data_7HFS
# 
_entry.id   7HFS 
# 
_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   7HFS         pdb_00007hfs 10.2210/pdb7hfs/pdb 
WWPDB D_1001407418 ?            ?                   
# 
_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                        7HFS 
_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 '[(2S)-1-(7H-pyrrolo[2,3-d]pyrimidin-4-yl)-1,2,5,6-tetrahydropyridin-2-yl]methanol' 230.266   1   ? ? ? ? 
3 non-polymer syn 'CHLORIDE ION'                                                                      35.453    1   ? ? ? ? 
4 water       nat water                                                                               18.015    423 ? ? ? ? 
# 
_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 '[(2S)-1-(7H-pyrrolo[2,3-d]pyrimidin-4-yl)-1,2,5,6-tetrahydropyridin-2-yl]methanol' A1BBT 
3 'CHLORIDE ION'                                                                      CL    
4 water                                                                               HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   SER n 
1 2   MET n 
1 3   VAL n 
1 4   ASN n 
1 5   SER n 
1 6   PHE n 
1 7   SER n 
1 8   GLY n 
1 9   TYR n 
1 10  LEU n 
1 11  LYS n 
1 12  LEU n 
1 13  THR n 
1 14  ASP n 
1 15  ASN n 
1 16  VAL n 
1 17  TYR n 
1 18  ILE n 
1 19  LYS n 
1 20  ASN n 
1 21  ALA n 
1 22  ASP n 
1 23  ILE n 
1 24  VAL n 
1 25  GLU n 
1 26  GLU n 
1 27  ALA n 
1 28  LYS n 
1 29  LYS n 
1 30  VAL n 
1 31  LYS n 
1 32  PRO n 
1 33  THR n 
1 34  VAL n 
1 35  VAL n 
1 36  VAL n 
1 37  ASN n 
1 38  ALA n 
1 39  ALA n 
1 40  ASN n 
1 41  VAL n 
1 42  TYR n 
1 43  LEU n 
1 44  LYS n 
1 45  HIS n 
1 46  GLY n 
1 47  GLY n 
1 48  GLY n 
1 49  VAL n 
1 50  ALA n 
1 51  GLY n 
1 52  ALA n 
1 53  LEU n 
1 54  ASN n 
1 55  LYS n 
1 56  ALA n 
1 57  THR n 
1 58  ASN n 
1 59  ASN n 
1 60  ALA n 
1 61  MET n 
1 62  GLN n 
1 63  VAL n 
1 64  GLU n 
1 65  SER n 
1 66  ASP n 
1 67  ASP n 
1 68  TYR n 
1 69  ILE n 
1 70  ALA n 
1 71  THR n 
1 72  ASN n 
1 73  GLY n 
1 74  PRO n 
1 75  LEU n 
1 76  LYS n 
1 77  VAL n 
1 78  GLY n 
1 79  GLY n 
1 80  SER n 
1 81  CYS n 
1 82  VAL n 
1 83  LEU n 
1 84  SER n 
1 85  GLY n 
1 86  HIS n 
1 87  ASN n 
1 88  LEU n 
1 89  ALA n 
1 90  LYS n 
1 91  HIS n 
1 92  CYS n 
1 93  LEU n 
1 94  HIS n 
1 95  VAL n 
1 96  VAL n 
1 97  GLY n 
1 98  PRO n 
1 99  ASN n 
1 100 VAL n 
1 101 ASN n 
1 102 LYS n 
1 103 GLY n 
1 104 GLU n 
1 105 ASP n 
1 106 ILE n 
1 107 GLN n 
1 108 LEU n 
1 109 LEU n 
1 110 LYS n 
1 111 SER n 
1 112 ALA n 
1 113 TYR n 
1 114 GLU n 
1 115 ASN n 
1 116 PHE n 
1 117 ASN n 
1 118 GLN n 
1 119 HIS n 
1 120 GLU n 
1 121 VAL n 
1 122 LEU n 
1 123 LEU n 
1 124 ALA n 
1 125 PRO n 
1 126 LEU n 
1 127 LEU n 
1 128 SER n 
1 129 ALA n 
1 130 GLY n 
1 131 ILE n 
1 132 PHE n 
1 133 GLY n 
1 134 ALA n 
1 135 ASP n 
1 136 PRO n 
1 137 ILE n 
1 138 HIS n 
1 139 SER n 
1 140 LEU n 
1 141 ARG n 
1 142 VAL n 
1 143 CYS n 
1 144 VAL n 
1 145 ASP n 
1 146 THR n 
1 147 VAL n 
1 148 ARG n 
1 149 THR n 
1 150 ASN n 
1 151 VAL n 
1 152 TYR n 
1 153 LEU n 
1 154 ALA n 
1 155 VAL n 
1 156 PHE n 
1 157 ASP n 
1 158 LYS n 
1 159 ASN n 
1 160 LEU n 
1 161 TYR n 
1 162 ASP n 
1 163 LYS n 
1 164 LEU n 
1 165 VAL n 
1 166 SER n 
1 167 SER n 
1 168 PHE n 
1 169 LEU n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   169 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'rep, 1a-1b' 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Severe acute respiratory syndrome coronavirus 2' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     2697049 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          plasmid 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       'pET22b(+)' 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
A1BBT non-polymer         . '[(2S)-1-(7H-pyrrolo[2,3-d]pyrimidin-4-yl)-1,2,5,6-tetrahydropyridin-2-yl]methanol' ? 'C12 H14 N4 O'   
230.266 
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 
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 A1BBT 1   201  201  A1BBT LA1 A . 
D 3 CL    1   202  1    CL    CL  A . 
E 4 HOH   1   1301 1301 HOH   HOH A . 
E 4 HOH   2   1302 409  HOH   HOH A . 
E 4 HOH   3   1303 1289 HOH   HOH A . 
E 4 HOH   4   1304 292  HOH   HOH A . 
E 4 HOH   5   1305 85   HOH   HOH A . 
E 4 HOH   6   1306 153  HOH   HOH A . 
E 4 HOH   7   1307 209  HOH   HOH A . 
E 4 HOH   8   1308 109  HOH   HOH A . 
E 4 HOH   9   1309 93   HOH   HOH A . 
E 4 HOH   10  1310 196  HOH   HOH A . 
E 4 HOH   11  1311 661  HOH   HOH A . 
E 4 HOH   12  1312 625  HOH   HOH A . 
E 4 HOH   13  1313 229  HOH   HOH A . 
E 4 HOH   14  1314 337  HOH   HOH A . 
E 4 HOH   15  1315 247  HOH   HOH A . 
E 4 HOH   16  1316 1295 HOH   HOH A . 
E 4 HOH   17  1317 124  HOH   HOH A . 
E 4 HOH   18  1318 136  HOH   HOH A . 
E 4 HOH   19  1319 76   HOH   HOH A . 
E 4 HOH   20  1320 8    HOH   HOH A . 
E 4 HOH   21  1321 281  HOH   HOH A . 
E 4 HOH   22  1322 78   HOH   HOH A . 
E 4 HOH   23  1323 493  HOH   HOH A . 
E 4 HOH   24  1324 964  HOH   HOH A . 
E 4 HOH   25  1325 49   HOH   HOH A . 
E 4 HOH   26  1326 393  HOH   HOH A . 
E 4 HOH   27  1327 1283 HOH   HOH A . 
E 4 HOH   28  1328 192  HOH   HOH A . 
E 4 HOH   29  1329 164  HOH   HOH A . 
E 4 HOH   30  1330 1310 HOH   HOH A . 
E 4 HOH   31  1331 1275 HOH   HOH A . 
E 4 HOH   32  1332 236  HOH   HOH A . 
E 4 HOH   33  1333 57   HOH   HOH A . 
E 4 HOH   34  1334 1290 HOH   HOH A . 
E 4 HOH   35  1335 132  HOH   HOH A . 
E 4 HOH   36  1336 1300 HOH   HOH A . 
E 4 HOH   37  1337 140  HOH   HOH A . 
E 4 HOH   38  1338 630  HOH   HOH A . 
E 4 HOH   39  1339 36   HOH   HOH A . 
E 4 HOH   40  1340 469  HOH   HOH A . 
E 4 HOH   41  1341 165  HOH   HOH A . 
E 4 HOH   42  1342 26   HOH   HOH A . 
E 4 HOH   43  1343 662  HOH   HOH A . 
E 4 HOH   44  1344 461  HOH   HOH A . 
E 4 HOH   45  1345 151  HOH   HOH A . 
E 4 HOH   46  1346 21   HOH   HOH A . 
E 4 HOH   47  1347 8    HOH   HOH A . 
E 4 HOH   48  1348 396  HOH   HOH A . 
E 4 HOH   49  1349 33   HOH   HOH A . 
E 4 HOH   50  1350 241  HOH   HOH A . 
E 4 HOH   51  1351 199  HOH   HOH A . 
E 4 HOH   52  1352 102  HOH   HOH A . 
E 4 HOH   53  1353 320  HOH   HOH A . 
E 4 HOH   54  1354 17   HOH   HOH A . 
E 4 HOH   55  1355 42   HOH   HOH A . 
E 4 HOH   56  1356 74   HOH   HOH A . 
E 4 HOH   57  1357 105  HOH   HOH A . 
E 4 HOH   58  1358 405  HOH   HOH A . 
E 4 HOH   59  1359 18   HOH   HOH A . 
E 4 HOH   60  1360 225  HOH   HOH A . 
E 4 HOH   61  1361 86   HOH   HOH A . 
E 4 HOH   62  1362 1309 HOH   HOH A . 
E 4 HOH   63  1363 169  HOH   HOH A . 
E 4 HOH   64  1364 7    HOH   HOH A . 
E 4 HOH   65  1365 92   HOH   HOH A . 
E 4 HOH   66  1366 34   HOH   HOH A . 
E 4 HOH   67  1367 162  HOH   HOH A . 
E 4 HOH   68  1368 66   HOH   HOH A . 
E 4 HOH   69  1369 354  HOH   HOH A . 
E 4 HOH   70  1370 17   HOH   HOH A . 
E 4 HOH   71  1371 2    HOH   HOH A . 
E 4 HOH   72  1372 139  HOH   HOH A . 
E 4 HOH   73  1373 45   HOH   HOH A . 
E 4 HOH   74  1374 70   HOH   HOH A . 
E 4 HOH   75  1375 138  HOH   HOH A . 
E 4 HOH   76  1376 2    HOH   HOH A . 
E 4 HOH   77  1377 5    HOH   HOH A . 
E 4 HOH   78  1378 218  HOH   HOH A . 
E 4 HOH   79  1379 19   HOH   HOH A . 
E 4 HOH   80  1380 46   HOH   HOH A . 
E 4 HOH   81  1381 939  HOH   HOH A . 
E 4 HOH   82  1382 159  HOH   HOH A . 
E 4 HOH   83  1383 56   HOH   HOH A . 
E 4 HOH   84  1384 366  HOH   HOH A . 
E 4 HOH   85  1385 62   HOH   HOH A . 
E 4 HOH   86  1386 381  HOH   HOH A . 
E 4 HOH   87  1387 186  HOH   HOH A . 
E 4 HOH   88  1388 155  HOH   HOH A . 
E 4 HOH   89  1389 27   HOH   HOH A . 
E 4 HOH   90  1390 134  HOH   HOH A . 
E 4 HOH   91  1391 1313 HOH   HOH A . 
E 4 HOH   92  1392 81   HOH   HOH A . 
E 4 HOH   93  1393 122  HOH   HOH A . 
E 4 HOH   94  1394 296  HOH   HOH A . 
E 4 HOH   95  1395 4    HOH   HOH A . 
E 4 HOH   96  1396 35   HOH   HOH A . 
E 4 HOH   97  1397 154  HOH   HOH A . 
E 4 HOH   98  1398 3    HOH   HOH A . 
E 4 HOH   99  1399 39   HOH   HOH A . 
E 4 HOH   100 1400 5    HOH   HOH A . 
E 4 HOH   101 1401 58   HOH   HOH A . 
E 4 HOH   102 1402 83   HOH   HOH A . 
E 4 HOH   103 1403 116  HOH   HOH A . 
E 4 HOH   104 1404 1308 HOH   HOH A . 
E 4 HOH   105 1405 6    HOH   HOH A . 
E 4 HOH   106 1406 96   HOH   HOH A . 
E 4 HOH   107 1407 67   HOH   HOH A . 
E 4 HOH   108 1408 12   HOH   HOH A . 
E 4 HOH   109 1409 1315 HOH   HOH A . 
E 4 HOH   110 1410 582  HOH   HOH A . 
E 4 HOH   111 1411 121  HOH   HOH A . 
E 4 HOH   112 1412 351  HOH   HOH A . 
E 4 HOH   113 1413 7    HOH   HOH A . 
E 4 HOH   114 1414 195  HOH   HOH A . 
E 4 HOH   115 1415 148  HOH   HOH A . 
E 4 HOH   116 1416 397  HOH   HOH A . 
E 4 HOH   117 1417 15   HOH   HOH A . 
E 4 HOH   118 1418 278  HOH   HOH A . 
E 4 HOH   119 1419 24   HOH   HOH A . 
E 4 HOH   120 1420 68   HOH   HOH A . 
E 4 HOH   121 1421 123  HOH   HOH A . 
E 4 HOH   122 1422 333  HOH   HOH A . 
E 4 HOH   123 1423 53   HOH   HOH A . 
E 4 HOH   124 1424 1068 HOH   HOH A . 
E 4 HOH   125 1425 156  HOH   HOH A . 
E 4 HOH   126 1426 212  HOH   HOH A . 
E 4 HOH   127 1427 25   HOH   HOH A . 
E 4 HOH   128 1428 303  HOH   HOH A . 
E 4 HOH   129 1429 125  HOH   HOH A . 
E 4 HOH   130 1430 95   HOH   HOH A . 
E 4 HOH   131 1431 1222 HOH   HOH A . 
E 4 HOH   132 1432 51   HOH   HOH A . 
E 4 HOH   133 1433 11   HOH   HOH A . 
E 4 HOH   134 1434 1296 HOH   HOH A . 
E 4 HOH   135 1435 1279 HOH   HOH A . 
E 4 HOH   136 1436 115  HOH   HOH A . 
E 4 HOH   137 1437 16   HOH   HOH A . 
E 4 HOH   138 1438 1286 HOH   HOH A . 
E 4 HOH   139 1439 71   HOH   HOH A . 
E 4 HOH   140 1440 1094 HOH   HOH A . 
E 4 HOH   141 1441 12   HOH   HOH A . 
E 4 HOH   142 1442 80   HOH   HOH A . 
E 4 HOH   143 1443 73   HOH   HOH A . 
E 4 HOH   144 1444 40   HOH   HOH A . 
E 4 HOH   145 1445 94   HOH   HOH A . 
E 4 HOH   146 1446 104  HOH   HOH A . 
E 4 HOH   147 1447 944  HOH   HOH A . 
E 4 HOH   148 1448 1189 HOH   HOH A . 
E 4 HOH   149 1449 188  HOH   HOH A . 
E 4 HOH   150 1450 97   HOH   HOH A . 
E 4 HOH   151 1451 3    HOH   HOH A . 
E 4 HOH   152 1452 952  HOH   HOH A . 
E 4 HOH   153 1453 1238 HOH   HOH A . 
E 4 HOH   154 1454 576  HOH   HOH A . 
E 4 HOH   155 1455 79   HOH   HOH A . 
E 4 HOH   156 1456 330  HOH   HOH A . 
E 4 HOH   157 1457 1119 HOH   HOH A . 
E 4 HOH   158 1458 1134 HOH   HOH A . 
E 4 HOH   159 1459 509  HOH   HOH A . 
E 4 HOH   160 1460 107  HOH   HOH A . 
E 4 HOH   161 1461 163  HOH   HOH A . 
E 4 HOH   162 1462 1276 HOH   HOH A . 
E 4 HOH   163 1463 408  HOH   HOH A . 
E 4 HOH   164 1464 726  HOH   HOH A . 
E 4 HOH   165 1465 756  HOH   HOH A . 
E 4 HOH   166 1466 6    HOH   HOH A . 
E 4 HOH   167 1467 361  HOH   HOH A . 
E 4 HOH   168 1468 280  HOH   HOH A . 
E 4 HOH   169 1469 319  HOH   HOH A . 
E 4 HOH   170 1470 556  HOH   HOH A . 
E 4 HOH   171 1471 126  HOH   HOH A . 
E 4 HOH   172 1472 63   HOH   HOH A . 
E 4 HOH   173 1473 801  HOH   HOH A . 
E 4 HOH   174 1474 250  HOH   HOH A . 
E 4 HOH   175 1475 1307 HOH   HOH A . 
E 4 HOH   176 1476 342  HOH   HOH A . 
E 4 HOH   177 1477 202  HOH   HOH A . 
E 4 HOH   178 1478 135  HOH   HOH A . 
E 4 HOH   179 1479 1287 HOH   HOH A . 
E 4 HOH   180 1480 370  HOH   HOH A . 
E 4 HOH   181 1481 1306 HOH   HOH A . 
E 4 HOH   182 1482 224  HOH   HOH A . 
E 4 HOH   183 1483 267  HOH   HOH A . 
E 4 HOH   184 1484 674  HOH   HOH A . 
E 4 HOH   185 1485 521  HOH   HOH A . 
E 4 HOH   186 1486 695  HOH   HOH A . 
E 4 HOH   187 1487 919  HOH   HOH A . 
E 4 HOH   188 1488 318  HOH   HOH A . 
E 4 HOH   189 1489 1299 HOH   HOH A . 
E 4 HOH   190 1490 309  HOH   HOH A . 
E 4 HOH   191 1491 711  HOH   HOH A . 
E 4 HOH   192 1492 315  HOH   HOH A . 
E 4 HOH   193 1493 331  HOH   HOH A . 
E 4 HOH   194 1494 152  HOH   HOH A . 
E 4 HOH   195 1495 805  HOH   HOH A . 
E 4 HOH   196 1496 208  HOH   HOH A . 
E 4 HOH   197 1497 356  HOH   HOH A . 
E 4 HOH   198 1498 941  HOH   HOH A . 
E 4 HOH   199 1499 263  HOH   HOH A . 
E 4 HOH   200 1500 326  HOH   HOH A . 
E 4 HOH   201 1501 1314 HOH   HOH A . 
E 4 HOH   202 1502 1071 HOH   HOH A . 
E 4 HOH   203 1503 9    HOH   HOH A . 
E 4 HOH   204 1504 180  HOH   HOH A . 
E 4 HOH   205 1505 363  HOH   HOH A . 
E 4 HOH   206 1506 371  HOH   HOH A . 
E 4 HOH   207 1507 16   HOH   HOH A . 
E 4 HOH   208 1508 4    HOH   HOH A . 
E 4 HOH   209 1509 313  HOH   HOH A . 
E 4 HOH   210 1510 10   HOH   HOH A . 
E 4 HOH   211 1511 1284 HOH   HOH A . 
E 4 HOH   212 1512 429  HOH   HOH A . 
E 4 HOH   213 1513 185  HOH   HOH A . 
E 4 HOH   214 1514 14   HOH   HOH A . 
E 4 HOH   215 1515 772  HOH   HOH A . 
E 4 HOH   216 1516 376  HOH   HOH A . 
E 4 HOH   217 1517 1074 HOH   HOH A . 
E 4 HOH   218 1518 346  HOH   HOH A . 
E 4 HOH   219 1519 1292 HOH   HOH A . 
E 4 HOH   220 1520 13   HOH   HOH A . 
E 4 HOH   221 1521 1078 HOH   HOH A . 
F 4 HOH   1   201  64   HOH   HOH B . 
F 4 HOH   2   202  549  HOH   HOH B . 
F 4 HOH   3   203  240  HOH   HOH B . 
F 4 HOH   4   204  398  HOH   HOH B . 
F 4 HOH   5   205  364  HOH   HOH B . 
F 4 HOH   6   206  900  HOH   HOH B . 
F 4 HOH   7   207  1249 HOH   HOH B . 
F 4 HOH   8   208  358  HOH   HOH B . 
F 4 HOH   9   209  531  HOH   HOH B . 
F 4 HOH   10  210  120  HOH   HOH B . 
F 4 HOH   11  211  205  HOH   HOH B . 
F 4 HOH   12  212  452  HOH   HOH B . 
F 4 HOH   13  213  232  HOH   HOH B . 
F 4 HOH   14  214  758  HOH   HOH B . 
F 4 HOH   15  215  50   HOH   HOH B . 
F 4 HOH   16  216  264  HOH   HOH B . 
F 4 HOH   17  217  654  HOH   HOH B . 
F 4 HOH   18  218  343  HOH   HOH B . 
F 4 HOH   19  219  15   HOH   HOH B . 
F 4 HOH   20  220  353  HOH   HOH B . 
F 4 HOH   21  221  444  HOH   HOH B . 
F 4 HOH   22  222  743  HOH   HOH B . 
F 4 HOH   23  223  332  HOH   HOH B . 
F 4 HOH   24  224  82   HOH   HOH B . 
F 4 HOH   25  225  75   HOH   HOH B . 
F 4 HOH   26  226  54   HOH   HOH B . 
F 4 HOH   27  227  128  HOH   HOH B . 
F 4 HOH   28  228  1312 HOH   HOH B . 
F 4 HOH   29  229  131  HOH   HOH B . 
F 4 HOH   30  230  1278 HOH   HOH B . 
F 4 HOH   31  231  127  HOH   HOH B . 
F 4 HOH   32  232  166  HOH   HOH B . 
F 4 HOH   33  233  129  HOH   HOH B . 
F 4 HOH   34  234  110  HOH   HOH B . 
F 4 HOH   35  235  60   HOH   HOH B . 
F 4 HOH   36  236  325  HOH   HOH B . 
F 4 HOH   37  237  300  HOH   HOH B . 
F 4 HOH   38  238  272  HOH   HOH B . 
F 4 HOH   39  239  276  HOH   HOH B . 
F 4 HOH   40  240  172  HOH   HOH B . 
F 4 HOH   41  241  69   HOH   HOH B . 
F 4 HOH   42  242  1140 HOH   HOH B . 
F 4 HOH   43  243  181  HOH   HOH B . 
F 4 HOH   44  244  72   HOH   HOH B . 
F 4 HOH   45  245  9    HOH   HOH B . 
F 4 HOH   46  246  150  HOH   HOH B . 
F 4 HOH   47  247  143  HOH   HOH B . 
F 4 HOH   48  248  52   HOH   HOH B . 
F 4 HOH   49  249  14   HOH   HOH B . 
F 4 HOH   50  250  30   HOH   HOH B . 
F 4 HOH   51  251  133  HOH   HOH B . 
F 4 HOH   52  252  31   HOH   HOH B . 
F 4 HOH   53  253  1    HOH   HOH B . 
F 4 HOH   54  254  723  HOH   HOH B . 
F 4 HOH   55  255  144  HOH   HOH B . 
F 4 HOH   56  256  41   HOH   HOH B . 
F 4 HOH   57  257  282  HOH   HOH B . 
F 4 HOH   58  258  243  HOH   HOH B . 
F 4 HOH   59  259  47   HOH   HOH B . 
F 4 HOH   60  260  347  HOH   HOH B . 
F 4 HOH   61  261  271  HOH   HOH B . 
F 4 HOH   62  262  391  HOH   HOH B . 
F 4 HOH   63  263  221  HOH   HOH B . 
F 4 HOH   64  264  287  HOH   HOH B . 
F 4 HOH   65  265  10   HOH   HOH B . 
F 4 HOH   66  266  84   HOH   HOH B . 
F 4 HOH   67  267  1305 HOH   HOH B . 
F 4 HOH   68  268  59   HOH   HOH B . 
F 4 HOH   69  269  231  HOH   HOH B . 
F 4 HOH   70  270  1277 HOH   HOH B . 
F 4 HOH   71  271  61   HOH   HOH B . 
F 4 HOH   72  272  20   HOH   HOH B . 
F 4 HOH   73  273  175  HOH   HOH B . 
F 4 HOH   74  274  242  HOH   HOH B . 
F 4 HOH   75  275  416  HOH   HOH B . 
F 4 HOH   76  276  117  HOH   HOH B . 
F 4 HOH   77  277  114  HOH   HOH B . 
F 4 HOH   78  278  302  HOH   HOH B . 
F 4 HOH   79  279  11   HOH   HOH B . 
F 4 HOH   80  280  147  HOH   HOH B . 
F 4 HOH   81  281  103  HOH   HOH B . 
F 4 HOH   82  282  77   HOH   HOH B . 
F 4 HOH   83  283  43   HOH   HOH B . 
F 4 HOH   84  284  1106 HOH   HOH B . 
F 4 HOH   85  285  22   HOH   HOH B . 
F 4 HOH   86  286  13   HOH   HOH B . 
F 4 HOH   87  287  88   HOH   HOH B . 
F 4 HOH   88  288  89   HOH   HOH B . 
F 4 HOH   89  289  1066 HOH   HOH B . 
F 4 HOH   90  290  106  HOH   HOH B . 
F 4 HOH   91  291  445  HOH   HOH B . 
F 4 HOH   92  292  235  HOH   HOH B . 
F 4 HOH   93  293  137  HOH   HOH B . 
F 4 HOH   94  294  160  HOH   HOH B . 
F 4 HOH   95  295  1285 HOH   HOH B . 
F 4 HOH   96  296  99   HOH   HOH B . 
F 4 HOH   97  297  252  HOH   HOH B . 
F 4 HOH   98  298  112  HOH   HOH B . 
F 4 HOH   99  299  216  HOH   HOH B . 
F 4 HOH   100 300  32   HOH   HOH B . 
F 4 HOH   101 301  387  HOH   HOH B . 
F 4 HOH   102 302  118  HOH   HOH B . 
F 4 HOH   103 303  38   HOH   HOH B . 
F 4 HOH   104 304  316  HOH   HOH B . 
F 4 HOH   105 305  297  HOH   HOH B . 
F 4 HOH   106 306  101  HOH   HOH B . 
F 4 HOH   107 307  170  HOH   HOH B . 
F 4 HOH   108 308  215  HOH   HOH B . 
F 4 HOH   109 309  311  HOH   HOH B . 
F 4 HOH   110 310  142  HOH   HOH B . 
F 4 HOH   111 311  91   HOH   HOH B . 
F 4 HOH   112 312  37   HOH   HOH B . 
F 4 HOH   113 313  704  HOH   HOH B . 
F 4 HOH   114 314  299  HOH   HOH B . 
F 4 HOH   115 315  177  HOH   HOH B . 
F 4 HOH   116 316  220  HOH   HOH B . 
F 4 HOH   117 317  23   HOH   HOH B . 
F 4 HOH   118 318  44   HOH   HOH B . 
F 4 HOH   119 319  48   HOH   HOH B . 
F 4 HOH   120 320  341  HOH   HOH B . 
F 4 HOH   121 321  197  HOH   HOH B . 
F 4 HOH   122 322  28   HOH   HOH B . 
F 4 HOH   123 323  1274 HOH   HOH B . 
F 4 HOH   124 324  635  HOH   HOH B . 
F 4 HOH   125 325  182  HOH   HOH B . 
F 4 HOH   126 326  1291 HOH   HOH B . 
F 4 HOH   127 327  100  HOH   HOH B . 
F 4 HOH   128 328  55   HOH   HOH B . 
F 4 HOH   129 329  29   HOH   HOH B . 
F 4 HOH   130 330  717  HOH   HOH B . 
F 4 HOH   131 331  141  HOH   HOH B . 
F 4 HOH   132 332  98   HOH   HOH B . 
F 4 HOH   133 333  207  HOH   HOH B . 
F 4 HOH   134 334  161  HOH   HOH B . 
F 4 HOH   135 335  1126 HOH   HOH B . 
F 4 HOH   136 336  234  HOH   HOH B . 
F 4 HOH   137 337  1294 HOH   HOH B . 
F 4 HOH   138 338  65   HOH   HOH B . 
F 4 HOH   139 339  334  HOH   HOH B . 
F 4 HOH   140 340  362  HOH   HOH B . 
F 4 HOH   141 341  1293 HOH   HOH B . 
F 4 HOH   142 342  619  HOH   HOH B . 
F 4 HOH   143 343  339  HOH   HOH B . 
F 4 HOH   144 344  178  HOH   HOH B . 
F 4 HOH   145 345  87   HOH   HOH B . 
F 4 HOH   146 346  960  HOH   HOH B . 
F 4 HOH   147 347  463  HOH   HOH B . 
F 4 HOH   148 348  90   HOH   HOH B . 
F 4 HOH   149 349  1280 HOH   HOH B . 
F 4 HOH   150 350  623  HOH   HOH B . 
F 4 HOH   151 351  191  HOH   HOH B . 
F 4 HOH   152 352  1304 HOH   HOH B . 
F 4 HOH   153 353  335  HOH   HOH B . 
F 4 HOH   154 354  1046 HOH   HOH B . 
F 4 HOH   155 355  304  HOH   HOH B . 
F 4 HOH   156 356  203  HOH   HOH B . 
F 4 HOH   157 357  290  HOH   HOH B . 
F 4 HOH   158 358  479  HOH   HOH B . 
F 4 HOH   159 359  1077 HOH   HOH B . 
F 4 HOH   160 360  389  HOH   HOH B . 
F 4 HOH   161 361  541  HOH   HOH B . 
F 4 HOH   162 362  718  HOH   HOH B . 
F 4 HOH   163 363  1072 HOH   HOH B . 
F 4 HOH   164 364  283  HOH   HOH B . 
F 4 HOH   165 365  291  HOH   HOH B . 
F 4 HOH   166 366  898  HOH   HOH B . 
F 4 HOH   167 367  1316 HOH   HOH B . 
F 4 HOH   168 368  373  HOH   HOH B . 
F 4 HOH   169 369  340  HOH   HOH B . 
F 4 HOH   170 370  615  HOH   HOH B . 
F 4 HOH   171 371  667  HOH   HOH B . 
F 4 HOH   172 372  310  HOH   HOH B . 
F 4 HOH   173 373  190  HOH   HOH B . 
F 4 HOH   174 374  1303 HOH   HOH B . 
F 4 HOH   175 375  1173 HOH   HOH B . 
F 4 HOH   176 376  431  HOH   HOH B . 
F 4 HOH   177 377  183  HOH   HOH B . 
F 4 HOH   178 378  1163 HOH   HOH B . 
F 4 HOH   179 379  149  HOH   HOH B . 
F 4 HOH   180 380  1000 HOH   HOH B . 
F 4 HOH   181 381  418  HOH   HOH B . 
F 4 HOH   182 382  1311 HOH   HOH B . 
F 4 HOH   183 383  176  HOH   HOH B . 
F 4 HOH   184 384  424  HOH   HOH B . 
F 4 HOH   185 385  491  HOH   HOH B . 
F 4 HOH   186 386  1298 HOH   HOH B . 
F 4 HOH   187 387  981  HOH   HOH B . 
F 4 HOH   188 388  248  HOH   HOH B . 
F 4 HOH   189 389  470  HOH   HOH B . 
F 4 HOH   190 390  265  HOH   HOH B . 
F 4 HOH   191 391  350  HOH   HOH B . 
F 4 HOH   192 392  184  HOH   HOH B . 
F 4 HOH   193 393  360  HOH   HOH B . 
F 4 HOH   194 394  410  HOH   HOH B . 
F 4 HOH   195 395  355  HOH   HOH B . 
F 4 HOH   196 396  274  HOH   HOH B . 
F 4 HOH   197 397  314  HOH   HOH B . 
F 4 HOH   198 398  566  HOH   HOH B . 
F 4 HOH   199 399  157  HOH   HOH B . 
F 4 HOH   200 400  321  HOH   HOH B . 
F 4 HOH   201 401  792  HOH   HOH B . 
F 4 HOH   202 402  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           7HFS 
_cell.length_a           88.827 
_cell.length_b           88.827 
_cell.length_c           39.470 
_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                         7HFS 
_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          7HFS 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_Matthews      2.14 
_exptl_crystal.density_percent_sol   42.67 
_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   2023-10-27 
_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                     7HFS 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             44.410 
_reflns.d_resolution_high            1.020 
_reflns.number_obs                   156367 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         99.800 
_reflns.pdbx_Rmerge_I_obs            0.070 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        12.000 
_reflns.B_iso_Wilson_estimate        11.680 
_reflns.pdbx_redundancy              6.500 
_reflns.pdbx_Rrim_I_all              0.076 
_reflns.pdbx_Rpim_I_all              0.029 
_reflns.pdbx_CC_half                 0.997 
_reflns.pdbx_netI_over_av_sigmaI     ? 
_reflns.pdbx_number_measured_all     1016509 
_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 1.020 1.040  ? 43889 7581 ? 0.854 ? ? ? 5.800 ? 1.300  ? ? ? ? ? ? 97.900 0.940 0.384 0.813 
1 2 5.590 44.410 ? 7086  1036 ? 0.059 ? ? ? 6.800 ? 30.100 ? ? ? ? ? ? 99.800 0.064 0.024 0.994 
# 
_refine.entry_id                                 7HFS 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_d_res_high                            1.0200 
_refine.ls_d_res_low                             44.4100 
_refine.pdbx_ls_sigma_F                          1.370 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.ls_percent_reflns_obs                    99.7900 
_refine.ls_number_reflns_obs                     156307 
_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                          0.1394 
_refine.ls_R_factor_R_work                       0.1388 
_refine.ls_wR_factor_R_work                      ? 
_refine.ls_R_factor_R_free                       0.1524 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_percent_reflns_R_free                 4.8200 
_refine.ls_number_reflns_R_free                  7540 
_refine.ls_number_reflns_R_work                  148767 
_refine.ls_R_factor_R_free_error                 ? 
_refine.B_iso_mean                               18.6250 
_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                            0.0900 
_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                                76.190 
_refine.B_iso_min                                8.530 
_refine.pdbx_overall_phase_error                 14.9000 
_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                       1.0200 
_refine_hist.d_res_low                        44.4100 
_refine_hist.pdbx_number_atoms_ligand         32 
_refine_hist.number_atoms_solvent             423 
_refine_hist.number_atoms_total               2997 
_refine_hist.pdbx_number_residues_total       336 
_refine_hist.pdbx_B_iso_mean_ligand           14.58 
_refine_hist.pdbx_B_iso_mean_solvent          30.81 
_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 
1.0200 1.0300  30 97.0000  4814 . 0.3034 0.3124 . 206 0.0000 5020 . 'X-RAY DIFFRACTION' 
1.0300 1.0400  30 100.0000 4937 . 0.2362 0.2278 . 277 0.0000 5214 . 'X-RAY DIFFRACTION' 
1.0400 1.0600  30 100.0000 4929 . 0.2032 0.1952 . 271 0.0000 5200 . 'X-RAY DIFFRACTION' 
1.0600 1.0700  30 100.0000 4884 . 0.1887 0.2019 . 276 0.0000 5160 . 'X-RAY DIFFRACTION' 
1.0700 1.0800  30 100.0000 4921 . 0.1927 0.2054 . 245 0.0000 5166 . 'X-RAY DIFFRACTION' 
1.0800 1.1000  30 100.0000 4963 . 0.1837 0.2040 . 236 0.0000 5199 . 'X-RAY DIFFRACTION' 
1.1000 1.1100  30 100.0000 4920 . 0.1695 0.1995 . 267 0.0000 5187 . 'X-RAY DIFFRACTION' 
1.1100 1.1300  30 100.0000 5020 . 0.1555 0.1690 . 219 0.0000 5239 . 'X-RAY DIFFRACTION' 
1.1300 1.1500  30 100.0000 4885 . 0.1474 0.1636 . 242 0.0000 5127 . 'X-RAY DIFFRACTION' 
1.1500 1.1700  30 100.0000 4999 . 0.1302 0.1591 . 252 0.0000 5251 . 'X-RAY DIFFRACTION' 
1.1700 1.1900  30 100.0000 4924 . 0.1282 0.1580 . 254 0.0000 5178 . 'X-RAY DIFFRACTION' 
1.1900 1.2100  30 100.0000 4879 . 0.1190 0.1539 . 265 0.0000 5144 . 'X-RAY DIFFRACTION' 
1.2100 1.2300  30 100.0000 5039 . 0.1158 0.1411 . 226 0.0000 5265 . 'X-RAY DIFFRACTION' 
1.2300 1.2600  30 100.0000 4927 . 0.1208 0.1305 . 246 0.0000 5173 . 'X-RAY DIFFRACTION' 
1.2600 1.2900  30 100.0000 4948 . 0.1213 0.1360 . 252 0.0000 5200 . 'X-RAY DIFFRACTION' 
1.2900 1.3100  30 100.0000 4966 . 0.1208 0.1427 . 266 0.0000 5232 . 'X-RAY DIFFRACTION' 
1.3200 1.3500  30 100.0000 4936 . 0.1296 0.1481 . 242 0.0000 5178 . 'X-RAY DIFFRACTION' 
1.3500 1.3800  30 100.0000 4948 . 0.1287 0.1513 . 264 0.0000 5212 . 'X-RAY DIFFRACTION' 
1.3800 1.4300  30 100.0000 4977 . 0.1244 0.1562 . 234 0.0000 5211 . 'X-RAY DIFFRACTION' 
1.4300 1.4700  30 100.0000 4962 . 0.1209 0.1263 . 250 0.0000 5212 . 'X-RAY DIFFRACTION' 
1.4700 1.5200  30 100.0000 4976 . 0.1146 0.1256 . 239 0.0000 5215 . 'X-RAY DIFFRACTION' 
1.5200 1.5800  30 100.0000 4963 . 0.1153 0.1269 . 264 0.0000 5227 . 'X-RAY DIFFRACTION' 
1.5800 1.6600  30 100.0000 4939 . 0.1197 0.1334 . 264 0.0000 5203 . 'X-RAY DIFFRACTION' 
1.6600 1.7400  30 100.0000 5029 . 0.1256 0.1401 . 206 0.0000 5235 . 'X-RAY DIFFRACTION' 
1.7400 1.8500  30 100.0000 4946 . 0.1297 0.1299 . 285 0.0000 5231 . 'X-RAY DIFFRACTION' 
1.8500 2.0000  30 100.0000 4984 . 0.1319 0.1270 . 249 0.0000 5233 . 'X-RAY DIFFRACTION' 
2.0000 2.2000  30 100.0000 4950 . 0.1344 0.1416 . 287 0.0000 5237 . 'X-RAY DIFFRACTION' 
2.2000 2.5100  30 100.0000 5014 . 0.1355 0.1377 . 252 0.0000 5266 . 'X-RAY DIFFRACTION' 
2.5200 3.1700  30 100.0000 5015 . 0.1489 0.1637 . 253 0.0000 5268 . 'X-RAY DIFFRACTION' 
3.1700 44.4100 30 100.0000 5173 . 0.1485 0.1760 . 251 0.0000 5424 . 'X-RAY DIFFRACTION' 
# 
_struct.entry_id                  7HFS 
_struct.title                     
'PanDDA analysis group deposition -- Crystal structure of SARS-CoV-2 NSP3 macrodomain in complex with AVI-0005998' 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_details        ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HFS 
_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 4 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    R1AB_SARS2 
_struct_ref.pdbx_db_accession          P0DTD1 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;VNSFSGYLKLTDNVYIKNADIVEEAKKVKPTVVVNAANVYLKHGGGVAGALNKATNNAMQVESDDYIATNGPLKVGGSCV
LSGHNLAKHCLHVVGPNVNKGEDIQLLKSAYENFNQHEVLLAPLLSAGIFGADPIHSLRVCVDTVRTNVYLAVFDKNLYD
KLVSSFL
;
_struct_ref.pdbx_align_begin           1025 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 7HFS A 3 ? 169 ? P0DTD1 1025 ? 1191 ? 3 169 
2 1 7HFS 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 7HFS SER A 1 ? UNP P0DTD1 ? ? 'expression tag' 1 1 
1 7HFS MET A 2 ? UNP P0DTD1 ? ? 'expression tag' 2 2 
2 7HFS SER B 1 ? UNP P0DTD1 ? ? 'expression tag' 1 3 
2 7HFS 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 
2 1 B,F     
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 ASP A 22  ? LYS A 31  ? ASP A 22  LYS A 31  1 ? 10 
HELX_P HELX_P2  AA2 GLY A 47  ? THR A 57  ? GLY A 47  THR A 57  1 ? 11 
HELX_P HELX_P3  AA3 ASN A 59  ? GLY A 73  ? ASN A 59  GLY A 73  1 ? 15 
HELX_P HELX_P4  AA4 ASN A 99  ? GLY A 103 ? ASN A 99  GLY A 103 5 ? 5  
HELX_P HELX_P5  AA5 GLN A 107 ? ASN A 115 ? GLN A 107 ASN A 115 1 ? 9  
HELX_P HELX_P6  AA6 PHE A 116 ? HIS A 119 ? PHE A 116 HIS A 119 5 ? 4  
HELX_P HELX_P7  AA7 ALA A 129 ? GLY A 133 ? ALA A 129 GLY A 133 5 ? 5  
HELX_P HELX_P8  AA8 ASP A 135 ? VAL A 147 ? ASP A 135 VAL A 147 1 ? 13 
HELX_P HELX_P9  AA9 ASP A 157 ? SER A 167 ? ASP A 157 SER A 167 1 ? 11 
HELX_P HELX_P10 AB1 ASP B 22  ? LYS B 31  ? ASP B 22  LYS B 31  1 ? 10 
HELX_P HELX_P11 AB2 GLY B 47  ? THR B 57  ? GLY B 47  THR B 57  1 ? 11 
HELX_P HELX_P12 AB3 ASN B 59  ? GLY B 73  ? ASN B 59  GLY B 73  1 ? 15 
HELX_P HELX_P13 AB4 ASN B 99  ? GLY B 103 ? ASN B 99  GLY B 103 5 ? 5  
HELX_P HELX_P14 AB5 ASP B 105 ? GLN B 107 ? ASP B 105 GLN B 107 5 ? 3  
HELX_P HELX_P15 AB6 LEU B 108 ? ASN B 115 ? LEU B 108 ASN B 115 1 ? 8  
HELX_P HELX_P16 AB7 PHE B 116 ? HIS B 119 ? PHE B 116 HIS B 119 5 ? 4  
HELX_P HELX_P17 AB8 ALA B 129 ? GLY B 133 ? ALA B 129 GLY B 133 5 ? 5  
HELX_P HELX_P18 AB9 ASP B 135 ? VAL B 147 ? ASP B 135 VAL B 147 1 ? 13 
HELX_P HELX_P19 AC1 ASP B 157 ? LEU B 169 ? ASP B 157 LEU B 169 1 ? 13 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 4 ? 
AA2 ? 3 ? 
AA3 ? 4 ? 
AA4 ? 3 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? parallel      
AA1 3 4 ? parallel      
AA2 1 2 ? parallel      
AA2 2 3 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? parallel      
AA3 3 4 ? parallel      
AA4 1 2 ? parallel      
AA4 2 3 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 LEU A 10  ? LYS A 11  ? LEU A 10  LYS A 11  
AA1 2 VAL A 16  ? ASN A 20  ? VAL A 16  ASN A 20  
AA1 3 ASN A 150 ? VAL A 155 ? ASN A 150 VAL A 155 
AA1 4 VAL A 121 ? ALA A 124 ? VAL A 121 ALA A 124 
AA2 1 VAL A 34  ? ALA A 38  ? VAL A 34  ALA A 38  
AA2 2 HIS A 91  ? VAL A 95  ? HIS A 91  VAL A 95  
AA2 3 SER A 80  ? SER A 84  ? SER A 80  SER A 84  
AA3 1 LEU B 10  ? LYS B 11  ? LEU B 10  LYS B 11  
AA3 2 VAL B 16  ? ASN B 20  ? VAL B 16  ASN B 20  
AA3 3 ASN B 150 ? VAL B 155 ? ASN B 150 VAL B 155 
AA3 4 VAL B 121 ? ALA B 124 ? VAL B 121 ALA B 124 
AA4 1 VAL B 34  ? ALA B 38  ? VAL B 34  ALA B 38  
AA4 2 HIS B 91  ? VAL B 95  ? HIS B 91  VAL B 95  
AA4 3 SER B 80  ? SER B 84  ? SER B 80  SER B 84  
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N LEU A 10  ? N LEU A 10  O ILE A 18  ? O ILE A 18  
AA1 2 3 N LYS A 19  ? N LYS A 19  O VAL A 155 ? O VAL A 155 
AA1 3 4 O TYR A 152 ? O TYR A 152 N LEU A 122 ? N LEU A 122 
AA2 1 2 N ASN A 37  ? N ASN A 37  O VAL A 95  ? O VAL A 95  
AA2 2 3 O CYS A 92  ? O CYS A 92  N LEU A 83  ? N LEU A 83  
AA3 1 2 N LEU B 10  ? N LEU B 10  O ILE B 18  ? O ILE B 18  
AA3 2 3 N TYR B 17  ? N TYR B 17  O LEU B 153 ? O LEU B 153 
AA3 3 4 O TYR B 152 ? O TYR B 152 N 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 CYS B 92  ? O CYS B 92  N LEU B 83  ? N LEU B 83  
# 
_pdbx_entry_details.entry_id                   7HFS 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 HIS A 86  ? ? 55.49  -132.74 
2 1 SER A 128 ? B 69.95  -12.26  
3 1 ALA A 129 ? B -85.19 -150.15 
4 1 HIS B 86  ? ? 57.52  -127.87 
# 
_phasing.method   MR 
# 
loop_
_pdbx_distant_solvent_atoms.id 
_pdbx_distant_solvent_atoms.PDB_model_num 
_pdbx_distant_solvent_atoms.auth_atom_id 
_pdbx_distant_solvent_atoms.label_alt_id 
_pdbx_distant_solvent_atoms.auth_asym_id 
_pdbx_distant_solvent_atoms.auth_comp_id 
_pdbx_distant_solvent_atoms.auth_seq_id 
_pdbx_distant_solvent_atoms.PDB_ins_code 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance 
1 1 O ? A HOH 1519 ? 6.12 . 
2 1 O B A HOH 1520 ? 6.40 . 
3 1 O ? A HOH 1521 ? 7.53 . 
