00 29.16 ?  44  LYS   B HZ3  1 
ATOM   4731 N  N    . HIS   B 1 45  ? 52.525 -19.826 6.860   1.00 11.54 ?  45  HIS   B N    1 
ATOM   4732 C  CA   . HIS   B 1 45  ? 52.550 -20.658 5.658   1.00 11.72 ?  45  HIS   B CA   1 
ATOM   4733 C  C    . HIS   B 1 45  ? 53.573 -21.778 5.822   1.00 13.86 ?  45  HIS   B C    1 
ATOM   4734 O  O    . HIS   B 1 45  ? 54.638 -21.788 5.215   1.00 16.12 ?  45  HIS   B O    1 
ATOM   4735 C  CB   . HIS   B 1 45  ? 52.866 -19.802 4.444   1.00 11.62 ?  45  HIS   B CB   1 
ATOM   4736 C  CG   . HIS   B 1 45  ? 51.994 -18.601 4.332   1.00 11.47 ?  45  HIS   B CG   1 
ATOM   4737 N  ND1  . HIS   B 1 45  ? 50.617 -18.679 4.304   1.00 11.50 ?  45  HIS   B ND1  1 
ATOM   4738 C  CD2  . HIS   B 1 45  ? 52.311 -17.287 4.253   1.00 12.39 ?  45  HIS   B CD2  1 
ATOM   4739 C  CE1  . HIS   B 1 45  ? 50.128 -17.455 4.200   1.00 11.43 ?  45  HIS   B CE1  1 
ATOM   4740 N  NE2  . HIS   B 1 45  ? 51.132 -16.595 4.163   1.00 12.04 ?  45  HIS   B NE2  1 
ATOM   4741 H  H    . HIS   B 1 45  ? 53.090 -19.182 6.845   1.00 13.83 ?  45  HIS   B H    1 
ATOM   4742 H  HA   . HIS   B 1 45  ? 51.670 -21.057 5.525   1.00 14.05 ?  45  HIS   B HA   1 
ATOM   4743 H  HB2  . HIS   B 1 45  ? 53.785 -19.505 4.503   1.00 13.93 ?  45  HIS   B HB2  1 
ATOM   4744 H  HB3  . HIS   B 1 45  ? 52.744 -20.341 3.642   1.00 13.93 ?  45  HIS   B HB3  1 
ATOM   4745 H  HD2  . HIS   B 1 45  ? 53.167 -16.922 4.257   1.00 14.85 ?  45  HIS   B HD2  1 
ATOM   4746 H  HE1  . HIS   B 1 45  ? 49.226 -17.237 4.150   1.00 13.70 ?  45  HIS   B HE1  1 
ATOM   4747 H  HE2  . HIS   B 1 45  ? 51.055 -15.739 4.110   1.00 14.44 ?  45  HIS   B HE2  1 
ATOM   4748 N  N    A GLY   B 1 46  ? 53.206 -22.752 6.651   0.62 14.85 ?  46  GLY   B N    1 
ATOM   4749 N  N    B GLY   B 1 46  ? 53.215 -22.738 6.666   0.38 14.77 ?  46  GLY   B N    1 
ATOM   4750 C  CA   A GLY   B 1 46  ? 54.132 -23.805 7.030   0.62 16.52 ?  46  GLY   B CA   1 
ATOM   4751 C  CA   B GLY   B 1 46  ? 54.136 -23.803 7.002   0.38 16.10 ?  46  GLY   B CA   1 
ATOM   4752 C  C    A GLY   B 1 46  ? 54.182 -25.033 6.142   0.62 17.89 ?  46  GLY   B C    1 
ATOM   4753 C  C    B GLY   B 1 46  ? 54.163 -24.947 6.010   0.38 17.32 ?  46  GLY   B C    1 
ATOM   4754 O  O    A GLY   B 1 46  ? 55.265 -25.482 5.754   0.62 20.32 ?  46  GLY   B O    1 
ATOM   4755 O  O    B GLY   B 1 46  ? 55.193 -25.220 5.385   0.38 18.32 ?  46  GLY   B O    1 
ATOM   4756 H  H    A GLY   B 1 46  ? 52.427 -22.807 7.024   0.62 17.81 ?  46  GLY   B H    1 
ATOM   4757 H  H    B GLY   B 1 46  ? 52.446 -22.783 7.061   0.38 17.71 ?  46  GLY   B H    1 
ATOM   4758 H  HA2  A GLY   B 1 46  ? 55.023 -23.427 7.067   0.62 19.81 ?  46  GLY   B HA2  1 
ATOM   4759 H  HA2  B GLY   B 1 46  ? 55.029 -23.432 7.061   0.38 19.31 ?  46  GLY   B HA2  1 
ATOM   4760 H  HA3  A GLY   B 1 46  ? 53.900 -24.110 7.919   0.62 19.81 ?  46  GLY   B HA3  1 
ATOM   4761 H  HA3  B GLY   B 1 46  ? 53.899 -24.155 7.874   0.38 19.31 ?  46  GLY   B HA3  1 
ATOM   4762 N  N    . GLY   B 1 47  ? 53.024 -25.614 5.834   1.00 17.68 ?  47  GLY   B N    1 
ATOM   4763 C  CA   . GLY   B 1 47  ? 52.967 -26.880 5.133   1.00 15.45 ?  47  GLY   B CA   1 
ATOM   4764 C  C    . GLY   B 1 47  ? 52.054 -26.854 3.923   1.00 13.30 ?  47  GLY   B C    1 
ATOM   4765 O  O    . GLY   B 1 47  ? 51.403 -25.851 3.629   1.00 13.57 ?  47  GLY   B O    1 
ATOM   4766 H  H    A GLY   B 1 47  ? 52.250 -25.300 6.049   0.62 21.20 ?  47  GLY   B H    1 
ATOM   4767 H  H    B GLY   B 1 47  ? 52.256 -25.341 6.119   0.38 21.20 ?  47  GLY   B H    1 
ATOM   4768 H  HA2  . GLY   B 1 47  ? 53.855 -27.130 4.834   1.00 18.52 ?  47  GLY   B HA2  1 
ATOM   4769 H  HA3  . GLY   B 1 47  ? 52.650 -27.567 5.743   1.00 18.52 ?  47  GLY   B HA3  1 
ATOM   4770 N  N    . GLY   B 1 48  ? 52.010 -27.992 3.235   1.00 12.51 ?  48  GLY   B N    1 
ATOM   4771 C  CA   . GLY   B 1 48  ? 51.089 -28.140 2.126   1.00 12.36 ?  48  GLY   B CA   1 
ATOM   4772 C  C    . GLY   B 1 48  ? 51.224 -27.027 1.112   1.00 11.80 ?  48  GLY   B C    1 
ATOM   4773 O  O    . GLY   B 1 48  ? 52.321 -26.558 0.800   1.00 12.35 ?  48  GLY   B O    1 
ATOM   4774 H  H    . GLY   B 1 48  ? 52.503 -28.676 3.387   1.00 14.99 ?  48  GLY   B H    1 
ATOM   4775 H  HA2  . GLY   B 1 48  ? 51.252 -28.986 1.683   1.00 14.81 ?  48  GLY   B HA2  1 
ATOM   4776 H  HA3  . GLY   B 1 48  ? 50.178 -28.139 2.460   1.00 14.81 ?  48  GLY   B HA3  1 
ATOM   4777 N  N    . VAL   B 1 49  ? 50.080 -26.599 0.579   1.00 11.82 ?  49  VAL   B N    1 
ATOM   4778 C  CA   . VAL   B 1 49  ? 50.060 -25.573 -0.461  1.00 11.75 ?  49  VAL   B CA   1 
ATOM   4779 C  C    . VAL   B 1 49  ? 50.716 -24.285 0.028   1.00 10.82 ?  49  VAL   B C    1 
ATOM   4780 O  O    . VAL   B 1 49  ? 51.504 -23.664 -0.692  1.00 11.56 ?  49  VAL   B O    1 
ATOM   4781 C  CB   . VAL   B 1 49  ? 48.613 -25.323 -0.930  1.00 12.89 ?  49  VAL   B CB   1 
ATOM   4782 C  CG1  . VAL   B 1 49  ? 48.528 -24.079 -1.805  1.00 12.94 ?  49  VAL   B CG1  1 
ATOM   4783 C  CG2  . VAL   B 1 49  ? 48.059 -26.539 -1.671  1.00 14.41 ?  49  VAL   B CG2  1 
ATOM   4784 H  H    . VAL   B 1 49  ? 49.296 -26.890 0.800   1.00 14.17 ?  49  VAL   B H    1 
ATOM   4785 H  HA   . VAL   B 1 49  ? 50.560 -25.892 -1.227  1.00 14.08 ?  49  VAL   B HA   1 
ATOM   4786 H  HB   . VAL   B 1 49  ? 48.052 -25.176 -0.154  1.00 15.45 ?  49  VAL   B HB   1 
ATOM   4787 H  HG11 . VAL   B 1 49  ? 47.692 -24.095 -2.301  1.00 15.51 ?  49  VAL   B HG11 1 
ATOM   4788 H  HG12 . VAL   B 1 49  ? 48.555 -23.288 -1.240  1.00 15.51 ?  49  VAL   B HG12 1 
ATOM   4789 H  HG13 . VAL   B 1 49  ? 49.275 -24.071 -2.423  1.00 15.51 ?  49  VAL   B HG13 1 
ATOM   4790 H  HG21 . VAL   B 1 49  ? 47.147 -26.354 -1.950  1.00 17.27 ?  49  VAL   B HG21 1 
ATOM   4791 H  HG22 . VAL   B 1 49  ? 48.612 -26.714 -2.450  1.00 17.27 ?  49  VAL   B HG22 1 
ATOM   4792 H  HG23 . VAL   B 1 49  ? 48.073 -27.305 -1.077  1.00 17.27 ?  49  VAL   B HG23 1 
ATOM   4793 N  N    . ALA   B 1 50  ? 50.369 -23.842 1.238   1.00 10.67 ?  50  ALA   B N    1 
ATOM   4794 C  CA   . ALA   B 1 50  ? 50.891 -22.565 1.713   1.00 10.52 ?  50  ALA   B CA   1 
ATOM   4795 C  C    . ALA   B 1 50  ? 52.409 -22.599 1.822   1.00 10.66 ?  50  ALA   B C    1 
ATOM   4796 O  O    . ALA   B 1 50  ? 53.094 -21.635 1.456   1.00 10.88 ?  50  ALA   B O    1 
ATOM   4797 C  CB   . ALA   B 1 50  ? 50.263 -22.208 3.056   1.00 10.87 ?  50  ALA   B CB   1 
ATOM   4798 H  H    . ALA   B 1 50  ? 49.847 -24.247 1.786   1.00 12.79 ?  50  ALA   B H    1 
ATOM   4799 H  HA   . ALA   B 1 50  ? 50.661 -21.870 1.080   1.00 12.60 ?  50  ALA   B HA   1 
ATOM   4800 H  HB1  . ALA   B 1 50  ? 50.622 -21.355 3.356   1.00 13.02 ?  50  ALA   B HB1  1 
ATOM   4801 H  HB2  . ALA   B 1 50  ? 49.302 -22.137 2.944   1.00 13.02 ?  50  ALA   B HB2  1 
ATOM   4802 H  HB3  . ALA   B 1 50  ? 50.474 -22.899 3.700   1.00 13.02 ?  50  ALA   B HB3  1 
ATOM   4803 N  N    . GLY   B 1 51  ? 52.959 -23.690 2.344   1.00 11.16 ?  51  GLY   B N    1 
ATOM   4804 C  CA   . GLY   B 1 51  ? 54.402 -23.799 2.411   1.00 11.77 ?  51  GLY   B CA   1 
ATOM   4805 C  C    . GLY   B 1 51  ? 55.050 -23.742 1.042   1.00 11.74 ?  51  GLY   B C    1 
ATOM   4806 O  O    . GLY   B 1 51  ? 56.093 -23.105 0.866   1.00 12.84 ?  51  GLY   B O    1 
ATOM   4807 H  H    . GLY   B 1 51  ? 52.527 -24.371 2.651   1.00 13.37 ?  51  GLY   B H    1 
ATOM   4808 H  HA2  . GLY   B 1 51  ? 54.759 -23.074 2.946   1.00 14.11 ?  51  GLY   B HA2  1 
ATOM   4809 H  HA3  . GLY   B 1 51  ? 54.648 -24.641 2.830   1.00 14.11 ?  51  GLY   B HA3  1 
ATOM   4810 N  N    . ALA   B 1 52  ? 54.445 -24.407 0.056   1.00 11.33 ?  52  ALA   B N    1 
ATOM   4811 C  CA   . ALA   B 1 52  ? 55.001 -24.415 -1.290  1.00 11.80 ?  52  ALA   B CA   1 
ATOM   4812 C  C    . ALA   B 1 52  ? 54.920 -23.038 -1.938  1.00 11.30 ?  52  ALA   B C    1 
ATOM   4813 O  O    . ALA   B 1 52  ? 55.890 -22.582 -2.563  1.00 12.02 ?  52  ALA   B O    1 
ATOM   4814 C  CB   . ALA   B 1 52  ? 54.290 -25.459 -2.143  1.00 12.81 ?  52  ALA   B CB   1 
ATOM   4815 H  H    . ALA   B 1 52  ? 53.710 -24.853 0.140   1.00 13.57 ?  52  ALA   B H    1 
ATOM   4816 H  HA   . ALA   B 1 52  ? 55.936 -24.659 -1.237  1.00 14.14 ?  52  ALA   B HA   1 
ATOM   4817 H  HB1  . ALA   B 1 52  ? 54.677 -25.451 -3.037  1.00 15.35 ?  52  ALA   B HB1  1 
ATOM   4818 H  HB2  . ALA   B 1 52  ? 54.416 -26.333 -1.741  1.00 15.35 ?  52  ALA   B HB2  1 
ATOM   4819 H  HB3  . ALA   B 1 52  ? 53.348 -25.246 -2.191  1.00 15.35 ?  52  ALA   B HB3  1 
ATOM   4820 N  N    . LEU   B 1 53  ? 53.779 -22.359 -1.812  1.00 10.97 ?  53  LEU   B N    1 
ATOM   4821 C  CA   . LEU   B 1 53  ? 53.666 -21.017 -2.378  1.00 11.12 ?  53  LEU   B CA   1 
ATOM   4822 C  C    . LEU   B 1 53  ? 54.671 -20.077 -1.729  1.00 11.07 ?  53  LEU   B C    1 
ATOM   4823 O  O    . LEU   B 1 53  ? 55.369 -19.326 -2.416  1.00 11.73 ?  53  LEU   B O    1 
ATOM   4824 C  CB   . LEU   B 1 53  ? 52.242 -20.474 -2.214  1.00 11.70 ?  53  LEU   B CB   1 
ATOM   4825 C  CG   . LEU   B 1 53  ? 51.103 -21.207 -2.930  1.00 11.81 ?  53  LEU   B CG   1 
ATOM   4826 C  CD1  . LEU   B 1 53  ? 49.770 -20.594 -2.565  1.00 13.05 ?  53  LEU   B CD1  1 
ATOM   4827 C  CD2  . LEU   B 1 53  ? 51.297 -21.215 -4.441  1.00 14.11 ?  53  LEU   B CD2  1 
ATOM   4828 H  H    . LEU   B 1 53  ? 53.073 -22.641 -1.410  1.00 13.14 ?  53  LEU   B H    1 
ATOM   4829 H  HA   . LEU   B 1 53  ? 53.865 -21.060 -3.330  1.00 13.33 ?  53  LEU   B HA   1 
ATOM   4830 H  HB2  . LEU   B 1 53  ? 52.033 -20.476 -1.270  1.00 14.03 ?  53  LEU   B HB2  1 
ATOM   4831 H  HB3  . LEU   B 1 53  ? 52.237 -19.559 -2.540  1.00 14.03 ?  53  LEU   B HB3  1 
ATOM   4832 H  HG   . LEU   B 1 53  ? 51.092 -22.128 -2.630  1.00 14.16 ?  53  LEU   B HG   1 
ATOM   4833 H  HD11 . LEU   B 1 53  ? 49.063 -21.078 -3.023  1.00 15.64 ?  53  LEU   B HD11 1 
ATOM   4834 H  HD12 . LEU   B 1 53  ? 49.642 -20.663 -1.603  1.00 15.64 ?  53  LEU   B HD12 1 
ATOM   4835 H  HD13 . LEU   B 1 53  ? 49.762 -19.664 -2.833  1.00 15.64 ?  53  LEU   B HD13 1 
ATOM   4836 H  HD21 . LEU   B 1 53  ? 50.581 -21.735 -4.846  1.00 16.91 ?  53  LEU   B HD21 1 
ATOM   4837 H  HD22 . LEU   B 1 53  ? 51.266 -20.305 -4.769  1.00 16.91 ?  53  LEU   B HD22 1 
ATOM   4838 H  HD23 . LEU   B 1 53  ? 52.152 -21.619 -4.650  1.00 16.91 ?  53  LEU   B HD23 1 
ATOM   4839 N  N    . ASN   B 1 54  ? 54.762 -20.106 -0.402  1.00 10.72 ?  54  ASN   B N    1 
ATOM   4840 C  CA   . ASN   B 1 54  ? 55.678 -19.196 0.267   1.00 11.33 ?  54  ASN   B CA   1 
ATOM   4841 C  C    . ASN   B 1 54  ? 57.120 -19.474 -0.137  1.00 11.87 ?  54  ASN   B C    1 
ATOM   4842 O  O    . ASN   B 1 54  ? 57.894 -18.538 -0.377  1.00 12.00 ?  54  ASN   B O    1 
ATOM   4843 C  CB   . ASN   B 1 54  ? 55.528 -19.279 1.777   1.00 12.25 ?  54  ASN   B CB   1 
ATOM   4844 C  CG   . ASN   B 1 54  ? 56.502 -18.362 2.483   1.00 12.27 ?  54  ASN   B CG   1 
ATOM   4845 O  OD1  . ASN   B 1 54  ? 56.521 -17.159 2.231   1.00 12.53 ?  54  ASN   B OD1  1 
ATOM   4846 N  ND2  . ASN   B 1 54  ? 57.341 -18.925 3.341   1.00 13.98 ?  54  ASN   B ND2  1 
ATOM   4847 H  H    . ASN   B 1 54  ? 54.318 -20.628 0.114   1.00 12.84 ?  54  ASN   B H    1 
ATOM   4848 H  HA   . ASN   B 1 54  ? 55.465 -18.288 -0.004  1.00 13.58 ?  54  ASN   B HA   1 
ATOM   4849 H  HB2  . ASN   B 1 54  ? 54.627 -19.015 2.024   1.00 14.68 ?  54  ASN   B HB2  1 
ATOM   4850 H  HB3  . ASN   B 1 54  ? 55.703 -20.188 2.066   1.00 14.68 ?  54  ASN   B HB3  1 
ATOM   4851 H  HD21 . ASN   B 1 54  ? 57.920 -18.441 3.759   1.00 16.76 ?  54  ASN   B HD21 1 
ATOM   4852 H  HD22 . ASN   B 1 54  ? 57.310 -19.772 3.485   1.00 16.76 ?  54  ASN   B HD22 1 
ATOM   4853 N  N    . LYS   B 1 55  ? 57.509 -20.751 -0.197  1.00 12.43 ?  55  LYS   B N    1 
ATOM   4854 C  CA   . LYS   B 1 55  ? 58.864 -21.092 -0.617  1.00 13.54 ?  55  LYS   B CA   1 
ATOM   4855 C  C    . LYS   B 1 55  ? 59.158 -20.552 -2.009  1.00 13.21 ?  55  LYS   B C    1 
ATOM   4856 O  O    . LYS   B 1 55  ? 60.259 -20.053 -2.267  1.00 13.82 ?  55  LYS   B O    1 
ATOM   4857 C  CB   . LYS   B 1 55  ? 59.056 -22.609 -0.573  1.00 15.47 ?  55  LYS   B CB   1 
ATOM   4858 C  CG   . LYS   B 1 55  ? 60.428 -23.076 -1.017  1.00 19.37 ?  55  LYS   B CG   1 
ATOM   4859 C  CD   . LYS   B 1 55  ? 60.583 -24.577 -0.854  1.00 22.84 ?  55  LYS   B CD   1 
ATOM   4860 C  CE   . LYS   B 1 55  ? 60.678 -24.978 0.615   1.00 25.87 ?  55  LYS   B CE   1 
ATOM   4861 N  NZ   . LYS   B 1 55  ? 61.054 -26.403 0.777   1.00 27.24 ?  55  LYS   B NZ   1 
ATOM   4862 H  H    . LYS   B 1 55  ? 57.008 -21.423 -0.003  1.00 14.90 ?  55  LYS   B H    1 
ATOM   4863 H  HA   . LYS   B 1 55  ? 59.494 -20.689 0.001   1.00 16.23 ?  55  LYS   B HA   1 
ATOM   4864 H  HB2  . LYS   B 1 55  ? 58.918 -22.907 0.339   1.00 18.54 ?  55  LYS   B HB2  1 
ATOM   4865 H  HB3  . LYS   B 1 55  ? 58.400 -23.021 -1.155  1.00 18.54 ?  55  LYS   B HB3  1 
ATOM   4866 H  HG2  . LYS   B 1 55  ? 60.554 -22.859 -1.953  1.00 23.23 ?  55  LYS   B HG2  1 
ATOM   4867 H  HG3  . LYS   B 1 55  ? 61.104 -22.639 -0.476  1.00 23.23 ?  55  LYS   B HG3  1 
ATOM   4868 H  HD2  . LYS   B 1 55  ? 59.814 -25.027 -1.241  1.00 27.39 ?  55  LYS   B HD2  1 
ATOM   4869 H  HD3  . LYS   B 1 55  ? 61.397 -24.868 -1.297  1.00 27.39 ?  55  LYS   B HD3  1 
ATOM   4870 H  HE2  . LYS   B 1 55  ? 61.351 -24.428 1.049   1.00 31.02 ?  55  LYS   B HE2  1 
ATOM   4871 H  HE3  . LYS   B 1 55  ? 59.814 -24.838 1.037   1.00 31.02 ?  55  LYS   B HE3  1 
ATOM   4872 H  HZ1  . LYS   B 1 55  ? 61.075 -26.613 1.641   1.00 32.67 ?  55  LYS   B HZ1  1 
ATOM   4873 H  HZ2  . LYS   B 1 55  ? 60.458 -26.920 0.366   1.00 32.67 ?  55  LYS   B HZ2  1 
ATOM   4874 H  HZ3  . LYS   B 1 55  ? 61.857 -26.546 0.423   1.00 32.67 ?  55  LYS   B HZ3  1 
ATOM   4875 N  N    . ALA   B 1 56  ? 58.186 -20.636 -2.922  1.00 12.76 ?  56  ALA   B N    1 
ATOM   4876 C  CA   . ALA   B 1 56  ? 58.409 -20.141 -4.275  1.00 13.45 ?  56  ALA   B CA   1 
ATOM   4877 C  C    . ALA   B 1 56  ? 58.683 -18.643 -4.281  1.00 13.15 ?  56  ALA   B C    1 
ATOM   4878 O  O    . ALA   B 1 56  ? 59.411 -18.148 -5.153  1.00 14.13 ?  56  ALA   B O    1 
ATOM   4879 C  CB   . ALA   B 1 56  ? 57.211 -20.485 -5.164  1.00 14.36 ?  56  ALA   B CB   1 
ATOM   4880 H  H    . ALA   B 1 56  ? 57.401 -20.964 -2.781  1.00 15.29 ?  56  ALA   B H    1 
ATOM   4881 H  HA   . ALA   B 1 56  ? 59.186 -20.582 -4.644  1.00 16.12 ?  56  ALA   B HA   1 
ATOM   4882 H  HB1  . ALA   B 1 56  ? 57.381 -20.156 -6.063  1.00 17.21 ?  56  ALA   B HB1  1 
ATOM   4883 H  HB2  . ALA   B 1 56  ? 57.102 -21.450 -5.185  1.00 17.21 ?  56  ALA   B HB2  1 
ATOM   4884 H  HB3  . ALA   B 1 56  ? 56.415 -20.070 -4.804  1.00 17.21 ?  56  ALA   B HB3  1 
ATOM   4885 N  N    . THR   B 1 57  ? 58.120 -17.908 -3.319  1.00 12.67 ?  57  THR   B N    1 
ATOM   4886 C  CA   . THR   B 1 57  ? 58.356 -16.473 -3.195  1.00 12.88 ?  57  THR   B CA   1 
ATOM   4887 C  C    . THR   B 1 57  ? 59.604 -16.147 -2.382  1.00 13.90 ?  57  THR   B C    1 
ATOM   4888 O  O    . THR   B 1 57  ? 59.839 -14.971 -2.076  1.00 14.22 ?  57  THR   B O    1 
ATOM   4889 C  CB   . THR   B 1 57  ? 57.152 -15.748 -2.562  1.00 12.13 ?  57  THR   B CB   1 
ATOM   4890 O  OG1  . THR   B 1 57  ? 57.133 -15.954 -1.140  1.00 12.54 ?  57  THR   B OG1  1 
ATOM   4891 C  CG2  . THR   B 1 57  ? 55.833 -16.167 -3.200  1.00 12.31 ?  57  THR   B CG2  1 
ATOM   4892 H  H    . THR   B 1 57  ? 57.582 -18.224 -2.723  1.00 15.18 ?  57  THR   B H    1 
ATOM   4893 H  HA   . THR   B 1 57  ? 58.476 -16.109 -4.086  1.00 15.45 ?  57  THR   B HA   1 
ATOM   4894 H  HB   . THR   B 1 57  ? 57.257 -14.799 -2.731  1.00 14.54 ?  57  THR   B HB   1 
ATOM   4895 H  HG1  . THR   B 1 57  ? 57.070 -16.774 -0.973  1.00 15.03 ?  57  THR   B HG1  1 
ATOM   4896 H  HG21 . THR   B 1 57  ? 55.105 -15.647 -2.828  1.00 14.75 ?  57  THR   B HG21 1 
ATOM   4897 H  HG22 . THR   B 1 57  ? 55.865 -16.024 -4.159  1.00 14.75 ?  57  THR   B HG22 1 
ATOM   4898 H  HG23 . THR   B 1 57  ? 55.664 -17.107 -3.031  1.00 14.75 ?  57  THR   B HG23 1 
ATOM   4899 N  N    . ASN   B 1 58  ? 60.401 -17.149 -2.021  1.00 14.39 ?  58  ASN   B N    1 
ATOM   4900 C  CA   . ASN   B 1 58  ? 61.597 -16.931 -1.212  1.00 16.79 ?  58  ASN   B CA   1 
ATOM   4901 C  C    . ASN   B 1 58  ? 61.258 -16.221 0.098   1.00 15.31 ?  58  ASN   B C    1 
ATOM   4902 O  O    . ASN   B 1 58  ? 61.996 -15.348 0.563   1.00 16.01 ?  58  ASN   B O    1 
ATOM   4903 C  CB   . ASN   B 1 58  ? 62.684 -16.184 -1.991  1.00 22.64 ?  58  ASN   B CB   1 
ATOM   4904 C  CG   . ASN   B 1 58  ? 64.053 -16.327 -1.357  1.00 29.82 ?  58  ASN   B CG   1 
ATOM   4905 O  OD1  . ASN   B 1 58  ? 64.344 -17.327 -0.702  1.00 32.49 ?  58  ASN   B OD1  1 
ATOM   4906 N  ND2  . ASN   B 1 58  ? 64.900 -15.324 -1.544  1.00 32.67 ?  58  ASN   B ND2  1 
ATOM   4907 H  H    . ASN   B 1 58  ? 60.262 -17.977 -2.226  1.00 17.26 ?  58  ASN   B H    1 
ATOM   4908 H  HA   . ASN   B 1 58  ? 61.959 -17.803 -0.988  1.00 20.13 ?  58  ASN   B HA   1 
ATOM   4909 H  HB2  . ASN   B 1 58  ? 62.730 -16.542 -2.896  1.00 27.15 ?  58  ASN   B HB2  1 
ATOM   4910 H  HB3  . ASN   B 1 58  ? 62.463 -15.242 -2.021  1.00 27.15 ?  58  ASN   B HB3  1 
ATOM   4911 H  HD21 . ASN   B 1 58  ? 65.690 -15.359 -1.205  1.00 39.19 ?  58  ASN   B HD21 1 
ATOM   4912 H  HD22 . ASN   B 1 58  ? 64.660 -14.640 -2.006  1.00 39.19 ?  58  ASN   B HD22 1 
ATOM   4913 N  N    . ASN   B 1 59  ? 60.132 -16.605 0.703   1.00 14.20 ?  59  ASN   B N    1 
ATOM   4914 C  CA   . ASN   B 1 59  ? 59.657 -16.130 2.003   1.00 14.10 ?  59  ASN   B CA   1 
ATOM   4915 C  C    . ASN   B 1 59  ? 59.064 -14.723 1.948   1.00 13.48 ?  59  ASN   B C    1 
ATOM   4916 O  O    . ASN   B 1 59  ? 58.630 -14.218 2.992   1.00 13.75 ?  59  ASN   B O    1 
ATOM   4917 C  CB   . ASN   B 1 59  ? 60.730 -16.191 3.105   1.00 15.31 ?  59  ASN   B CB   1 
ATOM   4918 C  CG   . ASN   B 1 59  ? 60.146 -16.376 4.485   1.00 16.45 ?  59  ASN   B CG   1 
ATOM   4919 O  OD1  . ASN   B 1 59  ? 59.324 -17.267 4.711   1.00 16.78 ?  59  ASN   B OD1  1 
ATOM   4920 N  ND2  . ASN   B 1 59  ? 60.570 -15.536 5.422   1.00 17.23 ?  59  ASN   B ND2  1 
ATOM   4921 H  H    . ASN   B 1 59  ? 59.590 -17.184 0.355   1.00 17.02 ?  59  ASN   B H    1 
ATOM   4922 H  HA   . ASN   B 1 59  ? 58.946 -16.724 2.287   1.00 16.90 ?  59  ASN   B HA   1 
ATOM   4923 H  HB2  . ASN   B 1 59  ? 61.324 -16.938 2.936   1.00 18.35 ?  59  ASN   B HB2  1 
ATOM   4924 H  HB3  . ASN   B 1 59  ? 61.232 -15.362 3.109   1.00 18.35 ?  59  ASN   B HB3  1 
ATOM   4925 H  HD21 . ASN   B 1 59  ? 60.264 -15.595 6.225   1.00 20.66 ?  59  ASN   B HD21 1 
ATOM   4926 H  HD22 . ASN   B 1 59  ? 61.138 -14.922 5.224   1.00 20.66 ?  59  ASN   B HD22 1 
ATOM   4927 N  N    . ALA   B 1 60  ? 59.002 -14.084 0.776   1.00 13.23 ?  60  ALA   B N    1 
ATOM   4928 C  CA   . ALA   B 1 60  ? 58.407 -12.751 0.700   1.00 13.09 ?  60  ALA   B CA   1 
ATOM   4929 C  C    . ALA   B 1 60  ? 56.937 -12.774 1.096   1.00 12.40 ?  60  ALA   B C    1 
ATOM   4930 O  O    . ALA   B 1 60  ? 56.431 -11.823 1.707   1.00 12.91 ?  60  ALA   B O    1 
ATOM   4931 C  CB   . ALA   B 1 60  ? 58.572 -12.175 -0.705  1.00 13.74 ?  60  ALA   B CB   1 
ATOM   4932 H  H    . ALA   B 1 60  ? 59.293 -14.397 0.030   1.00 15.86 ?  60  ALA   B H    1 
ATOM   4933 H  HA   . ALA   B 1 60  ? 58.868 -12.168 1.318   1.00 15.69 ?  60  ALA   B HA   1 
ATOM   4934 H  HB1  . ALA   B 1 60  ? 58.172 -11.295 -0.734  1.00 16.47 ?  60  ALA   B HB1  1 
ATOM   4935 H  HB2  . ALA   B 1 60  ? 59.520 -12.117 -0.912  1.00 16.47 ?  60  ALA   B HB2  1 
ATOM   4936 H  HB3  . ALA   B 1 60  ? 58.133 -12.762 -1.342  1.00 16.47 ?  60  ALA   B HB3  1 
ATOM   4937 N  N    . MET   B 1 61  ? 56.232 -13.853 0.755   1.00 11.80 ?  61  MET   B N    1 
ATOM   4938 C  CA   . MET   B 1 61  ? 54.837 -13.980 1.155   1.00 11.29 ?  61  MET   B CA   1 
ATOM   4939 C  C    . MET   B 1 61  ? 54.697 -13.988 2.678   1.00 11.68 ?  61  MET   B C    1 
ATOM   4940 O  O    . MET   B 1 61  ? 53.800 -13.337 3.229   1.00 11.49 ?  61  MET   B O    1 
ATOM   4941 C  CB   . MET   B 1 61  ? 54.258 -15.253 0.532   1.00 11.23 ?  61  MET   B CB   1 
ATOM   4942 C  CG   . MET   B 1 61  ? 52.814 -15.536 0.942   1.00 11.33 ?  61  MET   B CG   1 
ATOM   4943 S  SD   . MET   B 1 61  ? 52.174 -17.043 0.177   1.00 11.76 ?  61  MET   B SD   1 
ATOM   4944 C  CE   . MET   B 1 61  ? 51.902 -16.455 -1.492  1.00 13.27 ?  61  MET   B CE   1 
ATOM   4945 H  H    . MET   B 1 61  ? 56.535 -14.526 0.303   1.00 14.15 ?  61  MET   B H    1 
ATOM   4946 H  HA   . MET   B 1 61  ? 54.338 -13.230 0.795   1.00 13.54 ?  61  MET   B HA   1 
ATOM   4947 H  HB2  . MET   B 1 61  ? 54.273 -15.169 -0.437  1.00 13.46 ?  61  MET   B HB2  1 
ATOM   4948 H  HB3  . MET   B 1 61  ? 54.793 -16.012 0.803   1.00 13.46 ?  61  MET   B HB3  1 
ATOM   4949 H  HG2  . MET   B 1 61  ? 52.767 -15.653 1.906   1.00 13.58 ?  61  MET   B HG2  1 
ATOM   4950 H  HG3  . MET   B 1 61  ? 52.249 -14.792 0.673   1.00 13.58 ?  61  MET   B HG3  1 
ATOM   4951 H  HE1  . MET   B 1 61  ? 51.519 -17.171 -2.022  1.00 15.90 ?  61  MET   B HE1  1 
ATOM   4952 H  HE2  . MET   B 1 61  ? 51.282 -15.701 -1.467  1.00 15.90 ?  61  MET   B HE2  1 
ATOM   4953 H  HE3  . MET   B 1 61  ? 52.744 -16.171 -1.873  1.00 15.90 ?  61  MET   B HE3  1 
ATOM   4954 N  N    . GLN   B 1 62  ? 55.581 -14.702 3.379   1.00 11.56 ?  62  GLN   B N    1 
ATOM   4955 C  CA   . GLN   B 1 62  ? 55.475 -14.764 4.833   1.00 11.74 ?  62  GLN   B CA   1 
ATOM   4956 C  C    . GLN   B 1 62  ? 55.759 -13.408 5.466   1.00 12.17 ?  62  GLN   B C    1 
ATOM   4957 O  O    . GLN   B 1 62  ? 55.075 -13.005 6.413   1.00 12.56 ?  62  GLN   B O    1 
ATOM   4958 C  CB   . GLN   B 1 62  ? 56.428 -15.819 5.396   1.00 12.21 ?  62  GLN   B CB   1 
ATOM   4959 C  CG   . GLN   B 1 62  ? 56.208 -16.088 6.875   1.00 12.46 ?  62  GLN   B CG   1 
ATOM   4960 C  CD   . GLN   B 1 62  ? 54.836 -16.681 7.124   1.00 12.18 ?  62  GLN   B CD   1 
ATOM   4961 O  OE1  . GLN   B 1 62  ? 54.580 -17.832 6.765   1.00 12.60 ?  62  GLN   B OE1  1 
ATOM   4962 N  NE2  . GLN   B 1 62  ? 53.927 -15.890 7.689   1.00 12.47 ?  62  GLN   B NE2  1 
ATOM   4963 H  H    . GLN   B 1 62  ? 56.231 -15.153 3.038   1.00 13.86 ?  62  GLN   B H    1 
ATOM   4964 H  HA   . GLN   B 1 62  ? 54.568 -15.021 5.064   1.00 14.07 ?  62  GLN   B HA   1 
ATOM   4965 H  HB2  . GLN   B 1 62  ? 56.298 -16.653 4.919   1.00 14.63 ?  62  GLN   B HB2  1 
ATOM   4966 H  HB3  . GLN   B 1 62  ? 57.341 -15.511 5.279   1.00 14.63 ?  62  GLN   B HB3  1 
ATOM   4967 H  HG2  . GLN   B 1 62  ? 56.877 -16.721 7.185   1.00 14.94 ?  62  GLN   B HG2  1 
ATOM   4968 H  HG3  . GLN   B 1 62  ? 56.281 -15.256 7.369   1.00 14.94 ?  62  GLN   B HG3  1 
ATOM   4969 H  HE21 . GLN   B 1 62  ? 54.136 -15.089 7.917   1.00 14.95 ?  62  GLN   B HE21 1 
ATOM   4970 H  HE22 . GLN   B 1 62  ? 53.135 -16.189 7.841   1.00 14.95 ?  62  GLN   B HE22 1 
ATOM   4971 N  N    . VAL   B 1 63  ? 56.775 -12.695 4.976   1.00 12.88 ?  63  VAL   B N    1 
ATOM   4972 C  CA   . VAL   B 1 63  ? 57.081 -11.377 5.529   1.00 13.55 ?  63  VAL   B CA   1 
ATOM   4973 C  C    . VAL   B 1 63  ? 55.887 -10.443 5.352   1.00 12.83 ?  63  VAL   B C    1 
ATOM   4974 O  O    . VAL   B 1 63  ? 55.475 -9.739  6.286   1.00 13.62 ?  63  VAL   B O    1 
ATOM   4975 C  CB   . VAL   B 1 63  ? 58.369 -10.819 4.899   1.00 15.08 ?  63  VAL   B CB   1 
ATOM   4976 C  CG1  . VAL   B 1 63  ? 58.599 -9.384  5.348   1.00 15.63 ?  63  VAL   B CG1  1 
ATOM   4977 C  CG2  . VAL   B 1 63  ? 59.545 -11.693 5.291   1.00 15.25 ?  63  VAL   B CG2  1 
ATOM   4978 H  H    . VAL   B 1 63  ? 57.282 -12.947 4.325   1.00 15.43 ?  63  VAL   B H    1 
ATOM   4979 H  HA   . VAL   B 1 63  ? 57.238 -11.477 6.476   1.00 16.25 ?  63  VAL   B HA   1 
ATOM   4980 H  HB   . VAL   B 1 63  ? 58.295 -10.834 3.932   1.00 18.07 ?  63  VAL   B HB   1 
ATOM   4981 H  HG11 . VAL   B 1 63  ? 59.516 -9.141  5.159   1.00 18.74 ?  63  VAL   B HG11 1 
ATOM   4982 H  HG12 . VAL   B 1 63  ? 57.992 -8.805  4.866   1.00 18.74 ?  63  VAL   B HG12 1 
ATOM   4983 H  HG13 . VAL   B 1 63  ? 58.431 -9.328  6.303   1.00 18.74 ?  63  VAL   B HG13 1 
ATOM   4984 H  HG21 . VAL   B 1 63  ? 60.357 -11.320 4.913   1.00 18.28 ?  63  VAL   B HG21 1 
ATOM   4985 H  HG22 . VAL   B 1 63  ? 59.614 -11.712 6.262   1.00 18.28 ?  63  VAL   B HG22 1 
ATOM   4986 H  HG23 . VAL   B 1 63  ? 59.404 -12.590 4.955   1.00 18.28 ?  63  VAL   B HG23 1 
ATOM   4987 N  N    . GLU   B 1 64  ? 55.318 -10.424 4.145   1.00 12.46 ?  64  GLU   B N    1 
ATOM   4988 C  CA   . GLU   B 1 64  ? 54.148 -9.592  3.872   1.00 12.14 ?  64  GLU   B CA   1 
ATOM   4989 C  C    . GLU   B 1 64  ? 52.968 -9.997  4.750   1.00 11.73 ?  64  GLU   B C    1 
ATOM   4990 O  O    . GLU   B 1 64  ? 52.222 -9.140  5.254   1.00 12.25 ?  64  GLU   B O    1 
ATOM   4991 C  CB   . GLU   B 1 64  ? 53.787 -9.740  2.392   1.00 12.36 ?  64  GLU   B CB   1 
ATOM   4992 C  CG   . GLU   B 1 64  ? 52.524 -9.011  1.952   1.00 12.67 ?  64  GLU   B CG   1 
ATOM   4993 C  CD   . GLU   B 1 64  ? 51.990 -9.511  0.620   1.00 12.96 ?  64  GLU   B CD   1 
ATOM   4994 O  OE1  . GLU   B 1 64  ? 52.170 -10.722 0.304   1.00 13.74 ?  64  GLU   B OE1  1 
ATOM   4995 O  OE2  . GLU   B 1 64  ? 51.368 -8.693  -0.103  1.00 13.98 -1 64  GLU   B OE2  1 
ATOM   4996 H  H    . GLU   B 1 64  ? 55.591 -10.886 3.465   1.00 14.94 ?  64  GLU   B H    1 
ATOM   4997 H  HA   . GLU   B 1 64  ? 54.364 -8.664  4.046   1.00 14.55 ?  64  GLU   B HA   1 
ATOM   4998 H  HB2  . GLU   B 1 64  ? 54.518 -9.388  1.856   1.00 14.81 ?  64  GLU   B HB2  1 
ATOM   4999 H  HB3  . GLU   B 1 64  ? 53.662 -10.676 2.196   1.00 14.81 ?  64  GLU   B HB3  1 
ATOM   5000 H  HG2  . GLU   B 1 64  ? 51.824 -9.132  2.616   1.00 15.19 ?  64  GLU   B HG2  1 
ATOM   5001 H  HG3  . GLU   B 1 64  ? 52.721 -8.061  1.859   1.00 15.19 ?  64  GLU   B HG3  1 
ATOM   5002 N  N    . SER   B 1 65  ? 52.781 -11.305 4.929   1.00 11.32 ?  65  SER   B N    1 
ATOM   5003 C  CA   . SER   B 1 65  ? 51.676 -11.818 5.731   1.00 11.41 ?  65  SER   B CA   1 
ATOM   5004 C  C    . SER   B 1 65  ? 51.811 -11.417 7.194   1.00 11.75 ?  65  SER   B C    1 
ATOM   5005 O  O    . SER   B 1 65  ? 50.817 -11.045 7.833   1.00 12.04 ?  65  SER   B O    1 
ATOM   5006 C  CB   . SER   B 1 65  ? 51.604 -13.340 5.599   1.00 11.72 ?  65  SER   B CB   1 
ATOM   5007 O  OG   . SER   B 1 65  ? 51.248 -13.733 4.283   1.00 11.71 ?  65  SER   B OG   1 
ATOM   5008 H  H    . SER   B 1 65  ? 53.286 -11.924 4.600   1.00 13.57 ?  65  SER   B H    1 
ATOM   5009 H  HA   . SER   B 1 65  ? 50.843 -11.448 5.396   1.00 13.68 ?  65  SER   B HA   1 
ATOM   5010 H  HB2  . SER   B 1 65  ? 52.468 -13.715 5.815   1.00 14.05 ?  65  SER   B HB2  1 
ATOM   5011 H  HB3  . SER   B 1 65  ? 50.934 -13.675 6.220   1.00 14.05 ?  65  SER   B HB3  1 
ATOM   5012 H  HG   . SER   B 1 65  ? 51.814 -13.442 3.733   1.00 14.04 ?  65  SER   B HG   1 
ATOM   5013 N  N    . ASP   B 1 66  ? 53.022 -11.510 7.755   1.00 12.00 ?  66  ASP   B N    1 
ATOM   5014 C  CA   . ASP   B 1 66  ? 53.211 -11.120 9.150   1.00 12.31 ?  66  ASP   B CA   1 
ATOM   5015 C  C    . ASP   B 1 66  ? 52.899 -9.641  9.351   1.00 12.58 ?  66  ASP   B C    1 
ATOM   5016 O  O    . ASP   B 1 66  ? 52.320 -9.253  10.373  1.00 13.18 ?  66  ASP   B O    1 
ATOM   5017 C  CB   . ASP   B 1 66  ? 54.642 -11.427 9.600   1.00 13.55 ?  66  ASP   B CB   1 
ATOM   5018 C  CG   . ASP   B 1 66  ? 54.914 -12.920 9.757   1.00 15.52 ?  66  ASP   B CG   1 
ATOM   5019 O  OD1  . ASP   B 1 66  ? 53.967 -13.731 9.679   1.00 16.18 ?  66  ASP   B OD1  1 
ATOM   5020 O  OD2  . ASP   B 1 66  ? 56.092 -13.282 9.968   1.00 18.16 -1 66  ASP   B OD2  1 
ATOM   5021 H  H    . ASP   B 1 66  ? 53.725 -11.803 7.363   1.00 14.39 ?  66  ASP   B H    1 
ATOM   5022 H  HA   . ASP   B 1 66  ? 52.608 -11.627 9.713   1.00 14.75 ?  66  ASP   B HA   1 
ATOM   5023 H  HB2  . ASP   B 1 66  ? 55.262 -11.083 8.940   1.00 16.25 ?  66  ASP   B HB2  1 
ATOM   5024 H  HB3  . ASP   B 1 66  ? 54.803 -10.996 10.458  1.00 16.25 ?  66  ASP   B HB3  1 
ATOM   5025 N  N    . ASP   B 1 67  ? 53.272 -8.798  8.386   1.00 12.07 ?  67  ASP   B N    1 
ATOM   5026 C  CA   . ASP   B 1 67  ? 52.921 -7.385  8.470   1.00 12.54 ?  67  ASP   B CA   1 
ATOM   5027 C  C    . ASP   B 1 67  ? 51.408 -7.182  8.391   1.00 12.90 ?  67  ASP   B C    1 
ATOM   5028 O  O    . ASP   B 1 67  ? 50.842 -6.383  9.146   1.00 13.72 ?  67  ASP   B O    1 
ATOM   5029 C  CB   . ASP   B 1 67  ? 53.632 -6.617  7.362   1.00 13.98 ?  67  ASP   B CB   1 
ATOM   5030 C  CG   . ASP   B 1 67  ? 53.202 -5.173  7.312   1.00 15.39 ?  67  ASP   B CG   1 
ATOM   5031 O  OD1  . ASP   B 1 67  ? 53.703 -4.356  8.122   1.00 16.51 ?  67  ASP   B OD1  1 
ATOM   5032 O  OD2  . ASP   B 1 67  ? 52.328 -4.871  6.482   1.00 16.28 -1 67  ASP   B OD2  1 
ATOM   5033 H  H    . ASP   B 1 67  ? 53.726 -9.016  7.689   1.00 14.47 ?  67  ASP   B H    1 
ATOM   5034 H  HA   . ASP   B 1 67  ? 53.225 -7.032  9.320   1.00 15.04 ?  67  ASP   B HA   1 
ATOM   5035 H  HB2  . ASP   B 1 67  ? 54.589 -6.642  7.520   1.00 16.76 ?  67  ASP   B HB2  1 
ATOM   5036 H  HB3  . ASP   B 1 67  ? 53.430 -7.035  6.505   1.00 16.76 ?  67  ASP   B HB3  1 
ATOM   5037 N  N    . TYR   B 1 68  ? 50.731 -7.914  7.501   1.00 12.48 ?  68  TYR   B N    1 
ATOM   5038 C  CA   . TYR   B 1 68  ? 49.274 -7.841  7.434   1.00 13.02 ?  68  TYR   B CA   1 
ATOM   5039 C  C    . TYR   B 1 68  ? 48.646 -8.180  8.783   1.00 12.74 ?  68  TYR   B C    1 
ATOM   5040 O  O    . TYR   B 1 68  ? 47.715 -7.502  9.238   1.00 13.58 ?  68  TYR   B O    1 
ATOM   5041 C  CB   . TYR   B 1 68  ? 48.741 -8.778  6.338   1.00 13.88 ?  68  TYR   B CB   1 
ATOM   5042 C  CG   . TYR   B 1 68  ? 47.236 -8.931  6.398   1.00 14.63 ?  68  TYR   B CG   1 
ATOM   5043 C  CD1  . TYR   B 1 68  ? 46.649 -9.880  7.228   1.00 15.55 ?  68  TYR   B CD1  1 
ATOM   5044 C  CD2  . TYR   B 1 68  ? 46.405 -8.101  5.664   1.00 15.63 ?  68  TYR   B CD2  1 
ATOM   5045 C  CE1  . TYR   B 1 68  ? 45.286 -10.000 7.324   1.00 16.45 ?  68  TYR   B CE1  1 
ATOM   5046 C  CE2  . TYR   B 1 68  ? 45.021 -8.225  5.746   1.00 16.05 ?  68  TYR   B CE2  1 
ATOM   5047 C  CZ   . TYR   B 1 68  ? 44.483 -9.171  6.582   1.00 16.35 ?  68  TYR   B CZ   1 
ATOM   5048 O  OH   . TYR   B 1 68  ? 43.119 -9.287  6.679   1.00 17.81 ?  68  TYR   B OH   1 
ATOM   5049 H  H    . TYR   B 1 68  ? 51.090 -8.467  6.937   1.00 14.96 ?  68  TYR   B H    1 
ATOM   5050 H  HA   . TYR   B 1 68  ? 49.022 -6.937  7.208   1.00 15.61 ?  68  TYR   B HA   1 
ATOM   5051 H  HB2  . TYR   B 1 68  ? 48.967 -8.409  5.471   1.00 16.64 ?  68  TYR   B HB2  1 
ATOM   5052 H  HB3  . TYR   B 1 68  ? 49.135 -9.655  6.445   1.00 16.64 ?  68  TYR   B HB3  1 
ATOM   5053 H  HD1  . TYR   B 1 68  ? 47.192 -10.440 7.737   1.00 18.65 ?  68  TYR   B HD1  1 
ATOM   5054 H  HD2  . TYR   B 1 68  ? 46.779 -7.453  5.116   1.00 18.74 ?  68  TYR   B HD2  1 
ATOM   5055 H  HE1  . TYR   B 1 68  ? 44.908 -10.651 7.875   1.00 19.73 ?  68  TYR   B HE1  1 
ATOM   5056 H  HE2  . TYR   B 1 68  ? 44.465 -7.665  5.253   1.00 19.25 ?  68  TYR   B HE2  1 
ATOM   5057 H  HH   . TYR   B 1 68  ? 42.731 -8.740  6.165   1.00 21.36 ?  68  TYR   B HH   1 
ATOM   5058 N  N    . ILE   B 1 69  ? 49.128 -9.250  9.427   1.00 12.56 ?  69  ILE   B N    1 
ATOM   5059 C  CA   . ILE   B 1 69  ? 48.576 -9.676  10.711  1.00 13.32 ?  69  ILE   B CA   1 
ATOM   5060 C  C    . ILE   B 1 69  ? 48.823 -8.627  11.786  1.00 12.88 ?  69  ILE   B C    1 
ATOM   5061 O  O    . ILE   B 1 69  ? 47.951 -8.352  12.617  1.00 13.18 ?  69  ILE   B O    1 
ATOM   5062 C  CB   . ILE   B 1 69  ? 49.156 -11.049 11.103  1.00 13.91 ?  69  ILE   B CB   1 
ATOM   5063 C  CG1  . ILE   B 1 69  ? 48.619 -12.152 10.181  1.00 14.41 ?  69  ILE   B CG1  1 
ATOM   5064 C  CG2  . ILE   B 1 69  ? 48.874 -11.358 12.567  1.00 14.84 ?  69  ILE   B CG2  1 
ATOM   5065 C  CD1  . ILE   B 1 69  ? 47.138 -12.457 10.347  1.00 14.44 ?  69  ILE   B CD1  1 
ATOM   5066 H  H    . ILE   B 1 69  ? 49.770 -9.743  9.146   1.00 15.05 ?  69  ILE   B H    1 
ATOM   5067 H  HA   . ILE   B 1 69  ? 47.616 -9.776  10.621  1.00 15.96 ?  69  ILE   B HA   1 
ATOM   5068 H  HB   . ILE   B 1 69  ? 50.118 -11.005 10.991  1.00 16.68 ?  69  ILE   B HB   1 
ATOM   5069 H  HG12 . ILE   B 1 69  ? 48.766 -11.879 9.260   1.00 17.28 ?  69  ILE   B HG12 1 
ATOM   5070 H  HG13 . ILE   B 1 69  ? 49.113 -12.968 10.359  1.00 17.28 ?  69  ILE   B HG13 1 
ATOM   5071 H  HG21 . ILE   B 1 69  ? 49.010 -12.307 12.716  1.00 17.79 ?  69  ILE   B HG21 1 
ATOM   5072 H  HG22 . ILE   B 1 69  ? 49.486 -10.849 13.124  1.00 17.79 ?  69  ILE   B HG22 1 
ATOM   5073 H  HG23 . ILE   B 1 69  ? 47.958 -11.118 12.771  1.00 17.79 ?  69  ILE   B HG23 1 
ATOM   5074 H  HD11 . ILE   B 1 69  ? 46.904 -13.181 9.749   1.00 17.31 ?  69  ILE   B HD11 1 
ATOM   5075 H  HD12 . ILE   B 1 69  ? 46.970 -12.716 11.264  1.00 17.31 ?  69  ILE   B HD12 1 
ATOM   5076 H  HD13 . ILE   B 1 69  ? 46.626 -11.665 10.124  1.00 17.31 ?  69  ILE   B HD13 1 
ATOM   5077 N  N    . ALA   B 1 70  ? 50.015 -8.035  11.806  1.00 13.03 ?  70  ALA   B N    1 
ATOM   5078 C  CA   . ALA   B 1 70  ? 50.297 -7.000  12.796  1.00 12.83 ?  70  ALA   B CA   1 
ATOM   5079 C  C    . ALA   B 1 70  ? 49.302 -5.855  12.684  1.00 13.19 ?  70  ALA   B C    1 
ATOM   5080 O  O    . ALA   B 1 70  ? 48.858 -5.308  13.698  1.00 13.75 ?  70  ALA   B O    1 
ATOM   5081 C  CB   . ALA   B 1 70  ? 51.726 -6.490  12.625  1.00 13.49 ?  70  ALA   B CB   1 
ATOM   5082 H  H    . ALA   B 1 70  ? 50.655 -8.209  11.271  1.00 15.62 ?  70  ALA   B H    1 
ATOM   5083 H  HA   . ALA   B 1 70  ? 50.217 -7.379  13.686  1.00 15.39 ?  70  ALA   B HA   1 
ATOM   5084 H  HB1  . ALA   B 1 70  ? 51.909 -5.823  13.307  1.00 16.17 ?  70  ALA   B HB1  1 
ATOM   5085 H  HB2  . ALA   B 1 70  ? 52.341 -7.234  12.721  1.00 16.17 ?  70  ALA   B HB2  1 
ATOM   5086 H  HB3  . ALA   B 1 70  ? 51.820 -6.096  11.744  1.00 16.17 ?  70  ALA   B HB3  1 
ATOM   5087 N  N    . THR   B 1 71  ? 48.929 -5.492  11.460  1.00 13.64 ?  71  THR   B N    1 
ATOM   5088 C  CA   . THR   B 1 71  ? 48.033 -4.361  11.245  1.00 14.75 ?  71  THR   B CA   1 
ATOM   5089 C  C    . THR   B 1 71  ? 46.567 -4.731  11.453  1.00 15.38 ?  71  THR   B C    1 
ATOM   5090 O  O    . THR   B 1 71  ? 45.786 -3.912  11.959  1.00 16.74 ?  71  THR   B O    1 
ATOM   5091 C  CB   . THR   B 1 71  ? 48.245 -3.801  9.835   1.00 16.51 ?  71  THR   B CB   1 
ATOM   5092 O  OG1  . THR   B 1 71  ? 49.568 -3.261  9.729   1.00 18.58 ?  71  THR   B OG1  1 
ATOM   5093 C  CG2  . THR   B 1 71  ? 47.215 -2.719  9.505   1.00 17.82 ?  71  THR   B CG2  1 
ATOM   5094 H  H    . THR   B 1 71  ? 49.182 -5.882  10.738  1.00 16.35 ?  71  THR   B H    1 
ATOM   5095 H  HA   . THR   B 1 71  ? 48.250 -3.658  11.873  1.00 17.68 ?  71  THR   B HA   1 
ATOM   5096 H  HB   . THR   B 1 71  ? 48.153 -4.511  9.182   1.00 19.79 ?  71  THR   B HB   1 
ATOM   5097 H  HG1  . THR   B 1 71  ? 49.692 -2.930  8.960   1.00 22.28 ?  71  THR   B HG1  1 
ATOM   5098 H  HG21 . THR   B 1 71  ? 47.514 -2.192  8.744   1.00 21.37 ?  71  THR   B HG21 1 
ATOM   5099 H  HG22 . THR   B 1 71  ? 46.362 -3.124  9.287   1.00 21.37 ?  71  THR   B HG22 1 
ATOM   5100 H  HG23 . THR   B 1 71  ? 47.100 -2.126  10.265  1.00 21.37 ?  71  THR   B HG23 1 
ATOM   5101 N  N    . ASN   B 1 72  ? 46.171 -5.948  11.062  1.00 15.10 ?  72  ASN   B N    1 
ATOM   5102 C  CA   . ASN   B 1 72  ? 44.768 -6.313  10.936  1.00 15.55 ?  72  ASN   B CA   1 
ATOM   5103 C  C    . ASN   B 1 72  ? 44.298 -7.413  11.878  1.00 15.94 ?  72  ASN   B C    1 
ATOM   5104 O  O    . ASN   B 1 72  ? 43.080 -7.576  12.041  1.00 17.21 ?  72  ASN   B O    1 
ATOM   5105 C  CB   . ASN   B 1 72  ? 44.461 -6.739  9.492   1.00 16.55 ?  72  ASN   B CB   1 
ATOM   5106 C  CG   . ASN   B 1 72  ? 44.738 -5.639  8.499   1.00 17.52 ?  72  ASN   B CG   1 
ATOM   5107 O  OD1  . ASN   B 1 72  ? 45.754 -5.650  7.796   1.00 18.71 ?  72  ASN   B OD1  1 
ATOM   5108 N  ND2  . ASN   B 1 72  ? 43.860 -4.658  8.463   1.00 18.88 ?  72  ASN   B ND2  1 
ATOM   5109 H  H    . ASN   B 1 72  ? 46.716 -6.592  10.861  1.00 18.11 ?  72  ASN   B H    1 
ATOM   5110 H  HA   . ASN   B 1 72  ? 44.236 -5.528  11.122  1.00 18.64 ?  72  ASN   B HA   1 
ATOM   5111 H  HB2  . ASN   B 1 72  ? 45.021 -7.499  9.259   1.00 19.85 ?  72  ASN   B HB2  1 
ATOM   5112 H  HB3  . ASN   B 1 72  ? 43.527 -6.978  9.423   1.00 19.85 ?  72  ASN   B HB3  1 
ATOM   5113 H  HD21 . ASN   B 1 72  ? 43.964 -4.000  7.918   1.00 22.64 ?  72  ASN   B HD21 1 
ATOM   5114 H  HD22 . ASN   B 1 72  ? 43.165 -4.681  8.974   1.00 22.64 ?  72  ASN   B HD22 1 
ATOM   5115 N  N    . GLY   B 1 73  ? 45.204 -8.160  12.503  1.00 15.31 ?  73  GLY   B N    1 
ATOM   5116 C  CA   . GLY   B 1 73  ? 44.815 -9.306  13.290  1.00 14.65 ?  73  GLY   B CA   1 
ATOM   5117 C  C    . GLY   B 1 73  ? 44.448 -10.486 12.417  1.00 13.45 ?  73  GLY   B C    1 
ATOM   5118 O  O    . GLY   B 1 73  ? 44.439 -10.397 11.188  1.00 13.20 ?  73  GLY   B O    1 
ATOM   5119 H  H    . GLY   B 1 73  ? 46.056 -8.021  12.482  1.00 18.36 ?  73  GLY   B H    1 
ATOM   5120 H  HA2  . GLY   B 1 73  ? 45.548 -9.565  13.875  1.00 17.56 ?  73  GLY   B HA2  1 
ATOM   5121 H  HA3  . GLY   B 1 73  ? 44.050 -9.077  13.843  1.00 17.56 ?  73  GLY   B HA3  1 
ATOM   5122 N  N    . PRO   B 1 74  ? 44.140 -11.613 13.053  1.00 13.85 ?  74  PRO   B N    1 
ATOM   5123 C  CA   . PRO   B 1 74  ? 43.884 -12.846 12.306  1.00 13.27 ?  74  PRO   B CA   1 
ATOM   5124 C  C    . PRO   B 1 74  ? 42.585 -12.786 11.516  1.00 12.73 ?  74  PRO   B C    1 
ATOM   5125 O  O    . PRO   B 1 74  ? 41.641 -12.056 11.840  1.00 14.05 ?  74  PRO   B O    1 
ATOM   5126 C  CB   . PRO   B 1 74  ? 43.802 -13.908 13.409  1.00 14.19 ?  74  PRO   B CB   1 
ATOM   5127 C  CG   . PRO   B 1 74  ? 43.353 -13.156 14.616  1.00 15.68 ?  74  PRO   B CG   1 
ATOM   5128 C  CD   . PRO   B 1 74  ? 44.027 -11.815 14.507  1.00 15.29 ?  74  PRO   B CD   1 
ATOM   5129 H  HA   . PRO   B 1 74  ? 44.627 -13.043 11.711  1.00 15.91 ?  74  PRO   B HA   1 
ATOM   5130 H  HB2  . PRO   B 1 74  ? 43.154 -14.587 13.161  1.00 17.01 ?  74  PRO   B HB2  1 
ATOM   5131 H  HB3  . PRO   B 1 74  ? 44.677 -14.301 13.552  1.00 17.01 ?  74  PRO   B HB3  1 
ATOM   5132 H  HG2  . PRO   B 1 74  ? 42.385 -13.059 14.598  1.00 18.80 ?  74  PRO   B HG2  1 
ATOM   5133 H  HG3  . PRO   B 1 74  ? 43.636 -13.622 15.417  1.00 18.80 ?  74  PRO   B HG3  1 
ATOM   5134 H  HD2  . PRO   B 1 74  ? 43.469 -11.126 14.909  1.00 18.33 ?  74  PRO   B HD2  1 
ATOM   5135 H  HD3  . PRO   B 1 74  ? 44.904 -11.844 14.914  1.00 18.33 ?  74  PRO   B HD3  1 
ATOM   5136 N  N    . LEU   B 1 75  ? 42.554 -13.595 10.461  1.00 12.07 ?  75  LEU   B N    1 
ATOM   5137 C  CA   . LEU   B 1 75  ? 41.342 -13.812 9.695   1.00 12.18 ?  75  LEU   B CA   1 
ATOM   5138 C  C    . LEU   B 1 75  ? 40.366 -14.672 10.498  1.00 12.71 ?  75  LEU   B C    1 
ATOM   5139 O  O    . LEU   B 1 75  ? 40.706 -15.236 11.539  1.00 13.75 ?  75  LEU   B O    1 
ATOM   5140 C  CB   . LEU   B 1 75  ? 41.671 -14.524 8.383   1.00 12.13 ?  75  LEU   B CB   1 
ATOM   5141 C  CG   . LEU   B 1 75  ? 42.522 -13.777 7.349   1.00 13.94 ?  75  LEU   B CG   1 
ATOM   5142 C  CD1  . LEU   B 1 75  ? 42.752 -14.631 6.102   1.00 15.33 ?  75  LEU   B CD1  1 
ATOM   5143 C  CD2  . LEU   B 1 75  ? 41.916 -12.451 6.976   1.00 17.13 ?  75  LEU   B CD2  1 
ATOM   5144 H  H    . LEU   B 1 75  ? 43.232 -14.038 10.169  1.00 14.47 ?  75  LEU   B H    1 
ATOM   5145 H  HA   . LEU   B 1 75  ? 40.921 -12.962 9.494   1.00 14.60 ?  75  LEU   B HA   1 
ATOM   5146 H  HB2  . LEU   B 1 75  ? 42.145 -15.344 8.596   1.00 14.54 ?  75  LEU   B HB2  1 
ATOM   5147 H  HB3  . LEU   B 1 75  ? 40.834 -14.750 7.945   1.00 14.54 ?  75  LEU   B HB3  1 
ATOM   5148 H  HG   . LEU   B 1 75  ? 43.393 -13.600 7.737   1.00 16.71 ?  75  LEU   B HG   1 
ATOM   5149 H  HD11 . LEU   B 1 75  ? 43.298 -14.130 5.469   1.00 18.38 ?  75  LEU   B HD11 1 
ATOM   5150 H  HD12 . LEU   B 1 75  ? 43.213 -15.447 6.353   1.00 18.38 ?  75  LEU   B HD12 1 
ATOM   5151 H  HD13 . LEU   B 1 75  ? 41.897 -14.844 5.697   1.00 18.38 ?  75  LEU   B HD13 1 
ATOM   5152 H  HD21 . LEU   B 1 75  ? 42.442 -12.054 6.265   1.00 20.54 ?  75  LEU   B HD21 1 
ATOM   5153 H  HD22 . LEU   B 1 75  ? 41.007 -12.596 6.677   1.00 20.54 ?  75  LEU   B HD22 1 
ATOM   5154 H  HD23 . LEU   B 1 75  ? 41.924 -11.875 7.756   1.00 20.54 ?  75  LEU   B HD23 1 
ATOM   5155 N  N    . LYS   B 1 76  ? 39.131 -14.748 10.005  1.00 13.66 ?  76  LYS   B N    1 
ATOM   5156 C  CA   . LYS   B 1 76  ? 38.142 -15.710 10.476  1.00 15.06 ?  76  LYS   B CA   1 
ATOM   5157 C  C    . LYS   B 1 76  ? 38.241 -16.987 9.644   1.00 13.56 ?  76  LYS   B C    1 
ATOM   5158 O  O    . LYS   B 1 76  ? 38.511 -16.935 8.445   1.00 13.46 ?  76  LYS   B O    1 
ATOM   5159 C  CB   . LYS   B 1 76  ? 36.727 -15.143 10.275  1.00 17.12 ?  76  LYS   B CB   1 
ATOM   5160 C  CG   . LYS   B 1 76  ? 36.428 -13.780 10.924  1.00 18.99 ?  76  LYS   B CG   1 
ATOM   5161 C  CD   . LYS   B 1 76  ? 35.045 -13.232 10.526  1.00 20.35 ?  76  LYS   B CD   1 
ATOM   5162 C  CE   . LYS   B 1 76  ? 34.772 -11.876 11.158  1.00 22.41 ?  76  LYS   B CE   1 
ATOM   5163 N  NZ   . LYS   B 1 76  ? 33.471 -11.287 10.733  1.00 23.08 ?  76  LYS   B NZ   1 
ATOM   5164 H  H    . LYS   B 1 76  ? 38.837 -14.239 9.379   1.00 16.37 ?  76  LYS   B H    1 
ATOM   5165 H  HA   . LYS   B 1 76  ? 38.283 -15.920 11.414  1.00 18.05 ?  76  LYS   B HA   1 
ATOM   5166 H  HB2  . LYS   B 1 76  ? 36.573 -15.048 9.321   1.00 20.53 ?  76  LYS   B HB2  1 
ATOM   5167 H  HB3  . LYS   B 1 76  ? 36.091 -15.779 10.638  1.00 20.53 ?  76  LYS   B HB3  1 
ATOM   5168 H  HG2  . LYS   B 1 76  ? 36.450 -13.878 11.888  1.00 22.78 ?  76  LYS   B HG2  1 
ATOM   5169 H  HG3  . LYS   B 1 76  ? 37.102 -13.141 10.639  1.00 22.78 ?  76  LYS   B HG3  1 
ATOM   5170 H  HD2  . LYS   B 1 76  ? 35.010 -13.131 9.560   1.00 24.40 ?  76  LYS   B HD2  1 
ATOM   5171 H  HD3  . LYS   B 1 76  ? 34.361 -13.851 10.822  1.00 24.40 ?  76  LYS   B HD3  1 
ATOM   5172 H  HE2  . LYS   B 1 76  ? 34.755 -11.977 12.121  1.00 26.88 ?  76  LYS   B HE2  1 
ATOM   5173 H  HE3  . LYS   B 1 76  ? 35.477 -11.262 10.900  1.00 26.88 ?  76  LYS   B HE3  1 
ATOM   5174 H  HZ1  . LYS   B 1 76  ? 33.349 -10.495 11.125  1.00 27.68 ?  76  LYS   B HZ1  1 
ATOM   5175 H  HZ2  . LYS   B 1 76  ? 33.457 -11.173 9.849   1.00 27.68 ?  76  LYS   B HZ2  1 
ATOM   5176 H  HZ3  . LYS   B 1 76  ? 32.799 -11.826 10.963  1.00 27.68 ?  76  LYS   B HZ3  1 
ATOM   5177 N  N    . VAL   B 1 77  ? 38.002 -18.143 10.276  1.00 14.48 ?  77  VAL   B N    1 
ATOM   5178 C  CA   . VAL   B 1 77  ? 37.802 -19.356 9.490   1.00 14.37 ?  77  VAL   B CA   1 
ATOM   5179 C  C    . VAL   B 1 77  ? 36.607 -19.125 8.575   1.00 13.18 ?  77  VAL   B C    1 
ATOM   5180 O  O    . VAL   B 1 77  ? 35.543 -18.680 9.023   1.00 13.34 ?  77  VAL   B O    1 
ATOM   5181 C  CB   . VAL   B 1 77  ? 37.603 -20.581 10.397  1.00 15.93 ?  77  VAL   B CB   1 
ATOM   5182 C  CG1  . VAL   B 1 77  ? 37.333 -21.814 9.545   1.00 16.40 ?  77  VAL   B CG1  1 
ATOM   5183 C  CG2  . VAL   B 1 77  ? 38.824 -20.799 11.290  1.00 17.20 ?  77  VAL   B CG2  1 
ATOM   5184 H  H    . VAL   B 1 77  ? 37.951 -18.243 11.123  1.00 17.37 ?  77  VAL   B H    1 
ATOM   5185 H  HA   . VAL   B 1 77  ? 38.579 -19.510 8.933   1.00 17.23 ?  77  VAL   B HA   1 
ATOM   5186 H  HB   . VAL   B 1 77  ? 36.830 -20.432 10.965  1.00 19.10 ?  77  VAL   B HB   1 
ATOM   5187 H  HG11 . VAL   B 1 77  ? 37.402 -22.601 10.106  1.00 19.66 ?  77  VAL   B HG11 1 
ATOM   5188 H  HG12 . VAL   B 1 77  ? 36.438 -21.754 9.171   1.00 19.66 ?  77  VAL   B HG12 1 
ATOM   5189 H  HG13 . VAL   B 1 77  ? 37.988 -21.855 8.833   1.00 19.66 ?  77  VAL   B HG13 1 
ATOM   5190 H  HG21 . VAL   B 1 77  ? 38.684 -21.597 11.819  1.00 20.62 ?  77  VAL   B HG21 1 
ATOM   5191 H  HG22 . VAL   B 1 77  ? 39.606 -20.901 10.729  1.00 20.62 ?  77  VAL   B HG22 1 
ATOM   5192 H  HG23 . VAL   B 1 77  ? 38.927 -20.028 11.870  1.00 20.62 ?  77  VAL   B HG23 1 
ATOM   5193 N  N    . GLY   B 1 78  ? 36.782 -19.401 7.284   1.00 12.56 ?  78  GLY   B N    1 
ATOM   5194 C  CA   . GLY   B 1 78  ? 35.799 -19.081 6.273   1.00 12.36 ?  78  GLY   B CA   1 
ATOM   5195 C  C    . GLY   B 1 78  ? 36.043 -17.764 5.572   1.00 11.76 ?  78  GLY   B C    1 
ATOM   5196 O  O    . GLY   B 1 78  ? 35.358 -17.477 4.585   1.00 12.14 ?  78  GLY   B O    1 
ATOM   5197 H  H    . GLY   B 1 78  ? 37.486 -19.781 6.965   1.00 15.05 ?  78  GLY   B H    1 
ATOM   5198 H  HA2  . GLY   B 1 78  ? 35.794 -19.779 5.601   1.00 14.81 ?  78  GLY   B HA2  1 
ATOM   5199 H  HA3  . GLY   B 1 78  ? 34.921 -19.045 6.680   1.00 14.81 ?  78  GLY   B HA3  1 
ATOM   5200 N  N    . GLY   B 1 79  ? 36.996 -16.962 6.051   1.00 11.91 ?  79  GLY   B N    1 
ATOM   5201 C  CA   . GLY   B 1 79  ? 37.284 -15.667 5.472   1.00 11.51 ?  79  GLY   B CA   1 
ATOM   5202 C  C    . GLY   B 1 79  ? 38.525 -15.682 4.587   1.00 11.11 ?  79  GLY   B C    1 
ATOM   5203 O  O    . GLY   B 1 79  ? 39.147 -16.713 4.340   1.00 11.50 ?  79  GLY   B O    1 
ATOM   5204 H  H    . GLY   B 1 79  ? 37.498 -17.153 6.719   1.00 14.28 ?  79  GLY   B H    1 
ATOM   5205 H  HA2  . GLY   B 1 79  ? 36.529 -15.374 4.932   1.00 13.80 ?  79  GLY   B HA2  1 
ATOM   5206 H  HA3  . GLY   B 1 79  ? 37.426 -15.018 6.175   1.00 13.80 ?  79  GLY   B HA3  1 
ATOM   5207 N  N    . SER   B 1 80  ? 38.887 -14.489 4.113   1.00 11.19 ?  80  SER   B N    1 
ATOM   5208 C  CA   . SER   B 1 80  ? 40.001 -14.352 3.184   1.00 10.91 ?  80  SER   B CA   1 
ATOM   5209 C  C    . SER   B 1 80  ? 40.577 -12.945 3.240   1.00 10.78 ?  80  SER   B C    1 
ATOM   5210 O  O    . SER   B 1 80  ? 39.958 -12.009 3.752   1.00 11.92 ?  80  SER   B O    1 
ATOM   5211 C  CB   . SER   B 1 80  ? 39.564 -14.636 1.742   1.00 11.18 ?  80  SER   B CB   1 
ATOM   5212 O  OG   . SER   B 1 80  ? 38.716 -13.612 1.247   1.00 12.30 ?  80  SER   B OG   1 
ATOM   5213 H  H    . SER   B 1 80  ? 38.510 -13.746 4.314   1.00 13.41 ?  80  SER   B H    1 
ATOM   5214 H  HA   . SER   B 1 80  ? 40.694 -14.986 3.425   1.00 13.07 ?  80  SER   B HA   1 
ATOM   5215 H  HB2  . SER   B 1 80  ? 40.347 -14.686 1.172   1.00 13.40 ?  80  SER   B HB2  1 
ATOM   5216 H  HB3  . SER   B 1 80  ? 39.083 -15.479 1.715   1.00 13.40 ?  80  SER   B HB3  1 
ATOM   5217 H  HG   . SER   B 1 80  ? 38.021 -13.555 1.728   1.00 14.74 ?  80  SER   B HG   1 
ATOM   5218 N  N    . CYS   B 1 81  ? 41.765 -12.801 2.656   1.00 10.55 ?  81  CYS   B N    1 
ATOM   5219 C  CA   . CYS   B 1 81  ? 42.307 -11.485 2.340   1.00 10.81 ?  81  CYS   B CA   1 
ATOM   5220 C  C    . CYS   B 1 81  ? 43.079 -11.573 1.033   1.00 10.10 ?  81  CYS   B C    1 
ATOM   5221 O  O    . CYS   B 1 81  ? 43.590 -12.635 0.660   1.00 11.06 ?  81  CYS   B O    1 
ATOM   5222 C  CB   . CYS   B 1 81  ? 43.207 -10.926 3.454   1.00 11.62 ?  81  CYS   B CB   1 
ATOM   5223 S  SG   . CYS   B 1 81  ? 44.724 -11.873 3.709   1.00 11.91 ?  81  CYS   B SG   1 
ATOM   5224 H  H    . CYS   B 1 81  ? 42.285 -13.455 2.427   1.00 12.65 ?  81  CYS   B H    1 
ATOM   5225 H  HA   . CYS   B 1 81  ? 41.572 -10.867 2.210   1.00 12.95 ?  81  CYS   B HA   1 
ATOM   5226 H  HB2  . CYS   B 1 81  ? 43.460 -10.016 3.231   1.00 13.92 ?  81  CYS   B HB2  1 
ATOM   5227 H  HB3  . CYS   B 1 81  ? 42.710 -10.930 4.290   1.00 13.92 ?  81  CYS   B HB3  1 
ATOM   5228 H  HG   . CYS   B 1 81  ? 45.361 -11.372 4.597   1.00 14.28 ?  81  CYS   B HG   1 
ATOM   5229 N  N    . VAL   B 1 82  ? 43.188 -10.429 0.358   1.00 10.46 ?  82  VAL   B N    1 
ATOM   5230 C  CA   . VAL   B 1 82  ? 43.951 -10.304 -0.883  1.00 10.86 ?  82  VAL   B CA   1 
ATOM   5231 C  C    . VAL   B 1 82  ? 45.292 -9.663  -0.561  1.00 10.95 ?  82  VAL   B C    1 
ATOM   5232 O  O    . VAL   B 1 82  ? 45.342 -8.544  -0.030  1.00 12.03 ?  82  VAL   B O    1 
ATOM   5233 C  CB   . VAL   B 1 82  ? 43.208 -9.459  -1.928  1.00 11.88 ?  82  VAL   B CB   1 
ATOM   5234 C  CG1  . VAL   B 1 82  ? 44.049 -9.310  -3.193  1.00 13.40 ?  82  VAL   B CG1  1 
ATOM   5235 C  CG2  . VAL   B 1 82  ? 41.848 -10.060 -2.243  1.00 12.79 ?  82  VAL   B CG2  1 
ATOM   5236 H  H    . VAL   B 1 82  ? 42.817 -9.688  0.599   1.00 12.54 ?  82  VAL   B H    1 
ATOM   5237 H  HA   . VAL   B 1 82  ? 44.108 -11.184 -1.259  1.00 13.01 ?  82  VAL   B HA   1 
ATOM   5238 H  HB   . VAL   B 1 82  ? 43.059 -8.573  -1.568  1.00 14.24 ?  82  VAL   B HB   1 
ATOM   5239 H  HG11 . VAL   B 1 82  ? 43.487 -8.985  -3.914  1.00 16.06 ?  82  VAL   B HG11 1 
ATOM   5240 H  HG12 . VAL   B 1 82  ? 44.766 -8.673  -3.027  1.00 16.06 ?  82  VAL   B HG12 1 
ATOM   5241 H  HG13 . VAL   B 1 82  ? 44.424 -10.172 -3.431  1.00 16.06 ?  82  VAL   B HG13 1 
ATOM   5242 H  HG21 . VAL   B 1 82  ? 41.415 -9.531  -2.932  1.00 15.33 ?  82  VAL   B HG21 1 
ATOM   5243 H  HG22 . VAL   B 1 82  ? 41.966 -10.973 -2.554  1.00 15.33 ?  82  VAL   B HG22 1 
ATOM   5244 H  HG23 . VAL   B 1 82  ? 41.304 -10.057 -1.437  1.00 15.33 ?  82  VAL   B HG23 1 
ATOM   5245 N  N    . LEU   B 1 83  ? 46.370 -10.352 -0.923  1.00 10.74 ?  83  LEU   B N    1 
ATOM   5246 C  CA   . LEU   B 1 83  ? 47.729 -9.834  -0.807  1.00 10.43 ?  83  LEU   B CA   1 
ATOM   5247 C  C    . LEU   B 1 83  ? 48.429 -9.977  -2.159  1.00 10.63 ?  83  LEU   B C    1 
ATOM   5248 O  O    . LEU   B 1 83  ? 47.828 -10.395 -3.152  1.00 10.47 ?  83  LEU   B O    1 
ATOM   5249 C  CB   . LEU   B 1 83  ? 48.478 -10.513 0.347   1.00 11.02 ?  83  LEU   B CB   1 
ATOM   5250 C  CG   . LEU   B 1 83  ? 47.972 -10.148 1.749   1.00 12.20 ?  83  LEU   B CG   1 
ATOM   5251 C  CD1  . LEU   B 1 83  ? 48.600 -11.022 2.813   1.00 12.84 ?  83  LEU   B CD1  1 
ATOM   5252 C  CD2  . LEU   B 1 83  ? 48.188 -8.673  2.073   1.00 13.21 ?  83  LEU   B CD2  1 
ATOM   5253 H  H    . LEU   B 1 83  ? 46.334 -11.151 -1.250  1.00 12.87 ?  83  LEU   B H    1 
ATOM   5254 H  HA   . LEU   B 1 83  ? 47.676 -8.891  -0.615  1.00 12.50 ?  83  LEU   B HA   1 
ATOM   5255 H  HB2  . LEU   B 1 83  ? 48.406 -11.470 0.241   1.00 13.21 ?  83  LEU   B HB2  1 
ATOM   5256 H  HB3  . LEU   B 1 83  ? 49.414 -10.249 0.292   1.00 13.21 ?  83  LEU   B HB3  1 
ATOM   5257 H  HG   . LEU   B 1 83  ? 47.018 -10.308 1.774   1.00 14.62 ?  83  LEU   B HG   1 
ATOM   5258 H  HD11 . LEU   B 1 83  ? 48.245 -10.770 3.681   1.00 15.40 ?  83  LEU   B HD11 1 
ATOM   5259 H  HD12 . LEU   B 1 83  ? 48.376 -11.952 2.627   1.00 15.40 ?  83  LEU   B HD12 1 
ATOM   5260 H  HD13 . LEU   B 1 83  ? 49.559 -10.906 2.798   1.00 15.40 ?  83  LEU   B HD13 1 
ATOM   5261 H  HD21 . LEU   B 1 83  ? 47.972 -8.522  3.007   1.00 15.84 ?  83  LEU   B HD21 1 
ATOM   5262 H  HD22 . LEU   B 1 83  ? 49.112 -8.443  1.903   1.00 15.84 ?  83  LEU   B HD22 1 
ATOM   5263 H  HD23 . LEU   B 1 83  ? 47.603 -8.139  1.510   1.00 15.84 ?  83  LEU   B HD23 1 
ATOM   5264 N  N    . SER   B 1 84  ? 49.704 -9.597  -2.214  1.00 11.51 ?  84  SER   B N    1 
ATOM   5265 C  CA   . SER   B 1 84  ? 50.436 -9.717  -3.467  1.00 11.60 ?  84  SER   B CA   1 
ATOM   5266 C  C    . SER   B 1 84  ? 50.588 -11.178 -3.881  1.00 10.64 ?  84  SER   B C    1 
ATOM   5267 O  O    . SER   B 1 84  ? 50.699 -12.077 -3.047  1.00 10.93 ?  84  SER   B O    1 
ATOM   5268 C  CB   . SER   B 1 84  ? 51.830 -9.113  -3.320  1.00 13.63 ?  84  SER   B CB   1 
ATOM   5269 O  OG   . SER   B 1 84  ? 52.574 -9.323  -4.506  1.00 15.14 ?  84  SER   B OG   1 
ATOM   5270 H  H    . SER   B 1 84  ? 50.152 -9.264  -1.560  1.00 13.80 ?  84  SER   B H    1 
ATOM   5271 H  HA   . SER   B 1 84  ? 49.966 -9.244  -4.171  1.00 13.90 ?  84  SER   B HA   1 
ATOM   5272 H  HB2  . SER   B 1 84  ? 51.749 -8.158  -3.156  1.00 16.34 ?  84  SER   B HB2  1 
ATOM   5273 H  HB3  . SER   B 1 84  ? 52.289 -9.539  -2.581  1.00 16.34 ?  84  SER   B HB3  1 
ATOM   5274 H  HG   . SER   B 1 84  ? 53.346 -8.981  -4.434  1.00 18.15 ?  84  SER   B HG   1 
ATOM   5275 N  N    . GLY   B 1 85  ? 50.655 -11.401 -5.188  1.00 11.95 ?  85  GLY   B N    1 
ATOM   5276 C  CA   . GLY   B 1 85  ? 51.003 -12.692 -5.728  1.00 12.53 ?  85  GLY   B CA   1 
ATOM   5277 C  C    . GLY   B 1 85  ? 52.473 -12.886 -6.033  1.00 11.87 ?  85  GLY   B C    1 
ATOM   5278 O  O    . GLY   B 1 85  ? 52.852 -13.962 -6.499  1.00 12.45 ?  85  GLY   B O    1 
ATOM   5279 H  H    . GLY   B 1 85  ? 50.514 -10.806 -5.789  1.00 14.32 ?  85  GLY   B H    1 
ATOM   5280 H  HA2  . GLY   B 1 85  ? 50.743 -13.381 -5.098  1.00 15.02 ?  85  GLY   B HA2  1 
ATOM   5281 H  HA3  . GLY   B 1 85  ? 50.518 -12.836 -6.550  1.00 15.02 ?  85  GLY   B HA3  1 
ATOM   5282 N  N    . HIS   B 1 86  ? 53.325 -11.887 -5.805  1.00 11.95 ?  86  HIS   B N    1 
ATOM   5283 C  CA   . HIS   B 1 86  ? 54.788 -12.055 -5.892  1.00 11.91 ?  86  HIS   B CA   1 
ATOM   5284 C  C    . HIS   B 1 86  ? 55.162 -12.561 -7.283  1.00 12.08 ?  86  HIS   B C    1 
ATOM   5285 O  O    . HIS   B 1 86  ? 54.764 -11.948 -8.286  1.00 13.07 ?  86  HIS   B O    1 
ATOM   5286 C  CB   . HIS   B 1 86  ? 55.281 -12.898 -4.717  1.00 12.69 ?  86  HIS   B CB   1 
ATOM   5287 C  CG   . HIS   B 1 86  ? 54.967 -12.295 -3.390  1.00 12.63 ?  86  HIS   B CG   1 
ATOM   5288 N  ND1  . HIS   B 1 86  ? 55.806 -11.401 -2.758  1.00 13.95 ?  86  HIS   B ND1  1 
ATOM   5289 C  CD2  . HIS   B 1 86  ? 53.881 -12.429 -2.592  1.00 12.94 ?  86  HIS   B CD2  1 
ATOM   5290 C  CE1  . HIS   B 1 86  ? 55.242 -11.010 -1.628  1.00 13.65 ?  86  HIS   B CE1  1 
ATOM   5291 N  NE2  . HIS   B 1 86  ? 54.075 -11.618 -1.504  1.00 13.01 ?  86  HIS   B NE2  1 
ATOM   5292 H  H    . HIS   B 1 86  ? 53.086 -11.089 -5.596  1.00 14.32 ?  86  HIS   B H    1 
ATOM   5293 H  HA   . HIS   B 1 86  ? 55.197 -11.181 -5.797  1.00 14.28 ?  86  HIS   B HA   1 
ATOM   5294 H  HB2  . HIS   B 1 86  ? 54.863 -13.772 -4.759  1.00 15.21 ?  86  HIS   B HB2  1 
ATOM   5295 H  HB3  . HIS   B 1 86  ? 56.246 -12.991 -4.778  1.00 15.21 ?  86  HIS   B HB3  1 
ATOM   5296 H  HD2  . HIS   B 1 86  ? 53.129 -12.956 -2.763  1.00 15.51 ?  86  HIS   B HD2  1 
ATOM   5297 H  HE1  . HIS   B 1 86  ? 55.614 -10.425 -1.010  1.00 16.37 ?  86  HIS   B HE1  1 
ATOM   5298 H  HE2  . HIS   B 1 86  ? 53.528 -11.531 -0.842  1.00 15.60 ?  86  HIS   B HE2  1 
ATOM   5299 N  N    . ASN   B 1 87  ? 55.925 -13.647 -7.394  1.00 12.67 ?  87  ASN   B N    1 
ATOM   5300 C  CA   . ASN   B 1 87  ? 56.321 -14.221 -8.670  1.00 13.44 ?  87  ASN   B CA   1 
ATOM   5301 C  C    . ASN   B 1 87  ? 55.339 -15.270 -9.169  1.00 13.06 ?  87  ASN   B C    1 
ATOM   5302 O  O    . ASN   B 1 87  ? 55.653 -15.984 -10.127 1.00 14.53 ?  87  ASN   B O    1 
ATOM   5303 C  CB   . ASN   B 1 87  ? 57.718 -14.840 -8.552  1.00 15.10 ?  87  ASN   B CB   1 
ATOM   5304 C  CG   . ASN   B 1 87  ? 57.775 -15.958 -7.518  1.00 15.98 ?  87  ASN   B CG   1 
ATOM   5305 O  OD1  . ASN   B 1 87  ? 57.134 -15.883 -6.464  1.00 15.12 ?  87  ASN   B OD1  1 
ATOM   5306 N  ND2  . ASN   B 1 87  ? 58.518 -17.021 -7.832  1.00 18.43 ?  87  ASN   B ND2  1 
ATOM   5307 H  H    . ASN   B 1 87  ? 56.226 -14.091 -6.721  1.00 15.19 ?  87  ASN   B H    1 
ATOM   5308 H  HA   . ASN   B 1 87  ? 56.361 -13.512 -9.332  1.00 16.11 ?  87  ASN   B HA   1 
ATOM   5309 H  HB2  . ASN   B 1 87  ? 57.971 -15.211 -9.412  1.00 18.11 ?  87  ASN   B HB2  1 
ATOM   5310 H  HB3  . ASN   B 1 87  ? 58.344 -14.153 -8.287  1.00 18.11 ?  87  ASN   B HB3  1 
ATOM   5311 H  HD21 . ASN   B 1 87  ? 58.584 -17.676 -7.284  1.00 22.10 ?  87  ASN   B HD21 1 
ATOM   5312 H  HD22 . ASN   B 1 87  ? 58.945 -17.039 -8.581  1.00 22.10 ?  87  ASN   B HD22 1 
ATOM   5313 N  N    . LEU   B 1 88  ? 54.158 -15.364 -8.555  1.00 12.02 ?  88  LEU   B N    1 
ATOM   5314 C  CA   . LEU   B 1 88  ? 53.178 -16.395 -8.879  1.00 12.14 ?  88  LEU   B CA   1 
ATOM   5315 C  C    . LEU   B 1 88  ? 51.948 -15.878 -9.604  1.00 11.81 ?  88  LEU   B C    1 
ATOM   5316 O  O    . LEU   B 1 88  ? 51.347 -16.627 -10.383 1.00 13.67 ?  88  LEU   B O    1 
ATOM   5317 C  CB   . LEU   B 1 88  ? 52.703 -17.072 -7.590  1.00 13.18 ?  88  LEU   B CB   1 
ATOM   5318 C  CG   . LEU   B 1 88  ? 53.821 -17.745 -6.806  1.00 15.45 ?  88  LEU   B CG   1 
ATOM   5319 C  CD1  . LEU   B 1 88  ? 53.328 -18.126 -5.420  1.00 17.20 ?  88  LEU   B CD1  1 
ATOM   5320 C  CD2  . LEU   B 1 88  ? 54.321 -18.959 -7.564  1.00 18.43 ?  88  LEU   B CD2  1 
ATOM   5321 H  H    . LEU   B 1 88  ? 53.899 -14.832 -7.924  1.00 14.41 ?  88  LEU   B H    1 
ATOM   5322 H  HA   . LEU   B 1 88  ? 53.595 -17.064 -9.434  1.00 14.55 ?  88  LEU   B HA   1 
ATOM   5323 H  HB2  . LEU   B 1 88  ? 52.295 -16.406 -7.012  1.00 15.80 ?  88  LEU   B HB2  1 
ATOM   5324 H  HB3  . LEU   B 1 88  ? 52.048 -17.752 -7.816  1.00 15.80 ?  88  LEU   B HB3  1 
ATOM   5325 H  HG   . LEU   B 1 88  ? 54.557 -17.123 -6.703  1.00 18.52 ?  88  LEU   B HG   1 
ATOM   5326 H  HD11 . LEU   B 1 88  ? 54.007 -18.661 -4.981  1.00 20.63 ?  88  LEU   B HD11 1 
ATOM   5327 H  HD12 . LEU   B 1 88  ? 53.159 -17.319 -4.911  1.00 20.63 ?  88  LEU   B HD12 1 
ATOM   5328 H  HD13 . LEU   B 1 88  ? 52.509 -18.639 -5.510  1.00 20.63 ?  88  LEU   B HD13 1 
ATOM   5329 H  HD21 . LEU   B 1 88  ? 54.939 -19.448 -6.999  1.00 22.10 ?  88  LEU   B HD21 1 
ATOM   5330 H  HD22 . LEU   B 1 88  ? 53.565 -19.520 -7.795  1.00 22.10 ?  88  LEU   B HD22 1 
ATOM   5331 H  HD23 . LEU   B 1 88  ? 54.773 -18.663 -8.370  1.00 22.10 ?  88  LEU   B HD23 1 
ATOM   5332 N  N    . ALA   B 1 89  ? 51.539 -14.643 -9.334  1.00 11.57 ?  89  ALA   B N    1 
ATOM   5333 C  CA   . ALA   B 1 89  ? 50.247 -14.144 -9.779  1.00 11.07 ?  89  ALA   B CA   1 
ATOM   5334 C  C    . ALA   B 1 89  ? 50.218 -12.651 -9.492  1.00 11.37 ?  89  ALA   B C    1 
ATOM   5335 O  O    . ALA   B 1 89  ? 51.062 -12.129 -8.761  1.00 12.13 ?  89  ALA   B O    1 
ATOM   5336 C  CB   . ALA   B 1 89  ? 49.113 -14.832 -9.022  1.00 11.12 ?  89  ALA   B CB   1 
ATOM   5337 H  H    . ALA   B 1 89  ? 51.991 -14.066 -8.883  1.00 13.87 ?  89  ALA   B H    1 
ATOM   5338 H  HA   . ALA   B 1 89  ? 50.133 -14.290 -10.735 1.00 13.27 ?  89  ALA   B HA   1 
ATOM   5339 H  HB1  . ALA   B 1 89  ? 48.262 -14.503 -9.360  1.00 13.33 ?  89  ALA   B HB1  1 
ATOM   5340 H  HB2  . ALA   B 1 89  ? 49.175 -15.790 -9.173  1.00 13.33 ?  89  ALA   B HB2  1 
ATOM   5341 H  HB3  . ALA   B 1 89  ? 49.198 -14.636 -8.082  1.00 13.33 ?  89  ALA   B HB3  1 
ATOM   5342 N  N    . LYS   B 1 90  ? 49.221 -11.961 -10.046 1.00 12.14 ?  90  LYS   B N    1 
ATOM   5343 C  CA   . LYS   B 1 90  ? 49.035 -10.571 -9.645  1.00 12.31 ?  90  LYS   B CA   1 
ATOM   5344 C  C    . LYS   B 1 90  ? 48.719 -10.496 -8.158  1.00 12.09 ?  90  LYS   B C    1 
ATOM   5345 O  O    . LYS   B 1 90  ? 49.360 -9.743  -7.408  1.00 13.28 ?  90  LYS   B O    1 
ATOM   5346 C  CB   . LYS   B 1 90  ? 47.947 -9.914  -10.494 1.00 13.73 ?  90  LYS   B CB   1 
ATOM   5347 C  CG   . LYS   B 1 90  ? 47.673 -8.467  -10.120 1.00 14.34 ?  90  LYS   B CG   1 
ATOM   5348 C  CD   . LYS   B 1 90  ? 48.890 -7.583  -10.202 1.00 17.16 ?  90  LYS   B CD   1 
ATOM   5349 C  CE   . LYS   B 1 90  ? 48.458 -6.159  -9.954  1.00 19.30 ?  90  LYS   B CE   1 
ATOM   5350 N  NZ   . LYS   B 1 90  ? 49.609 -5.240  -9.830  1.00 19.12 ?  90  LYS   B NZ   1 
ATOM   5351 H  H    . LYS   B 1 90  ? 48.659 -12.268 -10.625 1.00 14.56 ?  90  LYS   B H    1 
ATOM   5352 H  HA   . LYS   B 1 90  ? 49.860 -10.097 -9.799  1.00 14.76 ?  90  LYS   B HA   1 
ATOM   5353 H  HB2  . LYS   B 1 90  ? 48.224 -9.932  -11.428 1.00 16.46 ?  90  LYS   B HB2  1 
ATOM   5354 H  HB3  . LYS   B 1 90  ? 47.119 -10.411 -10.394 1.00 16.46 ?  90  LYS   B HB3  1 
ATOM   5355 H  HG2  . LYS   B 1 90  ? 47.006 -8.109  -10.726 1.00 17.19 ?  90  LYS   B HG2  1 
ATOM   5356 H  HG3  . LYS   B 1 90  ? 47.338 -8.435  -9.210  1.00 17.19 ?  90  LYS   B HG3  1 
ATOM   5357 H  HD2  . LYS   B 1 90  ? 49.531 -7.837  -9.518  1.00 20.57 ?  90  LYS   B HD2  1 
ATOM   5358 H  HD3  . LYS   B 1 90  ? 49.286 -7.644  -11.085 1.00 20.57 ?  90  LYS   B HD3  1 
ATOM   5359 H  HE2  . LYS   B 1 90  ? 47.914 -5.851  -10.699 1.00 23.15 ?  90  LYS   B HE2  1 
ATOM   5360 H  HE3  . LYS   B 1 90  ? 47.949 -6.109  -9.130  1.00 23.15 ?  90  LYS   B HE3  1 
ATOM   5361 H  HZ1  . LYS   B 1 90  ? 49.328 -4.405  -9.687  1.00 22.93 ?  90  LYS   B HZ1  1 
ATOM   5362 H  HZ2  . LYS   B 1 90  ? 50.127 -5.487  -9.149  1.00 22.93 ?  90  LYS   B HZ2  1 
ATOM   5363 H  HZ3  . LYS   B 1 90  ? 50.095 -5.251  -10.578 1.00 22.93 ?  90  LYS   B HZ3  1 
ATOM   5364 N  N    . HIS   B 1 91  ? 47.763 -11.314 -7.711  1.00 10.68 ?  91  HIS   B N    1 
ATOM   5365 C  CA   . HIS   B 1 91  ? 47.299 -11.342 -6.337  1.00 10.73 ?  91  HIS   B CA   1 
ATOM   5366 C  C    . HIS   B 1 91  ? 47.294 -12.769 -5.821  1.00 10.09 ?  91  HIS   B C    1 
ATOM   5367 O  O    . HIS   B 1 91  ? 47.067 -13.720 -6.577  1.00 10.52 ?  91  HIS   B O    1 
ATOM   5368 C  CB   . HIS   B 1 91  ? 45.849 -10.862 -6.223  1.00 11.98 ?  91  HIS   B CB   1 
ATOM   5369 C  CG   . HIS   B 1 91  ? 45.641 -9.453  -6.654  1.00 15.44 ?  91  HIS   B CG   1 
ATOM   5370 N  ND1  . HIS   B 1 91  ? 46.248 -8.382  -6.034  1.00 18.02 ?  91  HIS   B ND1  1 
ATOM   5371 C  CD2  . HIS   B 1 91  ? 44.857 -8.935  -7.623  1.00 17.74 ?  91  HIS   B CD2  1 
ATOM   5372 C  CE1  . HIS   B 1 91  ? 45.864 -7.263  -6.621  1.00 19.14 ?  91  HIS   B CE1  1 
ATOM   5373 N  NE2  . HIS   B 1 91  ? 45.015 -7.572  -7.586  1.00 19.21 ?  91  HIS   B NE2  1 
ATOM   5374 H  H    . HIS   B 1 91  ? 47.350 -11.888 -8.209  1.00 12.80 ?  91  HIS   B H    1 
ATOM   5375 H  HA   . HIS   B 1 91  ? 47.870 -10.785 -5.773  1.00 12.86 ?  91  HIS   B HA   1 
ATOM   5376 H  HB2  . HIS   B 1 91  ? 45.291 -11.427 -6.778  1.00 14.36 ?  91  HIS   B HB2  1 
ATOM   5377 H  HB3  . HIS   B 1 91  ? 45.568 -10.934 -5.295  1.00 14.36 ?  91  HIS   B HB3  1 
ATOM   5378 H  HD1  . HIS   B 1 91  ? 46.796 -8.437  -5.373  1.00 21.61 ?  91  HIS   B HD1  1 
ATOM   5379 H  HD2  . HIS   B 1 91  ? 44.319 -9.404  -8.216  1.00 21.27 ?  91  HIS   B HD2  1 
ATOM   5380 H  HE1  . HIS   B 1 91  ? 46.140 -6.403  -6.385  1.00 22.95 ?  91  HIS   B HE1  1 
ATOM   5381 N  N    . CYS   B 1 92  ? 47.490 -12.904 -4.516  1.00 9.97  ?  92  CYS   B N    1 
ATOM   5382 C  CA   . CYS   B 1 92  ? 47.189 -14.138 -3.803  1.00 9.82  ?  92  CYS   B CA   1 
ATOM   5383 C  C    . CYS   B 1 92  ? 45.971 -13.900 -2.920  1.00 9.62  ?  92  CYS   B C    1 
ATOM   5384 O  O    . CYS   B 1 92  ? 45.975 -13.000 -2.069  1.00 10.31 ?  92  CYS   B O    1 
ATOM   5385 C  CB   . CYS   B 1 92  ? 48.368 -14.596 -2.950  1.00 10.47 ?  92  CYS   B CB   1 
ATOM   5386 S  SG   . CYS   B 1 92  ? 48.021 -16.138 -2.057  1.00 10.50 ?  92  CYS   B SG   1 
ATOM   5387 H  H    . CYS   B 1 92  ? 47.818 -12.282 -4.010  1.00 11.95 ?  92  CYS   B H    1 
ATOM   5388 H  HA   . CYS   B 1 92  ? 46.989 -14.835 -4.448  1.00 11.76 ?  92  CYS   B HA   1 
ATOM   5389 H  HB2  . CYS   B 1 92  ? 49.135 -14.737 -3.518  1.00 12.55 ?  92  CYS   B HB2  1 
ATOM   5390 H  HB3  . CYS   B 1 92  ? 48.559 -13.903 -2.294  1.00 12.55 ?  92  CYS   B HB3  1 
ATOM   5391 H  HG   . CYS   B 1 92  ? 48.996 -16.441 -1.423  1.00 12.58 ?  92  CYS   B HG   1 
ATOM   5392 N  N    . LEU   B 1 93  ? 44.937 -14.709 -3.130  1.00 9.45  ?  93  LEU   B N    1 
ATOM   5393 C  CA   . LEU   B 1 93  ? 43.760 -14.724 -2.274  1.00 9.64  ?  93  LEU   B CA   1 
ATOM   5394 C  C    . LEU   B 1 93  ? 43.981 -15.790 -1.207  1.00 9.15  ?  93  LEU   B C    1 
ATOM   5395 O  O    . LEU   B 1 93  ? 43.942 -16.992 -1.496  1.00 9.70  ?  93  LEU   B O    1 
ATOM   5396 C  CB   . LEU   B 1 93  ? 42.500 -15.011 -3.086  1.00 10.00 ?  93  LEU   B CB   1 
ATOM   5397 C  CG   . LEU   B 1 93  ? 41.204 -15.033 -2.274  1.00 10.51 ?  93  LEU   B CG   1 
ATOM   5398 C  CD1  . LEU   B 1 93  ? 40.854 -13.647 -1.761  1.00 11.11 ?  93  LEU   B CD1  1 
ATOM   5399 C  CD2  . LEU   B 1 93  ? 40.070 -15.620 -3.103  1.00 10.86 ?  93  LEU   B CD2  1 
ATOM   5400 H  H    . LEU   B 1 93  ? 44.899 -15.289 -3.780  1.00 11.32 ?  93  LEU   B H    1 
ATOM   5401 H  HA   . LEU   B 1 93  ? 43.672 -13.862 -1.845  1.00 11.56 ?  93  LEU   B HA   1 
ATOM   5402 H  HB2  . LEU   B 1 93  ? 42.406 -14.314 -3.760  1.00 11.99 ?  93  LEU   B HB2  1 
ATOM   5403 H  HB3  . LEU   B 1 93  ? 42.593 -15.868 -3.515  1.00 11.99 ?  93  LEU   B HB3  1 
ATOM   5404 H  HG   . LEU   B 1 93  ? 41.329 -15.605 -1.504  1.00 12.60 ?  93  LEU   B HG   1 
ATOM   5405 H  HD11 . LEU   B 1 93  ? 40.001 -13.683 -1.305  1.00 13.32 ?  93  LEU   B HD11 1 
ATOM   5406 H  HD12 . LEU   B 1 93  ? 41.546 -13.350 -1.149  1.00 13.32 ?  93  LEU   B HD12 1 
ATOM   5407 H  HD13 . LEU   B 1 93  ? 40.799 -13.035 -2.516  1.00 13.32 ?  93  LEU   B HD13 1 
ATOM   5408 H  HD21 . LEU   B 1 93  ? 39.261 -15.619 -2.570  1.00 13.02 ?  93  LEU   B HD21 1 
ATOM   5409 H  HD22 . LEU   B 1 93  ? 39.947 -15.077 -3.896  1.00 13.02 ?  93  LEU   B HD22 1 
ATOM   5410 H  HD23 . LEU   B 1 93  ? 40.303 -16.527 -3.354  1.00 13.02 ?  93  LEU   B HD23 1 
ATOM   5411 N  N    . HIS   B 1 94  ? 44.259 -15.350 0.014   1.00 9.06  ?  94  HIS   B N    1 
ATOM   5412 C  CA   . HIS   B 1 94  ? 44.484 -16.255 1.134   1.00 9.43  ?  94  HIS   B CA   1 
ATOM   5413 C  C    . HIS   B 1 94  ? 43.126 -16.613 1.715   1.00 9.77  ?  94  HIS   B C    1 
ATOM   5414 O  O    . HIS   B 1 94  ? 42.462 -15.739 2.274   1.00 11.06 ?  94  HIS   B O    1 
ATOM   5415 C  CB   . HIS   B 1 94  ? 45.355 -15.571 2.186   1.00 9.76  ?  94  HIS   B CB   1 
ATOM   5416 C  CG   . HIS   B 1 94  ? 46.739 -15.275 1.718   1.00 9.96  ?  94  HIS   B CG   1 
ATOM   5417 N  ND1  . HIS   B 1 94  ? 47.765 -16.192 1.806   1.00 10.15 ?  94  HIS   B ND1  1 
ATOM   5418 C  CD2  . HIS   B 1 94  ? 47.249 -14.172 1.119   1.00 10.23 ?  94  HIS   B CD2  1 
ATOM   5419 C  CE1  . HIS   B 1 94  ? 48.856 -15.642 1.299   1.00 9.98  ?  94  HIS   B CE1  1 
ATOM   5420 N  NE2  . HIS   B 1 94  ? 48.570 -14.421 0.873   1.00 10.26 ?  94  HIS   B NE2  1 
ATOM   5421 H  H    . HIS   B 1 94  ? 44.332 -14.515 0.217   1.00 10.85 ?  94  HIS   B H    1 
ATOM   5422 H  HA   . HIS   B 1 94  ? 44.924 -17.060 0.827   1.00 11.30 ?  94  HIS   B HA   1 
ATOM   5423 H  HB2  . HIS   B 1 94  ? 44.942 -14.732 2.438   1.00 11.69 ?  94  HIS   B HB2  1 
ATOM   5424 H  HB3  . HIS   B 1 94  ? 45.422 -16.153 2.958   1.00 11.69 ?  94  HIS   B HB3  1 
ATOM   5425 H  HD2  . HIS   B 1 94  ? 46.792 -13.389 0.918   1.00 12.26 ?  94  HIS   B HD2  1 
ATOM   5426 H  HE1  . HIS   B 1 94  ? 49.687 -16.057 1.244   1.00 11.96 ?  94  HIS   B HE1  1 
ATOM   5427 H  HE2  . HIS   B 1 94  ? 49.127 -13.881 0.504   1.00 12.30 ?  94  HIS   B HE2  1 
ATOM   5428 N  N    . VAL   B 1 95  ? 42.694 -17.867 1.563   1.00 9.59  ?  95  VAL   B N    1 
ATOM   5429 C  CA   . VAL   B 1 95  ? 41.366 -18.308 1.992   1.00 9.91  ?  95  VAL   B CA   1 
ATOM   5430 C  C    . VAL   B 1 95  ? 41.533 -19.342 3.092   1.00 10.09 ?  95  VAL   B C    1 
ATOM   5431 O  O    . VAL   B 1 95  ? 42.307 -20.292 2.935   1.00 10.61 ?  95  VAL   B O    1 
ATOM   5432 C  CB   . VAL   B 1 95  ? 40.548 -18.914 0.833   1.00 10.18 ?  95  VAL   B CB   1 
ATOM   5433 C  CG1  . VAL   B 1 95  ? 39.162 -19.352 1.315   1.00 11.24 ?  95  VAL   B CG1  1 
ATOM   5434 C  CG2  . VAL   B 1 95  ? 40.430 -17.933 -0.310  1.00 10.39 ?  95  VAL   B CG2  1 
ATOM   5435 H  H    . VAL   B 1 95  ? 43.163 -18.495 1.207   1.00 11.50 ?  95  VAL   B H    1 
ATOM   5436 H  HA   . VAL   B 1 95  ? 40.873 -17.554 2.354   1.00 11.87 ?  95  VAL   B HA   1 
ATOM   5437 H  HB   . VAL   B 1 95  ? 41.006 -19.699 0.503   1.00 12.19 ?  95  VAL   B HB   1 
ATOM   5438 H  HG11 . VAL   B 1 95  ? 38.606 -19.564 0.541   1.00 13.47 ?  95  VAL   B HG11 1 
ATOM   5439 H  HG12 . VAL   B 1 95  ? 39.246 -20.140 1.876   1.00 13.47 ?  95  VAL   B HG12 1 
ATOM   5440 H  HG13 . VAL   B 1 95  ? 38.750 -18.630 1.818   1.00 13.47 ?  95  VAL   B HG13 1 
ATOM   5441 H  HG21 . VAL   B 1 95  ? 39.857 -18.321 -0.994  1.00 12.45 ?  95  VAL   B HG21 1 
ATOM   5442 H  HG22 . VAL   B 1 95  ? 40.039 -17.111 0.020   1.00 12.45 ?  95  VAL   B HG22 1 
ATOM   5443 H  HG23 . VAL   B 1 95  ? 41.311 -17.767 -0.671  1.00 12.45 ?  95  VAL   B HG23 1 
ATOM   5444 N  N    . VAL   B 1 96  ? 40.801 -19.172 4.186   1.00 10.51 ?  96  VAL   B N    1 
ATOM   5445 C  CA   . VAL   B 1 96  ? 40.883 -20.086 5.325   1.00 10.93 ?  96  VAL   B CA   1 
ATOM   5446 C  C    . VAL   B 1 96  ? 39.694 -21.046 5.278   1.00 11.25 ?  96  VAL   B C    1 
ATOM   5447 O  O    . VAL   B 1 96  ? 38.575 -20.698 5.664   1.00 12.26 ?  96  VAL   B O    1 
ATOM   5448 C  CB   . VAL   B 1 96  ? 40.941 -19.341 6.663   1.00 11.55 ?  96  VAL   B CB   1 
ATOM   5449 C  CG1  . VAL   B 1 96  ? 41.112 -20.339 7.806   1.00 12.61 ?  96  VAL   B CG1  1 
ATOM   5450 C  CG2  . VAL   B 1 96  ? 42.057 -18.303 6.673   1.00 12.56 ?  96  VAL   B CG2  1 
ATOM   5451 H  H    . VAL   B 1 96  ? 40.239 -18.532 4.300   1.00 12.60 ?  96  VAL   B H    1 
ATOM   5452 H  HA   . VAL   B 1 96  ? 41.695 -20.615 5.250   1.00 13.10 ?  96  VAL   B HA   1 
ATOM   5453 H  HB   . VAL   B 1 96  ? 40.102 -18.875 6.803   1.00 13.84 ?  96  VAL   B HB   1 
ATOM   5454 H  HG11 . VAL   B 1 96  ? 41.308 -19.852 8.626   1.00 15.12 ?  96  VAL   B HG11 1 
ATOM   5455 H  HG12 . VAL   B 1 96  ? 40.295 -20.847 7.915   1.00 15.12 ?  96  VAL   B HG12 1 
ATOM   5456 H  HG13 . VAL   B 1 96  ? 41.851 -20.935 7.600   1.00 15.12 ?  96  VAL   B HG13 1 
ATOM   5457 H  HG21 . VAL   B 1 96  ? 42.102 -17.893 7.555   1.00 15.06 ?  96  VAL   B HG21 1 
ATOM   5458 H  HG22 . VAL   B 1 96  ? 42.898 -18.737 6.469   1.00 15.06 ?  96  VAL   B HG22 1 
ATOM   5459 H  HG23 . VAL   B 1 96  ? 41.863 -17.624 6.007   1.00 15.06 ?  96  VAL   B HG23 1 
ATOM   5460 N  N    . GLY   B 1 97  ? 39.932 -22.274 4.831   1.00 11.22 ?  97  GLY   B N    1 
ATOM   5461 C  CA   . GLY   B 1 97  ? 38.960 -23.333 4.991   1.00 11.97 ?  97  GLY   B CA   1 
ATOM   5462 C  C    . GLY   B 1 97  ? 39.088 -23.947 6.370   1.00 12.98 ?  97  GLY   B C    1 
ATOM   5463 O  O    . GLY   B 1 97  ? 40.135 -23.831 7.023   1.00 13.37 ?  97  GLY   B O    1 
ATOM   5464 H  H    . GLY   B 1 97  ? 40.659 -22.516 4.435   1.00 13.45 ?  97  GLY   B H    1 
ATOM   5465 H  HA2  . GLY   B 1 97  ? 38.064 -22.968 4.874   1.00 14.35 ?  97  GLY   B HA2  1 
ATOM   5466 H  HA3  . GLY   B 1 97  ? 39.103 -24.017 4.315   1.00 14.35 ?  97  GLY   B HA3  1 
ATOM   5467 N  N    . PRO   B 1 98  ? 38.043 -24.633 6.835   1.00 14.20 ?  98  PRO   B N    1 
ATOM   5468 C  CA   . PRO   B 1 98  ? 38.140 -25.328 8.122   1.00 14.99 ?  98  PRO   B CA   1 
ATOM   5469 C  C    . PRO   B 1 98  ? 39.164 -26.451 8.075   1.00 14.49 ?  98  PRO   B C    1 
ATOM   5470 O  O    . PRO   B 1 98  ? 39.267 -27.185 7.093   1.00 14.64 ?  98  PRO   B O    1 
ATOM   5471 C  CB   . PRO   B 1 98  ? 36.721 -25.870 8.336   1.00 15.36 ?  98  PRO   B CB   1 
ATOM   5472 C  CG   . PRO   B 1 98  ? 36.146 -25.995 6.973   1.00 15.08 ?  98  PRO   B CG   1 
ATOM   5473 C  CD   . PRO   B 1 98  ? 36.721 -24.823 6.209   1.00 13.96 ?  98  PRO   B CD   1 
ATOM   5474 H  HA   . PRO   B 1 98  ? 38.363 -24.704 8.825   1.00 17.97 ?  98  PRO   B HA   1 
ATOM   5475 H  HB2  . PRO   B 1 98  ? 36.766 -26.740 8.770   1.00 18.41 ?  98  PRO   B HB2  1 
ATOM   5476 H  HB3  . PRO   B 1 98  ? 36.206 -25.248 8.868   1.00 18.41 ?  98  PRO   B HB3  1 
ATOM   5477 H  HG2  . PRO   B 1 98  ? 36.424 -26.839 6.577   1.00 18.08 ?  98  PRO   B HG2  1 
ATOM   5478 H  HG3  . PRO   B 1 98  ? 35.179 -25.942 7.019   1.00 18.08 ?  98  PRO   B HG3  1 
ATOM   5479 H  HD2  . PRO   B 1 98  ? 36.810 -25.051 5.267   1.00 16.74 ?  98  PRO   B HD2  1 
ATOM   5480 H  HD3  . PRO   B 1 98  ? 36.167 -24.038 6.333   1.00 16.74 ?  98  PRO   B HD3  1 
ATOM   5481 N  N    . ASN   B 1 99  ? 39.912 -26.584 9.160   1.00 15.87 ?  99  ASN   B N    1 
ATOM   5482 C  CA   . ASN   B 1 99  ? 40.893 -27.653 9.317   1.00 16.87 ?  99  ASN   B CA   1 
ATOM   5483 C  C    . ASN   B 1 99  ? 40.272 -28.738 10.195  1.00 19.28 ?  99  ASN   B C    1 
ATOM   5484 O  O    . ASN   B 1 99  ? 40.201 -28.596 11.418  1.00 19.92 ?  99  ASN   B O    1 
ATOM   5485 C  CB   . ASN   B 1 99  ? 42.164 -27.090 9.936   1.00 17.12 ?  99  ASN   B CB   1 
ATOM   5486 C  CG   . ASN   B 1 99  ? 43.301 -28.088 9.939   1.00 18.10 ?  99  ASN   B CG   1 
ATOM   5487 O  OD1  . ASN   B 1 99  ? 43.082 -29.279 10.113  1.00 18.81 ?  99  ASN   B OD1  1 