4 1 O ? B HOH 402  ? 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 
A1BBT N2   N  Y N 1   
A1BBT C3   C  N N 2   
A1BBT C6   C  N N 3   
A1BBT C9   C  Y N 4   
A1BBT C12  C  Y N 5   
A1BBT C1   C  N N 6   
A1BBT C10  C  Y N 7   
A1BBT C11  C  Y N 8   
A1BBT C2   C  N S 9   
A1BBT C4   C  N N 10  
A1BBT C5   C  N N 11  
A1BBT C7   C  Y N 12  
A1BBT C8   C  Y N 13  
A1BBT N1   N  N N 14  
A1BBT N3   N  Y N 15  
A1BBT N4   N  Y N 16  
A1BBT O1   O  N N 17  
A1BBT H5   H  N N 18  
A1BBT H9   H  N N 19  
A1BBT H10  H  N N 20  
A1BBT H13  H  N N 21  
A1BBT H4   H  N N 22  
A1BBT H3   H  N N 23  
A1BBT H12  H  N N 24  
A1BBT H1   H  N N 25  
A1BBT H6   H  N N 26  
A1BBT H7   H  N N 27  
A1BBT H8   H  N N 28  
A1BBT H11  H  N N 29  
A1BBT H14  H  N N 30  
A1BBT H2   H  N N 31  
ALA   N    N  N N 32  
ALA   CA   C  N S 33  
ALA   C    C  N N 34  
ALA   O    O  N N 35  
ALA   CB   C  N N 36  
ALA   OXT  O  N N 37  
ALA   H    H  N N 38  
ALA   H2   H  N N 39  
ALA   HA   H  N N 40  
ALA   HB1  H  N N 41  
ALA   HB2  H  N N 42  
ALA   HB3  H  N N 43  
ALA   HXT  H  N N 44  
ARG   N    N  N N 45  
ARG   CA   C  N S 46  
ARG   C    C  N N 47  
ARG   O    O  N N 48  
ARG   CB   C  N N 49  
ARG   CG   C  N N 50  
ARG   CD   C  N N 51  
ARG   NE   N  N N 52  
ARG   CZ   C  N N 53  
ARG   NH1  N  N N 54  
ARG   NH2  N  N N 55  
ARG   OXT  O  N N 56  
ARG   H    H  N N 57  
ARG   H2   H  N N 58  
ARG   HA   H  N N 59  
ARG   HB2  H  N N 60  
ARG   HB3  H  N N 61  
ARG   HG2  H  N N 62  
ARG   HG3  H  N N 63  
ARG   HD2  H  N N 64  
ARG   HD3  H  N N 65  
ARG   HE   H  N N 66  
ARG   HH11 H  N N 67  
ARG   HH12 H  N N 68  
ARG   HH21 H  N N 69  
ARG   HH22 H  N N 70  
ARG   HXT  H  N N 71  
ASN   N    N  N N 72  
ASN   CA   C  N S 73  
ASN   C    C  N N 74  
ASN   O    O  N N 75  
ASN   CB   C  N N 76  
ASN   CG   C  N N 77  
ASN   OD1  O  N N 78  
ASN   ND2  N  N N 79  
ASN   OXT  O  N N 80  
ASN   H    H  N N 81  
ASN   H2   H  N N 82  
ASN   HA   H  N N 83  
ASN   HB2  H  N N 84  
ASN   HB3  H  N N 85  
ASN   HD21 H  N N 86  
ASN   HD22 H  N N 87  
ASN   HXT  H  N N 88  
ASP   N    N  N N 89  
ASP   CA   C  N S 90  
ASP   C    C  N N 91  
ASP   O    O  N N 92  
ASP   CB   C  N N 93  
ASP   CG   C  N N 94  
ASP   OD1  O  N N 95  
ASP   OD2  O  N N 96  
ASP   OXT  O  N N 97  
ASP   H    H  N N 98  
ASP   H2   H  N N 99  
ASP   HA   H  N N 100 
ASP   HB2  H  N N 101 
ASP   HB3  H  N N 102 
ASP   HD2  H  N N 103 
ASP   HXT  H  N N 104 
CL    CL   CL N N 105 
CYS   N    N  N N 106 
CYS   CA   C  N R 107 
CYS   C    C  N N 108 
CYS   O    O  N N 109 
CYS   CB   C  N N 110 
CYS   SG   S  N N 111 
CYS   OXT  O  N N 112 
CYS   H    H  N N 113 
CYS   H2   H  N N 114 
CYS   HA   H  N N 115 
CYS   HB2  H  N N 116 
CYS   HB3  H  N N 117 
CYS   HG   H  N N 118 
CYS   HXT  H  N N 119 
GLN   N    N  N N 120 
GLN   CA   C  N S 121 
GLN   C    C  N N 122 
GLN   O    O  N N 123 
GLN   CB   C  N N 124 
GLN   CG   C  N N 125 
GLN   CD   C  N N 126 
GLN   OE1  O  N N 127 
GLN   NE2  N  N N 128 
GLN   OXT  O  N N 129 
GLN   H    H  N N 130 
GLN   H2   H  N N 131 
GLN   HA   H  N N 132 
GLN   HB2  H  N N 133 
GLN   HB3  H  N N 134 
GLN   HG2  H  N N 135 
GLN   HG3  H  N N 136 
GLN   HE21 H  N N 137 
GLN   HE22 H  N N 138 
GLN   HXT  H  N N 139 
GLU   N    N  N N 140 
GLU   CA   C  N S 141 
GLU   C    C  N N 142 
GLU   O    O  N N 143 
GLU   CB   C  N N 144 
GLU   CG   C  N N 145 
GLU   CD   C  N N 146 
GLU   OE1  O  N N 147 
GLU   OE2  O  N N 148 
GLU   OXT  O  N N 149 
GLU   H    H  N N 150 
GLU   H2   H  N N 151 
GLU   HA   H  N N 152 
GLU   HB2  H  N N 153 
GLU   HB3  H  N N 154 
GLU   HG2  H  N N 155 
GLU   HG3  H  N N 156 
GLU   HE2  H  N N 157 
GLU   HXT  H  N N 158 
GLY   N    N  N N 159 
GLY   CA   C  N N 160 
GLY   C    C  N N 161 
GLY   O    O  N N 162 
GLY   OXT  O  N N 163 
GLY   H    H  N N 164 
GLY   H2   H  N N 165 
GLY   HA2  H  N N 166 
GLY   HA3  H  N N 167 
GLY   HXT  H  N N 168 
HIS   N    N  N N 169 
HIS   CA   C  N S 170 
HIS   C    C  N N 171 
HIS   O    O  N N 172 
HIS   CB   C  N N 173 
HIS   CG   C  Y N 174 
HIS   ND1  N  Y N 175 
HIS   CD2  C  Y N 176 
HIS   CE1  C  Y N 177 
HIS   NE2  N  Y N 178 
HIS   OXT  O  N N 179 
HIS   H    H  N N 180 
HIS   H2   H  N N 181 
HIS   HA   H  N N 182 
HIS   HB2  H  N N 183 
HIS   HB3  H  N N 184 
HIS   HD1  H  N N 185 
HIS   HD2  H  N N 186 
HIS   HE1  H  N N 187 
HIS   HE2  H  N N 188 
HIS   HXT  H  N N 189 
HOH   O    O  N N 190 
HOH   H1   H  N N 191 
HOH   H2   H  N N 192 
ILE   N    N  N N 193 
ILE   CA   C  N S 194 
ILE   C    C  N N 195 
ILE   O    O  N N 196 
ILE   CB   C  N S 197 
ILE   CG1  C  N N 198 
ILE   CG2  C  N N 199 
ILE   CD1  C  N N 200 
ILE   OXT  O  N N 201 
ILE   H    H  N N 202 
ILE   H2   H  N N 203 
ILE   HA   H  N N 204 
ILE   HB   H  N N 205 
ILE   HG12 H  N N 206 
ILE   HG13 H  N N 207 
ILE   HG21 H  N N 208 
ILE   HG22 H  N N 209 
ILE   HG23 H  N N 210 
ILE   HD11 H  N N 211 
ILE   HD12 H  N N 212 
ILE   HD13 H  N N 213 
ILE   HXT  H  N N 214 
LEU   N    N  N N 215 
LEU   CA   C  N S 216 
LEU   C    C  N N 217 
LEU   O    O  N N 218 
LEU   CB   C  N N 219 
LEU   CG   C  N N 220 
LEU   CD1  C  N N 221 
LEU   CD2  C  N N 222 
LEU   OXT  O  N N 223 
LEU   H    H  N N 224 
LEU   H2   H  N N 225 
LEU   HA   H  N N 226 
LEU   HB2  H  N N 227 
LEU   HB3  H  N N 228 
LEU   HG   H  N N 229 
LEU   HD11 H  N N 230 
LEU   HD12 H  N N 231 
LEU   HD13 H  N N 232 
LEU   HD21 H  N N 233 
LEU   HD22 H  N N 234 
LEU   HD23 H  N N 235 
LEU   HXT  H  N N 236 
LYS   N    N  N N 237 
LYS   CA   C  N S 238 
LYS   C    C  N N 239 
LYS   O    O  N N 240 
LYS   CB   C  N N 241 
LYS   CG   C  N N 242 
LYS   CD   C  N N 243 
LYS   CE   C  N N 244 
LYS   NZ   N  N N 245 
LYS   OXT  O  N N 246 
LYS   H    H  N N 247 
LYS   H2   H  N N 248 
LYS   HA   H  N N 249 
LYS   HB2  H  N N 250 
LYS   HB3  H  N N 251 
LYS   HG2  H  N N 252 
LYS   HG3  H  N N 253 
LYS   HD2  H  N N 254 
LYS   HD3  H  N N 255 
LYS   HE2  H  N N 256 
LYS   HE3  H  N N 257 
LYS   HZ1  H  N N 258 
LYS   HZ2  H  N N 259 
LYS   HZ3  H  N N 260 
LYS   HXT  H  N N 261 
MET   N    N  N N 262 
MET   CA   C  N S 263 
MET   C    C  N N 264 
MET   O    O  N N 265 
MET   CB   C  N N 266 
MET   CG   C  N N 267 
MET   SD   S  N N 268 
MET   CE   C  N N 269 
MET   OXT  O  N N 270 
MET   H    H  N N 271 
MET   H2   H  N N 272 
MET   HA   H  N N 273 
MET   HB2  H  N N 274 
MET   HB3  H  N N 275 
MET   HG2  H  N N 276 
MET   HG3  H  N N 277 
MET   HE1  H  N N 278 
MET   HE2  H  N N 279 
MET   HE3  H  N N 280 
MET   HXT  H  N N 281 
PHE   N    N  N N 282 
PHE   CA   C  N S 283 
PHE   C    C  N N 284 
PHE   O    O  N N 285 
PHE   CB   C  N N 286 
PHE   CG   C  Y N 287 
PHE   CD1  C  Y N 288 
PHE   CD2  C  Y N 289 
PHE   CE1  C  Y N 290 
PHE   CE2  C  Y N 291 
PHE   CZ   C  Y N 292 
PHE   OXT  O  N N 293 
PHE   H    H  N N 294 
PHE   H2   H  N N 295 
PHE   HA   H  N N 296 
PHE   HB2  H  N N 297 
PHE   HB3  H  N N 298 
PHE   HD1  H  N N 299 
PHE   HD2  H  N N 300 
PHE   HE1  H  N N 301 
PHE   HE2  H  N N 302 
PHE   HZ   H  N N 303 
PHE   HXT  H  N N 304 
PRO   N    N  N N 305 
PRO   CA   C  N S 306 
PRO   C    C  N N 307 
PRO   O    O  N N 308 
PRO   CB   C  N N 309 
PRO   CG   C  N N 310 
PRO   CD   C  N N 311 
PRO   OXT  O  N N 312 
PRO   H    H  N N 313 
PRO   HA   H  N N 314 
PRO   HB2  H  N N 315 
PRO   HB3  H  N N 316 
PRO   HG2  H  N N 317 
PRO   HG3  H  N N 318 
PRO   HD2  H  N N 319 
PRO   HD3  H  N N 320 
PRO   HXT  H  N N 321 
SER   N    N  N N 322 
SER   CA   C  N S 323 
SER   C    C  N N 324 
SER   O    O  N N 325 
SER   CB   C  N N 326 
SER   OG   O  N N 327 
SER   OXT  O  N N 328 
SER   H    H  N N 329 
SER   H2   H  N N 330 
SER   HA   H  N N 331 
SER   HB2  H  N N 332 
SER   HB3  H  N N 333 
SER   HG   H  N N 334 
SER   HXT  H  N N 335 
THR   N    N  N N 336 
THR   CA   C  N S 337 
THR   C    C  N N 338 
THR   O    O  N N 339 
THR   CB   C  N R 340 
THR   OG1  O  N N 341 
THR   CG2  C  N N 342 
THR   OXT  O  N N 343 
THR   H    H  N N 344 
THR   H2   H  N N 345 
THR   HA   H  N N 346 
THR   HB   H  N N 347 
THR   HG1  H  N N 348 
THR   HG21 H  N N 349 
THR   HG22 H  N N 350 
THR   HG23 H  N N 351 
THR   HXT  H  N N 352 
TYR   N    N  N N 353 
TYR   CA   C  N S 354 
TYR   C    C  N N 355 
TYR   O    O  N N 356 
TYR   CB   C  N N 357 
TYR   CG   C  Y N 358 
TYR   CD1  C  Y N 359 
TYR   CD2  C  Y N 360 
TYR   CE1  C  Y N 361 
TYR   CE2  C  Y N 362 
TYR   CZ   C  Y N 363 
TYR   OH   O  N N 364 
TYR   OXT  O  N N 365 
TYR   H    H  N N 366 
TYR   H2   H  N N 367 
TYR   HA   H  N N 368 
TYR   HB2  H  N N 369 
TYR   HB3  H  N N 370 
TYR   HD1  H  N N 371 
TYR   HD2  H  N N 372 
TYR   HE1  H  N N 373 
TYR   HE2  H  N N 374 
TYR   HH   H  N N 375 
TYR   HXT  H  N N 376 
VAL   N    N  N N 377 
VAL   CA   C  N S 378 
VAL   C    C  N N 379 
VAL   O    O  N N 380 
VAL   CB   C  N N 381 
VAL   CG1  C  N N 382 
VAL   CG2  C  N N 383 
VAL   OXT  O  N N 384 
VAL   H    H  N N 385 
VAL   H2   H  N N 386 
VAL   HA   H  N N 387 
VAL   HB   H  N N 388 
VAL   HG11 H  N N 389 
VAL   HG12 H  N N 390 
VAL   HG13 H  N N 391 
VAL   HG21 H  N N 392 
VAL   HG22 H  N N 393 
VAL   HG23 H  N N 394 
VAL   HXT  H  N N 395 
# 
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 
A1BBT C4  C3   doub N N 1   
A1BBT C4  C5   sing N N 2   
A1BBT O1  C1   sing N N 3   
A1BBT C3  C2   sing N N 4   
A1BBT C5  C6   sing N N 5   
A1BBT C1  C2   sing N N 6   
A1BBT C6  N1   sing N N 7   
A1BBT C2  N1   sing N N 8   
A1BBT N1  C7   sing N N 9   
A1BBT C7  N2   doub Y N 10  
A1BBT C7  C10  sing Y N 11  
A1BBT C11 C10  sing Y N 12  
A1BBT C11 C12  doub Y N 13  
A1BBT N2  C8   sing Y N 14  
A1BBT C10 C9   doub Y N 15  
A1BBT C12 N4   sing Y N 16  
A1BBT C8  N3   doub Y N 17  
A1BBT C9  N4   sing Y N 18  
A1BBT C9  N3   sing Y N 19  
A1BBT C3  H5   sing N N 20  
A1BBT C6  H9   sing N N 21  
A1BBT C6  H10  sing N N 22  
A1BBT C12 H13  sing N N 23  
A1BBT C1  H4   sing N N 24  
A1BBT C1  H3   sing N N 25  
A1BBT C11 H12  sing N N 26  
A1BBT C2  H1   sing N N 27  
A1BBT C4  H6   sing N N 28  
A1BBT C5  H7   sing N N 29  
A1BBT C5  H8   sing N N 30  
A1BBT C8  H11  sing N N 31  
A1BBT N4  H14  sing N N 32  
A1BBT O1  H2   sing N N 33  
ALA   N   CA   sing N N 34  
ALA   N   H    sing N N 35  
ALA   N   H2   sing N N 36  
ALA   CA  C    sing N N 37  
ALA   CA  CB   sing N N 38  
ALA   CA  HA   sing N N 39  
ALA   C   O    doub N N 40  
ALA   C   OXT  sing N N 41  
ALA   CB  HB1  sing N N 42  
ALA   CB  HB2  sing N N 43  
ALA   CB  HB3  sing N N 44  
ALA   OXT HXT  sing N N 45  
ARG   N   CA   sing N N 46  
ARG   N   H    sing N N 47  
ARG   N   H2   sing N N 48  
ARG   CA  C    sing N N 49  
ARG   CA  CB   sing N N 50  
ARG   CA  HA   sing N N 51  
ARG   C   O    doub N N 52  
ARG   C   OXT  sing N N 53  
ARG   CB  CG   sing N N 54  
ARG   CB  HB2  sing N N 55  
ARG   CB  HB3  sing N N 56  
ARG   CG  CD   sing N N 57  
ARG   CG  HG2  sing N N 58  
ARG   CG  HG3  sing N N 59  
ARG   CD  NE   sing N N 60  
ARG   CD  HD2  sing N N 61  
ARG   CD  HD3  sing N N 62  
ARG   NE  CZ   sing N N 63  
ARG   NE  HE   sing N N 64  
ARG   CZ  NH1  sing N N 65  
ARG   CZ  NH2  doub N N 66  
ARG   NH1 HH11 sing N N 67  
ARG   NH1 HH12 sing N N 68  
ARG   NH2 HH21 sing N N 69  
ARG   NH2 HH22 sing N N 70  
ARG   OXT HXT  sing N N 71  
ASN   N   CA   sing N N 72  
ASN   N   H    sing N N 73  
ASN   N   H2   sing N N 74  
ASN   CA  C    sing N N 75  
ASN   CA  CB   sing N N 76  
ASN   CA  HA   sing N N 77  
ASN   C   O    doub N N 78  
ASN   C   OXT  sing N N 79  
ASN   CB  CG   sing N N 80  
ASN   CB  HB2  sing N N 81  
ASN   CB  HB3  sing N N 82  
ASN   CG  OD1  doub N N 83  
ASN   CG  ND2  sing N N 84  
ASN   ND2 HD21 sing N N 85  
ASN   ND2 HD22 sing N N 86  
ASN   OXT HXT  sing N N 87  
ASP   N   CA   sing N N 88  
ASP   N   H    sing N N 89  
ASP   N   H2   sing N N 90  
ASP   CA  C    sing N N 91  
ASP   CA  CB   sing N N 92  
ASP   CA  HA   sing N N 93  
ASP   C   O    doub N N 94  
ASP   C   OXT  sing N N 95  
ASP   CB  CG   sing N N 96  
ASP   CB  HB2  sing N N 97  
ASP   CB  HB3  sing N N 98  
ASP   CG  OD1  doub N N 99  
ASP   CG  OD2  sing N N 100 
ASP   OD2 HD2  sing N N 101 
ASP   OXT HXT  sing N N 102 
CYS   N   CA   sing N N 103 
CYS   N   H    sing N N 104 
CYS   N   H2   sing N N 105 
CYS   CA  C    sing N N 106 
CYS   CA  CB   sing N N 107 
CYS   CA  HA   sing N N 108 
CYS   C   O    doub N N 109 
CYS   C   OXT  sing N N 110 
CYS   CB  SG   sing N N 111 
CYS   CB  HB2  sing N N 112 
CYS   CB  HB3  sing N N 113 
CYS   SG  HG   sing N N 114 
CYS   OXT HXT  sing N N 115 
GLN   N   CA   sing N N 116 
GLN   N   H    sing N N 117 
GLN   N   H2   sing N N 118 
GLN   CA  C    sing N N 119 
GLN   CA  CB   sing N N 120 
GLN   CA  HA   sing N N 121 
GLN   C   O    doub N N 122 
GLN   C   OXT  sing N N 123 
GLN   CB  CG   sing N N 124 
GLN   CB  HB2  sing N N 125 
GLN   CB  HB3  sing N N 126 
GLN   CG  CD   sing N N 127 
GLN   CG  HG2  sing N N 128 
GLN   CG  HG3  sing N N 129 
GLN   CD  OE1  doub N N 130 
GLN   CD  NE2  sing N N 131 
GLN   NE2 HE21 sing N N 132 
GLN   NE2 HE22 sing N N 133 
GLN   OXT HXT  sing N N 134 
GLU   N   CA   sing N N 135 
GLU   N   H    sing N N 136 
GLU   N   H2   sing N N 137 
GLU   CA  C    sing N N 138 
GLU   CA  CB   sing N N 139 
GLU   CA  HA   sing N N 140 
GLU   C   O    doub N N 141 
GLU   C   OXT  sing N N 142 
GLU   CB  CG   sing N N 143 
GLU   CB  HB2  sing N N 144 
GLU   CB  HB3  sing N N 145 
GLU   CG  CD   sing N N 146 
GLU   CG  HG2  sing N N 147 
GLU   CG  HG3  sing N N 148 
GLU   CD  OE1  doub N N 149 
GLU   CD  OE2  sing N N 150 
GLU   OE2 HE2  sing N N 151 
GLU   OXT HXT  sing N N 152 
GLY   N   CA   sing N N 153 
GLY   N   H    sing N N 154 
GLY   N   H2   sing N N 155 
GLY   CA  C    sing N N 156 
GLY   CA  HA2  sing N N 157 
GLY   CA  HA3  sing N N 158 
GLY   C   O    doub N N 159 
GLY   C   OXT  sing N N 160 
GLY   OXT HXT  sing N N 161 
HIS   N   CA   sing N N 162 
HIS   N   H    sing N N 163 
HIS   N   H2   sing N N 164 
HIS   CA  C    sing N N 165 
HIS   CA  CB   sing N N 166 
HIS   CA  HA   sing N N 167 
HIS   C   O    doub N N 168 
HIS   C   OXT  sing N N 169 
HIS   CB  CG   sing N N 170 
HIS   CB  HB2  sing N N 171 
HIS   CB  HB3  sing N N 172 
HIS   CG  ND1  sing Y N 173 
HIS   CG  CD2  doub Y N 174 
HIS   ND1 CE1  doub Y N 175 
HIS   ND1 HD1  sing N N 176 
HIS   CD2 NE2  sing Y N 177 
HIS   CD2 HD2  sing N N 178 
HIS   CE1 NE2  sing Y N 179 
HIS   CE1 HE1  sing N N 180 
HIS   NE2 HE2  sing N N 181 
HIS   OXT HXT  sing N N 182 
HOH   O   H1   sing N N 183 
HOH   O   H2   sing N N 184 
ILE   N   CA   sing N N 185 
ILE   N   H    sing N N 186 
ILE   N   H2   sing N N 187 
ILE   CA  C    sing N N 188 
ILE   CA  CB   sing N N 189 
ILE   CA  HA   sing N N 190 
ILE   C   O    doub N N 191 
ILE   C   OXT  sing N N 192 
ILE   CB  CG1  sing N N 193 
ILE   CB  CG2  sing N N 194 
ILE   CB  HB   sing N N 195 
ILE   CG1 CD1  sing N N 196 
ILE   CG1 HG12 sing N N 197 
ILE   CG1 HG13 sing N N 198 
ILE   CG2 HG21 sing N N 199 
ILE   CG2 HG22 sing N N 200 
ILE   CG2 HG23 sing N N 201 
ILE   CD1 HD11 sing N N 202 
ILE   CD1 HD12 sing N N 203 
ILE   CD1 HD13 sing N N 204 
ILE   OXT HXT  sing N N 205 
LEU   N   CA   sing N N 206 
LEU   N   H    sing N N 207 
LEU   N   H2   sing N N 208 
LEU   CA  C    sing N N 209 
LEU   CA  CB   sing N N 210 
LEU   CA  HA   sing N N 211 
LEU   C   O    doub N N 212 
LEU   C   OXT  sing N N 213 
LEU   CB  CG   sing N N 214 
LEU   CB  HB2  sing N N 215 
LEU   CB  HB3  sing N N 216 
LEU   CG  CD1  sing N N 217 
LEU   CG  CD2  sing N N 218 
LEU   CG  HG   sing N N 219 
LEU   CD1 HD11 sing N N 220 
LEU   CD1 HD12 sing N N 221 
LEU   CD1 HD13 sing N N 222 
LEU   CD2 HD21 sing N N 223 
LEU   CD2 HD22 sing N N 224 
LEU   CD2 HD23 sing N N 225 
LEU   OXT HXT  sing N N 226 
LYS   N   CA   sing N N 227 
LYS   N   H    sing N N 228 
LYS   N   H2   sing N N 229 
LYS   CA  C    sing N N 230 
LYS   CA  CB   sing N N 231 
LYS   CA  HA   sing N N 232 
LYS   C   O    doub N N 233 
LYS   C   OXT  sing N N 234 
LYS   CB  CG   sing N N 235 
LYS   CB  HB2  sing N N 236 
LYS   CB  HB3  sing N N 237 
LYS   CG  CD   sing N N 238 
LYS   CG  HG2  sing N N 239 
LYS   CG  HG3  sing N N 240 
LYS   CD  CE   sing N N 241 
LYS   CD  HD2  sing N N 242 
LYS   CD  HD3  sing N N 243 
LYS   CE  NZ   sing N N 244 
LYS   CE  HE2  sing N N 245 
LYS   CE  HE3  sing N N 246 
LYS   NZ  HZ1  sing N N 247 
LYS   NZ  HZ2  sing N N 248 
LYS   NZ  HZ3  sing N N 249 
LYS   OXT HXT  sing N N 250 
MET   N   CA   sing N N 251 
MET   N   H    sing N N 252 
MET   N   H2   sing N N 253 
MET   CA  C    sing N N 254 
MET   CA  CB   sing N N 255 
MET   CA  HA   sing N N 256 
MET   C   O    doub N N 257 
MET   C   OXT  sing N N 258 
MET   CB  CG   sing N N 259 
MET   CB  HB2  sing N N 260 
MET   CB  HB3  sing N N 261 
MET   CG  SD   sing N N 262 
MET   CG  HG2  sing N N 263 
MET   CG  HG3  sing N N 264 
MET   SD  CE   sing N N 265 
MET   CE  HE1  sing N N 266 
MET   CE  HE2  sing N N 267 
MET   CE  HE3  sing N N 268 
MET   OXT HXT  sing N N 269 
PHE   N   CA   sing N N 270 
PHE   N   H    sing N N 271 
PHE   N   H2   sing N N 272 
PHE   CA  C    sing N N 273 
PHE   CA  CB   sing N N 274 
PHE   CA  HA   sing N N 275 
PHE   C   O    doub N N 276 
PHE   C   OXT  sing N N 277 
PHE   CB  CG   sing N N 278 
PHE   CB  HB2  sing N N 279 
PHE   CB  HB3  sing N N 280 
PHE   CG  CD1  doub Y N 281 
PHE   CG  CD2  sing Y N 282 
PHE   CD1 CE1  sing Y N 283 
PHE   CD1 HD1  sing N N 284 
PHE   CD2 CE2  doub Y N 285 
PHE   CD2 HD2  sing N N 286 
PHE   CE1 CZ   doub Y N 287 
PHE   CE1 HE1  sing N N 288 
PHE   CE2 CZ   sing Y N 289 
PHE   CE2 HE2  sing N N 290 
PHE   CZ  HZ   sing N N 291 
PHE   OXT HXT  sing N N 292 
PRO   N   CA   sing N N 293 
PRO   N   CD   sing N N 294 
PRO   N   H    sing N N 295 
PRO   CA  C    sing N N 296 
PRO   CA  CB   sing N N 297 
PRO   CA  HA   sing N N 298 
PRO   C   O    doub N N 299 
PRO   C   OXT  sing N N 300 
PRO   CB  CG   sing N N 301 
PRO   CB  HB2  sing N N 302 
PRO   CB  HB3  sing N N 303 
PRO   CG  CD   sing N N 304 
PRO   CG  HG2  sing N N 305 
PRO   CG  HG3  sing N N 306 
PRO   CD  HD2  sing N N 307 
PRO   CD  HD3  sing N N 308 
PRO   OXT HXT  sing N N 309 
SER   N   CA   sing N N 310 
SER   N   H    sing N N 311 
SER   N   H2   sing N N 312 
SER   CA  C    sing N N 313 
SER   CA  CB   sing N N 314 
SER   CA  HA   sing N N 315 
SER   C   O    doub N N 316 
SER   C   OXT  sing N N 317 
SER   CB  OG   sing N N 318 
SER   CB  HB2  sing N N 319 
SER   CB  HB3  sing N N 320 
SER   OG  HG   sing N N 321 
SER   OXT HXT  sing N N 322 
THR   N   CA   sing N N 323 
THR   N   H    sing N N 324 
THR   N   H2   sing N N 325 
THR   CA  C    sing N N 326 
THR   CA  CB   sing N N 327 
THR   CA  HA   sing N N 328 
THR   C   O    doub N N 329 
THR   C   OXT  sing N N 330 
THR   CB  OG1  sing N N 331 
THR   CB  CG2  sing N N 332 
THR   CB  HB   sing N N 333 
THR   OG1 HG1  sing N N 334 
THR   CG2 HG21 sing N N 335 
THR   CG2 HG22 sing N N 336 
THR   CG2 HG23 sing N N 337 
THR   OXT HXT  sing N N 338 
TYR   N   CA   sing N N 339 
TYR   N   H    sing N N 340 
TYR   N   H2   sing N N 341 
TYR   CA  C    sing N N 342 
TYR   CA  CB   sing N N 343 
TYR   CA  HA   sing N N 344 
TYR   C   O    doub N N 345 
TYR   C   OXT  sing N N 346 
TYR   CB  CG   sing N N 347 
TYR   CB  HB2  sing N N 348 
TYR   CB  HB3  sing N N 349 
TYR   CG  CD1  doub Y N 350 
TYR   CG  CD2  sing Y N 351 
TYR   CD1 CE1  sing Y N 352 
TYR   CD1 HD1  sing N N 353 
TYR   CD2 CE2  doub Y N 354 
TYR   CD2 HD2  sing N N 355 
TYR   CE1 CZ   doub Y N 356 
TYR   CE1 HE1  sing N N 357 
TYR   CE2 CZ   sing Y N 358 
TYR   CE2 HE2  sing N N 359 
TYR   CZ  OH   sing N N 360 
TYR   OH  HH   sing N N 361 
TYR   OXT HXT  sing N N 362 
VAL   N   CA   sing N N 363 
VAL   N   H    sing N N 364 
VAL   N   H2   sing N N 365 
VAL   CA  C    sing N N 366 
VAL   CA  CB   sing N N 367 
VAL   CA  HA   sing N N 368 
VAL   C   O    doub N N 369 
VAL   C   OXT  sing N N 370 
VAL   CB  CG1  sing N N 371 
VAL   CB  CG2  sing N N 372 
VAL   CB  HB   sing N N 373 
VAL   CG1 HG11 sing N N 374 
VAL   CG1 HG12 sing N N 375 
VAL   CG1 HG13 sing N N 376 
VAL   CG2 HG21 sing N N 377 
VAL   CG2 HG22 sing N N 378 
VAL   CG2 HG23 sing N N 379 
VAL   OXT HXT  sing N N 380 
# 
_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                    7HFS 
_atom_sites.fract_transf_matrix[1][1]   0.011258 
_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]   0.011258 
_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]   0.025336 
_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 
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   ? 19.727 -16.236 22.201  0.62 56.45 ?  3    VAL   A N    1 
ATOM   2    N  N    B VAL   A 1 3   ? 19.685 -16.067 22.403  0.38 54.57 ?  3    VAL   A N    1 
ATOM   3    C  CA   A VAL   A 1 3   ? 18.752 -15.168 22.383  0.62 56.08 ?  3    VAL   A CA   1 
ATOM   4    C  CA   B VAL   A 1 3   ? 18.724 -14.985 22.574  0.38 54.21 ?  3    VAL   A CA   1 
ATOM   5    C  C    A VAL   A 1 3   ? 19.396 -13.814 22.102  0.62 54.47 ?  3    VAL   A C    1 
ATOM   6    C  C    B VAL   A 1 3   ? 19.376 -13.645 22.251  0.38 52.69 ?  3    VAL   A C    1 
ATOM   7    O  O    A VAL   A 1 3   ? 20.502 -13.536 22.567  0.62 54.89 ?  3    VAL   A O    1 
ATOM   8    O  O    B VAL   A 1 3   ? 20.438 -13.321 22.784  0.38 53.04 ?  3    VAL   A O    1 
ATOM   9    C  CB   A VAL   A 1 3   ? 18.129 -15.212 23.794  0.62 56.97 ?  3    VAL   A CB   1 
ATOM   10   C  CB   B VAL   A 1 3   ? 18.130 -14.983 23.995  0.38 55.07 ?  3    VAL   A CB   1 
ATOM   11   C  CG1  A VAL   A 1 3   ? 17.097 -14.106 23.958  0.62 57.24 ?  3    VAL   A CG1  1 
ATOM   12   C  CG1  B VAL   A 1 3   ? 17.106 -13.865 24.141  0.38 55.34 ?  3    VAL   A CG1  1 
ATOM   13   C  CG2  A VAL   A 1 3   ? 17.501 -16.574 24.058  0.62 57.25 ?  3    VAL   A CG2  1 
ATOM   14   C  CG2  B VAL   A 1 3   ? 17.502 -16.333 24.314  0.38 55.35 ?  3    VAL   A CG2  1 
ATOM   15   H  HA   A VAL   A 1 3   ? 18.035 -15.289 21.745  0.62 67.31 ?  3    VAL   A HA   1 
ATOM   16   H  HA   B VAL   A 1 3   ? 17.992 -15.114 21.954  0.38 65.07 ?  3    VAL   A HA   1 
ATOM   17   H  HB   A VAL   A 1 3   ? 18.825 -15.072 24.455  0.62 68.38 ?  3    VAL   A HB   1 
ATOM   18   H  HB   B VAL   A 1 3   ? 18.840 -14.826 24.637  0.38 66.10 ?  3    VAL   A HB   1 
ATOM   19   H  HG11 A VAL   A 1 3   ? 16.599 -14.258 24.777  0.62 68.71 ?  3    VAL   A HG11 1 
ATOM   20   H  HG11 B VAL   A 1 3   ? 16.618 -13.991 24.970  0.38 66.42 ?  3    VAL   A HG11 1 
ATOM   21   H  HG12 A VAL   A 1 3   ? 17.552 -13.251 24.004  0.62 68.71 ?  3    VAL   A HG12 1 
ATOM   22   H  HG12 B VAL   A 1 3   ? 17.567 -13.012 24.157  0.38 66.42 ?  3    VAL   A HG12 1 
ATOM   23   H  HG13 A VAL   A 1 3   ? 16.494 -14.122 23.198  0.62 68.71 ?  3    VAL   A HG13 1 
ATOM   24   H  HG13 B VAL   A 1 3   ? 16.494 -13.898 23.389  0.38 66.42 ?  3    VAL   A HG13 1 
ATOM   25   H  HG21 A VAL   A 1 3   ? 17.052 -16.554 24.918  0.62 68.71 ?  3    VAL   A HG21 1 
ATOM   26   H  HG21 B VAL   A 1 3   ? 17.064 -16.281 25.178  0.38 66.44 ?  3    VAL   A HG21 1 
ATOM   27   H  HG22 A VAL   A 1 3   ? 16.861 -16.767 23.355  0.62 68.71 ?  3    VAL   A HG22 1 
ATOM   28   H  HG22 B VAL   A 1 3   ? 16.853 -16.548 23.626  0.38 66.44 ?  3    VAL   A HG22 1 
ATOM   29   H  HG23 A VAL   A 1 3   ? 18.198 -17.248 24.065  0.62 68.71 ?  3    VAL   A HG23 1 
ATOM   30   H  HG23 B VAL   A 1 3   ? 18.198 -17.009 24.336  0.38 66.44 ?  3    VAL   A HG23 1 
ATOM   31   N  N    A ASN   A 1 4   ? 18.702 -12.976 21.332  0.62 52.07 ?  4    ASN   A N    1 
ATOM   32   N  N    B ASN   A 1 4   ? 18.739 -12.872 21.378  0.38 50.53 ?  4    ASN   A N    1 
ATOM   33   C  CA   A ASN   A 1 4   ? 19.150 -11.621 21.036  0.62 49.37 ?  4    ASN   A CA   1 
ATOM   34   C  CA   B ASN   A 1 4   ? 19.192 -11.529 21.031  0.38 48.13 ?  4    ASN   A CA   1 
ATOM   35   C  C    A ASN   A 1 4   ? 18.004 -10.644 21.292  0.62 46.77 ?  4    ASN   A C    1 
ATOM   36   C  C    B ASN   A 1 4   ? 18.072 -10.526 21.300  0.38 45.79 ?  4    ASN   A C    1 
ATOM   37   O  O    A ASN   A 1 4   ? 16.883 -11.038 21.625  0.62 46.92 ?  4    ASN   A O    1 
ATOM   38   O  O    B ASN   A 1 4   ? 16.954 -10.891 21.673  0.38 45.95 ?  4    ASN   A O    1 
ATOM   39   C  CB   A ASN   A 1 4   ? 19.710 -11.504 19.610  0.62 48.96 ?  4    ASN   A CB   1 
ATOM   40   C  CB   B ASN   A 1 4   ? 19.700 -11.457 19.586  0.38 47.82 ?  4    ASN   A CB   1 
ATOM   41   C  CG   A ASN   A 1 4   ? 18.723 -11.945 18.551  0.62 48.47 ?  4    ASN   A CG   1 
ATOM   42   C  CG   B ASN   A 1 4   ? 18.653 -11.867 18.572  0.38 47.46 ?  4    ASN   A CG   1 
ATOM   43   O  OD1  A ASN   A 1 4   ? 17.561 -11.537 18.558  0.62 48.30 ?  4    ASN   A OD1  1 
ATOM   44   O  OD1  B ASN   A 1 4   ? 17.515 -11.399 18.609  0.38 47.33 ?  4    ASN   A OD1  1 
ATOM   45   N  ND2  A ASN   A 1 4   ? 19.182 -12.788 17.632  0.62 48.35 ?  4    ASN   A ND2  1 
ATOM   46   N  ND2  B ASN   A 1 4   ? 19.036 -12.749 17.656  0.38 47.38 ?  4    ASN   A ND2  1 
ATOM   47   H  H    A ASN   A 1 4   ? 17.952 -13.181 20.965  0.62 62.51 ?  4    ASN   A H    1 
ATOM   48   H  H    B ASN   A 1 4   ? 18.019 -13.110 20.970  0.38 60.66 ?  4    ASN   A H    1 
ATOM   49   H  HA   A ASN   A 1 4   ? 19.868 -11.399 21.642  0.62 59.26 ?  4    ASN   A HA   1 
ATOM   50   H  HA   B ASN   A 1 4   ? 19.936 -11.303 21.604  0.38 57.77 ?  4    ASN   A HA   1 
ATOM   51   H  HB2  A ASN   A 1 4   ? 19.942 -10.576 19.438  0.62 58.77 ?  4    ASN   A HB2  1 
ATOM   52   H  HB2  B ASN   A 1 4   ? 19.966 -10.542 19.391  0.38 57.40 ?  4    ASN   A HB2  1 
ATOM   53   H  HB3  A ASN   A 1 4   ? 20.501 -12.060 19.534  0.62 58.77 ?  4    ASN   A HB3  1 
ATOM   54   H  HB3  B ASN   A 1 4   ? 20.461 -12.049 19.485  0.38 57.40 ?  4    ASN   A HB3  1 
ATOM   55   H  HD21 A ASN   A 1 4   ? 18.664 -13.068 17.006  0.62 58.04 ?  4    ASN   A HD21 1 
ATOM   56   H  HD21 B ASN   A 1 4   ? 18.483 -13.013 17.054  0.38 56.88 ?  4    ASN   A HD21 1 
ATOM   57   H  HD22 A ASN   A 1 4   ? 20.001 -13.053 17.662  0.62 58.04 ?  4    ASN   A HD22 1 
ATOM   58   H  HD22 B ASN   A 1 4   ? 19.841 -13.056 17.665  0.38 56.88 ?  4    ASN   A HD22 1 
ATOM   59   N  N    A SER   A 1 5   ? 18.296 -9.353  21.129  0.62 43.68 ?  5    SER   A N    1 
ATOM   60   N  N    B SER   A 1 5   ? 18.385 -9.246  21.104  0.38 43.04 ?  5    SER   A N    1 
ATOM   61   C  CA   A SER   A 1 5   ? 17.391 -8.282  21.529  0.62 40.52 ?  5    SER   A CA   1 
ATOM   62   C  CA   B SER   A 1 5   ? 17.495 -8.156  21.478  0.38 40.19 ?  5    SER   A CA   1 
ATOM   63   C  C    A SER   A 1 5   ? 16.523 -7.763  20.386  0.62 36.75 ?  5    SER   A C    1 
ATOM   64   C  C    B SER   A 1 5   ? 16.620 -7.672  20.328  0.38 36.72 ?  5    SER   A C    1 
ATOM   65   O  O    A SER   A 1 5   ? 15.844 -6.745  20.554  0.62 36.52 ?  5    SER   A O    1 
ATOM   66   O  O    B SER   A 1 5   ? 16.017 -6.599  20.436  0.38 36.71 ?  5    SER   A O    1 
ATOM   67   C  CB   A SER   A 1 5   ? 18.181 -7.127  22.147  0.62 41.20 ?  5    SER   A CB   1 
ATOM   68   C  CB   B SER   A 1 5   ? 18.296 -6.985  22.051  0.38 40.76 ?  5    SER   A CB   1 
ATOM   69   O  OG   A SER   A 1 5   ? 19.148 -6.629  21.239  0.62 41.57 ?  5    SER   A OG   1 
ATOM   70   O  OG   B SER   A 1 5   ? 19.197 -6.463  21.090  0.38 41.06 ?  5    SER   A OG   1 
ATOM   71   H  H    A SER   A 1 5   ? 19.027 -9.073  20.776  0.62 52.43 ?  5    SER   A H    1 
ATOM   72   H  H    B SER   A 1 5   ? 19.117 -8.985  20.741  0.38 51.67 ?  5    SER   A H    1 
ATOM   73   H  HA   A SER   A 1 5   ? 16.801 -8.626  22.219  0.62 48.64 ?  5    SER   A HA   1 
ATOM   74   H  HA   B SER   A 1 5   ? 16.909 -8.472  22.183  0.38 48.24 ?  5    SER   A HA   1 
ATOM   75   H  HB2  A SER   A 1 5   ? 17.565 -6.412  22.375  0.62 49.46 ?  5    SER   A HB2  1 
ATOM   76   H  HB2  B SER   A 1 5   ? 17.679 -6.284  22.321  0.38 48.93 ?  5    SER   A HB2  1 
ATOM   77   H  HB3  A SER   A 1 5   ? 18.630 -7.444  22.946  0.62 49.46 ?  5    SER   A HB3  1 
ATOM   78   H  HB3  B SER   A 1 5   ? 18.800 -7.294  22.819  0.38 48.93 ?  5    SER   A HB3  1 
ATOM   79   H  HG   A SER   A 1 5   ? 19.572 -5.995  21.592  0.62 49.90 ?  5    SER   A HG   1 
ATOM   80   H  HG   B SER   A 1 5   ? 19.625 -5.819  21.419  0.38 49.28 ?  5    SER   A HG   1 
ATOM   81   N  N    . PHE   A 1 6   ? 16.538 -8.424  19.232  1.00 33.09 ?  6    PHE   A N    1 
ATOM   82   C  CA   . PHE   A 1 6   ? 15.622 -8.069  18.155  1.00 26.34 ?  6    PHE   A CA   1 
ATOM   83   C  C    . PHE   A 1 6   ? 14.208 -8.458  18.568  1.00 25.29 ?  6    PHE   A C    1 
ATOM   84   O  O    . PHE   A 1 6   ? 13.981 -9.563  19.065  1.00 26.68 ?  6    PHE   A O    1 
ATOM   85   C  CB   . PHE   A 1 6   ? 16.008 -8.793  16.868  1.00 22.03 ?  6    PHE   A CB   1 
ATOM   86   C  CG   . PHE   A 1 6   ? 17.283 -8.291  16.246  1.00 19.24 ?  6    PHE   A CG   1 
ATOM   87   C  CD1  . PHE   A 1 6   ? 17.306 -7.095  15.551  1.00 18.56 ?  6    PHE   A CD1  1 
ATOM   88   C  CD2  . PHE   A 1 6   ? 18.450 -9.025  16.346  1.00 19.56 ?  6    PHE   A CD2  1 
ATOM   89   C  CE1  . PHE   A 1 6   ? 18.473 -6.636  14.971  1.00 18.42 ?  6    PHE   A CE1  1 
ATOM   90   C  CE2  . PHE   A 1 6   ? 19.619 -8.574  15.769  1.00 19.67 ?  6    PHE   A CE2  1 
ATOM   91   C  CZ   . PHE   A 1 6   ? 19.633 -7.376  15.080  1.00 18.88 ?  6    PHE   A CZ   1 
ATOM   92   H  H    A PHE   A 1 6   ? 17.066 -9.077  19.048  0.62 39.73 ?  6    PHE   A H    1 
ATOM   93   H  H    B PHE   A 1 6   ? 16.999 -9.137  19.090  0.38 39.73 ?  6    PHE   A H    1 
ATOM   94   H  HA   . PHE   A 1 6   ? 15.647 -7.118  18.001  1.00 31.62 ?  6    PHE   A HA   1 
ATOM   95   H  HB2  . PHE   A 1 6   ? 16.124 -9.739  17.063  1.00 26.45 ?  6    PHE   A HB2  1 
ATOM   96   H  HB3  . PHE   A 1 6   ? 15.296 -8.680  16.219  1.00 26.45 ?  6    PHE   A HB3  1 
ATOM   97   H  HD1  . PHE   A 1 6   ? 16.526 -6.593  15.475  1.00 22.29 ?  6    PHE   A HD1  1 
ATOM   98   H  HD2  . PHE   A 1 6   ? 18.444 -9.833  16.809  1.00 23.49 ?  6    PHE   A HD2  1 
ATOM   99   H  HE1  . PHE   A 1 6   ? 18.480 -5.826  14.508  1.00 22.12 ?  6    PHE   A HE1  1 
ATOM   100  H  HE2  . PHE   A 1 6   ? 20.399 -9.075  15.847  1.00 23.62 ?  6    PHE   A HE2  1 
ATOM   101  H  HZ   . PHE   A 1 6   ? 20.421 -7.066  14.692  1.00 22.67 ?  6    PHE   A HZ   1 
ATOM   102  N  N    A SER   A 1 7   ? 13.246 -7.574  18.276  0.62 23.62 ?  7    SER   A N    1 
ATOM   103  N  N    B SER   A 1 7   ? 13.267 -7.530  18.442  0.38 24.54 ?  7    SER   A N    1 
ATOM   104  C  CA   A SER   A 1 7   ? 11.864 -7.714  18.721  0.62 23.06 ?  7    SER   A CA   1 
ATOM   105  C  CA   B SER   A 1 7   ? 11.938 -7.740  18.996  0.38 24.36 ?  7    SER   A CA   1 
ATOM   106  C  C    A SER   A 1 7   ? 10.895 -7.468  17.568  0.62 20.72 ?  7    SER   A C    1 
ATOM   107  C  C    B SER   A 1 7   ? 10.878 -7.429  17.953  0.38 22.45 ?  7    SER   A C    1 
ATOM   108  O  O    A SER   A 1 7   ? 11.127 -6.597  16.725  0.62 20.19 ?  7    SER   A O    1 
ATOM   109  O  O    B SER   A 1 7   ? 10.999 -6.465  17.192  0.38 22.49 ?  7    SER   A O    1 
ATOM   110  C  CB   A SER   A 1 7   ? 11.578 -6.709  19.846  0.62 24.79 ?  7    SER   A CB   1 
ATOM   111  C  CB   B SER   A 1 7   ? 11.718 -6.887  20.253  0.38 25.96 ?  7    SER   A CB   1 
ATOM   112  O  OG   A SER   A 1 7   ? 10.221 -6.744  20.245  0.62 25.71 ?  7    SER   A OG   1 
ATOM   113  O  OG   B SER   A 1 7   ? 10.765 -7.490  21.109  0.38 27.06 ?  7    SER   A OG   1 
ATOM   114  H  H    A SER   A 1 7   ? 13.378 -6.870  17.803  0.62 28.36 ?  7    SER   A H    1 
ATOM   115  H  H    B SER   A 1 7   ? 13.373 -6.776  18.045  0.38 29.46 ?  7    SER   A H    1 
ATOM   116  H  HA   A SER   A 1 7   ? 11.715 -8.609  19.062  0.62 27.69 ?  7    SER   A HA   1 
ATOM   117  H  HA   B SER   A 1 7   ? 11.837 -8.670  19.251  0.38 29.24 ?  7    SER   A HA   1 
ATOM   118  H  HB2  A SER   A 1 7   ? 12.139 -6.926  20.609  0.62 29.76 ?  7    SER   A HB2  1 
ATOM   119  H  HB2  B SER   A 1 7   ? 12.563 -6.796  20.725  0.38 31.17 ?  7    SER   A HB2  1 
ATOM   120  H  HB3  A SER   A 1 7   ? 11.786 -5.816  19.530  0.62 29.76 ?  7    SER   A HB3  1 
ATOM   121  H  HB3  B SER   A 1 7   ? 11.389 -6.016  19.992  0.38 31.17 ?  7    SER   A HB3  1 
ATOM   122  H  HG   A SER   A 1 7   ? 10.091 -6.192  20.867  0.62 30.87 ?  7    SER   A HG   1 
ATOM   123  H  HG   B SER   A 1 7   ? 10.663 -7.026  21.802  0.38 32.49 ?  7    SER   A HG   1 
ATOM   124  N  N    A GLY   A 1 8   ? 9.807  -8.243  17.533  0.62 19.76 ?  8    GLY   A N    1 
ATOM   125  N  N    B GLY   A 1 8   ? 9.838  -8.257  17.926  0.38 20.83 ?  8    GLY   A N    1 
ATOM   126  C  CA   A GLY   A 1 8   ? 8.714  -7.969  16.617  0.62 19.04 ?  8    GLY   A CA   1 
ATOM   127  C  CA   B GLY   A 1 8   ? 8.759  -8.080  16.983  0.38 19.78 ?  8    GLY   A CA   1 
ATOM   128  C  C    A GLY   A 1 8   ? 8.881  -8.474  15.199  0.62 17.74 ?  8    GLY   A C    1 
ATOM   129  C  C    B GLY   A 1 8   ? 9.008  -8.639  15.604  0.38 18.25 ?  8    GLY   A C    1 
ATOM   130  O  O    A GLY   A 1 8   ? 8.147  -8.034  14.309  0.62 18.49 ?  8    GLY   A O    1 
ATOM   131  O  O    B GLY   A 1 8   ? 8.218  -8.361  14.695  0.38 18.51 ?  8    GLY   A O    1 
ATOM   132  H  H    A GLY   A 1 8   ? 9.685  -8.935  18.032  0.62 23.73 ?  8    GLY   A H    1 
ATOM   133  H  H    B GLY   A 1 8   ? 9.741  -8.928  18.453  0.38 25.01 ?  8    GLY   A H    1 
ATOM   134  H  HA2  A GLY   A 1 8   ? 7.900  -8.362  16.982  0.62 22.86 ?  8    GLY   A HA2  1 
ATOM   135  H  HA2  B GLY   A 1 8   ? 7.967  -8.512  17.329  0.38 23.75 ?  8    GLY   A HA2  1 
ATOM   136  H  HA3  A GLY   A 1 8   ? 8.579  -7.011  16.573  0.62 22.86 ?  8    GLY   A HA3  1 
ATOM   137  H  HA3  B GLY   A 1 8   ? 8.574  -7.133  16.893  0.38 23.75 ?  8    GLY   A HA3  1 
ATOM   138  N  N    A TYR   A 1 9   ? 9.820  -9.383  14.956  0.62 15.74 ?  9    TYR   A N    1 
ATOM   139  N  N    B TYR   A 1 9   ? 10.070 -9.419  15.412  0.38 16.75 ?  9    TYR   A N    1 
ATOM   140  C  CA   A TYR   A 1 9   ? 10.058 -9.917  13.623  0.62 13.82 ?  9    TYR   A CA   1 
ATOM   141  C  CA   B TYR   A 1 9   ? 10.380 -9.936  14.087  0.38 15.43 ?  9    TYR   A CA   1 
ATOM   142  C  C    A TYR   A 1 9   ? 9.181  -11.137 13.361  0.62 13.55 ?  9    TYR   A C    1 
ATOM   143  C  C    B TYR   A 1 9   ? 9.578  -11.195 13.780  0.38 14.86 ?  9    TYR   A C    1 
ATOM   144  O  O    A TYR   A 1 9   ? 8.872  -11.919 14.267  0.62 15.50 ?  9    TYR   A O    1 
ATOM   145  O  O    B TYR   A 1 9   ? 9.326  -12.029 14.657  0.38 15.35 ?  9    TYR   A O    1 
ATOM   146  C  CB   A TYR   A 1 9   ? 11.527 -10.327 13.455  0.62 13.61 ?  9    TYR   A CB   1 
ATOM   147  C  CB   B TYR   A 1 9   ? 11.879 -10.216 13.951  0.38 14.90 ?  9    TYR   A CB   1 
ATOM   148  C  CG   A TYR   A 1 9   ? 12.467 -9.159  13.298  0.62 14.17 ?  9    TYR   A CG   1 
ATOM   149  C  CG   B TYR   A 1 9   ? 12.687 -8.963  13.693  0.38 13.92 ?  9    TYR   A CG   1 
ATOM   150  C  CD1  A TYR   A 1 9   ? 12.823 -8.385  14.391  0.62 14.98 ?  9    TYR   A CD1  1 
ATOM   151  C  CD1  B TYR   A 1 9   ? 12.954 -8.061  14.717  0.38 14.05 ?  9    TYR   A CD1  1 
ATOM   152  C  CD2  A TYR   A 1 9   ? 12.990 -8.827  12.056  0.62 14.18 ?  9    TYR   A CD2  1 
ATOM   153  C  CD2  B TYR   A 1 9   ? 13.167 -8.672  12.423  0.38 13.28 ?  9    TYR   A CD2  1 
ATOM   154  C  CE1  A TYR   A 1 9   ? 13.668 -7.305  14.256  0.62 15.54 ?  9    TYR   A CE1  1 
ATOM   155  C  CE1  B TYR   A 1 9   ? 13.678 -6.907  14.483  0.38 13.79 ?  9    TYR   A CE1  1 
ATOM   156  C  CE2  A TYR   A 1 9   ? 13.838 -7.750  11.908  0.62 14.79 ?  9    TYR   A CE2  1 
ATOM   157  C  CE2  B TYR   A 1 9   ? 13.893 -7.522  12.180  0.38 13.19 ?  9    TYR   A CE2  1 
ATOM   158  C  CZ   A TYR   A 1 9   ? 14.174 -6.993  13.011  0.62 15.61 ?  9    TYR   A CZ   1 
ATOM   159  C  CZ   B TYR   A 1 9   ? 14.143 -6.646  13.213  0.38 13.71 ?  9    TYR   A CZ   1 
ATOM   160  O  OH   A TYR   A 1 9   ? 15.012 -5.920  12.868  0.62 16.66 ?  9    TYR   A OH   1 
ATOM   161  O  OH   B TYR   A 1 9   ? 14.857 -5.502  12.967  0.38 14.23 ?  9    TYR   A OH   1 
ATOM   162  H  H    A TYR   A 1 9   ? 10.334 -9.710  15.555  0.62 18.90 ?  9    TYR   A H    1 
ATOM   163  H  H    B TYR   A 1 9   ? 10.626 -9.661  16.029  0.38 20.12 ?  9    TYR   A H    1 
ATOM   164  H  HA   A TYR   A 1 9   ? 9.849  -9.235  12.959  0.62 16.60 ?  9    TYR   A HA   1 
ATOM   165  H  HA   B TYR   A 1 9   ? 10.148 -9.265  13.429  0.38 18.53 ?  9    TYR   A HA   1 
ATOM   166  H  HB2  A TYR   A 1 9   ? 11.800 -10.833 14.233  0.62 16.34 ?  9    TYR   A HB2  1 
ATOM   167  H  HB2  B TYR   A 1 9   ? 12.207 -10.628 14.764  0.38 17.89 ?  9    TYR   A HB2  1 
ATOM   168  H  HB3  A TYR   A 1 9   ? 11.597 -10.876 12.659  0.62 16.34 ?  9    TYR   A HB3  1 
ATOM   169  H  HB3  B TYR   A 1 9   ? 12.011 -10.815 13.200  0.38 17.89 ?  9    TYR   A HB3  1 
ATOM   170  H  HD1  A TYR   A 1 9   ? 12.472 -8.592  15.230  0.62 17.99 ?  9    TYR   A HD1  1 
ATOM   171  H  HD1  B TYR   A 1 9   ? 12.634 -8.237  15.574  0.38 16.88 ?  9    TYR   A HD1  1 
ATOM   172  H  HD2  A TYR   A 1 9   ? 12.758 -9.338  11.311  0.62 17.03 ?  9    TYR   A HD2  1 
ATOM   173  H  HD2  B TYR   A 1 9   ? 12.997 -9.262  11.725  0.38 15.95 ?  9    TYR   A HD2  1 
ATOM   174  H  HE1  A TYR   A 1 9   ? 13.897 -6.795  14.998  0.62 18.67 ?  9    TYR   A HE1  1 
ATOM   175  H  HE1  B TYR   A 1 9   ? 13.851 -6.312  15.177  0.38 16.56 ?  9    TYR   A HE1  1 
ATOM   176  H  HE2  A TYR   A 1 9   ? 14.185 -7.542  11.071  0.62 17.77 ?  9    TYR   A HE2  1 
ATOM   177  H  HE2  B TYR   A 1 9   ? 14.214 -7.340  11.324  0.38 15.85 ?  9    TYR   A HE2  1 
ATOM   178  H  HH   A TYR   A 1 9   ? 15.139 -5.554  13.613  0.62 20.01 ?  9    TYR   A HH   1 
ATOM   179  H  HH   B TYR   A 1 9   ? 14.952 -5.053  13.671  0.38 17.09 ?  9    TYR   A HH   1 
ATOM   180  N  N    A LEU   A 1 10  ? 8.785  -11.293 12.101  0.62 13.03 ?  10   LEU   A N    1 
ATOM   181  N  N    B LEU   A 1 10  ? 9.190  -11.324 12.515  0.38 14.04 ?  10   LEU   A N    1 
ATOM   182  C  CA   A LEU   A 1 10  ? 8.218  -12.539 11.610  0.62 12.93 ?  10   LEU   A CA   1 
ATOM   183  C  CA   B LEU   A 1 10  ? 8.476  -12.491 12.016  0.38 14.10 ?  10   LEU   A CA   1 
ATOM   184  C  C    A LEU   A 1 10  ? 9.366  -13.456 11.201  0.62 12.81 ?  10   LEU   A C    1 
ATOM   185  C  C    B LEU   A 1 10  ? 9.492  -13.481 11.456  0.38 13.14 ?  10   LEU   A C    1 
ATOM   186  O  O    A LEU   A 1 10  ? 10.384 -12.998 10.668  0.62 12.91 ?  10   LEU   A O    1 
ATOM   187  O  O    B LEU   A 1 10  ? 10.241 -13.152 10.528  0.38 13.08 ?  10   LEU   A O    1 
ATOM   188  C  CB   A LEU   A 1 10  ? 7.330  -12.261 10.396  0.62 14.16 ?  10   LEU   A CB   1 
ATOM   189  C  CB   B LEU   A 1 10  ? 7.498  -12.062 10.925  0.38 14.89 ?  10   LEU   A CB   1 
ATOM   190  C  CG   A LEU   A 1 10  ? 6.651  -13.476 9.760   0.62 16.53 ?  10   LEU   A CG   1 
ATOM   191  C  CG   B LEU   A 1 10  ? 6.697  -13.159 10.226  0.38 16.17 ?  10   LEU   A CG   1 
ATOM   192  C  CD1  A LEU   A 1 10  ? 5.587  -14.055 10.677  0.62 18.17 ?  10   LEU   A CD1  1 
ATOM   193  C  CD1  B LEU   A 1 10  ? 5.716  -13.789 11.190  0.38 17.26 ?  10   LEU   A CD1  1 
ATOM   194  C  CD2  A LEU   A 1 10  ? 6.063  -13.119 8.409   0.62 17.42 ?  10   LEU   A CD2  1 
ATOM   195  C  CD2  B LEU   A 1 10  ? 5.986  -12.581 9.016   0.38 17.26 ?  10   LEU   A CD2  1 
ATOM   196  H  H    A LEU   A 1 10  ? 8.835  -10.673 11.494  0.62 15.65 ?  10   LEU   A H    1 
ATOM   197  H  H    B LEU   A 1 10  ? 9.341  -10.728 11.913  0.38 16.86 ?  10   LEU   A H    1 
ATOM   198  H  HA   A LEU   A 1 10  ? 7.679  -12.958 12.308  0.62 15.54 ?  10   LEU   A HA   1 
ATOM   199  H  HA   B LEU   A 1 10  ? 7.985  -12.910 12.738  0.38 16.94 ?  10   LEU   A HA   1 
ATOM   200  H  HB2  A LEU   A 1 10  ? 6.625  -11.648 10.655  0.62 17.01 ?  10   LEU   A HB2  1 
ATOM   201  H  HB2  B LEU   A 1 10  ? 6.855  -11.452 11.318  0.38 17.89 ?  10   LEU   A HB2  1 
ATOM   202  H  HB3  A LEU   A 1 10  ? 7.877  -11.851 9.709   0.62 17.01 ?  10   LEU   A HB3  1 
ATOM   203  H  HB3  B LEU   A 1 10  ? 7.999  -11.597 10.237  0.38 17.89 ?  10   LEU   A HB3  1 
ATOM   204  H  HG   A LEU   A 1 10  ? 7.316  -14.169 9.611   0.62 19.85 ?  10   LEU   A HG   1 
ATOM   205  H  HG   B LEU   A 1 10  ? 7.304  -13.851 9.917   0.38 19.42 ?  10   LEU   A HG   1 
ATOM   206  H  HD11 A LEU   A 1 10  ? 5.238  -14.870 10.284  0.62 21.82 ?  10   LEU   A HD11 1 
ATOM   207  H  HD11 B LEU   A 1 10  ? 5.290  -14.548 10.760  0.38 20.73 ?  10   LEU   A HD11 1 
ATOM   208  H  HD12 A LEU   A 1 10  ? 5.983  -14.247 11.540  0.62 21.82 ?  10   LEU   A HD12 1 
ATOM   209  H  HD12 B LEU   A 1 10  ? 6.193  -14.078 11.980  0.38 20.73 ?  10   LEU   A HD12 1 
ATOM   210  H  HD13 A LEU   A 1 10  ? 4.873  -13.405 10.779  0.62 21.82 ?  10   LEU   A HD13 1 
ATOM   211  H  HD13 B LEU   A 1 10  ? 5.053  -13.127 11.436  0.38 20.73 ?  10   LEU   A HD13 1 
ATOM   212  H  HD21 A LEU   A 1 10  ? 5.635  -13.906 8.036   0.62 20.91 ?  10   LEU   A HD21 1 
ATOM   213  H  HD21 B LEU   A 1 10  ? 5.477  -13.284 8.585   0.38 20.73 ?  10   LEU   A HD21 1 
ATOM   214  H  HD22 A LEU   A 1 10  ? 5.413  -12.412 8.530   0.62 20.91 ?  10   LEU   A HD22 1 
ATOM   215  H  HD22 B LEU   A 1 10  ? 5.393  -11.872 9.310   0.38 20.73 ?  10   LEU   A HD22 1 
ATOM   216  H  HD23 A LEU   A 1 10  ? 6.777  -12.821 7.827   0.62 20.91 ?  10   LEU   A HD23 1 
ATOM   217  H  HD23 B LEU   A 1 10  ? 6.648  -12.226 8.402   0.38 20.73 ?  10   LEU   A HD23 1 
ATOM   218  N  N    A LYS   A 1 11  ? 9.199  -14.752 11.450  0.62 12.57 ?  11   LYS   A N    1 
ATOM   219  N  N    B LYS   A 1 11  ? 9.526  -14.682 12.029  0.38 12.11 ?  11   LYS   A N    1 
ATOM   220  C  CA   A LYS   A 1 11  ? 10.232 -15.742 11.183  0.62 13.02 ?  11   LYS   A CA   1 
ATOM   221  C  CA   B LYS   A 1 11  ? 10.420 -15.722 11.539  0.38 11.88 ?  11   LYS   A CA   1 
ATOM   222  C  C    A LYS   A 1 11  ? 9.926  -16.406 9.847   0.62 13.36 ?  11   LYS   A C    1 
ATOM   223  C  C    B LYS   A 1 11  ? 9.950  -16.180 10.165  0.38 11.49 ?  11   LYS   A C    1 
ATOM   224  O  O    A LYS   A 1 11  ? 8.901  -17.078 9.715   0.62 14.69 ?  11   LYS   A O    1 
ATOM   225  O  O    B LYS   A 1 11  ? 8.800  -16.599 10.002  0.38 11.78 ?  11   LYS   A O    1 
ATOM   226  C  CB   A LYS   A 1 11  ? 10.253 -16.765 12.320  0.62 13.40 ?  11   LYS   A CB   1 
ATOM   227  C  CB   B LYS   A 1 11  ? 10.442 -16.895 12.517  0.38 12.13 ?  11   LYS   A CB   1 
ATOM   228  C  CG   A LYS   A 1 11  ? 11.291 -17.863 12.192  0.62 13.30 ?  11   LYS   A CG   1 
ATOM   229  C  CG   B LYS   A 1 11  ? 11.475 -17.973 12.200  0.38 12.46 ?  11   LYS   A CG   1 
ATOM   230  C  CD   A LYS   A 1 11  ? 11.388 -18.671 13.488  0.62 13.55 ?  11   LYS   A CD   1 
ATOM   231  C  CD   B LYS   A 1 11  ? 11.574 -18.960 13.357  0.38 12.74 ?  11   LYS   A CD   1 
ATOM   232  C  CE   A LYS   A 1 11  ? 12.360 -19.841 13.362  0.62 13.88 ?  11   LYS   A CE   1 
ATOM   233  C  CE   B LYS   A 1 11  ? 12.644 -20.018 13.134  0.38 13.07 ?  11   LYS   A CE   1 
ATOM   234  N  NZ   A LYS   A 1 11  ? 13.746 -19.393 13.054  0.62 14.24 ?  11   LYS   A NZ   1 
ATOM   235  N  NZ   B LYS   A 1 11  ? 14.003 -19.426 13.024  0.38 13.42 ?  11   LYS   A NZ   1 
ATOM   236  H  H    A LYS   A 1 11  ? 8.466  -15.086 11.766  0.62 15.10 ?  11   LYS   A H    1 
ATOM   237  H  H    B LYS   A 1 11  ? 9.045  -14.908 12.707  0.38 14.55 ?  11   LYS   A H    1 
ATOM   238  H  HA   A LYS   A 1 11  ? 11.093 -15.305 11.130  0.62 15.64 ?  11   LYS   A HA   1 
ATOM   239  H  HA   B LYS   A 1 11  ? 11.316 -15.364 11.457  0.38 14.27 ?  11   LYS   A HA   1 
ATOM   240  H  HB2  A LYS   A 1 11  ? 10.427 -16.289 13.149  0.62 16.10 ?  11   LYS   A HB2  1 
ATOM   241  H  HB2  B LYS   A 1 11  ? 10.637 -16.554 13.403  0.38 14.57 ?  11   LYS   A HB2  1 
ATOM   242  H  HB3  A LYS   A 1 11  ? 9.381  -17.184 12.367  0.62 16.10 ?  11   LYS   A HB3  1 
ATOM   243  H  HB3  B LYS   A 1 11  ? 9.568  -17.315 12.513  0.38 14.57 ?  11   LYS   A HB3  1 
ATOM   244  H  HG2  A LYS   A 1 11  ? 11.035 -18.463 11.475  0.62 15.98 ?  11   LYS   A HG2  1 
ATOM   245  H  HG2  B LYS   A 1 11  ? 11.206 -18.458 11.402  0.38 14.96 ?  11   LYS   A HG2  1 
ATOM   246  H  HG3  A LYS   A 1 11  ? 12.157 -17.467 12.011  0.62 15.98 ?  11   LYS   A HG3  1 
ATOM   247  H  HG3  B LYS   A 1 11  ? 12.345 -17.563 12.068  0.38 14.96 ?  11   LYS   A HG3  1 
ATOM   248  H  HD2  A LYS   A 1 11  ? 11.697 -18.090 14.203  0.62 16.27 ?  11   LYS   A HD2  1 
ATOM   249  H  HD2  B LYS   A 1 11  ? 11.792 -18.475 14.166  0.38 15.31 ?  11   LYS   A HD2  1 
ATOM   250  H  HD3  A LYS   A 1 11  ? 10.510 -19.027 13.708  0.62 16.27 ?  11   LYS   A HD3  1 
ATOM   251  H  HD3  B LYS   A 1 11  ? 10.721 -19.412 13.458  0.38 15.31 ?  11   LYS   A HD3  1 
ATOM   252  H  HE2  A LYS   A 1 11  ? 12.382 -20.326 14.201  0.62 16.68 ?  11   LYS   A HE2  1 
ATOM   253  H  HE2  B LYS   A 1 11  ? 12.641 -20.634 13.884  0.38 15.70 ?  11   LYS   A HE2  1 
ATOM   254  H  HE3  A LYS   A 1 11  ? 12.065 -20.422 12.646  0.62 16.68 ?  11   LYS   A HE3  1 
ATOM   255  H  HE3  B LYS   A 1 11  ? 12.453 -20.492 12.311  0.38 15.70 ?  11   LYS   A HE3  1 
ATOM   256  H  HZ1  A LYS   A 1 11  ? 14.282 -20.099 12.969  0.62 17.10 ?  11   LYS   A HZ1  1 
ATOM   257  H  HZ1  B LYS   A 1 11  ? 14.607 -20.072 12.916  0.38 16.12 ?  11   LYS   A HZ1  1 
ATOM   258  H  HZ2  A LYS   A 1 11  ? 13.755 -18.932 12.292  0.62 17.10 ?  11   LYS   A HZ2  1 
ATOM   259  H  HZ2  B LYS   A 1 11  ? 14.040 -18.877 12.325  0.38 16.12 ?  11   LYS   A HZ2  1 
ATOM   260  H  HZ3  A LYS   A 1 11  ? 14.054 -18.875 13.708  0.62 17.10 ?  11   LYS   A HZ3  1 
ATOM   261  H  HZ3  B LYS   A 1 11  ? 14.197 -18.970 13.763  0.38 16.12 ?  11   LYS   A HZ3  1 
ATOM   262  N  N    A LEU   A 1 12  ? 10.803 -16.221 8.856   0.62 12.62 ?  12   LEU   A N    1 
ATOM   263  N  N    B LEU   A 1 12  ? 10.830 -16.085 9.172   0.38 11.84 ?  12   LEU   A N    1 
ATOM   264  C  CA   A LEU   A 1 12  ? 10.578 -16.845 7.555   0.62 12.81 ?  12   LEU   A CA   1 
ATOM   265  C  CA   B LEU   A 1 12  ? 10.532 -16.567 7.829   0.38 12.16 ?  12   LEU   A CA   1 
ATOM   266  C  C    A LEU   A 1 12  ? 11.196 -18.234 7.462   0.62 12.78 ?  12   LEU   A C    1 
ATOM   267  C  C    B LEU   A 1 12  ? 11.093 -17.958 7.557   0.38 12.38 ?  12   LEU   A C    1 
ATOM   268  O  O    A LEU   A 1 12  ? 10.590 -19.139 6.881   0.62 12.84 ?  12   LEU   A O    1 
ATOM   269  O  O    B LEU   A 1 12  ? 10.427 -18.776 6.914   0.38 11.85 ?  12   LEU   A O    1 
ATOM   270  C  CB   A LEU   A 1 12  ? 11.127 -15.968 6.425   0.62 12.78 ?  12   LEU   A CB   1 
ATOM   271  C  CB   B LEU   A 1 12  ? 11.071 -15.590 6.779   0.38 12.93 ?  12   LEU   A CB   1 
ATOM   272  C  CG   A LEU   A 1 12  ? 10.469 -14.600 6.249   0.62 13.28 ?  12   LEU   A CG   1 
ATOM   273  C  CG   B LEU   A 1 12  ? 10.383 -14.227 6.695   0.38 14.01 ?  12   LEU   A CG   1 
ATOM   274  C  CD1  A LEU   A 1 12  ? 11.220 -13.786 5.214   0.62 14.01 ?  12   LEU   A CD1  1 
ATOM   275  C  CD1  B LEU   A 1 12  ? 10.899 -13.443 5.495   0.38 14.65 ?  12   LEU   A CD1  1 
ATOM   276  C  CD2  A LEU   A 1 12  ? 9.001  -14.754 5.861   0.62 14.05 ?  12   LEU   A CD2  1 
ATOM   277  C  CD2  B LEU   A 1 12  ? 8.874  -14.404 6.621   0.38 14.79 ?  12   LEU   A CD2  1 
ATOM   278  H  H    A LEU   A 1 12  ? 11.527 -15.758 8.910   0.62 15.16 ?  12   LEU   A H    1 
ATOM   279  H  H    B LEU   A 1 12  ? 11.607 -15.726 9.258   0.38 14.22 ?  12   LEU   A H    1 
ATOM   280  H  HA   A LEU   A 1 12  ? 9.623  -16.945 7.416   0.62 15.38 ?  12   LEU   A HA   1 
ATOM   281  H  HA   B LEU   A 1 12  ? 9.568  -16.616 7.729   0.38 14.60 ?  12   LEU   A HA   1 
ATOM   282  H  HB2  A LEU   A 1 12  ? 12.069 -15.817 6.588   0.62 15.35 ?  12   LEU   A HB2  1 
ATOM   283  H  HB2  B LEU   A 1 12  ? 12.008 -15.426 6.971   0.38 15.54 ?  12   LEU   A HB2  1 
ATOM   284  H  HB3  A LEU   A 1 12  ? 11.020 -16.452 5.587   0.62 15.35 ?  12   LEU   A HB3  1 
ATOM   285  H  HB3  B LEU   A 1 12  ? 10.988 -16.007 5.910   0.38 15.54 ?  12   LEU   A HB3  1 
ATOM   286  H  HG   A LEU   A 1 12  ? 10.504 -14.128 7.092   0.62 15.95 ?  12   LEU   A HG   1 
ATOM   287  H  HG   B LEU   A 1 12  ? 10.587 -13.716 7.496   0.38 16.83 ?  12   LEU   A HG   1 
ATOM   288  H  HD11 A LEU   A 1 12  ? 10.785 -12.926 5.116   0.62 16.82 ?  12   LEU   A HD11 1 
ATOM   289  H  HD11 B LEU   A 1 12  ? 10.454 -12.582 5.463   0.38 17.59 ?  12   LEU   A HD11 1 
ATOM   290  H  HD12 A LEU   A 1 12  ? 12.134 -13.666 5.513   0.62 16.82 ?  12   LEU   A HD12 1 
ATOM   291  H  HD12 B LEU   A 1 12  ? 11.856 -13.318 5.587   0.38 17.59 ?  12   LEU   A HD12 1 
ATOM   292  H  HD13 A LEU   A 1 12  ? 11.208 -14.262 4.368   0.62 16.82 ?  12   LEU   A HD13 1 
ATOM   293  H  HD13 B LEU   A 1 12  ? 10.707 -13.944 4.686   0.38 17.59 ?  12   LEU   A HD13 1 
ATOM   294  H  HD21 A LEU   A 1 12  ? 8.635  -13.881 5.656   0.62 16.88 ?  12   LEU   A HD21 1 
ATOM   295  H  HD21 B LEU   A 1 12  ? 8.473  -13.580 6.311   0.38 17.76 ?  12   LEU   A HD21 1 
ATOM   296  H  HD22 A LEU   A 1 12  ? 8.936  -15.330 5.081   0.62 16.88 ?  12   LEU   A HD22 1 
ATOM   297  H  HD22 B LEU   A 1 12  ? 8.674  -15.126 6.005   0.38 17.76 ?  12   LEU   A HD22 1 
ATOM   298  H  HD23 A LEU   A 1 12  ? 8.513  -15.152 6.601   0.62 16.88 ?  12   LEU   A HD23 1 
ATOM   299  H  HD23 B LEU   A 1 12  ? 8.539  -14.625 7.506   0.38 17.76 ?  12   LEU   A HD23 1 
ATOM   300  N  N    A THR   A 1 13  ? 12.400 -18.402 8.002   0.62 12.79 ?  13   THR   A N    1 
ATOM   301  N  N    B THR   A 1 13  ? 12.311 -18.239 8.013   0.38 12.54 ?  13   THR   A N    1 
ATOM   302  C  CA   A THR   A 1 13  ? 13.127 -19.664 7.969   0.62 12.46 ?  13   THR   A CA   1 
ATOM   303  C  CA   B THR   A 1 13  ? 12.947 -19.537 7.815   0.38 12.62 ?  13   THR   A CA   1 
ATOM   304  C  C    A THR   A 1 13  ? 13.868 -19.821 9.290   0.62 12.72 ?  13   THR   A C    1 
ATOM   305  C  C    B THR   A 1 13  ? 13.779 -19.847 9.053   0.38 12.67 ?  13   THR   A C    1 
ATOM   306  O  O    A THR   A 1 13  ? 13.738 -19.009 10.210  0.62 13.32 ?  13   THR   A O    1 
ATOM   307  O  O    B THR   A 1 13  ? 13.732 -19.127 10.055  0.38 12.92 ?  13   THR   A O    1 
ATOM   308  C  CB   A THR   A 1 13  ? 14.134 -19.722 6.809   0.62 12.61 ?  13   THR   A CB   1 
ATOM   309  C  CB   B THR   A 1 13  ? 13.852 -19.538 6.575   0.38 12.54 ?  13   THR   A CB   1 
ATOM   310  O  OG1  A THR   A 1 13  ? 15.197 -18.801 7.068   0.62 11.95 ?  13   THR   A OG1  1 
ATOM   311  O  OG1  B THR   A 1 13  ? 14.912 -18.598 6.775   0.38 12.63 ?  13   THR   A OG1  1 
ATOM   312  C  CG2  A THR   A 1 13  ? 13.493 -19.401 5.466   0.62 13.02 ?  13   THR   A CG2  1 
ATOM   313  C  CG2  B THR   A 1 13  ? 13.087 -19.174 5.309   0.38 13.12 ?  13   THR   A CG2  1 
ATOM   314  H  H    A THR   A 1 13  ? 12.829 -17.776 8.396   0.62 15.37 ?  13   THR   A H    1 
ATOM   315  H  H    B THR   A 1 13  ? 12.800 -17.679 8.445   0.38 15.06 ?  13   THR   A H    1 
ATOM   316  H  HA   A THR   A 1 13  ? 12.507 -20.401 7.873   0.62 14.96 ?  13   THR   A HA   1 
ATOM   317  H  HA   B THR   A 1 13  ? 12.267 -20.224 7.704   0.38 15.16 ?  13   THR   A HA   1 
ATOM   318  H  HB   A THR   A 1 13  ? 14.505 -20.619 6.756   0.62 15.14 ?  13   THR   A HB   1 
ATOM   319  H  HB   B THR   A 1 13  ? 14.228 -20.424 6.455   0.38 15.06 ?  13   THR   A HB   1 
ATOM   320  H  HG1  A THR   A 1 13  ? 15.831 -19.192 7.461   0.62 14.35 ?  13   THR   A HG1  1 
ATOM   321  H  HG1  B THR   A 1 13  ? 15.424 -18.593 6.108   0.38 15.18 ?  13   THR   A HG1  1 
ATOM   322  H  HG21 A THR   A 1 13  ? 14.146 -19.516 4.752   0.62 15.64 ?  13   THR   A HG21 1 
ATOM   323  H  HG21 B THR   A 1 13  ? 13.668 -19.264 4.535   0.38 15.76 ?  13   THR   A HG21 1 
ATOM   324  H  HG22 A THR   A 1 13  ? 12.748 -19.999 5.305   0.62 15.64 ?  13   THR   A HG22 1 
ATOM   325  H  HG22 B THR   A 1 13  ? 12.328 -19.768 5.200   0.38 15.76 ?  13   THR   A HG22 1 
ATOM   326  H  HG23 A THR   A 1 13  ? 13.178 -18.487 5.457   0.62 15.64 ?  13   THR   A HG23 1 
ATOM   327  H  HG23 B THR   A 1 13  ? 12.770 -18.261 5.362   0.38 15.76 ?  13   THR   A HG23 1 
ATOM   328  N  N    A ASP   A 1 14  ? 14.680 -20.872 9.362   0.62 12.65 ?  14   ASP   A N    1 
ATOM   329  N  N    B ASP   A 1 14  ? 14.579 -20.912 8.971   0.38 12.90 ?  14   ASP   A N    1 
ATOM   330  C  CA   A ASP   A 1 14  ? 15.498 -21.109 10.542  0.62 12.60 ?  14   ASP   A CA   1 
ATOM   331  C  CA   B ASP   A 1 14  ? 15.462 -21.249 10.082  0.38 13.09 ?  14   ASP   A CA   1 
ATOM   332  C  C    A ASP   A 1 14  ? 16.292 -19.867 10.942  0.62 12.14 ?  14   ASP   A C    1 
ATOM   333  C  C    B ASP   A 1 14  ? 16.357 -20.076 10.480  0.38 11.65 ?  14   ASP   A C    1 
ATOM   334  O  O    A ASP   A 1 14  ? 16.466 -19.589 12.135  0.62 12.61 ?  14   ASP   A O    1 
ATOM   335  O  O    B ASP   A 1 14  ? 16.704 -19.936 11.658  0.38 11.57 ?  14   ASP   A O    1 
ATOM   336  C  CB   A ASP   A 1 14  ? 16.460 -22.257 10.257  0.62 14.85 ?  14   ASP   A CB   1 
ATOM   337  C  CB   B ASP   A 1 14  ? 16.317 -22.468 9.718   0.38 15.26 ?  14   ASP   A CB   1 
ATOM   338  C  CG   A ASP   A 1 14  ? 17.361 -22.534 11.422  0.62 18.93 ?  14   ASP   A CG   1 
ATOM   339  C  CG   B ASP   A 1 14  ? 17.220 -22.907 10.859  0.38 17.75 ?  14   ASP   A CG   1 
ATOM   340  O  OD1  A ASP   A 1 14  ? 16.847 -22.951 12.481  0.62 20.61 ?  14   ASP   A OD1  1 
ATOM   341  O  OD1  B ASP   A 1 14  ? 16.693 -23.337 11.909  0.38 18.65 ?  14   ASP   A OD1  1 
ATOM   342  O  OD2  A ASP   A 1 14  ? 18.578 -22.305 11.285  0.62 21.60 -1 14   ASP   A OD2  1 
ATOM   343  O  OD2  B ASP   A 1 14  ? 18.454 -22.836 10.702  0.38 19.09 -1 14   ASP   A OD2  1 
ATOM   344  H  H    A ASP   A 1 14  ? 14.786 -21.445 8.740   0.62 15.20 ?  14   ASP   A H    1 
ATOM   345  H  H    B ASP   A 1 14  ? 14.631 -21.443 8.292   0.38 15.50 ?  14   ASP   A H    1 
ATOM   346  H  HA   A ASP   A 1 14  ? 14.929 -21.362 11.286  0.62 15.13 ?  14   ASP   A HA   1 
ATOM   347  H  HA   B ASP   A 1 14  ? 14.925 -21.494 10.852  0.38 15.72 ?  14   ASP   A HA   1 
ATOM   348  H  HB2  A ASP   A 1 14  ? 15.942 -23.058 10.051  0.62 17.84 ?  14   ASP   A HB2  1 
ATOM   349  H  HB2  B ASP   A 1 14  ? 15.733 -23.220 9.505   0.38 18.33 ?  14   ASP   A HB2  1 
ATOM   350  H  HB3  A ASP   A 1 14  ? 17.016 -22.025 9.495   0.62 17.84 ?  14   ASP   A HB3  1 
ATOM   351  H  HB3  B ASP   A 1 14  ? 16.865 -22.255 8.944   0.38 18.33 ?  14   ASP   A HB3  1 
ATOM   352  N  N    A ASN   A 1 15  ? 16.791 -19.110 9.962   0.62 11.99 ?  15   ASN   A N    1 
ATOM   353  N  N    B ASN   A 1 15  ? 16.744 -19.218 9.523   0.38 10.24 ?  15   ASN   A N    1 
ATOM   354  C  CA   A ASN   A 1 15  ? 17.758 -18.050 10.223  0.62 12.45 ?  15   ASN   A CA   1 
ATOM   355  C  CA   B ASN   A 1 15  ? 17.752 -18.195 9.801   0.38 10.70 ?  15   ASN   A CA   1 
ATOM   356  C  C    A ASN   A 1 15  ? 17.379 -16.681 9.671   0.62 12.41 ?  15   ASN   A C    1 
ATOM   357  C  C    B ASN   A 1 15  ? 17.402 -16.783 9.325   0.38 11.71 ?  15   ASN   A C    1 
ATOM   358  O  O    A ASN   A 1 15  ? 18.088 -15.714 9.973   0.62 12.26 ?  15   ASN   A O    1 
ATOM   359  O  O    B ASN   A 1 15  ? 18.273 -15.903 9.377   0.38 11.98 ?  15   ASN   A O    1 
ATOM   360  C  CB   A ASN   A 1 15  ? 19.137 -18.429 9.655   0.62 12.65 ?  15   ASN   A CB   1 
ATOM   361  C  CB   B ASN   A 1 15  ? 19.119 -18.603 9.231   0.38 10.01 ?  15   ASN   A CB   1 
ATOM   362  C  CG   A ASN   A 1 15  ? 19.127 -18.557 8.144   0.62 12.64 ?  15   ASN   A CG   1 
ATOM   363  C  CG   B ASN   A 1 15  ? 19.123 -18.654 7.715   0.38 10.39 ?  15   ASN   A CG   1 
ATOM   364  O  OD1  A ASN   A 1 15  ? 18.348 -19.331 7.582   0.62 12.95 ?  15   ASN   A OD1  1 
ATOM   365  O  OD1  B ASN   A 1 15  ? 18.510 -19.537 7.112   0.38 10.73 ?  15   ASN   A OD1  1 
ATOM   366  N  ND2  A ASN   A 1 15  ? 19.978 -17.779 7.473   0.62 13.17 ?  15   ASN   A ND2  1 
ATOM   367  N  ND2  B ASN   A 1 15  ? 19.810 -17.701 7.089   0.38 10.39 ?  15   ASN   A ND2  1 
ATOM   368  H  H    A ASN   A 1 15  ? 16.579 -19.186 9.142   0.62 14.41 ?  15   ASN   A H    1 
ATOM   369  H  H    B ASN   A 1 15  ? 16.440 -19.221 8.718   0.38 12.30 ?  15   ASN   A H    1 
ATOM   370  H  HA   A ASN   A 1 15  ? 17.865 -17.952 11.185  0.62 14.95 ?  15   ASN   A HA   1 
ATOM   371  H  HA   B ASN   A 1 15  ? 17.860 -18.149 10.760  0.38 12.85 ?  15   ASN   A HA   1 
ATOM   372  H  HB2  A ASN   A 1 15  ? 19.783 -17.742 9.899   0.62 15.19 ?  15   ASN   A HB2  1 
ATOM   373  H  HB2  B ASN   A 1 15  ? 19.786 -17.951 9.516   0.38 12.03 ?  15   ASN   A HB2  1 
ATOM   374  H  HB3  A ASN   A 1 15  ? 19.412 -19.282 10.030  0.62 15.19 ?  15   ASN   A HB3  1 
ATOM   375  H  HB3  B ASN   A 1 15  ? 19.364 -19.483 9.570   0.38 12.03 ?  15   ASN   A HB3  1 
ATOM   376  H  HD21 A ASN   A 1 15  ? 20.010 -17.813 6.611   0.62 15.83 ?  15   ASN   A HD21 1 
ATOM   377  H  HD21 B ASN   A 1 15  ? 19.844 -17.695 6.230   0.38 12.48 ?  15   ASN   A HD21 1 
ATOM   378  H  HD22 A ASN   A 1 15  ? 20.503 -17.244 7.896   0.62 15.83 ?  15   ASN   A HD22 1 
ATOM   379  H  HD22 B ASN   A 1 15  ? 20.223 -17.096 7.540   0.38 12.48 ?  15   ASN   A HD22 1 
ATOM   380  N  N    A VAL   A 1 16  ? 16.308 -16.565 8.880   0.62 12.64 ?  16   VAL   A N    1 
ATOM   381  N  N    B VAL   A 1 16  ? 16.168 -16.523 8.891   0.38 12.39 ?  16   VAL   A N    1 
ATOM   382  C  CA   A VAL   A 1 16  ? 15.888 -15.299 8.282   0.62 12.62 ?  16   VAL   A CA   1 
ATOM   383  C  CA   B VAL   A 1 16  ? 15.789 -15.225 8.337   0.38 12.64 ?  16   VAL   A CA   1 
ATOM   384  C  C    A VAL   A 1 16  ? 14.593 -14.821 8.929   0.62 12.02 ?  16   VAL   A C    1 
ATOM   385  C  C    B VAL   A 1 16  ? 14.564 -14.701 9.081   0.38 12.58 ?  16   VAL   A C    1 
ATOM   386  O  O    A VAL   A 1 16  ? 13.587 -15.544 8.963   0.62 11.91 ?  16   VAL   A O    1 
ATOM   387  O  O    B VAL   A 1 16  ? 13.589 -15.435 9.283   0.38 12.89 ?  16   VAL   A O    1 
ATOM   388  C  CB   A VAL   A 1 16  ? 15.734 -15.396 6.754   0.62 13.00 ?  16   VAL   A CB   1 
ATOM   389  C  CB   B VAL   A 1 16  ? 15.528 -15.310 6.818   0.38 12.97 ?  16   VAL   A CB   1 
ATOM   390  C  CG1  A VAL   A 1 16  ? 15.276 -14.056 6.191   0.62 13.42 ?  16   VAL   A CG1  1 
ATOM   391  C  CG1  B VAL   A 1 16  ? 15.105 -13.957 6.250   0.38 13.22 ?  16   VAL   A CG1  1 
ATOM   392  C  CG2  A VAL   A 1 16  ? 17.036 -15.826 6.104   0.62 13.75 ?  16   VAL   A CG2  1 
ATOM   393  C  CG2  B VAL   A 1 16  ? 16.761 -15.841 6.080   0.38 13.49 ?  16   VAL   A CG2  1 
ATOM   394  H  H    A VAL   A 1 16  ? 15.808 -17.231 8.675   0.62 15.18 ?  16   VAL   A H    1 
ATOM   395  H  H    B VAL   A 1 16  ? 15.520 -17.089 8.920   0.38 14.89 ?  16   VAL   A H    1 
ATOM   396  H  HA   A VAL   A 1 16  ? 16.574 -14.637 8.461   0.62 15.16 ?  16   VAL   A HA   1 
ATOM   397  H  HA   B VAL   A 1 16  ? 16.516 -14.597 8.483   0.38 15.18 ?  16   VAL   A HA   1 
ATOM   398  H  HB   A VAL   A 1 16  ? 15.060 -16.061 6.545   0.62 15.61 ?  16   VAL   A HB   1 
ATOM   399  H  HB   B VAL   A 1 16  ? 14.807 -15.935 6.667   0.38 15.58 ?  16   VAL   A HB   1 
ATOM   400  H  HG11 A VAL   A 1 16  ? 15.404 -14.060 5.231   0.62 16.12 ?  16   VAL   A HG11 1 
ATOM   401  H  HG11 B VAL   A 1 16  ? 15.110 -14.012 5.280   0.38 15.88 ?  16   VAL   A HG11 1 
ATOM   402  H  HG12 A VAL   A 1 16  ? 14.337 -13.931 6.400   0.62 16.12 ?  16   VAL   A HG12 1 
ATOM   403  H  HG12 B VAL   A 1 16  ? 14.212 -13.749 6.563   0.38 15.88 ?  16   VAL   A HG12 1 
ATOM   404  H  HG13 A VAL   A 1 16  ? 15.804 -13.350 6.594   0.62 16.12 ?  16   VAL   A HG13 1 
ATOM   405  H  HG13 B VAL   A 1 16  ? 15.730 -13.279 6.545   0.38 15.88 ?  16   VAL   A HG13 1 
ATOM   406  H  HG21 A VAL   A 1 16  ? 16.921 -15.823 5.141   0.62 16.51 ?  16   VAL   A HG21 1 
ATOM   407  H  HG21 B VAL   A 1 16  ? 16.584 -15.839 5.125   0.38 16.21 ?  16   VAL   A HG21 1 
ATOM   408  H  HG22 A VAL   A 1 16  ? 17.735 -15.206 6.356   0.62 16.51 ?  16   VAL   A HG22 1 
ATOM   409  H  HG22 B VAL   A 1 16  ? 17.522 -15.271 6.274   0.38 16.21 ?  16   VAL   A HG22 1 
ATOM   410  H  HG23 A VAL   A 1 16  ? 17.260 -16.719 6.408   0.62 16.51 ?  16   VAL   A HG23 1 
ATOM   411  H  HG23 B VAL   A 1 16  ? 16.946 -16.748 6.377   0.38 16.21 ?  16   VAL   A HG23 1 
ATOM   412  N  N    A TYR   A 1 17  ? 14.619 -13.567 9.378   0.62 11.76 ?  17   TYR   A N    1 
ATOM   413  N  N    B TYR   A 1 17  ? 14.614 -13.422 9.465   0.38 12.29 ?  17   TYR   A N    1 
ATOM   414  C  CA   A TYR   A 1 17  ? 13.517 -12.874 10.026  0.62 11.94 ?  17   TYR   A CA   1 
ATOM   415  C  CA   B TYR   A 1 17  ? 13.582 -12.767 10.258  0.38 11.79 ?  17   TYR   A CA   1 
ATOM   416  C  C    A TYR   A 1 17  ? 13.240 -11.577 9.270   0.62 11.61 ?  17   TYR   A C    1 
ATOM   417  C  C    B TYR   A 1 17  ? 13.298 -11.404 9.641   0.38 11.15 ?  17   TYR   A C    1 
ATOM   418  O  O    A TYR   A 1 17  ? 14.133 -11.029 8.622   0.62 11.25 ?  17   TYR   A O    1 
ATOM   419  O  O    B TYR   A 1 17  ? 14.203 -10.775 9.091   0.38 10.84 ?  17   TYR   A O    1 
ATOM   420  C  CB   A TYR   A 1 17  ? 13.917 -12.541 11.467  0.62 12.46 ?  17   TYR   A CB   1 
ATOM   421  C  CB   B TYR   A 1 17  ? 14.074 -12.589 11.700  0.38 12.09 ?  17   TYR   A CB   1 
ATOM   422  C  CG   A TYR   A 1 17  ? 14.066 -13.772 12.333  0.62 13.44 ?  17   TYR   A CG   1 
ATOM   423  C  CG   B TYR   A 1 17  ? 14.340 -13.887 12.437  0.38 12.26 ?  17   TYR   A CG   1 
ATOM   424  C  CD1  A TYR   A 1 17  ? 15.219 -14.550 12.293  0.62 13.95 ?  17   TYR   A CD1  1 
ATOM   425  C  CD1  B TYR   A 1 17  ? 15.556 -14.556 12.315  0.38 12.56 ?  17   TYR   A CD1  1 
ATOM   426  C  CD2  A TYR   A 1 17  ? 13.036 -14.179 13.172  0.62 13.53 ?  17   TYR   A CD2  1 
ATOM   427  C  CD2  B TYR   A 1 17  ? 13.370 -14.443 13.260  0.38 12.17 ?  17   TYR   A CD2  1 
ATOM   428  C  CE1  A TYR   A 1 17  ? 15.343 -15.697 13.074  0.62 14.25 ?  17   TYR   A CE1  1 
ATOM   429  C  CE1  B TYR   A 1 17  ? 15.791 -15.748 12.995  0.38 12.89 ?  17   TYR   A CE1  1 
ATOM   430  C  CE2  A TYR   A 1 17  ? 13.153 -15.326 13.958  0.62 13.82 ?  17   TYR   A CE2  1 
ATOM   431  C  CE2  B TYR   A 1 17  ? 13.592 -15.624 13.942  0.38 12.23 ?  17   TYR   A CE2  1 
ATOM   432  C  CZ   A TYR   A 1 17  ? 14.310 -16.082 13.906  0.62 13.98 ?  17   TYR   A CZ   1 
ATOM   433  C  CZ   B TYR   A 1 17  ? 14.798 -16.276 13.807  0.38 12.23 ?  17   TYR   A CZ   1 
ATOM   434  O  OH   A TYR   A 1 17  ? 14.433 -17.216 14.682  0.62 14.52 ?  17   TYR   A OH   1 
ATOM   435  O  OH   B TYR   A 1 17  ? 14.995 -17.451 14.498  0.38 12.00 ?  17   TYR   A OH   1 
ATOM   436  H  H    A TYR   A 1 17  ? 15.319 -13.076 9.299   0.62 14.13 ?  17   TYR   A H    1 
ATOM   437  H  H    B TYR   A 1 17  ? 15.265 -12.887 9.261   0.38 14.77 ?  17   TYR   A H    1 
ATOM   438  H  HA   A TYR   A 1 17  ? 12.726 -13.441 10.020  0.62 14.34 ?  17   TYR   A HA   1 
ATOM   439  H  HA   B TYR   A 1 17  ? 12.769 -13.289 10.257  0.38 14.17 ?  17   TYR   A HA   1 
ATOM   440  H  HB2  A TYR   A 1 17  ? 14.772 -12.079 11.451  0.62 14.97 ?  17   TYR   A HB2  1 
ATOM   441  H  HB2  B TYR   A 1 17  ? 14.904 -12.088 11.686  0.38 14.53 ?  17   TYR   A HB2  1 
ATOM   442  H  HB3  A TYR   A 1 17  ? 13.240 -11.978 11.852  0.62 14.97 ?  17   TYR   A HB3  1 
ATOM   443  H  HB3  B TYR   A 1 17  ? 13.405 -12.105 12.201  0.38 14.53 ?  17   TYR   A HB3  1 
ATOM   444  H  HD1  A TYR   A 1 17  ? 15.923 -14.305 11.732  0.62 16.75 ?  17   TYR   A HD1  1 
ATOM   445  H  HD1  B TYR   A 1 17  ? 16.222 -14.207 11.766  0.38 15.08 ?  17   TYR   A HD1  1 
ATOM   446  H  HD2  A TYR   A 1 17  ? 12.254 -13.673 13.209  0.62 16.25 ?  17   TYR   A HD2  1 
ATOM   447  H  HD2  B TYR   A 1 17  ? 12.553 -14.014 13.354  0.38 14.62 ?  17   TYR   A HD2  1 
ATOM   448  H  HE1  A TYR   A 1 17  ? 16.125 -16.206 13.039  0.62 17.12 ?  17   TYR   A HE1  1 
ATOM   449  H  HE1  B TYR   A 1 17  ? 16.609 -16.191 12.905  0.38 15.48 ?  17   TYR   A HE1  1 
ATOM   450  H  HE2  A TYR   A 1 17  ? 12.452 -15.573 14.518  0.62 16.59 ?  17   TYR   A HE2  1 
ATOM   451  H  HE2  B TYR   A 1 17  ? 12.931 -15.983 14.488  0.38 14.70 ?  17   TYR   A HE2  1 
ATOM   452  H  HH   A TYR   A 1 17  ? 13.673 -17.442 14.964  0.62 17.44 ?  17   TYR   A HH   1 
ATOM   453  H  HH   B TYR   A 1 17  ? 15.753 -17.770 14.310  0.38 14.41 ?  17   TYR   A HH   1 
ATOM   454  N  N    A ILE   A 1 18  ? 12.008 -11.066 9.365   0.62 11.82 ?  18   ILE   A N    1 
ATOM   455  N  N    B ILE   A 1 18  ? 12.044 -10.935 9.727   0.38 11.03 ?  18   ILE   A N    1 
ATOM   456  C  CA   A ILE   A 1 18  ? 11.607 -9.895  8.582   0.62 12.30 ?  18   ILE   A CA   1 
ATOM   457  C  CA   B ILE   A 1 18  ? 11.643 -9.720  9.020   0.38 10.74 ?  18   ILE   A CA   1 
ATOM   458  C  C    A ILE   A 1 18  ? 10.631 -9.038  9.381   0.62 13.03 ?  18   ILE   A C    1 
ATOM   459  C  C    B ILE   A 1 18  ? 10.711 -8.863  9.869   0.38 11.15 ?  18   ILE   A C    1 
ATOM   460  O  O    A ILE   A 1 18  ? 9.809  -9.551  10.143  0.62 13.01 ?  18   ILE   A O    1 
ATOM   461  O  O    B ILE   A 1 18  ? 9.918  -9.370  10.669  0.38 11.86 ?  18   ILE   A O    1 
ATOM   462  C  CB   A ILE   A 1 18  ? 11.054 -10.329 7.200   0.62 12.26 ?  18   ILE   A CB   1 
ATOM   463  C  CB   B ILE   A 1 18  ? 11.007 -10.055 7.651   0.38 10.66 ?  18   ILE   A CB   1 
ATOM   464  C  CG1  A ILE   A 1 18  ? 10.946 -9.133  6.251   0.62 12.49 ?  18   ILE   A CG1  1 
ATOM   465  C  CG1  B ILE   A 1 18  ? 10.959 -8.827  6.742   0.38 11.65 ?  18   ILE   A CG1  1 
ATOM   466  C  CG2  A ILE   A 1 18  ? 9.737  -11.085 7.354   0.62 12.16 ?  18   ILE   A CG2  1 
ATOM   467  C  CG2  B ILE   A 1 18  ? 9.619  -10.648 7.828   0.38 10.54 ?  18   ILE   A CG2  1 
ATOM   468  C  CD1  A ILE   A 1 18  ? 10.793 -9.536  4.803   0.62 14.00 ?  18   ILE   A CD1  1 
ATOM   469  C  CD1  B ILE   A 1 18  ? 10.544 -9.177  5.335   0.38 12.55 ?  18   ILE   A CD1  1 
ATOM   470  H  H    A ILE   A 1 18  ? 11.393 -11.396 9.874   0.62 14.20 ?  18   ILE   A H    1 
ATOM   471  H  H    B ILE   A 1 18  ? 11.411 -11.312 10.181  0.38 13.25 ?  18   ILE   A H    1 
ATOM   472  H  HA   A ILE   A 1 18  ? 12.393 -9.368  8.416   0.62 14.78 ?  18   ILE   A HA   1 
ATOM   473  H  HA   B ILE   A 1 18  ? 12.443 -9.197  8.849   0.38 12.91 ?  18   ILE   A HA   1 
ATOM   474  H  HB   A ILE   A 1 18  ? 11.693 -10.950 6.812   0.62 14.73 ?  18   ILE   A HB   1 
ATOM   475  H  HB   B ILE   A 1 18  ? 11.563 -10.720 7.226   0.38 12.81 ?  18   ILE   A HB   1 
ATOM   476  H  HG12 A ILE   A 1 18  ? 10.173 -8.605  6.500   0.62 15.01 ?  18   ILE   A HG12 1 
ATOM   477  H  HG12 B ILE   A 1 18  ? 10.319 -8.190  7.094   0.38 14.00 ?  18   ILE   A HG12 1 
ATOM   478  H  HG13 A ILE   A 1 18  ? 11.753 -8.600  6.329   0.62 15.01 ?  18   ILE   A HG13 1 
ATOM   479  H  HG13 B ILE   A 1 18  ? 11.842 -8.425  6.701   0.38 14.00 ?  18   ILE   A HG13 1 
ATOM   480  H  HG21 A ILE   A 1 18  ? 9.482  -11.456 6.489   0.62 14.61 ?  18   ILE   A HG21 1 
ATOM   481  H  HG21 B ILE   A 1 18  ? 9.339  -11.045 6.988   0.38 12.67 ?  18   ILE   A HG21 1 
ATOM   482  H  HG22 A ILE   A 1 18  ? 9.859  -11.810 7.991   0.62 14.61 ?  18   ILE   A HG22 1 
ATOM   483  H  HG22 B ILE   A 1 18  ? 9.650  -11.323 8.521   0.38 12.67 ?  18   ILE   A HG22 1 
ATOM   484  H  HG23 A ILE   A 1 18  ? 9.053  -10.479 7.666   0.62 14.61 ?  18   ILE   A HG23 1 
ATOM   485  H  HG23 B ILE   A 1 18  ? 9.001  -9.942  8.080   0.38 12.67 ?  18   ILE   A HG23 1 
ATOM   486  H  HD11 A ILE   A 1 18  ? 10.757 -8.735  4.256   0.62 16.81 ?  18   ILE   A HD11 1 
ATOM   487  H  HD11 B ILE   A 1 18  ? 10.982 -8.578  4.713   0.38 15.07 ?  18   ILE   A HD11 1 
ATOM   488  H  HD12 A ILE   A 1 18  ? 11.552 -10.081 4.543   0.62 16.81 ?  18   ILE   A HD12 1 
ATOM   489  H  HD12 B ILE   A 1 18  ? 10.806 -10.094 5.148   0.38 15.07 ?  18   ILE   A HD12 1 
ATOM   490  H  HD13 A ILE   A 1 18  ? 9.971  -10.043 4.701   0.62 16.81 ?  18   ILE   A HD13 1 
ATOM   491  H  HD13 B ILE   A 1 18  ? 9.580  -9.092  5.259   0.38 15.07 ?  18   ILE   A HD13 1 
ATOM   492  N  N    A LYS   A 1 19  ? 10.716 -7.718  9.191   0.62 13.80 ?  19   LYS   A N    1 
ATOM   493  N  N    B LYS   A 1 19  ? 10.803 -7.546  9.670   0.38 11.61 ?  19   LYS   A N    1 
ATOM   494  C  CA   A LYS   A 1 19  ? 9.895  -6.766  9.933   0.62 15.02 ?  19   LYS   A CA   1 
ATOM   495  C  CA   B LYS   A 1 19  ? 9.994  -6.580  10.401  0.38 13.36 ?  19   LYS   A CA   1 
ATOM   496  C  C    A LYS   A 1 19  ? 9.708  -5.501  9.107   0.62 14.96 ?  19   LYS   A C    1 
ATOM   497  C  C    B LYS   A 1 19  ? 9.788  -5.355  9.517   0.38 14.08 ?  19   LYS   A C    1 
ATOM   498  O  O    A LYS   A 1 19  ? 10.583 -5.126  8.323   0.62 13.90 ?  19   LYS   A O    1 
ATOM   499  O  O    B LYS   A 1 19  ? 10.729 -4.901  8.865   0.38 13.95 ?  19   LYS   A O    1 
ATOM   500  C  CB   A LYS   A 1 19  ? 10.583 -6.394  11.254  0.62 16.07 ?  19   LYS   A CB   1 
ATOM   501  C  CB   B LYS   A 1 19  ? 10.727 -6.176  11.686  0.38 14.15 ?  19   LYS   A CB   1 
ATOM   502  C  CG   A LYS   A 1 19  ? 9.855  -5.395  12.157  0.62 17.62 ?  19   LYS   A CG   1 
ATOM   503  C  CG   B LYS   A 1 19  ? 9.954  -5.300  12.641  0.38 15.73 ?  19   LYS   A CG   1 
ATOM   504  C  CD   A LYS   A 1 19  ? 10.719 -5.112  13.390  0.62 18.86 ?  19   LYS   A CD   1 
ATOM   505  C  CD   B LYS   A 1 19  ? 10.836 -4.971  13.830  0.38 17.19 ?  19   LYS   A CD   1 
ATOM   506  C  CE   A LYS   A 1 19  ? 10.083 -4.136  14.371  0.62 20.18 ?  19   LYS   A CE   1 
ATOM   507  C  CE   B LYS   A 1 19  ? 10.120 -4.115  14.848  0.38 18.09 ?  19   LYS   A CE   1 
ATOM   508  N  NZ   A LYS   A 1 19  ? 10.975 -3.906  15.550  0.62 20.80 ?  19   LYS   A NZ   1 
ATOM   509  N  NZ   B LYS   A 1 19  ? 11.010 -3.832  16.003  0.38 18.72 ?  19   LYS   A NZ   1 
ATOM   510  H  H    A LYS   A 1 19  ? 11.252 -7.356  8.630   0.62 16.57 ?  19   LYS   A H    1 
ATOM   511  H  H    B LYS   A 1 19  ? 11.352 -7.176  9.111   0.38 13.95 ?  19   LYS   A H    1 
ATOM   512  H  HA   A LYS   A 1 19  ? 9.024  -7.165  10.122  0.62 18.04 ?  19   LYS   A HA   1 
ATOM   513  H  HA   B LYS   A 1 19  ? 9.136  -6.972  10.637  0.38 16.05 ?  19   LYS   A HA   1 
ATOM   514  H  HB2  A LYS   A 1 19  ? 10.703 -7.206  11.769  0.62 19.30 ?  19   LYS   A HB2  1 
ATOM   515  H  HB2  B LYS   A 1 19  ? 10.968 -6.980  12.176  0.38 16.99 ?  19   LYS   A HB2  1 
ATOM   516  H  HB3  A LYS   A 1 19  ? 11.445 -6.014  11.042  0.62 19.30 ?  19   LYS   A HB3  1 
ATOM   517  H  HB3  B LYS   A 1 19  ? 11.532 -5.694  11.445  0.38 16.99 ?  19   LYS   A HB3  1 
ATOM   518  H  HG2  A LYS   A 1 19  ? 9.714  -4.560  11.682  0.62 21.16 ?  19   LYS   A HG2  1 
ATOM   519  H  HG2  B LYS   A 1 19  ? 9.706  -4.473  12.200  0.38 18.89 ?  19   LYS   A HG2  1 
ATOM   520  H  HG3  A LYS   A 1 19  ? 9.008  -5.768  12.451  0.62 21.16 ?  19   LYS   A HG3  1 
ATOM   521  H  HG3  B LYS   A 1 19  ? 9.167  -5.772  12.958  0.38 18.89 ?  19   LYS   A HG3  1 
ATOM   522  H  HD2  A LYS   A 1 19  ? 10.874 -5.945  13.864  0.62 22.65 ?  19   LYS   A HD2  1 
ATOM   523  H  HD2  B LYS   A 1 19  ? 11.103 -5.798  14.264  0.38 20.64 ?  19   LYS   A HD2  1 
ATOM   524  H  HD3  A LYS   A 1 19  ? 11.565 -4.734  13.104  0.62 22.65 ?  19   LYS   A HD3  1 
ATOM   525  H  HD3  B LYS   A 1 19  ? 11.619 -4.489  13.521  0.38 20.64 ?  19   LYS   A HD3  1 
ATOM   526  H  HE2  A LYS   A 1 19  ? 9.938  -3.282  13.934  0.62 24.23 ?  19   LYS   A HE2  1 
ATOM   527  H  HE2  B LYS   A 1 19  ? 9.869  -3.272  14.437  0.38 21.73 ?  19   LYS   A HE2  1 
ATOM   528  H  HE3  A LYS   A 1 19  ? 9.243  -4.497  14.695  0.62 24.23 ?  19   LYS   A HE3  1 
ATOM   529  H  HE3  B LYS   A 1 19  ? 9.334  -4.584  15.168  0.38 21.73 ?  19   LYS   A HE3  1 
ATOM   530  H  HZ1  A LYS   A 1 19  ? 10.593 -3.337  16.119  0.62 24.98 ?  19   LYS   A HZ1  1 
ATOM   531  H  HZ1  B LYS   A 1 19  ? 10.581 -3.330  16.598  0.38 22.48 ?  19   LYS   A HZ1  1 
ATOM   532  H  HZ2  A LYS   A 1 19  ? 11.126 -4.676  15.973  0.62 24.98 ?  19   LYS   A HZ2  1 
ATOM   533  H  HZ2  B LYS   A 1 19  ? 11.255 -4.596  16.388  0.38 22.48 ?  19   LYS   A HZ2  1 
ATOM   534  H  HZ3  A LYS   A 1 19  ? 11.753 -3.567  15.283  0.62 24.98 ?  19   LYS   A HZ3  1 
ATOM   535  H  HZ3  B LYS   A 1 19  ? 11.737 -3.400  15.726  0.38 22.48 ?  19   LYS   A HZ3  1 
ATOM   536  N  N    A ASN   A 1 20  ? 8.556  -4.851  9.286   0.62 16.64 ?  20   ASN   A N    1 
ATOM   537  N  N    B ASN   A 1 20  ? 8.559  -4.831  9.479   0.38 15.50 ?  20   ASN   A N    1 
ATOM   538  C  CA   A ASN   A 1 20  ? 8.338  -3.504  8.766   0.62 17.63 ?  20   ASN   A CA   1 
ATOM   539  C  CA   B ASN   A 1 20  ? 8.284  -3.583  8.758   0.38 16.12 ?  20   ASN   A CA   1 
ATOM   540  C  C    A ASN   A 1 20  ? 8.963  -2.531  9.756   0.62 17.94 ?  20   ASN   A C    1 
ATOM   541  C  C    B ASN   A 1 20  ? 8.845  -2.431  9.578   0.38 16.52 ?  20   ASN   A C    1 
ATOM   542  O  O    A ASN   A 1 20  ? 8.463  -2.360  10.872  0.62 18.30 ?  20   ASN   A O    1 
ATOM   543  O  O    B ASN   A 1 20  ? 8.212  -1.961  10.527  0.38 17.17 ?  20   ASN   A O    1 
ATOM   544  C  CB   A ASN   A 1 20  ? 6.845  -3.234  8.577   0.62 18.83 ?  20   ASN   A CB   1 
ATOM   545  C  CB   B ASN   A 1 20  ? 6.785  -3.404  8.520   0.38 16.86 ?  20   ASN   A CB   1 
ATOM   546  C  CG   A ASN   A 1 20  ? 6.537  -1.769  8.266   0.62 19.97 ?  20   ASN   A CG   1 
ATOM   547  C  CG   B ASN   A 1 20  ? 6.433  -2.060  7.862   0.38 17.51 ?  20   ASN   A CG   1 
ATOM   548  O  OD1  A ASN   A 1 20  ? 5.670  -1.155  8.896   0.62 21.77 ?  20   ASN   A OD1  1 
ATOM   549  O  OD1  B ASN   A 1 20  ? 5.375  -1.474  8.146   0.38 18.40 ?  20   ASN   A OD1  1 
ATOM   550  N  ND2  A ASN   A 1 20  ? 7.244  -1.207  7.293   0.62 20.32 ?  20   ASN   A ND2  1 
ATOM   551  N  ND2  B ASN   A 1 20  ? 7.309  -1.574  6.980   0.38 18.26 ?  20   ASN   A ND2  1 
ATOM   552  H  H    A ASN   A 1 20  ? 7.882  -5.177  9.710   0.62 19.98 ?  20   ASN   A H    1 
ATOM   553  H  H    B ASN   A 1 20  ? 7.870  -5.189  9.850   0.38 18.61 ?  20   ASN   A H    1 
ATOM   554  H  HA   A ASN   A 1 20  ? 8.781  -3.414  7.910   0.62 21.17 ?  20   ASN   A HA   1 
ATOM   555  H  HA   B ASN   A 1 20  ? 8.743  -3.603  7.903   0.38 19.36 ?  20   ASN   A HA   1 
ATOM   556  H  HB2  A ASN   A 1 20  ? 6.521  -3.776  7.837   0.62 22.61 ?  20   ASN   A HB2  1 
ATOM   557  H  HB2  B ASN   A 1 20  ? 6.470  -4.106  7.943   0.38 20.25 ?  20   ASN   A HB2  1 
ATOM   558  H  HB3  A ASN   A 1 20  ? 6.378  -3.478  9.391   0.62 22.61 ?  20   ASN   A HB3  1 
ATOM   559  H  HB3  B ASN   A 1 20  ? 6.330  -3.446  9.373   0.38 20.25 ?  20   ASN   A HB3  1 
ATOM   560  H  HD21 A ASN   A 1 20  ? 7.103  -0.390  7.084   0.62 24.40 ?  20   ASN   A HD21 1 
ATOM   561  H  HD21 B ASN   A 1 20  ? 7.159  -0.821  6.592   0.38 21.93 ?  20   ASN   A HD21 1 
ATOM   562  H  HD22 A ASN   A 1 20  ? 7.843  -1.666  6.877   0.62 24.40 ?  20   ASN   A HD22 1 
ATOM   563  H  HD22 B ASN   A 1 20  ? 8.033  -2.008  6.798   0.38 21.93 ?  20   ASN   A HD22 1 
ATOM   564  N  N    A ALA   A 1 21  ? 10.079 -1.918  9.373   0.62 17.93 ?  21   ALA   A N    1 
ATOM   565  N  N    B ALA   A 1 21  ? 10.037 -1.964  9.214   0.38 16.14 ?  21   ALA   A N    1 
ATOM   566  C  CA   A ALA   A 1 21  ? 10.776 -1.029  10.288  0.62 17.81 ?  21   ALA   A CA   1 
ATOM   567  C  CA   B ALA   A 1 21  ? 10.704 -0.947  10.012  0.38 16.00 ?  21   ALA   A CA   1 
ATOM   568  C  C    A ALA   A 1 21  ? 11.718 -0.131  9.505   0.62 17.30 ?  21   ALA   A C    1 
ATOM   569  C  C    B ALA   A 1 21  ? 11.768 -0.259  9.172   0.38 14.96 ?  21   ALA   A C    1 
ATOM   570  O  O    A ALA   A 1 21  ? 12.152 -0.466  8.399   0.62 17.52 ?  21   ALA   A O    1 
ATOM   571  O  O    B ALA   A 1 21  ? 12.270 -0.815  8.192   0.38 14.70 ?  21   ALA   A O    1 
ATOM   572  C  CB   A ALA   A 1 21  ? 11.558 -1.820  11.339  0.62 18.68 ?  21   ALA   A CB   1 
ATOM   573  C  CB   B ALA   A 1 21  ? 11.331 -1.546  11.275  0.38 17.03 ?  21   ALA   A CB   1 
ATOM   574  H  H    A ALA   A 1 21  ? 10.444 -2.004  8.602   0.62 21.53 ?  21   ALA   A H    1 
ATOM   575  H  H    B ALA   A 1 21  ? 10.468 -2.209  8.510   0.38 19.39 ?  21   ALA   A H    1 
ATOM   576  H  HA   A ALA   A 1 21  ? 10.123 -0.468  10.746  0.62 21.39 ?  21   ALA   A HA   1 
ATOM   577  H  HA   B ALA   A 1 21  ? 10.054 -0.281  10.283  0.38 19.22 ?  21   ALA   A HA   1 
ATOM   578  H  HB1  A ALA   A 1 21  ? 11.949 -1.193  11.964  0.62 22.43 ?  21   ALA   A HB1  1 
ATOM   579  H  HB1  B ALA   A 1 21  ? 11.761 -0.840  11.781  0.38 20.45 ?  21   ALA   A HB1  1 
ATOM   580  H  HB2  A ALA   A 1 21  ? 10.943 -2.411  11.803  0.62 22.43 ?  21   ALA   A HB2  1 
ATOM   581  H  HB2  B ALA   A 1 21  ? 10.632 -1.957  11.812  0.38 20.45 ?  21   ALA   A HB2  1 
ATOM   582  H  HB3  A ALA   A 1 21  ? 12.244 -2.333  10.894  0.62 22.43 ?  21   ALA   A HB3  1 
ATOM   583  H  HB3  B ALA   A 1 21  ? 11.984 -2.216  11.019  0.38 20.45 ?  21   ALA   A HB3  1 
ATOM   584  N  N    A ASP   A 1 22  ? 12.017 1.020   10.104  0.62 16.63 ?  22   ASP   A N    1 
ATOM   585  N  N    B ASP   A 1 22  ? 12.081 0.973   9.569   0.38 14.46 ?  22   ASP   A N    1 
ATOM   586  C  CA   A ASP   A 1 22  ? 13.043 1.927   9.608   0.62 16.40 ?  22   ASP   A CA   1 
ATOM   587  C  CA   B ASP   A 1 22  ? 13.224 1.713   9.049   0.38 13.98 ?  22   ASP   A CA   1 
ATOM   588  C  C    A ASP   A 1 22  ? 14.387 1.465   10.155  0.62 15.04 ?  22   ASP   A C    1 
ATOM   589  C  C    B ASP   A 1 22  ? 14.493 1.150   9.685   0.38 12.91 ?  22   ASP   A C    1 
ATOM   590  O  O    A ASP   A 1 22  ? 14.604 1.479   11.371  0.62 15.44 ?  22   ASP   A O    1 
ATOM   591  O  O    B ASP   A 1 22  ? 14.607 1.115   10.915  0.38 12.97 ?  22   ASP   A O    1 
ATOM   592  C  CB   A ASP   A 1 22  ? 12.728 3.340   10.093  0.62 18.24 ?  22   ASP   A CB   1 
ATOM   593  C  CB   B ASP   A 1 22  ? 13.049 3.184   9.427   0.38 15.06 ?  22   ASP   A CB   1 
ATOM   594  C  CG   A ASP   A 1 22  ? 13.721 4.378   9.596   0.62 19.60 ?  22   ASP   A CG   1 
ATOM   595  C  CG   B ASP   A 1 22  ? 14.050 4.096   8.748   0.38 15.74 ?  22   ASP   A CG   1 
ATOM   596  O  OD1  A ASP   A 1 22  ? 14.826 4.018   9.148   0.62 19.70 ?  22   ASP   A OD1  1 
ATOM   597  O  OD1  B ASP   A 1 22  ? 15.187 3.656   8.485   0.38 14.77 ?  22   ASP   A OD1  1 
ATOM   598  O  OD2  A ASP   A 1 22  ? 13.390 5.580   9.669   0.62 21.07 -1 22   ASP   A OD2  1 
ATOM   599  O  OD2  B ASP   A 1 22  ? 13.696 5.262   8.475   0.38 17.45 -1 22   ASP   A OD2  1 
ATOM   600  H  H    A ASP   A 1 22  ? 11.622 1.304   10.814  0.62 19.98 ?  22   ASP   A H    1 
ATOM   601  H  H    B ASP   A 1 22  ? 11.618 1.419   10.146  0.38 17.37 ?  22   ASP   A H    1 
ATOM   602  H  HA   A ASP   A 1 22  ? 13.068 1.912   8.640   0.62 19.69 ?  22   ASP   A HA   1 
ATOM   603  H  HA   B ASP   A 1 22  ? 13.272 1.625   8.083   0.38 16.79 ?  22   ASP   A HA   1 
ATOM   604  H  HB2  A ASP   A 1 22  ? 11.849 3.594   9.773   0.62 21.90 ?  22   ASP   A HB2  1 
ATOM   605  H  HB2  B ASP   A 1 22  ? 12.167 3.475   9.164   0.38 18.09 ?  22   ASP   A HB2  1 
ATOM   606  H  HB3  A ASP   A 1 22  ? 12.741 3.349   11.064  0.62 21.90 ?  22   ASP   A HB3  1 
ATOM   607  H  HB3  B ASP   A 1 22  ? 13.159 3.273   10.387  0.38 18.09 ?  22   ASP   A HB3  1 
ATOM   608  N  N    A ILE   A 1 23  ? 15.286 1.047   9.261   0.62 14.13 ?  23   ILE   A N    1 
ATOM   609  N  N    B ILE   A 1 23  ? 15.443 0.702   8.855   0.38 12.35 ?  23   ILE   A N    1 
ATOM   610  C  CA   A ILE   A 1 23  ? 16.546 0.444   9.692   0.62 13.48 ?  23   ILE   A CA   1 
ATOM   611  C  CA   B ILE   A 1 23  ? 16.677 0.112   9.379   0.38 11.80 ?  23   ILE   A CA   1 
ATOM   612  C  C    A ILE   A 1 23  ? 17.351 1.407   10.553  0.62 13.43 ?  23   ILE   A C    1 
ATOM   613  C  C    B ILE   A 1 23  ? 17.393 1.083   10.306  0.38 12.33 ?  23   ILE   A C    1 
ATOM   614  O  O    A ILE   A 1 23  ? 18.088 0.982   11.451  0.62 13.97 ?  23   ILE   A O    1 
ATOM   615  O  O    B ILE   A 1 23  ? 18.056 0.667   11.264  0.38 12.42 ?  23   ILE   A O    1 
ATOM   616  C  CB   A ILE   A 1 23  ? 17.339 -0.075  8.473   0.62 13.50 ?  23   ILE   A CB   1 
ATOM   617  C  CB   B ILE   A 1 23  ? 17.598 -0.393  8.242   0.38 11.21 ?  23   ILE   A CB   1 
ATOM   618  C  CG1  A ILE   A 1 23  ? 18.506 -0.955  8.931   0.62 13.75 ?  23   ILE   A CG1  1 
ATOM   619  C  CG1  B ILE   A 1 23  ? 18.659 -1.346  8.811   0.38 11.44 ?  23   ILE   A CG1  1 
ATOM   620  C  CG2  A ILE   A 1 23  ? 17.809 1.082   7.594   0.62 13.56 ?  23   ILE   A CG2  1 
ATOM   621  C  CG2  B ILE   A 1 23  ? 18.251 0.773   7.492   0.38 10.87 ?  23   ILE   A CG2  1 
ATOM   622  C  CD1  A ILE   A 1 23  ? 19.181 -1.715  7.797   0.62 14.18 ?  23   ILE   A CD1  1 