ATOM   5488 N  ND2  . ASN   B 1 99  ? 44.515 -27.611 9.743   1.00 18.08 ?  99  ASN   B ND2  1 
ATOM   5489 H  H    . ASN   B 1 99  ? 39.864 -26.055 9.835   1.00 19.02 ?  99  ASN   B H    1 
ATOM   5490 H  HA   . ASN   B 1 99  ? 41.099 -28.038 8.452   1.00 20.23 ?  99  ASN   B HA   1 
ATOM   5491 H  HB2  . ASN   B 1 99  ? 42.437 -26.317 9.431   1.00 20.53 ?  99  ASN   B HB2  1 
ATOM   5492 H  HB3  . ASN   B 1 99  ? 41.973 -26.844 10.857  1.00 20.53 ?  99  ASN   B HB3  1 
ATOM   5493 H  HD21 . ASN   B 1 99  ? 45.187 -28.143 9.731   1.00 21.68 ?  99  ASN   B HD21 1 
ATOM   5494 H  HD22 . ASN   B 1 99  ? 44.624 -26.768 9.626   1.00 21.68 ?  99  ASN   B HD22 1 
ATOM   5495 N  N    A VAL   B 1 100 ? 39.795 -29.814 9.562   0.62 21.40 ?  100 VAL   B N    1 
ATOM   5496 N  N    B VAL   B 1 100 ? 39.813 -29.819 9.556   0.38 21.33 ?  100 VAL   B N    1 
ATOM   5497 C  CA   A VAL   B 1 100 ? 39.189 -30.910 10.316  0.62 23.96 ?  100 VAL   B CA   1 
ATOM   5498 C  CA   B VAL   B 1 100 ? 39.197 -30.926 10.284  0.38 23.58 ?  100 VAL   B CA   1 
ATOM   5499 C  C    A VAL   B 1 100 ? 40.208 -31.573 11.236  0.62 24.38 ?  100 VAL   B C    1 
ATOM   5500 C  C    B VAL   B 1 100 ? 40.202 -31.597 11.212  0.38 24.17 ?  100 VAL   B C    1 
ATOM   5501 O  O    A VAL   B 1 100 ? 39.850 -32.081 12.306  0.62 24.97 ?  100 VAL   B O    1 
ATOM   5502 O  O    B VAL   B 1 100 ? 39.828 -32.130 12.264  0.38 24.45 ?  100 VAL   B O    1 
ATOM   5503 C  CB   A VAL   B 1 100 ? 38.518 -31.920 9.362   0.62 26.08 ?  100 VAL   B CB   1 
ATOM   5504 C  CB   B VAL   B 1 100 ? 38.561 -31.923 9.293   0.38 25.14 ?  100 VAL   B CB   1 
ATOM   5505 C  CG1  A VAL   B 1 100 ? 38.011 -33.131 10.131  0.62 27.00 ?  100 VAL   B CG1  1 
ATOM   5506 C  CG1  B VAL   B 1 100 ? 38.052 -33.159 10.020  0.38 25.76 ?  100 VAL   B CG1  1 
ATOM   5507 C  CG2  A VAL   B 1 100 ? 37.374 -31.256 8.610   0.62 26.53 ?  100 VAL   B CG2  1 
ATOM   5508 C  CG2  B VAL   B 1 100 ? 37.429 -31.255 8.527   0.38 25.52 ?  100 VAL   B CG2  1 
ATOM   5509 H  H    A VAL   B 1 100 ? 39.798 -29.925 8.706   0.62 25.67 ?  100 VAL   B H    1 
ATOM   5510 H  H    B VAL   B 1 100 ? 39.843 -29.931 8.703   0.38 25.58 ?  100 VAL   B H    1 
ATOM   5511 H  HA   A VAL   B 1 100 ? 38.486 -30.544 10.875  0.62 28.73 ?  100 VAL   B HA   1 
ATOM   5512 H  HA   B VAL   B 1 100 ? 38.482 -30.574 10.834  0.38 28.28 ?  100 VAL   B HA   1 
ATOM   5513 H  HB   A VAL   B 1 100 ? 39.169 -32.230 8.715   0.62 31.28 ?  100 VAL   B HB   1 
ATOM   5514 H  HB   B VAL   B 1 100 ? 39.231 -32.209 8.652   0.38 30.15 ?  100 VAL   B HB   1 
ATOM   5515 H  HG11 A VAL   B 1 100 ? 37.418 -33.644 9.556   0.62 32.38 ?  100 VAL   B HG11 1 
ATOM   5516 H  HG11 B VAL   B 1 100 ? 37.475 -33.662 9.422   0.38 30.90 ?  100 VAL   B HG11 1 
ATOM   5517 H  HG12 A VAL   B 1 100 ? 38.764 -33.682 10.397  0.62 32.38 ?  100 VAL   B HG12 1 
ATOM   5518 H  HG12 B VAL   B 1 100 ? 38.806 -33.708 10.285  0.38 30.90 ?  100 VAL   B HG12 1 
ATOM   5519 H  HG13 A VAL   B 1 100 ? 37.525 -32.831 10.915  0.62 32.38 ?  100 VAL   B HG13 1 
ATOM   5520 H  HG13 B VAL   B 1 100 ? 37.550 -32.882 10.803  0.38 30.90 ?  100 VAL   B HG13 1 
ATOM   5521 H  HG21 A VAL   B 1 100 ? 36.958 -31.911 8.026   0.62 31.82 ?  100 VAL   B HG21 1 
ATOM   5522 H  HG21 B VAL   B 1 100 ? 37.029 -31.903 7.925   0.38 30.61 ?  100 VAL   B HG21 1 
ATOM   5523 H  HG22 A VAL   B 1 100 ? 36.724 -30.927 9.251   0.62 31.82 ?  100 VAL   B HG22 1 
ATOM   5524 H  HG22 B VAL   B 1 100 ? 36.765 -30.938 9.159   0.38 30.61 ?  100 VAL   B HG22 1 
ATOM   5525 H  HG23 A VAL   B 1 100 ? 37.726 -30.522 8.087   0.62 31.82 ?  100 VAL   B HG23 1 
ATOM   5526 H  HG23 B VAL   B 1 100 ? 37.788 -30.511 8.021   0.38 30.61 ?  100 VAL   B HG23 1 
ATOM   5527 N  N    . ASN   B 1 101 ? 41.484 -31.596 10.840  1.00 24.70 ?  101 ASN   B N    1 
ATOM   5528 C  CA   . ASN   B 1 101 ? 42.529 -32.128 11.714  1.00 26.40 ?  101 ASN   B CA   1 
ATOM   5529 C  C    . ASN   B 1 101 ? 42.729 -31.292 12.973  1.00 28.51 ?  101 ASN   B C    1 
ATOM   5530 O  O    . ASN   B 1 101 ? 43.380 -31.766 13.913  1.00 29.75 ?  101 ASN   B O    1 
ATOM   5531 C  CB   . ASN   B 1 101 ? 43.851 -32.258 10.954  1.00 26.06 ?  101 ASN   B CB   1 
ATOM   5532 C  CG   . ASN   B 1 101 ? 43.844 -33.414 9.972   1.00 25.47 ?  101 ASN   B CG   1 
ATOM   5533 O  OD1  . ASN   B 1 101 ? 43.163 -34.411 10.184  1.00 26.20 ?  101 ASN   B OD1  1 
ATOM   5534 N  ND2  . ASN   B 1 101 ? 44.590 -33.276 8.884   1.00 24.94 ?  101 ASN   B ND2  1 
ATOM   5535 H  H    A ASN   B 1 101 ? 41.762 -31.326 10.069  0.62 29.63 ?  101 ASN   B H    1 
ATOM   5536 H  H    B ASN   B 1 101 ? 41.769 -31.303 10.081  0.38 29.63 ?  101 ASN   B H    1 
ATOM   5537 H  HA   . ASN   B 1 101 ? 42.267 -33.012 11.997  1.00 31.66 ?  101 ASN   B HA   1 
ATOM   5538 H  HB2  . ASN   B 1 101 ? 44.021 -31.445 10.454  1.00 31.26 ?  101 ASN   B HB2  1 
ATOM   5539 H  HB3  . ASN   B 1 101 ? 44.569 -32.409 11.591  1.00 31.26 ?  101 ASN   B HB3  1 
ATOM   5540 H  HD21 . ASN   B 1 101 ? 44.620 -33.907 8.301   1.00 29.91 ?  101 ASN   B HD21 1 
ATOM   5541 H  HD22 . ASN   B 1 101 ? 45.047 -32.557 8.764   1.00 29.91 ?  101 ASN   B HD22 1 
ATOM   5542 N  N    . LYS   B 1 102 ? 42.195 -30.069 13.006  1.00 30.75 ?  102 LYS   B N    1 
ATOM   5543 C  CA   . LYS   B 1 102 ? 42.167 -29.239 14.204  1.00 33.25 ?  102 LYS   B CA   1 
ATOM   5544 C  C    . LYS   B 1 102 ? 40.787 -29.201 14.848  1.00 32.70 ?  102 LYS   B C    1 
ATOM   5545 O  O    . LYS   B 1 102 ? 40.565 -28.406 15.766  1.00 33.48 ?  102 LYS   B O    1 
ATOM   5546 C  CB   . LYS   B 1 102 ? 42.600 -27.807 13.878  1.00 36.32 ?  102 LYS   B CB   1 
ATOM   5547 C  CG   . LYS   B 1 102 ? 44.059 -27.635 13.495  1.00 39.26 ?  102 LYS   B CG   1 
ATOM   5548 C  CD   . LYS   B 1 102 ? 44.296 -26.214 13.004  1.00 41.92 ?  102 LYS   B CD   1 
ATOM   5549 C  CE   . LYS   B 1 102 ? 45.766 -25.913 12.787  1.00 43.93 ?  102 LYS   B CE   1 
ATOM   5550 N  NZ   . LYS   B 1 102 ? 45.956 -24.519 12.288  1.00 45.05 ?  102 LYS   B NZ   1 
ATOM   5551 H  H    . LYS   B 1 102 ? 41.827 -29.688 12.324  1.00 36.89 ?  102 LYS   B H    1 
ATOM   5552 H  HA   . LYS   B 1 102 ? 42.794 -29.597 14.849  1.00 39.88 ?  102 LYS   B HA   1 
ATOM   5553 H  HB2  . LYS   B 1 102 ? 42.066 -27.483 13.137  1.00 43.56 ?  102 LYS   B HB2  1 
ATOM   5554 H  HB3  . LYS   B 1 102 ? 42.440 -27.251 14.659  1.00 43.56 ?  102 LYS   B HB3  1 
ATOM   5555 H  HG2  . LYS   B 1 102 ? 44.622 -27.791 14.270  1.00 47.09 ?  102 LYS   B HG2  1 
ATOM   5556 H  HG3  . LYS   B 1 102 ? 44.283 -28.250 12.780  1.00 47.09 ?  102 LYS   B HG3  1 
ATOM   5557 H  HD2  . LYS   B 1 102 ? 43.835 -26.089 12.159  1.00 50.29 ?  102 LYS   B HD2  1 
ATOM   5558 H  HD3  . LYS   B 1 102 ? 43.954 -25.589 13.664  1.00 50.29 ?  102 LYS   B HD3  1 
ATOM   5559 H  HE2  . LYS   B 1 102 ? 46.242 -26.004 13.628  1.00 52.70 ?  102 LYS   B HE2  1 
ATOM   5560 H  HE3  . LYS   B 1 102 ? 46.127 -26.526 12.127  1.00 52.70 ?  102 LYS   B HE3  1 
ATOM   5561 H  HZ1  . LYS   B 1 102 ? 46.821 -24.355 12.165  1.00 54.05 ?  102 LYS   B HZ1  1 
ATOM   5562 H  HZ2  . LYS   B 1 102 ? 45.527 -24.413 11.515  1.00 54.05 ?  102 LYS   B HZ2  1 
ATOM   5563 H  HZ3  . LYS   B 1 102 ? 45.632 -23.938 12.880  1.00 54.05 ?  102 LYS   B HZ3  1 
ATOM   5564 N  N    . GLY   B 1 103 ? 39.850 -30.020 14.375  1.00 31.96 ?  103 GLY   B N    1 
ATOM   5565 C  CA   . GLY   B 1 103 ? 38.524 -30.073 14.954  1.00 31.65 ?  103 GLY   B CA   1 
ATOM   5566 C  C    . GLY   B 1 103 ? 37.576 -28.988 14.499  1.00 30.58 ?  103 GLY   B C    1 
ATOM   5567 O  O    . GLY   B 1 103 ? 36.494 -28.851 15.082  1.00 31.12 ?  103 GLY   B O    1 
ATOM   5568 H  H    . GLY   B 1 103 ? 39.961 -30.552 13.711  1.00 38.33 ?  103 GLY   B H    1 
ATOM   5569 H  HA2  . GLY   B 1 103 ? 38.120 -30.926 14.738  1.00 37.96 ?  103 GLY   B HA2  1 
ATOM   5570 H  HA3  . GLY   B 1 103 ? 38.600 -30.013 15.920  1.00 37.96 ?  103 GLY   B HA3  1 
ATOM   5571 N  N    A GLU   B 1 104 ? 37.949 -28.204 13.491  0.62 29.38 ?  104 GLU   B N    1 
ATOM   5572 N  N    B GLU   B 1 104 ? 37.928 -28.227 13.468  0.38 29.93 ?  104 GLU   B N    1 
ATOM   5573 C  CA   A GLU   B 1 104 ? 37.115 -27.102 13.043  0.62 28.17 ?  104 GLU   B CA   1 
ATOM   5574 C  CA   B GLU   B 1 104 ? 37.070 -27.147 13.006  0.38 29.14 ?  104 GLU   B CA   1 
ATOM   5575 C  C    A GLU   B 1 104 ? 35.925 -27.621 12.236  0.62 28.58 ?  104 GLU   B C    1 
ATOM   5576 C  C    B GLU   B 1 104 ? 35.910 -27.690 12.176  0.38 29.22 ?  104 GLU   B C    1 
ATOM   5577 O  O    A GLU   B 1 104 ? 35.953 -28.714 11.663  0.62 29.38 ?  104 GLU   B O    1 
ATOM   5578 O  O    B GLU   B 1 104 ? 35.993 -28.765 11.573  0.38 29.64 ?  104 GLU   B O    1 
ATOM   5579 C  CB   A GLU   B 1 104 ? 37.950 -26.103 12.238  0.62 27.05 ?  104 GLU   B CB   1 
ATOM   5580 C  CB   B GLU   B 1 104 ? 37.889 -26.127 12.214  0.38 28.42 ?  104 GLU   B CB   1 
ATOM   5581 C  CG   A GLU   B 1 104 ? 39.047 -25.457 13.077  0.62 26.01 ?  104 GLU   B CG   1 
ATOM   5582 C  CG   B GLU   B 1 104 ? 38.975 -25.479 13.062  0.38 27.76 ?  104 GLU   B CG   1 
ATOM   5583 C  CD   A GLU   B 1 104 ? 39.974 -24.559 12.285  0.62 24.76 ?  104 GLU   B CD   1 
ATOM   5584 C  CD   B GLU   B 1 104 ? 39.929 -24.615 12.264  0.38 27.05 ?  104 GLU   B CD   1 
ATOM   5585 O  OE1  A GLU   B 1 104 ? 39.973 -24.617 11.038  0.62 22.94 ?  104 GLU   B OE1  1 
ATOM   5586 O  OE1  B GLU   B 1 104 ? 39.870 -24.637 11.017  0.38 26.40 ?  104 GLU   B OE1  1 
ATOM   5587 O  OE2  A GLU   B 1 104 ? 40.715 -23.786 12.926  0.62 25.07 -1 104 GLU   B OE2  1 
ATOM   5588 O  OE2  B GLU   B 1 104 ? 40.746 -23.911 12.894  0.38 26.96 -1 104 GLU   B OE2  1 
ATOM   5589 H  H    A GLU   B 1 104 ? 38.689 -28.286 13.057  0.62 35.24 ?  104 GLU   B H    1 
ATOM   5590 H  H    B GLU   B 1 104 ? 38.660 -28.310 13.026  0.38 35.90 ?  104 GLU   B H    1 
ATOM   5591 H  HA   A GLU   B 1 104 ? 36.770 -26.634 13.821  0.62 33.79 ?  104 GLU   B HA   1 
ATOM   5592 H  HA   B GLU   B 1 104 ? 36.698 -26.692 13.774  0.38 34.95 ?  104 GLU   B HA   1 
ATOM   5593 H  HB2  A GLU   B 1 104 ? 38.371 -26.564 11.497  0.62 32.45 ?  104 GLU   B HB2  1 
ATOM   5594 H  HB2  B GLU   B 1 104 ? 38.315 -26.571 11.466  0.38 34.09 ?  104 GLU   B HB2  1 
ATOM   5595 H  HB3  A GLU   B 1 104 ? 37.372 -25.397 11.908  0.62 32.45 ?  104 GLU   B HB3  1 
ATOM   5596 H  HB3  B GLU   B 1 104 ? 37.299 -25.426 11.895  0.38 34.09 ?  104 GLU   B HB3  1 
ATOM   5597 H  HG2  A GLU   B 1 104 ? 38.639 -24.912 13.768  0.62 31.19 ?  104 GLU   B HG2  1 
ATOM   5598 H  HG2  B GLU   B 1 104 ? 38.557 -24.917 13.734  0.38 33.29 ?  104 GLU   B HG2  1 
ATOM   5599 H  HG3  A GLU   B 1 104 ? 39.587 -26.153 13.484  0.62 31.19 ?  104 GLU   B HG3  1 
ATOM   5600 H  HG3  B GLU   B 1 104 ? 39.495 -26.175 13.495  0.38 33.29 ?  104 GLU   B HG3  1 
ATOM   5601 N  N    A ASP   B 1 105 ? 34.865 -26.815 12.206  0.62 28.31 ?  105 ASP   B N    1 
ATOM   5602 N  N    B ASP   B 1 105 ? 34.817 -26.928 12.156  0.38 28.79 ?  105 ASP   B N    1 
ATOM   5603 C  CA   A ASP   B 1 105 ? 33.582 -27.256 11.670  0.62 28.84 ?  105 ASP   B CA   1 
ATOM   5604 C  CA   B ASP   B 1 105 ? 33.557 -27.403 11.596  0.38 28.74 ?  105 ASP   B CA   1 
ATOM   5605 C  C    A ASP   B 1 105 ? 33.631 -27.314 10.148  0.62 26.78 ?  105 ASP   B C    1 
ATOM   5606 C  C    B ASP   B 1 105 ? 33.626 -27.412 10.074  0.38 27.65 ?  105 ASP   B C    1 
ATOM   5607 O  O    A ASP   B 1 105 ? 33.777 -26.283 9.485   0.62 25.89 ?  105 ASP   B O    1 
ATOM   5608 O  O    B ASP   B 1 105 ? 33.813 -26.365 9.445   0.38 27.25 ?  105 ASP   B O    1 
ATOM   5609 C  CB   A ASP   B 1 105 ? 32.480 -26.301 12.127  0.62 31.75 ?  105 ASP   B CB   1 
ATOM   5610 C  CB   B ASP   B 1 105 ? 32.412 -26.509 12.072  0.38 29.77 ?  105 ASP   B CB   1 
ATOM   5611 C  CG   A ASP   B 1 105 ? 31.098 -26.765 11.712  0.62 34.16 ?  105 ASP   B CG   1 
ATOM   5612 C  CG   B ASP   B 1 105 ? 31.047 -27.090 11.750  0.38 30.60 ?  105 ASP   B CG   1 
ATOM   5613 O  OD1  A ASP   B 1 105 ? 30.980 -27.873 11.148  0.62 34.54 ?  105 ASP   B OD1  1 
ATOM   5614 O  OD1  B ASP   B 1 105 ? 30.984 -28.084 10.996  0.38 30.74 ?  105 ASP   B OD1  1 
ATOM   5615 O  OD2  A ASP   B 1 105 ? 30.124 -26.018 11.950  0.62 35.43 -1 105 ASP   B OD2  1 
ATOM   5616 O  OD2  B ASP   B 1 105 ? 30.036 -26.562 12.260  0.38 30.78 -1 105 ASP   B OD2  1 
ATOM   5617 H  H    A ASP   B 1 105 ? 34.865 -26.005 12.492  0.62 33.95 ?  105 ASP   B H    1 
ATOM   5618 H  H    B ASP   B 1 105 ? 34.784 -26.129 12.459  0.38 34.53 ?  105 ASP   B H    1 
ATOM   5619 H  HA   A ASP   B 1 105 ? 33.378 -28.142 12.005  0.62 34.60 ?  105 ASP   B HA   1 
ATOM   5620 H  HA   B ASP   B 1 105 ? 33.379 -28.306 11.901  0.38 34.47 ?  105 ASP   B HA   1 
ATOM   5621 H  HB2  A ASP   B 1 105 ? 32.508 -26.225 13.095  0.62 38.09 ?  105 ASP   B HB2  1 
ATOM   5622 H  HB2  B ASP   B 1 105 ? 32.470 -26.400 13.035  0.38 35.71 ?  105 ASP   B HB2  1 
ATOM   5623 H  HB3  A ASP   B 1 105 ? 32.625 -25.432 11.723  0.62 38.09 ?  105 ASP   B HB3  1 
ATOM   5624 H  HB3  B ASP   B 1 105 ? 32.484 -25.640 11.640  0.38 35.71 ?  105 ASP   B HB3  1 
ATOM   5625 N  N    A ILE   B 1 106 ? 33.477 -28.521 9.597   0.62 26.07 ?  106 ILE   B N    1 
ATOM   5626 N  N    B ILE   B 1 106 ? 33.461 -28.599 9.483   0.38 27.02 ?  106 ILE   B N    1 
ATOM   5627 C  CA   A ILE   B 1 106 ? 33.471 -28.709 8.151   0.62 25.29 ?  106 ILE   B CA   1 
ATOM   5628 C  CA   B ILE   B 1 106 ? 33.467 -28.739 8.032   0.38 26.42 ?  106 ILE   B CA   1 
ATOM   5629 C  C    A ILE   B 1 106 ? 32.369 -27.898 7.477   0.62 24.06 ?  106 ILE   B C    1 
ATOM   5630 C  C    B ILE   B 1 106 ? 32.363 -27.918 7.378   0.38 25.65 ?  106 ILE   B C    1 
ATOM   5631 O  O    A ILE   B 1 106 ? 32.475 -27.580 6.289   0.62 23.10 ?  106 ILE   B O    1 
ATOM   5632 O  O    B ILE   B 1 106 ? 32.437 -27.625 6.180   0.38 25.33 ?  106 ILE   B O    1 
ATOM   5633 C  CB   A ILE   B 1 106 ? 33.375 -30.217 7.822   0.62 26.20 ?  106 ILE   B CB   1 
ATOM   5634 C  CB   B ILE   B 1 106 ? 33.380 -30.237 7.657   0.38 26.81 ?  106 ILE   B CB   1 
ATOM   5635 C  CG1  A ILE   B 1 106 ? 33.625 -30.470 6.334   0.62 26.59 ?  106 ILE   B CG1  1 
ATOM   5636 C  CG1  B ILE   B 1 106 ? 33.658 -30.449 6.167   0.38 26.97 ?  106 ILE   B CG1  1 
ATOM   5637 C  CG2  A ILE   B 1 106 ? 32.018 -30.772 8.236   0.62 26.83 ?  106 ILE   B CG2  1 
ATOM   5638 C  CG2  B ILE   B 1 106 ? 32.017 -30.805 8.028   0.38 27.17 ?  106 ILE   B CG2  1 
ATOM   5639 C  CD1  A ILE   B 1 106 ? 34.986 -30.014 5.864   0.62 26.65 ?  106 ILE   B CD1  1 
ATOM   5640 C  CD1  B ILE   B 1 106 ? 35.016 -29.956 5.727   0.38 27.00 ?  106 ILE   B CD1  1 
ATOM   5641 H  H    A ILE   B 1 106 ? 33.378 -29.245 10.046  0.62 31.27 ?  106 ILE   B H    1 
ATOM   5642 H  H    B ILE   B 1 106 ? 33.352 -29.337 9.906   0.38 32.40 ?  106 ILE   B H    1 
ATOM   5643 H  HA   A ILE   B 1 106 ? 34.313 -28.387 7.805   0.62 30.33 ?  106 ILE   B HA   1 
ATOM   5644 H  HA   B ILE   B 1 106 ? 34.309 -28.400 7.704   0.38 31.69 ?  106 ILE   B HA   1 
ATOM   5645 H  HB   A ILE   B 1 106 ? 34.059 -30.685 8.328   0.62 31.43 ?  106 ILE   B HB   1 
ATOM   5646 H  HB   B ILE   B 1 106 ? 34.054 -30.716 8.161   0.38 32.15 ?  106 ILE   B HB   1 
ATOM   5647 H  HG12 A ILE   B 1 106 ? 33.561 -31.425 6.163   0.62 31.89 ?  106 ILE   B HG12 1 
ATOM   5648 H  HG12 B ILE   B 1 106 ? 33.614 -31.401 5.974   0.38 32.35 ?  106 ILE   B HG12 1 
ATOM   5649 H  HG13 A ILE   B 1 106 ? 32.957 -29.999 5.815   0.62 31.89 ?  106 ILE   B HG13 1 
ATOM   5650 H  HG13 B ILE   B 1 106 ? 32.988 -29.979 5.649   0.38 32.35 ?  106 ILE   B HG13 1 
ATOM   5651 H  HG21 A ILE   B 1 106 ? 32.035 -31.739 8.160   0.62 32.19 ?  106 ILE   B HG21 1 
ATOM   5652 H  HG21 B ILE   B 1 106 ? 32.039 -31.769 7.925   0.38 32.59 ?  106 ILE   B HG21 1 
ATOM   5653 H  HG22 A ILE   B 1 106 ? 31.840 -30.516 9.155   0.62 32.19 ?  106 ILE   B HG22 1 
ATOM   5654 H  HG22 B ILE   B 1 106 ? 31.821 -30.576 8.950   0.38 32.59 ?  106 ILE   B HG22 1 
ATOM   5655 H  HG23 A ILE   B 1 106 ? 31.334 -30.407 7.653   0.62 32.19 ?  106 ILE   B HG23 1 
ATOM   5656 H  HG23 B ILE   B 1 106 ? 31.343 -30.426 7.442   0.38 32.59 ?  106 ILE   B HG23 1 
ATOM   5657 H  HD11 A ILE   B 1 106 ? 35.176 -30.422 5.006   0.62 31.96 ?  106 ILE   B HD11 1 
ATOM   5658 H  HD11 B ILE   B 1 106 ? 35.226 -30.345 4.865   0.38 32.39 ?  106 ILE   B HD11 1 
ATOM   5659 H  HD12 A ILE   B 1 106 ? 34.983 -29.047 5.776   0.62 31.96 ?  106 ILE   B HD12 1 
ATOM   5660 H  HD12 B ILE   B 1 106 ? 34.993 -28.989 5.657   0.38 32.39 ?  106 ILE   B HD12 1 
ATOM   5661 H  HD13 A ILE   B 1 106 ? 35.653 -30.286 6.515   0.62 31.96 ?  106 ILE   B HD13 1 
ATOM   5662 H  HD13 B ILE   B 1 106 ? 35.677 -30.228 6.383   0.38 32.39 ?  106 ILE   B HD13 1 
ATOM   5663 N  N    A GLN   B 1 107 ? 31.310 -27.545 8.208   0.62 24.51 ?  107 GLN   B N    1 
ATOM   5664 N  N    B GLN   B 1 107 ? 31.337 -27.532 8.139   0.38 25.62 ?  107 GLN   B N    1 
ATOM   5665 C  CA   A GLN   B 1 107 ? 30.241 -26.735 7.632   0.62 24.93 ?  107 GLN   B CA   1 
ATOM   5666 C  CA   B GLN   B 1 107 ? 30.252 -26.732 7.583   0.38 25.49 ?  107 GLN   B CA   1 
ATOM   5667 C  C    A GLN   B 1 107 ? 30.735 -25.389 7.107   0.62 22.78 ?  107 GLN   B C    1 
ATOM   5668 C  C    B GLN   B 1 107 ? 30.726 -25.364 7.110   0.38 23.17 ?  107 GLN   B C    1 
ATOM   5669 O  O    A GLN   B 1 107 ? 30.094 -24.816 6.222   0.62 23.16 ?  107 GLN   B O    1 
ATOM   5670 O  O    B GLN   B 1 107 ? 30.058 -24.748 6.274   0.38 23.42 ?  107 GLN   B O    1 
ATOM   5671 C  CB   A GLN   B 1 107 ? 29.137 -26.516 8.672   0.62 28.58 ?  107 GLN   B CB   1 
ATOM   5672 C  CB   B GLN   B 1 107 ? 29.138 -26.576 8.622   0.38 28.10 ?  107 GLN   B CB   1 
ATOM   5673 C  CG   A GLN   B 1 107 ? 27.811 -26.008 8.103   0.62 32.17 ?  107 GLN   B CG   1 
ATOM   5674 C  CG   B GLN   B 1 107 ? 27.812 -26.067 8.071   0.38 30.58 ?  107 GLN   B CG   1 
ATOM   5675 C  CD   A GLN   B 1 107 ? 27.751 -24.494 7.980   0.62 34.91 ?  107 GLN   B CD   1 
ATOM   5676 C  CD   B GLN   B 1 107 ? 27.713 -24.552 8.072   0.38 32.54 ?  107 GLN   B CD   1 
ATOM   5677 O  OE1  A GLN   B 1 107 ? 28.595 -23.780 8.526   0.62 35.90 ?  107 GLN   B OE1  1 
ATOM   5678 O  OE1  B GLN   B 1 107 ? 28.550 -23.862 8.655   0.38 33.20 ?  107 GLN   B OE1  1 
ATOM   5679 N  NE2  A GLN   B 1 107 ? 26.745 -23.995 7.262   0.62 35.81 ?  107 GLN   B NE2  1 
ATOM   5680 N  NE2  B GLN   B 1 107 ? 26.681 -24.026 7.419   0.38 33.23 ?  107 GLN   B NE2  1 
ATOM   5681 H  H    A GLN   B 1 107 ? 31.187 -27.770 9.023   0.62 29.40 ?  107 GLN   B H    1 
ATOM   5682 H  H    B GLN   B 1 107 ? 31.244 -27.718 8.970   0.38 30.72 ?  107 GLN   B H    1 
ATOM   5683 H  HA   A GLN   B 1 107 ? 29.851 -27.218 6.883   0.62 29.90 ?  107 GLN   B HA   1 
ATOM   5684 H  HA   B GLN   B 1 107 ? 29.878 -27.197 6.819   0.38 30.58 ?  107 GLN   B HA   1 
ATOM   5685 H  HB2  A GLN   B 1 107 ? 28.960 -27.358 9.114   0.62 34.28 ?  107 GLN   B HB2  1 
ATOM   5686 H  HB2  B GLN   B 1 107 ? 28.972 -27.440 9.021   0.38 33.70 ?  107 GLN   B HB2  1 
ATOM   5687 H  HB3  A GLN   B 1 107 ? 29.450 -25.866 9.320   0.62 34.28 ?  107 GLN   B HB3  1 
ATOM   5688 H  HB3  B GLN   B 1 107 ? 29.434 -25.953 9.303   0.38 33.70 ?  107 GLN   B HB3  1 
ATOM   5689 H  HG2  A GLN   B 1 107 ? 27.681 -26.382 7.218   0.62 38.58 ?  107 GLN   B HG2  1 
ATOM   5690 H  HG2  B GLN   B 1 107 ? 27.708 -26.372 7.157   0.38 36.68 ?  107 GLN   B HG2  1 
ATOM   5691 H  HG3  A GLN   B 1 107 ? 27.089 -26.291 8.689   0.62 38.58 ?  107 GLN   B HG3  1 
ATOM   5692 H  HG3  B GLN   B 1 107 ? 27.089 -26.417 8.619   0.38 36.68 ?  107 GLN   B HG3  1 
ATOM   5693 H  HE21 A GLN   B 1 107 ? 26.174 -24.525 6.894   0.62 42.95 ?  107 GLN   B HE21 1 
ATOM   5694 H  HE21 B GLN   B 1 107 ? 26.115 -24.539 7.022   0.38 39.86 ?  107 GLN   B HE21 1 
ATOM   5695 H  HE22 A GLN   B 1 107 ? 26.662 -23.143 7.165   0.62 42.95 ?  107 GLN   B HE22 1 
ATOM   5696 H  HE22 B GLN   B 1 107 ? 26.578 -23.172 7.393   0.38 39.86 ?  107 GLN   B HE22 1 
ATOM   5697 N  N    . LEU   B 1 108 ? 31.859 -24.875 7.618   1.00 20.82 ?  108 LEU   B N    1 
ATOM   5698 C  CA   . LEU   B 1 108 ? 32.387 -23.572 7.206   1.00 18.39 ?  108 LEU   B CA   1 
ATOM   5699 C  C    . LEU   B 1 108 ? 33.036 -23.591 5.831   1.00 15.80 ?  108 LEU   B C    1 
ATOM   5700 O  O    . LEU   B 1 108 ? 33.470 -22.533 5.347   1.00 15.15 ?  108 LEU   B O    1 
ATOM   5701 C  CB   . LEU   B 1 108 ? 33.389 -23.061 8.240   1.00 18.81 ?  108 LEU   B CB   1 
ATOM   5702 C  CG   . LEU   B 1 108 ? 32.757 -22.606 9.553   1.00 20.10 ?  108 LEU   B CG   1 
ATOM   5703 C  CD1  . LEU   B 1 108 ? 33.771 -22.596 10.678  1.00 20.48 ?  108 LEU   B CD1  1 
ATOM   5704 C  CD2  . LEU   B 1 108 ? 32.159 -21.221 9.372   1.00 21.07 ?  108 LEU   B CD2  1 
ATOM   5705 H  H    A LEU   B 1 108 ? 32.330 -25.264 8.218   0.62 24.97 ?  108 LEU   B H    1 
ATOM   5706 H  H    B LEU   B 1 108 ? 32.329 -25.274 8.212   0.38 24.97 ?  108 LEU   B H    1 
ATOM   5707 H  HA   . LEU   B 1 108 ? 31.651 -22.943 7.169   1.00 22.05 ?  108 LEU   B HA   1 
ATOM   5708 H  HB2  . LEU   B 1 108 ? 34.011 -23.772 8.448   1.00 22.56 ?  108 LEU   B HB2  1 
ATOM   5709 H  HB3  . LEU   B 1 108 ? 33.862 -22.305 7.865   1.00 22.56 ?  108 LEU   B HB3  1 
ATOM   5710 H  HG   . LEU   B 1 108 ? 32.037 -23.213 9.795   1.00 24.11 ?  108 LEU   B HG   1 
ATOM   5711 H  HD11 . LEU   B 1 108 ? 33.334 -22.307 11.496  1.00 24.56 ?  108 LEU   B HD11 1 
ATOM   5712 H  HD12 . LEU   B 1 108 ? 34.125 -23.491 10.791  1.00 24.56 ?  108 LEU   B HD12 1 
ATOM   5713 H  HD13 . LEU   B 1 108 ? 34.486 -21.981 10.452  1.00 24.56 ?  108 LEU   B HD13 1 
ATOM   5714 H  HD21 . LEU   B 1 108 ? 31.777 -20.928 10.215  1.00 25.27 ?  108 LEU   B HD21 1 
ATOM   5715 H  HD22 . LEU   B 1 108 ? 32.859 -20.609 9.097   1.00 25.27 ?  108 LEU   B HD22 1 
ATOM   5716 H  HD23 . LEU   B 1 108 ? 31.467 -21.259 8.692   1.00 25.27 ?  108 LEU   B HD23 1 
ATOM   5717 N  N    . LEU   B 1 109 ? 33.105 -24.760 5.199   1.00 14.56 ?  109 LEU   B N    1 
ATOM   5718 C  CA   . LEU   B 1 109 ? 33.732 -24.865 3.892   1.00 13.58 ?  109 LEU   B CA   1 
ATOM   5719 C  C    . LEU   B 1 109 ? 32.967 -24.081 2.833   1.00 12.99 ?  109 LEU   B C    1 
ATOM   5720 O  O    . LEU   B 1 109 ? 33.578 -23.487 1.937   1.00 12.68 ?  109 LEU   B O    1 
ATOM   5721 C  CB   . LEU   B 1 109 ? 33.844 -26.338 3.513   1.00 13.82 ?  109 LEU   B CB   1 
ATOM   5722 C  CG   . LEU   B 1 109 ? 34.632 -26.678 2.255   1.00 13.57 ?  109 LEU   B CG   1 
ATOM   5723 C  CD1  . LEU   B 1 109 ? 36.015 -26.035 2.279   1.00 13.71 ?  109 LEU   B CD1  1 
ATOM   5724 C  CD2  . LEU   B 1 109 ? 34.745 -28.189 2.120   1.00 14.40 ?  109 LEU   B CD2  1 
ATOM   5725 H  H    . LEU   B 1 109 ? 32.804 -25.504 5.500   1.00 17.45 ?  109 LEU   B H    1 
ATOM   5726 H  HA   . LEU   B 1 109 ? 34.626 -24.503 3.936   1.00 16.28 ?  109 LEU   B HA   1 
ATOM   5727 H  HB2  . LEU   B 1 109 ? 34.273 -26.809 4.246   1.00 16.57 ?  109 LEU   B HB2  1 
ATOM   5728 H  HB3  . LEU   B 1 109 ? 32.950 -26.695 3.389   1.00 16.57 ?  109 LEU   B HB3  1 
ATOM   5729 H  HG   . LEU   B 1 109 ? 34.156 -26.351 1.474   1.00 16.27 ?  109 LEU   B HG   1 
ATOM   5730 H  HD11 . LEU   B 1 109 ? 36.552 -26.406 1.560   1.00 16.44 ?  109 LEU   B HD11 1 
ATOM   5731 H  HD12 . LEU   B 1 109 ? 35.917 -25.079 2.156   1.00 16.44 ?  109 LEU   B HD12 1 
ATOM   5732 H  HD13 . LEU   B 1 109 ? 36.434 -26.222 3.133   1.00 16.44 ?  109 LEU   B HD13 1 
ATOM   5733 H  HD21 . LEU   B 1 109 ? 35.315 -28.401 1.361   1.00 17.27 ?  109 LEU   B HD21 1 
ATOM   5734 H  HD22 . LEU   B 1 109 ? 35.131 -28.553 2.931   1.00 17.27 ?  109 LEU   B HD22 1 
ATOM   5735 H  HD23 . LEU   B 1 109 ? 33.860 -28.564 1.978   1.00 17.27 ?  109 LEU   B HD23 1 
ATOM   5736 N  N    . LYS   B 1 110 ? 31.635 -24.052 2.915   1.00 12.90 ?  110 LYS   B N    1 
ATOM   5737 C  CA   . LYS   B 1 110 ? 30.876 -23.287 1.930   1.00 12.52 ?  110 LYS   B CA   1 
ATOM   5738 C  C    . LYS   B 1 110 ? 31.211 -21.797 2.019   1.00 12.32 ?  110 LYS   B C    1 
ATOM   5739 O  O    . LYS   B 1 110 ? 31.466 -21.149 0.998   1.00 12.20 ?  110 LYS   B O    1 
ATOM   5740 C  CB   . LYS   B 1 110 ? 29.371 -23.536 2.081   1.00 13.25 ?  110 LYS   B CB   1 
ATOM   5741 C  CG   . LYS   B 1 110 ? 28.566 -22.904 0.949   1.00 13.64 ?  110 LYS   B CG   1 
ATOM   5742 C  CD   . LYS   B 1 110 ? 27.094 -23.335 0.967   1.00 13.86 ?  110 LYS   B CD   1 
ATOM   5743 C  CE   . LYS   B 1 110 ? 26.334 -22.799 -0.244  1.00 14.56 ?  110 LYS   B CE   1 
ATOM   5744 N  NZ   . LYS   B 1 110 ? 26.664 -23.524 -1.502  1.00 14.81 ?  110 LYS   B NZ   1 
ATOM   5745 H  H    . LYS   B 1 110 ? 31.163 -24.455 3.506   1.00 15.46 ?  110 LYS   B H    1 
ATOM   5746 H  HA   . LYS   B 1 110 ? 31.130 -23.588 1.040   1.00 15.01 ?  110 LYS   B HA   1 
ATOM   5747 H  HB2  . LYS   B 1 110 ? 29.205 -24.494 2.068   1.00 15.89 ?  110 LYS   B HB2  1 
ATOM   5748 H  HB3  . LYS   B 1 110 ? 29.067 -23.157 2.918   1.00 15.89 ?  110 LYS   B HB3  1 
ATOM   5749 H  HG2  . LYS   B 1 110 ? 28.589 -21.938 1.041   1.00 16.35 ?  110 LYS   B HG2  1 
ATOM   5750 H  HG3  . LYS   B 1 110 ? 28.943 -23.168 0.098   1.00 16.35 ?  110 LYS   B HG3  1 
ATOM   5751 H  HD2  . LYS   B 1 110 ? 27.045 -24.309 0.950   1.00 16.62 ?  110 LYS   B HD2  1 
ATOM   5752 H  HD3  . LYS   B 1 110 ? 26.666 -22.998 1.771   1.00 16.62 ?  110 LYS   B HD3  1 
ATOM   5753 H  HE2  . LYS   B 1 110 ? 25.382 -22.889 -0.089  1.00 17.45 ?  110 LYS   B HE2  1 
ATOM   5754 H  HE3  . LYS   B 1 110 ? 26.564 -21.865 -0.370  1.00 17.45 ?  110 LYS   B HE3  1 
ATOM   5755 H  HZ1  . LYS   B 1 110 ? 26.207 -23.181 -2.180  1.00 17.75 ?  110 LYS   B HZ1  1 
ATOM   5756 H  HZ2  . LYS   B 1 110 ? 27.536 -23.453 -1.673  1.00 17.75 ?  110 LYS   B HZ2  1 
ATOM   5757 H  HZ3  . LYS   B 1 110 ? 26.458 -24.386 -1.417  1.00 17.75 ?  110 LYS   B HZ3  1 
ATOM   5758 N  N    . SER   B 1 111 ? 31.229 -21.243 3.238   1.00 12.72 ?  111 SER   B N    1 
ATOM   5759 C  CA   . SER   B 1 111 ? 31.624 -19.846 3.415   1.00 12.51 ?  111 SER   B CA   1 
ATOM   5760 C  C    . SER   B 1 111 ? 33.006 -19.591 2.828   1.00 12.06 ?  111 SER   B C    1 
ATOM   5761 O  O    . SER   B 1 111 ? 33.237 -18.556 2.184   1.00 12.29 ?  111 SER   B O    1 
ATOM   5762 C  CB   . SER   B 1 111 ? 31.618 -19.484 4.900   1.00 13.83 ?  111 SER   B CB   1 
ATOM   5763 O  OG   . SER   B 1 111 ? 30.310 -19.481 5.428   1.00 15.34 ?  111 SER   B OG   1 
ATOM   5764 H  H    . SER   B 1 111 ? 31.024 -21.658 3.962   1.00 15.24 ?  111 SER   B H    1 
ATOM   5765 H  HA   . SER   B 1 111 ? 30.992 -19.277 2.958   1.00 14.99 ?  111 SER   B HA   1 
ATOM   5766 H  HB2  . SER   B 1 111 ? 32.143 -20.139 5.387   1.00 16.57 ?  111 SER   B HB2  1 
ATOM   5767 H  HB3  . SER   B 1 111 ? 32.005 -18.604 5.009   1.00 16.57 ?  111 SER   B HB3  1 
ATOM   5768 H  HG   . SER   B 1 111 ? 30.327 -19.270 6.246   1.00 18.40 ?  111 SER   B HG   1 
ATOM   5769 N  N    . ALA   B 1 112 ? 33.942 -20.515 3.050   1.00 11.88 ?  112 ALA   B N    1 
ATOM   5770 C  CA   . ALA   B 1 112 ? 35.285 -20.342 2.505   1.00 11.77 ?  112 ALA   B CA   1 
ATOM   5771 C  C    . ALA   B 1 112 ? 35.252 -20.245 0.982   1.00 11.12 ?  112 ALA   B C    1 
ATOM   5772 O  O    . ALA   B 1 112 ? 35.878 -19.357 0.390   1.00 11.51 ?  112 ALA   B O    1 
ATOM   5773 C  CB   . ALA   B 1 112 ? 36.187 -21.482 2.983   1.00 12.26 ?  112 ALA   B CB   1 
ATOM   5774 H  H    . ALA   B 1 112 ? 33.829 -21.235 3.517   1.00 14.24 ?  112 ALA   B H    1 
ATOM   5775 H  HA   . ALA   B 1 112 ? 35.650 -19.513 2.851   1.00 14.11 ?  112 ALA   B HA   1 
ATOM   5776 H  HB1  . ALA   B 1 112 ? 37.077 -21.347 2.617   1.00 14.70 ?  112 ALA   B HB1  1 
ATOM   5777 H  HB2  . ALA   B 1 112 ? 36.228 -21.466 3.955   1.00 14.70 ?  112 ALA   B HB2  1 
ATOM   5778 H  HB3  . ALA   B 1 112 ? 35.824 -22.323 2.679   1.00 14.70 ?  112 ALA   B HB3  1 
ATOM   5779 N  N    . TYR   B 1 113 ? 34.522 -21.150 0.325   1.00 11.24 ?  113 TYR   B N    1 
ATOM   5780 C  CA   . TYR   B 1 113 ? 34.445 -21.101 -1.130  1.00 10.86 ?  113 TYR   B CA   1 
ATOM   5781 C  C    . TYR   B 1 113 ? 33.737 -19.850 -1.645  1.00 10.37 ?  113 TYR   B C    1 
ATOM   5782 O  O    . TYR   B 1 113 ? 34.008 -19.415 -2.771  1.00 10.45 ?  113 TYR   B O    1 
ATOM   5783 C  CB   . TYR   B 1 113 ? 33.775 -22.362 -1.670  1.00 11.21 ?  113 TYR   B CB   1 
ATOM   5784 C  CG   . TYR   B 1 113 ? 34.735 -23.508 -1.932  1.00 11.47 ?  113 TYR   B CG   1 
ATOM   5785 C  CD1  . TYR   B 1 113 ? 35.726 -23.398 -2.901  1.00 12.10 ?  113 TYR   B CD1  1 
ATOM   5786 C  CD2  . TYR   B 1 113 ? 34.642 -24.694 -1.227  1.00 11.69 ?  113 TYR   B CD2  1 
ATOM   5787 C  CE1  . TYR   B 1 113 ? 36.607 -24.432 -3.150  1.00 12.14 ?  113 TYR   B CE1  1 
ATOM   5788 C  CE2  . TYR   B 1 113 ? 35.514 -25.740 -1.474  1.00 12.10 ?  113 TYR   B CE2  1 
ATOM   5789 C  CZ   . TYR   B 1 113 ? 36.489 -25.608 -2.441  1.00 12.01 ?  113 TYR   B CZ   1 
ATOM   5790 O  OH   . TYR   B 1 113 ? 37.370 -26.627 -2.717  1.00 12.89 ?  113 TYR   B OH   1 
ATOM   5791 H  H    . TYR   B 1 113 ? 34.062 -21.782 0.697   1.00 13.48 ?  113 TYR   B H    1 
ATOM   5792 H  HA   . TYR   B 1 113 ? 35.347 -21.085 -1.468  1.00 13.01 ?  113 TYR   B HA   1 
ATOM   5793 H  HB2  . TYR   B 1 113 ? 33.118 -22.675 -1.023  1.00 13.44 ?  113 TYR   B HB2  1 
ATOM   5794 H  HB3  . TYR   B 1 113 ? 33.332 -22.147 -2.504  1.00 13.44 ?  113 TYR   B HB3  1 
ATOM   5795 H  HD1  . TYR   B 1 113 ? 35.807 -22.601 -3.384  1.00 14.51 ?  113 TYR   B HD1  1 
ATOM   5796 H  HD2  . TYR   B 1 113 ? 33.975 -24.789 -0.587  1.00 14.01 ?  113 TYR   B HD2  1 
ATOM   5797 H  HE1  . TYR   B 1 113 ? 37.264 -24.340 -3.809  1.00 14.55 ?  113 TYR   B HE1  1 
ATOM   5798 H  HE2  . TYR   B 1 113 ? 35.426 -26.537 -1.004  1.00 14.50 ?  113 TYR   B HE2  1 
ATOM   5799 H  HH   . TYR   B 1 113 ? 37.197 -27.297 -2.243  1.00 15.45 ?  113 TYR   B HH   1 
ATOM   5800 N  N    . GLU   B 1 114 ? 32.819 -19.268 -0.864  1.00 10.82 ?  114 GLU   B N    1 
ATOM   5801 C  CA   . GLU   B 1 114 ? 32.130 -18.064 -1.326  1.00 10.90 ?  114 GLU   B CA   1 
ATOM   5802 C  C    . GLU   B 1 114 ? 33.114 -16.942 -1.625  1.00 10.33 ?  114 GLU   B C    1 
ATOM   5803 O  O    . GLU   B 1 114 ? 32.837 -16.080 -2.465  1.00 10.91 ?  114 GLU   B O    1 
ATOM   5804 C  CB   . GLU   B 1 114 ? 31.071 -17.635 -0.307  1.00 11.28 ?  114 GLU   B CB   1 
ATOM   5805 C  CG   . GLU   B 1 114 ? 29.852 -18.552 -0.375  1.00 11.46 ?  114 GLU   B CG   1 
ATOM   5806 C  CD   . GLU   B 1 114 ? 28.835 -18.361 0.736   1.00 11.75 ?  114 GLU   B CD   1 
ATOM   5807 O  OE1  . GLU   B 1 114 ? 29.129 -17.738 1.777   1.00 11.99 ?  114 GLU   B OE1  1 
ATOM   5808 O  OE2  . GLU   B 1 114 ? 27.712 -18.898 0.578   1.00 12.62 -1 114 GLU   B OE2  1 
ATOM   5809 H  H    . GLU   B 1 114 ? 32.575 -19.556 -0.086  1.00 12.96 ?  114 GLU   B H    1 
ATOM   5810 H  HA   . GLU   B 1 114 ? 31.671 -18.275 -2.149  1.00 13.06 ?  114 GLU   B HA   1 
ATOM   5811 H  HB2  . GLU   B 1 114 ? 31.442 -17.689 0.590   1.00 13.52 ?  114 GLU   B HB2  1 
ATOM   5812 H  HB3  . GLU   B 1 114 ? 30.785 -16.733 -0.502  1.00 13.52 ?  114 GLU   B HB3  1 
ATOM   5813 H  HG2  . GLU   B 1 114 ? 29.401 -18.400 -1.217  1.00 13.74 ?  114 GLU   B HG2  1 
ATOM   5814 H  HG3  . GLU   B 1 114 ? 30.159 -19.474 -0.333  1.00 13.74 ?  114 GLU   B HG3  1 
ATOM   5815 N  N    . ASN   B 1 115 ? 34.281 -16.941 -0.976  1.00 10.63 ?  115 ASN   B N    1 
ATOM   5816 C  CA   . ASN   B 1 115 ? 35.268 -15.905 -1.270  1.00 10.48 ?  115 ASN   B CA   1 
ATOM   5817 C  C    . ASN   B 1 115 ? 35.683 -15.927 -2.734  1.00 10.20 ?  115 ASN   B C    1 
ATOM   5818 O  O    . ASN   B 1 115 ? 36.070 -14.887 -3.287  1.00 10.78 ?  115 ASN   B O    1 
ATOM   5819 C  CB   . ASN   B 1 115 ? 36.509 -16.082 -0.391  1.00 11.16 ?  115 ASN   B CB   1 
ATOM   5820 C  CG   . ASN   B 1 115 ? 36.248 -15.815 1.073   1.00 11.52 ?  115 ASN   B CG   1 
ATOM   5821 O  OD1  . ASN   B 1 115 ? 36.253 -14.671 1.517   1.00 13.41 ?  115 ASN   B OD1  1 
ATOM   5822 N  ND2  . ASN   B 1 115 ? 36.078 -16.881 1.847   1.00 11.54 ?  115 ASN   B ND2  1 
ATOM   5823 H  H    . ASN   B 1 115 ? 34.520 -17.511 -0.371  1.00 12.74 ?  115 ASN   B H    1 
ATOM   5824 H  HA   . ASN   B 1 115 ? 34.888 -15.036 -1.077  1.00 12.56 ?  115 ASN   B HA   1 
ATOM   5825 H  HB2  . ASN   B 1 115 ? 36.831 -16.995 -0.479  1.00 13.37 ?  115 ASN   B HB2  1 
ATOM   5826 H  HB3  . ASN   B 1 115 ? 37.196 -15.464 -0.685  1.00 13.37 ?  115 ASN   B HB3  1 
ATOM   5827 H  HD21 . ASN   B 1 115 ? 35.936 -16.781 2.689   1.00 13.83 ?  115 ASN   B HD21 1 
ATOM   5828 H  HD22 . ASN   B 1 115 ? 36.097 -17.671 1.506   1.00 13.83 ?  115 ASN   B HD22 1 
ATOM   5829 N  N    . PHE   B 1 116 ? 35.657 -17.105 -3.369  1.00 9.97  ?  116 PHE   B N    1 
ATOM   5830 C  CA   . PHE   B 1 116 ? 36.091 -17.196 -4.758  1.00 10.28 ?  116 PHE   B CA   1 
ATOM   5831 C  C    . PHE   B 1 116 ? 35.189 -16.373 -5.674  1.00 10.01 ?  116 PHE   B C    1 
ATOM   5832 O  O    . PHE   B 1 116 ? 35.624 -15.946 -6.747  1.00 10.79 ?  116 PHE   B O    1 
ATOM   5833 C  CB   . PHE   B 1 116 ? 36.055 -18.643 -5.276  1.00 10.27 ?  116 PHE   B CB   1 
ATOM   5834 C  CG   . PHE   B 1 116 ? 37.126 -19.599 -4.728  1.00 10.05 ?  116 PHE   B CG   1 
ATOM   5835 C  CD1  . PHE   B 1 116 ? 37.776 -19.419 -3.517  1.00 10.97 ?  116 PHE   B CD1  1 
ATOM   5836 C  CD2  . PHE   B 1 116 ? 37.429 -20.733 -5.460  1.00 10.44 ?  116 PHE   B CD2  1 
ATOM   5837 C  CE1  . PHE   B 1 116 ? 38.709 -20.358 -3.062  1.00 11.09 ?  116 PHE   B CE1  1 
ATOM   5838 C  CE2  . PHE   B 1 116 ? 38.357 -21.667 -5.012  1.00 10.76 ?  116 PHE   B CE2  1 
ATOM   5839 C  CZ   . PHE   B 1 116 ? 38.994 -21.483 -3.817  1.00 10.67 ?  116 PHE   B CZ   1 
ATOM   5840 H  H    . PHE   B 1 116 ? 35.397 -17.855 -3.021  1.00 11.95 ?  116 PHE   B H    1 
ATOM   5841 H  HA   . PHE   B 1 116 ? 37.001 -16.868 -4.837  1.00 12.32 ?  116 PHE   B HA   1 
ATOM   5842 H  HB2  . PHE   B 1 116 ? 35.186 -19.020 -5.049  1.00 12.31 ?  116 PHE   B HB2  1 
ATOM   5843 H  HB3  . PHE   B 1 116 ? 36.151 -18.622 -6.239  1.00 12.31 ?  116 PHE   B HB3  1 
ATOM   5844 H  HD1  . PHE   B 1 116 ? 37.576 -18.671 -2.995  1.00 13.14 ?  116 PHE   B HD1  1 
ATOM   5845 H  HD2  . PHE   B 1 116 ? 36.997 -20.882 -6.267  1.00 12.51 ?  116 PHE   B HD2  1 
ATOM   5846 H  HE1  . PHE   B 1 116 ? 39.139 -20.223 -2.251  1.00 13.29 ?  116 PHE   B HE1  1 
ATOM   5847 H  HE2  . PHE   B 1 116 ? 38.551 -22.420 -5.524  1.00 12.89 ?  116 PHE   B HE2  1 
ATOM   5848 H  HZ   . PHE   B 1 116 ? 39.626 -22.098 -3.518  1.00 12.79 ?  116 PHE   B HZ   1 
ATOM   5849 N  N    . ASN   B 1 117 ? 33.922 -16.171 -5.289  1.00 10.46 ?  117 ASN   B N    1 
ATOM   5850 C  CA   . ASN   B 1 117 ? 32.973 -15.464 -6.149  1.00 10.65 ?  117 ASN   B CA   1 
ATOM   5851 C  C    . ASN   B 1 117 ? 33.289 -13.985 -6.299  1.00 11.02 ?  117 ASN   B C    1 
ATOM   5852 O  O    . ASN   B 1 117 ? 32.690 -13.330 -7.156  1.00 12.08 ?  117 ASN   B O    1 
ATOM   5853 C  CB   . ASN   B 1 117 ? 31.548 -15.688 -5.657  1.00 10.86 ?  117 ASN   B CB   1 
ATOM   5854 C  CG   . ASN   B 1 117 ? 31.099 -17.099 -5.901  1.00 11.14 ?  117 ASN   B CG   1 
ATOM   5855 O  OD1  . ASN   B 1 117 ? 31.447 -17.689 -6.924  1.00 12.11 ?  117 ASN   B OD1  1 
ATOM   5856 N  ND2  . ASN   B 1 117 ? 30.362 -17.668 -4.957  1.00 11.40 ?  117 ASN   B ND2  1 
ATOM   5857 H  H    . ASN   B 1 117 ? 33.595 -16.433 -4.532  1.00 12.53 ?  117 ASN   B H    1 
ATOM   5858 H  HA   . ASN   B 1 117 ? 33.034 -15.861 -7.028  1.00 12.77 ?  117 ASN   B HA   1 
ATOM   5859 H  HB2  . ASN   B 1 117 ? 31.509 -15.517 -4.699  1.00 13.01 ?  117 ASN   B HB2  1 
ATOM   5860 H  HB3  . ASN   B 1 117 ? 30.954 -15.082 -6.127  1.00 13.01 ?  117 ASN   B HB3  1 
ATOM   5861 H  HD21 . ASN   B 1 117 ? 30.081 -18.473 -5.058  1.00 13.66 ?  117 ASN   B HD21 1 
ATOM   5862 H  HD22 . ASN   B 1 117 ? 30.146 -17.222 -4.253  1.00 13.66 ?  117 ASN   B HD22 1 
ATOM   5863 N  N    . GLN   B 1 118 ? 34.228 -13.458 -5.523  1.00 10.74 ?  118 GLN   B N    1 
ATOM   5864 C  CA   . GLN   B 1 118 ? 34.655 -12.073 -5.662  1.00 11.38 ?  118 GLN   B CA   1 
ATOM   5865 C  C    . GLN   B 1 118 ? 35.719 -11.883 -6.738  1.00 11.49 ?  118 GLN   B C    1 
ATOM   5866 O  O    . GLN   B 1 118 ? 36.197 -10.759 -6.919  1.00 12.86 ?  118 GLN   B O    1 
ATOM   5867 C  CB   . GLN   B 1 118 ? 35.137 -11.546 -4.308  1.00 12.00 ?  118 GLN   B CB   1 
ATOM   5868 C  CG   . GLN   B 1 118 ? 34.049 -11.584 -3.241  1.00 11.97 ?  118 GLN   B CG   1 
ATOM   5869 C  CD   . GLN   B 1 118 ? 32.877 -10.676 -3.575  1.00 11.81 ?  118 GLN   B CD   1 
ATOM   5870 O  OE1  . GLN   B 1 118 ? 33.064 -9.537  -4.014  1.00 12.61 ?  118 GLN   B OE1  1 
ATOM   5871 N  NE2  . GLN   B 1 118 ? 31.661 -11.176 -3.375  1.00 12.19 ?  118 GLN   B NE2  1 
ATOM   5872 H  H    . GLN   B 1 118 ? 34.654 -13.890 -4.909  1.00 12.87 ?  118 GLN   B H    1 
ATOM   5873 H  HA   . GLN   B 1 118 ? 33.885 -11.546 -5.928  1.00 13.64 ?  118 GLN   B HA   1 
ATOM   5874 H  HB2  . GLN   B 1 118 ? 35.882 -12.081 -4.002  1.00 14.38 ?  118 GLN   B HB2  1 
ATOM   5875 H  HB3  . GLN   B 1 118 ? 35.419 -10.617 -4.413  1.00 14.38 ?  118 GLN   B HB3  1 
ATOM   5876 H  HG2  . GLN   B 1 118 ? 33.716 -12.491 -3.163  1.00 14.35 ?  118 GLN   B HG2  1 
ATOM   5877 H  HG3  . GLN   B 1 118 ? 34.424 -11.292 -2.395  1.00 14.35 ?  118 GLN   B HG3  1 
ATOM   5878 H  HE21 . GLN   B 1 118 ? 31.575 -11.975 -3.063  1.00 14.61 ?  118 GLN   B HE21 1 
ATOM   5879 H  HE22 . GLN   B 1 118 ? 30.973 -10.702 -3.547  1.00 14.61 ?  118 GLN   B HE22 1 
ATOM   5880 N  N    . HIS   B 1 119 ? 36.073 -12.942 -7.468  1.00 10.99 ?  119 HIS   B N    1 
ATOM   5881 C  CA   . HIS   B 1 119 ? 37.114 -12.895 -8.484  1.00 11.24 ?  119 HIS   B CA   1 
ATOM   5882 C  C    . HIS   B 1 119 ? 36.630 -13.625 -9.723  1.00 11.03 ?  119 HIS   B C    1 
ATOM   5883 O  O    . HIS   B 1 119 ? 36.115 -14.739 -9.622  1.00 11.75 ?  119 HIS   B O    1 
ATOM   5884 C  CB   . HIS   B 1 119 ? 38.397 -13.523 -7.940  1.00 11.74 ?  119 HIS   B CB   1 
ATOM   5885 C  CG   . HIS   B 1 119 ? 38.883 -12.825 -6.718  1.00 12.87 ?  119 HIS   B CG   1 
ATOM   5886 N  ND1  . HIS   B 1 119 ? 39.682 -11.703 -6.777  1.00 14.41 ?  119 HIS   B ND1  1 
ATOM   5887 C  CD2  . HIS   B 1 119 ? 38.591 -13.018 -5.411  1.00 14.14 ?  119 HIS   B CD2  1 
ATOM   5888 C  CE1  . HIS   B 1 119 ? 39.894 -11.262 -5.550  1.00 15.50 ?  119 HIS   B CE1  1 
ATOM   5889 N  NE2  . HIS   B 1 119 ? 39.236 -12.034 -4.704  1.00 15.58 ?  119 HIS   B NE2  1 
ATOM   5890 H  H    . HIS   B 1 119 ? 35.709 -13.721 -7.395  1.00 13.17 ?  119 HIS   B H    1 
ATOM   5891 H  HA   . HIS   B 1 119 ? 37.295 -11.972 -8.726  1.00 13.48 ?  119 HIS   B HA   1 
ATOM   5892 H  HB2  . HIS   B 1 119 ? 38.228 -14.448 -7.717  1.00 14.07 ?  119 HIS   B HB2  1 
ATOM   5893 H  HB3  . HIS   B 1 119 ? 39.091 -13.462 -8.618  1.00 14.07 ?  119 HIS   B HB3  1 
ATOM   5894 H  HD2  . HIS   B 1 119 ? 38.051 -13.690 -5.058  1.00 16.96 ?  119 HIS   B HD2  1 
ATOM   5895 H  HE1  . HIS   B 1 119 ? 40.424 -10.535 -5.317  1.00 18.59 ?  119 HIS   B HE1  1 
ATOM   5896 H  HE2  . HIS   B 1 119 ? 39.237 -11.954 -3.846  1.00 18.69 ?  119 HIS   B HE2  1 
ATOM   5897 N  N    . GLU   B 1 120 ? 36.779 -13.006 -10.892 1.00 11.84 ?  120 GLU   B N    1 
ATOM   5898 C  CA   . GLU   B 1 120 ? 36.185 -13.588 -12.093 1.00 13.08 ?  120 GLU   B CA   1 
ATOM   5899 C  C    . GLU   B 1 120 ? 36.859 -14.888 -12.510 1.00 12.08 ?  120 GLU   B C    1 
ATOM   5900 O  O    . GLU   B 1 120 ? 36.193 -15.761 -13.084 1.00 12.17 ?  120 GLU   B O    1 
ATOM   5901 C  CB   . GLU   B 1 120 ? 36.199 -12.583 -13.244 1.00 17.74 ?  120 GLU   B CB   1 
ATOM   5902 C  CG   . GLU   B 1 120 ? 35.233 -11.432 -13.039 1.00 23.81 ?  120 GLU   B CG   1 
ATOM   5903 C  CD   . GLU   B 1 120 ? 35.087 -10.550 -14.262 1.00 29.46 ?  120 GLU   B CD   1 
ATOM   5904 O  OE1  . GLU   B 1 120 ? 36.081 -10.381 -15.002 1.00 31.53 ?  120 GLU   B OE1  1 
ATOM   5905 O  OE2  . GLU   B 1 120 ? 33.974 -10.028 -14.481 1.00 32.08 -1 120 GLU   B OE2  1 
ATOM   5906 H  H    . GLU   B 1 120 ? 37.198 -12.263 -11.020 1.00 14.20 ?  120 GLU   B H    1 
ATOM   5907 H  HA   . GLU   B 1 120 ? 35.259 -13.796 -11.907 1.00 15.68 ?  120 GLU   B HA   1 
ATOM   5908 H  HB2  . GLU   B 1 120 ? 37.088 -12.212 -13.334 1.00 21.27 ?  120 GLU   B HB2  1 
ATOM   5909 H  HB3  . GLU   B 1 120 ? 35.946 -13.038 -14.066 1.00 21.27 ?  120 GLU   B HB3  1 
ATOM   5910 H  HG2  . GLU   B 1 120 ? 34.353 -11.788 -12.835 1.00 28.56 ?  120 GLU   B HG2  1 
ATOM   5911 H  HG3  . GLU   B 1 120 ? 35.546 -10.883 -12.306 1.00 28.56 ?  120 GLU   B HG3  1 
ATOM   5912 N  N    . VAL   B 1 121 ? 38.162 -15.027 -12.255 1.00 11.74 ?  121 VAL   B N    1 
ATOM   5913 C  CA   . VAL   B 1 121 ? 38.912 -16.233 -12.603 1.00 11.55 ?  121 VAL   B CA   1 
ATOM   5914 C  C    . VAL   B 1 121 ? 40.023 -16.441 -11.582 1.00 11.11 ?  121 VAL   B C    1 
ATOM   5915 O  O    . VAL   B 1 121 ? 40.698 -15.486 -11.187 1.00 11.83 ?  121 VAL   B O    1 
ATOM   5916 C  CB   . VAL   B 1 121 ? 39.425 -16.191 -14.062 1.00 13.36 ?  121 VAL   B CB   1 
ATOM   5917 C  CG1  . VAL   B 1 121 ? 40.277 -14.950 -14.323 1.00 14.59 ?  121 VAL   B CG1  1 
ATOM   5918 C  CG2  . VAL   B 1 121 ? 40.184 -17.469 -14.412 1.00 14.79 ?  121 VAL   B CG2  1 
ATOM   5919 H  H    . VAL   B 1 121 ? 38.646 -14.424 -11.877 1.00 14.07 ?  121 VAL   B H    1 
ATOM   5920 H  HA   . VAL   B 1 121 ? 38.308 -16.991 -12.537 1.00 13.84 ?  121 VAL   B HA   1 
ATOM   5921 H  HB   . VAL   B 1 121 ? 38.655 -16.144 -14.655 1.00 16.02 ?  121 VAL   B HB   1 
ATOM   5922 H  HG11 . VAL   B 1 121 ? 40.591 -14.966 -15.241 1.00 17.49 ?  121 VAL   B HG11 1 
ATOM   5923 H  HG12 . VAL   B 1 121 ? 39.734 -14.156 -14.177 1.00 17.49 ?  121 VAL   B HG12 1 
ATOM   5924 H  HG13 . VAL   B 1 121 ? 41.031 -14.949 -13.715 1.00 17.49 ?  121 VAL   B HG13 1 
ATOM   5925 H  HG21 . VAL   B 1 121 ? 40.381 -17.468 -15.364 1.00 17.74 ?  121 VAL   B HG21 1 
ATOM   5926 H  HG22 . VAL   B 1 121 ? 41.011 -17.495 -13.907 1.00 17.74 ?  121 VAL   B HG22 1 
ATOM   5927 H  HG23 . VAL   B 1 121 ? 39.634 -18.236 -14.191 1.00 17.74 ?  121 VAL   B HG23 1 
ATOM   5928 N  N    . LEU   B 1 122 ? 40.210 -17.694 -11.152 1.00 10.56 ?  122 LEU   B N    1 
ATOM   5929 C  CA   . LEU   B 1 122 ? 41.192 -18.043 -10.129 1.00 10.30 ?  122 LEU   B CA   1 
ATOM   5930 C  C    . LEU   B 1 122 ? 41.841 -19.380 -10.450 1.00 10.50 ?  122 LEU   B C    1 
ATOM   5931 O  O    . LEU   B 1 122 ? 41.180 -20.297 -10.951 1.00 11.65 ?  122 LEU   B O    1 
ATOM   5932 C  CB   . LEU   B 1 122 ? 40.545 -18.270 -8.748  1.00 12.10 ?  122 LEU   B CB   1 
ATOM   5933 C  CG   . LEU   B 1 122 ? 39.505 -17.259 -8.263  1.00 12.22 ?  122 LEU   B CG   1 
ATOM   5934 C  CD1  . LEU   B 1 122 ? 38.119 -17.631 -8.750  1.00 13.06 ?  122 LEU   B CD1  1 
ATOM   5935 C  CD2  . LEU   B 1 122 ? 39.536 -17.149 -6.752  1.00 11.91 ?  122 LEU   B CD2  1 
ATOM   5936 H  H    . LEU   B 1 122 ? 39.770 -18.375 -11.448 1.00 12.66 ?  122 LEU   B H    1 
ATOM   5937 H  HA   . LEU   B 1 122 ? 41.871 -17.354 -10.059 1.00 12.34 ?  122 LEU   B HA   1 
ATOM   5938 H  HB2  . LEU   B 1 122 ? 40.110 -19.132 -8.762  1.00 14.50 ?  122 LEU   B HB2  1 
ATOM   5939 H  HB3  . LEU   B 1 122 ? 41.252 -18.276 -8.087  1.00 14.50 ?  122 LEU   B HB3  1 
ATOM   5940 H  HG   . LEU   B 1 122 ? 39.722 -16.387 -8.628  1.00 14.65 ?  122 LEU   B HG   1 
ATOM   5941 H  HD11 . LEU   B 1 122 ? 37.479 -17.001 -8.385  1.00 15.65 ?  122 LEU   B HD11 1 
ATOM   5942 H  HD12 . LEU   B 1 122 ? 38.103 -17.589 -9.722  1.00 15.65 ?  122 LEU   B HD12 1 
ATOM   5943 H  HD13 . LEU   B 1 122 ? 37.910 -18.528 -8.455  1.00 15.65 ?  122 LEU   B HD13 1 
ATOM   5944 H  HD21 . LEU   B 1 122 ? 38.849 -16.529 -6.464  1.00 14.28 ?  122 LEU   B HD21 1 
ATOM   5945 H  HD22 . LEU   B 1 122 ? 39.375 -18.025 -6.368  1.00 14.28 ?  122 LEU   B HD22 1 
ATOM   5946 H  HD23 . LEU   B 1 122 ? 40.410 -16.825 -6.478  1.00 14.28 ?  122 LEU   B HD23 1 
ATOM   5947 N  N    . LEU   B 1 123 ? 43.131 -19.489 -10.102 1.00 10.09 ?  123 LEU   B N    1 
ATOM   5948 C  CA   . LEU   B 1 123 ? 43.844 -20.758 -9.975  1.00 10.15 ?  123 LEU   B CA   1 
ATOM   5949 C  C    . LEU   B 1 123 ? 43.818 -21.154 -8.502  1.00 9.92  ?  123 LEU   B C    1 
ATOM   5950 O  O    . LEU   B 1 123 ? 44.173 -20.330 -7.648  1.00 10.45 ?  123 LEU   B O    1 
ATOM   5951 C  CB   . LEU   B 1 123 ? 45.294 -20.568 -10.433 1.00 10.75 ?  123 LEU   B CB   1 
ATOM   5952 C  CG   . LEU   B 1 123 ? 46.232 -21.758 -10.189 1.00 11.21 ?  123 LEU   B CG   1 
ATOM   5953 C  CD1  . LEU   B 1 123 ? 45.807 -23.001 -10.971 1.00 11.81 ?  123 LEU   B CD1  1 
ATOM   5954 C  CD2  . LEU   B 1 123 ? 47.653 -21.371 -10.554 1.00 12.21 ?  123 LEU   B CD2  1 
ATOM   5955 H  H    . LEU   B 1 123 ? 43.634 -18.809 -9.918  1.00 12.09 ?  123 LEU   B H    1 
ATOM   5956 H  HA   . LEU   B 1 123 ? 43.413 -21.449 -10.507 1.00 12.16 ?  123 LEU   B HA   1 
ATOM   5957 H  HB2  . LEU   B 1 123 ? 45.287 -20.395 -11.387 1.00 12.89 ?  123 LEU   B HB2  1 
ATOM   5958 H  HB3  . LEU   B 1 123 ? 45.661 -19.807 -9.965  1.00 12.89 ?  123 LEU   B HB3  1 
ATOM   5959 H  HG   . LEU   B 1 123 ? 46.224 -21.983 -9.247  1.00 13.44 ?  123 LEU   B HG   1 
ATOM   5960 H  HD11 . LEU   B 1 123 ? 46.444 -23.711 -10.802 1.00 14.15 ?  123 LEU   B HD11 1 
ATOM   5961 H  HD12 . LEU   B 1 123 ? 44.923 -23.270 -10.676 1.00 14.15 ?  123 LEU   B HD12 1 
ATOM   5962 H  HD13 . LEU   B 1 123 ? 45.791 -22.786 -11.916 1.00 14.15 ?  123 LEU   B HD13 1 
ATOM   5963 H  HD21 . LEU   B 1 123 ? 48.237 -22.128 -10.397 1.00 14.63 ?  123 LEU   B HD21 1 
ATOM   5964 H  HD22 . LEU   B 1 123 ? 47.681 -21.119 -11.492 1.00 14.63 ?  123 LEU   B HD22 1 
ATOM   5965 H  HD23 . LEU   B 1 123 ? 47.927 -20.621 -10.003 1.00 14.63 ?  123 LEU   B HD23 1 
ATOM   5966 N  N    . ALA   B 1 124 ? 43.388 -22.383 -8.192  1.00 9.71  ?  124 ALA   B N    1 
ATOM   5967 C  CA   . ALA   B 1 124 ? 43.130 -22.695 -6.795  1.00 9.96  ?  124 ALA   B CA   1 
ATOM   5968 C  C    . ALA   B 1 124 ? 43.407 -24.154 -6.470  1.00 9.82  ?  124 ALA   B C    1 
ATOM   5969 O  O    . ALA   B 1 124 ? 43.268 -25.031 -7.333  1.00 10.57 ?  124 ALA   B O    1 
ATOM   5970 C  CB   . ALA   B 1 124 ? 41.675 -22.379 -6.432  1.00 10.79 ?  124 ALA   B CB   1 
ATOM   5971 H  H    . ALA   B 1 124 ? 43.226 -23.023 -8.755  1.00 11.64 ?  124 ALA   B H    1 
ATOM   5972 H  HA   . ALA   B 1 124 ? 43.707 -22.145 -6.251  1.00 11.94 ?  124 ALA   B HA   1 
ATOM   5973 H  HB1  . ALA   B 1 124 ? 41.521 -22.593 -5.500  1.00 12.93 ?  124 ALA   B HB1  1 
ATOM   5974 H  HB2  . ALA   B 1 124 ? 41.512 -21.432 -6.586  1.00 12.93 ?  124 ALA   B HB2  1 
ATOM   5975 H  HB3  . ALA   B 1 124 ? 41.082 -22.906 -6.994  1.00 12.93 ?  124 ALA   B HB3  1 
ATOM   5976 N  N    . PRO   B 1 125 ? 43.706 -24.449 -5.205  1.00 10.09 ?  125 PRO   B N    1 
ATOM   5977 C  CA   . PRO   B 1 125 ? 43.640 -25.814 -4.680  1.00 10.85 ?  125 PRO   B CA   1 
ATOM   5978 C  C    . PRO   B 1 125 ? 42.239 -26.089 -4.133  1.00 10.81 ?  125 PRO   B C    1 
ATOM   5979 O  O    . PRO   B 1 125 ? 41.441 -25.174 -3.930  1.00 11.53 ?  125 PRO   B O    1 
ATOM   5980 C  CB   . PRO   B 1 125 ? 44.627 -25.737 -3.509  1.00 11.87 ?  125 PRO   B CB   1 
ATOM   5981 C  CG   . PRO   B 1 125 ? 44.373 -24.351 -2.940  1.00 11.95 ?  125 PRO   B CG   1 
ATOM   5982 C  CD   . PRO   B 1 125 ? 44.021 -23.478 -4.141  1.00 10.88 ?  125 PRO   B CD   1 
ATOM   5983 H  HA   . PRO   B 1 125 ? 43.914 -26.482 -5.326  1.00 13.00 ?  125 PRO   B HA   1 
ATOM   5984 H  HB2  . PRO   B 1 125 ? 44.427 -26.423 -2.849  1.00 14.23 ?  125 PRO   B HB2  1 
ATOM   5985 H  HB3  . PRO   B 1 125 ? 45.539 -25.817 -3.828  1.00 14.23 ?  125 PRO   B HB3  1 
ATOM   5986 H  HG2  . PRO   B 1 125 ? 43.632 -24.381 -2.310  1.00 14.32 ?  125 PRO   B HG2  1 
ATOM   5987 H  HG3  . PRO   B 1 125 ? 45.176 -24.021 -2.496  1.00 14.32 ?  125 PRO   B HG3  1 
ATOM   5988 H  HD2  . PRO   B 1 125 ? 43.252 -22.924 -3.945  1.00 13.04 ?  125 PRO   B HD2  1 
ATOM   5989 H  HD3  . PRO   B 1 125 ? 44.791 -22.937 -4.397  1.00 13.04 ?  125 PRO   B HD3  1 
ATOM   5990 N  N    . LEU   B 1 126 ? 41.976 -27.365 -3.846  1.00 11.52 ?  126 LEU   B N    1 
ATOM   5991 C  CA   . LEU   B 1 126 ? 40.753 -27.734 -3.138  1.00 12.02 ?  126 LEU   B CA   1 
ATOM   5992 C  C    . LEU   B 1 126 ? 40.865 -27.332 -1.675  1.00 12.32 ?  126 LEU   B C    1 
ATOM   5993 O  O    . LEU   B 1 126 ? 41.751 -27.796 -0.953  1.00 14.04 ?  126 LEU   B O    1 
ATOM   5994 C  CB   . LEU   B 1 126 ? 40.508 -29.232 -3.255  1.00 13.39 ?  126 LEU   B CB   1 
ATOM   5995 C  CG   . LEU   B 1 126 ? 39.969 -29.709 -4.604  1.00 14.31 ?  126 LEU   B CG   1 
ATOM   5996 C  CD1  . LEU   B 1 126 ? 40.028 -31.221 -4.699  1.00 15.95 ?  126 LEU   B CD1  1 
ATOM   5997 C  CD2  . LEU   B 1 126 ? 38.548 -29.222 -4.833  1.00 14.54 ?  126 LEU   B CD2  1 
ATOM   5998 H  H    . LEU   B 1 126 ? 42.487 -28.029 -4.042  1.00 13.81 ?  126 LEU   B H    1 
ATOM   5999 H  HA   . LEU   B 1 126 ? 40.001 -27.266 -3.530  1.00 14.41 ?  126 LEU   B HA   1 
ATOM   6000 H  HB2  . LEU   B 1 126 ? 41.347 -29.692 -3.093  1.00 16.05 ?  126 LEU   B HB2  1 
ATOM   6001 H  HB3  . LEU   B 1 126 ? 39.863 -29.489 -2.577  1.00 16.05 ?  126 LEU   B HB3  1 
ATOM   6002 H  HG   . LEU   B 1 126 ? 40.532 -29.346 -5.309  1.00 17.15 ?  126 LEU   B HG   1 
ATOM   6003 H  HD11 . LEU   B 1 126 ? 39.685 -31.494 -5.564  1.00 19.12 ?  126 LEU   B HD11 1 
ATOM   6004 H  HD12 . LEU   B 1 126 ? 40.947 -31.511 -4.600  1.00 19.12 ?  126 LEU   B HD12 1 
ATOM   6005 H  HD13 . LEU   B 1 126 ? 39.482 -31.601 -3.992  1.00 19.12 ?  126 LEU   B HD13 1 
ATOM   6006 H  HD21 . LEU   B 1 126 ? 38.197 -29.641 -5.633  1.00 17.44 ?  126 LEU   B HD21 1 
ATOM   6007 H  HD22 . LEU   B 1 126 ? 38.006 -29.460 -4.066  1.00 17.44 ?  126 LEU   B HD22 1 
ATOM   6008 H  HD23 . LEU   B 1 126 ? 38.558 -28.257 -4.943  1.00 17.44 ?  126 LEU   B HD23 1 
ATOM   6009 N  N    . LEU   B 1 127 ? 39.941 -26.497 -1.224  1.00 12.03 ?  127 LEU   B N    1 
ATOM   6010 C  CA   . LEU   B 1 127 ? 39.994 -26.009 0.140   1.00 12.35 ?  127 LEU   B CA   1 
ATOM   6011 C  C    . LEU   B 1 127 ? 39.723 -27.128 1.135   1.00 12.30 ?  127 LEU   B C    1 
ATOM   6012 O  O    . LEU   B 1 127 ? 38.903 -28.026 0.903   1.00 12.65 ?  127 LEU   B O    1 
ATOM   6013 C  CB   . LEU   B 1 127 ? 38.971 -24.894 0.346   1.00 12.84 ?  127 LEU   B CB   1 
ATOM   6014 C  CG   . LEU   B 1 127 ? 39.153 -23.625 -0.486  1.00 13.51 ?  127 LEU   B CG   1 
ATOM   6015 C  CD1  . LEU   B 1 127 ? 38.029 -22.661 -0.160  1.00 13.89 ?  127 LEU   B CD1  1 
ATOM   6016 C  CD2  . LEU   B 1 127 ? 40.513 -22.974 -0.240  1.00 14.19 ?  127 LEU   B CD2  1 
ATOM   6017 H  H    . LEU   B 1 127 ? 39.274 -26.198 -1.686  1.00 14.42 ?  127 LEU   B H    1 
ATOM   6018 H  HA   . LEU   B 1 127 ? 40.879 -25.648 0.315   1.00 14.80 ?  127 LEU   B HA   1 
ATOM   6019 H  HB2  . LEU   B 1 127 ? 38.090 -25.246 0.139   1.00 15.39 ?  127 LEU   B HB2  1 
ATOM   6020 H  HB3  . LEU   B 1 127 ? 38.994 -24.625 1.278   1.00 15.39 ?  127 LEU   B HB3  1 
ATOM   6021 H  HG   . LEU   B 1 127 ? 39.078 -23.845 -1.425  1.00 16.20 ?  127 LEU   B HG   1 
ATOM   6022 H  HD11 . LEU   B 1 127 ? 38.148 -21.847 -0.681  1.00 16.65 ?  127 LEU   B HD11 1 
ATOM   6023 H  HD12 . LEU   B 1 127 ? 37.178 -23.068 -0.377  1.00 16.65 ?  127 LEU   B HD12 1 
ATOM   6024 H  HD13 . LEU   B 1 127 ? 38.060 -22.445 0.788   1.00 16.65 ?  127 LEU   B HD13 1 
ATOM   6025 H  HD21 . LEU   B 1 127 ? 40.546 -22.122 -0.704  1.00 17.01 ?  127 LEU   B HD21 1 
ATOM   6026 H  HD22 . LEU   B 1 127 ? 40.629 -22.835 0.714   1.00 17.01 ?  127 LEU   B HD22 1 
ATOM   6027 H  HD23 . LEU   B 1 127 ? 41.205 -23.562 -0.576  1.00 17.01 ?  127 LEU   B HD23 1 
ATOM   6028 N  N    . SER   B 1 128 ? 40.408 -27.047 2.267   1.00 12.20 ?  128 SER   B N    1 
ATOM   6029 C  CA   . SER   B 1 128 ? 40.300 -27.962 3.392   1.00 12.95 ?  128 SER   B CA   1 
ATOM   6030 C  C    . SER   B 1 128 ? 40.795 -29.367 3.072   1.00 13.93 ?  128 SER   B C    1 
ATOM   6031 O  O    . SER   B 1 128 ? 40.700 -30.247 3.926   1.00 15.36 ?  128 SER   B O    1 
ATOM   6032 C  CB   . SER   B 1 128 ? 38.899 -27.975 4.023   1.00 13.34 ?  128 SER   B CB   1 
ATOM   6033 O  OG   . SER   B 1 128 ? 38.578 -26.697 4.561   1.00 13.71 ?  128 SER   B OG   1 
ATOM   6034 H  H    . SER   B 1 128 ? 40.979 -26.420 2.414   1.00 14.63 ?  128 SER   B H    1 
ATOM   6035 H  HA   . SER   B 1 128 ? 40.889 -27.626 4.076   1.00 15.52 ?  128 SER   B HA   1 
ATOM   6036 H  HB2  . SER   B 1 128 ? 38.242 -28.218 3.352   1.00 15.99 ?  128 SER   B HB2  1 
ATOM   6037 H  HB3  . SER   B 1 128 ? 38.885 -28.640 4.744   1.00 15.99 ?  128 SER   B HB3  1 
ATOM   6038 H  HG   . SER   B 1 128 ? 39.143 -26.489 5.149   1.00 16.44 ?  128 SER   B HG   1 
ATOM   6039 N  N    . ALA   B 1 129 ? 41.374 -29.588 1.890   1.00 15.01 ?  129 ALA   B N    1 
ATOM   6040 C  CA   . ALA   B 1 129 ? 41.910 -30.890 1.531   1.00 15.66 ?  129 ALA   B CA   1 
ATOM   6041 C  C    . ALA   B 1 129 ? 43.304 -31.069 2.120   1.00 14.98 ?  129 ALA   B C    1 
ATOM   6042 O  O    . ALA   B 1 129 ? 43.867 -30.169 2.758   1.00 14.84 ?  129 ALA   B O    1 
ATOM   6043 C  CB   . ALA   B 1 129 ? 41.950 -31.049 0.013   1.00 17.51 ?  129 ALA   B CB   1 
ATOM   6044 H  H    . ALA   B 1 129 ? 41.463 -28.991 1.271   1.00 18.00 ?  129 ALA   B H    1 
ATOM   6045 H  HA   . ALA   B 1 129 ? 41.333 -31.580 1.892   1.00 18.78 ?  129 ALA   B HA   1 
ATOM   6046 H  HB1  . ALA   B 1 129 ? 42.300 -31.929 -0.203  1.00 20.99 ?  129 ALA   B HB1  1 
ATOM   6047 H  HB2  . ALA   B 1 129 ? 41.052 -30.955 -0.340  1.00 20.99 ?  129 ALA   B HB2  1 
ATOM   6048 H  HB3  . ALA   B 1 129 ? 42.527 -30.365 -0.362  1.00 20.99 ?  129 ALA   B HB3  1 
ATOM   6049 N  N    . GLY   B 1 130 ? 43.869 -32.251 1.884   1.00 14.79 ?  130 GLY   B N    1 
ATOM   6050 C  CA   . GLY   B 1 130 ? 45.258 -32.480 2.233   1.00 15.49 ?  130 GLY   B CA   1 
ATOM   6051 C  C    . GLY   B 1 130 ? 45.470 -32.389 3.725   1.00 15.45 ?  130 GLY   B C    1 
ATOM   6052 O  O    . GLY   B 1 130 ? 44.769 -33.035 4.520   1.00 16.22 ?  130 GLY   B O    1 
ATOM   6053 H  H    . GLY   B 1 130 ? 43.473 -32.923 1.519   1.00 17.73 ?  130 GLY   B H    1 
ATOM   6054 H  HA2  . GLY   B 1 130 ? 45.527 -33.363 1.934   1.00 18.57 ?  130 GLY   B HA2  1 
ATOM   6055 H  HA3  . GLY   B 1 130 ? 45.818 -31.820 1.795   1.00 18.57 ?  130 GLY   B HA3  1 
ATOM   6056 N  N    . ILE   B 1 131 ? 46.450 -31.567 4.113   1.00 16.03 ?  131 ILE   B N    1 
ATOM   6057 C  CA   . ILE   B 1 131 ? 46.813 -31.429 5.513   1.00 16.91 ?  131 ILE   B CA   1 
ATOM   6058 C  C    . ILE   B 1 131 ? 45.698 -30.832 6.350   1.00 16.06 ?  131 ILE   B C    1 
ATOM   6059 O  O    . ILE   B 1 131 ? 45.770 -30.899 7.578   1.00 17.28 ?  131 ILE   B O    1 
ATOM   6060 C  CB   . ILE   B 1 131 ? 48.139 -30.648 5.701   1.00 18.74 ?  131 ILE   B CB   1 
ATOM   6061 C  CG1  . ILE   B 1 131 ? 47.963 -29.163 5.347   1.00 19.86 ?  131 ILE   B CG1  1 
ATOM   6062 C  CG2  . ILE   B 1 131 ? 49.249 -31.280 4.873   1.00 19.61 ?  131 ILE   B CG2  1 
ATOM   6063 C  CD1  . ILE   B 1 131 ? 49.176 -28.296 5.670   1.00 21.07 ?  131 ILE   B CD1  1 
ATOM   6064 H  H    . ILE   B 1 131 ? 46.924 -31.084 3.579   1.00 19.22 ?  131 ILE   B H    1 
ATOM   6065 H  HA   . ILE   B 1 131 ? 46.962 -32.317 5.864   1.00 20.28 ?  131 ILE   B HA   1 
ATOM   6066 H  HB   . ILE   B 1 131 ? 48.384 -30.705 6.639   1.00 22.47 ?  131 ILE   B HB   1 
ATOM   6067 H  HG12 . ILE   B 1 131 ? 47.787 -29.092 4.397   1.00 23.82 ?  131 ILE   B HG12 1 
ATOM   6068 H  HG13 . ILE   B 1 131 ? 47.210 -28.801 5.845   1.00 23.82 ?  131 ILE   B HG13 1 
ATOM   6069 H  HG21 . ILE   B 1 131 ? 50.091 -30.873 5.120   1.00 23.52 ?  131 ILE   B HG21 1 
ATOM   6070 H  HG22 . ILE   B 1 131 ? 49.268 -32.230 5.053   1.00 23.52 ?  131 ILE   B HG22 1 
ATOM   6071 H  HG23 . ILE   B 1 131 ? 49.063 -31.122 3.934   1.00 23.52 ?  131 ILE   B HG23 1 
ATOM   6072 H  HD11 . ILE   B 1 131 ? 48.955 -27.369 5.493   1.00 25.27 ?  131 ILE   B HD11 1 
ATOM   6073 H  HD12 . ILE   B 1 131 ? 49.405 -28.410 6.606   1.00 25.27 ?  131 ILE   B HD12 1 
ATOM   6074 H  HD13 . ILE   B 1 131 ? 49.918 -28.573 5.111   1.00 25.27 ?  131 ILE   B HD13 1 
ATOM   6075 N  N    . PHE   B 1 132 ? 44.665 -30.257 5.719   1.00 14.76 ?  132 PHE   B N    1 
ATOM   6076 C  CA   . PHE   B 1 132 ? 43.506 -29.753 6.449   1.00 15.13 ?  132 PHE   B CA   1 
ATOM   6077 C  C    . PHE   B 1 132 ? 42.481 -30.841 6.773   1.00 16.51 ?  132 PHE   B C    1 
ATOM   6078 O  O    . PHE   B 1 132 ? 41.574 -30.590 7.574   1.00 18.20 ?  132 PHE   B O    1 
ATOM   6079 C  CB   . PHE   B 1 132 ? 42.829 -28.619 5.670   1.00 14.10 ?  132 PHE   B CB   1 
ATOM   6080 C  CG   . PHE   B 1 132 ? 43.524 -27.275 5.779   1.00 13.84 ?  132 PHE   B CG   1 
ATOM   6081 C  CD1  . PHE   B 1 132 ? 44.818 -27.094 5.315   1.00 14.87 ?  132 PHE   B CD1  1 
ATOM   6082 C  CD2  . PHE   B 1 132 ? 42.852 -26.176 6.298   1.00 13.47 ?  132 PHE   B CD2  1 
ATOM   6083 C  CE1  . PHE   B 1 132 ? 45.440 -25.852 5.405   1.00 15.29 ?  132 PHE   B CE1  1 
ATOM   6084 C  CE2  . PHE   B 1 132 ? 43.460 -24.936 6.380   1.00 13.81 ?  132 PHE   B CE2  1 
ATOM   6085 C  CZ   . PHE   B 1 132 ? 44.753 -24.773 5.935   1.00 14.69 ?  132 PHE   B CZ   1 
ATOM   6086 H  H    . PHE   B 1 132 ? 44.612 -30.149 4.864   1.00 17.70 ?  132 PHE   B H    1 
ATOM   6087 H  HA   . PHE   B 1 132 ? 43.810 -29.386 7.290   1.00 18.14 ?  132 PHE   B HA   1 
ATOM   6088 H  HB2  . PHE   B 1 132 ? 42.816 -28.858 4.732   1.00 16.90 ?  132 PHE   B HB2  1 
ATOM   6089 H  HB3  . PHE   B 1 132 ? 41.925 -28.510 5.998   1.00 16.90 ?  132 PHE   B HB3  1 
ATOM   6090 H  HD1  . PHE   B 1 132 ? 45.290 -27.818 4.963   1.00 17.82 ?  132 PHE   B HD1  1 
ATOM   6091 H  HD2  . PHE   B 1 132 ? 41.980 -26.278 6.602   1.00 16.14 ?  132 PHE   B HD2  1 
ATOM   6092 H  HE1  . PHE   B 1 132 ? 46.313 -25.744 5.104   1.00 18.33 ?  132 PHE   B HE1  1 
ATOM   6093 H  HE2  . PHE   B 1 132 ? 42.998 -24.214 6.743   1.00 16.56 ?  132 PHE   B HE2  1 
ATOM   6094 H  HZ   . PHE   B 1 132 ? 45.162 -23.936 6.000   1.00 17.61 ?  132 PHE   B HZ   1 
ATOM   6095 N  N    . GLY   B 1 133 ? 42.583 -32.032 6.167   1.00 16.17 ?  133 GLY   B N    1 
ATOM   6096 C  CA   . GLY   B 1 133 ? 41.874 -33.202 6.656   1.00 17.22 ?  133 GLY   B CA   1 
ATOM   6097 C  C    . GLY   B 1 133 ? 40.473 -33.467 6.132   1.00 17.62 ?  133 GLY   B C    1 
ATOM   6098 O  O    . GLY   B 1 133 ? 39.890 -34.492 6.502   1.00 19.57 ?  133 GLY   B O    1 
ATOM   6099 H  H    . GLY   B 1 133 ? 43.069 -32.181 5.468   1.00 19.38 ?  133 GLY   B H    1 
ATOM   6100 H  HA2  . GLY   B 1 133 ? 42.412 -33.984 6.458   1.00 20.65 ?  133 GLY   B HA2  1 
ATOM   6101 H  HA3  . GLY   B 1 133 ? 41.805 -33.129 7.618   1.00 20.65 ?  133 GLY   B HA3  1 
ATOM   6102 N  N    . ALA   B 1 134 ? 39.897 -32.594 5.314   1.00 16.59 ?  134 ALA   B N    1 
ATOM   6103 C  CA   . ALA   B 1 134 ? 38.574 -32.883 4.781   1.00 16.68 ?  134 ALA   B CA   1 
ATOM   6104 C  C    . ALA   B 1 134 ? 38.663 -33.878 3.629   1.00 16.93 ?  134 ALA   B C    1 
ATOM   6105 O  O    . ALA   B 1 134 ? 39.717 -34.066 3.014   1.00 17.77 ?  134 ALA   B O    1 
ATOM   6106 C  CB   . ALA   B 1 134 ? 37.894 -31.603 4.300   1.00 17.25 ?  134 ALA   B CB   1 
ATOM   6107 H  H    . ALA   B 1 134 ? 40.237 -31.840 5.068   1.00 19.89 ?  134 ALA   B H    1 
ATOM   6108 H  HA   . ALA   B 1 134 ? 38.027 -33.271 5.484   1.00 20.00 ?  134 ALA   B HA   1 
ATOM   6109 H  HB1  . ALA   B 1 134 ? 37.010 -31.825 3.964   1.00 20.68 ?  134 ALA   B HB1  1 
ATOM   6110 H  HB2  . ALA   B 1 134 ? 37.819 -30.985 5.043   1.00 20.68 ?  134 ALA   B HB2  1 
ATOM   6111 H  HB3  . ALA   B 1 134 ? 38.427 -31.210 3.593   1.00 20.68 ?  134 ALA   B HB3  1 
ATOM   6112 N  N    . ASP   B 1 135 ? 37.531 -34.506 3.338   1.00 17.19 ?  135 ASP   B N    1 
ATOM   6113 C  CA   . ASP   B 1 135 ? 37.432 -35.397 2.193   1.00 17.85 ?  135 ASP   B CA   1 
ATOM   6114 C  C    . ASP   B 1 135 ? 37.534 -34.557 0.926   1.00 16.60 ?  135 ASP   B C    1 
ATOM   6115 O  O    . ASP   B 1 135 ? 36.683 -33.682 0.707   1.00 16.23 ?  135 ASP   B O    1 
ATOM   6116 C  CB   . ASP   B 1 135 ? 36.090 -36.124 2.248   1.00 19.55 ?  135 ASP   B CB   1 
ATOM   6117 C  CG   . ASP   B 1 135 ? 35.905 -37.115 1.118   1.00 21.36 ?  135 ASP   B CG   1 
ATOM   6118 O  OD1  . ASP   B 1 135 ? 36.769 -37.162 0.216   1.00 21.07 ?  135 ASP   B OD1  1 
ATOM   6119 O  OD2  . ASP   B 1 135 ? 34.901 -37.864 1.146   1.00 24.01 -1 135 ASP   B OD2  1 
ATOM   6120 H  H    . ASP   B 1 135 ? 36.803 -34.434 3.789   1.00 20.61 ?  135 ASP   B H    1 
ATOM   6121 H  HA   . ASP   B 1 135 ? 38.150 -36.053 2.222   1.00 21.40 ?  135 ASP   B HA   1 
ATOM   6122 H  HB2  . ASP   B 1 135 ? 36.034 -36.614 3.081   1.00 23.44 ?  135 ASP   B HB2  1 
ATOM   6123 H  HB3  . ASP   B 1 135 ? 35.380 -35.471 2.190   1.00 23.44 ?  135 ASP   B HB3  1 
ATOM   6124 N  N    . PRO   B 1 136 ? 38.547 -34.759 0.082   1.00 16.60 ?  136 PRO   B N    1 
ATOM   6125 C  CA   . PRO   B 1 136 ? 38.641 -33.935 -1.133  1.00 15.84 ?  136 PRO   B CA   1 
ATOM   6126 C  C    . PRO   B 1 136 ? 37.449 -34.089 -2.057  1.00 15.39 ?  136 PRO   B C    1 
ATOM   6127 O  O    . PRO   B 1 136 ? 37.121 -33.140 -2.779  1.00 14.88 ?  136 PRO   B O    1 
ATOM   6128 C  CB   . PRO   B 1 136 ? 39.953 -34.406 -1.780  1.00 16.88 ?  136 PRO   B CB   1 
ATOM   6129 C  CG   . PRO   B 1 136 ? 40.156 -35.799 -1.245  1.00 18.04 ?  136 PRO   B CG   1 
ATOM   6130 C  CD   . PRO   B 1 136 ? 39.632 -35.752 0.160   1.00 17.73 ?  136 PRO   B CD   1 
ATOM   6131 H  HA   . PRO   B 1 136 ? 38.726 -32.999 -0.894  1.00 18.99 ?  136 PRO   B HA   1 
ATOM   6132 H  HB2  . PRO   B 1 136 ? 39.858 -34.415 -2.748  1.00 20.23 ?  136 PRO   B HB2  1 
ATOM   6133 H  HB3  . PRO   B 1 136 ? 40.677 -33.819 -1.513  1.00 20.23 ?  136 PRO   B HB3  1 
ATOM   6134 H  HG2  . PRO   B 1 136 ? 39.653 -36.434 -1.778  1.00 21.63 ?  136 PRO   B HG2  1 
ATOM   6135 H  HG3  . PRO   B 1 136 ? 41.102 -36.018 -1.252  1.00 21.63 ?  136 PRO   B HG3  1 
ATOM   6136 H  HD2  . PRO   B 1 136 ? 39.284 -36.618 0.421   1.00 21.26 ?  136 PRO   B HD2  1 
ATOM   6137 H  HD3  . PRO   B 1 136 ? 40.322 -35.445 0.772   1.00 21.26 ?  136 PRO   B HD3  1 
ATOM   6138 N  N    . ILE   B 1 137 ? 36.789 -35.253 -2.056  1.00 15.84 ?  137 ILE   B N    1 
ATOM   6139 C  CA   . ILE   B 1 137 ? 35.573 -35.426 -2.848  1.00 16.06 ?  137 ILE   B CA   1 
ATOM   6140 C  C    . ILE   B 1 137 ? 34.496 -34.454 -2.377  1.00 15.88 ?  137 ILE   B C    1 
ATOM   6141 O  O    . ILE   B 1 137 ? 33.783 -33.841 -3.183  1.00 15.33 ?  137 ILE   B O    1 
ATOM   6142 C  CB   . ILE   B 1 137 ? 35.103 -36.894 -2.778  1.00 18.23 ?  137 ILE   B CB   1 
ATOM   6143 C  CG1  . ILE   B 1 137 ? 36.113 -37.800 -3.486  1.00 20.59 ?  137 ILE   B CG1  1 
ATOM   6144 C  CG2  . ILE   B 1 137 ? 33.703 -37.046 -3.377  1.00 19.06 ?  137 ILE   B CG2  1 
ATOM   6145 C  CD1  . ILE   B 1 137 ? 35.805 -39.281 -3.370  1.00 22.78 ?  137 ILE   B CD1  1 
ATOM   6146 H  H    . ILE   B 1 137 ? 37.022 -35.953 -1.611  1.00 18.99 ?  137 ILE   B H    1 
ATOM   6147 H  HA   . ILE   B 1 137 ? 35.769 -35.225 -3.777  1.00 19.26 ?  137 ILE   B HA   1 
ATOM   6148 H  HB   . ILE   B 1 137 ? 35.057 -37.155 -1.850  1.00 21.85 ?  137 ILE   B HB   1 
ATOM   6149 H  HG12 . ILE   B 1 137 ? 36.130 -37.581 -4.430  1.00 24.69 ?  137 ILE   B HG12 1 
ATOM   6150 H  HG13 . ILE   B 1 137 ? 36.988 -37.655 -3.097  1.00 24.69 ?  137 ILE   B HG13 1 
ATOM   6151 H  HG21 . ILE   B 1 137 ? 33.463 -37.988 -3.412  1.00 22.86 ?  137 ILE   B HG21 1 
ATOM   6152 H  HG22 . ILE   B 1 137 ? 33.061 -36.579 -2.821  1.00 22.86 ?  137 ILE   B HG22 1 
ATOM   6153 H  HG23 . ILE   B 1 137 ? 33.696 -36.676 -4.273  1.00 22.86 ?  137 ILE   B HG23 1 
ATOM   6154 H  HD11 . ILE   B 1 137 ? 36.496 -39.773 -3.839  1.00 27.32 ?  137 ILE   B HD11 1 
ATOM   6155 H  HD12 . ILE   B 1 137 ? 35.795 -39.535 -2.433  1.00 27.32 ?  137 ILE   B HD12 1 
ATOM   6156 H  HD13 . ILE   B 1 137 ? 34.945 -39.471 -3.775  1.00 27.32 ?  137 ILE   B HD13 1 
ATOM   6157 N  N    . HIS   B 1 138 ? 34.359 -34.303 -1.063  1.00 16.02 ?  138 HIS   B N    1 
ATOM   6158 C  CA   . HIS   B 1 138 ? 33.409 -33.336 -0.531  1.00 16.41 ?  138 HIS   B CA   1 
ATOM   6159 C  C    . HIS   B 1 138 ? 33.833 -31.908 -0.851  1.00 15.23 ?  138 HIS   B C    1 
ATOM   6160 O  O    . HIS   B 1 138 ? 32.992 -31.060 -1.166  1.00 15.57 ?  138 HIS   B O    1 
ATOM   6161 C  CB   . HIS   B 1 138 ? 33.286 -33.513 0.973   1.00 17.64 ?  138 HIS   B CB   1 
ATOM   6162 C  CG   . HIS   B 1 138 ? 32.350 -32.536 1.606   1.00 18.72 ?  138 HIS   B CG   1 
ATOM   6163 N  ND1  . HIS   B 1 138 ? 31.012 -32.469 1.278   1.00 20.08 ?  138 HIS   B ND1  1 
ATOM   6164 C  CD2  . HIS   B 1 138 ? 32.560 -31.566 2.525   1.00 19.47 ?  138 HIS   B CD2  1 
ATOM   6165 C  CE1  . HIS   B 1 138 ? 30.436 -31.509 1.978   1.00 20.21 ?  138 HIS   B CE1  1 
ATOM   6166 N  NE2  . HIS   B 1 138 ? 31.354 -30.945 2.743   1.00 19.67 ?  138 HIS   B NE2  1 
ATOM   6167 H  H    . HIS   B 1 138 ? 34.801 -34.740 -0.471  1.00 19.21 ?  138 HIS   B H    1 
ATOM   6168 H  HA   . HIS   B 1 138 ? 32.537 -33.496 -0.933  1.00 19.68 ?  138 HIS   B HA   1 
ATOM   6169 H  HB2  . HIS   B 1 138 ? 32.953 -34.404 1.159   1.00 21.15 ?  138 HIS   B HB2  1 
ATOM   6170 H  HB3  . HIS   B 1 138 ? 34.157 -33.390 1.375   1.00 21.15 ?  138 HIS   B HB3  1 
ATOM   6171 H  HD1  . HIS   B 1 138 ? 30.613 -32.980 0.708   1.00 24.08 ?  138 HIS   B HD1  1 
ATOM   6172 H  HD2  . HIS   B 1 138 ? 33.361 -31.359 2.939   1.00 23.35 ?  138 HIS   B HD2  1 
ATOM   6173 H  HE1  . HIS   B 1 138 ? 29.531 -31.279 1.940   1.00 24.23 ?  138 HIS   B HE1  1 
ATOM   6174 N  N    . SER   B 1 139 ? 35.127 -31.612 -0.766  1.00 14.72 ?  139 SER   B N    1 
ATOM   6175 C  CA   . SER   B 1 139 ? 35.566 -30.263 -1.086  1.00 13.96 ?  139 SER   B CA   1 
ATOM   6176 C  C    . SER   B 1 139 ? 35.233 -29.915 -2.527  1.00 13.15 ?  139 SER   B C    1 
ATOM   6177 O  O    . SER   B 1 139 ? 34.783 -28.801 -2.810  1.00 13.22 ?  139 SER   B O    1 
ATOM   6178 C  CB   . SER   B 1 139 ? 37.057 -30.119 -0.810  1.00 14.09 ?  139 SER   B CB   1 
ATOM   6179 O  OG   . SER   B 1 139 ? 37.460 -28.787 -1.081  1.00 14.03 ?  139 SER   B OG   1 
ATOM   6180 H  H    . SER   B 1 139 ? 35.746 -32.158 -0.541  1.00 17.65 ?  139 SER   B H    1 
ATOM   6181 H  HA   . SER   B 1 139 ? 35.088 -29.640 -0.520  1.00 16.73 ?  139 SER   B HA   1 
ATOM   6182 H  HB2  . SER   B 1 139 ? 37.225 -30.319 0.125   1.00 16.89 ?  139 SER   B HB2  1 
ATOM   6183 H  HB3  . SER   B 1 139 ? 37.550 -30.726 -1.378  1.00 16.89 ?  139 SER   B HB3  1 
ATOM   6184 H  HG   . SER   B 1 139 ? 38.285 -28.701 -0.926  1.00 16.82 ?  139 SER   B HG   1 
ATOM   6185 N  N    . LEU   B 1 140 ? 35.424 -30.857 -3.453  1.00 13.06 ?  140 LEU   B N    1 
ATOM   6186 C  CA   . LEU   B 1 140 ? 35.056 -30.606 -4.839  1.00 12.92 ?  140 LEU   B CA   1 
ATOM   6187 C  C    . LEU   B 1 140 ? 33.553 -30.383 -4.969  1.00 13.22 ?  140 LEU   B C    1 
ATOM   6188 O  O    . LEU   B 1 140 ? 33.114 -29.496 -5.706  1.00 12.98 ?  140 LEU   B O    1 
ATOM   6189 C  CB   . LEU   B 1 140 ? 35.527 -31.764 -5.718  1.00 13.00 ?  140 LEU   B CB   1 
ATOM   6190 C  CG   . LEU   B 1 140 ? 35.156 -31.661 -7.191  1.00 13.30 ?  140 LEU   B CG   1 
ATOM   6191 C  CD1  . LEU   B 1 140 ? 35.724 -30.388 -7.791  1.00 14.38 ?  140 LEU   B CD1  1 
ATOM   6192 C  CD2  . LEU   B 1 140 ? 35.638 -32.892 -7.934  1.00 14.43 ?  140 LEU   B CD2  1 
ATOM   6193 H  H    . LEU   B 1 140 ? 35.757 -31.633 -3.308  1.00 15.66 ?  140 LEU   B H    1 
ATOM   6194 H  HA   . LEU   B 1 140 ? 35.508 -29.801 -5.143  1.00 15.49 ?  140 LEU   B HA   1 
ATOM   6195 H  HB2  . LEU   B 1 140 ? 36.496 -31.817 -5.670  1.00 15.58 ?  140 LEU   B HB2  1 
ATOM   6196 H  HB3  . LEU   B 1 140 ? 35.140 -32.585 -5.384  1.00 15.58 ?  140 LEU   B HB3  1 
ATOM   6197 H  HG   . LEU   B 1 140 ? 34.191 -31.618 -7.272  1.00 15.94 ?  140 LEU   B HG   1 
ATOM   6198 H  HD11 . LEU   B 1 140 ? 35.607 -30.413 -8.752  1.00 17.24 ?  140 LEU   B HD11 1 
ATOM   6199 H  HD12 . LEU   B 1 140 ? 35.252 -29.623 -7.420  1.00 17.24 ?  140 LEU   B HD12 1 
ATOM   6200 H  HD13 . LEU   B 1 140 ? 36.668 -30.330 -7.573  1.00 17.24 ?  140 LEU   B HD13 1 
ATOM   6201 H  HD21 . LEU   B 1 140 ? 35.390 -32.806 -8.868  1.00 17.30 ?  140 LEU   B HD21 1 
ATOM   6202 H  HD22 . LEU   B 1 140 ? 36.598 -32.954 -7.846  1.00 17.30 ?  140 LEU   B HD22 1 
ATOM   6203 H  HD23 . LEU   B 1 140 ? 35.212 -33.671 -7.547  1.00 17.30 ?  140 LEU   B HD23 1 
ATOM   6204 N  N    . ARG   B 1 141 ? 32.752 -31.175 -4.254  1.00 13.42 ?  141 ARG   B N    1 
ATOM   6205 C  CA   . ARG   B 1 141 ? 31.302 -30.997 -4.233  1.00 14.57 ?  141 ARG   B CA   1 
ATOM   6206 C  C    . ARG   B 1 141 ? 30.924 -29.584 -3.809  1.00 14.11 ?  141 ARG   B C    1 
ATOM   6207 O  O    . ARG   B 1 141 ? 30.116 -28.911 -4.468  1.00 14.35 ?  141 ARG   B O    1 
ATOM   6208 C  CB   . ARG   B 1 141 ? 30.717 -32.017 -3.249  1.00 16.05 ?  141 ARG   B CB   1 
ATOM   6209 C  CG   . ARG   B 1 141 ? 29.254 -31.899 -2.929  1.00 17.83 ?  141 ARG   B CG   1 
ATOM   6210 C  CD   . ARG   B 1 141 ? 28.462 -32.545 -3.989  1.00 19.31 ?  141 ARG   B CD   1 
ATOM   6211 N  NE   . ARG   B 1 141 ? 28.194 -31.644 -5.097  1.00 19.91 ?  141 ARG   B NE   1 
ATOM   6212 C  CZ   . ARG   B 1 141 ? 28.202 -31.995 -6.375  1.00 19.46 ?  141 ARG   B CZ   1 
ATOM   6213 N  NH1  . ARG   B 1 141 ? 28.651 -33.179 -6.766  1.00 19.35 ?  141 ARG   B NH1  1 
ATOM   6214 N  NH2  . ARG   B 1 141 ? 27.748 -31.137 -7.283  1.00 20.14 ?  141 ARG   B NH2  1 
ATOM   6215 H  H    . ARG   B 1 141 ? 33.032 -31.820 -3.765  1.00 16.09 ?  141 ARG   B H    1 
ATOM   6216 H  HA   . ARG   B 1 141 ? 30.936 -31.163 -5.113  1.00 17.47 ?  141 ARG   B HA   1 
ATOM   6217 H  HB2  . ARG   B 1 141 ? 30.873 -32.904 -3.607  1.00 19.24 ?  141 ARG   B HB2  1 
ATOM   6218 H  HB3  . ARG   B 1 141 ? 31.196 -31.932 -2.410  1.00 19.24 ?  141 ARG   B HB3  1 
ATOM   6219 H  HG2  . ARG   B 1 141 ? 29.079 -32.343 -2.087  1.00 21.38 ?  141 ARG   B HG2  1 
ATOM   6220 H  HG3  . ARG   B 1 141 ? 28.998 -30.961 -2.871  1.00 21.38 ?  141 ARG   B HG3  1 
ATOM   6221 H  HD2  . ARG   B 1 141 ? 28.947 -33.321 -4.321  1.00 23.16 ?  141 ARG   B HD2  1 
ATOM   6222 H  HD3  . ARG   B 1 141 ? 27.619 -32.828 -3.616  1.00 23.16 ?  141 ARG   B HD3  1 
ATOM   6223 H  HE   . ARG   B 1 141 ? 27.996 -30.829 -4.906  1.00 23.88 ?  141 ARG   B HE   1 
ATOM   6224 H  HH11 . ARG   B 1 141 ? 28.945 -33.749 -6.192  1.00 23.21 ?  141 ARG   B HH11 1 
ATOM   6225 H  HH12 . ARG   B 1 141 ? 28.662 -33.377 -7.602  1.00 23.21 ?  141 ARG   B HH12 1 
ATOM   6226 H  HH21 . ARG   B 1 141 ? 27.464 -30.363 -7.041  1.00 24.15 ?  141 ARG   B HH21 1 
ATOM   6227 H  HH22 . ARG   B 1 141 ? 27.772 -31.343 -8.119  1.00 24.15 ?  141 ARG   B HH22 1 
ATOM   6228 N  N    . VAL   B 1 142 ? 31.470 -29.134 -2.682  1.00 13.62 ?  142 VAL   B N    1 
ATOM   6229 C  CA   . VAL   B 1 142 ? 31.135 -27.801 -2.197  1.00 13.43 ?  142 VAL   B CA   1 
ATOM   6230 C  C    . VAL   B 1 142 ? 31.606 -26.743 -3.184  1.00 13.40 ?  142 VAL   B C    1 
ATOM   6231 O  O    . VAL   B 1 142 ? 30.905 -25.756 -3.436  1.00 13.60 ?  142 VAL   B O    1 
ATOM   6232 C  CB   . VAL   B 1 142 ? 31.682 -27.577 -0.776  1.00 14.01 ?  142 VAL   B CB   1 
ATOM   6233 C  CG1  . VAL   B 1 142 ? 31.365 -26.154 -0.304  1.00 14.06 ?  142 VAL   B CG1  1 
ATOM   6234 C  CG2  . VAL   B 1 142 ? 31.093 -28.601 0.177   1.00 14.73 ?  142 VAL   B CG2  1 
ATOM   6235 H  H    . VAL   B 1 142 ? 32.032 -29.568 -2.193  1.00 16.33 ?  142 VAL   B H    1 
ATOM   6236 H  HA   . VAL   B 1 142 ? 30.174 -27.734 -2.144  1.00 16.10 ?  142 VAL   B HA   1 
ATOM   6237 H  HB   . VAL   B 1 142 ? 32.646 -27.688 -0.781  1.00 16.80 ?  142 VAL   B HB   1 
ATOM   6238 H  HG11 . VAL   B 1 142 ? 31.547 -26.091 0.645   1.00 16.85 ?  142 VAL   B HG11 1 
ATOM   6239 H  HG12 . VAL   B 1 142 ? 31.927 -25.527 -0.790  1.00 16.85 ?  142 VAL   B HG12 1 
ATOM   6240 H  HG13 . VAL   B 1 142 ? 30.431 -25.965 -0.477  1.00 16.85 ?  142 VAL   B HG13 1 
ATOM   6241 H  HG21 . VAL   B 1 142 ? 31.402 -28.412 1.075   1.00 17.66 ?  142 VAL   B HG21 1 
ATOM   6242 H  HG22 . VAL   B 1 142 ? 30.123 -28.542 0.141   1.00 17.66 ?  142 VAL   B HG22 1 
ATOM   6243 H  HG23 . VAL   B 1 142 ? 31.378 -29.487 -0.094  1.00 17.66 ?  142 VAL   B HG23 1 
ATOM   6244 N  N    . CYS   B 1 143 ? 32.791 -26.934 -3.766  1.00 12.78 ?  143 CYS   B N    1 
ATOM   6245 C  CA   . CYS   B 1 143 ? 33.285 -26.000 -4.775  1.00 12.78 ?  143 CYS   B CA   1 
ATOM   6246 C  C    . CYS   B 1 143 ? 32.281 -25.856 -5.916  1.00 12.67 ?  143 CYS   B C    1 
ATOM   6247 O  O    . CYS   B 1 143 ? 31.876 -24.746 -6.278  1.00 13.06 ?  143 CYS   B O    1 
ATOM   6248 C  CB   . CYS   B 1 143 ? 34.638 -26.488 -5.304  1.00 13.09 ?  143 CYS   B CB   1 
ATOM   6249 S  SG   . CYS   B 1 143 ? 35.386 -25.393 -6.528  1.00 13.17 ?  143 CYS   B SG   1 
ATOM   6250 H  H    . CYS   B 1 143 ? 33.327 -27.584 -3.592  1.00 15.31 ?  143 CYS   B H    1 
ATOM   6251 H  HA   . CYS   B 1 143 ? 33.420 -25.126 -4.372  1.00 15.31 ?  143 CYS   B HA   1 
ATOM   6252 H  HB2  . CYS   B 1 143 ? 35.264 -26.572 -4.565  1.00 15.69 ?  143 CYS   B HB2  1 
ATOM   6253 H  HB3  . CYS   B 1 143 ? 34.520 -27.353 -5.723  1.00 15.69 ?  143 CYS   B HB3  1 
ATOM   6254 H  HG   . CYS   B 1 143 ? 36.458 -25.832 -6.852  1.00 15.79 ?  143 CYS   B HG   1 
ATOM   6255 N  N    . VAL   B 1 144 ? 31.879 -26.977 -6.504  1.00 13.18 ?  144 VAL   B N    1 
ATOM   6256 C  CA   . VAL   B 1 144 ? 30.968 -26.929 -7.643  1.00 14.16 ?  144 VAL   B CA   1 
ATOM   6257 C  C    . VAL   B 1 144 ? 29.628 -26.306 -7.264  1.00 14.21 ?  144 VAL   B C    1 
ATOM   6258 O  O    . VAL   B 1 144 ? 29.015 -25.590 -8.065  1.00 15.62 ?  144 VAL   B O    1 
ATOM   6259 C  CB   . VAL   B 1 144 ? 30.803 -28.347 -8.202  1.00 16.58 ?  144 VAL   B CB   1 
ATOM   6260 C  CG1  . VAL   B 1 144 ? 29.542 -28.475 -9.043  1.00 19.02 ?  144 VAL   B CG1  1 
ATOM   6261 C  CG2  . VAL   B 1 144 ? 32.051 -28.754 -8.971  1.00 16.82 ?  144 VAL   B CG2  1 
ATOM   6262 H  H    . VAL   B 1 144 ? 32.124 -27.772 -6.276  1.00 15.80 ?  144 VAL   B H    1 
ATOM   6263 H  HA   . VAL   B 1 144 ? 31.358 -26.384 -8.341  1.00 16.98 ?  144 VAL   B HA   1 
ATOM   6264 H  HB   . VAL   B 1 144 ? 30.720 -28.965 -7.455  1.00 19.88 ?  144 VAL   B HB   1 
ATOM   6265 H  HG11 . VAL   B 1 144 ? 29.620 -29.267 -9.601  1.00 22.81 ?  144 VAL   B HG11 1 
ATOM   6266 H  HG12 . VAL   B 1 144 ? 28.780 -28.564 -8.453  1.00 22.81 ?  144 VAL   B HG12 1 
ATOM   6267 H  HG13 . VAL   B 1 144 ? 29.455 -27.689 -9.598  1.00 22.81 ?  144 VAL   B HG13 1 
ATOM   6268 H  HG21 . VAL   B 1 144 ? 31.936 -29.656 -9.309  1.00 20.17 ?  144 VAL   B HG21 1 
ATOM   6269 H  HG22 . VAL   B 1 144 ? 32.179 -28.138 -9.709  1.00 20.17 ?  144 VAL   B HG22 1 
ATOM   6270 H  HG23 . VAL   B 1 144 ? 32.816 -28.719 -8.375  1.00 20.17 ?  144 VAL   B HG23 1 
ATOM   6271 N  N    . ASP   B 1 145 ? 29.158 -26.559 -6.049  1.00 14.27 ?  145 ASP   B N    1 
ATOM   6272 C  CA   . ASP   B 1 145 ? 27.851 -26.086 -5.614  1.00 14.84 ?  145 ASP   B CA   1 
ATOM   6273 C  C    . ASP   B 1 145 ? 27.883 -24.662 -5.073  1.00 14.62 ?  145 ASP   B C    1 
ATOM   6274 O  O    . ASP   B 1 145 ? 26.824 -24.119 -4.737  1.00 16.36 ?  145 ASP   B O    1 
ATOM   6275 C  CB   . ASP   B 1 145 ? 27.278 -27.002 -4.524  1.00 16.64 ?  145 ASP   B CB   1 
ATOM   6276 C  CG   . ASP   B 1 145 ? 26.911 -28.380 -5.030  1.00 18.09 ?  145 ASP   B CG   1 
ATOM   6277 O  OD1  . ASP   B 1 145 ? 26.796 -28.573 -6.258  1.00 18.21 ?  145 ASP   B OD1  1 
ATOM   6278 O  OD2  . ASP   B 1 145 ? 26.726 -29.270 -4.178  1.00 20.13 -1 145 ASP   B OD2  1 
ATOM   6279 H  H    . ASP   B 1 145 ? 29.582 -27.001 -5.450  1.00 17.11 ?  145 ASP   B H    1 
ATOM   6280 H  HA   . ASP   B 1 145 ? 27.243 -26.087 -6.369  1.00 17.79 ?  145 ASP   B HA   1 
ATOM   6281 H  HB2  . ASP   B 1 145 ? 27.934 -27.110 -3.827  1.00 19.95 ?  145 ASP   B HB2  1 
ATOM   6282 H  HB3  . ASP   B 1 145 ? 26.471 -26.592 -4.166  1.00 19.95 ?  145 ASP   B HB3  1 
ATOM   6283 N  N    . THR   B 1 146 ? 29.062 -24.051 -4.966  1.00 12.93 ?  146 THR   B N    1 
ATOM   6284 C  CA   . THR   B 1 146 ? 29.192 -22.726 -4.362  1.00 12.46 ?  146 THR   B CA   1 
ATOM   6285 C  C    . THR   B 1 146 ? 29.824 -21.693 -5.279  1.00 12.33 ?  146 THR   B C    1 
ATOM   6286 O  O    . THR   B 1 146 ? 29.371 -20.531 -5.315  1.00 12.50 ?  146 THR   B O    1 
ATOM   6287 C  CB   . THR   B 1 146 ? 30.019 -22.825 -3.073  1.00 12.64 ?  146 THR   B CB   1 
ATOM   6288 O  OG1  . THR   B 1 146 ? 29.451 -23.814 -2.211  1.00 12.92 ?  146 THR   B OG1  1 
ATOM   6289 C  CG2  . THR   B 1 146 ? 30.096 -21.487 -2.358  1.00 12.90 ?  146 THR   B CG2  1 
ATOM   6290 H  H    . THR   B 1 146 ? 29.815 -24.377 -5.237  1.00 15.50 ?  146 THR   B H    1 
ATOM   6291 H  HA   . THR   B 1 146 ? 28.317 -22.399 -4.124  1.00 14.94 ?  146 THR   B HA   1 
ATOM   6292 H  HB   . THR   B 1 146 ? 30.924 -23.086 -3.297  1.00 15.15 ?  146 THR   B HB   1 
ATOM   6293 H  HG1  . THR   B 1 146 ? 29.486 -24.574 -2.584  1.00 15.48 ?  146 THR   B HG1  1 
ATOM   6294 H  HG21 . THR   B 1 146 ? 30.443 -21.611 -1.463  1.00 15.46 ?  146 THR   B HG21 1 
ATOM   6295 H  HG22 . THR   B 1 146 ? 30.692 -20.888 -2.844  1.00 15.46 ?  146 THR   B HG22 1 
ATOM   6296 H  HG23 . THR   B 1 146 ? 29.218 -21.086 -2.309  1.00 15.46 ?  146 THR   B HG23 1 
ATOM   6297 N  N    . VAL   B 1 147 ? 30.886 -22.065 -5.983  1.00 12.13 ?  147 VAL   B N    1 
ATOM   6298 C  CA   . VAL   B 1 147 ? 31.610 -21.121 -6.819  1.00 11.77 ?  147 VAL   B CA   1 
ATOM   6299 C  C    . VAL   B 1 147 ? 30.877 -20.990 -8.141  1.00 12.07 ?  147 VAL   B C    1 
ATOM   6300 O  O    . VAL   B 1 147 ? 30.508 -21.997 -8.764  1.00 12.96 ?  147 VAL   B O    1 
ATOM   6301 C  CB   . VAL   B 1 147 ? 33.064 -21.578 -7.023  1.00 12.00 ?  147 VAL   B CB   1 
ATOM   6302 C  CG1  . VAL   B 1 147 ? 33.823 -20.557 -7.841  1.00 11.87 ?  147 VAL   B CG1  1 
ATOM   6303 C  CG2  . VAL   B 1 147 ? 33.741 -21.789 -5.683  1.00 12.20 ?  147 VAL   B CG2  1 
ATOM   6304 H  H    . VAL   B 1 147 ? 31.208 -22.868 -6.008  1.00 14.54 ?  147 VAL   B H    1 
ATOM   6305 H  HA   . VAL   B 1 147 ? 31.629 -20.253 -6.388  1.00 14.10 ?  147 VAL   B HA   1 
ATOM   6306 H  HB   . VAL   B 1 147 ? 33.073 -22.426 -7.507  1.00 14.38 ?  147 VAL   B HB   1 
ATOM   6307 H  HG11 . VAL   B 1 147 ? 34.765 -20.773 -7.823  1.00 14.22 ?  147 VAL   B HG11 1 
ATOM   6308 H  HG12 . VAL   B 1 147 ? 33.494 -20.570 -8.752  1.00 14.22 ?  147 VAL   B HG12 1 
ATOM   6309 H  HG13 . VAL   B 1 147 ? 33.677 -19.678 -7.449  1.00 14.22 ?  147 VAL   B HG13 1 
ATOM   6310 H  HG21 . VAL   B 1 147 ? 34.680 -21.985 -5.830  1.00 14.62 ?  147 VAL   B HG21 1 
ATOM   6311 H  HG22 . VAL   B 1 147 ? 33.652 -20.977 -5.159  1.00 14.62 ?  147 VAL   B HG22 1 
ATOM   6312 H  HG23 . VAL   B 1 147 ? 33.317 -22.528 -5.223  1.00 14.62 ?  147 VAL   B HG23 1 
ATOM   6313 N  N    . ARG   B 1 148 ? 30.670 -19.744 -8.567  1.00 11.94 ?  148 ARG   B N    1 
ATOM   6314 C  CA   . ARG   B 1 148 ? 30.043 -19.427 -9.839  1.00 12.17 ?  148 ARG   B CA   1 
ATOM   6315 C  C    . ARG   B 1 148 ? 30.996 -18.751 -10.814 1.00 11.90 ?  148 ARG   B C    1 
ATOM   6316 O  O    . ARG   B 1 148 ? 30.712 -18.730 -12.014 1.00 13.58 ?  148 ARG   B O    1 
ATOM   6317 C  CB   . ARG   B 1 148 ? 28.802 -18.544 -9.618  1.00 12.60 ?  148 ARG   B CB   1 
ATOM   6318 C  CG   . ARG   B 1 148 ? 27.727 -19.252 -8.805  1.00 13.53 ?  148 ARG   B CG   1 
ATOM   6319 C  CD   . ARG   B 1 148 ? 26.521 -18.367 -8.502  1.00 14.44 ?  148 ARG   B CD   1 
ATOM   6320 N  NE   . ARG   B 1 148 ? 26.908 -17.169 -7.769  1.00 14.21 ?  148 ARG   B NE   1 
ATOM   6321 C  CZ   . ARG   B 1 148 ? 27.211 -17.135 -6.478  1.00 13.36 ?  148 ARG   B CZ   1 
ATOM   6322 N  NH1  . ARG   B 1 148 ? 27.150 -18.221 -5.723  1.00 13.26 ?  148 ARG   B NH1  1 
ATOM   6323 N  NH2  . ARG   B 1 148 ? 27.604 -15.985 -5.933  1.00 13.56 ?  148 ARG   B NH2  1 
ATOM   6324 H  H    . ARG   B 1 148 ? 30.895 -19.041 -8.111  1.00 14.31 ?  148 ARG   B H    1 
ATOM   6325 H  HA   . ARG   B 1 148 ? 29.746 -20.252 -10.243 1.00 14.59 ?  148 ARG   B HA   1 
ATOM   6326 H  HB2  . ARG   B 1 148 ? 29.060 -17.743 -9.136  1.00 15.11 ?  148 ARG   B HB2  1 
ATOM   6327 H  HB3  . ARG   B 1 148 ? 28.423 -18.310 -10.477 1.00 15.11 ?  148 ARG   B HB3  1 
ATOM   6328 H  HG2  . ARG   B 1 148 ? 27.408 -20.023 -9.305  1.00 16.22 ?  148 ARG   B HG2  1 
ATOM   6329 H  HG3  . ARG   B 1 148 ? 28.101 -19.540 -7.960  1.00 16.22 ?  148 ARG   B HG3  1 
ATOM   6330 H  HD2  . ARG   B 1 148 ? 26.105 -18.093 -9.334  1.00 17.32 ?  148 ARG   B HD2  1 
ATOM   6331 H  HD3  . ARG   B 1 148 ? 25.884 -18.865 -7.960  1.00 17.32 ?  148 ARG   B HD3  1 
ATOM   6332 H  HE   . ARG   B 1 148 ? 26.950 -16.433 -8.206  1.00 17.03 ?  148 ARG   B HE   1 
ATOM   6333 H  HH11 . ARG   B 1 148 ? 26.896 -18.974 -6.061  1.00 15.90 ?  148 ARG   B HH11 1 
ATOM   6334 H  HH12 . ARG   B 1 148 ? 27.346 -18.179 -4.886  1.00 15.90 ?  148 ARG   B HH12 1 
ATOM   6335 H  HH21 . ARG   B 1 148 ? 27.648 -15.277 -6.416  1.00 16.25 ?  148 ARG   B HH21 1 
ATOM   6336 H  HH22 . ARG   B 1 148 ? 27.800 -15.951 -5.098  1.00 16.25 ?  148 ARG   B HH22 1 
ATOM   6337 N  N    . THR   B 1 149 ? 32.103 -18.194 -10.328 1.00 11.84 ?  149 THR   B N    1 
ATOM   6338 C  CA   . THR   B 1 149 ? 33.142 -17.636 -11.175 1.00 12.09 ?  149 THR   B CA   1 
ATOM   6339 C  C    . THR   B 1 149 ? 34.028 -18.775 -11.684 1.00 11.57 ?  149 THR   B C    1 
ATOM   6340 O  O    . THR   B 1 149 ? 33.837 -19.946 -11.341 1.00 12.17 ?  149 THR   B O    1 
ATOM   6341 C  CB   . THR   B 1 149 ? 33.917 -16.582 -10.393 1.00 11.88 ?  149 THR   B CB   1 
ATOM   6342 O  OG1  . THR   B 1 149 ? 34.376 -17.182 -9.181  1.00 12.03 ?  149 THR   B OG1  1 
ATOM   6343 C  CG2  . THR   B 1 149 ? 33.026 -15.379 -10.090 1.00 12.59 ?  149 THR   B CG2  1 
ATOM   6344 H  H    . THR   B 1 149 ? 32.271 -18.126 -9.487  1.00 14.19 ?  149 THR   B H    1 
ATOM   6345 H  HA   . THR   B 1 149 ? 32.735 -17.201 -11.941 1.00 14.49 ?  149 THR   B HA   1 
ATOM   6346 H  HB   . THR   B 1 149 ? 34.678 -16.289 -10.910 1.00 14.24 ?  149 THR   B HB   1 
ATOM   6347 H  HG1  . THR   B 1 149 ? 34.800 -16.614 -8.720  1.00 14.42 ?  149 THR   B HG1  1 
ATOM   6348 H  HG21 . THR   B 1 149 ? 33.530 -14.706 -9.603  1.00 15.10 ?  149 THR   B HG21 1 
ATOM   6349 H  HG22 . THR   B 1 149 ? 32.703 -14.990 -10.918 1.00 15.10 ?  149 THR   B HG22 1 
ATOM   6350 H  HG23 . THR   B 1 149 ? 32.265 -15.650 -9.552  1.00 15.10 ?  149 THR   B HG23 1 
ATOM   6351 N  N    . ASN   B 1 150 ? 34.993 -18.447 -12.533 1.00 11.84 ?  150 ASN   B N    1 
ATOM   6352 C  CA   . ASN   B 1 150 ? 35.759 -19.470 -13.235 1.00 12.30 ?  150 ASN   B CA   1 
ATOM   6353 C  C    . ASN   B 1 150 ? 36.925 -19.923 -12.367 1.00 12.05 ?  150 ASN   B C    1 
ATOM   6354 O  O    . ASN   B 1 150 ? 37.859 -19.157 -12.115 1.00 12.50 ?  150 ASN   B O    1 
ATOM   6355 C  CB   . ASN   B 1 150 ? 36.231 -18.942 -14.580 1.00 14.01 ?  150 ASN   B CB   1 
ATOM   6356 C  CG   . ASN   B 1 150 ? 35.087 -18.723 -15.523 1.00 16.81 ?  150 ASN   B CG   1 
ATOM   6357 O  OD1  . ASN   B 1 150 ? 34.185 -19.548 -15.605 1.00 17.83 ?  150 ASN   B OD1  1 
ATOM   6358 N  ND2  . ASN   B 1 150 ? 35.086 -17.596 -16.214 1.00 18.69 ?  150 ASN   B ND2  1 
ATOM   6359 H  H    . ASN   B 1 150 ? 35.234 -17.640 -12.715 1.00 14.19 ?  150 ASN   B H    1 
ATOM   6360 H  HA   . ASN   B 1 150 ? 35.184 -20.238 -13.398 1.00 14.74 ?  150 ASN   B HA   1 
ATOM   6361 H  HB2  . ASN   B 1 150 ? 36.678 -18.089 -14.445 1.00 16.80 ?  150 ASN   B HB2  1 
ATOM   6362 H  HB3  . ASN   B 1 150 ? 36.835 -19.579 -14.982 1.00 16.80 ?  150 ASN   B HB3  1 
ATOM   6363 H  HD21 . ASN   B 1 150 ? 34.446 -17.426 -16.765 1.00 22.41 ?  150 ASN   B HD21 1 
ATOM   6364 H  HD22 . ASN   B 1 150 ? 35.733 -17.035 -16.124 1.00 22.41 ?  150 ASN   B HD22 1 
ATOM   6365 N  N    . VAL   B 1 151 ? 36.878 -21.169 -11.908 1.00 11.75 ?  151 VAL   B N    1 
ATOM   6366 C  CA   . VAL   B 1 151 ? 37.895 -21.703 -11.018 1.00 11.95 ?  151 VAL   B CA   1 
ATOM   6367 C  C    . VAL   B 1 151 ? 38.598 -22.872 -11.694 1.00 11.58 ?  151 VAL   B C    1 
ATOM   6368 O  O    . VAL   B 1 151 ? 37.954 -23.807 -12.196 1.00 12.78 ?  151 VAL   B O    1 
ATOM   6369 C  CB   . VAL   B 1 151 ? 37.339 -22.045 -9.619  1.00 13.28 ?  151 VAL   B CB   1 
ATOM   6370 C  CG1  . VAL   B 1 151 ? 36.173 -23.037 -9.695  1.00 14.18 ?  151 VAL   B CG1  1 
ATOM   6371 C  CG2  . VAL   B 1 151 ? 38.453 -22.541 -8.699  1.00 13.47 ?  151 VAL   B CG2  1 
ATOM   6372 H  H    . VAL   B 1 151 ? 36.254 -21.733 -12.107 1.00 14.08 ?  151 VAL   B H    1 
ATOM   6373 H  HA   . VAL   B 1 151 ? 38.563 -21.013 -10.885 1.00 14.33 ?  151 VAL   B HA   1 
ATOM   6374 H  HB   . VAL   B 1 151 ? 36.989 -21.229 -9.227  1.00 15.92 ?  151 VAL   B HB   1 
ATOM   6375 H  HG11 . VAL   B 1 151 ? 35.856 -23.227 -8.797  1.00 17.00 ?  151 VAL   B HG11 1 
ATOM   6376 H  HG12 . VAL   B 1 151 ? 35.454 -22.646 -10.220 1.00 17.00 ?  151 VAL   B HG12 1 
ATOM   6377 H  HG13 . VAL   B 1 151 ? 36.477 -23.857 -10.117 1.00 17.00 ?  151 VAL   B HG13 1 
ATOM   6378 H  HG21 . VAL   B 1 151 ? 38.099 -22.624 -7.798  1.00 16.15 ?  151 VAL   B HG21 1 
ATOM   6379 H  HG22 . VAL   B 1 151 ? 38.765 -23.401 -9.013  1.00 16.15 ?  151 VAL   B HG22 1 
ATOM   6380 H  HG23 . VAL   B 1 151 ? 39.178 -21.897 -8.709  1.00 16.15 ?  151 VAL   B HG23 1 
ATOM   6381 N  N    . TYR   B 1 152 ? 39.931 -22.787 -11.712 1.00 10.99 ?  152 TYR   B N    1 
ATOM   6382 C  CA   . TYR   B 1 152 ? 40.834 -23.767 -12.298 1.00 11.25 ?  152 TYR   B CA   1 
ATOM   6383 C  C    . TYR   B 1 152 ? 41.558 -24.445 -11.140 1.00 10.82 ?  152 TYR   B C    1 
ATOM   6384 O  O    . TYR   B 1 152 ? 42.402 -23.827 -10.483 1.00 11.42 ?  152 TYR   B O    1 
ATOM   6385 C  CB   . TYR   B 1 152 ? 41.802 -23.057 -13.245 1.00 12.22 ?  152 TYR   B CB   1 
ATOM   6386 C  CG   . TYR   B 1 152 ? 41.120 -22.590 -14.510 1.00 12.63 ?  152 TYR   B CG   1 
ATOM   6387 C  CD1  . TYR   B 1 152 ? 40.455 -21.369 -14.574 1.00 13.10 ?  152 TYR   B CD1  1 
ATOM   6388 C  CD2  . TYR   B 1 152 ? 41.117 -23.395 -15.635 1.00 13.79 ?  152 TYR   B CD2  1 
ATOM   6389 C  CE1  . TYR   B 1 152 ? 39.812 -20.969 -15.733 1.00 14.52 ?  152 TYR   B CE1  1 
ATOM   6390 C  CE2  . TYR   B 1 152 ? 40.480 -23.011 -16.790 1.00 14.61 ?  152 TYR   B CE2  1 
ATOM   6391 C  CZ   . TYR   B 1 152 ? 39.834 -21.794 -16.839 1.00 14.82 ?  152 TYR   B CZ   1 
ATOM   6392 O  OH   . TYR   B 1 152 ? 39.202 -21.427 -18.001 1.00 17.32 ?  152 TYR   B OH   1 
ATOM   6393 H  H    . TYR   B 1 152 ? 40.365 -22.130 -11.355 1.00 13.17 ?  152 TYR   B H    1 
ATOM   6394 H  HA   . TYR   B 1 152 ? 40.328 -24.435 -12.795 1.00 13.48 ?  152 TYR   B HA   1 
ATOM   6395 H  HB2  . TYR   B 1 152 ? 42.166 -22.281 -12.792 1.00 14.64 ?  152 TYR   B HB2  1 
ATOM   6396 H  HB3  . TYR   B 1 152 ? 42.513 -23.666 -13.490 1.00 14.64 ?  152 TYR   B HB3  1 
ATOM   6397 H  HD1  . TYR   B 1 152 ? 40.434 -20.814 -13.827 1.00 15.71 ?  152 TYR   B HD1  1 
ATOM   6398 H  HD2  . TYR   B 1 152 ? 41.549 -24.218 -15.606 1.00 16.54 ?  152 TYR   B HD2  1 
ATOM   6399 H  HE1  . TYR   B 1 152 ? 39.371 -20.152 -15.770 1.00 17.40 ?  152 TYR   B HE1  1 
ATOM   6400 H  HE2  . TYR   B 1 152 ? 40.497 -23.566 -17.537 1.00 17.52 ?  152 TYR   B HE2  1 
ATOM   6401 H  HH   . TYR   B 1 152 ? 38.841 -20.675 -17.904 1.00 20.77 ?  152 TYR   B HH   1 
ATOM   6402 N  N    . LEU   B 1 153 ? 41.192 -25.698 -10.869 1.00 10.91 ?  153 LEU   B N    1 
ATOM   6403 C  CA   . LEU   B 1 153 ? 41.701 -26.448 -9.732  1.00 10.83 ?  153 LEU   B CA   1 
ATOM   6404 C  C    . LEU   B 1 153 ? 42.933 -27.248 -10.128 1.00 11.20 ?  153 LEU   B C    1 
ATOM   6405 O  O    . LEU   B 1 153 ? 42.913 -27.976 -11.122 1.00 12.21 ?  153 LEU   B O    1 
ATOM   6406 C  CB   . LEU   B 1 153 ? 40.623 -27.408 -9.223  1.00 11.14 ?  153 LEU   B CB   1 
ATOM   6407 C  CG   . LEU   B 1 153 ? 39.361 -26.759 -8.651  1.00 12.31 ?  153 LEU   B CG   1 
ATOM   6408 C  CD1  . LEU   B 1 153 ? 38.267 -27.803 -8.492  1.00 13.24 ?  153 LEU   B CD1  1 
ATOM   6409 C  CD2  . LEU   B 1 153 ? 39.663 -26.094 -7.312  1.00 13.06 ?  153 LEU   B CD2  1 
ATOM   6410 H  H    . LEU   B 1 153 ? 40.612 -26.141 -11.340 1.00 13.07 ?  153 LEU   B H    1 
ATOM   6411 H  HA   . LEU   B 1 153 ? 41.926 -25.834 -9.020  1.00 12.97 ?  153 LEU   B HA   1 
ATOM   6412 H  HB2  . LEU   B 1 153 ? 40.345 -27.980 -9.955  1.00 13.35 ?  153 LEU   B HB2  1 
ATOM   6413 H  HB3  . LEU   B 1 153 ? 41.009 -27.954 -8.517  1.00 13.35 ?  153 LEU   B HB3  1 
ATOM   6414 H  HG   . LEU   B 1 153 ? 39.041 -26.071 -9.261  1.00 14.75 ?  153 LEU   B HG   1 
ATOM   6415 H  HD11 . LEU   B 1 153 ? 37.460 -27.368 -8.168  1.00 15.87 ?  153 LEU   B HD11 1 
ATOM   6416 H  HD12 . LEU   B 1 153 ? 38.100 -28.210 -9.353  1.00 15.87 ?  153 LEU   B HD12 1 
ATOM   6417 H  HD13 . LEU   B 1 153 ? 38.562 -28.469 -7.855  1.00 15.87 ?  153 LEU   B HD13 1 
ATOM   6418 H  HD21 . LEU   B 1 153 ? 38.845 -25.725 -6.944  1.00 15.66 ?  153 LEU   B HD21 1 
ATOM   6419 H  HD22 . LEU   B 1 153 ? 40.031 -26.756 -6.707  1.00 15.66 ?  153 LEU   B HD22 1 
ATOM   6420 H  HD23 . LEU   B 1 153 ? 40.311 -25.381 -7.452  1.00 15.66 ?  153 LEU   B HD23 1 
ATOM   6421 N  N    . ALA   B 1 154 ? 43.988 -27.137 -9.326  1.00 11.66 ?  154 ALA   B N    1 
ATOM   6422 C  CA   . ALA   B 1 154 ? 45.216 -27.898 -9.511  1.00 12.87 ?  154 ALA   B CA   1 
ATOM   6423 C  C    . ALA   B 1 154 ? 45.280 -28.973 -8.434  1.00 13.24 ?  154 ALA   B C    1 
ATOM   6424 O  O    . ALA   B 1 154 ? 45.204 -28.670 -7.236  1.00 14.30 ?  154 ALA   B O    1 
ATOM   6425 C  CB   . ALA   B 1 154 ? 46.435 -26.979 -9.443  1.00 13.41 ?  154 ALA   B CB   1 
ATOM   6426 H  H    . ALA   B 1 154 ? 44.007 -26.608 -8.645  1.00 13.97 ?  154 ALA   B H    1 
ATOM   6427 H  HA   . ALA   B 1 154 ? 45.205 -28.323 -10.378 1.00 15.42 ?  154 ALA   B HA   1 
ATOM   6428 H  HB1  . ALA   B 1 154 ? 47.239 -27.505 -9.569  1.00 16.08 ?  154 ALA   B HB1  1 
ATOM   6429 H  HB2  . ALA   B 1 154 ? 46.370 -26.306 -10.145 1.00 16.08 ?  154 ALA   B HB2  1 
ATOM   6430 H  HB3  . ALA   B 1 154 ? 46.460 -26.540 -8.576  1.00 16.08 ?  154 ALA   B HB3  1 
ATOM   6431 N  N    . VAL   B 1 155 ? 45.398 -30.223 -8.863  1.00 12.71 ?  155 VAL   B N    1 
ATOM   6432 C  CA   . VAL   B 1 155 ? 45.512 -31.367 -7.966  1.00 12.92 ?  155 VAL   B CA   1 
ATOM   6433 C  C    . VAL   B 1 155 ? 46.851 -32.036 -8.250  1.00 13.08 ?  155 VAL   B C    1 
ATOM   6434 O  O    . VAL   B 1 155 ? 47.078 -32.532 -9.362  1.00 14.78 ?  155 VAL   B O    1 
ATOM   6435 C  CB   . VAL   B 1 155 ? 44.360 -32.363 -8.164  1.00 14.23 ?  155 VAL   B CB   1 
ATOM   6436 C  CG1  . VAL   B 1 155 ? 44.549 -33.561 -7.254  1.00 14.42 ?  155 VAL   B CG1  1 
ATOM   6437 C  CG2  . VAL   B 1 155 ? 43.024 -31.678 -7.905  1.00 14.99 ?  155 VAL   B CG2  1 
ATOM   6438 H  H    . VAL   B 1 155 ? 45.424 -30.439 -9.696  1.00 15.23 ?  155 VAL   B H    1 
ATOM   6439 H  HA   . VAL   B 1 155 ? 45.503 -31.062 -7.044  1.00 15.49 ?  155 VAL   B HA   1 
ATOM   6440 H  HB   . VAL   B 1 155 ? 44.365 -32.671 -9.085  1.00 17.06 ?  155 VAL   B HB   1 
ATOM   6441 H  HG11 . VAL   B 1 155 ? 43.724 -34.066 -7.215  1.00 17.29 ?  155 VAL   B HG11 1 
ATOM   6442 H  HG12 . VAL   B 1 155 ? 45.260 -34.125 -7.609  1.00 17.29 ?  155 VAL   B HG12 1 
ATOM   6443 H  HG13 . VAL   B 1 155 ? 44.790 -33.253 -6.366  1.00 17.29 ?  155 VAL   B HG13 1 
ATOM   6444 H  HG21 . VAL   B 1 155 ? 42.314 -32.337 -7.993  1.00 17.97 ?  155 VAL   B HG21 1 
ATOM   6445 H  HG22 . VAL   B 1 155 ? 43.026 -31.315 -7.007  1.00 17.97 ?  155 VAL   B HG22 1 
ATOM   6446 H  HG23 . VAL   B 1 155 ? 42.897 -30.969 -8.552  1.00 17.97 ?  155 VAL   B HG23 1 
ATOM   6447 N  N    . PHE   B 1 156 ? 47.721 -32.076 -7.239  1.00 13.23 ?  156 PHE   B N    1 
ATOM   6448 C  CA   . PHE   B 1 156 ? 49.098 -32.531 -7.445  1.00 14.19 ?  156 PHE   B CA   1 
ATOM   6449 C  C    . PHE   B 1 156 ? 49.193 -34.029 -7.725  1.00 15.26 ?  156 PHE   B C    1 
ATOM   6450 O  O    . PHE   B 1 156 ? 49.923 -34.456 -8.631  1.00 17.17 ?  156 PHE   B O    1 
ATOM   6451 C  CB   . PHE   B 1 156 ? 49.934 -32.153 -6.224  1.00 14.30 ?  156 PHE   B CB   1 
ATOM   6452 C  CG   . PHE   B 1 156 ? 51.359 -32.617 -6.283  1.00 14.95 ?  156 PHE   B CG   1 
ATOM   6453 C  CD1  . PHE   B 1 156 ? 52.243 -32.081 -7.202  1.00 16.43 ?  156 PHE   B CD1  1 
ATOM   6454 C  CD2  . PHE   B 1 156 ? 51.818 -33.573 -5.400  1.00 15.48 ?  156 PHE   B CD2  1 
ATOM   6455 C  CE1  . PHE   B 1 156 ? 53.564 -32.495 -7.246  1.00 17.43 ?  156 PHE   B CE1  1 
ATOM   6456 C  CE2  . PHE   B 1 156 ? 53.137 -33.993 -5.438  1.00 16.74 ?  156 PHE   B CE2  1 
ATOM   6457 C  CZ   . PHE   B 1 156 ? 54.003 -33.455 -6.369  1.00 17.19 ?  156 PHE   B CZ   1 
ATOM   6458 H  H    . PHE   B 1 156 ? 47.538 -31.856 -6.427  1.00 15.86 ?  156 PHE   B H    1 
ATOM   6459 H  HA   . PHE   B 1 156 ? 49.464 -32.064 -8.210  1.00 17.01 ?  156 PHE   B HA   1 
ATOM   6460 H  HB2  . PHE   B 1 156 ? 49.946 -31.184 -6.146  1.00 17.14 ?  156 PHE   B HB2  1 
ATOM   6461 H  HB3  . PHE   B 1 156 ? 49.531 -32.539 -5.433  1.00 17.14 ?  156 PHE   B HB3  1 
ATOM   6462 H  HD1  . PHE   B 1 156 ? 51.956 -31.428 -7.799  1.00 19.70 ?  156 PHE   B HD1  1 
ATOM   6463 H  HD2  . PHE   B 1 156 ? 51.228 -33.940 -4.776  1.00 18.56 ?  156 PHE   B HD2  1 
ATOM   6464 H  HE1  . PHE   B 1 156 ? 54.152 -32.132 -7.871  1.00 20.90 ?  156 PHE   B HE1  1 
ATOM   6465 H  HE2  . PHE   B 1 156 ? 53.431 -34.651 -4.844  1.00 20.07 ?  156 PHE   B HE2  1 
ATOM   6466 H  HZ   . PHE   B 1 156 ? 54.889 -33.743 -6.396  1.00 20.61 ?  156 PHE   B HZ   1 
ATOM   6467 N  N    . ASP   B 1 157 ? 48.530 -34.848 -6.923  1.00 15.54 ?  157 ASP   B N    1 
ATOM   6468 C  CA   . ASP   B 1 157 ? 48.678 -36.294 -7.023  1.00 16.87 ?  157 ASP   B CA   1 
ATOM   6469 C  C    . ASP   B 1 157 ? 47.760 -36.842 -8.111  1.00 17.06 ?  157 ASP   B C    1 
ATOM   6470 O  O    . ASP   B 1 157 ? 46.533 -36.721 -8.011  1.00 16.37 ?  157 ASP   B O    1 
ATOM   6471 C  CB   . ASP   B 1 157 ? 48.326 -36.911 -5.676  1.00 18.62 ?  157 ASP   B CB   1 
ATOM   6472 C  CG   . ASP   B 1 157 ? 48.462 -38.424 -5.665  1.00 20.51 ?  157 ASP   B CG   1 
ATOM   6473 O  OD1  . ASP   B 1 157 ? 48.808 -39.027 -6.711  1.00 21.07 ?  157 ASP   B OD1  1 
ATOM   6474 O  OD2  . ASP   B 1 157 ? 48.232 -39.015 -4.592  1.00 22.44 -1 157 ASP   B OD2  1 
ATOM   6475 H  H    . ASP   B 1 157 ? 47.994 -34.595 -6.308  1.00 18.63 ?  157 ASP   B H    1 
ATOM   6476 H  HA   . ASP   B 1 157 ? 49.599 -36.527 -7.239  1.00 20.22 ?  157 ASP   B HA   1 
ATOM   6477 H  HB2  . ASP   B 1 157 ? 48.907 -36.538 -4.996  1.00 22.33 ?  157 ASP   B HB2  1 
ATOM   6478 H  HB3  . ASP   B 1 157 ? 47.401 -36.696 -5.469  1.00 22.33 ?  157 ASP   B HB3  1 
ATOM   6479 N  N    A LYS   B 1 158 ? 48.354 -37.489 -9.121  0.62 18.26 ?  158 LYS   B N    1 
ATOM   6480 N  N    B LYS   B 1 158 ? 48.357 -37.445 -9.147  0.38 17.97 ?  158 LYS   B N    1 
ATOM   6481 C  CA   A LYS   B 1 158 ? 47.579 -38.107 -10.198 0.62 19.12 ?  158 LYS   B CA   1 
ATOM   6482 C  CA   B LYS   B 1 158 ? 47.586 -38.013 -10.252 0.38 18.80 ?  158 LYS   B CA   1 
ATOM   6483 C  C    A LYS   B 1 158 ? 46.518 -39.063 -9.658  0.62 19.10 ?  158 LYS   B C    1 
ATOM   6484 C  C    B LYS   B 1 158 ? 46.525 -38.990 -9.756  0.38 18.72 ?  158 LYS   B C    1 
ATOM   6485 O  O    A LYS   B 1 158 ? 45.402 -39.130 -10.189 0.62 19.09 ?  158 LYS   B O    1 
ATOM   6486 O  O    B LYS   B 1 158 ? 45.433 -39.081 -10.330 0.38 18.72 ?  158 LYS   B O    1 
ATOM   6487 C  CB   A LYS   B 1 158 ? 48.523 -38.835 -11.163 0.62 20.52 ?  158 LYS   B CB   1 
ATOM   6488 C  CB   B LYS   B 1 158 ? 48.538 -38.701 -11.239 0.38 19.97 ?  158 LYS   B CB   1 
ATOM   6489 C  CG   A LYS   B 1 158 ? 47.837 -39.737 -12.180 0.62 22.34 ?  158 LYS   B CG   1 
ATOM   6490 C  CG   B LYS   B 1 158 ? 47.874 -39.615 -12.264 0.38 21.28 ?  158 LYS   B CG   1 
ATOM   6491 C  CD   A LYS   B 1 158 ? 46.971 -38.962 -13.151 0.62 24.20 ?  158 LYS   B CD   1 
ATOM   6492 C  CD   B LYS   B 1 158 ? 46.977 -38.851 -13.218 0.38 22.74 ?  158 LYS   B CD   1 
ATOM   6493 C  CE   A LYS   B 1 158 ? 46.400 -39.884 -14.215 0.62 25.68 ?  158 LYS   B CE   1 
ATOM   6494 C  CE   B LYS   B 1 158 ? 46.400 -39.774 -14.279 0.38 23.92 ?  158 LYS   B CE   1 
ATOM   6495 N  NZ   A LYS   B 1 158 ? 45.318 -39.232 -15.004 0.62 25.99 ?  158 LYS   B NZ   1 
ATOM   6496 N  NZ   B LYS   B 1 158 ? 45.351 -39.103 -15.097 0.38 24.29 ?  158 LYS   B NZ   1 
ATOM   6497 H  H    A LYS   B 1 158 ? 49.208 -37.586 -9.202  0.62 21.90 ?  158 LYS   B H    1 
ATOM   6498 H  H    B LYS   B 1 158 ? 49.209 -37.538 -9.232  0.38 21.55 ?  158 LYS   B H    1 
ATOM   6499 H  HA   A LYS   B 1 158 ? 47.129 -37.411 -10.697 0.62 22.93 ?  158 LYS   B HA   1 
ATOM   6500 H  HA   B LYS   B 1 158 ? 47.136 -37.297 -10.726 0.38 22.54 ?  158 LYS   B HA   1 
ATOM   6501 H  HB2  A LYS   B 1 158 ? 49.031 -38.171 -11.662 0.62 24.60 ?  158 LYS   B HB2  1 
ATOM   6502 H  HB2  B LYS   B 1 158 ? 49.020 -38.016 -11.734 0.38 23.95 ?  158 LYS   B HB2  1 
ATOM   6503 H  HB3  A LYS   B 1 158 ? 49.134 -39.386 -10.648 0.62 24.60 ?  158 LYS   B HB3  1 
ATOM   6504 H  HB3  B LYS   B 1 158 ? 49.171 -39.238 -10.737 0.38 23.95 ?  158 LYS   B HB3  1 
ATOM   6505 H  HG2  A LYS   B 1 158 ? 48.518 -40.197 -12.696 0.62 26.79 ?  158 LYS   B HG2  1 
ATOM   6506 H  HG2  B LYS   B 1 158 ? 48.565 -40.047 -12.789 0.38 25.52 ?  158 LYS   B HG2  1 
ATOM   6507 H  HG3  A LYS   B 1 158 ? 47.281 -40.389 -11.725 0.62 26.79 ?  158 LYS   B HG3  1 
ATOM   6508 H  HG3  B LYS   B 1 158 ? 47.341 -40.289 -11.813 0.38 25.52 ?  158 LYS   B HG3  1 
ATOM   6509 H  HD2  A LYS   B 1 158 ? 46.233 -38.552 -12.672 0.62 29.03 ?  158 LYS   B HD2  1 
ATOM   6510 H  HD2  B LYS   B 1 158 ? 46.243 -38.455 -12.725 0.38 27.28 ?  158 LYS   B HD2  1 
ATOM   6511 H  HD3  A LYS   B 1 158 ? 47.506 -38.283 -13.591 0.62 29.03 ?  158 LYS   B HD3  1 
ATOM   6512 H  HD3  B LYS   B 1 158 ? 47.496 -38.162 -13.664 0.38 27.28 ?  158 LYS   B HD3  1 
ATOM   6513 H  HE2  A LYS   B 1 158 ? 47.106 -40.139 -14.828 0.62 30.80 ?  158 LYS   B HE2  1 
ATOM   6514 H  HE2  B LYS   B 1 158 ? 47.110 -40.061 -14.874 0.38 28.68 ?  158 LYS   B HE2  1 
ATOM   6515 H  HE3  A LYS   B 1 158 ? 46.029 -40.673 -13.789 0.62 30.80 ?  158 LYS   B HE3  1 
ATOM   6516 H  HE3  B LYS   B 1 158 ? 45.998 -40.545 -13.846 0.38 28.68 ?  158 LYS   B HE3  1 
ATOM   6517 H  HZ1  A LYS   B 1 158 ? 45.004 -39.796 -15.616 0.62 31.17 ?  158 LYS   B HZ1  1 
ATOM   6518 H  HZ1  B LYS   B 1 158 ? 45.032 -39.668 -15.707 0.38 29.13 ?  158 LYS   B HZ1  1 
ATOM   6519 H  HZ2  A LYS   B 1 158 ? 44.652 -38.989 -14.465 0.62 31.17 ?  158 LYS   B HZ2  1 
ATOM   6520 H  HZ2  B LYS   B 1 158 ? 44.683 -38.835 -14.574 0.38 29.13 ?  158 LYS   B HZ2  1 
ATOM   6521 H  HZ3  A LYS   B 1 158 ? 45.636 -38.508 -15.413 0.62 31.17 ?  158 LYS   B HZ3  1 
ATOM   6522 H  HZ3  B LYS   B 1 158 ? 45.697 -38.395 -15.511 0.38 29.13 ?  158 LYS   B HZ3  1 
ATOM   6523 N  N    A ASN   B 1 159 ? 46.849 -39.829 -8.617  0.62 19.31 ?  159 ASN   B N    1 
ATOM   6524 N  N    B ASN   B 1 159 ? 46.831 -39.742 -8.697  0.38 18.86 ?  159 ASN   B N    1 
ATOM   6525 C  CA   A ASN   B 1 159 ? 45.891 -40.801 -8.100  0.62 19.97 ?  159 ASN   B CA   1 
ATOM   6526 C  CA   B ASN   B 1 159 ? 45.881 -40.734 -8.201  0.38 19.14 ?  159 ASN   B CA   1 
ATOM   6527 C  C    A ASN   B 1 159 ? 44.697 -40.120 -7.434  0.62 19.19 ?  159 ASN   B C    1 
ATOM   6528 C  C    B ASN   B 1 159 ? 44.686 -40.072 -7.516  0.38 18.67 ?  159 ASN   B C    1 
ATOM   6529 O  O    A ASN   B 1 159 ? 43.569 -40.627 -7.515  0.62 19.39 ?  159 ASN   B O    1 
ATOM   6530 O  O    B ASN   B 1 159 ? 43.550 -40.545 -7.649  0.38 18.68 ?  159 ASN   B O    1 
ATOM   6531 C  CB   A ASN   B 1 159 ? 46.593 -41.768 -7.148  0.62 21.93 ?  159 ASN   B CB   1 
ATOM   6532 C  CB   B ASN   B 1 159 ? 46.596 -41.720 -7.276  0.38 20.13 ?  159 ASN   B CB   1 
ATOM   6533 C  CG   A ASN   B 1 159 ? 47.619 -42.632 -7.854  0.62 23.84 ?  159 ASN   B CG   1 
ATOM   6534 C  CG   B ASN   B 1 159 ? 47.640 -42.548 -8.006  0.38 21.20 ?  159 ASN   B CG   1 
ATOM   6535 O  OD1  A ASN   B 1 159 ? 47.367 -43.151 -8.948  0.62 24.58 ?  159 ASN   B OD1  1 
ATOM   6536 O  OD1  B ASN   B 1 159 ? 47.422 -42.984 -9.139  0.38 21.79 ?  159 ASN   B OD1  1 
ATOM   6537 N  ND2  A ASN   B 1 159 ? 48.783 -42.799 -7.231  0.62 24.48 ?  159 ASN   B ND2  1 
ATOM   6538 N  ND2  B ASN   B 1 159 ? 48.781 -42.769 -7.360  0.38 21.52 ?  159 ASN   B ND2  1 
ATOM   6539 H  H    A ASN   B 1 159 ? 47.602 -39.801 -8.204  0.62 23.15 ?  159 ASN   B H    1 
ATOM   6540 H  H    B ASN   B 1 159 ? 47.568 -39.699 -8.262  0.38 22.61 ?  159 ASN   B H    1 
ATOM   6541 H  HA   A ASN   B 1 159 ? 45.554 -41.323 -8.846  0.62 23.94 ?  159 ASN   B HA   1 
ATOM   6542 H  HA   B ASN   B 1 159 ? 45.545 -41.242 -8.959  0.38 22.95 ?  159 ASN   B HA   1 
ATOM   6543 H  HB2  A ASN   B 1 159 ? 47.050 -41.263 -6.459  0.62 26.30 ?  159 ASN   B HB2  1 
ATOM   6544 H  HB2  B ASN   B 1 159 ? 47.046 -41.231 -6.572  0.38 24.14 ?  159 ASN   B HB2  1 
ATOM   6545 H  HB3  A ASN   B 1 159 ? 45.936 -42.358 -6.754  0.62 26.30 ?  159 ASN   B HB3  1 
ATOM   6546 H  HB3  B ASN   B 1 159 ? 45.945 -42.331 -6.897  0.38 24.14 ?  159 ASN   B HB3  1 
ATOM   6547 H  HD21 A ASN   B 1 159 ? 49.402 -43.280 -7.591  0.62 29.36 ?  159 ASN   B HD21 1 
ATOM   6548 H  HD21 B ASN   B 1 159 ? 49.405 -43.236 -7.731  0.38 25.81 ?  159 ASN   B HD21 1 
ATOM   6549 H  HD22 A ASN   B 1 159 ? 48.919 -42.436 -6.463  0.62 29.36 ?  159 ASN   B HD22 1 
ATOM   6550 H  HD22 B ASN   B 1 159 ? 48.898 -42.455 -6.569  0.38 25.81 ?  159 ASN   B HD22 1 
ATOM   6551 N  N    . LEU   B 1 160 ? 44.910 -38.970 -6.791  1.00 18.17 ?  160 LEU   B N    1 
ATOM   6552 C  CA   . LEU   B 1 160 ? 43.782 -38.237 -6.231  1.00 17.24 ?  160 LEU   B CA   1 
ATOM   6553 C  C    . LEU   B 1 160 ? 42.985 -37.571 -7.340  1.00 16.44 ?  160 LEU   B C    1 
ATOM   6554 O  O    . LEU   B 1 160 ? 41.748 -37.576 -7.316  1.00 16.24 ?  160 LEU   B O    1 
ATOM   6555 C  CB   . LEU   B 1 160 ? 44.252 -37.209 -5.203  1.00 16.93 ?  160 LEU   B CB   1 
ATOM   6556 C  CG   . LEU   B 1 160 ? 43.118 -36.318 -4.673  1.00 16.62 ?  160 LEU   B CG   1 
ATOM   6557 C  CD1  . LEU   B 1 160 ? 42.005 -37.145 -4.054  1.00 17.41 ?  160 LEU   B CD1  1 
ATOM   6558 C  CD2  . LEU   B 1 160 ? 43.653 -35.312 -3.670  1.00 16.72 ?  160 LEU   B CD2  1 
ATOM   6559 H  H    A LEU   B 1 160 ? 45.682 -38.606 -6.676  0.62 21.79 ?  160 LEU   B H    1 
ATOM   6560 H  H    B LEU   B 1 160 ? 45.687 -38.640 -6.622  0.38 21.79 ?  160 LEU   B H    1 
ATOM   6561 H  HA   . LEU   B 1 160 ? 43.199 -38.867 -5.784  1.00 20.67 ?  160 LEU   B HA   1 
ATOM   6562 H  HB2  . LEU   B 1 160 ? 44.647 -37.682 -4.450  1.00 20.30 ?  160 LEU   B HB2  1 
ATOM   6563 H  HB3  . LEU   B 1 160 ? 44.921 -36.638 -5.616  1.00 20.30 ?  160 LEU   B HB3  1 
ATOM   6564 H  HG   . LEU   B 1 160 ? 42.741 -35.823 -5.413  1.00 19.92 ?  160 LEU   B HG   1 
ATOM   6565 H  HD11 . LEU   B 1 160 ? 41.380 -36.552 -3.616  1.00 20.87 ?  160 LEU   B HD11 1 
ATOM   6566 H  HD12 . LEU   B 1 160 ? 41.551 -37.648 -4.751  1.00 20.87 ?  160 LEU   B HD12 1 
ATOM   6567 H  HD13 . LEU   B 1 160 ? 42.388 -37.760 -3.405  1.00 20.87 ?  160 LEU   B HD13 1 
ATOM   6568 H  HD21 . LEU   B 1 160 ? 42.922 -34.745 -3.380  1.00 20.05 ?  160 LEU   B HD21 1 
ATOM   6569 H  HD22 . LEU   B 1 160 ? 44.026 -35.788 -2.913  1.00 20.05 ?  160 LEU   B HD22 1 
ATOM   6570 H  HD23 . LEU   B 1 160 ? 44.339 -34.776 -4.098  1.00 20.05 ?  160 LEU   B HD23 1 
ATOM   6571 N  N    . TYR   B 1 161 ? 43.681 -37.003 -8.328  1.00 16.52 ?  161 TYR   B N    1 
ATOM   6572 C  CA   . TYR   B 1 161 ? 43.006 -36.436 -9.490  1.00 16.36 ?  161 TYR   B CA   1 
ATOM   6573 C  C    . TYR   B 1 161 ? 42.061 -37.459 -10.107 1.00 16.22 ?  161 TYR   B C    1 
ATOM   6574 O  O    . TYR   B 1 161 ? 40.890 -37.165 -10.366 1.00 15.89 ?  161 TYR   B O    1 
ATOM   6575 C  CB   . TYR   B 1 161 ? 44.046 -35.955 -10.515 1.00 16.74 ?  161 TYR   B CB   1 
ATOM   6576 C  CG   . TYR   B 1 161 ? 43.462 -35.487 -11.829 1.00 17.14 ?  161 TYR   B CG   1 
ATOM   6577 C  CD1  . TYR   B 1 161 ? 43.061 -34.168 -11.998 1.00 17.10 ?  161 TYR   B CD1  1 
ATOM   6578 C  CD2  . TYR   B 1 161 ? 43.295 -36.365 -12.896 1.00 17.63 ?  161 TYR   B CD2  1 
ATOM   6579 C  CE1  . TYR   B 1 161 ? 42.520 -33.737 -13.181 1.00 18.25 ?  161 TYR   B CE1  1 
ATOM   6580 C  CE2  . TYR   B 1 161 ? 42.750 -35.940 -14.088 1.00 18.83 ?  161 TYR   B CE2  1 
ATOM   6581 C  CZ   . TYR   B 1 161 ? 42.367 -34.621 -14.226 1.00 18.91 ?  161 TYR   B CZ   1 
ATOM   6582 O  OH   . TYR   B 1 161 ? 41.820 -34.178 -15.405 1.00 20.87 ?  161 TYR   B OH   1 
ATOM   6583 H  H    . TYR   B 1 161 ? 44.538 -36.944 -8.354  1.00 19.80 ?  161 TYR   B H    1 
ATOM   6584 H  HA   . TYR   B 1 161 ? 42.480 -35.672 -9.211  1.00 19.61 ?  161 TYR   B HA   1 
ATOM   6585 H  HB2  . TYR   B 1 161 ? 44.536 -35.211 -10.135 1.00 20.07 ?  161 TYR   B HB2  1 
ATOM   6586 H  HB3  . TYR   B 1 161 ? 44.653 -36.684 -10.711 1.00 20.07 ?  161 TYR   B HB3  1 
ATOM   6587 H  HD1  . TYR   B 1 161 ? 43.161 -33.562 -11.301 1.00 20.51 ?  161 TYR   B HD1  1 
ATOM   6588 H  HD2  . TYR   B 1 161 ? 43.546 -37.257 -12.806 1.00 21.14 ?  161 TYR   B HD2  1 
ATOM   6589 H  HE1  . TYR   B 1 161 ? 42.262 -32.845 -13.277 1.00 21.89 ?  161 TYR   B HE1  1 
ATOM   6590 H  HE2  . TYR   B 1 161 ? 42.641 -36.536 -14.795 1.00 22.58 ?  161 TYR   B HE2  1 
ATOM   6591 H  HH   . TYR   B 1 161 ? 41.777 -34.809 -15.959 1.00 25.03 ?  161 TYR   B HH   1 
ATOM   6592 N  N    . ASP   B 1 162 ? 42.555 -38.678 -10.334 1.00 16.87 ?  162 ASP   B N    1 
ATOM   6593 C  CA   . ASP   B 1 162 ? 41.725 -39.710 -10.950 1.00 17.42 ?  162 ASP   B CA   1 
ATOM   6594 C  C    . ASP   B 1 162 ? 40.520 -40.053 -10.077 1.00 16.65 ?  162 ASP   B C    1 
ATOM   6595 O  O    . ASP   B 1 162 ? 39.413 -40.265 -10.588 1.00 16.91 ?  162 ASP   B O    1 
ATOM   6596 C  CB   . ASP   B 1 162 ? 42.553 -40.970 -11.213 1.00 18.93 ?  162 ASP   B CB   1 
ATOM   6597 C  CG   . ASP   B 1 162 ? 43.556 -40.801 -12.341 1.00 20.53 ?  162 ASP   B CG   1 
ATOM   6598 O  OD1  . ASP   B 1 162 ? 43.436 -39.847 -13.130 1.00 21.31 ?  162 ASP   B OD1  1 
ATOM   6599 O  OD2  . ASP   B 1 162 ? 44.458 -41.658 -12.457 1.00 21.99 -1 162 ASP   B OD2  1 
ATOM   6600 H  H    . ASP   B 1 162 ? 43.354 -38.928 -10.142 1.00 20.22 ?  162 ASP   B H    1 
ATOM   6601 H  HA   . ASP   B 1 162 ? 41.393 -39.385 -11.799 1.00 20.89 ?  162 ASP   B HA   1 
ATOM   6602 H  HB2  . ASP   B 1 162 ? 43.054 -41.196 -10.417 1.00 22.70 ?  162 ASP   B HB2  1 
ATOM   6603 H  HB3  . ASP   B 1 162 ? 41.956 -41.698 -11.450 1.00 22.70 ?  162 ASP   B HB3  1 
ATOM   6604 N  N    . LYS   B 1 163 ? 40.718 -40.131 -8.760  1.00 16.14 ?  163 LYS   B N    1 
ATOM   6605 C  CA   . LYS   B 1 163 ? 39.597 -40.407 -7.867  1.00 16.66 ?  163 LYS   B CA   1 
ATOM   6606 C  C    . LYS   B 1 163 ? 38.556 -39.295 -7.927  1.00 15.71 ?  163 LYS   B C    1 
ATOM   6607 O  O    . LYS   B 1 163 ? 37.347 -39.565 -7.925  1.00 16.55 ?  163 LYS   B O    1 
ATOM   6608 C  CB   . LYS   B 1 163 ? 40.094 -40.585 -6.435  1.00 19.25 ?  163 LYS   B CB   1 
ATOM   6609 C  CG   . LYS   B 1 163 ? 39.012 -41.066 -5.494  1.00 24.22 ?  163 LYS   B CG   1 
ATOM   6610 C  CD   . LYS   B 1 163 ? 39.494 -41.192 -4.063  1.00 28.84 ?  163 LYS   B CD   1 
ATOM   6611 C  CE   . LYS   B 1 163 ? 38.426 -41.860 -3.207  1.00 32.19 ?  163 LYS   B CE   1 
ATOM   6612 N  NZ   . LYS   B 1 163 ? 38.598 -41.587 -1.754  1.00 34.15 ?  163 LYS   B NZ   1 
ATOM   6613 H  H    . LYS   B 1 163 ? 41.478 -40.021 -8.368  1.00 19.36 ?  163 LYS   B H    1 
ATOM   6614 H  HA   . LYS   B 1 163 ? 39.173 -41.231 -8.143  1.00 19.97 ?  163 LYS   B HA   1 
ATOM   6615 H  HB2  . LYS   B 1 163 ? 40.809 -41.245 -6.429  1.00 23.08 ?  163 LYS   B HB2  1 
ATOM   6616 H  HB3  . LYS   B 1 163 ? 40.424 -39.738 -6.104  1.00 23.08 ?  163 LYS   B HB3  1 
ATOM   6617 H  HG2  . LYS   B 1 163 ? 38.276 -40.435 -5.506  1.00 29.05 ?  163 LYS   B HG2  1 
ATOM   6618 H  HG3  . LYS   B 1 163 ? 38.703 -41.940 -5.786  1.00 29.05 ?  163 LYS   B HG3  1 
ATOM   6619 H  HD2  . LYS   B 1 163 ? 40.295 -41.740 -4.039  1.00 34.59 ?  163 LYS   B HD2  1 
ATOM   6620 H  HD3  . LYS   B 1 163 ? 39.674 -40.311 -3.703  1.00 34.59 ?  163 LYS   B HD3  1 
ATOM   6621 H  HE2  . LYS   B 1 163 ? 37.552 -41.542 -3.479  1.00 38.61 ?  163 LYS   B HE2  1 
ATOM   6622 H  HE3  . LYS   B 1 163 ? 38.478 -42.819 -3.338  1.00 38.61 ?  163 LYS   B HE3  1 
ATOM   6623 H  HZ1  . LYS   B 1 163 ? 37.954 -41.992 -1.292  1.00 40.96 ?  163 LYS   B HZ1  1 
ATOM   6624 H  HZ2  . LYS   B 1 163 ? 39.387 -41.891 -1.480  1.00 40.96 ?  163 LYS   B HZ2  1 
ATOM   6625 H  HZ3  . LYS   B 1 163 ? 38.555 -40.711 -1.602  1.00 40.96 ?  163 LYS   B HZ3  1 
ATOM   6626 N  N    . LEU   B 1 164 ? 39.009 -38.039 -7.976  1.00 14.44 ?  164 LEU   B N    1 
ATOM   6627 C  CA   . LEU   B 1 164 ? 38.096 -36.902 -8.030  1.00 14.22 ?  164 LEU   B CA   1 
ATOM   6628 C  C    . LEU   B 1 164 ? 37.310 -36.886 -9.337  1.00 14.43 ?  164 LEU   B C    1 
ATOM   6629 O  O    . LEU   B 1 164 ? 36.085 -36.692 -9.338  1.00 15.45 ?  164 LEU   B O    1 
ATOM   6630 C  CB   . LEU   B 1 164 ? 38.894 -35.608 -7.868  1.00 13.75 ?  164 LEU   B CB   1 
ATOM   6631 C  CG   . LEU   B 1 164 ? 39.425 -35.335 -6.463  1.00 14.47 ?  164 LEU   B CG   1 
ATOM   6632 C  CD1  . LEU   B 1 164 ? 40.515 -34.270 -6.525  1.00 14.51 ?  164 LEU   B CD1  1 
ATOM   6633 C  CD2  . LEU   B 1 164 ? 38.319 -34.895 -5.527  1.00 15.95 ?  164 LEU   B CD2  1 
ATOM   6634 H  H    . LEU   B 1 164 ? 39.845 -37.823 -7.980  1.00 17.31 ?  164 LEU   B H    1 
ATOM   6635 H  HA   . LEU   B 1 164 ? 37.467 -36.963 -7.303  1.00 17.05 ?  164 LEU   B HA   1 
ATOM   6636 H  HB2  . LEU   B 1 164 ? 39.660 -35.638 -8.469  1.00 16.48 ?  164 LEU   B HB2  1 
ATOM   6637 H  HB3  . LEU   B 1 164 ? 38.326 -34.863 -8.113  1.00 16.48 ?  164 LEU   B HB3  1 
ATOM   6638 H  HG   . LEU   B 1 164 ? 39.826 -36.144 -6.109  1.00 17.34 ?  164 LEU   B HG   1 
ATOM   6639 H  HD11 . LEU   B 1 164 ? 40.842 -34.094 -5.626  1.00 17.40 ?  164 LEU   B HD11 1 
ATOM   6640 H  HD12 . LEU   B 1 164 ? 41.247 -34.589 -7.081  1.00 17.40 ?  164 LEU   B HD12 1 
ATOM   6641 H  HD13 . LEU   B 1 164 ? 40.147 -33.456 -6.905  1.00 17.40 ?  164 LEU   B HD13 1 
ATOM   6642 H  HD21 . LEU   B 1 164 ? 38.701 -34.687 -4.661  1.00 19.12 ?  164 LEU   B HD21 1 
ATOM   6643 H  HD22 . LEU   B 1 164 ? 37.887 -34.109 -5.897  1.00 19.12 ?  164 LEU   B HD22 1 
ATOM   6644 H  HD23 . LEU   B 1 164 ? 37.678 -35.617 -5.443  1.00 19.12 ?  164 LEU   B HD23 1 
ATOM   6645 N  N    . VAL   B 1 165 ? 38.004 -37.062 -10.463 1.00 15.83 ?  165 VAL   B N    1 
ATOM   6646 C  CA   . VAL   B 1 165 ? 37.348 -37.003 -11.764 1.00 17.33 ?  165 VAL   B CA   1 
ATOM   6647 C  C    . VAL   B 1 165 ? 36.421 -38.196 -11.941 1.00 19.19 ?  165 VAL   B C    1 
ATOM   6648 O  O    . VAL   B 1 165 ? 35.256 -38.051 -12.333 1.00 20.35 ?  165 VAL   B O    1 
ATOM   6649 C  CB   . VAL   B 1 165 ? 38.392 -36.928 -12.893 1.00 18.26 ?  165 VAL   B CB   1 
ATOM   6650 C  CG1  . VAL   B 1 165 ? 37.726 -37.036 -14.245 1.00 19.40 ?  165 VAL   B CG1  1 
ATOM   6651 C  CG2  . VAL   B 1 165 ? 39.187 -35.645 -12.793 1.00 17.86 ?  165 VAL   B CG2  1 
ATOM   6652 H  H    . VAL   B 1 165 ? 38.855 -37.218 -10.502 1.00 18.98 ?  165 VAL   B H    1 
ATOM   6653 H  HA   . VAL   B 1 165 ? 36.811 -36.203 -11.809 1.00 20.78 ?  165 VAL   B HA   1 
ATOM   6654 H  HB   . VAL   B 1 165 ? 39.017 -37.667 -12.802 1.00 21.90 ?  165 VAL   B HB   1 
ATOM   6655 H  HG11 . VAL   B 1 165 ? 38.344 -36.737 -14.927 1.00 23.26 ?  165 VAL   B HG11 1 
ATOM   6656 H  HG12 . VAL   B 1 165 ? 37.492 -37.967 -14.402 1.00 23.26 ?  165 VAL   B HG12 1 
ATOM   6657 H  HG13 . VAL   B 1 165 ? 36.930 -36.489 -14.248 1.00 23.26 ?  165 VAL   B HG13 1 
ATOM   6658 H  HG21 . VAL   B 1 165 ? 39.822 -35.604 -13.527 1.00 21.41 ?  165 VAL   B HG21 1 
ATOM   6659 H  HG22 . VAL   B 1 165 ? 38.579 -34.890 -12.843 1.00 21.41 ?  165 VAL   B HG22 1 
ATOM   6660 H  HG23 . VAL   B 1 165 ? 39.664 -35.628 -11.947 1.00 21.41 ?  165 VAL   B HG23 1 
ATOM   6661 N  N    . SER   B 1 166 ? 36.929 -39.398 -11.652 1.00 20.08 ?  166 SER   B N    1 
ATOM   6662 C  CA   . SER   B 1 166 ? 36.169 -40.606 -11.937 1.00 21.38 ?  166 SER   B CA   1 
ATOM   6663 C  C    . SER   B 1 166 ? 34.912 -40.690 -11.087 1.00 21.82 ?  166 SER   B C    1 
ATOM   6664 O  O    . SER   B 1 166 ? 33.940 -41.314 -11.509 1.00 23.35 ?  166 SER   B O    1 
ATOM   6665 C  CB   . SER   B 1 166 ? 37.033 -41.863 -11.761 1.00 22.30 ?  166 SER   B CB   1 
ATOM   6666 O  OG   . SER   B 1 166 ? 37.413 -42.067 -10.411 1.00 22.52 ?  166 SER   B OG   1 
ATOM   6667 H  H    . SER   B 1 166 ? 37.703 -39.537 -11.298 1.00 24.08 ?  166 SER   B H    1 
ATOM   6668 H  HA   . SER   B 1 166 ? 35.893 -40.583 -12.866 1.00 25.64 ?  166 SER   B HA   1 
ATOM   6669 H  HB2  . SER   B 1 166 ? 36.525 -42.637 -12.060 1.00 26.74 ?  166 SER   B HB2  1 
ATOM   6670 H  HB3  . SER   B 1 166 ? 37.834 -41.772 -12.301 1.00 26.74 ?  166 SER   B HB3  1 
ATOM   6671 H  HG   . SER   B 1 166 ? 37.860 -41.410 -10.138 1.00 27.01 ?  166 SER   B HG   1 
ATOM   6672 N  N    . SER   B 1 167 ? 34.897 -40.082 -9.903  1.00 20.60 ?  167 SER   B N    1 
ATOM   6673 C  CA   . SER   B 1 167 ? 33.742 -40.137 -9.014  1.00 19.63 ?  167 SER   B CA   1 
ATOM   6674 C  C    . SER   B 1 167 ? 32.825 -38.919 -9.113  1.00 18.74 ?  167 SER   B C    1 
ATOM   6675 O  O    . SER   B 1 167 ? 31.748 -38.923 -8.505  1.00 18.82 ?  167 SER   B O    1 
ATOM   6676 C  CB   . SER   B 1 167 ? 34.192 -40.314 -7.557  1.00 19.66 ?  167 SER   B CB   1 
ATOM   6677 O  OG   . SER   B 1 167 ? 34.868 -39.154 -7.085  1.00 19.26 ?  167 SER   B OG   1 
ATOM   6678 H  H    . SER   B 1 167 ? 35.550 -39.633 -9.593  1.00 24.70 ?  167 SER   B H    1 
ATOM   6679 H  HA   . SER   B 1 167 ? 33.210 -40.917 -9.250  1.00 23.54 ?  167 SER   B HA   1 
ATOM   6680 H  HB2  . SER   B 1 167 ? 33.408 -40.479 -7.007  1.00 23.58 ?  167 SER   B HB2  1 
ATOM   6681 H  HB3  . SER   B 1 167 ? 34.790 -41.082 -7.510  1.00 23.58 ?  167 SER   B HB3  1 
ATOM   6682 H  HG   . SER   B 1 167 ? 35.545 -39.015 -7.559  1.00 23.09 ?  167 SER   B HG   1 
ATOM   6683 N  N    . PHE   B 1 168 ? 33.205 -37.881 -9.861  1.00 18.44 ?  168 PHE   B N    1 
ATOM   6684 C  CA   . PHE   B 1 168 ? 32.367 -36.682 -9.926  1.00 17.85 ?  168 PHE   B CA   1 
ATOM   6685 C  C    . PHE   B 1 168 ? 31.054 -36.948 -10.659 1.00 15.56 ?  168 PHE   B C    1 
ATOM   6686 O  O    . PHE   B 1 168 ? 30.006 -36.361 -10.319 1.00 16.07 ?  168 PHE   B O    1 
ATOM   6687 C  CB   . PHE   B 1 168 ? 33.128 -35.549 -10.607 1.00 18.54 ?  168 PHE   B CB   1 
ATOM   6688 C  CG   . PHE   B 1 168 ? 32.325 -34.299 -10.741 1.00 18.54 ?  168 PHE   B CG   1 
ATOM   6689 C  CD1  . PHE   B 1 168 ? 31.990 -33.563 -9.616  1.00 19.81 ?  168 PHE   B CD1  1 
ATOM   6690 C  CD2  . PHE   B 1 168 ? 31.883 -33.870 -11.974 1.00 17.76 ?  168 PHE   B CD2  1 
ATOM   6691 C  CE1  . PHE   B 1 168 ? 31.228 -32.418 -9.716  1.00 20.32 ?  168 PHE   B CE1  1 
ATOM   6692 C  CE2  . PHE   B 1 168 ? 31.134 -32.706 -12.090 1.00 18.89 ?  168 PHE   B CE2  1 
ATOM   6693 C  CZ   . PHE   B 1 168 ? 30.800 -31.980 -10.953 1.00 19.28 ?  168 PHE   B CZ   1 
ATOM   6694 H  H    . PHE   B 1 168 ? 33.926 -37.847 -10.327 1.00 22.12 ?  168 PHE   B H    1 
ATOM   6695 H  HA   . PHE   B 1 168 ? 32.149 -36.399 -9.029  1.00 21.40 ?  168 PHE   B HA   1 
ATOM   6696 H  HB2  . PHE   B 1 168 ? 33.915 -35.337 -10.082 1.00 22.23 ?  168 PHE   B HB2  1 
ATOM   6697 H  HB3  . PHE   B 1 168 ? 33.388 -35.827 -11.498 1.00 22.23 ?  168 PHE   B HB3  1 
ATOM   6698 H  HD1  . PHE   B 1 168 ? 32.271 -33.856 -8.779  1.00 23.76 ?  168 PHE   B HD1  1 
ATOM   6699 H  HD2  . PHE   B 1 168 ? 32.105 -34.346 -12.738 1.00 21.30 ?  168 PHE   B HD2  1 
ATOM   6700 H  HE1  . PHE   B 1 168 ? 31.012 -31.935 -8.951  1.00 24.36 ?  168 PHE   B HE1  1 
ATOM   6701 H  HE2  . PHE   B 1 168 ? 30.840 -32.417 -12.927 1.00 22.65 ?  168 PHE   B HE2  1 
ATOM   6702 H  HZ   . PHE   B 1 168 ? 30.289 -31.205 -11.026 1.00 23.12 ?  168 PHE   B HZ   1 
ATOM   6703 N  N    . LEU   B 1 169 ? 31.099 -37.818 -11.664 1.00 16.04 ?  169 LEU   B N    1 
ATOM   6704 C  CA   . LEU   B 1 169 ? 29.930 -38.147 -12.471 1.00 18.14 ?  169 LEU   B CA   1 
ATOM   6705 C  C    . LEU   B 1 169 ? 29.922 -39.588 -12.955 1.00 20.88 ?  169 LEU   B C    1 
ATOM   6706 O  O    . LEU   B 1 169 ? 29.019 -40.005 -13.683 1.00 23.16 ?  169 LEU   B O    1 
ATOM   6707 C  CB   . LEU   B 1 169 ? 29.858 -37.227 -13.686 1.00 19.83 ?  169 LEU   B CB   1 
ATOM   6708 C  CG   . LEU   B 1 169 ? 28.611 -36.350 -13.773 1.00 22.70 ?  169 LEU   B CG   1 
ATOM   6709 C  CD1  . LEU   B 1 169 ? 28.546 -35.698 -15.137 1.00 23.78 ?  169 LEU   B CD1  1 
ATOM   6710 C  CD2  . LEU   B 1 169 ? 27.346 -37.141 -13.492 1.00 22.69 ?  169 LEU   B CD2  1 
ATOM   6711 O  OXT  . LEU   B 1 169 ? 30.828 -40.350 -12.642 1.00 21.71 -1 169 LEU   B OXT  1 
ATOM   6712 H  H    . LEU   B 1 169 ? 31.812 -38.235 -11.912 1.00 19.23 ?  169 LEU   B H    1 
ATOM   6713 H  HA   . LEU   B 1 169 ? 29.142 -38.012 -11.933 1.00 21.75 ?  169 LEU   B HA   1 
ATOM   6714 H  HB2  . LEU   B 1 169 ? 30.626 -36.635 -13.675 1.00 23.78 ?  169 LEU   B HB2  1 
ATOM   6715 H  HB3  . LEU   B 1 169 ? 29.881 -37.769 -14.493 1.00 23.78 ?  169 LEU   B HB3  1 
ATOM   6716 H  HG   . LEU   B 1 169 ? 28.676 -35.643 -13.112 1.00 27.23 ?  169 LEU   B HG   1 
ATOM   6717 H  HD11 . LEU   B 1 169 ? 27.768 -35.119 -15.172 1.00 28.52 ?  169 LEU   B HD11 1 
ATOM   6718 H  HD12 . LEU   B 1 169 ? 29.352 -35.178 -15.276 1.00 28.52 ?  169 LEU   B HD12 1 
ATOM   6719 H  HD13 . LEU   B 1 169 ? 28.475 -36.390 -15.812 1.00 28.52 ?  169 LEU   B HD13 1 
ATOM   6720 H  HD21 . LEU   B 1 169 ? 26.599 -36.718 -13.938 1.00 27.22 ?  169 LEU   B HD21 1 
ATOM   6721 H  HD22 . LEU   B 1 169 ? 27.461 -38.047 -13.826 1.00 27.22 ?  169 LEU   B HD22 1 
ATOM   6722 H  HD23 . LEU   B 1 169 ? 27.195 -37.161 -12.535 1.00 27.22 ?  169 LEU   B HD23 1 
HETATM 6723 C  C1   T TFA   C 2 .   ? 12.148 -1.345  1.497   0.30 11.00 ?  201 TFA   A C1   1 
HETATM 6724 C  C2   T TFA   C 2 .   ? 12.785 -1.802  0.154   0.30 13.55 ?  201 TFA   A C2   1 
HETATM 6725 O  O    T TFA   C 2 .   ? 12.838 -1.608  2.487   0.30 9.36  ?  201 TFA   A O    1 
HETATM 6726 F  F1   T TFA   C 2 .   ? 12.811 -3.148  0.074   0.30 14.79 ?  201 TFA   A F1   1 
HETATM 6727 F  F2   T TFA   C 2 .   ? 12.093 -1.378  -0.916  0.30 13.77 ?  201 TFA   A F2   1 
HETATM 6728 F  F3   T TFA   C 2 .   ? 14.036 -1.355  -0.023  0.30 15.08 ?  201 TFA   A F3   1 
HETATM 6729 O  OXT  T TFA   C 2 .   ? 11.056 -0.780  1.414   0.30 10.59 ?  201 TFA   A OXT  1 
HETATM 6730 N  N2   B A1A9R D 3 .   ? 15.111 0.830   1.718   0.38 9.65  ?  202 A1A9R A N2   1 
HETATM 6731 C  C3   B A1A9R D 3 .   ? 14.076 -0.020  -0.365  0.38 12.98 ?  202 A1A9R A C3   1 
HETATM 6732 C  C6   B A1A9R D 3 .   ? 10.881 2.330   0.069   0.38 13.83 ?  202 A1A9R A C6   1 
HETATM 6733 C  C9   B A1A9R D 3 .   ? 15.381 2.078   5.178   0.38 9.72  ?  202 A1A9R A C9   1 
HETATM 6734 C  C12  B A1A9R D 3 .   ? 15.810 4.223   4.632   0.38 9.79  ?  202 A1A9R A C12  1 
HETATM 6735 C  C1   B A1A9R D 3 .   ? 16.008 -1.220  0.713   0.38 12.50 ?  202 A1A9R A C1   1 
HETATM 6736 C  C10  B A1A9R D 3 .   ? 15.382 2.146   3.744   0.38 9.75  ?  202 A1A9R A C10  1 
HETATM 6737 C  C11  B A1A9R D 3 .   ? 15.668 3.534   3.433   0.38 9.91  ?  202 A1A9R A C11  1 
HETATM 6738 C  C2   B A1A9R D 3 .   ? 14.719 -0.378  0.988   0.38 11.46 ?  202 A1A9R A C2   1 
HETATM 6739 C  C4   B A1A9R D 3 .   ? 12.799 0.762   -0.311  0.38 13.69 ?  202 A1A9R A C4   1 
HETATM 6740 C  C5   B A1A9R D 3 .   ? 10.669 1.315   -0.834  0.38 13.64 ?  202 A1A9R A C5   1 
HETATM 6741 C  C7   B A1A9R D 3 .   ? 15.135 0.919   3.095   0.38 9.65  ?  202 A1A9R A C7   1 
HETATM 6742 C  C8   B A1A9R D 3 .   ? 14.946 -0.119  5.194   0.38 10.18 ?  202 A1A9R A C8   1 
HETATM 6743 N  N1   B A1A9R D 3 .   ? 11.747 0.432   -1.046  0.38 13.99 ?  202 A1A9R A N1   1 
HETATM 6744 N  N3   B A1A9R D 3 .   ? 14.919 -0.210  3.829   0.38 9.91  ?  202 A1A9R A N3   1 
HETATM 6745 N  N4   B A1A9R D 3 .   ? 15.167 0.980   5.920   0.38 10.13 ?  202 A1A9R A N4   1 
HETATM 6746 N  N5   B A1A9R D 3 .   ? 15.639 3.322   5.651   0.38 9.50  ?  202 A1A9R A N5   1 
HETATM 6747 O  O1   B A1A9R D 3 .   ? 15.574 -2.365  0.024   0.38 12.98 ?  202 A1A9R A O1   1 
HETATM 6748 S  S1   B A1A9R D 3 .   ? 12.485 2.204   0.684   0.38 14.05 ?  202 A1A9R A S1   1 
HETATM 6749 H  H9   B A1A9R D 3 .   ? 15.373 1.643   1.192   0.38 11.57 ?  202 A1A9R A H9   1 
HETATM 6750 H  H5   B A1A9R D 3 .   ? 14.790 0.539   -0.962  0.38 15.56 ?  202 A1A9R A H5   1 
HETATM 6751 H  H6   B A1A9R D 3 .   ? 13.918 -0.921  -1.005  0.38 15.56 ?  202 A1A9R A H6   1 
HETATM 6752 H  H8   B A1A9R D 3 .   ? 10.180 3.092   0.356   0.38 16.58 ?  202 A1A9R A H8   1 
HETATM 6753 H  H12  B A1A9R D 3 .   ? 16.013 5.235   4.898   0.38 11.74 ?  202 A1A9R A H12  1 
HETATM 6754 H  H4   B A1A9R D 3 .   ? 16.738 -0.655  0.102   0.38 14.99 ?  202 A1A9R A H4   1 
HETATM 6755 H  H3   B A1A9R D 3 .   ? 16.545 -1.521  1.640   0.38 14.99 ?  202 A1A9R A H3   1 
HETATM 6756 H  H11  B A1A9R D 3 .   ? 15.750 3.995   2.479   0.38 11.88 ?  202 A1A9R A H11  1 
HETATM 6757 H  H1   B A1A9R D 3 .   ? 13.973 -0.950  1.570   0.38 13.73 ?  202 A1A9R A H1   1 
HETATM 6758 H  H7   B A1A9R D 3 .   ? 9.769  1.103   -1.397  0.38 16.35 ?  202 A1A9R A H7   1 
HETATM 6759 H  H10  B A1A9R D 3 .   ? 14.758 -1.022  5.803   0.38 12.20 ?  202 A1A9R A H10  1 
HETATM 6760 H  H13  B A1A9R D 3 .   ? 15.687 3.568   6.681   0.38 11.38 ?  202 A1A9R A H13  1 
HETATM 6761 H  H2   B A1A9R D 3 .   ? 16.301 -2.999  0.042   0.38 15.56 ?  202 A1A9R A H2   1 
HETATM 6762 CL CL   B CL    E 4 .   ? 16.121 2.767   -1.109  0.38 13.79 ?  203 CL    A CL   1 
HETATM 6763 O  O    . HOH   F 5 .   ? 4.721  3.766   0.727   1.00 22.07 ?  301 HOH   A O    1 
HETATM 6764 O  O    . HOH   F 5 .   ? 14.735 -4.576  20.490  1.00 45.30 ?  302 HOH   A O    1 
HETATM 6765 O  O    . HOH   F 5 .   ? 18.582 -2.363  -16.445 1.00 49.42 ?  303 HOH   A O    1 
HETATM 6766 O  O    . HOH   F 5 .   ? 34.280 -1.836  12.527  1.00 37.35 ?  304 HOH   A O    1 
HETATM 6767 O  O    . HOH   F 5 .   ? 28.908 0.426   -9.713  1.00 20.35 ?  305 HOH   A O    1 
HETATM 6768 O  O    . HOH   F 5 .   ? 7.587  -6.236  -6.581  1.00 41.59 ?  306 HOH   A O    1 
HETATM 6769 O  O    . HOH   F 5 .   ? 15.073 -12.207 18.627  1.00 40.86 ?  307 HOH   A O    1 
HETATM 6770 O  O    . HOH   F 5 .   ? 11.899 0.430   14.703  1.00 31.87 ?  308 HOH   A O    1 
HETATM 6771 O  O    . HOH   F 5 .   ? 28.100 -6.265  19.714  1.00 43.87 ?  309 HOH   A O    1 
HETATM 6772 O  O    B HOH   F 5 .   ? 13.311 -1.114  -6.435  0.38 30.30 ?  310 HOH   A O    1 
HETATM 6773 O  O    . HOH   F 5 .   ? 11.646 -10.800 -10.044 1.00 45.36 ?  311 HOH   A O    1 
HETATM 6774 O  O    . HOH   F 5 .   ? 14.656 -13.897 16.669  1.00 25.02 ?  312 HOH   A O    1 
HETATM 6775 O  O    . HOH   F 5 .   ? 22.707 12.505  1.623   1.00 13.70 ?  313 HOH   A O    1 
HETATM 6776 O  O    . HOH   F 5 .   ? 7.904  -12.618 -0.834  1.00 19.83 ?  314 HOH   A O    1 
HETATM 6777 O  O    . HOH   F 5 .   ? 13.900 -4.819  17.377  1.00 25.35 ?  315 HOH   A O    1 
HETATM 6778 O  O    . HOH   F 5 .   ? 14.168 -4.513  -11.887 1.00 39.12 ?  316 HOH   A O    1 
HETATM 6779 O  O    . HOH   F 5 .   ? 42.453 10.541  5.162   1.00 19.74 ?  317 HOH   A O    1 
HETATM 6780 O  O    . HOH   F 5 .   ? 0.687  -4.284  0.011   1.00 28.62 ?  318 HOH   A O    1 
HETATM 6781 O  O    A HOH   F 5 .   ? -0.499 -3.058  3.113   0.62 32.26 ?  319 HOH   A O    1 
HETATM 6782 O  O    . HOH   F 5 .   ? 30.210 -13.344 -8.495  1.00 19.02 ?  320 HOH   A O    1 
HETATM 6783 O  O    B HOH   F 5 .   ? 21.584 2.965   -0.089  0.38 14.14 ?  321 HOH   A O    1 
HETATM 6784 O  O    . HOH   F 5 .   ? 36.102 -5.110  -0.553  1.00 30.98 ?  322 HOH   A O    1 
HETATM 6785 O  O    . HOH   F 5 .   ? 18.907 -21.941 6.964   1.00 30.62 ?  323 HOH   A O    1 
HETATM 6786 O  O    . HOH   F 5 .   ? 16.962 -19.227 4.931   1.00 14.19 ?  324 HOH   A O    1 
HETATM 6787 O  O    . HOH   F 5 .   ? 14.509 -0.537  -12.109 1.00 24.47 ?  325 HOH   A O    1 
HETATM 6788 O  O    A HOH   F 5 .   ? 6.928  -8.126  11.862  0.62 14.35 ?  326 HOH   A O    1 
HETATM 6789 O  O    . HOH   F 5 .   ? 9.292  -10.079 19.477  1.00 39.88 ?  327 HOH   A O    1 
HETATM 6790 O  O    B HOH   F 5 .   ? 10.930 -1.074  2.098   0.38 17.32 ?  328 HOH   A O    1 
HETATM 6791 O  O    . HOH   F 5 .   ? 17.058 -17.949 15.070  1.00 26.30 ?  329 HOH   A O    1 
HETATM 6792 O  O    A HOH   F 5 .   ? 3.577  -9.427  9.746   0.62 24.81 ?  330 HOH   A O    1 
HETATM 6793 O  O    . HOH   F 5 .   ? 14.463 -24.650 11.586  1.00 36.59 ?  331 HOH   A O    1 
HETATM 6794 O  O    . HOH   F 5 .   ? 26.463 -19.324 -1.737  1.00 13.43 ?  332 HOH   A O    1 
HETATM 6795 O  O    B HOH   F 5 .   ? 15.302 6.852   6.900   0.38 17.55 ?  333 HOH   A O    1 
HETATM 6796 O  O    . HOH   F 5 .   ? 13.519 -15.198 -7.406  1.00 24.09 ?  334 HOH   A O    1 
HETATM 6797 O  O    A HOH   F 5 .   ? 17.474 -1.691  0.447   0.62 17.11 ?  335 HOH   A O    1 
HETATM 6798 O  O    . HOH   F 5 .   ? 30.941 6.221   -12.273 1.00 27.92 ?  336 HOH   A O    1 
HETATM 6799 O  O    . HOH   F 5 .   ? 30.990 -18.121 7.825   1.00 18.67 ?  337 HOH   A O    1 
HETATM 6800 O  O    . HOH   F 5 .   ? 27.909 0.806   -7.158  1.00 13.46 ?  338 HOH   A O    1 
HETATM 6801 O  O    . HOH   F 5 .   ? 19.861 -12.539 -8.808  1.00 24.47 ?  339 HOH   A O    1 
HETATM 6802 O  O    . HOH   F 5 .   ? 27.270 13.786  2.866   1.00 27.35 ?  340 HOH   A O    1 
HETATM 6803 O  O    . HOH   F 5 .   ? 28.285 -0.158  -13.409 1.00 33.24 ?  341 HOH   A O    1 
HETATM 6804 O  O    . HOH   F 5 .   ? 37.511 2.819   10.234  1.00 27.77 ?  342 HOH   A O    1 
HETATM 6805 O  O    . HOH   F 5 .   ? 38.253 10.142  7.141   1.00 38.94 ?  343 HOH   A O    1 
HETATM 6806 O  O    . HOH   F 5 .   ? 9.868  -21.362 5.709   1.00 17.26 ?  344 HOH   A O    1 
HETATM 6807 O  O    A HOH   F 5 .   ? 14.257 0.602   6.805   0.62 20.78 ?  345 HOH   A O    1 
HETATM 6808 O  O    . HOH   F 5 .   ? 20.601 -19.680 -5.032  1.00 24.45 ?  346 HOH   A O    1 
HETATM 6809 O  O    . HOH   F 5 .   ? -0.728 -8.480  2.009   1.00 42.62 ?  347 HOH   A O    1 
HETATM 6810 O  O    A HOH   F 5 .   ? 14.613 -3.628  3.105   0.62 15.53 ?  348 HOH   A O    1 
HETATM 6811 O  O    . HOH   F 5 .   ? 18.629 -19.338 13.546  1.00 32.96 ?  349 HOH   A O    1 
HETATM 6812 O  O    . HOH   F 5 .   ? 33.980 -1.087  -8.962  1.00 26.33 ?  350 HOH   A O    1 
HETATM 6813 O  O    . HOH   F 5 .   ? 22.278 5.419   18.946  1.00 41.72 ?  351 HOH   A O    1 
HETATM 6814 O  O    . HOH   F 5 .   ? 38.555 4.987   6.966   1.00 14.81 ?  352 HOH   A O    1 
HETATM 6815 O  O    A HOH   F 5 .   ? 15.174 4.017   17.824  0.62 41.49 ?  353 HOH   A O    1 
HETATM 6816 O  O    . HOH   F 5 .   ? 26.849 11.421  1.645   1.00 15.44 ?  354 HOH   A O    1 
HETATM 6817 O  O    A HOH   F 5 .   ? 13.283 -1.416  -6.517  0.62 12.75 ?  355 HOH   A O    1 
HETATM 6818 O  O    . HOH   F 5 .   ? 42.545 4.274   5.385   1.00 29.74 ?  356 HOH   A O    1 
HETATM 6819 O  O    . HOH   F 5 .   ? 15.189 -21.515 14.249  1.00 17.16 ?  357 HOH   A O    1 
HETATM 6820 O  O    . HOH   F 5 .   ? 44.334 7.097   6.412   1.00 25.24 ?  358 HOH   A O    1 
HETATM 6821 O  O    . HOH   F 5 .   ? 31.679 8.255   14.806  1.00 24.03 ?  359 HOH   A O    1 
HETATM 6822 O  O    . HOH   F 5 .   ? 39.741 -1.058  -5.165  1.00 20.83 ?  360 HOH   A O    1 
HETATM 6823 O  O    B HOH   F 5 .   ? 14.790 4.039   17.049  0.38 27.79 ?  361 HOH   A O    1 
HETATM 6824 O  O    . HOH   F 5 .   ? 25.685 -0.821  -7.383  1.00 15.04 ?  362 HOH   A O    1 
HETATM 6825 O  O    . HOH   F 5 .   ? 14.336 -21.168 -4.218  1.00 28.16 ?  363 HOH   A O    1 
HETATM 6826 O  O    . HOH   F 5 .   ? 11.711 -10.646 17.005  1.00 23.51 ?  364 HOH   A O    1 
HETATM 6827 O  O    . HOH   F 5 .   ? 37.244 -2.767  9.661   1.00 40.38 ?  365 HOH   A O    1 
HETATM 6828 O  O    B HOH   F 5 .   ? 11.334 6.434   9.011   0.38 22.17 ?  366 HOH   A O    1 
HETATM 6829 O  O    . HOH   F 5 .   ? 16.171 16.626  8.651   1.00 33.71 ?  367 HOH   A O    1 
HETATM 6830 O  O    B HOH   F 5 .   ? 11.114 2.024   11.984  0.38 18.11 ?  368 HOH   A O    1 
HETATM 6831 O  O    . HOH   F 5 .   ? 35.756 -12.654 6.873   1.00 15.24 ?  369 HOH   A O    1 
HETATM 6832 O  O    . HOH   F 5 .   ? 17.111 -17.748 -5.011  1.00 26.24 ?  370 HOH   A O    1 
HETATM 6833 O  O    B HOH   F 5 .   ? 13.198 -3.401  -0.885  0.38 23.06 ?  371 HOH   A O    1 
HETATM 6834 O  O    . HOH   F 5 .   ? 24.020 -2.102  -2.109  1.00 10.25 ?  372 HOH   A O    1 
HETATM 6835 O  O    . HOH   F 5 .   ? 30.783 3.102   8.269   1.00 11.43 ?  373 HOH   A O    1 
HETATM 6836 O  O    . HOH   F 5 .   ? 33.614 -7.148  4.322   1.00 16.15 ?  374 HOH   A O    1 
HETATM 6837 O  O    . HOH   F 5 .   ? 21.291 -2.270  -2.426  1.00 15.42 ?  375 HOH   A O    1 
HETATM 6838 O  O    . HOH   F 5 .   ? 37.341 11.979  4.928   1.00 30.47 ?  376 HOH   A O    1 
HETATM 6839 O  O    . HOH   F 5 .   ? 31.055 -13.937 -2.433  1.00 12.95 ?  377 HOH   A O    1 
HETATM 6840 O  O    . HOH   F 5 .   ? 22.110 -19.252 11.449  1.00 33.31 ?  378 HOH   A O    1 
HETATM 6841 O  O    . HOH   F 5 .   ? 31.878 -9.327  -6.613  1.00 21.54 ?  379 HOH   A O    1 
HETATM 6842 O  O    . HOH   F 5 .   ? 43.944 8.428   -3.073  1.00 26.89 ?  380 HOH   A O    1 
HETATM 6843 O  O    . HOH   F 5 .   ? 21.860 -21.883 8.465   1.00 26.27 ?  381 HOH   A O    1 
HETATM 6844 O  O    . HOH   F 5 .   ? 14.059 -23.020 7.455   1.00 17.04 ?  382 HOH   A O    1 
HETATM 6845 O  O    . HOH   F 5 .   ? 16.543 -22.035 0.974   1.00 28.10 ?  383 HOH   A O    1 
HETATM 6846 O  O    . HOH   F 5 .   ? 22.624 -11.907 21.815  1.00 48.30 ?  384 HOH   A O    1 
HETATM 6847 O  O    . HOH   F 5 .   ? 15.465 11.809  7.881   1.00 42.57 ?  385 HOH   A O    1 
HETATM 6848 O  O    . HOH   F 5 .   ? 33.513 -16.951 8.119   1.00 19.22 ?  386 HOH   A O    1 
HETATM 6849 O  O    . HOH   F 5 .   ? 18.580 9.509   8.995   1.00 20.95 ?  387 HOH   A O    1 
HETATM 6850 O  O    . HOH   F 5 .   ? 43.354 7.806   2.669   1.00 26.48 ?  388 HOH   A O    1 
HETATM 6851 O  O    . HOH   F 5 .   ? 27.430 -10.571 14.082  1.00 16.81 ?  389 HOH   A O    1 
HETATM 6852 O  O    B HOH   F 5 .   ? 14.869 -2.999  3.298   0.38 13.55 ?  390 HOH   A O    1 
HETATM 6853 O  O    . HOH   F 5 .   ? 15.077 -8.094  -9.689  1.00 22.64 ?  391 HOH   A O    1 
HETATM 6854 O  O    . HOH   F 5 .   ? 31.740 -7.327  -9.853  1.00 21.13 ?  392 HOH   A O    1 
HETATM 6855 O  O    . HOH   F 5 .   ? 21.195 10.264  15.007  1.00 37.17 ?  393 HOH   A O    1 
HETATM 6856 O  O    . HOH   F 5 .   ? 24.407 3.572   -1.826  1.00 14.10 ?  394 HOH   A O    1 
HETATM 6857 O  O    . HOH   F 5 .   ? 6.413  -5.450  11.139  1.00 16.97 ?  395 HOH   A O    1 
HETATM 6858 O  O    . HOH   F 5 .   ? 24.633 -17.487 12.763  1.00 24.26 ?  396 HOH   A O    1 
HETATM 6859 O  O    T HOH   F 5 .   ? 15.386 -0.396  2.391   0.30 12.32 ?  397 HOH   A O    1 
HETATM 6860 O  O    . HOH   F 5 .   ? 6.678  -3.149  12.766  1.00 26.80 ?  398 HOH   A O    1 
HETATM 6861 O  O    . HOH   F 5 .   ? 24.143 -7.673  14.437  1.00 16.05 ?  399 HOH   A O    1 
HETATM 6862 O  O    A HOH   F 5 .   ? 24.559 2.055   -6.988  0.62 15.81 ?  400 HOH   A O    1 
HETATM 6863 O  O    . HOH   F 5 .   ? 20.538 -19.986 2.827   1.00 17.04 ?  401 HOH   A O    1 
HETATM 6864 O  O    . HOH   F 5 .   ? 37.512 -1.997  5.785   1.00 26.32 ?  402 HOH   A O    1 
HETATM 6865 O  O    . HOH   F 5 .   ? 32.767 -9.236  5.994   1.00 19.59 ?  403 HOH   A O    1 
HETATM 6866 O  O    B HOH   F 5 .   ? 12.078 -1.809  -2.865  0.38 14.99 ?  404 HOH   A O    1 
HETATM 6867 O  O    . HOH   F 5 .   ? 27.332 2.359   18.670  1.00 29.36 ?  405 HOH   A O    1 
HETATM 6868 O  O    A HOH   F 5 .   ? 11.046 -0.353  1.940   0.32 17.20 ?  406 HOH   A O    1 
HETATM 6869 O  O    . HOH   F 5 .   ? 23.912 -15.722 -9.143  1.00 37.14 ?  407 HOH   A O    1 
HETATM 6870 O  O    . HOH   F 5 .   ? 27.398 -6.087  -14.014 1.00 33.69 ?  408 HOH   A O    1 
HETATM 6871 O  O    . HOH   F 5 .   ? 30.674 1.919   16.682  1.00 20.35 ?  409 HOH   A O    1 
HETATM 6872 O  O    B HOH   F 5 .   ? 22.481 5.431   -1.978  0.38 20.02 ?  410 HOH   A O    1 
HETATM 6873 O  O    . HOH   F 5 .   ? 23.479 11.396  4.055   1.00 11.51 ?  411 HOH   A O    1 
HETATM 6874 O  O    . HOH   F 5 .   ? 5.415  2.829   4.928   1.00 30.66 ?  412 HOH   A O    1 
HETATM 6875 O  O    . HOH   F 5 .   ? 15.847 2.091   24.724  1.00 45.18 ?  413 HOH   A O    1 
HETATM 6876 O  O    . HOH   F 5 .   ? 28.592 -10.586 -14.008 1.00 42.16 ?  414 HOH   A O    1 
HETATM 6877 O  O    . HOH   F 5 .   ? 23.893 -20.256 -1.328  1.00 15.61 ?  415 HOH   A O    1 
HETATM 6878 O  O    A HOH   F 5 .   ? 15.780 -0.918  5.275   0.62 20.46 ?  416 HOH   A O    1 
HETATM 6879 O  O    . HOH   F 5 .   ? 30.018 -10.043 13.053  1.00 20.95 ?  417 HOH   A O    1 
HETATM 6880 O  O    . HOH   F 5 .   ? 26.944 4.151   -0.666  1.00 12.01 ?  418 HOH   A O    1 
HETATM 6881 O  O    B HOH   F 5 .   ? 8.170  4.008   1.135   0.38 19.25 ?  419 HOH   A O    1 
HETATM 6882 O  O    . HOH   F 5 .   ? 38.102 -1.360  -1.945  1.00 18.07 ?  420 HOH   A O    1 
HETATM 6883 O  O    . HOH   F 5 .   ? 32.665 -4.303  -9.864  1.00 27.83 ?  421 HOH   A O    1 
HETATM 6884 O  O    . HOH   F 5 .   ? 30.283 -12.887 13.548  1.00 19.17 ?  422 HOH   A O    1 
HETATM 6885 O  O    . HOH   F 5 .   ? 40.861 -8.232  -6.848  1.00 38.59 ?  423 HOH   A O    1 
HETATM 6886 O  O    A HOH   F 5 .   ? 21.328 3.176   -0.349  0.62 10.07 ?  424 HOH   A O    1 
HETATM 6887 O  O    A HOH   F 5 .   ? 18.936 -0.648  -1.622  0.62 12.38 ?  425 HOH   A O    1 
HETATM 6888 O  O    . HOH   F 5 .   ? 8.481  -21.300 4.081   1.00 49.06 ?  426 HOH   A O    1 
HETATM 6889 O  O    A HOH   F 5 .   ? 20.075 4.559   -7.546  0.62 16.09 ?  427 HOH   A O    1 
HETATM 6890 O  O    . HOH   F 5 .   ? 21.718 -13.825 -8.120  1.00 45.45 ?  428 HOH   A O    1 
HETATM 6891 O  O    . HOH   F 5 .   ? 10.341 -13.684 -1.642  1.00 15.65 ?  429 HOH   A O    1 
HETATM 6892 O  O    . HOH   F 5 .   ? 16.214 -14.105 20.188  1.00 51.09 ?  430 HOH   A O    1 
HETATM 6893 O  O    . HOH   F 5 .   ? -1.274 -4.476  7.629   1.00 53.65 ?  431 HOH   A O    1 
HETATM 6894 O  O    . HOH   F 5 .   ? 35.052 -5.234  -3.084  1.00 17.02 ?  432 HOH   A O    1 
HETATM 6895 O  O    . HOH   F 5 .   ? 16.005 6.856   3.005   1.00 23.02 ?  433 HOH   A O    1 
HETATM 6896 O  O    . HOH   F 5 .   ? 41.577 1.517   5.009   1.00 37.10 ?  434 HOH   A O    1 
HETATM 6897 O  O    A HOH   F 5 .   ? 24.069 3.975   -4.918  0.62 19.31 ?  435 HOH   A O    1 
HETATM 6898 O  O    . HOH   F 5 .   ? 32.518 -10.647 3.240   1.00 31.26 ?  436 HOH   A O    1 
HETATM 6899 O  O    . HOH   F 5 .   ? 44.905 -0.599  3.074   1.00 42.93 ?  437 HOH   A O    1 
HETATM 6900 O  O    . HOH   F 5 .   ? 27.043 -3.078  19.348  1.00 36.21 ?  438 HOH   A O    1 
HETATM 6901 O  O    . HOH   F 5 .   ? 36.728 -4.952  5.391   1.00 23.56 ?  439 HOH   A O    1 
HETATM 6902 O  O    B HOH   F 5 .   ? 23.192 7.875   -3.061  0.38 31.21 ?  440 HOH   A O    1 
HETATM 6903 O  O    . HOH   F 5 .   ? 22.632 8.158   18.334  1.00 46.89 ?  441 HOH   A O    1 
HETATM 6904 O  O    A HOH   F 5 .   ? 8.987  -12.084 17.204  0.62 38.81 ?  442 HOH   A O    1 
HETATM 6905 O  O    A HOH   F 5 .   ? 11.020 1.586   12.757  0.62 19.12 ?  443 HOH   A O    1 
HETATM 6906 O  O    B HOH   F 5 .   ? 18.746 -1.070  -1.541  0.38 12.26 ?  444 HOH   A O    1 
HETATM 6907 O  O    . HOH   F 5 .   ? 19.410 -10.866 23.935  1.00 68.25 ?  445 HOH   A O    1 
HETATM 6908 O  O    . HOH   F 5 .   ? 23.501 -7.979  17.104  1.00 20.33 ?  446 HOH   A O    1 
HETATM 6909 O  O    A HOH   F 5 .   ? 16.237 2.970   -1.439  0.62 21.05 ?  447 HOH   A O    1 
HETATM 6910 O  O    . HOH   F 5 .   ? 37.702 -8.829  -3.421  1.00 22.83 ?  448 HOH   A O    1 
HETATM 6911 O  O    . HOH   F 5 .   ? 23.288 -20.903 1.376   1.00 17.55 ?  449 HOH   A O    1 
HETATM 6912 O  O    . HOH   F 5 .   ? 21.267 -9.155  21.305  1.00 54.46 ?  450 HOH   A O    1 
HETATM 6913 O  O    A HOH   F 5 .   ? 23.180 7.530   -3.240  0.62 23.73 ?  451 HOH   A O    1 
HETATM 6914 O  O    . HOH   F 5 .   ? 18.424 4.930   -15.098 1.00 49.15 ?  452 HOH   A O    1 
HETATM 6915 O  O    . HOH   F 5 .   ? 34.401 -8.090  -0.533  1.00 27.55 ?  453 HOH   A O    1 
HETATM 6916 O  O    . HOH   F 5 .   ? 10.384 -22.198 -1.171  1.00 54.46 ?  454 HOH   A O    1 
HETATM 6917 O  O    . HOH   F 5 .   ? 18.354 -15.944 16.321  1.00 37.12 ?  455 HOH   A O    1 
HETATM 6918 O  O    A HOH   F 5 .   ? 18.842 2.055   -0.749  0.62 9.60  ?  456 HOH   A O    1 
HETATM 6919 O  O    . HOH   F 5 .   ? 30.605 14.779  2.775   1.00 18.41 ?  457 HOH   A O    1 
HETATM 6920 O  O    . HOH   F 5 .   ? 9.451  -16.279 -1.984  1.00 42.34 ?  458 HOH   A O    1 
HETATM 6921 O  O    . HOH   F 5 .   ? 31.297 -12.792 0.021   1.00 19.13 ?  459 HOH   A O    1 
HETATM 6922 O  O    A HOH   F 5 .   ? 14.007 -0.312  3.467   0.32 31.27 ?  460 HOH   A O    1 
HETATM 6923 O  O    . HOH   F 5 .   ? 20.549 -17.758 24.828  1.00 59.35 ?  461 HOH   A O    1 
HETATM 6924 O  O    . HOH   F 5 .   ? 29.704 -16.033 10.689  1.00 34.10 ?  462 HOH   A O    1 
HETATM 6925 O  O    . HOH   F 5 .   ? 21.466 -14.691 17.922  1.00 55.27 ?  463 HOH   A O    1 
HETATM 6926 O  O    B HOH   F 5 .   ? 19.036 1.524   -0.505  0.38 11.68 ?  464 HOH   A O    1 
HETATM 6927 O  O    . HOH   F 5 .   ? 27.765 7.048   -6.433  1.00 34.43 ?  465 HOH   A O    1 
HETATM 6928 O  O    . HOH   F 5 .   ? 25.369 8.242   -4.825  1.00 27.08 ?  466 HOH   A O    1 
HETATM 6929 O  O    . HOH   F 5 .   ? 32.416 -15.922 10.834  1.00 31.65 ?  467 HOH   A O    1 
HETATM 6930 O  O    . HOH   F 5 .   ? 29.737 -1.970  -12.774 1.00 47.15 ?  468 HOH   A O    1 
HETATM 6931 O  O    . HOH   F 5 .   ? 24.833 5.712   20.729  1.00 48.15 ?  469 HOH   A O    1 
HETATM 6932 O  O    . HOH   F 5 .   ? 19.810 -17.292 -5.021  1.00 23.21 ?  470 HOH   A O    1 
HETATM 6933 O  O    . HOH   F 5 .   ? 23.143 -22.309 -3.356  1.00 34.05 ?  471 HOH   A O    1 
HETATM 6934 O  O    . HOH   F 5 .   ? 24.627 14.602  7.836   1.00 34.55 ?  472 HOH   A O    1 
HETATM 6935 O  O    . HOH   F 5 .   ? 11.949 -13.366 16.431  1.00 54.83 ?  473 HOH   A O    1 
HETATM 6936 O  O    B HOH   F 5 .   ? 12.497 -3.218  1.931   0.38 18.88 ?  474 HOH   A O    1 
HETATM 6937 O  O    . HOH   F 5 .   ? 15.694 -21.446 3.708   1.00 22.36 ?  475 HOH   A O    1 
HETATM 6938 O  O    . HOH   F 5 .   ? 39.620 -7.055  -3.507  1.00 46.67 ?  476 HOH   A O    1 
HETATM 6939 O  O    . HOH   F 5 .   ? 23.504 13.742  5.478   1.00 17.20 ?  477 HOH   A O    1 
HETATM 6940 O  O    . HOH   F 5 .   ? 18.763 10.945  11.233  1.00 33.14 ?  478 HOH   A O    1 
HETATM 6941 O  O    A HOH   F 5 .   ? 21.943 5.284   -5.837  0.62 26.46 ?  479 HOH   A O    1 
HETATM 6942 O  O    . HOH   F 5 .   ? 26.906 11.698  -1.365  1.00 31.38 ?  480 HOH   A O    1 
HETATM 6943 O  O    . HOH   F 5 .   ? 18.103 -16.182 -8.807  1.00 40.04 ?  481 HOH   A O    1 
HETATM 6944 O  O    . HOH   F 5 .   ? 27.461 -11.380 16.591  1.00 38.04 ?  482 HOH   A O    1 
HETATM 6945 O  O    . HOH   F 5 .   ? 10.997 -15.007 -6.121  1.00 33.74 ?  483 HOH   A O    1 
HETATM 6946 O  O    . HOH   F 5 .   ? 12.281 1.593   17.311  1.00 42.45 ?  484 HOH   A O    1 
HETATM 6947 O  O    . HOH   F 5 .   ? 25.803 10.790  -3.743  1.00 24.71 ?  485 HOH   A O    1 
HETATM 6948 O  O    B HOH   F 5 .   ? 16.257 8.509   8.682   0.38 24.34 ?  486 HOH   A O    1 
HETATM 6949 O  O    . HOH   F 5 .   ? 15.668 -17.049 -6.971  1.00 28.30 ?  487 HOH   A O    1 
HETATM 6950 O  O    . HOH   F 5 .   ? 13.918 -10.352 -10.896 1.00 33.78 ?  488 HOH   A O    1 
HETATM 6951 O  O    . HOH   F 5 .   ? 35.196 7.489   12.243  1.00 46.55 ?  489 HOH   A O    1 
HETATM 6952 O  O    . HOH   F 5 .   ? 28.813 9.078   17.509  1.00 39.61 ?  490 HOH   A O    1 
HETATM 6953 O  O    . HOH   F 5 .   ? 23.130 11.832  -4.040  1.00 18.41 ?  491 HOH   A O    1 
HETATM 6954 O  O    . HOH   F 5 .   ? 17.383 -18.662 19.807  1.00 52.21 ?  492 HOH   A O    1 
HETATM 6955 O  O    . HOH   F 5 .   ? 30.827 0.785   19.107  1.00 39.70 ?  493 HOH   A O    1 
HETATM 6956 O  O    . HOH   F 5 .   ? 40.948 -3.981  -0.350  1.00 38.46 ?  494 HOH   A O    1 
HETATM 6957 O  O    . HOH   F 5 .   ? 16.785 -20.490 16.184  1.00 27.93 ?  495 HOH   A O    1 
HETATM 6958 O  O    B HOH   F 5 .   ? 10.645 -1.488  -5.091  0.38 15.95 ?  496 HOH   A O    1 
HETATM 6959 O  O    . HOH   F 5 .   ? 23.222 -12.810 19.345  1.00 48.68 ?  497 HOH   A O    1 
HETATM 6960 O  O    . HOH   F 5 .   ? 15.843 -7.042  -11.816 1.00 44.99 ?  498 HOH   A O    1 
HETATM 6961 O  O    . HOH   F 5 .   ? 28.551 -4.709  -12.300 1.00 37.60 ?  499 HOH   A O    1 
HETATM 6962 O  O    . HOH   F 5 .   ? 20.493 -15.944 -7.370  1.00 28.02 ?  500 HOH   A O    1 
HETATM 6963 O  O    . HOH   F 5 .   ? 41.726 9.419   -3.923  1.00 31.92 ?  501 HOH   A O    1 
HETATM 6964 O  O    B HOH   F 5 .   ? 11.383 8.864   7.623   0.38 29.80 ?  502 HOH   A O    1 
HETATM 6965 O  O    . HOH   F 5 .   ? 39.163 2.437   7.470   1.00 33.12 ?  503 HOH   A O    1 
HETATM 6966 O  O    . HOH   F 5 .   ? 44.518 10.464  -1.607  1.00 28.52 ?  504 HOH   A O    1 
HETATM 6967 O  O    . HOH   F 5 .   ? 28.690 -7.935  -15.261 1.00 46.76 ?  505 HOH   A O    1 
HETATM 6968 O  O    . HOH   F 5 .   ? 31.452 -0.612  -10.568 1.00 28.22 ?  506 HOH   A O    1 
HETATM 6969 O  O    . HOH   F 5 .   ? 18.381 -23.221 1.957   1.00 40.76 ?  507 HOH   A O    1 
HETATM 6970 O  O    . HOH   F 5 .   ? 40.603 -0.249  -7.753  1.00 33.79 ?  508 HOH   A O    1 
HETATM 6971 O  O    . HOH   F 5 .   ? 13.877 -25.210 8.924   1.00 31.41 ?  509 HOH   A O    1 
HETATM 6972 O  O    . HOH   F 5 .   ? 20.028 -22.304 4.217   1.00 27.19 ?  510 HOH   A O    1 
HETATM 6973 O  O    B HOH   F 5 .   ? 9.712  1.013   -5.022  0.38 17.46 ?  511 HOH   A O    1 
HETATM 6974 O  O    . HOH   F 5 .   ? 16.167 -23.353 5.724   1.00 27.11 ?  512 HOH   A O    1 
HETATM 6975 O  O    . HOH   F 5 .   ? 30.668 5.864   -14.727 1.00 33.53 ?  513 HOH   A O    1 
HETATM 6976 O  O    . HOH   F 5 .   ? 8.213  -3.141  -5.761  1.00 42.70 ?  514 HOH   A O    1 
HETATM 6977 O  O    . HOH   F 5 .   ? 30.753 -5.861  -11.856 1.00 46.02 ?  515 HOH   A O    1 
HETATM 6978 O  O    . HOH   F 5 .   ? 37.364 -6.629  7.581   1.00 25.10 ?  516 HOH   A O    1 
HETATM 6979 O  O    . HOH   F 5 .   ? 23.139 -23.764 1.627   1.00 29.93 ?  517 HOH   A O    1 
HETATM 6980 O  O    . HOH   F 5 .   ? 39.486 -0.015  6.584   1.00 29.94 ?  518 HOH   A O    1 
HETATM 6981 O  O    B HOH   F 5 .   ? 14.665 8.129   4.814   0.38 17.69 ?  519 HOH   A O    1 
HETATM 6982 O  O    . HOH   F 5 .   ? 28.986 14.418  0.864   1.00 50.43 ?  520 HOH   A O    1 
HETATM 6983 O  O    . HOH   F 5 .   ? 38.020 13.953  6.707   1.00 43.07 ?  521 HOH   A O    1 
HETATM 6984 O  O    . HOH   F 5 .   ? 21.975 -24.011 4.490   1.00 26.21 ?  522 HOH   A O    1 
HETATM 6985 O  O    . HOH   F 5 .   ? 36.446 -6.535  10.195  1.00 44.66 ?  523 HOH   A O    1 
HETATM 6986 O  O    . HOH   F 5 .   ? 17.287 -6.595  -14.108 1.00 40.45 ?  524 HOH   A O    1 
HETATM 6987 O  O    T HOH   F 5 .   ? 11.897 -2.126  -3.647  0.30 13.75 ?  525 HOH   A O    1 
HETATM 6988 O  O    A HOH   F 5 .   ? 14.834 8.678   4.888   0.62 43.46 ?  526 HOH   A O    1 
HETATM 6989 O  O    . HOH   F 5 .   ? 24.074 9.065   -7.211  1.00 36.18 ?  527 HOH   A O    1 
HETATM 6990 O  O    . HOH   F 5 .   ? 15.790 -12.193 27.414  1.00 49.63 ?  528 HOH   A O    1 
HETATM 6991 O  O    . HOH   F 5 .   ? 16.324 -21.109 18.774  1.00 41.33 ?  529 HOH   A O    1 
HETATM 6992 O  O    B HOH   F 5 .   ? 8.013  7.286   2.427   0.38 23.14 ?  530 HOH   A O    1 
HETATM 6993 O  O    . HOH   F 5 .   ? 14.765 -22.794 19.804  1.00 33.60 ?  531 HOH   A O    1 
HETATM 6994 O  O    . HOH   G 5 .   ? 29.803 -22.431 5.515   1.00 19.62 ?  201 HOH   B O    1 
HETATM 6995 O  O    . HOH   G 5 .   ? 41.734 -35.974 -17.187 1.00 31.26 ?  202 HOH   B O    1 
HETATM 6996 O  O    . HOH   G 5 .   ? 52.897 -13.452 -20.242 1.00 33.23 ?  203 HOH   B O    1 
HETATM 6997 O  O    . HOH   G 5 .   ? 59.157 -18.708 6.823   1.00 38.10 ?  204 HOH   B O    1 
HETATM 6998 O  O    . HOH   G 5 .   ? 49.346 -22.687 -19.738 1.00 45.74 ?  205 HOH   B O    1 
HETATM 6999 O  O    . HOH   G 5 .   ? 27.854 -41.836 -15.083 1.00 37.25 ?  206 HOH   B O    1 
HETATM 7000 O  O    . HOH   G 5 .   ? 27.692 -29.180 -1.777  1.00 36.82 ?  207 HOH   B O    1 