ATOM   623  C  CD1  B ILE   A 1 23  ? 19.599 -1.939  7.766   0.38 11.01 ?  23   ILE   A CD1  1 
ATOM   624  H  H    A ILE   A 1 23  ? 15.187 1.103   8.413   0.62 16.98 ?  23   ILE   A H    1 
ATOM   625  H  H    B ILE   A 1 23  ? 15.399 0.724   8.005   0.38 14.84 ?  23   ILE   A H    1 
ATOM   626  H  HA   A ILE   A 1 23  ? 16.341 -0.324  10.243  0.62 16.19 ?  23   ILE   A HA   1 
ATOM   627  H  HA   B ILE   A 1 23  ? 16.435 -0.664  9.905   0.38 14.18 ?  23   ILE   A HA   1 
ATOM   628  H  HB   A ILE   A 1 23  ? 16.745 -0.625  7.944   0.62 16.21 ?  23   ILE   A HB   1 
ATOM   629  H  HB   B ILE   A 1 23  ? 17.059 -0.893  7.611   0.38 13.47 ?  23   ILE   A HB   1 
ATOM   630  H  HG12 A ILE   A 1 23  ? 19.177 -0.397  9.352   0.62 16.52 ?  23   ILE   A HG12 1 
ATOM   631  H  HG12 B ILE   A 1 23  ? 19.204 -0.864  9.452   0.38 13.74 ?  23   ILE   A HG12 1 
ATOM   632  H  HG13 A ILE   A 1 23  ? 18.175 -1.609  9.567   0.62 16.52 ?  23   ILE   A HG13 1 
ATOM   633  H  HG13 B ILE   A 1 23  ? 18.212 -2.086  9.252   0.38 13.74 ?  23   ILE   A HG13 1 
ATOM   634  H  HG21 A ILE   A 1 23  ? 18.175 0.725   6.769   0.62 16.29 ?  23   ILE   A HG21 1 
ATOM   635  H  HG21 B ILE   A 1 23  ? 18.651 0.437   6.671   0.38 13.06 ?  23   ILE   A HG21 1 
ATOM   636  H  HG22 A ILE   A 1 23  ? 17.048 1.653   7.393   0.62 16.29 ?  23   ILE   A HG22 1 
ATOM   637  H  HG22 B ILE   A 1 23  ? 17.574 1.431   7.282   0.38 13.06 ?  23   ILE   A HG22 1 
ATOM   638  H  HG23 A ILE   A 1 23  ? 18.485 1.589   8.066   0.62 16.29 ?  23   ILE   A HG23 1 
ATOM   639  H  HG23 B ILE   A 1 23  ? 18.938 1.168   8.052   0.38 13.06 ?  23   ILE   A HG23 1 
ATOM   640  H  HD11 A ILE   A 1 23  ? 19.870 -2.287  8.167   0.62 17.04 ?  23   ILE   A HD11 1 
ATOM   641  H  HD11 B ILE   A 1 23  ? 20.169 -2.600  8.193   0.38 13.23 ?  23   ILE   A HD11 1 
ATOM   642  H  HD12 A ILE   A 1 23  ? 18.515 -2.252  7.339   0.62 17.04 ?  23   ILE   A HD12 1 
ATOM   643  H  HD12 B ILE   A 1 23  ? 19.073 -2.359  7.069   0.38 13.23 ?  23   ILE   A HD12 1 
ATOM   644  H  HD13 A ILE   A 1 23  ? 19.573 -1.078  7.180   0.62 17.04 ?  23   ILE   A HD13 1 
ATOM   645  H  HD13 B ILE   A 1 23  ? 20.144 -1.230  7.390   0.38 13.23 ?  23   ILE   A HD13 1 
ATOM   646  N  N    A VAL   A 1 24  ? 17.220 2.713   10.310  0.62 13.69 ?  24   VAL   A N    1 
ATOM   647  N  N    B VAL   A 1 24  ? 17.267 2.385   10.047  0.38 13.28 ?  24   VAL   A N    1 
ATOM   648  C  CA   A VAL   A 1 24  ? 17.901 3.694   11.151  0.62 14.72 ?  24   VAL   A CA   1 
ATOM   649  C  CA   B VAL   A 1 24  ? 17.923 3.379   10.889  0.38 14.34 ?  24   VAL   A CA   1 
ATOM   650  C  C    A VAL   A 1 24  ? 17.386 3.612   12.579  0.62 15.50 ?  24   VAL   A C    1 
ATOM   651  C  C    B VAL   A 1 24  ? 17.326 3.372   12.290  0.38 15.19 ?  24   VAL   A C    1 
ATOM   652  O  O    A VAL   A 1 24  ? 18.162 3.540   13.540  0.62 15.84 ?  24   VAL   A O    1 
ATOM   653  O  O    B VAL   A 1 24  ? 18.054 3.413   13.288  0.38 15.61 ?  24   VAL   A O    1 
ATOM   654  C  CB   A VAL   A 1 24  ? 17.728 5.107   10.571  0.62 15.52 ?  24   VAL   A CB   1 
ATOM   655  C  CB   B VAL   A 1 24  ? 17.851 4.766   10.226  0.38 15.07 ?  24   VAL   A CB   1 
ATOM   656  C  CG1  A VAL   A 1 24  ? 18.230 6.156   11.561  0.62 16.13 ?  24   VAL   A CG1  1 
ATOM   657  C  CG1  B VAL   A 1 24  ? 18.557 5.798   11.080  0.38 16.22 ?  24   VAL   A CG1  1 
ATOM   658  C  CG2  A VAL   A 1 24  ? 18.448 5.217   9.241   0.62 16.23 ?  24   VAL   A CG2  1 
ATOM   659  C  CG2  B VAL   A 1 24  ? 18.459 4.711   8.832   0.38 15.24 ?  24   VAL   A CG2  1 
ATOM   660  H  H    A VAL   A 1 24  ? 16.747 3.050   9.675   0.62 16.44 ?  24   VAL   A H    1 
ATOM   661  H  H    B VAL   A 1 24  ? 16.808 2.713   9.404   0.38 15.95 ?  24   VAL   A H    1 
ATOM   662  H  HA   A VAL   A 1 24  ? 18.846 3.493   11.165  0.62 17.67 ?  24   VAL   A HA   1 
ATOM   663  H  HA   B VAL   A 1 24  ? 18.857 3.146   10.977  0.38 17.23 ?  24   VAL   A HA   1 
ATOM   664  H  HB   A VAL   A 1 24  ? 16.784 5.273   10.413  0.62 18.64 ?  24   VAL   A HB   1 
ATOM   665  H  HB   B VAL   A 1 24  ? 16.922 5.031   10.138  0.38 18.10 ?  24   VAL   A HB   1 
ATOM   666  H  HG11 A VAL   A 1 24  ? 18.376 6.989   11.087  0.62 19.37 ?  24   VAL   A HG11 1 
ATOM   667  H  HG11 B VAL   A 1 24  ? 18.652 6.617   10.570  0.38 19.48 ?  24   VAL   A HG11 1 
ATOM   668  H  HG12 A VAL   A 1 24  ? 17.567 6.281   12.255  0.62 19.37 ?  24   VAL   A HG12 1 
ATOM   669  H  HG12 B VAL   A 1 24  ? 18.026 5.964   11.874  0.38 19.48 ?  24   VAL   A HG12 1 
ATOM   670  H  HG13 A VAL   A 1 24  ? 19.065 5.846   11.947  0.62 19.37 ?  24   VAL   A HG13 1 
ATOM   671  H  HG13 B VAL   A 1 24  ? 19.430 5.459   11.328  0.38 19.48 ?  24   VAL   A HG13 1 
ATOM   672  H  HG21 A VAL   A 1 24  ? 18.236 6.071   8.835   0.62 19.49 ?  24   VAL   A HG21 1 
ATOM   673  H  HG21 B VAL   A 1 24  ? 18.526 5.611   8.480   0.38 18.30 ?  24   VAL   A HG21 1 
ATOM   674  H  HG22 A VAL   A 1 24  ? 19.404 5.153   9.393   0.62 19.49 ?  24   VAL   A HG22 1 
ATOM   675  H  HG22 B VAL   A 1 24  ? 19.342 4.312   8.890   0.38 18.30 ?  24   VAL   A HG22 1 
ATOM   676  H  HG23 A VAL   A 1 24  ? 18.157 4.495   8.660   0.62 19.49 ?  24   VAL   A HG23 1 
ATOM   677  H  HG23 B VAL   A 1 24  ? 17.892 4.172   8.259   0.38 18.30 ?  24   VAL   A HG23 1 
ATOM   678  N  N    A GLU   A 1 25  ? 16.062 3.640   12.739  0.62 16.37 ?  25   GLU   A N    1 
ATOM   679  N  N    B GLU   A 1 25  ? 15.995 3.301   12.393  0.38 15.78 ?  25   GLU   A N    1 
ATOM   680  C  CA   A GLU   A 1 25  ? 15.482 3.569   14.075  0.62 17.99 ?  25   GLU   A CA   1 
ATOM   681  C  CA   B GLU   A 1 25  ? 15.366 3.261   13.710  0.38 16.78 ?  25   GLU   A CA   1 
ATOM   682  C  C    A GLU   A 1 25  ? 15.726 2.206   14.708  0.62 16.70 ?  25   GLU   A C    1 
ATOM   683  C  C    B GLU   A 1 25  ? 15.642 1.939   14.416  0.38 16.80 ?  25   GLU   A C    1 
ATOM   684  O  O    A GLU   A 1 25  ? 15.957 2.114   15.920  0.62 17.09 ?  25   GLU   A O    1 
ATOM   685  O  O    B GLU   A 1 25  ? 15.853 1.913   15.634  0.38 17.39 ?  25   GLU   A O    1 
ATOM   686  C  CB   A GLU   A 1 25  ? 13.991 3.911   14.021  0.62 20.86 ?  25   GLU   A CB   1 
ATOM   687  C  CB   B GLU   A 1 25  ? 13.863 3.532   13.597  0.38 18.21 ?  25   GLU   A CB   1 
ATOM   688  C  CG   A GLU   A 1 25  ? 13.724 5.371   13.663  0.62 24.31 ?  25   GLU   A CG   1 
ATOM   689  C  CG   B GLU   A 1 25  ? 13.531 4.964   13.208  0.38 20.71 ?  25   GLU   A CG   1 
ATOM   690  C  CD   A GLU   A 1 25  ? 14.523 6.349   14.516  0.62 27.13 ?  25   GLU   A CD   1 
ATOM   691  C  CD   B GLU   A 1 25  ? 14.121 5.976   14.161  0.38 22.84 ?  25   GLU   A CD   1 
ATOM   692  O  OE1  A GLU   A 1 25  ? 14.553 6.185   15.755  0.62 28.20 ?  25   GLU   A OE1  1 
ATOM   693  O  OE1  B GLU   A 1 25  ? 14.137 5.701   15.380  0.38 23.99 ?  25   GLU   A OE1  1 
ATOM   694  O  OE2  A GLU   A 1 25  ? 15.143 7.268   13.941  0.62 28.33 -1 25   GLU   A OE2  1 
ATOM   695  O  OE2  B GLU   A 1 25  ? 14.571 7.041   13.691  0.38 23.46 -1 25   GLU   A OE2  1 
ATOM   696  H  H    A GLU   A 1 25  ? 15.487 3.707   12.101  0.62 19.66 ?  25   GLU   A H    1 
ATOM   697  H  H    B GLU   A 1 25  ? 15.446 3.273   11.731  0.38 18.95 ?  25   GLU   A H    1 
ATOM   698  H  HA   A GLU   A 1 25  ? 15.918 4.223   14.639  0.62 21.61 ?  25   GLU   A HA   1 
ATOM   699  H  HA   B GLU   A 1 25  ? 15.752 3.959   14.257  0.38 20.15 ?  25   GLU   A HA   1 
ATOM   700  H  HB2  A GLU   A 1 25  ? 13.558 3.359   13.347  0.62 25.05 ?  25   GLU   A HB2  1 
ATOM   701  H  HB2  B GLU   A 1 25  ? 13.486 2.951   12.920  0.38 21.86 ?  25   GLU   A HB2  1 
ATOM   702  H  HB3  A GLU   A 1 25  ? 13.589 3.742   14.888  0.62 25.05 ?  25   GLU   A HB3  1 
ATOM   703  H  HB3  B GLU   A 1 25  ? 13.444 3.354   14.455  0.38 21.86 ?  25   GLU   A HB3  1 
ATOM   704  H  HG2  A GLU   A 1 25  ? 13.984 5.518   12.743  0.62 29.19 ?  25   GLU   A HG2  1 
ATOM   705  H  HG2  B GLU   A 1 25  ? 13.878 5.144   12.321  0.38 24.87 ?  25   GLU   A HG2  1 
ATOM   706  H  HG3  A GLU   A 1 25  ? 12.776 5.553   13.778  0.62 29.19 ?  25   GLU   A HG3  1 
ATOM   707  H  HG3  B GLU   A 1 25  ? 12.573 5.091   13.227  0.38 24.87 ?  25   GLU   A HG3  1 
ATOM   708  N  N    A GLU   A 1 26  ? 15.693 1.139   13.907  0.62 16.17 ?  26   GLU   A N    1 
ATOM   709  N  N    B GLU   A 1 26  ? 15.651 0.831   13.671  0.38 16.84 ?  26   GLU   A N    1 
ATOM   710  C  CA   A GLU   A 1 26  ? 15.998 -0.190  14.433  0.62 16.24 ?  26   GLU   A CA   1 
ATOM   711  C  CA   B GLU   A 1 26  ? 16.022 -0.448  14.268  0.38 17.11 ?  26   GLU   A CA   1 
ATOM   712  C  C    A GLU   A 1 26  ? 17.419 -0.243  14.984  0.62 15.34 ?  26   GLU   A C    1 
ATOM   713  C  C    B GLU   A 1 26  ? 17.450 -0.422  14.789  0.38 16.17 ?  26   GLU   A C    1 
ATOM   714  O  O    A GLU   A 1 26  ? 17.646 -0.703  16.108  0.62 15.42 ?  26   GLU   A O    1 
ATOM   715  O  O    B GLU   A 1 26  ? 17.754 -1.054  15.807  0.38 16.34 ?  26   GLU   A O    1 
ATOM   716  C  CB   A GLU   A 1 26  ? 15.826 -1.248  13.340  0.62 18.21 ?  26   GLU   A CB   1 
ATOM   717  C  CB   B GLU   A 1 26  ? 15.865 -1.574  13.246  0.38 18.27 ?  26   GLU   A CB   1 
ATOM   718  C  CG   A GLU   A 1 26  ? 14.442 -1.852  13.213  0.62 20.86 ?  26   GLU   A CG   1 
ATOM   719  C  CG   B GLU   A 1 26  ? 14.435 -1.997  13.009  0.38 19.26 ?  26   GLU   A CG   1 
ATOM   720  C  CD   A GLU   A 1 26  ? 14.034 -2.678  14.429  0.62 22.04 ?  26   GLU   A CD   1 
ATOM   721  C  CD   B GLU   A 1 26  ? 13.771 -2.513  14.261  0.38 19.73 ?  26   GLU   A CD   1 
ATOM   722  O  OE1  A GLU   A 1 26  ? 14.408 -3.869  14.551  0.62 22.00 ?  26   GLU   A OE1  1 
ATOM   723  O  OE1  B GLU   A 1 26  ? 14.409 -3.303  14.989  0.38 20.03 ?  26   GLU   A OE1  1 
ATOM   724  O  OE2  A GLU   A 1 26  ? 13.326 -2.121  15.278  0.62 22.52 -1 26   GLU   A OE2  1 
ATOM   725  O  OE2  B GLU   A 1 26  ? 12.623 -2.106  14.524  0.38 19.11 -1 26   GLU   A OE2  1 
ATOM   726  H  H    A GLU   A 1 26  ? 15.502 1.163   13.068  0.62 19.42 ?  26   GLU   A H    1 
ATOM   727  H  H    B GLU   A 1 26  ? 15.451 0.794   12.837  0.38 20.23 ?  26   GLU   A H    1 
ATOM   728  H  HA   A GLU   A 1 26  ? 15.386 -0.392  15.152  0.62 19.51 ?  26   GLU   A HA   1 
ATOM   729  H  HA   B GLU   A 1 26  ? 15.433 -0.631  15.016  0.38 20.55 ?  26   GLU   A HA   1 
ATOM   730  H  HB2  A GLU   A 1 26  ? 16.048 -0.843  12.485  0.62 21.87 ?  26   GLU   A HB2  1 
ATOM   731  H  HB2  B GLU   A 1 26  ? 16.228 -1.275  12.395  0.38 21.94 ?  26   GLU   A HB2  1 
ATOM   732  H  HB3  A GLU   A 1 26  ? 16.444 -1.972  13.521  0.62 21.87 ?  26   GLU   A HB3  1 
ATOM   733  H  HB3  B GLU   A 1 26  ? 16.359 -2.350  13.555  0.38 21.94 ?  26   GLU   A HB3  1 
ATOM   734  H  HG2  A GLU   A 1 26  ? 13.805 -1.127  13.091  0.62 25.04 ?  26   GLU   A HG2  1 
ATOM   735  H  HG2  B GLU   A 1 26  ? 13.924 -1.234  12.703  0.38 23.12 ?  26   GLU   A HG2  1 
ATOM   736  H  HG3  A GLU   A 1 26  ? 14.424 -2.438  12.443  0.62 25.04 ?  26   GLU   A HG3  1 
ATOM   737  H  HG3  B GLU   A 1 26  ? 14.416 -2.704  12.348  0.38 23.12 ?  26   GLU   A HG3  1 
ATOM   738  N  N    A ALA   A 1 27  ? 18.394 0.217   14.195  0.62 14.45 ?  27   ALA   A N    1 
ATOM   739  N  N    B ALA   A 1 27  ? 18.341 0.292   14.102  0.38 15.01 ?  27   ALA   A N    1 
ATOM   740  C  CA   A ALA   A 1 27  ? 19.787 0.155   14.628  0.62 14.43 ?  27   ALA   A CA   1 
ATOM   741  C  CA   B ALA   A 1 27  ? 19.722 0.383   14.563  0.38 14.42 ?  27   ALA   A CA   1 
ATOM   742  C  C    A ALA   A 1 27  ? 20.005 0.954   15.909  0.62 15.94 ?  27   ALA   A C    1 
ATOM   743  C  C    B ALA   A 1 27  ? 19.822 1.230   15.827  0.38 14.85 ?  27   ALA   A C    1 
ATOM   744  O  O    A ALA   A 1 27  ? 20.695 0.495   16.826  0.62 16.61 ?  27   ALA   A O    1 
ATOM   745  O  O    B ALA   A 1 27  ? 20.470 0.835   16.803  0.38 14.32 ?  27   ALA   A O    1 
ATOM   746  C  CB   A ALA   A 1 27  ? 20.712 0.650   13.511  0.62 13.85 ?  27   ALA   A CB   1 
ATOM   747  C  CB   B ALA   A 1 27  ? 20.606 0.948   13.451  0.38 13.81 ?  27   ALA   A CB   1 
ATOM   748  H  H    A ALA   A 1 27  ? 18.277 0.565   13.419  0.62 17.36 ?  27   ALA   A H    1 
ATOM   749  H  H    B ALA   A 1 27  ? 18.170 0.718   13.375  0.38 18.03 ?  27   ALA   A H    1 
ATOM   750  H  HA   A ALA   A 1 27  ? 20.017 -0.768  14.812  0.62 17.33 ?  27   ALA   A HA   1 
ATOM   751  H  HA   B ALA   A 1 27  ? 20.039 -0.506  14.772  0.38 17.32 ?  27   ALA   A HA   1 
ATOM   752  H  HB1  A ALA   A 1 27  ? 21.634 0.598   13.814  0.62 16.63 ?  27   ALA   A HB1  1 
ATOM   753  H  HB1  B ALA   A 1 27  ? 21.521 0.986   13.767  0.38 16.58 ?  27   ALA   A HB1  1 
ATOM   754  H  HB2  A ALA   A 1 27  ? 20.594 0.083   12.729  0.62 16.63 ?  27   ALA   A HB2  1 
ATOM   755  H  HB2  B ALA   A 1 27  ? 20.547 0.367   12.675  0.38 16.58 ?  27   ALA   A HB2  1 
ATOM   756  H  HB3  A ALA   A 1 27  ? 20.487 1.566   13.291  0.62 16.63 ?  27   ALA   A HB3  1 
ATOM   757  H  HB3  B ALA   A 1 27  ? 20.296 1.838   13.220  0.38 16.58 ?  27   ALA   A HB3  1 
ATOM   758  N  N    A LYS   A 1 28  ? 19.411 2.146   16.000  0.62 18.42 ?  28   LYS   A N    1 
ATOM   759  N  N    B LYS   A 1 28  ? 19.172 2.397   15.836  0.38 16.36 ?  28   LYS   A N    1 
ATOM   760  C  CA   A LYS   A 1 28  ? 19.575 2.954   17.206  0.62 21.19 ?  28   LYS   A CA   1 
ATOM   761  C  CA   B LYS   A 1 28  ? 19.242 3.268   17.006  0.38 18.41 ?  28   LYS   A CA   1 
ATOM   762  C  C    A LYS   A 1 28  ? 19.026 2.238   18.434  0.62 22.31 ?  28   LYS   A C    1 
ATOM   763  C  C    B LYS   A 1 28  ? 18.709 2.584   18.256  0.38 19.64 ?  28   LYS   A C    1 
ATOM   764  O  O    A LYS   A 1 28  ? 19.592 2.349   19.528  0.62 23.50 ?  28   LYS   A O    1 
ATOM   765  O  O    B LYS   A 1 28  ? 19.182 2.865   19.364  0.38 20.23 ?  28   LYS   A O    1 
ATOM   766  C  CB   A LYS   A 1 28  ? 18.929 4.330   17.025  0.62 23.49 ?  28   LYS   A CB   1 
ATOM   767  C  CB   B LYS   A 1 28  ? 18.458 4.556   16.761  0.38 19.81 ?  28   LYS   A CB   1 
ATOM   768  C  CG   A LYS   A 1 28  ? 19.775 5.291   16.200  0.62 25.46 ?  28   LYS   A CG   1 
ATOM   769  C  CG   B LYS   A 1 28  ? 19.001 5.414   15.638  0.38 21.20 ?  28   LYS   A CG   1 
ATOM   770  C  CD   A LYS   A 1 28  ? 19.241 6.713   16.237  0.62 27.55 ?  28   LYS   A CD   1 
ATOM   771  C  CD   B LYS   A 1 28  ? 18.397 6.809   15.676  0.38 22.76 ?  28   LYS   A CD   1 
ATOM   772  C  CE   A LYS   A 1 28  ? 17.940 6.835   15.470  0.62 28.95 ?  28   LYS   A CE   1 
ATOM   773  C  CE   B LYS   A 1 28  ? 18.562 7.524   14.344  0.38 23.81 ?  28   LYS   A CE   1 
ATOM   774  N  NZ   A LYS   A 1 28  ? 17.498 8.253   15.374  0.62 29.77 ?  28   LYS   A NZ   1 
ATOM   775  N  NZ   B LYS   A 1 28  ? 18.339 8.993   14.459  0.38 24.40 ?  28   LYS   A NZ   1 
ATOM   776  H  H    A LYS   A 1 28  ? 18.925 2.501   15.392  0.62 22.12 ?  28   LYS   A H    1 
ATOM   777  H  H    B LYS   A 1 28  ? 18.695 2.704   15.190  0.38 19.64 ?  28   LYS   A H    1 
ATOM   778  H  HA   A LYS   A 1 28  ? 20.520 3.094   17.363  0.62 25.44 ?  28   LYS   A HA   1 
ATOM   779  H  HA   B LYS   A 1 28  ? 20.164 3.506   17.171  0.38 22.11 ?  28   LYS   A HA   1 
ATOM   780  H  HB2  A LYS   A 1 28  ? 18.079 4.224   16.573  0.62 28.20 ?  28   LYS   A HB2  1 
ATOM   781  H  HB2  B LYS   A 1 28  ? 17.542 4.326   16.540  0.38 23.78 ?  28   LYS   A HB2  1 
ATOM   782  H  HB3  A LYS   A 1 28  ? 18.792 4.733   17.897  0.62 28.20 ?  28   LYS   A HB3  1 
ATOM   783  H  HB3  B LYS   A 1 28  ? 18.474 5.089   17.572  0.38 23.78 ?  28   LYS   A HB3  1 
ATOM   784  H  HG2  A LYS   A 1 28  ? 20.679 5.302   16.552  0.62 30.57 ?  28   LYS   A HG2  1 
ATOM   785  H  HG2  B LYS   A 1 28  ? 19.962 5.494   15.732  0.38 25.46 ?  28   LYS   A HG2  1 
ATOM   786  H  HG3  A LYS   A 1 28  ? 19.780 4.997   15.276  0.62 30.57 ?  28   LYS   A HG3  1 
ATOM   787  H  HG3  B LYS   A 1 28  ? 18.778 5.012   14.786  0.38 25.46 ?  28   LYS   A HG3  1 
ATOM   788  H  HD2  A LYS   A 1 28  ? 19.076 6.972   17.158  0.62 33.08 ?  28   LYS   A HD2  1 
ATOM   789  H  HD2  B LYS   A 1 28  ? 17.449 6.743   15.874  0.38 27.33 ?  28   LYS   A HD2  1 
ATOM   790  H  HD3  A LYS   A 1 28  ? 19.890 7.312   15.832  0.62 33.08 ?  28   LYS   A HD3  1 
ATOM   791  H  HD3  B LYS   A 1 28  ? 18.846 7.333   16.360  0.38 27.33 ?  28   LYS   A HD3  1 
ATOM   792  H  HE2  A LYS   A 1 28  ? 18.066 6.493   14.571  0.62 34.75 ?  28   LYS   A HE2  1 
ATOM   793  H  HE2  B LYS   A 1 28  ? 19.461 7.376   14.012  0.38 28.59 ?  28   LYS   A HE2  1 
ATOM   794  H  HE3  A LYS   A 1 28  ? 17.250 6.331   15.928  0.62 34.75 ?  28   LYS   A HE3  1 
ATOM   795  H  HE3  B LYS   A 1 28  ? 17.911 7.170   13.717  0.38 28.59 ?  28   LYS   A HE3  1 
ATOM   796  H  HZ1  A LYS   A 1 28  ? 16.735 8.304   14.921  0.62 35.74 ?  28   LYS   A HZ1  1 
ATOM   797  H  HZ1  B LYS   A 1 28  ? 18.442 9.380   13.664  0.38 29.29 ?  28   LYS   A HZ1  1 
ATOM   798  H  HZ2  A LYS   A 1 28  ? 17.375 8.589   16.189  0.62 35.74 ?  28   LYS   A HZ2  1 
ATOM   799  H  HZ2  B LYS   A 1 28  ? 17.515 9.155   14.754  0.38 29.29 ?  28   LYS   A HZ2  1 
ATOM   800  H  HZ3  A LYS   A 1 28  ? 18.117 8.737   14.954  0.62 35.74 ?  28   LYS   A HZ3  1 
ATOM   801  H  HZ3  B LYS   A 1 28  ? 18.924 9.346   15.029  0.38 29.29 ?  28   LYS   A HZ3  1 
ATOM   802  N  N    A LYS   A 1 29  ? 17.934 1.487   18.275  0.62 22.90 ?  29   LYS   A N    1 
ATOM   803  N  N    B LYS   A 1 29  ? 17.723 1.701   18.106  0.38 20.64 ?  29   LYS   A N    1 
ATOM   804  C  CA   A LYS   A 1 29  ? 17.332 0.792   19.410  0.62 24.44 ?  29   LYS   A CA   1 
ATOM   805  C  CA   B LYS   A 1 29  ? 17.123 1.048   19.264  0.38 22.49 ?  29   LYS   A CA   1 
ATOM   806  C  C    A LYS   A 1 29  ? 18.141 -0.439  19.807  0.62 23.54 ?  29   LYS   A C    1 
ATOM   807  C  C    B LYS   A 1 29  ? 17.925 -0.173  19.690  0.38 21.70 ?  29   LYS   A C    1 
ATOM   808  O  O    A LYS   A 1 29  ? 18.418 -0.654  20.994  0.62 24.56 ?  29   LYS   A O    1 
ATOM   809  O  O    B LYS   A 1 29  ? 18.228 -0.344  20.877  0.38 22.24 ?  29   LYS   A O    1 
ATOM   810  C  CB   A LYS   A 1 29  ? 15.900 0.381   19.064  0.62 27.37 ?  29   LYS   A CB   1 
ATOM   811  C  CB   B LYS   A 1 29  ? 15.683 0.647   18.942  0.38 25.34 ?  29   LYS   A CB   1 
ATOM   812  C  CG   A LYS   A 1 29  ? 15.164 -0.323  20.195  0.62 30.71 ?  29   LYS   A CG   1 
ATOM   813  C  CG   B LYS   A 1 29  ? 14.971 -0.079  20.071  0.38 28.32 ?  29   LYS   A CG   1 
ATOM   814  C  CD   A LYS   A 1 29  ? 14.845 0.638   21.330  0.62 33.85 ?  29   LYS   A CD   1 
ATOM   815  C  CD   B LYS   A 1 29  ? 14.687 0.854   21.232  0.38 30.84 ?  29   LYS   A CD   1 
ATOM   816  C  CE   A LYS   A 1 29  ? 13.981 -0.022  22.392  0.62 35.88 ?  29   LYS   A CE   1 
ATOM   817  C  CE   B LYS   A 1 29  ? 13.878 0.161   22.314  0.38 32.56 ?  29   LYS   A CE   1 
ATOM   818  N  NZ   A LYS   A 1 29  ? 13.552 0.950   23.435  0.62 37.05 ?  29   LYS   A NZ   1 
ATOM   819  N  NZ   B LYS   A 1 29  ? 13.545 1.095   23.422  0.38 33.55 ?  29   LYS   A NZ   1 
ATOM   820  H  H    A LYS   A 1 29  ? 17.526 1.365   17.528  0.62 27.50 ?  29   LYS   A H    1 
ATOM   821  H  H    B LYS   A 1 29  ? 17.385 1.466   17.351  0.38 24.79 ?  29   LYS   A H    1 
ATOM   822  H  HA   A LYS   A 1 29  ? 17.299 1.392   20.171  0.62 29.34 ?  29   LYS   A HA   1 
ATOM   823  H  HA   B LYS   A 1 29  ? 17.106 1.667   20.007  0.38 27.00 ?  29   LYS   A HA   1 
ATOM   824  H  HB2  A LYS   A 1 29  ? 15.393 1.175   18.836  0.62 32.86 ?  29   LYS   A HB2  1 
ATOM   825  H  HB2  B LYS   A 1 29  ? 15.175 1.448   18.745  0.38 30.42 ?  29   LYS   A HB2  1 
ATOM   826  H  HB3  A LYS   A 1 29  ? 15.922 -0.224  18.308  0.62 32.86 ?  29   LYS   A HB3  1 
ATOM   827  H  HB3  B LYS   A 1 29  ? 15.685 0.060   18.171  0.38 30.42 ?  29   LYS   A HB3  1 
ATOM   828  H  HG2  A LYS   A 1 29  ? 14.328 -0.679  19.858  0.62 36.87 ?  29   LYS   A HG2  1 
ATOM   829  H  HG2  B LYS   A 1 29  ? 14.126 -0.419  19.743  0.38 34.00 ?  29   LYS   A HG2  1 
ATOM   830  H  HG3  A LYS   A 1 29  ? 15.712 -1.042  20.549  0.62 36.87 ?  29   LYS   A HG3  1 
ATOM   831  H  HG3  B LYS   A 1 29  ? 15.521 -0.812  20.393  0.38 34.00 ?  29   LYS   A HG3  1 
ATOM   832  H  HD2  A LYS   A 1 29  ? 15.672 0.927   21.748  0.62 40.63 ?  29   LYS   A HD2  1 
ATOM   833  H  HD2  B LYS   A 1 29  ? 15.526 1.148   21.621  0.38 37.02 ?  29   LYS   A HD2  1 
ATOM   834  H  HD3  A LYS   A 1 29  ? 14.363 1.402   20.976  0.62 40.63 ?  29   LYS   A HD3  1 
ATOM   835  H  HD3  B LYS   A 1 29  ? 14.180 1.616   20.912  0.38 37.02 ?  29   LYS   A HD3  1 
ATOM   836  H  HE2  A LYS   A 1 29  ? 13.186 -0.390  21.974  0.62 43.07 ?  29   LYS   A HE2  1 
ATOM   837  H  HE2  B LYS   A 1 29  ? 13.049 -0.170  21.932  0.38 39.09 ?  29   LYS   A HE2  1 
ATOM   838  H  HE3  A LYS   A 1 29  ? 14.488 -0.728  22.824  0.62 43.07 ?  29   LYS   A HE3  1 
ATOM   839  H  HE3  B LYS   A 1 29  ? 14.395 -0.575  22.679  0.38 39.09 ?  29   LYS   A HE3  1 
ATOM   840  H  HZ1  A LYS   A 1 29  ? 13.048 0.541   24.044  0.62 44.48 ?  29   LYS   A HZ1  1 
ATOM   841  H  HZ1  B LYS   A 1 29  ? 13.071 0.672   24.044  0.38 40.27 ?  29   LYS   A HZ1  1 
ATOM   842  H  HZ2  A LYS   A 1 29  ? 14.265 1.299   23.837  0.62 44.48 ?  29   LYS   A HZ2  1 
ATOM   843  H  HZ2  B LYS   A 1 29  ? 14.292 1.409   23.789  0.38 40.27 ?  29   LYS   A HZ2  1 
ATOM   844  H  HZ3  A LYS   A 1 29  ? 13.080 1.606   23.063  0.62 44.48 ?  29   LYS   A HZ3  1 
ATOM   845  H  HZ3  B LYS   A 1 29  ? 13.067 1.778   23.109  0.38 40.27 ?  29   LYS   A HZ3  1 
ATOM   846  N  N    A VAL   A 1 30  ? 18.503 -1.269  18.830  0.62 22.07 ?  30   VAL   A N    1 
ATOM   847  N  N    B VAL   A 1 30  ? 18.268 -1.037  18.735  0.38 20.75 ?  30   VAL   A N    1 
ATOM   848  C  CA   A VAL   A 1 30  ? 19.152 -2.543  19.122  0.62 21.00 ?  30   VAL   A CA   1 
ATOM   849  C  CA   B VAL   A 1 30  ? 18.915 -2.300  19.067  0.38 19.90 ?  30   VAL   A CA   1 
ATOM   850  C  C    A VAL   A 1 30  ? 20.654 -2.375  19.341  0.62 19.13 ?  30   VAL   A C    1 
ATOM   851  C  C    B VAL   A 1 30  ? 20.409 -2.117  19.308  0.38 19.22 ?  30   VAL   A C    1 
ATOM   852  O  O    A VAL   A 1 30  ? 21.253 -3.100  20.142  0.62 19.53 ?  30   VAL   A O    1 
ATOM   853  O  O    B VAL   A 1 30  ? 20.992 -2.800  20.157  0.38 19.18 ?  30   VAL   A O    1 
ATOM   854  C  CB   A VAL   A 1 30  ? 18.856 -3.541  17.987  0.62 21.99 ?  30   VAL   A CB   1 
ATOM   855  C  CB   B VAL   A 1 30  ? 18.643 -3.331  17.957  0.38 20.10 ?  30   VAL   A CB   1 
ATOM   856  C  CG1  A VAL   A 1 30  ? 19.638 -4.835  18.185  0.62 22.62 ?  30   VAL   A CG1  1 
ATOM   857  C  CG1  B VAL   A 1 30  ? 19.393 -4.626  18.233  0.38 20.49 ?  30   VAL   A CG1  1 
ATOM   858  C  CG2  A VAL   A 1 30  ? 17.362 -3.820  17.894  0.62 22.78 ?  30   VAL   A CG2  1 
ATOM   859  C  CG2  B VAL   A 1 30  ? 17.149 -3.592  17.828  0.38 20.47 ?  30   VAL   A CG2  1 
ATOM   860  H  H    A VAL   A 1 30  ? 18.373 -1.124  17.994  0.62 26.50 ?  30   VAL   A H    1 
ATOM   861  H  H    B VAL   A 1 30  ? 18.134 -0.918  17.894  0.38 24.92 ?  30   VAL   A H    1 
ATOM   862  H  HA   A VAL   A 1 30  ? 18.766 -2.907  19.935  0.62 25.21 ?  30   VAL   A HA   1 
ATOM   863  H  HA   B VAL   A 1 30  ? 18.521 -2.644  19.882  0.38 23.89 ?  30   VAL   A HA   1 
ATOM   864  H  HB   A VAL   A 1 30  ? 19.141 -3.152  17.144  0.62 26.40 ?  30   VAL   A HB   1 
ATOM   865  H  HB   B VAL   A 1 30  ? 18.962 -2.981  17.110  0.38 24.14 ?  30   VAL   A HB   1 
ATOM   866  H  HG11 A VAL   A 1 30  ? 19.271 -5.517  17.599  0.62 27.16 ?  30   VAL   A HG11 1 
ATOM   867  H  HG11 B VAL   A 1 30  ? 19.036 -5.324  17.662  0.38 24.61 ?  30   VAL   A HG11 1 
ATOM   868  H  HG12 A VAL   A 1 30  ? 20.571 -4.683  17.968  0.62 27.16 ?  30   VAL   A HG12 1 
ATOM   869  H  HG12 B VAL   A 1 30  ? 20.335 -4.495  18.043  0.38 24.61 ?  30   VAL   A HG12 1 
ATOM   870  H  HG13 A VAL   A 1 30  ? 19.552 -5.117  19.110  0.62 27.16 ?  30   VAL   A HG13 1 
ATOM   871  H  HG13 B VAL   A 1 30  ? 19.271 -4.867  19.164  0.38 24.61 ?  30   VAL   A HG13 1 
ATOM   872  H  HG21 A VAL   A 1 30  ? 17.207 -4.479  17.199  0.62 27.35 ?  30   VAL   A HG21 1 
ATOM   873  H  HG21 B VAL   A 1 30  ? 17.004 -4.280  17.159  0.38 24.58 ?  30   VAL   A HG21 1 
ATOM   874  H  HG22 A VAL   A 1 30  ? 17.053 -4.159  18.748  0.62 27.35 ?  30   VAL   A HG22 1 
ATOM   875  H  HG22 B VAL   A 1 30  ? 16.806 -3.888  18.686  0.38 24.58 ?  30   VAL   A HG22 1 
ATOM   876  H  HG23 A VAL   A 1 30  ? 16.902 -2.995  17.678  0.62 27.35 ?  30   VAL   A HG23 1 
ATOM   877  H  HG23 B VAL   A 1 30  ? 16.708 -2.772  17.560  0.38 24.58 ?  30   VAL   A HG23 1 
ATOM   878  N  N    A LYS   A 1 31  ? 21.284 -1.433  18.648  0.62 17.99 ?  31   LYS   A N    1 
ATOM   879  N  N    B LYS   A 1 31  ? 21.045 -1.199  18.589  0.38 19.26 ?  31   LYS   A N    1 
ATOM   880  C  CA   A LYS   A 1 31  ? 22.737 -1.319  18.606  0.62 18.31 ?  31   LYS   A CA   1 
ATOM   881  C  CA   B LYS   A 1 31  ? 22.498 -1.090  18.548  0.38 19.90 ?  31   LYS   A CA   1 
ATOM   882  C  C    A LYS   A 1 31  ? 23.359 -2.675  18.259  0.62 16.46 ?  31   LYS   A C    1 
ATOM   883  C  C    B LYS   A 1 31  ? 23.121 -2.461  18.279  0.38 18.36 ?  31   LYS   A C    1 
ATOM   884  O  O    A LYS   A 1 31  ? 24.142 -3.225  19.039  0.62 17.58 ?  31   LYS   A O    1 
ATOM   885  O  O    B LYS   A 1 31  ? 23.864 -2.988  19.114  0.38 18.95 ?  31   LYS   A O    1 
ATOM   886  C  CB   A LYS   A 1 31  ? 23.309 -0.774  19.907  0.62 22.90 ?  31   LYS   A CB   1 
ATOM   887  C  CB   B LYS   A 1 31  ? 23.062 -0.475  19.821  0.38 22.88 ?  31   LYS   A CB   1 
ATOM   888  C  CG   A LYS   A 1 31  ? 22.618 0.477   20.417  0.62 28.12 ?  31   LYS   A CG   1 
ATOM   889  C  CG   B LYS   A 1 31  ? 22.436 0.850   20.202  0.38 26.42 ?  31   LYS   A CG   1 
ATOM   890  C  CD   A LYS   A 1 31  ? 23.626 1.529   20.855  0.62 31.84 ?  31   LYS   A CD   1 
ATOM   891  C  CD   B LYS   A 1 31  ? 23.427 1.726   20.945  0.38 29.19 ?  31   LYS   A CD   1 
ATOM   892  C  CE   A LYS   A 1 31  ? 22.980 2.585   21.738  0.62 34.20 ?  31   LYS   A CE   1 
ATOM   893  C  CE   B LYS   A 1 31  ? 22.718 2.778   21.774  0.38 31.09 ?  31   LYS   A CE   1 
ATOM   894  N  NZ   A LYS   A 1 31  ? 21.798 3.223   21.098  0.62 35.50 ?  31   LYS   A NZ   1 
ATOM   895  N  NZ   B LYS   A 1 31  ? 21.644 3.466   21.009  0.38 32.22 ?  31   LYS   A NZ   1 
ATOM   896  H  H    A LYS   A 1 31  ? 20.878 -0.838  18.186  0.62 21.60 ?  31   LYS   A H    1 
ATOM   897  H  H    B LYS   A 1 31  ? 20.640 -0.615  18.109  0.38 23.13 ?  31   LYS   A H    1 
ATOM   898  H  HA   A LYS   A 1 31  ? 22.965 -0.698  17.902  0.62 21.98 ?  31   LYS   A HA   1 
ATOM   899  H  HA   B LYS   A 1 31  ? 22.737 -0.507  17.817  0.38 23.90 ?  31   LYS   A HA   1 
ATOM   900  H  HB2  A LYS   A 1 31  ? 23.235 -1.457  20.590  0.62 27.50 ?  31   LYS   A HB2  1 
ATOM   901  H  HB2  B LYS   A 1 31  ? 22.918 -1.090  20.552  0.38 27.47 ?  31   LYS   A HB2  1 
ATOM   902  H  HB3  A LYS   A 1 31  ? 24.245 -0.557  19.762  0.62 27.50 ?  31   LYS   A HB3  1 
ATOM   903  H  HB3  B LYS   A 1 31  ? 24.015 -0.328  19.697  0.38 27.47 ?  31   LYS   A HB3  1 
ATOM   904  H  HG2  A LYS   A 1 31  ? 22.073 0.854   19.709  0.62 33.76 ?  31   LYS   A HG2  1 
ATOM   905  H  HG2  B LYS   A 1 31  ? 22.155 1.318   19.400  0.38 31.72 ?  31   LYS   A HG2  1 
ATOM   906  H  HG3  A LYS   A 1 31  ? 22.066 0.248   21.181  0.62 33.76 ?  31   LYS   A HG3  1 
ATOM   907  H  HG3  B LYS   A 1 31  ? 21.675 0.690   20.782  0.38 31.72 ?  31   LYS   A HG3  1 
ATOM   908  H  HD2  A LYS   A 1 31  ? 24.336 1.103   21.360  0.62 38.22 ?  31   LYS   A HD2  1 
ATOM   909  H  HD2  B LYS   A 1 31  ? 23.959 1.173   21.540  0.38 35.05 ?  31   LYS   A HD2  1 
ATOM   910  H  HD3  A LYS   A 1 31  ? 23.991 1.969   20.070  0.62 38.22 ?  31   LYS   A HD3  1 
ATOM   911  H  HD3  B LYS   A 1 31  ? 24.000 2.175   20.304  0.38 35.05 ?  31   LYS   A HD3  1 
ATOM   912  H  HE2  A LYS   A 1 31  ? 22.687 2.170   22.564  0.62 41.06 ?  31   LYS   A HE2  1 
ATOM   913  H  HE2  B LYS   A 1 31  ? 22.316 2.351   22.545  0.38 37.32 ?  31   LYS   A HE2  1 
ATOM   914  H  HE3  A LYS   A 1 31  ? 23.630 3.280   21.928  0.62 41.06 ?  31   LYS   A HE3  1 
ATOM   915  H  HE3  B LYS   A 1 31  ? 23.361 3.444   22.059  0.38 37.32 ?  31   LYS   A HE3  1 
ATOM   916  H  HZ1  A LYS   A 1 31  ? 21.462 3.849   21.635  0.62 42.62 ?  31   LYS   A HZ1  1 
ATOM   917  H  HZ1  B LYS   A 1 31  ? 21.309 4.134   21.491  0.38 38.68 ?  31   LYS   A HZ1  1 
ATOM   918  H  HZ2  A LYS   A 1 31  ? 22.035 3.600   20.328  0.62 42.62 ?  31   LYS   A HZ2  1 
ATOM   919  H  HZ2  B LYS   A 1 31  ? 21.974 3.792   20.250  0.38 38.68 ?  31   LYS   A HZ2  1 
ATOM   920  H  HZ3  A LYS   A 1 31  ? 21.170 2.612   20.940  0.62 42.62 ?  31   LYS   A HZ3  1 
ATOM   921  H  HZ3  B LYS   A 1 31  ? 20.990 2.892   20.817  0.38 38.68 ?  31   LYS   A HZ3  1 
ATOM   922  N  N    A PRO   A 1 32  ? 23.028 -3.230  17.097  0.62 14.67 ?  32   PRO   A N    1 
ATOM   923  N  N    B PRO   A 1 32  ? 22.841 -3.058  17.125  0.38 16.49 ?  32   PRO   A N    1 
ATOM   924  C  CA   A PRO   A 1 32  ? 23.506 -4.570  16.751  0.62 15.29 ?  32   PRO   A CA   1 
ATOM   925  C  CA   B PRO   A 1 32  ? 23.324 -4.413  16.852  0.38 15.93 ?  32   PRO   A CA   1 
ATOM   926  C  C    A PRO   A 1 32  ? 25.008 -4.588  16.536  0.62 15.24 ?  32   PRO   A C    1 
ATOM   927  C  C    B PRO   A 1 32  ? 24.832 -4.429  16.666  0.38 15.39 ?  32   PRO   A C    1 
ATOM   928  O  O    A PRO   A 1 32  ? 25.643 -3.565  16.267  0.62 15.01 ?  32   PRO   A O    1 
ATOM   929  O  O    B PRO   A 1 32  ? 25.493 -3.394  16.567  0.38 15.74 ?  32   PRO   A O    1 
ATOM   930  C  CB   A PRO   A 1 32  ? 22.779 -4.865  15.436  0.62 15.76 ?  32   PRO   A CB   1 
ATOM   931  C  CB   B PRO   A 1 32  ? 22.605 -4.772  15.550  0.38 16.05 ?  32   PRO   A CB   1 
ATOM   932  C  CG   A PRO   A 1 32  ? 22.596 -3.506  14.820  0.62 14.67 ?  32   PRO   A CG   1 
ATOM   933  C  CG   B PRO   A 1 32  ? 22.459 -3.457  14.854  0.38 15.82 ?  32   PRO   A CG   1 
ATOM   934  C  CD   A PRO   A 1 32  ? 22.297 -2.604  15.984  0.62 14.23 ?  32   PRO   A CD   1 
ATOM   935  C  CD   B PRO   A 1 32  ? 22.168 -2.470  15.954  0.38 16.02 ?  32   PRO   A CD   1 
ATOM   936  H  HA   A PRO   A 1 32  ? 23.251 -5.219  17.427  0.62 18.36 ?  32   PRO   A HA   1 
ATOM   937  H  HA   B PRO   A 1 32  ? 23.065 -5.029  17.555  0.38 19.13 ?  32   PRO   A HA   1 
ATOM   938  H  HB2  A PRO   A 1 32  ? 23.331 -5.433  14.872  0.62 18.92 ?  32   PRO   A HB2  1 
ATOM   939  H  HB2  B PRO   A 1 32  ? 23.145 -5.383  15.026  0.38 19.27 ?  32   PRO   A HB2  1 
ATOM   940  H  HB3  A PRO   A 1 32  ? 21.923 -5.286  15.616  0.62 18.92 ?  32   PRO   A HB3  1 
ATOM   941  H  HB3  B PRO   A 1 32  ? 21.734 -5.157  15.744  0.38 19.27 ?  32   PRO   A HB3  1 
ATOM   942  H  HG2  A PRO   A 1 32  ? 23.412 -3.241  14.371  0.62 17.62 ?  32   PRO   A HG2  1 
ATOM   943  H  HG2  B PRO   A 1 32  ? 23.287 -3.234  14.401  0.38 19.00 ?  32   PRO   A HG2  1 
ATOM   944  H  HG3  A PRO   A 1 32  ? 21.851 -3.531  14.197  0.62 17.62 ?  32   PRO   A HG3  1 
ATOM   945  H  HG3  B PRO   A 1 32  ? 21.723 -3.498  14.223  0.38 19.00 ?  32   PRO   A HG3  1 
ATOM   946  H  HD2  A PRO   A 1 32  ? 22.640 -1.714  15.803  0.62 17.10 ?  32   PRO   A HD2  1 
ATOM   947  H  HD2  B PRO   A 1 32  ? 22.553 -1.606  15.736  0.38 19.24 ?  32   PRO   A HD2  1 
ATOM   948  H  HD3  A PRO   A 1 32  ? 21.346 -2.592  16.159  0.62 17.10 ?  32   PRO   A HD3  1 
ATOM   949  H  HD3  B PRO   A 1 32  ? 21.212 -2.407  16.103  0.38 19.24 ?  32   PRO   A HD3  1 
ATOM   950  N  N    A THR   A 1 33  ? 25.572 -5.793  16.625  0.62 15.14 ?  33   THR   A N    1 
ATOM   951  N  N    B THR   A 1 33  ? 25.376 -5.644  16.614  0.38 15.07 ?  33   THR   A N    1 
ATOM   952  C  CA   A THR   A 1 33  ? 26.979 -5.963  16.292  0.62 15.60 ?  33   THR   A CA   1 
ATOM   953  C  CA   B THR   A 1 33  ? 26.798 -5.801  16.331  0.38 14.82 ?  33   THR   A CA   1 
ATOM   954  C  C    A THR   A 1 33  ? 27.261 -5.511  14.863  0.62 14.23 ?  33   THR   A C    1 
ATOM   955  C  C    B THR   A 1 33  ? 27.127 -5.341  14.914  0.38 13.84 ?  33   THR   A C    1 
ATOM   956  O  O    A THR   A 1 33  ? 28.315 -4.917  14.592  0.62 13.81 ?  33   THR   A O    1 
ATOM   957  O  O    B THR   A 1 33  ? 28.094 -4.600  14.698  0.38 14.00 ?  33   THR   A O    1 
ATOM   958  C  CB   A THR   A 1 33  ? 27.394 -7.422  16.499  0.62 17.49 ?  33   THR   A CB   1 
ATOM   959  C  CB   B THR   A 1 33  ? 27.204 -7.259  16.541  0.38 15.84 ?  33   THR   A CB   1 
ATOM   960  O  OG1  A THR   A 1 33  ? 27.143 -7.809  17.855  0.62 19.29 ?  33   THR   A OG1  1 
ATOM   961  O  OG1  B THR   A 1 33  ? 26.849 -7.661  17.870  0.38 17.04 ?  33   THR   A OG1  1 
ATOM   962  C  CG2  A THR   A 1 33  ? 28.870 -7.613  16.206  0.62 18.06 ?  33   THR   A CG2  1 
ATOM   963  C  CG2  B THR   A 1 33  ? 28.705 -7.439  16.339  0.38 16.35 ?  33   THR   A CG2  1 
ATOM   964  H  H    A THR   A 1 33  ? 25.166 -6.514  16.862  0.62 18.18 ?  33   THR   A H    1 
ATOM   965  H  H    B THR   A 1 33  ? 24.949 -6.382  16.746  0.38 18.10 ?  33   THR   A H    1 
ATOM   966  H  HA   A THR   A 1 33  ? 27.513 -5.416  16.888  0.62 18.74 ?  33   THR   A HA   1 
ATOM   967  H  HA   B THR   A 1 33  ? 27.305 -5.260  16.954  0.38 17.80 ?  33   THR   A HA   1 
ATOM   968  H  HB   A THR   A 1 33  ? 26.881 -7.994  15.904  0.62 21.00 ?  33   THR   A HB   1 
ATOM   969  H  HB   B THR   A 1 33  ? 26.741 -7.825  15.902  0.38 19.02 ?  33   THR   A HB   1 
ATOM   970  H  HG1  A THR   A 1 33  ? 27.573 -7.315  18.383  0.62 23.16 ?  33   THR   A HG1  1 
ATOM   971  H  HG1  B THR   A 1 33  ? 27.262 -7.193  18.435  0.38 20.47 ?  33   THR   A HG1  1 
ATOM   972  H  HG21 A THR   A 1 33  ? 29.153 -8.493  16.503  0.62 21.69 ?  33   THR   A HG21 1 
ATOM   973  H  HG21 B THR   A 1 33  ? 28.975 -8.328  16.622  0.38 19.63 ?  33   THR   A HG21 1 
ATOM   974  H  HG22 A THR   A 1 33  ? 29.034 -7.534  15.256  0.62 21.69 ?  33   THR   A HG22 1 
ATOM   975  H  HG22 B THR   A 1 33  ? 28.931 -7.327  15.402  0.38 19.63 ?  33   THR   A HG22 1 
ATOM   976  H  HG23 A THR   A 1 33  ? 29.389 -6.942  16.677  0.62 21.69 ?  33   THR   A HG23 1 
ATOM   977  H  HG23 B THR   A 1 33  ? 29.191 -6.783  16.863  0.38 19.63 ?  33   THR   A HG23 1 
ATOM   978  N  N    . VAL   A 1 34  ? 26.333 -5.777  13.938  1.00 13.23 ?  34   VAL   A N    1 
ATOM   979  C  CA   . VAL   A 1 34  ? 26.527 -5.445  12.528  1.00 12.19 ?  34   VAL   A CA   1 
ATOM   980  C  C    . VAL   A 1 34  ? 25.227 -4.898  11.957  1.00 11.53 ?  34   VAL   A C    1 
ATOM   981  O  O    . VAL   A 1 34  ? 24.190 -5.572  12.008  1.00 12.41 ?  34   VAL   A O    1 
ATOM   982  C  CB   . VAL   A 1 34  ? 26.990 -6.656  11.694  1.00 12.87 ?  34   VAL   A CB   1 
ATOM   983  C  CG1  . VAL   A 1 34  ? 27.185 -6.260  10.238  1.00 13.15 ?  34   VAL   A CG1  1 
ATOM   984  C  CG2  . VAL   A 1 34  ? 28.269 -7.272  12.260  1.00 14.38 ?  34   VAL   A CG2  1 
ATOM   985  H  H    A VAL   A 1 34  ? 25.578 -6.156  14.108  0.62 15.89 ?  34   VAL   A H    1 
ATOM   986  H  H    B VAL   A 1 34  ? 25.652 -6.289  14.075  0.38 15.89 ?  34   VAL   A H    1 
ATOM   987  H  HA   . VAL   A 1 34  ? 27.201 -4.752  12.453  1.00 14.64 ?  34   VAL   A HA   1 
ATOM   988  H  HB   . VAL   A 1 34  ? 26.299 -7.334  11.726  1.00 15.46 ?  34   VAL   A HB   1 
ATOM   989  H  HG11 . VAL   A 1 34  ? 27.674 -6.965  9.784   1.00 15.79 ?  34   VAL   A HG11 1 
ATOM   990  H  HG12 . VAL   A 1 34  ? 26.321 -6.136  9.821   1.00 15.79 ?  34   VAL   A HG12 1 
ATOM   991  H  HG13 . VAL   A 1 34  ? 27.696 -5.433  10.201  1.00 15.79 ?  34   VAL   A HG13 1 
ATOM   992  H  HG21 . VAL   A 1 34  ? 28.554 -7.997  11.678  1.00 17.27 ?  34   VAL   A HG21 1 
ATOM   993  H  HG22 . VAL   A 1 34  ? 28.959 -6.592  12.301  1.00 17.27 ?  34   VAL   A HG22 1 
ATOM   994  H  HG23 . VAL   A 1 34  ? 28.090 -7.617  13.149  1.00 17.27 ?  34   VAL   A HG23 1 
ATOM   995  N  N    . VAL   A 1 35  ? 25.291 -3.695  11.385  1.00 11.09 ?  35   VAL   A N    1 
ATOM   996  C  CA   . VAL   A 1 35  ? 24.255 -3.191  10.492  1.00 10.72 ?  35   VAL   A CA   1 
ATOM   997  C  C    . VAL   A 1 35  ? 24.810 -3.197  9.075   1.00 10.27 ?  35   VAL   A C    1 
ATOM   998  O  O    . VAL   A 1 35  ? 25.955 -2.790  8.846   1.00 10.93 ?  35   VAL   A O    1 
ATOM   999  C  CB   . VAL   A 1 35  ? 23.726 -1.794  10.893  1.00 11.15 ?  35   VAL   A CB   1 
ATOM   1000 C  CG1  . VAL   A 1 35  ? 24.787 -0.696  10.738  1.00 11.90 ?  35   VAL   A CG1  1 
ATOM   1001 C  CG2  . VAL   A 1 35  ? 22.478 -1.449  10.085  1.00 12.16 ?  35   VAL   A CG2  1 
ATOM   1002 H  H    . VAL   A 1 35  ? 25.943 -3.143  11.495  1.00 13.33 ?  35   VAL   A H    1 
ATOM   1003 H  HA   . VAL   A 1 35  ? 23.503 -3.801  10.513  1.00 12.88 ?  35   VAL   A HA   1 
ATOM   1004 H  HB   . VAL   A 1 35  ? 23.463 -1.815  11.822  1.00 13.39 ?  35   VAL   A HB   1 
ATOM   1005 H  HG11 . VAL   A 1 35  ? 24.446 0.133   11.111  1.00 14.30 ?  35   VAL   A HG11 1 
ATOM   1006 H  HG12 . VAL   A 1 35  ? 25.590 -0.966  11.204  1.00 14.30 ?  35   VAL   A HG12 1 
ATOM   1007 H  HG13 . VAL   A 1 35  ? 24.982 -0.570  9.791   1.00 14.30 ?  35   VAL   A HG13 1 
ATOM   1008 H  HG21 . VAL   A 1 35  ? 22.127 -0.595  10.382  1.00 14.60 ?  35   VAL   A HG21 1 
ATOM   1009 H  HG22 . VAL   A 1 35  ? 22.710 -1.394  9.140   1.00 14.60 ?  35   VAL   A HG22 1 
ATOM   1010 H  HG23 . VAL   A 1 35  ? 21.810 -2.142  10.215  1.00 14.60 ?  35   VAL   A HG23 1 
ATOM   1011 N  N    . VAL   A 1 36  ? 23.998 -3.655  8.123   1.00 9.65  ?  36   VAL   A N    1 
ATOM   1012 C  CA   . VAL   A 1 36  ? 24.375 -3.662  6.716   1.00 9.58  ?  36   VAL   A CA   1 
ATOM   1013 C  C    . VAL   A 1 36  ? 23.913 -2.369  6.055   1.00 9.52  ?  36   VAL   A C    1 
ATOM   1014 O  O    . VAL   A 1 36  ? 22.749 -1.972  6.191   1.00 10.20 ?  36   VAL   A O    1 
ATOM   1015 C  CB   . VAL   A 1 36  ? 23.777 -4.883  6.001   1.00 9.66  ?  36   VAL   A CB   1 
ATOM   1016 C  CG1  . VAL   A 1 36  ? 24.032 -4.819  4.513   1.00 10.09 ?  36   VAL   A CG1  1 
ATOM   1017 C  CG2  . VAL   A 1 36  ? 24.324 -6.173  6.594   1.00 10.55 ?  36   VAL   A CG2  1 
ATOM   1018 H  H    . VAL   A 1 36  ? 23.208 -3.972  8.275   1.00 11.59 ?  36   VAL   A H    1 
ATOM   1019 H  HA   . VAL   A 1 36  ? 25.344 -3.718  6.651   1.00 11.51 ?  36   VAL   A HA   1 
ATOM   1020 H  HB   . VAL   A 1 36  ? 22.815 -4.881  6.137   1.00 11.60 ?  36   VAL   A HB   1 
ATOM   1021 H  HG11 . VAL   A 1 36  ? 23.879 -5.696  4.129   1.00 12.13 ?  36   VAL   A HG11 1 
ATOM   1022 H  HG12 . VAL   A 1 36  ? 23.431 -4.173  4.112   1.00 12.13 ?  36   VAL   A HG12 1 
ATOM   1023 H  HG13 . VAL   A 1 36  ? 24.955 -4.553  4.364   1.00 12.13 ?  36   VAL   A HG13 1 
ATOM   1024 H  HG21 . VAL   A 1 36  ? 23.942 -6.927  6.115   1.00 12.67 ?  36   VAL   A HG21 1 
ATOM   1025 H  HG22 . VAL   A 1 36  ? 25.289 -6.178  6.503   1.00 12.67 ?  36   VAL   A HG22 1 
ATOM   1026 H  HG23 . VAL   A 1 36  ? 24.079 -6.223  7.532   1.00 12.67 ?  36   VAL   A HG23 1 
ATOM   1027 N  N    . ASN   A 1 37  ? 24.823 -1.743  5.308   1.00 9.13  ?  37   ASN   A N    1 
ATOM   1028 C  CA   . ASN   A 1 37  ? 24.493 -0.626  4.439   1.00 9.12  ?  37   ASN   A CA   1 
ATOM   1029 C  C    . ASN   A 1 37  ? 24.366 -1.104  3.000   1.00 9.25  ?  37   ASN   A C    1 
ATOM   1030 O  O    . ASN   A 1 37  ? 25.153 -1.936  2.533   1.00 9.58  ?  37   ASN   A O    1 
ATOM   1031 C  CB   . ASN   A 1 37  ? 25.567 0.456   4.523   1.00 9.75  ?  37   ASN   A CB   1 
ATOM   1032 C  CG   . ASN   A 1 37  ? 25.242 1.650   3.666   1.00 9.75  ?  37   ASN   A CG   1 
ATOM   1033 O  OD1  . ASN   A 1 37  ? 24.065 1.979   3.471   1.00 10.44 ?  37   ASN   A OD1  1 
ATOM   1034 N  ND2  . ASN   A 1 37  ? 26.273 2.302   3.140   1.00 10.17 ?  37   ASN   A ND2  1 
ATOM   1035 H  H    . ASN   A 1 37  ? 25.661 -1.955  5.294   1.00 10.97 ?  37   ASN   A H    1 
ATOM   1036 H  HA   . ASN   A 1 37  ? 23.651 -0.243  4.717   1.00 10.96 ?  37   ASN   A HA   1 
ATOM   1037 H  HB2  . ASN   A 1 37  ? 25.644 0.760   5.443   1.00 11.72 ?  37   ASN   A HB2  1 
ATOM   1038 H  HB3  . ASN   A 1 37  ? 26.418 0.088   4.227   1.00 11.72 ?  37   ASN   A HB3  1 
ATOM   1039 H  HD21 . ASN   A 1 37  ? 26.135 2.987   2.636   1.00 12.22 ?  37   ASN   A HD21 1 
ATOM   1040 H  HD22 . ASN   A 1 37  ? 27.074 2.043   3.290   1.00 12.22 ?  37   ASN   A HD22 1 
ATOM   1041 N  N    A ALA   A 1 38  ? 23.349 -0.563  2.319   0.62 9.67  ?  38   ALA   A N    1 