HETATM 7001 O  O    . HOH   G 5 .   ? 48.050 -6.945  15.542  1.00 32.37 ?  208 HOH   B O    1 
HETATM 7002 O  O    . HOH   G 5 .   ? 50.184 -3.340  7.185   1.00 36.84 ?  209 HOH   B O    1 
HETATM 7003 O  O    . HOH   G 5 .   ? 29.881 -26.298 4.071   1.00 26.31 ?  210 HOH   B O    1 
HETATM 7004 O  O    . HOH   G 5 .   ? 30.206 -40.999 -8.056  1.00 16.55 ?  211 HOH   B O    1 
HETATM 7005 O  O    . HOH   G 5 .   ? 55.375 -16.570 -14.318 1.00 35.56 ?  212 HOH   B O    1 
HETATM 7006 O  O    . HOH   G 5 .   ? 47.400 -7.358  -3.904  1.00 39.48 ?  213 HOH   B O    1 
HETATM 7007 O  O    . HOH   G 5 .   ? 44.428 -7.259  2.075   1.00 32.63 ?  214 HOH   B O    1 
HETATM 7008 O  O    . HOH   G 5 .   ? 38.032 -39.437 -0.180  1.00 40.97 ?  215 HOH   B O    1 
HETATM 7009 O  O    . HOH   G 5 .   ? 41.334 -7.758  5.488   1.00 39.16 ?  216 HOH   B O    1 
HETATM 7010 O  O    . HOH   G 5 .   ? 54.471 -9.363  -8.730  1.00 18.39 ?  217 HOH   B O    1 
HETATM 7011 O  O    . HOH   G 5 .   ? 58.210 -12.929 8.427   1.00 30.81 ?  218 HOH   B O    1 
HETATM 7012 O  O    . HOH   G 5 .   ? 50.785 -6.120  0.131   1.00 26.13 ?  219 HOH   B O    1 
HETATM 7013 O  O    . HOH   G 5 .   ? 57.701 -24.435 5.031   1.00 32.97 ?  220 HOH   B O    1 
HETATM 7014 O  O    . HOH   G 5 .   ? 56.316 -19.746 7.366   1.00 32.39 ?  221 HOH   B O    1 
HETATM 7015 O  O    . HOH   G 5 .   ? 57.128 -26.851 -7.665  1.00 41.35 ?  222 HOH   B O    1 
HETATM 7016 O  O    . HOH   G 5 .   ? 30.898 -28.778 4.334   1.00 27.25 ?  223 HOH   B O    1 
HETATM 7017 O  O    . HOH   G 5 .   ? 56.668 -30.750 -7.740  1.00 31.06 ?  224 HOH   B O    1 
HETATM 7018 O  O    . HOH   G 5 .   ? 48.524 -36.482 -15.477 1.00 46.59 ?  225 HOH   B O    1 
HETATM 7019 O  O    . HOH   G 5 .   ? 35.998 -43.287 -8.478  1.00 35.16 ?  226 HOH   B O    1 
HETATM 7020 O  O    . HOH   G 5 .   ? 34.890 -24.684 13.852  1.00 33.35 ?  227 HOH   B O    1 
HETATM 7021 O  O    . HOH   G 5 .   ? 34.539 -36.375 -7.152  1.00 17.85 ?  228 HOH   B O    1 
HETATM 7022 O  O    . HOH   G 5 .   ? 41.491 -39.152 -14.868 1.00 22.67 ?  229 HOH   B O    1 
HETATM 7023 O  O    . HOH   G 5 .   ? 57.364 -16.273 -12.203 1.00 18.44 ?  230 HOH   B O    1 
HETATM 7024 O  O    . HOH   G 5 .   ? 37.052 -19.785 -18.056 1.00 36.38 ?  231 HOH   B O    1 
HETATM 7025 O  O    . HOH   G 5 .   ? 51.639 -6.472  4.402   1.00 18.69 ?  232 HOH   B O    1 
HETATM 7026 O  O    . HOH   G 5 .   ? 44.958 -43.520 -10.545 1.00 27.02 ?  233 HOH   B O    1 
HETATM 7027 O  O    . HOH   G 5 .   ? 29.776 -34.197 -0.427  1.00 33.28 ?  234 HOH   B O    1 
HETATM 7028 O  O    . HOH   G 5 .   ? 32.798 -43.777 -11.281 1.00 20.09 ?  235 HOH   B O    1 
HETATM 7029 O  O    . HOH   G 5 .   ? 45.155 -34.988 6.841   1.00 42.67 ?  236 HOH   B O    1 
HETATM 7030 O  O    . HOH   G 5 .   ? 39.287 -10.910 6.154   1.00 24.17 ?  237 HOH   B O    1 
HETATM 7031 O  O    . HOH   G 5 .   ? 40.607 -16.063 14.134  1.00 22.99 ?  238 HOH   B O    1 
HETATM 7032 O  O    . HOH   G 5 .   ? 44.467 -27.765 -0.679  1.00 21.42 ?  239 HOH   B O    1 
HETATM 7033 O  O    . HOH   G 5 .   ? 50.711 -12.975 -0.464  1.00 11.37 ?  240 HOH   B O    1 
HETATM 7034 O  O    . HOH   G 5 .   ? 25.410 -25.945 -1.287  1.00 32.10 ?  241 HOH   B O    1 
HETATM 7035 O  O    . HOH   G 5 .   ? 41.358 -9.635  13.104  1.00 21.63 ?  242 HOH   B O    1 
HETATM 7036 O  O    . HOH   G 5 .   ? 46.373 -1.551  13.232  1.00 27.45 ?  243 HOH   B O    1 
HETATM 7037 O  O    . HOH   G 5 .   ? 28.353 -19.671 -13.058 1.00 22.94 ?  244 HOH   B O    1 
HETATM 7038 O  O    . HOH   G 5 .   ? 42.551 -25.367 2.652   1.00 14.42 ?  245 HOH   B O    1 
HETATM 7039 O  O    . HOH   G 5 .   ? 35.103 -8.003  -2.981  1.00 17.86 ?  246 HOH   B O    1 
HETATM 7040 O  O    . HOH   G 5 .   ? 43.055 -43.234 -8.235  1.00 28.85 ?  247 HOH   B O    1 
HETATM 7041 O  O    . HOH   G 5 .   ? 43.155 -32.394 -17.030 1.00 23.51 ?  248 HOH   B O    1 
HETATM 7042 O  O    . HOH   G 5 .   ? 42.625 -22.870 3.874   1.00 11.26 ?  249 HOH   B O    1 
HETATM 7043 O  O    . HOH   G 5 .   ? 39.475 -11.103 0.367   1.00 15.84 ?  250 HOH   B O    1 
HETATM 7044 O  O    . HOH   G 5 .   ? 34.203 -18.496 11.440  1.00 24.18 ?  251 HOH   B O    1 
HETATM 7045 O  O    . HOH   G 5 .   ? 38.919 -11.974 12.349  1.00 32.86 ?  252 HOH   B O    1 
HETATM 7046 O  O    . HOH   G 5 .   ? 57.583 -24.380 -3.820  1.00 20.95 ?  253 HOH   B O    1 
HETATM 7047 O  O    . HOH   G 5 .   ? 41.854 -23.526 9.320   1.00 17.53 ?  254 HOH   B O    1 
HETATM 7048 O  O    . HOH   G 5 .   ? 51.559 -13.854 11.048  1.00 27.75 ?  255 HOH   B O    1 
HETATM 7049 O  O    . HOH   G 5 .   ? 50.961 -39.918 -8.214  1.00 36.17 ?  256 HOH   B O    1 
HETATM 7050 O  O    . HOH   G 5 .   ? 38.475 -11.040 -2.225  1.00 17.55 ?  257 HOH   B O    1 
HETATM 7051 O  O    . HOH   G 5 .   ? 27.116 -31.839 -9.900  1.00 19.01 ?  258 HOH   B O    1 
HETATM 7052 O  O    . HOH   G 5 .   ? 58.152 -10.651 -4.055  1.00 19.69 ?  259 HOH   B O    1 
HETATM 7053 O  O    . HOH   G 5 .   ? 40.300 -12.745 -11.483 1.00 14.60 ?  260 HOH   B O    1 
HETATM 7054 O  O    . HOH   G 5 .   ? 47.955 -24.494 -17.772 1.00 31.12 ?  261 HOH   B O    1 
HETATM 7055 O  O    . HOH   G 5 .   ? 29.698 -25.225 -10.780 1.00 16.32 ?  262 HOH   B O    1 
HETATM 7056 O  O    . HOH   G 5 .   ? 31.779 -17.904 -14.463 1.00 31.10 ?  263 HOH   B O    1 
HETATM 7057 O  O    . HOH   G 5 .   ? 30.845 -15.728 2.702   1.00 13.32 ?  264 HOH   B O    1 
HETATM 7058 O  O    . HOH   G 5 .   ? 48.005 -22.778 5.848   1.00 16.60 ?  265 HOH   B O    1 
HETATM 7059 O  O    . HOH   G 5 .   ? 34.902 -33.355 -19.104 1.00 34.68 ?  266 HOH   B O    1 
HETATM 7060 O  O    . HOH   G 5 .   ? 43.327 -15.782 -12.140 1.00 13.48 ?  267 HOH   B O    1 
HETATM 7061 O  O    . HOH   G 5 .   ? 28.451 -30.884 -14.727 1.00 31.70 ?  268 HOH   B O    1 
HETATM 7062 O  O    . HOH   G 5 .   ? 56.140 -23.500 -14.689 1.00 26.10 ?  269 HOH   B O    1 
HETATM 7063 O  O    . HOH   G 5 .   ? 28.267 -34.354 -9.390  1.00 17.03 ?  270 HOH   B O    1 
HETATM 7064 O  O    . HOH   G 5 .   ? 57.473 -9.222  1.436   1.00 19.07 ?  271 HOH   B O    1 
HETATM 7065 O  O    . HOH   G 5 .   ? 49.305 -28.696 -6.866  1.00 14.88 ?  272 HOH   B O    1 
HETATM 7066 O  O    . HOH   G 5 .   ? 56.928 -8.638  8.447   1.00 18.36 ?  273 HOH   B O    1 
HETATM 7067 O  O    . HOH   G 5 .   ? 42.300 -9.921  9.397   1.00 20.15 ?  274 HOH   B O    1 
HETATM 7068 O  O    . HOH   G 5 .   ? 27.579 -26.687 -15.608 1.00 32.33 ?  275 HOH   B O    1 
HETATM 7069 O  O    . HOH   G 5 .   ? 46.875 -29.560 9.824   1.00 31.81 ?  276 HOH   B O    1 
HETATM 7070 O  O    . HOH   G 5 .   ? 27.938 -22.895 -7.958  1.00 16.96 ?  277 HOH   B O    1 
HETATM 7071 O  O    . HOH   G 5 .   ? 59.785 -15.304 8.142   1.00 33.09 ?  278 HOH   B O    1 
HETATM 7072 O  O    . HOH   G 5 .   ? 42.376 -34.707 3.787   1.00 25.58 ?  279 HOH   B O    1 
HETATM 7073 O  O    . HOH   G 5 .   ? 49.706 -0.456  10.181  1.00 30.86 ?  280 HOH   B O    1 
HETATM 7074 O  O    . HOH   G 5 .   ? 34.438 -12.785 2.632   1.00 22.26 ?  281 HOH   B O    1 
HETATM 7075 O  O    . HOH   G 5 .   ? 42.851 -20.268 -20.726 1.00 35.79 ?  282 HOH   B O    1 
HETATM 7076 O  O    . HOH   G 5 .   ? 46.587 -31.255 -4.749  1.00 23.62 ?  283 HOH   B O    1 
HETATM 7077 O  O    . HOH   G 5 .   ? 41.128 -5.537  11.574  1.00 45.54 ?  284 HOH   B O    1 
HETATM 7078 O  O    . HOH   G 5 .   ? 30.514 -42.255 -10.525 1.00 28.42 ?  285 HOH   B O    1 
HETATM 7079 O  O    . HOH   G 5 .   ? 57.118 -12.064 12.351  1.00 36.49 ?  286 HOH   B O    1 
HETATM 7080 O  O    . HOH   G 5 .   ? 48.397 -25.054 3.134   1.00 13.02 ?  287 HOH   B O    1 
HETATM 7081 O  O    . HOH   G 5 .   ? 48.692 -20.033 5.949   1.00 13.38 ?  288 HOH   B O    1 
HETATM 7082 O  O    . HOH   G 5 .   ? 33.471 -15.311 -13.910 1.00 20.21 ?  289 HOH   B O    1 
HETATM 7083 O  O    . HOH   G 5 .   ? 47.059 -33.962 -4.607  1.00 17.27 ?  290 HOH   B O    1 
HETATM 7084 O  O    . HOH   G 5 .   ? 51.209 -37.581 -9.569  1.00 26.04 ?  291 HOH   B O    1 
HETATM 7085 O  O    . HOH   G 5 .   ? 42.262 -9.957  -14.865 1.00 39.85 ?  292 HOH   B O    1 
HETATM 7086 O  O    . HOH   G 5 .   ? 52.520 -10.382 13.025  1.00 21.44 ?  293 HOH   B O    1 
HETATM 7087 O  O    . HOH   G 5 .   ? 45.316 -33.364 -15.926 1.00 23.34 ?  294 HOH   B O    1 
HETATM 7088 O  O    . HOH   G 5 .   ? 36.789 -12.762 -1.455  1.00 25.74 ?  295 HOH   B O    1 
HETATM 7089 O  O    . HOH   G 5 .   ? 37.428 -18.163 13.117  1.00 29.51 ?  296 HOH   B O    1 
HETATM 7090 O  O    . HOH   G 5 .   ? 51.679 -5.982  -7.937  1.00 48.50 ?  297 HOH   B O    1 
HETATM 7091 O  O    . HOH   G 5 .   ? 44.602 -27.452 2.033   1.00 14.74 ?  298 HOH   B O    1 
HETATM 7092 O  O    . HOH   G 5 .   ? 45.876 -40.361 -3.530  1.00 28.77 ?  299 HOH   B O    1 
HETATM 7093 O  O    . HOH   G 5 .   ? 43.989 -29.349 -4.676  1.00 22.54 ?  300 HOH   B O    1 
HETATM 7094 O  O    . HOH   G 5 .   ? 57.673 -22.084 3.094   1.00 26.81 ?  301 HOH   B O    1 
HETATM 7095 O  O    . HOH   G 5 .   ? 40.214 -10.834 -9.510  1.00 16.45 ?  302 HOH   B O    1 
HETATM 7096 O  O    . HOH   G 5 .   ? 50.051 -24.571 5.879   1.00 32.95 ?  303 HOH   B O    1 
HETATM 7097 O  O    . HOH   G 5 .   ? 35.061 -33.556 4.581   1.00 27.88 ?  304 HOH   B O    1 
HETATM 7098 O  O    . HOH   G 5 .   ? 52.599 -35.636 -8.605  1.00 29.71 ?  305 HOH   B O    1 
HETATM 7099 O  O    . HOH   G 5 .   ? 52.983 -15.996 -12.724 1.00 26.47 ?  306 HOH   B O    1 
HETATM 7100 O  O    . HOH   G 5 .   ? 52.462 -29.231 -13.030 1.00 24.11 ?  307 HOH   B O    1 
HETATM 7101 O  O    . HOH   G 5 .   ? 25.921 -21.477 -3.466  1.00 15.60 ?  308 HOH   B O    1 
HETATM 7102 O  O    . HOH   G 5 .   ? 53.469 -30.186 4.524   1.00 18.44 ?  309 HOH   B O    1 
HETATM 7103 O  O    . HOH   G 5 .   ? 42.648 -12.289 -18.500 1.00 29.45 ?  310 HOH   B O    1 
HETATM 7104 O  O    . HOH   G 5 .   ? 37.294 -35.668 7.260   1.00 33.18 ?  311 HOH   B O    1 
HETATM 7105 O  O    . HOH   G 5 .   ? 32.802 -34.586 -5.865  1.00 16.64 ?  312 HOH   B O    1 
HETATM 7106 O  O    . HOH   G 5 .   ? 53.620 -12.567 -22.139 1.00 35.34 ?  313 HOH   B O    1 
HETATM 7107 O  O    . HOH   G 5 .   ? 62.706 -13.582 4.787   1.00 27.53 ?  314 HOH   B O    1 
HETATM 7108 O  O    . HOH   G 5 .   ? 37.133 -30.533 -20.979 1.00 29.33 ?  315 HOH   B O    1 
HETATM 7109 O  O    . HOH   G 5 .   ? 37.833 -10.241 -10.710 1.00 16.31 ?  316 HOH   B O    1 
HETATM 7110 O  O    . HOH   G 5 .   ? 51.373 -32.991 -10.766 1.00 40.55 ?  317 HOH   B O    1 
HETATM 7111 O  O    . HOH   G 5 .   ? 41.716 -8.071  1.413   1.00 22.96 ?  318 HOH   B O    1 
HETATM 7112 O  O    . HOH   G 5 .   ? 26.329 -21.039 -6.206  1.00 15.88 ?  319 HOH   B O    1 
HETATM 7113 O  O    . HOH   G 5 .   ? 59.932 -17.165 -10.446 1.00 33.41 ?  320 HOH   B O    1 
HETATM 7114 O  O    . HOH   G 5 .   ? 43.198 -21.451 10.705  1.00 15.67 ?  321 HOH   B O    1 
HETATM 7115 O  O    . HOH   G 5 .   ? 38.315 -12.731 7.957   1.00 18.05 ?  322 HOH   B O    1 
HETATM 7116 O  O    . HOH   G 5 .   ? 43.466 -15.376 18.155  1.00 28.58 ?  323 HOH   B O    1 
HETATM 7117 O  O    . HOH   G 5 .   ? 48.053 -32.651 -16.635 1.00 41.31 ?  324 HOH   B O    1 
HETATM 7118 O  O    . HOH   G 5 .   ? 44.613 -24.608 9.583   1.00 19.72 ?  325 HOH   B O    1 
HETATM 7119 O  O    . HOH   G 5 .   ? 62.869 -20.133 -0.770  1.00 37.98 ?  326 HOH   B O    1 
HETATM 7120 O  O    . HOH   G 5 .   ? 36.709 -12.418 4.336   1.00 17.22 ?  327 HOH   B O    1 
HETATM 7121 O  O    . HOH   G 5 .   ? 45.681 -36.264 -16.104 1.00 34.43 ?  328 HOH   B O    1 
HETATM 7122 O  O    . HOH   G 5 .   ? 43.111 -34.597 0.122   1.00 19.95 ?  329 HOH   B O    1 
HETATM 7123 O  O    . HOH   G 5 .   ? 44.171 -1.748  7.648   1.00 47.45 ?  330 HOH   B O    1 
HETATM 7124 O  O    . HOH   G 5 .   ? 27.754 -14.774 -9.439  1.00 35.16 ?  331 HOH   B O    1 
HETATM 7125 O  O    . HOH   G 5 .   ? 38.349 -9.358  -13.253 1.00 25.61 ?  332 HOH   B O    1 
HETATM 7126 O  O    . HOH   G 5 .   ? 47.202 -24.499 8.188   1.00 24.89 ?  333 HOH   B O    1 
HETATM 7127 O  O    . HOH   G 5 .   ? 41.184 -24.492 15.859  1.00 43.46 ?  334 HOH   B O    1 
HETATM 7128 O  O    . HOH   G 5 .   ? 42.804 -43.499 -14.281 1.00 45.21 ?  335 HOH   B O    1 
HETATM 7129 O  O    . HOH   G 5 .   ? 33.611 -31.216 11.106  1.00 33.94 ?  336 HOH   B O    1 
HETATM 7130 O  O    . HOH   G 5 .   ? 48.544 -11.966 -13.988 1.00 26.51 ?  337 HOH   B O    1 
HETATM 7131 O  O    . HOH   G 5 .   ? 36.971 -15.143 -16.510 1.00 41.75 ?  338 HOH   B O    1 
HETATM 7132 O  O    . HOH   G 5 .   ? 47.458 -27.420 2.052   1.00 14.62 ?  339 HOH   B O    1 
HETATM 7133 O  O    . HOH   G 5 .   ? 46.813 -19.904 12.283  1.00 27.52 ?  340 HOH   B O    1 
HETATM 7134 O  O    . HOH   G 5 .   ? 39.472 -23.613 -20.306 1.00 36.71 ?  341 HOH   B O    1 
HETATM 7135 O  O    . HOH   G 5 .   ? 38.385 -12.258 -16.248 1.00 44.36 ?  342 HOH   B O    1 
HETATM 7136 O  O    . HOH   G 5 .   ? 28.862 -42.939 -12.337 1.00 37.98 ?  343 HOH   B O    1 
HETATM 7137 O  O    . HOH   G 5 .   ? 37.024 -45.240 -9.724  1.00 34.90 ?  344 HOH   B O    1 
HETATM 7138 O  O    . HOH   G 5 .   ? 32.994 -14.691 1.072   1.00 18.35 ?  345 HOH   B O    1 
HETATM 7139 O  O    . HOH   G 5 .   ? 38.572 -22.389 15.054  1.00 38.60 ?  346 HOH   B O    1 
HETATM 7140 O  O    . HOH   G 5 .   ? 39.790 -44.283 -11.165 1.00 41.73 ?  347 HOH   B O    1 
HETATM 7141 O  O    . HOH   G 5 .   ? 40.433 -43.478 -9.075  1.00 26.55 ?  348 HOH   B O    1 
HETATM 7142 O  O    . HOH   G 5 .   ? 33.697 -9.462  -8.788  1.00 31.95 ?  349 HOH   B O    1 
HETATM 7143 O  O    . HOH   G 5 .   ? 27.749 -26.600 -0.551  1.00 31.37 ?  350 HOH   B O    1 
HETATM 7144 O  O    . HOH   G 5 .   ? 62.524 -20.079 -4.800  1.00 45.23 ?  351 HOH   B O    1 
HETATM 7145 O  O    . HOH   G 5 .   ? 44.144 -37.318 -17.756 1.00 33.37 ?  352 HOH   B O    1 
HETATM 7146 O  O    . HOH   G 5 .   ? 34.561 -10.315 7.629   1.00 23.85 ?  353 HOH   B O    1 
HETATM 7147 O  O    . HOH   G 5 .   ? 55.655 -8.274  10.800  1.00 26.82 ?  354 HOH   B O    1 
HETATM 7148 O  O    . HOH   G 5 .   ? 56.592 -7.277  3.116   1.00 25.20 ?  355 HOH   B O    1 
HETATM 7149 O  O    . HOH   G 5 .   ? 36.035 -8.541  -9.702  1.00 33.11 ?  356 HOH   B O    1 
HETATM 7150 O  O    . HOH   G 5 .   ? 23.136 -23.627 6.895   1.00 31.30 ?  357 HOH   B O    1 
HETATM 7151 O  O    . HOH   G 5 .   ? 43.126 -12.676 -21.168 1.00 39.28 ?  358 HOH   B O    1 
HETATM 7152 O  O    . HOH   G 5 .   ? 34.129 -7.716  11.437  1.00 40.11 ?  359 HOH   B O    1 
HETATM 7153 O  O    . HOH   G 5 .   ? 61.478 -19.924 1.669   1.00 34.13 ?  360 HOH   B O    1 
HETATM 7154 O  O    . HOH   G 5 .   ? 56.899 -21.545 -16.328 1.00 40.05 ?  361 HOH   B O    1 
HETATM 7155 O  O    . HOH   G 5 .   ? 40.212 -8.841  9.920   1.00 34.92 ?  362 HOH   B O    1 
HETATM 7156 O  O    . HOH   G 5 .   ? 27.157 -25.966 -11.372 1.00 32.78 ?  363 HOH   B O    1 
HETATM 7157 O  O    . HOH   G 5 .   ? 58.827 -10.472 9.240   1.00 38.15 ?  364 HOH   B O    1 
HETATM 7158 O  O    . HOH   G 5 .   ? 32.504 -23.619 14.097  1.00 39.81 ?  365 HOH   B O    1 
HETATM 7159 O  O    . HOH   G 5 .   ? 54.199 -5.749  2.985   1.00 36.11 ?  366 HOH   B O    1 
HETATM 7160 O  O    . HOH   G 5 .   ? 48.386 -26.491 8.866   1.00 40.00 ?  367 HOH   B O    1 
HETATM 7161 O  O    . HOH   G 5 .   ? 39.849 -7.012  7.847   1.00 40.35 ?  368 HOH   B O    1 
HETATM 7162 O  O    . HOH   G 5 .   ? 36.151 -8.662  8.945   1.00 39.07 ?  369 HOH   B O    1 
HETATM 7163 O  O    . HOH   G 5 .   ? 40.024 -11.365 -13.958 1.00 29.64 ?  370 HOH   B O    1 
HETATM 7164 O  O    . HOH   G 5 .   ? 41.845 -10.025 -17.474 1.00 53.19 ?  371 HOH   B O    1 
HETATM 7165 O  O    . HOH   G 5 .   ? 56.045 -7.806  -0.597  1.00 34.56 ?  372 HOH   B O    1 
HETATM 7166 O  O    . HOH   G 5 .   ? 63.001 -12.390 6.931   1.00 38.61 ?  373 HOH   B O    1 
HETATM 7167 O  O    . HOH   G 5 .   ? 52.043 -12.899 13.389  1.00 30.00 ?  374 HOH   B O    1 
HETATM 7168 O  O    . HOH   G 5 .   ? 41.834 -6.740  -4.821  1.00 45.69 ?  375 HOH   B O    1 
HETATM 7169 O  O    . HOH   G 5 .   ? 38.009 -10.559 10.083  1.00 29.05 ?  376 HOH   B O    1 
HETATM 7170 O  O    . HOH   G 5 .   ? 36.498 -22.865 13.310  1.00 25.75 ?  377 HOH   B O    1 
HETATM 7171 O  O    . HOH   G 5 .   ? 42.659 -17.066 -23.143 1.00 42.42 ?  378 HOH   B O    1 
HETATM 7172 O  O    . HOH   G 5 .   ? 44.033 -5.616  -3.479  1.00 44.09 ?  379 HOH   B O    1 
HETATM 7173 O  O    . HOH   G 5 .   ? 40.116 -7.667  3.201   1.00 39.76 ?  380 HOH   B O    1 
HETATM 7174 O  O    . HOH   G 5 .   ? 52.838 -29.868 7.195   1.00 23.30 ?  381 HOH   B O    1 
HETATM 7175 O  O    . HOH   G 5 .   ? 39.667 -14.032 15.706  1.00 48.66 ?  382 HOH   B O    1 
HETATM 7176 O  O    . HOH   G 5 .   ? 60.477 -22.258 2.867   1.00 47.21 ?  383 HOH   B O    1 
HETATM 7177 O  O    . HOH   G 5 .   ? 46.731 -5.373  2.883   1.00 36.30 ?  384 HOH   B O    1 
HETATM 7178 O  O    . HOH   G 5 .   ? 25.903 -18.843 -11.858 1.00 38.58 ?  385 HOH   B O    1 
HETATM 7179 O  O    . HOH   G 5 .   ? 40.980 -9.794  15.803  1.00 43.45 ?  386 HOH   B O    1 
HETATM 7180 O  O    . HOH   G 5 .   ? 35.393 -33.728 7.353   1.00 39.90 ?  387 HOH   B O    1 
HETATM 7181 O  O    . HOH   G 5 .   ? 23.930 -20.924 -7.628  1.00 26.81 ?  388 HOH   B O    1 
HETATM 7182 O  O    . HOH   G 5 .   ? 35.312 -20.374 13.332  1.00 29.53 ?  389 HOH   B O    1 
HETATM 7183 O  O    . HOH   G 5 .   ? 40.703 -6.638  -0.809  1.00 25.35 ?  390 HOH   B O    1 
HETATM 7184 O  O    . HOH   G 5 .   ? 44.061 -31.735 -3.803  1.00 35.52 ?  391 HOH   B O    1 
HETATM 7185 O  O    . HOH   G 5 .   ? 27.911 -27.089 2.272   1.00 29.54 ?  392 HOH   B O    1 
HETATM 7186 O  O    . HOH   G 5 .   ? 26.599 -27.980 -13.457 1.00 36.37 ?  393 HOH   B O    1 
HETATM 7187 O  O    . HOH   G 5 .   ? 34.367 -33.449 9.668   1.00 35.65 ?  394 HOH   B O    1 
HETATM 7188 O  O    . HOH   G 5 .   ? 24.609 -20.657 -10.466 1.00 35.69 ?  395 HOH   B O    1 
HETATM 7189 O  O    . HOH   G 5 .   ? 50.612 -30.822 8.722   1.00 27.91 ?  396 HOH   B O    1 
HETATM 7190 O  O    . HOH   G 5 .   ? 26.839 -30.673 -12.595 1.00 28.12 ?  397 HOH   B O    1 
HETATM 7191 O  O    . HOH   G 5 .   ? 57.649 -6.570  -2.333  1.00 34.55 ?  398 HOH   B O    1 
HETATM 7192 O  O    . HOH   G 5 .   ? 45.731 -20.164 15.251  1.00 47.87 ?  399 HOH   B O    1 
HETATM 7193 O  O    . HOH   G 5 .   ? 40.906 -11.788 -22.290 1.00 39.08 ?  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   A VAL   A 3   ? 0.6420 0.6543 0.7136 0.0042  -0.0363 0.1000  3   VAL   A N   
2    N  N   B VAL   A 3   ? 0.6413 0.6523 0.7001 0.0002  -0.0314 0.0824  3   VAL   A N   
3    C  CA  A VAL   A 3   ? 0.6394 0.6519 0.7048 0.0025  -0.0350 0.0997  3   VAL   A CA  
4    C  CA  B VAL   A 3   ? 0.6387 0.6500 0.6927 -0.0011 -0.0308 0.0834  3   VAL   A CA  
5    C  C   A VAL   A 3   ? 0.6246 0.6398 0.6774 -0.0053 -0.0354 0.0996  3   VAL   A C   
6    C  C   B VAL   A 3   ? 0.6245 0.6386 0.6707 -0.0073 -0.0330 0.0905  3   VAL   A C   
7    O  O   A VAL   A 3   ? 0.6272 0.6427 0.6864 -0.0038 -0.0379 0.1016  3   VAL   A O   
8    O  O   B VAL   A 3   ? 0.6274 0.6413 0.6794 -0.0063 -0.0352 0.0914  3   VAL   A O   
9    C  CB  A VAL   A 3   ? 0.6489 0.6597 0.7177 0.0067  -0.0328 0.0993  3   VAL   A CB  
10   C  CB  B VAL   A 3   ? 0.6476 0.6572 0.7026 0.0023  -0.0279 0.0782  3   VAL   A CB  
11   C  CG1 A VAL   A 3   ? 0.6521 0.6622 0.7213 0.0082  -0.0322 0.0997  3   VAL   A CG1 
12   C  CG1 B VAL   A 3   ? 0.6506 0.6596 0.7053 0.0036  -0.0269 0.0767  3   VAL   A CG1 
13   C  CG2 A VAL   A 3   ? 0.6520 0.6623 0.7217 0.0081  -0.0321 0.0990  3   VAL   A CG2 
14   C  CG2 B VAL   A 3   ? 0.6505 0.6597 0.7057 0.0035  -0.0269 0.0763  3   VAL   A CG2 
31   N  N   . ASN   A 4   ? 0.6043 0.6220 0.6339 -0.0152 -0.0326 0.0966  4   ASN   A N   
32   C  CA  . ASN   A 4   ? 0.5606 0.5847 0.5464 -0.0343 -0.0286 0.0969  4   ASN   A CA  
33   C  C   . ASN   A 4   ? 0.5032 0.5394 0.4855 -0.0530 -0.0148 0.0604  4   ASN   A C   
34   O  O   . ASN   A 4   ? 0.5064 0.5423 0.4889 -0.0543 -0.0174 0.0632  4   ASN   A O   
35   C  CB  . ASN   A 4   ? 0.5714 0.5905 0.5097 -0.0350 -0.0375 0.1328  4   ASN   A CB  
36   C  CG  . ASN   A 4   ? 0.5787 0.5934 0.4765 -0.0363 -0.0454 0.1649  4   ASN   A CG  
37   O  OD1 . ASN   A 4   ? 0.5822 0.5936 0.4633 -0.0368 -0.0502 0.1774  4   ASN   A OD1 
38   N  ND2 . ASN   A 4   ? 0.5801 0.5941 0.4684 -0.0359 -0.0471 0.1783  4   ASN   A ND2 
46   N  N   A SER   A 5   ? 0.4691 0.5174 0.4455 -0.0640 -0.0068 0.0403  5   SER   A N   
47   N  N   B SER   A 5   ? 0.4740 0.5091 0.4526 -0.0602 -0.0055 0.0423  5   SER   A N   
48   C  CA  A SER   A 5   ? 0.4320 0.4934 0.4034 -0.0744 0.0043  0.0212  5   SER   A CA  
49   C  CA  B SER   A 5   ? 0.4422 0.4768 0.4163 -0.0670 0.0064  0.0256  5   SER   A CA  
50   C  C   A SER   A 5   ? 0.3884 0.4584 0.3562 -0.0830 0.0194  0.0116  5   SER   A C   
51   C  C   B SER   A 5   ? 0.4053 0.4369 0.3716 -0.0726 0.0215  0.0166  5   SER   A C   
52   O  O   A SER   A 5   ? 0.3935 0.4639 0.3591 -0.0765 0.0212  0.0038  5   SER   A O   
53   O  O   B SER   A 5   ? 0.4089 0.4404 0.3751 -0.0684 0.0224  0.0114  5   SER   A O   
54   C  CB  A SER   A 5   ? 0.4381 0.5020 0.4130 -0.0767 0.0035  0.0140  5   SER   A CB  
55   C  CB  B SER   A 5   ? 0.4464 0.4828 0.4264 -0.0685 0.0055  0.0201  5   SER   A CB  
56   O  OG  A SER   A 5   ? 0.4417 0.5065 0.4173 -0.0779 0.0036  0.0110  5   SER   A OG  
57   O  OG  B SER   A 5   ? 0.4487 0.4859 0.4305 -0.0693 0.0053  0.0177  5   SER   A OG  
68   N  N   A PHE   A 6   ? 0.3357 0.4156 0.2951 -0.0988 0.0359  0.0150  6   PHE   A N   
69   N  N   B PHE   A 6   ? 0.3621 0.3918 0.3163 -0.0837 0.0382  0.0165  6   PHE   A N   
70   C  CA  A PHE   A 6   ? 0.2870 0.3706 0.2391 -0.1094 0.0477  0.0251  6   PHE   A CA  
71   C  CA  B PHE   A 6   ? 0.3203 0.3451 0.2640 -0.0926 0.0537  0.0207  6   PHE   A CA  
72   C  C   A PHE   A 6   ? 0.2771 0.3598 0.2382 -0.1158 0.0607  0.0209  6   PHE   A C   
73   C  C   B PHE   A 6   ? 0.3084 0.3273 0.2531 -0.0956 0.0736  0.0188  6   PHE   A C   
74   O  O   A PHE   A 6   ? 0.2844 0.3668 0.2680 -0.1162 0.0598  0.0276  6   PHE   A O   
75   O  O   B PHE   A 6   ? 0.3113 0.3275 0.2599 -0.0967 0.0766  0.0299  6   PHE   A O   
76   C  CB  A PHE   A 6   ? 0.2591 0.3382 0.1985 -0.1023 0.0352  0.0358  6   PHE   A CB  
77   C  CB  B PHE   A 6   ? 0.2962 0.3193 0.2323 -0.0914 0.0405  0.0218  6   PHE   A CB  
78   C  CG  A PHE   A 6   ? 0.2353 0.3095 0.1713 -0.0940 0.0214  0.0410  6   PHE   A CG  
79   C  CG  B PHE   A 6   ? 0.2739 0.2959 0.2083 -0.0901 0.0276  0.0202  6   PHE   A CG  
80   C  CD1 A PHE   A 6   ? 0.2253 0.2967 0.1663 -0.0891 0.0126  0.0375  6   PHE   A CD1 
81   C  CD1 B PHE   A 6   ? 0.2640 0.2853 0.1987 -0.0895 0.0224  0.0187  6   PHE   A CD1 
82   C  CD2 A PHE   A 6   ? 0.2385 0.3028 0.1910 -0.0760 0.0134  0.0425  6   PHE   A CD2 
83   C  CD2 B PHE   A 6   ? 0.2706 0.2886 0.2157 -0.0828 0.0197  0.0169  6   PHE   A CD2 
84   C  CE1 A PHE   A 6   ? 0.2196 0.2911 0.1746 -0.0859 0.0159  0.0363  6   PHE   A CE1 
85   C  CE1 B PHE   A 6   ? 0.2581 0.2797 0.2018 -0.0889 0.0214  0.0155  6   PHE   A CE1 
86   C  CE2 A PHE   A 6   ? 0.2339 0.2977 0.1934 -0.0711 0.0107  0.0386  6   PHE   A CE2 
87   C  CE2 B PHE   A 6   ? 0.2643 0.2821 0.2145 -0.0824 0.0161  0.0133  6   PHE   A CE2 
88   C  CZ  A PHE   A 6   ? 0.2248 0.2917 0.1772 -0.0785 0.0125  0.0349  6   PHE   A CZ  
89   C  CZ  B PHE   A 6   ? 0.2589 0.2787 0.2038 -0.0860 0.0181  0.0121  6   PHE   A CZ  
108  N  N   A SER   A 7   ? 0.2622 0.3405 0.2104 -0.1141 0.0671  0.0074  7   SER   A N   
109  N  N   B SER   A 7   ? 0.2948 0.3085 0.2411 -0.0934 0.0809  0.0028  7   SER   A N   
110  C  CA  A SER   A 7   ? 0.2547 0.3254 0.2062 -0.1013 0.0611  -0.0158 7   SER   A CA  
111  C  CA  B SER   A 7   ? 0.2874 0.2953 0.2457 -0.0811 0.0796  -0.0138 7   SER   A CA  
112  C  C   A SER   A 7   ? 0.2333 0.2909 0.1758 -0.0939 0.0606  -0.0145 7   SER   A C   
113  C  C   B SER   A 7   ? 0.2722 0.2767 0.2310 -0.0675 0.0834  -0.0124 7   SER   A C   
114  O  O   A SER   A 7   ? 0.2464 0.2822 0.1779 -0.0990 0.0678  -0.0148 7   SER   A O   
115  O  O   B SER   A 7   ? 0.2785 0.2761 0.2288 -0.0661 0.0870  -0.0128 7   SER   A O   
116  C  CB  A SER   A 7   ? 0.2702 0.3425 0.2377 -0.0906 0.0621  -0.0218 7   SER   A CB  
117  C  CB  B SER   A 7   ? 0.2921 0.2988 0.2607 -0.0850 0.0742  -0.0266 7   SER   A CB  
118  O  OG  A SER   A 7   ? 0.2843 0.3527 0.2641 -0.0830 0.0570  -0.0266 7   SER   A OG  
119  O  OG  B SER   A 7   ? 0.2981 0.3030 0.2798 -0.0857 0.0634  -0.0350 7   SER   A OG  
130  N  N   A GLY   A 8   ? 0.2050 0.2647 0.1652 -0.0800 0.0440  -0.0183 8   GLY   A N   
131  N  N   B GLY   A 8   ? 0.2528 0.2618 0.2235 -0.0563 0.0780  -0.0084 8   GLY   A N   
132  C  CA  A GLY   A 8   ? 0.1880 0.2399 0.1682 -0.0553 0.0386  -0.0045 8   GLY   A CA  
133  C  CA  B GLY   A 8   ? 0.2320 0.2405 0.2062 -0.0487 0.0702  0.0013  8   GLY   A CA  
134  C  C   A GLY   A 8   ? 0.1663 0.2183 0.1679 -0.0319 0.0289  0.0035  8   GLY   A C   
135  C  C   B GLY   A 8   ? 0.2084 0.2208 0.1805 -0.0410 0.0597  0.0078  8   GLY   A C   
136  O  O   A GLY   A 8   ? 0.1664 0.2180 0.1711 -0.0131 0.0283  -0.0085 8   GLY   A O   
137  O  O   B GLY   A 8   ? 0.2096 0.2201 0.1840 -0.0377 0.0653  0.0045  8   GLY   A O   
144  N  N   A TYR   A 9   ? 0.1484 0.2021 0.1611 -0.0233 0.0269  0.0183  9   TYR   A N   
145  N  N   B TYR   A 9   ? 0.1819 0.2026 0.1576 -0.0331 0.0411  0.0181  9   TYR   A N   
146  C  CA  A TYR   A 9   ? 0.1367 0.1849 0.1541 -0.0240 0.0148  0.0194  9   TYR   A CA  
147  C  CA  B TYR   A 9   ? 0.1644 0.1833 0.1469 -0.0274 0.0239  0.0253  9   TYR   A CA  
148  C  C   A TYR   A 9   ? 0.1297 0.1656 0.1516 -0.0177 0.0131  0.0325  9   TYR   A C   
149  C  C   B TYR   A 9   ? 0.1562 0.1670 0.1476 -0.0236 0.0172  0.0384  9   TYR   A C   
150  O  O   A TYR   A 9   ? 0.1480 0.1841 0.1759 -0.0125 0.0060  0.0319  9   TYR   A O   
151  O  O   B TYR   A 9   ? 0.1599 0.1799 0.1637 -0.0255 0.0046  0.0509  9   TYR   A O   
152  C  CB  A TYR   A 9   ? 0.1341 0.1915 0.1606 -0.0239 0.0159  0.0071  9   TYR   A CB  
153  C  CB  B TYR   A 9   ? 0.1533 0.1829 0.1531 -0.0260 0.0243  0.0149  9   TYR   A CB  
154  C  CG  A TYR   A 9   ? 0.1378 0.1891 0.1729 -0.0161 0.0256  -0.0037 9   TYR   A CG  
155  C  CG  B TYR   A 9   ? 0.1460 0.1799 0.1507 -0.0204 0.0294  0.0076  9   TYR   A CG  
156  C  CD1 A TYR   A 9   ? 0.1455 0.1898 0.1832 -0.0172 0.0361  -0.0137 9   TYR   A CD1 
157  C  CD1 B TYR   A 9   ? 0.1531 0.1777 0.1608 -0.0201 0.0338  0.0032  9   TYR   A CD1 
158  C  CD2 A TYR   A 9   ? 0.1362 0.1855 0.1819 -0.0127 0.0194  0.0038  9   TYR   A CD2 
159  C  CD2 B TYR   A 9   ? 0.1413 0.1762 0.1422 -0.0111 0.0306  0.0083  9   TYR   A CD2 
160  C  CE1 A TYR   A 9   ? 0.1513 0.1906 0.1988 -0.0127 0.0341  -0.0224 9   TYR   A CE1 
161  C  CE1 B TYR   A 9   ? 0.1514 0.1718 0.1599 -0.0177 0.0372  -0.0007 9   TYR   A CE1 
162  C  CE2 A TYR   A 9   ? 0.1429 0.1877 0.1905 -0.0136 0.0277  -0.0000 9   TYR   A CE2 
163  C  CE2 B TYR   A 9   ? 0.1397 0.1737 0.1422 -0.0060 0.0384  0.0089  9   TYR   A CE2 
164  C  CZ  A TYR   A 9   ? 0.1463 0.1899 0.2107 -0.0209 0.0385  -0.0091 9   TYR   A CZ  
165  C  CZ  B TYR   A 9   ? 0.1394 0.1684 0.1565 -0.0092 0.0475  0.0040  9   TYR   A CZ  
166  O  OH  A TYR   A 9   ? 0.1543 0.1964 0.2321 -0.0257 0.0367  -0.0128 9   TYR   A OH  
167  O  OH  B TYR   A 9   ? 0.1328 0.1652 0.1635 -0.0097 0.0517  0.0134  9   TYR   A OH  
186  N  N   A LEU   A 10  ? 0.1360 0.1528 0.1479 -0.0192 0.0119  0.0199  10  LEU   A N   
187  N  N   B LEU   A 10  ? 0.1544 0.1504 0.1395 -0.0168 0.0218  0.0311  10  LEU   A N   
188  C  CA  A LEU   A 10  ? 0.1307 0.1428 0.1526 -0.0190 0.0120  0.0240  10  LEU   A CA  
189  C  CA  B LEU   A 10  ? 0.1487 0.1432 0.1509 -0.0168 0.0239  0.0147  10  LEU   A CA  
190  C  C   A LEU   A 10  ? 0.1256 0.1399 0.1585 -0.0179 0.0171  0.0343  10  LEU   A C   
191  C  C   B LEU   A 10  ? 0.1421 0.1363 0.1424 -0.0173 0.0197  0.0246  10  LEU   A C   
192  O  O   A LEU   A 10  ? 0.1270 0.1407 0.1819 -0.0099 0.0255  0.0354  10  LEU   A O   
193  O  O   B LEU   A 10  ? 0.1411 0.1365 0.1580 -0.0129 0.0318  0.0301  10  LEU   A O   
194  C  CB  A LEU   A 10  ? 0.1365 0.1383 0.1800 -0.0107 0.0098  0.0300  10  LEU   A CB  
195  C  CB  B LEU   A 10  ? 0.1461 0.1367 0.1606 -0.0224 0.0268  0.0070  10  LEU   A CB  
196  C  CG  A LEU   A 10  ? 0.1599 0.1456 0.2270 0.0007  0.0010  0.0301  10  LEU   A CG  
197  C  CG  B LEU   A 10  ? 0.1508 0.1395 0.1706 -0.0144 0.0162  -0.0069 10  LEU   A CG  
198  C  CD1 A LEU   A 10  ? 0.1736 0.1570 0.2493 -0.0024 0.0131  0.0226  10  LEU   A CD1 
199  C  CD1 B LEU   A 10  ? 0.1599 0.1515 0.1889 -0.0213 0.0130  -0.0106 10  LEU   A CD1 
200  C  CD2 A LEU   A 10  ? 0.1730 0.1562 0.2433 0.0146  0.0041  0.0134  10  LEU   A CD2 
201  C  CD2 B LEU   A 10  ? 0.1587 0.1497 0.1907 -0.0073 0.0017  -0.0166 10  LEU   A CD2 
224  N  N   A LYS   A 11  ? 0.1337 0.1450 0.1604 -0.0246 0.0146  0.0345  11  LYS   A N   
225  N  N   B LYS   A 11  ? 0.1438 0.1335 0.1314 -0.0190 0.0055  0.0199  11  LYS   A N   
226  C  CA  A LYS   A 11  ? 0.1323 0.1432 0.1608 -0.0345 0.0094  0.0322  11  LYS   A CA  
227  C  CA  B LYS   A 11  ? 0.1503 0.1320 0.1385 -0.0152 0.0085  0.0207  11  LYS   A CA  
228  C  C   A LYS   A 11  ? 0.1294 0.1460 0.1672 -0.0255 0.0144  0.0195  11  LYS   A C   
229  C  C   B LYS   A 11  ? 0.1396 0.1164 0.1328 -0.0187 0.0134  0.0072  11  LYS   A C   
230  O  O   A LYS   A 11  ? 0.1385 0.1561 0.1954 -0.0436 0.0189  0.0017  11  LYS   A O   
231  O  O   B LYS   A 11  ? 0.1340 0.1152 0.1495 -0.0216 0.0240  -0.0117 11  LYS   A O   
232  C  CB  A LYS   A 11  ? 0.1449 0.1454 0.1633 -0.0367 0.0059  0.0189  11  LYS   A CB  
233  C  CB  B LYS   A 11  ? 0.1616 0.1309 0.1547 -0.0122 0.0055  0.0219  11  LYS   A CB  
234  C  CG  A LYS   A 11  ? 0.1621 0.1433 0.1590 -0.0324 0.0154  0.0272  11  LYS   A CG  
235  C  CG  B LYS   A 11  ? 0.1755 0.1312 0.1625 -0.0061 0.0085  0.0384  11  LYS   A CG  
236  C  CD  A LYS   A 11  ? 0.1752 0.1398 0.1555 -0.0298 0.0191  0.0216  11  LYS   A CD  
237  C  CD  B LYS   A 11  ? 0.1849 0.1336 0.1759 -0.0026 0.0083  0.0380  11  LYS   A CD  
238  C  CE  A LYS   A 11  ? 0.1839 0.1400 0.1562 -0.0249 0.0177  0.0263  11  LYS   A CE  
239  C  CE  B LYS   A 11  ? 0.1882 0.1344 0.1812 -0.0011 0.0054  0.0464  11  LYS   A CE  
240  N  NZ  A LYS   A 11  ? 0.1819 0.1458 0.1765 -0.0152 0.0089  0.0302  11  LYS   A NZ  
241  N  NZ  B LYS   A 11  ? 0.1848 0.1367 0.1923 0.0074  -0.0057 0.0514  11  LYS   A NZ  
268  N  N   A LEU   A 12  ? 0.1246 0.1407 0.1534 -0.0258 0.0176  0.0168  12  LEU   A N   
269  N  N   B LEU   A 12  ? 0.1372 0.1311 0.1396 -0.0118 0.0122  0.0071  12  LEU   A N   
270  C  CA  A LEU   A 12  ? 0.1255 0.1411 0.1482 -0.0190 0.0048  0.0238  12  LEU   A CA  
271  C  CA  B LEU   A 12  ? 0.1329 0.1392 0.1502 -0.0059 0.0136  0.0073  12  LEU   A CA  
272  C  C   A LEU   A 12  ? 0.1282 0.1324 0.1558 -0.0255 0.0099  0.0300  12  LEU   A C   
273  C  C   B LEU   A 12  ? 0.1336 0.1401 0.1586 -0.0038 0.0270  0.0165  12  LEU   A C   
274  O  O   A LEU   A 12  ? 0.1361 0.1278 0.1652 -0.0187 0.0123  0.0036  12  LEU   A O   
275  O  O   B LEU   A 12  ? 0.1372 0.1289 0.1581 0.0061  0.0239  0.0137  12  LEU   A O   
276  C  CB  A LEU   A 12  ? 0.1369 0.1340 0.1455 -0.0144 -0.0042 0.0201  12  LEU   A CB  
277  C  CB  B LEU   A 12  ? 0.1357 0.1471 0.1513 -0.0009 0.0129  0.0014  12  LEU   A CB  
278  C  CG  A LEU   A 12  ? 0.1506 0.1398 0.1729 -0.0111 0.0104  0.0216  12  LEU   A CG  
279  C  CG  B LEU   A 12  ? 0.1399 0.1504 0.1682 0.0076  0.0099  -0.0053 12  LEU   A CG  
280  C  CD1 A LEU   A 12  ? 0.1611 0.1405 0.1793 0.0031  0.0256  0.0260  12  LEU   A CD1 
281  C  CD1 B LEU   A 12  ? 0.1407 0.1557 0.1817 0.0165  0.0210  -0.0063 12  LEU   A CD1 
282  C  CD2 A LEU   A 12  ? 0.1530 0.1418 0.1814 -0.0140 0.0070  0.0208  12  LEU   A CD2 
283  C  CD2 B LEU   A 12  ? 0.1431 0.1527 0.1783 0.0108  0.0012  -0.0114 12  LEU   A CD2 
306  N  N   A THR   A 13  ? 0.1256 0.1350 0.1677 -0.0215 0.0022  0.0311  13  THR   A N   
307  N  N   B THR   A 13  ? 0.1312 0.1439 0.1718 -0.0035 0.0243  0.0157  13  THR   A N   
308  C  CA  A THR   A 13  ? 0.1298 0.1404 0.1727 -0.0189 0.0093  0.0363  13  THR   A CA  
309  C  CA  B THR   A 13  ? 0.1308 0.1483 0.1790 -0.0085 0.0239  0.0201  13  THR   A CA  
310  C  C   A THR   A 13  ? 0.1303 0.1370 0.1763 -0.0240 0.0026  0.0432  13  THR   A C   
311  C  C   B THR   A 13  ? 0.1354 0.1525 0.1795 -0.0167 0.0191  0.0226  13  THR   A C   
312  O  O   A THR   A 13  ? 0.1386 0.1408 0.1852 -0.0249 -0.0012 0.0392  13  THR   A O   
313  O  O   B THR   A 13  ? 0.1419 0.1555 0.1783 -0.0148 0.0147  0.0238  13  THR   A O   
314  C  CB  A THR   A 13  ? 0.1312 0.1498 0.1884 -0.0134 0.0045  0.0398  13  THR   A CB  
315  C  CB  B THR   A 13  ? 0.1250 0.1507 0.1842 -0.0063 0.0174  0.0313  13  THR   A CB  
316  O  OG1 A THR   A 13  ? 0.1287 0.1433 0.1971 -0.0113 -0.0132 0.0504  13  THR   A OG1 
317  O  OG1 B THR   A 13  ? 0.1156 0.1486 0.1955 -0.0079 0.0216  0.0413  13  THR   A OG1 
318  C  CG2 A THR   A 13  ? 0.1386 0.1651 0.1894 -0.0084 0.0159  0.0366  13  THR   A CG2 
319  C  CG2 B THR   A 13  ? 0.1312 0.1582 0.1944 0.0015  0.0195  0.0247  13  THR   A CG2 
334  N  N   A ASP   A 14  ? 0.1374 0.1364 0.1770 -0.0244 0.0007  0.0456  14  ASP   A N   
335  N  N   B ASP   A 14  ? 0.1427 0.1565 0.1843 -0.0200 0.0139  0.0246  14  ASP   A N   
336  C  CA  A ASP   A 14  ? 0.1436 0.1406 0.1926 -0.0188 -0.0079 0.0509  14  ASP   A CA  
337  C  CA  B ASP   A 14  ? 0.1466 0.1567 0.1796 -0.0212 0.0093  0.0280  14  ASP   A CA  
338  C  C   A ASP   A 14  ? 0.1400 0.1464 0.1723 -0.0184 -0.0086 0.0470  14  ASP   A C   
339  C  C   B ASP   A 14  ? 0.1345 0.1439 0.1480 -0.0191 0.0071  0.0271  14  ASP   A C   
340  O  O   A ASP   A 14  ? 0.1578 0.1502 0.1769 -0.0208 -0.0059 0.0343  14  ASP   A O   
341  O  O   B ASP   A 14  ? 0.1387 0.1414 0.1446 -0.0120 0.0127  0.0230  14  ASP   A O   
342  C  CB  A ASP   A 14  ? 0.1626 0.1468 0.2528 -0.0209 -0.0089 0.0603  14  ASP   A CB  
343  C  CB  B ASP   A 14  ? 0.1652 0.1796 0.2263 -0.0222 0.0103  0.0342  14  ASP   A CB  
344  C  CG  A ASP   A 14  ? 0.1834 0.1868 0.3375 -0.0202 -0.0054 0.0479  14  ASP   A CG  
345  C  CG  B ASP   A 14  ? 0.1777 0.2060 0.2734 -0.0272 0.0093  0.0290  14  ASP   A CG  
346  O  OD1 A ASP   A 14  ? 0.1954 0.1997 0.3599 -0.0037 -0.0177 0.0480  14  ASP   A OD1 
347  O  OD1 B ASP   A 14  ? 0.1890 0.2124 0.2913 -0.0258 0.0074  0.0302  14  ASP   A OD1 
348  O  OD2 A ASP   A 14  ? 0.2039 0.2183 0.3865 -0.0217 -0.0092 0.0223  14  ASP   A OD2 
349  O  OD2 B ASP   A 14  ? 0.1831 0.2280 0.2955 -0.0232 -0.0008 0.0141  14  ASP   A OD2 
358  N  N   A ASN   A 15  ? 0.1338 0.1428 0.1753 -0.0176 -0.0072 0.0536  15  ASN   A N   
359  N  N   B ASN   A 15  ? 0.1244 0.1347 0.1357 -0.0293 0.0069  0.0333  15  ASN   A N   
360  C  CA  A ASN   A 15  ? 0.1355 0.1447 0.1846 -0.0086 -0.0132 0.0415  15  ASN   A CA  
361  C  CA  B ASN   A 15  ? 0.1237 0.1339 0.1502 -0.0251 0.0098  0.0262  15  ASN   A CA  
362  C  C   A ASN   A 15  ? 0.1322 0.1380 0.1908 -0.0102 0.0058  0.0334  15  ASN   A C   
363  C  C   B ASN   A 15  ? 0.1241 0.1326 0.1693 -0.0204 0.0179  0.0245  15  ASN   A C   
364  O  O   A ASN   A 15  ? 0.1305 0.1327 0.1714 -0.0125 0.0041  0.0214  15  ASN   A O   
365  O  O   B ASN   A 15  ? 0.1249 0.1296 0.1796 -0.0151 0.0176  0.0115  15  ASN   A O   
366  C  CB  A ASN   A 15  ? 0.1330 0.1477 0.1829 -0.0011 -0.0116 0.0397  15  ASN   A CB  
367  C  CB  B ASN   A 15  ? 0.1165 0.1326 0.1475 -0.0280 0.0135  0.0225  15  ASN   A CB  
368  C  CG  A ASN   A 15  ? 0.1368 0.1555 0.1787 0.0016  0.0079  0.0227  15  ASN   A CG  
369  C  CG  B ASN   A 15  ? 0.1188 0.1415 0.1625 -0.0247 0.0171  0.0146  15  ASN   A CG  
370  O  OD1 A ASN   A 15  ? 0.1495 0.1593 0.1814 -0.0066 0.0083  0.0166  15  ASN   A OD1 
371  O  OD1 B ASN   A 15  ? 0.1289 0.1436 0.1598 -0.0306 0.0219  0.0087  15  ASN   A OD1 
372  N  ND2 A ASN   A 15  ? 0.1422 0.1664 0.1755 -0.0020 0.0178  0.0285  15  ASN   A ND2 
373  N  ND2 B ASN   A 15  ? 0.1220 0.1506 0.1649 -0.0266 0.0142  0.0196  15  ASN   A ND2 
386  N  N   A VAL   A 16  ? 0.1324 0.1376 0.2072 -0.0127 0.0067  0.0409  16  VAL   A N   
387  N  N   B VAL   A 16  ? 0.1226 0.1391 0.1747 -0.0177 0.0097  0.0312  16  VAL   A N   
388  C  CA  A VAL   A 16  ? 0.1324 0.1393 0.1927 -0.0073 0.0069  0.0452  16  VAL   A CA  
389  C  CA  B VAL   A 16  ? 0.1217 0.1405 0.1692 -0.0218 0.0078  0.0361  16  VAL   A CA  
390  C  C   A VAL   A 16  ? 0.1310 0.1403 0.1822 -0.0133 -0.0006 0.0493  16  VAL   A C   
391  C  C   B VAL   A 16  ? 0.1174 0.1400 0.1680 -0.0237 -0.0043 0.0390  16  VAL   A C   
392  O  O   A VAL   A 16  ? 0.1277 0.1366 0.2001 -0.0091 0.0131  0.0374  16  VAL   A O   
393  O  O   B VAL   A 16  ? 0.1053 0.1360 0.1785 -0.0261 -0.0022 0.0323  16  VAL   A O   
394  C  CB  A VAL   A 16  ? 0.1369 0.1534 0.1854 0.0073  0.0163  0.0463  16  VAL   A CB  
395  C  CB  B VAL   A 16  ? 0.1334 0.1546 0.1694 -0.0182 0.0222  0.0381  16  VAL   A CB  
396  C  CG1 A VAL   A 16  ? 0.1479 0.1639 0.1895 0.0120  0.0144  0.0504  16  VAL   A CG1 
397  C  CG1 B VAL   A 16  ? 0.1394 0.1660 0.1751 -0.0142 0.0222  0.0382  16  VAL   A CG1 
398  C  CG2 A VAL   A 16  ? 0.1406 0.1634 0.1929 0.0111  0.0338  0.0429  16  VAL   A CG2 
399  C  CG2 B VAL   A 16  ? 0.1382 0.1609 0.1733 -0.0193 0.0315  0.0341  16  VAL   A CG2 
418  N  N   . TYR   A 17  ? 0.1232 0.1390 0.1763 -0.0163 0.0082  0.0437  17  TYR   A N   
419  C  CA  . TYR   A 17  ? 0.1257 0.1412 0.1596 -0.0169 0.0135  0.0453  17  TYR   A CA  
420  C  C   . TYR   A 17  ? 0.1296 0.1371 0.1738 -0.0170 0.0097  0.0379  17  TYR   A C   
421  O  O   . TYR   A 17  ? 0.1236 0.1451 0.1937 -0.0179 0.0142  0.0512  17  TYR   A O   
422  C  CB  . TYR   A 17  ? 0.1421 0.1444 0.1774 -0.0189 -0.0006 0.0414  17  TYR   A CB  
423  C  CG  . TYR   A 17  ? 0.1653 0.1522 0.1816 -0.0271 -0.0053 0.0389  17  TYR   A CG  
424  C  CD1 . TYR   A 17  ? 0.1821 0.1611 0.2019 -0.0088 -0.0169 0.0366  17  TYR   A CD1 
425  C  CD2 . TYR   A 17  ? 0.1823 0.1608 0.1721 -0.0422 -0.0103 0.0425  17  TYR   A CD2 
426  C  CE1 . TYR   A 17  ? 0.1974 0.1605 0.2080 -0.0175 -0.0237 0.0420  17  TYR   A CE1 
427  C  CE2 . TYR   A 17  ? 0.2010 0.1622 0.1884 -0.0443 -0.0214 0.0313  17  TYR   A CE2 
428  C  CZ  . TYR   A 17  ? 0.2116 0.1562 0.1948 -0.0328 -0.0337 0.0435  17  TYR   A CZ  
429  O  OH  . TYR   A 17  ? 0.2354 0.1578 0.2060 -0.0305 -0.0389 0.0461  17  TYR   A OH  
440  N  N   A ILE   A 18  ? 0.1291 0.1346 0.1753 -0.0193 0.0033  0.0358  18  ILE   A N   
441  N  N   B ILE   A 18  ? 0.1249 0.1352 0.1581 -0.0125 0.0129  0.0362  18  ILE   A N   
442  C  CA  A ILE   A 18  ? 0.1338 0.1317 0.1722 -0.0156 0.0094  0.0333  18  ILE   A CA  
443  C  CA  B ILE   A 18  ? 0.1209 0.1339 0.1365 -0.0041 0.0194  0.0303  18  ILE   A CA  
444  C  C   A ILE   A 18  ? 0.1378 0.1423 0.1763 -0.0274 0.0099  0.0300  18  ILE   A C   
445  C  C   B ILE   A 18  ? 0.1128 0.1414 0.1190 -0.0086 0.0104  0.0258  18  ILE   A C   
446  O  O   A ILE   A 18  ? 0.1364 0.1547 0.1720 -0.0398 0.0075  0.0368  18  ILE   A O   
447  O  O   B ILE   A 18  ? 0.1113 0.1535 0.1226 -0.0135 0.0170  0.0232  18  ILE   A O   
448  C  CB  A ILE   A 18  ? 0.1411 0.1294 0.1550 0.0004  0.0152  0.0296  18  ILE   A CB  
449  C  CB  B ILE   A 18  ? 0.1303 0.1287 0.1238 0.0042  0.0321  0.0253  18  ILE   A CB  
450  C  CG1 A ILE   A 18  ? 0.1468 0.1343 0.1435 0.0096  0.0086  0.0233  18  ILE   A CG1 
451  C  CG1 B ILE   A 18  ? 0.1473 0.1366 0.1374 -0.0003 0.0386  0.0279  18  ILE   A CG1 
452  C  CG2 A ILE   A 18  ? 0.1386 0.1241 0.1593 0.0089  0.0147  0.0172  18  ILE   A CG2 
453  C  CG2 B ILE   A 18  ? 0.1387 0.1356 0.1242 -0.0019 0.0268  0.0238  18  ILE   A CG2 
454  C  CD1 A ILE   A 18  ? 0.1648 0.1459 0.1466 0.0279  0.0066  0.0302  18  ILE   A CD1 
455  C  CD1 B ILE   A 18  ? 0.1636 0.1519 0.1571 0.0037  0.0423  0.0192  18  ILE   A CD1 
478  N  N   A LYS   A 19  ? 0.1473 0.1428 0.1801 -0.0215 0.0270  0.0282  19  LYS   A N   
479  N  N   B LYS   A 19  ? 0.1159 0.1394 0.1181 -0.0024 0.0209  0.0182  19  LYS   A N   
480  C  CA  A LYS   A 19  ? 0.1584 0.1534 0.1825 -0.0191 0.0359  0.0277  19  LYS   A CA  
481  C  CA  B LYS   A 19  ? 0.1309 0.1519 0.1388 0.0035  0.0273  0.0103  19  LYS   A CA  
482  C  C   A LYS   A 19  ? 0.1513 0.1452 0.1905 -0.0164 0.0324  0.0300  19  LYS   A C   
483  C  C   B LYS   A 19  ? 0.1280 0.1467 0.1507 0.0072  0.0234  0.0116  19  LYS   A C   
484  O  O   A LYS   A 19  ? 0.1430 0.1437 0.1735 -0.0121 0.0264  0.0342  19  LYS   A O   
485  O  O   B LYS   A 19  ? 0.1241 0.1419 0.1522 -0.0016 0.0134  0.0137  19  LYS   A O   
486  C  CB  A LYS   A 19  ? 0.1823 0.1759 0.1886 -0.0222 0.0430  0.0281  19  LYS   A CB  
487  C  CB  B LYS   A 19  ? 0.1475 0.1724 0.1473 0.0067  0.0292  0.0004  19  LYS   A CB  
488  C  CG  A LYS   A 19  ? 0.2094 0.1931 0.2016 -0.0239 0.0461  0.0200  19  LYS   A CG  
489  C  CG  B LYS   A 19  ? 0.1709 0.1892 0.1583 0.0097  0.0307  -0.0072 19  LYS   A CG  
490  C  CD  A LYS   A 19  ? 0.2325 0.2102 0.2087 -0.0272 0.0590  0.0089  19  LYS   A CD  
491  C  CD  B LYS   A 19  ? 0.1953 0.2073 0.1793 0.0080  0.0334  -0.0105 19  LYS   A CD  
492  C  CE  A LYS   A 19  ? 0.2490 0.2168 0.2215 -0.0316 0.0661  0.0009  19  LYS   A CE  
493  C  CE  B LYS   A 19  ? 0.2118 0.2188 0.1926 0.0032  0.0377  -0.0104 19  LYS   A CE  
494  N  NZ  A LYS   A 19  ? 0.2577 0.2146 0.2140 -0.0381 0.0779  -0.0142 19  LYS   A NZ  
495  N  NZ  B LYS   A 19  ? 0.2208 0.2221 0.1956 0.0014  0.0439  -0.0184 19  LYS   A NZ  
522  N  N   A ASN   A 20  ? 0.1569 0.1473 0.2167 -0.0194 0.0364  0.0418  20  ASN   A N   
523  N  N   B ASN   A 20  ? 0.1300 0.1494 0.1720 0.0110  0.0316  0.0165  20  ASN   A N   
524  C  CA  A ASN   A 20  ? 0.1718 0.1557 0.2384 -0.0034 0.0486  0.0396  20  ASN   A CA  
525  C  CA  B ASN   A 20  ? 0.1359 0.1551 0.1944 0.0177  0.0413  0.0178  20  ASN   A CA  
526  C  C   A ASN   A 20  ? 0.1847 0.1590 0.2372 -0.0058 0.0596  0.0309  20  ASN   A C   
527  C  C   B ASN   A 20  ? 0.1540 0.1536 0.2052 0.0138  0.0542  0.0130  20  ASN   A C   
528  O  O   A ASN   A 20  ? 0.1961 0.1547 0.2366 -0.0101 0.0561  0.0232  20  ASN   A O   
529  O  O   B ASN   A 20  ? 0.1663 0.1518 0.2178 0.0140  0.0562  0.0127  20  ASN   A O   
530  C  CB  A ASN   A 20  ? 0.1818 0.1612 0.2623 0.0051  0.0480  0.0472  20  ASN   A CB  
531  C  CB  B ASN   A 20  ? 0.1310 0.1611 0.2086 0.0203  0.0370  0.0234  20  ASN   A CB  
532  C  CG  A ASN   A 20  ? 0.1929 0.1646 0.2919 0.0162  0.0508  0.0475  20  ASN   A CG  
533  C  CG  B ASN   A 20  ? 0.1285 0.1612 0.2195 0.0261  0.0387  0.0284  20  ASN   A CG  
534  O  OD1 A ASN   A 20  ? 0.2140 0.1841 0.3309 0.0187  0.0508  0.0248  20  ASN   A OD1 
535  O  OD1 B ASN   A 20  ? 0.1265 0.1490 0.2261 0.0276  0.0450  0.0172  20  ASN   A OD1 
536  N  ND2 A ASN   A 20  ? 0.1962 0.1550 0.2946 0.0220  0.0407  0.0658  20  ASN   A ND2 
537  N  ND2 B ASN   A 20  ? 0.1413 0.1691 0.2359 0.0254  0.0312  0.0475  20  ASN   A ND2 
550  N  N   A ALA   A 21  ? 0.1868 0.1639 0.2313 -0.0036 0.0549  0.0233  21  ALA   A N   
551  N  N   B ALA   A 21  ? 0.1594 0.1513 0.2012 0.0094  0.0488  0.0056  21  ALA   A N   
552  C  CA  A ALA   A 21  ? 0.1957 0.1704 0.2291 -0.0040 0.0476  0.0310  21  ALA   A CA  
553  C  CA  B ALA   A 21  ? 0.1695 0.1489 0.2029 0.0012  0.0440  0.0122  21  ALA   A CA  
554  C  C   A ALA   A 21  ? 0.1849 0.1709 0.2235 -0.0025 0.0413  0.0328  21  ALA   A C   
555  C  C   B ALA   A 21  ? 0.1570 0.1410 0.1878 -0.0020 0.0445  0.0193  21  ALA   A C   
556  O  O   A ALA   A 21  ? 0.1810 0.1765 0.2264 0.0025  0.0401  0.0317  21  ALA   A O   
557  O  O   B ALA   A 21  ? 0.1538 0.1319 0.2021 0.0015  0.0345  0.0111  21  ALA   A O   
558  C  CB  A ALA   A 21  ? 0.2060 0.1760 0.2384 -0.0036 0.0464  0.0295  21  ALA   A CB  
559  C  CB  B ALA   A 21  ? 0.1794 0.1514 0.2204 0.0008  0.0361  0.0107  21  ALA   A CB  
570  N  N   A ASP   A 22  ? 0.1835 0.1673 0.2378 -0.0084 0.0317  0.0309  22  ASP   A N   
571  N  N   B ASP   A 22  ? 0.1526 0.1411 0.1785 -0.0062 0.0521  0.0250  22  ASP   A N   
572  C  CA  A ASP   A 22  ? 0.1846 0.1666 0.2487 -0.0063 0.0193  0.0328  22  ASP   A CA  
573  C  CA  B ASP   A 22  ? 0.1565 0.1408 0.1662 -0.0063 0.0449  0.0230  22  ASP   A CA  
574  C  C   A ASP   A 22  ? 0.1746 0.1660 0.2082 -0.0059 0.0209  0.0242  22  ASP   A C   
575  C  C   B ASP   A 22  ? 0.1440 0.1413 0.1380 -0.0184 0.0437  0.0198  22  ASP   A C   
576  O  O   A ASP   A 22  ? 0.1782 0.1682 0.2175 -0.0061 0.0182  0.0174  22  ASP   A O   
577  O  O   B ASP   A 22  ? 0.1408 0.1476 0.1398 -0.0244 0.0365  -0.0042 22  ASP   A O   
578  C  CB  A ASP   A 22  ? 0.2001 0.1684 0.3013 -0.0065 0.0123  0.0297  22  ASP   A CB  
579  C  CB  B ASP   A 22  ? 0.1762 0.1443 0.1905 0.0061  0.0431  0.0160  22  ASP   A CB  
580  C  CG  A ASP   A 22  ? 0.2178 0.1779 0.3491 -0.0085 -0.0002 0.0368  22  ASP   A CG  
581  C  CG  B ASP   A 22  ? 0.1889 0.1446 0.1860 0.0132  0.0429  0.0196  22  ASP   A CG  
582  O  OD1 A ASP   A 22  ? 0.2094 0.1793 0.3720 -0.0252 -0.0101 0.0489  22  ASP   A OD1 
583  O  OD1 B ASP   A 22  ? 0.1828 0.1415 0.1561 0.0103  0.0383  0.0119  22  ASP   A OD1 
584  O  OD2 A ASP   A 22  ? 0.2415 0.1862 0.3692 -0.0037 -0.0004 0.0271  22  ASP   A OD2 
585  O  OD2 B ASP   A 22  ? 0.2059 0.1491 0.2152 0.0129  0.0544  0.0251  22  ASP   A OD2 
594  N  N   A ILE   A 23  ? 0.1734 0.1666 0.1807 0.0006  0.0225  0.0190  23  ILE   A N   
595  N  N   B ILE   A 23  ? 0.1427 0.1410 0.1350 -0.0148 0.0328  0.0186  23  ILE   A N   
596  C  CA  A ILE   A 23  ? 0.1692 0.1613 0.1703 -0.0034 0.0310  0.0213  23  ILE   A CA  
597  C  CA  B ILE   A 23  ? 0.1347 0.1484 0.1244 -0.0142 0.0254  0.0204  23  ILE   A CA  
598  C  C   A ILE   A 23  ? 0.1667 0.1686 0.1574 -0.0059 0.0408  0.0177  23  ILE   A C   
599  C  C   B ILE   A 23  ? 0.1430 0.1602 0.1364 -0.0225 0.0227  0.0078  23  ILE   A C   
600  O  O   A ILE   A 23  ? 0.1772 0.1757 0.1514 -0.0049 0.0347  0.0029  23  ILE   A O   
601  O  O   B ILE   A 23  ? 0.1491 0.1590 0.1426 -0.0231 0.0149  0.0049  23  ILE   A O   
602  C  CB  A ILE   A 23  ? 0.1781 0.1585 0.1491 0.0040  0.0300  0.0185  23  ILE   A CB  
603  C  CB  B ILE   A 23  ? 0.1295 0.1465 0.1152 -0.0044 0.0159  0.0230  23  ILE   A CB  
604  C  CG1 A ILE   A 23  ? 0.1830 0.1560 0.1492 0.0023  0.0230  0.0162  23  ILE   A CG1 
605  C  CG1 B ILE   A 23  ? 0.1324 0.1448 0.1156 -0.0111 0.0109  0.0182  23  ILE   A CG1 
606  C  CG2 A ILE   A 23  ? 0.1784 0.1600 0.1477 0.0124  0.0297  0.0187  23  ILE   A CG2 
607  C  CG2 B ILE   A 23  ? 0.1254 0.1432 0.1061 0.0050  0.0021  0.0174  23  ILE   A CG2 
608  C  CD1 A ILE   A 23  ? 0.1860 0.1584 0.1465 -0.0004 0.0107  0.0034  23  ILE   A CD1 
609  C  CD1 B ILE   A 23  ? 0.1351 0.1494 0.1178 -0.0055 0.0043  0.0127  23  ILE   A CD1 
632  N  N   A VAL   A 24  ? 0.1704 0.1747 0.1742 -0.0131 0.0338  0.0193  24  VAL   A N   
633  N  N   B VAL   A 24  ? 0.1531 0.1667 0.1521 -0.0329 0.0188  0.0030  24  VAL   A N   
634  C  CA  A VAL   A 24  ? 0.1837 0.1898 0.1911 -0.0184 0.0313  0.0097  24  VAL   A CA  
635  C  CA  B VAL   A 24  ? 0.1708 0.1726 0.1660 -0.0384 0.0305  0.0039  24  VAL   A CA  
636  C  C   A VAL   A 24  ? 0.1869 0.2062 0.1921 -0.0263 0.0190  0.0066  24  VAL   A C   
637  C  C   B VAL   A 24  ? 0.1770 0.1885 0.1705 -0.0407 0.0356  -0.0043 24  VAL   A C   
638  O  O   A VAL   A 24  ? 0.1930 0.2087 0.1879 -0.0225 0.0221  0.0048  24  VAL   A O   
639  O  O   B VAL   A 24  ? 0.1860 0.1942 0.1881 -0.0381 0.0368  -0.0008 24  VAL   A O   
640  C  CB  A VAL   A 24  ? 0.1944 0.1902 0.2127 -0.0158 0.0409  0.0079  24  VAL   A CB  
641  C  CB  B VAL   A 24  ? 0.1799 0.1705 0.1927 -0.0381 0.0322  0.0137  24  VAL   A CB  
642  C  CG1 A VAL   A 24  ? 0.2027 0.1974 0.2250 -0.0091 0.0454  -0.0046 24  VAL   A CG1 
643  C  CG1 B VAL   A 24  ? 0.1928 0.1789 0.2193 -0.0304 0.0269  0.0127  24  VAL   A CG1 
644  C  CG2 A VAL   A 24  ? 0.2032 0.1915 0.2256 -0.0132 0.0487  0.0211  24  VAL   A CG2 
645  C  CG2 B VAL   A 24  ? 0.1854 0.1664 0.1909 -0.0412 0.0378  0.0122  24  VAL   A CG2 
664  N  N   A GLU   A 25  ? 0.1930 0.2293 0.1951 -0.0312 0.0218  -0.0051 25  GLU   A N   
665  N  N   B GLU   A 25  ? 0.1764 0.2008 0.1659 -0.0401 0.0462  -0.0146 25  GLU   A N   
666  C  CA  A GLU   A 25  ? 0.2064 0.2528 0.2065 -0.0257 0.0324  -0.0119 25  GLU   A CA  
667  C  CA  B GLU   A 25  ? 0.1857 0.2207 0.1735 -0.0360 0.0471  -0.0181 25  GLU   A CA  
668  C  C   A GLU   A 25  ? 0.1973 0.2542 0.1706 -0.0347 0.0426  -0.0156 25  GLU   A C   
669  C  C   B GLU   A 25  ? 0.1881 0.2319 0.1614 -0.0316 0.0494  -0.0179 25  GLU   A C   
670  O  O   A GLU   A 25  ? 0.1984 0.2631 0.1662 -0.0373 0.0412  -0.0191 25  GLU   A O   
671  O  O   B GLU   A 25  ? 0.1927 0.2375 0.1663 -0.0302 0.0552  -0.0207 25  GLU   A O   
672  C  CB  A GLU   A 25  ? 0.2303 0.2790 0.2609 -0.0176 0.0266  -0.0122 25  GLU   A CB  
673  C  CB  B GLU   A 25  ? 0.1976 0.2320 0.2102 -0.0325 0.0444  -0.0202 25  GLU   A CB  
674  C  CG  A GLU   A 25  ? 0.2567 0.3040 0.3244 -0.0175 0.0112  -0.0166 25  GLU   A CG  
675  C  CG  B GLU   A 25  ? 0.2180 0.2468 0.2681 -0.0311 0.0299  -0.0209 25  GLU   A CG  
676  C  CD  A GLU   A 25  ? 0.2769 0.3272 0.3772 -0.0140 -0.0017 -0.0207 25  GLU   A CD  
677  C  CD  B GLU   A 25  ? 0.2321 0.2621 0.3224 -0.0319 0.0138  -0.0193 25  GLU   A CD  
678  O  OE1 A GLU   A 25  ? 0.2853 0.3360 0.3878 -0.0101 -0.0122 -0.0266 25  GLU   A OE1 
679  O  OE1 B GLU   A 25  ? 0.2386 0.2687 0.3484 -0.0321 0.0084  -0.0191 25  GLU   A OE1 
680  O  OE2 A GLU   A 25  ? 0.2856 0.3385 0.4061 -0.0138 -0.0035 -0.0242 25  GLU   A OE2 
681  O  OE2 B GLU   A 25  ? 0.2370 0.2684 0.3423 -0.0307 0.0067  -0.0160 25  GLU   A OE2 
694  N  N   A GLU   A 26  ? 0.1864 0.2443 0.1697 -0.0523 0.0518  -0.0135 26  GLU   A N   
695  N  N   B GLU   A 26  ? 0.1846 0.2330 0.1546 -0.0334 0.0499  -0.0149 26  GLU   A N   
696  C  CA  A GLU   A 26  ? 0.1939 0.2430 0.1482 -0.0649 0.0457  -0.0131 26  GLU   A CA  
697  C  CA  B GLU   A 26  ? 0.1921 0.2394 0.1557 -0.0300 0.0418  -0.0063 26  GLU   A CA  
698  C  C   A GLU   A 26  ? 0.1910 0.2358 0.1275 -0.0609 0.0398  -0.0098 26  GLU   A C   
699  C  C   B GLU   A 26  ? 0.1906 0.2297 0.1468 -0.0217 0.0387  0.0051  26  GLU   A C   
700  O  O   A GLU   A 26  ? 0.1999 0.2417 0.1132 -0.0613 0.0405  -0.0128 26  GLU   A O   
701  O  O   B GLU   A 26  ? 0.1950 0.2309 0.1383 -0.0264 0.0473  0.0038  26  GLU   A O   
702  C  CB  A GLU   A 26  ? 0.2105 0.2441 0.1774 -0.0781 0.0466  -0.0103 26  GLU   A CB  
703  C  CB  B GLU   A 26  ? 0.2016 0.2502 0.1665 -0.0348 0.0329  -0.0073 26  GLU   A CB  
704  C  CG  A GLU   A 26  ? 0.2354 0.2565 0.2495 -0.0829 0.0479  -0.0209 26  GLU   A CG  
705  C  CG  B GLU   A 26  ? 0.2131 0.2620 0.1784 -0.0364 0.0351  -0.0137 26  GLU   A CG  
706  C  CD  A GLU   A 26  ? 0.2523 0.2642 0.2896 -0.0911 0.0612  -0.0298 26  GLU   A CD  
707  C  CD  B GLU   A 26  ? 0.2221 0.2719 0.1738 -0.0437 0.0392  -0.0156 26  GLU   A CD  
708  O  OE1 A GLU   A 26  ? 0.2475 0.2762 0.2828 -0.0864 0.0863  -0.0634 26  GLU   A OE1 
709  O  OE1 B GLU   A 26  ? 0.2275 0.2845 0.1685 -0.0382 0.0455  -0.0227 26  GLU   A OE1 
710  O  OE2 A GLU   A 26  ? 0.2709 0.2689 0.3071 -0.0937 0.0554  -0.0180 26  GLU   A OE2 
711  O  OE2 B GLU   A 26  ? 0.2228 0.2710 0.1432 -0.0529 0.0459  -0.0158 26  GLU   A OE2 
724  N  N   A ALA   A 27  ? 0.1749 0.2193 0.1416 -0.0616 0.0395  -0.0033 27  ALA   A N   
725  N  N   B ALA   A 27  ? 0.1802 0.2176 0.1371 -0.0073 0.0327  0.0212  27  ALA   A N   
726  C  CA  A ALA   A 27  ? 0.1791 0.2217 0.1371 -0.0532 0.0319  -0.0017 27  ALA   A CA  
727  C  CA  B ALA   A 27  ? 0.1812 0.2165 0.1233 0.0038  0.0242  0.0309  27  ALA   A CA  
728  C  C   A ALA   A 27  ? 0.1969 0.2333 0.1479 -0.0630 0.0259  -0.0126 27  ALA   A C   
729  C  C   B ALA   A 27  ? 0.1912 0.2242 0.1247 0.0118  0.0144  0.0260  27  ALA   A C   
730  O  O   A ALA   A 27  ? 0.2035 0.2315 0.1628 -0.0656 0.0161  -0.0089 27  ALA   A O   
731  O  O   B ALA   A 27  ? 0.1871 0.2227 0.1333 0.0170  0.0124  0.0241  27  ALA   A O   
732  C  CB  A ALA   A 27  ? 0.1719 0.2123 0.1323 -0.0471 0.0216  0.0086  27  ALA   A CB  
733  C  CB  B ALA   A 27  ? 0.1760 0.2124 0.1097 0.0007  0.0182  0.0392  27  ALA   A CB  
744  N  N   A LYS   A 28  ? 0.2248 0.2571 0.1613 -0.0588 0.0200  -0.0338 28  LYS   A N   
745  N  N   B LYS   A 28  ? 0.2124 0.2341 0.1392 0.0195  0.0061  0.0152  28  LYS   A N   
746  C  CA  A LYS   A 28  ? 0.2586 0.2867 0.1935 -0.0517 0.0212  -0.0405 28  LYS   A CA  
747  C  CA  B LYS   A 28  ? 0.2351 0.2502 0.1657 0.0291  -0.0149 -0.0032 28  LYS   A CA  
748  C  C   A LYS   A 28  ? 0.2779 0.3122 0.1756 -0.0523 0.0366  -0.0315 28  LYS   A C   
749  C  C   B LYS   A 28  ? 0.2523 0.2621 0.1577 0.0287  -0.0155 0.0076  28  LYS   A C   
750  O  O   A LYS   A 28  ? 0.2829 0.3184 0.2054 -0.0471 0.0162  -0.0278 28  LYS   A O   
751  O  O   B LYS   A 28  ? 0.2607 0.2644 0.1599 0.0283  -0.0264 0.0114  28  LYS   A O   
752  C  CB  A LYS   A 28  ? 0.2750 0.2971 0.2485 -0.0390 0.0112  -0.0437 28  LYS   A CB  
753  C  CB  B LYS   A 28  ? 0.2448 0.2592 0.2155 0.0360  -0.0337 -0.0248 28  LYS   A CB  
754  C  CG  A LYS   A 28  ? 0.2896 0.3059 0.3009 -0.0296 0.0028  -0.0454 28  LYS   A CG  
755  C  CG  B LYS   A 28  ? 0.2572 0.2705 0.2685 0.0357  -0.0453 -0.0324 28  LYS   A CG  
756  C  CD  A LYS   A 28  ? 0.3007 0.3194 0.3595 -0.0223 -0.0082 -0.0420 28  LYS   A CD  
757  C  CD  B LYS   A 28  ? 0.2700 0.2845 0.3205 0.0343  -0.0508 -0.0316 28  LYS   A CD  
758  C  CE  A LYS   A 28  ? 0.3068 0.3296 0.4039 -0.0180 -0.0170 -0.0426 28  LYS   A CE  
759  C  CE  B LYS   A 28  ? 0.2798 0.2958 0.3611 0.0296  -0.0549 -0.0310 28  LYS   A CE  
760  N  NZ  A LYS   A 28  ? 0.3128 0.3358 0.4331 -0.0134 -0.0166 -0.0459 28  LYS   A NZ  
761  N  NZ  B LYS   A 28  ? 0.2829 0.3011 0.3784 0.0280  -0.0606 -0.0324 28  LYS   A NZ  
788  N  N   A LYS   A 29  ? 0.2908 0.3333 0.1619 -0.0580 0.0706  -0.0138 29  LYS   A N   
789  N  N   B LYS   A 29  ? 0.2619 0.2727 0.1658 0.0262  0.0053  0.0219  29  LYS   A N   
790  C  CA  A LYS   A 29  ? 0.3100 0.3546 0.1834 -0.0598 0.0916  0.0021  29  LYS   A CA  
791  C  CA  B LYS   A 29  ? 0.2772 0.2887 0.1896 0.0216  0.0213  0.0372  29  LYS   A CA  
792  C  C   A LYS   A 29  ? 0.3105 0.3501 0.1542 -0.0651 0.0769  0.0075  29  LYS   A C   
793  C  C   B LYS   A 29  ? 0.2805 0.2843 0.1700 0.0143  0.0157  0.0523  29  LYS   A C   
794  O  O   A LYS   A 29  ? 0.3214 0.3615 0.1611 -0.0561 0.0722  0.0055  29  LYS   A O   
795  O  O   B LYS   A 29  ? 0.2863 0.2888 0.1765 0.0187  0.0165  0.0574  29  LYS   A O   
796  C  CB  A LYS   A 29  ? 0.3264 0.3796 0.2478 -0.0522 0.1123  0.0096  29  LYS   A CB  
797  C  CB  B LYS   A 29  ? 0.2907 0.3092 0.2393 0.0226  0.0423  0.0366  29  LYS   A CB  
798  C  CG  A LYS   A 29  ? 0.3440 0.4015 0.3166 -0.0437 0.1217  0.0139  29  LYS   A CG  
799  C  CG  B LYS   A 29  ? 0.3047 0.3283 0.2966 0.0256  0.0544  0.0332  29  LYS   A CG  
800  C  CD  A LYS   A 29  ? 0.3603 0.4194 0.3796 -0.0375 0.1244  0.0153  29  LYS   A CD  
801  C  CD  B LYS   A 29  ? 0.3157 0.3433 0.3515 0.0312  0.0603  0.0277  29  LYS   A CD  
802  C  CE  A LYS   A 29  ? 0.3701 0.4311 0.4195 -0.0328 0.1285  0.0156  29  LYS   A CE  
803  C  CE  B LYS   A 29  ? 0.3219 0.3537 0.3879 0.0356  0.0654  0.0207  29  LYS   A CE  
804  N  NZ  A LYS   A 29  ? 0.3750 0.4381 0.4500 -0.0300 0.1279  0.0159  29  LYS   A NZ  
805  N  NZ  B LYS   A 29  ? 0.3255 0.3597 0.4132 0.0379  0.0667  0.0175  29  LYS   A NZ  
832  N  N   A VAL   A 30  ? 0.2952 0.3300 0.1397 -0.0791 0.0674  0.0167  30  VAL   A N   
833  N  N   B VAL   A 30  ? 0.2779 0.2756 0.1658 0.0026  0.0126  0.0531  30  VAL   A N   
834  C  CA  A VAL   A 30  ? 0.2879 0.3111 0.1353 -0.0915 0.0407  0.0327  30  VAL   A CA  
835  C  CA  B VAL   A 30  ? 0.2758 0.2669 0.1781 -0.0077 -0.0019 0.0525  30  VAL   A CA  
836  C  C   A VAL   A 30  ? 0.2790 0.2903 0.1107 -0.0848 0.0223  0.0380  30  VAL   A C   
837  C  C   B VAL   A 30  ? 0.2741 0.2624 0.1731 -0.0088 -0.0096 0.0459  30  VAL   A C   
838  O  O   A VAL   A 30  ? 0.2861 0.2915 0.1093 -0.0821 0.0180  0.0397  30  VAL   A O   
839  O  O   B VAL   A 30  ? 0.2756 0.2590 0.1708 -0.0107 -0.0104 0.0548  30  VAL   A O   
840  C  CB  A VAL   A 30  ? 0.2849 0.3056 0.1723 -0.1004 0.0261  0.0340  30  VAL   A CB  
841  C  CB  B VAL   A 30  ? 0.2756 0.2620 0.1895 -0.0139 -0.0108 0.0592  30  VAL   A CB  
842  C  CG1 A VAL   A 30  ? 0.2885 0.3042 0.1837 -0.1056 0.0202  0.0337  30  VAL   A CG1 
843  C  CG1 B VAL   A 30  ? 0.2786 0.2623 0.1980 -0.0153 -0.0138 0.0619  30  VAL   A CG1 
844  C  CG2 A VAL   A 30  ? 0.2849 0.3081 0.1990 -0.1073 0.0259  0.0305  30  VAL   A CG2 
845  C  CG2 B VAL   A 30  ? 0.2740 0.2578 0.1977 -0.0169 -0.0132 0.0671  30  VAL   A CG2 
864  N  N   A LYS   A 31  ? 0.2664 0.2732 0.1034 -0.0891 0.0090  0.0361  31  LYS   A N   
865  N  N   B LYS   A 31  ? 0.2709 0.2626 0.1818 -0.0104 -0.0168 0.0314  31  LYS   A N   
866  C  CA  A LYS   A 31  ? 0.2765 0.2710 0.1128 -0.0852 -0.0149 0.0370  31  LYS   A CA  
867  C  CA  B LYS   A 31  ? 0.2696 0.2659 0.1915 -0.0078 -0.0256 0.0169  31  LYS   A CA  
868  C  C   A LYS   A 31  ? 0.2478 0.2491 0.0998 -0.0601 -0.0133 0.0561  31  LYS   A C   
869  C  C   B LYS   A 31  ? 0.2547 0.2603 0.1751 -0.0029 -0.0253 0.0250  31  LYS   A C   
870  O  O   A LYS   A 31  ? 0.2517 0.2655 0.1082 -0.0556 -0.0174 0.0665  31  LYS   A O   
871  O  O   B LYS   A 31  ? 0.2591 0.2645 0.1880 0.0027  -0.0271 0.0258  31  LYS   A O   
872  C  CB  A LYS   A 31  ? 0.3115 0.2872 0.2028 -0.0781 -0.0315 0.0208  31  LYS   A CB  
873  C  CB  B LYS   A 31  ? 0.2826 0.2788 0.2201 -0.0077 -0.0332 -0.0040 31  LYS   A CB  
874  C  CG  A LYS   A 31  ? 0.3534 0.3079 0.3215 -0.0728 -0.0424 0.0119  31  LYS   A CG  
875  C  CG  B LYS   A 31  ? 0.2973 0.2940 0.2628 -0.0063 -0.0427 -0.0212 31  LYS   A CG  
876  C  CD  A LYS   A 31  ? 0.3852 0.3232 0.4168 -0.0631 -0.0537 0.0012  31  LYS   A CD  
877  C  CD  B LYS   A 31  ? 0.3067 0.3056 0.2936 -0.0047 -0.0519 -0.0349 31  LYS   A CD  
878  C  CE  A LYS   A 31  ? 0.4059 0.3333 0.4768 -0.0562 -0.0651 -0.0066 31  LYS   A CE  
879  C  CE  B LYS   A 31  ? 0.3139 0.3150 0.3122 -0.0040 -0.0572 -0.0407 31  LYS   A CE  
880  N  NZ  A LYS   A 31  ? 0.4169 0.3391 0.5111 -0.0521 -0.0719 -0.0093 31  LYS   A NZ  
881  N  NZ  B LYS   A 31  ? 0.3166 0.3187 0.3166 -0.0035 -0.0586 -0.0458 31  LYS   A NZ  
908  N  N   A PRO   A 32  ? 0.2246 0.2273 0.0877 -0.0644 -0.0030 0.0416  32  PRO   A N   
909  N  N   B PRO   A 32  ? 0.2344 0.2477 0.1514 -0.0055 -0.0204 0.0212  32  PRO   A N   
910  C  CA  A PRO   A 32  ? 0.2283 0.2229 0.1066 -0.0671 -0.0080 0.0551  32  PRO   A CA  
911  C  CA  B PRO   A 32  ? 0.2240 0.2410 0.1482 -0.0061 -0.0200 0.0281  32  PRO   A CA  
912  C  C   A PRO   A 32  ? 0.2265 0.2209 0.1173 -0.0574 -0.0157 0.0563  32  PRO   A C   
913  C  C   B PRO   A 32  ? 0.2165 0.2331 0.1389 -0.0067 -0.0306 0.0376  32  PRO   A C   
914  O  O   A PRO   A 32  ? 0.2230 0.2168 0.1133 -0.0658 -0.0272 0.0447  32  PRO   A O   
915  O  O   B PRO   A 32  ? 0.2117 0.2312 0.1525 -0.0076 -0.0409 0.0355  32  PRO   A O   
916  C  CB  A PRO   A 32  ? 0.2214 0.2256 0.1205 -0.0629 -0.0111 0.0400  32  PRO   A CB  
917  C  CB  B PRO   A 32  ? 0.2206 0.2447 0.1541 -0.0025 -0.0152 0.0197  32  PRO   A CB  
918  C  CG  A PRO   A 32  ? 0.2160 0.2273 0.0819 -0.0618 -0.0177 0.0289  32  PRO   A CG  
919  C  CG  B PRO   A 32  ? 0.2219 0.2471 0.1450 -0.0007 -0.0175 0.0119  32  PRO   A CG  
920  C  CD  A PRO   A 32  ? 0.2121 0.2199 0.0815 -0.0661 -0.0145 0.0356  32  PRO   A CD  
921  C  CD  B PRO   A 32  ? 0.2247 0.2468 0.1483 -0.0038 -0.0184 0.0158  32  PRO   A CD  
936  N  N   A THR   A 33  ? 0.2312 0.2254 0.1258 -0.0486 -0.0186 0.0591  33  THR   A N   
937  N  N   B THR   A 33  ? 0.2153 0.2283 0.1300 -0.0089 -0.0337 0.0466  33  THR   A N   
938  C  CA  A THR   A 33  ? 0.2297 0.2286 0.1373 -0.0332 -0.0324 0.0581  33  THR   A CA  
939  C  CA  B THR   A 33  ? 0.2121 0.2222 0.1237 -0.0100 -0.0408 0.0552  33  THR   A CA  
940  C  C   A THR   A 33  ? 0.2077 0.2079 0.1261 -0.0304 -0.0298 0.0444  33  THR   A C   
941  C  C   B THR   A 33  ? 0.1997 0.2011 0.1260 -0.0201 -0.0303 0.0454  33  THR   A C   
942  O  O   A THR   A 33  ? 0.2009 0.1996 0.1222 -0.0298 -0.0418 0.0422  33  THR   A O   
943  O  O   B THR   A 33  ? 0.1979 0.1887 0.1424 -0.0233 -0.0257 0.0402  33  THR   A O   
944  C  CB  A THR   A 33  ? 0.2504 0.2509 0.1671 -0.0240 -0.0445 0.0745  33  THR   A CB  
945  C  CB  B THR   A 33  ? 0.2240 0.2378 0.1396 -0.0058 -0.0410 0.0693  33  THR   A CB  
946  O  OG1 A THR   A 33  ? 0.2655 0.2639 0.1942 -0.0179 -0.0346 0.0834  33  THR   A OG1 
947  O  OG1 B THR   A 33  ? 0.2308 0.2473 0.1474 -0.0022 -0.0427 0.0825  33  THR   A OG1 
948  C  CG2 A THR   A 33  ? 0.2577 0.2586 0.1897 -0.0213 -0.0483 0.0736  33  THR   A CG2 
949  C  CG2 B THR   A 33  ? 0.2278 0.2435 0.1536 -0.0057 -0.0364 0.0675  33  THR   A CG2 
964  N  N   . VAL   A 34  ? 0.1926 0.1960 0.1134 -0.0309 -0.0305 0.0453  34  VAL   A N   
965  C  CA  . VAL   A 34  ? 0.1684 0.1782 0.1076 -0.0288 -0.0244 0.0365  34  VAL   A CA  
966  C  C   . VAL   A 34  ? 0.1590 0.1682 0.0989 -0.0226 -0.0094 0.0283  34  VAL   A C   
967  O  O   . VAL   A 34  ? 0.1559 0.1710 0.1382 -0.0286 -0.0089 0.0378  34  VAL   A O   
968  C  CB  . VAL   A 34  ? 0.1735 0.1785 0.1363 -0.0264 -0.0150 0.0283  34  VAL   A CB  
969  C  CG1 . VAL   A 34  ? 0.1798 0.1814 0.1324 -0.0249 0.0041  0.0210  34  VAL   A CG1 
970  C  CG2 . VAL   A 34  ? 0.1771 0.1918 0.1661 -0.0165 -0.0233 0.0320  34  VAL   A CG2 
981  N  N   . VAL   A 35  ? 0.1446 0.1523 0.1032 -0.0250 -0.0126 0.0295  35  VAL   A N   
982  C  CA  . VAL   A 35  ? 0.1421 0.1513 0.0978 -0.0212 -0.0047 0.0217  35  VAL   A CA  
983  C  C   . VAL   A 35  ? 0.1322 0.1393 0.0993 -0.0164 -0.0052 0.0221  35  VAL   A C   
984  O  O   . VAL   A 35  ? 0.1242 0.1523 0.1270 -0.0243 0.0056  0.0128  35  VAL   A O   
985  C  CB  . VAL   A 35  ? 0.1476 0.1553 0.1168 -0.0121 0.0051  0.0102  35  VAL   A CB  
986  C  CG1 . VAL   A 35  ? 0.1524 0.1665 0.1330 -0.0096 -0.0009 0.0098  35  VAL   A CG1 
987  C  CG2 . VAL   A 35  ? 0.1462 0.1550 0.1382 -0.0092 0.0136  0.0079  35  VAL   A CG2 
997  N  N   . VAL   A 36  ? 0.1218 0.1378 0.0917 -0.0153 -0.0032 0.0225  36  VAL   A N   
998  C  CA  . VAL   A 36  ? 0.1185 0.1240 0.0918 -0.0080 0.0006  0.0112  36  VAL   A CA  
999  C  C   . VAL   A 36  ? 0.1142 0.1265 0.1030 -0.0144 0.0018  0.0126  36  VAL   A C   
1000 O  O   . VAL   A 36  ? 0.1187 0.1291 0.1271 -0.0051 0.0135  0.0178  36  VAL   A O   
1001 C  CB  . VAL   A 36  ? 0.1197 0.1192 0.1090 -0.0108 0.0030  0.0211  36  VAL   A CB  
1002 C  CG1 . VAL   A 36  ? 0.1269 0.1200 0.1274 -0.0145 -0.0022 0.0081  36  VAL   A CG1 
1003 C  CG2 . VAL   A 36  ? 0.1271 0.1262 0.1326 -0.0068 -0.0049 0.0273  36  VAL   A CG2 
1013 N  N   . ASN   A 37  ? 0.1100 0.1213 0.1049 -0.0038 0.0037  0.0175  37  ASN   A N   
1014 C  CA  . ASN   A 37  ? 0.1119 0.1170 0.1006 0.0032  0.0030  0.0229  37  ASN   A CA  
1015 C  C   . ASN   A 37  ? 0.1114 0.1172 0.1012 0.0009  0.0105  0.0281  37  ASN   A C   
1016 O  O   . ASN   A 37  ? 0.1263 0.1282 0.1067 0.0070  0.0103  0.0165  37  ASN   A O   
1017 C  CB  . ASN   A 37  ? 0.1170 0.1214 0.1154 0.0024  0.0019  0.0187  37  ASN   A CB  
1018 C  CG  . ASN   A 37  ? 0.1165 0.1201 0.1199 0.0018  0.0076  0.0129  37  ASN   A CG  
1019 O  OD1 . ASN   A 37  ? 0.1139 0.1205 0.1465 -0.0005 0.0064  0.0212  37  ASN   A OD1 
1020 N  ND2 . ASN   A 37  ? 0.1161 0.1183 0.1339 -0.0038 0.0020  0.0303  37  ASN   A ND2 
1027 N  N   A ALA   A 38  ? 0.1108 0.1225 0.1072 -0.0033 0.0116  0.0143  38  ALA   A N   
1028 N  N   B ALA   A 38  ? 0.1161 0.1224 0.1066 0.0014  0.0035  0.0187  38  ALA   A N   
1029 C  CA  A ALA   A 38  ? 0.1173 0.1277 0.1058 -0.0091 0.0122  0.0087  38  ALA   A CA  
1030 C  CA  B ALA   A 38  ? 0.1236 0.1285 0.1139 0.0011  -0.0027 0.0142  38  ALA   A CA  
1031 C  C   A ALA   A 38  ? 0.1207 0.1261 0.1024 -0.0033 0.0036  0.0012  38  ALA   A C   
1032 C  C   B ALA   A 38  ? 0.1205 0.1278 0.1061 0.0026  -0.0047 0.0090  38  ALA   A C   
1033 O  O   A ALA   A 38  ? 0.1218 0.1177 0.1042 -0.0023 -0.0052 -0.0013 38  ALA   A O   
1034 O  O   B ALA   A 38  ? 0.1171 0.1285 0.1153 0.0020  -0.0174 0.0183  38  ALA   A O   
1035 C  CB  A ALA   A 38  ? 0.1189 0.1479 0.1125 -0.0153 0.0006  0.0020  38  ALA   A CB  
1036 C  CB  B ALA   A 38  ? 0.1298 0.1396 0.1303 0.0025  -0.0110 0.0057  38  ALA   A CB  
1047 N  N   . ALA   A 39  ? 0.1214 0.1255 0.1144 -0.0014 0.0078  0.0166  39  ALA   A N   
1048 C  CA  . ALA   A 39  ? 0.1267 0.1262 0.1137 -0.0006 0.0111  0.0051  39  ALA   A CA  
1049 C  C   . ALA   A 39  ? 0.1208 0.1224 0.1199 -0.0008 0.0062  0.0088  39  ALA   A C   
1050 O  O   . ALA   A 39  ? 0.1296 0.1260 0.1255 -0.0069 0.0077  0.0068  39  ALA   A O   
1051 C  CB  . ALA   A 39  ? 0.1271 0.1474 0.1298 -0.0040 -0.0041 0.0046  39  ALA   A CB  
1058 N  N   A ASN   A 40  ? 0.1303 0.1260 0.1217 -0.0061 0.0181  0.0048  40  ASN   A N   
1059 N  N   B ASN   A 40  ? 0.1315 0.1201 0.1210 -0.0051 0.0184  0.0123  40  ASN   A N   
1060 C  CA  A ASN   A 40  ? 0.1275 0.1229 0.1170 -0.0037 0.0097  0.0021  40  ASN   A CA  
1061 C  CA  B ASN   A 40  ? 0.1301 0.1160 0.1285 -0.0028 0.0109  0.0153  40  ASN   A CA  
1062 C  C   A ASN   A 40  ? 0.1262 0.1153 0.0898 -0.0038 0.0113  0.0122  40  ASN   A C   
1063 C  C   B ASN   A 40  ? 0.1313 0.1117 0.1177 -0.0029 0.0077  0.0214  40  ASN   A C   
1064 O  O   A ASN   A 40  ? 0.1284 0.1200 0.0929 -0.0045 0.0143  0.0129  40  ASN   A O   
1065 O  O   B ASN   A 40  ? 0.1352 0.1100 0.1289 -0.0050 0.0043  0.0209  40  ASN   A O   
1066 C  CB  A ASN   A 40  ? 0.1399 0.1288 0.1295 0.0054  0.0017  0.0072  40  ASN   A CB  
1067 C  CB  B ASN   A 40  ? 0.1380 0.1193 0.1422 -0.0048 0.0099  0.0153  40  ASN   A CB  
1068 C  CG  A ASN   A 40  ? 0.1564 0.1336 0.1340 0.0100  0.0016  0.0099  40  ASN   A CG  
1069 C  CG  B ASN   A 40  ? 0.1443 0.1286 0.1656 -0.0075 0.0107  0.0121  40  ASN   A CG  
1070 O  OD1 A ASN   A 40  ? 0.1691 0.1302 0.1442 0.0058  -0.0027 0.0105  40  ASN   A OD1 
1071 O  OD1 B ASN   A 40  ? 0.1481 0.1277 0.1723 -0.0160 0.0093  0.0141  40  ASN   A OD1 
1072 N  ND2 A ASN   A 40  ? 0.1613 0.1467 0.1422 0.0121  0.0042  -0.0044 40  ASN   A ND2 
1073 N  ND2 B ASN   A 40  ? 0.1455 0.1453 0.1802 -0.0073 0.0240  -0.0014 40  ASN   A ND2 
1086 N  N   A VAL   A 41  ? 0.1231 0.1214 0.0941 -0.0009 0.0078  0.0139  41  VAL   A N   
1087 N  N   B VAL   A 41  ? 0.1319 0.1180 0.1172 -0.0010 -0.0007 0.0276  41  VAL   A N   
1088 C  CA  A VAL   A 41  ? 0.1253 0.1232 0.1091 0.0005  0.0093  0.0168  41  VAL   A CA  
1089 C  CA  B VAL   A 41  ? 0.1377 0.1251 0.1215 -0.0039 0.0050  0.0295  41  VAL   A CA  
1090 C  C   A VAL   A 41  ? 0.1197 0.1188 0.1093 0.0047  0.0139  0.0132  41  VAL   A C   
1091 C  C   B VAL   A 41  ? 0.1398 0.1257 0.1199 -0.0072 0.0116  0.0228  41  VAL   A C   
1092 O  O   A VAL   A 41  ? 0.1279 0.1137 0.1214 0.0055  0.0020  0.0060  41  VAL   A O   
1093 O  O   B VAL   A 41  ? 0.1472 0.1184 0.1112 -0.0085 0.0035  0.0178  41  VAL   A O   
1094 C  CB  A VAL   A 41  ? 0.1235 0.1305 0.1028 -0.0014 0.0151  0.0124  41  VAL   A CB  
1095 C  CB  B VAL   A 41  ? 0.1446 0.1402 0.1349 -0.0045 0.0087  0.0323  41  VAL   A CB  
1096 C  CG1 A VAL   A 41  ? 0.1310 0.1368 0.1213 0.0035  0.0081  0.0048  41  VAL   A CG1 
1097 C  CG1 B VAL   A 41  ? 0.1542 0.1448 0.1461 -0.0075 0.0118  0.0266  41  VAL   A CG1 
1098 C  CG2 A VAL   A 41  ? 0.1314 0.1340 0.1048 -0.0021 0.0224  0.0077  41  VAL   A CG2 
1099 C  CG2 B VAL   A 41  ? 0.1470 0.1488 0.1371 -0.0050 -0.0030 0.0245  41  VAL   A CG2 
1118 N  N   A TYR   A 42  ? 0.1123 0.1142 0.1322 -0.0052 0.0170  0.0151  42  TYR   A N   
1119 N  N   B TYR   A 42  ? 0.1322 0.1292 0.1345 -0.0066 0.0226  0.0276  42  TYR   A N   
1120 C  CA  A TYR   A 42  ? 0.1212 0.1083 0.1412 -0.0074 0.0155  0.0200  42  TYR   A CA  
1121 C  CA  B TYR   A 42  ? 0.1322 0.1349 0.1259 -0.0036 0.0232  0.0363  42  TYR   A CA  
1122 C  C   A TYR   A 42  ? 0.1124 0.1042 0.1555 -0.0031 0.0117  0.0169  42  TYR   A C   
1123 C  C   B TYR   A 42  ? 0.1313 0.1368 0.1033 -0.0070 0.0226  0.0480  42  TYR   A C   
1124 O  O   A TYR   A 42  ? 0.1145 0.1065 0.1748 -0.0122 0.0095  -0.0065 42  TYR   A O   
1125 O  O   B TYR   A 42  ? 0.1312 0.1436 0.1226 -0.0128 0.0196  0.0379  42  TYR   A O   
1126 C  CB  A TYR   A 42  ? 0.1350 0.1192 0.1283 -0.0047 0.0267  0.0292  42  TYR   A CB  
1127 C  CB  B TYR   A 42  ? 0.1409 0.1410 0.1372 0.0024  0.0206  0.0406  42  TYR   A CB  
1128 C  CG  A TYR   A 42  ? 0.1520 0.1295 0.1232 -0.0097 0.0152  0.0405  42  TYR   A CG  
1129 C  CG  B TYR   A 42  ? 0.1563 0.1485 0.1413 0.0077  0.0104  0.0410  42  TYR   A CG  
1130 C  CD1 A TYR   A 42  ? 0.1669 0.1475 0.1342 -0.0228 0.0209  0.0281  42  TYR   A CD1 
1131 C  CD1 B TYR   A 42  ? 0.1661 0.1571 0.1316 0.0021  0.0128  0.0434  42  TYR   A CD1 
1132 C  CD2 A TYR   A 42  ? 0.1637 0.1522 0.1513 -0.0042 0.0047  0.0257  42  TYR   A CD2 
1133 C  CD2 B TYR   A 42  ? 0.1709 0.1626 0.1574 0.0120  0.0077  0.0320  42  TYR   A CD2 
1134 C  CE1 A TYR   A 42  ? 0.1790 0.1579 0.1365 -0.0215 0.0228  0.0211  42  TYR   A CE1 
1135 C  CE1 B TYR   A 42  ? 0.1732 0.1630 0.1306 0.0027  0.0144  0.0367  42  TYR   A CE1 
1136 C  CE2 A TYR   A 42  ? 0.1785 0.1690 0.1650 -0.0132 0.0018  0.0233  42  TYR   A CE2 
1137 C  CE2 B TYR   A 42  ? 0.1832 0.1732 0.1609 0.0102  0.0071  0.0321  42  TYR   A CE2 
1138 C  CZ  A TYR   A 42  ? 0.1914 0.1683 0.1474 -0.0231 0.0219  0.0233  42  TYR   A CZ  
1139 C  CZ  B TYR   A 42  ? 0.1850 0.1721 0.1376 0.0026  0.0153  0.0297  42  TYR   A CZ  
1140 O  OH  A TYR   A 42  ? 0.2118 0.1836 0.1690 -0.0287 0.0200  0.0180  42  TYR   A OH  
1141 O  OH  B TYR   A 42  ? 0.1943 0.1836 0.1460 -0.0022 0.0153  0.0188  42  TYR   A OH  
1160 N  N   A LEU   A 43  ? 0.1179 0.1077 0.1514 -0.0051 0.0059  -0.0071 43  LEU   A N   
1161 N  N   B LEU   A 43  ? 0.1276 0.1346 0.1005 -0.0040 0.0152  0.0394  43  LEU   A N   
1162 C  CA  A LEU   A 43  ? 0.1126 0.1104 0.1436 -0.0059 0.0095  -0.0047 43  LEU   A CA  
1163 C  CA  B LEU   A 43  ? 0.1243 0.1315 0.1087 -0.0059 0.0079  0.0308  43  LEU   A CA  
1164 C  C   A LEU   A 43  ? 0.1166 0.1164 0.1447 -0.0025 0.0045  -0.0020 43  LEU   A C   
1165 C  C   B LEU   A 43  ? 0.1273 0.1337 0.1134 -0.0026 -0.0031 0.0205  43  LEU   A C   
1166 O  O   A LEU   A 43  ? 0.1329 0.1152 0.1661 0.0067  -0.0079 0.0050  43  LEU   A O   
1167 O  O   B LEU   A 43  ? 0.1364 0.1361 0.1153 -0.0031 -0.0135 0.0118  43  LEU   A O   
1168 C  CB  A LEU   A 43  ? 0.1220 0.1118 0.1477 -0.0073 0.0046  0.0005  43  LEU   A CB  
1169 C  CB  B LEU   A 43  ? 0.1194 0.1262 0.1275 -0.0082 0.0027  0.0300  43  LEU   A CB  
1170 C  CG  A LEU   A 43  ? 0.1263 0.1162 0.1520 -0.0014 0.0066  0.0002  43  LEU   A CG  
1171 C  CG  B LEU   A 43  ? 0.1165 0.1243 0.1461 -0.0030 0.0037  0.0274  43  LEU   A CG  
1172 C  CD1 A LEU   A 43  ? 0.1341 0.1249 0.1632 -0.0003 -0.0064 0.0011  43  LEU   A CD1 
1173 C  CD1 B LEU   A 43  ? 0.1185 0.1292 0.1558 -0.0058 -0.0048 0.0267  43  LEU   A CD1 
1174 C  CD2 A LEU   A 43  ? 0.1354 0.1184 0.1556 -0.0008 0.0058  0.0027  43  LEU   A CD2 
1175 C  CD2 B LEU   A 43  ? 0.1249 0.1189 0.1536 0.0019  -0.0019 0.0349  43  LEU   A CD2 
1198 N  N   A LYS   A 44  ? 0.1247 0.1099 0.1340 -0.0065 0.0141  0.0047  44  LYS   A N   
1199 N  N   B LYS   A 44  ? 0.1280 0.1290 0.1202 0.0021  -0.0059 0.0245  44  LYS   A N   
1200 C  CA  A LYS   A 44  ? 0.1381 0.1177 0.1391 -0.0115 0.0183  0.0125  44  LYS   A CA  
1201 C  CA  B LYS   A 44  ? 0.1378 0.1309 0.1222 0.0034  -0.0043 0.0251  44  LYS   A CA  
1202 C  C   A LYS   A 44  ? 0.1274 0.1227 0.1244 -0.0005 -0.0003 0.0121  44  LYS   A C   
1203 C  C   B LYS   A 44  ? 0.1288 0.1253 0.1019 0.0059  -0.0048 0.0200  44  LYS   A C   
1204 O  O   A LYS   A 44  ? 0.1273 0.1359 0.1488 0.0037  0.0026  0.0003  44  LYS   A O   
1205 O  O   B LYS   A 44  ? 0.1359 0.1331 0.1029 0.0055  0.0060  0.0003  44  LYS   A O   
1206 C  CB  A LYS   A 44  ? 0.1625 0.1320 0.1620 -0.0122 0.0307  0.0259  44  LYS   A CB  
1207 C  CB  B LYS   A 44  ? 0.1571 0.1485 0.1729 0.0112  0.0057  0.0269  44  LYS   A CB  
1208 C  CG  A LYS   A 44  ? 0.1927 0.1532 0.2230 -0.0190 0.0501  0.0381  44  LYS   A CG  
1209 C  CG  B LYS   A 44  ? 0.1754 0.1773 0.2397 0.0146  0.0124  0.0325  44  LYS   A CG  
1210 C  CD  A LYS   A 44  ? 0.2272 0.1958 0.3239 -0.0206 0.0520  0.0269  44  LYS   A CD  
1211 C  CD  B LYS   A 44  ? 0.1973 0.2127 0.3177 0.0091  0.0073  0.0287  44  LYS   A CD  
1212 C  CE  A LYS   A 44  ? 0.2412 0.2229 0.3887 -0.0113 0.0533  0.0171  44  LYS   A CE  
1213 C  CE  B LYS   A 44  ? 0.2016 0.2302 0.3643 0.0045  0.0048  0.0298  44  LYS   A CE  
1214 N  NZ  A LYS   A 44  ? 0.2450 0.2409 0.4172 -0.0054 0.0531  0.0136  44  LYS   A NZ  
1215 N  NZ  B LYS   A 44  ? 0.2086 0.2452 0.3933 -0.0064 0.0065  0.0270  44  LYS   A NZ  
1242 N  N   . HIS   A 45  ? 0.1197 0.1187 0.1191 0.0007  -0.0036 0.0186  45  HIS   A N   
1243 C  CA  . HIS   A 45  ? 0.1179 0.1159 0.1297 -0.0007 -0.0022 0.0117  45  HIS   A CA  
1244 C  C   . HIS   A 45  ? 0.1227 0.1302 0.1379 0.0022  0.0010  0.0145  45  HIS   A C   
1245 O  O   . HIS   A 45  ? 0.1427 0.1454 0.1640 0.0231  -0.0045 -0.0081 45  HIS   A O   
1246 C  CB  . HIS   A 45  ? 0.1185 0.1167 0.1292 -0.0015 0.0018  0.0058  45  HIS   A CB  
1247 C  CG  . HIS   A 45  ? 0.1137 0.1154 0.1237 -0.0079 0.0050  0.0131  45  HIS   A CG  
1248 N  ND1 . HIS   A 45  ? 0.1105 0.1198 0.1365 -0.0063 -0.0054 0.0149  45  HIS   A ND1 
1249 C  CD2 . HIS   A 45  ? 0.1144 0.1199 0.1318 -0.0114 -0.0080 0.0168  45  HIS   A CD2 
1250 C  CE1 . HIS   A 45  ? 0.1134 0.1251 0.1186 -0.0099 0.0007  0.0203  45  HIS   A CE1 
1251 N  NE2 . HIS   A 45  ? 0.1135 0.1281 0.1277 -0.0047 -0.0013 0.0194  45  HIS   A NE2 
1260 N  N   A GLY   A 46  ? 0.1385 0.1319 0.1539 0.0098  -0.0155 0.0179  46  GLY   A N   
1261 N  N   B GLY   A 46  ? 0.1322 0.1347 0.1398 0.0089  -0.0091 0.0144  46  GLY   A N   
1262 C  CA  A GLY   A 46  ? 0.1437 0.1394 0.1764 0.0097  -0.0180 0.0207  46  GLY   A CA  
1263 C  CA  B GLY   A 46  ? 0.1340 0.1408 0.1424 0.0107  -0.0106 0.0154  46  GLY   A CA  
1264 C  C   A GLY   A 46  ? 0.1461 0.1360 0.1704 0.0181  -0.0289 0.0313  46  GLY   A C   
1265 C  C   B GLY   A 46  ? 0.1336 0.1377 0.1256 0.0195  -0.0220 0.0189  46  GLY   A C   
1266 O  O   A GLY   A 46  ? 0.1486 0.1431 0.1952 0.0141  -0.0478 0.0113  46  GLY   A O   
1267 O  O   B GLY   A 46  ? 0.1323 0.1461 0.1434 0.0235  -0.0258 0.0051  46  GLY   A O   
1274 N  N   A GLY   A 47  ? 0.1465 0.1386 0.1550 0.0203  -0.0186 0.0154  47  GLY   A N   
1275 N  N   B GLY   A 47  ? 0.1361 0.1371 0.1137 0.0166  -0.0171 0.0075  47  GLY   A N   
1276 C  CA  A GLY   A 47  ? 0.1452 0.1414 0.1425 0.0202  -0.0229 0.0006  47  GLY   A CA  
1277 C  CA  B GLY   A 47  ? 0.1374 0.1364 0.1027 0.0182  -0.0281 0.0047  47  GLY   A CA  
1278 C  C   A GLY   A 47  ? 0.1362 0.1356 0.1384 0.0204  -0.0337 -0.0068 47  GLY   A C   
1279 C  C   B GLY   A 47  ? 0.1369 0.1330 0.1010 0.0216  -0.0184 -0.0052 47  GLY   A C   
1280 O  O   A GLY   A 47  ? 0.1326 0.1310 0.1581 0.0181  -0.0316 -0.0002 47  GLY   A O   
1281 O  O   B GLY   A 47  ? 0.1377 0.1293 0.0976 0.0237  -0.0176 0.0064  47  GLY   A O   
1288 N  N   A GLY   A 48  ? 0.1368 0.1345 0.1360 0.0201  -0.0352 -0.0030 48  GLY   A N   
1289 N  N   B GLY   A 48  ? 0.1382 0.1355 0.1221 0.0124  -0.0200 -0.0048 48  GLY   A N   
1290 C  CA  A GLY   A 48  ? 0.1376 0.1312 0.1714 0.0071  -0.0271 -0.0041 48  GLY   A CA  
1291 C  CA  B GLY   A 48  ? 0.1326 0.1282 0.1297 0.0042  -0.0186 -0.0105 48  GLY   A CA  
1292 C  C   A GLY   A 48  ? 0.1242 0.1266 0.1527 -0.0004 -0.0162 -0.0016 48  GLY   A C   
1293 C  C   B GLY   A 48  ? 0.1230 0.1290 0.1268 -0.0042 -0.0054 -0.0023 48  GLY   A C   
1294 O  O   A GLY   A 48  ? 0.1374 0.1231 0.1467 -0.0044 -0.0009 0.0063  48  GLY   A O   
1295 O  O   B GLY   A 48  ? 0.1381 0.1292 0.1251 -0.0071 0.0065  -0.0008 48  GLY   A O   
1302 N  N   A VAL   A 49  ? 0.1169 0.1217 0.1579 -0.0057 -0.0141 -0.0049 49  VAL   A N   
1303 N  N   B VAL   A 49  ? 0.1091 0.1262 0.1313 -0.0071 -0.0046 0.0001  49  VAL   A N   
1304 C  CA  A VAL   A 49  ? 0.1277 0.1200 0.1513 -0.0039 0.0023  -0.0041 49  VAL   A CA  
1305 C  CA  B VAL   A 49  ? 0.1052 0.1275 0.1258 -0.0053 0.0040  0.0095  49  VAL   A CA  
1306 C  C   A VAL   A 49  ? 0.1272 0.1134 0.1292 -0.0043 0.0002  0.0014  49  VAL   A C   
1307 C  C   B VAL   A 49  ? 0.1083 0.1192 0.0958 0.0017  0.0089  0.0064  49  VAL   A C   
1308 O  O   A VAL   A 49  ? 0.1305 0.1223 0.1341 -0.0090 0.0061  -0.0002 49  VAL   A O   
1309 O  O   B VAL   A 49  ? 0.1126 0.1201 0.0935 0.0027  0.0123  0.0031  49  VAL   A O   
1310 C  CB  A VAL   A 49  ? 0.1439 0.1216 0.1582 -0.0063 0.0059  -0.0144 49  VAL   A CB  
1311 C  CB  B VAL   A 49  ? 0.0985 0.1225 0.1298 0.0001  0.0039  0.0084  49  VAL   A CB  
1312 C  CG1 A VAL   A 49  ? 0.1432 0.1085 0.1606 -0.0007 0.0171  -0.0045 49  VAL   A CG1 
1313 C  CG1 B VAL   A 49  ? 0.0968 0.1176 0.1225 0.0035  0.0103  0.0138  49  VAL   A CG1 
1314 C  CG2 A VAL   A 49  ? 0.1549 0.1307 0.2032 -0.0205 0.0042  -0.0145 49  VAL   A CG2 
1315 C  CG2 B VAL   A 49  ? 0.1007 0.1230 0.1272 0.0065  0.0115  0.0011  49  VAL   A CG2 
1334 N  N   A ALA   A 50  ? 0.1198 0.1122 0.1309 -0.0074 -0.0165 0.0074  50  ALA   A N   
1335 N  N   B ALA   A 50  ? 0.1113 0.1181 0.0909 0.0035  0.0044  0.0086  50  ALA   A N   
1336 C  CA  A ALA   A 50  ? 0.1143 0.1135 0.1273 -0.0136 -0.0085 0.0146  50  ALA   A CA  
1337 C  CA  B ALA   A 50  ? 0.1146 0.1153 0.0944 -0.0022 -0.0004 0.0113  50  ALA   A CA  
1338 C  C   A ALA   A 50  ? 0.1136 0.1160 0.1214 -0.0117 -0.0127 0.0072  50  ALA   A C   
1339 C  C   B ALA   A 50  ? 0.1171 0.1173 0.0987 -0.0010 -0.0048 0.0058  50  ALA   A C   
1340 O  O   A ALA   A 50  ? 0.1086 0.1195 0.1351 -0.0061 -0.0096 0.0049  50  ALA   A O   
1341 O  O   B ALA   A 50  ? 0.1155 0.1198 0.1057 0.0033  -0.0035 0.0035  50  ALA   A O   
1342 C  CB  A ALA   A 50  ? 0.1141 0.1149 0.1290 -0.0083 -0.0096 0.0025  50  ALA   A CB  
1343 C  CB  B ALA   A 50  ? 0.1196 0.1100 0.0892 0.0042  0.0042  0.0002  50  ALA   A CB  
1354 N  N   A GLY   A 51  ? 0.1202 0.1084 0.1273 -0.0027 -0.0134 0.0053  51  GLY   A N   
1355 N  N   B GLY   A 51  ? 0.1216 0.1146 0.1108 0.0019  -0.0114 0.0021  51  GLY   A N   
1356 C  CA  A GLY   A 51  ? 0.1290 0.1103 0.1366 0.0038  -0.0154 0.0079  51  GLY   A CA  
1357 C  CA  B GLY   A 51  ? 0.1279 0.1170 0.1196 0.0041  -0.0145 0.0011  51  GLY   A CA  
1358 C  C   A GLY   A 51  ? 0.1181 0.1158 0.1323 0.0063  -0.0072 -0.0050 51  GLY   A C   
1359 C  C   B GLY   A 51  ? 0.1216 0.1215 0.1225 0.0039  -0.0092 -0.0071 51  GLY   A C   
1360 O  O   A GLY   A 51  ? 0.1220 0.1247 0.1445 0.0003  -0.0061 -0.0081 51  GLY   A O   
1361 O  O   B GLY   A 51  ? 0.1252 0.1272 0.1279 0.0008  -0.0096 -0.0105 51  GLY   A O   
1368 N  N   . ALA   A 52  ? 0.1201 0.1284 0.1251 -0.0012 -0.0057 -0.0091 52  ALA   A N   
1369 C  CA  . ALA   A 52  ? 0.1173 0.1396 0.1456 -0.0055 0.0032  -0.0154 52  ALA   A CA  
1370 C  C   . ALA   A 52  ? 0.1163 0.1339 0.1225 -0.0123 0.0027  -0.0126 52  ALA   A C   
1371 O  O   . ALA   A 52  ? 0.1281 0.1444 0.1339 -0.0078 0.0057  -0.0124 52  ALA   A O   
1372 C  CB  . ALA   A 52  ? 0.1270 0.1693 0.1667 -0.0119 0.0004  -0.0045 52  ALA   A CB  
1379 N  N   A LEU   A 53  ? 0.1156 0.1284 0.1144 -0.0097 0.0003  -0.0004 53  LEU   A N   
1380 N  N   B LEU   A 53  ? 0.1117 0.1307 0.1194 -0.0057 -0.0014 -0.0038 53  LEU   A N   
1381 C  CA  A LEU   A 53  ? 0.1313 0.1317 0.1124 -0.0093 0.0021  0.0071  53  LEU   A CA  
1382 C  CA  B LEU   A 53  ? 0.1179 0.1326 0.1197 -0.0006 -0.0023 0.0016  53  LEU   A CA  
1383 C  C   A LEU   A 53  ? 0.1302 0.1382 0.0906 -0.0036 0.0077  0.0036  53  LEU   A C   
1384 C  C   B LEU   A 53  ? 0.1201 0.1382 0.1088 0.0089  -0.0019 -0.0027 53  LEU   A C   
1385 O  O   A LEU   A 53  ? 0.1394 0.1501 0.1037 -0.0216 0.0055  0.0078  53  LEU   A O   
1386 O  O   B LEU   A 53  ? 0.1270 0.1438 0.1266 0.0008  0.0002  -0.0015 53  LEU   A O   
1387 C  CB  A LEU   A 53  ? 0.1377 0.1378 0.1236 -0.0121 0.0004  0.0105  53  LEU   A CB  
1388 C  CB  B LEU   A 53  ? 0.1155 0.1326 0.1232 -0.0036 -0.0047 0.0062  53  LEU   A CB  
1389 C  CG  A LEU   A 53  ? 0.1364 0.1390 0.1384 -0.0089 -0.0036 0.0115  53  LEU   A CG  
1390 C  CG  B LEU   A 53  ? 0.1102 0.1286 0.1198 -0.0055 -0.0097 0.0111  53  LEU   A CG  
1391 C  CD1 A LEU   A 53  ? 0.1358 0.1481 0.1409 -0.0085 0.0048  0.0177  53  LEU   A CD1 
1392 C  CD1 B LEU   A 53  ? 0.1131 0.1360 0.1206 -0.0106 -0.0005 0.0061  53  LEU   A CD1 
1393 C  CD2 A LEU   A 53  ? 0.1367 0.1543 0.1457 -0.0130 -0.0021 0.0167  53  LEU   A CD2 
1394 C  CD2 B LEU   A 53  ? 0.1124 0.1271 0.1190 -0.0030 -0.0066 0.0049  53  LEU   A CD2 
1417 N  N   A ASN   A 54  ? 0.1236 0.1290 0.1024 -0.0059 0.0003  0.0085  54  ASN   A N   
1418 N  N   B ASN   A 54  ? 0.1204 0.1345 0.0996 0.0131  -0.0117 -0.0021 54  ASN   A N   
1419 C  CA  A ASN   A 54  ? 0.1139 0.1208 0.1284 -0.0118 0.0022  0.0031  54  ASN   A CA  
1420 C  CA  B ASN   A 54  ? 0.1162 0.1312 0.0943 0.0139  -0.0159 -0.0082 54  ASN   A CA  
1421 C  C   A ASN   A 54  ? 0.1192 0.1236 0.1371 -0.0199 0.0118  0.0062  54  ASN   A C   
1422 C  C   B ASN   A 54  ? 0.1242 0.1328 0.0866 0.0088  -0.0110 -0.0128 54  ASN   A C   
1423 O  O   A ASN   A 54  ? 0.1201 0.1307 0.1475 -0.0200 0.0040  0.0004  54  ASN   A O   
1424 O  O   B ASN   A 54  ? 0.1203 0.1364 0.0720 0.0089  -0.0132 -0.0155 54  ASN   A O   
1425 C  CB  A ASN   A 54  ? 0.1172 0.1174 0.1369 -0.0171 -0.0060 -0.0028 54  ASN   A CB  
1426 C  CB  B ASN   A 54  ? 0.1156 0.1311 0.0885 0.0163  -0.0176 -0.0062 54  ASN   A CB  
1427 C  CG  A ASN   A 54  ? 0.1141 0.1174 0.1478 -0.0148 0.0008  0.0019  54  ASN   A CG  
1428 C  CG  B ASN   A 54  ? 0.1101 0.1262 0.0834 0.0177  -0.0053 -0.0136 54  ASN   A CG  
1429 O  OD1 A ASN   A 54  ? 0.1142 0.1219 0.1593 -0.0155 -0.0086 0.0171  54  ASN   A OD1 
1430 O  OD1 B ASN   A 54  ? 0.1099 0.1167 0.0871 0.0161  -0.0080 -0.0262 54  ASN   A OD1 
1431 N  ND2 A ASN   A 54  ? 0.1174 0.1194 0.1624 -0.0122 -0.0005 0.0037  54  ASN   A ND2 
1432 N  ND2 B ASN   A 54  ? 0.1133 0.1292 0.1001 0.0136  -0.0086 0.0011  54  ASN   A ND2 
1445 N  N   A LYS   A 55  ? 0.1167 0.1268 0.1418 -0.0148 0.0037  -0.0046 55  LYS   A N   
1446 N  N   B LYS   A 55  ? 0.1270 0.1304 0.1006 0.0083  -0.0093 -0.0198 55  LYS   A N   
1447 C  CA  A LYS   A 55  ? 0.1257 0.1369 0.1405 -0.0046 -0.0005 -0.0115 55  LYS   A CA  
1448 C  CA  B LYS   A 55  ? 0.1369 0.1377 0.1255 0.0126  -0.0078 -0.0164 55  LYS   A CA  
1449 C  C   A LYS   A 55  ? 0.1227 0.1456 0.1401 -0.0046 0.0004  -0.0211 55  LYS   A C   
1450 C  C   B LYS   A 55  ? 0.1316 0.1438 0.1358 0.0038  -0.0068 -0.0246 55  LYS   A C   
1451 O  O   A LYS   A 55  ? 0.1279 0.1551 0.1504 -0.0021 0.0002  -0.0173 55  LYS   A O   
1452 O  O   B LYS   A 55  ? 0.1361 0.1486 0.1418 0.0045  -0.0103 -0.0253 55  LYS   A O   
1453 C  CB  A LYS   A 55  ? 0.1335 0.1442 0.1433 0.0084  -0.0060 -0.0238 55  LYS   A CB  
1454 C  CB  B LYS   A 55  ? 0.1466 0.1430 0.1456 0.0191  -0.0096 -0.0098 55  LYS   A CB  
1455 C  CG  A LYS   A 55  ? 0.1535 0.1725 0.1479 0.0247  -0.0214 -0.0283 55  LYS   A CG  
1456 C  CG  B LYS   A 55  ? 0.1585 0.1602 0.1697 0.0279  -0.0208 -0.0107 55  LYS   A CG  
1457 C  CD  A LYS   A 55  ? 0.1711 0.2006 0.1549 0.0322  -0.0150 -0.0289 55  LYS   A CD  
1458 C  CD  B LYS   A 55  ? 0.1717 0.1783 0.1940 0.0300  -0.0153 -0.0084 55  LYS   A CD  
1459 C  CE  A LYS   A 55  ? 0.1866 0.2283 0.1719 0.0424  -0.0261 -0.0242 55  LYS   A CE  
1460 C  CE  B LYS   A 55  ? 0.1852 0.1977 0.2191 0.0305  -0.0182 -0.0111 55  LYS   A CE  
1461 N  NZ  A LYS   A 55  ? 0.1944 0.2428 0.1830 0.0514  -0.0283 -0.0206 55  LYS   A NZ  
1462 N  NZ  B LYS   A 55  ? 0.1905 0.2074 0.2312 0.0328  -0.0205 -0.0162 55  LYS   A NZ  
1489 N  N   . ALA   A 56  ? 0.1295 0.1490 0.1353 -0.0123 -0.0045 -0.0216 56  ALA   A N   
1490 C  CA  . ALA   A 56  ? 0.1422 0.1655 0.1302 -0.0144 0.0081  -0.0185 56  ALA   A CA  
1491 C  C   . ALA   A 56  ? 0.1462 0.1737 0.0997 -0.0136 0.0075  -0.0212 56  ALA   A C   
1492 O  O   . ALA   A 56  ? 0.1546 0.2105 0.1194 -0.0017 0.0118  -0.0161 56  ALA   A O   
1493 C  CB  . ALA   A 56  ? 0.1494 0.1867 0.1511 -0.0237 0.0098  -0.0059 56  ALA   A CB  
1500 N  N   . THR   A 57  ? 0.1332 0.1594 0.1123 -0.0085 0.0035  -0.0159 57  THR   A N   
1501 C  CA  . THR   A 57  ? 0.1388 0.1616 0.1116 -0.0103 -0.0020 -0.0091 57  THR   A CA  
1502 C  C   . THR   A 57  ? 0.1368 0.1668 0.1274 -0.0076 -0.0070 -0.0152 57  THR   A C   
1503 O  O   . THR   A 57  ? 0.1342 0.1734 0.1486 -0.0127 -0.0119 -0.0252 57  THR   A O   
1504 C  CB  . THR   A 57  ? 0.1342 0.1593 0.1170 -0.0109 0.0005  -0.0106 57  THR   A CB  
1505 O  OG1 . THR   A 57  ? 0.1234 0.1536 0.1278 -0.0098 -0.0029 -0.0088 57  THR   A OG1 
1506 C  CG2 . THR   A 57  ? 0.1445 0.1563 0.1191 -0.0093 -0.0015 0.0066  57  THR   A CG2 
1514 N  N   . ASN   A 58  ? 0.1329 0.1624 0.1436 -0.0086 0.0010  -0.0245 58  ASN   A N   
1515 C  CA  . ASN   A 58  ? 0.1600 0.1527 0.1669 -0.0141 0.0127  -0.0406 58  ASN   A CA  
1516 C  C   . ASN   A 58  ? 0.1388 0.1395 0.1583 -0.0035 -0.0075 -0.0259 58  ASN   A C   
1517 O  O   . ASN   A 58  ? 0.1333 0.1527 0.1698 -0.0128 -0.0083 -0.0300 58  ASN   A O   
1518 C  CB  . ASN   A 58  ? 0.2068 0.1730 0.2118 -0.0221 0.0395  -0.0535 58  ASN   A CB  
1519 C  CG  . ASN   A 58  ? 0.2474 0.1958 0.2912 -0.0184 0.0427  -0.0422 58  ASN   A CG  
1520 O  OD1 . ASN   A 58  ? 0.2729 0.1924 0.3345 0.0157  0.0709  -0.0348 58  ASN   A OD1 
1521 N  ND2 . ASN   A 58  ? 0.2561 0.2050 0.3175 -0.0229 0.0248  -0.0461 58  ASN   A ND2 
1528 N  N   . ASN   A 59  ? 0.1221 0.1326 0.1444 -0.0087 -0.0061 -0.0113 59  ASN   A N   
1529 C  CA  . ASN   A 59  ? 0.1245 0.1259 0.1459 -0.0054 -0.0097 -0.0060 59  ASN   A CA  
1530 C  C   . ASN   A 59  ? 0.1264 0.1301 0.1289 -0.0099 -0.0097 -0.0044 59  ASN   A C   
1531 O  O   . ASN   A 59  ? 0.1266 0.1316 0.1457 -0.0069 -0.0025 0.0054  59  ASN   A O   
1532 C  CB  . ASN   A 59  ? 0.1289 0.1278 0.1451 -0.0025 -0.0175 -0.0151 59  ASN   A CB  
1533 C  CG  . ASN   A 59  ? 0.1319 0.1344 0.1466 -0.0021 -0.0297 0.0022  59  ASN   A CG  
1534 O  OD1 . ASN   A 59  ? 0.1420 0.1352 0.1482 -0.0130 -0.0235 0.0051  59  ASN   A OD1 
1535 N  ND2 . ASN   A 59  ? 0.1339 0.1411 0.1595 -0.0150 -0.0163 0.0101  59  ASN   A ND2 
1542 N  N   . ALA   A 60  ? 0.1200 0.1343 0.1252 -0.0062 -0.0059 -0.0037 60  ALA   A N   
1543 C  CA  . ALA   A 60  ? 0.1183 0.1360 0.1393 -0.0031 -0.0145 -0.0029 60  ALA   A CA  
1544 C  C   . ALA   A 60  ? 0.1205 0.1310 0.1413 -0.0035 -0.0070 0.0027  60  ALA   A C   
1545 O  O   . ALA   A 60  ? 0.1157 0.1310 0.1686 -0.0056 -0.0093 -0.0082 60  ALA   A O   
1546 C  CB  . ALA   A 60  ? 0.1351 0.1490 0.1439 -0.0031 -0.0187 -0.0177 60  ALA   A CB  
1552 N  N   . MET   A 61  ? 0.1167 0.1278 0.1348 -0.0073 -0.0071 -0.0013 61  MET   A N   
1553 C  CA  . MET   A 61  ? 0.1166 0.1238 0.1317 -0.0063 0.0002  0.0064  61  MET   A CA  
1554 C  C   . MET   A 61  ? 0.1142 0.1240 0.1358 -0.0046 -0.0016 -0.0028 61  MET   A C   
1555 O  O   . MET   A 61  ? 0.1211 0.1224 0.1443 -0.0052 0.0059  0.0043  61  MET   A O   
1556 C  CB  . MET   A 61  ? 0.1245 0.1253 0.1182 -0.0082 0.0007  -0.0045 61  MET   A CB  
1557 C  CG  . MET   A 61  ? 0.1220 0.1332 0.1473 -0.0056 0.0043  0.0022  61  MET   A CG  
1558 S  SD  . MET   A 61  ? 0.1280 0.1347 0.1696 -0.0116 -0.0026 -0.0134 61  MET   A SD  
1559 C  CE  . MET   A 61  ? 0.1476 0.1417 0.1944 -0.0177 0.0165  -0.0095 61  MET   A CE  
1569 N  N   . GLN   A 62  ? 0.1170 0.1209 0.1316 -0.0050 -0.0012 -0.0042 62  GLN   A N   
1570 C  CA  . GLN   A 62  ? 0.1186 0.1170 0.1392 -0.0058 0.0008  0.0085  62  GLN   A CA  
1571 C  C   . GLN   A 62  ? 0.1232 0.1099 0.1334 0.0003  0.0063  0.0024  62  GLN   A C   
1572 O  O   . GLN   A 62  ? 0.1229 0.1219 0.1433 -0.0044 0.0032  0.0015  62  GLN   A O   
1573 C  CB  . GLN   A 62  ? 0.1204 0.1150 0.1480 -0.0018 0.0024  0.0022  62  GLN   A CB  
1574 C  CG  . GLN   A 62  ? 0.1227 0.1108 0.1502 -0.0040 -0.0021 0.0148  62  GLN   A CG  
1575 C  CD  . GLN   A 62  ? 0.1287 0.1140 0.1503 -0.0025 0.0002  0.0150  62  GLN   A CD  
1576 O  OE1 . GLN   A 62  ? 0.1324 0.1305 0.1466 -0.0063 -0.0017 0.0052  62  GLN   A OE1 
1577 N  NE2 . GLN   A 62  ? 0.1301 0.1235 0.1563 0.0018  0.0034  -0.0009 62  GLN   A NE2 
1586 N  N   . VAL   A 63  ? 0.1144 0.1179 0.1550 -0.0061 0.0087  -0.0117 63  VAL   A N   
1587 C  CA  . VAL   A 63  ? 0.1193 0.1305 0.1777 -0.0122 0.0032  -0.0072 63  VAL   A CA  
1588 C  C   . VAL   A 63  ? 0.1055 0.1268 0.1660 -0.0148 -0.0033 -0.0080 63  VAL   A C   
1589 O  O   . VAL   A 63  ? 0.1126 0.1322 0.1864 -0.0153 -0.0008 -0.0032 63  VAL   A O   
1590 C  CB  . VAL   A 63  ? 0.1313 0.1455 0.2126 -0.0147 -0.0021 -0.0325 63  VAL   A CB  
1591 C  CG1 . VAL   A 63  ? 0.1461 0.1632 0.2489 -0.0099 -0.0109 -0.0523 63  VAL   A CG1 
1592 C  CG2 . VAL   A 63  ? 0.1450 0.1352 0.2276 -0.0111 0.0110  -0.0284 63  VAL   A CG2 
1602 N  N   . GLU   A 64  ? 0.1128 0.1313 0.1513 -0.0078 -0.0047 -0.0038 64  GLU   A N   
1603 C  CA  . GLU   A 64  ? 0.1182 0.1332 0.1603 -0.0053 -0.0068 0.0032  64  GLU   A CA  
1604 C  C   . GLU   A 64  ? 0.1099 0.1259 0.1552 -0.0092 0.0010  0.0067  64  GLU   A C   
1605 O  O   . GLU   A 64  ? 0.1188 0.1329 0.1636 -0.0023 -0.0001 0.0014  64  GLU   A O   
1606 C  CB  . GLU   A 64  ? 0.1208 0.1411 0.1553 -0.0071 -0.0024 -0.0009 64  GLU   A CB  
1607 C  CG  . GLU   A 64  ? 0.1309 0.1456 0.1736 -0.0070 0.0044  -0.0002 64  GLU   A CG  
1608 C  CD  . GLU   A 64  ? 0.1426 0.1531 0.1697 -0.0145 0.0113  0.0041  64  GLU   A CD  
1609 O  OE1 . GLU   A 64  ? 0.1426 0.1632 0.1959 -0.0205 0.0176  0.0017  64  GLU   A OE1 
1610 O  OE2 . GLU   A 64  ? 0.1611 0.1530 0.1686 -0.0281 -0.0075 0.0060  64  GLU   A OE2 
1617 N  N   . SER   A 65  ? 0.1024 0.1276 0.1468 0.0006  0.0008  0.0040  65  SER   A N   
1618 C  CA  . SER   A 65  ? 0.1187 0.1200 0.1363 -0.0019 -0.0029 -0.0011 65  SER   A CA  
1619 C  C   . SER   A 65  ? 0.1178 0.1303 0.1392 -0.0029 0.0048  0.0017  65  SER   A C   
1620 O  O   . SER   A 65  ? 0.1269 0.1318 0.1662 0.0002  0.0180  -0.0013 65  SER   A O   
1621 C  CB  . SER   A 65  ? 0.1174 0.1205 0.1376 -0.0030 0.0081  0.0094  65  SER   A CB  
1622 O  OG  . SER   A 65  ? 0.1151 0.1342 0.1515 -0.0085 -0.0041 0.0158  65  SER   A OG  
1628 N  N   . ASP   A 66  ? 0.1189 0.1255 0.1464 -0.0029 0.0167  0.0089  66  ASP   A N   
1629 C  CA  . ASP   A 66  ? 0.1270 0.1353 0.1654 -0.0047 0.0105  0.0145  66  ASP   A CA  
1630 C  C   . ASP   A 66  ? 0.1249 0.1334 0.1646 -0.0052 0.0132  0.0153  66  ASP   A C   
1631 O  O   . ASP   A 66  ? 0.1324 0.1421 0.1918 -0.0043 0.0279  0.0218  66  ASP   A O   
1632 C  CB  . ASP   A 66  ? 0.1327 0.1424 0.1985 0.0055  0.0192  0.0263  66  ASP   A CB  
1633 C  CG  . ASP   A 66  ? 0.1550 0.1566 0.2344 -0.0007 0.0094  0.0457  66  ASP   A CG  
1634 O  OD1 . ASP   A 66  ? 0.1517 0.1846 0.2100 -0.0061 0.0011  0.0530  66  ASP   A OD1 
1635 O  OD2 . ASP   A 66  ? 0.1730 0.1673 0.3193 0.0145  -0.0094 0.0285  66  ASP   A OD2 
1640 N  N   . ASP   A 67  ? 0.1184 0.1330 0.1738 -0.0035 0.0098  0.0168  67  ASP   A N   
1641 C  CA  . ASP   A 67  ? 0.1205 0.1506 0.1918 -0.0042 0.0030  0.0261  67  ASP   A CA  
1642 C  C   . ASP   A 67  ? 0.1222 0.1478 0.1940 0.0022  0.0110  0.0240  67  ASP   A C   
1643 O  O   . ASP   A 67  ? 0.1169 0.1570 0.2084 0.0032  0.0258  0.0269  67  ASP   A O   
1644 C  CB  . ASP   A 67  ? 0.1301 0.1628 0.2242 -0.0068 -0.0080 0.0347  67  ASP   A CB  
1645 C  CG  . ASP   A 67  ? 0.1263 0.1700 0.2627 -0.0096 -0.0200 0.0376  67  ASP   A CG  
1646 O  OD1 . ASP   A 67  ? 0.1334 0.1869 0.3353 -0.0139 -0.0302 0.0493  67  ASP   A OD1 
1647 O  OD2 . ASP   A 67  ? 0.1301 0.1739 0.2448 0.0020  -0.0168 0.0292  67  ASP   A OD2 
1652 N  N   . TYR   A 68  ? 0.1204 0.1336 0.1864 0.0011  0.0171  0.0276  68  TYR   A N   
1653 C  CA  . TYR   A 68  ? 0.1336 0.1351 0.1765 0.0052  0.0222  0.0312  68  TYR   A CA  
1654 C  C   . TYR   A 68  ? 0.1262 0.1383 0.1797 0.0018  0.0257  0.0223  68  TYR   A C   
1655 O  O   . TYR   A 68  ? 0.1368 0.1370 0.1897 0.0062  0.0273  0.0211  68  TYR   A O   
1656 C  CB  . TYR   A 68  ? 0.1393 0.1386 0.1854 0.0048  0.0365  0.0268  68  TYR   A CB  
1657 C  CG  . TYR   A 68  ? 0.1462 0.1499 0.2141 0.0035  0.0518  0.0351  68  TYR   A CG  
1658 C  CD1 . TYR   A 68  ? 0.1543 0.1594 0.2440 -0.0165 0.0426  0.0046  68  TYR   A CD1 
1659 C  CD2 . TYR   A 68  ? 0.1608 0.1525 0.2530 0.0074  0.0474  0.0438  68  TYR   A CD2 
1660 C  CE1 . TYR   A 68  ? 0.1628 0.1680 0.2766 -0.0160 0.0430  -0.0009 68  TYR   A CE1 
1661 C  CE2 . TYR   A 68  ? 0.1640 0.1591 0.2610 0.0028  0.0540  0.0282  68  TYR   A CE2 
1662 C  CZ  . TYR   A 68  ? 0.1644 0.1608 0.2756 -0.0167 0.0439  -0.0032 68  TYR   A CZ  
1663 O  OH  . TYR   A 68  ? 0.1896 0.1614 0.2996 -0.0147 0.0251  -0.0210 68  TYR   A OH  
1673 N  N   . ILE   A 69  ? 0.1218 0.1279 0.1712 -0.0028 0.0163  0.0192  69  ILE   A N   
1674 C  CA  . ILE   A 69  ? 0.1277 0.1347 0.1682 -0.0008 0.0153  0.0136  69  ILE   A CA  
1675 C  C   . ILE   A 69  ? 0.1318 0.1335 0.1642 0.0072  0.0212  0.0199  69  ILE   A C   
1676 O  O   . ILE   A 69  ? 0.1407 0.1413 0.1638 -0.0006 0.0262  0.0189  69  ILE   A O   
1677 C  CB  . ILE   A 69  ? 0.1374 0.1518 0.1678 0.0047  0.0168  -0.0010 69  ILE   A CB  
1678 C  CG1 . ILE   A 69  ? 0.1388 0.1610 0.1788 0.0028  0.0147  -0.0160 69  ILE   A CG1 
1679 C  CG2 . ILE   A 69  ? 0.1566 0.1713 0.1881 0.0134  0.0063  -0.0026 69  ILE   A CG2 
1680 C  CD1 . ILE   A 69  ? 0.1380 0.1717 0.1934 -0.0100 0.0170  -0.0195 69  ILE   A CD1 
1692 N  N   . ALA   A 70  ? 0.1376 0.1334 0.1743 -0.0040 0.0285  0.0204  70  ALA   A N   
1693 C  CA  . ALA   A 70  ? 0.1418 0.1450 0.1969 -0.0118 0.0284  0.0284  70  ALA   A CA  
1694 C  C   . ALA   A 70  ? 0.1370 0.1647 0.1938 -0.0080 0.0310  0.0278  70  ALA   A C   
1695 O  O   . ALA   A 70  ? 0.1579 0.1990 0.2062 0.0118  0.0517  0.0421  70  ALA   A O   
1696 C  CB  . ALA   A 70  ? 0.1439 0.1426 0.2248 -0.0169 0.0279  0.0231  70  ALA   A CB  
1702 N  N   . THR   A 71  ? 0.1315 0.1589 0.1856 -0.0050 0.0218  0.0210  71  THR   A N   
1703 C  CA  . THR   A 71  ? 0.1404 0.1785 0.2172 0.0098  0.0238  0.0230  71  THR   A CA  
1704 C  C   . THR   A 71  ? 0.1334 0.1681 0.2398 0.0160  0.0283  0.0251  71  THR   A C   
1705 O  O   . THR   A 71  ? 0.1364 0.1893 0.2862 0.0106  0.0395  -0.0032 71  THR   A O   
1706 C  CB  . THR   A 71  ? 0.1660 0.2023 0.2412 0.0172  -0.0077 0.0326  71  THR   A CB  
1707 O  OG1 . THR   A 71  ? 0.1914 0.2186 0.2465 0.0083  -0.0322 0.0244  71  THR   A OG1 
1708 C  CG2 . THR   A 71  ? 0.1748 0.2181 0.2725 0.0269  -0.0177 0.0431  71  THR   A CG2 
1716 N  N   . ASN   A 72  ? 0.1364 0.1476 0.2150 0.0114  0.0283  0.0279  72  ASN   A N   
1717 C  CA  . ASN   A 72  ? 0.1417 0.1549 0.2148 0.0156  0.0399  0.0248  72  ASN   A CA  
1718 C  C   . ASN   A 72  ? 0.1552 0.1497 0.2066 0.0095  0.0528  0.0185  72  ASN   A C   
1719 O  O   . ASN   A 72  ? 0.1730 0.1458 0.2429 0.0147  0.0443  0.0114  72  ASN   A O   
1720 C  CB  . ASN   A 72  ? 0.1605 0.1606 0.2167 0.0180  0.0379  0.0289  72  ASN   A CB  
1721 C  CG  . ASN   A 72  ? 0.1812 0.1708 0.2288 0.0246  0.0376  0.0338  72  ASN   A CG  
1722 O  OD1 . ASN   A 72  ? 0.1972 0.2037 0.2466 0.0289  0.0383  0.0345  72  ASN   A OD1 
1723 N  ND2 . ASN   A 72  ? 0.1970 0.1700 0.2404 0.0511  0.0167  0.0211  72  ASN   A ND2 
1730 N  N   . GLY   A 73  ? 0.1551 0.1454 0.1926 0.0039  0.0429  0.0104  73  GLY   A N   
1731 C  CA  . GLY   A 73  ? 0.1591 0.1435 0.1785 -0.0062 0.0433  0.0120  73  GLY   A CA  
1732 C  C   . GLY   A 73  ? 0.1585 0.1366 0.1670 0.0030  0.0531  0.0208  73  GLY   A C   
1733 O  O   . GLY   A 73  ? 0.1603 0.1430 0.1797 0.0089  0.0403  0.0224  73  GLY   A O   
1737 N  N   . PRO   A 74  ? 0.1703 0.1400 0.1753 -0.0124 0.0495  0.0132  74  PRO   A N   
1738 C  CA  . PRO   A 74  ? 0.1624 0.1359 0.1833 -0.0056 0.0427  0.0159  74  PRO   A CA  
1739 C  C   . PRO   A 74  ? 0.1552 0.1284 0.1834 0.0030  0.0365  0.0062  74  PRO   A C   
1740 O  O   . PRO   A 74  ? 0.1610 0.1342 0.1959 0.0033  0.0359  -0.0037 74  PRO   A O   
1741 C  CB  . PRO   A 74  ? 0.1763 0.1630 0.1994 0.0005  0.0388  0.0257  74  PRO   A CB  
1742 C  CG  . PRO   A 74  ? 0.2032 0.1958 0.2415 -0.0165 0.0322  0.0147  74  PRO   A CG  
1743 C  CD  . PRO   A 74  ? 0.1872 0.1757 0.1950 -0.0184 0.0332  0.0097  74  PRO   A CD  
1751 N  N   . LEU   A 75  ? 0.1547 0.1195 0.1626 0.0006  0.0280  0.0039  75  LEU   A N   
1752 C  CA  . LEU   A 75  ? 0.1581 0.1198 0.1440 -0.0003 0.0110  0.0117  75  LEU   A CA  
1753 C  C   . LEU   A 75  ? 0.1659 0.1339 0.1384 0.0026  0.0194  0.0147  75  LEU   A C   
1754 O  O   . LEU   A 75  ? 0.1998 0.1471 0.1462 0.0089  0.0098  0.0064  75  LEU   A O   
1755 C  CB  . LEU   A 75  ? 0.1596 0.1258 0.1327 -0.0092 0.0143  0.0176  75  LEU   A CB  
1756 C  CG  . LEU   A 75  ? 0.1770 0.1629 0.1429 -0.0310 0.0108  0.0140  75  LEU   A CG  
1757 C  CD1 . LEU   A 75  ? 0.1900 0.2095 0.1533 -0.0338 0.0114  -0.0049 75  LEU   A CD1 
1758 C  CD2 . LEU   A 75  ? 0.1990 0.1989 0.1985 -0.0119 0.0078  0.0166  75  LEU   A CD2 
1770 N  N   . LYS   A 76  ? 0.1668 0.1318 0.1546 -0.0065 0.0175  0.0018  76  LYS   A N   
1771 C  CA  . LYS   A 76  ? 0.1655 0.1479 0.1609 -0.0075 0.0151  -0.0083 76  LYS   A CA  
1772 C  C   . LYS   A 76  ? 0.1610 0.1302 0.1234 -0.0004 0.0157  0.0113  76  LYS   A C   
1773 O  O   . LYS   A 76  ? 0.1621 0.1288 0.1308 -0.0014 0.0169  0.0141  76  LYS   A O   
1774 C  CB  . LYS   A 76  ? 0.1657 0.1691 0.2024 0.0028  0.0146  -0.0252 76  LYS   A CB  
1775 C  CG  . LYS   A 76  ? 0.1719 0.1659 0.2506 0.0095  0.0079  -0.0215 76  LYS   A CG  
1776 C  CD  . LYS   A 76  ? 0.1787 0.1668 0.2915 0.0128  -0.0034 -0.0359 76  LYS   A CD  
1777 C  CE  . LYS   A 76  ? 0.1980 0.1885 0.3475 0.0033  0.0022  -0.0374 76  LYS   A CE  
1778 N  NZ  . LYS   A 76  ? 0.2023 0.1854 0.3870 -0.0112 -0.0002 -0.0448 76  LYS   A NZ  
1792 N  N   . VAL   A 77  ? 0.1693 0.1357 0.1311 -0.0003 0.0261  0.0146  77  VAL   A N   
1793 C  CA  . VAL   A 77  ? 0.1666 0.1371 0.1246 0.0072  0.0151  0.0080  77  VAL   A CA  
1794 C  C   . VAL   A 77  ? 0.1606 0.1324 0.1250 0.0094  0.0128  0.0088  77  VAL   A C   
1795 O  O   . VAL   A 77  ? 0.1674 0.1376 0.1367 0.0109  0.0335  0.0017  77  VAL   A O   
1796 C  CB  . VAL   A 77  ? 0.1831 0.1563 0.1375 0.0062  0.0113  0.0205  77  VAL   A CB  
1797 C  CG1 . VAL   A 77  ? 0.1777 0.1721 0.1594 0.0121  0.0042  0.0079  77  VAL   A CG1 
1798 C  CG2 . VAL   A 77  ? 0.2098 0.1639 0.1486 0.0049  0.0054  0.0257  77  VAL   A CG2 
1808 N  N   . GLY   A 78  ? 0.1546 0.1320 0.1233 0.0074  0.0188  0.0068  78  GLY   A N   
1809 C  CA  . GLY   A 78  ? 0.1540 0.1302 0.1387 0.0033  0.0250  0.0175  78  GLY   A CA  
1810 C  C   . GLY   A 78  ? 0.1416 0.1209 0.1358 0.0046  0.0218  0.0194  78  GLY   A C   
1811 O  O   . GLY   A 78  ? 0.1381 0.1305 0.1477 0.0068  0.0165  0.0236  78  GLY   A O   
1815 N  N   . GLY   A 79  ? 0.1482 0.1197 0.1379 0.0023  0.0184  0.0174  79  GLY   A N   
1816 C  CA  . GLY   A 79  ? 0.1448 0.1258 0.1444 -0.0011 0.0182  0.0170  79  GLY   A CA  
1817 C  C   . GLY   A 79  ? 0.1298 0.1225 0.1397 -0.0037 0.0163  0.0046  79  GLY   A C   
1818 O  O   . GLY   A 79  ? 0.1333 0.1306 0.1448 0.0146  0.0125  0.0041  79  GLY   A O   
1822 N  N   . SER   A 80  ? 0.1214 0.1365 0.1545 -0.0039 0.0141  -0.0021 80  SER   A N   
1823 C  CA  . SER   A 80  ? 0.1224 0.1299 0.1492 -0.0039 0.0091  0.0057  80  SER   A CA  
1824 C  C   . SER   A 80  ? 0.1165 0.1324 0.1430 -0.0038 0.0087  0.0124  80  SER   A C   
1825 O  O   . SER   A 80  ? 0.1197 0.1532 0.1821 0.0059  0.0104  0.0048  80  SER   A O   
1826 C  CB  . SER   A 80  ? 0.1342 0.1320 0.1743 -0.0046 0.0115  0.0053  80  SER   A CB  
1827 O  OG  . SER   A 80  ? 0.1573 0.1316 0.2170 0.0042  -0.0031 0.0278  80  SER   A OG  
1833 N  N   . CYS   A 81  ? 0.1162 0.1258 0.1442 -0.0014 -0.0022 0.0123  81  CYS   A N   
1834 C  CA  . CYS   A 81  ? 0.1182 0.1325 0.1440 -0.0070 -0.0026 0.0213  81  CYS   A CA  
1835 C  C   . CYS   A 81  ? 0.1156 0.1308 0.1359 -0.0119 -0.0030 0.0282  81  CYS   A C   
1836 O  O   . CYS   A 81  ? 0.1134 0.1601 0.1541 0.0000  0.0022  0.0366  81  CYS   A O   
1837 C  CB  . CYS   A 81  ? 0.1224 0.1385 0.1596 -0.0119 -0.0005 0.0274  81  CYS   A CB  
1838 S  SG  . CYS   A 81  ? 0.1387 0.1315 0.1578 -0.0126 0.0014  0.0171  81  CYS   A SG  
1844 N  N   . VAL   A 82  ? 0.1182 0.1400 0.1427 -0.0010 -0.0119 0.0188  82  VAL   A N   
1845 C  CA  . VAL   A 82  ? 0.1319 0.1420 0.1374 -0.0004 -0.0061 0.0274  82  VAL   A CA  
1846 C  C   . VAL   A 82  ? 0.1244 0.1456 0.1511 0.0014  -0.0076 0.0272  82  VAL   A C   
1847 O  O   . VAL   A 82  ? 0.1212 0.1518 0.1777 0.0015  -0.0072 0.0071  82  VAL   A O   
1848 C  CB  . VAL   A 82  ? 0.1629 0.1553 0.1570 0.0045  -0.0065 0.0275  82  VAL   A CB  
1849 C  CG1 . VAL   A 82  ? 0.1855 0.1692 0.1809 0.0081  -0.0073 0.0282  82  VAL   A CG1 
1850 C  CG2 . VAL   A 82  ? 0.1693 0.1566 0.1894 0.0008  -0.0046 0.0301  82  VAL   A CG2 
1860 N  N   . LEU   A 83  ? 0.1213 0.1441 0.1416 -0.0077 -0.0116 0.0181  83  LEU   A N   
1861 C  CA  . LEU   A 83  ? 0.1262 0.1421 0.1335 -0.0129 -0.0115 0.0117  83  LEU   A CA  
1862 C  C   . LEU   A 83  ? 0.1318 0.1444 0.1328 -0.0144 -0.0133 0.0168  83  LEU   A C   
1863 O  O   . LEU   A 83  ? 0.1411 0.1480 0.1413 -0.0168 -0.0075 0.0219  83  LEU   A O   
1864 C  CB  . LEU   A 83  ? 0.1387 0.1453 0.1396 -0.0105 -0.0102 0.0156  83  LEU   A CB  
1865 C  CG  . LEU   A 83  ? 0.1495 0.1564 0.1463 -0.0124 0.0043  0.0095  83  LEU   A CG  
1866 C  CD1 . LEU   A 83  ? 0.1637 0.1603 0.1602 -0.0256 0.0046  0.0266  83  LEU   A CD1 
1867 C  CD2 . LEU   A 83  ? 0.1490 0.1697 0.1592 -0.0130 0.0132  0.0132  83  LEU   A CD2 
1879 N  N   . SER   A 84  ? 0.1474 0.1489 0.1349 -0.0152 -0.0094 0.0194  84  SER   A N   
1880 C  CA  . SER   A 84  ? 0.1561 0.1567 0.1173 -0.0145 -0.0061 0.0207  84  SER   A CA  
1881 C  C   . SER   A 84  ? 0.1589 0.1572 0.1168 -0.0193 0.0028  0.0189  84  SER   A C   
1882 O  O   . SER   A 84  ? 0.1500 0.1698 0.1187 -0.0161 -0.0133 0.0149  84  SER   A O   
1883 C  CB  . SER   A 84  ? 0.1616 0.1795 0.1267 -0.0113 -0.0114 0.0079  84  SER   A CB  
1884 O  OG  . SER   A 84  ? 0.1655 0.2020 0.1414 -0.0157 -0.0180 -0.0028 84  SER   A OG  
1890 N  N   . GLY   A 85  ? 0.1706 0.1724 0.1244 -0.0195 0.0030  0.0134  85  GLY   A N   
1891 C  CA  . GLY   A 85  ? 0.1721 0.1781 0.1312 -0.0244 0.0107  0.0034  85  GLY   A CA  
1892 C  C   . GLY   A 85  ? 0.1662 0.1813 0.1149 -0.0214 0.0006  0.0012  85  GLY   A C   
1893 O  O   . GLY   A 85  ? 0.1668 0.1911 0.1395 -0.0280 0.0104  -0.0106 85  GLY   A O   
1897 N  N   . HIS   A 86  ? 0.1715 0.1717 0.1117 -0.0186 -0.0122 0.0019  86  HIS   A N   
1898 C  CA  . HIS   A 86  ? 0.1851 0.1790 0.1119 -0.0225 -0.0098 0.0047  86  HIS   A CA  
1899 C  C   . HIS   A 86  ? 0.2055 0.1928 0.1023 -0.0255 -0.0172 0.0048  86  HIS   A C   
1900 O  O   . HIS   A 86  ? 0.2133 0.2194 0.1132 -0.0213 0.0008  0.0048  86  HIS   A O   
1901 C  CB  . HIS   A 86  ? 0.1825 0.1746 0.1285 -0.0168 -0.0059 0.0101  86  HIS   A CB  
1902 C  CG  . HIS   A 86  ? 0.1762 0.1701 0.1327 -0.0086 0.0062  0.0128  86  HIS   A CG  
1903 N  ND1 . HIS   A 86  ? 0.1830 0.1701 0.1644 -0.0191 0.0040  0.0125  86  HIS   A ND1 
1904 C  CD2 . HIS   A 86  ? 0.1749 0.1641 0.1255 0.0056  0.0086  0.0168  86  HIS   A CD2 
1905 C  CE1 . HIS   A 86  ? 0.1768 0.1694 0.1569 -0.0107 0.0133  0.0174  86  HIS   A CE1 
1906 N  NE2 . HIS   A 86  ? 0.1746 0.1659 0.1404 0.0041  0.0075  0.0229  86  HIS   A NE2 
1914 N  N   . ASN   A 87  ? 0.2171 0.2023 0.1161 -0.0199 0.0063  -0.0030 87  ASN   A N   
1915 C  CA  . ASN   A 87  ? 0.2392 0.2189 0.1249 -0.0180 0.0300  -0.0082 87  ASN   A CA  
1916 C  C   . ASN   A 87  ? 0.2393 0.2329 0.1463 -0.0237 0.0470  -0.0012 87  ASN   A C   
1917 O  O   . ASN   A 87  ? 0.2651 0.2545 0.1906 -0.0309 0.0792  -0.0093 87  ASN   A O   
1918 C  CB  . ASN   A 87  ? 0.2582 0.2279 0.1262 -0.0068 0.0343  -0.0119 87  ASN   A CB  
1919 C  CG  . ASN   A 87  ? 0.2711 0.2396 0.1366 -0.0015 0.0451  -0.0020 87  ASN   A CG  
1920 O  OD1 . ASN   A 87  ? 0.2848 0.2362 0.1366 0.0131  0.0429  0.0063  87  ASN   A OD1 
1921 N  ND2 . ASN   A 87  ? 0.2738 0.2605 0.1564 -0.0039 0.0442  0.0039  87  ASN   A ND2 
1928 N  N   . LEU   A 88  ? 0.2090 0.2167 0.1349 -0.0302 0.0283  0.0131  88  LEU   A N   
1929 C  CA  . LEU   A 88  ? 0.1892 0.2170 0.1497 -0.0324 0.0259  0.0242  88  LEU   A CA  
1930 C  C   . LEU   A 88  ? 0.1828 0.2205 0.1464 -0.0295 0.0211  0.0349  88  LEU   A C   
1931 O  O   . LEU   A 88  ? 0.1848 0.2225 0.1861 -0.0253 0.0229  0.0488  88  LEU   A O   
1932 C  CB  . LEU   A 88  ? 0.1916 0.2229 0.1566 -0.0431 -0.0100 0.0386  88  LEU   A CB  
1933 C  CG  . LEU   A 88  ? 0.2069 0.2346 0.1920 -0.0439 -0.0201 0.0404  88  LEU   A CG  
1934 C  CD1 . LEU   A 88  ? 0.2202 0.2436 0.1887 -0.0397 -0.0266 0.0346  88  LEU   A CD1 
1935 C  CD2 . LEU   A 88  ? 0.2217 0.2455 0.2329 -0.0339 -0.0113 0.0327  88  LEU   A CD2 
1947 N  N   . ALA   A 89  ? 0.1816 0.2138 0.1324 -0.0316 0.0055  0.0133  89  ALA   A N   
1948 C  CA  . ALA   A 89  ? 0.1869 0.2110 0.1169 -0.0251 -0.0021 0.0224  89  ALA   A CA  
1949 C  C   . ALA   A 89  ? 0.1958 0.2135 0.1321 -0.0211 -0.0160 0.0171  89  ALA   A C   
1950 O  O   . ALA   A 89  ? 0.1899 0.2081 0.1678 -0.0292 -0.0167 -0.0087 89  ALA   A O   
1951 C  CB  . ALA   A 89  ? 0.1792 0.2049 0.1109 -0.0222 -0.0027 0.0237  89  ALA   A CB  
1957 N  N   . LYS   A 90  ? 0.2027 0.2254 0.1348 -0.0293 -0.0243 0.0215  90  LYS   A N   
1958 C  CA  . LYS   A 90  ? 0.2065 0.2331 0.1389 -0.0188 -0.0378 0.0250  90  LYS   A CA  
1959 C  C   . LYS   A 90  ? 0.1898 0.2161 0.1403 -0.0232 -0.0366 0.0164  90  LYS   A C   
1960 O  O   . LYS   A 90  ? 0.1917 0.2297 0.1719 -0.0273 -0.0446 0.0040  90  LYS   A O   
1961 C  CB  . LYS   A 90  ? 0.2295 0.2656 0.1706 -0.0095 -0.0451 0.0475  90  LYS   A CB  
1962 C  CG  . LYS   A 90  ? 0.2639 0.2971 0.2665 -0.0039 -0.0483 0.0547  90  LYS   A CG  
1963 C  CD  . LYS   A 90  ? 0.3042 0.3273 0.3570 -0.0033 -0.0375 0.0571  90  LYS   A CD  
1964 C  CE  . LYS   A 90  ? 0.3367 0.3538 0.4300 -0.0038 -0.0257 0.0517  90  LYS   A CE  
1965 N  NZ  . LYS   A 90  ? 0.3506 0.3664 0.4793 -0.0062 -0.0158 0.0450  90  LYS   A NZ  
1979 N  N   . HIS   A 91  ? 0.1799 0.1887 0.1168 -0.0232 -0.0353 0.0244  91  HIS   A N   
1980 C  CA  . HIS   A 91  ? 0.1648 0.1730 0.1230 -0.0140 -0.0284 0.0142  91  HIS   A CA  
1981 C  C   . HIS   A 91  ? 0.1478 0.1602 0.1096 -0.0128 -0.0163 0.0194  91  HIS   A C   
1982 O  O   . HIS   A 91  ? 0.1448 0.1760 0.1279 -0.0223 -0.0079 0.0258  91  HIS   A O   
1983 C  CB  . HIS   A 91  ? 0.1813 0.2053 0.1713 0.0020  -0.0401 0.0200  91  HIS   A CB  
1984 C  CG  . HIS   A 91  ? 0.2223 0.2536 0.2384 0.0165  -0.0639 0.0159  91  HIS   A CG  
1985 N  ND1 . HIS   A 91  ? 0.2333 0.2812 0.2785 0.0218  -0.0751 -0.0003 91  HIS   A ND1 
1986 C  CD2 . HIS   A 91  ? 0.2477 0.2746 0.2666 0.0226  -0.0796 0.0243  91  HIS   A CD2 
1987 C  CE1 . HIS   A 91  ? 0.2449 0.2906 0.2883 0.0232  -0.0849 0.0097  91  HIS   A CE1 
1988 N  NE2 . HIS   A 91  ? 0.2586 0.2908 0.2900 0.0258  -0.0873 0.0156  91  HIS   A NE2 
1996 N  N   . CYS   A 92  ? 0.1387 0.1556 0.1155 -0.0198 -0.0137 0.0219  92  CYS   A N   
1997 C  CA  . CYS   A 92  ? 0.1340 0.1475 0.1205 -0.0181 -0.0030 0.0173  92  CYS   A CA  
1998 C  C   . CYS   A 92  ? 0.1286 0.1427 0.1196 -0.0178 0.0007  0.0177  92  CYS   A C   
1999 O  O   . CYS   A 92  ? 0.1293 0.1455 0.1382 -0.0166 -0.0049 0.0132  92  CYS   A O   
2000 C  CB  . CYS   A 92  ? 0.1368 0.1438 0.1323 -0.0084 -0.0110 0.0094  92  CYS   A CB  
2001 S  SG  . CYS   A 92  ? 0.1318 0.1345 0.1375 -0.0107 -0.0056 0.0152  92  CYS   A SG  
2007 N  N   . LEU   A 93  ? 0.1285 0.1318 0.1153 -0.0147 0.0049  0.0188  93  LEU   A N   
2008 C  CA  . LEU   A 93  ? 0.1181 0.1298 0.1123 -0.0094 -0.0001 0.0174  93  LEU   A CA  
2009 C  C   . LEU   A 93  ? 0.1190 0.1205 0.1080 -0.0029 0.0038  0.0127  93  LEU   A C   
2010 O  O   . LEU   A 93  ? 0.1117 0.1252 0.1197 -0.0047 0.0005  0.0156  93  LEU   A O   
2011 C  CB  . LEU   A 93  ? 0.1250 0.1270 0.1320 -0.0080 0.0020  0.0251  93  LEU   A CB  
2012 C  CG  . LEU   A 93  ? 0.1349 0.1274 0.1337 -0.0019 -0.0024 0.0276  93  LEU   A CG  
2013 C  CD1 . LEU   A 93  ? 0.1372 0.1331 0.1685 0.0010  0.0101  0.0177  93  LEU   A CD1 
2014 C  CD2 . LEU   A 93  ? 0.1458 0.1266 0.1521 -0.0107 -0.0011 0.0127  93  LEU   A CD2 
2026 N  N   . HIS   A 94  ? 0.1156 0.1162 0.1130 -0.0030 0.0017  0.0201  94  HIS   A N   
2027 C  CA  . HIS   A 94  ? 0.1105 0.1168 0.1180 -0.0054 -0.0032 0.0162  94  HIS   A CA  
2028 C  C   . HIS   A 94  ? 0.1102 0.1129 0.1265 -0.0066 -0.0032 0.0130  94  HIS   A C   
2029 O  O   . HIS   A 94  ? 0.1127 0.1317 0.1613 0.0004  -0.0010 -0.0042 94  HIS   A O   
2030 C  CB  . HIS   A 94  ? 0.1093 0.1156 0.1323 -0.0063 -0.0045 0.0136  94  HIS   A CB  
2031 C  CG  . HIS   A 94  ? 0.1156 0.1192 0.1162 -0.0020 0.0009  0.0139  94  HIS   A CG  
2032 N  ND1 . HIS   A 94  ? 0.1172 0.1148 0.1289 -0.0052 -0.0013 0.0182  94  HIS   A ND1 
2033 C  CD2 . HIS   A 94  ? 0.1203 0.1295 0.1369 -0.0063 -0.0102 0.0027  94  HIS   A CD2 
2034 C  CE1 . HIS   A 94  ? 0.1205 0.1183 0.1258 -0.0108 -0.0043 0.0072  94  HIS   A CE1 
2035 N  NE2 . HIS   A 94  ? 0.1234 0.1193 0.1393 -0.0101 -0.0077 0.0050  94  HIS   A NE2 
2043 N  N   . VAL   A 95  ? 0.1087 0.1102 0.1157 -0.0039 0.0072  0.0041  95  VAL   A N   
2044 C  CA  . VAL   A 95  ? 0.1174 0.1156 0.1145 -0.0076 0.0096  0.0150  95  VAL   A CA  
2045 C  C   . VAL   A 95  ? 0.1168 0.1131 0.0993 -0.0118 0.0062  0.0122  95  VAL   A C   
2046 O  O   . VAL   A 95  ? 0.1196 0.1259 0.1124 0.0037  0.0041  0.0082  95  VAL   A O   
2047 C  CB  . VAL   A 95  ? 0.1156 0.1169 0.1382 -0.0092 0.0026  0.0076  95  VAL   A CB  
2048 C  CG1 . VAL   A 95  ? 0.1298 0.1178 0.1412 -0.0163 -0.0020 0.0049  95  VAL   A CG1 
2049 C  CG2 . VAL   A 95  ? 0.1200 0.1212 0.1378 -0.0113 0.0035  0.0205  95  VAL   A CG2 
2059 N  N   . VAL   A 96  ? 0.1219 0.1157 0.0915 -0.0041 0.0056  0.0118  96  VAL   A N   
2060 C  CA  . VAL   A 96  ? 0.1303 0.1191 0.1125 -0.0043 0.0106  0.0193  96  VAL   A CA  
2061 C  C   . VAL   A 96  ? 0.1298 0.1247 0.1166 -0.0053 0.0134  0.0166  96  VAL   A C   
2062 O  O   . VAL   A 96  ? 0.1396 0.1305 0.1372 -0.0039 0.0188  0.0014  96  VAL   A O   
2063 C  CB  . VAL   A 96  ? 0.1319 0.1195 0.1261 -0.0002 0.0219  0.0182  96  VAL   A CB  
2064 C  CG1 . VAL   A 96  ? 0.1421 0.1275 0.1158 -0.0059 0.0145  0.0105  96  VAL   A CG1 
2065 C  CG2 . VAL   A 96  ? 0.1366 0.1296 0.1441 -0.0170 0.0221  0.0132  96  VAL   A CG2 
2075 N  N   A GLY   A 97  ? 0.1283 0.1276 0.1244 -0.0077 0.0026  0.0078  97  GLY   A N   
2076 N  N   B GLY   A 97  ? 0.1343 0.1280 0.1060 -0.0042 0.0065  0.0098  97  GLY   A N   
2077 C  CA  A GLY   A 97  ? 0.1374 0.1415 0.1194 -0.0042 -0.0017 0.0084  97  GLY   A CA  
2078 C  CA  B GLY   A 97  ? 0.1443 0.1353 0.0969 -0.0018 0.0085  0.0075  97  GLY   A CA  
2079 C  C   A GLY   A 97  ? 0.1387 0.1493 0.1066 -0.0037 -0.0034 0.0114  97  GLY   A C   
2080 C  C   B GLY   A 97  ? 0.1497 0.1385 0.0997 0.0005  0.0104  0.0078  97  GLY   A C   
2081 O  O   A GLY   A 97  ? 0.1492 0.1502 0.1216 -0.0109 -0.0046 0.0162  97  GLY   A O   
2082 O  O   B GLY   A 97  ? 0.1567 0.1385 0.1136 -0.0009 0.0081  0.0164  97  GLY   A O   
2089 N  N   A PRO   A 98  ? 0.1379 0.1531 0.0837 0.0038  -0.0039 0.0168  98  PRO   A N   
2090 N  N   B PRO   A 98  ? 0.1540 0.1410 0.1095 0.0018  0.0119  0.0142  98  PRO   A N   
2091 C  CA  A PRO   A 98  ? 0.1514 0.1661 0.0966 0.0055  0.0020  0.0051  98  PRO   A CA  
2092 C  CA  B PRO   A 98  ? 0.1692 0.1471 0.1260 0.0017  0.0145  0.0071  98  PRO   A CA  
2093 C  C   A PRO   A 98  ? 0.1515 0.1649 0.0857 -0.0037 0.0052  0.0143  98  PRO   A C   
2094 C  C   B PRO   A 98  ? 0.1910 0.1436 0.1223 -0.0041 0.0087  0.0170  98  PRO   A C   
2095 O  O   A PRO   A 98  ? 0.1446 0.1500 0.1052 0.0010  0.0037  0.0213  98  PRO   A O   
2096 O  O   B PRO   A 98  ? 0.1864 0.1471 0.1472 -0.0037 0.0116  0.0079  98  PRO   A O   
2097 C  CB  A PRO   A 98  ? 0.1586 0.1714 0.0887 0.0166  -0.0043 -0.0042 98  PRO   A CB  
2098 C  CB  B PRO   A 98  ? 0.1665 0.1461 0.1154 0.0112  0.0143  0.0105  98  PRO   A CB  
2099 C  CG  A PRO   A 98  ? 0.1478 0.1596 0.1038 0.0234  -0.0014 -0.0076 98  PRO   A CG  
2100 C  CG  B PRO   A 98  ? 0.1691 0.1458 0.1287 0.0059  0.0121  0.0123  98  PRO   A CG  
2101 C  CD  A PRO   A 98  ? 0.1441 0.1511 0.0913 0.0134  0.0002  0.0092  98  PRO   A CD  
2102 C  CD  B PRO   A 98  ? 0.1577 0.1402 0.1179 0.0052  0.0098  0.0184  98  PRO   A CD  
2117 N  N   A ASN   A 99  ? 0.1534 0.1851 0.1034 -0.0078 0.0108  0.0213  99  ASN   A N   
2118 N  N   B ASN   A 99  ? 0.2188 0.1409 0.0937 -0.0005 0.0028  0.0260  99  ASN   A N   
2119 C  CA  A ASN   A 99  ? 0.1756 0.2028 0.1107 -0.0127 0.0060  0.0295  99  ASN   A CA  
2120 C  CA  B ASN   A 99  ? 0.2494 0.1439 0.0999 0.0066  -0.0079 0.0345  99  ASN   A CA  
2121 C  C   A ASN   A 99  ? 0.1889 0.2346 0.1038 -0.0330 -0.0037 0.0518  99  ASN   A C   
2122 C  C   B ASN   A 99  ? 0.2669 0.1527 0.1216 0.0057  -0.0230 0.0353  99  ASN   A C   
2123 O  O   A ASN   A 99  ? 0.1976 0.2557 0.1118 -0.0292 -0.0109 0.0390  99  ASN   A O   
2124 O  O   B ASN   A 99  ? 0.2697 0.1408 0.1279 0.0032  -0.0265 0.0136  99  ASN   A O   
2125 C  CB  A ASN   A 99  ? 0.1761 0.1961 0.1304 -0.0120 0.0002  0.0202  99  ASN   A CB  
2126 C  CB  B ASN   A 99  ? 0.2597 0.1389 0.1160 0.0126  -0.0128 0.0252  99  ASN   A CB  
2127 C  CG  A ASN   A 99  ? 0.1758 0.1845 0.1360 -0.0042 -0.0078 0.0060  99  ASN   A CG  
2128 C  CG  B ASN   A 99  ? 0.2673 0.1480 0.1325 0.0146  -0.0153 0.0170  99  ASN   A CG  
2129 O  OD1 A ASN   A 99  ? 0.1800 0.1938 0.1281 0.0101  -0.0121 0.0064  99  ASN   A OD1 
2130 O  OD1 B ASN   A 99  ? 0.2726 0.1586 0.1332 0.0139  -0.0157 0.0300  99  ASN   A OD1 
2131 N  ND2 A ASN   A 99  ? 0.1765 0.1820 0.1323 -0.0078 -0.0153 0.0086  99  ASN   A ND2 
2132 N  ND2 B ASN   A 99  ? 0.2699 0.1553 0.1485 0.0211  -0.0241 -0.0121 99  ASN   A ND2 
2145 N  N   A VAL   A 100 ? 0.2034 0.2542 0.1223 -0.0486 -0.0304 0.0601  100 VAL   A N   
2146 N  N   B VAL   A 100 ? 0.2789 0.1756 0.1597 0.0030  -0.0313 0.0412  100 VAL   A N   
2147 C  CA  A VAL   A 100 ? 0.2284 0.2772 0.1522 -0.0570 -0.0347 0.0526  100 VAL   A CA  
2148 C  CA  B VAL   A 100 ? 0.2893 0.1980 0.1871 0.0016  -0.0301 0.0365  100 VAL   A CA  
2149 C  C   A VAL   A 100 ? 0.2374 0.2870 0.1470 -0.0615 -0.0376 0.0694  100 VAL   A C   
2150 C  C   B VAL   A 100 ? 0.2961 0.1954 0.1768 0.0036  -0.0373 0.0396  100 VAL   A C   
2151 O  O   A VAL   A 100 ? 0.2418 0.2916 0.1529 -0.0580 -0.0163 0.0723  100 VAL   A O   
2152 O  O   B VAL   A 100 ? 0.2983 0.1863 0.1799 -0.0001 -0.0333 0.0355  100 VAL   A O   
2153 C  CB  A VAL   A 100 ? 0.2464 0.2875 0.2003 -0.0643 -0.0362 0.0328  100 VAL   A CB  
2154 C  CB  B VAL   A 100 ? 0.2924 0.2238 0.2278 0.0053  -0.0226 0.0206  100 VAL   A CB  
2155 C  CG1 A VAL   A 100 ? 0.2483 0.2960 0.2234 -0.0643 -0.0272 0.0315  100 VAL   A CG1 
2156 C  CG1 B VAL   A 100 ? 0.2935 0.2294 0.2456 0.0085  -0.0181 0.0153  100 VAL   A CG1 
2157 C  CG2 A VAL   A 100 ? 0.2546 0.2862 0.2097 -0.0691 -0.0453 0.0189  100 VAL   A CG2 
2158 C  CG2 B VAL   A 100 ? 0.2941 0.2356 0.2477 0.0028  -0.0218 0.0162  100 VAL   A CG2 
2177 N  N   A ASN   A 101 ? 0.2456 0.2969 0.1695 -0.0678 -0.0388 0.0863  101 ASN   A N   
2178 N  N   B ASN   A 101 ? 0.2990 0.2024 0.1740 0.0084  -0.0425 0.0471  101 ASN   A N   
2179 C  CA  A ASN   A 101 ? 0.2659 0.3089 0.1817 -0.0671 -0.0375 0.1013  101 ASN   A CA  
2180 C  CA  B ASN   A 101 ? 0.3024 0.2106 0.1846 0.0105  -0.0379 0.0488  101 ASN   A CA  
2181 C  C   A ASN   A 101 ? 0.2909 0.3373 0.2133 -0.0729 -0.0136 0.1190  101 ASN   A C   
2182 C  C   B ASN   A 101 ? 0.3107 0.2255 0.1902 0.0117  -0.0164 0.0647  101 ASN   A C   
2183 O  O   A ASN   A 101 ? 0.3034 0.3423 0.2453 -0.0703 -0.0120 0.1157  101 ASN   A O   
2184 O  O   B ASN   A 101 ? 0.3171 0.2315 0.1910 0.0086  -0.0091 0.0681  101 ASN   A O   
2185 C  CB  A ASN   A 101 ? 0.2639 0.2941 0.1724 -0.0594 -0.0521 0.0944  101 ASN   A CB  
2186 C  CB  B ASN   A 101 ? 0.2977 0.2055 0.1870 0.0070  -0.0432 0.0453  101 ASN   A CB  
2187 C  CG  A ASN   A 101 ? 0.2617 0.2823 0.1749 -0.0529 -0.0583 0.0709  101 ASN   A CG  
2188 C  CG  B ASN   A 101 ? 0.2955 0.2088 0.2026 0.0008  -0.0453 0.0416  101 ASN   A CG  
2189 O  OD1 A ASN   A 101 ? 0.2585 0.2770 0.1972 -0.0414 -0.0539 0.0368  101 ASN   A OD1 
2190 O  OD1 B ASN   A 101 ? 0.2982 0.2136 0.2132 -0.0065 -0.0447 0.0438  101 ASN   A OD1 
2191 N  ND2 A ASN   A 101 ? 0.2628 0.2787 0.1744 -0.0590 -0.0608 0.0720  101 ASN   A ND2 
2192 N  ND2 B ASN   A 101 ? 0.2915 0.2033 0.2133 0.0013  -0.0399 0.0295  101 ASN   A ND2 
2205 N  N   A LYS   A 102 ? 0.2990 0.3609 0.2341 -0.0835 0.0007  0.1219  102 LYS   A N   
2206 N  N   B LYS   A 102 ? 0.3138 0.2380 0.2241 0.0135  0.0018  0.0649  102 LYS   A N   
2207 C  CA  A LYS   A 102 ? 0.3132 0.3825 0.2383 -0.0874 0.0002  0.1149  102 LYS   A CA  
2208 C  CA  B LYS   A 102 ? 0.3189 0.2509 0.2407 0.0106  0.0159  0.0668  102 LYS   A CA  
2209 C  C   A LYS   A 102 ? 0.3214 0.3984 0.2261 -0.0773 0.0032  0.1072  102 LYS   A C   
2210 C  C   B LYS   A 102 ? 0.3184 0.2499 0.2239 0.0089  0.0096  0.0817  102 LYS   A C   
2211 O  O   A LYS   A 102 ? 0.3253 0.4063 0.2312 -0.0723 0.0097  0.1017  102 LYS   A O   
2212 O  O   B LYS   A 102 ? 0.3195 0.2465 0.2123 0.0055  0.0156  0.0986  102 LYS   A O   
2213 C  CB  A LYS   A 102 ? 0.3244 0.3889 0.2774 -0.0972 -0.0094 0.0973  102 LYS   A CB  
2214 C  CB  B LYS   A 102 ? 0.3240 0.2650 0.2758 0.0086  0.0229  0.0503  102 LYS   A CB  
2215 C  CG  A LYS   A 102 ? 0.3355 0.3937 0.3092 -0.1030 -0.0183 0.0808  102 LYS   A CG  
2216 C  CG  B LYS   A 102 ? 0.3276 0.2775 0.3000 0.0051  0.0298  0.0390  102 LYS   A CG  
2217 C  CD  A LYS   A 102 ? 0.3485 0.3993 0.3432 -0.1054 -0.0240 0.0617  102 LYS   A CD  
2218 C  CD  B LYS   A 102 ? 0.3326 0.2888 0.3248 0.0026  0.0352  0.0297  102 LYS   A CD  
2219 C  CE  A LYS   A 102 ? 0.3584 0.4014 0.3734 -0.1068 -0.0292 0.0504  102 LYS   A CE  
2220 C  CE  B LYS   A 102 ? 0.3370 0.2972 0.3453 0.0011  0.0371  0.0273  102 LYS   A CE  
2221 N  NZ  A LYS   A 102 ? 0.3633 0.4018 0.3851 -0.1093 -0.0311 0.0434  102 LYS   A NZ  
2222 N  NZ  B LYS   A 102 ? 0.3390 0.3016 0.3525 0.0028  0.0400  0.0265  102 LYS   A NZ  
2249 N  N   A GLY   A 103 ? 0.3224 0.4074 0.2423 -0.0685 -0.0058 0.0853  103 GLY   A N   
2250 N  N   B GLY   A 103 ? 0.3169 0.2542 0.2163 0.0094  -0.0107 0.0751  103 GLY   A N   
2251 C  CA  A GLY   A 103 ? 0.3232 0.4127 0.2412 -0.0579 -0.0037 0.0696  103 GLY   A CA  
2252 C  CA  B GLY   A 103 ? 0.3134 0.2531 0.2011 0.0069  -0.0210 0.0761  103 GLY   A CA  
2253 C  C   A GLY   A 103 ? 0.3203 0.4172 0.2455 -0.0502 0.0049  0.0572  103 GLY   A C   
2254 C  C   B GLY   A 103 ? 0.3046 0.2461 0.1720 0.0020  -0.0215 0.0747  103 GLY   A C   
2255 O  O   A GLY   A 103 ? 0.3285 0.4215 0.2602 -0.0511 0.0091  0.0537  103 GLY   A O   
2256 O  O   B GLY   A 103 ? 0.3105 0.2495 0.1627 0.0018  -0.0270 0.0771  103 GLY   A O   
2263 N  N   A GLU   A 104 ? 0.3053 0.4133 0.2198 -0.0454 0.0126  0.0441  104 GLU   A N   
2264 N  N   B GLU   A 104 ? 0.2879 0.2348 0.1584 0.0008  -0.0257 0.0681  104 GLU   A N   
2265 C  CA  A GLU   A 104 ? 0.2855 0.4046 0.1965 -0.0471 0.0190  0.0292  104 GLU   A CA  
2266 C  CA  B GLU   A 104 ? 0.2703 0.2209 0.1436 -0.0043 -0.0268 0.0548  104 GLU   A CA  
2267 C  C   A GLU   A 104 ? 0.2890 0.4109 0.1961 -0.0432 0.0167  0.0089  104 GLU   A C   
2268 C  C   B GLU   A 104 ? 0.2625 0.2140 0.1500 0.0023  -0.0258 0.0319  104 GLU   A C   
2269 O  O   A GLU   A 104 ? 0.2848 0.4127 0.2112 -0.0429 0.0040  0.0098  104 GLU   A O   
2270 O  O   B GLU   A 104 ? 0.2600 0.2102 0.1779 0.0032  -0.0235 0.0306  104 GLU   A O   
2271 C  CB  A GLU   A 104 ? 0.2570 0.3883 0.1736 -0.0548 0.0271  0.0401  104 GLU   A CB  
2272 C  CB  B GLU   A 104 ? 0.2615 0.2176 0.1412 -0.0138 -0.0266 0.0592  104 GLU   A CB  
2273 C  CG  A GLU   A 104 ? 0.2362 0.3737 0.1696 -0.0596 0.0243  0.0496  104 GLU   A CG  
2274 C  CG  B GLU   A 104 ? 0.2610 0.2229 0.1557 -0.0224 -0.0284 0.0591  104 GLU   A CG  
2275 C  CD  A GLU   A 104 ? 0.2158 0.3584 0.1624 -0.0642 0.0249  0.0599  104 GLU   A CD  
2276 C  CD  B GLU   A 104 ? 0.2593 0.2255 0.1592 -0.0270 -0.0310 0.0621  104 GLU   A CD  
2277 O  OE1 A GLU   A 104 ? 0.2001 0.3461 0.1218 -0.0606 0.0203  0.0584  104 GLU   A OE1 
2278 O  OE1 B GLU   A 104 ? 0.2571 0.2258 0.1598 -0.0242 -0.0295 0.0632  104 GLU   A OE1 
2279 O  OE2 A GLU   A 104 ? 0.2264 0.3589 0.1894 -0.0694 0.0231  0.0713  104 GLU   A OE2 
2280 O  OE2 B GLU   A 104 ? 0.2666 0.2300 0.1653 -0.0355 -0.0312 0.0603  104 GLU   A OE2 
2293 N  N   A ASP   A 105 ? 0.2971 0.4149 0.2026 -0.0377 0.0256  -0.0155 105 ASP   A N   
2294 N  N   B ASP   A 105 ? 0.2653 0.2127 0.1582 0.0003  -0.0154 0.0112  105 ASP   A N   
2295 C  CA  A ASP   A 105 ? 0.3005 0.4165 0.2278 -0.0334 0.0312  -0.0380 105 ASP   A CA  
2296 C  CA  B ASP   A 105 ? 0.2671 0.2166 0.1854 0.0020  0.0002  -0.0173 105 ASP   A CA  
2297 C  C   A ASP   A 105 ? 0.2720 0.4005 0.1885 -0.0423 0.0231  -0.0585 105 ASP   A C   
2298 C  C   B ASP   A 105 ? 0.2524 0.2092 0.1666 -0.0056 0.0022  -0.0208 105 ASP   A C   
2299 O  O   A ASP   A 105 ? 0.2591 0.4001 0.1446 -0.0452 0.0242  -0.0737 105 ASP   A O   
2300 O  O   B ASP   A 105 ? 0.2376 0.2029 0.1358 -0.0055 0.0029  -0.0223 105 ASP   A O   
2301 C  CB  A ASP   A 105 ? 0.3273 0.4312 0.2863 -0.0221 0.0422  -0.0418 105 ASP   A CB  
2302 C  CB  B ASP   A 105 ? 0.2821 0.2307 0.2332 0.0114  0.0133  -0.0392 105 ASP   A CB  
2303 C  CG  A ASP   A 105 ? 0.3489 0.4436 0.3395 -0.0136 0.0454  -0.0469 105 ASP   A CG  
2304 C  CG  B ASP   A 105 ? 0.2945 0.2425 0.2709 0.0224  0.0173  -0.0560 105 ASP   A CG  
2305 O  OD1 A ASP   A 105 ? 0.3553 0.4483 0.3499 -0.0125 0.0435  -0.0566 105 ASP   A OD1 
2306 O  OD1 B ASP   A 105 ? 0.2978 0.2431 0.2673 0.0211  0.0156  -0.0668 105 ASP   A OD1 
2307 O  OD2 A ASP   A 105 ? 0.3595 0.4491 0.3694 -0.0108 0.0512  -0.0373 105 ASP   A OD2 
2308 O  OD2 B ASP   A 105 ? 0.3028 0.2523 0.3094 0.0260  0.0147  -0.0490 105 ASP   A OD2 
2317 N  N   A ILE   A 106 ? 0.2532 0.3833 0.2042 -0.0491 0.0037  -0.0630 106 ILE   A N   
2318 N  N   B ILE   A 106 ? 0.2501 0.2155 0.1892 -0.0081 -0.0033 -0.0109 106 ILE   A N   
2319 C  CA  A ILE   A 106 ? 0.2255 0.3620 0.2149 -0.0586 -0.0175 -0.0744 106 ILE   A CA  
2320 C  CA  B ILE   A 106 ? 0.2465 0.2237 0.2092 -0.0155 -0.0057 -0.0110 106 ILE   A CA  
2321 C  C   A ILE   A 106 ? 0.2041 0.3372 0.2126 -0.0749 -0.0166 -0.0922 106 ILE   A C   
2322 C  C   B ILE   A 106 ? 0.2457 0.2174 0.2043 -0.0154 -0.0007 0.0055  106 ILE   A C   
2323 O  O   A ILE   A 106 ? 0.1829 0.3301 0.2140 -0.0803 -0.0028 -0.0948 106 ILE   A O   
2324 O  O   B ILE   A 106 ? 0.2421 0.2194 0.2086 -0.0161 0.0043  0.0092  106 ILE   A O   
2325 C  CB  A ILE   A 106 ? 0.2246 0.3640 0.2429 -0.0475 -0.0372 -0.0559 106 ILE   A CB  
2326 C  CB  B ILE   A 106 ? 0.2473 0.2428 0.2356 -0.0226 -0.0167 -0.0178 106 ILE   A CB  
2327 C  CG1 A ILE   A 106 ? 0.2166 0.3625 0.2642 -0.0351 -0.0450 -0.0373 106 ILE   A CG1 
2328 C  CG1 B ILE   A 106 ? 0.2423 0.2521 0.2437 -0.0219 -0.0195 -0.0210 106 ILE   A CG1 
2329 C  CG2 A ILE   A 106 ? 0.2299 0.3652 0.2471 -0.0461 -0.0470 -0.0577 106 ILE   A CG2 
2330 C  CG2 B ILE   A 106 ? 0.2503 0.2493 0.2428 -0.0247 -0.0218 -0.0187 106 ILE   A CG2 
2331 C  CD1 A ILE   A 106 ? 0.2136 0.3609 0.2774 -0.0238 -0.0400 -0.0236 106 ILE   A CD1 
2332 C  CD1 B ILE   A 106 ? 0.2379 0.2558 0.2495 -0.0229 -0.0198 -0.0218 106 ILE   A CD1 
2355 N  N   A GLN   A 107 ? 0.2198 0.3209 0.2424 -0.0731 -0.0068 -0.1019 107 GLN   A N   
2356 N  N   B GLN   A 107 ? 0.2507 0.2066 0.2141 -0.0122 0.0005  0.0190  107 GLN   A N   
2357 C  CA  A GLN   A 107 ? 0.2401 0.3027 0.3058 -0.0570 0.0145  -0.0954 107 GLN   A CA  
2358 C  CA  B GLN   A 107 ? 0.2581 0.2072 0.2504 -0.0134 0.0039  0.0277  107 GLN   A CA  
2359 C  C   A GLN   A 107 ? 0.2169 0.2598 0.2870 -0.0479 0.0408  -0.0800 107 GLN   A C   
2360 C  C   B GLN   A 107 ? 0.2349 0.1832 0.2261 -0.0111 0.0112  0.0411  107 GLN   A C   
2361 O  O   A GLN   A 107 ? 0.2248 0.2587 0.3402 -0.0379 0.0565  -0.0818 107 GLN   A O   
2362 O  O   B GLN   A 107 ? 0.2367 0.1815 0.2296 -0.0081 0.0030  0.0451  107 GLN   A O   
2363 C  CB  A GLN   A 107 ? 0.2812 0.3262 0.3968 -0.0561 0.0026  -0.0905 107 GLN   A CB  
2364 C  CB  B GLN   A 107 ? 0.2851 0.2344 0.3089 -0.0198 -0.0068 0.0272  107 GLN   A CB  
2365 C  CG  A GLN   A 107 ? 0.3234 0.3503 0.4927 -0.0508 -0.0067 -0.0791 107 GLN   A CG  
2366 C  CG  B GLN   A 107 ? 0.3097 0.2597 0.3670 -0.0214 -0.0191 0.0356  107 GLN   A CG  
2367 C  CD  A GLN   A 107 ? 0.3549 0.3679 0.5730 -0.0476 -0.0134 -0.0669 107 GLN   A CD  
2368 C  CD  B GLN   A 107 ? 0.3310 0.2823 0.4161 -0.0204 -0.0273 0.0433  107 GLN   A CD  
2369 O  OE1 A GLN   A 107 ? 0.3671 0.3749 0.6055 -0.0463 -0.0161 -0.0630 107 GLN   A OE1 
2370 O  OE1 B GLN   A 107 ? 0.3390 0.2910 0.4301 -0.0187 -0.0289 0.0487  107 GLN   A OE1 
2371 N  NE2 A GLN   A 107 ? 0.3643 0.3735 0.5995 -0.0475 -0.0154 -0.0649 107 GLN   A NE2 
2372 N  NE2 B GLN   A 107 ? 0.3374 0.2888 0.4305 -0.0189 -0.0338 0.0475  107 GLN   A NE2 
2389 N  N   A LEU   A 108 ? 0.1878 0.2141 0.2180 -0.0437 0.0439  -0.0749 108 LEU   A N   
2390 N  N   B LEU   A 108 ? 0.2117 0.1710 0.2048 -0.0168 0.0227  0.0261  108 LEU   A N   
2391 C  CA  A LEU   A 108 ? 0.1735 0.1834 0.1966 -0.0173 0.0345  -0.0322 108 LEU   A CA  
2392 C  CA  B LEU   A 108 ? 0.1912 0.1631 0.1925 -0.0113 0.0255  0.0120  108 LEU   A CA  
2393 C  C   A LEU   A 108 ? 0.1574 0.1486 0.1843 -0.0081 0.0300  -0.0044 108 LEU   A C   
2394 C  C   B LEU   A 108 ? 0.1686 0.1449 0.1829 -0.0053 0.0261  0.0168  108 LEU   A C   
2395 O  O   A LEU   A 108 ? 0.1553 0.1485 0.1899 -0.0021 0.0359  -0.0026 108 LEU   A O   
2396 O  O   B LEU   A 108 ? 0.1683 0.1460 0.1871 -0.0016 0.0329  0.0195  108 LEU   A O   
2397 C  CB  A LEU   A 108 ? 0.1748 0.1959 0.1811 -0.0170 0.0415  -0.0160 108 LEU   A CB  
2398 C  CB  B LEU   A 108 ? 0.1920 0.1785 0.1827 -0.0210 0.0332  -0.0051 108 LEU   A CB  
2399 C  CG  A LEU   A 108 ? 0.1869 0.2139 0.2096 -0.0113 0.0499  -0.0056 108 LEU   A CG  
2400 C  CG  B LEU   A 108 ? 0.1961 0.1952 0.1960 -0.0260 0.0399  -0.0213 108 LEU   A CG  
2401 C  CD1 A LEU   A 108 ? 0.1962 0.2187 0.2140 -0.0146 0.0514  -0.0073 108 LEU   A CD1 
2402 C  CD1 B LEU   A 108 ? 0.1993 0.2003 0.1993 -0.0290 0.0438  -0.0286 108 LEU   A CD1 
2403 C  CD2 A LEU   A 108 ? 0.1918 0.2271 0.2517 -0.0036 0.0480  -0.0004 108 LEU   A CD2 
2404 C  CD2 B LEU   A 108 ? 0.1983 0.2028 0.2159 -0.0272 0.0383  -0.0242 108 LEU   A CD2 
2427 N  N   . LEU   A 109 ? 0.1493 0.1412 0.1733 -0.0005 0.0213  0.0172  109 LEU   A N   
2428 C  CA  . LEU   A 109 ? 0.1471 0.1342 0.1569 0.0035  0.0112  0.0151  109 LEU   A CA  
2429 C  C   . LEU   A 109 ? 0.1358 0.1285 0.1438 -0.0049 0.0130  0.0137  109 LEU   A C   
2430 O  O   . LEU   A 109 ? 0.1417 0.1207 0.1685 -0.0046 0.0033  0.0093  109 LEU   A O   
2431 C  CB  . LEU   A 109 ? 0.1495 0.1402 0.1855 0.0162  0.0049  0.0296  109 LEU   A CB  
2432 C  CG  . LEU   A 109 ? 0.1450 0.1435 0.1874 0.0074  0.0127  0.0395  109 LEU   A CG  
2433 C  CD1 . LEU   A 109 ? 0.1492 0.1322 0.2057 0.0030  0.0218  0.0206  109 LEU   A CD1 
2434 C  CD2 . LEU   A 109 ? 0.1430 0.1647 0.2057 0.0059  0.0140  0.0393  109 LEU   A CD2 
2447 N  N   . LYS   A 110 ? 0.1350 0.1285 0.1520 -0.0070 0.0040  0.0065  110 LYS   A N   
2448 C  CA  . LYS   A 110 ? 0.1329 0.1214 0.1619 -0.0050 0.0017  0.0124  110 LYS   A CA  
2449 C  C   . LYS   A 110 ? 0.1351 0.1170 0.1445 -0.0078 0.0114  -0.0037 110 LYS   A C   
2450 O  O   . LYS   A 110 ? 0.1284 0.1171 0.1632 -0.0071 0.0132  -0.0051 110 LYS   A O   
2451 C  CB  . LYS   A 110 ? 0.1400 0.1270 0.1882 -0.0053 0.0009  -0.0012 110 LYS   A CB  
2452 C  CG  . LYS   A 110 ? 0.1409 0.1272 0.1954 -0.0010 -0.0052 -0.0022 110 LYS   A CG  
2453 C  CD  . LYS   A 110 ? 0.1449 0.1323 0.2074 -0.0051 0.0000  -0.0085 110 LYS   A CD  
2454 C  CE  . LYS   A 110 ? 0.1486 0.1408 0.2165 -0.0057 0.0165  -0.0135 110 LYS   A CE  
2455 N  NZ  . LYS   A 110 ? 0.1513 0.1464 0.2310 -0.0179 0.0242  -0.0008 110 LYS   A NZ  
2469 N  N   . SER   A 111 ? 0.1324 0.1227 0.1453 0.0005  0.0084  0.0050  111 SER   A N   
2470 C  CA  . SER   A 111 ? 0.1252 0.1303 0.1511 0.0005  0.0147  0.0002  111 SER   A CA  
2471 C  C   . SER   A 111 ? 0.1206 0.1245 0.1519 -0.0119 0.0123  0.0060  111 SER   A C   
2472 O  O   . SER   A 111 ? 0.1344 0.1172 0.1626 -0.0058 0.0124  0.0081  111 SER   A O   
2473 C  CB  . SER   A 111 ? 0.1467 0.1480 0.1697 0.0010  0.0207  -0.0052 111 SER   A CB  
2474 O  OG  . SER   A 111 ? 0.1898 0.1705 0.1751 0.0044  0.0308  -0.0198 111 SER   A OG  
2480 N  N   . ALA   A 112 ? 0.1234 0.1155 0.1627 -0.0006 0.0140  0.0037  112 ALA   A N   
2481 C  CA  . ALA   A 112 ? 0.1311 0.1168 0.1550 -0.0020 0.0154  0.0046  112 ALA   A CA  
2482 C  C   . ALA   A 112 ? 0.1241 0.1105 0.1560 0.0001  0.0084  0.0064  112 ALA   A C   
2483 O  O   . ALA   A 112 ? 0.1283 0.1111 0.1634 -0.0115 0.0191  0.0046  112 ALA   A O   
2484 C  CB  . ALA   A 112 ? 0.1366 0.1207 0.1651 -0.0029 0.0149  0.0014  112 ALA   A CB  
2490 N  N   . TYR   A 113 ? 0.1167 0.1132 0.1565 -0.0007 0.0129  0.0120  113 TYR   A N   
2491 C  CA  . TYR   A 113 ? 0.1182 0.1124 0.1575 -0.0008 0.0173  0.0141  113 TYR   A CA  
2492 C  C   . TYR   A 113 ? 0.1148 0.1106 0.1477 -0.0090 0.0136  0.0075  113 TYR   A C   
2493 O  O   . TYR   A 113 ? 0.1189 0.1206 0.1661 -0.0063 0.0166  0.0058  113 TYR   A O   
2494 C  CB  . TYR   A 113 ? 0.1170 0.1214 0.1715 -0.0055 0.0082  0.0209  113 TYR   A CB  
2495 C  CG  . TYR   A 113 ? 0.1189 0.1183 0.1546 -0.0089 0.0115  0.0211  113 TYR   A CG  
2496 C  CD1 . TYR   A 113 ? 0.1231 0.1282 0.1499 0.0018  0.0119  0.0200  113 TYR   A CD1 
2497 C  CD2 . TYR   A 113 ? 0.1227 0.1250 0.1508 -0.0067 0.0040  0.0202  113 TYR   A CD2 
2498 C  CE1 . TYR   A 113 ? 0.1218 0.1328 0.1495 0.0010  0.0131  0.0195  113 TYR   A CE1 
2499 C  CE2 . TYR   A 113 ? 0.1231 0.1320 0.1551 -0.0102 -0.0007 0.0224  113 TYR   A CE2 
2500 C  CZ  . TYR   A 113 ? 0.1229 0.1330 0.1541 0.0032  0.0089  0.0238  113 TYR   A CZ  
2501 O  OH  . TYR   A 113 ? 0.1234 0.1407 0.1674 0.0115  0.0069  0.0213  113 TYR   A OH  
2511 N  N   . GLU   A 114 ? 0.1141 0.1109 0.1560 -0.0053 0.0152  0.0101  114 GLU   A N   
2512 C  CA  . GLU   A 114 ? 0.1190 0.1050 0.1696 0.0063  0.0082  0.0156  114 GLU   A CA  
2513 C  C   . GLU   A 114 ? 0.1152 0.1151 0.1699 0.0058  0.0135  0.0127  114 GLU   A C   
2514 O  O   . GLU   A 114 ? 0.1229 0.1172 0.1719 0.0002  0.0066  0.0115  114 GLU   A O   
2515 C  CB  . GLU   A 114 ? 0.1184 0.1122 0.1638 -0.0061 0.0099  0.0086  114 GLU   A CB  
2516 C  CG  . GLU   A 114 ? 0.1272 0.1164 0.1693 -0.0017 0.0111  0.0040  114 GLU   A CG  
2517 C  CD  . GLU   A 114 ? 0.1354 0.1177 0.1777 -0.0064 0.0093  0.0059  114 GLU   A CD  
2518 O  OE1 . GLU   A 114 ? 0.1393 0.1202 0.1833 -0.0101 0.0155  -0.0048 114 GLU   A OE1 
2519 O  OE2 . GLU   A 114 ? 0.1515 0.1225 0.2036 -0.0118 0.0130  -0.0094 114 GLU   A OE2 
2526 N  N   . ASN   A 115 ? 0.1187 0.1155 0.1554 -0.0052 0.0134  0.0044  115 ASN   A N   
2527 C  CA  . ASN   A 115 ? 0.1196 0.1218 0.1635 -0.0063 0.0125  0.0122  115 ASN   A CA  
2528 C  C   . ASN   A 115 ? 0.1209 0.1171 0.1413 -0.0081 0.0030  0.0193  115 ASN   A C   
2529 O  O   . ASN   A 115 ? 0.1219 0.1347 0.1547 -0.0090 0.0074  0.0196  115 ASN   A O   
2530 C  CB  . ASN   A 115 ? 0.1296 0.1248 0.1523 -0.0133 0.0110  0.0052  115 ASN   A CB  
2531 C  CG  . ASN   A 115 ? 0.1273 0.1451 0.1613 -0.0162 0.0211  0.0099  115 ASN   A CG  
2532 O  OD1 . ASN   A 115 ? 0.1310 0.2432 0.1933 -0.0133 0.0269  0.0208  115 ASN   A OD1 
2533 N  ND2 . ASN   A 115 ? 0.1307 0.1286 0.1601 -0.0093 0.0229  0.0169  115 ASN   A ND2 
2540 N  N   . PHE   A 116 ? 0.1137 0.1174 0.1546 0.0009  0.0105  0.0237  116 PHE   A N   
2541 C  CA  . PHE   A 116 ? 0.1200 0.1263 0.1409 0.0006  0.0113  0.0147  116 PHE   A CA  
2542 C  C   . PHE   A 116 ? 0.1145 0.1343 0.1539 -0.0086 0.0129  0.0176  116 PHE   A C   
2543 O  O   . PHE   A 116 ? 0.1248 0.1305 0.1645 0.0018  0.0142  0.0258  116 PHE   A O   
2544 C  CB  . PHE   A 116 ? 0.1211 0.1162 0.1544 -0.0028 0.0149  0.0150  116 PHE   A CB  
2545 C  CG  . PHE   A 116 ? 0.1215 0.1186 0.1455 0.0003  0.0132  0.0107  116 PHE   A CG  
2546 C  CD1 . PHE   A 116 ? 0.1235 0.1193 0.1534 -0.0066 0.0126  0.0134  116 PHE   A CD1 
2547 C  CD2 . PHE   A 116 ? 0.1267 0.1204 0.1641 -0.0054 0.0164  0.0164  116 PHE   A CD2 
2548 C  CE1 . PHE   A 116 ? 0.1247 0.1167 0.1627 -0.0131 0.0093  0.0134  116 PHE   A CE1 
2549 C  CE2 . PHE   A 116 ? 0.1208 0.1177 0.1718 -0.0064 0.0137  0.0136  116 PHE   A CE2 
2550 C  CZ  . PHE   A 116 ? 0.1274 0.1061 0.1561 -0.0006 -0.0014 0.0128  116 PHE   A CZ  
2560 N  N   . ASN   A 117 ? 0.1181 0.1292 0.1669 -0.0006 0.0170  0.0212  117 ASN   A N   
2561 C  CA  . ASN   A 117 ? 0.1194 0.1222 0.1783 -0.0030 0.0137  0.0236  117 ASN   A CA  
2562 C  C   . ASN   A 117 ? 0.1222 0.1305 0.1870 0.0030  0.0149  0.0251  117 ASN   A C   
2563 O  O   . ASN   A 117 ? 0.1295 0.1338 0.2089 -0.0060 -0.0060 0.0387  117 ASN   A O   
2564 C  CB  . ASN   A 117 ? 0.1206 0.1289 0.1796 0.0003  0.0148  0.0302  117 ASN   A CB  
2565 C  CG  . ASN   A 117 ? 0.1167 0.1276 0.1767 -0.0039 0.0175  0.0293  117 ASN   A CG  
2566 O  OD1 . ASN   A 117 ? 0.1204 0.1506 0.1895 -0.0136 0.0125  0.0213  117 ASN   A OD1 
2567 N  ND2 . ASN   A 117 ? 0.1142 0.1232 0.1802 -0.0037 0.0107  0.0223  117 ASN   A ND2 
2574 N  N   . GLN   A 118 ? 0.1194 0.1321 0.1849 -0.0046 0.0033  0.0280  118 GLN   A N   
2575 C  CA  . GLN   A 118 ? 0.1238 0.1429 0.1972 -0.0027 0.0047  0.0238  118 GLN   A CA  
2576 C  C   . GLN   A 118 ? 0.1274 0.1540 0.1851 -0.0064 -0.0000 0.0314  118 GLN   A C   
2577 O  O   . GLN   A 118 ? 0.1292 0.1860 0.2104 -0.0034 -0.0114 0.0109  118 GLN   A O   
2578 C  CB  . GLN   A 118 ? 0.1152 0.1442 0.2078 -0.0042 0.0155  0.0257  118 GLN   A CB  
2579 C  CG  . GLN   A 118 ? 0.1198 0.1481 0.2095 -0.0029 0.0095  0.0293  118 GLN   A CG  
2580 C  CD  . GLN   A 118 ? 0.1174 0.1544 0.2136 -0.0008 0.0028  0.0217  118 GLN   A CD  
2581 O  OE1 . GLN   A 118 ? 0.1245 0.1638 0.2237 0.0114  0.0005  0.0135  118 GLN   A OE1 
2582 N  NE2 . GLN   A 118 ? 0.1265 0.1504 0.2116 0.0013  0.0005  0.0269  118 GLN   A NE2 
2591 N  N   . HIS   A 119 ? 0.1311 0.1484 0.1682 -0.0028 0.0039  0.0344  119 HIS   A N   
2592 C  CA  . HIS   A 119 ? 0.1392 0.1530 0.1723 -0.0066 0.0013  0.0381  119 HIS   A CA  
2593 C  C   . HIS   A 119 ? 0.1428 0.1614 0.1666 -0.0063 0.0050  0.0359  119 HIS   A C   
2594 O  O   . HIS   A 119 ? 0.1478 0.1692 0.1709 -0.0239 0.0001  0.0361  119 HIS   A O   
2595 C  CB  . HIS   A 119 ? 0.1441 0.1525 0.1927 -0.0086 0.0168  0.0336  119 HIS   A CB  
2596 C  CG  . HIS   A 119 ? 0.1439 0.1555 0.2391 0.0062  0.0128  0.0463  119 HIS   A CG  
2597 N  ND1 . HIS   A 119 ? 0.1566 0.1696 0.2944 -0.0039 0.0040  0.0351  119 HIS   A ND1 
2598 C  CD2 . HIS   A 119 ? 0.1537 0.1684 0.2565 0.0139  0.0298  0.0686  119 HIS   A CD2 
2599 C  CE1 . HIS   A 119 ? 0.1551 0.1694 0.3033 -0.0081 0.0213  0.0611  119 HIS   A CE1 
2600 N  NE2 . HIS   A 119 ? 0.1638 0.1703 0.2942 0.0044  0.0403  0.0779  119 HIS   A NE2 
2608 N  N   . GLU   A 120 ? 0.1510 0.1828 0.1758 -0.0056 -0.0077 0.0578  120 GLU   A N   
2609 C  CA  . GLU   A 120 ? 0.1694 0.2091 0.2024 0.0040  -0.0116 0.0936  120 GLU   A CA  
2610 C  C   . GLU   A 120 ? 0.1527 0.1944 0.1739 -0.0063 -0.0058 0.0869  120 GLU   A C   
2611 O  O   . GLU   A 120 ? 0.1532 0.1887 0.1820 -0.0151 -0.0011 0.0810  120 GLU   A O   
2612 C  CB  . GLU   A 120 ? 0.2298 0.2704 0.2558 0.0177  -0.0069 0.1331  120 GLU   A CB  
2613 C  CG  . GLU   A 120 ? 0.3171 0.3357 0.3545 0.0326  -0.0067 0.1409  120 GLU   A CG  
2614 C  CD  . GLU   A 120 ? 0.3889 0.3904 0.4663 0.0475  0.0010  0.1269  120 GLU   A CD  
2615 O  OE1 . GLU   A 120 ? 0.4114 0.4099 0.4914 0.0500  0.0038  0.1201  120 GLU   A OE1 
2616 O  OE2 . GLU   A 120 ? 0.4230 0.4230 0.5169 0.0521  0.0035  0.1226  120 GLU   A OE2 
2623 N  N   . VAL   A 121 ? 0.1528 0.1985 0.1507 -0.0103 -0.0012 0.0688  121 VAL   A N   
2624 C  CA  . VAL   A 121 ? 0.1612 0.2037 0.1291 -0.0112 0.0041  0.0660  121 VAL   A CA  
2625 C  C   . VAL   A 121 ? 0.1511 0.1841 0.1176 -0.0218 -0.0058 0.0510  121 VAL   A C   
2626 O  O   . VAL   A 121 ? 0.1521 0.1842 0.1456 -0.0267 -0.0094 0.0433  121 VAL   A O   
2627 C  CB  . VAL   A 121 ? 0.1990 0.2416 0.1709 0.0039  0.0137  0.0750  121 VAL   A CB  
2628 C  CG1 . VAL   A 121 ? 0.2003 0.2620 0.1584 0.0110  0.0315  0.0738  121 VAL   A CG1 
2629 C  CG2 . VAL   A 121 ? 0.2245 0.2587 0.2248 -0.0068 0.0142  0.0641  121 VAL   A CG2 
2639 N  N   . LEU   A 122 ? 0.1393 0.1646 0.1265 -0.0222 0.0042  0.0443  122 LEU   A N   
2640 C  CA  . LEU   A 122 ? 0.1434 0.1489 0.1201 -0.0167 0.0135  0.0406  122 LEU   A CA  
2641 C  C   . LEU   A 122 ? 0.1412 0.1509 0.1239 -0.0251 -0.0026 0.0339  122 LEU   A C   
2642 O  O   . LEU   A 122 ? 0.1413 0.1531 0.1560 -0.0256 -0.0021 0.0336  122 LEU   A O   
2643 C  CB  . LEU   A 122 ? 0.1576 0.1505 0.1540 -0.0091 0.0037  0.0425  122 LEU   A CB  
2644 C  CG  . LEU   A 122 ? 0.1587 0.1555 0.1565 -0.0034 0.0160  0.0361  122 LEU   A CG  
2645 C  CD1 . LEU   A 122 ? 0.1741 0.1601 0.1791 -0.0121 0.0193  0.0356  122 LEU   A CD1 
2646 C  CD2 . LEU   A 122 ? 0.1543 0.1487 0.1660 -0.0029 0.0225  0.0271  122 LEU   A CD2 
2658 N  N   . LEU   A 123 ? 0.1363 0.1465 0.1253 -0.0225 -0.0067 0.0309  123 LEU   A N   
2659 C  CA  . LEU   A 123 ? 0.1344 0.1451 0.1214 -0.0178 -0.0041 0.0261  123 LEU   A CA  
2660 C  C   . LEU   A 123 ? 0.1343 0.1373 0.1077 -0.0158 0.0001  0.0292  123 LEU   A C   
2661 O  O   . LEU   A 123 ? 0.1254 0.1530 0.1275 -0.0255 0.0004  0.0338  123 LEU   A O   
2662 C  CB  . LEU   A 123 ? 0.1439 0.1508 0.1201 -0.0214 0.0044  0.0281  123 LEU   A CB  
2663 C  CG  . LEU   A 123 ? 0.1460 0.1723 0.1344 -0.0159 0.0120  0.0120  123 LEU   A CG  
2664 C  CD1 . LEU   A 123 ? 0.1464 0.1794 0.1491 -0.0080 0.0112  0.0104  123 LEU   A CD1 
2665 C  CD2 . LEU   A 123 ? 0.1604 0.1770 0.1461 -0.0163 0.0072  0.0100  123 LEU   A CD2 
2677 N  N   A ALA   A 124 ? 0.1280 0.1317 0.0954 -0.0072 -0.0018 0.0189  124 ALA   A N   
2678 N  N   B ALA   A 124 ? 0.1299 0.1322 0.1246 -0.0204 0.0024  0.0186  124 ALA   A N   
2679 C  CA  A ALA   A 124 ? 0.1236 0.1247 0.0913 0.0026  -0.0033 0.0178  124 ALA   A CA  
2680 C  CA  B ALA   A 124 ? 0.1274 0.1285 0.1440 -0.0268 0.0028  0.0188  124 ALA   A CA  
2681 C  C   A ALA   A 124 ? 0.1188 0.1250 0.0981 0.0021  0.0086  0.0203  124 ALA   A C   
2682 C  C   B ALA   A 124 ? 0.1208 0.1188 0.1408 -0.0191 0.0041  0.0216  124 ALA   A C   
2683 O  O   A ALA   A 124 ? 0.1195 0.1319 0.1158 -0.0024 0.0185  0.0178  124 ALA   A O   
2684 O  O   B ALA   A 124 ? 0.1173 0.1169 0.1549 -0.0140 0.0126  0.0156  124 ALA   A O   
2685 C  CB  A ALA   A 124 ? 0.1182 0.1179 0.1257 0.0150  -0.0015 0.0291  124 ALA   A CB  
2686 C  CB  B ALA   A 124 ? 0.1293 0.1264 0.1627 -0.0338 0.0142  0.0256  124 ALA   A CB  
2697 N  N   A PRO   A 125 ? 0.1182 0.1254 0.1138 0.0044  0.0117  0.0298  125 PRO   A N   
2698 N  N   B PRO   A 125 ? 0.1101 0.1090 0.1084 -0.0109 -0.0026 0.0224  125 PRO   A N   
2699 C  CA  A PRO   A 125 ? 0.1233 0.1312 0.1377 -0.0014 0.0049  0.0208  125 PRO   A CA  
2700 C  CA  B PRO   A 125 ? 0.1146 0.1119 0.1120 -0.0110 -0.0027 0.0208  125 PRO   A CA  
2701 C  C   A PRO   A 125 ? 0.1162 0.1337 0.1316 -0.0032 0.0095  0.0200  125 PRO   A C   
2702 C  C   B PRO   A 125 ? 0.1191 0.1201 0.1198 -0.0109 -0.0058 0.0200  125 PRO   A C   
2703 O  O   A PRO   A 125 ? 0.1256 0.1342 0.1349 0.0049  0.0071  0.0145  125 PRO   A O   
2704 O  O   B PRO   A 125 ? 0.1265 0.1207 0.1319 -0.0068 -0.0077 0.0144  125 PRO   A O   
2705 C  CB  A PRO   A 125 ? 0.1331 0.1351 0.1451 -0.0050 0.0041  0.0184  125 PRO   A CB  
2706 C  CB  B PRO   A 125 ? 0.1112 0.1069 0.0924 -0.0117 -0.0051 0.0253  125 PRO   A CB  
2707 C  CG  A PRO   A 125 ? 0.1388 0.1344 0.1518 -0.0048 0.0086  0.0216  125 PRO   A CG  
2708 C  CG  B PRO   A 125 ? 0.1057 0.1027 0.0933 -0.0093 0.0035  0.0202  125 PRO   A CG  
2709 C  CD  A PRO   A 125 ? 0.1245 0.1310 0.1359 0.0012  0.0170  0.0183  125 PRO   A CD  
2710 C  CD  B PRO   A 125 ? 0.0965 0.0942 0.0888 -0.0073 0.0035  0.0152  125 PRO   A CD  
2725 N  N   A LEU   A 126 ? 0.1065 0.1319 0.1282 -0.0007 0.0094  0.0177  126 LEU   A N   
2726 N  N   B LEU   A 126 ? 0.1211 0.1250 0.1287 -0.0097 -0.0071 0.0154  126 LEU   A N   
2727 C  CA  A LEU   A 126 ? 0.1129 0.1358 0.1440 0.0027  0.0044  0.0217  126 LEU   A CA  
2728 C  CA  B LEU   A 126 ? 0.1220 0.1237 0.1294 -0.0050 -0.0013 0.0201  126 LEU   A CA  
2729 C  C   A LEU   A 126 ? 0.1195 0.1343 0.1342 0.0045  -0.0014 0.0204  126 LEU   A C   
2730 C  C   B LEU   A 126 ? 0.1191 0.1181 0.1199 -0.0017 0.0026  0.0152  126 LEU   A C   
2731 O  O   A LEU   A 126 ? 0.1300 0.1452 0.1458 0.0186  0.0097  0.0227  126 LEU   A O   
2732 O  O   B LEU   A 126 ? 0.1250 0.1207 0.1294 -0.0019 -0.0003 0.0219  126 LEU   A O   
2733 C  CB  A LEU   A 126 ? 0.1163 0.1338 0.1542 0.0030  0.0078  0.0141  126 LEU   A CB  
2734 C  CB  B LEU   A 126 ? 0.1221 0.1262 0.1362 -0.0056 0.0031  0.0041  126 LEU   A CB  
2735 C  CG  A LEU   A 126 ? 0.1172 0.1339 0.1830 0.0064  0.0140  0.0085  126 LEU   A CG  
2736 C  CG  B LEU   A 126 ? 0.1185 0.1246 0.1508 -0.0028 0.0101  -0.0079 126 LEU   A CG  
2737 C  CD1 A LEU   A 126 ? 0.1261 0.1404 0.2232 0.0009  0.0091  0.0091  126 LEU   A CD1 
2738 C  CD1 B LEU   A 126 ? 0.1203 0.1216 0.1686 -0.0040 0.0026  -0.0197 126 LEU   A CD1 
2739 C  CD2 A LEU   A 126 ? 0.1269 0.1339 0.1716 0.0017  0.0193  0.0111  126 LEU   A CD2 
2740 C  CD2 B LEU   A 126 ? 0.1154 0.1262 0.1530 0.0013  0.0108  -0.0009 126 LEU   A CD2 
2763 N  N   A LEU   A 127 ? 0.1220 0.1360 0.1424 0.0005  0.0057  0.0172  127 LEU   A N   
2764 N  N   B LEU   A 127 ? 0.1188 0.1192 0.1126 0.0016  0.0110  0.0156  127 LEU   A N   
2765 C  CA  A LEU   A 127 ? 0.1222 0.1318 0.1266 -0.0023 0.0030  0.0161  127 LEU   A CA  
2766 C  CA  B LEU   A 127 ? 0.1219 0.1224 0.1277 0.0004  0.0080  0.0199  127 LEU   A CA  
2767 C  C   A LEU   A 127 ? 0.1235 0.1246 0.1111 -0.0047 0.0026  0.0143  127 LEU   A C   
2768 C  C   B LEU   A 127 ? 0.1257 0.1230 0.1439 0.0018  0.0019  0.0103  127 LEU   A C   
2769 O  O   A LEU   A 127 ? 0.1277 0.1278 0.1172 -0.0132 -0.0010 0.0088  127 LEU   A O   
2770 O  O   B LEU   A 127 ? 0.1299 0.1292 0.1478 -0.0032 0.0077  0.0139  127 LEU   A O   
2771 C  CB  A LEU   A 127 ? 0.1239 0.1347 0.1372 0.0080  0.0078  0.0175  127 LEU   A CB  
2772 C  CB  B LEU   A 127 ? 0.1232 0.1344 0.1374 -0.0003 0.0026  0.0201  127 LEU   A CB  
2773 C  CG  A LEU   A 127 ? 0.1288 0.1349 0.1356 0.0045  -0.0023 0.0156  127 LEU   A CG  
2774 C  CG  B LEU   A 127 ? 0.1298 0.1475 0.1378 0.0022  -0.0095 0.0202  127 LEU   A CG  
2775 C  CD1 A LEU   A 127 ? 0.1311 0.1267 0.1539 0.0032  -0.0016 0.0091  127 LEU   A CD1 
2776 C  CD1 B LEU   A 127 ? 0.1283 0.1568 0.1584 0.0064  -0.0087 0.0217  127 LEU   A CD1 
2777 C  CD2 A LEU   A 127 ? 0.1354 0.1367 0.1430 0.0098  -0.0076 0.0076  127 LEU   A CD2 
2778 C  CD2 B LEU   A 127 ? 0.1351 0.1534 0.1304 -0.0044 -0.0187 0.0071  127 LEU   A CD2 
2801 N  N   A SER   A 128 ? 0.1247 0.1249 0.1058 -0.0072 0.0033  0.0182  128 SER   A N   
2802 N  N   B SER   A 128 ? 0.1290 0.1218 0.1496 -0.0008 -0.0074 0.0055  128 SER   A N   
2803 C  CA  A SER   A 128 ? 0.1351 0.1264 0.0973 -0.0006 0.0048  0.0126  128 SER   A CA  
2804 C  CA  B SER   A 128 ? 0.1317 0.1225 0.1459 0.0028  -0.0055 -0.0018 128 SER   A CA  
2805 C  C   A SER   A 128 ? 0.1397 0.1333 0.0955 0.0076  0.0081  0.0125  128 SER   A C   
2806 C  C   B SER   A 128 ? 0.1296 0.1253 0.1398 0.0047  -0.0192 0.0030  128 SER   A C   
2807 O  O   A SER   A 128 ? 0.1443 0.1479 0.1129 0.0100  0.0161  0.0125  128 SER   A O   
2808 O  O   B SER   A 128 ? 0.1272 0.1259 0.1418 0.0068  -0.0188 0.0091  128 SER   A O   
2809 C  CB  A SER   A 128 ? 0.1368 0.1222 0.0997 0.0008  0.0046  0.0115  128 SER   A CB  
2810 C  CB  B SER   A 128 ? 0.1357 0.1241 0.1563 0.0025  -0.0035 0.0019  128 SER   A CB  
2811 O  OG  A SER   A 128 ? 0.1404 0.1275 0.1118 0.0047  0.0099  0.0084  128 SER   A OG  
2812 O  OG  B SER   A 128 ? 0.1326 0.1302 0.1626 0.0017  0.0040  0.0086  128 SER   A OG  
2823 N  N   A ALA   A 129 ? 0.1351 0.1356 0.0981 0.0055  0.0004  0.0116  129 ALA   A N   
2824 N  N   B ALA   A 129 ? 0.1262 0.1305 0.1483 0.0062  -0.0244 0.0000  129 ALA   A N   