ATOM   1042 N  N    B ALA   A 1 38  ? 23.356 -0.597  2.294   0.38 9.77  ?  38   ALA   A N    1 
ATOM   1043 C  CA   A ALA   A 1 38  ? 23.150 -0.684  0.876   0.62 9.88  ?  38   ALA   A CA   1 
ATOM   1044 C  CA   B ALA   A 1 38  ? 23.206 -0.888  0.867   0.38 10.29 ?  38   ALA   A CA   1 
ATOM   1045 C  C    A ALA   A 1 38  ? 24.081 0.306   0.178   0.62 9.48  ?  38   ALA   A C    1 
ATOM   1046 C  C    B ALA   A 1 38  ? 24.013 0.146   0.086   0.38 10.17 ?  38   ALA   A C    1 
ATOM   1047 O  O    A ALA   A 1 38  ? 23.691 1.410   -0.212  0.62 9.14  ?  38   ALA   A O    1 
ATOM   1048 O  O    B ALA   A 1 38  ? 23.493 1.137   -0.436  0.38 10.24 ?  38   ALA   A O    1 
ATOM   1049 C  CB   A ALA   A 1 38  ? 21.692 -0.398  0.529   0.62 10.38 ?  38   ALA   A CB   1 
ATOM   1050 C  CB   B ALA   A 1 38  ? 21.738 -0.900  0.468   0.38 10.46 ?  38   ALA   A CB   1 
ATOM   1051 H  H    A ALA   A 1 38  ? 22.741 -0.088  2.698   0.62 11.62 ?  38   ALA   A H    1 
ATOM   1052 H  H    B ALA   A 1 38  ? 22.748 -0.079  2.618   0.38 11.74 ?  38   ALA   A H    1 
ATOM   1053 H  HA   A ALA   A 1 38  ? 23.374 -1.577  0.585   0.62 11.87 ?  38   ALA   A HA   1 
ATOM   1054 H  HA   B ALA   A 1 38  ? 23.579 -1.766  0.684   0.38 12.37 ?  38   ALA   A HA   1 
ATOM   1055 H  HB1  A ALA   A 1 38  ? 21.573 -0.482  -0.429  0.62 12.47 ?  38   ALA   A HB1  1 
ATOM   1056 H  HB1  B ALA   A 1 38  ? 21.681 -0.995  -0.495  0.38 12.57 ?  38   ALA   A HB1  1 
ATOM   1057 H  HB2  A ALA   A 1 38  ? 21.128 -1.032  0.994   0.62 12.47 ?  38   ALA   A HB2  1 
ATOM   1058 H  HB2  B ALA   A 1 38  ? 21.297 -1.647  0.902   0.38 12.57 ?  38   ALA   A HB2  1 
ATOM   1059 H  HB3  A ALA   A 1 38  ? 21.473 0.508   0.810   0.62 12.47 ?  38   ALA   A HB3  1 
ATOM   1060 H  HB3  B ALA   A 1 38  ? 21.332 -0.066  0.740   0.38 12.57 ?  38   ALA   A HB3  1 
ATOM   1061 N  N    A ALA   A 1 39  ? 25.341 -0.102  0.029   0.62 9.66  ?  39   ALA   A N    1 
ATOM   1062 N  N    B ALA   A 1 39  ? 25.320 -0.096  0.015   0.38 10.64 ?  39   ALA   A N    1 
ATOM   1063 C  CA   A ALA   A 1 39  ? 26.413 0.761   -0.441  0.62 9.48  ?  39   ALA   A CA   1 
ATOM   1064 C  CA   B ALA   A 1 39  ? 26.260 0.874   -0.521  0.38 10.60 ?  39   ALA   A CA   1 
ATOM   1065 C  C    A ALA   A 1 39  ? 26.552 0.719   -1.961  0.62 9.57  ?  39   ALA   A C    1 
ATOM   1066 C  C    B ALA   A 1 39  ? 26.404 0.737   -2.035  0.38 10.29 ?  39   ALA   A C    1 
ATOM   1067 O  O    A ALA   A 1 39  ? 26.074 -0.198  -2.636  0.62 9.93  ?  39   ALA   A O    1 
ATOM   1068 O  O    B ALA   A 1 39  ? 25.989 -0.255  -2.642  0.38 10.74 ?  39   ALA   A O    1 
ATOM   1069 C  CB   A ALA   A 1 39  ? 27.738 0.337   0.202   0.62 9.73  ?  39   ALA   A CB   1 
ATOM   1070 C  CB   B ALA   A 1 39  ? 27.625 0.700   0.150   0.38 11.03 ?  39   ALA   A CB   1 
ATOM   1071 H  H    A ALA   A 1 39  ? 25.602 -0.907  0.199   0.62 11.60 ?  39   ALA   A H    1 
ATOM   1072 H  H    B ALA   A 1 39  ? 25.691 -0.834  0.279   0.38 12.79 ?  39   ALA   A H    1 
ATOM   1073 H  HA   A ALA   A 1 39  ? 26.226 1.675   -0.178  0.62 11.39 ?  39   ALA   A HA   1 
ATOM   1074 H  HA   B ALA   A 1 39  ? 25.939 1.763   -0.320  0.38 12.73 ?  39   ALA   A HA   1 
ATOM   1075 H  HB1  A ALA   A 1 39  ? 28.443 0.921   -0.117  0.62 11.69 ?  39   ALA   A HB1  1 
ATOM   1076 H  HB1  B ALA   A 1 39  ? 28.238 1.356   -0.214  0.38 13.25 ?  39   ALA   A HB1  1 
ATOM   1077 H  HB2  A ALA   A 1 39  ? 27.657 0.416   1.168   0.62 11.69 ?  39   ALA   A HB2  1 
ATOM   1078 H  HB2  B ALA   A 1 39  ? 27.527 0.838   1.108   0.38 13.25 ?  39   ALA   A HB2  1 
ATOM   1079 H  HB3  A ALA   A 1 39  ? 27.928 -0.580  -0.041  0.62 11.69 ?  39   ALA   A HB3  1 
ATOM   1080 H  HB3  B ALA   A 1 39  ? 27.954 -0.195  -0.021  0.38 13.25 ?  39   ALA   A HB3  1 
ATOM   1081 N  N    A ASN   A 1 40  ? 27.234 1.733   -2.497  0.62 9.74  ?  40   ASN   A N    1 
ATOM   1082 N  N    B ASN   A 1 40  ? 26.989 1.767   -2.643  0.38 9.78  ?  40   ASN   A N    1 
ATOM   1083 C  CA   A ASN   A 1 40  ? 27.778 1.695   -3.850  0.62 9.81  ?  40   ASN   A CA   1 
ATOM   1084 C  CA   B ASN   A 1 40  ? 27.489 1.699   -4.008  0.38 9.59  ?  40   ASN   A CA   1 
ATOM   1085 C  C    A ASN   A 1 40  ? 29.301 1.591   -3.777  0.62 9.17  ?  40   ASN   A C    1 
ATOM   1086 C  C    B ASN   A 1 40  ? 29.014 1.584   -3.986  0.38 9.43  ?  40   ASN   A C    1 
ATOM   1087 O  O    A ASN   A 1 40  ? 29.900 1.702   -2.703  0.62 9.19  ?  40   ASN   A O    1 
ATOM   1088 O  O    B ASN   A 1 40  ? 29.651 1.693   -2.937  0.38 9.55  ?  40   ASN   A O    1 
ATOM   1089 C  CB   A ASN   A 1 40  ? 27.299 2.880   -4.708  0.62 10.57 ?  40   ASN   A CB   1 
ATOM   1090 C  CB   B ASN   A 1 40  ? 27.022 2.904   -4.837  0.38 9.98  ?  40   ASN   A CB   1 
ATOM   1091 C  CG   A ASN   A 1 40  ? 27.676 4.229   -4.133  0.62 11.70 ?  40   ASN   A CG   1 
ATOM   1092 C  CG   B ASN   A 1 40  ? 27.396 4.232   -4.214  0.38 10.05 ?  40   ASN   A CG   1 
ATOM   1093 O  OD1  A ASN   A 1 40  ? 28.839 4.478   -3.801  0.62 12.25 ?  40   ASN   A OD1  1 
ATOM   1094 O  OD1  B ASN   A 1 40  ? 28.574 4.559   -4.077  0.38 10.42 ?  40   ASN   A OD1  1 
ATOM   1095 N  ND2  A ASN   A 1 40  ? 26.686 5.114   -4.021  0.62 12.96 ?  40   ASN   A ND2  1 
ATOM   1096 N  ND2  B ASN   A 1 40  ? 26.388 5.015   -3.852  0.38 10.57 ?  40   ASN   A ND2  1 
ATOM   1097 H  H    A ASN   A 1 40  ? 27.406 2.468   -2.086  0.62 11.70 ?  40   ASN   A H    1 
ATOM   1098 H  H    B ASN   A 1 40  ? 27.109 2.530   -2.270  0.38 11.75 ?  40   ASN   A H    1 
ATOM   1099 H  HA   A ASN   A 1 40  ? 27.459 0.887   -4.282  0.62 11.78 ?  40   ASN   A HA   1 
ATOM   1100 H  HA   B ASN   A 1 40  ? 27.136 0.894   -4.428  0.38 11.53 ?  40   ASN   A HA   1 
ATOM   1101 H  HB2  A ASN   A 1 40  ? 27.692 2.804   -5.597  0.62 12.70 ?  40   ASN   A HB2  1 
ATOM   1102 H  HB2  B ASN   A 1 40  ? 27.428 2.853   -5.712  0.38 11.99 ?  40   ASN   A HB2  1 
ATOM   1103 H  HB3  A ASN   A 1 40  ? 26.330 2.842   -4.781  0.62 12.70 ?  40   ASN   A HB3  1 
ATOM   1104 H  HB3  B ASN   A 1 40  ? 26.054 2.863   -4.917  0.38 11.99 ?  40   ASN   A HB3  1 
ATOM   1105 H  HD21 A ASN   A 1 40  ? 26.841 5.901   -3.709  0.62 15.57 ?  40   ASN   A HD21 1 
ATOM   1106 H  HD21 B ASN   A 1 40  ? 26.549 5.779   -3.492  0.38 12.70 ?  40   ASN   A HD21 1 
ATOM   1107 H  HD22 A ASN   A 1 40  ? 25.885 4.898   -4.256  0.62 15.57 ?  40   ASN   A HD22 1 
ATOM   1108 H  HD22 B ASN   A 1 40  ? 25.576 4.759   -3.974  0.38 12.70 ?  40   ASN   A HD22 1 
ATOM   1109 N  N    A VAL   A 1 41  ? 29.928 1.343   -4.931  0.62 9.33  ?  41   VAL   A N    1 
ATOM   1110 N  N    B VAL   A 1 41  ? 29.601 1.354   -5.163  0.38 9.95  ?  41   VAL   A N    1 
ATOM   1111 C  CA   A VAL   A 1 41  ? 31.354 1.025   -4.941  0.62 9.79  ?  41   VAL   A CA   1 
ATOM   1112 C  CA   B VAL   A 1 41  ? 31.029 1.048   -5.232  0.38 9.97  ?  41   VAL   A CA   1 
ATOM   1113 C  C    A VAL   A 1 41  ? 32.209 2.179   -4.452  0.62 9.59  ?  41   VAL   A C    1 
ATOM   1114 C  C    B VAL   A 1 41  ? 31.896 2.203   -4.754  0.38 9.53  ?  41   VAL   A C    1 
ATOM   1115 O  O    A VAL   A 1 41  ? 33.339 1.961   -4.000  0.62 10.11 ?  41   VAL   A O    1 
ATOM   1116 O  O    B VAL   A 1 41  ? 33.061 1.992   -4.392  0.38 9.65  ?  41   VAL   A O    1 
ATOM   1117 C  CB   A VAL   A 1 41  ? 31.857 0.522   -6.317  0.62 10.09 ?  41   VAL   A CB   1 
ATOM   1118 C  CB   B VAL   A 1 41  ? 31.450 0.611   -6.652  0.38 10.70 ?  41   VAL   A CB   1 
ATOM   1119 C  CG1  A VAL   A 1 41  ? 31.159 -0.776  -6.715  0.62 11.12 ?  41   VAL   A CG1  1 
ATOM   1120 C  CG1  B VAL   A 1 41  ? 30.750 -0.678  -7.043  0.38 11.56 ?  41   VAL   A CG1  1 
ATOM   1121 C  CG2  A VAL   A 1 41  ? 31.735 1.587   -7.412  0.62 10.17 ?  41   VAL   A CG2  1 
ATOM   1122 C  CG2  B VAL   A 1 41  ? 31.175 1.713   -7.668  0.38 10.69 ?  41   VAL   A CG2  1 
ATOM   1123 H  H    A VAL   A 1 41  ? 29.557 1.338   -5.706  0.62 11.21 ?  41   VAL   A H    1 
ATOM   1124 H  H    B VAL   A 1 41  ? 29.196 1.363   -5.921  0.38 11.96 ?  41   VAL   A H    1 
ATOM   1125 H  HA   A VAL   A 1 41  ? 31.501 0.299   -4.317  0.62 11.76 ?  41   VAL   A HA   1 
ATOM   1126 H  HA   B VAL   A 1 41  ? 31.199 0.292   -4.644  0.38 11.98 ?  41   VAL   A HA   1 
ATOM   1127 H  HB   A VAL   A 1 41  ? 32.800 0.313   -6.232  0.62 12.12 ?  41   VAL   A HB   1 
ATOM   1128 H  HB   B VAL   A 1 41  ? 32.404 0.438   -6.652  0.38 12.85 ?  41   VAL   A HB   1 
ATOM   1129 H  HG11 A VAL   A 1 41  ? 31.502 -1.077  -7.572  0.62 13.36 ?  41   VAL   A HG11 1 
ATOM   1130 H  HG11 B VAL   A 1 41  ? 30.964 -0.884  -7.966  0.38 13.89 ?  41   VAL   A HG11 1 
ATOM   1131 H  HG12 A VAL   A 1 41  ? 31.327 -1.452  -6.037  0.62 13.36 ?  41   VAL   A HG12 1 
ATOM   1132 H  HG12 B VAL   A 1 41  ? 31.061 -1.394  -6.464  0.38 13.89 ?  41   VAL   A HG12 1 
ATOM   1133 H  HG13 A VAL   A 1 41  ? 30.202 -0.615  -6.785  0.62 13.36 ?  41   VAL   A HG13 1 
ATOM   1134 H  HG13 B VAL   A 1 41  ? 29.794 -0.566  -6.942  0.38 13.89 ?  41   VAL   A HG13 1 
ATOM   1135 H  HG21 A VAL   A 1 41  ? 31.989 1.188   -8.264  0.62 12.22 ?  41   VAL   A HG21 1 
ATOM   1136 H  HG21 B VAL   A 1 41  ? 31.435 1.398   -8.549  0.38 12.85 ?  41   VAL   A HG21 1 
ATOM   1137 H  HG22 A VAL   A 1 41  ? 30.823 1.896   -7.450  0.62 12.22 ?  41   VAL   A HG22 1 
ATOM   1138 H  HG22 B VAL   A 1 41  ? 30.227 1.923   -7.661  0.38 12.85 ?  41   VAL   A HG22 1 
ATOM   1139 H  HG23 A VAL   A 1 41  ? 32.334 2.319   -7.203  0.62 12.22 ?  41   VAL   A HG23 1 
ATOM   1140 H  HG23 B VAL   A 1 41  ? 31.690 2.498   -7.433  0.38 12.85 ?  41   VAL   A HG23 1 
ATOM   1141 N  N    A TYR   A 1 42  ? 31.713 3.411   -4.557  0.62 9.88  ?  42   TYR   A N    1 
ATOM   1142 N  N    B TYR   A 1 42  ? 31.372 3.428   -4.773  0.38 9.63  ?  42   TYR   A N    1 
ATOM   1143 C  CA   A TYR   A 1 42  ? 32.449 4.599   -4.138  0.62 10.06 ?  42   TYR   A CA   1 
ATOM   1144 C  CA   B TYR   A 1 42  ? 32.125 4.609   -4.362  0.38 9.67  ?  42   TYR   A CA   1 
ATOM   1145 C  C    A TYR   A 1 42  ? 32.168 4.977   -2.694  0.62 9.63  ?  42   TYR   A C    1 
ATOM   1146 C  C    B TYR   A 1 42  ? 31.895 4.990   -2.907  0.38 9.95  ?  42   TYR   A C    1 
ATOM   1147 O  O    A TYR   A 1 42  ? 32.734 5.959   -2.199  0.62 10.34 ?  42   TYR   A O    1 
ATOM   1148 O  O    B TYR   A 1 42  ? 32.460 5.989   -2.448  0.38 10.08 ?  42   TYR   A O    1 
ATOM   1149 C  CB   A TYR   A 1 42  ? 32.122 5.785   -5.064  0.62 10.79 ?  42   TYR   A CB   1 
ATOM   1150 C  CB   B TYR   A 1 42  ? 31.766 5.803   -5.252  0.38 10.06 ?  42   TYR   A CB   1 
ATOM   1151 C  CG   A TYR   A 1 42  ? 32.305 5.462   -6.536  0.62 11.19 ?  42   TYR   A CG   1 
ATOM   1152 C  CG   B TYR   A 1 42  ? 31.917 5.516   -6.722  0.38 10.64 ?  42   TYR   A CG   1 
ATOM   1153 C  CD1  A TYR   A 1 42  ? 33.571 5.269   -7.067  0.62 11.47 ?  42   TYR   A CD1  1 
ATOM   1154 C  CD1  B TYR   A 1 42  ? 33.171 5.338   -7.286  0.38 10.63 ?  42   TYR   A CD1  1 
ATOM   1155 C  CD2  A TYR   A 1 42  ? 31.215 5.318   -7.387  0.62 12.13 ?  42   TYR   A CD2  1 
ATOM   1156 C  CD2  B TYR   A 1 42  ? 30.805 5.409   -7.545  0.38 12.22 ?  42   TYR   A CD2  1 
ATOM   1157 C  CE1  A TYR   A 1 42  ? 33.749 4.954   -8.406  0.62 11.93 ?  42   TYR   A CE1  1 
ATOM   1158 C  CE1  B TYR   A 1 42  ? 33.315 5.066   -8.633  0.38 11.13 ?  42   TYR   A CE1  1 
ATOM   1159 C  CE2  A TYR   A 1 42  ? 31.387 5.007   -8.732  0.62 13.15 ?  42   TYR   A CE2  1 
ATOM   1160 C  CE2  B TYR   A 1 42  ? 30.936 5.145   -8.892  0.38 12.65 ?  42   TYR   A CE2  1 
ATOM   1161 C  CZ   A TYR   A 1 42  ? 32.658 4.830   -9.234  0.62 12.58 ?  42   TYR   A CZ   1 
ATOM   1162 C  CZ   B TYR   A 1 42  ? 32.192 4.970   -9.433  0.38 11.94 ?  42   TYR   A CZ   1 
ATOM   1163 O  OH   A TYR   A 1 42  ? 32.847 4.516   -10.561 0.62 13.75 ?  42   TYR   A OH   1 
ATOM   1164 O  OH   B TYR   A 1 42  ? 32.318 4.709   -10.777 0.38 12.48 ?  42   TYR   A OH   1 
ATOM   1165 H  H    A TYR   A 1 42  ? 30.938 3.587   -4.880  0.62 11.88 ?  42   TYR   A H    1 
ATOM   1166 H  H    B TYR   A 1 42  ? 30.571 3.601   -5.041  0.38 11.57 ?  42   TYR   A H    1 
ATOM   1167 H  HA   A TYR   A 1 42  ? 33.400 4.427   -4.210  0.62 12.09 ?  42   TYR   A HA   1 
ATOM   1168 H  HA   B TYR   A 1 42  ? 33.069 4.430   -4.481  0.38 11.62 ?  42   TYR   A HA   1 
ATOM   1169 H  HB2  A TYR   A 1 42  ? 31.200 6.050   -4.929  0.62 12.96 ?  42   TYR   A HB2  1 
ATOM   1170 H  HB2  B TYR   A 1 42  ? 30.844 6.052   -5.091  0.38 12.08 ?  42   TYR   A HB2  1 
ATOM   1171 H  HB3  A TYR   A 1 42  ? 32.712 6.529   -4.847  0.62 12.96 ?  42   TYR   A HB3  1 
ATOM   1172 H  HB3  B TYR   A 1 42  ? 32.352 6.545   -5.033  0.38 12.08 ?  42   TYR   A HB3  1 
ATOM   1173 H  HD1  A TYR   A 1 42  ? 34.318 5.356   -6.518  0.62 13.78 ?  42   TYR   A HD1  1 
ATOM   1174 H  HD1  B TYR   A 1 42  ? 33.930 5.402   -6.746  0.38 12.77 ?  42   TYR   A HD1  1 
ATOM   1175 H  HD2  A TYR   A 1 42  ? 30.354 5.443   -7.054  0.62 14.57 ?  42   TYR   A HD2  1 
ATOM   1176 H  HD2  B TYR   A 1 42  ? 29.956 5.528   -7.182  0.38 14.68 ?  42   TYR   A HD2  1 
ATOM   1177 H  HE1  A TYR   A 1 42  ? 34.608 4.835   -8.750  0.62 14.33 ?  42   TYR   A HE1  1 
ATOM   1178 H  HE1  B TYR   A 1 42  ? 34.165 4.952   -8.996  0.38 13.37 ?  42   TYR   A HE1  1 
ATOM   1179 H  HE2  A TYR   A 1 42  ? 30.645 4.921   -9.292  0.62 15.80 ?  42   TYR   A HE2  1 
ATOM   1180 H  HE2  B TYR   A 1 42  ? 30.182 5.080   -9.429  0.38 15.20 ?  42   TYR   A HE2  1 
ATOM   1181 H  HH   A TYR   A 1 42  ? 33.663 4.378   -10.711 0.62 16.51 ?  42   TYR   A HH   1 
ATOM   1182 H  HH   B TYR   A 1 42  ? 31.559 4.680   -11.131 0.38 14.99 ?  42   TYR   A HH   1 
ATOM   1183 N  N    A LEU   A 1 43  ? 31.305 4.220   -2.017  0.62 9.54  ?  43   LEU   A N    1 
ATOM   1184 N  N    B LEU   A 1 43  ? 31.080 4.228   -2.182  0.38 10.25 ?  43   LEU   A N    1 
ATOM   1185 C  CA   A LEU   A 1 43  ? 30.843 4.554   -0.671  0.62 9.19  ?  43   LEU   A CA   1 
ATOM   1186 C  CA   B LEU   A 1 43  ? 30.664 4.572   -0.820  0.38 10.31 ?  43   LEU   A CA   1 
ATOM   1187 C  C    A LEU   A 1 43  ? 30.370 6.004   -0.584  0.62 9.26  ?  43   LEU   A C    1 
ATOM   1188 C  C    B LEU   A 1 43  ? 30.163 6.013   -0.719  0.38 10.30 ?  43   LEU   A C    1 
ATOM   1189 O  O    A LEU   A 1 43  ? 30.646 6.712   0.388   0.62 10.28 ?  43   LEU   A O    1 
ATOM   1190 O  O    B LEU   A 1 43  ? 30.398 6.708   0.271   0.38 10.59 ?  43   LEU   A O    1 
ATOM   1191 C  CB   A LEU   A 1 43  ? 31.884 4.237   0.400   0.62 10.01 ?  43   LEU   A CB   1 
ATOM   1192 C  CB   B LEU   A 1 43  ? 31.747 4.275   0.220   0.38 10.05 ?  43   LEU   A CB   1 
ATOM   1193 C  CG   A LEU   A 1 43  ? 32.395 2.796   0.469   0.62 10.71 ?  43   LEU   A CG   1 
ATOM   1194 C  CG   B LEU   A 1 43  ? 32.209 2.821   0.347   0.38 10.12 ?  43   LEU   A CG   1 
ATOM   1195 C  CD1  A LEU   A 1 43  ? 33.463 2.697   1.545   0.62 11.65 ?  43   LEU   A CD1  1 
ATOM   1196 C  CD1  B LEU   A 1 43  ? 33.249 2.711   1.451   0.38 10.68 ?  43   LEU   A CD1  1 
ATOM   1197 C  CD2  A LEU   A 1 43  ? 31.271 1.808   0.729   0.62 10.97 ?  43   LEU   A CD2  1 
ATOM   1198 C  CD2  B LEU   A 1 43  ? 31.042 1.875   0.602   0.38 10.27 ?  43   LEU   A CD2  1 
ATOM   1199 H  H    A LEU   A 1 43  ? 30.953 3.490   -2.321  0.62 11.47 ?  43   LEU   A H    1 
ATOM   1200 H  H    B LEU   A 1 43  ? 30.750 3.485   -2.459  0.38 12.31 ?  43   LEU   A H    1 
ATOM   1201 H  HA   A LEU   A 1 43  ? 30.070 3.994   -0.476  0.62 11.04 ?  43   LEU   A HA   1 
ATOM   1202 H  HA   B LEU   A 1 43  ? 29.910 4.009   -0.599  0.38 12.39 ?  43   LEU   A HA   1 
ATOM   1203 H  HB2  A LEU   A 1 43  ? 32.652 4.811   0.252   0.62 12.02 ?  43   LEU   A HB2  1 
ATOM   1204 H  HB2  B LEU   A 1 43  ? 32.530 4.806   0.008   0.38 12.07 ?  43   LEU   A HB2  1 
ATOM   1205 H  HB3  A LEU   A 1 43  ? 31.495 4.441   1.266   0.62 12.02 ?  43   LEU   A HB3  1 
ATOM   1206 H  HB3  B LEU   A 1 43  ? 31.409 4.541   1.092   0.38 12.07 ?  43   LEU   A HB3  1 
ATOM   1207 H  HG   A LEU   A 1 43  ? 32.809 2.567   -0.379  0.62 12.86 ?  43   LEU   A HG   1 
ATOM   1208 H  HG   B LEU   A 1 43  ? 32.633 2.553   -0.484  0.38 12.15 ?  43   LEU   A HG   1 
ATOM   1209 H  HD11 A LEU   A 1 43  ? 33.784 1.783   1.584   0.62 14.00 ?  43   LEU   A HD11 1 
ATOM   1210 H  HD11 B LEU   A 1 43  ? 33.538 1.788   1.522   0.38 12.84 ?  43   LEU   A HD11 1 
ATOM   1211 H  HD12 A LEU   A 1 43  ? 34.191 3.297   1.323   0.62 14.00 ?  43   LEU   A HD12 1 
ATOM   1212 H  HD12 B LEU   A 1 43  ? 34.004 3.278   1.230   0.38 12.84 ?  43   LEU   A HD12 1 
ATOM   1213 H  HD13 A LEU   A 1 43  ? 33.072 2.949   2.396   0.62 14.00 ?  43   LEU   A HD13 1 
ATOM   1214 H  HD13 B LEU   A 1 43  ? 32.852 2.999   2.288   0.38 12.84 ?  43   LEU   A HD13 1 
ATOM   1215 H  HD21 A LEU   A 1 43  ? 31.649 0.925   0.847   0.62 13.18 ?  43   LEU   A HD21 1 
ATOM   1216 H  HD21 B LEU   A 1 43  ? 31.390 0.995   0.814   0.38 12.34 ?  43   LEU   A HD21 1 
ATOM   1217 H  HD22 A LEU   A 1 43  ? 30.798 2.078   1.532   0.62 13.18 ?  43   LEU   A HD22 1 
ATOM   1218 H  HD22 B LEU   A 1 43  ? 30.520 2.214   1.346   0.38 12.34 ?  43   LEU   A HD22 1 
ATOM   1219 H  HD23 A LEU   A 1 43  ? 30.667 1.815   -0.029  0.62 13.18 ?  43   LEU   A HD23 1 
ATOM   1220 H  HD23 B LEU   A 1 43  ? 30.494 1.832   -0.196  0.38 12.34 ?  43   LEU   A HD23 1 
ATOM   1221 N  N    A LYS   A 1 44  ? 29.646 6.446   -1.616  0.62 9.67  ?  44   LYS   A N    1 
ATOM   1222 N  N    B LYS   A 1 44  ? 29.439 6.456   -1.746  0.38 10.11 ?  44   LYS   A N    1 
ATOM   1223 C  CA   A LYS   A 1 44  ? 29.007 7.760   -1.628  0.62 10.11 ?  44   LYS   A CA   1 
ATOM   1224 C  CA   B LYS   A 1 44  ? 28.775 7.760   -1.738  0.38 10.17 ?  44   LYS   A CA   1 
ATOM   1225 C  C    A LYS   A 1 44  ? 27.570 7.582   -1.156  0.62 9.71  ?  44   LYS   A C    1 
ATOM   1226 C  C    B LYS   A 1 44  ? 27.372 7.563   -1.176  0.38 9.88  ?  44   LYS   A C    1 
ATOM   1227 O  O    A LYS   A 1 44  ? 26.724 7.052   -1.886  0.62 11.04 ?  44   LYS   A O    1 
ATOM   1228 O  O    B LYS   A 1 44  ? 26.462 7.117   -1.880  0.38 9.72  ?  44   LYS   A O    1 
ATOM   1229 C  CB   A LYS   A 1 44  ? 29.084 8.387   -3.018  0.62 12.23 ?  44   LYS   A CB   1 
ATOM   1230 C  CB   B LYS   A 1 44  ? 28.745 8.353   -3.143  0.38 12.54 ?  44   LYS   A CB   1 
ATOM   1231 C  CG   A LYS   A 1 44  ? 30.489 8.803   -3.427  0.62 15.22 ?  44   LYS   A CG   1 
ATOM   1232 C  CG   B LYS   A 1 44  ? 30.082 8.901   -3.625  0.38 15.13 ?  44   LYS   A CG   1 
ATOM   1233 C  CD   A LYS   A 1 44  ? 31.135 9.742   -2.411  0.62 20.69 ?  44   LYS   A CD   1 
ATOM   1234 C  CD   B LYS   A 1 44  ? 30.710 9.834   -2.593  0.38 18.93 ?  44   LYS   A CD   1 
ATOM   1235 C  CE   A LYS   A 1 44  ? 32.444 10.302  -2.927  0.62 24.14 ?  44   LYS   A CE   1 
ATOM   1236 C  CE   B LYS   A 1 44  ? 32.017 10.418  -3.087  0.38 21.28 ?  44   LYS   A CE   1 
ATOM   1237 N  NZ   A LYS   A 1 44  ? 33.242 10.912  -1.835  0.62 25.96 ?  44   LYS   A NZ   1 
ATOM   1238 N  NZ   B LYS   A 1 44  ? 32.881 10.878  -1.965  0.38 22.66 ?  44   LYS   A NZ   1 
ATOM   1239 H  H    A LYS   A 1 44  ? 29.519 5.995   -2.341  0.62 11.61 ?  44   LYS   A H    1 
ATOM   1240 H  H    B LYS   A 1 44  ? 29.320 6.012   -2.471  0.38 12.15 ?  44   LYS   A H    1 
ATOM   1241 H  HA   A LYS   A 1 44  ? 29.455 8.340   -0.995  0.62 12.15 ?  44   LYS   A HA   1 
ATOM   1242 H  HA   B LYS   A 1 44  ? 29.245 8.359   -1.136  0.38 12.22 ?  44   LYS   A HA   1 
ATOM   1243 H  HB2  A LYS   A 1 44  ? 28.761 7.749   -3.671  0.62 14.69 ?  44   LYS   A HB2  1 
ATOM   1244 H  HB2  B LYS   A 1 44  ? 28.473 7.662   -3.768  0.38 15.06 ?  44   LYS   A HB2  1 
ATOM   1245 H  HB3  A LYS   A 1 44  ? 28.526 9.183   -3.033  0.62 14.69 ?  44   LYS   A HB3  1 
ATOM   1246 H  HB3  B LYS   A 1 44  ? 28.108 9.082   -3.162  0.38 15.06 ?  44   LYS   A HB3  1 
ATOM   1247 H  HG2  A LYS   A 1 44  ? 31.048 8.011   -3.501  0.62 18.28 ?  44   LYS   A HG2  1 
ATOM   1248 H  HG2  B LYS   A 1 44  ? 30.695 8.167   -3.787  0.38 18.18 ?  44   LYS   A HG2  1 
ATOM   1249 H  HG3  A LYS   A 1 44  ? 30.454 9.265   -4.280  0.62 18.28 ?  44   LYS   A HG3  1 
ATOM   1250 H  HG3  B LYS   A 1 44  ? 29.946 9.409   -4.445  0.38 18.18 ?  44   LYS   A HG3  1 
ATOM   1251 H  HD2  A LYS   A 1 44  ? 30.526 10.477  -2.230  0.62 24.85 ?  44   LYS   A HD2  1 
ATOM   1252 H  HD2  B LYS   A 1 44  ? 30.093 10.556  -2.395  0.38 22.73 ?  44   LYS   A HD2  1 
ATOM   1253 H  HD3  A LYS   A 1 44  ? 31.317 9.248   -1.594  0.62 24.85 ?  44   LYS   A HD3  1 
ATOM   1254 H  HD3  B LYS   A 1 44  ? 30.912 9.332   -1.786  0.38 22.73 ?  44   LYS   A HD3  1 
ATOM   1255 H  HE2  A LYS   A 1 44  ? 32.961 9.582   -3.321  0.62 28.98 ?  44   LYS   A HE2  1 
ATOM   1256 H  HE2  B LYS   A 1 44  ? 32.502 9.738   -3.581  0.38 25.55 ?  44   LYS   A HE2  1 
ATOM   1257 H  HE3  A LYS   A 1 44  ? 32.255 10.983  -3.591  0.62 28.98 ?  44   LYS   A HE3  1 
ATOM   1258 H  HE3  B LYS   A 1 44  ? 31.830 11.177  -3.656  0.38 25.55 ?  44   LYS   A HE3  1 
ATOM   1259 H  HZ1  A LYS   A 1 44  ? 34.007 11.224  -2.160  0.62 31.17 ?  44   LYS   A HZ1  1 
ATOM   1260 H  HZ1  B LYS   A 1 44  ? 33.641 11.217  -2.285  0.38 27.20 ?  44   LYS   A HZ1  1 
ATOM   1261 H  HZ2  A LYS   A 1 44  ? 32.786 11.586  -1.469  0.62 31.17 ?  44   LYS   A HZ2  1 
ATOM   1262 H  HZ2  B LYS   A 1 44  ? 32.462 11.507  -1.495  0.38 27.20 ?  44   LYS   A HZ2  1 
ATOM   1263 H  HZ3  A LYS   A 1 44  ? 33.414 10.306  -1.209  0.62 31.17 ?  44   LYS   A HZ3  1 
ATOM   1264 H  HZ3  B LYS   A 1 44  ? 33.075 10.196  -1.426  0.38 27.20 ?  44   LYS   A HZ3  1 
ATOM   1265 N  N    A HIS   A 1 45  ? 27.306 8.000   0.075   0.62 9.18  ?  45   HIS   A N    1 
ATOM   1266 N  N    B HIS   A 1 45  ? 27.197 7.895   0.102   0.38 10.45 ?  45   HIS   A N    1 
ATOM   1267 C  CA   A HIS   A 1 45  ? 26.080 7.626   0.773   0.62 8.88  ?  45   HIS   A CA   1 
ATOM   1268 C  CA   B HIS   A 1 45  ? 25.942 7.638   0.808   0.38 11.03 ?  45   HIS   A CA   1 
ATOM   1269 C  C    A HIS   A 1 45  ? 25.024 8.723   0.615   0.62 9.64  ?  45   HIS   A C    1 
ATOM   1270 C  C    B HIS   A 1 45  ? 25.014 8.829   0.612   0.38 11.57 ?  45   HIS   A C    1 
ATOM   1271 O  O    A HIS   A 1 45  ? 24.639 9.412   1.561   0.62 9.84  ?  45   HIS   A O    1 
ATOM   1272 O  O    B HIS   A 1 45  ? 24.958 9.744   1.435   0.38 12.20 ?  45   HIS   A O    1 
ATOM   1273 C  CB   A HIS   A 1 45  ? 26.393 7.346   2.234   0.62 8.84  ?  45   HIS   A CB   1 
ATOM   1274 C  CB   B HIS   A 1 45  ? 26.209 7.398   2.285   0.38 11.10 ?  45   HIS   A CB   1 
ATOM   1275 C  CG   A HIS   A 1 45  ? 27.493 6.353   2.438   0.62 8.88  ?  45   HIS   A CG   1 
ATOM   1276 C  CG   B HIS   A 1 45  ? 27.359 6.482   2.548   0.38 10.40 ?  45   HIS   A CG   1 
ATOM   1277 N  ND1  A HIS   A 1 45  ? 27.457 5.071   1.924   0.62 9.23  ?  45   HIS   A ND1  1 
ATOM   1278 N  ND1  B HIS   A 1 45  ? 27.414 5.194   2.061   0.38 10.55 ?  45   HIS   A ND1  1 
ATOM   1279 C  CD2  A HIS   A 1 45  ? 28.665 6.465   3.106   0.62 9.33  ?  45   HIS   A CD2  1 
ATOM   1280 C  CD2  B HIS   A 1 45  ? 28.504 6.675   3.245   0.38 9.42  ?  45   HIS   A CD2  1 
ATOM   1281 C  CE1  A HIS   A 1 45  ? 28.564 4.439   2.278   0.62 9.71  ?  45   HIS   A CE1  1 
ATOM   1282 C  CE1  B HIS   A 1 45  ? 28.545 4.633   2.451   0.38 9.18  ?  45   HIS   A CE1  1 
ATOM   1283 N  NE2  A HIS   A 1 45  ? 29.312 5.261   2.995   0.62 9.74  ?  45   HIS   A NE2  1 
ATOM   1284 N  NE2  B HIS   A 1 45  ? 29.223 5.509   3.172   0.38 8.70  ?  45   HIS   A NE2  1 
ATOM   1285 H  H    A HIS   A 1 45  ? 27.828 8.510   0.536   0.62 11.03 ?  45   HIS   A H    1 
ATOM   1286 H  H    B HIS   A 1 45  ? 27.799 8.277   0.587   0.38 12.56 ?  45   HIS   A H    1 
ATOM   1287 H  HA   A HIS   A 1 45  ? 25.730 6.813   0.381   0.62 10.67 ?  45   HIS   A HA   1 
ATOM   1288 H  HA   B HIS   A 1 45  ? 25.518 6.851   0.433   0.38 13.25 ?  45   HIS   A HA   1 
ATOM   1289 H  HB2  A HIS   A 1 45  ? 26.654 8.172   2.666   0.62 10.63 ?  45   HIS   A HB2  1 
ATOM   1290 H  HB2  B HIS   A 1 45  ? 26.402 8.247   2.709   0.38 13.33 ?  45   HIS   A HB2  1 
ATOM   1291 H  HB3  A HIS   A 1 45  ? 25.595 6.990   2.661   0.62 10.63 ?  45   HIS   A HB3  1 
ATOM   1292 H  HB3  B HIS   A 1 45  ? 25.419 7.002   2.681   0.38 13.33 ?  45   HIS   A HB3  1 
ATOM   1293 H  HD2  A HIS   A 1 45  ? 28.980 7.220   3.554   0.62 11.21 ?  45   HIS   A HD2  1 
ATOM   1294 H  HD2  B HIS   A 1 45  ? 28.757 7.454   3.691   0.38 11.31 ?  45   HIS   A HD2  1 
ATOM   1295 H  HE1  A HIS   A 1 45  ? 28.783 3.557   2.070   0.62 11.66 ?  45   HIS   A HE1  1 
ATOM   1296 H  HE1  B HIS   A 1 45  ? 28.817 3.765   2.256   0.38 11.04 ?  45   HIS   A HE1  1 
ATOM   1297 H  HE2  A HIS   A 1 45  ? 30.088 5.075   3.332   0.62 11.70 ?  45   HIS   A HE2  1 
ATOM   1298 H  HE2  B HIS   A 1 45  ? 29.993 5.371   3.534   0.38 10.45 ?  45   HIS   A HE2  1 
ATOM   1299 N  N    A GLY   A 1 46  ? 24.550 8.872   -0.618  0.62 10.48 ?  46   GLY   A N    1 
ATOM   1300 N  N    B GLY   A 1 46  ? 24.262 8.812   -0.481  0.38 11.45 ?  46   GLY   A N    1 
ATOM   1301 C  CA   A GLY   A 1 46  ? 23.757 10.035  -0.971  0.62 11.67 ?  46   GLY   A CA   1 
ATOM   1302 C  CA   B GLY   A 1 46  ? 23.437 9.955   -0.815  0.38 11.31 ?  46   GLY   A CA   1 
ATOM   1303 C  C    A GLY   A 1 46  ? 22.265 9.921   -0.723  0.62 11.14 ?  46   GLY   A C    1 
ATOM   1304 C  C    B GLY   A 1 46  ? 21.980 9.820   -0.424  0.38 10.50 ?  46   GLY   A C    1 
ATOM   1305 O  O    A GLY   A 1 46  ? 21.599 10.928  -0.453  0.62 11.49 ?  46   GLY   A O    1 
ATOM   1306 O  O    B GLY   A 1 46  ? 21.360 10.788  0.029   0.38 10.98 ?  46   GLY   A O    1 
ATOM   1307 H  H    A GLY   A 1 46  ? 24.670 8.309   -1.255  0.62 12.59 ?  46   GLY   A H    1 
ATOM   1308 H  H    B GLY   A 1 46  ? 24.220 8.153   -1.036  0.38 13.76 ?  46   GLY   A H    1 
ATOM   1309 H  HA2  A GLY   A 1 46  ? 24.087 10.796  -0.465  0.62 14.02 ?  46   GLY   A HA2  1 
ATOM   1310 H  HA2  B GLY   A 1 46  ? 23.794 10.741  -0.371  0.38 13.59 ?  46   GLY   A HA2  1 
ATOM   1311 H  HA3  A GLY   A 1 46  ? 23.891 10.223  -1.910  0.62 14.02 ?  46   GLY   A HA3  1 
ATOM   1312 H  HA3  B GLY   A 1 46  ? 23.486 10.102  -1.769  0.38 13.59 ?  46   GLY   A HA3  1 
ATOM   1313 N  N    A GLY   A 1 47  ? 21.723 8.714   -0.840  0.62 10.76 ?  47   GLY   A N    1 
ATOM   1314 N  N    B GLY   A 1 47  ? 21.419 8.626   -0.593  0.38 10.82 ?  47   GLY   A N    1 
ATOM   1315 C  CA   A GLY   A 1 47  ? 20.287 8.516   -0.793  0.62 11.11 ?  47   GLY   A CA   1 
ATOM   1316 C  CA   B GLY   A 1 47  ? 19.994 8.438   -0.400  0.38 11.09 ?  47   GLY   A CA   1 
ATOM   1317 C  C    A GLY   A 1 47  ? 19.960 7.080   -0.448  0.62 10.82 ?  47   GLY   A C    1 
ATOM   1318 C  C    B GLY   A 1 47  ? 19.666 6.996   -0.083  0.38 9.99  ?  47   GLY   A C    1 
ATOM   1319 O  O    A GLY   A 1 47  ? 20.847 6.254   -0.221  0.62 10.94 ?  47   GLY   A O    1 
ATOM   1320 O  O    B GLY   A 1 47  ? 20.549 6.143   0.032   0.38 10.14 ?  47   GLY   A O    1 
ATOM   1321 H  H    A GLY   A 1 47  ? 22.171 7.991   -0.937  0.62 12.92 ?  47   GLY   A H    1 
ATOM   1322 H  H    B GLY   A 1 47  ? 21.847 7.911   -0.806  0.38 12.99 ?  47   GLY   A H    1 
ATOM   1323 H  HA2  A GLY   A 1 47  ? 19.890 9.102   -0.127  0.62 13.35 ?  47   GLY   A HA2  1 
ATOM   1324 H  HA2  B GLY   A 1 47  ? 19.686 8.990   0.334   0.38 13.32 ?  47   GLY   A HA2  1 
ATOM   1325 H  HA3  A GLY   A 1 47  ? 19.899 8.722   -1.659  0.62 13.35 ?  47   GLY   A HA3  1 
ATOM   1326 H  HA3  B GLY   A 1 47  ? 19.520 8.699   -1.206  0.38 13.32 ?  47   GLY   A HA3  1 
ATOM   1327 N  N    A GLY   A 1 48  ? 18.665 6.780   -0.426  0.62 10.42 ?  48   GLY   A N    1 
ATOM   1328 N  N    B GLY   A 1 48  ? 18.367 6.731   0.049   0.38 10.32 ?  48   GLY   A N    1 
ATOM   1329 C  CA   A GLY   A 1 48  ? 18.264 5.442   -0.044  0.62 10.74 ?  48   GLY   A CA   1 
ATOM   1330 C  CA   B GLY   A 1 48  ? 17.928 5.402   0.437   0.38 9.67  ?  48   GLY   A CA   1 
ATOM   1331 C  C    A GLY   A 1 48  ? 18.680 5.116   1.380   0.62 10.41 ?  48   GLY   A C    1 
ATOM   1332 C  C    B GLY   A 1 48  ? 18.546 4.986   1.756   0.38 9.63  ?  48   GLY   A C    1 
ATOM   1333 O  O    A GLY   A 1 48  ? 18.845 6.002   2.229   0.62 10.60 ?  48   GLY   A O    1 
ATOM   1334 O  O    B GLY   A 1 48  ? 18.702 5.790   2.684   0.38 9.50  ?  48   GLY   A O    1 
ATOM   1335 H  H    A GLY   A 1 48  ? 18.019 7.320   -0.617  0.62 12.51 ?  48   GLY   A H    1 
ATOM   1336 H  H    B GLY   A 1 48  ? 17.722 7.295   -0.080  0.38 12.40 ?  48   GLY   A H    1 
ATOM   1337 H  HA2  A GLY   A 1 48  ? 17.306 5.348   -0.112  0.62 12.90 ?  48   GLY   A HA2  1 
ATOM   1338 H  HA2  B GLY   A 1 48  ? 16.960 5.383   0.525   0.38 11.62 ?  48   GLY   A HA2  1 
ATOM   1339 H  HA3  A GLY   A 1 48  ? 18.688 4.796   -0.629  0.62 12.90 ?  48   GLY   A HA3  1 
ATOM   1340 H  HA3  B GLY   A 1 48  ? 18.188 4.758   -0.241  0.38 11.62 ?  48   GLY   A HA3  1 
ATOM   1341 N  N    A VAL   A 1 49  ? 18.844 3.818   1.651   0.62 10.78 ?  49   VAL   A N    1 
ATOM   1342 N  N    B VAL   A 1 49  ? 18.900 3.705   1.843   0.38 10.22 ?  49   VAL   A N    1 
ATOM   1343 C  CA   A VAL   A 1 49  ? 19.304 3.384   2.970   0.62 10.51 ?  49   VAL   A CA   1 
ATOM   1344 C  CA   B VAL   A 1 49  ? 19.502 3.166   3.059   0.38 9.98  ?  49   VAL   A CA   1 
ATOM   1345 C  C    A VAL   A 1 49  ? 20.615 4.068   3.334   0.62 9.68  ?  49   VAL   A C    1 
ATOM   1346 C  C    B VAL   A 1 49  ? 20.762 3.939   3.425   0.38 9.28  ?  49   VAL   A C    1 
ATOM   1347 O  O    A VAL   A 1 49  ? 20.800 4.522   4.467   0.62 10.23 ?  49   VAL   A O    1 
ATOM   1348 O  O    B VAL   A 1 49  ? 20.960 4.320   4.584   0.38 8.91  ?  49   VAL   A O    1 
ATOM   1349 C  CB   A VAL   A 1 49  ? 19.433 1.849   3.019   0.62 11.51 ?  49   VAL   A CB   1 
ATOM   1350 C  CB   B VAL   A 1 49  ? 19.797 1.667   2.877   0.38 10.37 ?  49   VAL   A CB   1 
ATOM   1351 C  CG1  A VAL   A 1 49  ? 20.204 1.401   4.263   0.62 11.70 ?  49   VAL   A CG1  1 
ATOM   1352 C  CG1  B VAL   A 1 49  ? 20.620 1.148   4.045   0.38 9.92  ?  49   VAL   A CG1  1 
ATOM   1353 C  CG2  A VAL   A 1 49  ? 18.058 1.186   2.983   0.62 13.42 ?  49   VAL   A CG2  1 
ATOM   1354 C  CG2  B VAL   A 1 49  ? 18.503 0.876   2.717   0.38 10.88 ?  49   VAL   A CG2  1 
ATOM   1355 H  H    A VAL   A 1 49  ? 18.695 3.176   1.099   0.62 12.96 ?  49   VAL   A H    1 
ATOM   1356 H  H    B VAL   A 1 49  ? 18.802 3.132   1.214   0.38 12.28 ?  49   VAL   A H    1 
ATOM   1357 H  HA   A VAL   A 1 49  ? 18.649 3.636   3.637   0.62 12.62 ?  49   VAL   A HA   1 
ATOM   1358 H  HA   B VAL   A 1 49  ? 18.874 3.259   3.793   0.38 11.99 ?  49   VAL   A HA   1 
ATOM   1359 H  HB   A VAL   A 1 49  ? 19.930 1.542   2.244   0.62 13.83 ?  49   VAL   A HB   1 
ATOM   1360 H  HB   B VAL   A 1 49  ? 20.320 1.546   2.071   0.38 12.46 ?  49   VAL   A HB   1 
ATOM   1361 H  HG11 A VAL   A 1 49  ? 20.028 0.459   4.424   0.62 14.06 ?  49   VAL   A HG11 1 
ATOM   1362 H  HG11 B VAL   A 1 49  ? 20.546 0.182   4.077   0.38 11.92 ?  49   VAL   A HG11 1 
ATOM   1363 H  HG12 A VAL   A 1 49  ? 21.152 1.538   4.119   0.62 14.06 ?  49   VAL   A HG12 1 
ATOM   1364 H  HG12 B VAL   A 1 49  ? 21.550 1.401   3.918   0.38 11.92 ?  49   VAL   A HG12 1 
ATOM   1365 H  HG13 A VAL   A 1 49  ? 19.902 1.923   5.025   0.62 14.06 ?  49   VAL   A HG13 1 
ATOM   1366 H  HG13 B VAL   A 1 49  ? 20.281 1.532   4.868   0.38 11.92 ?  49   VAL   A HG13 1 
ATOM   1367 H  HG21 A VAL   A 1 49  ? 18.169 0.220   3.006   0.62 16.12 ?  49   VAL   A HG21 1 
ATOM   1368 H  HG21 B VAL   A 1 49  ? 18.717 -0.061  2.588   0.38 13.07 ?  49   VAL   A HG21 1 
ATOM   1369 H  HG22 A VAL   A 1 49  ? 17.549 1.476   3.758   0.62 16.12 ?  49   VAL   A HG22 1 
ATOM   1370 H  HG22 B VAL   A 1 49  ? 17.966 0.984   3.519   0.38 13.07 ?  49   VAL   A HG22 1 
ATOM   1371 H  HG23 A VAL   A 1 49  ? 17.605 1.448   2.170   0.62 16.12 ?  49   VAL   A HG23 1 
ATOM   1372 H  HG23 B VAL   A 1 49  ? 18.018 1.215   1.948   0.38 13.07 ?  49   VAL   A HG23 1 
ATOM   1373 N  N    A ALA   A 1 50  ? 21.555 4.115   2.386   0.62 9.67  ?  50   ALA   A N    1 
ATOM   1374 N  N    B ALA   A 1 50  ? 21.652 4.141   2.451   0.38 9.01  ?  50   ALA   A N    1 
ATOM   1375 C  CA   A ALA   A 1 50  ? 22.880 4.660   2.675   0.62 9.54  ?  50   ALA   A CA   1 
ATOM   1376 C  CA   B ALA   A 1 50  ? 22.952 4.735   2.749   0.38 8.83  ?  50   ALA   A CA   1 
ATOM   1377 C  C    A ALA   A 1 50  ? 22.802 6.118   3.100   0.62 9.38  ?  50   ALA   A C    1 
ATOM   1378 C  C    B ALA   A 1 50  ? 22.807 6.184   3.190   0.38 9.26  ?  50   ALA   A C    1 
ATOM   1379 O  O    A ALA   A 1 50  ? 23.478 6.534   4.048   0.62 9.76  ?  50   ALA   A O    1 
ATOM   1380 O  O    B ALA   A 1 50  ? 23.365 6.592   4.217   0.38 9.42  ?  50   ALA   A O    1 
ATOM   1381 C  CB   A ALA   A 1 50  ? 23.775 4.520   1.448   0.62 10.00 ?  50   ALA   A CB   1 
ATOM   1382 C  CB   B ALA   A 1 50  ? 23.864 4.631   1.529   0.38 8.72  ?  50   ALA   A CB   1 
ATOM   1383 H  H    A ALA   A 1 50  ? 21.450 3.849   1.576   0.62 11.62 ?  50   ALA   A H    1 
ATOM   1384 H  H    B ALA   A 1 50  ? 21.520 3.952   1.619   0.38 10.83 ?  50   ALA   A H    1 
ATOM   1385 H  HA   A ALA   A 1 50  ? 23.279 4.162   3.403   0.62 11.46 ?  50   ALA   A HA   1 
ATOM   1386 H  HA   B ALA   A 1 50  ? 23.359 4.243   3.474   0.38 10.61 ?  50   ALA   A HA   1 
ATOM   1387 H  HB1  A ALA   A 1 50  ? 24.649 4.888   1.653   0.62 12.02 ?  50   ALA   A HB1  1 
ATOM   1388 H  HB1  B ALA   A 1 50  ? 24.725 5.016   1.747   0.38 10.48 ?  50   ALA   A HB1  1 
ATOM   1389 H  HB2  A ALA   A 1 50  ? 23.853 3.582   1.220   0.62 12.02 ?  50   ALA   A HB2  1 
ATOM   1390 H  HB2  B ALA   A 1 50  ? 23.969 3.695   1.293   0.38 10.48 ?  50   ALA   A HB2  1 
ATOM   1391 H  HB3  A ALA   A 1 50  ? 23.375 5.009   0.710   0.62 12.02 ?  50   ALA   A HB3  1 
ATOM   1392 H  HB3  B ALA   A 1 50  ? 23.461 5.114   0.789   0.38 10.48 ?  50   ALA   A HB3  1 
ATOM   1393 N  N    A GLY   A 1 51  ? 22.008 6.921   2.393   0.62 9.49  ?  51   GLY   A N    1 
ATOM   1394 N  N    B GLY   A 1 51  ? 22.066 6.981   2.422   0.38 9.85  ?  51   GLY   A N    1 
ATOM   1395 C  CA   A GLY   A 1 51  ? 21.867 8.314   2.782   0.62 9.83  ?  51   GLY   A CA   1 
ATOM   1396 C  CA   B GLY   A 1 51  ? 21.867 8.368   2.805   0.38 10.09 ?  51   GLY   A CA   1 
ATOM   1397 C  C    A GLY   A 1 51  ? 21.257 8.464   4.162   0.62 9.86  ?  51   GLY   A C    1 
ATOM   1398 C  C    B GLY   A 1 51  ? 21.224 8.502   4.170   0.38 10.13 ?  51   GLY   A C    1 
ATOM   1399 O  O    A GLY   A 1 51  ? 21.658 9.337   4.936   0.62 10.45 ?  51   GLY   A O    1 
ATOM   1400 O  O    B GLY   A 1 51  ? 21.568 9.401   4.942   0.38 10.47 ?  51   GLY   A O    1 
ATOM   1401 H  H    A GLY   A 1 51  ? 21.561 6.693   1.694   0.62 11.40 ?  51   GLY   A H    1 
ATOM   1402 H  H    B GLY   A 1 51  ? 21.675 6.749   1.692   0.38 11.84 ?  51   GLY   A H    1 
ATOM   1403 H  HA2  A GLY   A 1 51  ? 22.734 8.744   2.789   0.62 11.81 ?  51   GLY   A HA2  1 
ATOM   1404 H  HA2  B GLY   A 1 51  ? 22.721 8.827   2.823   0.38 12.12 ?  51   GLY   A HA2  1 
ATOM   1405 H  HA3  A GLY   A 1 51  ? 21.299 8.778   2.144   0.62 11.81 ?  51   GLY   A HA3  1 
ATOM   1406 H  HA3  B GLY   A 1 51  ? 21.294 8.807   2.157   0.38 12.12 ?  51   GLY   A HA3  1 
ATOM   1407 N  N    . ALA   A 1 52  ? 20.280 7.610   4.487   1.00 9.97  ?  52   ALA   A N    1 
ATOM   1408 C  CA   . ALA   A 1 52  ? 19.623 7.667   5.789   1.00 10.81 ?  52   ALA   A CA   1 
ATOM   1409 C  C    . ALA   A 1 52  ? 20.566 7.248   6.915   1.00 10.34 ?  52   ALA   A C    1 
ATOM   1410 O  O    . ALA   A 1 52  ? 20.628 7.905   7.959   1.00 11.05 ?  52   ALA   A O    1 
ATOM   1411 C  CB   . ALA   A 1 52  ? 18.365 6.793   5.767   1.00 12.24 ?  52   ALA   A CB   1 
ATOM   1412 H  H    A ALA   A 1 52  ? 19.987 6.983   3.972   0.62 11.97 ?  52   ALA   A H    1 
ATOM   1413 H  H    B ALA   A 1 52  ? 20.010 6.970   3.975   0.38 11.97 ?  52   ALA   A H    1 
ATOM   1414 H  HA   . ALA   A 1 52  ? 19.344 8.579   5.958   1.00 12.98 ?  52   ALA   A HA   1 
ATOM   1415 H  HB1  . ALA   A 1 52  ? 17.921 6.855   6.630   1.00 14.71 ?  52   ALA   A HB1  1 
ATOM   1416 H  HB2  . ALA   A 1 52  ? 17.768 7.115   5.071   1.00 14.71 ?  52   ALA   A HB2  1 
ATOM   1417 H  HB3  . ALA   A 1 52  ? 18.616 5.875   5.589   1.00 14.71 ?  52   ALA   A HB3  1 
ATOM   1418 N  N    A LEU   A 1 53  ? 21.303 6.150   6.730   0.62 10.16 ?  53   LEU   A N    1 
ATOM   1419 N  N    B LEU   A 1 53  ? 21.308 6.154   6.725   0.38 9.92  ?  53   LEU   A N    1 
ATOM   1420 C  CA   A LEU   A 1 53  ? 22.255 5.735   7.759   0.62 10.74 ?  53   LEU   A CA   1 
ATOM   1421 C  CA   B LEU   A 1 53  ? 22.289 5.755   7.733   0.38 9.97  ?  53   LEU   A CA   1 
ATOM   1422 C  C    A LEU   A 1 53  ? 23.323 6.796   7.956   0.62 9.93  ?  53   LEU   A C    1 
ATOM   1423 C  C    B LEU   A 1 53  ? 23.309 6.865   7.953   0.38 9.14  ?  53   LEU   A C    1 
ATOM   1424 O  O    A LEU   A 1 53  ? 23.702 7.106   9.091   0.62 10.78 ?  53   LEU   A O    1 
ATOM   1425 O  O    B LEU   A 1 53  ? 23.562 7.275   9.091   0.38 9.56  ?  53   LEU   A O    1 
ATOM   1426 C  CB   A LEU   A 1 53  ? 22.905 4.396   7.396   0.62 11.34 ?  53   LEU   A CB   1 
ATOM   1427 C  CB   B LEU   A 1 53  ? 22.993 4.452   7.328   0.38 10.10 ?  53   LEU   A CB   1 
ATOM   1428 C  CG   A LEU   A 1 53  ? 21.998 3.160   7.428   0.62 11.40 ?  53   LEU   A CG   1 
ATOM   1429 C  CG   B LEU   A 1 53  ? 22.261 3.106   7.455   0.38 10.14 ?  53   LEU   A CG   1 
ATOM   1430 C  CD1  A LEU   A 1 53  ? 22.723 1.967   6.839   0.62 11.43 ?  53   LEU   A CD1  1 
ATOM   1431 C  CD1  B LEU   A 1 53  ? 23.115 2.000   6.850   0.38 10.98 ?  53   LEU   A CD1  1 
ATOM   1432 C  CD2  A LEU   A 1 53  ? 21.532 2.852   8.841   0.62 12.46 ?  53   LEU   A CD2  1 
ATOM   1433 C  CD2  B LEU   A 1 53  ? 21.920 2.762   8.898   0.38 10.64 ?  53   LEU   A CD2  1 
ATOM   1434 H  H    A LEU   A 1 53  ? 21.269 5.639   6.036   0.62 12.21 ?  53   LEU   A H    1 
ATOM   1435 H  H    B LEU   A 1 53  ? 21.261 5.636   6.038   0.38 11.91 ?  53   LEU   A H    1 
ATOM   1436 H  HA   A LEU   A 1 53  ? 21.784 5.621   8.599   0.62 12.91 ?  53   LEU   A HA   1 
ATOM   1437 H  HA   B LEU   A 1 53  ? 21.831 5.601   8.572   0.38 11.97 ?  53   LEU   A HA   1 
ATOM   1438 H  HB2  A LEU   A 1 53  ? 23.264 4.464   6.497   0.62 13.62 ?  53   LEU   A HB2  1 
ATOM   1439 H  HB2  B LEU   A 1 53  ? 23.247 4.535   6.398   0.38 12.13 ?  53   LEU   A HB2  1 
ATOM   1440 H  HB3  A LEU   A 1 53  ? 23.631 4.230   8.018   0.62 13.62 ?  53   LEU   A HB3  1 
ATOM   1441 H  HB3  B LEU   A 1 53  ? 23.793 4.375   7.867   0.38 12.13 ?  53   LEU   A HB3  1 
ATOM   1442 H  HG   A LEU   A 1 53  ? 21.213 3.331   6.880   0.62 13.70 ?  53   LEU   A HG   1 
ATOM   1443 H  HG   B LEU   A 1 53  ? 21.433 3.144   6.951   0.38 12.19 ?  53   LEU   A HG   1 
ATOM   1444 H  HD11 A LEU   A 1 53  ? 22.138 1.196   6.868   0.62 13.74 ?  53   LEU   A HD11 1 
ATOM   1445 H  HD11 B LEU   A 1 53  ? 22.645 1.153   6.937   0.38 13.19 ?  53   LEU   A HD11 1 
ATOM   1446 H  HD12 A LEU   A 1 53  ? 22.969 2.166   5.922   0.62 13.74 ?  53   LEU   A HD12 1 
ATOM   1447 H  HD12 B LEU   A 1 53  ? 23.270 2.195   5.913   0.38 13.19 ?  53   LEU   A HD12 1 
ATOM   1448 H  HD13 A LEU   A 1 53  ? 23.523 1.797   7.365   0.62 13.74 ?  53   LEU   A HD13 1 
ATOM   1449 H  HD13 B LEU   A 1 53  ? 23.960 1.957   7.325   0.38 13.19 ?  53   LEU   A HD13 1 
ATOM   1450 H  HD21 A LEU   A 1 53  ? 21.010 2.035   8.831   0.62 14.97 ?  53   LEU   A HD21 1 
ATOM   1451 H  HD21 B LEU   A 1 53  ? 21.400 1.941   8.915   0.38 12.78 ?  53   LEU   A HD21 1 
ATOM   1452 H  HD22 A LEU   A 1 53  ? 22.309 2.740   9.411   0.62 14.97 ?  53   LEU   A HD22 1 
ATOM   1453 H  HD22 B LEU   A 1 53  ? 22.739 2.645   9.400   0.38 12.78 ?  53   LEU   A HD22 1 
ATOM   1454 H  HD23 A LEU   A 1 53  ? 20.989 3.587   9.164   0.62 14.97 ?  53   LEU   A HD23 1 
ATOM   1455 H  HD23 B LEU   A 1 53  ? 21.398 3.487   9.280   0.38 12.78 ?  53   LEU   A HD23 1 
ATOM   1456 N  N    A ASN   A 1 54  ? 23.819 7.365   6.860   0.62 10.11 ?  54   ASN   A N    1 
ATOM   1457 N  N    B ASN   A 1 54  ? 23.891 7.377   6.866   0.38 9.30  ?  54   ASN   A N    1 
ATOM   1458 C  CA   A ASN   A 1 54  ? 24.883 8.349   6.990   0.62 10.07 ?  54   ASN   A CA   1 
ATOM   1459 C  CA   B ASN   A 1 54  ? 24.924 8.394   7.012   0.38 9.24  ?  54   ASN   A CA   1 
ATOM   1460 C  C    A ASN   A 1 54  ? 24.390 9.603   7.709   0.62 10.09 ?  54   ASN   A C    1 
ATOM   1461 C  C    B ASN   A 1 54  ? 24.389 9.625   7.732   0.38 9.72  ?  54   ASN   A C    1 
ATOM   1462 O  O    A ASN   A 1 54  ? 25.099 10.152  8.562   0.62 10.74 ?  54   ASN   A O    1 
ATOM   1463 O  O    B ASN   A 1 54  ? 25.063 10.181  8.608   0.38 10.21 ?  54   ASN   A O    1 
ATOM   1464 C  CB   A ASN   A 1 54  ? 25.465 8.686   5.627   0.62 10.15 ?  54   ASN   A CB   1 
ATOM   1465 C  CB   B ASN   A 1 54  ? 25.504 8.783   5.658   0.38 8.85  ?  54   ASN   A CB   1 
ATOM   1466 C  CG   A ASN   A 1 54  ? 26.514 9.762   5.724   0.62 10.49 ?  54   ASN   A CG   1 
ATOM   1467 C  CG   B ASN   A 1 54  ? 26.469 9.937   5.776   0.38 8.66  ?  54   ASN   A CG   1 
ATOM   1468 O  OD1  A ASN   A 1 54  ? 27.508 9.602   6.437   0.62 10.79 ?  54   ASN   A OD1  1 
ATOM   1469 O  OD1  B ASN   A 1 54  ? 27.499 9.819   6.445   0.38 8.53  ?  54   ASN   A OD1  1 
ATOM   1470 N  ND2  A ASN   A 1 54  ? 26.296 10.875  5.042   0.62 11.08 ?  54   ASN   A ND2  1 
ATOM   1471 N  ND2  B ASN   A 1 54  ? 26.135 11.068  5.162   0.38 9.16  ?  54   ASN   A ND2  1 
ATOM   1472 H  H    A ASN   A 1 54  ? 23.560 7.200   6.056   0.62 12.15 ?  54   ASN   A H    1 
ATOM   1473 H  H    B ASN   A 1 54  ? 23.701 7.162   6.057   0.38 11.17 ?  54   ASN   A H    1 
ATOM   1474 H  HA   A ASN   A 1 54  ? 25.586 7.963   7.525   0.62 12.10 ?  54   ASN   A HA   1 
ATOM   1475 H  HA   B ASN   A 1 54  ? 25.638 8.032   7.550   0.38 11.10 ?  54   ASN   A HA   1 
ATOM   1476 H  HB2  A ASN   A 1 54  ? 25.875 7.888   5.252   0.62 12.19 ?  54   ASN   A HB2  1 
ATOM   1477 H  HB2  B ASN   A 1 54  ? 25.986 8.023   5.293   0.38 10.63 ?  54   ASN   A HB2  1 
ATOM   1478 H  HB3  A ASN   A 1 54  ? 24.757 9.001   5.044   0.62 12.19 ?  54   ASN   A HB3  1 
ATOM   1479 H  HB3  B ASN   A 1 54  ? 24.787 9.043   5.063   0.38 10.63 ?  54   ASN   A HB3  1 
ATOM   1480 H  HD21 A ASN   A 1 54  ? 26.869 11.515  5.076   0.62 13.31 ?  54   ASN   A HD21 1 
ATOM   1481 H  HD21 B ASN   A 1 54  ? 26.653 11.755  5.210   0.38 11.01 ?  54   ASN   A HD21 1 
ATOM   1482 H  HD22 A ASN   A 1 54  ? 25.588 10.952  4.564   0.62 13.31 ?  54   ASN   A HD22 1 
ATOM   1483 H  HD22 B ASN   A 1 54  ? 25.406 11.112  4.710   0.38 11.01 ?  54   ASN   A HD22 1 
ATOM   1484 N  N    . LYS   A 1 55  ? 23.179 10.070  7.376   1.00 10.17 ?  55   LYS   A N    1 
ATOM   1485 C  CA   . LYS   A 1 55  ? 22.599 11.227  8.050   1.00 10.76 ?  55   LYS   A CA   1 
ATOM   1486 C  C    . LYS   A 1 55  ? 22.499 10.988  9.551   1.00 10.95 ?  55   LYS   A C    1 
ATOM   1487 O  O    . LYS   A 1 55  ? 22.783 11.884  10.355  1.00 11.70 ?  55   LYS   A O    1 
ATOM   1488 C  CB   . LYS   A 1 55  ? 21.225 11.534  7.446   1.00 11.48 ?  55   LYS   A CB   1 
ATOM   1489 C  CG   . LYS   A 1 55  ? 20.483 12.690  8.097   1.00 13.14 ?  55   LYS   A CG   1 
ATOM   1490 C  CD   . LYS   A 1 55  ? 19.152 12.952  7.386   1.00 14.75 ?  55   LYS   A CD   1 
ATOM   1491 C  CE   . LYS   A 1 55  ? 18.339 14.041  8.071   1.00 16.95 ?  55   LYS   A CE   1 
ATOM   1492 N  NZ   . LYS   A 1 55  ? 17.015 14.240  7.414   1.00 17.90 ?  55   LYS   A NZ   1 
ATOM   1493 H  H    A LYS   A 1 55  ? 22.672 9.730   6.768   0.62 12.21 ?  55   LYS   A H    1 
ATOM   1494 H  H    B LYS   A 1 55  ? 22.674 9.715   6.775   0.38 12.21 ?  55   LYS   A H    1 
ATOM   1495 H  HA   . LYS   A 1 55  ? 23.171 12.000  7.904   1.00 12.93 ?  55   LYS   A HA   1 
ATOM   1496 H  HB2  . LYS   A 1 55  ? 21.343 11.758  6.510   1.00 13.79 ?  55   LYS   A HB2  1 
ATOM   1497 H  HB3  . LYS   A 1 55  ? 20.669 10.748  7.528   1.00 13.79 ?  55   LYS   A HB3  1 
ATOM   1498 H  HG2  . LYS   A 1 55  ? 20.292 12.471  9.022   1.00 15.78 ?  55   LYS   A HG2  1 
ATOM   1499 H  HG3  . LYS   A 1 55  ? 21.021 13.492  8.041   1.00 15.78 ?  55   LYS   A HG3  1 
ATOM   1500 H  HD2  . LYS   A 1 55  ? 19.333 13.230  6.474   1.00 17.71 ?  55   LYS   A HD2  1 
ATOM   1501 H  HD3  . LYS   A 1 55  ? 18.630 12.132  7.385   1.00 17.71 ?  55   LYS   A HD3  1 
ATOM   1502 H  HE2  . LYS   A 1 55  ? 18.185 13.786  8.996   1.00 20.36 ?  55   LYS   A HE2  1 
ATOM   1503 H  HE3  . LYS   A 1 55  ? 18.830 14.875  8.031   1.00 20.36 ?  55   LYS   A HE3  1 
ATOM   1504 H  HZ1  . LYS   A 1 55  ? 16.474 14.696  7.954   1.00 21.49 ?  55   LYS   A HZ1  1 
ATOM   1505 H  HZ2  . LYS   A 1 55  ? 17.116 14.696  6.656   1.00 21.49 ?  55   LYS   A HZ2  1 
ATOM   1506 H  HZ3  . LYS   A 1 55  ? 16.641 13.453  7.231   1.00 21.49 ?  55   LYS   A HZ3  1 
ATOM   1507 N  N    . ALA   A 1 56  ? 22.108 9.777   9.949   1.00 11.18 ?  56   ALA   A N    1 
ATOM   1508 C  CA   . ALA   A 1 56  ? 21.984 9.459   11.364  1.00 12.00 ?  56   ALA   A CA   1 
ATOM   1509 C  C    . ALA   A 1 56  ? 23.325 9.484   12.088  1.00 11.53 ?  56   ALA   A C    1 
ATOM   1510 O  O    . ALA   A 1 56  ? 23.341 9.660   13.309  1.00 13.30 ?  56   ALA   A O    1 
ATOM   1511 C  CB   . ALA   A 1 56  ? 21.282 8.109   11.547  1.00 12.86 ?  56   ALA   A CB   1 
ATOM   1512 H  H    . ALA   A 1 56  ? 21.919 9.134   9.419   1.00 13.43 ?  56   ALA   A H    1 
ATOM   1513 H  HA   . ALA   A 1 56  ? 21.433 10.127  11.783  1.00 14.42 ?  56   ALA   A HA   1 
ATOM   1514 H  HB1  . ALA   A 1 56  ? 21.212 7.914   12.497  1.00 15.45 ?  56   ALA   A HB1  1 
ATOM   1515 H  HB2  . ALA   A 1 56  ? 20.394 8.164   11.158  1.00 15.45 ?  56   ALA   A HB2  1 
ATOM   1516 H  HB3  . ALA   A 1 56  ? 21.795 7.416   11.106  1.00 15.45 ?  56   ALA   A HB3  1 
ATOM   1517 N  N    . THR   A 1 57  ? 24.443 9.302   11.371  1.00 10.61 ?  57   THR   A N    1 
ATOM   1518 C  CA   . THR   A 1 57  ? 25.782 9.429   11.950  1.00 11.09 ?  57   THR   A CA   1 
ATOM   1519 C  C    . THR   A 1 57  ? 26.328 10.851  11.878  1.00 11.40 ?  57   THR   A C    1 
ATOM   1520 O  O    . THR   A 1 57  ? 27.513 11.061  12.175  1.00 11.92 ?  57   THR   A O    1 
ATOM   1521 C  CB   . THR   A 1 57  ? 26.799 8.482   11.280  1.00 11.25 ?  57   THR   A CB   1 
ATOM   1522 O  OG1  . THR   A 1 57  ? 27.191 8.977   9.982   1.00 10.71 ?  57   THR   A OG1  1 
ATOM   1523 C  CG2  . THR   A 1 57  ? 26.281 7.052   11.178  1.00 11.18 ?  57   THR   A CG2  1 
ATOM   1524 H  H    . THR   A 1 57  ? 24.451 9.080   10.535  1.00 12.75 ?  57   THR   A H    1 
ATOM   1525 H  HA   . THR   A 1 57  ? 25.736 9.173   12.888  1.00 13.32 ?  57   THR   A HA   1 
ATOM   1526 H  HB   . THR   A 1 57  ? 27.597 8.446   11.842  1.00 13.51 ?  57   THR   A HB   1 
ATOM   1527 H  HG1  . THR   A 1 57  ? 26.514 9.044   9.492   1.00 12.87 ?  57   THR   A HG1  1 
ATOM   1528 H  HG21 . THR   A 1 57  ? 26.959 6.476   10.781  1.00 13.44 ?  57   THR   A HG21 1 
ATOM   1529 H  HG22 . THR   A 1 57  ? 26.060 6.709   12.058  1.00 13.44 ?  57   THR   A HG22 1 
ATOM   1530 H  HG23 . THR   A 1 57  ? 25.489 7.024   10.622  1.00 13.44 ?  57   THR   A HG23 1 
ATOM   1531 N  N    . ASN   A 1 58  ? 25.515 11.825  11.469  1.00 11.69 ?  58   ASN   A N    1 
ATOM   1532 C  CA   . ASN   A 1 58  ? 25.987 13.205  11.373  1.00 12.76 ?  58   ASN   A CA   1 
ATOM   1533 C  C    . ASN   A 1 58  ? 27.134 13.330  10.362  1.00 11.42 ?  58   ASN   A C    1 
ATOM   1534 O  O    . ASN   A 1 58  ? 28.031 14.164  10.516  1.00 12.20 ?  58   ASN   A O    1 
ATOM   1535 C  CB   . ASN   A 1 58  ? 26.375 13.731  12.770  1.00 15.33 ?  58   ASN   A CB   1 
ATOM   1536 C  CG   . ASN   A 1 58  ? 26.793 15.183  12.775  1.00 19.07 ?  58   ASN   A CG   1 
ATOM   1537 O  OD1  . ASN   A 1 58  ? 26.173 16.016  12.125  1.00 20.95 ?  58   ASN   A OD1  1 
ATOM   1538 N  ND2  . ASN   A 1 58  ? 27.845 15.500  13.534  1.00 20.23 ?  58   ASN   A ND2  1 
ATOM   1539 H  H    . ASN   A 1 58  ? 24.695 11.703  11.231  1.00 14.05 ?  58   ASN   A H    1 
ATOM   1540 H  HA   . ASN   A 1 58  ? 25.252 13.744  11.051  1.00 15.32 ?  58   ASN   A HA   1 
ATOM   1541 H  HB2  . ASN   A 1 58  ? 25.607 13.633  13.364  1.00 18.41 ?  58   ASN   A HB2  1 
ATOM   1542 H  HB3  . ASN   A 1 58  ? 27.116 13.210  13.112  1.00 18.41 ?  58   ASN   A HB3  1 
ATOM   1543 H  HD21 . ASN   A 1 58  ? 28.114 16.315  13.573  1.00 24.30 ?  58   ASN   A HD21 1 
ATOM   1544 H  HD22 . ASN   A 1 58  ? 28.249 14.888  13.978  1.00 24.30 ?  58   ASN   A HD22 1 
ATOM   1545 N  N    . ASN   A 1 59  ? 27.115 12.503  9.311   1.00 10.66 ?  59   ASN   A N    1 
ATOM   1546 C  CA   . ASN   A 1 59  ? 28.094 12.481  8.218   1.00 10.33 ?  59   ASN   A CA   1 
ATOM   1547 C  C    . ASN   A 1 59  ? 29.412 11.803  8.609   1.00 10.37 ?  59   ASN   A C    1 
ATOM   1548 O  O    . ASN   A 1 59  ? 30.333 11.767  7.783   1.00 10.65 ?  59   ASN   A O    1 
ATOM   1549 C  CB   . ASN   A 1 59  ? 28.389 13.867  7.617   1.00 10.87 ?  59   ASN   A CB   1 
ATOM   1550 C  CG   . ASN   A 1 59  ? 28.752 13.802  6.150   1.00 10.90 ?  59   ASN   A CG   1 
ATOM   1551 O  OD1  . ASN   A 1 59  ? 28.047 13.182  5.355   1.00 11.32 ?  59   ASN   A OD1  1 
ATOM   1552 N  ND2  . ASN   A 1 59  ? 29.838 14.463  5.773   1.00 11.67 ?  59   ASN   A ND2  1 
ATOM   1553 H  H    . ASN   A 1 59  ? 26.502 11.904  9.200   1.00 12.80 ?  59   ASN   A H    1 
ATOM   1554 H  HA   . ASN   A 1 59  ? 27.716 11.956  7.504   1.00 12.42 ?  59   ASN   A HA   1 
ATOM   1555 H  HB2  . ASN   A 1 59  ? 27.602 14.432  7.701   1.00 13.06 ?  59   ASN   A HB2  1 
ATOM   1556 H  HB3  . ASN   A 1 59  ? 29.135 14.274  8.087   1.00 13.06 ?  59   ASN   A HB3  1 
ATOM   1557 H  HD21 . ASN   A 1 59  ? 30.087 14.461  4.947   1.00 14.02 ?  59   ASN   A HD21 1 
ATOM   1558 H  HD22 . ASN   A 1 59  ? 30.314 14.891  6.355   1.00 14.02 ?  59   ASN   A HD22 1 
ATOM   1559 N  N    . ALA   A 1 60  ? 29.536 11.262  9.821   1.00 10.21 ?  60   ALA   A N    1 
ATOM   1560 C  CA   . ALA   A 1 60  ? 30.775 10.579  10.183  1.00 10.61 ?  60   ALA   A CA   1 
ATOM   1561 C  C    . ALA   A 1 60  ? 31.001 9.341   9.323   1.00 10.72 ?  60   ALA   A C    1 
ATOM   1562 O  O    . ALA   A 1 60  ? 32.150 9.018   8.991   1.00 11.14 ?  60   ALA   A O    1 
ATOM   1563 C  CB   . ALA   A 1 60  ? 30.766 10.215  11.667  1.00 11.61 ?  60   ALA   A CB   1 
ATOM   1564 H  H    . ALA   A 1 60  ? 28.935 11.273  10.438  1.00 12.26 ?  60   ALA   A H    1 
ATOM   1565 H  HA   . ALA   A 1 60  ? 31.520 11.187  10.033  1.00 12.74 ?  60   ALA   A HA   1 
ATOM   1566 H  HB1  . ALA   A 1 60  ? 31.593 9.766   11.889  1.00 13.94 ?  60   ALA   A HB1  1 
ATOM   1567 H  HB2  . ALA   A 1 60  ? 30.677 11.029  12.192  1.00 13.94 ?  60   ALA   A HB2  1 
ATOM   1568 H  HB3  . ALA   A 1 60  ? 30.011 9.630   11.841  1.00 13.94 ?  60   ALA   A HB3  1 
ATOM   1569 N  N    . MET   A 1 61  ? 29.930 8.644   8.939   1.00 9.98  ?  61   MET   A N    1 
ATOM   1570 C  CA   . MET   A 1 61  ? 30.079 7.509   8.036   1.00 9.98  ?  61   MET   A CA   1 
ATOM   1571 C  C    . MET   A 1 61  ? 30.711 7.932   6.710   1.00 10.00 ?  61   MET   A C    1 
ATOM   1572 O  O    . MET   A 1 61  ? 31.604 7.250   6.192   1.00 10.25 ?  61   MET   A O    1 
ATOM   1573 C  CB   . MET   A 1 61  ? 28.718 6.850   7.813   1.00 10.06 ?  61   MET   A CB   1 
ATOM   1574 C  CG   . MET   A 1 61  ? 28.731 5.675   6.839   1.00 10.87 ?  61   MET   A CG   1 
ATOM   1575 S  SD   . MET   A 1 61  ? 27.104 4.932   6.622   1.00 11.61 ?  61   MET   A SD   1 
ATOM   1576 C  CE   . MET   A 1 61  ? 26.969 4.046   8.180   1.00 13.22 ?  61   MET   A CE   1 
ATOM   1577 H  H    . MET   A 1 61  ? 29.120 8.804   9.180   1.00 11.99 ?  61   MET   A H    1 
ATOM   1578 H  HA   . MET   A 1 61  ? 30.658 6.851   8.454   1.00 11.99 ?  61   MET   A HA   1 
ATOM   1579 H  HB2  . MET   A 1 61  ? 28.393 6.523   8.662   1.00 12.09 ?  61   MET   A HB2  1 
ATOM   1580 H  HB3  . MET   A 1 61  ? 28.108 7.514   7.459   1.00 12.09 ?  61   MET   A HB3  1 
ATOM   1581 H  HG2  . MET   A 1 61  ? 29.026 5.974   5.966   1.00 13.06 ?  61   MET   A HG2  1 
ATOM   1582 H  HG3  . MET   A 1 61  ? 29.323 4.984   7.173   1.00 13.06 ?  61   MET   A HG3  1 
ATOM   1583 H  HE1  . MET   A 1 61  ? 26.126 3.563   8.201   1.00 15.88 ?  61   MET   A HE1  1 
ATOM   1584 H  HE2  . MET   A 1 61  ? 27.708 3.422   8.255   1.00 15.88 ?  61   MET   A HE2  1 
ATOM   1585 H  HE3  . MET   A 1 61  ? 26.999 4.682   8.915   1.00 15.88 ?  61   MET   A HE3  1 
ATOM   1586 N  N    . GLN   A 1 62  ? 30.267 9.057   6.146   1.00 9.93  ?  62   GLN   A N    1 
ATOM   1587 C  CA   . GLN   A 1 62  ? 30.830 9.525   4.883   1.00 10.15 ?  62   GLN   A CA   1 
ATOM   1588 C  C    . GLN   A 1 62  ? 32.298 9.912   5.031   1.00 10.12 ?  62   GLN   A C    1 
ATOM   1589 O  O    . GLN   A 1 62  ? 33.111 9.605   4.151   1.00 10.57 ?  62   GLN   A O    1 
ATOM   1590 C  CB   . GLN   A 1 62  ? 30.023 10.706  4.346   1.00 10.20 ?  62   GLN   A CB   1 
ATOM   1591 C  CG   . GLN   A 1 62  ? 30.408 11.074  2.921   1.00 10.31 ?  62   GLN   A CG   1 
ATOM   1592 C  CD   . GLN   A 1 62  ? 30.079 9.942   1.969   1.00 10.34 ?  62   GLN   A CD   1 
ATOM   1593 O  OE1  . GLN   A 1 62  ? 28.902 9.629   1.761   1.00 10.80 ?  62   GLN   A OE1  1 
ATOM   1594 N  NE2  . GLN   A 1 62  ? 31.103 9.265   1.447   1.00 11.06 ?  62   GLN   A NE2  1 
ATOM   1595 H  H    . GLN   A 1 62  ? 29.648 9.555   6.470   1.00 11.93 ?  62   GLN   A H    1 
ATOM   1596 H  HA   . GLN   A 1 62  ? 30.781 8.805   4.238   1.00 12.19 ?  62   GLN   A HA   1 
ATOM   1597 H  HB2  . GLN   A 1 62  ? 29.084 10.480  4.356   1.00 12.26 ?  62   GLN   A HB2  1 
ATOM   1598 H  HB3  . GLN   A 1 62  ? 30.189 11.483  4.905   1.00 12.26 ?  62   GLN   A HB3  1 
ATOM   1599 H  HG2  . GLN   A 1 62  ? 29.907 11.852  2.642   1.00 12.38 ?  62   GLN   A HG2  1 
ATOM   1600 H  HG3  . GLN   A 1 62  ? 31.361 11.245  2.871   1.00 12.38 ?  62   GLN   A HG3  1 
ATOM   1601 H  HE21 . GLN   A 1 62  ? 31.913 9.497   1.631   1.00 13.28 ?  62   GLN   A HE21 1 
ATOM   1602 H  HE22 . GLN   A 1 62  ? 30.961 8.606   0.911   1.00 13.28 ?  62   GLN   A HE22 1 
ATOM   1603 N  N    . VAL   A 1 63  ? 32.654 10.596  6.121   1.00 10.44 ?  63   VAL   A N    1 
ATOM   1604 C  CA   . VAL   A 1 63  ? 34.046 10.991  6.335   1.00 11.36 ?  63   VAL   A CA   1 
ATOM   1605 C  C    . VAL   A 1 63  ? 34.945 9.758   6.399   1.00 11.00 ?  63   VAL   A C    1 
ATOM   1606 O  O    . VAL   A 1 63  ? 35.999 9.692   5.750   1.00 11.36 ?  63   VAL   A O    1 
ATOM   1607 C  CB   . VAL   A 1 63  ? 34.157 11.867  7.598   1.00 12.98 ?  63   VAL   A CB   1 
ATOM   1608 C  CG1  . VAL   A 1 63  ? 35.607 12.100  7.965   1.00 14.70 ?  63   VAL   A CG1  1 
ATOM   1609 C  CG2  . VAL   A 1 63  ? 33.433 13.203  7.381   1.00 13.51 ?  63   VAL   A CG2  1 
ATOM   1610 H  H    . VAL   A 1 63  ? 32.110 10.838  6.746   1.00 12.55 ?  63   VAL   A H    1 
ATOM   1611 H  HA   . VAL   A 1 63  ? 34.330 11.528  5.582   1.00 13.65 ?  63   VAL   A HA   1 
ATOM   1612 H  HB   . VAL   A 1 63  ? 33.727 11.414  8.341   1.00 15.59 ?  63   VAL   A HB   1 
ATOM   1613 H  HG11 . VAL   A 1 63  ? 35.655 12.840  8.591   1.00 17.66 ?  63   VAL   A HG11 1 
ATOM   1614 H  HG12 . VAL   A 1 63  ? 35.963 11.298  8.371   1.00 17.66 ?  63   VAL   A HG12 1 
ATOM   1615 H  HG13 . VAL   A 1 63  ? 36.101 12.319  7.160   1.00 17.66 ?  63   VAL   A HG13 1 
ATOM   1616 H  HG21 . VAL   A 1 63  ? 33.521 13.745  8.184   1.00 16.23 ?  63   VAL   A HG21 1 
ATOM   1617 H  HG22 . VAL   A 1 63  ? 33.835 13.663  6.628   1.00 16.23 ?  63   VAL   A HG22 1 
ATOM   1618 H  HG23 . VAL   A 1 63  ? 32.495 13.031  7.203   1.00 16.23 ?  63   VAL   A HG23 1 
ATOM   1619 N  N    . GLU   A 1 64  ? 34.525 8.747   7.164   1.00 10.91 ?  64   GLU   A N    1 
ATOM   1620 C  CA   . GLU   A 1 64  ? 35.293 7.515   7.267   1.00 10.87 ?  64   GLU   A CA   1 
ATOM   1621 C  C    . GLU   A 1 64  ? 35.384 6.821   5.912   1.00 10.52 ?  64   GLU   A C    1 
ATOM   1622 O  O    . GLU   A 1 64  ? 36.437 6.277   5.539   1.00 11.05 ?  64   GLU   A O    1 
ATOM   1623 C  CB   . GLU   A 1 64  ? 34.606 6.611   8.293   1.00 11.51 ?  64   GLU   A CB   1 
ATOM   1624 C  CG   . GLU   A 1 64  ? 35.263 5.260   8.461   1.00 12.24 ?  64   GLU   A CG   1 
ATOM   1625 C  CD   . GLU   A 1 64  ? 34.388 4.265   9.191   1.00 12.97 ?  64   GLU   A CD   1 
ATOM   1626 O  OE1  . GLU   A 1 64  ? 33.147 4.354   9.059   1.00 13.94 ?  64   GLU   A OE1  1 
ATOM   1627 O  OE2  . GLU   A 1 64  ? 34.949 3.377   9.876   1.00 13.32 -1 64   GLU   A OE2  1 
ATOM   1628 H  H    . GLU   A 1 64  ? 33.784 8.745   7.609   1.00 13.11 ?  64   GLU   A H    1 
ATOM   1629 H  HA   . GLU   A 1 64  ? 36.185 7.721   7.583   1.00 13.06 ?  64   GLU   A HA   1 
ATOM   1630 H  HB2  . GLU   A 1 64  ? 34.619 7.056   9.160   1.00 13.83 ?  64   GLU   A HB2  1 
ATOM   1631 H  HB3  . GLU   A 1 64  ? 33.688 6.469   8.017   1.00 13.83 ?  64   GLU   A HB3  1 
ATOM   1632 H  HG2  . GLU   A 1 64  ? 35.471 4.890   7.588   1.00 14.70 ?  64   GLU   A HG2  1 
ATOM   1633 H  HG3  . GLU   A 1 64  ? 36.078 5.370   8.972   1.00 14.70 ?  64   GLU   A HG3  1 
ATOM   1634 N  N    . SER   A 1 65  ? 34.269 6.801   5.178   1.00 10.14 ?  65   SER   A N    1 
ATOM   1635 C  CA   . SER   A 1 65  ? 34.221 6.142   3.879   1.00 10.27 ?  65   SER   A CA   1 
ATOM   1636 C  C    . SER   A 1 65  ? 35.137 6.813   2.866   1.00 10.27 ?  65   SER   A C    1 
ATOM   1637 O  O    . SER   A 1 65  ? 35.772 6.135   2.054   1.00 11.49 ?  65   SER   A O    1 
ATOM   1638 C  CB   . SER   A 1 65  ? 32.784 6.148   3.356   1.00 10.25 ?  65   SER   A CB   1 
ATOM   1639 O  OG   . SER   A 1 65  ? 31.933 5.340   4.157   1.00 10.76 ?  65   SER   A OG   1 
ATOM   1640 H  H    . SER   A 1 65  ? 33.529 7.167   5.416   1.00 12.19 ?  65   SER   A H    1 
ATOM   1641 H  HA   . SER   A 1 65  ? 34.506 5.224   3.977   1.00 12.34 ?  65   SER   A HA   1 
ATOM   1642 H  HB2  . SER   A 1 65  ? 32.448 7.057   3.365   1.00 12.32 ?  65   SER   A HB2  1 
ATOM   1643 H  HB3  . SER   A 1 65  ? 32.784 5.805   2.450   1.00 12.32 ?  65   SER   A HB3  1 
ATOM   1644 H  HG   . SER   A 1 65  ? 31.931 5.623   4.951   1.00 12.93 ?  65   SER   A HG   1 
ATOM   1645 N  N    . ASP   A 1 66  ? 35.205 8.146   2.881   1.00 10.56 ?  66   ASP   A N    1 
ATOM   1646 C  CA   . ASP   A 1 66  ? 36.068 8.842   1.929   1.00 11.49 ?  66   ASP   A CA   1 
ATOM   1647 C  C    . ASP   A 1 66  ? 37.533 8.495   2.172   1.00 11.43 ?  66   ASP   A C    1 
ATOM   1648 O  O    . ASP   A 1 66  ? 38.308 8.322   1.223   1.00 12.47 ?  66   ASP   A O    1 
ATOM   1649 C  CB   . ASP   A 1 66  ? 35.850 10.350  2.016   1.00 12.67 ?  66   ASP   A CB   1 
ATOM   1650 C  CG   . ASP   A 1 66  ? 34.506 10.804  1.420   1.00 14.36 ?  66   ASP   A CG   1 
ATOM   1651 O  OD1  . ASP   A 1 66  ? 33.795 10.005  0.777   1.00 14.63 ?  66   ASP   A OD1  1 
ATOM   1652 O  OD2  . ASP   A 1 66  ? 34.197 12.004  1.570   1.00 17.04 -1 66   ASP   A OD2  1 
ATOM   1653 H  H    . ASP   A 1 66  ? 34.758 8.667   3.408   1.00 12.69 ?  66   ASP   A H    1 
ATOM   1654 H  HA   . ASP   A 1 66  ? 35.837 8.559   1.029   1.00 13.80 ?  66   ASP   A HA   1 
ATOM   1655 H  HB2  . ASP   A 1 66  ? 35.867 10.620  2.945   1.00 15.22 ?  66   ASP   A HB2  1 
ATOM   1656 H  HB3  . ASP   A 1 66  ? 36.563 10.799  1.528   1.00 15.22 ?  66   ASP   A HB3  1 
ATOM   1657 N  N    . ASP   A 1 67  ? 37.927 8.364   3.437   1.00 11.69 ?  67   ASP   A N    1 
ATOM   1658 C  CA   . ASP   A 1 67  ? 39.283 7.916   3.739   1.00 12.50 ?  67   ASP   A CA   1 
ATOM   1659 C  C    . ASP   A 1 67  ? 39.507 6.481   3.274   1.00 12.53 ?  67   ASP   A C    1 
ATOM   1660 O  O    . ASP   A 1 67  ? 40.573 6.158   2.739   1.00 13.20 ?  67   ASP   A O    1 
ATOM   1661 C  CB   . ASP   A 1 67  ? 39.555 8.052   5.236   1.00 13.81 ?  67   ASP   A CB   1 
ATOM   1662 C  CG   . ASP   A 1 67  ? 40.858 7.398   5.653   1.00 15.24 ?  67   ASP   A CG   1 
ATOM   1663 O  OD1  . ASP   A 1 67  ? 41.928 8.035   5.511   1.00 18.49 ?  67   ASP   A OD1  1 
ATOM   1664 O  OD2  . ASP   A 1 67  ? 40.806 6.238   6.116   1.00 14.87 -1 67   ASP   A OD2  1 
ATOM   1665 H  H    . ASP   A 1 67  ? 37.439 8.521   4.122   1.00 14.05 ?  67   ASP   A H    1 
ATOM   1666 H  HA   . ASP   A 1 67  ? 39.916 8.482   3.266   1.00 15.02 ?  67   ASP   A HA   1 
ATOM   1667 H  HB2  . ASP   A 1 67  ? 39.606 8.993   5.459   1.00 16.59 ?  67   ASP   A HB2  1 
ATOM   1668 H  HB3  . ASP   A 1 67  ? 38.833 7.630   5.726   1.00 16.59 ?  67   ASP   A HB3  1 
ATOM   1669 N  N    . TYR   A 1 68  ? 38.515 5.604   3.466   1.00 11.95 ?  68   TYR   A N    1 
ATOM   1670 C  CA   . TYR   A 1 68  ? 38.637 4.225   2.991   1.00 12.07 ?  68   TYR   A CA   1 
ATOM   1671 C  C    . TYR   A 1 68  ? 38.881 4.182   1.483   1.00 12.18 ?  68   TYR   A C    1 
ATOM   1672 O  O    . TYR   A 1 68  ? 39.762 3.451   1.009   1.00 12.64 ?  68   TYR   A O    1 
ATOM   1673 C  CB   . TYR   A 1 68  ? 37.394 3.396   3.378   1.00 12.69 ?  68   TYR   A CB   1 
ATOM   1674 C  CG   . TYR   A 1 68  ? 37.426 2.011   2.757   1.00 13.93 ?  68   TYR   A CG   1 
ATOM   1675 C  CD1  . TYR   A 1 68  ? 36.968 1.812   1.459   1.00 15.61 ?  68   TYR   A CD1  1 
ATOM   1676 C  CD2  . TYR   A 1 68  ? 37.970 0.933   3.428   1.00 16.15 ?  68   TYR   A CD2  1 
ATOM   1677 C  CE1  . TYR   A 1 68  ? 37.044 0.598   0.847   1.00 17.08 ?  68   TYR   A CE1  1 
ATOM   1678 C  CE2  . TYR   A 1 68  ? 38.035 -0.325  2.819   1.00 17.18 ?  68   TYR   A CE2  1 
ATOM   1679 C  CZ   . TYR   A 1 68  ? 37.574 -0.466  1.527   1.00 17.79 ?  68   TYR   A CZ   1 
ATOM   1680 O  OH   . TYR   A 1 68  ? 37.661 -1.681  0.901   1.00 19.53 ?  68   TYR   A OH   1 
ATOM   1681 H  H    . TYR   A 1 68  ? 37.768 5.784   3.865   1.00 14.36 ?  68   TYR   A H    1 
ATOM   1682 H  HA   . TYR   A 1 68  ? 39.400 3.822   3.423   1.00 14.50 ?  68   TYR   A HA   1 
ATOM   1683 H  HB2  . TYR   A 1 68  ? 37.365 3.296   4.341   1.00 15.25 ?  68   TYR   A HB2  1 
ATOM   1684 H  HB3  . TYR   A 1 68  ? 36.595 3.851   3.064   1.00 15.25 ?  68   TYR   A HB3  1 
ATOM   1685 H  HD1  . TYR   A 1 68  ? 36.619 2.537   0.989   1.00 18.75 ?  68   TYR   A HD1  1 
ATOM   1686 H  HD2  . TYR   A 1 68  ? 38.300 1.041   4.288   1.00 19.40 ?  68   TYR   A HD2  1 
ATOM   1687 H  HE1  . TYR   A 1 68  ? 36.721 0.494   -0.021  1.00 20.52 ?  68   TYR   A HE1  1 
ATOM   1688 H  HE2  . TYR   A 1 68  ? 38.406 -1.054  3.260   1.00 20.63 ?  68   TYR   A HE2  1 
ATOM   1689 H  HH   . TYR   A 1 68  ? 37.990 -2.249  1.425   1.00 23.45 ?  68   TYR   A HH   1 
ATOM   1690 N  N    . ILE   A 1 69  ? 38.097 4.941   0.710   1.00 11.41 ?  69   ILE   A N    1 
ATOM   1691 C  CA   . ILE   A 1 69  ? 38.234 4.921   -0.744  1.00 11.45 ?  69   ILE   A CA   1 
ATOM   1692 C  C    . ILE   A 1 69  ? 39.563 5.532   -1.171  1.00 11.40 ?  69   ILE   A C    1 
ATOM   1693 O  O    . ILE   A 1 69  ? 40.215 5.048   -2.103  1.00 11.91 ?  69   ILE   A O    1 
ATOM   1694 C  CB   . ILE   A 1 69  ? 37.038 5.636   -1.407  1.00 12.52 ?  69   ILE   A CB   1 
ATOM   1695 C  CG1  . ILE   A 1 69  ? 35.721 4.907   -1.129  1.00 12.82 ?  69   ILE   A CG1  1 
ATOM   1696 C  CG2  . ILE   A 1 69  ? 37.282 5.827   -2.912  1.00 13.79 ?  69   ILE   A CG2  1 
ATOM   1697 C  CD1  . ILE   A 1 69  ? 35.557 3.614   -1.890  1.00 13.94 ?  69   ILE   A CD1  1 
ATOM   1698 H  H    . ILE   A 1 69  ? 37.483 5.474   1.001   1.00 13.70 ?  69   ILE   A H    1 
ATOM   1699 H  HA   . ILE   A 1 69  ? 38.229 4.002   -1.042  1.00 13.75 ?  69   ILE   A HA   1 
ATOM   1700 H  HB   . ILE   A 1 69  ? 36.971 6.518   -1.016  1.00 15.03 ?  69   ILE   A HB   1 
ATOM   1701 H  HG12 . ILE   A 1 69  ? 35.677 4.704   -0.180  1.00 15.40 ?  69   ILE   A HG12 1 
ATOM   1702 H  HG13 . ILE   A 1 69  ? 34.986 5.494   -1.369  1.00 15.40 ?  69   ILE   A HG13 1 
ATOM   1703 H  HG21 . ILE   A 1 69  ? 36.437 6.034   -3.345  1.00 16.56 ?  69   ILE   A HG21 1 
ATOM   1704 H  HG22 . ILE   A 1 69  ? 37.902 6.565   -3.043  1.00 16.56 ?  69   ILE   A HG22 1 
ATOM   1705 H  HG23 . ILE   A 1 69  ? 37.652 5.013   -3.282  1.00 16.56 ?  69   ILE   A HG23 1 
ATOM   1706 H  HD11 . ILE   A 1 69  ? 34.751 3.172   -1.581  1.00 16.74 ?  69   ILE   A HD11 1 
ATOM   1707 H  HD12 . ILE   A 1 69  ? 35.480 3.814   -2.837  1.00 16.74 ?  69   ILE   A HD12 1 
ATOM   1708 H  HD13 . ILE   A 1 69  ? 36.327 3.051   -1.729  1.00 16.74 ?  69   ILE   A HD13 1 
ATOM   1709 N  N    . ALA   A 1 70  ? 39.977 6.612   -0.512  1.00 11.99 ?  70   ALA   A N    1 
ATOM   1710 C  CA   . ALA   A 1 70  ? 41.250 7.236   -0.858  1.00 12.75 ?  70   ALA   A CA   1 
ATOM   1711 C  C    . ALA   A 1 70  ? 42.410 6.262   -0.686  1.00 13.23 ?  70   ALA   A C    1 
ATOM   1712 O  O    . ALA   A 1 70  ? 43.388 6.323   -1.437  1.00 15.16 ?  70   ALA   A O    1 
ATOM   1713 C  CB   . ALA   A 1 70  ? 41.469 8.493   -0.015  1.00 13.33 ?  70   ALA   A CB   1 
ATOM   1714 H  H    . ALA   A 1 70  ? 39.547 6.997   0.121   1.00 14.41 ?  70   ALA   A H    1 
ATOM   1715 H  HA   . ALA   A 1 70  ? 41.227 7.505   -1.789  1.00 15.31 ?  70   ALA   A HA   1 
ATOM   1716 H  HB1  . ALA   A 1 70  ? 42.322 8.889   -0.256  1.00 16.02 ?  70   ALA   A HB1  1 
ATOM   1717 H  HB2  . ALA   A 1 70  ? 40.751 9.119   -0.188  1.00 16.02 ?  70   ALA   A HB2  1 
ATOM   1718 H  HB3  . ALA   A 1 70  ? 41.476 8.245   0.924   1.00 16.02 ?  70   ALA   A HB3  1 
ATOM   1719 N  N    . THR   A 1 71  ? 42.310 5.346   0.273   1.00 12.85 ?  71   THR   A N    1 
ATOM   1720 C  CA   . THR   A 1 71  ? 43.361 4.367   0.525   1.00 14.21 ?  71   THR   A CA   1 
ATOM   1721 C  C    . THR   A 1 71  ? 43.247 3.136   -0.360  1.00 14.38 ?  71   THR   A C    1 
ATOM   1722 O  O    . THR   A 1 71  ? 44.264 2.631   -0.853  1.00 16.58 ?  71   THR   A O    1 
ATOM   1723 C  CB   . THR   A 1 71  ? 43.299 3.921   1.986   1.00 16.68 ?  71   THR   A CB   1 
ATOM   1724 O  OG1  . THR   A 1 71  ? 43.552 5.048   2.831   1.00 18.28 ?  71   THR   A OG1  1 
ATOM   1725 C  CG2  . THR   A 1 71  ? 44.304 2.803   2.280   1.00 18.22 ?  71   THR   A CG2  1 
ATOM   1726 H  H    . THR   A 1 71  ? 41.627 5.253   0.789   1.00 15.43 ?  71   THR   A H    1 
ATOM   1727 H  HA   . THR   A 1 71  ? 44.225 4.771   0.360   1.00 17.06 ?  71   THR   A HA   1 
ATOM   1728 H  HB   . THR   A 1 71  ? 42.411 3.576   2.171   1.00 20.03 ?  71   THR   A HB   1 
ATOM   1729 H  HG1  . THR   A 1 71  ? 42.975 5.637   2.695   1.00 21.96 ?  71   THR   A HG1  1 
ATOM   1730 H  HG21 . THR   A 1 71  ? 44.441 2.728   3.238   1.00 21.88 ?  71   THR   A HG21 1 
ATOM   1731 H  HG22 . THR   A 1 71  ? 43.975 1.954   1.944   1.00 21.88 ?  71   THR   A HG22 1 
ATOM   1732 H  HG23 . THR   A 1 71  ? 45.155 3.001   1.858   1.00 21.88 ?  71   THR   A HG23 1 
ATOM   1733 N  N    . ASN   A 1 72  ? 42.024 2.635   -0.560  1.00 13.24 ?  72   ASN   A N    1 
ATOM   1734 C  CA   . ASN   A 1 72  ? 41.807 1.308   -1.120  1.00 13.71 ?  72   ASN   A CA   1 
ATOM   1735 C  C    . ASN   A 1 72  ? 41.183 1.299   -2.504  1.00 13.71 ?  72   ASN   A C    1 
ATOM   1736 O  O    . ASN   A 1 72  ? 41.197 0.248   -3.158  1.00 14.91 ?  72   ASN   A O    1 
ATOM   1737 C  CB   . ASN   A 1 72  ? 40.920 0.484   -0.178  1.00 14.67 ?  72   ASN   A CB   1 
ATOM   1738 C  CG   . ASN   A 1 72  ? 41.533 0.333   1.190   1.00 15.75 ?  72   ASN   A CG   1 
ATOM   1739 O  OD1  . ASN   A 1 72  ? 41.073 0.926   2.165   1.00 17.48 ?  72   ASN   A OD1  1 
ATOM   1740 N  ND2  . ASN   A 1 72  ? 42.597 -0.436  1.267   1.00 16.39 ?  72   ASN   A ND2  1 
ATOM   1741 H  H    . ASN   A 1 72  ? 41.287 3.058   -0.379  1.00 15.90 ?  72   ASN   A H    1 
ATOM   1742 H  HA   . ASN   A 1 72  ? 42.659 0.862   -1.188  1.00 16.46 ?  72   ASN   A HA   1 
ATOM   1743 H  HB2  . ASN   A 1 72  ? 40.061 0.921   -0.080  1.00 17.62 ?  72   ASN   A HB2  1 
ATOM   1744 H  HB3  . ASN   A 1 72  ? 40.802 -0.405  -0.552  1.00 17.62 ?  72   ASN   A HB3  1 
ATOM   1745 H  HD21 . ASN   A 1 72  ? 42.990 -0.549  2.025   1.00 19.69 ?  72   ASN   A HD21 1 
ATOM   1746 H  HD22 . ASN   A 1 72  ? 42.898 -0.828  0.565   1.00 19.69 ?  72   ASN   A HD22 1 
ATOM   1747 N  N    . GLY   A 1 73  ? 40.632 2.413   -2.964  1.00 13.28 ?  73   GLY   A N    1 
ATOM   1748 C  CA   . GLY   A 1 73  ? 39.893 2.427   -4.202  1.00 13.14 ?  73   GLY   A CA   1 
ATOM   1749 C  C    . GLY   A 1 73  ? 38.502 1.849   -4.031  1.00 12.45 ?  73   GLY   A C    1 
ATOM   1750 O  O    . GLY   A 1 73  ? 38.116 1.396   -2.946  1.00 12.86 ?  73   GLY   A O    1 
ATOM   1751 H  H    . GLY   A 1 73  ? 40.677 3.188   -2.576  1.00 15.95 ?  73   GLY   A H    1 
ATOM   1752 H  HA2  . GLY   A 1 73  ? 39.814 3.344   -4.522  1.00 15.78 ?  73   GLY   A HA2  1 
ATOM   1753 H  HA3  . GLY   A 1 73  ? 40.367 1.911   -4.870  1.00 15.78 ?  73   GLY   A HA3  1 
ATOM   1754 N  N    . PRO   A 1 74  ? 37.720 1.864   -5.110  1.00 12.85 ?  74   PRO   A N    1 
ATOM   1755 C  CA   . PRO   A 1 74  ? 36.325 1.424   -5.025  1.00 13.01 ?  74   PRO   A CA   1 
ATOM   1756 C  C    . PRO   A 1 74  ? 36.179 -0.059  -4.709  1.00 12.31 ?  74   PRO   A C    1 
ATOM   1757 O  O    . PRO   A 1 74  ? 37.051 -0.886  -4.997  1.00 13.51 ?  74   PRO   A O    1 
ATOM   1758 C  CB   . PRO   A 1 74  ? 35.769 1.730   -6.422  1.00 14.42 ?  74   PRO   A CB   1 
ATOM   1759 C  CG   . PRO   A 1 74  ? 36.706 2.738   -7.013  1.00 17.29 ?  74   PRO   A CG   1 
ATOM   1760 C  CD   . PRO   A 1 74  ? 38.049 2.390   -6.445  1.00 14.67 ?  74   PRO   A CD   1 
ATOM   1761 H  HA   . PRO   A 1 74  ? 35.844 1.947   -4.359  1.00 15.63 ?  74   PRO   A HA   1 
ATOM   1762 H  HB2  . PRO   A 1 74  ? 35.753 0.918   -6.949  1.00 17.32 ?  74   PRO   A HB2  1 
ATOM   1763 H  HB3  . PRO   A 1 74  ? 34.872 2.101   -6.339  1.00 17.32 ?  74   PRO   A HB3  1 
ATOM   1764 H  HG2  . PRO   A 1 74  ? 36.710 2.656   -7.978  1.00 20.76 ?  74   PRO   A HG2  1 
ATOM   1765 H  HG3  . PRO   A 1 74  ? 36.442 3.631   -6.742  1.00 20.76 ?  74   PRO   A HG3  1 
ATOM   1766 H  HD2  . PRO   A 1 74  ? 38.481 1.704   -6.983  1.00 17.62 ?  74   PRO   A HD2  1 
ATOM   1767 H  HD3  . PRO   A 1 74  ? 38.602 3.186   -6.380  1.00 17.62 ?  74   PRO   A HD3  1 
ATOM   1768 N  N    . LEU   A 1 75  ? 35.038 -0.385  -4.113  1.00 11.72 ?  75   LEU   A N    1 
ATOM   1769 C  CA   . LEU   A 1 75  ? 34.652 -1.775  -3.953  1.00 11.51 ?  75   LEU   A CA   1 
ATOM   1770 C  C    . LEU   A 1 75  ? 34.269 -2.368  -5.309  1.00 11.78 ?  75   LEU   A C    1 
ATOM   1771 O  O    . LEU   A 1 75  ? 34.115 -1.662  -6.308  1.00 13.57 ?  75   LEU   A O    1 
ATOM   1772 C  CB   . LEU   A 1 75  ? 33.460 -1.900  -3.006  1.00 11.34 ?  75   LEU   A CB   1 
ATOM   1773 C  CG   . LEU   A 1 75  ? 33.675 -1.491  -1.552  1.00 13.03 ?  75   LEU   A CG   1 
ATOM   1774 C  CD1  . LEU   A 1 75  ? 32.388 -1.682  -0.756  1.00 14.81 ?  75   LEU   A CD1  1 
ATOM   1775 C  CD2  . LEU   A 1 75  ? 34.807 -2.230  -0.904  1.00 16.48 ?  75   LEU   A CD2  1 
ATOM   1776 H  H    . LEU   A 1 75  ? 34.469 0.180   -3.803  1.00 14.08 ?  75   LEU   A H    1 
ATOM   1777 H  HA   . LEU   A 1 75  ? 35.397 -2.279  -3.594  1.00 13.82 ?  75   LEU   A HA   1 
ATOM   1778 H  HB2  . LEU   A 1 75  ? 32.740 -1.354  -3.353  1.00 13.62 ?  75   LEU   A HB2  1 
ATOM   1779 H  HB3  . LEU   A 1 75  ? 33.179 -2.831  -3.002  1.00 13.62 ?  75   LEU   A HB3  1 
ATOM   1780 H  HG   . LEU   A 1 75  ? 33.900 -0.548  -1.531  1.00 15.66 ?  75   LEU   A HG   1 
ATOM   1781 H  HD11 . LEU   A 1 75  ? 32.544 -1.413  0.162   1.00 17.78 ?  75   LEU   A HD11 1 
ATOM   1782 H  HD12 . LEU   A 1 75  ? 31.694 -1.129  -1.150  1.00 17.78 ?  75   LEU   A HD12 1 
ATOM   1783 H  HD13 . LEU   A 1 75  ? 32.130 -2.614  -0.791  1.00 17.78 ?  75   LEU   A HD13 1 
ATOM   1784 H  HD21 . LEU   A 1 75  ? 34.849 -1.988  0.034   1.00 19.79 ?  75   LEU   A HD21 1 
ATOM   1785 H  HD22 . LEU   A 1 75  ? 34.658 -3.184  -0.993  1.00 19.79 ?  75   LEU   A HD22 1 
ATOM   1786 H  HD23 . LEU   A 1 75  ? 35.642 -1.987  -1.342  1.00 19.79 ?  75   LEU   A HD23 1 
ATOM   1787 N  N    . LYS   A 1 76  ? 34.119 -3.691  -5.326  1.00 11.96 ?  76   LYS   A N    1 
ATOM   1788 C  CA   . LYS   A 1 76  ? 33.531 -4.413  -6.446  1.00 12.30 ?  76   LYS   A CA   1 
ATOM   1789 C  C    . LYS   A 1 76  ? 32.018 -4.495  -6.264  1.00 11.22 ?  76   LYS   A C    1 
ATOM   1790 O  O    . LYS   A 1 76  ? 31.526 -4.604  -5.142  1.00 11.37 ?  76   LYS   A O    1 
ATOM   1791 C  CB   . LYS   A 1 76  ? 34.080 -5.848  -6.482  1.00 13.97 ?  76   LYS   A CB   1 
ATOM   1792 C  CG   . LYS   A 1 76  ? 35.590 -5.954  -6.693  1.00 15.26 ?  76   LYS   A CG   1 
ATOM   1793 C  CD   . LYS   A 1 76  ? 36.113 -7.355  -6.455  1.00 16.65 ?  76   LYS   A CD   1 
ATOM   1794 C  CE   . LYS   A 1 76  ? 37.611 -7.423  -6.668  1.00 19.44 ?  76   LYS   A CE   1 
ATOM   1795 N  NZ   . LYS   A 1 76  ? 38.145 -8.780  -6.445  1.00 20.73 ?  76   LYS   A NZ   1 
ATOM   1796 H  H    . LYS   A 1 76  ? 34.358 -4.205  -4.675  1.00 14.37 ?  76   LYS   A H    1 
ATOM   1797 H  HA   . LYS   A 1 76  ? 33.738 -3.967  -7.282  1.00 14.77 ?  76   LYS   A HA   1 
ATOM   1798 H  HB2  . LYS   A 1 76  ? 33.872 -6.281  -5.641  1.00 16.78 ?  76   LYS   A HB2  1 
ATOM   1799 H  HB3  . LYS   A 1 76  ? 33.650 -6.324  -7.210  1.00 16.78 ?  76   LYS   A HB3  1 
ATOM   1800 H  HG2  . LYS   A 1 76  ? 35.801 -5.704  -7.608  1.00 18.33 ?  76   LYS   A HG2  1 
ATOM   1801 H  HG3  . LYS   A 1 76  ? 36.040 -5.356  -6.075  1.00 18.33 ?  76   LYS   A HG3  1 
ATOM   1802 H  HD2  . LYS   A 1 76  ? 35.917 -7.618  -5.542  1.00 20.00 ?  76   LYS   A HD2  1 
ATOM   1803 H  HD3  . LYS   A 1 76  ? 35.683 -7.965  -7.079  1.00 20.00 ?  76   LYS   A HD3  1 
ATOM   1804 H  HE2  . LYS   A 1 76  ? 37.811 -7.167  -7.580  1.00 23.35 ?  76   LYS   A HE2  1 
ATOM   1805 H  HE3  . LYS   A 1 76  ? 38.045 -6.825  -6.045  1.00 23.35 ?  76   LYS   A HE3  1 
ATOM   1806 H  HZ1  . LYS   A 1 76  ? 39.023 -8.794  -6.579  1.00 24.90 ?  76   LYS   A HZ1  1 
ATOM   1807 H  HZ2  . LYS   A 1 76  ? 37.974 -9.049  -5.612  1.00 24.90 ?  76   LYS   A HZ2  1 
ATOM   1808 H  HZ3  . LYS   A 1 76  ? 37.762 -9.360  -7.011  1.00 24.90 ?  76   LYS   A HZ3  1 
ATOM   1809 N  N    . VAL   A 1 77  ? 31.277 -4.482  -7.375  1.00 11.68 ?  77   VAL   A N    1 
ATOM   1810 C  CA   . VAL   A 1 77  ? 29.869 -4.861  -7.292  1.00 11.51 ?  77   VAL   A CA   1 
ATOM   1811 C  C    . VAL   A 1 77  ? 29.803 -6.311  -6.841  1.00 11.04 ?  77   VAL   A C    1 
ATOM   1812 O  O    . VAL   A 1 77  ? 30.459 -7.183  -7.421  1.00 11.84 ?  77   VAL   A O    1 
ATOM   1813 C  CB   . VAL   A 1 77  ? 29.155 -4.656  -8.636  1.00 12.72 ?  77   VAL   A CB   1 
ATOM   1814 C  CG1  . VAL   A 1 77  ? 27.694 -5.085  -8.534  1.00 13.90 ?  77   VAL   A CG1  1 
ATOM   1815 C  CG2  . VAL   A 1 77  ? 29.259 -3.206  -9.072  1.00 14.13 ?  77   VAL   A CG2  1 
ATOM   1816 H  H    . VAL   A 1 77  ? 31.562 -4.270  -8.159  1.00 14.03 ?  77   VAL   A H    1 
ATOM   1817 H  HA   . VAL   A 1 77  ? 29.431 -4.312  -6.625  1.00 13.83 ?  77   VAL   A HA   1 
ATOM   1818 H  HB   . VAL   A 1 77  ? 29.588 -5.202  -9.312  1.00 15.28 ?  77   VAL   A HB   1 
ATOM   1819 H  HG11 . VAL   A 1 77  ? 27.229 -4.795  -9.332  1.00 16.69 ?  77   VAL   A HG11 1 
ATOM   1820 H  HG12 . VAL   A 1 77  ? 27.654 -6.050  -8.458  1.00 16.69 ?  77   VAL   A HG12 1 
ATOM   1821 H  HG13 . VAL   A 1 77  ? 27.302 -4.670  -7.751  1.00 16.69 ?  77   VAL   A HG13 1 
ATOM   1822 H  HG21 . VAL   A 1 77  ? 28.749 -3.088  -9.886  1.00 16.97 ?  77   VAL   A HG21 1 
ATOM   1823 H  HG22 . VAL   A 1 77  ? 28.899 -2.644  -8.368  1.00 16.97 ?  77   VAL   A HG22 1 
ATOM   1824 H  HG23 . VAL   A 1 77  ? 30.191 -2.989  -9.227  1.00 16.97 ?  77   VAL   A HG23 1 
ATOM   1825 N  N    . GLY   A 1 78  ? 29.020 -6.578  -5.791  1.00 10.90 ?  78   GLY   A N    1 
ATOM   1826 C  CA   . GLY   A 1 78  ? 28.998 -7.866  -5.132  1.00 11.32 ?  78   GLY   A CA   1 
ATOM   1827 C  C    . GLY   A 1 78  ? 29.906 -7.948  -3.923  1.00 10.97 ?  78   GLY   A C    1 
ATOM   1828 O  O    . GLY   A 1 78  ? 29.846 -8.944  -3.185  1.00 11.30 ?  78   GLY   A O    1 
ATOM   1829 H  H    . GLY   A 1 78  ? 28.474 -6.004  -5.448  1.00 13.10 ?  78   GLY   A H    1 
ATOM   1830 H  HA2  . GLY   A 1 78  ? 28.094 -8.060  -4.848  1.00 13.60 ?  78   GLY   A HA2  1 
ATOM   1831 H  HA3  . GLY   A 1 78  ? 29.271 -8.548  -5.767  1.00 13.60 ?  78   GLY   A HA3  1 
ATOM   1832 N  N    . GLY   A 1 79  ? 30.759 -6.942  -3.712  1.00 10.85 ?  79   GLY   A N    1 
ATOM   1833 C  CA   . GLY   A 1 79  ? 31.718 -6.946  -2.632  1.00 11.14 ?  79   GLY   A CA   1 
ATOM   1834 C  C    . GLY   A 1 79  ? 31.261 -6.150  -1.418  1.00 10.39 ?  79   GLY   A C    1 
ATOM   1835 O  O    . GLY   A 1 79  ? 30.141 -5.646  -1.346  1.00 11.02 ?  79   GLY   A O    1 
ATOM   1836 H  H    . GLY   A 1 79  ? 30.808 -6.236  -4.202  1.00 13.04 ?  79   GLY   A H    1 
ATOM   1837 H  HA2  . GLY   A 1 79  ? 31.881 -7.869  -2.353  1.00 13.38 ?  79   GLY   A HA2  1 
ATOM   1838 H  HA3  . GLY   A 1 79  ? 32.558 -6.578  -2.940  1.00 13.38 ?  79   GLY   A HA3  1 
ATOM   1839 N  N    . SER   A 1 80  ? 32.163 -6.055  -0.442  1.00 11.26 ?  80   SER   A N    1 
ATOM   1840 C  CA   . SER   A 1 80  ? 31.844 -5.424  0.829   1.00 10.64 ?  80   SER   A CA   1 
ATOM   1841 C  C    . SER   A 1 80  ? 33.110 -4.964  1.531   1.00 10.73 ?  80   SER   A C    1 
ATOM   1842 O  O    . SER   A 1 80  ? 34.224 -5.393  1.209   1.00 12.08 ?  80   SER   A O    1 
ATOM   1843 C  CB   . SER   A 1 80  ? 31.085 -6.379  1.760   1.00 11.64 ?  80   SER   A CB   1 
ATOM   1844 O  OG   . SER   A 1 80  ? 31.920 -7.426  2.232   1.00 13.47 ?  80   SER   A OG   1 
ATOM   1845 H  H    . SER   A 1 80  ? 32.972 -6.337  -0.501  1.00 13.53 ?  80   SER   A H    1 
ATOM   1846 H  HA   . SER   A 1 80  ? 31.288 -4.648  0.652   1.00 12.79 ?  80   SER   A HA   1 
ATOM   1847 H  HB2  . SER   A 1 80  ? 30.753 -5.874  2.519   1.00 13.99 ?  80   SER   A HB2  1 
ATOM   1848 H  HB3  . SER   A 1 80  ? 30.337 -6.762  1.271   1.00 13.99 ?  80   SER   A HB3  1 
ATOM   1849 H  HG   . SER   A 1 80  ? 32.206 -7.869  1.577   1.00 16.17 ?  80   SER   A HG   1 
ATOM   1850 N  N    . CYS   A 1 81  ? 32.911 -4.111  2.531   1.00 10.50 ?  81   CYS   A N    1 
ATOM   1851 C  CA   . CYS   A 1 81  ? 33.957 -3.822  3.500   1.00 10.71 ?  81   CYS   A CA   1 
ATOM   1852 C  C    . CYS   A 1 81  ? 33.317 -3.588  4.859   1.00 10.43 ?  81   CYS   A C    1 
ATOM   1853 O  O    . CYS   A 1 81  ? 32.152 -3.187  4.950   1.00 11.46 ?  81   CYS   A O    1 
ATOM   1854 C  CB   . CYS   A 1 81  ? 34.827 -2.633  3.082   1.00 11.53 ?  81   CYS   A CB   1 
ATOM   1855 S  SG   . CYS   A 1 81  ? 33.928 -1.052  3.086   1.00 11.45 ?  81   CYS   A SG   1 
ATOM   1856 H  H    . CYS   A 1 81  ? 32.173 -3.686  2.671   1.00 12.61 ?  81   CYS   A H    1 
ATOM   1857 H  HA   . CYS   A 1 81  ? 34.534 -4.591  3.573   1.00 12.87 ?  81   CYS   A HA   1 
ATOM   1858 H  HB2  . CYS   A 1 81  ? 35.574 -2.555  3.696   1.00 13.85 ?  81   CYS   A HB2  1 
ATOM   1859 H  HB3  . CYS   A 1 81  ? 35.160 -2.784  2.180   1.00 13.85 ?  81   CYS   A HB3  1 
ATOM   1860 H  HG   . CYS   A 1 81  ? 34.678 -0.175  2.750   1.00 13.76 ?  81   CYS   A HG   1 
ATOM   1861 N  N    . VAL   A 1 82  ? 34.087 -3.846  5.914   1.00 10.79 ?  82   VAL   A N    1 
ATOM   1862 C  CA   . VAL   A 1 82  ? 33.664 -3.599  7.286   1.00 11.27 ?  82   VAL   A CA   1 
ATOM   1863 C  C    . VAL   A 1 82  ? 34.260 -2.280  7.755   1.00 11.26 ?  82   VAL   A C    1 
ATOM   1864 O  O    . VAL   A 1 82  ? 35.483 -2.105  7.744   1.00 12.12 ?  82   VAL   A O    1 
ATOM   1865 C  CB   . VAL   A 1 82  ? 34.083 -4.738  8.229   1.00 12.79 ?  82   VAL   A CB   1 
ATOM   1866 C  CG1  . VAL   A 1 82  ? 33.618 -4.440  9.649   1.00 14.32 ?  82   VAL   A CG1  1 
ATOM   1867 C  CG2  . VAL   A 1 82  ? 33.530 -6.072  7.753   1.00 13.82 ?  82   VAL   A CG2  1 
ATOM   1868 H  H    . VAL   A 1 82  ? 34.878 -4.191  5.854   1.00 12.97 ?  82   VAL   A H    1 
ATOM   1869 H  HA   . VAL   A 1 82  ? 32.701 -3.520  7.312   1.00 13.54 ?  82   VAL   A HA   1 
ATOM   1870 H  HB   . VAL   A 1 82  ? 35.050 -4.799  8.239   1.00 15.36 ?  82   VAL   A HB   1 
ATOM   1871 H  HG11 . VAL   A 1 82  ? 33.707 -5.243  10.186  1.00 17.20 ?  82   VAL   A HG11 1 
ATOM   1872 H  HG12 . VAL   A 1 82  ? 34.162 -3.731  10.026  1.00 17.20 ?  82   VAL   A HG12 1 
ATOM   1873 H  HG13 . VAL   A 1 82  ? 32.685 -4.164  9.628   1.00 17.20 ?  82   VAL   A HG13 1 
ATOM   1874 H  HG21 . VAL   A 1 82  ? 33.772 -6.759  8.390   1.00 16.60 ?  82   VAL   A HG21 1 
ATOM   1875 H  HG22 . VAL   A 1 82  ? 32.563 -6.007  7.685   1.00 16.60 ?  82   VAL   A HG22 1 
ATOM   1876 H  HG23 . VAL   A 1 82  ? 33.907 -6.277  6.882   1.00 16.60 ?  82   VAL   A HG23 1 
ATOM   1877 N  N    . LEU   A 1 83  ? 33.401 -1.357  8.171   1.00 10.89 ?  83   LEU   A N    1 
ATOM   1878 C  CA   . LEU   A 1 83  ? 33.812 -0.087  8.750   1.00 10.91 ?  83   LEU   A CA   1 