2825 C  CA  A ALA   A 129 ? 0.1302 0.1367 0.1052 0.0056  -0.0009 0.0063  129 ALA   A CA  
2826 C  CA  B ALA   A 129 ? 0.1314 0.1391 0.1510 0.0060  -0.0190 0.0008  129 ALA   A CA  
2827 C  C   A ALA   A 129 ? 0.1312 0.1289 0.0948 0.0039  -0.0003 -0.0046 129 ALA   A C   
2828 C  C   B ALA   A 129 ? 0.1418 0.1480 0.1544 0.0101  -0.0191 0.0066  129 ALA   A C   
2829 O  O   A ALA   A 129 ? 0.1326 0.1316 0.1111 -0.0008 0.0033  0.0068  129 ALA   A O   
2830 O  O   B ALA   A 129 ? 0.1454 0.1531 0.1600 0.0047  -0.0148 0.0064  129 ALA   A O   
2831 C  CB  A ALA   A 129 ? 0.1365 0.1506 0.1275 0.0058  0.0117  0.0173  129 ALA   A CB  
2832 C  CB  B ALA   A 129 ? 0.1355 0.1427 0.1617 -0.0037 -0.0139 -0.0071 129 ALA   A CB  
2843 N  N   A GLY   A 130 ? 0.1337 0.1247 0.1220 -0.0011 0.0036  -0.0048 130 GLY   A N   
2844 N  N   B GLY   A 130 ? 0.1478 0.1476 0.1453 0.0113  -0.0242 0.0059  130 GLY   A N   
2845 C  CA  A GLY   A 130 ? 0.1467 0.1286 0.1285 0.0011  0.0096  -0.0115 130 GLY   A CA  
2846 C  CA  B GLY   A 130 ? 0.1604 0.1511 0.1507 0.0102  -0.0159 0.0072  130 GLY   A CA  
2847 C  C   A GLY   A 130 ? 0.1447 0.1325 0.1227 0.0059  0.0100  -0.0044 130 GLY   A C   
2848 C  C   B GLY   A 130 ? 0.1649 0.1504 0.1480 0.0085  -0.0281 0.0127  130 GLY   A C   
2849 O  O   A GLY   A 130 ? 0.1486 0.1347 0.1284 -0.0008 0.0041  0.0026  130 GLY   A O   
2850 O  O   B GLY   A 130 ? 0.1675 0.1535 0.1419 0.0113  -0.0257 0.0219  130 GLY   A O   
2857 N  N   A ILE   A 131 ? 0.1552 0.1283 0.1433 0.0001  0.0001  0.0034  131 ILE   A N   
2858 N  N   B ILE   A 131 ? 0.1675 0.1420 0.1535 0.0020  -0.0347 0.0220  131 ILE   A N   
2859 C  CA  A ILE   A 131 ? 0.1675 0.1332 0.1304 -0.0041 -0.0159 0.0113  131 ILE   A CA  
2860 C  CA  B ILE   A 131 ? 0.1721 0.1404 0.1438 -0.0004 -0.0422 0.0263  131 ILE   A CA  
2861 C  C   A ILE   A 131 ? 0.1669 0.1377 0.1255 -0.0042 -0.0027 0.0198  131 ILE   A C   
2862 C  C   B ILE   A 131 ? 0.1703 0.1444 0.1416 0.0058  -0.0391 0.0336  131 ILE   A C   
2863 O  O   A ILE   A 131 ? 0.1805 0.1411 0.1465 0.0034  -0.0013 0.0221  131 ILE   A O   
2864 O  O   B ILE   A 131 ? 0.1805 0.1508 0.1586 0.0067  -0.0384 0.0360  131 ILE   A O   
2865 C  CB  A ILE   A 131 ? 0.1751 0.1460 0.1513 -0.0060 -0.0226 0.0038  131 ILE   A CB  
2866 C  CB  B ILE   A 131 ? 0.1768 0.1438 0.1559 -0.0036 -0.0439 0.0165  131 ILE   A CB  
2867 C  CG1 A ILE   A 131 ? 0.1827 0.1705 0.1644 -0.0097 -0.0272 0.0064  131 ILE   A CG1 
2868 C  CG1 B ILE   A 131 ? 0.1820 0.1548 0.1609 -0.0027 -0.0479 0.0145  131 ILE   A CG1 
2869 C  CG2 A ILE   A 131 ? 0.1797 0.1353 0.1731 0.0017  -0.0220 -0.0094 131 ILE   A CG2 
2870 C  CG2 B ILE   A 131 ? 0.1789 0.1410 0.1653 -0.0023 -0.0387 0.0113  131 ILE   A CG2 
2871 C  CD1 A ILE   A 131 ? 0.1894 0.1769 0.1819 -0.0118 -0.0314 0.0100  131 ILE   A CD1 
2872 C  CD1 B ILE   A 131 ? 0.1878 0.1591 0.1703 -0.0055 -0.0468 0.0142  131 ILE   A CD1 
2895 N  N   A PHE   A 132 ? 0.1583 0.1365 0.1326 -0.0028 0.0042  0.0173  132 PHE   A N   
2896 N  N   B PHE   A 132 ? 0.1603 0.1400 0.1414 0.0136  -0.0354 0.0245  132 PHE   A N   
2897 C  CA  A PHE   A 132 ? 0.1555 0.1408 0.1219 -0.0099 0.0094  0.0131  132 PHE   A CA  
2898 C  CA  B PHE   A 132 ? 0.1592 0.1396 0.1463 0.0100  -0.0258 0.0168  132 PHE   A CA  
2899 C  C   A PHE   A 132 ? 0.1540 0.1569 0.1160 -0.0126 0.0043  0.0057  132 PHE   A C   
2900 C  C   B PHE   A 132 ? 0.1636 0.1564 0.1624 0.0133  -0.0274 0.0136  132 PHE   A C   
2901 O  O   A PHE   A 132 ? 0.1574 0.1685 0.1288 -0.0196 0.0066  0.0059  132 PHE   A O   
2902 O  O   B PHE   A 132 ? 0.1725 0.1722 0.1751 0.0111  -0.0185 0.0164  132 PHE   A O   
2903 C  CB  A PHE   A 132 ? 0.1557 0.1375 0.1359 -0.0081 0.0005  0.0188  132 PHE   A CB  
2904 C  CB  B PHE   A 132 ? 0.1552 0.1277 0.1305 0.0070  -0.0198 0.0206  132 PHE   A CB  
2905 C  CG  A PHE   A 132 ? 0.1548 0.1412 0.1379 -0.0030 -0.0066 0.0181  132 PHE   A CG  
2906 C  CG  B PHE   A 132 ? 0.1533 0.1240 0.1160 0.0091  -0.0206 0.0062  132 PHE   A CG  
2907 C  CD1 A PHE   A 132 ? 0.1619 0.1533 0.1579 0.0030  -0.0123 0.0127  132 PHE   A CD1 
2908 C  CD1 B PHE   A 132 ? 0.1570 0.1327 0.1384 0.0162  -0.0132 -0.0063 132 PHE   A CD1 
2909 C  CD2 A PHE   A 132 ? 0.1545 0.1477 0.1490 -0.0097 -0.0025 0.0148  132 PHE   A CD2 
2910 C  CD2 B PHE   A 132 ? 0.1509 0.1264 0.1157 0.0094  -0.0213 -0.0056 132 PHE   A CD2 
2911 C  CE1 A PHE   A 132 ? 0.1632 0.1598 0.1554 -0.0034 -0.0150 0.0038  132 PHE   A CE1 
2912 C  CE1 B PHE   A 132 ? 0.1566 0.1402 0.1371 0.0132  -0.0154 -0.0134 132 PHE   A CE1 
2913 C  CE2 A PHE   A 132 ? 0.1561 0.1504 0.1527 -0.0077 -0.0078 0.0117  132 PHE   A CE2 
2914 C  CE2 B PHE   A 132 ? 0.1501 0.1343 0.1299 0.0138  -0.0172 -0.0126 132 PHE   A CE2 
2915 C  CZ  A PHE   A 132 ? 0.1585 0.1551 0.1471 -0.0102 -0.0197 0.0123  132 PHE   A CZ  
2916 C  CZ  B PHE   A 132 ? 0.1533 0.1386 0.1328 0.0114  -0.0216 -0.0098 132 PHE   A CZ  
2935 N  N   A GLY   A 133 ? 0.1562 0.1567 0.1102 -0.0017 -0.0109 0.0138  133 GLY   A N   
2936 N  N   B GLY   A 133 ? 0.1636 0.1558 0.1638 0.0122  -0.0319 0.0135  133 GLY   A N   
2937 C  CA  A GLY   A 133 ? 0.1676 0.1727 0.1214 -0.0045 -0.0161 0.0129  133 GLY   A CA  
2938 C  CA  B GLY   A 133 ? 0.1636 0.1586 0.1621 0.0092  -0.0318 0.0063  133 GLY   A CA  
2939 C  C   A GLY   A 133 ? 0.1776 0.1843 0.1341 -0.0044 -0.0331 0.0052  133 GLY   A C   
2940 C  C   B GLY   A 133 ? 0.1632 0.1641 0.1546 0.0055  -0.0383 -0.0028 133 GLY   A C   
2941 O  O   A GLY   A 133 ? 0.1875 0.1948 0.1432 -0.0030 -0.0266 -0.0118 133 GLY   A O   
2942 O  O   B GLY   A 133 ? 0.1579 0.1741 0.1535 0.0121  -0.0399 -0.0175 133 GLY   A O   
2949 N  N   A ALA   A 134 ? 0.1780 0.1769 0.1437 -0.0065 -0.0283 0.0077  134 ALA   A N   
2950 N  N   B ALA   A 134 ? 0.1679 0.1534 0.1549 -0.0039 -0.0287 -0.0006 134 ALA   A N   
2951 C  CA  A ALA   A 134 ? 0.1749 0.1747 0.1667 -0.0046 -0.0257 -0.0003 134 ALA   A CA  
2952 C  CA  B ALA   A 134 ? 0.1695 0.1467 0.1657 -0.0067 -0.0203 -0.0051 134 ALA   A CA  
2953 C  C   A ALA   A 134 ? 0.1743 0.1724 0.1659 -0.0052 -0.0255 -0.0004 134 ALA   A C   
2954 C  C   B ALA   A 134 ? 0.1705 0.1444 0.1553 -0.0015 -0.0164 -0.0075 134 ALA   A C   
2955 O  O   A ALA   A 134 ? 0.1886 0.1785 0.1796 -0.0065 -0.0159 -0.0052 134 ALA   A O   
2956 O  O   B ALA   A 134 ? 0.1742 0.1470 0.1508 -0.0034 -0.0021 -0.0138 134 ALA   A O   
2957 C  CB  A ALA   A 134 ? 0.1841 0.1729 0.1899 -0.0007 -0.0268 -0.0037 134 ALA   A CB  
2958 C  CB  B ALA   A 134 ? 0.1703 0.1407 0.1818 -0.0114 -0.0223 -0.0070 134 ALA   A CB  
2969 N  N   A ASP   A 135 ? 0.1709 0.1664 0.1724 -0.0075 -0.0154 0.0029  135 ASP   A N   
2970 N  N   B ASP   A 135 ? 0.1746 0.1461 0.1596 -0.0061 -0.0167 -0.0020 135 ASP   A N   
2971 C  CA  A ASP   A 135 ? 0.1725 0.1709 0.1857 -0.0117 -0.0226 0.0014  135 ASP   A CA  
2972 C  CA  B ASP   A 135 ? 0.1749 0.1504 0.1697 -0.0069 -0.0248 -0.0027 135 ASP   A CA  
2973 C  C   A ASP   A 135 ? 0.1607 0.1627 0.1914 -0.0065 -0.0201 0.0121  135 ASP   A C   
2974 C  C   B ASP   A 135 ? 0.1599 0.1418 0.1597 -0.0003 -0.0226 -0.0038 135 ASP   A C   
2975 O  O   A ASP   A 135 ? 0.1548 0.1534 0.2036 -0.0052 -0.0167 0.0213  135 ASP   A O   
2976 O  O   B ASP   A 135 ? 0.1569 0.1385 0.1640 -0.0004 -0.0205 0.0005  135 ASP   A O   
2977 C  CB  A ASP   A 135 ? 0.1920 0.1966 0.2141 -0.0282 -0.0330 -0.0094 135 ASP   A CB  
2978 C  CB  B ASP   A 135 ? 0.1875 0.1641 0.1820 -0.0128 -0.0389 -0.0044 135 ASP   A CB  
2979 C  CG  A ASP   A 135 ? 0.2097 0.2204 0.2528 -0.0438 -0.0423 -0.0117 135 ASP   A CG  
2980 C  CG  B ASP   A 135 ? 0.1964 0.1822 0.2085 -0.0158 -0.0452 0.0009  135 ASP   A CG  
2981 O  OD1 A ASP   A 135 ? 0.2077 0.2317 0.2555 -0.0497 -0.0513 -0.0031 135 ASP   A OD1 
2982 O  OD1 B ASP   A 135 ? 0.1954 0.1800 0.2122 -0.0109 -0.0471 0.0056  135 ASP   A OD1 
2983 O  OD2 A ASP   A 135 ? 0.2314 0.2385 0.2903 -0.0479 -0.0331 -0.0100 135 ASP   A OD2 
2984 O  OD2 B ASP   A 135 ? 0.2055 0.1970 0.2333 -0.0199 -0.0481 -0.0033 135 ASP   A OD2 
2993 N  N   A PRO   A 136 ? 0.1512 0.1606 0.1894 0.0025  -0.0156 0.0145  136 PRO   A N   
2994 N  N   B PRO   A 136 ? 0.1506 0.1351 0.1466 0.0046  -0.0192 -0.0076 136 PRO   A N   
2995 C  CA  A PRO   A 136 ? 0.1431 0.1619 0.1990 -0.0029 -0.0087 0.0076  136 PRO   A CA  
2996 C  CA  B PRO   A 136 ? 0.1446 0.1412 0.1551 -0.0040 -0.0135 -0.0196 136 PRO   A CA  
2997 C  C   A PRO   A 136 ? 0.1252 0.1568 0.1940 0.0022  -0.0071 0.0105  136 PRO   A C   
2998 C  C   B PRO   A 136 ? 0.1354 0.1455 0.1492 -0.0034 -0.0054 -0.0169 136 PRO   A C   
2999 O  O   A PRO   A 136 ? 0.1274 0.1605 0.1815 -0.0034 -0.0033 0.0166  136 PRO   A O   
3000 O  O   B PRO   A 136 ? 0.1350 0.1443 0.1351 -0.0031 0.0094  -0.0149 136 PRO   A O   
3001 C  CB  A PRO   A 136 ? 0.1598 0.1668 0.2109 -0.0050 -0.0050 0.0102  136 PRO   A CB  
3002 C  CB  B PRO   A 136 ? 0.1554 0.1403 0.1666 0.0009  -0.0107 -0.0274 136 PRO   A CB  
3003 C  CG  A PRO   A 136 ? 0.1688 0.1705 0.2194 0.0018  -0.0105 0.0066  136 PRO   A CG  
3004 C  CG  B PRO   A 136 ? 0.1623 0.1385 0.1720 0.0088  -0.0124 -0.0248 136 PRO   A CG  
3005 C  CD  A PRO   A 136 ? 0.1648 0.1659 0.2082 0.0084  -0.0112 0.0142  136 PRO   A CD  
3006 C  CD  B PRO   A 136 ? 0.1585 0.1324 0.1535 0.0116  -0.0183 -0.0055 136 PRO   A CD  
3021 N  N   A ILE   A 137 ? 0.1261 0.1565 0.2000 -0.0005 -0.0125 0.0157  137 ILE   A N   
3022 N  N   B ILE   A 137 ? 0.1405 0.1459 0.1603 -0.0068 -0.0102 -0.0113 137 ILE   A N   
3023 C  CA  A ILE   A 137 ? 0.1298 0.1617 0.2057 -0.0096 -0.0182 0.0185  137 ILE   A CA  
3024 C  CA  B ILE   A 137 ? 0.1442 0.1507 0.1757 -0.0052 -0.0029 -0.0146 137 ILE   A CA  
3025 C  C   A ILE   A 137 ? 0.1324 0.1582 0.1872 -0.0106 -0.0201 0.0201  137 ILE   A C   
3026 C  C   B ILE   A 137 ? 0.1408 0.1514 0.1635 -0.0066 0.0086  -0.0078 137 ILE   A C   
3027 O  O   A ILE   A 137 ? 0.1414 0.1558 0.1970 -0.0136 -0.0186 0.0130  137 ILE   A O   
3028 O  O   B ILE   A 137 ? 0.1408 0.1523 0.1543 -0.0041 0.0149  -0.0079 137 ILE   A O   
3029 C  CB  A ILE   A 137 ? 0.1345 0.1702 0.2444 -0.0156 -0.0349 0.0177  137 ILE   A CB  
3030 C  CB  B ILE   A 137 ? 0.1529 0.1536 0.2078 -0.0067 -0.0149 -0.0199 137 ILE   A CB  
3031 C  CG1 A ILE   A 137 ? 0.1388 0.1803 0.2832 -0.0207 -0.0347 0.0272  137 ILE   A CG1 
3032 C  CG1 B ILE   A 137 ? 0.1670 0.1609 0.2455 -0.0079 -0.0278 -0.0178 137 ILE   A CG1 
3033 C  CG2 A ILE   A 137 ? 0.1461 0.1737 0.2499 -0.0135 -0.0299 0.0013  137 ILE   A CG2 
3034 C  CG2 B ILE   A 137 ? 0.1533 0.1514 0.2112 -0.0011 -0.0156 -0.0283 137 ILE   A CG2 
3035 C  CD1 A ILE   A 137 ? 0.1532 0.1908 0.3069 -0.0207 -0.0283 0.0380  137 ILE   A CD1 
3036 C  CD1 B ILE   A 137 ? 0.1794 0.1645 0.2700 -0.0107 -0.0328 -0.0142 137 ILE   A CD1 
3059 N  N   A HIS   A 138 ? 0.1314 0.1685 0.1873 -0.0080 -0.0144 0.0225  138 HIS   A N   
3060 N  N   B HIS   A 138 ? 0.1397 0.1578 0.1634 -0.0056 0.0166  -0.0106 138 HIS   A N   
3061 C  CA  A HIS   A 138 ? 0.1398 0.1774 0.1820 -0.0047 -0.0136 0.0254  138 HIS   A CA  
3062 C  CA  B HIS   A 138 ? 0.1449 0.1599 0.1623 -0.0049 0.0125  -0.0070 138 HIS   A CA  
3063 C  C   A HIS   A 138 ? 0.1319 0.1711 0.1734 -0.0025 -0.0071 0.0274  138 HIS   A C   
3064 C  C   B HIS   A 138 ? 0.1363 0.1595 0.1654 -0.0028 0.0097  0.0114  138 HIS   A C   
3065 O  O   A HIS   A 138 ? 0.1362 0.1725 0.1714 -0.0055 -0.0085 0.0229  138 HIS   A O   
3066 O  O   B HIS   A 138 ? 0.1397 0.1590 0.1702 -0.0050 0.0064  0.0067  138 HIS   A O   
3067 C  CB  A HIS   A 138 ? 0.1621 0.1943 0.1865 -0.0029 -0.0183 0.0243  138 HIS   A CB  
3068 C  CB  B HIS   A 138 ? 0.1518 0.1644 0.1598 -0.0015 0.0135  -0.0256 138 HIS   A CB  
3069 C  CG  A HIS   A 138 ? 0.1803 0.1995 0.1885 -0.0079 -0.0108 0.0211  138 HIS   A CG  
3070 C  CG  B HIS   A 138 ? 0.1614 0.1647 0.1652 -0.0042 0.0053  -0.0322 138 HIS   A CG  
3071 N  ND1 A HIS   A 138 ? 0.1953 0.2063 0.2099 -0.0101 -0.0062 0.0203  138 HIS   A ND1 
3072 N  ND1 B HIS   A 138 ? 0.1734 0.1688 0.1877 -0.0041 0.0005  -0.0345 138 HIS   A ND1 
3073 C  CD2 A HIS   A 138 ? 0.1822 0.2013 0.1830 -0.0047 -0.0032 0.0184  138 HIS   A CD2 
3074 C  CD2 B HIS   A 138 ? 0.1613 0.1585 0.1638 -0.0002 0.0068  -0.0308 138 HIS   A CD2 
3075 C  CE1 A HIS   A 138 ? 0.1995 0.2076 0.2154 -0.0010 -0.0051 0.0191  138 HIS   A CE1 
3076 C  CE1 B HIS   A 138 ? 0.1745 0.1651 0.1882 0.0003  -0.0015 -0.0295 138 HIS   A CE1 
3077 N  NE2 A HIS   A 138 ? 0.1896 0.2050 0.1899 0.0023  0.0025  0.0175  138 HIS   A NE2 
3078 N  NE2 B HIS   A 138 ? 0.1684 0.1588 0.1750 0.0025  0.0032  -0.0297 138 HIS   A NE2 
3093 N  N   . SER   A 139 ? 0.1280 0.1575 0.1729 -0.0023 -0.0019 0.0280  139 SER   A N   
3094 C  CA  . SER   A 139 ? 0.1238 0.1526 0.1713 -0.0088 0.0027  0.0279  139 SER   A CA  
3095 C  C   . SER   A 139 ? 0.1202 0.1427 0.1612 -0.0035 0.0059  0.0200  139 SER   A C   
3096 O  O   . SER   A 139 ? 0.1155 0.1395 0.1761 -0.0094 0.0005  0.0224  139 SER   A O   
3097 C  CB  . SER   A 139 ? 0.1252 0.1540 0.1768 -0.0135 -0.0067 0.0341  139 SER   A CB  
3098 O  OG  . SER   A 139 ? 0.1352 0.1496 0.1789 -0.0182 -0.0103 0.0379  139 SER   A OG  
3105 N  N   . LEU   A 140 ? 0.1186 0.1478 0.1598 -0.0043 0.0013  0.0305  140 LEU   A N   
3106 C  CA  . LEU   A 140 ? 0.1206 0.1375 0.1645 -0.0050 -0.0013 0.0263  140 LEU   A CA  
3107 C  C   . LEU   A 140 ? 0.1137 0.1459 0.1636 -0.0142 0.0020  0.0293  140 LEU   A C   
3108 O  O   . LEU   A 140 ? 0.1221 0.1518 0.1827 -0.0057 0.0038  0.0296  140 LEU   A O   
3109 C  CB  . LEU   A 140 ? 0.1225 0.1479 0.1732 -0.0085 -0.0003 0.0210  140 LEU   A CB  
3110 C  CG  . LEU   A 140 ? 0.1226 0.1581 0.1779 -0.0160 -0.0005 0.0288  140 LEU   A CG  
3111 C  CD1 . LEU   A 140 ? 0.1284 0.1629 0.1880 -0.0135 0.0067  0.0264  140 LEU   A CD1 
3112 C  CD2 . LEU   A 140 ? 0.1220 0.1736 0.1904 -0.0105 0.0087  0.0325  140 LEU   A CD2 
3124 N  N   . ARG   A 141 ? 0.1228 0.1513 0.1704 -0.0069 -0.0050 0.0231  141 ARG   A N   
3125 C  CA  . ARG   A 141 ? 0.1292 0.1660 0.1865 -0.0171 -0.0034 0.0034  141 ARG   A CA  
3126 C  C   . ARG   A 141 ? 0.1360 0.1493 0.1769 -0.0149 -0.0001 0.0056  141 ARG   A C   
3127 O  O   . ARG   A 141 ? 0.1276 0.1457 0.1987 -0.0117 0.0080  0.0105  141 ARG   A O   
3128 C  CB  . ARG   A 141 ? 0.1421 0.1954 0.2156 -0.0231 -0.0020 -0.0167 141 ARG   A CB  
3129 C  CG  . ARG   A 141 ? 0.1772 0.2352 0.2505 -0.0285 0.0184  -0.0211 141 ARG   A CG  
3130 C  CD  . ARG   A 141 ? 0.2099 0.2693 0.2875 -0.0392 0.0259  -0.0352 141 ARG   A CD  
3131 N  NE  . ARG   A 141 ? 0.1978 0.2995 0.3011 -0.0420 0.0140  -0.0434 141 ARG   A NE  
3132 C  CZ  . ARG   A 141 ? 0.2018 0.3223 0.3006 -0.0590 0.0268  -0.0338 141 ARG   A CZ  
3133 N  NH1 . ARG   A 141 ? 0.1890 0.3220 0.2803 -0.0767 0.0616  -0.0483 141 ARG   A NH1 
3134 N  NH2 . ARG   A 141 ? 0.2111 0.3388 0.3199 -0.0595 0.0104  -0.0152 141 ARG   A NH2 
3148 N  N   . VAL   A 142 ? 0.1287 0.1461 0.1620 -0.0095 0.0039  0.0023  142 VAL   A N   
3149 C  CA  . VAL   A 142 ? 0.1317 0.1375 0.1690 -0.0081 0.0190  0.0085  142 VAL   A CA  
3150 C  C   . VAL   A 142 ? 0.1149 0.1351 0.1693 -0.0091 0.0127  0.0151  142 VAL   A C   
3151 O  O   . VAL   A 142 ? 0.1223 0.1397 0.1861 0.0004  0.0131  0.0141  142 VAL   A O   
3152 C  CB  . VAL   A 142 ? 0.1407 0.1485 0.1674 -0.0064 0.0157  0.0128  142 VAL   A CB  
3153 C  CG1 . VAL   A 142 ? 0.1433 0.1416 0.1736 -0.0094 0.0195  0.0097  142 VAL   A CG1 
3154 C  CG2 . VAL   A 142 ? 0.1552 0.1650 0.1812 -0.0063 0.0139  0.0117  142 VAL   A CG2 
3164 N  N   . CYS   A 143 ? 0.1176 0.1355 0.1560 -0.0088 0.0013  0.0110  143 CYS   A N   
3165 C  CA  . CYS   A 143 ? 0.1199 0.1365 0.1665 -0.0118 0.0090  0.0119  143 CYS   A CA  
3166 C  C   . CYS   A 143 ? 0.1188 0.1321 0.1748 -0.0104 0.0080  0.0238  143 CYS   A C   
3167 O  O   . CYS   A 143 ? 0.1179 0.1351 0.1802 -0.0001 0.0051  0.0256  143 CYS   A O   
3168 C  CB  . CYS   A 143 ? 0.1298 0.1420 0.1773 -0.0034 0.0177  0.0262  143 CYS   A CB  
3169 S  SG  . CYS   A 143 ? 0.1453 0.1475 0.1628 0.0040  0.0089  0.0124  143 CYS   A SG  
3175 N  N   . VAL   A 144 ? 0.1168 0.1419 0.1868 -0.0096 0.0103  0.0278  144 VAL   A N   
3176 C  CA  . VAL   A 144 ? 0.1228 0.1450 0.2149 -0.0103 0.0158  0.0295  144 VAL   A CA  
3177 C  C   . VAL   A 144 ? 0.1290 0.1373 0.2023 -0.0181 -0.0024 0.0303  144 VAL   A C   
3178 O  O   . VAL   A 144 ? 0.1434 0.1416 0.2108 -0.0072 -0.0045 0.0337  144 VAL   A O   
3179 C  CB  . VAL   A 144 ? 0.1463 0.1679 0.2761 -0.0005 0.0323  0.0351  144 VAL   A CB  
3180 C  CG1 . VAL   A 144 ? 0.1611 0.1864 0.3131 -0.0116 0.0215  0.0374  144 VAL   A CG1 
3181 C  CG2 . VAL   A 144 ? 0.1337 0.1733 0.2859 0.0011  0.0465  0.0481  144 VAL   A CG2 
3191 N  N   . ASP   A 145 ? 0.1284 0.1319 0.2095 -0.0145 0.0022  0.0251  145 ASP   A N   
3192 C  CA  . ASP   A 145 ? 0.1399 0.1397 0.2226 -0.0161 0.0015  0.0080  145 ASP   A CA  
3193 C  C   . ASP   A 145 ? 0.1380 0.1322 0.2253 -0.0094 0.0082  -0.0007 145 ASP   A C   
3194 O  O   . ASP   A 145 ? 0.1484 0.1422 0.2777 -0.0138 0.0051  -0.0247 145 ASP   A O   
3195 C  CB  . ASP   A 145 ? 0.1532 0.1651 0.2408 -0.0236 -0.0060 0.0067  145 ASP   A CB  
3196 C  CG  . ASP   A 145 ? 0.1665 0.2002 0.2683 -0.0375 -0.0194 0.0102  145 ASP   A CG  
3197 O  OD1 . ASP   A 145 ? 0.1610 0.2129 0.2769 -0.0492 -0.0081 0.0153  145 ASP   A OD1 
3198 O  OD2 . ASP   A 145 ? 0.1909 0.2252 0.2725 -0.0427 -0.0394 0.0078  145 ASP   A OD2 
3203 N  N   . THR   A 146 ? 0.1231 0.1276 0.1911 -0.0070 0.0112  0.0125  146 THR   A N   
3204 C  CA  . THR   A 146 ? 0.1245 0.1262 0.1728 -0.0066 0.0093  0.0060  146 THR   A CA  
3205 C  C   . THR   A 146 ? 0.1195 0.1252 0.1787 -0.0072 0.0097  0.0159  146 THR   A C   
3206 O  O   . THR   A 146 ? 0.1335 0.1379 0.1995 0.0085  0.0014  0.0146  146 THR   A O   
3207 C  CB  . THR   A 146 ? 0.1207 0.1285 0.1784 -0.0014 0.0084  0.0138  146 THR   A CB  
3208 O  OG1 . THR   A 146 ? 0.1232 0.1436 0.1806 0.0011  0.0057  0.0119  146 THR   A OG1 
3209 C  CG2 . THR   A 146 ? 0.1206 0.1342 0.1972 -0.0072 0.0102  0.0081  146 THR   A CG2 
3217 N  N   . VAL   A 147 ? 0.1185 0.1326 0.1721 -0.0014 0.0137  0.0122  147 VAL   A N   
3218 C  CA  . VAL   A 147 ? 0.1224 0.1339 0.1697 -0.0066 0.0192  0.0229  147 VAL   A CA  
3219 C  C   . VAL   A 147 ? 0.1258 0.1316 0.1930 -0.0084 0.0208  0.0318  147 VAL   A C   
3220 O  O   . VAL   A 147 ? 0.1231 0.1360 0.2149 -0.0143 0.0136  0.0302  147 VAL   A O   
3221 C  CB  . VAL   A 147 ? 0.1347 0.1317 0.1691 -0.0096 0.0205  0.0246  147 VAL   A CB  
3222 C  CG1 . VAL   A 147 ? 0.1617 0.1409 0.1702 -0.0068 0.0165  0.0305  147 VAL   A CG1 
3223 C  CG2 . VAL   A 147 ? 0.1378 0.1340 0.1735 -0.0142 0.0133  0.0232  147 VAL   A CG2 
3233 N  N   . ARG   A 148 ? 0.1211 0.1291 0.2029 -0.0105 0.0169  0.0430  148 ARG   A N   
3234 C  CA  . ARG   A 148 ? 0.1303 0.1336 0.2030 -0.0119 0.0138  0.0472  148 ARG   A CA  
3235 C  C   . ARG   A 148 ? 0.1409 0.1406 0.1989 -0.0146 0.0120  0.0609  148 ARG   A C   
3236 O  O   . ARG   A 148 ? 0.1669 0.1516 0.2256 -0.0207 0.0213  0.0524  148 ARG   A O   
3237 C  CB  . ARG   A 148 ? 0.1368 0.1365 0.2189 -0.0082 0.0191  0.0384  148 ARG   A CB  
3238 C  CG  . ARG   A 148 ? 0.1527 0.1347 0.2557 -0.0073 0.0368  0.0304  148 ARG   A CG  
3239 C  CD  . ARG   A 148 ? 0.1642 0.1335 0.2827 -0.0028 0.0443  0.0486  148 ARG   A CD  
3240 N  NE  . ARG   A 148 ? 0.1569 0.1409 0.2761 0.0146  0.0486  0.0536  148 ARG   A NE  
3241 C  CZ  . ARG   A 148 ? 0.1577 0.1316 0.2613 0.0062  0.0456  0.0421  148 ARG   A CZ  
3242 N  NH1 . ARG   A 148 ? 0.1670 0.1331 0.2619 -0.0080 0.0470  0.0229  148 ARG   A NH1 
3243 N  NH2 . ARG   A 148 ? 0.1567 0.1524 0.2588 0.0142  0.0473  0.0469  148 ARG   A NH2 
3257 N  N   . THR   A 149 ? 0.1359 0.1515 0.1860 -0.0172 0.0032  0.0537  149 THR   A N   
3258 C  CA  . THR   A 149 ? 0.1379 0.1549 0.1855 -0.0134 0.0039  0.0484  149 THR   A CA  
3259 C  C   . THR   A 149 ? 0.1361 0.1511 0.1770 -0.0175 0.0041  0.0543  149 THR   A C   
3260 O  O   . THR   A 149 ? 0.1338 0.1603 0.1956 -0.0174 0.0058  0.0512  149 THR   A O   
3261 C  CB  . THR   A 149 ? 0.1417 0.1671 0.1910 -0.0133 0.0019  0.0420  149 THR   A CB  
3262 O  OG1 . THR   A 149 ? 0.1420 0.1554 0.2015 -0.0214 0.0035  0.0412  149 THR   A OG1 
3263 C  CG2 . THR   A 149 ? 0.1391 0.1747 0.2047 -0.0072 -0.0111 0.0380  149 THR   A CG2 
3271 N  N   . ASN   A 150 ? 0.1387 0.1586 0.1766 -0.0087 -0.0021 0.0627  150 ASN   A N   
3272 C  CA  . ASN   A 150 ? 0.1490 0.1619 0.1772 -0.0089 0.0044  0.0599  150 ASN   A CA  
3273 C  C   . ASN   A 150 ? 0.1361 0.1533 0.1729 -0.0149 0.0022  0.0486  150 ASN   A C   
3274 O  O   . ASN   A 150 ? 0.1415 0.1659 0.2054 -0.0148 -0.0159 0.0397  150 ASN   A O   
3275 C  CB  . ASN   A 150 ? 0.1828 0.1892 0.2124 -0.0152 0.0228  0.0700  150 ASN   A CB  
3276 C  CG  . ASN   A 150 ? 0.2354 0.2226 0.2752 -0.0122 0.0064  0.0728  150 ASN   A CG  
3277 O  OD1 . ASN   A 150 ? 0.2563 0.2310 0.2902 -0.0214 0.0141  0.0856  150 ASN   A OD1 
3278 N  ND2 . ASN   A 150 ? 0.2684 0.2463 0.3043 -0.0096 -0.0056 0.0684  150 ASN   A ND2 
3285 N  N   . VAL   A 151 ? 0.1331 0.1390 0.1717 -0.0135 -0.0018 0.0446  151 VAL   A N   
3286 C  CA  . VAL   A 151 ? 0.1381 0.1407 0.1604 -0.0193 -0.0015 0.0401  151 VAL   A CA  
3287 C  C   . VAL   A 151 ? 0.1305 0.1406 0.1679 -0.0231 0.0003  0.0454  151 VAL   A C   
3288 O  O   . VAL   A 151 ? 0.1406 0.1498 0.1999 -0.0203 0.0079  0.0336  151 VAL   A O   
3289 C  CB  . VAL   A 151 ? 0.1685 0.1636 0.1627 -0.0030 -0.0014 0.0408  151 VAL   A CB  
3290 C  CG1 . VAL   A 151 ? 0.1641 0.1835 0.1882 -0.0078 -0.0083 0.0366  151 VAL   A CG1 
3291 C  CG2 . VAL   A 151 ? 0.1767 0.1573 0.1668 -0.0052 0.0174  0.0296  151 VAL   A CG2 
3301 N  N   . TYR   A 152 ? 0.1322 0.1403 0.1759 -0.0241 0.0031  0.0411  152 TYR   A N   
3302 C  CA  . TYR   A 152 ? 0.1347 0.1456 0.1537 -0.0220 0.0019  0.0372  152 TYR   A CA  
3303 C  C   . TYR   A 152 ? 0.1306 0.1407 0.1459 -0.0177 0.0113  0.0355  152 TYR   A C   
3304 O  O   . TYR   A 152 ? 0.1371 0.1375 0.1561 -0.0238 0.0091  0.0291  152 TYR   A O   
3305 C  CB  . TYR   A 152 ? 0.1475 0.1587 0.1581 -0.0211 0.0100  0.0444  152 TYR   A CB  
3306 C  CG  . TYR   A 152 ? 0.1574 0.1849 0.1520 -0.0170 0.0175  0.0494  152 TYR   A CG  
3307 C  CD1 . TYR   A 152 ? 0.1732 0.2071 0.1648 -0.0065 0.0226  0.0518  152 TYR   A CD1 
3308 C  CD2 . TYR   A 152 ? 0.1631 0.1987 0.1596 -0.0306 0.0142  0.0468  152 TYR   A CD2 
3309 C  CE1 . TYR   A 152 ? 0.2043 0.2213 0.1764 -0.0077 0.0087  0.0661  152 TYR   A CE1 
3310 C  CE2 . TYR   A 152 ? 0.1926 0.2152 0.1733 -0.0316 0.0187  0.0562  152 TYR   A CE2 
3311 C  CZ  . TYR   A 152 ? 0.2175 0.2180 0.1697 -0.0215 0.0080  0.0783  152 TYR   A CZ  
3312 O  OH  . TYR   A 152 ? 0.2471 0.2379 0.2092 -0.0186 0.0142  0.0919  152 TYR   A OH  
3322 N  N   . LEU   A 153 ? 0.1304 0.1408 0.1510 -0.0216 0.0099  0.0382  153 LEU   A N   
3323 C  CA  . LEU   A 153 ? 0.1276 0.1383 0.1570 -0.0107 0.0104  0.0391  153 LEU   A CA  
3324 C  C   . LEU   A 153 ? 0.1263 0.1385 0.1658 -0.0094 0.0158  0.0348  153 LEU   A C   
3325 O  O   . LEU   A 153 ? 0.1310 0.1503 0.1851 -0.0135 0.0357  0.0291  153 LEU   A O   
3326 C  CB  . LEU   A 153 ? 0.1205 0.1404 0.1672 -0.0096 0.0132  0.0348  153 LEU   A CB  
3327 C  CG  . LEU   A 153 ? 0.1288 0.1409 0.1641 -0.0113 0.0109  0.0256  153 LEU   A CG  
3328 C  CD1 . LEU   A 153 ? 0.1366 0.1445 0.1679 -0.0110 -0.0026 0.0328  153 LEU   A CD1 
3329 C  CD2 . LEU   A 153 ? 0.1378 0.1440 0.1710 -0.0183 0.0181  0.0074  153 LEU   A CD2 
3341 N  N   A ALA   A 154 ? 0.1265 0.1300 0.1732 -0.0103 0.0170  0.0367  154 ALA   A N   
3342 N  N   B ALA   A 154 ? 0.1266 0.1353 0.1644 -0.0053 0.0132  0.0333  154 ALA   A N   
3343 C  CA  A ALA   A 154 ? 0.1359 0.1322 0.1740 -0.0059 0.0222  0.0378  154 ALA   A CA  
3344 C  CA  B ALA   A 154 ? 0.1324 0.1373 0.1654 0.0006  0.0126  0.0306  154 ALA   A CA  
3345 C  C   A ALA   A 154 ? 0.1326 0.1273 0.1626 -0.0008 0.0228  0.0344  154 ALA   A C   
3346 C  C   B ALA   A 154 ? 0.1269 0.1361 0.1464 -0.0011 0.0098  0.0285  154 ALA   A C   
3347 O  O   A ALA   A 154 ? 0.1408 0.1319 0.1730 -0.0051 0.0286  0.0286  154 ALA   A O   
3348 O  O   B ALA   A 154 ? 0.1344 0.1354 0.1339 -0.0055 0.0094  0.0265  154 ALA   A O   
3349 C  CB  A ALA   A 154 ? 0.1455 0.1413 0.1838 -0.0021 0.0151  0.0278  154 ALA   A CB  
3350 C  CB  B ALA   A 154 ? 0.1406 0.1387 0.1768 0.0049  0.0065  0.0243  154 ALA   A CB  
3361 N  N   A VAL   A 155 ? 0.1204 0.1118 0.1335 0.0080  0.0260  0.0533  155 VAL   A N   
3362 N  N   B VAL   A 155 ? 0.1135 0.1253 0.1322 0.0027  0.0204  0.0312  155 VAL   A N   
3363 C  CA  A VAL   A 155 ? 0.1361 0.1295 0.1736 0.0082  0.0160  0.0507  155 VAL   A CA  
3364 C  CA  B VAL   A 155 ? 0.1278 0.1365 0.1492 -0.0034 0.0222  0.0378  155 VAL   A CA  
3365 C  CA  T VAL   A 155 ? 0.1782 0.1666 0.1972 0.0006  0.0060  0.0316  155 VAL   A CA  
3366 C  C   A VAL   A 155 ? 0.1377 0.1365 0.1936 0.0084  0.0121  0.0461  155 VAL   A C   
3367 C  C   B VAL   A 155 ? 0.1342 0.1400 0.1647 0.0067  0.0160  0.0373  155 VAL   A C   
3368 C  C   T VAL   A 155 ? 0.1727 0.1678 0.1919 0.0034  0.0092  0.0298  155 VAL   A C   
3369 O  O   A VAL   A 155 ? 0.1304 0.1345 0.2014 0.0007  0.0238  0.0366  155 VAL   A O   
3370 O  O   B VAL   A 155 ? 0.1294 0.1432 0.1435 0.0192  0.0090  0.0233  155 VAL   A O   
3371 O  O   T VAL   A 155 ? 0.1669 0.1684 0.1898 0.0016  0.0112  0.0227  155 VAL   A O   
3372 C  CB  A VAL   A 155 ? 0.1423 0.1386 0.1748 0.0156  0.0136  0.0447  155 VAL   A CB  
3373 C  CB  B VAL   A 155 ? 0.1288 0.1443 0.1470 -0.0051 0.0157  0.0328  155 VAL   A CB  
3374 C  CB  T VAL   A 155 ? 0.1793 0.1679 0.1907 0.0023  -0.0013 0.0299  155 VAL   A CB  
3375 C  CG1 A VAL   A 155 ? 0.1536 0.1495 0.1794 0.0189  0.0131  0.0357  155 VAL   A CG1 
3376 C  CG1 B VAL   A 155 ? 0.1382 0.1566 0.1526 -0.0057 0.0084  0.0355  155 VAL   A CG1 
3377 C  CG1 T VAL   A 155 ? 0.1854 0.1742 0.1919 0.0038  -0.0032 0.0271  155 VAL   A CG1 
3378 C  CG2 A VAL   A 155 ? 0.1488 0.1429 0.1815 0.0186  0.0047  0.0395  155 VAL   A CG2 
3379 C  CG2 B VAL   A 155 ? 0.1310 0.1474 0.1525 -0.0023 0.0119  0.0248  155 VAL   A CG2 
3380 C  CG2 T VAL   A 155 ? 0.1813 0.1692 0.1919 0.0044  -0.0096 0.0271  155 VAL   A CG2 
3406 N  N   A PHE   A 156 ? 0.1468 0.1449 0.2036 0.0163  0.0068  0.0469  156 PHE   A N   
3407 N  N   B PHE   A 156 ? 0.1461 0.1370 0.1863 0.0040  0.0246  0.0494  156 PHE   A N   
3408 N  N   T PHE   A 156 ? 0.1746 0.1688 0.1924 0.0080  0.0134  0.0334  156 PHE   A N   
3409 C  CA  A PHE   A 156 ? 0.1658 0.1547 0.2197 0.0300  0.0088  0.0478  156 PHE   A CA  
3410 C  CA  B PHE   A 156 ? 0.1610 0.1376 0.1999 0.0076  0.0253  0.0587  156 PHE   A CA  
3411 C  CA  T PHE   A 156 ? 0.1828 0.1729 0.1948 0.0154  0.0196  0.0340  156 PHE   A CA  
3412 C  C   A PHE   A 156 ? 0.1645 0.1551 0.2181 0.0397  0.0205  0.0526  156 PHE   A C   
3413 C  C   B PHE   A 156 ? 0.1663 0.1455 0.2185 0.0166  0.0470  0.0728  156 PHE   A C   
3414 C  C   T PHE   A 156 ? 0.1824 0.1780 0.2032 0.0157  0.0268  0.0407  156 PHE   A C   
3415 O  O   A PHE   A 156 ? 0.1684 0.1605 0.2149 0.0333  0.0349  0.0514  156 PHE   A O   
3416 O  O   B PHE   A 156 ? 0.1797 0.1475 0.2242 0.0174  0.0633  0.0664  156 PHE   A O   
3417 O  O   T PHE   A 156 ? 0.1890 0.1804 0.2081 0.0174  0.0322  0.0327  156 PHE   A O   
3418 C  CB  A PHE   A 156 ? 0.1851 0.1663 0.2371 0.0270  0.0014  0.0469  156 PHE   A CB  
3419 C  CB  B PHE   A 156 ? 0.1645 0.1287 0.1872 -0.0064 0.0115  0.0608  156 PHE   A CB  
3420 C  CB  T PHE   A 156 ? 0.1854 0.1707 0.1846 0.0204  0.0227  0.0310  156 PHE   A CB  
3421 C  CG  A PHE   A 156 ? 0.2030 0.1753 0.2543 0.0298  -0.0086 0.0419  156 PHE   A CG  
3422 C  CG  B PHE   A 156 ? 0.1691 0.1337 0.1871 -0.0075 -0.0107 0.0720  156 PHE   A CG  
3423 C  CG  T PHE   A 156 ? 0.1908 0.1753 0.1862 0.0276  0.0218  0.0315  156 PHE   A CG  
3424 C  CD1 A PHE   A 156 ? 0.2142 0.1823 0.2628 0.0305  -0.0034 0.0402  156 PHE   A CD1 
3425 C  CD1 B PHE   A 156 ? 0.1726 0.1435 0.2089 -0.0085 -0.0112 0.0677  156 PHE   A CD1 
3426 C  CD1 T PHE   A 156 ? 0.1937 0.1796 0.2028 0.0350  0.0196  0.0281  156 PHE   A CD1 
3427 C  CD2 A PHE   A 156 ? 0.2126 0.1866 0.2616 0.0352  -0.0147 0.0379  156 PHE   A CD2 
3428 C  CD2 B PHE   A 156 ? 0.1789 0.1440 0.2139 -0.0059 -0.0252 0.0640  156 PHE   A CD2 
3429 C  CD2 T PHE   A 156 ? 0.1974 0.1809 0.1926 0.0262  0.0209  0.0361  156 PHE   A CD2 
3430 C  CE1 A PHE   A 156 ? 0.2206 0.1857 0.2686 0.0328  0.0015  0.0367  156 PHE   A CE1 
3431 C  CE1 B PHE   A 156 ? 0.1776 0.1499 0.2303 -0.0113 -0.0113 0.0538  156 PHE   A CE1 
3432 C  CE1 T PHE   A 156 ? 0.1985 0.1822 0.2182 0.0351  0.0174  0.0236  156 PHE   A CE1 
3433 C  CE2 A PHE   A 156 ? 0.2208 0.1915 0.2684 0.0375  -0.0140 0.0293  156 PHE   A CE2 
3434 C  CE2 B PHE   A 156 ? 0.1880 0.1525 0.2397 -0.0057 -0.0259 0.0562  156 PHE   A CE2 
3435 C  CE2 T PHE   A 156 ? 0.2034 0.1854 0.2050 0.0278  0.0159  0.0340  156 PHE   A CE2 
3436 C  CZ  A PHE   A 156 ? 0.2235 0.1915 0.2712 0.0365  -0.0026 0.0313  156 PHE   A CZ  
3437 C  CZ  B PHE   A 156 ? 0.1849 0.1477 0.2508 -0.0109 -0.0135 0.0542  156 PHE   A CZ  
3438 C  CZ  T PHE   A 156 ? 0.2036 0.1827 0.2232 0.0295  0.0157  0.0279  156 PHE   A CZ  
3466 N  N   A ASP   A 157 ? 0.1632 0.1594 0.2244 0.0481  0.0146  0.0513  157 ASP   A N   
3467 N  N   B ASP   A 157 ? 0.1624 0.1644 0.2344 0.0204  0.0389  0.0854  157 ASP   A N   
3468 N  N   T ASP   A 157 ? 0.1735 0.1849 0.2095 0.0134  0.0200  0.0506  157 ASP   A N   
3469 C  CA  A ASP   A 157 ? 0.1745 0.1780 0.2380 0.0491  0.0178  0.0548  157 ASP   A CA  
3470 C  CA  B ASP   A 157 ? 0.1675 0.1861 0.2469 0.0259  0.0289  0.0894  157 ASP   A CA  
3471 C  CA  T ASP   A 157 ? 0.1751 0.1978 0.2224 0.0143  0.0129  0.0575  157 ASP   A CA  
3472 C  C   A ASP   A 157 ? 0.1700 0.1918 0.2468 0.0492  0.0226  0.0581  157 ASP   A C   
3473 C  C   B ASP   A 157 ? 0.1519 0.2030 0.2406 0.0315  0.0357  0.0979  157 ASP   A C   
3474 C  C   T ASP   A 157 ? 0.1828 0.2141 0.2320 0.0200  0.0157  0.0620  157 ASP   A C   
3475 O  O   A ASP   A 157 ? 0.1645 0.1872 0.2406 0.0456  0.0167  0.0576  157 ASP   A O   
3476 O  O   B ASP   A 157 ? 0.1361 0.1959 0.2268 0.0243  0.0414  0.0946  157 ASP   A O   
3477 O  O   T ASP   A 157 ? 0.1771 0.2099 0.2240 0.0148  0.0129  0.0618  157 ASP   A O   
3478 C  CB  A ASP   A 157 ? 0.1907 0.1842 0.2496 0.0508  0.0194  0.0549  157 ASP   A CB  
3479 C  CB  B ASP   A 157 ? 0.1858 0.1899 0.2699 0.0286  0.0159  0.0903  157 ASP   A CB  
3480 C  CB  T ASP   A 157 ? 0.1709 0.1957 0.2299 0.0134  0.0045  0.0626  157 ASP   A CB  
3481 C  CG  A ASP   A 157 ? 0.2053 0.1933 0.2733 0.0522  0.0198  0.0548  157 ASP   A CG  
3482 C  CG  B ASP   A 157 ? 0.1986 0.1908 0.2966 0.0332  0.0043  0.0888  157 ASP   A CG  
3483 C  CG  T ASP   A 157 ? 0.1633 0.1921 0.2409 0.0138  -0.0061 0.0681  157 ASP   A CG  
3484 O  OD1 A ASP   A 157 ? 0.2150 0.1982 0.2881 0.0516  0.0193  0.0522  157 ASP   A OD1 
3485 O  OD1 B ASP   A 157 ? 0.1973 0.1851 0.3199 0.0399  0.0044  0.0936  157 ASP   A OD1 
3486 O  OD1 T ASP   A 157 ? 0.1566 0.1929 0.2666 0.0155  -0.0055 0.0572  157 ASP   A OD1 
3487 O  OD2 A ASP   A 157 ? 0.2020 0.1922 0.2846 0.0546  0.0242  0.0612  157 ASP   A OD2 
3488 O  OD2 B ASP   A 157 ? 0.2056 0.1943 0.2984 0.0295  -0.0062 0.0827  157 ASP   A OD2 
3489 O  OD2 T ASP   A 157 ? 0.1612 0.1872 0.2291 0.0181  -0.0157 0.0813  157 ASP   A OD2 
3502 N  N   A LYS   A 158 ? 0.1786 0.2119 0.2725 0.0445  0.0376  0.0588  158 LYS   A N   
3503 N  N   B LYS   A 158 ? 0.1593 0.2276 0.2535 0.0357  0.0526  0.1003  158 LYS   A N   
3504 N  N   T LYS   A 158 ? 0.1993 0.2346 0.2555 0.0241  0.0285  0.0628  158 LYS   A N   
3505 C  CA  A LYS   A 158 ? 0.1820 0.2326 0.2973 0.0417  0.0454  0.0627  158 LYS   A CA  
3506 C  CA  B LYS   A 158 ? 0.1619 0.2534 0.2655 0.0465  0.0563  0.1004  158 LYS   A CA  
3507 C  CA  T LYS   A 158 ? 0.2119 0.2548 0.2816 0.0313  0.0338  0.0648  158 LYS   A CA  
3508 C  C   A LYS   A 158 ? 0.1654 0.2403 0.2858 0.0417  0.0345  0.0671  158 LYS   A C   
3509 C  C   B LYS   A 158 ? 0.1454 0.2631 0.2456 0.0533  0.0347  0.1062  158 LYS   A C   
3510 C  C   T LYS   A 158 ? 0.2100 0.2605 0.2733 0.0356  0.0239  0.0663  158 LYS   A C   
3511 O  O   A LYS   A 158 ? 0.1641 0.2469 0.2914 0.0359  0.0382  0.0657  158 LYS   A O   
3512 O  O   B LYS   A 158 ? 0.1356 0.2668 0.2393 0.0455  0.0349  0.1056  158 LYS   A O   
3513 O  O   T LYS   A 158 ? 0.2103 0.2640 0.2753 0.0340  0.0250  0.0658  158 LYS   A O   
3514 C  CB  A LYS   A 158 ? 0.2022 0.2408 0.3283 0.0398  0.0637  0.0698  158 LYS   A CB  
3515 C  CB  B LYS   A 158 ? 0.1829 0.2699 0.3026 0.0448  0.0785  0.0965  158 LYS   A CB  
3516 C  CB  T LYS   A 158 ? 0.2289 0.2669 0.3179 0.0325  0.0483  0.0663  158 LYS   A CB  
3517 C  CG  A LYS   A 158 ? 0.2220 0.2478 0.3563 0.0430  0.0685  0.0809  158 LYS   A CG  
3518 C  CG  B LYS   A 158 ? 0.2071 0.2864 0.3469 0.0461  0.0841  0.0935  158 LYS   A CG  
3519 C  CG  T LYS   A 158 ? 0.2444 0.2777 0.3514 0.0353  0.0545  0.0732  158 LYS   A CG  
3520 C  CD  A LYS   A 158 ? 0.2408 0.2550 0.3823 0.0429  0.0750  0.0908  158 LYS   A CD  
3521 C  CD  B LYS   A 158 ? 0.2299 0.2992 0.3914 0.0479  0.0806  0.0929  158 LYS   A CD  
3522 C  CD  T LYS   A 158 ? 0.2604 0.2870 0.3855 0.0380  0.0581  0.0798  158 LYS   A CD  
3523 C  CE  A LYS   A 158 ? 0.2529 0.2554 0.3953 0.0402  0.0824  0.1074  158 LYS   A CE  
3524 C  CE  B LYS   A 158 ? 0.2380 0.3041 0.4197 0.0553  0.0782  0.0952  158 LYS   A CE  
3525 C  CE  T LYS   A 158 ? 0.2712 0.2906 0.4091 0.0412  0.0596  0.0879  158 LYS   A CE  
3526 N  NZ  A LYS   A 158 ? 0.2580 0.2548 0.4030 0.0386  0.0873  0.1143  158 LYS   A NZ  
3527 N  NZ  B LYS   A 158 ? 0.2403 0.3061 0.4351 0.0584  0.0768  0.0976  158 LYS   A NZ  
3528 N  NZ  T LYS   A 158 ? 0.2767 0.2925 0.4223 0.0449  0.0587  0.0911  158 LYS   A NZ  
3568 N  N   A ASN   A 159 ? 0.1553 0.2394 0.2780 0.0398  0.0208  0.0702  159 ASN   A N   
3569 N  N   B ASN   A 159 ? 0.1503 0.2710 0.2528 0.0554  0.0241  0.0992  159 ASN   A N   
3570 N  N   T ASN   A 159 ? 0.2108 0.2625 0.2744 0.0348  0.0150  0.0649  159 ASN   A N   
3571 C  CA  A ASN   A 159 ? 0.1495 0.2392 0.2673 0.0333  0.0004  0.0803  159 ASN   A CA  
3572 C  CA  B ASN   A 159 ? 0.1583 0.2767 0.2565 0.0513  0.0107  0.0973  159 ASN   A CA  
3573 C  CA  T ASN   A 159 ? 0.2144 0.2650 0.2744 0.0310  0.0038  0.0698  159 ASN   A CA  
3574 C  C   A ASN   A 159 ? 0.1375 0.2325 0.2406 0.0220  0.0000  0.0740  159 ASN   A C   
3575 C  C   B ASN   A 159 ? 0.1436 0.2700 0.2368 0.0397  0.0098  0.0784  159 ASN   A C   
3576 C  C   T ASN   A 159 ? 0.2181 0.2649 0.2647 0.0246  0.0073  0.0612  159 ASN   A C   
3577 O  O   A ASN   A 159 ? 0.1326 0.2362 0.2368 0.0201  -0.0063 0.0610  159 ASN   A O   
3578 O  O   B ASN   A 159 ? 0.1408 0.2820 0.2427 0.0401  0.0023  0.0687  159 ASN   A O   
3579 O  O   T ASN   A 159 ? 0.2171 0.2660 0.2642 0.0211  0.0059  0.0506  159 ASN   A O   
3580 C  CB  A ASN   A 159 ? 0.1595 0.2456 0.2925 0.0364  -0.0118 0.0919  159 ASN   A CB  
3581 C  CB  B ASN   A 159 ? 0.1847 0.2877 0.2947 0.0524  0.0026  0.1044  159 ASN   A CB  
3582 C  CB  T ASN   A 159 ? 0.2173 0.2687 0.2940 0.0326  -0.0064 0.0794  159 ASN   A CB  
3583 C  CG  A ASN   A 159 ? 0.1707 0.2536 0.3278 0.0353  -0.0160 0.0914  159 ASN   A CG  
3584 C  CG  B ASN   A 159 ? 0.2106 0.2995 0.3374 0.0452  0.0030  0.0957  159 ASN   A CG  
3585 C  CG  T ASN   A 159 ? 0.2216 0.2735 0.3209 0.0319  -0.0117 0.0807  159 ASN   A CG  
3586 O  OD1 A ASN   A 159 ? 0.1797 0.2614 0.3451 0.0323  -0.0117 0.0922  159 ASN   A OD1 
3587 O  OD1 B ASN   A 159 ? 0.2179 0.3071 0.3578 0.0441  0.0097  0.0880  159 ASN   A OD1 
3588 O  OD1 T ASN   A 159 ? 0.2247 0.2792 0.3342 0.0312  -0.0082 0.0802  159 ASN   A OD1 
3589 N  ND2 A ASN   A 159 ? 0.1714 0.2563 0.3429 0.0358  -0.0189 0.0848  159 ASN   A ND2 
3590 N  ND2 B ASN   A 159 ? 0.2220 0.3048 0.3576 0.0383  0.0038  0.0882  159 ASN   A ND2 
3591 N  ND2 T ASN   A 159 ? 0.2217 0.2757 0.3327 0.0319  -0.0164 0.0772  159 ASN   A ND2 
3610 N  N   A LEU   A 160 ? 0.1288 0.2178 0.2179 0.0162  0.0025  0.0798  160 LEU   A N   
3611 N  N   B LEU   A 160 ? 0.1351 0.2492 0.2141 0.0265  0.0024  0.0741  160 LEU   A N   
3612 N  N   T LEU   A 160 ? 0.2217 0.2618 0.2576 0.0235  0.0092  0.0631  160 LEU   A N   
3613 C  CA  A LEU   A 160 ? 0.1249 0.2019 0.1935 0.0054  0.0140  0.0889  160 LEU   A CA  
3614 C  CA  B LEU   A 160 ? 0.1375 0.2326 0.2001 0.0126  0.0087  0.0683  160 LEU   A CA  
3615 C  CA  T LEU   A 160 ? 0.2296 0.2592 0.2508 0.0195  0.0145  0.0682  160 LEU   A CA  
3616 C  C   A LEU   A 160 ? 0.1169 0.1942 0.1817 0.0004  0.0204  0.0823  160 LEU   A C   
3617 C  C   B LEU   A 160 ? 0.1228 0.2204 0.1833 0.0107  0.0100  0.0691  160 LEU   A C   
3618 O  O   A LEU   A 160 ? 0.1101 0.1921 0.1742 -0.0027 0.0173  0.0774  160 LEU   A O   
3619 O  O   B LEU   A 160 ? 0.1202 0.2165 0.1855 0.0086  0.0002  0.0623  160 LEU   A O   
3620 C  CB  A LEU   A 160 ? 0.1210 0.1979 0.1768 0.0035  0.0158  0.0999  160 LEU   A CB  
3621 C  CB  B LEU   A 160 ? 0.1574 0.2356 0.1998 0.0018  0.0168  0.0509  160 LEU   A CB  
3622 C  CB  T LEU   A 160 ? 0.2350 0.2585 0.2458 0.0179  0.0186  0.0734  160 LEU   A CB  
3623 C  CG  A LEU   A 160 ? 0.1138 0.1962 0.1706 -0.0000 0.0134  0.0940  160 LEU   A CG  
3624 C  CG  B LEU   A 160 ? 0.1815 0.2466 0.2260 -0.0020 0.0212  0.0321  160 LEU   A CG  
3625 C  CG  T LEU   A 160 ? 0.2396 0.2591 0.2413 0.0161  0.0202  0.0748  160 LEU   A CG  
3626 C  CD1 A LEU   A 160 ? 0.1226 0.2016 0.1887 -0.0045 0.0202  0.0813  160 LEU   A CD1 
3627 C  CD1 B LEU   A 160 ? 0.1877 0.2487 0.2401 -0.0007 0.0198  0.0257  160 LEU   A CD1 
3628 C  CD1 T LEU   A 160 ? 0.2383 0.2555 0.2356 0.0121  0.0248  0.0757  160 LEU   A CD1 
3629 C  CD2 A LEU   A 160 ? 0.1110 0.1963 0.1799 -0.0051 0.0221  0.0800  160 LEU   A CD2 
3630 C  CD2 B LEU   A 160 ? 0.1915 0.2512 0.2235 -0.0046 0.0296  0.0300  160 LEU   A CD2 
3631 C  CD2 T LEU   A 160 ? 0.2401 0.2579 0.2344 0.0196  0.0187  0.0848  160 LEU   A CD2 
3664 N  N   A TYR   A 161 ? 0.1333 0.1931 0.2168 0.0019  0.0183  0.0714  161 TYR   A N   
3665 N  N   B TYR   A 161 ? 0.1273 0.2128 0.1840 0.0136  0.0215  0.0635  161 TYR   A N   
3666 C  CA  A TYR   A 161 ? 0.1373 0.1979 0.2164 -0.0002 0.0132  0.0627  161 TYR   A CA  
3667 C  CA  B TYR   A 161 ? 0.1327 0.2101 0.1795 0.0112  0.0226  0.0663  161 TYR   A CA  
3668 C  C   A TYR   A 161 ? 0.1356 0.2177 0.2315 0.0025  0.0147  0.0648  161 TYR   A C   
3669 C  C   B TYR   A 161 ? 0.1320 0.2233 0.1871 0.0054  0.0204  0.0706  161 TYR   A C   
3670 O  O   A TYR   A 161 ? 0.1268 0.2172 0.2305 -0.0027 0.0128  0.0590  161 TYR   A O   
3671 O  O   B TYR   A 161 ? 0.1271 0.2217 0.1747 -0.0022 0.0235  0.0665  161 TYR   A O   
3672 C  CB  A TYR   A 161 ? 0.1488 0.1903 0.2165 0.0028  0.0147  0.0535  161 TYR   A CB  
3673 C  CB  B TYR   A 161 ? 0.1422 0.1968 0.1826 0.0137  0.0288  0.0619  161 TYR   A CB  
3674 C  CG  A TYR   A 161 ? 0.1484 0.1806 0.2128 0.0040  0.0108  0.0435  161 TYR   A CG  
3675 C  CG  B TYR   A 161 ? 0.1419 0.1802 0.1909 0.0148  0.0362  0.0507  161 TYR   A CG  
3676 C  CD1 A TYR   A 161 ? 0.1463 0.1795 0.2164 0.0053  0.0057  0.0317  161 TYR   A CD1 
3677 C  CD1 B TYR   A 161 ? 0.1413 0.1729 0.1984 0.0150  0.0378  0.0410  161 TYR   A CD1 
3678 C  CD2 A TYR   A 161 ? 0.1484 0.1797 0.2116 0.0084  0.0026  0.0377  161 TYR   A CD2 
3679 C  CD2 B TYR   A 161 ? 0.1415 0.1730 0.1962 0.0168  0.0400  0.0490  161 TYR   A CD2 
3680 C  CE1 A TYR   A 161 ? 0.1443 0.1670 0.2116 0.0038  -0.0059 0.0292  161 TYR   A CE1 
3681 C  CE1 B TYR   A 161 ? 0.1422 0.1639 0.2024 0.0163  0.0359  0.0372  161 TYR   A CE1 
3682 C  CE2 A TYR   A 161 ? 0.1528 0.1687 0.2116 0.0032  -0.0042 0.0353  161 TYR   A CE2 
3683 C  CE2 B TYR   A 161 ? 0.1451 0.1635 0.2022 0.0119  0.0382  0.0474  161 TYR   A CE2 
3684 C  CZ  A TYR   A 161 ? 0.1555 0.1587 0.2044 -0.0007 -0.0085 0.0360  161 TYR   A CZ  
3685 C  CZ  B TYR   A 161 ? 0.1505 0.1586 0.2065 0.0091  0.0382  0.0421  161 TYR   A CZ  
3686 O  OH  A TYR   A 161 ? 0.1703 0.1455 0.2119 -0.0029 -0.0143 0.0379  161 TYR   A OH  
3687 O  OH  B TYR   A 161 ? 0.1621 0.1517 0.2299 0.0029  0.0297  0.0313  161 TYR   A OH  
3706 N  N   A ASP   A 162 ? 0.1366 0.2396 0.2475 0.0089  0.0222  0.0733  162 ASP   A N   
3707 N  N   B ASP   A 162 ? 0.1320 0.2371 0.2083 0.0044  0.0201  0.0806  162 ASP   A N   
3708 C  CA  A ASP   A 162 ? 0.1369 0.2641 0.2599 0.0096  0.0236  0.0693  162 ASP   A CA  
3709 C  CA  B ASP   A 162 ? 0.1321 0.2532 0.2270 -0.0000 0.0156  0.0810  162 ASP   A CA  
3710 C  C   A ASP   A 162 ? 0.1273 0.2789 0.2602 0.0036  0.0176  0.0686  162 ASP   A C   
3711 C  C   B ASP   A 162 ? 0.1326 0.2601 0.2276 -0.0151 0.0123  0.0839  162 ASP   A C   
3712 O  O   A ASP   A 162 ? 0.1297 0.2796 0.2728 -0.0003 0.0136  0.0591  162 ASP   A O   
3713 O  O   B ASP   A 162 ? 0.1333 0.2580 0.2359 -0.0225 0.0106  0.0792  162 ASP   A O   
3714 C  CB  A ASP   A 162 ? 0.1524 0.2727 0.2769 0.0130  0.0319  0.0666  162 ASP   A CB  
3715 C  CB  B ASP   A 162 ? 0.1361 0.2620 0.2510 0.0073  0.0212  0.0793  162 ASP   A CB  
3716 C  CG  A ASP   A 162 ? 0.1663 0.2851 0.2912 0.0116  0.0432  0.0648  162 ASP   A CG  
3717 C  CG  B ASP   A 162 ? 0.1390 0.2677 0.2646 0.0111  0.0314  0.0882  162 ASP   A CG  
3718 O  OD1 A ASP   A 162 ? 0.1783 0.2898 0.3020 0.0072  0.0421  0.0710  162 ASP   A OD1 
3719 O  OD1 B ASP   A 162 ? 0.1463 0.2702 0.2775 0.0134  0.0304  0.0941  162 ASP   A OD1 
3720 O  OD2 A ASP   A 162 ? 0.1749 0.2872 0.2935 0.0148  0.0597  0.0602  162 ASP   A OD2 
3721 O  OD2 B ASP   A 162 ? 0.1411 0.2732 0.2703 0.0145  0.0450  0.0907  162 ASP   A OD2 
3730 N  N   A LYS   A 163 ? 0.1334 0.2944 0.2562 0.0052  0.0033  0.0691  163 LYS   A N   
3731 N  N   B LYS   A 163 ? 0.1413 0.2687 0.2298 -0.0223 0.0005  0.0815  163 LYS   A N   
3732 C  CA  A LYS   A 163 ? 0.1413 0.3113 0.2515 -0.0022 -0.0087 0.0659  163 LYS   A CA  
3733 C  CA  B LYS   A 163 ? 0.1609 0.2807 0.2396 -0.0264 0.0018  0.0729  163 LYS   A CA  
3734 C  C   A LYS   A 163 ? 0.1381 0.3006 0.2361 -0.0092 0.0050  0.0647  163 LYS   A C   
3735 C  C   B LYS   A 163 ? 0.1553 0.2720 0.2249 -0.0253 0.0106  0.0632  163 LYS   A C   
3736 O  O   A LYS   A 163 ? 0.1374 0.3092 0.2402 -0.0104 0.0073  0.0623  163 LYS   A O   
3737 O  O   B LYS   A 163 ? 0.1573 0.2813 0.2307 -0.0256 0.0088  0.0613  163 LYS   A O   
3738 C  CB  A LYS   A 163 ? 0.1717 0.3353 0.2893 0.0123  -0.0255 0.0614  163 LYS   A CB  
3739 C  CB  B LYS   A 163 ? 0.1909 0.3004 0.2808 -0.0248 -0.0040 0.0669  163 LYS   A CB  
3740 C  CG  A LYS   A 163 ? 0.2030 0.3566 0.3365 0.0153  -0.0257 0.0602  163 LYS   A CG  
3741 C  CG  B LYS   A 163 ? 0.2172 0.3180 0.3299 -0.0267 -0.0019 0.0605  163 LYS   A CG  
3742 C  CD  A LYS   A 163 ? 0.2278 0.3743 0.3931 0.0152  -0.0235 0.0569  163 LYS   A CD  
3743 C  CD  B LYS   A 163 ? 0.2385 0.3328 0.3788 -0.0271 0.0000  0.0543  163 LYS   A CD  
3744 C  CE  A LYS   A 163 ? 0.2514 0.3860 0.4390 0.0154  -0.0162 0.0590  163 LYS   A CE  
3745 C  CE  B LYS   A 163 ? 0.2540 0.3432 0.4167 -0.0269 0.0012  0.0493  163 LYS   A CE  
3746 N  NZ  A LYS   A 163 ? 0.2676 0.3939 0.4652 0.0154  -0.0137 0.0614  163 LYS   A NZ  
3747 N  NZ  B LYS   A 163 ? 0.2630 0.3494 0.4361 -0.0274 0.0020  0.0494  163 LYS   A NZ  
3774 N  N   A LEU   A 164 ? 0.1274 0.2726 0.2151 -0.0160 0.0056  0.0555  164 LEU   A N   
3775 N  N   B LEU   A 164 ? 0.1435 0.2497 0.2040 -0.0243 0.0127  0.0516  164 LEU   A N   
3776 C  CA  A LEU   A 164 ? 0.1368 0.2474 0.1967 -0.0250 0.0158  0.0428  164 LEU   A CA  
3777 C  CA  B LEU   A 164 ? 0.1416 0.2281 0.1821 -0.0243 0.0168  0.0367  164 LEU   A CA  
3778 C  C   A LEU   A 164 ? 0.1452 0.2317 0.1781 -0.0219 0.0120  0.0338  164 LEU   A C   
3779 C  C   B LEU   A 164 ? 0.1452 0.2203 0.1709 -0.0260 0.0240  0.0330  164 LEU   A C   
3780 O  O   A LEU   A 164 ? 0.1495 0.2345 0.1755 -0.0281 0.0187  0.0064  164 LEU   A O   
3781 O  O   B LEU   A 164 ? 0.1531 0.2240 0.1691 -0.0351 0.0253  0.0273  164 LEU   A O   
3782 C  CB  A LEU   A 164 ? 0.1335 0.2384 0.1923 -0.0298 0.0257  0.0468  164 LEU   A CB  
3783 C  CB  B LEU   A 164 ? 0.1380 0.2139 0.1673 -0.0129 0.0198  0.0316  164 LEU   A CB  
3784 C  CG  A LEU   A 164 ? 0.1376 0.2346 0.1976 -0.0263 0.0131  0.0419  164 LEU   A CG  
3785 C  CG  B LEU   A 164 ? 0.1426 0.2047 0.1590 -0.0063 0.0110  0.0378  164 LEU   A CG  
3786 C  CD1 A LEU   A 164 ? 0.1312 0.2291 0.2061 -0.0216 0.0127  0.0458  164 LEU   A CD1 
3787 C  CD1 B LEU   A 164 ? 0.1445 0.1988 0.1570 -0.0065 0.0107  0.0456  164 LEU   A CD1 
3788 C  CD2 A LEU   A 164 ? 0.1489 0.2392 0.1868 -0.0265 0.0161  0.0382  164 LEU   A CD2 
3789 C  CD2 B LEU   A 164 ? 0.1421 0.2026 0.1372 -0.0052 0.0146  0.0417  164 LEU   A CD2 
3812 N  N   A VAL   A 165 ? 0.1452 0.2199 0.1741 -0.0133 0.0164  0.0395  165 VAL   A N   
3813 N  N   B VAL   A 165 ? 0.1344 0.2113 0.1643 -0.0214 0.0274  0.0330  165 VAL   A N   
3814 C  CA  A VAL   A 165 ? 0.1506 0.2179 0.1670 -0.0164 0.0288  0.0387  165 VAL   A CA  
3815 C  CA  B VAL   A 165 ? 0.1401 0.2103 0.1743 -0.0201 0.0239  0.0364  165 VAL   A CA  
3816 C  C   A VAL   A 165 ? 0.1446 0.2313 0.1727 -0.0180 0.0227  0.0393  165 VAL   A C   
3817 C  C   B VAL   A 165 ? 0.1319 0.2192 0.1777 -0.0186 0.0193  0.0319  165 VAL   A C   
3818 O  O   A VAL   A 165 ? 0.1440 0.2317 0.1516 -0.0218 0.0239  0.0259  165 VAL   A O   
3819 O  O   B VAL   A 165 ? 0.1367 0.2231 0.1693 -0.0157 0.0143  0.0189  165 VAL   A O   
3820 C  CB  A VAL   A 165 ? 0.1675 0.2066 0.1763 -0.0098 0.0315  0.0256  165 VAL   A CB  
3821 C  CB  B VAL   A 165 ? 0.1570 0.2053 0.1873 -0.0152 0.0209  0.0353  165 VAL   A CB  
3822 C  CG1 A VAL   A 165 ? 0.1722 0.2052 0.1693 -0.0124 0.0352  0.0165  165 VAL   A CG1 
3823 C  CG1 B VAL   A 165 ? 0.1599 0.2065 0.1837 -0.0155 0.0180  0.0287  165 VAL   A CG1 
3824 C  CG2 A VAL   A 165 ? 0.1776 0.2037 0.1902 -0.0067 0.0318  0.0303  165 VAL   A CG2 
3825 C  CG2 B VAL   A 165 ? 0.1645 0.2020 0.1938 -0.0109 0.0169  0.0391  165 VAL   A CG2 
3844 N  N   A SER   A 166 ? 0.1438 0.2447 0.2058 -0.0145 0.0172  0.0426  166 SER   A N   
3845 N  N   B SER   A 166 ? 0.1231 0.2284 0.1936 -0.0188 0.0208  0.0416  166 SER   A N   
3846 C  CA  A SER   A 166 ? 0.1484 0.2593 0.2173 -0.0162 0.0160  0.0459  166 SER   A CA  
3847 C  CA  B SER   A 166 ? 0.1245 0.2391 0.1937 -0.0193 0.0117  0.0473  166 SER   A CA  
3848 C  C   A SER   A 166 ? 0.1565 0.2696 0.2086 -0.0122 -0.0042 0.0443  166 SER   A C   
3849 C  C   B SER   A 166 ? 0.1318 0.2507 0.1742 -0.0205 0.0046  0.0547  166 SER   A C   
3850 O  O   A SER   A 166 ? 0.1718 0.2794 0.2182 -0.0214 -0.0106 0.0321  166 SER   A O   
3851 O  O   B SER   A 166 ? 0.1384 0.2551 0.1667 -0.0252 0.0037  0.0601  166 SER   A O   
3852 C  CB  A SER   A 166 ? 0.1573 0.2638 0.2388 -0.0112 0.0224  0.0499  166 SER   A CB  
3853 C  CB  B SER   A 166 ? 0.1342 0.2415 0.2176 -0.0167 0.0037  0.0462  166 SER   A CB  
3854 O  OG  A SER   A 166 ? 0.1658 0.2700 0.2642 -0.0028 0.0273  0.0526  166 SER   A OG  
3855 O  OG  B SER   A 166 ? 0.1411 0.2447 0.2355 -0.0126 -0.0029 0.0473  166 SER   A OG  
3866 N  N   A SER   A 167 ? 0.1588 0.2650 0.1790 0.0021  -0.0087 0.0558  167 SER   A N   
3867 N  N   B SER   A 167 ? 0.1387 0.2527 0.1818 -0.0154 0.0086  0.0520  167 SER   A N   
3868 C  CA  A SER   A 167 ? 0.1763 0.2627 0.1871 0.0030  -0.0039 0.0406  167 SER   A CA  
3869 C  CA  B SER   A 167 ? 0.1537 0.2555 0.1833 -0.0092 0.0195  0.0455  167 SER   A CA  
3870 C  C   A SER   A 167 ? 0.1845 0.2608 0.2019 0.0138  0.0110  0.0377  167 SER   A C   
3871 C  C   B SER   A 167 ? 0.1498 0.2651 0.1877 0.0044  0.0271  0.0367  167 SER   A C   
3872 O  O   A SER   A 167 ? 0.2026 0.2703 0.2223 0.0247  -0.0030 0.0367  167 SER   A O   
3873 O  O   B SER   A 167 ? 0.1657 0.2762 0.2041 0.0131  0.0202  0.0273  167 SER   A O   
3874 C  CB  A SER   A 167 ? 0.1774 0.2618 0.1934 -0.0003 0.0014  0.0345  167 SER   A CB  
3875 C  CB  B SER   A 167 ? 0.1701 0.2524 0.1947 -0.0067 0.0256  0.0317  167 SER   A CB  
3876 O  OG  A SER   A 167 ? 0.1793 0.2626 0.2048 -0.0015 0.0104  0.0243  167 SER   A OG  
3877 O  OG  B SER   A 167 ? 0.1804 0.2511 0.2043 -0.0056 0.0304  0.0203  167 SER   A OG  
3888 N  N   A PHE   A 168 ? 0.1704 0.2496 0.1951 0.0159  0.0198  0.0417  168 PHE   A N   
3889 N  N   B PHE   A 168 ? 0.1357 0.2639 0.1804 0.0091  0.0285  0.0322  168 PHE   A N   
3890 C  CA  A PHE   A 168 ? 0.1766 0.2510 0.2185 0.0098  0.0212  0.0422  168 PHE   A CA  
3891 C  CA  B PHE   A 168 ? 0.1339 0.2640 0.1857 0.0077  0.0288  0.0275  168 PHE   A CA  
3892 C  C   A PHE   A 168 ? 0.1852 0.2620 0.2600 0.0034  0.0380  0.0336  168 PHE   A C   
3893 C  C   B PHE   A 168 ? 0.1370 0.2650 0.2063 -0.0013 0.0379  0.0141  168 PHE   A C   
3894 O  O   A PHE   A 168 ? 0.1912 0.2694 0.2999 -0.0027 0.0469  0.0481  168 PHE   A O   
3895 O  O   B PHE   A 168 ? 0.1295 0.2625 0.1972 -0.0051 0.0489  -0.0007 168 PHE   A O   
3896 C  CB  A PHE   A 168 ? 0.1748 0.2452 0.1995 0.0041  0.0094  0.0385  168 PHE   A CB  
3897 C  CB  B PHE   A 168 ? 0.1381 0.2637 0.1867 0.0064  0.0235  0.0314  168 PHE   A CB  
3898 C  CG  A PHE   A 168 ? 0.1690 0.2396 0.1786 -0.0026 0.0026  0.0294  168 PHE   A CG  
3899 C  CG  B PHE   A 168 ? 0.1402 0.2614 0.1930 0.0065  0.0216  0.0362  168 PHE   A CG  
3900 C  CD1 A PHE   A 168 ? 0.1624 0.2422 0.1732 -0.0107 0.0016  0.0257  168 PHE   A CD1 
3901 C  CD1 B PHE   A 168 ? 0.1416 0.2635 0.2025 0.0047  0.0251  0.0394  168 PHE   A CD1 
3902 C  CD2 A PHE   A 168 ? 0.1686 0.2352 0.1762 -0.0041 0.0047  0.0199  168 PHE   A CD2 
3903 C  CD2 B PHE   A 168 ? 0.1426 0.2573 0.1982 0.0094  0.0129  0.0377  168 PHE   A CD2 
3904 C  CE1 A PHE   A 168 ? 0.1532 0.2356 0.1724 -0.0121 -0.0065 0.0144  168 PHE   A CE1 
3905 C  CE1 B PHE   A 168 ? 0.1423 0.2622 0.2090 0.0047  0.0227  0.0444  168 PHE   A CE1 
3906 C  CE2 A PHE   A 168 ? 0.1688 0.2301 0.1815 -0.0063 0.0009  0.0193  168 PHE   A CE2 
3907 C  CE2 B PHE   A 168 ? 0.1469 0.2562 0.2066 0.0083  0.0087  0.0429  168 PHE   A CE2 
3908 C  CZ  A PHE   A 168 ? 0.1577 0.2327 0.1731 -0.0113 -0.0088 0.0144  168 PHE   A CZ  
3909 C  CZ  B PHE   A 168 ? 0.1471 0.2586 0.2099 0.0044  0.0196  0.0418  168 PHE   A CZ  
3928 N  N   A LEU   A 169 ? 0.2061 0.2653 0.2861 -0.0015 0.0418  0.0087  169 LEU   A N   
3929 N  N   B LEU   A 169 ? 0.1565 0.2717 0.2456 -0.0020 0.0330  0.0205  169 LEU   A N   
3930 C  CA  A LEU   A 169 ? 0.2258 0.2723 0.3171 -0.0005 0.0352  -0.0005 169 LEU   A CA  
3931 C  CA  B LEU   A 169 ? 0.1844 0.2819 0.2892 -0.0051 0.0282  0.0217  169 LEU   A CA  
3932 C  C   A LEU   A 169 ? 0.2126 0.2654 0.3214 -0.0004 0.0492  0.0153  169 LEU   A C   
3933 C  C   B LEU   A 169 ? 0.1963 0.2896 0.3212 -0.0029 0.0206  0.0198  169 LEU   A C   
3934 O  O   A LEU   A 169 ? 0.2147 0.2700 0.3355 0.0012  0.0436  0.0149  169 LEU   A O   
3935 O  O   B LEU   A 169 ? 0.1938 0.2922 0.3302 -0.0046 0.0135  0.0179  169 LEU   A O   
3936 C  CB  A LEU   A 169 ? 0.2520 0.2857 0.3248 0.0010  0.0277  -0.0224 169 LEU   A CB  
3937 C  CB  B LEU   A 169 ? 0.1993 0.2860 0.2916 -0.0065 0.0346  0.0264  169 LEU   A CB  
3938 C  CG  A LEU   A 169 ? 0.2757 0.2973 0.3299 -0.0015 0.0240  -0.0461 169 LEU   A CG  
3939 C  CG  B LEU   A 169 ? 0.2124 0.2895 0.2985 -0.0089 0.0467  0.0305  169 LEU   A CG  
3940 C  CD1 A LEU   A 169 ? 0.2846 0.2998 0.3361 -0.0021 0.0189  -0.0515 169 LEU   A CD1 
3941 C  CD1 B LEU   A 169 ? 0.2214 0.2928 0.3110 -0.0067 0.0510  0.0316  169 LEU   A CD1 
3942 C  CD2 A LEU   A 169 ? 0.2825 0.3030 0.3278 -0.0045 0.0266  -0.0545 169 LEU   A CD2 
3943 C  CD2 B LEU   A 169 ? 0.2209 0.2908 0.2954 -0.0095 0.0538  0.0319  169 LEU   A CD2 
3944 O  OXT A LEU   A 169 ? 0.1964 0.2637 0.3053 -0.0040 0.0722  0.0208  169 LEU   A OXT 
3945 O  OXT B LEU   A 169 ? 0.2117 0.2955 0.3379 -0.0045 0.0211  0.0198  169 LEU   A OXT 
3968 N  N   A SER   B 1   ? 0.3530 0.3499 0.3645 -0.1124 -0.1004 0.0459  1   SER   B N   
3969 N  N   B SER   B 1   ? 0.3140 0.3371 0.3470 -0.0890 -0.0646 0.0518  1   SER   B N   
3970 C  CA  A SER   B 1   ? 0.3443 0.3528 0.3675 -0.1174 -0.1072 0.0392  1   SER   B CA  
3971 C  CA  B SER   B 1   ? 0.3073 0.3396 0.3466 -0.0921 -0.0663 0.0490  1   SER   B CA  
3972 C  C   A SER   B 1   ? 0.3193 0.3521 0.3503 -0.1176 -0.1121 0.0550  1   SER   B C   
3973 C  C   B SER   B 1   ? 0.2883 0.3365 0.3237 -0.0928 -0.0712 0.0608  1   SER   B C   
3974 O  O   A SER   B 1   ? 0.3289 0.3556 0.3366 -0.1126 -0.1058 0.0524  1   SER   B O   
3975 O  O   B SER   B 1   ? 0.2947 0.3385 0.3126 -0.0895 -0.0683 0.0569  1   SER   B O   
3976 C  CB  A SER   B 1   ? 0.3566 0.3527 0.3825 -0.1198 -0.1016 0.0227  1   SER   B CB  
3977 C  CB  B SER   B 1   ? 0.3153 0.3424 0.3648 -0.0927 -0.0595 0.0381  1   SER   B CB  
3978 O  OG  A SER   B 1   ? 0.3712 0.3610 0.4193 -0.1153 -0.0929 0.0159  1   SER   B OG  
3979 O  OG  B SER   B 1   ? 0.3239 0.3497 0.3930 -0.0904 -0.0551 0.0332  1   SER   B OG  
3994 N  N   A MET   B 2   ? 0.2937 0.3469 0.3471 -0.1145 -0.1063 0.0879  2   MET   B N   
3995 N  N   B MET   B 2   ? 0.2684 0.3302 0.3080 -0.0926 -0.0690 0.0886  2   MET   B N   
3996 C  CA  A MET   B 2   ? 0.2739 0.3428 0.3566 -0.0949 -0.0989 0.1104  2   MET   B CA  
3997 C  CA  B MET   B 2   ? 0.2518 0.3245 0.2984 -0.0802 -0.0680 0.1088  2   MET   B CA  
3998 C  C   A MET   B 2   ? 0.2384 0.3174 0.3223 -0.0768 -0.1033 0.1346  2   MET   B C   
3999 C  C   B MET   B 2   ? 0.2283 0.3049 0.2812 -0.0688 -0.0623 0.1171  2   MET   B C   
4000 O  O   A MET   B 2   ? 0.2338 0.3267 0.3185 -0.0675 -0.1160 0.1392  2   MET   B O   
4001 O  O   B MET   B 2   ? 0.2266 0.3120 0.2840 -0.0641 -0.0591 0.1133  2   MET   B O   
4002 C  CB  A MET   B 2   ? 0.2993 0.3708 0.4331 -0.0781 -0.0772 0.0892  2   MET   B CB  
4003 C  CB  B MET   B 2   ? 0.2654 0.3439 0.3274 -0.0683 -0.0678 0.1078  2   MET   B CB  
4004 C  CG  A MET   B 2   ? 0.3239 0.3951 0.5098 -0.0577 -0.0551 0.0743  2   MET   B CG  
4005 C  CG  B MET   B 2   ? 0.2770 0.3611 0.3498 -0.0539 -0.0657 0.1159  2   MET   B CG  
4006 S  SD  A MET   B 2   ? 0.3492 0.4174 0.5796 -0.0392 -0.0396 0.0633  2   MET   B SD  
4007 S  SD  B MET   B 2   ? 0.2917 0.3792 0.3688 -0.0398 -0.0661 0.1237  2   MET   B SD  
4008 C  CE  A MET   B 2   ? 0.3510 0.4220 0.5835 -0.0385 -0.0338 0.0637  2   MET   B CE  
4009 C  CE  B MET   B 2   ? 0.2910 0.3811 0.3737 -0.0405 -0.0667 0.1174  2   MET   B CE  
4028 N  N   A VAL   B 3   ? 0.2095 0.2767 0.3011 -0.0749 -0.0888 0.1464  3   VAL   B N   
4029 N  N   B VAL   B 3   ? 0.2070 0.2756 0.2663 -0.0652 -0.0572 0.1257  3   VAL   B N   
4030 C  CA  A VAL   B 3   ? 0.2025 0.2450 0.3021 -0.0666 -0.0707 0.1270  3   VAL   B CA  
4031 C  CA  B VAL   B 3   ? 0.1989 0.2510 0.2653 -0.0554 -0.0489 0.1123  3   VAL   B CA  
4032 C  C   A VAL   B 3   ? 0.1817 0.2284 0.2633 -0.0595 -0.0649 0.1108  3   VAL   B C   
4033 C  C   B VAL   B 3   ? 0.1814 0.2359 0.2445 -0.0508 -0.0527 0.1058  3   VAL   B C   
4034 O  O   A VAL   B 3   ? 0.1846 0.2276 0.2616 -0.0517 -0.0705 0.1088  3   VAL   B O   
4035 O  O   B VAL   B 3   ? 0.1810 0.2446 0.2461 -0.0360 -0.0600 0.1063  3   VAL   B O   
4036 C  CB  A VAL   B 3   ? 0.2172 0.2414 0.3410 -0.0669 -0.0664 0.1119  3   VAL   B CB  
4037 C  CB  B VAL   B 3   ? 0.2107 0.2450 0.2865 -0.0510 -0.0441 0.1034  3   VAL   B CB  
4038 C  CG1 A VAL   B 3   ? 0.2226 0.2359 0.3560 -0.0738 -0.0625 0.1088  3   VAL   B CG1 
4039 C  CG1 B VAL   B 3   ? 0.2156 0.2404 0.2950 -0.0537 -0.0404 0.1014  3   VAL   B CG1 
4040 C  CG2 A VAL   B 3   ? 0.2196 0.2479 0.3590 -0.0610 -0.0575 0.1114  3   VAL   B CG2 
4041 C  CG2 B VAL   B 3   ? 0.2128 0.2467 0.2965 -0.0461 -0.0415 0.1029  3   VAL   B CG2 
4060 N  N   . ASN   B 4   ? 0.1726 0.2138 0.2314 -0.0562 -0.0552 0.0939  4   ASN   B N   
4061 C  CA  . ASN   B 4   ? 0.1742 0.2100 0.1892 -0.0565 -0.0477 0.0537  4   ASN   B CA  
4062 C  C   . ASN   B 4   ? 0.1790 0.2264 0.1863 -0.0559 -0.0371 0.0365  4   ASN   B C   
4063 O  O   . ASN   B 4   ? 0.1808 0.2323 0.2063 -0.0532 -0.0287 0.0152  4   ASN   B O   
4064 C  CB  . ASN   B 4   ? 0.1760 0.2082 0.1735 -0.0500 -0.0547 0.0370  4   ASN   B CB  
4065 C  CG  . ASN   B 4   ? 0.1804 0.1956 0.1547 -0.0498 -0.0466 0.0327  4   ASN   B CG  
4066 O  OD1 . ASN   B 4   ? 0.1842 0.1776 0.1557 -0.0482 -0.0452 0.0280  4   ASN   B OD1 
4067 N  ND2 . ASN   B 4   ? 0.1980 0.2062 0.1665 -0.0272 -0.0330 0.0319  4   ASN   B ND2 
4075 N  N   . SER   B 5   ? 0.1936 0.2462 0.1851 -0.0572 -0.0260 0.0394  5   SER   B N   
4076 C  CA  . SER   B 5   ? 0.2241 0.2787 0.2073 -0.0492 -0.0090 0.0359  5   SER   B CA  
4077 C  C   . SER   B 5   ? 0.2431 0.2819 0.2446 -0.0649 0.0133  0.0305  5   SER   B C   
4078 O  O   . SER   B 5   ? 0.2608 0.2772 0.3190 -0.0571 0.0468  0.0250  5   SER   B O   
4079 C  CB  . SER   B 5   ? 0.2387 0.2991 0.2221 -0.0400 0.0026  0.0452  5   SER   B CB  
4080 O  OG  . SER   B 5   ? 0.2635 0.3227 0.2755 -0.0272 0.0066  0.0435  5   SER   B OG  
4086 N  N   . PHE   B 6   ? 0.2583 0.3007 0.2224 -0.0699 0.0243  0.0376  6   PHE   B N   
4087 C  CA  . PHE   B 6   ? 0.2667 0.3050 0.1905 -0.0890 0.0303  0.0173  6   PHE   B CA  
4088 C  C   . PHE   B 6   ? 0.3187 0.3374 0.2320 -0.0946 0.0601  -0.0109 6   PHE   B C   
4089 O  O   . PHE   B 6   ? 0.3312 0.3673 0.2635 -0.0859 0.0558  -0.0212 6   PHE   B O   
4090 C  CB  . PHE   B 6   ? 0.2385 0.2848 0.1702 -0.0813 0.0125  0.0140  6   PHE   B CB  
4091 C  CG  . PHE   B 6   ? 0.2085 0.2516 0.1502 -0.0750 0.0026  0.0139  6   PHE   B CG  
4092 C  CD1 . PHE   B 6   ? 0.2127 0.2271 0.1393 -0.0639 -0.0077 0.0065  6   PHE   B CD1 
4093 C  CD2 . PHE   B 6   ? 0.1880 0.2485 0.1621 -0.0646 0.0011  0.0376  6   PHE   B CD2 
4094 C  CE1 . PHE   B 6   ? 0.2047 0.2041 0.1460 -0.0602 -0.0131 0.0064  6   PHE   B CE1 
4095 C  CE2 . PHE   B 6   ? 0.1916 0.2371 0.1903 -0.0539 0.0104  0.0324  6   PHE   B CE2 
4096 C  CZ  . PHE   B 6   ? 0.1962 0.2138 0.1707 -0.0538 -0.0023 0.0116  6   PHE   B CZ  
4106 N  N   . SER   B 7   ? 0.3558 0.3224 0.2394 -0.1170 0.0926  -0.0383 7   SER   B N   
4107 C  CA  . SER   B 7   ? 0.3918 0.3346 0.2868 -0.1162 0.1137  -0.0479 7   SER   B CA  
4108 C  C   . SER   B 7   ? 0.3925 0.3191 0.2772 -0.1177 0.1372  -0.0603 7   SER   B C   
4109 O  O   . SER   B 7   ? 0.4009 0.3195 0.3097 -0.1186 0.1345  -0.0664 7   SER   B O   
4110 C  CB  . SER   B 7   ? 0.4146 0.3519 0.3431 -0.1135 0.1183  -0.0474 7   SER   B CB  
4111 O  OG  . SER   B 7   ? 0.4287 0.3589 0.3893 -0.1118 0.1160  -0.0439 7   SER   B OG  
4117 N  N   . GLY   B 8   ? 0.3889 0.3091 0.2813 -0.1044 0.1482  -0.0670 8   GLY   B N   
4118 C  CA  . GLY   B 8   ? 0.3741 0.2938 0.2889 -0.0970 0.1478  -0.0723 8   GLY   B CA  
4119 C  C   . GLY   B 8   ? 0.3518 0.2663 0.2806 -0.0938 0.1470  -0.0701 8   GLY   B C   
4120 O  O   . GLY   B 8   ? 0.3642 0.2710 0.3210 -0.0862 0.1430  -0.0744 8   GLY   B O   
4124 N  N   . TYR   B 9   ? 0.3302 0.2439 0.2597 -0.0808 0.1172  -0.0816 9   TYR   B N   
4125 C  CA  . TYR   B 9   ? 0.3050 0.2157 0.2329 -0.0689 0.0873  -0.0658 9   TYR   B CA  
4126 C  C   . TYR   B 9   ? 0.3028 0.2115 0.2166 -0.0660 0.0591  -0.0505 9   TYR   B C   
4127 O  O   . TYR   B 9   ? 0.3161 0.2322 0.2587 -0.0670 0.0632  -0.0362 9   TYR   B O   
4128 C  CB  . TYR   B 9   ? 0.2901 0.1939 0.2392 -0.0611 0.0807  -0.0576 9   TYR   B CB  
4129 C  CG  . TYR   B 9   ? 0.2769 0.1792 0.2467 -0.0616 0.0697  -0.0613 9   TYR   B CG  
4130 C  CD1 . TYR   B 9   ? 0.2792 0.1805 0.2516 -0.0739 0.0747  -0.0556 9   TYR   B CD1 
4131 C  CD2 . TYR   B 9   ? 0.2636 0.1736 0.2362 -0.0586 0.0620  -0.0634 9   TYR   B CD2 
4132 C  CE1 . TYR   B 9   ? 0.2763 0.1901 0.2460 -0.0789 0.0767  -0.0601 9   TYR   B CE1 
4133 C  CE2 . TYR   B 9   ? 0.2658 0.1781 0.2340 -0.0584 0.0652  -0.0591 9   TYR   B CE2 
4134 C  CZ  . TYR   B 9   ? 0.2720 0.1907 0.2435 -0.0748 0.0697  -0.0631 9   TYR   B CZ  
4135 O  OH  . TYR   B 9   ? 0.2751 0.2022 0.2597 -0.0842 0.0669  -0.0802 9   TYR   B OH  
4145 N  N   . LEU   B 10  ? 0.2864 0.1890 0.1936 -0.0639 0.0307  -0.0465 10  LEU   B N   
4146 C  CA  . LEU   B 10  ? 0.2834 0.1872 0.1967 -0.0722 -0.0054 -0.0347 10  LEU   B CA  
4147 C  C   . LEU   B 10  ? 0.2647 0.1835 0.1972 -0.0672 -0.0162 -0.0308 10  LEU   B C   
4148 O  O   . LEU   B 10  ? 0.2490 0.1878 0.2064 -0.0514 -0.0080 -0.0247 10  LEU   B O   
4149 C  CB  . LEU   B 10  ? 0.2993 0.1850 0.2126 -0.0778 -0.0257 -0.0133 10  LEU   B CB  
4150 C  CG  . LEU   B 10  ? 0.3216 0.1937 0.2494 -0.0713 -0.0563 -0.0035 10  LEU   B CG  
4151 C  CD1 . LEU   B 10  ? 0.3382 0.2063 0.2689 -0.0642 -0.0536 -0.0041 10  LEU   B CD1 
4152 C  CD2 . LEU   B 10  ? 0.3293 0.1994 0.2800 -0.0710 -0.0541 0.0202  10  LEU   B CD2 
4164 N  N   . LYS   B 11  ? 0.2805 0.2081 0.2003 -0.0615 -0.0219 -0.0257 11  LYS   B N   
4165 C  CA  . LYS   B 11  ? 0.2964 0.2354 0.2328 -0.0472 -0.0294 -0.0283 11  LYS   B CA  
4166 C  C   . LYS   B 11  ? 0.2753 0.2153 0.2402 -0.0666 -0.0279 -0.0419 11  LYS   B C   
4167 O  O   . LYS   B 11  ? 0.2876 0.2349 0.2792 -0.0832 -0.0277 -0.0699 11  LYS   B O   
4168 C  CB  . LYS   B 11  ? 0.3320 0.2830 0.2962 -0.0221 -0.0367 -0.0263 11  LYS   B CB  
4169 C  CG  . LYS   B 11  ? 0.3617 0.3151 0.3705 -0.0062 -0.0397 -0.0250 11  LYS   B CG  
4170 C  CD  . LYS   B 11  ? 0.3844 0.3364 0.4361 0.0035  -0.0401 -0.0245 11  LYS   B CD  
4171 C  CE  . LYS   B 11  ? 0.4017 0.3514 0.4835 0.0039  -0.0422 -0.0267 11  LYS   B CE  
4172 N  NZ  . LYS   B 11  ? 0.4105 0.3610 0.5092 0.0023  -0.0455 -0.0258 11  LYS   B NZ  
4186 N  N   . LEU   B 12  ? 0.2423 0.1869 0.2396 -0.0590 -0.0238 -0.0389 12  LEU   B N   
4187 C  CA  . LEU   B 12  ? 0.2243 0.1719 0.2521 -0.0516 -0.0200 -0.0293 12  LEU   B CA  
4188 C  C   . LEU   B 12  ? 0.2104 0.1722 0.2635 -0.0531 -0.0315 -0.0283 12  LEU   B C   
4189 O  O   . LEU   B 12  ? 0.2083 0.1754 0.2792 -0.0591 -0.0508 -0.0216 12  LEU   B O   
4190 C  CB  . LEU   B 12  ? 0.2227 0.1554 0.2513 -0.0394 -0.0202 -0.0311 12  LEU   B CB  
4191 C  CG  . LEU   B 12  ? 0.2235 0.1503 0.2520 -0.0428 -0.0139 -0.0231 12  LEU   B CG  
4192 C  CD1 . LEU   B 12  ? 0.2366 0.1530 0.2517 -0.0302 -0.0145 -0.0057 12  LEU   B CD1 
4193 C  CD2 . LEU   B 12  ? 0.2344 0.1566 0.2586 -0.0435 -0.0137 -0.0262 12  LEU   B CD2 
4205 N  N   . THR   B 13  ? 0.2042 0.1783 0.2598 -0.0537 -0.0390 -0.0404 13  THR   B N   
4206 C  CA  . THR   B 13  ? 0.2029 0.1865 0.2565 -0.0578 -0.0498 -0.0210 13  THR   B CA  
4207 C  C   . THR   B 13  ? 0.2401 0.2030 0.2762 -0.0649 -0.0728 -0.0154 13  THR   B C   
4208 O  O   . THR   B 13  ? 0.2564 0.2048 0.2890 -0.0626 -0.0444 -0.0140 13  THR   B O   
4209 C  CB  . THR   B 13  ? 0.1832 0.1895 0.2546 -0.0513 -0.0405 -0.0150 13  THR   B CB  
4210 O  OG1 . THR   B 13  ? 0.1755 0.1808 0.2640 -0.0482 -0.0378 -0.0206 13  THR   B OG1 
4211 C  CG2 . THR   B 13  ? 0.1862 0.1976 0.2552 -0.0466 -0.0262 -0.0036 13  THR   B CG2 
4219 N  N   A ASP   B 14  ? 0.2520 0.2193 0.2859 -0.0679 -0.1074 -0.0049 14  ASP   B N   
4220 N  N   B ASP   B 14  ? 0.2492 0.2146 0.2820 -0.0626 -0.0890 -0.0034 14  ASP   B N   
4221 C  CA  A ASP   B 14  ? 0.2640 0.2319 0.3139 -0.0674 -0.1115 0.0172  14  ASP   B CA  
4222 C  CA  B ASP   B 14  ? 0.2572 0.2232 0.2975 -0.0598 -0.0891 0.0129  14  ASP   B CA  
4223 C  C   A ASP   B 14  ? 0.2500 0.2124 0.2726 -0.0692 -0.0930 0.0208  14  ASP   B C   
4224 C  C   B ASP   B 14  ? 0.2415 0.2057 0.2656 -0.0611 -0.0830 0.0138  14  ASP   B C   
4225 O  O   A ASP   B 14  ? 0.2713 0.2214 0.2718 -0.0664 -0.0888 0.0322  14  ASP   B O   
4226 O  O   B ASP   B 14  ? 0.2528 0.2058 0.2638 -0.0567 -0.0800 0.0166  14  ASP   B O   
4227 C  CB  A ASP   B 14  ? 0.2878 0.2638 0.3973 -0.0637 -0.1226 0.0183  14  ASP   B CB  
4228 C  CB  B ASP   B 14  ? 0.2792 0.2487 0.3536 -0.0543 -0.0889 0.0177  14  ASP   B CB  
4229 C  CG  A ASP   B 14  ? 0.3126 0.2896 0.4751 -0.0588 -0.1188 0.0077  14  ASP   B CG  
4230 C  CG  B ASP   B 14  ? 0.3000 0.2696 0.4045 -0.0492 -0.0832 0.0142  14  ASP   B CG  
4231 O  OD1 A ASP   B 14  ? 0.3270 0.2987 0.4979 -0.0624 -0.1170 -0.0043 14  ASP   B OD1 
4232 O  OD1 B ASP   B 14  ? 0.3087 0.2799 0.4191 -0.0484 -0.0780 0.0110  14  ASP   B OD1 
4233 O  OD2 A ASP   B 14  ? 0.3161 0.2997 0.5098 -0.0576 -0.1158 0.0084  14  ASP   B OD2 
4234 O  OD2 B ASP   B 14  ? 0.3054 0.2749 0.4250 -0.0521 -0.0832 0.0138  14  ASP   B OD2 
4243 N  N   . ASN   B 15  ? 0.2169 0.1893 0.2465 -0.0560 -0.0797 0.0154  15  ASN   B N   
4244 C  CA  . ASN   B 15  ? 0.1791 0.1645 0.2286 -0.0368 -0.0567 0.0037  15  ASN   B CA  
4245 C  C   . ASN   B 15  ? 0.1597 0.1508 0.2138 -0.0274 -0.0422 -0.0075 15  ASN   B C   
4246 O  O   . ASN   B 15  ? 0.1604 0.1453 0.2265 -0.0237 -0.0471 -0.0171 15  ASN   B O   
4247 C  CB  . ASN   B 15  ? 0.1749 0.1596 0.2390 -0.0218 -0.0514 0.0091  15  ASN   B CB  
4248 C  CG  . ASN   B 15  ? 0.1617 0.1540 0.2407 -0.0286 -0.0230 0.0128  15  ASN   B CG  
4249 O  OD1 . ASN   B 15  ? 0.1670 0.1804 0.2668 -0.0474 -0.0276 0.0164  15  ASN   B OD1 
4250 N  ND2 . ASN   B 15  ? 0.1599 0.1377 0.2269 -0.0151 -0.0006 -0.0084 15  ASN   B ND2 
4258 N  N   . VAL   B 16  ? 0.1653 0.1409 0.2102 -0.0348 -0.0429 -0.0085 16  VAL   B N   
4259 C  CA  . VAL   B 16  ? 0.1678 0.1427 0.1953 -0.0291 -0.0324 -0.0192 16  VAL   B CA  
4260 C  C   . VAL   B 16  ? 0.1664 0.1517 0.1981 -0.0375 -0.0306 -0.0149 16  VAL   B C   
4261 O  O   . VAL   B 16  ? 0.1690 0.1644 0.2172 -0.0374 -0.0259 -0.0281 16  VAL   B O   
4262 C  CB  . VAL   B 16  ? 0.1744 0.1429 0.2044 -0.0179 -0.0284 -0.0194 16  VAL   B CB  
4263 C  CG1 . VAL   B 16  ? 0.1843 0.1394 0.1983 -0.0075 -0.0254 -0.0109 16  VAL   B CG1 
4264 C  CG2 . VAL   B 16  ? 0.1733 0.1529 0.2175 -0.0072 -0.0225 -0.0214 16  VAL   B CG2 
4274 N  N   . TYR   B 17  ? 0.1694 0.1629 0.2031 -0.0363 -0.0268 -0.0227 17  TYR   B N   
4275 C  CA  . TYR   B 17  ? 0.1713 0.1760 0.1934 -0.0425 -0.0264 -0.0014 17  TYR   B CA  
4276 C  C   . TYR   B 17  ? 0.1665 0.1494 0.1902 -0.0399 -0.0150 -0.0104 17  TYR   B C   
4277 O  O   . TYR   B 17  ? 0.1685 0.1544 0.1916 -0.0339 -0.0171 -0.0348 17  TYR   B O   
4278 C  CB  . TYR   B 17  ? 0.2048 0.2187 0.2092 -0.0253 -0.0218 0.0285  17  TYR   B CB  
4279 C  CG  . TYR   B 17  ? 0.2290 0.2643 0.2305 -0.0163 -0.0352 0.0345  17  TYR   B CG  
4280 C  CD1 . TYR   B 17  ? 0.2462 0.2781 0.2599 -0.0182 -0.0389 0.0451  17  TYR   B CD1 
4281 C  CD2 . TYR   B 17  ? 0.2463 0.2904 0.2540 -0.0063 -0.0445 0.0303  17  TYR   B CD2 
4282 C  CE1 . TYR   B 17  ? 0.2628 0.3011 0.2768 -0.0101 -0.0499 0.0415  17  TYR   B CE1 
4283 C  CE2 . TYR   B 17  ? 0.2618 0.3085 0.2773 0.0046  -0.0590 0.0387  17  TYR   B CE2 
4284 C  CZ  . TYR   B 17  ? 0.2753 0.3156 0.2891 0.0050  -0.0623 0.0459  17  TYR   B CZ  
4285 O  OH  . TYR   B 17  ? 0.2941 0.3311 0.3128 0.0127  -0.0696 0.0467  17  TYR   B OH  
4295 N  N   . ILE   B 18  ? 0.1782 0.1502 0.1797 -0.0337 -0.0107 -0.0195 18  ILE   B N   
4296 C  CA  . ILE   B 18  ? 0.1848 0.1444 0.1846 -0.0354 -0.0045 -0.0244 18  ILE   B CA  
4297 C  C   . ILE   B 18  ? 0.1953 0.1497 0.1797 -0.0422 0.0006  -0.0388 18  ILE   B C   
4298 O  O   . ILE   B 18  ? 0.2166 0.1657 0.1934 -0.0372 0.0033  -0.0418 18  ILE   B O   
4299 C  CB  . ILE   B 18  ? 0.1925 0.1486 0.1945 -0.0416 -0.0076 -0.0182 18  ILE   B CB  
4300 C  CG1 . ILE   B 18  ? 0.1944 0.1512 0.2094 -0.0376 -0.0009 -0.0091 18  ILE   B CG1 
4301 C  CG2 . ILE   B 18  ? 0.1947 0.1549 0.1965 -0.0471 -0.0095 -0.0111 18  ILE   B CG2 
4302 C  CD1 . ILE   B 18  ? 0.2027 0.1793 0.2210 -0.0400 -0.0106 0.0115  18  ILE   B CD1 
4314 N  N   . LYS   B 19  ? 0.1931 0.1495 0.1939 -0.0236 0.0308  -0.0436 19  LYS   B N   
4315 C  CA  . LYS   B 19  ? 0.2010 0.1556 0.2190 -0.0258 0.0306  -0.0417 19  LYS   B CA  
4316 C  C   . LYS   B 19  ? 0.1811 0.1500 0.2282 -0.0276 0.0343  -0.0490 19  LYS   B C   
4317 O  O   . LYS   B 19  ? 0.1795 0.1544 0.2075 -0.0191 0.0225  -0.0474 19  LYS   B O   
4318 C  CB  . LYS   B 19  ? 0.2261 0.1795 0.2285 -0.0338 0.0420  -0.0333 19  LYS   B CB  
4319 C  CG  . LYS   B 19  ? 0.2517 0.1991 0.2490 -0.0448 0.0486  -0.0327 19  LYS   B CG  
4320 C  CD  . LYS   B 19  ? 0.2796 0.2279 0.2579 -0.0493 0.0597  -0.0271 19  LYS   B CD  
4321 C  CE  . LYS   B 19  ? 0.3063 0.2551 0.2785 -0.0482 0.0597  -0.0316 19  LYS   B CE  
4322 N  NZ  . LYS   B 19  ? 0.3220 0.2707 0.2804 -0.0530 0.0649  -0.0274 19  LYS   B NZ  
4336 N  N   . ASN   B 20  ? 0.1795 0.1641 0.2636 -0.0213 0.0412  -0.0660 20  ASN   B N   
4337 C  CA  . ASN   B 20  ? 0.1853 0.1789 0.2844 -0.0155 0.0458  -0.0798 20  ASN   B CA  
4338 C  C   . ASN   B 20  ? 0.1830 0.1941 0.2846 -0.0227 0.0571  -0.0863 20  ASN   B C   
4339 O  O   . ASN   B 20  ? 0.1996 0.2293 0.3063 -0.0346 0.0534  -0.0855 20  ASN   B O   
4340 C  CB  . ASN   B 20  ? 0.2150 0.1873 0.3180 0.0086  0.0302  -0.0799 20  ASN   B CB  
4341 C  CG  . ASN   B 20  ? 0.2411 0.1973 0.3410 0.0373  0.0282  -0.0906 20  ASN   B CG  
4342 O  OD1 . ASN   B 20  ? 0.2700 0.2216 0.3726 0.0495  0.0309  -0.0946 20  ASN   B OD1 
4343 N  ND2 . ASN   B 20  ? 0.2314 0.1960 0.3366 0.0375  0.0132  -0.0836 20  ASN   B ND2 
4350 N  N   . ALA   B 21  ? 0.1824 0.1823 0.2853 -0.0256 0.0545  -0.0693 21  ALA   B N   
4351 C  CA  . ALA   B 21  ? 0.1922 0.1869 0.2922 -0.0291 0.0417  -0.0554 21  ALA   B CA  
4352 C  C   . ALA   B 21  ? 0.1956 0.1642 0.2720 -0.0201 0.0424  -0.0383 21  ALA   B C   
4353 O  O   . ALA   B 21  ? 0.1996 0.1494 0.2695 -0.0271 0.0402  -0.0348 21  ALA   B O   
4354 C  CB  . ALA   B 21  ? 0.2087 0.2098 0.2989 -0.0408 0.0441  -0.0432 21  ALA   B CB  
4360 N  N   . ASP   B 22  ? 0.1833 0.1565 0.2670 -0.0199 0.0368  -0.0317 22  ASP   B N   
4361 C  CA  . ASP   B 22  ? 0.1799 0.1503 0.2581 -0.0078 0.0262  -0.0242 22  ASP   B CA  
4362 C  C   . ASP   B 22  ? 0.1725 0.1461 0.2100 -0.0184 0.0168  -0.0135 22  ASP   B C   
4363 O  O   . ASP   B 22  ? 0.1759 0.1540 0.2103 -0.0139 0.0122  -0.0024 22  ASP   B O   
4364 C  CB  . ASP   B 22  ? 0.1879 0.1579 0.2959 -0.0022 0.0187  -0.0123 22  ASP   B CB  
4365 C  CG  . ASP   B 22  ? 0.1852 0.1729 0.3426 0.0016  0.0030  -0.0111 22  ASP   B CG  
4366 O  OD1 . ASP   B 22  ? 0.1960 0.1684 0.3393 0.0033  -0.0171 -0.0095 22  ASP   B OD1 
4367 O  OD2 . ASP   B 22  ? 0.1923 0.1992 0.4037 0.0095  -0.0108 -0.0207 22  ASP   B OD2 
4372 N  N   . ILE   B 23  ? 0.1713 0.1380 0.1809 -0.0131 0.0077  0.0152  23  ILE   B N   
4373 C  CA  . ILE   B 23  ? 0.1626 0.1356 0.1689 -0.0084 -0.0025 0.0036  23  ILE   B CA  
4374 C  C   . ILE   B 23  ? 0.1529 0.1383 0.1658 -0.0074 -0.0091 0.0004  23  ILE   B C   
4375 O  O   . ILE   B 23  ? 0.1490 0.1401 0.1597 -0.0078 -0.0037 0.0077  23  ILE   B O   
4376 C  CB  . ILE   B 23  ? 0.1593 0.1412 0.1938 -0.0191 0.0035  0.0131  23  ILE   B CB  
4377 C  CG1 . ILE   B 23  ? 0.1604 0.1455 0.2023 -0.0154 0.0122  0.0302  23  ILE   B CG1 
4378 C  CG2 . ILE   B 23  ? 0.1643 0.1619 0.1994 -0.0154 0.0033  0.0037  23  ILE   B CG2 
4379 C  CD1 . ILE   B 23  ? 0.1703 0.1570 0.2088 -0.0072 0.0101  0.0264  23  ILE   B CD1 
4391 N  N   . VAL   B 24  ? 0.1571 0.1373 0.1725 -0.0104 -0.0076 0.0006  24  VAL   B N   
4392 C  CA  . VAL   B 24  ? 0.1552 0.1490 0.1939 -0.0060 -0.0177 -0.0050 24  VAL   B CA  
4393 C  C   . VAL   B 24  ? 0.1469 0.1520 0.1997 -0.0100 -0.0101 0.0024  24  VAL   B C   
4394 O  O   . VAL   B 24  ? 0.1491 0.1550 0.2209 -0.0168 -0.0067 0.0080  24  VAL   B O   
4395 C  CB  . VAL   B 24  ? 0.1684 0.1661 0.1958 0.0009  -0.0264 -0.0080 24  VAL   B CB  
4396 C  CG1 . VAL   B 24  ? 0.1652 0.1715 0.2247 -0.0068 -0.0251 -0.0034 24  VAL   B CG1 
4397 C  CG2 . VAL   B 24  ? 0.1733 0.1911 0.1984 0.0035  -0.0232 -0.0126 24  VAL   B CG2 
4407 N  N   . GLU   B 25  ? 0.1677 0.1634 0.1969 -0.0099 0.0070  -0.0009 25  GLU   B N   
4408 C  CA  . GLU   B 25  ? 0.1800 0.1870 0.2179 -0.0018 0.0193  -0.0035 25  GLU   B CA  
4409 C  C   . GLU   B 25  ? 0.1757 0.1784 0.1978 -0.0131 0.0127  0.0040  25  GLU   B C   
4410 O  O   . GLU   B 25  ? 0.1729 0.1990 0.2123 -0.0124 0.0177  0.0126  25  GLU   B O   
4411 C  CB  . GLU   B 25  ? 0.2127 0.2338 0.2771 0.0228  0.0385  -0.0038 25  GLU   B CB  
4412 C  CG  . GLU   B 25  ? 0.2545 0.2959 0.3866 0.0294  0.0334  -0.0043 25  GLU   B CG  
4413 C  CD  . GLU   B 25  ? 0.2948 0.3513 0.4717 0.0247  0.0260  -0.0053 25  GLU   B CD  
4414 O  OE1 . GLU   B 25  ? 0.3103 0.3723 0.5006 0.0284  0.0296  -0.0030 25  GLU   B OE1 
4415 O  OE2 . GLU   B 25  ? 0.3084 0.3690 0.4992 0.0237  0.0171  -0.0115 25  GLU   B OE2 
4422 N  N   . GLU   B 26  ? 0.1775 0.1680 0.1765 -0.0255 0.0044  0.0015  26  GLU   B N   
4423 C  CA  . GLU   B 26  ? 0.1763 0.1788 0.1831 -0.0375 -0.0061 0.0053  26  GLU   B CA  
4424 C  C   . GLU   B 26  ? 0.1603 0.1783 0.1700 -0.0257 0.0022  0.0198  26  GLU   B C   