ATOM   1879 C  C    . LEU   A 1 83  ? 33.091 0.095   10.080  1.00 10.93 ?  83   LEU   A C    1 
ATOM   1880 O  O    . LEU   A 1 83  ? 32.369 -0.793  10.545  1.00 11.66 ?  83   LEU   A O    1 
ATOM   1881 C  CB   . LEU   A 1 83  ? 33.567 1.072   7.770   1.00 11.41 ?  83   LEU   A CB   1 
ATOM   1882 C  CG   . LEU   A 1 83  ? 34.457 1.063   6.522   1.00 12.28 ?  83   LEU   A CG   1 
ATOM   1883 C  CD1  . LEU   A 1 83  ? 34.004 2.107   5.522   1.00 12.95 ?  83   LEU   A CD1  1 
ATOM   1884 C  CD2  . LEU   A 1 83  ? 35.924 1.284   6.886   1.00 13.05 ?  83   LEU   A CD2  1 
ATOM   1885 H  H    . LEU   A 1 83  ? 32.549 -1.445  8.121   1.00 13.08 ?  83   LEU   A H    1 
ATOM   1886 H  HA   . LEU   A 1 83  ? 34.763 -0.109  8.932   1.00 13.11 ?  83   LEU   A HA   1 
ATOM   1887 H  HB2  . LEU   A 1 83  ? 32.643 1.039   7.467   1.00 13.70 ?  83   LEU   A HB2  1 
ATOM   1888 H  HB3  . LEU   A 1 83  ? 33.721 1.915   8.228   1.00 13.70 ?  83   LEU   A HB3  1 
ATOM   1889 H  HG   . LEU   A 1 83  ? 34.385 0.196   6.096   1.00 14.75 ?  83   LEU   A HG   1 
ATOM   1890 H  HD11 . LEU   A 1 83  ? 34.581 2.069   4.743   1.00 15.56 ?  83   LEU   A HD11 1 
ATOM   1891 H  HD12 . LEU   A 1 83  ? 33.087 1.914   5.260   1.00 15.56 ?  83   LEU   A HD12 1 
ATOM   1892 H  HD13 . LEU   A 1 83  ? 34.054 2.982   5.932   1.00 15.56 ?  83   LEU   A HD13 1 
ATOM   1893 H  HD21 . LEU   A 1 83  ? 36.438 1.416   6.072   1.00 15.68 ?  83   LEU   A HD21 1 
ATOM   1894 H  HD22 . LEU   A 1 83  ? 35.996 2.074   7.448   1.00 15.68 ?  83   LEU   A HD22 1 
ATOM   1895 H  HD23 . LEU   A 1 83  ? 36.256 0.510   7.363   1.00 15.68 ?  83   LEU   A HD23 1 
ATOM   1896 N  N    . SER   A 1 84  ? 33.295 1.248   10.706  1.00 11.87 ?  84   SER   A N    1 
ATOM   1897 C  CA   . SER   A 1 84  ? 32.651 1.500   11.983  1.00 11.81 ?  84   SER   A CA   1 
ATOM   1898 C  C    . SER   A 1 84  ? 31.135 1.581   11.830  1.00 11.60 ?  84   SER   A C    1 
ATOM   1899 O  O    . SER   A 1 84  ? 30.614 2.041   10.815  1.00 11.74 ?  84   SER   A O    1 
ATOM   1900 C  CB   . SER   A 1 84  ? 33.146 2.823   12.554  1.00 13.20 ?  84   SER   A CB   1 
ATOM   1901 O  OG   . SER   A 1 84  ? 32.514 3.105   13.781  1.00 14.18 ?  84   SER   A OG   1 
ATOM   1902 H  H    . SER   A 1 84  ? 33.780 1.901   10.409  1.00 14.26 ?  84   SER   A H    1 
ATOM   1903 H  HA   . SER   A 1 84  ? 32.871 0.787   12.600  1.00 14.18 ?  84   SER   A HA   1 
ATOM   1904 H  HB2  . SER   A 1 84  ? 34.106 2.770   12.685  1.00 15.86 ?  84   SER   A HB2  1 
ATOM   1905 H  HB3  . SER   A 1 84  ? 32.937 3.534   11.928  1.00 15.86 ?  84   SER   A HB3  1 
ATOM   1906 H  HG   . SER   A 1 84  ? 32.806 3.829   14.094  1.00 17.03 ?  84   SER   A HG   1 
ATOM   1907 N  N    . GLY   A 1 85  ? 30.422 1.166   12.875  1.00 12.45 ?  85   GLY   A N    1 
ATOM   1908 C  CA   . GLY   A 1 85  ? 28.998 1.406   12.951  1.00 13.12 ?  85   GLY   A CA   1 
ATOM   1909 C  C    . GLY   A 1 85  ? 28.622 2.716   13.603  1.00 12.61 ?  85   GLY   A C    1 
ATOM   1910 O  O    . GLY   A 1 85  ? 27.433 3.030   13.716  1.00 13.02 ?  85   GLY   A O    1 
ATOM   1911 H  H    . GLY   A 1 85  ? 30.748 0.742   13.550  1.00 14.96 ?  85   GLY   A H    1 
ATOM   1912 H  HA2  . GLY   A 1 85  ? 28.630 1.396   12.053  1.00 15.76 ?  85   GLY   A HA2  1 
ATOM   1913 H  HA3  . GLY   A 1 85  ? 28.584 0.696   13.455  1.00 15.76 ?  85   GLY   A HA3  1 
ATOM   1914 N  N    . HIS   A 1 86  ? 29.603 3.496   14.042  1.00 12.44 ?  86   HIS   A N    1 
ATOM   1915 C  CA   . HIS   A 1 86  ? 29.374 4.832   14.605  1.00 12.92 ?  86   HIS   A CA   1 
ATOM   1916 C  C    . HIS   A 1 86  ? 28.386 4.713   15.759  1.00 13.45 ?  86   HIS   A C    1 
ATOM   1917 O  O    . HIS   A 1 86  ? 28.569 3.842   16.625  1.00 14.82 ?  86   HIS   A O    1 
ATOM   1918 C  CB   . HIS   A 1 86  ? 28.995 5.802   13.490  1.00 13.21 ?  86   HIS   A CB   1 
ATOM   1919 C  CG   . HIS   A 1 86  ? 30.054 5.907   12.451  1.00 12.96 ?  86   HIS   A CG   1 
ATOM   1920 N  ND1  . HIS   A 1 86  ? 31.142 6.744   12.588  1.00 14.48 ?  86   HIS   A ND1  1 
ATOM   1921 C  CD2  . HIS   A 1 86  ? 30.245 5.217   11.305  1.00 12.84 ?  86   HIS   A CD2  1 
ATOM   1922 C  CE1  . HIS   A 1 86  ? 31.941 6.584   11.549  1.00 14.45 ?  86   HIS   A CE1  1 
ATOM   1923 N  NE2  . HIS   A 1 86  ? 31.424 5.661   10.760  1.00 13.60 ?  86   HIS   A NE2  1 
ATOM   1924 H  H    . HIS   A 1 86  ? 30.429 3.279   14.028  1.00 14.95 ?  86   HIS   A H    1 
ATOM   1925 H  HA   . HIS   A 1 86  ? 30.210 5.154   14.973  1.00 15.52 ?  86   HIS   A HA   1 
ATOM   1926 H  HB2  . HIS   A 1 86  ? 28.179 5.499   13.058  1.00 15.87 ?  86   HIS   A HB2  1 
ATOM   1927 H  HB3  . HIS   A 1 86  ? 28.858 6.691   13.862  1.00 15.87 ?  86   HIS   A HB3  1 
ATOM   1928 H  HD2  . HIS   A 1 86  ? 29.684 4.561   10.947  1.00 15.43 ?  86   HIS   A HD2  1 
ATOM   1929 H  HE1  . HIS   A 1 86  ? 32.734 7.044   11.388  1.00 17.35 ?  86   HIS   A HE1  1 
ATOM   1930 H  HE2  . HIS   A 1 86  ? 31.764 5.387   10.009  1.00 16.33 ?  86   HIS   A HE2  1 
ATOM   1931 N  N    . ASN   A 1 87  ? 27.366 5.558   15.820  1.00 14.48 ?  87   ASN   A N    1 
ATOM   1932 C  CA   . ASN   A 1 87  ? 26.370 5.538   16.875  1.00 15.40 ?  87   ASN   A CA   1 
ATOM   1933 C  C    . ASN   A 1 87  ? 25.252 4.537   16.622  1.00 16.81 ?  87   ASN   A C    1 
ATOM   1934 O  O    . ASN   A 1 87  ? 24.323 4.466   17.429  1.00 19.07 ?  87   ASN   A O    1 
ATOM   1935 C  CB   . ASN   A 1 87  ? 25.761 6.939   17.038  1.00 16.37 ?  87   ASN   A CB   1 
ATOM   1936 C  CG   . ASN   A 1 87  ? 25.247 7.516   15.723  1.00 17.05 ?  87   ASN   A CG   1 
ATOM   1937 O  OD1  . ASN   A 1 87  ? 25.897 7.409   14.686  1.00 17.51 ?  87   ASN   A OD1  1 
ATOM   1938 N  ND2  . ASN   A 1 87  ? 24.079 8.135   15.766  1.00 18.30 ?  87   ASN   A ND2  1 
ATOM   1939 H  H    . ASN   A 1 87  ? 27.224 6.173   15.238  1.00 17.39 ?  87   ASN   A H    1 
ATOM   1940 H  HA   . ASN   A 1 87  ? 26.800 5.300   17.715  1.00 18.49 ?  87   ASN   A HA   1 
ATOM   1941 H  HB2  . ASN   A 1 87  ? 25.014 6.885   17.659  1.00 19.66 ?  87   ASN   A HB2  1 
ATOM   1942 H  HB3  . ASN   A 1 87  ? 26.438 7.536   17.387  1.00 19.66 ?  87   ASN   A HB3  1 
ATOM   1943 H  HD21 . ASN   A 1 87  ? 23.750 8.474   15.049  1.00 21.97 ?  87   ASN   A HD21 1 
ATOM   1944 H  HD22 . ASN   A 1 87  ? 23.653 8.199   16.509  1.00 21.97 ?  87   ASN   A HD22 1 
ATOM   1945 N  N    . LEU   A 1 88  ? 25.319 3.759   15.544  1.00 15.39 ?  88   LEU   A N    1 
ATOM   1946 C  CA   . LEU   A 1 88  ? 24.213 2.889   15.157  1.00 15.02 ?  88   LEU   A CA   1 
ATOM   1947 C  C    . LEU   A 1 88  ? 24.436 1.413   15.459  1.00 14.65 ?  88   LEU   A C    1 
ATOM   1948 O  O    . LEU   A 1 88  ? 23.462 0.670   15.613  1.00 16.01 ?  88   LEU   A O    1 
ATOM   1949 C  CB   . LEU   A 1 88  ? 23.950 3.042   13.658  1.00 15.66 ?  88   LEU   A CB   1 
ATOM   1950 C  CG   . LEU   A 1 88  ? 23.668 4.469   13.183  1.00 17.10 ?  88   LEU   A CG   1 
ATOM   1951 C  CD1  . LEU   A 1 88  ? 23.495 4.494   11.674  1.00 17.49 ?  88   LEU   A CD1  1 
ATOM   1952 C  CD2  . LEU   A 1 88  ? 22.440 5.064   13.871  1.00 19.03 ?  88   LEU   A CD2  1 
ATOM   1953 H  H    . LEU   A 1 88  ? 26.006 3.714   15.025  1.00 18.49 ?  88   LEU   A H    1 
ATOM   1954 H  HA   . LEU   A 1 88  ? 23.418 3.175   15.629  1.00 18.04 ?  88   LEU   A HA   1 
ATOM   1955 H  HB2  . LEU   A 1 88  ? 24.721 2.726   13.170  1.00 18.80 ?  88   LEU   A HB2  1 
ATOM   1956 H  HB3  . LEU   A 1 88  ? 23.174 2.508   13.427  1.00 18.80 ?  88   LEU   A HB3  1 
ATOM   1957 H  HG   . LEU   A 1 88  ? 24.429 5.032   13.399  1.00 20.53 ?  88   LEU   A HG   1 
ATOM   1958 H  HD11 . LEU   A 1 88  ? 23.321 5.407   11.388  1.00 21.01 ?  88   LEU   A HD11 1 
ATOM   1959 H  HD12 . LEU   A 1 88  ? 24.307 4.168   11.257  1.00 21.01 ?  88   LEU   A HD12 1 
ATOM   1960 H  HD13 . LEU   A 1 88  ? 22.747 3.926   11.432  1.00 21.01 ?  88   LEU   A HD13 1 
ATOM   1961 H  HD21 . LEU   A 1 88  ? 22.241 5.926   13.470  1.00 22.85 ?  88   LEU   A HD21 1 
ATOM   1962 H  HD22 . LEU   A 1 88  ? 21.693 4.462   13.754  1.00 22.85 ?  88   LEU   A HD22 1 
ATOM   1963 H  HD23 . LEU   A 1 88  ? 22.635 5.177   14.814  1.00 22.85 ?  88   LEU   A HD23 1 
ATOM   1964 N  N    . ALA   A 1 89  ? 25.686 0.974   15.528  1.00 14.07 ?  89   ALA   A N    1 
ATOM   1965 C  CA   . ALA   A 1 89  ? 26.042 -0.433  15.629  1.00 13.79 ?  89   ALA   A CA   1 
ATOM   1966 C  C    . ALA   A 1 89  ? 27.527 -0.475  15.944  1.00 14.30 ?  89   ALA   A C    1 
ATOM   1967 O  O    . ALA   A 1 89  ? 28.225 0.532   15.833  1.00 14.92 ?  89   ALA   A O    1 
ATOM   1968 C  CB   . ALA   A 1 89  ? 25.782 -1.143  14.301  1.00 13.28 ?  89   ALA   A CB   1 
ATOM   1969 H  H    . ALA   A 1 89  ? 26.369 1.497   15.510  1.00 16.90 ?  89   ALA   A H    1 
ATOM   1970 H  HA   . ALA   A 1 89  ? 25.538 -0.860  16.341  1.00 16.56 ?  89   ALA   A HA   1 
ATOM   1971 H  HB1  . ALA   A 1 89  ? 26.039 -2.074  14.386  1.00 15.95 ?  89   ALA   A HB1  1 
ATOM   1972 H  HB2  . ALA   A 1 89  ? 24.836 -1.080  14.085  1.00 15.95 ?  89   ALA   A HB2  1 
ATOM   1973 H  HB3  . ALA   A 1 89  ? 26.307 -0.716  13.606  1.00 15.95 ?  89   ALA   A HB3  1 
ATOM   1974 N  N    A LYS   A 1 90  ? 28.012 -1.649  16.342  0.62 14.45 ?  90   LYS   A N    1 
ATOM   1975 N  N    B LYS   A 1 90  ? 28.015 -1.651  16.331  0.38 14.97 ?  90   LYS   A N    1 
ATOM   1976 C  CA   A LYS   A 1 90  ? 29.455 -1.796  16.493  0.62 14.81 ?  90   LYS   A CA   1 
ATOM   1977 C  CA   B LYS   A 1 90  ? 29.459 -1.794  16.492  0.38 15.76 ?  90   LYS   A CA   1 
ATOM   1978 C  C    A LYS   A 1 90  ? 30.154 -1.617  15.148  0.62 14.21 ?  90   LYS   A C    1 
ATOM   1979 C  C    B LYS   A 1 90  ? 30.170 -1.636  15.153  0.38 14.64 ?  90   LYS   A C    1 
ATOM   1980 O  O    A LYS   A 1 90  ? 31.077 -0.799  15.010  0.62 15.51 ?  90   LYS   A O    1 
ATOM   1981 O  O    B LYS   A 1 90  ? 31.133 -0.866  15.031  0.38 15.60 ?  90   LYS   A O    1 
ATOM   1982 C  CB   A LYS   A 1 90  ? 29.794 -3.148  17.121  0.62 17.04 ?  90   LYS   A CB   1 
ATOM   1983 C  CB   B LYS   A 1 90  ? 29.799 -3.138  17.134  0.38 18.30 ?  90   LYS   A CB   1 
ATOM   1984 C  CG   A LYS   A 1 90  ? 31.276 -3.326  17.418  0.62 21.22 ?  90   LYS   A CG   1 
ATOM   1985 C  CG   B LYS   A 1 90  ? 31.283 -3.304  17.436  0.38 21.53 ?  90   LYS   A CG   1 
ATOM   1986 C  CD   A LYS   A 1 90  ? 31.517 -4.559  18.276  0.62 24.94 ?  90   LYS   A CD   1 
ATOM   1987 C  CD   B LYS   A 1 90  ? 31.548 -4.561  18.247  0.38 24.37 ?  90   LYS   A CD   1 
ATOM   1988 C  CE   A LYS   A 1 90  ? 32.931 -4.596  18.841  0.62 28.09 ?  90   LYS   A CE   1 
ATOM   1989 C  CE   B LYS   A 1 90  ? 32.940 -4.550  18.863  0.38 26.69 ?  90   LYS   A CE   1 
ATOM   1990 N  NZ   A LYS   A 1 90  ? 33.939 -5.047  17.842  0.62 30.08 ?  90   LYS   A NZ   1 
ATOM   1991 N  NZ   B LYS   A 1 90  ? 34.019 -4.671  17.845  0.38 28.08 ?  90   LYS   A NZ   1 
ATOM   1992 H  H    A LYS   A 1 90  ? 27.543 -2.342  16.526  0.62 17.36 ?  90   LYS   A H    1 
ATOM   1993 H  H    B LYS   A 1 90  ? 27.548 -2.348  16.505  0.38 17.98 ?  90   LYS   A H    1 
ATOM   1994 H  HA   A LYS   A 1 90  ? 29.780 -1.103  17.086  0.62 17.79 ?  90   LYS   A HA   1 
ATOM   1995 H  HA   B LYS   A 1 90  ? 29.779 -1.093  17.079  0.38 18.92 ?  90   LYS   A HA   1 
ATOM   1996 H  HB2  A LYS   A 1 90  ? 29.308 -3.232  17.959  0.62 20.46 ?  90   LYS   A HB2  1 
ATOM   1997 H  HB2  B LYS   A 1 90  ? 29.312 -3.217  17.969  0.38 21.97 ?  90   LYS   A HB2  1 
ATOM   1998 H  HB3  A LYS   A 1 90  ? 29.522 -3.853  16.514  0.62 20.46 ?  90   LYS   A HB3  1 
ATOM   1999 H  HB3  B LYS   A 1 90  ? 29.535 -3.850  16.530  0.38 21.97 ?  90   LYS   A HB3  1 
ATOM   2000 H  HG2  A LYS   A 1 90  ? 31.761 -3.434  16.585  0.62 25.48 ?  90   LYS   A HG2  1 
ATOM   2001 H  HG2  B LYS   A 1 90  ? 31.776 -3.371  16.602  0.38 25.86 ?  90   LYS   A HG2  1 
ATOM   2002 H  HG3  A LYS   A 1 90  ? 31.604 -2.550  17.900  0.62 25.48 ?  90   LYS   A HG3  1 
ATOM   2003 H  HG3  B LYS   A 1 90  ? 31.594 -2.540  17.947  0.38 25.86 ?  90   LYS   A HG3  1 
ATOM   2004 H  HD2  A LYS   A 1 90  ? 30.894 -4.556  19.021  0.62 29.95 ?  90   LYS   A HD2  1 
ATOM   2005 H  HD2  B LYS   A 1 90  ? 30.898 -4.620  18.965  0.38 29.26 ?  90   LYS   A HD2  1 
ATOM   2006 H  HD3  A LYS   A 1 90  ? 31.386 -5.355  17.736  0.62 29.95 ?  90   LYS   A HD3  1 
ATOM   2007 H  HD3  B LYS   A 1 90  ? 31.477 -5.336  17.668  0.38 29.26 ?  90   LYS   A HD3  1 
ATOM   2008 H  HE2  A LYS   A 1 90  ? 33.178 -3.705  19.135  0.62 33.72 ?  90   LYS   A HE2  1 
ATOM   2009 H  HE2  B LYS   A 1 90  ? 33.069 -3.715  19.339  0.38 32.04 ?  90   LYS   A HE2  1 
ATOM   2010 H  HE3  A LYS   A 1 90  ? 32.956 -5.211  19.591  0.62 33.72 ?  90   LYS   A HE3  1 
ATOM   2011 H  HE3  B LYS   A 1 90  ? 33.020 -5.297  19.476  0.38 32.04 ?  90   LYS   A HE3  1 
ATOM   2012 H  HZ1  A LYS   A 1 90  ? 34.740 -5.114  18.227  0.62 36.12 ?  90   LYS   A HZ1  1 
ATOM   2013 H  HZ1  B LYS   A 1 90  ? 34.815 -4.661  18.243  0.38 33.71 ?  90   LYS   A HZ1  1 
ATOM   2014 H  HZ2  A LYS   A 1 90  ? 33.709 -5.841  17.514  0.62 36.12 ?  90   LYS   A HZ2  1 
ATOM   2015 H  HZ2  B LYS   A 1 90  ? 33.930 -5.436  17.398  0.38 33.71 ?  90   LYS   A HZ2  1 
ATOM   2016 H  HZ3  A LYS   A 1 90  ? 33.989 -4.461  17.174  0.62 36.12 ?  90   LYS   A HZ3  1 
ATOM   2017 H  HZ3  B LYS   A 1 90  ? 33.973 -3.994  17.271  0.38 33.71 ?  90   LYS   A HZ3  1 
ATOM   2018 N  N    . HIS   A 1 91  ? 29.693 -2.347  14.133  1.00 13.02 ?  91   HIS   A N    1 
ATOM   2019 C  CA   . HIS   A 1 91  ? 30.275 -2.325  12.805  1.00 12.19 ?  91   HIS   A CA   1 
ATOM   2020 C  C    . HIS   A 1 91  ? 29.186 -2.065  11.779  1.00 11.13 ?  91   HIS   A C    1 
ATOM   2021 O  O    . HIS   A 1 91  ? 28.021 -2.437  11.967  1.00 11.88 ?  91   HIS   A O    1 
ATOM   2022 C  CB   . HIS   A 1 91  ? 30.880 -3.686  12.448  1.00 14.51 ?  91   HIS   A CB   1 
ATOM   2023 C  CG   . HIS   A 1 91  ? 31.857 -4.201  13.455  1.00 18.14 ?  91   HIS   A CG   1 
ATOM   2024 N  ND1  . HIS   A 1 91  ? 33.133 -3.698  13.575  1.00 20.48 ?  91   HIS   A ND1  1 
ATOM   2025 C  CD2  . HIS   A 1 91  ? 31.753 -5.187  14.376  1.00 20.32 ?  91   HIS   A CD2  1 
ATOM   2026 C  CE1  . HIS   A 1 91  ? 33.772 -4.347  14.534  1.00 21.58 ?  91   HIS   A CE1  1 
ATOM   2027 N  NE2  . HIS   A 1 91  ? 32.956 -5.258  15.035  1.00 21.80 ?  91   HIS   A NE2  1 
ATOM   2028 H  H    A HIS   A 1 91  ? 29.017 -2.886  14.199  0.62 15.64 ?  91   HIS   A H    1 
ATOM   2029 H  H    B HIS   A 1 91  ? 29.011 -2.878  14.198  0.38 15.64 ?  91   HIS   A H    1 
ATOM   2030 H  HA   . HIS   A 1 91  ? 30.955 -1.644  12.738  1.00 14.65 ?  91   HIS   A HA   1 
ATOM   2031 H  HB2  . HIS   A 1 91  ? 30.165 -4.338  12.373  1.00 17.43 ?  91   HIS   A HB2  1 
ATOM   2032 H  HB3  . HIS   A 1 91  ? 31.341 -3.608  11.598  1.00 17.43 ?  91   HIS   A HB3  1 
ATOM   2033 H  HD1  . HIS   A 1 91  ? 33.465 -3.058  13.099  1.00 24.59 ?  91   HIS   A HD1  1 
ATOM   2034 H  HD2  . HIS   A 1 91  ? 31.008 -5.715  14.535  1.00 24.40 ?  91   HIS   A HD2  1 
ATOM   2035 H  HE1  . HIS   A 1 91  ? 34.650 -4.185  14.805  1.00 25.92 ?  91   HIS   A HE1  1 
ATOM   2036 N  N    . CYS   A 1 92  ? 29.590 -1.460  10.665  1.00 10.96 ?  92   CYS   A N    1 
ATOM   2037 C  CA   . CYS   A 1 92  ? 28.762 -1.387  9.470   1.00 10.82 ?  92   CYS   A CA   1 
ATOM   2038 C  C    . CYS   A 1 92  ? 29.409 -2.211  8.366   1.00 10.29 ?  92   CYS   A C    1 
ATOM   2039 O  O    . CYS   A 1 92  ? 30.564 -1.960  7.992   1.00 11.19 ?  92   CYS   A O    1 
ATOM   2040 C  CB   . CYS   A 1 92  ? 28.544 0.053   9.002   1.00 11.22 ?  92   CYS   A CB   1 
ATOM   2041 S  SG   . CYS   A 1 92  ? 27.526 0.148   7.493   1.00 10.78 ?  92   CYS   A SG   1 
ATOM   2042 H  H    . CYS   A 1 92  ? 30.358 -1.071  10.576  1.00 13.17 ?  92   CYS   A H    1 
ATOM   2043 H  HA   . CYS   A 1 92  ? 27.896 -1.768  9.663   1.00 13.00 ?  92   CYS   A HA   1 
ATOM   2044 H  HB2  . CYS   A 1 92  ? 28.092 0.553   9.700   1.00 13.48 ?  92   CYS   A HB2  1 
ATOM   2045 H  HB3  . CYS   A 1 92  ? 29.404 0.462   8.806   1.00 13.48 ?  92   CYS   A HB3  1 
ATOM   2046 H  HG   . CYS   A 1 92  ? 27.382 1.298   7.190   1.00 12.96 ?  92   CYS   A HG   1 
ATOM   2047 N  N    . LEU   A 1 93  ? 28.672 -3.197  7.867   1.00 10.15 ?  93   LEU   A N    1 
ATOM   2048 C  CA   . LEU   A 1 93  ? 29.079 -3.963  6.695   1.00 9.90  ?  93   LEU   A CA   1 
ATOM   2049 C  C    . LEU   A 1 93  ? 28.484 -3.277  5.469   1.00 9.65  ?  93   LEU   A C    1 
ATOM   2050 O  O    . LEU   A 1 93  ? 27.270 -3.343  5.238   1.00 9.67  ?  93   LEU   A O    1 
ATOM   2051 C  CB   . LEU   A 1 93  ? 28.611 -5.414  6.814   1.00 10.42 ?  93   LEU   A CB   1 
ATOM   2052 C  CG   . LEU   A 1 93  ? 28.994 -6.304  5.636   1.00 10.55 ?  93   LEU   A CG   1 
ATOM   2053 C  CD1  . LEU   A 1 93  ? 30.504 -6.551  5.619   1.00 11.65 ?  93   LEU   A CD1  1 
ATOM   2054 C  CD2  . LEU   A 1 93  ? 28.237 -7.636  5.674   1.00 11.73 ?  93   LEU   A CD2  1 
ATOM   2055 H  H    . LEU   A 1 93  ? 27.915 -3.443  8.204   1.00 12.19 ?  93   LEU   A H    1 
ATOM   2056 H  HA   . LEU   A 1 93  ? 30.043 -3.946  6.626   1.00 11.89 ?  93   LEU   A HA   1 
ATOM   2057 H  HB2  . LEU   A 1 93  ? 29.001 -5.795  7.620   1.00 12.52 ?  93   LEU   A HB2  1 
ATOM   2058 H  HB3  . LEU   A 1 93  ? 27.645 -5.421  6.890   1.00 12.52 ?  93   LEU   A HB3  1 
ATOM   2059 H  HG   . LEU   A 1 93  ? 28.765 -5.856  4.814   1.00 12.67 ?  93   LEU   A HG   1 
ATOM   2060 H  HD11 . LEU   A 1 93  ? 30.718 -7.162  4.899   1.00 14.00 ?  93   LEU   A HD11 1 
ATOM   2061 H  HD12 . LEU   A 1 93  ? 30.965 -5.706  5.485   1.00 14.00 ?  93   LEU   A HD12 1 
ATOM   2062 H  HD13 . LEU   A 1 93  ? 30.775 -6.938  6.470   1.00 14.00 ?  93   LEU   A HD13 1 
ATOM   2063 H  HD21 . LEU   A 1 93  ? 28.514 -8.175  4.914   1.00 14.09 ?  93   LEU   A HD21 1 
ATOM   2064 H  HD22 . LEU   A 1 93  ? 28.453 -8.101  6.499   1.00 14.09 ?  93   LEU   A HD22 1 
ATOM   2065 H  HD23 . LEU   A 1 93  ? 27.288 -7.460  5.629   1.00 14.09 ?  93   LEU   A HD23 1 
ATOM   2066 N  N    . HIS   A 1 94  ? 29.332 -2.582  4.708   1.00 9.49  ?  94   HIS   A N    1 
ATOM   2067 C  CA   . HIS   A 1 94  ? 28.912 -1.915  3.480   1.00 9.52  ?  94   HIS   A CA   1 
ATOM   2068 C  C    . HIS   A 1 94  ? 28.925 -2.955  2.374   1.00 9.44  ?  94   HIS   A C    1 
ATOM   2069 O  O    . HIS   A 1 94  ? 29.995 -3.470  2.034   1.00 10.92 ?  94   HIS   A O    1 
ATOM   2070 C  CB   . HIS   A 1 94  ? 29.867 -0.769  3.148   1.00 9.88  ?  94   HIS   A CB   1 
ATOM   2071 C  CG   . HIS   A 1 94  ? 29.851 0.331   4.154   1.00 9.51  ?  94   HIS   A CG   1 
ATOM   2072 N  ND1  . HIS   A 1 94  ? 28.971 1.390   4.091   1.00 9.80  ?  94   HIS   A ND1  1 
ATOM   2073 C  CD2  . HIS   A 1 94  ? 30.587 0.506   5.274   1.00 10.26 ?  94   HIS   A CD2  1 
ATOM   2074 C  CE1  . HIS   A 1 94  ? 29.182 2.176   5.131   1.00 9.81  ?  94   HIS   A CE1  1 
ATOM   2075 N  NE2  . HIS   A 1 94  ? 30.157 1.663   5.862   1.00 10.47 ?  94   HIS   A NE2  1 
ATOM   2076 H  H    . HIS   A 1 94  ? 30.167 -2.480  4.890   1.00 11.40 ?  94   HIS   A H    1 
ATOM   2077 H  HA   . HIS   A 1 94  ? 28.011 -1.563  3.580   1.00 11.44 ?  94   HIS   A HA   1 
ATOM   2078 H  HB2  . HIS   A 1 94  ? 30.766 -1.117  3.101   1.00 11.87 ?  94   HIS   A HB2  1 
ATOM   2079 H  HB3  . HIS   A 1 94  ? 29.609 -0.388  2.294   1.00 11.87 ?  94   HIS   A HB3  1 
ATOM   2080 H  HD2  . HIS   A 1 94  ? 31.266 -0.045  5.585   1.00 12.33 ?  94   HIS   A HD2  1 
ATOM   2081 H  HE1  . HIS   A 1 94  ? 28.716 2.965   5.316   1.00 11.79 ?  94   HIS   A HE1  1 
ATOM   2082 H  HE2  . HIS   A 1 94  ? 30.472 2.015   6.584   1.00 12.58 ?  94   HIS   A HE2  1 
ATOM   2083 N  N    . VAL   A 1 95  ? 27.758 -3.275  1.814   1.00 8.87  ?  95   VAL   A N    1 
ATOM   2084 C  CA   . VAL   A 1 95  ? 27.626 -4.315  0.796   1.00 9.43  ?  95   VAL   A CA   1 
ATOM   2085 C  C    . VAL   A 1 95  ? 27.080 -3.690  -0.472  1.00 9.17  ?  95   VAL   A C    1 
ATOM   2086 O  O    . VAL   A 1 95  ? 26.069 -2.978  -0.425  1.00 9.90  ?  95   VAL   A O    1 
ATOM   2087 C  CB   . VAL   A 1 95  ? 26.702 -5.462  1.253   1.00 10.05 ?  95   VAL   A CB   1 
ATOM   2088 C  CG1  . VAL   A 1 95  ? 26.600 -6.512  0.156   1.00 10.65 ?  95   VAL   A CG1  1 
ATOM   2089 C  CG2  . VAL   A 1 95  ? 27.197 -6.069  2.548   1.00 10.07 ?  95   VAL   A CG2  1 
ATOM   2090 H  H    . VAL   A 1 95  ? 27.006 -2.904  2.024   1.00 10.66 ?  95   VAL   A H    1 
ATOM   2091 H  HA   . VAL   A 1 95  ? 28.495 -4.688  0.603   1.00 11.33 ?  95   VAL   A HA   1 
ATOM   2092 H  HB   . VAL   A 1 95  ? 25.813 -5.113  1.411   1.00 12.07 ?  95   VAL   A HB   1 
ATOM   2093 H  HG11 . VAL   A 1 95  ? 26.211 -7.323  0.527   1.00 12.80 ?  95   VAL   A HG11 1 
ATOM   2094 H  HG12 . VAL   A 1 95  ? 26.034 -6.178  -0.558  1.00 12.80 ?  95   VAL   A HG12 1 
ATOM   2095 H  HG13 . VAL   A 1 95  ? 27.488 -6.704  -0.186  1.00 12.80 ?  95   VAL   A HG13 1 
ATOM   2096 H  HG21 . VAL   A 1 95  ? 26.642 -6.831  2.770   1.00 12.10 ?  95   VAL   A HG21 1 
ATOM   2097 H  HG22 . VAL   A 1 95  ? 28.117 -6.351  2.427   1.00 12.10 ?  95   VAL   A HG22 1 
ATOM   2098 H  HG23 . VAL   A 1 95  ? 27.142 -5.400  3.245   1.00 12.10 ?  95   VAL   A HG23 1 
ATOM   2099 N  N    . VAL   A 1 96  ? 27.717 -3.981  -1.606  1.00 9.29  ?  96   VAL   A N    1 
ATOM   2100 C  CA   . VAL   A 1 96  ? 27.304 -3.436  -2.895  1.00 10.11 ?  96   VAL   A CA   1 
ATOM   2101 C  C    . VAL   A 1 96  ? 26.508 -4.494  -3.652  1.00 10.26 ?  96   VAL   A C    1 
ATOM   2102 O  O    . VAL   A 1 96  ? 27.077 -5.438  -4.210  1.00 11.09 ?  96   VAL   A O    1 
ATOM   2103 C  CB   . VAL   A 1 96  ? 28.497 -2.963  -3.723  1.00 10.42 ?  96   VAL   A CB   1 
ATOM   2104 C  CG1  . VAL   A 1 96  ? 27.995 -2.338  -5.006  1.00 10.67 ?  96   VAL   A CG1  1 
ATOM   2105 C  CG2  . VAL   A 1 96  ? 29.350 -1.983  -2.941  1.00 10.96 ?  96   VAL   A CG2  1 
ATOM   2106 H  H    . VAL   A 1 96  ? 28.409 -4.494  -1.649  1.00 11.16 ?  96   VAL   A H    1 
ATOM   2107 H  HA   . VAL   A 1 96  ? 26.724 -2.674  -2.743  1.00 12.14 ?  96   VAL   A HA   1 
ATOM   2108 H  HB   . VAL   A 1 96  ? 29.046 -3.721  -3.954  1.00 12.52 ?  96   VAL   A HB   1 
ATOM   2109 H  HG11 . VAL   A 1 96  ? 28.729 -1.862  -5.427  1.00 12.82 ?  96   VAL   A HG11 1 
ATOM   2110 H  HG12 . VAL   A 1 96  ? 27.671 -3.033  -5.594  1.00 12.82 ?  96   VAL   A HG12 1 
ATOM   2111 H  HG13 . VAL   A 1 96  ? 27.280 -1.715  -4.796  1.00 12.82 ?  96   VAL   A HG13 1 
ATOM   2112 H  HG21 . VAL   A 1 96  ? 30.053 -1.643  -3.516  1.00 13.17 ?  96   VAL   A HG21 1 
ATOM   2113 H  HG22 . VAL   A 1 96  ? 28.791 -1.246  -2.636  1.00 13.17 ?  96   VAL   A HG22 1 
ATOM   2114 H  HG23 . VAL   A 1 96  ? 29.736 -2.437  -2.176  1.00 13.17 ?  96   VAL   A HG23 1 
ATOM   2115 N  N    . GLY   A 1 97  ? 25.187 -4.339  -3.692  1.00 10.17 ?  97   GLY   A N    1 
ATOM   2116 C  CA   . GLY   A 1 97  ? 24.378 -5.109  -4.600  1.00 10.65 ?  97   GLY   A CA   1 
ATOM   2117 C  C    . GLY   A 1 97  ? 24.401 -4.478  -5.979  1.00 11.01 ?  97   GLY   A C    1 
ATOM   2118 O  O    . GLY   A 1 97  ? 24.684 -3.284  -6.128  1.00 11.80 ?  97   GLY   A O    1 
ATOM   2119 H  H    . GLY   A 1 97  ? 24.738 -3.792  -3.196  1.00 12.21 ?  97   GLY   A H    1 
ATOM   2120 H  HA2  . GLY   A 1 97  ? 24.724 -6.014  -4.641  1.00 12.80 ?  97   GLY   A HA2  1 
ATOM   2121 H  HA3  . GLY   A 1 97  ? 23.458 -5.143  -4.281  1.00 12.80 ?  97   GLY   A HA3  1 
ATOM   2122 N  N    A PRO   A 1 98  ? 24.025 -5.227  -7.011  0.62 11.16 ?  98   PRO   A N    1 
ATOM   2123 N  N    B PRO   A 1 98  ? 24.170 -5.294  -7.010  0.38 11.42 ?  98   PRO   A N    1 
ATOM   2124 C  CA   A PRO   A 1 98  ? 23.892 -4.613  -8.338  0.62 11.92 ?  98   PRO   A CA   1 
ATOM   2125 C  CA   B PRO   A 1 98  ? 24.169 -4.777  -8.384  0.38 11.95 ?  98   PRO   A CA   1 
ATOM   2126 C  C    A PRO   A 1 98  ? 22.793 -3.560  -8.355  0.62 12.01 ?  98   PRO   A C    1 
ATOM   2127 C  C    B PRO   A 1 98  ? 23.047 -3.775  -8.604  0.38 12.05 ?  98   PRO   A C    1 
ATOM   2128 O  O    A PRO   A 1 98  ? 21.727 -3.730  -7.757  0.62 11.76 ?  98   PRO   A O    1 
ATOM   2129 O  O    B PRO   A 1 98  ? 21.941 -3.916  -8.077  0.38 12.48 ?  98   PRO   A O    1 
ATOM   2130 C  CB   A PRO   A 1 98  ? 23.550 -5.799  -9.247  0.62 11.92 ?  98   PRO   A CB   1 
ATOM   2131 C  CB   B PRO   A 1 98  ? 23.970 -6.038  -9.237  0.38 11.84 ?  98   PRO   A CB   1 
ATOM   2132 C  CG   A PRO   A 1 98  ? 22.927 -6.811  -8.340  0.62 11.38 ?  98   PRO   A CG   1 
ATOM   2133 C  CG   B PRO   A 1 98  ? 23.347 -7.040  -8.307  0.38 12.43 ?  98   PRO   A CG   1 
ATOM   2134 C  CD   A PRO   A 1 98  ? 23.647 -6.653  -7.019  0.62 10.94 ?  98   PRO   A CD   1 
ATOM   2135 C  CD   B PRO   A 1 98  ? 23.962 -6.753  -6.971  0.38 11.59 ?  98   PRO   A CD   1 
ATOM   2136 H  HA   A PRO   A 1 98  ? 24.731 -4.220  -8.608  0.62 14.32 ?  98   PRO   A HA   1 
ATOM   2137 H  HA   B PRO   A 1 98  ? 25.026 -4.373  -8.597  0.38 14.35 ?  98   PRO   A HA   1 
ATOM   2138 H  HB2  A PRO   A 1 98  ? 22.917 -5.515  -9.926  0.62 14.32 ?  98   PRO   A HB2  1 
ATOM   2139 H  HB2  B PRO   A 1 98  ? 23.375 -5.842  -9.977  0.38 14.22 ?  98   PRO   A HB2  1 
ATOM   2140 H  HB3  A PRO   A 1 98  ? 24.358 -6.146  -9.648  0.62 14.32 ?  98   PRO   A HB3  1 
ATOM   2141 H  HB3  B PRO   A 1 98  ? 24.827 -6.361  -9.561  0.38 14.22 ?  98   PRO   A HB3  1 
ATOM   2142 H  HG2  A PRO   A 1 98  ? 21.981 -6.628  -8.240  0.62 13.67 ?  98   PRO   A HG2  1 
ATOM   2143 H  HG2  B PRO   A 1 98  ? 22.385 -6.909  -8.276  0.38 14.93 ?  98   PRO   A HG2  1 
ATOM   2144 H  HG3  A PRO   A 1 98  ? 23.067 -7.702  -8.701  0.62 13.67 ?  98   PRO   A HG3  1 
ATOM   2145 H  HG3  B PRO   A 1 98  ? 23.559 -7.942  -8.600  0.38 14.93 ?  98   PRO   A HG3  1 
ATOM   2146 H  HD2  A PRO   A 1 98  ? 23.044 -6.859  -6.282  0.62 13.15 ?  98   PRO   A HD2  1 
ATOM   2147 H  HD2  B PRO   A 1 98  ? 23.350 -6.996  -6.256  0.38 13.93 ?  98   PRO   A HD2  1 
ATOM   2148 H  HD3  A PRO   A 1 98  ? 24.438 -7.214  -6.994  0.62 13.15 ?  98   PRO   A HD3  1 
ATOM   2149 H  HD3  B PRO   A 1 98  ? 24.811 -7.224  -6.880  0.38 13.93 ?  98   PRO   A HD3  1 
ATOM   2150 N  N    A ASN   A 1 99  ? 23.067 -2.456  -9.049  0.62 12.79 ?  99   ASN   A N    1 
ATOM   2151 N  N    B ASN   A 1 99  ? 23.344 -2.757  -9.400  0.38 11.90 ?  99   ASN   A N    1 
ATOM   2152 C  CA   A ASN   A 1 99  ? 22.090 -1.395  -9.272  0.62 13.62 ?  99   ASN   A CA   1 
ATOM   2153 C  CA   B ASN   A 1 99  ? 22.394 -1.706  -9.735  0.38 12.37 ?  99   ASN   A CA   1 
ATOM   2154 C  C    A ASN   A 1 99  ? 21.520 -1.580  -10.674 0.62 14.92 ?  99   ASN   A C    1 
ATOM   2155 C  C    B ASN   A 1 99  ? 21.833 -2.009  -11.119 0.38 12.50 ?  99   ASN   A C    1 
ATOM   2156 O  O    A ASN   A 1 99  ? 22.210 -1.333  -11.670 0.62 16.05 ?  99   ASN   A O    1 
ATOM   2157 O  O    B ASN   A 1 99  ? 22.524 -1.838  -12.129 0.38 12.37 ?  99   ASN   A O    1 
ATOM   2158 C  CB   A ASN   A 1 99  ? 22.738 -0.021  -9.120  0.62 13.98 ?  99   ASN   A CB   1 
ATOM   2159 C  CB   B ASN   A 1 99  ? 23.089 -0.348  -9.713  0.38 13.10 ?  99   ASN   A CB   1 
ATOM   2160 C  CG   A ASN   A 1 99  ? 21.719 1.117   -9.092  0.62 14.95 ?  99   ASN   A CG   1 
ATOM   2161 C  CG   B ASN   A 1 99  ? 22.129 0.799   -9.921  0.38 13.35 ?  99   ASN   A CG   1 
ATOM   2162 O  OD1  A ASN   A 1 99  ? 20.703 1.073   -9.784  0.62 15.34 ?  99   ASN   A OD1  1 
ATOM   2163 O  OD1  B ASN   A 1 99  ? 21.146 0.671   -10.644 0.38 13.12 ?  99   ASN   A OD1  1 
ATOM   2164 N  ND2  A ASN   A 1 99  ? 21.998 2.145   -8.296  0.62 15.34 ?  99   ASN   A ND2  1 
ATOM   2165 N  ND2  B ASN   A 1 99  ? 22.409 1.930   -9.283  0.38 14.48 ?  99   ASN   A ND2  1 
ATOM   2166 H  H    A ASN   A 1 99  ? 23.835 -2.292  -9.394  0.62 15.37 ?  99   ASN   A H    1 
ATOM   2167 H  H    B ASN   A 1 99  ? 24.117 -2.656  -9.758  0.38 14.29 ?  99   ASN   A H    1 
ATOM   2168 H  HA   A ASN   A 1 99  ? 21.366 -1.476  -8.626  0.62 16.36 ?  99   ASN   A HA   1 
ATOM   2169 H  HA   B ASN   A 1 99  ? 21.666 -1.709  -9.093  0.38 14.86 ?  99   ASN   A HA   1 
ATOM   2170 H  HB2  A ASN   A 1 99  ? 23.241 0.001   -8.295  0.62 16.80 ?  99   ASN   A HB2  1 
ATOM   2171 H  HB2  B ASN   A 1 99  ? 23.522 -0.235  -8.854  0.38 15.74 ?  99   ASN   A HB2  1 
ATOM   2172 H  HB3  A ASN   A 1 99  ? 23.330 0.126   -9.877  0.62 16.80 ?  99   ASN   A HB3  1 
ATOM   2173 H  HB3  B ASN   A 1 99  ? 23.746 -0.327  -10.425 0.38 15.74 ?  99   ASN   A HB3  1 
ATOM   2174 H  HD21 A ASN   A 1 99  ? 21.456 2.810   -8.240  0.62 18.42 ?  99   ASN   A HD21 1 
ATOM   2175 H  HD21 B ASN   A 1 99  ? 21.892 2.610   -9.366  0.38 17.39 ?  99   ASN   A HD21 1 
ATOM   2176 H  HD22 A ASN   A 1 99  ? 22.720 2.139   -7.827  0.62 18.42 ?  99   ASN   A HD22 1 
ATOM   2177 H  HD22 B ASN   A 1 99  ? 23.109 1.978   -8.784  0.38 17.39 ?  99   ASN   A HD22 1 
ATOM   2178 N  N    A VAL   A 1 100 ? 20.263 -2.029  -10.743 0.62 15.94 ?  100  VAL   A N    1 
ATOM   2179 N  N    B VAL   A 1 100 ? 20.580 -2.467  -11.158 0.38 13.98 ?  100  VAL   A N    1 
ATOM   2180 C  CA   A VAL   A 1 100 ? 19.625 -2.281  -12.032 0.62 17.75 ?  100  VAL   A CA   1 
ATOM   2181 C  CA   B VAL   A 1 100 ? 19.967 -2.844  -12.427 0.38 16.18 ?  100  VAL   A CA   1 
ATOM   2182 C  C    A VAL   A 1 100 ? 19.545 -0.999  -12.850 0.62 18.93 ?  100  VAL   A C    1 
ATOM   2183 C  C    B VAL   A 1 100 ? 19.748 -1.626  -13.315 0.38 16.01 ?  100  VAL   A C    1 
ATOM   2184 O  O    A VAL   A 1 100 ? 19.647 -1.030  -14.082 0.62 19.04 ?  100  VAL   A O    1 
ATOM   2185 O  O    B VAL   A 1 100 ? 19.712 -1.749  -14.546 0.38 16.40 ?  100  VAL   A O    1 
ATOM   2186 C  CB   A VAL   A 1 100 ? 18.244 -2.948  -11.832 0.62 19.03 ?  100  VAL   A CB   1 
ATOM   2187 C  CB   B VAL   A 1 100 ? 18.670 -3.636  -12.175 0.38 18.49 ?  100  VAL   A CB   1 
ATOM   2188 C  CG1  A VAL   A 1 100 ? 17.519 -3.115  -13.160 0.62 19.92 ?  100  VAL   A CG1  1 
ATOM   2189 C  CG1  B VAL   A 1 100 ? 17.781 -3.644  -13.412 0.38 19.31 ?  100  VAL   A CG1  1 
ATOM   2190 C  CG2  A VAL   A 1 100 ? 18.404 -4.302  -11.147 0.62 19.08 ?  100  VAL   A CG2  1 
ATOM   2191 C  CG2  B VAL   A 1 100 ? 19.002 -5.055  -11.748 0.38 19.38 ?  100  VAL   A CG2  1 
ATOM   2192 H  H    A VAL   A 1 100 ? 19.756 -2.195  -10.061 0.62 19.15 ?  100  VAL   A H    1 
ATOM   2193 H  H    B VAL   A 1 100 ? 20.074 -2.581  -10.469 0.38 16.79 ?  100  VAL   A H    1 
ATOM   2194 H  HA   A VAL   A 1 100 ? 20.170 -2.911  -12.528 0.62 21.31 ?  100  VAL   A HA   1 
ATOM   2195 H  HA   B VAL   A 1 100 ? 20.576 -3.438  -12.893 0.38 19.43 ?  100  VAL   A HA   1 
ATOM   2196 H  HB   A VAL   A 1 100 ? 17.695 -2.390  -11.261 0.62 22.85 ?  100  VAL   A HB   1 
ATOM   2197 H  HB   B VAL   A 1 100 ? 18.176 -3.210  -11.458 0.38 22.20 ?  100  VAL   A HB   1 
ATOM   2198 H  HG11 A VAL   A 1 100 ? 16.756 -3.705  -13.035 0.62 23.92 ?  100  VAL   A HG11 1 
ATOM   2199 H  HG11 B VAL   A 1 100 ? 17.103 -4.329  -13.306 0.38 23.19 ?  100  VAL   A HG11 1 
ATOM   2200 H  HG12 A VAL   A 1 100 ? 17.215 -2.249  -13.470 0.62 23.92 ?  100  VAL   A HG12 1 
ATOM   2201 H  HG12 B VAL   A 1 100 ? 17.355 -2.775  -13.507 0.38 23.19 ?  100  VAL   A HG12 1 
ATOM   2202 H  HG13 A VAL   A 1 100 ? 18.128 -3.506  -13.807 0.62 23.92 ?  100  VAL   A HG13 1 
ATOM   2203 H  HG13 B VAL   A 1 100 ? 18.322 -3.835  -14.193 0.38 23.19 ?  100  VAL   A HG13 1 
ATOM   2204 H  HG21 A VAL   A 1 100 ? 17.532 -4.722  -11.064 0.62 22.91 ?  100  VAL   A HG21 1 
ATOM   2205 H  HG21 B VAL   A 1 100 ? 18.176 -5.533  -11.578 0.38 23.27 ?  100  VAL   A HG21 1 
ATOM   2206 H  HG22 A VAL   A 1 100 ? 18.988 -4.861  -11.684 0.62 22.91 ?  100  VAL   A HG22 1 
ATOM   2207 H  HG22 B VAL   A 1 100 ? 19.496 -5.491  -12.461 0.38 23.27 ?  100  VAL   A HG22 1 
ATOM   2208 H  HG23 A VAL   A 1 100 ? 18.790 -4.168  -10.268 0.62 22.91 ?  100  VAL   A HG23 1 
ATOM   2209 H  HG23 B VAL   A 1 100 ? 19.540 -5.022  -10.944 0.38 23.27 ?  100  VAL   A HG23 1 
ATOM   2210 N  N    A ASN   A 1 101 ? 19.375 0.145   -12.189 0.62 20.45 ?  101  ASN   A N    1 
ATOM   2211 N  N    B ASN   A 1 101 ? 19.585 -0.439  -12.722 0.38 15.86 ?  101  ASN   A N    1 
ATOM   2212 C  CA   A ASN   A 1 101 ? 19.319 1.421   -12.896 0.62 22.37 ?  101  ASN   A CA   1 
ATOM   2213 C  CA   B ASN   A 1 101 ? 19.497 0.781   -13.516 0.38 16.49 ?  101  ASN   A CA   1 
ATOM   2214 C  C    A ASN   A 1 101 ? 20.674 1.852   -13.455 0.62 24.04 ?  101  ASN   A C    1 
ATOM   2215 C  C    B ASN   A 1 101 ? 20.798 1.083   -14.248 0.38 17.07 ?  101  ASN   A C    1 
ATOM   2216 O  O    A ASN   A 1 101 ? 20.740 2.871   -14.155 0.62 25.50 ?  101  ASN   A O    1 
ATOM   2217 O  O    B ASN   A 1 101 ? 20.767 1.780   -15.268 0.38 17.55 ?  101  ASN   A O    1 
ATOM   2218 C  CB   A ASN   A 1 101 ? 18.727 2.495   -11.981 0.62 21.74 ?  101  ASN   A CB   1 
ATOM   2219 C  CB   B ASN   A 1 101 ? 19.107 1.970   -12.633 0.38 16.34 ?  101  ASN   A CB   1 
ATOM   2220 C  CG   A ASN   A 1 101 ? 17.362 2.105   -11.434 0.62 21.26 ?  101  ASN   A CG   1 
ATOM   2221 C  CG   B ASN   A 1 101 ? 17.827 1.725   -11.851 0.38 17.22 ?  101  ASN   A CG   1 
ATOM   2222 O  OD1  A ASN   A 1 101 ? 16.499 1.621   -12.169 0.62 21.59 ?  101  ASN   A OD1  1 
ATOM   2223 O  OD1  B ASN   A 1 101 ? 16.875 1.127   -12.356 0.38 18.58 ?  101  ASN   A OD1  1 
ATOM   2224 N  ND2  A ASN   A 1 101 ? 17.165 2.305   -10.135 0.62 21.56 ?  101  ASN   A ND2  1 
ATOM   2225 N  ND2  B ASN   A 1 101 ? 17.804 2.177   -10.605 0.38 17.46 ?  101  ASN   A ND2  1 
ATOM   2226 H  H    A ASN   A 1 101 ? 19.283 0.203   -11.338 0.62 24.56 ?  101  ASN   A H    1 
ATOM   2227 H  H    B ASN   A 1 101 ? 19.516 -0.319  -11.873 0.38 19.05 ?  101  ASN   A H    1 
ATOM   2228 H  HA   A ASN   A 1 101 ? 18.720 1.320   -13.649 0.62 26.86 ?  101  ASN   A HA   1 
ATOM   2229 H  HA   B ASN   A 1 101 ? 18.809 0.671   -14.184 0.38 19.80 ?  101  ASN   A HA   1 
ATOM   2230 H  HB2  A ASN   A 1 101 ? 19.322 2.639   -11.231 0.62 26.10 ?  101  ASN   A HB2  1 
ATOM   2231 H  HB2  B ASN   A 1 101 ? 19.821 2.145   -11.998 0.38 19.62 ?  101  ASN   A HB2  1 
ATOM   2232 H  HB3  A ASN   A 1 101 ? 18.620 3.314   -12.488 0.62 26.10 ?  101  ASN   A HB3  1 
ATOM   2233 H  HB3  B ASN   A 1 101 ? 18.969 2.748   -13.195 0.38 19.62 ?  101  ASN   A HB3  1 
ATOM   2234 H  HD21 A ASN   A 1 101 ? 16.410 2.097   -9.778  0.62 25.89 ?  101  ASN   A HD21 1 
ATOM   2235 H  HD21 B ASN   A 1 101 ? 17.104 2.061   -10.123 0.38 20.97 ?  101  ASN   A HD21 1 
ATOM   2236 H  HD22 A ASN   A 1 101 ? 17.787 2.650   -9.655  0.62 25.89 ?  101  ASN   A HD22 1 
ATOM   2237 H  HD22 B ASN   A 1 101 ? 18.488 2.588   -10.284 0.38 20.97 ?  101  ASN   A HD22 1 
ATOM   2238 N  N    A LYS   A 1 102 ? 21.744 1.106   -13.171 0.62 25.30 ?  102  LYS   A N    1 
ATOM   2239 N  N    B LYS   A 1 102 ? 21.930 0.579   -13.752 0.38 18.35 ?  102  LYS   A N    1 
ATOM   2240 C  CA   A LYS   A 1 102 ? 23.033 1.293   -13.824 0.62 26.48 ?  102  LYS   A CA   1 
ATOM   2241 C  CA   B LYS   A 1 102 ? 23.225 0.719   -14.411 0.38 19.66 ?  102  LYS   A CA   1 
ATOM   2242 C  C    A LYS   A 1 102 ? 23.347 0.187   -14.821 0.62 26.30 ?  102  LYS   A C    1 
ATOM   2243 C  C    B LYS   A 1 102 ? 23.554 -0.469  -15.312 0.38 19.69 ?  102  LYS   A C    1 
ATOM   2244 O  O    A LYS   A 1 102 ? 24.420 0.213   -15.434 0.62 26.80 ?  102  LYS   A O    1 
ATOM   2245 O  O    B LYS   A 1 102 ? 24.687 -0.573  -15.792 0.38 20.05 ?  102  LYS   A O    1 
ATOM   2246 C  CB   A LYS   A 1 102 ? 24.160 1.367   -12.786 0.62 28.27 ?  102  LYS   A CB   1 
ATOM   2247 C  CB   B LYS   A 1 102 ? 24.346 0.874   -13.374 0.38 21.83 ?  102  LYS   A CB   1 
ATOM   2248 C  CG   A LYS   A 1 102 ? 24.026 2.499   -11.787 0.62 29.83 ?  102  LYS   A CG   1 
ATOM   2249 C  CG   B LYS   A 1 102 ? 24.294 2.139   -12.531 0.38 24.10 ?  102  LYS   A CG   1 
ATOM   2250 C  CD   A LYS   A 1 102 ? 25.182 2.487   -10.797 0.62 31.52 ?  102  LYS   A CD   1 
ATOM   2251 C  CD   B LYS   A 1 102 ? 25.402 2.124   -11.482 0.38 26.30 ?  102  LYS   A CD   1 
ATOM   2252 C  CE   A LYS   A 1 102 ? 25.104 3.655   -9.827  0.62 32.84 ?  102  LYS   A CE   1 
ATOM   2253 C  CE   B LYS   A 1 102 ? 25.228 3.233   -10.459 0.38 28.00 ?  102  LYS   A CE   1 
ATOM   2254 N  NZ   A LYS   A 1 102 ? 26.192 3.601   -8.808  0.62 33.46 ?  102  LYS   A NZ   1 
ATOM   2255 N  NZ   B LYS   A 1 102 ? 25.620 2.786   -9.090  0.38 29.07 ?  102  LYS   A NZ   1 
ATOM   2256 H  H    A LYS   A 1 102 ? 21.747 0.470   -12.589 0.62 30.38 ?  102  LYS   A H    1 
ATOM   2257 H  H    B LYS   A 1 102 ? 21.972 0.135   -13.012 0.38 22.03 ?  102  LYS   A H    1 
ATOM   2258 H  HA   A LYS   A 1 102 ? 23.021 2.131   -14.306 0.62 31.79 ?  102  LYS   A HA   1 
ATOM   2259 H  HA   B LYS   A 1 102 ? 23.216 1.524   -14.950 0.38 23.61 ?  102  LYS   A HA   1 
ATOM   2260 H  HB2  A LYS   A 1 102 ? 24.179 0.536   -12.288 0.62 33.94 ?  102  LYS   A HB2  1 
ATOM   2261 H  HB2  B LYS   A 1 102 ? 24.314 0.122   -12.764 0.38 26.21 ?  102  LYS   A HB2  1 
ATOM   2262 H  HB3  A LYS   A 1 102 ? 25.002 1.486   -13.254 0.62 33.94 ?  102  LYS   A HB3  1 
ATOM   2263 H  HB3  B LYS   A 1 102 ? 25.200 0.877   -13.838 0.38 26.21 ?  102  LYS   A HB3  1 
ATOM   2264 H  HG2  A LYS   A 1 102 ? 24.035 3.347   -12.259 0.62 35.81 ?  102  LYS   A HG2  1 
ATOM   2265 H  HG2  B LYS   A 1 102 ? 24.423 2.916   -13.099 0.38 28.93 ?  102  LYS   A HG2  1 
ATOM   2266 H  HG3  A LYS   A 1 102 ? 23.198 2.396   -11.293 0.62 35.81 ?  102  LYS   A HG3  1 
ATOM   2267 H  HG3  B LYS   A 1 102 ? 23.442 2.189   -12.074 0.38 28.93 ?  102  LYS   A HG3  1 
ATOM   2268 H  HD2  A LYS   A 1 102 ? 25.155 1.663   -10.285 0.62 37.84 ?  102  LYS   A HD2  1 
ATOM   2269 H  HD2  B LYS   A 1 102 ? 25.388 1.275   -11.014 0.38 31.57 ?  102  LYS   A HD2  1 
ATOM   2270 H  HD3  A LYS   A 1 102 ? 26.020 2.551   -11.284 0.62 37.84 ?  102  LYS   A HD3  1 
ATOM   2271 H  HD3  B LYS   A 1 102 ? 26.260 2.248   -11.921 0.38 31.57 ?  102  LYS   A HD3  1 
ATOM   2272 H  HE2  A LYS   A 1 102 ? 25.192 4.486   -10.321 0.62 39.42 ?  102  LYS   A HE2  1 
ATOM   2273 H  HE2  B LYS   A 1 102 ? 25.785 3.990   -10.704 0.38 33.62 ?  102  LYS   A HE2  1 
ATOM   2274 H  HE3  A LYS   A 1 102 ? 24.252 3.628   -9.364  0.62 39.42 ?  102  LYS   A HE3  1 
ATOM   2275 H  HE3  B LYS   A 1 102 ? 24.296 3.494   -10.435 0.38 33.62 ?  102  LYS   A HE3  1 
ATOM   2276 H  HZ1  A LYS   A 1 102 ? 26.124 4.293   -8.254  0.62 40.16 ?  102  LYS   A HZ1  1 
ATOM   2277 H  HZ1  B LYS   A 1 102 ? 25.121 2.090   -8.845  0.38 34.89 ?  102  LYS   A HZ1  1 
ATOM   2278 H  HZ2  A LYS   A 1 102 ? 26.131 2.847   -8.339  0.62 40.16 ?  102  LYS   A HZ2  1 
ATOM   2279 H  HZ2  B LYS   A 1 102 ? 26.476 2.544   -9.082  0.38 34.89 ?  102  LYS   A HZ2  1 
ATOM   2280 H  HZ3  A LYS   A 1 102 ? 26.986 3.627   -9.210  0.62 40.16 ?  102  LYS   A HZ3  1 
ATOM   2281 H  HZ3  B LYS   A 1 102 ? 25.499 3.447   -8.507  0.38 34.89 ?  102  LYS   A HZ3  1 
ATOM   2282 N  N    A GLY   A 1 103 ? 22.452 -0.784  -14.994 0.62 26.40 ?  103  GLY   A N    1 
ATOM   2283 N  N    B GLY   A 1 103 ? 22.604 -1.373  -15.531 0.38 19.55 ?  103  GLY   A N    1 
ATOM   2284 C  CA   A GLY   A 1 103 ? 22.691 -1.879  -15.914 0.62 26.30 ?  103  GLY   A CA   1 
ATOM   2285 C  CA   B GLY   A 1 103 ? 22.864 -2.543  -16.349 0.38 19.80 ?  103  GLY   A CA   1 
ATOM   2286 C  C    A GLY   A 1 103 ? 23.543 -3.001  -15.366 0.62 25.89 ?  103  GLY   A C    1 
ATOM   2287 C  C    B GLY   A 1 103 ? 23.698 -3.623  -15.690 0.38 19.13 ?  103  GLY   A C    1 
ATOM   2288 O  O    A GLY   A 1 103 ? 24.102 -3.775  -16.149 0.62 27.00 ?  103  GLY   A O    1 
ATOM   2289 O  O    B GLY   A 1 103 ? 24.205 -4.511  -16.381 0.38 19.61 ?  103  GLY   A O    1 
ATOM   2290 H  H    A GLY   A 1 103 ? 21.696 -0.829  -14.587 0.62 31.70 ?  103  GLY   A H    1 
ATOM   2291 H  H    B GLY   A 1 103 ? 21.804 -1.316  -15.224 0.38 23.48 ?  103  GLY   A H    1 
ATOM   2292 H  HA2  A GLY   A 1 103 ? 21.837 -2.244  -16.200 0.62 31.58 ?  103  GLY   A HA2  1 
ATOM   2293 H  HA2  B GLY   A 1 103 ? 22.017 -2.942  -16.589 0.38 23.77 ?  103  GLY   A HA2  1 
ATOM   2294 H  HA3  A GLY   A 1 103 ? 23.143 -1.534  -16.699 0.62 31.58 ?  103  GLY   A HA3  1 
ATOM   2295 H  HA3  B GLY   A 1 103 ? 23.302 -2.252  -17.168 0.38 23.77 ?  103  GLY   A HA3  1 
ATOM   2296 N  N    A GLU   A 1 104 ? 23.668 -3.114  -14.047 0.62 23.93 ?  104  GLU   A N    1 