4425 O  O   . GLU   B 26  ? 0.1845 0.2019 0.1695 -0.0272 0.0021  0.0185  26  GLU   B O   
4426 C  CB  . GLU   B 26  ? 0.2065 0.1959 0.2130 -0.0439 -0.0057 0.0206  26  GLU   B CB  
4427 C  CG  . GLU   B 26  ? 0.2502 0.2348 0.2761 -0.0476 0.0056  -0.0062 26  GLU   B CG  
4428 C  CD  . GLU   B 26  ? 0.2742 0.2590 0.2858 -0.0684 0.0205  -0.0447 26  GLU   B CD  
4429 O  OE1 . GLU   B 26  ? 0.2921 0.2468 0.2920 -0.0792 0.0673  -0.0464 26  GLU   B OE1 
4430 O  OE2 . GLU   B 26  ? 0.2760 0.2946 0.3224 -0.0612 0.0117  -0.0431 26  GLU   B OE2 
4437 N  N   . ALA   B 27  ? 0.1451 0.1602 0.1707 -0.0240 0.0056  0.0174  27  ALA   B N   
4438 C  CA  . ALA   B 27  ? 0.1483 0.1623 0.1775 -0.0195 0.0024  0.0281  27  ALA   B CA  
4439 C  C   . ALA   B 27  ? 0.1496 0.1697 0.2019 -0.0176 0.0099  0.0390  27  ALA   B C   
4440 O  O   . ALA   B 27  ? 0.1636 0.1787 0.2053 0.0009  0.0154  0.0452  27  ALA   B O   
4441 C  CB  . ALA   B 27  ? 0.1634 0.1518 0.1722 -0.0148 0.0041  0.0246  27  ALA   B CB  
4447 N  N   . LYS   B 28  ? 0.1449 0.1881 0.2482 -0.0190 0.0130  0.0601  28  LYS   B N   
4448 C  CA  . LYS   B 28  ? 0.1598 0.2261 0.2710 -0.0083 0.0416  0.0886  28  LYS   B CA  
4449 C  C   . LYS   B 28  ? 0.1847 0.2435 0.2590 -0.0022 0.0570  0.0794  28  LYS   B C   
4450 O  O   . LYS   B 28  ? 0.2094 0.2488 0.2760 -0.0028 0.0584  0.0812  28  LYS   B O   
4451 C  CB  . LYS   B 28  ? 0.1775 0.2572 0.3298 -0.0012 0.0586  0.1093  28  LYS   B CB  
4452 C  CG  . LYS   B 28  ? 0.2060 0.3017 0.3769 -0.0005 0.0607  0.1191  28  LYS   B CG  
4453 C  CD  . LYS   B 28  ? 0.2545 0.3586 0.4341 0.0065  0.0739  0.1196  28  LYS   B CD  
4454 C  CE  . LYS   B 28  ? 0.2916 0.3999 0.4787 0.0160  0.0772  0.1216  28  LYS   B CE  
4455 N  NZ  . LYS   B 28  ? 0.3003 0.4136 0.4993 0.0239  0.0768  0.1268  28  LYS   B NZ  
4469 N  N   . LYS   B 29  ? 0.1980 0.2667 0.2543 0.0114  0.0642  0.0677  29  LYS   B N   
4470 C  CA  . LYS   B 29  ? 0.2408 0.2992 0.2775 0.0142  0.0639  0.0607  29  LYS   B CA  
4471 C  C   . LYS   B 29  ? 0.2375 0.3026 0.2485 0.0127  0.0494  0.0729  29  LYS   B C   
4472 O  O   . LYS   B 29  ? 0.2563 0.3236 0.2545 0.0172  0.0442  0.0769  29  LYS   B O   
4473 C  CB  . LYS   B 29  ? 0.2951 0.3317 0.3460 0.0155  0.0653  0.0442  29  LYS   B CB  
4474 C  CG  . LYS   B 29  ? 0.3426 0.3581 0.4237 0.0127  0.0682  0.0392  29  LYS   B CG  
4475 C  CD  . LYS   B 29  ? 0.3853 0.3767 0.4848 0.0098  0.0749  0.0319  29  LYS   B CD  
4476 C  CE  . LYS   B 29  ? 0.4161 0.3881 0.5254 0.0058  0.0822  0.0260  29  LYS   B CE  
4477 N  NZ  . LYS   B 29  ? 0.4285 0.3945 0.5539 0.0032  0.0848  0.0207  29  LYS   B NZ  
4491 N  N   . VAL   B 30  ? 0.2074 0.2832 0.2322 0.0004  0.0365  0.0786  30  VAL   B N   
4492 C  CA  . VAL   B 30  ? 0.1973 0.2737 0.2539 -0.0113 0.0049  0.0839  30  VAL   B CA  
4493 C  C   . VAL   B 30  ? 0.1790 0.2670 0.2425 -0.0107 0.0084  0.0991  30  VAL   B C   
4494 O  O   . VAL   B 30  ? 0.1949 0.2813 0.2491 -0.0008 0.0091  0.1119  30  VAL   B O   
4495 C  CB  . VAL   B 30  ? 0.2012 0.2693 0.3030 -0.0276 -0.0246 0.0761  30  VAL   B CB  
4496 C  CG1 . VAL   B 30  ? 0.2075 0.2753 0.3059 -0.0263 -0.0248 0.0694  30  VAL   B CG1 
4497 C  CG2 . VAL   B 30  ? 0.2118 0.2700 0.3257 -0.0380 -0.0378 0.0672  30  VAL   B CG2 
4507 N  N   . LYS   B 31  ? 0.1635 0.2354 0.2728 -0.0266 0.0075  0.1021  31  LYS   B N   
4508 C  CA  . LYS   B 31  ? 0.1536 0.2268 0.3066 -0.0359 -0.0011 0.1065  31  LYS   B CA  
4509 C  C   . LYS   B 31  ? 0.1475 0.1895 0.2618 -0.0355 -0.0294 0.0857  31  LYS   B C   
4510 O  O   . LYS   B 31  ? 0.1585 0.2041 0.2788 -0.0266 -0.0221 0.1010  31  LYS   B O   
4511 C  CB  . LYS   B 31  ? 0.1709 0.2687 0.3734 -0.0300 0.0192  0.1201  31  LYS   B CB  
4512 C  CG  . LYS   B 31  ? 0.2023 0.3099 0.4216 -0.0329 0.0360  0.1181  31  LYS   B CG  
4513 C  CD  . LYS   B 31  ? 0.2317 0.3543 0.4682 -0.0265 0.0293  0.1049  31  LYS   B CD  
4514 C  CE  . LYS   B 31  ? 0.2466 0.3833 0.5110 -0.0234 0.0159  0.0913  31  LYS   B CE  
4515 N  NZ  . LYS   B 31  ? 0.2669 0.4001 0.5267 -0.0172 0.0025  0.0800  31  LYS   B NZ  
4529 N  N   . PRO   B 32  ? 0.1619 0.1535 0.1984 -0.0352 -0.0409 0.0485  32  PRO   B N   
4530 C  CA  . PRO   B 32  ? 0.1726 0.1519 0.1564 -0.0385 -0.0425 0.0274  32  PRO   B CA  
4531 C  C   . PRO   B 32  ? 0.1851 0.1461 0.1647 -0.0396 -0.0510 0.0306  32  PRO   B C   
4532 O  O   . PRO   B 32  ? 0.1960 0.1443 0.1993 -0.0433 -0.0720 0.0325  32  PRO   B O   
4533 C  CB  . PRO   B 32  ? 0.1866 0.1468 0.1541 -0.0394 -0.0318 0.0111  32  PRO   B CB  
4534 C  CG  . PRO   B 32  ? 0.2012 0.1373 0.1601 -0.0294 -0.0499 0.0238  32  PRO   B CG  
4535 C  CD  . PRO   B 32  ? 0.1879 0.1415 0.1899 -0.0259 -0.0519 0.0240  32  PRO   B CD  
4543 N  N   . THR   B 33  ? 0.1851 0.1362 0.1601 -0.0306 -0.0506 0.0231  33  THR   B N   
4544 C  CA  . THR   B 33  ? 0.1890 0.1383 0.1583 -0.0360 -0.0461 0.0283  33  THR   B CA  
4545 C  C   . THR   B 33  ? 0.1917 0.1311 0.1508 -0.0334 -0.0476 0.0199  33  THR   B C   
4546 O  O   . THR   B 33  ? 0.2201 0.1344 0.1632 -0.0433 -0.0537 0.0158  33  THR   B O   
4547 C  CB  . THR   B 33  ? 0.2002 0.1477 0.1613 -0.0217 -0.0530 0.0275  33  THR   B CB  
4548 O  OG1 . THR   B 33  ? 0.1893 0.1542 0.1695 -0.0245 -0.0489 0.0327  33  THR   B OG1 
4549 C  CG2 . THR   B 33  ? 0.2258 0.1598 0.1767 -0.0160 -0.0451 0.0294  33  THR   B CG2 
4557 N  N   . VAL   B 34  ? 0.1734 0.1302 0.1433 -0.0360 -0.0437 0.0168  34  VAL   B N   
4558 C  CA  . VAL   B 34  ? 0.1575 0.1256 0.1339 -0.0279 -0.0365 0.0069  34  VAL   B CA  
4559 C  C   . VAL   B 34  ? 0.1466 0.1220 0.1251 -0.0298 -0.0177 0.0073  34  VAL   B C   
4560 O  O   . VAL   B 34  ? 0.1646 0.1260 0.1311 -0.0280 -0.0310 0.0042  34  VAL   B O   
4561 C  CB  . VAL   B 34  ? 0.1668 0.1357 0.1616 -0.0087 -0.0331 0.0039  34  VAL   B CB  
4562 C  CG1 . VAL   B 34  ? 0.1645 0.1482 0.1600 -0.0042 -0.0180 0.0035  34  VAL   B CG1 
4563 C  CG2 . VAL   B 34  ? 0.1753 0.1425 0.1848 -0.0097 -0.0312 0.0036  34  VAL   B CG2 
4573 N  N   . VAL   B 35  ? 0.1370 0.1198 0.1184 -0.0261 -0.0122 0.0097  35  VAL   B N   
4574 C  CA  . VAL   B 35  ? 0.1337 0.1201 0.1154 -0.0194 -0.0068 0.0057  35  VAL   B CA  
4575 C  C   . VAL   B 35  ? 0.1248 0.1142 0.1125 -0.0135 -0.0129 0.0033  35  VAL   B C   
4576 O  O   . VAL   B 35  ? 0.1306 0.1188 0.1259 -0.0211 -0.0029 -0.0045 35  VAL   B O   
4577 C  CB  . VAL   B 35  ? 0.1328 0.1342 0.1213 -0.0157 0.0079  0.0040  35  VAL   B CB  
4578 C  CG1 . VAL   B 35  ? 0.1279 0.1459 0.1546 -0.0200 -0.0001 -0.0027 35  VAL   B CG1 
4579 C  CG2 . VAL   B 35  ? 0.1376 0.1381 0.1424 -0.0084 0.0008  0.0018  35  VAL   B CG2 
4589 N  N   . VAL   B 36  ? 0.1280 0.1165 0.1149 -0.0150 -0.0138 0.0089  36  VAL   B N   
4590 C  CA  . VAL   B 36  ? 0.1248 0.1104 0.1094 -0.0140 -0.0069 0.0065  36  VAL   B CA  
4591 C  C   . VAL   B 36  ? 0.1227 0.1139 0.1015 -0.0098 -0.0002 0.0056  36  VAL   B C   
4592 O  O   . VAL   B 36  ? 0.1266 0.1251 0.1316 -0.0084 -0.0057 -0.0033 36  VAL   B O   
4593 C  CB  . VAL   B 36  ? 0.1271 0.1196 0.1176 -0.0141 -0.0074 0.0083  36  VAL   B CB  
4594 C  CG1 . VAL   B 36  ? 0.1274 0.1306 0.1287 -0.0155 -0.0055 0.0040  36  VAL   B CG1 
4595 C  CG2 . VAL   B 36  ? 0.1287 0.1237 0.1312 -0.0116 -0.0133 0.0121  36  VAL   B CG2 
4605 N  N   . ASN   B 37  ? 0.1232 0.1213 0.0984 0.0004  -0.0030 0.0023  37  ASN   B N   
4606 C  CA  . ASN   B 37  ? 0.1260 0.1224 0.1160 0.0010  -0.0074 0.0068  37  ASN   B CA  
4607 C  C   . ASN   B 37  ? 0.1231 0.1241 0.1210 0.0022  -0.0049 0.0065  37  ASN   B C   
4608 O  O   . ASN   B 37  ? 0.1327 0.1285 0.1261 0.0012  0.0014  0.0070  37  ASN   B O   
4609 C  CB  . ASN   B 37  ? 0.1237 0.1225 0.1140 -0.0044 -0.0082 0.0090  37  ASN   B CB  
4610 C  CG  . ASN   B 37  ? 0.1333 0.1229 0.1277 -0.0015 -0.0142 0.0080  37  ASN   B CG  
4611 O  OD1 . ASN   B 37  ? 0.1397 0.1273 0.1473 0.0103  -0.0170 0.0044  37  ASN   B OD1 
4612 N  ND2 . ASN   B 37  ? 0.1353 0.1219 0.1309 0.0009  -0.0182 0.0076  37  ASN   B ND2 
4619 N  N   . ALA   B 38  ? 0.1290 0.1214 0.1167 0.0078  0.0048  0.0066  38  ALA   B N   
4620 C  CA  . ALA   B 38  ? 0.1433 0.1235 0.1222 0.0020  -0.0000 0.0096  38  ALA   B CA  
4621 C  C   . ALA   B 38  ? 0.1377 0.1220 0.1196 0.0023  0.0041  0.0128  38  ALA   B C   
4622 O  O   . ALA   B 38  ? 0.1461 0.1307 0.1351 0.0063  -0.0055 0.0037  38  ALA   B O   
4623 C  CB  . ALA   B 38  ? 0.1645 0.1291 0.1377 -0.0113 0.0039  0.0099  38  ALA   B CB  
4629 N  N   . ALA   B 39  ? 0.1393 0.1222 0.1141 0.0068  -0.0062 0.0067  39  ALA   B N   
4630 C  CA  . ALA   B 39  ? 0.1452 0.1312 0.1102 0.0075  -0.0097 0.0044  39  ALA   B CA  
4631 C  C   . ALA   B 39  ? 0.1522 0.1358 0.0921 0.0138  -0.0077 0.0053  39  ALA   B C   
4632 O  O   . ALA   B 39  ? 0.1546 0.1432 0.1326 0.0032  -0.0044 0.0071  39  ALA   B O   
4633 C  CB  . ALA   B 39  ? 0.1424 0.1359 0.1358 -0.0022 -0.0026 -0.0001 39  ALA   B CB  
4639 N  N   . ASN   B 40  ? 0.1565 0.1573 0.0943 -0.0012 -0.0028 -0.0024 40  ASN   B N   
4640 C  CA  . ASN   B 40  ? 0.1599 0.1607 0.1180 0.0032  -0.0053 -0.0080 40  ASN   B CA  
4641 C  C   . ASN   B 40  ? 0.1665 0.1598 0.1117 0.0112  -0.0057 0.0019  40  ASN   B C   
4642 O  O   . ASN   B 40  ? 0.1599 0.1509 0.1188 0.0112  -0.0063 0.0003  40  ASN   B O   
4643 C  CB  . ASN   B 40  ? 0.1750 0.1613 0.1371 0.0113  -0.0125 0.0132  40  ASN   B CB  
4644 C  CG  . ASN   B 40  ? 0.1786 0.1649 0.1818 0.0061  -0.0192 0.0181  40  ASN   B CG  
4645 O  OD1 . ASN   B 40  ? 0.1765 0.1608 0.2557 0.0073  -0.0351 0.0178  40  ASN   B OD1 
4646 N  ND2 . ASN   B 40  ? 0.1805 0.1645 0.1743 0.0073  -0.0210 0.0173  40  ASN   B ND2 
4653 N  N   . VAL   B 41  ? 0.1739 0.1612 0.1135 0.0148  0.0067  0.0004  41  VAL   B N   
4654 C  CA  . VAL   B 41  ? 0.1799 0.1729 0.1156 0.0106  0.0015  -0.0069 41  VAL   B CA  
4655 C  C   . VAL   B 41  ? 0.1796 0.1718 0.1170 0.0169  -0.0059 -0.0028 41  VAL   B C   
4656 O  O   . VAL   B 41  ? 0.1790 0.1723 0.1305 0.0152  -0.0123 -0.0095 41  VAL   B O   
4657 C  CB  . VAL   B 41  ? 0.1950 0.1935 0.1485 -0.0003 0.0186  -0.0204 41  VAL   B CB  
4658 C  CG1 . VAL   B 41  ? 0.1939 0.1951 0.1623 -0.0040 0.0273  -0.0252 41  VAL   B CG1 
4659 C  CG2 . VAL   B 41  ? 0.2100 0.2122 0.1536 -0.0151 0.0107  -0.0204 41  VAL   B CG2 
4669 N  N   . TYR   B 42  ? 0.1819 0.1726 0.1200 0.0139  -0.0175 0.0041  42  TYR   B N   
4670 C  CA  . TYR   B 42  ? 0.1888 0.1820 0.1199 0.0175  -0.0230 -0.0082 42  TYR   B CA  
4671 C  C   . TYR   B 42  ? 0.1698 0.1627 0.1364 0.0204  -0.0203 -0.0076 42  TYR   B C   
4672 O  O   . TYR   B 42  ? 0.1696 0.1702 0.1676 0.0163  -0.0234 -0.0192 42  TYR   B O   
4673 C  CB  . TYR   B 42  ? 0.2124 0.2065 0.1384 0.0129  -0.0299 -0.0010 42  TYR   B CB  
4674 C  CG  . TYR   B 42  ? 0.2143 0.2173 0.1345 0.0026  -0.0319 0.0114  42  TYR   B CG  
4675 C  CD1 . TYR   B 42  ? 0.2083 0.2179 0.1186 0.0026  -0.0196 0.0027  42  TYR   B CD1 
4676 C  CD2 . TYR   B 42  ? 0.2277 0.2271 0.1746 0.0020  -0.0131 0.0168  42  TYR   B CD2 
4677 C  CE1 . TYR   B 42  ? 0.2234 0.2349 0.1300 0.0039  -0.0096 0.0026  42  TYR   B CE1 
4678 C  CE2 . TYR   B 42  ? 0.2327 0.2431 0.1804 0.0062  0.0104  0.0273  42  TYR   B CE2 
4679 C  CZ  . TYR   B 42  ? 0.2417 0.2520 0.1661 0.0199  0.0108  0.0153  42  TYR   B CZ  
4680 O  OH  . TYR   B 42  ? 0.2696 0.2763 0.2145 0.0379  0.0179  0.0224  42  TYR   B OH  
4690 N  N   . LEU   B 43  ? 0.1564 0.1463 0.1229 0.0092  -0.0117 -0.0066 43  LEU   B N   
4691 C  CA  . LEU   B 43  ? 0.1589 0.1433 0.1234 0.0047  -0.0172 -0.0042 43  LEU   B CA  
4692 C  C   . LEU   B 43  ? 0.1635 0.1451 0.1307 0.0060  -0.0160 0.0021  43  LEU   B C   
4693 O  O   . LEU   B 43  ? 0.1614 0.1496 0.1550 0.0075  -0.0243 0.0069  43  LEU   B O   
4694 C  CB  . LEU   B 43  ? 0.1529 0.1382 0.1501 0.0044  -0.0245 -0.0115 43  LEU   B CB  
4695 C  CG  . LEU   B 43  ? 0.1589 0.1386 0.1468 0.0046  -0.0237 -0.0099 43  LEU   B CG  
4696 C  CD1 . LEU   B 43  ? 0.1686 0.1467 0.1790 -0.0002 -0.0401 -0.0102 43  LEU   B CD1 
4697 C  CD2 . LEU   B 43  ? 0.1563 0.1394 0.1601 0.0044  -0.0303 -0.0086 43  LEU   B CD2 
4709 N  N   . LYS   B 44  ? 0.1623 0.1427 0.1331 0.0109  -0.0103 -0.0049 44  LYS   B N   
4710 C  CA  . LYS   B 44  ? 0.1752 0.1554 0.1316 0.0128  -0.0129 0.0052  44  LYS   B CA  
4711 C  C   . LYS   B 44  ? 0.1649 0.1489 0.1337 0.0160  -0.0164 0.0026  44  LYS   B C   
4712 O  O   . LYS   B 44  ? 0.1822 0.1477 0.1605 0.0038  -0.0088 0.0058  44  LYS   B O   
4713 C  CB  . LYS   B 44  ? 0.2046 0.1766 0.1512 0.0200  -0.0296 -0.0000 44  LYS   B CB  
4714 C  CG  . LYS   B 44  ? 0.2436 0.2035 0.1876 0.0153  -0.0602 -0.0003 44  LYS   B CG  
4715 C  CD  . LYS   B 44  ? 0.2782 0.2232 0.2566 0.0031  -0.0638 -0.0038 44  LYS   B CD  
4716 C  CE  . LYS   B 44  ? 0.3111 0.2510 0.3104 -0.0029 -0.0629 0.0109  44  LYS   B CE  
4717 N  NZ  . LYS   B 44  ? 0.3250 0.2618 0.3370 -0.0031 -0.0673 0.0322  44  LYS   B NZ  
4731 N  N   . HIS   B 45  ? 0.1564 0.1512 0.1307 0.0092  -0.0124 0.0079  45  HIS   B N   
4732 C  CA  . HIS   B 45  ? 0.1598 0.1446 0.1409 0.0131  -0.0066 0.0015  45  HIS   B CA  
4733 C  C   . HIS   B 45  ? 0.1819 0.1669 0.1776 0.0184  -0.0162 -0.0024 45  HIS   B C   
4734 O  O   . HIS   B 45  ? 0.1936 0.1991 0.2197 0.0408  0.0057  -0.0003 45  HIS   B O   
4735 C  CB  . HIS   B 45  ? 0.1525 0.1499 0.1392 0.0014  -0.0113 -0.0067 45  HIS   B CB  
4736 C  CG  . HIS   B 45  ? 0.1540 0.1463 0.1356 -0.0036 -0.0106 0.0014  45  HIS   B CG  
4737 N  ND1 . HIS   B 45  ? 0.1562 0.1382 0.1426 0.0019  -0.0204 -0.0068 45  HIS   B ND1 
4738 C  CD2 . HIS   B 45  ? 0.1681 0.1490 0.1537 -0.0078 -0.0163 0.0022  45  HIS   B CD2 
4739 C  CE1 . HIS   B 45  ? 0.1700 0.1332 0.1310 -0.0027 -0.0256 -0.0090 45  HIS   B CE1 
4740 N  NE2 . HIS   B 45  ? 0.1774 0.1370 0.1432 -0.0030 -0.0201 -0.0040 45  HIS   B NE2 
4748 N  N   A GLY   B 46  ? 0.1933 0.1663 0.2048 0.0161  -0.0361 0.0099  46  GLY   B N   
4749 N  N   B GLY   B 46  ? 0.1929 0.1730 0.1954 0.0170  -0.0293 0.0097  46  GLY   B N   
4750 C  CA  A GLY   B 46  ? 0.2059 0.1765 0.2455 0.0164  -0.0444 0.0099  46  GLY   B CA  
4751 C  CA  B GLY   B 46  ? 0.2044 0.1845 0.2229 0.0168  -0.0356 0.0154  46  GLY   B CA  
4752 C  C   A GLY   B 46  ? 0.2067 0.1867 0.2862 0.0252  -0.0427 0.0059  46  GLY   B C   
4753 C  C   B GLY   B 46  ? 0.2092 0.1959 0.2529 0.0218  -0.0344 0.0203  46  GLY   B C   
4754 O  O   A GLY   B 46  ? 0.2169 0.1963 0.3588 0.0293  -0.0264 -0.0215 46  GLY   B O   
4755 O  O   B GLY   B 46  ? 0.2194 0.2062 0.2704 0.0279  -0.0306 0.0327  46  GLY   B O   
4762 N  N   . GLY   B 47  ? 0.2067 0.1998 0.2652 0.0091  -0.0240 0.0029  47  GLY   B N   
4763 C  CA  . GLY   B 47  ? 0.1916 0.1729 0.2224 0.0037  -0.0167 0.0013  47  GLY   B CA  
4764 C  C   . GLY   B 47  ? 0.1706 0.1492 0.1854 0.0032  -0.0028 0.0059  47  GLY   B C   
4765 O  O   . GLY   B 47  ? 0.1839 0.1352 0.1963 0.0040  -0.0077 0.0091  47  GLY   B O   
4770 N  N   . GLY   B 48  ? 0.1536 0.1427 0.1788 0.0037  -0.0139 0.0185  48  GLY   B N   
4771 C  CA  . GLY   B 48  ? 0.1493 0.1411 0.1792 0.0022  -0.0051 0.0058  48  GLY   B CA  
4772 C  C   . GLY   B 48  ? 0.1439 0.1378 0.1666 0.0060  0.0005  0.0040  48  GLY   B C   
4773 O  O   . GLY   B 48  ? 0.1372 0.1422 0.1896 0.0074  -0.0095 0.0019  48  GLY   B O   
4777 N  N   . VAL   B 49  ? 0.1472 0.1416 0.1604 0.0116  -0.0003 0.0077  49  VAL   B N   
4778 C  CA  . VAL   B 49  ? 0.1470 0.1457 0.1536 0.0102  -0.0118 -0.0061 49  VAL   B CA  
4779 C  C   . VAL   B 49  ? 0.1374 0.1358 0.1378 0.0119  -0.0067 0.0019  49  VAL   B C   
4780 O  O   . VAL   B 49  ? 0.1442 0.1408 0.1542 0.0059  0.0008  0.0058  49  VAL   B O   
4781 C  CB  . VAL   B 49  ? 0.1456 0.1613 0.1830 0.0018  -0.0234 -0.0028 49  VAL   B CB  
4782 C  CG1 . VAL   B 49  ? 0.1471 0.1674 0.1770 0.0073  -0.0287 -0.0080 49  VAL   B CG1 
4783 C  CG2 . VAL   B 49  ? 0.1628 0.1757 0.2089 -0.0100 -0.0361 -0.0064 49  VAL   B CG2 
4793 N  N   . ALA   B 50  ? 0.1321 0.1324 0.1411 0.0060  -0.0028 0.0024  50  ALA   B N   
4794 C  CA  . ALA   B 50  ? 0.1345 0.1283 0.1368 0.0046  -0.0076 -0.0016 50  ALA   B CA  
4795 C  C   . ALA   B 50  ? 0.1400 0.1306 0.1346 0.0026  -0.0079 0.0026  50  ALA   B C   
4796 O  O   . ALA   B 50  ? 0.1408 0.1321 0.1405 0.0032  -0.0045 0.0012  50  ALA   B O   
4797 C  CB  . ALA   B 50  ? 0.1410 0.1270 0.1448 0.0011  -0.0068 0.0112  50  ALA   B CB  
4803 N  N   . GLY   B 51  ? 0.1393 0.1431 0.1416 0.0104  -0.0150 0.0119  51  GLY   B N   
4804 C  CA  . GLY   B 51  ? 0.1391 0.1486 0.1594 0.0177  -0.0184 0.0058  51  GLY   B CA  
4805 C  C   . GLY   B 51  ? 0.1351 0.1466 0.1642 0.0195  -0.0115 0.0030  51  GLY   B C   
4806 O  O   . GLY   B 51  ? 0.1392 0.1578 0.1910 0.0111  -0.0144 -0.0020 51  GLY   B O   
4810 N  N   . ALA   B 52  ? 0.1344 0.1418 0.1541 0.0182  -0.0092 0.0027  52  ALA   B N   
4811 C  CA  . ALA   B 52  ? 0.1466 0.1460 0.1557 0.0171  0.0018  -0.0046 52  ALA   B CA  
4812 C  C   . ALA   B 52  ? 0.1360 0.1426 0.1507 0.0081  -0.0032 0.0020  52  ALA   B C   
4813 O  O   . ALA   B 52  ? 0.1384 0.1493 0.1688 0.0129  0.0046  0.0001  52  ALA   B O   
4814 C  CB  . ALA   B 52  ? 0.1655 0.1507 0.1704 0.0104  0.0073  -0.0054 52  ALA   B CB  
4820 N  N   . LEU   B 53  ? 0.1289 0.1404 0.1473 0.0153  -0.0021 0.0043  53  LEU   B N   
4821 C  CA  . LEU   B 53  ? 0.1292 0.1479 0.1453 0.0112  -0.0038 0.0048  53  LEU   B CA  
4822 C  C   . LEU   B 53  ? 0.1383 0.1433 0.1389 0.0089  0.0051  0.0070  53  LEU   B C   
4823 O  O   . LEU   B 53  ? 0.1447 0.1494 0.1517 0.0003  0.0049  0.0112  53  LEU   B O   
4824 C  CB  . LEU   B 53  ? 0.1324 0.1543 0.1581 0.0071  -0.0057 0.0159  53  LEU   B CB  
4825 C  CG  . LEU   B 53  ? 0.1326 0.1616 0.1546 0.0014  -0.0043 0.0209  53  LEU   B CG  
4826 C  CD1 . LEU   B 53  ? 0.1400 0.1792 0.1766 0.0095  -0.0028 0.0027  53  LEU   B CD1 
4827 C  CD2 . LEU   B 53  ? 0.1516 0.1968 0.1876 -0.0067 -0.0110 -0.0091 53  LEU   B CD2 
4839 N  N   . ASN   B 54  ? 0.1378 0.1350 0.1344 0.0060  -0.0040 0.0091  54  ASN   B N   
4840 C  CA  . ASN   B 54  ? 0.1412 0.1458 0.1436 0.0054  -0.0125 -0.0008 54  ASN   B CA  
4841 C  C   . ASN   B 54  ? 0.1387 0.1463 0.1661 0.0013  -0.0018 0.0015  54  ASN   B C   
4842 O  O   . ASN   B 54  ? 0.1297 0.1516 0.1746 -0.0002 0.0048  -0.0026 54  ASN   B O   
4843 C  CB  . ASN   B 54  ? 0.1453 0.1623 0.1578 0.0044  -0.0016 -0.0017 54  ASN   B CB  
4844 C  CG  . ASN   B 54  ? 0.1446 0.1648 0.1568 0.0035  -0.0108 -0.0032 54  ASN   B CG  
4845 O  OD1 . ASN   B 54  ? 0.1395 0.1580 0.1788 0.0019  -0.0105 -0.0177 54  ASN   B OD1 
4846 N  ND2 . ASN   B 54  ? 0.1618 0.1881 0.1814 -0.0005 -0.0304 0.0066  54  ASN   B ND2 
4853 N  N   . LYS   B 55  ? 0.1328 0.1528 0.1866 0.0089  -0.0054 0.0034  55  LYS   B N   
4854 C  CA  . LYS   B 55  ? 0.1394 0.1658 0.2092 0.0149  -0.0068 0.0022  55  LYS   B CA  
4855 C  C   . LYS   B 55  ? 0.1386 0.1621 0.2011 0.0094  0.0049  -0.0050 55  LYS   B C   
4856 O  O   . LYS   B 55  ? 0.1331 0.1747 0.2172 0.0143  0.0076  -0.0069 55  LYS   B O   
4857 C  CB  . LYS   B 55  ? 0.1525 0.1767 0.2585 0.0263  0.0028  0.0107  55  LYS   B CB  
4858 C  CG  . LYS   B 55  ? 0.1943 0.1996 0.3420 0.0300  0.0195  0.0241  55  LYS   B CG  
4859 C  CD  . LYS   B 55  ? 0.2344 0.2202 0.4132 0.0356  0.0335  0.0302  55  LYS   B CD  
4860 C  CE  . LYS   B 55  ? 0.2641 0.2387 0.4801 0.0328  0.0474  0.0306  55  LYS   B CE  
4861 N  NZ  . LYS   B 55  ? 0.2717 0.2495 0.5138 0.0289  0.0374  0.0348  55  LYS   B NZ  
4875 N  N   . ALA   B 56  ? 0.1366 0.1671 0.1811 0.0090  0.0042  -0.0077 56  ALA   B N   
4876 C  CA  . ALA   B 56  ? 0.1510 0.1832 0.1769 0.0063  0.0009  -0.0076 56  ALA   B CA  
4877 C  C   . ALA   B 56  ? 0.1483 0.1793 0.1718 0.0009  0.0094  -0.0008 56  ALA   B C   
4878 O  O   . ALA   B 56  ? 0.1585 0.1891 0.1893 0.0053  0.0276  0.0082  56  ALA   B O   
4879 C  CB  . ALA   B 56  ? 0.1635 0.2004 0.1817 -0.0086 0.0034  -0.0057 56  ALA   B CB  
4885 N  N   . THR   B 57  ? 0.1423 0.1676 0.1714 -0.0010 0.0186  -0.0009 57  THR   B N   
4886 C  CA  . THR   B 57  ? 0.1478 0.1687 0.1731 -0.0012 0.0171  0.0062  57  THR   B CA  
4887 C  C   . THR   B 57  ? 0.1515 0.1786 0.1981 -0.0008 0.0228  0.0019  57  THR   B C   
4888 O  O   . THR   B 57  ? 0.1597 0.1779 0.2028 -0.0208 0.0220  0.0001  57  THR   B O   
4889 C  CB  . THR   B 57  ? 0.1550 0.1534 0.1526 -0.0013 0.0147  0.0139  57  THR   B CB  
4890 O  OG1 . THR   B 57  ? 0.1536 0.1497 0.1730 -0.0051 0.0163  0.0053  57  THR   B OG1 
4891 C  CG2 . THR   B 57  ? 0.1490 0.1587 0.1599 -0.0075 0.0071  0.0085  57  THR   B CG2 
4899 N  N   . ASN   B 58  ? 0.1380 0.1919 0.2170 -0.0078 0.0067  -0.0105 58  ASN   B N   
4900 C  CA  . ASN   B 58  ? 0.1496 0.2232 0.2650 -0.0197 0.0262  -0.0058 58  ASN   B CA  
4901 C  C   . ASN   B 58  ? 0.1396 0.2108 0.2314 -0.0147 0.0000  -0.0040 58  ASN   B C   
4902 O  O   . ASN   B 58  ? 0.1468 0.2215 0.2398 -0.0165 0.0023  -0.0126 58  ASN   B O   
4903 C  CB  . ASN   B 58  ? 0.2120 0.2727 0.3755 -0.0323 0.0599  -0.0013 58  ASN   B CB  
4904 C  CG  . ASN   B 58  ? 0.2936 0.3259 0.5136 -0.0348 0.0744  0.0221  58  ASN   B CG  
4905 O  OD1 . ASN   B 58  ? 0.3177 0.3455 0.5713 -0.0348 0.0744  0.0288  58  ASN   B OD1 
4906 N  ND2 . ASN   B 58  ? 0.3425 0.3437 0.5552 -0.0390 0.0827  0.0288  58  ASN   B ND2 
4913 N  N   . ASN   B 59  ? 0.1379 0.1988 0.2029 -0.0075 -0.0023 -0.0001 59  ASN   B N   
4914 C  CA  . ASN   B 59  ? 0.1458 0.1991 0.1908 -0.0128 -0.0112 0.0138  59  ASN   B CA  
4915 C  C   . ASN   B 59  ? 0.1382 0.1906 0.1836 -0.0141 -0.0095 -0.0014 59  ASN   B C   
4916 O  O   . ASN   B 59  ? 0.1416 0.1940 0.1867 -0.0172 -0.0133 -0.0026 59  ASN   B O   
4917 C  CB  . ASN   B 59  ? 0.1542 0.2172 0.2102 -0.0085 -0.0235 0.0137  59  ASN   B CB  
4918 C  CG  . ASN   B 59  ? 0.1626 0.2299 0.2323 -0.0031 -0.0388 0.0062  59  ASN   B CG  
4919 O  OD1 . ASN   B 59  ? 0.1678 0.2337 0.2361 -0.0021 -0.0251 0.0212  59  ASN   B OD1 
4920 N  ND2 . ASN   B 59  ? 0.1653 0.2432 0.2460 -0.0084 -0.0452 -0.0013 59  ASN   B ND2 
4927 N  N   . ALA   B 60  ? 0.1395 0.1773 0.1857 -0.0186 -0.0012 -0.0058 60  ALA   B N   
4928 C  CA  . ALA   B 60  ? 0.1506 0.1659 0.1807 -0.0206 -0.0039 0.0005  60  ALA   B CA  
4929 C  C   . ALA   B 60  ? 0.1504 0.1530 0.1679 -0.0161 -0.0044 0.0050  60  ALA   B C   
4930 O  O   . ALA   B 60  ? 0.1509 0.1575 0.1821 -0.0198 -0.0001 -0.0101 60  ALA   B O   
4931 C  CB  . ALA   B 60  ? 0.1609 0.1638 0.1974 -0.0140 -0.0015 -0.0005 60  ALA   B CB  
4937 N  N   . MET   B 61  ? 0.1416 0.1433 0.1636 -0.0125 -0.0001 0.0049  61  MET   B N   
4938 C  CA  . MET   B 61  ? 0.1362 0.1404 0.1525 -0.0079 -0.0109 -0.0012 61  MET   B CA  
4939 C  C   . MET   B 61  ? 0.1466 0.1383 0.1590 -0.0122 -0.0113 0.0045  61  MET   B C   
4940 O  O   . MET   B 61  ? 0.1458 0.1380 0.1528 -0.0044 -0.0036 -0.0076 61  MET   B O   
4941 C  CB  . MET   B 61  ? 0.1308 0.1445 0.1514 0.0013  -0.0046 0.0004  61  MET   B CB  
4942 C  CG  . MET   B 61  ? 0.1342 0.1456 0.1508 0.0024  -0.0016 0.0020  61  MET   B CG  
4943 S  SD  . MET   B 61  ? 0.1356 0.1448 0.1666 -0.0015 -0.0082 -0.0079 61  MET   B SD  
4944 C  CE  . MET   B 61  ? 0.1453 0.1672 0.1916 0.0021  -0.0029 -0.0196 61  MET   B CE  
4954 N  N   . GLN   B 62  ? 0.1444 0.1478 0.1472 -0.0032 -0.0225 0.0058  62  GLN   B N   
4955 C  CA  . GLN   B 62  ? 0.1452 0.1524 0.1483 -0.0005 -0.0191 -0.0076 62  GLN   B CA  
4956 C  C   . GLN   B 62  ? 0.1414 0.1590 0.1620 -0.0009 -0.0262 -0.0070 62  GLN   B C   
4957 O  O   . GLN   B 62  ? 0.1537 0.1591 0.1643 -0.0009 -0.0292 -0.0136 62  GLN   B O   
4958 C  CB  . GLN   B 62  ? 0.1501 0.1549 0.1588 0.0035  -0.0122 0.0010  62  GLN   B CB  
4959 C  CG  . GLN   B 62  ? 0.1529 0.1569 0.1636 0.0021  -0.0269 -0.0031 62  GLN   B CG  
4960 C  CD  . GLN   B 62  ? 0.1528 0.1539 0.1562 0.0061  -0.0267 0.0051  62  GLN   B CD  
4961 O  OE1 . GLN   B 62  ? 0.1543 0.1509 0.1736 0.0007  -0.0285 -0.0054 62  GLN   B OE1 
4962 N  NE2 . GLN   B 62  ? 0.1517 0.1611 0.1612 0.0039  -0.0186 -0.0092 62  GLN   B NE2 
4971 N  N   . VAL   B 63  ? 0.1429 0.1635 0.1828 -0.0072 -0.0285 -0.0148 63  VAL   B N   
4972 C  CA  . VAL   B 63  ? 0.1565 0.1617 0.1968 -0.0127 -0.0309 -0.0116 63  VAL   B CA  
4973 C  C   . VAL   B 63  ? 0.1605 0.1499 0.1772 -0.0175 -0.0335 -0.0152 63  VAL   B C   
4974 O  O   . VAL   B 63  ? 0.1717 0.1513 0.1946 -0.0132 -0.0446 -0.0169 63  VAL   B O   
4975 C  CB  . VAL   B 63  ? 0.1568 0.1813 0.2347 -0.0186 -0.0318 -0.0146 63  VAL   B CB  
4976 C  CG1 . VAL   B 63  ? 0.1629 0.1853 0.2456 -0.0264 -0.0215 -0.0235 63  VAL   B CG1 
4977 C  CG2 . VAL   B 63  ? 0.1460 0.1967 0.2366 -0.0108 -0.0350 -0.0149 63  VAL   B CG2 
4987 N  N   . GLU   B 64  ? 0.1570 0.1456 0.1708 -0.0078 -0.0266 -0.0141 64  GLU   B N   
4988 C  CA  . GLU   B 64  ? 0.1582 0.1379 0.1651 -0.0073 -0.0278 -0.0068 64  GLU   B CA  
4989 C  C   . GLU   B 64  ? 0.1521 0.1383 0.1554 -0.0055 -0.0289 -0.0153 64  GLU   B C   
4990 O  O   . GLU   B 64  ? 0.1641 0.1483 0.1530 -0.0091 -0.0243 -0.0130 64  GLU   B O   
4991 C  CB  . GLU   B 64  ? 0.1590 0.1476 0.1630 -0.0138 -0.0210 -0.0045 64  GLU   B CB  
4992 C  CG  . GLU   B 64  ? 0.1637 0.1540 0.1639 -0.0249 -0.0240 -0.0157 64  GLU   B CG  
4993 C  CD  . GLU   B 64  ? 0.1662 0.1653 0.1611 -0.0326 -0.0304 -0.0083 64  GLU   B CD  
4994 O  OE1 . GLU   B 64  ? 0.1715 0.1754 0.1751 -0.0312 -0.0241 -0.0252 64  GLU   B OE1 
4995 O  OE2 . GLU   B 64  ? 0.1784 0.1768 0.1759 -0.0338 -0.0382 -0.0067 64  GLU   B OE2 
5002 N  N   . SER   B 65  ? 0.1507 0.1385 0.1409 -0.0058 -0.0177 -0.0189 65  SER   B N   
5003 C  CA  . SER   B 65  ? 0.1515 0.1377 0.1444 0.0011  -0.0200 -0.0116 65  SER   B CA  
5004 C  C   . SER   B 65  ? 0.1574 0.1384 0.1508 0.0061  -0.0218 -0.0149 65  SER   B C   
5005 O  O   . SER   B 65  ? 0.1615 0.1452 0.1508 0.0023  -0.0243 -0.0214 65  SER   B O   
5006 C  CB  . SER   B 65  ? 0.1525 0.1478 0.1452 -0.0077 -0.0139 -0.0086 65  SER   B CB  
5007 O  OG  . SER   B 65  ? 0.1539 0.1438 0.1474 -0.0075 -0.0168 -0.0131 65  SER   B OG  
5013 N  N   . ASP   B 66  ? 0.1653 0.1475 0.1432 -0.0017 -0.0265 -0.0142 66  ASP   B N   
5014 C  CA  . ASP   B 66  ? 0.1721 0.1553 0.1402 0.0018  -0.0327 -0.0109 66  ASP   B CA  
5015 C  C   . ASP   B 66  ? 0.1788 0.1583 0.1410 -0.0036 -0.0275 -0.0122 66  ASP   B C   
5016 O  O   . ASP   B 66  ? 0.1850 0.1623 0.1535 0.0042  -0.0264 -0.0233 66  ASP   B O   
5017 C  CB  . ASP   B 66  ? 0.1838 0.1692 0.1619 0.0137  -0.0448 -0.0160 66  ASP   B CB  
5018 C  CG  . ASP   B 66  ? 0.2135 0.1810 0.1951 0.0216  -0.0610 -0.0119 66  ASP   B CG  
5019 O  OD1 . ASP   B 66  ? 0.2360 0.1734 0.2054 0.0140  -0.0607 -0.0077 66  ASP   B OD1 
5020 O  OD2 . ASP   B 66  ? 0.2311 0.2042 0.2547 0.0382  -0.0601 -0.0130 66  ASP   B OD2 
5025 N  N   . ASP   B 67  ? 0.1687 0.1545 0.1355 -0.0053 -0.0293 -0.0206 67  ASP   B N   
5026 C  CA  . ASP   B 67  ? 0.1854 0.1475 0.1438 -0.0052 -0.0317 -0.0112 67  ASP   B CA  
5027 C  C   . ASP   B 67  ? 0.1783 0.1497 0.1620 0.0043  -0.0283 -0.0148 67  ASP   B C   
5028 O  O   . ASP   B 67  ? 0.1832 0.1565 0.1818 0.0010  -0.0216 -0.0265 67  ASP   B O   
5029 C  CB  . ASP   B 67  ? 0.2090 0.1558 0.1665 -0.0158 -0.0386 -0.0087 67  ASP   B CB  
5030 C  CG  . ASP   B 67  ? 0.2474 0.1613 0.1759 -0.0138 -0.0662 -0.0111 67  ASP   B CG  
5031 O  OD1 . ASP   B 67  ? 0.2674 0.1645 0.1953 -0.0163 -0.0651 -0.0124 67  ASP   B OD1 
5032 O  OD2 . ASP   B 67  ? 0.2620 0.1648 0.1919 0.0010  -0.0737 -0.0040 67  ASP   B OD2 
5037 N  N   . TYR   B 68  ? 0.1695 0.1488 0.1559 0.0049  -0.0365 -0.0255 68  TYR   B N   
5038 C  CA  . TYR   B 68  ? 0.1664 0.1601 0.1681 0.0104  -0.0401 -0.0320 68  TYR   B CA  
5039 C  C   . TYR   B 68  ? 0.1587 0.1585 0.1669 0.0078  -0.0399 -0.0395 68  TYR   B C   
5040 O  O   . TYR   B 68  ? 0.1661 0.1662 0.1835 0.0093  -0.0334 -0.0480 68  TYR   B O   
5041 C  CB  . TYR   B 68  ? 0.1719 0.1832 0.1722 0.0133  -0.0427 -0.0362 68  TYR   B CB  
5042 C  CG  . TYR   B 68  ? 0.1838 0.2008 0.1713 0.0143  -0.0375 -0.0562 68  TYR   B CG  
5043 C  CD1 . TYR   B 68  ? 0.1885 0.2038 0.1987 -0.0033 -0.0350 -0.0630 68  TYR   B CD1 
5044 C  CD2 . TYR   B 68  ? 0.1867 0.2187 0.1883 0.0181  -0.0548 -0.0487 68  TYR   B CD2 
5045 C  CE1 . TYR   B 68  ? 0.1939 0.2165 0.2148 -0.0022 -0.0312 -0.0591 68  TYR   B CE1 
5046 C  CE2 . TYR   B 68  ? 0.1910 0.2233 0.1957 0.0201  -0.0404 -0.0543 68  TYR   B CE2 
5047 C  CZ  . TYR   B 68  ? 0.1879 0.2222 0.2111 0.0046  -0.0353 -0.0632 68  TYR   B CZ  
5048 O  OH  . TYR   B 68  ? 0.1846 0.2429 0.2492 0.0021  -0.0277 -0.0408 68  TYR   B OH  
5058 N  N   . ILE   B 69  ? 0.1620 0.1507 0.1643 0.0092  -0.0333 -0.0329 69  ILE   B N   
5059 C  CA  . ILE   B 69  ? 0.1755 0.1567 0.1737 0.0027  -0.0192 -0.0329 69  ILE   B CA  
5060 C  C   . ILE   B 69  ? 0.1697 0.1568 0.1629 0.0066  -0.0291 -0.0301 69  ILE   B C   
5061 O  O   . ILE   B 69  ? 0.1762 0.1637 0.1607 0.0039  -0.0192 -0.0316 69  ILE   B O   
5062 C  CB  . ILE   B 69  ? 0.1830 0.1588 0.1868 0.0018  -0.0080 -0.0300 69  ILE   B CB  
5063 C  CG1 . ILE   B 69  ? 0.1790 0.1661 0.2026 -0.0023 -0.0004 -0.0269 69  ILE   B CG1 
5064 C  CG2 . ILE   B 69  ? 0.1956 0.1691 0.1991 0.0036  -0.0066 -0.0232 69  ILE   B CG2 
5065 C  CD1 . ILE   B 69  ? 0.1716 0.1715 0.2054 -0.0158 0.0026  -0.0282 69  ILE   B CD1 
5077 N  N   . ALA   B 70  ? 0.1643 0.1613 0.1696 0.0069  -0.0312 -0.0295 70  ALA   B N   
5078 C  CA  . ALA   B 70  ? 0.1678 0.1608 0.1591 0.0062  -0.0379 -0.0265 70  ALA   B CA  
5079 C  C   . ALA   B 70  ? 0.1767 0.1585 0.1660 0.0027  -0.0407 -0.0387 70  ALA   B C   
5080 O  O   . ALA   B 70  ? 0.1816 0.1594 0.1815 0.0054  -0.0355 -0.0395 70  ALA   B O   
5081 C  CB  . ALA   B 70  ? 0.1708 0.1765 0.1653 0.0028  -0.0345 -0.0310 70  ALA   B CB  
5087 N  N   . THR   B 71  ? 0.1854 0.1594 0.1733 0.0060  -0.0489 -0.0327 71  THR   B N   
5088 C  CA  . THR   B 71  ? 0.1947 0.1636 0.2020 0.0106  -0.0621 -0.0313 71  THR   B CA  
5089 C  C   . THR   B 71  ? 0.1893 0.1702 0.2250 0.0297  -0.0626 -0.0492 71  THR   B C   
5090 O  O   . THR   B 71  ? 0.1997 0.1772 0.2590 0.0345  -0.0573 -0.0629 71  THR   B O   
5091 C  CB  . THR   B 71  ? 0.2199 0.1813 0.2259 -0.0017 -0.0725 -0.0121 71  THR   B CB  
5092 O  OG1 . THR   B 71  ? 0.2359 0.2080 0.2619 -0.0237 -0.0719 0.0158  71  THR   B OG1 
5093 C  CG2 . THR   B 71  ? 0.2395 0.1790 0.2585 0.0007  -0.0584 -0.0032 71  THR   B CG2 
5101 N  N   . ASN   B 72  ? 0.1746 0.1763 0.2229 0.0222  -0.0641 -0.0690 72  ASN   B N   
5102 C  CA  . ASN   B 72  ? 0.1788 0.1887 0.2232 0.0245  -0.0492 -0.0730 72  ASN   B CA  
5103 C  C   . ASN   B 72  ? 0.1789 0.2017 0.2250 0.0092  -0.0321 -0.0701 72  ASN   B C   
5104 O  O   . ASN   B 72  ? 0.1814 0.2173 0.2551 0.0100  -0.0193 -0.0749 72  ASN   B O   
5105 C  CB  . ASN   B 72  ? 0.1871 0.2028 0.2391 0.0206  -0.0595 -0.0631 72  ASN   B CB  
5106 C  CG  . ASN   B 72  ? 0.2029 0.2168 0.2459 0.0349  -0.0675 -0.0457 72  ASN   B CG  
5107 O  OD1 . ASN   B 72  ? 0.2245 0.2319 0.2545 0.0251  -0.0524 -0.0493 72  ASN   B OD1 
5108 N  ND2 . ASN   B 72  ? 0.2130 0.2231 0.2813 0.0513  -0.0533 -0.0137 72  ASN   B ND2 
5115 N  N   . GLY   B 73  ? 0.1834 0.2005 0.1979 0.0012  -0.0380 -0.0636 73  GLY   B N   
5116 C  CA  . GLY   B 73  ? 0.1784 0.2052 0.1730 -0.0001 -0.0309 -0.0523 73  GLY   B CA  
5117 C  C   . GLY   B 73  ? 0.1758 0.2025 0.1326 0.0084  -0.0329 -0.0476 73  GLY   B C   
5118 O  O   . GLY   B 73  ? 0.1658 0.1865 0.1493 0.0083  -0.0239 -0.0356 73  GLY   B O   
5122 N  N   . PRO   B 74  ? 0.1797 0.2127 0.1339 0.0070  -0.0269 -0.0353 74  PRO   B N   
5123 C  CA  . PRO   B 74  ? 0.1725 0.2107 0.1210 0.0103  -0.0212 -0.0191 74  PRO   B CA  
5124 C  C   . PRO   B 74  ? 0.1565 0.1985 0.1287 0.0106  -0.0188 -0.0138 74  PRO   B C   
5125 O  O   . PRO   B 74  ? 0.1600 0.2002 0.1738 0.0141  -0.0111 -0.0280 74  PRO   B O   
5126 C  CB  . PRO   B 74  ? 0.1843 0.2268 0.1280 0.0046  -0.0159 -0.0114 74  PRO   B CB  
5127 C  CG  . PRO   B 74  ? 0.2027 0.2401 0.1530 0.0054  -0.0132 -0.0113 74  PRO   B CG  
5128 C  CD  . PRO   B 74  ? 0.2021 0.2298 0.1492 0.0096  -0.0130 -0.0250 74  PRO   B CD  
5136 N  N   . LEU   B 75  ? 0.1537 0.1830 0.1220 0.0088  -0.0223 -0.0177 75  LEU   B N   
5137 C  CA  . LEU   B 75  ? 0.1611 0.1822 0.1194 0.0044  -0.0211 -0.0030 75  LEU   B CA  
5138 C  C   . LEU   B 75  ? 0.1623 0.1943 0.1262 0.0096  -0.0053 -0.0053 75  LEU   B C   
5139 O  O   . LEU   B 75  ? 0.1829 0.2031 0.1364 0.0041  -0.0035 0.0015  75  LEU   B O   
5140 C  CB  . LEU   B 75  ? 0.1669 0.1834 0.1106 -0.0061 -0.0260 0.0132  75  LEU   B CB  
5141 C  CG  . LEU   B 75  ? 0.1984 0.1967 0.1346 -0.0228 -0.0087 0.0037  75  LEU   B CG  
5142 C  CD1 . LEU   B 75  ? 0.2272 0.2130 0.1424 -0.0323 0.0102  -0.0015 75  LEU   B CD1 
5143 C  CD2 . LEU   B 75  ? 0.2332 0.2146 0.2032 -0.0155 0.0095  0.0086  75  LEU   B CD2 
5155 N  N   . LYS   B 76  ? 0.1617 0.2116 0.1456 0.0082  0.0001  0.0017  76  LYS   B N   
5156 C  CA  . LYS   B 76  ? 0.1779 0.2187 0.1754 -0.0019 0.0176  -0.0006 76  LYS   B CA  
5157 C  C   . LYS   B 76  ? 0.1683 0.2036 0.1434 0.0059  0.0079  0.0186  76  LYS   B C   
5158 O  O   . LYS   B 76  ? 0.1696 0.1880 0.1539 0.0055  0.0105  0.0154  76  LYS   B O   
5159 C  CB  . LYS   B 76  ? 0.1913 0.2291 0.2303 -0.0118 0.0350  -0.0280 76  LYS   B CB  
5160 C  CG  . LYS   B 76  ? 0.1964 0.2497 0.2756 0.0034  0.0298  -0.0415 76  LYS   B CG  
5161 C  CD  . LYS   B 76  ? 0.1952 0.2586 0.3193 0.0100  0.0215  -0.0606 76  LYS   B CD  
5162 C  CE  . LYS   B 76  ? 0.1988 0.2750 0.3777 0.0069  0.0018  -0.0695 76  LYS   B CE  
5163 N  NZ  . LYS   B 76  ? 0.1976 0.2817 0.3976 0.0042  -0.0182 -0.0887 76  LYS   B NZ  
5177 N  N   . VAL   B 77  ? 0.1756 0.2154 0.1593 0.0115  0.0107  0.0291  77  VAL   B N   
5178 C  CA  . VAL   B 77  ? 0.1728 0.2058 0.1675 0.0195  0.0138  0.0507  77  VAL   B CA  
5179 C  C   . VAL   B 77  ? 0.1600 0.1841 0.1568 0.0209  0.0211  0.0371  77  VAL   B C   
5180 O  O   . VAL   B 77  ? 0.1641 0.1773 0.1655 0.0245  0.0268  0.0314  77  VAL   B O   
5181 C  CB  . VAL   B 77  ? 0.1843 0.2161 0.2050 0.0187  0.0251  0.0638  77  VAL   B CB  
5182 C  CG1 . VAL   B 77  ? 0.1845 0.2087 0.2300 0.0105  0.0333  0.0793  77  VAL   B CG1 
5183 C  CG2 . VAL   B 77  ? 0.1966 0.2323 0.2244 0.0143  0.0080  0.0669  77  VAL   B CG2 
5193 N  N   . GLY   B 78  ? 0.1549 0.1695 0.1527 0.0144  0.0198  0.0315  78  GLY   B N   
5194 C  CA  . GLY   B 78  ? 0.1568 0.1635 0.1492 0.0125  0.0262  0.0229  78  GLY   B CA  
5195 C  C   . GLY   B 78  ? 0.1457 0.1551 0.1460 0.0115  0.0202  0.0217  78  GLY   B C   
5196 O  O   . GLY   B 78  ? 0.1461 0.1542 0.1611 0.0171  0.0143  0.0215  78  GLY   B O   
5200 N  N   . GLY   B 79  ? 0.1455 0.1624 0.1447 0.0133  0.0127  0.0135  79  GLY   B N   
5201 C  CA  . GLY   B 79  ? 0.1462 0.1540 0.1373 0.0104  0.0025  0.0094  79  GLY   B CA  
5202 C  C   . GLY   B 79  ? 0.1357 0.1442 0.1423 0.0089  0.0101  0.0069  79  GLY   B C   
5203 O  O   . GLY   B 79  ? 0.1449 0.1437 0.1482 0.0124  0.0180  0.0152  79  GLY   B O   
5207 N  N   . SER   B 80  ? 0.1364 0.1349 0.1539 0.0069  0.0177  0.0057  80  SER   B N   
5208 C  CA  . SER   B 80  ? 0.1325 0.1368 0.1451 0.0042  0.0025  0.0096  80  SER   B CA  
5209 C  C   . SER   B 80  ? 0.1349 0.1331 0.1417 0.0111  -0.0066 0.0045  80  SER   B C   
5210 O  O   . SER   B 80  ? 0.1433 0.1350 0.1746 0.0113  0.0001  -0.0017 80  SER   B O   
5211 C  CB  . SER   B 80  ? 0.1363 0.1397 0.1486 -0.0039 0.0055  0.0105  80  SER   B CB  
5212 O  OG  . SER   B 80  ? 0.1432 0.1533 0.1707 0.0012  -0.0106 0.0111  80  SER   B OG  
5218 N  N   . CYS   B 81  ? 0.1331 0.1224 0.1455 0.0031  -0.0071 -0.0025 81  CYS   B N   
5219 C  CA  . CYS   B 81  ? 0.1410 0.1244 0.1453 0.0055  -0.0099 -0.0054 81  CYS   B CA  
5220 C  C   . CYS   B 81  ? 0.1354 0.1170 0.1314 -0.0003 -0.0143 -0.0005 81  CYS   B C   
5221 O  O   . CYS   B 81  ? 0.1556 0.1209 0.1436 0.0072  0.0001  -0.0042 81  CYS   B O   
5222 C  CB  . CYS   B 81  ? 0.1568 0.1355 0.1490 -0.0018 -0.0148 -0.0071 81  CYS   B CB  
5223 S  SG  . CYS   B 81  ? 0.1555 0.1511 0.1460 -0.0031 -0.0237 -0.0110 81  CYS   B SG  
5229 N  N   . VAL   B 82  ? 0.1390 0.1163 0.1421 -0.0014 -0.0102 -0.0077 82  VAL   B N   
5230 C  CA  . VAL   B 82  ? 0.1489 0.1244 0.1393 -0.0080 -0.0161 0.0057  82  VAL   B CA  
5231 C  C   . VAL   B 82  ? 0.1518 0.1161 0.1482 -0.0029 -0.0063 0.0013  82  VAL   B C   
5232 O  O   . VAL   B 82  ? 0.1606 0.1172 0.1793 -0.0053 -0.0106 -0.0172 82  VAL   B O   
5233 C  CB  . VAL   B 82  ? 0.1559 0.1421 0.1535 -0.0049 -0.0206 0.0109  82  VAL   B CB  
5234 C  CG1 . VAL   B 82  ? 0.1772 0.1647 0.1671 0.0043  -0.0211 0.0179  82  VAL   B CG1 
5235 C  CG2 . VAL   B 82  ? 0.1589 0.1593 0.1677 -0.0027 -0.0307 0.0146  82  VAL   B CG2 
5245 N  N   . LEU   B 83  ? 0.1391 0.1167 0.1523 -0.0085 -0.0186 -0.0079 83  LEU   B N   
5246 C  CA  . LEU   B 83  ? 0.1398 0.1219 0.1346 -0.0133 -0.0205 -0.0022 83  LEU   B CA  
5247 C  C   . LEU   B 83  ? 0.1426 0.1256 0.1355 -0.0178 -0.0221 -0.0007 83  LEU   B C   
5248 O  O   . LEU   B 83  ? 0.1456 0.1309 0.1214 -0.0169 -0.0132 0.0065  83  LEU   B O   
5249 C  CB  . LEU   B 83  ? 0.1501 0.1346 0.1343 -0.0124 -0.0232 -0.0111 83  LEU   B CB  
5250 C  CG  . LEU   B 83  ? 0.1704 0.1566 0.1365 -0.0184 -0.0152 -0.0102 83  LEU   B CG  
5251 C  CD1 . LEU   B 83  ? 0.1802 0.1635 0.1443 -0.0119 -0.0247 0.0021  83  LEU   B CD1 
5252 C  CD2 . LEU   B 83  ? 0.1871 0.1562 0.1586 -0.0096 -0.0182 -0.0234 83  LEU   B CD2 
5264 N  N   . SER   B 84  ? 0.1490 0.1337 0.1548 -0.0222 -0.0171 -0.0017 84  SER   B N   
5265 C  CA  . SER   B 84  ? 0.1450 0.1517 0.1439 -0.0251 -0.0109 0.0082  84  SER   B CA  
5266 C  C   . SER   B 84  ? 0.1377 0.1679 0.0985 -0.0218 -0.0088 0.0167  84  SER   B C   
5267 O  O   . SER   B 84  ? 0.1465 0.1578 0.1112 -0.0206 -0.0114 0.0054  84  SER   B O   
5268 C  CB  . SER   B 84  ? 0.1677 0.1562 0.1940 -0.0236 0.0086  0.0081  84  SER   B CB  
5269 O  OG  . SER   B 84  ? 0.1685 0.1709 0.2357 -0.0325 0.0027  0.0260  84  SER   B OG  
5275 N  N   . GLY   B 85  ? 0.1450 0.1885 0.1205 -0.0223 -0.0117 0.0183  85  GLY   B N   
5276 C  CA  . GLY   B 85  ? 0.1415 0.1960 0.1385 -0.0316 -0.0038 -0.0084 85  GLY   B CA  
5277 C  C   . GLY   B 85  ? 0.1411 0.1778 0.1322 -0.0423 -0.0018 -0.0029 85  GLY   B C   
5278 O  O   . GLY   B 85  ? 0.1476 0.1778 0.1478 -0.0493 0.0108  -0.0111 85  GLY   B O   
5282 N  N   . HIS   B 86  ? 0.1416 0.1639 0.1484 -0.0308 -0.0130 0.0189  86  HIS   B N   
5283 C  CA  . HIS   B 86  ? 0.1441 0.1638 0.1448 -0.0288 -0.0158 0.0184  86  HIS   B CA  
5284 C  C   . HIS   B 86  ? 0.1410 0.1754 0.1427 -0.0434 -0.0105 0.0286  86  HIS   B C   
5285 O  O   . HIS   B 86  ? 0.1564 0.1893 0.1509 -0.0317 0.0012  0.0280  86  HIS   B O   
5286 C  CB  . HIS   B 86  ? 0.1528 0.1679 0.1614 -0.0207 -0.0169 0.0076  86  HIS   B CB  
5287 C  CG  . HIS   B 86  ? 0.1536 0.1723 0.1540 -0.0139 -0.0247 0.0115  86  HIS   B CG  
5288 N  ND1 . HIS   B 86  ? 0.1652 0.1909 0.1738 -0.0229 -0.0282 -0.0047 86  HIS   B ND1 
5289 C  CD2 . HIS   B 86  ? 0.1575 0.1774 0.1568 -0.0058 -0.0224 0.0075  86  HIS   B CD2 
5290 C  CE1 . HIS   B 86  ? 0.1729 0.1894 0.1565 -0.0176 -0.0116 -0.0179 86  HIS   B CE1 
5291 N  NE2 . HIS   B 86  ? 0.1626 0.1821 0.1497 -0.0025 -0.0133 -0.0012 86  HIS   B NE2 
5299 N  N   . ASN   B 87  ? 0.1415 0.1791 0.1609 -0.0378 0.0001  0.0213  87  ASN   B N   
5300 C  CA  . ASN   B 87  ? 0.1515 0.1981 0.1610 -0.0401 0.0189  0.0169  87  ASN   B CA  
5301 C  C   . ASN   B 87  ? 0.1654 0.1829 0.1481 -0.0273 0.0293  0.0180  87  ASN   B C   
5302 O  O   . ASN   B 87  ? 0.1884 0.1876 0.1760 -0.0228 0.0422  0.0122  87  ASN   B O   
5303 C  CB  . ASN   B 87  ? 0.1540 0.2330 0.1868 -0.0342 0.0243  0.0148  87  ASN   B CB  
5304 C  CG  . ASN   B 87  ? 0.1618 0.2517 0.1936 -0.0020 0.0267  0.0284  87  ASN   B CG  
5305 O  OD1 . ASN   B 87  ? 0.1570 0.2374 0.1801 0.0008  0.0406  0.0392  87  ASN   B OD1 
5306 N  ND2 . ASN   B 87  ? 0.2003 0.2649 0.2350 0.0034  0.0243  0.0279  87  ASN   B ND2 
5313 N  N   . LEU   B 88  ? 0.1553 0.1701 0.1312 -0.0309 0.0127  0.0084  88  LEU   B N   
5314 C  CA  . LEU   B 88  ? 0.1623 0.1637 0.1352 -0.0364 0.0073  -0.0067 88  LEU   B CA  
5315 C  C   . LEU   B 88  ? 0.1640 0.1530 0.1318 -0.0394 0.0033  0.0036  88  LEU   B C   
5316 O  O   . LEU   B 88  ? 0.1892 0.1612 0.1691 -0.0228 -0.0264 -0.0048 88  LEU   B O   
5317 C  CB  . LEU   B 88  ? 0.1726 0.1635 0.1648 -0.0412 -0.0096 0.0084  88  LEU   B CB  
5318 C  CG  . LEU   B 88  ? 0.2124 0.1889 0.1857 -0.0348 -0.0312 0.0317  88  LEU   B CG  
5319 C  CD1 . LEU   B 88  ? 0.2294 0.2183 0.2060 -0.0402 -0.0220 0.0490  88  LEU   B CD1 
5320 C  CD2 . LEU   B 88  ? 0.2497 0.2117 0.2387 0.0010  -0.0539 0.0142  88  LEU   B CD2 
5332 N  N   . ALA   B 89  ? 0.1538 0.1507 0.1352 -0.0395 0.0145  0.0045  89  ALA   B N   
5333 C  CA  . ALA   B 89  ? 0.1535 0.1487 0.1184 -0.0322 0.0060  0.0091  89  ALA   B CA  
5334 C  C   . ALA   B 89  ? 0.1610 0.1510 0.1199 -0.0424 0.0172  0.0041  89  ALA   B C   
5335 O  O   . ALA   B 89  ? 0.1445 0.1585 0.1576 -0.0406 0.0159  -0.0215 89  ALA   B O   
5336 C  CB  . ALA   B 89  ? 0.1504 0.1503 0.1218 -0.0348 0.0043  0.0147  89  ALA   B CB  
5342 N  N   . LYS   B 90  ? 0.1926 0.1377 0.1311 -0.0464 -0.0003 0.0095  90  LYS   B N   
5343 C  CA  . LYS   B 90  ? 0.2087 0.1351 0.1240 -0.0444 -0.0036 0.0053  90  LYS   B CA  
5344 C  C   . LYS   B 90  ? 0.1911 0.1284 0.1398 -0.0451 -0.0060 0.0005  90  LYS   B C   
5345 O  O   . LYS   B 90  ? 0.2003 0.1436 0.1608 -0.0562 -0.0020 -0.0033 90  LYS   B O   
5346 C  CB  . LYS   B 90  ? 0.2319 0.1456 0.1443 -0.0308 0.0033  0.0230  90  LYS   B CB  
5347 C  CG  . LYS   B 90  ? 0.2333 0.1573 0.1543 -0.0193 0.0197  0.0159  90  LYS   B CG  
5348 C  CD  . LYS   B 90  ? 0.2581 0.1785 0.2153 -0.0096 0.0341  -0.0005 90  LYS   B CD  
5349 C  CE  . LYS   B 90  ? 0.2673 0.1954 0.2709 -0.0176 0.0426  -0.0008 90  LYS   B CE  
5350 N  NZ  . LYS   B 90  ? 0.2709 0.1915 0.2642 -0.0277 0.0568  -0.0005 90  LYS   B NZ  
5364 N  N   . HIS   B 91  ? 0.1637 0.1202 0.1219 -0.0319 -0.0141 0.0085  91  HIS   B N   
5365 C  CA  . HIS   B 91  ? 0.1516 0.1251 0.1311 -0.0227 -0.0160 -0.0008 91  HIS   B CA  
5366 C  C   . HIS   B 91  ? 0.1405 0.1262 0.1164 -0.0266 -0.0015 -0.0003 91  HIS   B C   
5367 O  O   . HIS   B 91  ? 0.1559 0.1286 0.1150 -0.0301 -0.0157 0.0023  91  HIS   B O   
5368 C  CB  . HIS   B 91  ? 0.1699 0.1261 0.1591 -0.0097 -0.0106 0.0118  91  HIS   B CB  
5369 C  CG  . HIS   B 91  ? 0.2143 0.1437 0.2286 0.0019  0.0229  0.0295  91  HIS   B CG  
5370 N  ND1 . HIS   B 91  ? 0.2435 0.1526 0.2887 0.0024  0.0317  0.0191  91  HIS   B ND1 
5371 C  CD2 . HIS   B 91  ? 0.2255 0.1720 0.2766 0.0178  0.0134  0.0544  91  HIS   B CD2 
5372 C  CE1 . HIS   B 91  ? 0.2487 0.1663 0.3122 0.0175  0.0254  0.0195  91  HIS   B CE1 
5373 N  NE2 . HIS   B 91  ? 0.2402 0.1803 0.3096 0.0295  0.0226  0.0574  91  HIS   B NE2 
5381 N  N   . CYS   B 92  ? 0.1341 0.1249 0.1197 -0.0247 -0.0152 -0.0038 92  CYS   B N   
5382 C  CA  . CYS   B 92  ? 0.1319 0.1200 0.1211 -0.0223 -0.0056 0.0042  92  CYS   B CA  
5383 C  C   . CYS   B 92  ? 0.1321 0.1174 0.1160 -0.0138 -0.0081 -0.0005 92  CYS   B C   
5384 O  O   . CYS   B 92  ? 0.1417 0.1244 0.1258 -0.0171 -0.0016 -0.0040 92  CYS   B O   
5385 C  CB  . CYS   B 92  ? 0.1327 0.1313 0.1338 -0.0188 -0.0084 0.0031  92  CYS   B CB  
5386 S  SG  . CYS   B 92  ? 0.1354 0.1296 0.1338 -0.0115 -0.0102 0.0052  92  CYS   B SG  
5392 N  N   . LEU   B 93  ? 0.1238 0.1201 0.1150 -0.0114 -0.0078 -0.0045 93  LEU   B N   
5393 C  CA  . LEU   B 93  ? 0.1254 0.1232 0.1178 -0.0031 -0.0082 0.0037  93  LEU   B CA  
5394 C  C   . LEU   B 93  ? 0.1229 0.1183 0.1065 -0.0029 -0.0084 0.0086  93  LEU   B C   
5395 O  O   . LEU   B 93  ? 0.1274 0.1158 0.1252 -0.0062 -0.0075 0.0031  93  LEU   B O   
5396 C  CB  . LEU   B 93  ? 0.1293 0.1244 0.1263 0.0029  -0.0045 0.0045  93  LEU   B CB  
5397 C  CG  . LEU   B 93  ? 0.1278 0.1330 0.1387 -0.0024 0.0005  0.0168  93  LEU   B CG  
5398 C  CD1 . LEU   B 93  ? 0.1352 0.1437 0.1434 0.0021  -0.0066 0.0034  93  LEU   B CD1 
5399 C  CD2 . LEU   B 93  ? 0.1267 0.1386 0.1475 -0.0015 -0.0099 0.0072  93  LEU   B CD2 
5411 N  N   . HIS   B 94  ? 0.1240 0.1137 0.1065 -0.0045 -0.0123 0.0039  94  HIS   B N   
5412 C  CA  . HIS   B 94  ? 0.1265 0.1182 0.1135 -0.0008 -0.0025 0.0037  94  HIS   B CA  
5413 C  C   . HIS   B 94  ? 0.1243 0.1191 0.1278 -0.0041 -0.0024 0.0081  94  HIS   B C   
5414 O  O   . HIS   B 94  ? 0.1282 0.1273 0.1646 -0.0053 0.0121  -0.0060 94  HIS   B O   
5415 C  CB  . HIS   B 94  ? 0.1264 0.1186 0.1258 -0.0014 -0.0096 0.0003  94  HIS   B CB  
5416 C  CG  . HIS   B 94  ? 0.1323 0.1184 0.1279 -0.0024 -0.0149 0.0001  94  HIS   B CG  
5417 N  ND1 . HIS   B 94  ? 0.1354 0.1241 0.1259 -0.0031 -0.0201 0.0010  94  HIS   B ND1 
5418 C  CD2 . HIS   B 94  ? 0.1359 0.1200 0.1330 0.0000  -0.0154 0.0048  94  HIS   B CD2 
5419 C  CE1 . HIS   B 94  ? 0.1338 0.1238 0.1218 -0.0044 -0.0172 0.0038  94  HIS   B CE1 
5420 N  NE2 . HIS   B 94  ? 0.1317 0.1270 0.1313 -0.0129 -0.0133 0.0037  94  HIS   B NE2 
5428 N  N   . VAL   B 95  ? 0.1201 0.1157 0.1287 0.0013  0.0030  0.0079  95  VAL   B N   
5429 C  CA  . VAL   B 95  ? 0.1220 0.1277 0.1267 0.0026  0.0005  0.0131  95  VAL   B CA  
5430 C  C   . VAL   B 95  ? 0.1285 0.1268 0.1281 0.0002  0.0093  0.0145  95  VAL   B C   
5431 O  O   . VAL   B 95  ? 0.1354 0.1193 0.1483 0.0059  0.0080  0.0165  95  VAL   B O   
5432 C  CB  . VAL   B 95  ? 0.1251 0.1246 0.1369 -0.0008 -0.0073 0.0055  95  VAL   B CB  
5433 C  CG1 . VAL   B 95  ? 0.1326 0.1426 0.1518 -0.0090 -0.0004 0.0158  95  VAL   B CG1 
5434 C  CG2 . VAL   B 95  ? 0.1353 0.1242 0.1353 0.0018  -0.0185 0.0044  95  VAL   B CG2 
5444 N  N   . VAL   B 96  ? 0.1380 0.1330 0.1284 0.0098  0.0032  0.0199  96  VAL   B N   
5445 C  CA  . VAL   B 96  ? 0.1470 0.1446 0.1236 0.0102  0.0062  0.0171  96  VAL   B CA  
5446 C  C   . VAL   B 96  ? 0.1482 0.1457 0.1335 0.0070  0.0135  0.0150  96  VAL   B C   
5447 O  O   . VAL   B 96  ? 0.1493 0.1533 0.1633 0.0034  0.0227  0.0035  96  VAL   B O   
5448 C  CB  . VAL   B 96  ? 0.1530 0.1610 0.1247 0.0140  0.0044  0.0111  96  VAL   B CB  
5449 C  CG1 . VAL   B 96  ? 0.1583 0.1783 0.1426 0.0200  0.0046  0.0066  96  VAL   B CG1 
5450 C  CG2 . VAL   B 96  ? 0.1617 0.1657 0.1499 0.0078  0.0064  0.0051  96  VAL   B CG2 
5460 N  N   . GLY   B 97  ? 0.1504 0.1460 0.1299 0.0038  0.0119  0.0127  97  GLY   B N   
5461 C  CA  . GLY   B 97  ? 0.1658 0.1472 0.1420 -0.0001 0.0152  0.0192  97  GLY   B CA  
5462 C  C   . GLY   B 97  ? 0.1853 0.1599 0.1479 0.0136  0.0102  0.0198  97  GLY   B C   
5463 O  O   . GLY   B 97  ? 0.1986 0.1623 0.1470 0.0092  0.0048  0.0157  97  GLY   B O   
5467 N  N   . PRO   B 98  ? 0.2012 0.1670 0.1712 0.0144  0.0336  0.0343  98  PRO   B N   
5468 C  CA  . PRO   B 98  ? 0.2122 0.1824 0.1750 0.0247  0.0417  0.0335  98  PRO   B CA  
5469 C  C   . PRO   B 98  ? 0.2254 0.1824 0.1426 0.0389  0.0470  0.0513  98  PRO   B C   
5470 O  O   . PRO   B 98  ? 0.2133 0.1797 0.1632 0.0319  0.0515  0.0478  98  PRO   B O   
5471 C  CB  . PRO   B 98  ? 0.2011 0.1879 0.1945 0.0196  0.0517  0.0392  98  PRO   B CB  
5472 C  CG  . PRO   B 98  ? 0.1947 0.1825 0.1957 0.0142  0.0460  0.0517  98  PRO   B CG  
5473 C  CD  . PRO   B 98  ? 0.1854 0.1694 0.1758 0.0183  0.0407  0.0487  98  PRO   B CD  
5481 N  N   . ASN   B 99  ? 0.2387 0.2003 0.1638 0.0550  0.0502  0.0326  99  ASN   B N   
5482 C  CA  . ASN   B 99  ? 0.2641 0.2084 0.1687 0.0639  0.0437  0.0538  99  ASN   B CA  
5483 C  C   . ASN   B 99  ? 0.2904 0.2403 0.2020 0.0641  0.0630  0.0873  99  ASN   B C   
5484 O  O   . ASN   B 99  ? 0.3032 0.2486 0.2051 0.0673  0.0538  0.0847  99  ASN   B O   
5485 C  CB  . ASN   B 99  ? 0.2759 0.2032 0.1714 0.0650  0.0299  0.0448  99  ASN   B CB  
5486 C  CG  . ASN   B 99  ? 0.2824 0.2115 0.1939 0.0586  0.0225  0.0404  99  ASN   B CG  
5487 O  OD1 . ASN   B 99  ? 0.2830 0.2125 0.2192 0.0648  0.0262  0.0497  99  ASN   B OD1 
5488 N  ND2 . ASN   B 99  ? 0.2834 0.2065 0.1971 0.0614  -0.0023 0.0343  99  ASN   B ND2 
5495 N  N   A VAL   B 100 ? 0.3074 0.2514 0.2545 0.0557  0.0688  0.1023  100 VAL   B N   
5496 N  N   B VAL   B 100 ? 0.3094 0.2517 0.2493 0.0556  0.0618  0.0998  100 VAL   B N   
5497 C  CA  A VAL   B 100 ? 0.3321 0.2681 0.3101 0.0439  0.0696  0.1122  100 VAL   B CA  
5498 C  CA  B VAL   B 100 ? 0.3331 0.2662 0.2965 0.0451  0.0576  0.1083  100 VAL   B CA  
5499 C  C   A VAL   B 100 ? 0.3521 0.2717 0.3025 0.0484  0.0657  0.1279  100 VAL   B C   
5500 C  C   B VAL   B 100 ? 0.3518 0.2705 0.2961 0.0485  0.0556  0.1235  100 VAL   B C   
5501 O  O   A VAL   B 100 ? 0.3593 0.2813 0.3081 0.0455  0.0741  0.1219  100 VAL   B O   
5502 O  O   B VAL   B 100 ? 0.3565 0.2759 0.2967 0.0448  0.0594  0.1190  100 VAL   B O   
5503 C  CB  A VAL   B 100 ? 0.3396 0.2807 0.3706 0.0249  0.0689  0.1140  100 VAL   B CB  
5504 C  CB  B VAL   B 100 ? 0.3393 0.2756 0.3401 0.0302  0.0537  0.1070  100 VAL   B CB  
5505 C  CG1 A VAL   B 100 ? 0.3446 0.2858 0.3953 0.0213  0.0680  0.1118  100 VAL   B CG1 
5506 C  CG1 B VAL   B 100 ? 0.3429 0.2791 0.3569 0.0272  0.0521  0.1057  100 VAL   B CG1 
5507 C  CG2 A VAL   B 100 ? 0.3397 0.2849 0.3834 0.0173  0.0714  0.1204  100 VAL   B CG2 
5508 C  CG2 B VAL   B 100 ? 0.3402 0.2787 0.3509 0.0243  0.0535  0.1099  100 VAL   B CG2 
5527 N  N   . ASN   B 101 ? 0.3658 0.2736 0.2992 0.0566  0.0493  0.1340  101 ASN   B N   
5528 C  CA  . ASN   B 101 ? 0.4032 0.2895 0.3102 0.0640  0.0296  0.1427  101 ASN   B CA  
5529 C  C   . ASN   B 101 ? 0.4442 0.3270 0.3122 0.0656  0.0183  0.1564  101 ASN   B C   
5530 O  O   . ASN   B 101 ? 0.4497 0.3412 0.3395 0.0704  0.0233  0.1301  101 ASN   B O   
5531 C  CB  . ASN   B 101 ? 0.4011 0.2737 0.3155 0.0595  0.0321  0.1269  101 ASN   B CB  
5532 C  CG  . ASN   B 101 ? 0.3977 0.2593 0.3109 0.0561  0.0363  0.1232  101 ASN   B CG  
5533 O  OD1 . ASN   B 101 ? 0.4006 0.2589 0.3362 0.0524  0.0518  0.1163  101 ASN   B OD1 
5534 N  ND2 . ASN   B 101 ? 0.3928 0.2563 0.2985 0.0520  0.0343  0.1117  101 ASN   B ND2 
5542 N  N   . LYS   B 102 ? 0.4764 0.3585 0.3336 0.0567  0.0197  0.1536  102 LYS   B N   
5543 C  CA  . LYS   B 102 ? 0.5044 0.3957 0.3631 0.0418  0.0305  0.1277  102 LYS   B CA  
5544 C  C   . LYS   B 102 ? 0.5025 0.3995 0.3406 0.0420  0.0425  0.1302  102 LYS   B C   
5545 O  O   . LYS   B 102 ? 0.5126 0.4047 0.3549 0.0435  0.0294  0.1248  102 LYS   B O   
5546 C  CB  . LYS   B 102 ? 0.5294 0.4258 0.4247 0.0275  0.0406  0.0905  102 LYS   B CB  
5547 C  CG  . LYS   B 102 ? 0.5507 0.4524 0.4885 0.0164  0.0504  0.0541  102 LYS   B CG  
5548 C  CD  . LYS   B 102 ? 0.5684 0.4737 0.5506 0.0082  0.0596  0.0250  102 LYS   B CD  
5549 C  CE  . LYS   B 102 ? 0.5810 0.4888 0.5994 0.0017  0.0644  0.0035  102 LYS   B CE  
5550 N  NZ  . LYS   B 102 ? 0.5877 0.4976 0.6265 -0.0013 0.0647  -0.0097 102 LYS   B NZ  
5564 N  N   . GLY   B 103 ? 0.4868 0.3956 0.3318 0.0399  0.0677  0.1259  103 GLY   B N   
5565 C  CA  . GLY   B 103 ? 0.4682 0.3898 0.3445 0.0417  0.0880  0.1039  103 GLY   B CA  
5566 C  C   . GLY   B 103 ? 0.4455 0.3788 0.3376 0.0415  0.1052  0.0840  103 GLY   B C   
5567 O  O   . GLY   B 103 ? 0.4518 0.3865 0.3441 0.0389  0.1097  0.0861  103 GLY   B O   
5571 N  N   A GLU   B 104 ? 0.4279 0.3662 0.3222 0.0501  0.1204  0.0709  104 GLU   B N   
5572 N  N   B GLU   B 104 ? 0.4321 0.3702 0.3350 0.0358  0.0966  0.0693  104 GLU   B N   
5573 C  CA  A GLU   B 104 ? 0.4093 0.3532 0.3079 0.0609  0.1286  0.0564  104 GLU   B CA  
5574 C  CA  B GLU   B 104 ? 0.4174 0.3607 0.3289 0.0307  0.0855  0.0532  104 GLU   B CA  
5575 C  C   A GLU   B 104 ? 0.4105 0.3555 0.3200 0.0432  0.1616  0.0621  104 GLU   B C   
5576 C  C   B GLU   B 104 ? 0.4125 0.3585 0.3392 0.0224  0.0991  0.0511  104 GLU   B C   
5577 O  O   A GLU   B 104 ? 0.4121 0.3596 0.3445 0.0397  0.1604  0.0592  104 GLU   B O   
5578 O  O   B GLU   B 104 ? 0.4132 0.3599 0.3531 0.0211  0.0985  0.0479  104 GLU   B O   
5579 C  CB  A GLU   B 104 ? 0.3939 0.3375 0.2965 0.0882  0.0928  0.0281  104 GLU   B CB  
5580 C  CB  B GLU   B 104 ? 0.4097 0.3527 0.3174 0.0329  0.0580  0.0346  104 GLU   B CB  
5581 C  CG  A GLU   B 104 ? 0.3810 0.3259 0.2812 0.1112  0.0532  -0.0037 104 GLU   B CG  
5582 C  CG  B GLU   B 104 ? 0.4034 0.3464 0.3048 0.0342  0.0296  0.0134  104 GLU   B CG  
5583 C  CD  A GLU   B 104 ? 0.3693 0.3154 0.2562 0.1288  0.0173  -0.0218 104 GLU   B CD  
5584 C  CD  B GLU   B 104 ? 0.3981 0.3401 0.2894 0.0333  0.0059  -0.0011 104 GLU   B CD  
5585 O  OE1 A GLU   B 104 ? 0.3562 0.3019 0.2134 0.1441  0.0158  -0.0244 104 GLU   B OE1 
5586 O  OE1 B GLU   B 104 ? 0.3938 0.3355 0.2738 0.0324  0.0034  -0.0036 104 GLU   B OE1 
5587 O  OE2 A GLU   B 104 ? 0.3700 0.3210 0.2617 0.1261  -0.0075 -0.0352 104 GLU   B OE2 
5588 O  OE2 B GLU   B 104 ? 0.3977 0.3402 0.2866 0.0320  -0.0101 -0.0105 104 GLU   B OE2 
5601 N  N   A ASP   B 105 ? 0.4069 0.3537 0.3150 0.0302  0.1877  0.0688  105 ASP   B N   
5602 N  N   B ASP   B 105 ? 0.4056 0.3548 0.3334 0.0156  0.1105  0.0515  105 ASP   B N   
5603 C  CA  A ASP   B 105 ? 0.4070 0.3529 0.3360 0.0192  0.1996  0.0556  105 ASP   B CA  
5604 C  CA  B ASP   B 105 ? 0.4003 0.3511 0.3405 0.0098  0.1167  0.0433  105 ASP   B CA  
5605 C  C   A ASP   B 105 ? 0.3867 0.3275 0.3035 0.0059  0.1955  0.0499  105 ASP   B C   
5606 C  C   B ASP   B 105 ? 0.3898 0.3389 0.3218 0.0042  0.1159  0.0348  105 ASP   B C   
5607 O  O   A ASP   B 105 ? 0.3706 0.3224 0.2908 0.0047  0.1869  0.0496  105 ASP   B O   
5608 O  O   B ASP   B 105 ? 0.3875 0.3370 0.3108 0.0042  0.1207  0.0372  105 ASP   B O   
5609 C  CB  A ASP   B 105 ? 0.4215 0.3739 0.4111 0.0256  0.2042  0.0387  105 ASP   B CB  
5610 C  CB  B ASP   B 105 ? 0.4031 0.3577 0.3703 0.0113  0.1222  0.0404  105 ASP   B CB  
5611 C  CG  A ASP   B 105 ? 0.4320 0.3893 0.4768 0.0286  0.2110  0.0273  105 ASP   B CG  
5612 C  CG  B ASP   B 105 ? 0.4042 0.3617 0.3966 0.0105  0.1309  0.0414  105 ASP   B CG  
5613 O  OD1 A ASP   B 105 ? 0.4318 0.3934 0.4872 0.0242  0.2242  0.0316  105 ASP   B OD1 
5614 O  OD1 B ASP   B 105 ? 0.4035 0.3632 0.4015 0.0070  0.1351  0.0442  105 ASP   B OD1 
5615 O  OD2 A ASP   B 105 ? 0.4379 0.3965 0.5116 0.0343  0.2027  0.0172  105 ASP   B OD2 
5616 O  OD2 B ASP   B 105 ? 0.4031 0.3631 0.4032 0.0102  0.1370  0.0432  105 ASP   B OD2 
5625 N  N   A ILE   B 106 ? 0.3811 0.3038 0.3058 -0.0031 0.1915  0.0499  106 ILE   B N   
5626 N  N   B ILE   B 106 ? 0.3798 0.3272 0.3194 0.0013  0.1069  0.0266  106 ILE   B N   
5627 C  CA  A ILE   B 106 ? 0.3652 0.2767 0.3191 -0.0166 0.1880  0.0429  106 ILE   B CA  
5628 C  CA  B ILE   B 106 ? 0.3658 0.3155 0.3226 -0.0029 0.1018  0.0170  106 ILE   B CA  
5629 C  C   A ILE   B 106 ? 0.3331 0.2665 0.3145 -0.0152 0.1858  0.0299  106 ILE   B C   
5630 C  C   B ILE   B 106 ? 0.3434 0.3092 0.3219 -0.0016 0.0994  0.0073  106 ILE   B C   
5631 O  O   A ILE   B 106 ? 0.3241 0.2445 0.3091 -0.0201 0.1808  0.0296  106 ILE   B O   
5632 O  O   B ILE   B 106 ? 0.3408 0.3021 0.3193 -0.0044 0.0955  0.0027  106 ILE   B O   
5633 C  CB  A ILE   B 106 ? 0.3839 0.2674 0.3444 -0.0286 0.1787  0.0457  106 ILE   B CB  
5634 C  CB  B ILE   B 106 ? 0.3747 0.3138 0.3301 -0.0079 0.0987  0.0167  106 ILE   B CB  
5635 C  CG1 A ILE   B 106 ? 0.3909 0.2663 0.3530 -0.0254 0.1688  0.0376  106 ILE   B CG1 
5636 C  CG1 B ILE   B 106 ? 0.3780 0.3134 0.3334 -0.0068 0.0941  0.0145  106 ILE   B CG1 
5637 C  CG2 A ILE   B 106 ? 0.3904 0.2684 0.3608 -0.0373 0.1786  0.0501  106 ILE   B CG2 
5638 C  CG2 B ILE   B 106 ? 0.3782 0.3158 0.3384 -0.0112 0.0997  0.0167  106 ILE   B CG2 
5639 C  CD1 A ILE   B 106 ? 0.3939 0.2677 0.3510 -0.0213 0.1665  0.0361  106 ILE   B CD1 
5640 C  CD1 B ILE   B 106 ? 0.3794 0.3136 0.3330 -0.0051 0.0927  0.0145  106 ILE   B CD1 
5663 N  N   A GLN   B 107 ? 0.3158 0.2843 0.3313 -0.0134 0.1724  0.0275  107 GLN   B N   
5664 N  N   B GLN   B 107 ? 0.3260 0.3123 0.3349 0.0002  0.0980  0.0065  107 GLN   B N   
5665 C  CA  A GLN   B 107 ? 0.2965 0.3011 0.3496 -0.0142 0.1532  0.0254  107 GLN   B CA  
5666 C  CA  B GLN   B 107 ? 0.3080 0.3138 0.3468 0.0009  0.0943  0.0096  107 GLN   B CA  
5667 C  C   A GLN   B 107 ? 0.2640 0.2798 0.3217 -0.0075 0.1203  0.0174  107 GLN   B C   
5668 C  C   B GLN   B 107 ? 0.2743 0.2891 0.3168 0.0035  0.0930  0.0097  107 GLN   B C   
5669 O  O   A GLN   B 107 ? 0.2536 0.2772 0.3491 -0.0040 0.0932  0.0023  107 GLN   B O   
5670 O  O   B GLN   B 107 ? 0.2699 0.2903 0.3297 0.0055  0.0793  0.0002  107 GLN   B O   
5671 C  CB  A GLN   B 107 ? 0.3255 0.3401 0.4205 -0.0148 0.1319  0.0245  107 GLN   B CB  
5672 C  CB  B GLN   B 107 ? 0.3287 0.3400 0.3988 0.0008  0.0823  0.0109  107 GLN   B CB  
5673 C  CG  A GLN   B 107 ? 0.3562 0.3751 0.4909 -0.0098 0.0977  0.0216  107 GLN   B CG  
5674 C  CG  B GLN   B 107 ? 0.3487 0.3632 0.4501 0.0032  0.0644  0.0119  107 GLN   B CG  
5675 C  CD  A GLN   B 107 ? 0.3790 0.4013 0.5460 -0.0085 0.0721  0.0214  107 GLN   B CD  
5676 C  CD  B GLN   B 107 ? 0.3639 0.3808 0.4916 0.0033  0.0497  0.0135  107 GLN   B CD  
5677 O  OE1 A GLN   B 107 ? 0.3872 0.4114 0.5656 -0.0072 0.0671  0.0182  107 GLN   B OE1 
5678 O  OE1 B GLN   B 107 ? 0.3691 0.3873 0.5051 0.0037  0.0475  0.0129  107 GLN   B OE1 
5679 N  NE2 A GLN   B 107 ? 0.3876 0.4090 0.5639 -0.0069 0.0609  0.0249  107 GLN   B NE2 
5680 N  NE2 B GLN   B 107 ? 0.3698 0.3863 0.5063 0.0042  0.0430  0.0159  107 GLN   B NE2 
5697 N  N   . LEU   B 108 ? 0.2437 0.2622 0.2853 0.0126  0.0984  0.0168  108 LEU   B N   
5698 C  CA  . LEU   B 108 ? 0.2208 0.2353 0.2427 0.0214  0.0706  0.0279  108 LEU   B CA  
5699 C  C   . LEU   B 108 ? 0.1840 0.1923 0.2241 0.0200  0.0471  0.0341  108 LEU   B C   
5700 O  O   . LEU   B 108 ? 0.1831 0.1811 0.2116 0.0215  0.0409  0.0318  108 LEU   B O   
5701 C  CB  . LEU   B 108 ? 0.2372 0.2534 0.2243 0.0201  0.0697  0.0320  108 LEU   B CB  
5702 C  CG  . LEU   B 108 ? 0.2532 0.2795 0.2311 0.0229  0.0633  0.0072  108 LEU   B CG  
5703 C  CD1 . LEU   B 108 ? 0.2621 0.2901 0.2260 0.0181  0.0675  0.0062  108 LEU   B CD1 
5704 C  CD2 . LEU   B 108 ? 0.2661 0.2938 0.2407 0.0321  0.0511  -0.0059 108 LEU   B CD2 
5717 N  N   . LEU   B 109 ? 0.1690 0.1686 0.2155 0.0151  0.0378  0.0288  109 LEU   B N   
5718 C  CA  . LEU   B 109 ? 0.1501 0.1432 0.2228 0.0103  0.0345  0.0319  109 LEU   B CA  
5719 C  C   . LEU   B 109 ? 0.1428 0.1297 0.2210 0.0056  0.0341  0.0182  109 LEU   B C   
5720 O  O   . LEU   B 109 ? 0.1397 0.1274 0.2148 0.0038  0.0317  0.0317  109 LEU   B O   
5721 C  CB  . LEU   B 109 ? 0.1587 0.1343 0.2322 0.0058  0.0238  0.0369  109 LEU   B CB  
5722 C  CG  . LEU   B 109 ? 0.1536 0.1334 0.2287 0.0021  0.0212  0.0272  109 LEU   B CG  
5723 C  CD1 . LEU   B 109 ? 0.1534 0.1458 0.2218 0.0137  0.0245  0.0257  109 LEU   B CD1 
5724 C  CD2 . LEU   B 109 ? 0.1659 0.1415 0.2398 0.0083  0.0178  0.0247  109 LEU   B CD2 
5736 N  N   . LYS   B 110 ? 0.1388 0.1305 0.2208 -0.0041 0.0333  0.0253  110 LYS   B N   
5737 C  CA  . LYS   B 110 ? 0.1336 0.1285 0.2135 0.0016  0.0234  0.0206  110 LYS   B CA  
5738 C  C   . LYS   B 110 ? 0.1343 0.1288 0.2049 -0.0009 0.0248  0.0168  110 LYS   B C   
5739 O  O   . LYS   B 110 ? 0.1290 0.1320 0.2027 -0.0012 0.0220  0.0071  110 LYS   B O   
5740 C  CB  . LYS   B 110 ? 0.1373 0.1343 0.2319 -0.0030 0.0335  0.0152  110 LYS   B CB  
5741 C  CG  . LYS   B 110 ? 0.1387 0.1304 0.2492 -0.0070 0.0209  0.0201  110 LYS   B CG  
5742 C  CD  . LYS   B 110 ? 0.1439 0.1319 0.2508 -0.0052 0.0235  0.0180  110 LYS   B CD  
5743 C  CE  . LYS   B 110 ? 0.1378 0.1443 0.2710 -0.0046 0.0182  0.0085  110 LYS   B CE  
5744 N  NZ  . LYS   B 110 ? 0.1427 0.1584 0.2615 0.0013  0.0097  0.0052  110 LYS   B NZ  
5758 N  N   . SER   B 111 ? 0.1371 0.1277 0.2183 -0.0026 0.0308  0.0166  111 SER   B N   
5759 C  CA  . SER   B 111 ? 0.1442 0.1305 0.2004 0.0017  0.0224  0.0163  111 SER   B CA  
5760 C  C   . SER   B 111 ? 0.1390 0.1257 0.1935 -0.0011 0.0132  0.0138  111 SER   B C   
5761 O  O   . SER   B 111 ? 0.1333 0.1344 0.1991 -0.0008 0.0104  0.0131  111 SER   B O   
5762 C  CB  . SER   B 111 ? 0.1549 0.1561 0.2143 0.0095  0.0347  0.0229  111 SER   B CB  
5763 O  OG  . SER   B 111 ? 0.1731 0.1912 0.2187 0.0126  0.0440  0.0248  111 SER   B OG  
5769 N  N   . ALA   B 112 ? 0.1299 0.1272 0.1944 0.0086  0.0208  0.0256  112 ALA   B N   
5770 C  CA  . ALA   B 112 ? 0.1335 0.1366 0.1772 0.0077  0.0138  0.0127  112 ALA   B CA  
5771 C  C   . ALA   B 112 ? 0.1244 0.1263 0.1718 0.0024  0.0152  0.0113  112 ALA   B C   
5772 O  O   . ALA   B 112 ? 0.1282 0.1310 0.1781 -0.0049 0.0149  0.0053  112 ALA   B O   
5773 C  CB  . ALA   B 112 ? 0.1353 0.1420 0.1885 0.0083  0.0111  0.0153  112 ALA   B CB  
5779 N  N   . TYR   B 113 ? 0.1219 0.1200 0.1852 -0.0016 0.0178  0.0139  113 TYR   B N   
5780 C  CA  . TYR   B 113 ? 0.1168 0.1170 0.1787 -0.0025 0.0116  0.0052  113 TYR   B CA  
5781 C  C   . TYR   B 113 ? 0.1149 0.1131 0.1661 -0.0038 0.0124  0.0072  113 TYR   B C   
5782 O  O   . TYR   B 113 ? 0.1201 0.1169 0.1601 -0.0035 0.0097  0.0018  113 TYR   B O   
5783 C  CB  . TYR   B 113 ? 0.1232 0.1133 0.1895 -0.0029 0.0191  0.0107  113 TYR   B CB  
5784 C  CG  . TYR   B 113 ? 0.1227 0.1184 0.1948 -0.0005 0.0116  0.0123  113 TYR   B CG  
5785 C  CD1 . TYR   B 113 ? 0.1314 0.1177 0.2107 0.0003  0.0178  0.0169  113 TYR   B CD1 
5786 C  CD2 . TYR   B 113 ? 0.1341 0.1161 0.1938 -0.0027 0.0080  0.0163  113 TYR   B CD2 
5787 C  CE1 . TYR   B 113 ? 0.1310 0.1214 0.2088 0.0021  0.0242  0.0099  113 TYR   B CE1 
5788 C  CE2 . TYR   B 113 ? 0.1378 0.1106 0.2114 0.0044  0.0114  0.0196  113 TYR   B CE2 
5789 C  CZ  . TYR   B 113 ? 0.1254 0.1188 0.2122 0.0110  0.0113  0.0133  113 TYR   B CZ  
5790 O  OH  . TYR   B 113 ? 0.1368 0.1170 0.2359 0.0082  0.0192  0.0134  113 TYR   B OH  
5800 N  N   . GLU   B 114 ? 0.1161 0.1090 0.1859 -0.0003 0.0168  0.0111  114 GLU   B N   
5801 C  CA  . GLU   B 114 ? 0.1180 0.1097 0.1864 0.0020  0.0075  -0.0004 114 GLU   B CA  
5802 C  C   . GLU   B 114 ? 0.1157 0.1132 0.1638 -0.0023 0.0078  0.0031  114 GLU   B C   
5803 O  O   . GLU   B 114 ? 0.1175 0.1154 0.1816 0.0020  0.0011  0.0106  114 GLU   B O   
5804 C  CB  . GLU   B 114 ? 0.1193 0.1178 0.1916 -0.0044 0.0124  0.0086  114 GLU   B CB  
5805 C  CG  . GLU   B 114 ? 0.1239 0.1176 0.1940 -0.0023 0.0129  0.0052  114 GLU   B CG  
5806 C  CD  . GLU   B 114 ? 0.1245 0.1201 0.2020 -0.0049 0.0076  0.0054  114 GLU   B CD  
5807 O  OE1 . GLU   B 114 ? 0.1186 0.1352 0.2019 -0.0091 0.0149  0.0082  114 GLU   B OE1 
5808 O  OE2 . GLU   B 114 ? 0.1233 0.1385 0.2177 -0.0165 0.0170  0.0043  114 GLU   B OE2 
5815 N  N   . ASN   B 115 ? 0.1219 0.1083 0.1736 -0.0034 0.0019  0.0052  115 ASN   B N   
5816 C  CA  . ASN   B 115 ? 0.1222 0.1169 0.1592 -0.0052 0.0015  0.0083  115 ASN   B CA  
5817 C  C   . ASN   B 115 ? 0.1189 0.1109 0.1576 -0.0082 -0.0019 0.0007  115 ASN   B C   
5818 O  O   . ASN   B 115 ? 0.1297 0.1122 0.1679 -0.0091 0.0023  0.0033  115 ASN   B O   
5819 C  CB  . ASN   B 115 ? 0.1330 0.1279 0.1630 -0.0090 0.0030  0.0037  115 ASN   B CB  
5820 C  CG  . ASN   B 115 ? 0.1433 0.1358 0.1586 0.0031  0.0025  0.0007  115 ASN   B CG  
5821 O  OD1 . ASN   B 115 ? 0.1773 0.1465 0.1856 0.0025  0.0163  -0.0125 115 ASN   B OD1 
5822 N  ND2 . ASN   B 115 ? 0.1421 0.1440 0.1523 0.0024  0.0071  0.0069  115 ASN   B ND2 
5829 N  N   . PHE   B 116 ? 0.1214 0.1127 0.1448 -0.0078 0.0005  0.0007  116 PHE   B N   
5830 C  CA  . PHE   B 116 ? 0.1227 0.1183 0.1495 -0.0064 -0.0010 0.0032  116 PHE   B CA  
5831 C  C   . PHE   B 116 ? 0.1232 0.1064 0.1505 -0.0097 -0.0034 0.0083  116 PHE   B C   
5832 O  O   . PHE   B 116 ? 0.1270 0.1195 0.1633 -0.0022 -0.0037 0.0066  116 PHE   B O   
5833 C  CB  . PHE   B 116 ? 0.1210 0.1122 0.1571 -0.0062 -0.0091 0.0088  116 PHE   B CB  
5834 C  CG  . PHE   B 116 ? 0.1167 0.1132 0.1518 -0.0047 0.0003  0.0077  116 PHE   B CG  
5835 C  CD1 . PHE   B 116 ? 0.1247 0.1164 0.1756 -0.0024 0.0056  0.0024  116 PHE   B CD1 
5836 C  CD2 . PHE   B 116 ? 0.1215 0.1186 0.1565 -0.0049 0.0007  0.0023  116 PHE   B CD2 
5837 C  CE1 . PHE   B 116 ? 0.1250 0.1209 0.1753 0.0028  -0.0106 0.0052  116 PHE   B CE1 
5838 C  CE2 . PHE   B 116 ? 0.1238 0.1196 0.1654 -0.0037 0.0012  -0.0006 116 PHE   B CE2 
5839 C  CZ  . PHE   B 116 ? 0.1170 0.1218 0.1669 -0.0014 -0.0073 0.0071  116 PHE   B CZ  
5849 N  N   . ASN   B 117 ? 0.1189 0.1138 0.1647 -0.0053 -0.0062 0.0074  117 ASN   B N   
5850 C  CA  . ASN   B 117 ? 0.1264 0.1170 0.1614 -0.0060 -0.0040 -0.0004 117 ASN   B CA  
5851 C  C   . ASN   B 117 ? 0.1315 0.1149 0.1725 -0.0003 -0.0056 0.0095  117 ASN   B C   
5852 O  O   . ASN   B 117 ? 0.1381 0.1209 0.1999 -0.0060 -0.0257 0.0148  117 ASN   B O   
5853 C  CB  . ASN   B 117 ? 0.1306 0.1186 0.1634 -0.0022 -0.0014 -0.0058 117 ASN   B CB  
5854 C  CG  . ASN   B 117 ? 0.1265 0.1195 0.1772 0.0044  0.0006  -0.0083 117 ASN   B CG  
5855 O  OD1 . ASN   B 117 ? 0.1465 0.1207 0.1930 -0.0131 0.0078  -0.0031 117 ASN   B OD1 
5856 N  ND2 . ASN   B 117 ? 0.1279 0.1253 0.1799 0.0011  0.0030  -0.0017 117 ASN   B ND2 
5863 N  N   . GLN   B 118 ? 0.1294 0.1104 0.1682 -0.0069 -0.0100 0.0015  118 GLN   B N   
5864 C  CA  . GLN   B 118 ? 0.1354 0.1119 0.1851 0.0007  -0.0091 -0.0015 118 GLN   B CA  
5865 C  C   . GLN   B 118 ? 0.1399 0.1133 0.1834 0.0004  -0.0058 -0.0024 118 GLN   B C   
5866 O  O   . GLN   B 118 ? 0.1588 0.1142 0.2157 -0.0105 0.0096  0.0039  118 GLN   B O   
5867 C  CB  . GLN   B 118 ? 0.1386 0.1181 0.1993 -0.0002 -0.0152 0.0049  118 GLN   B CB  
5868 C  CG  . GLN   B 118 ? 0.1515 0.1159 0.1876 0.0050  -0.0028 -0.0049 118 GLN   B CG  
5869 C  CD  . GLN   B 118 ? 0.1533 0.1154 0.1801 0.0009  -0.0105 -0.0120 118 GLN   B CD  
5870 O  OE1 . GLN   B 118 ? 0.1573 0.1156 0.2061 0.0043  0.0101  0.0037  118 GLN   B OE1 
5871 N  NE2 . GLN   B 118 ? 0.1619 0.1193 0.1818 0.0023  -0.0121 0.0015  118 GLN   B NE2 
5880 N  N   . HIS   B 119 ? 0.1360 0.1201 0.1614 -0.0090 -0.0097 0.0103  119 HIS   B N   
5881 C  CA  . HIS   B 119 ? 0.1416 0.1331 0.1524 -0.0057 -0.0078 0.0114  119 HIS   B CA  
5882 C  C   . HIS   B 119 ? 0.1445 0.1329 0.1418 -0.0072 -0.0196 0.0077  119 HIS   B C   
5883 O  O   . HIS   B 119 ? 0.1551 0.1264 0.1648 -0.0240 -0.0224 0.0090  119 HIS   B O   
5884 C  CB  . HIS   B 119 ? 0.1443 0.1415 0.1602 -0.0015 -0.0160 0.0009  119 HIS   B CB  
5885 C  CG  . HIS   B 119 ? 0.1479 0.1668 0.1743 0.0074  -0.0343 -0.0135 119 HIS   B CG  
5886 N  ND1 . HIS   B 119 ? 0.1632 0.1816 0.2029 -0.0004 -0.0419 -0.0286 119 HIS   B ND1 
5887 C  CD2 . HIS   B 119 ? 0.1653 0.1854 0.1866 0.0343  -0.0458 -0.0119 119 HIS   B CD2 
5888 C  CE1 . HIS   B 119 ? 0.1789 0.1976 0.2125 0.0113  -0.0476 -0.0431 119 HIS   B CE1 
5889 N  NE2 . HIS   B 119 ? 0.1845 0.2055 0.2021 0.0299  -0.0484 -0.0316 119 HIS   B NE2 
5897 N  N   . GLU   B 120 ? 0.1660 0.1355 0.1485 -0.0115 -0.0304 0.0171  120 GLU   B N   
5898 C  CA  . GLU   B 120 ? 0.1897 0.1453 0.1619 -0.0053 -0.0411 0.0319  120 GLU   B CA  
5899 C  C   . GLU   B 120 ? 0.1694 0.1372 0.1525 -0.0155 -0.0255 0.0275  120 GLU   B C   
5900 O  O   . GLU   B 120 ? 0.1662 0.1455 0.1507 -0.0148 -0.0276 0.0172  120 GLU   B O   
5901 C  CB  . GLU   B 120 ? 0.2538 0.1811 0.2390 0.0139  -0.0751 0.0487  120 GLU   B CB  
5902 C  CG  . GLU   B 120 ? 0.3081 0.2537 0.3429 0.0235  -0.0963 0.0595  120 GLU   B CG  
5903 C  CD  . GLU   B 120 ? 0.3489 0.3183 0.4523 0.0249  -0.0998 0.0671  120 GLU   B CD  
5904 O  OE1 . GLU   B 120 ? 0.3682 0.3384 0.4913 0.0182  -0.0936 0.0775  120 GLU   B OE1 
5905 O  OE2 . GLU   B 120 ? 0.3686 0.3448 0.5055 0.0245  -0.0983 0.0595  120 GLU   B OE2 
5912 N  N   . VAL   B 121 ? 0.1631 0.1304 0.1526 -0.0216 -0.0161 0.0203  121 VAL   B N   
5913 C  CA  . VAL   B 121 ? 0.1609 0.1455 0.1325 -0.0187 -0.0156 0.0121  121 VAL   B CA  
5914 C  C   . VAL   B 121 ? 0.1518 0.1374 0.1329 -0.0212 -0.0162 0.0104  121 VAL   B C   
5915 O  O   . VAL   B 121 ? 0.1545 0.1346 0.1605 -0.0294 -0.0227 0.0085  121 VAL   B O   
5916 C  CB  . VAL   B 121 ? 0.1822 0.1798 0.1456 -0.0106 -0.0197 0.0124  121 VAL   B CB  
5917 C  CG1 . VAL   B 121 ? 0.1834 0.1900 0.1809 -0.0136 -0.0120 0.0097  121 VAL   B CG1 
5918 C  CG2 . VAL   B 121 ? 0.2081 0.2019 0.1522 -0.0001 -0.0191 0.0068  121 VAL   B CG2 
5928 N  N   . LEU   B 122 ? 0.1424 0.1314 0.1275 -0.0150 -0.0210 0.0075  122 LEU   B N   
5929 C  CA  . LEU   B 122 ? 0.1339 0.1392 0.1182 -0.0173 -0.0176 0.0035  122 LEU   B CA  
5930 C  C   . LEU   B 122 ? 0.1355 0.1299 0.1338 -0.0266 -0.0119 0.0047  122 LEU   B C   
5931 O  O   . LEU   B 122 ? 0.1416 0.1283 0.1729 -0.0305 -0.0220 0.0029  122 LEU   B O   
5932 C  CB  . LEU   B 122 ? 0.1591 0.1468 0.1539 -0.0050 -0.0271 0.0104  122 LEU   B CB  
5933 C  CG  . LEU   B 122 ? 0.1485 0.1546 0.1612 -0.0115 -0.0076 0.0121  122 LEU   B CG  
5934 C  CD1 . LEU   B 122 ? 0.1476 0.1790 0.1695 -0.0204 -0.0203 0.0040  122 LEU   B CD1 
5935 C  CD2 . LEU   B 122 ? 0.1510 0.1545 0.1471 -0.0074 -0.0114 -0.0029 122 LEU   B CD2 
5947 N  N   . LEU   B 123 ? 0.1366 0.1164 0.1302 -0.0249 -0.0113 0.0088  123 LEU   B N   
5948 C  CA  . LEU   B 123 ? 0.1406 0.1172 0.1278 -0.0262 -0.0157 0.0007  123 LEU   B CA  
5949 C  C   . LEU   B 123 ? 0.1378 0.1174 0.1216 -0.0248 -0.0135 -0.0017 123 LEU   B C   
5950 O  O   . LEU   B 123 ? 0.1474 0.1212 0.1283 -0.0282 -0.0136 0.0044  123 LEU   B O   
5951 C  CB  . LEU   B 123 ? 0.1435 0.1219 0.1431 -0.0254 -0.0126 0.0017  123 LEU   B CB  
5952 C  CG  . LEU   B 123 ? 0.1387 0.1326 0.1548 -0.0183 -0.0016 0.0067  123 LEU   B CG  
5953 C  CD1 . LEU   B 123 ? 0.1496 0.1319 0.1670 -0.0172 0.0034  -0.0118 123 LEU   B CD1 
5954 C  CD2 . LEU   B 123 ? 0.1459 0.1423 0.1755 -0.0143 0.0069  0.0143  123 LEU   B CD2 
5966 N  N   . ALA   B 124 ? 0.1320 0.1162 0.1209 -0.0199 -0.0029 -0.0042 124 ALA   B N   
5967 C  CA  . ALA   B 124 ? 0.1239 0.1161 0.1386 -0.0160 -0.0080 -0.0068 124 ALA   B CA  
5968 C  C   . ALA   B 124 ? 0.1232 0.1185 0.1313 -0.0175 -0.0071 0.0005  124 ALA   B C   
5969 O  O   . ALA   B 124 ? 0.1342 0.1199 0.1475 -0.0124 -0.0090 -0.0008 124 ALA   B O   
5970 C  CB  . ALA   B 124 ? 0.1326 0.1245 0.1527 -0.0049 0.0013  0.0058  124 ALA   B CB  
5976 N  N   . PRO   B 125 ? 0.1320 0.1171 0.1342 -0.0131 -0.0095 0.0092  125 PRO   B N   
5977 C  CA  . PRO   B 125 ? 0.1444 0.1207 0.1471 -0.0152 -0.0108 0.0184  125 PRO   B CA  
5978 C  C   . PRO   B 125 ? 0.1339 0.1162 0.1606 -0.0132 -0.0076 0.0063  125 PRO   B C   
5979 O  O   . PRO   B 125 ? 0.1397 0.1176 0.1807 -0.0097 0.0040  0.0142  125 PRO   B O   
5980 C  CB  . PRO   B 125 ? 0.1444 0.1448 0.1620 -0.0164 -0.0194 0.0349  125 PRO   B CB  
5981 C  CG  . PRO   B 125 ? 0.1495 0.1507 0.1538 -0.0288 -0.0195 0.0185  125 PRO   B CG  
5982 C  CD  . PRO   B 125 ? 0.1443 0.1313 0.1378 -0.0277 -0.0112 0.0081  125 PRO   B CD  
5990 N  N   . LEU   B 126 ? 0.1415 0.1109 0.1855 -0.0156 0.0052  0.0136  126 LEU   B N   
5991 C  CA  . LEU   B 126 ? 0.1454 0.1232 0.1882 -0.0121 0.0209  0.0146  126 LEU   B CA  
5992 C  C   . LEU   B 126 ? 0.1409 0.1324 0.1949 -0.0019 0.0248  0.0214  126 LEU   B C   
5993 O  O   . LEU   B 126 ? 0.1604 0.1569 0.2162 0.0182  0.0025  0.0001  126 LEU   B O   
5994 C  CB  . LEU   B 126 ? 0.1645 0.1271 0.2171 -0.0161 0.0244  0.0127  126 LEU   B CB  
5995 C  CG  . LEU   B 126 ? 0.1758 0.1368 0.2310 -0.0251 0.0219  -0.0045 126 LEU   B CG  
5996 C  CD1 . LEU   B 126 ? 0.1889 0.1427 0.2745 -0.0195 0.0160  -0.0061 126 LEU   B CD1 
5997 C  CD2 . LEU   B 126 ? 0.1803 0.1454 0.2270 -0.0301 0.0147  -0.0096 126 LEU   B CD2 
6009 N  N   . LEU   B 127 ? 0.1364 0.1192 0.2015 0.0024  0.0261  0.0120  127 LEU   B N   
6010 C  CA  . LEU   B 127 ? 0.1387 0.1287 0.2017 -0.0030 0.0286  0.0215  127 LEU   B CA  
6011 C  C   . LEU   B 127 ? 0.1366 0.1272 0.2036 0.0007  0.0214  0.0185  127 LEU   B C   
6012 O  O   . LEU   B 127 ? 0.1368 0.1312 0.2127 -0.0123 0.0127  0.0197  127 LEU   B O   
6013 C  CB  . LEU   B 127 ? 0.1498 0.1285 0.2096 -0.0023 0.0238  0.0287  127 LEU   B CB  
6014 C  CG  . LEU   B 127 ? 0.1642 0.1296 0.2196 0.0019  0.0236  0.0216  127 LEU   B CG  
6015 C  CD1 . LEU   B 127 ? 0.1738 0.1286 0.2254 0.0060  0.0187  0.0176  127 LEU   B CD1 
6016 C  CD2 . LEU   B 127 ? 0.1665 0.1367 0.2358 -0.0077 0.0237  0.0248  127 LEU   B CD2 
6028 N  N   . SER   B 128 ? 0.1378 0.1247 0.2011 0.0005  0.0076  0.0127  128 SER   B N   
6029 C  CA  . SER   B 128 ? 0.1545 0.1308 0.2067 0.0100  -0.0013 0.0227  128 SER   B CA  
6030 C  C   . SER   B 128 ? 0.1653 0.1351 0.2288 0.0104  -0.0234 0.0231  128 SER   B C   
6031 O  O   . SER   B 128 ? 0.1814 0.1393 0.2629 0.0068  -0.0209 0.0331  128 SER   B O   
6032 C  CB  . SER   B 128 ? 0.1658 0.1356 0.2055 0.0131  0.0029  0.0288  128 SER   B CB  
6033 O  OG  . SER   B 128 ? 0.1678 0.1514 0.2019 0.0109  0.0136  0.0323  128 SER   B OG  
6039 N  N   . ALA   B 129 ? 0.1780 0.1405 0.2520 0.0232  -0.0124 0.0063  129 ALA   B N   
6040 C  CA  . ALA   B 129 ? 0.1916 0.1454 0.2581 0.0305  -0.0104 0.0019  129 ALA   B CA  
6041 C  C   . ALA   B 129 ? 0.1819 0.1404 0.2469 0.0200  0.0028  0.0046  129 ALA   B C   
6042 O  O   . ALA   B 129 ? 0.1708 0.1429 0.2499 0.0162  -0.0030 0.0068  129 ALA   B O   
6043 C  CB  . ALA   B 129 ? 0.2127 0.1676 0.2850 0.0312  -0.0010 -0.0096 129 ALA   B CB  
6049 N  N   . GLY   B 130 ? 0.1809 0.1392 0.2419 0.0253  0.0061  0.0021  130 GLY   B N   
6050 C  CA  . GLY   B 130 ? 0.1852 0.1541 0.2493 0.0181  0.0239  0.0012  130 GLY   B CA  
6051 C  C   . GLY   B 130 ? 0.1882 0.1542 0.2447 0.0152  0.0206  0.0058  130 GLY   B C   
6052 O  O   . GLY   B 130 ? 0.2042 0.1596 0.2526 0.0164  0.0146  0.0160  130 GLY   B O   
6056 N  N   . ILE   B 131 ? 0.1849 0.1677 0.2565 0.0353  0.0141  0.0059  131 ILE   B N   
6057 C  CA  . ILE   B 131 ? 0.2027 0.1859 0.2539 0.0306  0.0047  0.0199  131 ILE   B CA  
6058 C  C   . ILE   B 131 ? 0.2132 0.1752 0.2219 0.0214  -0.0003 0.0249  131 ILE   B C   
6059 O  O   . ILE   B 131 ? 0.2383 0.1883 0.2301 0.0233  -0.0201 0.0192  131 ILE   B O   
6060 C  CB  . ILE   B 131 ? 0.1981 0.2178 0.2962 0.0279  -0.0019 0.0310  131 ILE   B CB  
6061 C  CG1 . ILE   B 131 ? 0.2039 0.2383 0.3124 0.0042  0.0080  0.0374  131 ILE   B CG1 
6062 C  CG2 . ILE   B 131 ? 0.1946 0.2332 0.3175 0.0324  0.0023  0.0218  131 ILE   B CG2 
6063 C  CD1 . ILE   B 131 ? 0.2114 0.2583 0.3311 -0.0148 0.0038  0.0402  131 ILE   B CD1 
6075 N  N   . PHE   B 132 ? 0.1977 0.1556 0.2077 0.0188  0.0155  0.0279  132 PHE   B N   
6076 C  CA  . PHE   B 132 ? 0.2082 0.1572 0.2095 0.0120  0.0367  0.0187  132 PHE   B CA  
6077 C  C   . PHE   B 132 ? 0.2273 0.1712 0.2287 0.0119  0.0457  0.0175  132 PHE   B C   
6078 O  O   . PHE   B 132 ? 0.2450 0.1930 0.2536 0.0073  0.0543  0.0206  132 PHE   B O   
6079 C  CB  . PHE   B 132 ? 0.1926 0.1529 0.1902 0.0123  0.0391  0.0229  132 PHE   B CB  
6080 C  CG  . PHE   B 132 ? 0.1844 0.1527 0.1889 0.0154  0.0341  0.0198  132 PHE   B CG  
6081 C  CD1 . PHE   B 132 ? 0.1883 0.1536 0.2229 0.0176  0.0268  0.0187  132 PHE   B CD1 
6082 C  CD2 . PHE   B 132 ? 0.1823 0.1609 0.1684 0.0247  0.0277  0.0231  132 PHE   B CD2 
6083 C  CE1 . PHE   B 132 ? 0.1941 0.1593 0.2275 0.0107  0.0183  0.0154  132 PHE   B CE1 
6084 C  CE2 . PHE   B 132 ? 0.1903 0.1670 0.1675 0.0245  0.0146  0.0176  132 PHE   B CE2 
6085 C  CZ  . PHE   B 132 ? 0.1927 0.1626 0.2028 0.0109  -0.0001 0.0233  132 PHE   B CZ  
6095 N  N   . GLY   B 133 ? 0.2248 0.1591 0.2304 0.0071  0.0283  0.0394  133 GLY   B N   
6096 C  CA  . GLY   B 133 ? 0.2351 0.1735 0.2457 -0.0120 0.0251  0.0450  133 GLY   B CA  
6097 C  C   . GLY   B 133 ? 0.2378 0.1796 0.2522 -0.0247 0.0305  0.0471  133 GLY   B C   
6098 O  O   . GLY   B 133 ? 0.2567 0.1945 0.2924 -0.0368 0.0352  0.0592  133 GLY   B O   
6102 N  N   . ALA   B 134 ? 0.2180 0.1723 0.2400 -0.0235 0.0320  0.0288  134 ALA   B N   
6103 C  CA  . ALA   B 134 ? 0.2093 0.1737 0.2508 -0.0175 0.0384  0.0166  134 ALA   B CA  
6104 C  C   . ALA   B 134 ? 0.2158 0.1663 0.2610 -0.0100 0.0385  0.0314  134 ALA   B C   
6105 O  O   . ALA   B 134 ? 0.2185 0.1842 0.2723 0.0047  0.0282  0.0224  134 ALA   B O   
6106 C  CB  . ALA   B 134 ? 0.2081 0.1776 0.2698 -0.0132 0.0279  0.0084  134 ALA   B CB  
6112 N  N   . ASP   B 135 ? 0.2285 0.1643 0.2604 -0.0169 0.0243  0.0427  135 ASP   B N   
6113 C  CA  . ASP   B 135 ? 0.2418 0.1592 0.2772 -0.0166 0.0093  0.0402  135 ASP   B CA  
6114 C  C   . ASP   B 135 ? 0.2231 0.1491 0.2586 -0.0060 0.0078  0.0341  135 ASP   B C   
6115 O  O   . ASP   B 135 ? 0.2148 0.1397 0.2619 -0.0073 0.0058  0.0270  135 ASP   B O   
6116 C  CB  . ASP   B 135 ? 0.2688 0.1668 0.3072 -0.0343 0.0007  0.0445  135 ASP   B CB  
6117 C  CG  . ASP   B 135 ? 0.2953 0.1655 0.3509 -0.0542 -0.0015 0.0375  135 ASP   B CG  
6118 O  OD1 . ASP   B 135 ? 0.2997 0.1492 0.3515 -0.0393 -0.0100 0.0361  135 ASP   B OD1 
6119 O  OD2 . ASP   B 135 ? 0.3163 0.1992 0.3968 -0.0713 -0.0004 0.0158  135 ASP   B OD2 
6124 N  N   . PRO   B 136 ? 0.2167 0.1494 0.2647 0.0134  -0.0084 0.0300  136 PRO   B N   
6125 C  CA  . PRO   B 136 ? 0.1957 0.1396 0.2667 0.0074  -0.0092 0.0132  136 PRO   B CA  
6126 C  C   . PRO   B 136 ? 0.1765 0.1273 0.2810 0.0077  0.0001  0.0103  136 PRO   B C   
6127 O  O   . PRO   B 136 ? 0.1619 0.1264 0.2771 0.0066  0.0060  0.0123  136 PRO   B O   
6128 C  CB  . PRO   B 136 ? 0.2037 0.1616 0.2759 0.0219  -0.0155 0.0082  136 PRO   B CB  
6129 C  CG  . PRO   B 136 ? 0.2199 0.1703 0.2953 0.0276  -0.0088 0.0117  136 PRO   B CG  
6130 C  CD  . PRO   B 136 ? 0.2233 0.1648 0.2854 0.0347  -0.0056 0.0199  136 PRO   B CD  
6138 N  N   . ILE   B 137 ? 0.1864 0.1248 0.2906 0.0069  -0.0039 0.0109  137 ILE   B N   
6139 C  CA  . ILE   B 137 ? 0.1924 0.1211 0.2968 0.0000  0.0015  0.0087  137 ILE   B CA  
6140 C  C   . ILE   B 137 ? 0.1857 0.1283 0.2892 -0.0062 0.0138  0.0162  137 ILE   B C   
6141 O  O   . ILE   B 137 ? 0.1745 0.1291 0.2788 -0.0121 0.0095  0.0119  137 ILE   B O   
6142 C  CB  . ILE   B 137 ? 0.2185 0.1273 0.3467 -0.0047 -0.0014 0.0101  137 ILE   B CB  
6143 C  CG1 . ILE   B 137 ? 0.2443 0.1460 0.3918 0.0079  0.0095  0.0011  137 ILE   B CG1 
6144 C  CG2 . ILE   B 137 ? 0.2269 0.1323 0.3651 -0.0261 -0.0045 0.0096  137 ILE   B CG2 
6145 C  CD1 . ILE   B 137 ? 0.2643 0.1732 0.4280 0.0218  0.0066  0.0052  137 ILE   B CD1 
6157 N  N   . HIS   B 138 ? 0.1917 0.1255 0.2917 -0.0066 0.0294  0.0245  138 HIS   B N   
6158 C  CA  . HIS   B 138 ? 0.2003 0.1360 0.2872 -0.0062 0.0404  0.0223  138 HIS   B CA  
6159 C  C   . HIS   B 138 ? 0.1785 0.1328 0.2674 -0.0055 0.0337  0.0274  138 HIS   B C   
6160 O  O   . HIS   B 138 ? 0.1676 0.1328 0.2913 0.0002  0.0367  0.0365  138 HIS   B O   
6161 C  CB  . HIS   B 138 ? 0.2279 0.1494 0.2930 -0.0073 0.0598  0.0201  138 HIS   B CB  
6162 C  CG  . HIS   B 138 ? 0.2502 0.1672 0.2940 -0.0083 0.0795  0.0413  138 HIS   B CG  
6163 N  ND1 . HIS   B 138 ? 0.2583 0.1848 0.3198 -0.0036 0.0895  0.0310  138 HIS   B ND1 
6164 C  CD2 . HIS   B 138 ? 0.2680 0.1796 0.2921 -0.0062 0.0838  0.0384  138 HIS   B CD2 
6165 C  CE1 . HIS   B 138 ? 0.2648 0.1869 0.3161 -0.0019 0.0957  0.0346  138 HIS   B CE1 
6166 N  NE2 . HIS   B 138 ? 0.2729 0.1774 0.2971 0.0025  0.0930  0.0322  138 HIS   B NE2 
6174 N  N   . SER   B 139 ? 0.1743 0.1263 0.2587 -0.0001 0.0288  0.0244  139 SER   B N   
6175 C  CA  . SER   B 139 ? 0.1706 0.1181 0.2417 -0.0016 0.0253  0.0127  139 SER   B CA  
6176 C  C   . SER   B 139 ? 0.1494 0.1105 0.2397 -0.0031 0.0199  0.0107  139 SER   B C   
6177 O  O   . SER   B 139 ? 0.1494 0.1151 0.2377 0.0016  0.0106  0.0125  139 SER   B O   
6178 C  CB  . SER   B 139 ? 0.1783 0.1217 0.2351 0.0051  0.0076  0.0110  139 SER   B CB  
6179 O  OG  . SER   B 139 ? 0.1775 0.1206 0.2349 -0.0015 -0.0066 0.0165  139 SER   B OG  
6185 N  N   . LEU   B 140 ? 0.1485 0.1080 0.2397 -0.0056 0.0181  0.0044  140 LEU   B N   
6186 C  CA  . LEU   B 140 ? 0.1444 0.1092 0.2375 0.0015  0.0146  0.0030  140 LEU   B CA  
6187 C  C   . LEU   B 140 ? 0.1408 0.1125 0.2488 -0.0003 0.0039  -0.0013 140 LEU   B C   
6188 O  O   . LEU   B 140 ? 0.1395 0.1173 0.2364 -0.0024 0.0004  0.0059  140 LEU   B O   
6189 C  CB  . LEU   B 140 ? 0.1405 0.1158 0.2375 -0.0095 0.0198  -0.0066 140 LEU   B CB  
6190 C  CG  . LEU   B 140 ? 0.1480 0.1178 0.2394 -0.0086 0.0050  0.0010  140 LEU   B CG  
6191 C  CD1 . LEU   B 140 ? 0.1605 0.1276 0.2584 -0.0103 0.0165  -0.0032 140 LEU   B CD1 
6192 C  CD2 . LEU   B 140 ? 0.1642 0.1273 0.2568 -0.0080 0.0039  -0.0046 140 LEU   B CD2 
6204 N  N   . ARG   B 141 ? 0.1335 0.1106 0.2659 -0.0097 0.0094  -0.0051 141 ARG   B N   
6205 C  CA  . ARG   B 141 ? 0.1387 0.1163 0.2986 -0.0147 0.0289  -0.0034 141 ARG   B CA  
6206 C  C   . ARG   B 141 ? 0.1345 0.1146 0.2870 -0.0111 0.0157  -0.0032 141 ARG   B C   
6207 O  O   . ARG   B 141 ? 0.1331 0.1185 0.2937 -0.0143 0.0052  -0.0068 141 ARG   B O   
6208 C  CB  . ARG   B 141 ? 0.1581 0.1325 0.3193 -0.0143 0.0402  0.0000  141 ARG   B CB  
6209 C  CG  . ARG   B 141 ? 0.1900 0.1560 0.3315 -0.0134 0.0363  -0.0031 141 ARG   B CG  
6210 C  CD  . ARG   B 141 ? 0.2216 0.1778 0.3343 -0.0075 0.0184  -0.0202 141 ARG   B CD  
6211 N  NE  . ARG   B 141 ? 0.2434 0.1771 0.3360 -0.0254 0.0212  -0.0233 141 ARG   B NE  
6212 C  CZ  . ARG   B 141 ? 0.2554 0.1588 0.3251 -0.0249 0.0365  -0.0295 141 ARG   B CZ  
6213 N  NH1 . ARG   B 141 ? 0.2656 0.1533 0.3165 -0.0261 0.0336  -0.0322 141 ARG   B NH1 
6214 N  NH2 . ARG   B 141 ? 0.2630 0.1692 0.3331 -0.0091 0.0233  -0.0211 141 ARG   B NH2 
6228 N  N   . VAL   B 142 ? 0.1400 0.1096 0.2678 -0.0081 0.0202  -0.0009 142 VAL   B N   
6229 C  CA  . VAL   B 142 ? 0.1364 0.1140 0.2601 -0.0071 0.0254  -0.0056 142 VAL   B CA  
6230 C  C   . VAL   B 142 ? 0.1334 0.1128 0.2629 -0.0049 0.0146  -0.0024 142 VAL   B C   
6231 O  O   . VAL   B 142 ? 0.1380 0.1118 0.2669 0.0016  0.0132  0.0021  142 VAL   B O   
6232 C  CB  . VAL   B 142 ? 0.1467 0.1267 0.2590 0.0011  0.0275  0.0105  142 VAL   B CB  
6233 C  CG1 . VAL   B 142 ? 0.1463 0.1256 0.2622 0.0048  0.0277  0.0061  142 VAL   B CG1 
6234 C  CG2 . VAL   B 142 ? 0.1636 0.1304 0.2657 0.0039  0.0222  0.0165  142 VAL   B CG2 
6244 N  N   . CYS   B 143 ? 0.1292 0.1133 0.2429 0.0014  0.0133  0.0078  143 CYS   B N   
6245 C  CA  . CYS   B 143 ? 0.1250 0.1165 0.2440 -0.0072 0.0037  0.0048  143 CYS   B CA  
6246 C  C   . CYS   B 143 ? 0.1194 0.1204 0.2418 -0.0069 0.0110  -0.0026 143 CYS   B C   
6247 O  O   . CYS   B 143 ? 0.1268 0.1240 0.2454 -0.0024 0.0036  -0.0013 143 CYS   B O   
6248 C  CB  . CYS   B 143 ? 0.1328 0.1256 0.2389 -0.0027 0.0053  0.0043  143 CYS   B CB  
6249 S  SG  . CYS   B 143 ? 0.1344 0.1399 0.2262 -0.0049 0.0069  0.0046  143 CYS   B SG  
6255 N  N   . VAL   B 144 ? 0.1275 0.1162 0.2573 -0.0109 0.0047  -0.0126 144 VAL   B N   
6256 C  CA  . VAL   B 144 ? 0.1329 0.1244 0.2808 -0.0169 -0.0003 -0.0180 144 VAL   B CA  
6257 C  C   . VAL   B 144 ? 0.1282 0.1276 0.2840 -0.0095 -0.0016 -0.0013 144 VAL   B C   
6258 O  O   . VAL   B 144 ? 0.1406 0.1481 0.3047 0.0006  -0.0050 0.0183  144 VAL   B O   
6259 C  CB  . VAL   B 144 ? 0.1561 0.1382 0.3357 -0.0185 -0.0130 -0.0305 144 VAL   B CB  
6260 C  CG1 . VAL   B 144 ? 0.1821 0.1767 0.3639 -0.0070 -0.0150 -0.0229 144 VAL   B CG1 
6261 C  CG2 . VAL   B 144 ? 0.1638 0.1417 0.3337 -0.0033 -0.0309 -0.0310 144 VAL   B CG2 
6271 N  N   . ASP   B 145 ? 0.1304 0.1178 0.2939 -0.0093 0.0006  -0.0164 145 ASP   B N   
6272 C  CA  . ASP   B 145 ? 0.1302 0.1231 0.3104 -0.0102 0.0076  -0.0113 145 ASP   B CA  
6273 C  C   . ASP   B 145 ? 0.1296 0.1260 0.2997 -0.0063 0.0068  -0.0095 145 ASP   B C   
6274 O  O   . ASP   B 145 ? 0.1308 0.1422 0.3486 -0.0128 0.0155  -0.0267 145 ASP   B O   
6275 C  CB  . ASP   B 145 ? 0.1441 0.1371 0.3509 -0.0134 0.0230  -0.0018 145 ASP   B CB  
6276 C  CG  . ASP   B 145 ? 0.1580 0.1383 0.3910 -0.0220 0.0313  -0.0050 145 ASP   B CG  
6277 O  OD1 . ASP   B 145 ? 0.1573 0.1411 0.3936 -0.0197 -0.0028 -0.0118 145 ASP   B OD1 
6278 O  OD2 . ASP   B 145 ? 0.1895 0.1464 0.4292 -0.0256 0.0575  0.0008  145 ASP   B OD2 
6283 N  N   . THR   B 146 ? 0.1252 0.1156 0.2505 -0.0071 0.0011  0.0046  146 THR   B N   
6284 C  CA  . THR   B 146 ? 0.1297 0.1184 0.2255 -0.0082 0.0083  0.0053  146 THR   B CA  
6285 C  C   . THR   B 146 ? 0.1279 0.1178 0.2228 -0.0051 0.0027  0.0044  146 THR   B C   
6286 O  O   . THR   B 146 ? 0.1319 0.1187 0.2242 -0.0037 0.0089  0.0014  146 THR   B O   
6287 C  CB  . THR   B 146 ? 0.1375 0.1147 0.2279 -0.0054 0.0173  0.0062  146 THR   B CB  
6288 O  OG1 . THR   B 146 ? 0.1435 0.1174 0.2300 -0.0098 0.0234  0.0079  146 THR   B OG1 
6289 C  CG2 . THR   B 146 ? 0.1443 0.1197 0.2260 -0.0042 0.0141  0.0021  146 THR   B CG2 
6297 N  N   . VAL   B 147 ? 0.1323 0.1169 0.2117 -0.0040 0.0138  0.0034  147 VAL   B N   
6298 C  CA  . VAL   B 147 ? 0.1317 0.1150 0.2003 -0.0121 -0.0007 -0.0011 147 VAL   B CA  
6299 C  C   . VAL   B 147 ? 0.1304 0.1178 0.2105 -0.0158 -0.0022 -0.0070 147 VAL   B C   
6300 O  O   . VAL   B 147 ? 0.1432 0.1285 0.2209 -0.0204 -0.0283 -0.0110 147 VAL   B O   
6301 C  CB  . VAL   B 147 ? 0.1368 0.1295 0.1896 -0.0079 -0.0080 0.0013  147 VAL   B CB  
6302 C  CG1 . VAL   B 147 ? 0.1289 0.1439 0.1781 -0.0153 -0.0063 0.0024  147 VAL   B CG1 
6303 C  CG2 . VAL   B 147 ? 0.1417 0.1314 0.1903 -0.0078 0.0024  0.0036  147 VAL   B CG2 
6313 N  N   . ARG   B 148 ? 0.1318 0.1163 0.2057 -0.0069 -0.0174 -0.0104 148 ARG   B N   
6314 C  CA  . ARG   B 148 ? 0.1340 0.1310 0.1974 -0.0093 -0.0241 -0.0112 148 ARG   B CA  
6315 C  C   . ARG   B 148 ? 0.1374 0.1395 0.1754 -0.0112 -0.0198 -0.0068 148 ARG   B C   
6316 O  O   . ARG   B 148 ? 0.1551 0.1726 0.1882 -0.0269 -0.0285 -0.0024 148 ARG   B O   
6317 C  CB  . ARG   B 148 ? 0.1371 0.1327 0.2090 -0.0025 -0.0309 -0.0145 148 ARG   B CB  
6318 C  CG  . ARG   B 148 ? 0.1373 0.1523 0.2246 -0.0120 -0.0219 -0.0281 148 ARG   B CG  
6319 C  CD  . ARG   B 148 ? 0.1411 0.1677 0.2399 0.0090  -0.0245 -0.0294 148 ARG   B CD  
6320 N  NE  . ARG   B 148 ? 0.1466 0.1629 0.2305 0.0245  -0.0212 -0.0275 148 ARG   B NE  
6321 C  CZ  . ARG   B 148 ? 0.1419 0.1543 0.2113 0.0168  -0.0101 -0.0156 148 ARG   B CZ  
6322 N  NH1 . ARG   B 148 ? 0.1388 0.1598 0.2054 -0.0022 0.0037  -0.0122 148 ARG   B NH1 
6323 N  NH2 . ARG   B 148 ? 0.1647 0.1451 0.2053 0.0141  -0.0093 -0.0053 148 ARG   B NH2 
6337 N  N   . THR   B 149 ? 0.1399 0.1349 0.1750 -0.0140 -0.0218 0.0029  149 THR   B N   
6338 C  CA  . THR   B 149 ? 0.1464 0.1370 0.1759 -0.0147 -0.0190 0.0062  149 THR   B CA  
6339 C  C   . THR   B 149 ? 0.1435 0.1327 0.1633 -0.0153 -0.0258 0.0024  149 THR   B C   
6340 O  O   . THR   B 149 ? 0.1506 0.1305 0.1811 -0.0183 -0.0147 -0.0016 149 THR   B O   
6341 C  CB  . THR   B 149 ? 0.1470 0.1305 0.1739 -0.0172 -0.0237 0.0005  149 THR   B CB  
6342 O  OG1 . THR   B 149 ? 0.1475 0.1416 0.1680 -0.0222 -0.0199 0.0006  149 THR   B OG1 
6343 C  CG2 . THR   B 149 ? 0.1545 0.1329 0.1910 -0.0055 -0.0188 0.0004  149 THR   B CG2 
6351 N  N   . ASN   B 150 ? 0.1499 0.1378 0.1620 -0.0168 -0.0293 0.0000  150 ASN   B N   
6352 C  CA  . ASN   B 150 ? 0.1575 0.1487 0.1611 -0.0217 -0.0259 -0.0076 150 ASN   B CA  
6353 C  C   . ASN   B 150 ? 0.1508 0.1426 0.1644 -0.0193 -0.0205 -0.0052 150 ASN   B C   
6354 O  O   . ASN   B 150 ? 0.1596 0.1380 0.1775 -0.0291 -0.0399 0.0005  150 ASN   B O   
6355 C  CB  . ASN   B 150 ? 0.1794 0.1781 0.1749 -0.0240 -0.0287 0.0068  150 ASN   B CB  
6356 C  CG  . ASN   B 150 ? 0.2066 0.2190 0.2132 -0.0226 -0.0328 0.0243  150 ASN   B CG  
6357 O  OD1 . ASN   B 150 ? 0.2100 0.2372 0.2302 -0.0299 -0.0508 0.0254  150 ASN   B OD1 
6358 N  ND2 . ASN   B 150 ? 0.2209 0.2376 0.2515 -0.0120 -0.0414 0.0610  150 ASN   B ND2 
6365 N  N   . VAL   B 151 ? 0.1401 0.1390 0.1673 -0.0181 -0.0282 -0.0036 151 VAL   B N   
6366 C  CA  . VAL   B 151 ? 0.1435 0.1420 0.1687 -0.0216 -0.0190 -0.0025 151 VAL   B CA  
6367 C  C   . VAL   B 151 ? 0.1460 0.1323 0.1617 -0.0301 -0.0249 -0.0009 151 VAL   B C   
6368 O  O   . VAL   B 151 ? 0.1529 0.1404 0.1924 -0.0282 -0.0157 -0.0113 151 VAL   B O   
6369 C  CB  . VAL   B 151 ? 0.1628 0.1552 0.1866 -0.0120 -0.0142 -0.0027 151 VAL   B CB  
6370 C  CG1 . VAL   B 151 ? 0.1718 0.1595 0.2077 -0.0144 0.0033  -0.0056 151 VAL   B CG1 
6371 C  CG2 . VAL   B 151 ? 0.1728 0.1662 0.1730 0.0039  -0.0138 0.0045  151 VAL   B CG2 
6381 N  N   . TYR   B 152 ? 0.1412 0.1236 0.1529 -0.0244 -0.0206 -0.0055 152 TYR   B N   
6382 C  CA  . TYR   B 152 ? 0.1410 0.1408 0.1455 -0.0274 -0.0126 -0.0037 152 TYR   B CA  
6383 C  C   . TYR   B 152 ? 0.1439 0.1272 0.1399 -0.0224 -0.0081 -0.0075 152 TYR   B C   
6384 O  O   . TYR   B 152 ? 0.1508 0.1299 0.1533 -0.0244 -0.0081 -0.0026 152 TYR   B O   
6385 C  CB  . TYR   B 152 ? 0.1551 0.1520 0.1571 -0.0281 -0.0062 0.0097  152 TYR   B CB  
6386 C  CG  . TYR   B 152 ? 0.1727 0.1605 0.1468 -0.0388 -0.0057 0.0065  152 TYR   B CG  
6387 C  CD1 . TYR   B 152 ? 0.1810 0.1752 0.1417 -0.0362 -0.0194 0.0028  152 TYR   B CD1 
6388 C  CD2 . TYR   B 152 ? 0.1900 0.1778 0.1563 -0.0375 -0.0048 -0.0056 152 TYR   B CD2 
6389 C  CE1 . TYR   B 152 ? 0.1979 0.1946 0.1591 -0.0314 -0.0253 0.0157  152 TYR   B CE1 
6390 C  CE2 . TYR   B 152 ? 0.2023 0.1989 0.1541 -0.0373 -0.0154 -0.0132 152 TYR   B CE2 
6391 C  CZ  . TYR   B 152 ? 0.2071 0.2126 0.1435 -0.0355 -0.0334 0.0132  152 TYR   B CZ  
6392 O  OH  . TYR   B 152 ? 0.2315 0.2437 0.1829 -0.0273 -0.0411 0.0179  152 TYR   B OH  
6402 N  N   . LEU   B 153 ? 0.1460 0.1247 0.1436 -0.0311 -0.0146 -0.0043 153 LEU   B N   
6403 C  CA  . LEU   B 153 ? 0.1492 0.1201 0.1420 -0.0252 -0.0051 -0.0062 153 LEU   B CA  
6404 C  C   . LEU   B 153 ? 0.1512 0.1192 0.1551 -0.0270 -0.0048 -0.0115 153 LEU   B C   
6405 O  O   . LEU   B 153 ? 0.1563 0.1403 0.1675 -0.0149 -0.0010 -0.0331 153 LEU   B O   
6406 C  CB  . LEU   B 153 ? 0.1479 0.1171 0.1583 -0.0248 0.0010  -0.0069 153 LEU   B CB  
6407 C  CG  . LEU   B 153 ? 0.1430 0.1288 0.1959 -0.0232 -0.0027 -0.0053 153 LEU   B CG  
6408 C  CD1 . LEU   B 153 ? 0.1504 0.1431 0.2095 -0.0269 0.0027  0.0024  153 LEU   B CD1 
6409 C  CD2 . LEU   B 153 ? 0.1475 0.1398 0.2090 -0.0293 0.0170  -0.0003 153 LEU   B CD2 
6421 N  N   . ALA   B 154 ? 0.1419 0.1240 0.1771 -0.0109 -0.0151 -0.0129 154 ALA   B N   
6422 C  CA  . ALA   B 154 ? 0.1541 0.1357 0.1992 -0.0015 -0.0124 -0.0219 154 ALA   B CA  
6423 C  C   . ALA   B 154 ? 0.1648 0.1369 0.2014 0.0044  -0.0219 -0.0293 154 ALA   B C   
6424 O  O   . ALA   B 154 ? 0.1929 0.1380 0.2126 0.0061  -0.0062 -0.0114 154 ALA   B O   
6425 C  CB  . ALA   B 154 ? 0.1535 0.1480 0.2083 -0.0037 -0.0148 -0.0243 154 ALA   B CB  
6431 N  N   . VAL   B 155 ? 0.1357 0.1273 0.2198 -0.0028 -0.0012 -0.0189 155 VAL   B N   
6432 C  CA  . VAL   B 155 ? 0.1332 0.1247 0.2331 -0.0027 -0.0098 -0.0099 155 VAL   B CA  
6433 C  C   . VAL   B 155 ? 0.1379 0.1271 0.2322 -0.0047 -0.0151 -0.0218 155 VAL   B C   
6434 O  O   . VAL   B 155 ? 0.1527 0.1437 0.2650 -0.0006 -0.0122 -0.0434 155 VAL   B O   
6435 C  CB  . VAL   B 155 ? 0.1361 0.1454 0.2594 -0.0040 -0.0217 0.0008  155 VAL   B CB  
6436 C  CG1 . VAL   B 155 ? 0.1420 0.1445 0.2614 -0.0145 -0.0159 -0.0043 155 VAL   B CG1 
6437 C  CG2 . VAL   B 155 ? 0.1331 0.1542 0.2823 -0.0091 -0.0203 0.0279  155 VAL   B CG2 
6447 N  N   . PHE   B 156 ? 0.1272 0.1331 0.2424 -0.0013 -0.0083 -0.0176 156 PHE   B N   
6448 C  CA  . PHE   B 156 ? 0.1346 0.1396 0.2651 0.0057  -0.0039 -0.0180 156 PHE   B CA  
6449 C  C   . PHE   B 156 ? 0.1306 0.1527 0.2966 0.0139  -0.0102 -0.0339 156 PHE   B C   
6450 O  O   . PHE   B 156 ? 0.1536 0.1754 0.3233 0.0241  0.0023  -0.0424 156 PHE   B O   
6451 C  CB  . PHE   B 156 ? 0.1422 0.1351 0.2659 0.0026  -0.0110 -0.0127 156 PHE   B CB  
6452 C  CG  . PHE   B 156 ? 0.1429 0.1476 0.2777 0.0009  -0.0078 0.0039  156 PHE   B CG  
6453 C  CD1 . PHE   B 156 ? 0.1417 0.1716 0.3110 0.0072  -0.0030 0.0357  156 PHE   B CD1 
6454 C  CD2 . PHE   B 156 ? 0.1483 0.1602 0.2798 0.0096  -0.0159 0.0091  156 PHE   B CD2 
6455 C  CE1 . PHE   B 156 ? 0.1444 0.1826 0.3351 0.0033  -0.0042 0.0373  156 PHE   B CE1 
6456 C  CE2 . PHE   B 156 ? 0.1540 0.1767 0.3052 0.0094  -0.0206 0.0111  156 PHE   B CE2 
6457 C  CZ  . PHE   B 156 ? 0.1457 0.1797 0.3279 0.0124  -0.0202 0.0191  156 PHE   B CZ  
6467 N  N   . ASP   B 157 ? 0.1353 0.1425 0.3127 0.0131  -0.0200 -0.0221 157 ASP   B N   
6468 C  CA  . ASP   B 157 ? 0.1413 0.1520 0.3475 0.0088  -0.0231 -0.0306 157 ASP   B CA  
6469 C  C   . ASP   B 157 ? 0.1430 0.1507 0.3547 0.0062  -0.0203 -0.0466 157 ASP   B C   
6470 O  O   . ASP   B 157 ? 0.1330 0.1510 0.3381 0.0038  -0.0198 -0.0359 157 ASP   B O   
6471 C  CB  . ASP   B 157 ? 0.1672 0.1718 0.3687 -0.0004 -0.0464 -0.0142 157 ASP   B CB  
6472 C  CG  . ASP   B 157 ? 0.1989 0.1836 0.3968 -0.0018 -0.0286 -0.0115 157 ASP   B CG  
6473 O  OD1 . ASP   B 157 ? 0.2096 0.1771 0.4137 0.0068  -0.0259 -0.0118 157 ASP   B OD1 
6474 O  OD2 . ASP   B 157 ? 0.2285 0.2027 0.4215 0.0005  -0.0138 -0.0084 157 ASP   B OD2 
6479 N  N   A LYS   B 158 ? 0.1468 0.1745 0.3726 0.0069  -0.0100 -0.0732 158 LYS   B N   
6480 N  N   B LYS   B 158 ? 0.1589 0.1760 0.3480 0.0094  -0.0113 -0.0585 158 LYS   B N   
6481 C  CA  A LYS   B 158 ? 0.1617 0.1841 0.3809 0.0045  -0.0076 -0.0889 158 LYS   B CA  
6482 C  CA  B LYS   B 158 ? 0.1804 0.1927 0.3410 0.0119  -0.0084 -0.0644 158 LYS   B CA  
6483 C  C   A LYS   B 158 ? 0.1625 0.1677 0.3956 0.0060  -0.0132 -0.0860 158 LYS   B C   
6484 C  C   B LYS   B 158 ? 0.1826 0.1864 0.3424 0.0138  -0.0127 -0.0617 158 LYS   B C   
6485 O  O   A LYS   B 158 ? 0.1617 0.1632 0.4005 -0.0034 -0.0092 -0.0975 158 LYS   B O   
6486 O  O   B LYS   B 158 ? 0.1853 0.1881 0.3379 0.0094  -0.0099 -0.0654 158 LYS   B O   
6487 C  CB  A LYS   B 158 ? 0.1799 0.2207 0.3790 0.0051  -0.0030 -0.0981 158 LYS   B CB  
6488 C  CB  B LYS   B 158 ? 0.2008 0.2190 0.3389 0.0154  -0.0028 -0.0693 158 LYS   B CB  
6489 C  CG  A LYS   B 158 ? 0.2105 0.2539 0.3843 0.0067  0.0019  -0.0993 158 LYS   B CG  
6490 C  CG  B LYS   B 158 ? 0.2248 0.2416 0.3422 0.0176  0.0032  -0.0712 158 LYS   B CG  
6491 C  CD  A LYS   B 158 ? 0.2348 0.2893 0.3954 0.0030  -0.0001 -0.0898 158 LYS   B CD  
6492 C  CD  B LYS   B 158 ? 0.2455 0.2669 0.3518 0.0158  0.0029  -0.0668 158 LYS   B CD  
6493 C  CE  A LYS   B 158 ? 0.2538 0.3139 0.4079 0.0034  -0.0044 -0.0836 158 LYS   B CE  
6494 C  CE  B LYS   B 158 ? 0.2615 0.2841 0.3631 0.0165  0.0017  -0.0633 158 LYS   B CE  
6495 N  NZ  A LYS   B 158 ? 0.2559 0.3230 0.4085 -0.0013 -0.0076 -0.0822 158 LYS   B NZ  
6496 N  NZ  B LYS   B 158 ? 0.2658 0.2916 0.3654 0.0151  0.0022  -0.0626 158 LYS   B NZ  
6523 N  N   A ASN   B 159 ? 0.1657 0.1553 0.4125 0.0080  -0.0253 -0.0689 159 ASN   B N   
6524 N  N   B ASN   B 159 ? 0.1822 0.1791 0.3552 0.0143  -0.0218 -0.0529 159 ASN   B N   
6525 C  CA  A ASN   B 159 ? 0.1773 0.1521 0.4292 0.0141  -0.0390 -0.0538 159 ASN   B CA  
6526 C  CA  B ASN   B 159 ? 0.1843 0.1729 0.3702 0.0178  -0.0305 -0.0443 159 ASN   B CA  
6527 C  C   A ASN   B 159 ? 0.1657 0.1440 0.4195 0.0098  -0.0475 -0.0374 159 ASN   B C   
6528 C  C   B ASN   B 159 ? 0.1700 0.1555 0.3838 0.0146  -0.0388 -0.0367 159 ASN   B C   
6529 O  O   A ASN   B 159 ? 0.1674 0.1340 0.4352 -0.0056 -0.0570 -0.0214 159 ASN   B O   
6530 O  O   B ASN   B 159 ? 0.1711 0.1486 0.3900 0.0114  -0.0414 -0.0260 159 ASN   B O   
6531 C  CB  A ASN   B 159 ? 0.2005 0.1700 0.4626 0.0230  -0.0413 -0.0537 159 ASN   B CB  
6532 C  CB  B ASN   B 159 ? 0.1987 0.1883 0.3778 0.0234  -0.0311 -0.0407 159 ASN   B CB  
6533 C  CG  A ASN   B 159 ? 0.2270 0.1894 0.4896 0.0244  -0.0480 -0.0661 159 ASN   B CG  
6534 C  CG  B ASN   B 159 ? 0.2147 0.2040 0.3867 0.0260  -0.0358 -0.0425 159 ASN   B CG  
6535 O  OD1 A ASN   B 159 ? 0.2429 0.1944 0.4966 0.0253  -0.0496 -0.0742 159 ASN   B OD1 
6536 O  OD1 B ASN   B 159 ? 0.2250 0.2141 0.3890 0.0273  -0.0384 -0.0409 159 ASN   B OD1 
6537 N  ND2 A ASN   B 159 ? 0.2301 0.1967 0.5032 0.0282  -0.0485 -0.0654 159 ASN   B ND2 
6538 N  ND2 B ASN   B 159 ? 0.2164 0.2078 0.3935 0.0305  -0.0362 -0.0417 159 ASN   B ND2 
6551 N  N   . LEU   B 160 ? 0.1551 0.1458 0.3896 0.0094  -0.0448 -0.0354 160 LEU   B N   
6552 C  CA  . LEU   B 160 ? 0.1492 0.1473 0.3585 0.0097  -0.0373 -0.0221 160 LEU   B CA  
6553 C  C   . LEU   B 160 ? 0.1433 0.1332 0.3481 0.0029  -0.0291 -0.0290 160 LEU   B C   
6554 O  O   . LEU   B 160 ? 0.1380 0.1380 0.3410 -0.0015 -0.0240 -0.0189 160 LEU   B O   
6555 C  CB  . LEU   B 160 ? 0.1505 0.1560 0.3367 0.0091  -0.0371 -0.0112 160 LEU   B CB  
6556 C  CG  . LEU   B 160 ? 0.1479 0.1679 0.3156 0.0084  -0.0357 -0.0099 160 LEU   B CG  
6557 C  CD1 . LEU   B 160 ? 0.1630 0.1843 0.3141 -0.0064 -0.0213 -0.0135 160 LEU   B CD1 
6558 C  CD2 . LEU   B 160 ? 0.1522 0.1701 0.3132 0.0174  -0.0404 -0.0198 160 LEU   B CD2 
6571 N  N   . TYR   B 161 ? 0.1384 0.1401 0.3490 -0.0045 -0.0050 -0.0395 161 TYR   B N   
6572 C  CA  . TYR   B 161 ? 0.1472 0.1428 0.3317 -0.0136 0.0091  -0.0459 161 TYR   B CA  
6573 C  C   . TYR   B 161 ? 0.1553 0.1415 0.3195 -0.0075 0.0113  -0.0420 161 TYR   B C   
6574 O  O   . TYR   B 161 ? 0.1576 0.1398 0.3062 -0.0195 0.0058  -0.0373 161 TYR   B O   
6575 C  CB  . TYR   B 161 ? 0.1590 0.1528 0.3242 -0.0205 0.0271  -0.0529 161 TYR   B CB  
6576 C  CG  . TYR   B 161 ? 0.1834 0.1531 0.3146 -0.0277 0.0357  -0.0547 161 TYR   B CG  
6577 C  CD1 . TYR   B 161 ? 0.1887 0.1533 0.3079 -0.0346 0.0448  -0.0520 161 TYR   B CD1 
6578 C  CD2 . TYR   B 161 ? 0.2072 0.1586 0.3043 -0.0293 0.0265  -0.0558 161 TYR   B CD2 
6579 C  CE1 . TYR   B 161 ? 0.2101 0.1722 0.3111 -0.0391 0.0402  -0.0508 161 TYR   B CE1 
6580 C  CE2 . TYR   B 161 ? 0.2300 0.1770 0.3085 -0.0292 0.0317  -0.0543 161 TYR   B CE2 
6581 C  CZ  . TYR   B 161 ? 0.2290 0.1811 0.3083 -0.0445 0.0297  -0.0497 161 TYR   B CZ  
6582 O  OH  . TYR   B 161 ? 0.2591 0.2024 0.3314 -0.0483 0.0306  -0.0451 161 TYR   B OH  
6592 N  N   . ASP   B 162 ? 0.1621 0.1433 0.3354 -0.0050 -0.0027 -0.0580 162 ASP   B N   
6593 C  CA  . ASP   B 162 ? 0.1676 0.1508 0.3434 0.0016  -0.0095 -0.0556 162 ASP   B CA  
6594 C  C   . ASP   B 162 ? 0.1634 0.1378 0.3314 -0.0042 -0.0074 -0.0437 162 ASP   B C   
6595 O  O   . ASP   B 162 ? 0.1710 0.1426 0.3288 -0.0144 -0.0185 -0.0320 162 ASP   B O   
6596 C  CB  . ASP   B 162 ? 0.1845 0.1676 0.3671 0.0034  -0.0136 -0.0818 162 ASP   B CB  
6597 C  CG  . ASP   B 162 ? 0.1902 0.1961 0.3937 0.0095  -0.0099 -0.0988 162 ASP   B CG  
6598 O  OD1 . ASP   B 162 ? 0.1947 0.2174 0.3977 0.0002  0.0087  -0.0908 162 ASP   B OD1 
6599 O  OD2 . ASP   B 162 ? 0.2014 0.2145 0.4197 0.0268  -0.0068 -0.0945 162 ASP   B OD2 
6604 N  N   . LYS   B 163 ? 0.1613 0.1255 0.3266 -0.0062 -0.0250 -0.0269 163 LYS   B N   
6605 C  CA  . LYS   B 163 ? 0.1727 0.1337 0.3264 -0.0120 -0.0232 -0.0047 163 LYS   B CA  
6606 C  C   . LYS   B 163 ? 0.1466 0.1343 0.3161 -0.0149 -0.0186 -0.0045 163 LYS   B C   
6607 O  O   . LYS   B 163 ? 0.1420 0.1428 0.3440 -0.0179 -0.0191 -0.0038 163 LYS   B O   
6608 C  CB  . LYS   B 163 ? 0.2111 0.1625 0.3578 -0.0087 -0.0295 0.0243  163 LYS   B CB  
6609 C  CG  . LYS   B 163 ? 0.2809 0.2322 0.4072 -0.0127 -0.0196 0.0323  163 LYS   B CG  
6610 C  CD  . LYS   B 163 ? 0.3396 0.2953 0.4610 -0.0201 -0.0169 0.0290  163 LYS   B CD  
6611 C  CE  . LYS   B 163 ? 0.3857 0.3407 0.4968 -0.0268 -0.0099 0.0281  163 LYS   B CE  
6612 N  NZ  . LYS   B 163 ? 0.4135 0.3660 0.5181 -0.0305 -0.0065 0.0237  163 LYS   B NZ  
6626 N  N   . LEU   B 164 ? 0.1345 0.1235 0.2907 -0.0132 -0.0186 -0.0049 164 LEU   B N   
6627 C  CA  . LEU   B 164 ? 0.1405 0.1270 0.2727 -0.0154 -0.0240 0.0011  164 LEU   B CA  
6628 C  C   . LEU   B 164 ? 0.1441 0.1284 0.2758 -0.0181 -0.0302 0.0034  164 LEU   B C   
6629 O  O   . LEU   B 164 ? 0.1443 0.1465 0.2961 -0.0163 -0.0271 0.0017  164 LEU   B O   
6630 C  CB  . LEU   B 164 ? 0.1337 0.1261 0.2625 -0.0108 -0.0225 -0.0044 164 LEU   B CB  
6631 C  CG  . LEU   B 164 ? 0.1437 0.1407 0.2652 -0.0107 -0.0096 -0.0001 164 LEU   B CG  
6632 C  CD1 . LEU   B 164 ? 0.1484 0.1377 0.2652 -0.0105 -0.0177 -0.0105 164 LEU   B CD1 
6633 C  CD2 . LEU   B 164 ? 0.1603 0.1722 0.2736 -0.0094 0.0002  -0.0139 164 LEU   B CD2 
6645 N  N   . VAL   B 165 ? 0.1731 0.1398 0.2885 -0.0240 -0.0324 -0.0076 165 VAL   B N   
6646 C  CA  . VAL   B 165 ? 0.2102 0.1529 0.2955 -0.0328 -0.0511 -0.0062 165 VAL   B CA  
6647 C  C   . VAL   B 165 ? 0.2387 0.1623 0.3281 -0.0419 -0.0757 -0.0114 165 VAL   B C   
6648 O  O   . VAL   B 165 ? 0.2576 0.1783 0.3374 -0.0481 -0.0817 -0.0002 165 VAL   B O   
6649 C  CB  . VAL   B 165 ? 0.2295 0.1670 0.2974 -0.0170 -0.0278 -0.0134 165 VAL   B CB  
6650 C  CG1 . VAL   B 165 ? 0.2454 0.1756 0.3160 -0.0149 -0.0174 -0.0103 165 VAL   B CG1 
6651 C  CG2 . VAL   B 165 ? 0.2230 0.1657 0.2898 -0.0128 -0.0158 -0.0058 165 VAL   B CG2 
6661 N  N   . SER   B 166 ? 0.2444 0.1506 0.3680 -0.0390 -0.0837 -0.0269 166 SER   B N   
6662 C  CA  . SER   B 166 ? 0.2422 0.1506 0.4197 -0.0382 -0.0744 -0.0342 166 SER   B CA  
6663 C  C   . SER   B 166 ? 0.2277 0.1643 0.4370 -0.0434 -0.0747 -0.0064 166 SER   B C   
6664 O  O   . SER   B 166 ? 0.2349 0.1872 0.4652 -0.0577 -0.0873 -0.0236 166 SER   B O   
6665 C  CB  . SER   B 166 ? 0.2413 0.1613 0.4447 -0.0280 -0.0723 -0.0466 166 SER   B CB  
6666 O  OG  . SER   B 166 ? 0.2290 0.1632 0.4637 -0.0220 -0.0733 -0.0304 166 SER   B OG  
6672 N  N   . SER   B 167 ? 0.2062 0.1607 0.4157 -0.0420 -0.0745 0.0320  167 SER   B N   
6673 C  CA  . SER   B 167 ? 0.1945 0.1636 0.3879 -0.0347 -0.0568 0.0322  167 SER   B CA  
6674 C  C   . SER   B 167 ? 0.1876 0.1696 0.3548 -0.0504 -0.0492 0.0457  167 SER   B C   
6675 O  O   . SER   B 167 ? 0.1883 0.1821 0.3447 -0.0592 -0.0465 0.0452  167 SER   B O   
6676 C  CB  . SER   B 167 ? 0.1869 0.1717 0.3885 -0.0257 -0.0278 0.0299  167 SER   B CB  
6677 O  OG  . SER   B 167 ? 0.1768 0.1803 0.3746 -0.0163 -0.0113 0.0274  167 SER   B OG  
6683 N  N   . PHE   B 168 ? 0.1903 0.1660 0.3444 -0.0450 -0.0364 0.0526  168 PHE   B N   
6684 C  CA  . PHE   B 168 ? 0.1946 0.1647 0.3188 -0.0449 -0.0287 0.0319  168 PHE   B CA  
6685 C  C   . PHE   B 168 ? 0.1665 0.1518 0.2728 -0.0243 -0.0083 0.0168  168 PHE   B C   
6686 O  O   . PHE   B 168 ? 0.1929 0.1438 0.2738 -0.0001 -0.0099 0.0025  168 PHE   B O   
6687 C  CB  . PHE   B 168 ? 0.2106 0.1710 0.3228 -0.0528 -0.0417 0.0452  168 PHE   B CB  
6688 C  CG  . PHE   B 168 ? 0.2336 0.1578 0.3130 -0.0512 -0.0404 0.0250  168 PHE   B CG  
6689 C  CD1 . PHE   B 168 ? 0.2644 0.1624 0.3260 -0.0421 -0.0479 0.0215  168 PHE   B CD1 
6690 C  CD2 . PHE   B 168 ? 0.2191 0.1478 0.3081 -0.0451 -0.0394 0.0246  168 PHE   B CD2 
6691 C  CE1 . PHE   B 168 ? 0.2736 0.1720 0.3264 -0.0320 -0.0420 0.0233  168 PHE   B CE1 
6692 C  CE2 . PHE   B 168 ? 0.2461 0.1547 0.3169 -0.0291 -0.0476 0.0188  168 PHE   B CE2 
6693 C  CZ  . PHE   B 168 ? 0.2602 0.1537 0.3187 -0.0188 -0.0510 0.0292  168 PHE   B CZ  
6703 N  N   . LEU   B 169 ? 0.1755 0.1668 0.2672 -0.0039 0.0022  -0.0012 169 LEU   B N   
6704 C  CA  . LEU   B 169 ? 0.1990 0.1969 0.2932 -0.0108 0.0078  -0.0258 169 LEU   B CA  
6705 C  C   . LEU   B 169 ? 0.2270 0.2247 0.3416 0.0058  0.0001  -0.0488 169 LEU   B C   
6706 O  O   . LEU   B 169 ? 0.2474 0.2441 0.3884 0.0071  -0.0042 -0.0707 169 LEU   B O   
6707 C  CB  . LEU   B 169 ? 0.2146 0.2344 0.3045 -0.0184 0.0073  -0.0001 169 LEU   B CB  
6708 C  CG  . LEU   B 169 ? 0.2508 0.2708 0.3411 -0.0074 0.0064  0.0067  169 LEU   B CG  
6709 C  CD1 . LEU   B 169 ? 0.2676 0.2892 0.3466 -0.0059 0.0008  0.0208  169 LEU   B CD1 
6710 C  CD2 . LEU   B 169 ? 0.2420 0.2790 0.3413 0.0063  0.0213  -0.0037 169 LEU   B CD2 
6711 O  OXT . LEU   B 169 ? 0.2447 0.2417 0.3387 0.0350  0.0116  -0.0456 169 LEU   B OXT 
6723 C  C1  T TFA   C .   ? 0.1351 0.1462 0.1366 -0.0034 0.0192  0.0142  201 TFA   A C1  
6724 C  C2  T TFA   C .   ? 0.1626 0.1725 0.1797 -0.0179 0.0132  -0.0010 201 TFA   A C2  
6725 O  O   T TFA   C .   ? 0.1106 0.1279 0.1170 -0.0036 0.0160  0.0173  201 TFA   A O   
6726 F  F1  T TFA   C .   ? 0.1702 0.1770 0.2148 -0.0229 0.0057  -0.0025 201 TFA   A F1  
6727 F  F2  T TFA   C .   ? 0.1742 0.1785 0.1707 -0.0221 0.0188  -0.0076 201 TFA   A F2  
6728 F  F3  T TFA   C .   ? 0.1758 0.1928 0.2043 -0.0271 0.0192  -0.0072 201 TFA   A F3  
6729 O  OXT T TFA   C .   ? 0.1285 0.1396 0.1341 0.0138  0.0260  0.0125  201 TFA   A OXT 
6730 N  N2  B A1A9R D .   ? 0.1178 0.1288 0.1202 -0.0106 -0.0028 0.0104  202 A1A9R A N2  
6731 C  C3  B A1A9R D .   ? 0.1530 0.1637 0.1765 0.0033  -0.0080 0.0014  202 A1A9R A C3  
6732 C  C6  B A1A9R D .   ? 0.1778 0.1698 0.1778 0.0042  -0.0114 0.0195  202 A1A9R A C6  
6733 C  C9  B A1A9R D .   ? 0.1106 0.1228 0.1359 -0.0038 -0.0047 0.0262  202 A1A9R A C9  
6734 C  C12 B A1A9R D .   ? 0.1010 0.1204 0.1507 -0.0099 -0.0170 0.0222  202 A1A9R A C12 
6735 C  C1  B A1A9R D .   ? 0.1388 0.1450 0.1914 0.0034  0.0032  -0.0099 202 A1A9R A C1  
6736 C  C10 B A1A9R D .   ? 0.1079 0.1311 0.1316 -0.0061 -0.0067 0.0235  202 A1A9R A C10 
6737 C  C11 B A1A9R D .   ? 0.1031 0.1320 0.1416 -0.0015 -0.0066 0.0224  202 A1A9R A C11 
6738 C  C2  B A1A9R D .   ? 0.1341 0.1435 0.1577 -0.0015 0.0020  0.0027  202 A1A9R A C2  
6739 C  C4  B A1A9R D .   ? 0.1660 0.1664 0.1877 0.0080  -0.0152 0.0046  202 A1A9R A C4  
6740 C  C5  B A1A9R D .   ? 0.1800 0.1692 0.1691 0.0098  -0.0119 0.0178  202 A1A9R A C5  
6741 C  C7  B A1A9R D .   ? 0.1167 0.1335 0.1164 -0.0055 -0.0061 0.0166  202 A1A9R A C7  
6742 C  C8  B A1A9R D .   ? 0.1232 0.1324 0.1312 -0.0006 0.0022  0.0197  202 A1A9R A C8  
6743 N  N1  B A1A9R D .   ? 0.1758 0.1744 0.1815 0.0139  -0.0201 0.0067  202 A1A9R A N1  
6744 N  N3  B A1A9R D .   ? 0.1220 0.1314 0.1229 -0.0054 -0.0081 0.0128  202 A1A9R A N3  
6745 N  N4  B A1A9R D .   ? 0.1200 0.1312 0.1335 -0.0051 0.0036  0.0302  202 A1A9R A N4  
6746 N  N5  B A1A9R D .   ? 0.1074 0.1149 0.1386 -0.0010 -0.0162 0.0295  202 A1A9R A N5  
6747 O  O1  B A1A9R D .   ? 0.1381 0.1485 0.2065 0.0001  0.0044  -0.0053 202 A1A9R A O1  
6748 S  S1  B A1A9R D .   ? 0.1708 0.1616 0.2015 0.0110  -0.0097 0.0104  202 A1A9R A S1  
6762 CL CL  B CL    E .   ? 0.1410 0.1282 0.2548 -0.0088 -0.0147 0.0031  203 CL    A CL  
6763 O  O   . HOH   F .   ? 0.2496 0.2113 0.3776 -0.0206 -0.0117 0.0674  301 HOH   A O   
6764 O  O   . HOH   F .   ? 0.4036 0.8889 0.4287 -0.1114 0.0398  0.1123  302 HOH   A O   
6765 O  O   . HOH   F .   ? 0.7637 0.6621 0.4521 -0.1582 -0.1029 0.2433  303 HOH   A O   
6766 O  O   . HOH   F .   ? 0.5893 0.5304 0.2994 0.2158  -0.1263 0.0428  304 HOH   A O   
6767 O  O   . HOH   F .   ? 0.2989 0.3114 0.1631 -0.0283 0.0391  0.0376  305 HOH   A O   
6768 O  O   . HOH   F .   ? 0.3067 0.6364 0.6371 -0.0631 -0.0908 0.2561  306 HOH   A O   
6769 O  O   . HOH   F .   ? 0.6190 0.4316 0.5020 -0.0909 0.1829  0.0921  307 HOH   A O   
6770 O  O   . HOH   F .   ? 0.4942 0.3311 0.3855 -0.0369 0.0880  0.0012  308 HOH   A O   
6771 O  O   . HOH   F .   ? 0.7648 0.5537 0.3485 -0.0664 -0.0062 0.1116  309 HOH   A O   
6772 O  O   B HOH   F .   ? 0.2913 0.4542 0.4056 0.0695  -0.0133 0.0497  310 HOH   A O   
6773 O  O   . HOH   F .   ? 0.6166 0.6589 0.4482 -0.1186 -0.1154 -0.1070 311 HOH   A O   
6774 O  O   . HOH   F .   ? 0.3050 0.3397 0.3060 -0.0952 -0.0101 0.1123  312 HOH   A O   
6775 O  O   . HOH   F .   ? 0.1611 0.1587 0.2006 0.0168  -0.0256 0.0277  313 HOH   A O   
6776 O  O   . HOH   F .   ? 0.1469 0.3749 0.2318 -0.0072 0.0256  0.0348  314 HOH   A O   
6777 O  O   . HOH   F .   ? 0.3011 0.3666 0.2954 -0.1357 0.0734  -0.0145 315 HOH   A O   
6778 O  O   . HOH   F .   ? 0.6632 0.4262 0.3968 -0.1263 -0.0966 0.0653  316 HOH   A O   
6779 O  O   . HOH   F .   ? 0.1983 0.1835 0.3682 -0.0431 0.0045  -0.0219 317 HOH   A O   
6780 O  O   . HOH   F .   ? 0.2344 0.4790 0.3740 -0.0028 -0.0567 0.0625  318 HOH   A O   
6781 O  O   A HOH   F .   ? 0.1987 0.4727 0.5543 0.0586  0.0459  0.1177  319 HOH   A O   
6782 O  O   . HOH   F .   ? 0.1722 0.2637 0.2867 0.0302  -0.0180 -0.0265 320 HOH   A O   
6783 O  O   B HOH   F .   ? 0.2385 0.1277 0.1711 0.0393  -0.0244 0.0213  321 HOH   A O   
6784 O  O   . HOH   F .   ? 0.3998 0.4100 0.3673 -0.0913 0.1834  0.0217  322 HOH   A O   
6785 O  O   . HOH   F .   ? 0.4503 0.1819 0.5313 0.0479  0.0322  0.0128  323 HOH   A O   
6786 O  O   . HOH   F .   ? 0.1590 0.1675 0.2127 -0.0180 0.0124  0.0397  324 HOH   A O   
6787 O  O   . HOH   F .   ? 0.3567 0.3699 0.2032 -0.0520 -0.0948 0.0415  325 HOH   A O   
6788 O  O   A HOH   F .   ? 0.1734 0.1930 0.1787 -0.0340 0.0298  0.0326  326 HOH   A O   
6789 O  O   . HOH   F .   ? 0.5851 0.4810 0.4491 -0.0365 0.1457  0.2305  327 HOH   A O   
6790 O  O   B HOH   F .   ? 0.1839 0.1961 0.2779 0.0181  0.0205  0.1070  328 HOH   A O   
6791 O  O   . HOH   F .   ? 0.2908 0.2579 0.4507 -0.0347 -0.1340 0.1290  329 HOH   A O   
6792 O  O   A HOH   F .   ? 0.2032 0.3170 0.4225 0.0045  0.0861  0.1730  330 HOH   A O   
6793 O  O   . HOH   F .   ? 0.4042 0.3677 0.6183 0.0676  0.1773  -0.1300 331 HOH   A O   
6794 O  O   . HOH   F .   ? 0.1460 0.1464 0.2176 -0.0217 0.0094  0.0099  332 HOH   A O   
6795 O  O   B HOH   F .   ? 0.1551 0.2165 0.2953 -0.0316 0.0197  0.0296  333 HOH   A O   
6796 O  O   . HOH   F .   ? 0.2959 0.2870 0.3325 -0.0824 0.0281  -0.0217 334 HOH   A O   
6797 O  O   A HOH   F .   ? 0.3258 0.1520 0.1722 0.0116  0.0153  0.0056  335 HOH   A O   
6798 O  O   . HOH   F .   ? 0.4922 0.2598 0.3089 -0.1180 0.0640  0.0201  336 HOH   A O   
6799 O  O   . HOH   F .   ? 0.2346 0.2201 0.2545 0.0434  0.0253  0.0367  337 HOH   A O   
6800 O  O   . HOH   F .   ? 0.2017 0.1554 0.1544 -0.0071 0.0194  0.0212  338 HOH   A O   
6801 O  O   . HOH   F .   ? 0.1799 0.3464 0.4035 -0.0344 0.0460  -0.1049 339 HOH   A O   
6802 O  O   . HOH   F .   ? 0.3968 0.1964 0.4460 0.0200  -0.1827 0.0239  340 HOH   A O   
6803 O  O   . HOH   F .   ? 0.4765 0.5114 0.2749 -0.1528 0.1132  0.0846  341 HOH   A O   
6804 O  O   . HOH   F .   ? 0.2143 0.4482 0.3925 -0.0338 -0.0637 0.1862  342 HOH   A O   
6805 O  O   . HOH   F .   ? 0.5634 0.4787 0.4376 0.0214  -0.0808 -0.0924 343 HOH   A O   
6806 O  O   . HOH   F .   ? 0.2368 0.1970 0.2219 -0.0305 0.0214  -0.0068 344 HOH   A O   
6807 O  O   A HOH   F .   ? 0.2176 0.3641 0.2078 0.0950  -0.0065 -0.0157 345 HOH   A O   
6808 O  O   . HOH   F .   ? 0.2349 0.3119 0.3821 -0.0561 -0.0358 -0.0269 346 HOH   A O   
6809 O  O   . HOH   F .   ? 0.5847 0.4203 0.6144 0.0124  -0.1048 0.0354  347 HOH   A O   
6810 O  O   A HOH   F .   ? 0.1474 0.2481 0.1947 0.0508  0.0345  0.0493  348 HOH   A O   
6811 O  O   . HOH   F .   ? 0.4482 0.3943 0.4097 -0.1789 -0.0957 0.1955  349 HOH   A O   
6812 O  O   . HOH   F .   ? 0.3145 0.4112 0.2746 -0.0378 0.0624  0.0462  350 HOH   A O   
6813 O  O   . HOH   F .   ? 0.5423 0.5142 0.5287 0.0329  0.2307  -0.0669 351 HOH   A O   
6814 O  O   . HOH   F .   ? 0.1407 0.2138 0.2081 0.0067  -0.0060 0.0523  352 HOH   A O   
6815 O  O   A HOH   F .   ? 0.4498 0.5220 0.6045 0.1585  0.0995  0.0097  353 HOH   A O   
6816 O  O   . HOH   F .   ? 0.1948 0.1605 0.2314 0.0201  -0.0271 -0.0009 354 HOH   A O   
6817 O  O   A HOH   F .   ? 0.1679 0.1230 0.1934 -0.0022 -0.0368 0.0052  355 HOH   A O   
6818 O  O   . HOH   F .   ? 0.3541 0.3992 0.3765 0.1627  0.0632  0.0207  356 HOH   A O   
6819 O  O   . HOH   F .   ? 0.1797 0.2031 0.2691 -0.0165 -0.0174 0.0857  357 HOH   A O   
6820 O  O   . HOH   F .   ? 0.2260 0.3812 0.3519 0.0730  -0.0601 -0.0084 358 HOH   A O   
6821 O  O   . HOH   F .   ? 0.3142 0.3818 0.2168 -0.0910 -0.0264 -0.0749 359 HOH   A O   
6822 O  O   . HOH   F .   ? 0.1956 0.1915 0.4043 0.0173  0.1052  -0.0181 360 HOH   A O   
6823 O  O   B HOH   F .   ? 0.2880 0.4784 0.2896 0.1244  -0.0096 -0.0699 361 HOH   A O   
6824 O  O   . HOH   F .   ? 0.1730 0.2063 0.1923 -0.0095 0.0098  0.0605  362 HOH   A O   
6825 O  O   . HOH   F .   ? 0.2879 0.3115 0.4705 -0.0542 -0.0981 -0.0946 363 HOH   A O   
6826 O  O   . HOH   F .   ? 0.3288 0.3170 0.2473 -0.0327 -0.0292 0.0406  364 HOH   A O   
6827 O  O   . HOH   F .   ? 0.3550 0.6956 0.4834 -0.0570 -0.1371 0.0797  365 HOH   A O   
6828 O  O   B HOH   F .   ? 0.2411 0.2654 0.3361 0.0179  0.0370  -0.0171 366 HOH   A O   
6829 O  O   . HOH   F .   ? 0.4549 0.5058 0.3203 0.1650  -0.0883 -0.1461 367 HOH   A O   
6830 O  O   B HOH   F .   ? 0.2598 0.2862 0.1422 -0.0166 0.0453  0.0194  368 HOH   A O   
6831 O  O   . HOH   F .   ? 0.1410 0.1858 0.2523 0.0057  -0.0099 0.0121  369 HOH   A O   
6832 O  O   . HOH   F .   ? 0.2625 0.4147 0.3200 -0.0370 0.0728  0.0229  370 HOH   A O   
6833 O  O   B HOH   F .   ? 0.3603 0.2649 0.2510 -0.0328 0.0680  0.0682  371 HOH   A O   
6834 O  O   . HOH   F .   ? 0.1341 0.1235 0.1317 -0.0031 0.0125  0.0109  372 HOH   A O   
6835 O  O   . HOH   F .   ? 0.1439 0.1495 0.1408 -0.0051 -0.0157 0.0018  373 HOH   A O   
6836 O  O   . HOH   F .   ? 0.1922 0.1815 0.2400 -0.0235 0.0151  0.0321  374 HOH   A O   
6837 O  O   . HOH   F .   ? 0.1583 0.1697 0.2578 0.0078  -0.0380 -0.0517 375 HOH   A O   
6838 O  O   . HOH   F .   ? 0.5271 0.2701 0.3604 -0.1739 0.1736  -0.0661 376 HOH   A O   
6839 O  O   . HOH   F .   ? 0.1480 0.1289 0.2153 -0.0043 0.0145  -0.0061 377 HOH   A O   
6840 O  O   . HOH   F .   ? 0.6220 0.3721 0.2716 -0.0038 0.0014  0.1228  378 HOH   A O   
6841 O  O   . HOH   F .   ? 0.4002 0.2070 0.2114 0.1198  0.0468  0.0284  379 HOH   A O   
6842 O  O   . HOH   F .   ? 0.2685 0.4585 0.2949 0.0568  0.0805  0.1850  380 HOH   A O   
6843 O  O   . HOH   F .   ? 0.3947 0.2200 0.3834 -0.0972 0.1144  0.0146  381 HOH   A O   
6844 O  O   . HOH   F .   ? 0.2262 0.1658 0.2555 0.0039  0.0168  0.0222  382 HOH   A O   
6845 O  O   . HOH   F .   ? 0.3076 0.2401 0.5200 -0.0793 -0.0485 0.0305  383 HOH   A O   
6846 O  O   . HOH   F .   ? 0.5955 0.5428 0.6968 -0.0608 -0.0487 0.1670  384 HOH   A O   
6847 O  O   . HOH   F .   ? 0.3197 0.7345 0.5632 0.0574  -0.0009 0.2806  385 HOH   A O   
6848 O  O   . HOH   F .   ? 0.1792 0.2732 0.2779 0.0474  0.0438  0.1059  386 HOH   A O   
6849 O  O   . HOH   F .   ? 0.1980 0.2501 0.3479 0.0309  0.0800  -0.0455 387 HOH   A O   
6850 O  O   . HOH   F .   ? 0.2955 0.3871 0.3233 -0.0391 -0.0089 0.1011  388 HOH   A O   
6851 O  O   . HOH   F .   ? 0.1914 0.2152 0.2320 -0.0329 -0.0562 0.0520  389 HOH   A O   
6852 O  O   B HOH   F .   ? 0.1471 0.1570 0.2109 0.0019  -0.0249 0.0122  390 HOH   A O   
6853 O  O   . HOH   F .   ? 0.2931 0.2687 0.2983 0.0079  -0.0444 -0.0656 391 HOH   A O   
6854 O  O   . HOH   F .   ? 0.2970 0.2842 0.2218 0.0421  0.0787  0.0166  392 HOH   A O   
6855 O  O   . HOH   F .   ? 0.3043 0.7469 0.3609 0.1773  0.0395  -0.0960 393 HOH   A O   
6856 O  O   . HOH   F .   ? 0.1876 0.1830 0.1650 0.0018  0.0082  0.0186  394 HOH   A O   
6857 O  O   . HOH   F .   ? 0.1667 0.2113 0.2669 -0.0213 0.0524  0.0413  395 HOH   A O   
6858 O  O   . HOH   F .   ? 0.3359 0.2362 0.3496 -0.0087 -0.0328 0.0939  396 HOH   A O   
6859 O  O   T HOH   F .   ? 0.1148 0.1414 0.2118 -0.0226 0.0068  0.0271  397 HOH   A O   
6860 O  O   . HOH   F .   ? 0.3076 0.3380 0.3728 -0.0724 0.1419  0.0114  398 HOH   A O   
6861 O  O   . HOH   F .   ? 0.2402 0.1952 0.1745 -0.0590 0.0059  0.0303  399 HOH   A O   
6862 O  O   A HOH   F .   ? 0.1603 0.1804 0.2602 0.0011  -0.0348 0.0368  400 HOH   A O   
6863 O  O   . HOH   F .   ? 0.2064 0.1649 0.2763 0.0019  -0.0294 0.0152  401 HOH   A O   
6864 O  O   . HOH   F .   ? 0.2424 0.3963 0.3614 -0.0329 0.0891  -0.0630 402 HOH   A O   
6865 O  O   . HOH   F .   ? 0.1870 0.1863 0.3711 0.0396  0.1005  0.1004  403 HOH   A O   
6866 O  O   B HOH   F .   ? 0.1108 0.1403 0.3183 -0.0157 -0.0118 0.0048  404 HOH   A O   
6867 O  O   . HOH   F .   ? 0.4381 0.4863 0.1912 0.0042  0.0826  0.0949  405 HOH   A O   
6868 O  O   A HOH   F .   ? 0.2544 0.1730 0.2262 0.0958  0.0588  0.0522  406 HOH   A O   
6869 O  O   . HOH   F .   ? 0.6171 0.2839 0.5102 0.1079  0.0009  0.0165  407 HOH   A O   
6870 O  O   . HOH   F .   ? 0.3379 0.5697 0.3726 -0.0263 0.0407  0.1075  408 HOH   A O   
6871 O  O   . HOH   F .   ? 0.3070 0.2422 0.2242 -0.0792 -0.0971 0.0306  409 HOH   A O   
6872 O  O   B HOH   F .   ? 0.2312 0.3311 0.1982 0.1426  0.0641  0.1118  410 HOH   A O   
6873 O  O   . HOH   F .   ? 0.1285 0.1384 0.1705 -0.0019 -0.0211 0.0105  411 HOH   A O   
6874 O  O   . HOH   F .   ? 0.3801 0.3719 0.4130 0.1486  0.0441  -0.0591 412 HOH   A O   
6875 O  O   . HOH   F .   ? 0.5511 0.6381 0.5277 0.1228  0.0891  0.0481  413 HOH   A O   
6876 O  O   . HOH   F .   ? 0.6378 0.5997 0.3645 0.2345  -0.0429 -0.0244 414 HOH   A O   
6877 O  O   . HOH   F .   ? 0.1476 0.1591 0.2866 -0.0024 0.0049  0.0193  415 HOH   A O   
6878 O  O   A HOH   F .   ? 0.2070 0.1986 0.3717 -0.0249 0.0521  -0.0418 416 HOH   A O   
6879 O  O   . HOH   F .   ? 0.1759 0.2522 0.3681 -0.0043 -0.0252 0.0199  417 HOH   A O   
6880 O  O   . HOH   F .   ? 0.1680 0.1399 0.1486 -0.0233 0.0084  -0.0002 418 HOH   A O   
6881 O  O   B HOH   F .   ? 0.2896 0.2057 0.2359 0.1031  -0.0715 -0.0054 419 HOH   A O   
6882 O  O   . HOH   F .   ? 0.2420 0.2109 0.2336 -0.0548 -0.0030 0.0613  420 HOH   A O   
6883 O  O   . HOH   F .   ? 0.2859 0.5937 0.1777 -0.0233 0.0511  0.0294  421 HOH   A O   
6884 O  O   . HOH   F .   ? 0.2099 0.2818 0.2367 -0.0132 -0.0639 0.0527  422 HOH   A O   
6885 O  O   . HOH   F .   ? 0.2994 0.3779 0.7888 -0.0376 0.1106  -0.0622 423 HOH   A O   
6886 O  O   A HOH   F .   ? 0.1074 0.1566 0.1188 0.0119  -0.0233 -0.0191 424 HOH   A O   
6887 O  O   A HOH   F .   ? 0.1511 0.1221 0.1972 -0.0063 0.0009  0.0072  425 HOH   A O   
6888 O  O   . HOH   F .   ? 0.8019 0.3587 0.7034 -0.0189 -0.1339 0.1557  426 HOH   A O   
6889 O  O   A HOH   F .   ? 0.1943 0.1841 0.2329 0.0119  0.0013  0.0430  427 HOH   A O   
6890 O  O   . HOH   F .   ? 0.4055 0.6971 0.6244 0.1326  0.1110  0.1030  428 HOH   A O   
6891 O  O   . HOH   F .   ? 0.1562 0.1858 0.2525 -0.0047 0.0071  0.0365  429 HOH   A O   
6892 O  O   . HOH   F .   ? 0.6741 0.6033 0.6638 -0.1444 -0.1135 0.0007  430 HOH   A O   
6893 O  O   . HOH   F .   ? 0.7689 0.7040 0.5656 -0.0353 0.1070  0.1120  431 HOH   A O   
6894 O  O   . HOH   F .   ? 0.3188 0.1236 0.2043 -0.0016 -0.0397 0.0106  432 HOH   A O   
6895 O  O   . HOH   F .   ? 0.2667 0.1996 0.4086 0.0291  -0.1196 0.0220  433 HOH   A O   
6896 O  O   . HOH   F .   ? 0.4587 0.6527 0.2983 -0.1046 -0.0200 0.1077  434 HOH   A O   
6897 O  O   A HOH   F .   ? 0.1880 0.2186 0.3271 0.0136  -0.0407 -0.0662 435 HOH   A O   
6898 O  O   . HOH   F .   ? 0.3927 0.2322 0.5627 -0.0882 -0.2219 0.1188  436 HOH   A O   
6899 O  O   . HOH   F .   ? 0.6723 0.4141 0.5448 0.2088  -0.0714 0.1558  437 HOH   A O   
6900 O  O   . HOH   F .   ? 0.4796 0.4797 0.4165 -0.0751 -0.1610 0.0333  438 HOH   A O   
6901 O  O   . HOH   F .   ? 0.2293 0.4030 0.2628 0.1520  0.0084  0.0346  439 HOH   A O   
6902 O  O   B HOH   F .   ? 0.2957 0.4957 0.3945 0.0105  0.0425  -0.0157 440 HOH   A O   
6903 O  O   . HOH   F .   ? 0.6080 0.6925 0.4810 0.1174  0.3005  -0.0066 441 HOH   A O   
6904 O  O   A HOH   F .   ? 0.5678 0.4630 0.4437 -0.1179 0.1474  0.1336  442 HOH   A O   
6905 O  O   A HOH   F .   ? 0.2442 0.2368 0.2454 -0.0357 0.0884  -0.0158 443 HOH   A O   
6906 O  O   B HOH   F .   ? 0.1333 0.2036 0.1289 -0.0388 -0.0439 0.0201  444 HOH   A O   
6907 O  O   . HOH   F .   ? 0.9145 0.9831 0.6955 0.0351  -0.0872 0.0490  445 HOH   A O   
6908 O  O   . HOH   F .   ? 0.3418 0.2695 0.1610 -0.0715 0.0319  0.0493  446 HOH   A O   
6909 O  O   A HOH   F .   ? 0.3288 0.2043 0.2668 -0.0508 0.0012  -0.0360 447 HOH   A O   
6910 O  O   . HOH   F .   ? 0.1845 0.2275 0.4555 -0.0261 -0.0771 0.0732  448 HOH   A O   
6911 O  O   . HOH   F .   ? 0.2433 0.1518 0.2716 0.0092  0.0115  0.0056  449 HOH   A O   
6912 O  O   . HOH   F .   ? 0.7212 0.6783 0.6697 -0.1331 -0.0241 -0.1323 450 HOH   A O   
6913 O  O   A HOH   F .   ? 0.2494 0.2398 0.4125 0.0070  0.0619  -0.0984 451 HOH   A O   
6914 O  O   . HOH   F .   ? 0.5904 0.8697 0.4075 0.1744  -0.1019 0.1828  452 HOH   A O   
6915 O  O   . HOH   F .   ? 0.3982 0.3603 0.2884 0.2155  -0.0598 -0.0418 453 HOH   A O   
6916 O  O   . HOH   F .   ? 0.6917 0.7328 0.6448 -0.0895 0.0405  0.0781  454 HOH   A O   
6917 O  O   . HOH   F .   ? 0.3969 0.5105 0.5031 -0.0666 -0.1133 -0.1365 455 HOH   A O   
6918 O  O   A HOH   F .   ? 0.1402 0.1049 0.1197 0.0108  -0.0277 0.0215  456 HOH   A O   
6919 O  O   . HOH   F .   ? 0.2226 0.1978 0.2790 0.0175  0.0372  0.0338  457 HOH   A O   
6920 O  O   . HOH   F .   ? 0.4524 0.5587 0.5976 0.0702  0.0855  -0.1234 458 HOH   A O   
6921 O  O   . HOH   F .   ? 0.2069 0.2733 0.2466 -0.0055 -0.0142 -0.0509 459 HOH   A O   
6922 O  O   A HOH   F .   ? 0.5612 0.3223 0.3047 0.0429  0.0786  0.1368  460 HOH   A O   
6923 O  O   . HOH   F .   ? 0.8691 0.6539 0.7319 0.1441  -0.1141 0.0360  461 HOH   A O   
6924 O  O   . HOH   F .   ? 0.5141 0.3620 0.4195 -0.0611 0.0424  0.0225  462 HOH   A O   
6925 O  O   . HOH   F .   ? 0.7159 0.5666 0.8176 0.0696  -0.1301 0.1967  463 HOH   A O   
6926 O  O   B HOH   F .   ? 0.1556 0.1126 0.1755 -0.0038 -0.0337 0.0618  464 HOH   A O   
6927 O  O   . HOH   F .   ? 0.4176 0.4698 0.4207 0.1005  -0.0787 0.0644  465 HOH   A O   
6928 O  O   . HOH   F .   ? 0.2775 0.4094 0.3419 0.1362  0.0024  0.0435  466 HOH   A O   
6929 O  O   . HOH   F .   ? 0.4119 0.3606 0.4301 0.0112  -0.0538 0.0473  467 HOH   A O   
6930 O  O   . HOH   F .   ? 0.6601 0.6070 0.5243 -0.0422 0.1576  0.1587  468 HOH   A O   
6931 O  O   . HOH   F .   ? 0.6874 0.7225 0.4195 0.0715  -0.1128 -0.0745 469 HOH   A O   
6932 O  O   . HOH   F .   ? 0.2522 0.2687 0.3610 -0.0547 0.0538  -0.0901 470 HOH   A O   
6933 O  O   . HOH   F .   ? 0.3224 0.4195 0.5519 -0.1300 0.0689  -0.1849 471 HOH   A O   
6934 O  O   . HOH   F .   ? 0.4000 0.4078 0.5049 0.0751  -0.0461 0.1128  472 HOH   A O   
6935 O  O   . HOH   F .   ? 0.6982 0.6700 0.7152 0.1577  0.1829  0.2260  473 HOH   A O   
6936 O  O   B HOH   F .   ? 0.1816 0.2226 0.3130 -0.0140 -0.0467 0.1023  474 HOH   A O   
6937 O  O   . HOH   F .   ? 0.2459 0.2503 0.3532 -0.0821 0.0490  -0.0311 475 HOH   A O   
6938 O  O   . HOH   F .   ? 0.6568 0.3689 0.7475 0.1327  0.1014  0.2413  476 HOH   A O   
6939 O  O   . HOH   F .   ? 0.2430 0.1646 0.2461 0.0256  -0.0872 -0.0386 477 HOH   A O   
6940 O  O   . HOH   F .   ? 0.2567 0.4285 0.5739 0.0472  0.0208  -0.1969 478 HOH   A O   
6941 O  O   A HOH   F .   ? 0.2653 0.2138 0.5263 0.0740  -0.0844 -0.0566 479 HOH   A O   
6942 O  O   . HOH   F .   ? 0.3073 0.4925 0.3924 -0.0981 -0.0082 -0.0095 480 HOH   A O   
6943 O  O   . HOH   F .   ? 0.4900 0.5755 0.4560 0.0950  -0.0927 -0.0988 481 HOH   A O   
6944 O  O   . HOH   F .   ? 0.4104 0.6285 0.4063 -0.1077 -0.1131 0.2638  482 HOH   A O   
6945 O  O   . HOH   F .   ? 0.3956 0.5304 0.3561 0.0702  -0.0606 -0.0895 483 HOH   A O   
6946 O  O   . HOH   F .   ? 0.6282 0.4941 0.4907 0.0308  0.1839  0.0392  484 HOH   A O   
6947 O  O   . HOH   F .   ? 0.3399 0.2264 0.3725 0.0297  0.1003  0.0053  485 HOH   A O   
6948 O  O   B HOH   F .   ? 0.1481 0.3852 0.3913 -0.0105 -0.0742 -0.0906 486 HOH   A O   
6949 O  O   . HOH   F .   ? 0.3932 0.4051 0.2772 0.0063  -0.0016 -0.0032 487 HOH   A O   
6950 O  O   . HOH   F .   ? 0.4903 0.4645 0.3285 -0.0859 -0.0450 -0.0213 488 HOH   A O   
6951 O  O   . HOH   F .   ? 0.5904 0.5631 0.6153 -0.1673 -0.1391 0.0776  489 HOH   A O   
6952 O  O   . HOH   F .   ? 0.4412 0.4747 0.5892 -0.2167 -0.0511 -0.0246 490 HOH   A O   
6953 O  O   . HOH   F .   ? 0.2283 0.2252 0.2461 0.0292  0.0011  0.0156  491 HOH   A O   
6954 O  O   . HOH   F .   ? 0.7450 0.5483 0.6905 -0.0978 0.0954  -0.1245 492 HOH   A O   
6955 O  O   . HOH   F .   ? 0.8215 0.3930 0.2941 -0.0919 -0.1368 0.0434  493 HOH   A O   
6956 O  O   . HOH   F .   ? 0.5638 0.4447 0.4529 0.0677  -0.0371 -0.1315 494 HOH   A O   
6957 O  O   . HOH   F .   ? 0.4610 0.2604 0.3397 -0.0531 -0.1483 0.0611  495 HOH   A O   
6958 O  O   B HOH   F .   ? 0.1923 0.1616 0.2520 0.0421  -0.0573 0.0442  496 HOH   A O   
6959 O  O   . HOH   F .   ? 0.6711 0.7191 0.4596 -0.1197 0.0851  0.0942  497 HOH   A O   
6960 O  O   . HOH   F .   ? 0.7102 0.4714 0.5278 -0.0863 -0.0960 -0.0895 498 HOH   A O   
6961 O  O   . HOH   F .   ? 0.5662 0.3726 0.4899 -0.0029 0.1278  -0.0048 499 HOH   A O   
6962 O  O   . HOH   F .   ? 0.2907 0.4655 0.3084 -0.0301 -0.0035 -0.0742 500 HOH   A O   
6963 O  O   . HOH   F .   ? 0.2745 0.5398 0.3985 0.1244  0.1090  0.2568  501 HOH   A O   
6964 O  O   B HOH   F .   ? 0.3996 0.3706 0.3619 0.0397  -0.1356 -0.0423 502 HOH   A O   
6965 O  O   . HOH   F .   ? 0.2463 0.2377 0.7744 -0.0113 -0.1438 0.0484  503 HOH   A O   
6966 O  O   . HOH   F .   ? 0.2667 0.3780 0.4389 -0.0109 0.1035  0.0729  504 HOH   A O   
6967 O  O   . HOH   F .   ? 0.5349 0.5521 0.6897 0.0479  0.2202  -0.1125 505 HOH   A O   
6968 O  O   . HOH   F .   ? 0.4585 0.3679 0.2459 -0.0966 0.1493  -0.0514 506 HOH   A O   
6969 O  O   . HOH   F .   ? 0.4860 0.5035 0.5593 0.0466  -0.1058 0.0573  507 HOH   A O   
6970 O  O   . HOH   F .   ? 0.4576 0.3226 0.5039 -0.0307 0.2516  0.0187  508 HOH   A O   
6971 O  O   . HOH   F .   ? 0.4378 0.3348 0.4209 -0.0564 0.0042  0.1631  509 HOH   A O   
6972 O  O   . HOH   F .   ? 0.2854 0.2209 0.5267 0.0155  0.0307  0.1186  510 HOH   A O   
6973 O  O   B HOH   F .   ? 0.2562 0.1516 0.2555 0.0415  -0.0608 0.0192  511 HOH   A O   
6974 O  O   . HOH   F .   ? 0.2444 0.2906 0.4950 0.0012  0.0989  -0.0400 512 HOH   A O   
6975 O  O   . HOH   F .   ? 0.6362 0.2505 0.3874 -0.0768 0.0869  0.0465  513 HOH   A O   
6976 O  O   . HOH   F .   ? 0.6564 0.5813 0.3848 0.2156  -0.1375 0.0697  514 HOH   A O   
6977 O  O   . HOH   F .   ? 0.3973 0.7829 0.5684 -0.0959 -0.0283 0.2789  515 HOH   A O   
6978 O  O   . HOH   F .   ? 0.2741 0.3264 0.3531 0.0825  -0.0727 0.0442  516 HOH   A O   
6979 O  O   . HOH   F .   ? 0.4937 0.2448 0.3988 -0.1461 0.0207  0.0056  517 HOH   A O   
6980 O  O   . HOH   F .   ? 0.2808 0.4007 0.4561 0.0790  -0.0576 -0.0283 518 HOH   A O   
6981 O  O   B HOH   F .   ? 0.2338 0.2565 0.1819 0.0154  -0.0191 0.1017  519 HOH   A O   
6982 O  O   . HOH   F .   ? 0.5144 0.7922 0.6094 0.0703  -0.0797 0.1891  520 HOH   A O   
6983 O  O   . HOH   F .   ? 0.7796 0.3802 0.4767 0.2308  0.0687  0.1131  521 HOH   A O   
6984 O  O   . HOH   F .   ? 0.2550 0.2268 0.5140 0.0064  0.0453  0.0713  522 HOH   A O   
6985 O  O   . HOH   F .   ? 0.4975 0.6978 0.5014 0.3198  0.0168  0.1401  523 HOH   A O   
6986 O  O   . HOH   F .   ? 0.4613 0.5896 0.4860 -0.0778 -0.0377 -0.1454 524 HOH   A O   
6987 O  O   T HOH   F .   ? 0.1359 0.1543 0.2323 -0.0474 -0.0526 0.0556  525 HOH   A O   
6988 O  O   A HOH   F .   ? 0.3858 0.8329 0.4325 0.1958  0.0112  0.0428  526 HOH   A O   
6989 O  O   . HOH   F .   ? 0.2482 0.7433 0.3834 0.0465  0.0380  -0.0247 527 HOH   A O   
6990 O  O   . HOH   F .   ? 0.5041 0.7382 0.6432 -0.1142 -0.0919 0.0821  528 HOH   A O   
6991 O  O   . HOH   F .   ? 0.5181 0.5393 0.5130 0.1826  -0.0216 0.1991  529 HOH   A O   
6992 O  O   B HOH   F .   ? 0.2301 0.3226 0.3268 0.0908  0.0722  0.1318  530 HOH   A O   
6993 O  O   . HOH   F .   ? 0.2797 0.4363 0.5605 -0.0031 -0.0804 0.2636  531 HOH   A O   
6994 O  O   . HOH   G .   ? 0.2276 0.2111 0.3067 0.0195  0.0734  0.0357  201 HOH   B O   
6995 O  O   . HOH   G .   ? 0.4537 0.3411 0.3932 -0.0572 0.0560  -0.1470 202 HOH   B O   
6996 O  O   . HOH   G .   ? 0.3268 0.4334 0.5024 -0.1139 0.0476  -0.1625 203 HOH   B O   
6997 O  O   . HOH   G .   ? 0.3034 0.7301 0.4142 0.0457  0.0159  0.2770  204 HOH   B O   
6998 O  O   . HOH   G .   ? 0.6301 0.5762 0.5317 0.2090  0.0473  0.0031  205 HOH   B O   
6999 O  O   . HOH   G .   ? 0.3121 0.5442 0.5591 0.0292  0.1829  -0.1532 206 HOH   B O   
7000 O  O   . HOH   G .   ? 0.3329 0.3521 0.7138 -0.0436 0.0307  -0.0905 207 HOH   B O   
7001 O  O   . HOH   G .   ? 0.4613 0.5049 0.2638 0.0407  -0.0389 -0.1392 208 HOH   B O   
7002 O  O   . HOH   G .   ? 0.3984 0.5714 0.4301 0.2527  -0.0493 -0.0257 209 HOH   B O   
7003 O  O   . HOH   G .   ? 0.2924 0.2055 0.5018 0.0221  0.1757  0.1010  210 HOH   B O   
7004 O  O   . HOH   G .   ? 0.1587 0.1890 0.2810 -0.0196 -0.0072 0.0066  211 HOH   B O   
7005 O  O   . HOH   G .   ? 0.6605 0.2909 0.3995 -0.2073 -0.0117 0.0339  212 HOH   B O   
7006 O  O   . HOH   G .   ? 0.5114 0.3895 0.5991 0.0511  -0.0876 0.2523  213 HOH   B O   
7007 O  O   . HOH   G .   ? 0.4387 0.4242 0.3770 0.0092  0.0781  -0.1650 214 HOH   B O   
7008 O  O   . HOH   G .   ? 0.8036 0.3046 0.4484 0.0286  0.1406  -0.0265 215 HOH   B O   
7009 O  O   . HOH   G .   ? 0.4653 0.6520 0.3704 0.2852  -0.0974 -0.0011 216 HOH   B O   
7010 O  O   . HOH   G .   ? 0.1863 0.2278 0.2847 -0.0009 0.0152  -0.0293 217 HOH   B O   
7011 O  O   . HOH   G .   ? 0.3980 0.3660 0.4065 0.0243  -0.1182 0.0455  218 HOH   B O   
7012 O  O   . HOH   G .   ? 0.5046 0.2060 0.2822 -0.0107 -0.0822 0.0095  219 HOH   B O   
7013 O  O   . HOH   G .   ? 0.3007 0.4992 0.4527 0.1876  0.0417  0.0009  220 HOH   B O   
7014 O  O   . HOH   G .   ? 0.2768 0.2597 0.6943 0.0515  -0.1214 0.0622  221 HOH   B O   
7015 O  O   . HOH   G .   ? 0.4756 0.3873 0.7084 -0.0522 -0.1563 -0.0964 222 HOH   B O   
7016 O  O   . HOH   G .   ? 0.3159 0.2144 0.5051 0.0092  0.1777  0.0466  223 HOH   B O   
7017 O  O   . HOH   G .   ? 0.3410 0.3770 0.4621 0.0819  -0.0258 0.0117  224 HOH   B O   
7018 O  O   . HOH   G .   ? 0.7789 0.4531 0.5384 0.2136  -0.0466 -0.1195 225 HOH   B O   
7019 O  O   . HOH   G .   ? 0.3070 0.3744 0.6546 0.0113  0.0696  -0.0445 226 HOH   B O   
7020 O  O   . HOH   G .   ? 0.6119 0.4068 0.2484 -0.0470 0.0278  -0.0009 227 HOH   B O   
7021 O  O   . HOH   G .   ? 0.1657 0.2149 0.2976 -0.0156 0.0004  -0.0147 228 HOH   B O   
7022 O  O   . HOH   G .   ? 0.2158 0.2176 0.4281 -0.0304 -0.0108 -0.0745 229 HOH   B O   
7023 O  O   . HOH   G .   ? 0.2437 0.1716 0.2855 -0.0325 0.1185  -0.0143 230 HOH   B O   
7024 O  O   . HOH   G .   ? 0.4176 0.6396 0.3251 0.2109  0.0142  -0.0494 231 HOH   B O   
7025 O  O   . HOH   G .   ? 0.3581 0.1698 0.1823 0.0133  -0.0821 -0.0068 232 HOH   B O   
7026 O  O   . HOH   G .   ? 0.3797 0.2614 0.3854 0.0836  -0.0304 -0.0634 233 HOH   B O   
7027 O  O   . HOH   G .   ? 0.3825 0.4078 0.4742 -0.1496 0.0187  0.1039  234 HOH   B O   
7028 O  O   . HOH   G .   ? 0.2112 0.2395 0.3125 -0.0571 0.0049  -0.0282 235 HOH   B O   
7029 O  O   . HOH   G .   ? 0.7125 0.5748 0.3338 0.1249  -0.0194 0.0564  236 HOH   B O   
7030 O  O   . HOH   G .   ? 0.2612 0.3628 0.2945 -0.0674 0.0552  -0.0068 237 HOH   B O   
7031 O  O   . HOH   G .   ? 0.3670 0.3040 0.2027 0.0357  0.0644  0.0492  238 HOH   B O   
7032 O  O   . HOH   G .   ? 0.2039 0.3710 0.2389 -0.0326 -0.0208 0.0539  239 HOH   B O   
7033 O  O   . HOH   G .   ? 0.1446 0.1385 0.1488 -0.0121 -0.0062 -0.0016 240 HOH   B O   
7034 O  O   . HOH   G .   ? 0.4875 0.3169 0.4152 -0.2247 0.0016  0.0116  241 HOH   B O   
7035 O  O   . HOH   G .   ? 0.2432 0.2500 0.3285 0.0342  0.0154  -0.0850 242 HOH   B O   
7036 O  O   . HOH   G .   ? 0.3467 0.2451 0.4513 0.0424  -0.0906 -0.1132 243 HOH   B O   
7037 O  O   . HOH   G .   ? 0.2085 0.3544 0.3089 -0.0340 -0.0649 -0.0480 244 HOH   B O   
7038 O  O   . HOH   G .   ? 0.1548 0.1423 0.2508 -0.0048 0.0026  -0.0096 245 HOH   B O   
7039 O  O   . HOH   G .   ? 0.2036 0.1294 0.3456 0.0093  -0.0527 -0.0156 246 HOH   B O   
7040 O  O   . HOH   G .   ? 0.3062 0.1737 0.6161 -0.0168 -0.1234 -0.0300 247 HOH   B O   
7041 O  O   . HOH   G .   ? 0.3061 0.2557 0.3314 -0.0319 0.0163  -0.0697 248 HOH   B O   
7042 O  O   . HOH   G .   ? 0.1410 0.1278 0.1589 0.0008  -0.0076 0.0058  249 HOH   B O   
7043 O  O   . HOH   G .   ? 0.2028 0.1896 0.2093 -0.0301 -0.0499 0.0229  250 HOH   B O   
7044 O  O   . HOH   G .   ? 0.3432 0.3565 0.2189 0.0456  0.0822  0.0194  251 HOH   B O   
7045 O  O   . HOH   G .   ? 0.2531 0.4170 0.5783 0.0029  0.0143  -0.1304 252 HOH   B O   
7046 O  O   . HOH   G .   ? 0.2876 0.2192 0.2890 0.0876  0.0840  0.0047  253 HOH   B O   
7047 O  O   . HOH   G .   ? 0.2606 0.2094 0.1961 0.0269  -0.0178 -0.0032 254 HOH   B O   
7048 O  O   . HOH   G .   ? 0.2873 0.4752 0.2921 -0.0961 -0.0490 -0.0804 255 HOH   B O   
7049 O  O   . HOH   G .   ? 0.2489 0.4986 0.6267 0.1378  -0.0681 -0.0997 256 HOH   B O   
7050 O  O   . HOH   G .   ? 0.2219 0.1995 0.2455 0.0606  -0.0679 -0.0435 257 HOH   B O   
7051 O  O   . HOH   G .   ? 0.2066 0.1837 0.3320 0.0030  -0.0434 -0.0300 258 HOH   B O   
7052 O  O   . HOH   G .   ? 0.2232 0.3052 0.2198 -0.0598 0.0323  0.0418  259 HOH   B O   
7053 O  O   . HOH   G .   ? 0.2026 0.1518 0.2003 -0.0313 -0.0301 0.0233  260 HOH   B O   
7054 O  O   . HOH   G .   ? 0.4274 0.3764 0.3787 -0.1085 0.1599  -0.1223 261 HOH   B O   
7055 O  O   . HOH   G .   ? 0.1504 0.1660 0.3039 -0.0239 -0.0212 0.0134  262 HOH   B O   
7056 O  O   . HOH   G .   ? 0.3050 0.5228 0.3539 -0.0484 -0.1057 0.1194  263 HOH   B O   
7057 O  O   . HOH   G .   ? 0.1312 0.1573 0.2178 -0.0038 0.0082  0.0169  264 HOH   B O   
7058 O  O   . HOH   G .   ? 0.2237 0.2021 0.2050 0.0137  -0.0102 0.0039  265 HOH   B O   
7059 O  O   . HOH   G .   ? 0.3666 0.4178 0.5334 0.0777  0.0926  0.0214  266 HOH   B O   
7060 O  O   . HOH   G .   ? 0.1789 0.1771 0.1561 -0.0442 -0.0347 0.0072  267 HOH   B O   
7061 O  O   . HOH   G .   ? 0.2073 0.4370 0.5603 -0.0551 -0.0388 -0.1498 268 HOH   B O   
7062 O  O   . HOH   G .   ? 0.2446 0.3912 0.3558 0.0377  0.0997  0.0205  269 HOH   B O   
7063 O  O   . HOH   G .   ? 0.1690 0.1421 0.3360 -0.0065 -0.0232 -0.0060 270 HOH   B O   
7064 O  O   . HOH   G .   ? 0.2573 0.1921 0.2754 -0.0640 0.0198  -0.0163 271 HOH   B O   
7065 O  O   . HOH   G .   ? 0.1965 0.1513 0.2177 -0.0249 -0.0118 0.0117  272 HOH   B O   
7066 O  O   . HOH   G .   ? 0.2258 0.2451 0.2266 -0.0387 -0.0604 -0.0286 273 HOH   B O   
7067 O  O   . HOH   G .   ? 0.2442 0.2749 0.2466 -0.0453 -0.0767 0.0178  274 HOH   B O   
7068 O  O   . HOH   G .   ? 0.2570 0.4612 0.5102 -0.0885 -0.1197 0.0900  275 HOH   B O   
7069 O  O   . HOH   G .   ? 0.3288 0.3950 0.4848 0.1366  -0.0835 -0.0989 276 HOH   B O   
7070 O  O   . HOH   G .   ? 0.1529 0.1523 0.3393 -0.0088 0.0053  -0.0033 277 HOH   B O   
7071 O  O   . HOH   G .   ? 0.2474 0.7516 0.2582 0.0531  -0.0199 -0.0525 278 HOH   B O   
7072 O  O   . HOH   G .   ? 0.2728 0.1994 0.4996 0.0211  0.0429  0.0133  279 HOH   B O   
7073 O  O   . HOH   G .   ? 0.3942 0.2935 0.4847 -0.0212 -0.1339 -0.0915 280 HOH   B O   
7074 O  O   . HOH   G .   ? 0.2024 0.2833 0.3600 -0.0282 0.0197  -0.0822 281 HOH   B O   
7075 O  O   . HOH   G .   ? 0.4769 0.6238 0.2590 -0.0197 -0.1262 0.0841  282 HOH   B O   
7076 O  O   . HOH   G .   ? 0.2541 0.4026 0.2407 0.1572  -0.0508 -0.0827 283 HOH   B O   
7077 O  O   . HOH   G .   ? 0.2884 0.7026 0.7394 0.1579  -0.1002 -0.1411 284 HOH   B O   
7078 O  O   . HOH   G .   ? 0.4637 0.3400 0.2763 0.0419  -0.0226 -0.0727 285 HOH   B O   
7079 O  O   . HOH   G .   ? 0.3871 0.5220 0.4772 -0.0033 -0.1573 0.0271  286 HOH   B O   
7080 O  O   . HOH   G .   ? 0.1617 0.1503 0.1829 0.0034  0.0058  0.0014  287 HOH   B O   
7081 O  O   . HOH   G .   ? 0.1634 0.2016 0.1433 -0.0140 -0.0183 0.0063  288 HOH   B O   
7082 O  O   . HOH   G .   ? 0.2316 0.2540 0.2823 0.0205  -0.0841 0.0103  289 HOH   B O   
7083 O  O   . HOH   G .   ? 0.1666 0.2014 0.2881 0.0111  -0.0061 0.0240  290 HOH   B O   
7084 O  O   . HOH   G .   ? 0.1682 0.3377 0.4835 0.0337  -0.0163 -0.1415 291 HOH   B O   
7085 O  O   . HOH   G .   ? 0.3630 0.7641 0.3871 0.1433  -0.0915 0.1407  292 HOH   B O   
7086 O  O   . HOH   G .   ? 0.3494 0.2433 0.2221 0.0145  -0.0757 0.0029  293 HOH   B O   
7087 O  O   . HOH   G .   ? 0.3106 0.2850 0.2911 -0.0035 -0.0019 -0.1249 294 HOH   B O   
7088 O  O   . HOH   G .   ? 0.3855 0.2078 0.3846 -0.1013 -0.2106 0.0863  295 HOH   B O   
7089 O  O   . HOH   G .   ? 0.3945 0.5163 0.2106 0.0206  0.0675  0.0810  296 HOH   B O   
7090 O  O   . HOH   G .   ? 0.6325 0.7156 0.4948 0.3490  -0.0727 -0.0625 297 HOH   B O   
7091 O  O   . HOH   G .   ? 0.1721 0.1569 0.2310 0.0062  0.0061  0.0118  298 HOH   B O   
7092 O  O   . HOH   G .   ? 0.2974 0.2887 0.5070 -0.0445 -0.0871 0.1239  299 HOH   B O   
7093 O  O   . HOH   G .   ? 0.3415 0.1812 0.3337 0.0638  0.1280  0.0474  300 HOH   B O   
7094 O  O   . HOH   G .   ? 0.2650 0.3086 0.4449 -0.0460 -0.1213 0.1084  301 HOH   B O   
7095 O  O   . HOH   G .   ? 0.2009 0.1541 0.2699 -0.0215 -0.0263 -0.0024 302 HOH   B O   
7096 O  O   . HOH   G .   ? 0.5549 0.3680 0.3291 0.2464  0.1261  0.1009  303 HOH   B O   
7097 O  O   . HOH   G .   ? 0.3097 0.3480 0.4016 -0.1041 0.1018  -0.0179 304 HOH   B O   
7098 O  O   . HOH   G .   ? 0.1989 0.2865 0.6434 0.0468  -0.0414 -0.1504 305 HOH   B O   
7099 O  O   . HOH   G .   ? 0.4856 0.2776 0.2427 -0.1730 0.0619  -0.0124 306 HOH   B O   
7100 O  O   . HOH   G .   ? 0.2731 0.2883 0.3548 -0.0359 0.1087  -0.0864 307 HOH   B O   
7101 O  O   . HOH   G .   ? 0.1535 0.1440 0.2953 0.0099  -0.0009 0.0038  308 HOH   B O   
7102 O  O   . HOH   G .   ? 0.1961 0.1563 0.3484 0.0314  -0.0928 0.0094  309 HOH   B O   
7103 O  O   . HOH   G .   ? 0.4876 0.3850 0.2461 0.1393  -0.0995 0.0515  310 HOH   B O   
7104 O  O   . HOH   G .   ? 0.4670 0.3281 0.4657 -0.0792 0.0360  0.1452  311 HOH   B O   
7105 O  O   . HOH   G .   ? 0.1513 0.1863 0.2945 -0.0239 -0.0066 0.0132  312 HOH   B O   
7106 O  O   . HOH   G .   ? 0.2105 0.6034 0.5288 -0.0854 -0.0311 -0.0135 313 HOH   B O   
7107 O  O   . HOH   G .   ? 0.2174 0.3145 0.5142 -0.0038 -0.0665 -0.0366 314 HOH   B O   
7108 O  O   . HOH   G .   ? 0.4632 0.4107 0.2404 0.0427  -0.0370 -0.0536 315 HOH   B O   
7109 O  O   . HOH   G .   ? 0.2361 0.1508 0.2327 -0.0185 -0.0219 0.0358  316 HOH   B O   
7110 O  O   . HOH   G .   ? 0.3340 0.4275 0.7792 -0.0335 -0.0959 0.2157  317 HOH   B O   
7111 O  O   . HOH   G .   ? 0.3760 0.2147 0.2818 0.1265  0.0933  0.0299  318 HOH   B O   
7112 O  O   . HOH   G .   ? 0.1487 0.1606 0.2940 -0.0103 -0.0138 -0.0113 319 HOH   B O   
7113 O  O   . HOH   G .   ? 0.4222 0.3075 0.5399 0.0966  0.2224  0.1812  320 HOH   B O   
7114 O  O   . HOH   G .   ? 0.2207 0.1949 0.1799 0.0025  0.0203  0.0266  321 HOH   B O   
7115 O  O   . HOH   G .   ? 0.1648 0.2864 0.2346 -0.0165 -0.0142 0.0653  322 HOH   B O   
7116 O  O   . HOH   G .   ? 0.4390 0.4165 0.2303 0.1345  -0.0674 -0.0271 323 HOH   B O   
7117 O  O   . HOH   G .   ? 0.6849 0.4210 0.4637 0.1561  0.1279  0.0054  324 HOH   B O   
7118 O  O   . HOH   G .   ? 0.2917 0.2185 0.2391 0.0309  -0.0316 0.0220  325 HOH   B O   
7119 O  O   . HOH   G .   ? 0.3977 0.4284 0.6169 0.0608  -0.0130 0.0930  326 HOH   B O   
7120 O  O   . HOH   G .   ? 0.1806 0.1911 0.2826 0.0292  0.0376  0.0151  327 HOH   B O   
7121 O  O   . HOH   G .   ? 0.5316 0.3301 0.4463 0.0295  0.1163  -0.1401 328 HOH   B O   
7122 O  O   . HOH   G .   ? 0.1748 0.2855 0.2978 0.0323  -0.0117 -0.0682 329 HOH   B O   
7123 O  O   . HOH   G .   ? 0.5996 0.5079 0.6953 0.0958  -0.1349 0.2516  330 HOH   B O   
7124 O  O   . HOH   G .   ? 0.7968 0.2048 0.3343 0.0096  -0.0888 -0.0090 331 HOH   B O   
7125 O  O   . HOH   G .   ? 0.4516 0.2403 0.2810 0.0210  0.0579  0.0751  332 HOH   B O   
7126 O  O   . HOH   G .   ? 0.2591 0.2002 0.4864 0.0044  0.0145  0.0394  333 HOH   B O   
7127 O  O   . HOH   G .   ? 0.5717 0.5295 0.5499 -0.1088 -0.0241 0.1453  334 HOH   B O   
7128 O  O   . HOH   G .   ? 0.5683 0.4114 0.7382 -0.0637 -0.0576 -0.1281 335 HOH   B O   
7129 O  O   . HOH   G .   ? 0.5853 0.3537 0.3505 0.0271  0.1256  0.1318  336 HOH   B O   
7130 O  O   . HOH   G .   ? 0.2122 0.2335 0.5617 -0.0455 0.0012  0.1345  337 HOH   B O   
7131 O  O   . HOH   G .   ? 0.4356 0.7612 0.3897 -0.0260 -0.0741 0.2403  338 HOH   B O   
7132 O  O   . HOH   G .   ? 0.1715 0.1429 0.2411 0.0097  -0.0187 0.0065  339 HOH   B O   
7133 O  O   . HOH   G .   ? 0.4386 0.3045 0.3024 0.0592  -0.1194 -0.0748 340 HOH   B O   
7134 O  O   . HOH   G .   ? 0.4748 0.5692 0.3508 0.0069  -0.1036 -0.0062 341 HOH   B O   
7135 O  O   . HOH   G .   ? 0.7213 0.6541 0.3100 0.0176  -0.0451 0.1324  342 HOH   B O   
7136 O  O   . HOH   G .   ? 0.2030 0.5507 0.6892 0.0028  -0.0199 0.0535  343 HOH   B O   
7137 O  O   . HOH   G .   ? 0.3324 0.6103 0.3833 -0.0679 -0.0506 -0.0905 344 HOH   B O   
7138 O  O   . HOH   G .   ? 0.2081 0.1996 0.2895 -0.0152 0.0595  -0.0141 345 HOH   B O   
7139 O  O   . HOH   G .   ? 0.4728 0.5307 0.4632 -0.1141 0.0311  0.0985  346 HOH   B O   
7140 O  O   . HOH   G .   ? 0.4215 0.5483 0.6158 -0.0038 -0.1059 0.1502  347 HOH   B O   
7141 O  O   . HOH   G .   ? 0.2725 0.2214 0.5149 -0.0321 -0.0865 -0.0542 348 HOH   B O   
7142 O  O   . HOH   G .   ? 0.2570 0.6254 0.3314 0.1691  -0.0643 -0.1613 349 HOH   B O   
7143 O  O   . HOH   G .   ? 0.2138 0.4384 0.5397 0.0226  0.0616  0.0340  350 HOH   B O   
7144 O  O   . HOH   G .   ? 0.3945 0.7046 0.6195 0.0373  0.0191  -0.0627 351 HOH   B O   
7145 O  O   . HOH   G .   ? 0.3307 0.4276 0.5095 -0.1494 0.0306  -0.0612 352 HOH   B O   
7146 O  O   . HOH   G .   ? 0.3030 0.1791 0.4240 0.0326  -0.1375 -0.0517 353 HOH   B O   
7147 O  O   . HOH   G .   ? 0.4055 0.2095 0.4039 -0.0858 0.0701  -0.0947 354 HOH   B O   
7148 O  O   . HOH   G .   ? 0.3524 0.2707 0.3345 -0.0883 0.0017  -0.0744 355 HOH   B O   
7149 O  O   . HOH   G .   ? 0.5025 0.3518 0.4038 0.0586  0.1268  -0.0799 356 HOH   B O   
7150 O  O   . HOH   G .   ? 0.4534 0.3174 0.4186 -0.1385 0.0951  0.0354  357 HOH   B O   
7151 O  O   . HOH   G .   ? 0.5743 0.4575 0.4607 -0.0347 -0.0429 0.0039  358 HOH   B O   
7152 O  O   . HOH   G .   ? 0.4777 0.5338 0.5124 0.1684  -0.1505 0.1771  359 HOH   B O   
7153 O  O   . HOH   G .   ? 0.5118 0.3443 0.4408 0.0040  -0.1723 -0.0416 360 HOH   B O   
7154 O  O   . HOH   G .   ? 0.4437 0.3943 0.6835 0.0206  0.0379  0.0944  361 HOH   B O   
7155 O  O   . HOH   G .   ? 0.4103 0.6372 0.2793 0.1923  0.0005  -0.0000 362 HOH   B O   
7156 O  O   . HOH   G .   ? 0.2198 0.3613 0.6644 -0.0712 -0.0634 -0.0824 363 HOH   B O   
7157 O  O   . HOH   G .   ? 0.5071 0.5981 0.3443 0.1934  -0.1537 0.0542  364 HOH   B O   
7158 O  O   . HOH   G .   ? 0.6250 0.4841 0.4035 0.1504  0.0678  0.0746  365 HOH   B O   
7159 O  O   . HOH   G .   ? 0.4390 0.3020 0.6312 -0.1291 -0.0801 0.0245  366 HOH   B O   
7160 O  O   . HOH   G .   ? 0.5065 0.6036 0.4095 -0.0856 -0.0226 -0.1115 367 HOH   B O   
7161 O  O   . HOH   G .   ? 0.4047 0.6315 0.4969 0.2739  0.0968  0.1292  368 HOH   B O   
7162 O  O   . HOH   G .   ? 0.5360 0.3937 0.5546 0.1363  -0.1104 0.0337  369 HOH   B O   
7163 O  O   . HOH   G .   ? 0.6301 0.2085 0.2877 -0.0066 0.0180  0.0158  370 HOH   B O   
7164 O  O   . HOH   G .   ? 0.7808 0.7550 0.4851 0.3064  -0.1346 0.0609  371 HOH   B O   
7165 O  O   . HOH   G .   ? 0.6269 0.3907 0.2954 -0.1383 -0.1050 -0.0411 372 HOH   B O   
7166 O  O   . HOH   G .   ? 0.4716 0.5027 0.4929 -0.0901 -0.0917 0.0469  373 HOH   B O   
7167 O  O   . HOH   G .   ? 0.3980 0.2985 0.4435 0.0733  -0.1102 -0.0623 374 HOH   B O   
7168 O  O   . HOH   G .   ? 0.4259 0.7059 0.6041 0.1371  0.0361  0.3121  375 HOH   B O   
7169 O  O   . HOH   G .   ? 0.2344 0.4648 0.4047 0.0425  -0.0384 -0.1057 376 HOH   B O   
7170 O  O   . HOH   G .   ? 0.2866 0.4729 0.2189 0.0298  0.0320  -0.0013 377 HOH   B O   
7171 O  O   . HOH   G .   ? 0.5564 0.6933 0.3619 -0.1368 0.0691  -0.1439 378 HOH   B O   
7172 O  O   . HOH   G .   ? 0.7447 0.3673 0.5634 -0.1038 -0.0652 0.0165  379 HOH   B O   
7173 O  O   . HOH   G .   ? 0.3847 0.5786 0.5474 0.0338  -0.0226 -0.0352 380 HOH   B O   
7174 O  O   . HOH   G .   ? 0.3242 0.2498 0.3114 0.0053  0.0270  0.0365  381 HOH   B O   
7175 O  O   . HOH   G .   ? 0.5780 0.6797 0.5912 0.0051  0.2770  0.1454  382 HOH   B O   
7176 O  O   . HOH   G .   ? 0.4331 0.7956 0.5652 0.1198  0.2148  0.1184  383 HOH   B O   
7177 O  O   . HOH   G .   ? 0.6189 0.3962 0.3641 0.0762  0.0521  -0.0447 384 HOH   B O   
7178 O  O   . HOH   G .   ? 0.4406 0.5790 0.4463 0.0902  -0.0654 -0.1010 385 HOH   B O   
7179 O  O   . HOH   G .   ? 0.7045 0.5703 0.3762 0.1833  0.0219  -0.0644 386 HOH   B O   
7180 O  O   . HOH   G .   ? 0.5247 0.4666 0.5246 -0.0728 0.0737  -0.0231 387 HOH   B O   
7181 O  O   . HOH   G .   ? 0.2266 0.4031 0.3889 -0.0632 -0.0761 -0.0377 388 HOH   B O   
7182 O  O   . HOH   G .   ? 0.4594 0.3608 0.3018 0.0085  0.0420  -0.0207 389 HOH   B O   
7183 O  O   . HOH   G .   ? 0.3707 0.2148 0.3776 0.0554  -0.0561 0.0269  390 HOH   B O   
7184 O  O   . HOH   G .   ? 0.5234 0.3996 0.4267 0.0374  0.0937  0.0851  391 HOH   B O   
7185 O  O   . HOH   G .   ? 0.4113 0.2157 0.4953 -0.0433 0.0602  0.0394  392 HOH   B O   
7186 O  O   . HOH   G .   ? 0.2517 0.4445 0.6859 -0.1317 -0.0615 -0.0376 393 HOH   B O   
7187 O  O   . HOH   G .   ? 0.4195 0.4480 0.4869 0.0293  0.0945  0.1287  394 HOH   B O   
7188 O  O   . HOH   G .   ? 0.3977 0.5836 0.3748 0.0460  0.0036  -0.1029 395 HOH   B O   
7189 O  O   . HOH   G .   ? 0.3037 0.3702 0.3867 0.0378  0.0140  -0.0752 396 HOH   B O   
7190 O  O   . HOH   G .   ? 0.2066 0.2890 0.5729 -0.0726 -0.0812 0.0334  397 HOH   B O   
7191 O  O   . HOH   G .   ? 0.5720 0.4279 0.3127 -0.2412 -0.0725 0.1308  398 HOH   B O   
7192 O  O   . HOH   G .   ? 0.5181 0.6406 0.6602 0.1452  -0.1325 0.1511  399 HOH   B O   
7193 O  O   . HOH   G .   ? 0.5019 0.6314 0.3517 0.1937  -0.0019 -0.0482 400 HOH   B O   
# 