ATOM   2297 N  N    B GLU   A 1 104 ? 23.835 -3.593  -14.370 0.38 17.49 ?  104  GLU   A N    1 
ATOM   2298 C  CA   A GLU   A 1 104 ? 24.537 -4.119  -13.450 0.62 22.17 ?  104  GLU   A CA   1 
ATOM   2299 C  CA   B GLU   A 1 104 ? 24.716 -4.528  -13.688 0.38 15.91 ?  104  GLU   A CA   1 
ATOM   2300 C  C    A GLU   A 1 104 ? 23.840 -5.475  -13.350 0.62 22.12 ?  104  GLU   A C    1 
ATOM   2301 C  C    B GLU   A 1 104 ? 24.033 -5.880  -13.507 0.38 15.87 ?  104  GLU   A C    1 
ATOM   2302 O  O    A GLU   A 1 104 ? 22.619 -5.567  -13.193 0.62 22.69 ?  104  GLU   A O    1 
ATOM   2303 O  O    B GLU   A 1 104 ? 22.804 -5.983  -13.441 0.38 16.69 ?  104  GLU   A O    1 
ATOM   2304 C  CB   A GLU   A 1 104 ? 25.039 -3.630  -12.089 0.62 20.79 ?  104  GLU   A CB   1 
ATOM   2305 C  CB   B GLU   A 1 104 ? 25.177 -3.950  -12.350 0.38 15.44 ?  104  GLU   A CB   1 
ATOM   2306 C  CG   A GLU   A 1 104 ? 26.005 -2.452  -12.251 0.62 20.43 ?  104  GLU   A CG   1 
ATOM   2307 C  CG   B GLU   A 1 104 ? 26.001 -2.679  -12.531 0.38 16.04 ?  104  GLU   A CG   1 
ATOM   2308 C  CD   A GLU   A 1 104 ? 26.326 -1.682  -10.979 0.62 19.55 ?  104  GLU   A CD   1 
ATOM   2309 C  CD   B GLU   A 1 104 ? 26.330 -1.948  -11.237 0.38 16.14 ?  104  GLU   A CD   1 
ATOM   2310 O  OE1  A GLU   A 1 104 ? 25.713 -1.930  -9.924  0.62 18.01 ?  104  GLU   A OE1  1 
ATOM   2311 O  OE1  B GLU   A 1 104 ? 25.857 -2.356  -10.159 0.38 16.70 ?  104  GLU   A OE1  1 
ATOM   2312 O  OE2  A GLU   A 1 104 ? 27.210 -0.798  -11.052 0.62 20.66 -1 104  GLU   A OE2  1 
ATOM   2313 O  OE2  B GLU   A 1 104 ? 27.066 -0.940  -11.309 0.38 16.38 -1 104  GLU   A OE2  1 
ATOM   2314 H  H    A GLU   A 1 104 ? 23.272 -2.607  -13.479 0.62 28.73 ?  104  GLU   A H    1 
ATOM   2315 H  H    B GLU   A 1 104 ? 23.415 -3.053  -13.853 0.38 21.01 ?  104  GLU   A H    1 
ATOM   2316 H  HA   A GLU   A 1 104 ? 25.311 -4.230  -14.022 0.62 26.61 ?  104  GLU   A HA   1 
ATOM   2317 H  HA   B GLU   A 1 104 ? 25.501 -4.669  -14.240 0.38 19.11 ?  104  GLU   A HA   1 
ATOM   2318 H  HB2  A GLU   A 1 104 ? 24.283 -3.339  -11.555 0.62 24.96 ?  104  GLU   A HB2  1 
ATOM   2319 H  HB2  B GLU   A 1 104 ? 24.400 -3.740  -11.814 0.38 18.54 ?  104  GLU   A HB2  1 
ATOM   2320 H  HB3  A GLU   A 1 104 ? 25.508 -4.353  -11.644 0.62 24.96 ?  104  GLU   A HB3  1 
ATOM   2321 H  HB3  B GLU   A 1 104 ? 25.729 -4.611  -11.901 0.38 18.54 ?  104  GLU   A HB3  1 
ATOM   2322 H  HG2  A GLU   A 1 104 ? 26.842 -2.789  -12.598 0.62 24.54 ?  104  GLU   A HG2  1 
ATOM   2323 H  HG2  B GLU   A 1 104 ? 26.835 -2.912  -12.968 0.38 19.26 ?  104  GLU   A HG2  1 
ATOM   2324 H  HG3  A GLU   A 1 104 ? 25.617 -1.824  -12.880 0.62 24.54 ?  104  GLU   A HG3  1 
ATOM   2325 H  HG3  B GLU   A 1 104 ? 25.500 -2.064  -13.091 0.38 19.26 ?  104  GLU   A HG3  1 
ATOM   2326 N  N    A ASP   A 1 105 ? 24.646 -6.533  -13.438 0.62 22.20 ?  105  ASP   A N    1 
ATOM   2327 N  N    B ASP   A 1 105 ? 24.859 -6.921  -13.421 0.38 16.14 ?  105  ASP   A N    1 
ATOM   2328 C  CA   A ASP   A 1 105 ? 24.144 -7.895  -13.584 0.62 22.59 ?  105  ASP   A CA   1 
ATOM   2329 C  CA   B ASP   A 1 105 ? 24.401 -8.304  -13.498 0.38 16.71 ?  105  ASP   A CA   1 
ATOM   2330 C  C    A ASP   A 1 105 ? 23.478 -8.366  -12.294 0.62 20.35 ?  105  ASP   A C    1 
ATOM   2331 C  C    B ASP   A 1 105 ? 23.633 -8.694  -12.238 0.38 15.91 ?  105  ASP   A C    1 
ATOM   2332 O  O    A ASP   A 1 105 ? 24.133 -8.475  -11.255 0.62 18.88 ?  105  ASP   A O    1 
ATOM   2333 O  O    B ASP   A 1 105 ? 24.191 -8.696  -11.137 0.38 15.02 ?  105  ASP   A O    1 
ATOM   2334 C  CB   A ASP   A 1 105 ? 25.311 -8.812  -13.944 0.62 25.48 ?  105  ASP   A CB   1 
ATOM   2335 C  CB   B ASP   A 1 105 ? 25.624 -9.202  -13.676 0.38 18.29 ?  105  ASP   A CB   1 
ATOM   2336 C  CG   A ASP   A 1 105 ? 24.882 -10.244 -14.155 0.62 28.24 ?  105  ASP   A CG   1 
ATOM   2337 C  CG   B ASP   A 1 105 ? 25.269 -10.659 -13.855 0.38 19.72 ?  105  ASP   A CG   1 
ATOM   2338 O  OD1  A ASP   A 1 105 ? 23.661 -10.486 -14.251 0.62 28.81 ?  105  ASP   A OD1  1 
ATOM   2339 O  OD1  B ASP   A 1 105 ? 24.068 -10.988 -13.928 0.38 19.68 ?  105  ASP   A OD1  1 
ATOM   2340 O  OD2  A ASP   A 1 105 ? 25.764 -11.127 -14.224 0.62 29.95 -1 105  ASP   A OD2  1 
ATOM   2341 O  OD2  B ASP   A 1 105 ? 26.211 -11.481 -13.914 0.38 21.08 -1 105  ASP   A OD2  1 
ATOM   2342 H  H    A ASP   A 1 105 ? 25.505 -6.484  -13.411 0.62 26.65 ?  105  ASP   A H    1 
ATOM   2343 H  H    B ASP   A 1 105 ? 25.709 -6.849  -13.309 0.38 19.39 ?  105  ASP   A H    1 
ATOM   2344 H  HA   A ASP   A 1 105 ? 23.492 -7.931  -14.299 0.62 27.13 ?  105  ASP   A HA   1 
ATOM   2345 H  HA   B ASP   A 1 105 ? 23.820 -8.419  -14.266 0.38 20.07 ?  105  ASP   A HA   1 
ATOM   2346 H  HB2  A ASP   A 1 105 ? 25.723 -8.492  -14.766 0.62 30.59 ?  105  ASP   A HB2  1 
ATOM   2347 H  HB2  B ASP   A 1 105 ? 26.128 -8.901  -14.453 0.38 21.96 ?  105  ASP   A HB2  1 
ATOM   2348 H  HB3  A ASP   A 1 105 ? 25.964 -8.794  -13.225 0.62 30.59 ?  105  ASP   A HB3  1 
ATOM   2349 H  HB3  B ASP   A 1 105 ? 26.179 -9.148  -12.885 0.38 21.96 ?  105  ASP   A HB3  1 
ATOM   2350 N  N    A ILE   A 1 106 ? 22.180 -8.672  -12.368 0.62 19.65 ?  106  ILE   A N    1 
ATOM   2351 N  N    B ILE   A 1 106 ? 22.360 -9.061  -12.408 0.38 16.77 ?  106  ILE   A N    1 
ATOM   2352 C  CA   A ILE   A 1 106 ? 21.430 -9.081  -11.184 0.62 18.97 ?  106  ILE   A CA   1 
ATOM   2353 C  CA   B ILE   A 1 106 ? 21.535 -9.466  -11.273 0.38 17.56 ?  106  ILE   A CA   1 
ATOM   2354 C  C    A ILE   A 1 106 ? 21.965 -10.375 -10.587 0.62 18.13 ?  106  ILE   A C    1 
ATOM   2355 C  C    B ILE   A 1 106 ? 22.133 -10.669 -10.560 0.38 17.57 ?  106  ILE   A C    1 
ATOM   2356 O  O    A ILE   A 1 106 ? 21.755 -10.636 -9.397  0.62 17.37 ?  106  ILE   A O    1 
ATOM   2357 O  O    B ILE   A 1 106 ? 21.924 -10.847 -9.354  0.38 17.66 ?  106  ILE   A O    1 
ATOM   2358 C  CB   A ILE   A 1 106 ? 19.923 -9.176  -11.513 0.62 20.20 ?  106  ILE   A CB   1 
ATOM   2359 C  CB   B ILE   A 1 106 ? 20.090 -9.741  -11.736 0.38 18.94 ?  106  ILE   A CB   1 
ATOM   2360 C  CG1  A ILE   A 1 106 ? 19.090 -9.270  -10.232 0.62 20.50 ?  106  ILE   A CG1  1 
ATOM   2361 C  CG1  B ILE   A 1 106 ? 19.152 -9.921  -10.541 0.38 19.31 ?  106  ILE   A CG1  1 
ATOM   2362 C  CG2  A ILE   A 1 106 ? 19.643 -10.375 -12.406 0.62 20.69 ?  106  ILE   A CG2  1 
ATOM   2363 C  CG2  B ILE   A 1 106 ? 20.038 -10.996 -12.580 0.38 19.60 ?  106  ILE   A CG2  1 
ATOM   2364 C  CD1  A ILE   A 1 106 ? 19.234 -8.067  -9.317  0.62 20.37 ?  106  ILE   A CD1  1 
ATOM   2365 C  CD1  B ILE   A 1 106 ? 19.000 -8.692  -9.684  0.38 19.56 ?  106  ILE   A CD1  1 
ATOM   2366 H  H    A ILE   A 1 106 ? 21.720 -8.640  -13.087 0.62 23.59 ?  106  ILE   A H    1 
ATOM   2367 H  H    B ILE   A 1 106 ? 21.960 -9.098  -13.164 0.38 20.14 ?  106  ILE   A H    1 
ATOM   2368 H  HA   A ILE   A 1 106 ? 21.541 -8.394  -10.513 0.62 22.78 ?  106  ILE   A HA   1 
ATOM   2369 H  HA   B ILE   A 1 106 ? 21.514 -8.746  -10.633 0.38 21.09 ?  106  ILE   A HA   1 
ATOM   2370 H  HB   A ILE   A 1 106 ? 19.661 -8.372  -11.990 0.62 24.26 ?  106  ILE   A HB   1 
ATOM   2371 H  HB   B ILE   A 1 106 ? 19.785 -8.992  -12.269 0.38 22.74 ?  106  ILE   A HB   1 
ATOM   2372 H  HG12 A ILE   A 1 106 ? 18.153 -9.343  -10.473 0.62 24.61 ?  106  ILE   A HG12 1 
ATOM   2373 H  HG12 B ILE   A 1 106 ? 18.272 -10.160 -10.874 0.38 23.19 ?  106  ILE   A HG12 1 
ATOM   2374 H  HG13 A ILE   A 1 106 ? 19.362 -10.055 -9.734  0.62 24.61 ?  106  ILE   A HG13 1 
ATOM   2375 H  HG13 B ILE   A 1 106 ? 19.491 -10.636 -9.981  0.38 23.19 ?  106  ILE   A HG13 1 
ATOM   2376 H  HG21 A ILE   A 1 106 ? 18.745 -10.298 -12.762 0.62 24.84 ?  106  ILE   A HG21 1 
ATOM   2377 H  HG21 B ILE   A 1 106 ? 19.165 -11.056 -12.993 0.38 23.54 ?  106  ILE   A HG21 1 
ATOM   2378 H  HG22 A ILE   A 1 106 ? 20.289 -10.382 -13.129 0.62 24.84 ?  106  ILE   A HG22 1 
ATOM   2379 H  HG22 B ILE   A 1 106 ? 20.727 -10.948 -13.259 0.38 23.54 ?  106  ILE   A HG22 1 
ATOM   2380 H  HG23 A ILE   A 1 106 ? 19.724 -11.185 -11.880 0.62 24.84 ?  106  ILE   A HG23 1 
ATOM   2381 H  HG23 B ILE   A 1 106 ? 20.186 -11.768 -12.010 0.38 23.54 ?  106  ILE   A HG23 1 
ATOM   2382 H  HD11 A ILE   A 1 106 ? 18.504 -8.068  -8.679  0.62 24.46 ?  106  ILE   A HD11 1 
ATOM   2383 H  HD11 B ILE   A 1 106 ? 18.256 -8.828  -9.078  0.38 23.49 ?  106  ILE   A HD11 1 
ATOM   2384 H  HD12 A ILE   A 1 106 ? 20.082 -8.125  -8.848  0.62 24.46 ?  106  ILE   A HD12 1 
ATOM   2385 H  HD12 B ILE   A 1 106 ? 19.817 -8.557  -9.182  0.38 23.49 ?  106  ILE   A HD12 1 
ATOM   2386 H  HD13 A ILE   A 1 106 ? 19.205 -7.258  -9.852  0.62 24.46 ?  106  ILE   A HD13 1 
ATOM   2387 H  HD13 B ILE   A 1 106 ? 18.828 -7.931  -10.258 0.38 23.49 ?  106  ILE   A HD13 1 
ATOM   2388 N  N    A GLN   A 1 107 ? 22.666 -11.190 -11.383 0.62 19.15 ?  107  GLN   A N    1 
ATOM   2389 N  N    B GLN   A 1 107 ? 22.875 -11.516 -11.283 0.38 17.90 ?  107  GLN   A N    1 
ATOM   2390 C  CA   A GLN   A 1 107 ? 23.284 -12.403 -10.860 0.62 21.25 ?  107  GLN   A CA   1 
ATOM   2391 C  CA   B GLN   A 1 107 ? 23.498 -12.675 -10.649 0.38 19.50 ?  107  GLN   A CA   1 
ATOM   2392 C  C    A GLN   A 1 107 ? 24.269 -12.099 -9.736  0.62 19.00 ?  107  GLN   A C    1 
ATOM   2393 C  C    B GLN   A 1 107 ? 24.440 -12.250 -9.531  0.38 17.25 ?  107  GLN   A C    1 
ATOM   2394 O  O    A GLN   A 1 107 ? 24.512 -12.960 -8.884  0.62 20.83 ?  107  GLN   A O    1 
ATOM   2395 O  O    B GLN   A 1 107 ? 24.681 -13.018 -8.590  0.38 17.44 ?  107  GLN   A O    1 
ATOM   2396 C  CB   A GLN   A 1 107 ? 23.981 -13.159 -11.999 0.62 26.10 ?  107  GLN   A CB   1 
ATOM   2397 C  CB   B GLN   A 1 107 ? 24.238 -13.515 -11.694 0.38 23.36 ?  107  GLN   A CB   1 
ATOM   2398 C  CG   A GLN   A 1 107 ? 23.098 -13.400 -13.221 0.62 31.36 ?  107  GLN   A CG   1 
ATOM   2399 C  CG   B GLN   A 1 107 ? 23.344 -14.002 -12.828 0.38 27.00 ?  107  GLN   A CG   1 
ATOM   2400 C  CD   A GLN   A 1 107 ? 21.817 -14.137 -12.883 0.62 35.64 ?  107  GLN   A CD   1 
ATOM   2401 C  CD   B GLN   A 1 107 ? 22.266 -14.958 -12.352 0.38 30.06 ?  107  GLN   A CD   1 
ATOM   2402 O  OE1  A GLN   A 1 107 ? 21.839 -15.177 -12.223 0.62 37.25 ?  107  GLN   A OE1  1 
ATOM   2403 O  OE1  B GLN   A 1 107 ? 22.496 -15.773 -11.458 0.38 31.01 ?  107  GLN   A OE1  1 
ATOM   2404 N  NE2  A GLN   A 1 107 ? 20.690 -13.597 -13.331 0.62 36.99 ?  107  GLN   A NE2  1 
ATOM   2405 N  NE2  B GLN   A 1 107 ? 21.080 -14.858 -12.944 0.38 30.98 ?  107  GLN   A NE2  1 
ATOM   2406 H  H    A GLN   A 1 107 ? 22.800 -11.053 -12.220 0.62 23.00 ?  107  GLN   A H    1 
ATOM   2407 H  H    B GLN   A 1 107 ? 23.038 -11.443 -12.126 0.38 21.49 ?  107  GLN   A H    1 
ATOM   2408 H  HA   A GLN   A 1 107 ? 22.594 -12.982 -10.505 0.62 25.52 ?  107  GLN   A HA   1 
ATOM   2409 H  HA   B GLN   A 1 107 ? 22.812 -13.235 -10.264 0.38 23.42 ?  107  GLN   A HA   1 
ATOM   2410 H  HB2  A GLN   A 1 107 ? 24.751 -12.648 -12.293 0.62 31.34 ?  107  GLN   A HB2  1 
ATOM   2411 H  HB2  B GLN   A 1 107 ? 24.949 -12.985 -12.088 0.38 28.04 ?  107  GLN   A HB2  1 
ATOM   2412 H  HB3  A GLN   A 1 107 ? 24.267 -14.027 -11.675 0.62 31.34 ?  107  GLN   A HB3  1 
ATOM   2413 H  HB3  B GLN   A 1 107 ? 24.617 -14.301 -11.263 0.38 28.04 ?  107  GLN   A HB3  1 
ATOM   2414 H  HG2  A GLN   A 1 107 ? 22.854 -12.548 -13.616 0.62 37.65 ?  107  GLN   A HG2  1 
ATOM   2415 H  HG2  B GLN   A 1 107 ? 22.910 -13.239 -13.239 0.38 32.41 ?  107  GLN   A HG2  1 
ATOM   2416 H  HG3  A GLN   A 1 107 ? 23.590 -13.931 -13.869 0.62 37.65 ?  107  GLN   A HG3  1 
ATOM   2417 H  HG3  B GLN   A 1 107 ? 23.888 -14.466 -13.484 0.38 32.41 ?  107  GLN   A HG3  1 
ATOM   2418 H  HE21 A GLN   A 1 107 ? 20.711 -12.869 -13.788 0.62 44.41 ?  107  GLN   A HE21 1 
ATOM   2419 H  HE21 B GLN   A 1 107 ? 20.955 -14.275 -13.564 0.38 37.19 ?  107  GLN   A HE21 1 
ATOM   2420 H  HE22 A GLN   A 1 107 ? 19.938 -13.979 -13.165 0.62 44.41 ?  107  GLN   A HE22 1 
ATOM   2421 H  HE22 B GLN   A 1 107 ? 20.436 -15.379 -12.709 0.38 37.19 ?  107  GLN   A HE22 1 
ATOM   2422 N  N    A LEU   A 1 108 ? 24.820 -10.882 -9.695  0.62 15.24 ?  108  LEU   A N    1 
ATOM   2423 N  N    B LEU   A 1 108 ? 24.974 -11.032 -9.611  0.38 15.48 ?  108  LEU   A N    1 
ATOM   2424 C  CA   A LEU   A 1 108 ? 25.755 -10.500 -8.643  0.62 13.90 ?  108  LEU   A CA   1 
ATOM   2425 C  CA   B LEU   A 1 108 ? 25.828 -10.511 -8.555  0.38 14.78 ?  108  LEU   A CA   1 
ATOM   2426 C  C    A LEU   A 1 108 ? 25.070 -10.327 -7.293  0.62 12.54 ?  108  LEU   A C    1 
ATOM   2427 C  C    B LEU   A 1 108 ? 25.072 -10.261 -7.258  0.38 13.51 ?  108  LEU   A C    1 
ATOM   2428 O  O    A LEU   A 1 108 ? 25.760 -10.202 -6.276  0.62 12.94 ?  108  LEU   A O    1 
ATOM   2429 O  O    B LEU   A 1 108 ? 25.714 -9.999  -6.236  0.38 14.08 ?  108  LEU   A O    1 
ATOM   2430 C  CB   A LEU   A 1 108 ? 26.501 -9.223  -9.041  0.62 13.93 ?  108  LEU   A CB   1 
ATOM   2431 C  CB   B LEU   A 1 108 ? 26.531 -9.236  -9.026  0.38 15.31 ?  108  LEU   A CB   1 
ATOM   2432 C  CG   A LEU   A 1 108 ? 27.512 -9.415  -10.173 0.62 15.56 ?  108  LEU   A CG   1 
ATOM   2433 C  CG   B LEU   A 1 108 ? 27.530 -9.441  -10.168 0.38 16.40 ?  108  LEU   A CG   1 
ATOM   2434 C  CD1  A LEU   A 1 108 ? 27.937 -8.086  -10.775 0.62 16.18 ?  108  LEU   A CD1  1 
ATOM   2435 C  CD1  B LEU   A 1 108 ? 28.081 -8.112  -10.657 0.38 16.82 ?  108  LEU   A CD1  1 
ATOM   2436 C  CD2  A LEU   A 1 108 ? 28.733 -10.177 -9.673  0.62 17.15 ?  108  LEU   A CD2  1 
ATOM   2437 C  CD2  B LEU   A 1 108 ? 28.666 -10.358 -9.733  0.38 17.34 ?  108  LEU   A CD2  1 
ATOM   2438 H  H    A LEU   A 1 108 ? 24.656 -10.268 -10.266 0.62 18.30 ?  108  LEU   A H    1 
ATOM   2439 H  H    B LEU   A 1 108 ? 24.860 -10.496 -10.270 0.38 18.59 ?  108  LEU   A H    1 
ATOM   2440 H  HA   A LEU   A 1 108 ? 26.407 -11.210 -8.545  0.62 16.70 ?  108  LEU   A HA   1 
ATOM   2441 H  HA   B LEU   A 1 108 ? 26.512 -11.170 -8.362  0.38 17.75 ?  108  LEU   A HA   1 
ATOM   2442 H  HB2  A LEU   A 1 108 ? 25.853 -8.566  -9.337  0.62 16.73 ?  108  LEU   A HB2  1 
ATOM   2443 H  HB2  B LEU   A 1 108 ? 25.861 -8.607  -9.333  0.38 18.39 ?  108  LEU   A HB2  1 
ATOM   2444 H  HB3  A LEU   A 1 108 ? 26.980 -8.895  -8.270  0.62 16.73 ?  108  LEU   A HB3  1 
ATOM   2445 H  HB3  B LEU   A 1 108 ? 27.017 -8.857  -8.279  0.38 18.39 ?  108  LEU   A HB3  1 
ATOM   2446 H  HG   A LEU   A 1 108 ? 27.105 -9.942  -10.879 0.62 18.69 ?  108  LEU   A HG   1 
ATOM   2447 H  HG   B LEU   A 1 108 ? 27.075 -9.865  -10.913 0.38 19.70 ?  108  LEU   A HG   1 
ATOM   2448 H  HD11 A LEU   A 1 108 ? 28.560 -8.252  -11.504 0.62 19.43 ?  108  LEU   A HD11 1 
ATOM   2449 H  HD11 B LEU   A 1 108 ? 28.696 -8.274  -11.390 0.38 20.20 ?  108  LEU   A HD11 1 
ATOM   2450 H  HD12 A LEU   A 1 108 ? 27.154 -7.624  -11.111 0.62 19.43 ?  108  LEU   A HD12 1 
ATOM   2451 H  HD12 B LEU   A 1 108 ? 27.345 -7.557  -10.961 0.38 20.20 ?  108  LEU   A HD12 1 
ATOM   2452 H  HD13 A LEU   A 1 108 ? 28.370 -7.551  -10.091 0.62 19.43 ?  108  LEU   A HD13 1 
ATOM   2453 H  HD13 B LEU   A 1 108 ? 28.545 -7.674  -9.927  0.38 20.20 ?  108  LEU   A HD13 1 
ATOM   2454 H  HD21 A LEU   A 1 108 ? 29.403 -10.196 -10.373 0.62 20.59 ?  108  LEU   A HD21 1 
ATOM   2455 H  HD21 B LEU   A 1 108 ? 29.378 -10.310 -10.389 0.38 20.82 ?  108  LEU   A HD21 1 
ATOM   2456 H  HD22 A LEU   A 1 108 ? 29.085 -9.727  -8.889  0.62 20.59 ?  108  LEU   A HD22 1 
ATOM   2457 H  HD22 B LEU   A 1 108 ? 28.992 -10.062 -8.868  0.38 20.82 ?  108  LEU   A HD22 1 
ATOM   2458 H  HD23 A LEU   A 1 108 ? 28.468 -11.082 -9.444  0.62 20.59 ?  108  LEU   A HD23 1 
ATOM   2459 H  HD23 B LEU   A 1 108 ? 28.332 -11.265 -9.669  0.38 20.82 ?  108  LEU   A HD23 1 
ATOM   2460 N  N    . LEU   A 1 109 ? 23.736 -10.347 -7.258  1.00 12.68 ?  109  LEU   A N    1 
ATOM   2461 C  CA   . LEU   A 1 109 ? 23.021 -10.221 -5.994  1.00 12.14 ?  109  LEU   A CA   1 
ATOM   2462 C  C    . LEU   A 1 109 ? 23.359 -11.373 -5.053  1.00 11.58 ?  109  LEU   A C    1 
ATOM   2463 O  O    . LEU   A 1 109 ? 23.488 -11.177 -3.840  1.00 11.97 ?  109  LEU   A O    1 
ATOM   2464 C  CB   . LEU   A 1 109 ? 21.518 -10.136 -6.253  1.00 13.14 ?  109  LEU   A CB   1 
ATOM   2465 C  CG   . LEU   A 1 109 ? 20.622 -9.852  -5.045  1.00 13.64 ?  109  LEU   A CG   1 
ATOM   2466 C  CD1  . LEU   A 1 109 ? 21.075 -8.601  -4.314  1.00 13.74 ?  109  LEU   A CD1  1 
ATOM   2467 C  CD2  . LEU   A 1 109 ? 19.167 -9.724  -5.476  1.00 14.59 ?  109  LEU   A CD2  1 
ATOM   2468 H  H    A LEU   A 1 109 ? 23.226 -10.440 -7.945  0.62 15.24 ?  109  LEU   A H    1 
ATOM   2469 H  H    B LEU   A 1 109 ? 23.241 -10.480 -7.950  0.38 15.24 ?  109  LEU   A H    1 
ATOM   2470 H  HA   . LEU   A 1 109 ? 23.299 -9.395  -5.567  1.00 14.58 ?  109  LEU   A HA   1 
ATOM   2471 H  HB2  . LEU   A 1 109 ? 21.360 -9.422  -6.894  1.00 15.79 ?  109  LEU   A HB2  1 
ATOM   2472 H  HB3  . LEU   A 1 109 ? 21.225 -10.976 -6.632  1.00 15.79 ?  109  LEU   A HB3  1 
ATOM   2473 H  HG   . LEU   A 1 109 ? 20.680 -10.595 -4.426  1.00 16.38 ?  109  LEU   A HG   1 
ATOM   2474 H  HD11 . LEU   A 1 109 ? 20.377 -8.309  -3.712  1.00 16.51 ?  109  LEU   A HD11 1 
ATOM   2475 H  HD12 . LEU   A 1 109 ? 21.884 -8.801  -3.816  1.00 16.51 ?  109  LEU   A HD12 1 
ATOM   2476 H  HD13 . LEU   A 1 109 ? 21.259 -7.905  -4.969  1.00 16.51 ?  109  LEU   A HD13 1 
ATOM   2477 H  HD21 . LEU   A 1 109 ? 18.629 -9.448  -4.713  1.00 17.53 ?  109  LEU   A HD21 1 
ATOM   2478 H  HD22 . LEU   A 1 109 ? 19.097 -9.060  -6.180  1.00 17.53 ?  109  LEU   A HD22 1 
ATOM   2479 H  HD23 . LEU   A 1 109 ? 18.851 -10.583 -5.803  1.00 17.53 ?  109  LEU   A HD23 1 
ATOM   2480 N  N    . LYS   A 1 110 ? 23.509 -12.586 -5.587  1.00 11.39 ?  110  LYS   A N    1 
ATOM   2481 C  CA   . LYS   A 1 110 ? 23.887 -13.704 -4.732  1.00 11.34 ?  110  LYS   A CA   1 
ATOM   2482 C  C    . LYS   A 1 110 ? 25.265 -13.472 -4.120  1.00 10.84 ?  110  LYS   A C    1 
ATOM   2483 O  O    . LYS   A 1 110 ? 25.461 -13.677 -2.919  1.00 11.29 ?  110  LYS   A O    1 
ATOM   2484 C  CB   . LYS   A 1 110 ? 23.817 -15.026 -5.501  1.00 12.54 ?  110  LYS   A CB   1 
ATOM   2485 C  CG   . LYS   A 1 110 ? 24.005 -16.241 -4.593  1.00 12.33 ?  110  LYS   A CG   1 
ATOM   2486 C  CD   . LYS   A 1 110 ? 23.776 -17.559 -5.317  1.00 13.34 ?  110  LYS   A CD   1 
ATOM   2487 C  CE   . LYS   A 1 110 ? 23.871 -18.756 -4.378  1.00 14.35 ?  110  LYS   A CE   1 
ATOM   2488 N  NZ   . LYS   A 1 110 ? 22.694 -18.883 -3.484  1.00 14.66 ?  110  LYS   A NZ   1 
ATOM   2489 H  H    . LYS   A 1 110 ? 23.400 -12.781 -6.415  1.00 13.69 ?  110  LYS   A H    1 
ATOM   2490 H  HA   . LYS   A 1 110 ? 23.247 -13.760 -4.000  1.00 13.62 ?  110  LYS   A HA   1 
ATOM   2491 H  HB2  . LYS   A 1 110 ? 22.952 -15.097 -5.928  1.00 15.07 ?  110  LYS   A HB2  1 
ATOM   2492 H  HB3  . LYS   A 1 110 ? 24.522 -15.038 -6.165  1.00 15.07 ?  110  LYS   A HB3  1 
ATOM   2493 H  HG2  . LYS   A 1 110 ? 24.906 -16.239 -4.241  1.00 14.81 ?  110  LYS   A HG2  1 
ATOM   2494 H  HG3  . LYS   A 1 110 ? 23.364 -16.186 -3.861  1.00 14.81 ?  110  LYS   A HG3  1 
ATOM   2495 H  HD2  . LYS   A 1 110 ? 22.893 -17.553 -5.710  1.00 16.02 ?  110  LYS   A HD2  1 
ATOM   2496 H  HD3  . LYS   A 1 110 ? 24.452 -17.656 -6.004  1.00 16.02 ?  110  LYS   A HD3  1 
ATOM   2497 H  HE2  . LYS   A 1 110 ? 23.941 -19.566 -4.906  1.00 17.23 ?  110  LYS   A HE2  1 
ATOM   2498 H  HE3  . LYS   A 1 110 ? 24.663 -18.659 -3.819  1.00 17.23 ?  110  LYS   A HE3  1 
ATOM   2499 H  HZ1  . LYS   A 1 110 ? 22.784 -19.590 -2.957  1.00 17.60 ?  110  LYS   A HZ1  1 
ATOM   2500 H  HZ2  . LYS   A 1 110 ? 22.612 -18.151 -2.984  1.00 17.60 ?  110  LYS   A HZ2  1 
ATOM   2501 H  HZ3  . LYS   A 1 110 ? 21.954 -18.978 -3.975  1.00 17.60 ?  110  LYS   A HZ3  1 
ATOM   2502 N  N    . SER   A 1 111 ? 26.228 -13.029 -4.934  1.00 11.05 ?  111  SER   A N    1 
ATOM   2503 C  CA   . SER   A 1 111 ? 27.557 -12.724 -4.413  1.00 11.16 ?  111  SER   A CA   1 
ATOM   2504 C  C    . SER   A 1 111 ? 27.487 -11.677 -3.305  1.00 10.78 ?  111  SER   A C    1 
ATOM   2505 O  O    . SER   A 1 111 ? 28.186 -11.782 -2.289  1.00 11.51 ?  111  SER   A O    1 
ATOM   2506 C  CB   . SER   A 1 111 ? 28.448 -12.236 -5.553  1.00 12.69 ?  111  SER   A CB   1 
ATOM   2507 O  OG   . SER   A 1 111 ? 28.502 -13.201 -6.592  1.00 14.60 ?  111  SER   A OG   1 
ATOM   2508 H  H    . SER   A 1 111 ? 26.129 -12.890 -5.773  1.00 13.27 ?  111  SER   A H    1 
ATOM   2509 H  HA   . SER   A 1 111 ? 27.947 -13.534 -4.044  1.00 13.41 ?  111  SER   A HA   1 
ATOM   2510 H  HB2  . SER   A 1 111 ? 28.074 -11.415 -5.913  1.00 15.24 ?  111  SER   A HB2  1 
ATOM   2511 H  HB3  . SER   A 1 111 ? 29.338 -12.070 -5.208  1.00 15.24 ?  111  SER   A HB3  1 
ATOM   2512 H  HG   . SER   A 1 111 ? 29.015 -12.919 -7.209  1.00 17.54 ?  111  SER   A HG   1 
ATOM   2513 N  N    . ALA   A 1 112 ? 26.640 -10.660 -3.484  1.00 10.66 ?  112  ALA   A N    1 
ATOM   2514 C  CA   . ALA   A 1 112 ? 26.488 -9.620  -2.470  1.00 10.55 ?  112  ALA   A CA   1 
ATOM   2515 C  C    . ALA   A 1 112 ? 26.006 -10.219 -1.151  1.00 10.10 ?  112  ALA   A C    1 
ATOM   2516 O  O    . ALA   A 1 112 ? 26.553 -9.930  -0.081  1.00 10.69 ?  112  ALA   A O    1 
ATOM   2517 C  CB   . ALA   A 1 112 ? 25.522 -8.537  -2.967  1.00 11.13 ?  112  ALA   A CB   1 
ATOM   2518 H  H    . ALA   A 1 112 ? 26.155 -10.542 -4.184  1.00 12.81 ?  112  ALA   A H    1 
ATOM   2519 H  HA   . ALA   A 1 112 ? 27.348 -9.196  -2.312  1.00 12.68 ?  112  ALA   A HA   1 
ATOM   2520 H  HB1  . ALA   A 1 112 ? 25.449 -7.841  -2.290  1.00 13.37 ?  112  ALA   A HB1  1 
ATOM   2521 H  HB2  . ALA   A 1 112 ? 25.864 -8.156  -3.790  1.00 13.37 ?  112  ALA   A HB2  1 
ATOM   2522 H  HB3  . ALA   A 1 112 ? 24.651 -8.934  -3.122  1.00 13.37 ?  112  ALA   A HB3  1 
ATOM   2523 N  N    . TYR   A 1 113 ? 24.971 -11.062 -1.206  1.00 10.44 ?  113  TYR   A N    1 
ATOM   2524 C  CA   . TYR   A 1 113 ? 24.461 -11.665 0.021   1.00 10.22 ?  113  TYR   A CA   1 
ATOM   2525 C  C    . TYR   A 1 113 ? 25.466 -12.615 0.671   1.00 10.22 ?  113  TYR   A C    1 
ATOM   2526 O  O    . TYR   A 1 113 ? 25.424 -12.801 1.892   1.00 10.70 ?  113  TYR   A O    1 
ATOM   2527 C  CB   . TYR   A 1 113 ? 23.144 -12.397 -0.251  1.00 10.86 ?  113  TYR   A CB   1 
ATOM   2528 C  CG   . TYR   A 1 113 ? 21.924 -11.506 -0.187  1.00 10.80 ?  113  TYR   A CG   1 
ATOM   2529 C  CD1  . TYR   A 1 113 ? 21.551 -10.890 1.006   1.00 11.10 ?  113  TYR   A CD1  1 
ATOM   2530 C  CD2  . TYR   A 1 113 ? 21.130 -11.297 -1.304  1.00 11.25 ?  113  TYR   A CD2  1 
ATOM   2531 C  CE1  . TYR   A 1 113 ? 20.416 -10.101 1.084   1.00 11.88 ?  113  TYR   A CE1  1 
ATOM   2532 C  CE2  . TYR   A 1 113 ? 19.977 -10.497 -1.238  1.00 11.68 ?  113  TYR   A CE2  1 
ATOM   2533 C  CZ   . TYR   A 1 113 ? 19.635 -9.903  -0.039  1.00 11.57 ?  113  TYR   A CZ   1 
ATOM   2534 O  OH   . TYR   A 1 113 ? 18.507 -9.118  0.072   1.00 12.41 ?  113  TYR   A OH   1 
ATOM   2535 H  H    . TYR   A 1 113 ? 24.564 -11.298 -1.925  1.00 12.55 ?  113  TYR   A H    1 
ATOM   2536 H  HA   . TYR   A 1 113 ? 24.282 -10.960 0.657   1.00 12.28 ?  113  TYR   A HA   1 
ATOM   2537 H  HB2  . TYR   A 1 113 ? 23.178 -12.782 -1.139  1.00 13.05 ?  113  TYR   A HB2  1 
ATOM   2538 H  HB3  . TYR   A 1 113 ? 23.036 -13.100 0.409   1.00 13.05 ?  113  TYR   A HB3  1 
ATOM   2539 H  HD1  . TYR   A 1 113 ? 22.071 -11.031 1.770   1.00 13.34 ?  113  TYR   A HD1  1 
ATOM   2540 H  HD2  . TYR   A 1 113 ? 21.353 -11.706 -2.106  1.00 13.52 ?  113  TYR   A HD2  1 
ATOM   2541 H  HE1  . TYR   A 1 113 ? 20.191 -9.703  1.894   1.00 14.27 ?  113  TYR   A HE1  1 
ATOM   2542 H  HE2  . TYR   A 1 113 ? 19.447 -10.363 -1.989  1.00 14.03 ?  113  TYR   A HE2  1 
ATOM   2543 H  HH   . TYR   A 1 113 ? 18.120 -9.072  -0.676  1.00 14.91 ?  113  TYR   A HH   1 
ATOM   2544 N  N    . GLU   A 1 114 ? 26.365 -13.229 -0.111  1.00 10.29 ?  114  GLU   A N    1 
ATOM   2545 C  CA   . GLU   A 1 114 ? 27.358 -14.127 0.487   1.00 10.73 ?  114  GLU   A CA   1 
ATOM   2546 C  C    . GLU   A 1 114 ? 28.209 -13.416 1.534   1.00 10.34 ?  114  GLU   A C    1 
ATOM   2547 O  O    . GLU   A 1 114 ? 28.690 -14.049 2.483   1.00 10.91 ?  114  GLU   A O    1 
ATOM   2548 C  CB   . GLU   A 1 114 ? 28.232 -14.764 -0.602  1.00 10.75 ?  114  GLU   A CB   1 
ATOM   2549 C  CG   . GLU   A 1 114 ? 27.480 -15.826 -1.387  1.00 11.58 ?  114  GLU   A CG   1 
ATOM   2550 C  CD   . GLU   A 1 114 ? 28.202 -16.357 -2.626  1.00 11.80 ?  114  GLU   A CD   1 
ATOM   2551 O  OE1  . GLU   A 1 114 ? 29.150 -15.713 -3.131  1.00 12.10 ?  114  GLU   A OE1  1 
ATOM   2552 O  OE2  . GLU   A 1 114 ? 27.766 -17.424 -3.123  1.00 13.07 -1 114  GLU   A OE2  1 
ATOM   2553 H  H    . GLU   A 1 114 ? 26.419 -13.141 -0.969  1.00 12.36 ?  114  GLU   A H    1 
ATOM   2554 H  HA   . GLU   A 1 114 ? 26.884 -14.844 0.932   1.00 12.89 ?  114  GLU   A HA   1 
ATOM   2555 H  HB2  . GLU   A 1 114 ? 28.519 -14.076 -1.227  1.00 12.91 ?  114  GLU   A HB2  1 
ATOM   2556 H  HB3  . GLU   A 1 114 ? 29.001 -15.182 -0.191  1.00 12.91 ?  114  GLU   A HB3  1 
ATOM   2557 H  HG2  . GLU   A 1 114 ? 27.323 -16.585 -0.809  1.00 13.91 ?  114  GLU   A HG2  1 
ATOM   2558 H  HG3  . GLU   A 1 114 ? 26.635 -15.457 -1.682  1.00 13.91 ?  114  GLU   A HG3  1 
ATOM   2559 N  N    . ASN   A 1 115 ? 28.386 -12.097 1.400   1.00 10.22 ?  115  ASN   A N    1 
ATOM   2560 C  CA   . ASN   A 1 115 ? 29.152 -11.360 2.402   1.00 10.66 ?  115  ASN   A CA   1 
ATOM   2561 C  C    . ASN   A 1 115 ? 28.537 -11.487 3.791   1.00 10.28 ?  115  ASN   A C    1 
ATOM   2562 O  O    . ASN   A 1 115 ? 29.252 -11.411 4.798   1.00 10.86 ?  115  ASN   A O    1 
ATOM   2563 C  CB   . ASN   A 1 115 ? 29.259 -9.887  2.014   1.00 11.16 ?  115  ASN   A CB   1 
ATOM   2564 C  CG   . ASN   A 1 115 ? 30.063 -9.681  0.757   1.00 11.86 ?  115  ASN   A CG   1 
ATOM   2565 O  OD1  . ASN   A 1 115 ? 31.282 -9.802  0.774   1.00 14.96 ?  115  ASN   A OD1  1 
ATOM   2566 N  ND2  . ASN   A 1 115 ? 29.391 -9.372  -0.341  1.00 11.58 ?  115  ASN   A ND2  1 
ATOM   2567 H  H    . ASN   A 1 115 ? 28.073 -11.613 0.756   1.00 12.28 ?  115  ASN   A H    1 
ATOM   2568 H  HA   . ASN   A 1 115 ? 30.046 -11.727 2.439   1.00 12.80 ?  115  ASN   A HA   1 
ATOM   2569 H  HB2  . ASN   A 1 115 ? 28.368 -9.529  1.874   1.00 13.41 ?  115  ASN   A HB2  1 
ATOM   2570 H  HB3  . ASN   A 1 115 ? 29.696 -9.404  2.737   1.00 13.41 ?  115  ASN   A HB3  1 
ATOM   2571 H  HD21 . ASN   A 1 115 ? 29.810 -9.247  -1.082  1.00 13.91 ?  115  ASN   A HD21 1 
ATOM   2572 H  HD22 . ASN   A 1 115 ? 28.533 -9.313  -0.319  1.00 13.91 ?  115  ASN   A HD22 1 
ATOM   2573 N  N    . PHE   A 1 116 ? 27.210 -11.664 3.872   1.00 10.30 ?  116  PHE   A N    1 
ATOM   2574 C  CA   . PHE   A 1 116 ? 26.559 -11.761 5.176   1.00 10.34 ?  116  PHE   A CA   1 
ATOM   2575 C  C    . PHE   A 1 116 ? 27.035 -12.987 5.954   1.00 10.76 ?  116  PHE   A C    1 
ATOM   2576 O  O    . PHE   A 1 116 ? 26.965 -12.997 7.184   1.00 11.42 ?  116  PHE   A O    1 
ATOM   2577 C  CB   . PHE   A 1 116 ? 25.029 -11.889 5.047   1.00 10.66 ?  116  PHE   A CB   1 
ATOM   2578 C  CG   . PHE   A 1 116 ? 24.273 -10.649 4.567   1.00 10.52 ?  116  PHE   A CG   1 
ATOM   2579 C  CD1  . PHE   A 1 116 ? 24.843 -9.627  3.809   1.00 10.50 ?  116  PHE   A CD1  1 
ATOM   2580 C  CD2  . PHE   A 1 116 ? 22.919 -10.549 4.879   1.00 11.21 ?  116  PHE   A CD2  1 
ATOM   2581 C  CE1  . PHE   A 1 116 ? 24.076 -8.553  3.377   1.00 10.75 ?  116  PHE   A CE1  1 
ATOM   2582 C  CE2  . PHE   A 1 116 ? 22.152 -9.479  4.456   1.00 11.64 ?  116  PHE   A CE2  1 
ATOM   2583 C  CZ   . PHE   A 1 116 ? 22.721 -8.477  3.703   1.00 10.67 ?  116  PHE   A CZ   1 
ATOM   2584 H  H    . PHE   A 1 116 ? 26.677 -11.731 3.195   1.00 12.37 ?  116  PHE   A H    1 
ATOM   2585 H  HA   . PHE   A 1 116 ? 26.757 -10.968 5.695   1.00 12.43 ?  116  PHE   A HA   1 
ATOM   2586 H  HB2  . PHE   A 1 116 ? 24.839 -12.610 4.422   1.00 12.80 ?  116  PHE   A HB2  1 
ATOM   2587 H  HB3  . PHE   A 1 116 ? 24.675 -12.131 5.920   1.00 12.80 ?  116  PHE   A HB3  1 
ATOM   2588 H  HD1  . PHE   A 1 116 ? 25.738 -9.688  3.582   1.00 12.61 ?  116  PHE   A HD1  1 
ATOM   2589 H  HD2  . PHE   A 1 116 ? 22.513 -11.234 5.379   1.00 13.47 ?  116  PHE   A HD2  1 
ATOM   2590 H  HE1  . PHE   A 1 116 ? 24.471 -7.881  2.877   1.00 12.92 ?  116  PHE   A HE1  1 
ATOM   2591 H  HE2  . PHE   A 1 116 ? 21.245 -9.442  4.682   1.00 13.99 ?  116  PHE   A HE2  1 
ATOM   2592 H  HZ   . PHE   A 1 116 ? 22.210 -7.753  3.428   1.00 12.82 ?  116  PHE   A HZ   1 
ATOM   2593 N  N    . ASN   A 1 117 ? 27.484 -14.036 5.258   1.00 10.87 ?  117  ASN   A N    1 
ATOM   2594 C  CA   . ASN   A 1 117 ? 27.853 -15.280 5.928   1.00 11.16 ?  117  ASN   A CA   1 
ATOM   2595 C  C    . ASN   A 1 117 ? 29.118 -15.157 6.759   1.00 11.42 ?  117  ASN   A C    1 
ATOM   2596 O  O    . ASN   A 1 117 ? 29.418 -16.075 7.531   1.00 12.22 ?  117  ASN   A O    1 
ATOM   2597 C  CB   . ASN   A 1 117 ? 27.971 -16.403 4.905   1.00 11.21 ?  117  ASN   A CB   1 
ATOM   2598 C  CG   . ASN   A 1 117 ? 26.620 -16.792 4.359   1.00 11.56 ?  117  ASN   A CG   1 
ATOM   2599 O  OD1  . ASN   A 1 117 ? 25.640 -16.827 5.103   1.00 12.34 ?  117  ASN   A OD1  1 
ATOM   2600 N  ND2  . ASN   A 1 117 ? 26.544 -17.053 3.068   1.00 11.47 ?  117  ASN   A ND2  1 
ATOM   2601 H  H    . ASN   A 1 117 ? 27.571 -14.053 4.401   1.00 13.05 ?  117  ASN   A H    1 
ATOM   2602 H  HA   . ASN   A 1 117 ? 27.131 -15.513 6.535   1.00 13.41 ?  117  ASN   A HA   1 
ATOM   2603 H  HB2  . ASN   A 1 117 ? 28.529 -16.104 4.170   1.00 13.47 ?  117  ASN   A HB2  1 
ATOM   2604 H  HB3  . ASN   A 1 117 ? 28.363 -17.177 5.334   1.00 13.47 ?  117  ASN   A HB3  1 
ATOM   2605 H  HD21 . ASN   A 1 117 ? 25.795 -17.271 2.722   1.00 13.78 ?  117  ASN   A HD21 1 
ATOM   2606 H  HD22 . ASN   A 1 117 ? 27.254 -17.002 2.583   1.00 13.78 ?  117  ASN   A HD22 1 
ATOM   2607 N  N    . GLN   A 1 118 ? 29.847 -14.047 6.639   1.00 11.50 ?  118  GLN   A N    1 
ATOM   2608 C  CA   . GLN   A 1 118 ? 31.020 -13.809 7.470   1.00 12.25 ?  118  GLN   A CA   1 
ATOM   2609 C  C    . GLN   A 1 118 ? 30.671 -13.235 8.837   1.00 12.03 ?  118  GLN   A C    1 
ATOM   2610 O  O    . GLN   A 1 118 ? 31.585 -12.950 9.619   1.00 13.37 ?  118  GLN   A O    1 
ATOM   2611 C  CB   . GLN   A 1 118 ? 32.016 -12.902 6.737   1.00 12.52 ?  118  GLN   A CB   1 
ATOM   2612 C  CG   . GLN   A 1 118 ? 32.488 -13.483 5.408   1.00 12.60 ?  118  GLN   A CG   1 
ATOM   2613 C  CD   . GLN   A 1 118 ? 33.322 -14.743 5.586   1.00 12.58 ?  118  GLN   A CD   1 
ATOM   2614 O  OE1  . GLN   A 1 118 ? 34.185 -14.807 6.470   1.00 13.55 ?  118  GLN   A OE1  1 
ATOM   2615 N  NE2  . GLN   A 1 118 ? 33.078 -15.745 4.739   1.00 13.00 ?  118  GLN   A NE2  1 
ATOM   2616 H  H    . GLN   A 1 118 ? 29.671 -13.401 6.089   1.00 13.82 ?  118  GLN   A H    1 
ATOM   2617 H  HA   . GLN   A 1 118 ? 31.452 -14.662 7.619   1.00 14.72 ?  118  GLN   A HA   1 
ATOM   2618 H  HB2  . GLN   A 1 118 ? 31.597 -12.048 6.563   1.00 15.04 ?  118  GLN   A HB2  1 
ATOM   2619 H  HB3  . GLN   A 1 118 ? 32.797 -12.779 7.304   1.00 15.04 ?  118  GLN   A HB3  1 
ATOM   2620 H  HG2  . GLN   A 1 118 ? 31.714 -13.705 4.864   1.00 15.13 ?  118  GLN   A HG2  1 
ATOM   2621 H  HG3  . GLN   A 1 118 ? 33.035 -12.825 4.951   1.00 15.13 ?  118  GLN   A HG3  1 
ATOM   2622 H  HE21 . GLN   A 1 118 ? 32.463 -15.660 4.136   1.00 15.62 ?  118  GLN   A HE21 1 
ATOM   2623 H  HE22 . GLN   A 1 118 ? 33.518 -16.478 4.797   1.00 15.62 ?  118  GLN   A HE22 1 
ATOM   2624 N  N    . HIS   A 1 119 ? 29.381 -13.072 9.143   1.00 11.69 ?  119  HIS   A N    1 
ATOM   2625 C  CA   . HIS   A 1 119 ? 28.923 -12.460 10.385  1.00 12.19 ?  119  HIS   A CA   1 
ATOM   2626 C  C    . HIS   A 1 119 ? 27.788 -13.286 10.964  1.00 12.63 ?  119  HIS   A C    1 
ATOM   2627 O  O    . HIS   A 1 119 ? 26.843 -13.626 10.251  1.00 12.89 ?  119  HIS   A O    1 
ATOM   2628 C  CB   . HIS   A 1 119 ? 28.463 -11.030 10.107  1.00 12.45 ?  119  HIS   A CB   1 
ATOM   2629 C  CG   . HIS   A 1 119 ? 29.544 -10.220 9.493   1.00 13.58 ?  119  HIS   A CG   1 
ATOM   2630 N  ND1  . HIS   A 1 119 ? 30.522 -9.612  10.246  1.00 16.08 ?  119  HIS   A ND1  1 
ATOM   2631 C  CD2  . HIS   A 1 119 ? 29.880 -10.027 8.199   1.00 14.74 ?  119  HIS   A CD2  1 
ATOM   2632 C  CE1  . HIS   A 1 119 ? 31.390 -9.032  9.438   1.00 16.54 ?  119  HIS   A CE1  1 
ATOM   2633 N  NE2  . HIS   A 1 119 ? 31.030 -9.276  8.191   1.00 16.42 ?  119  HIS   A NE2  1 
ATOM   2634 H  H    . HIS   A 1 119 ? 28.729 -13.332 8.636   1.00 14.05 ?  119  HIS   A H    1 
ATOM   2635 H  HA   . HIS   A 1 119 ? 29.650 -12.441 11.027  1.00 14.65 ?  119  HIS   A HA   1 
ATOM   2636 H  HB2  . HIS   A 1 119 ? 27.709 -11.058 9.498   1.00 14.96 ?  119  HIS   A HB2  1 
ATOM   2637 H  HB3  . HIS   A 1 119 ? 28.204 -10.618 10.945  1.00 14.96 ?  119  HIS   A HB3  1 
ATOM   2638 H  HD2  . HIS   A 1 119 ? 29.419 -10.341 7.453   1.00 17.71 ?  119  HIS   A HD2  1 
ATOM   2639 H  HE1  . HIS   A 1 119 ? 32.128 -8.534  9.701   1.00 19.86 ?  119  HIS   A HE1  1 
ATOM   2640 H  HE2  . HIS   A 1 119 ? 31.434 -8.988  7.488   1.00 19.72 ?  119  HIS   A HE2  1 
ATOM   2641 N  N    A GLU   A 1 120 ? 27.881 -13.596 12.259  0.62 12.89 ?  120  GLU   A N    1 
ATOM   2642 N  N    B GLU   A 1 120 ? 27.881 -13.593 12.261  0.38 13.86 ?  120  GLU   A N    1 
ATOM   2643 C  CA   A GLU   A 1 120 ? 26.929 -14.525 12.865  0.62 14.31 ?  120  GLU   A CA   1 
ATOM   2644 C  CA   B GLU   A 1 120 ? 26.931 -14.520 12.872  0.38 15.63 ?  120  GLU   A CA   1 
ATOM   2645 C  C    A GLU   A 1 120 ? 25.512 -13.962 12.935  0.62 13.27 ?  120  GLU   A C    1 
ATOM   2646 C  C    B GLU   A 1 120 ? 25.514 -13.955 12.898  0.38 14.20 ?  120  GLU   A C    1 
ATOM   2647 O  O    A GLU   A 1 120 ? 24.541 -14.729 12.854  0.62 13.45 ?  120  GLU   A O    1 
ATOM   2648 O  O    B GLU   A 1 120 ? 24.542 -14.701 12.724  0.38 14.51 ?  120  GLU   A O    1 
ATOM   2649 C  CB   A GLU   A 1 120 ? 27.405 -14.931 14.261  0.62 17.87 ?  120  GLU   A CB   1 
ATOM   2650 C  CB   B GLU   A 1 120 ? 27.394 -14.896 14.281  0.38 19.30 ?  120  GLU   A CB   1 
ATOM   2651 C  CG   A GLU   A 1 120 ? 28.573 -15.900 14.254  0.62 23.40 ?  120  GLU   A CG   1 
ATOM   2652 C  CG   B GLU   A 1 120 ? 28.624 -15.789 14.308  0.38 23.47 ?  120  GLU   A CG   1 
ATOM   2653 C  CD   A GLU   A 1 120 ? 28.687 -16.676 15.549  0.62 28.13 ?  120  GLU   A CD   1 
ATOM   2654 C  CD   B GLU   A 1 120 ? 28.844 -16.440 15.657  0.38 26.85 ?  120  GLU   A CD   1 
ATOM   2655 O  OE1  A GLU   A 1 120 ? 28.427 -16.089 16.622  0.62 29.76 ?  120  GLU   A OE1  1 
ATOM   2656 O  OE1  B GLU   A 1 120 ? 28.245 -15.967 16.648  0.38 27.96 ?  120  GLU   A OE1  1 
ATOM   2657 O  OE2  A GLU   A 1 120 ? 29.020 -17.878 15.492  0.62 29.82 -1 120  GLU   A OE2  1 
ATOM   2658 O  OE2  B GLU   A 1 120 ? 29.617 -17.420 15.726  0.38 27.97 -1 120  GLU   A OE2  1 
ATOM   2659 H  H    A GLU   A 1 120 ? 28.480 -13.292 12.799  0.62 15.48 ?  120  GLU   A H    1 
ATOM   2660 H  H    B GLU   A 1 120 ? 28.477 -13.281 12.801  0.38 16.64 ?  120  GLU   A H    1 
ATOM   2661 H  HA   A GLU   A 1 120 ? 26.899 -15.328 12.328  0.62 17.18 ?  120  GLU   A HA   1 
ATOM   2662 H  HA   B GLU   A 1 120 ? 26.914 -15.333 12.349  0.38 18.77 ?  120  GLU   A HA   1 
ATOM   2663 H  HB2  A GLU   A 1 120 ? 27.684 -14.140 14.747  0.62 21.46 ?  120  GLU   A HB2  1 
ATOM   2664 H  HB2  B GLU   A 1 120 ? 27.611 -14.089 14.772  0.38 23.17 ?  120  GLU   A HB2  1 
ATOM   2665 H  HB3  A GLU   A 1 120 ? 26.672 -15.362 14.732  0.62 21.46 ?  120  GLU   A HB3  1 
ATOM   2666 H  HB3  B GLU   A 1 120 ? 26.678 -15.372 14.732  0.38 23.17 ?  120  GLU   A HB3  1 
ATOM   2667 H  HG2  A GLU   A 1 120 ? 28.455 -16.540 13.536  0.62 28.10 ?  120  GLU   A HG2  1 
ATOM   2668 H  HG2  B GLU   A 1 120 ? 28.529 -16.479 13.630  0.38 28.18 ?  120  GLU   A HG2  1 
ATOM   2669 H  HG3  A GLU   A 1 120 ? 29.398 -15.405 14.128  0.62 28.10 ?  120  GLU   A HG3  1 
ATOM   2670 H  HG3  B GLU   A 1 120 ? 29.410 -15.255 14.132  0.38 28.18 ?  120  GLU   A HG3  1 
ATOM   2671 N  N    . VAL   A 1 121 ? 25.374 -12.649 13.120  1.00 13.08 ?  121  VAL   A N    1 
ATOM   2672 C  CA   . VAL   A 1 121 ? 24.071 -11.995 13.228  1.00 12.95 ?  121  VAL   A CA   1 
ATOM   2673 C  C    . VAL   A 1 121 ? 24.178 -10.612 12.594  1.00 12.13 ?  121  VAL   A C    1 
ATOM   2674 O  O    . VAL   A 1 121 ? 25.138 -9.879  12.846  1.00 13.04 ?  121  VAL   A O    1 
ATOM   2675 C  CB   . VAL   A 1 121 ? 23.610 -11.852 14.700  1.00 16.47 ?  121  VAL   A CB   1 
ATOM   2676 C  CG1  . VAL   A 1 121 ? 22.211 -11.255 14.762  1.00 16.97 ?  121  VAL   A CG1  1 
ATOM   2677 C  CG2  . VAL   A 1 121 ? 23.637 -13.170 15.459  1.00 19.24 ?  121  VAL   A CG2  1 
ATOM   2678 H  H    A VAL   A 1 121 ? 26.034 -12.102 13.187  0.62 15.72 ?  121  VAL   A H    1 
ATOM   2679 H  H    B VAL   A 1 121 ? 26.034 -12.104 13.201  0.38 15.72 ?  121  VAL   A H    1 
ATOM   2680 H  HA   . VAL   A 1 121 ? 23.407 -12.511 12.746  1.00 15.56 ?  121  VAL   A HA   1 
ATOM   2681 H  HB   . VAL   A 1 121 ? 24.205 -11.239 15.153  1.00 19.78 ?  121  VAL   A HB   1 
ATOM   2682 H  HG11 . VAL   A 1 121 ? 21.881 -11.310 15.675  1.00 20.38 ?  121  VAL   A HG11 1 
ATOM   2683 H  HG12 . VAL   A 1 121 ? 22.243 -10.327 14.482  1.00 20.38 ?  121  VAL   A HG12 1 
ATOM   2684 H  HG13 . VAL   A 1 121 ? 21.622 -11.758 14.174  1.00 20.38 ?  121  VAL   A HG13 1 
ATOM   2685 H  HG21 . VAL   A 1 121 ? 23.282 -13.025 16.358  1.00 23.10 ?  121  VAL   A HG21 1 
ATOM   2686 H  HG22 . VAL   A 1 121 ? 23.083 -13.819 14.996  1.00 23.10 ?  121  VAL   A HG22 1 
ATOM   2687 H  HG23 . VAL   A 1 121 ? 24.547 -13.488 15.516  1.00 23.10 ?  121  VAL   A HG23 1 
ATOM   2688 N  N    . LEU   A 1 122 ? 23.169 -10.233 11.802  1.00 11.60 ?  122  LEU   A N    1 
ATOM   2689 C  CA   . LEU   A 1 122 ? 23.165 -8.934  11.129  1.00 11.52 ?  122  LEU   A CA   1 
ATOM   2690 C  C    . LEU   A 1 122 ? 21.761 -8.349  11.095  1.00 11.32 ?  122  LEU   A C    1 
ATOM   2691 O  O    . LEU   A 1 122 ? 20.778 -9.076  10.946  1.00 12.41 ?  122  LEU   A O    1 
ATOM   2692 C  CB   . LEU   A 1 122 ? 23.583 -9.030  9.657   1.00 13.03 ?  122  LEU   A CB   1 
ATOM   2693 C  CG   . LEU   A 1 122 ? 24.801 -9.862  9.302   1.00 12.91 ?  122  LEU   A CG   1 
ATOM   2694 C  CD1  . LEU   A 1 122 ? 24.415 -11.320 9.094   1.00 13.88 ?  122  LEU   A CD1  1 
ATOM   2695 C  CD2  . LEU   A 1 122 ? 25.459 -9.303  8.057   1.00 12.44 ?  122  LEU   A CD2  1 
ATOM   2696 H  H    . LEU   A 1 122 ? 22.469 -10.709 11.640  1.00 13.93 ?  122  LEU   A H    1 
ATOM   2697 H  HA   . LEU   A 1 122 ? 23.761 -8.317  11.587  1.00 13.83 ?  122  LEU   A HA   1 
ATOM   2698 H  HB2  . LEU   A 1 122 ? 22.844 -9.406  9.160   1.00 15.65 ?  122  LEU   A HB2  1 
ATOM   2699 H  HB3  . LEU   A 1 122 ? 23.762 -8.135  9.336   1.00 15.65 ?  122  LEU   A HB3  1 
ATOM   2700 H  HG   . LEU   A 1 122 ? 25.456 -9.824  10.019  1.00 15.51 ?  122  LEU   A HG   1 
ATOM   2701 H  HD11 . LEU   A 1 122 ? 25.195 -11.827 8.813   1.00 16.67 ?  122  LEU   A HD11 1 
ATOM   2702 H  HD12 . LEU   A 1 122 ? 24.077 -11.680 9.930   1.00 16.67 ?  122  LEU   A HD12 1 
ATOM   2703 H  HD13 . LEU   A 1 122 ? 23.728 -11.373 8.411   1.00 16.67 ?  122  LEU   A HD13 1 
ATOM   2704 H  HD21 . LEU   A 1 122 ? 26.211 -9.867  7.802   1.00 14.95 ?  122  LEU   A HD21 1 
ATOM   2705 H  HD22 . LEU   A 1 122 ? 24.809 -9.284  7.335   1.00 14.95 ?  122  LEU   A HD22 1 
ATOM   2706 H  HD23 . LEU   A 1 122 ? 25.774 -8.403  8.238   1.00 14.95 ?  122  LEU   A HD23 1 
ATOM   2707 N  N    . LEU   A 1 123 ? 21.689 -7.020  11.197  1.00 11.16 ?  123  LEU   A N    1 
ATOM   2708 C  CA   . LEU   A 1 123 ? 20.516 -6.231  10.820  1.00 10.76 ?  123  LEU   A CA   1 
ATOM   2709 C  C    . LEU   A 1 123 ? 20.762 -5.709  9.410   1.00 10.59 ?  123  LEU   A C    1 
ATOM   2710 O  O    . LEU   A 1 123 ? 21.813 -5.119  9.158   1.00 11.18 ?  123  LEU   A O    1 
ATOM   2711 C  CB   . LEU   A 1 123 ? 20.382 -5.046  11.778  1.00 11.28 ?  123  LEU   A CB   1 
ATOM   2712 C  CG   . LEU   A 1 123 ? 19.329 -3.996  11.426  1.00 12.07 ?  123  LEU   A CG   1 
ATOM   2713 C  CD1  . LEU   A 1 123 ? 17.928 -4.601  11.455  1.00 13.20 ?  123  LEU   A CD1  1 
ATOM   2714 C  CD2  . LEU   A 1 123 ? 19.428 -2.812  12.372  1.00 12.88 ?  123  LEU   A CD2  1 
ATOM   2715 H  H    . LEU   A 1 123 ? 22.341 -6.532  11.489  1.00 13.40 ?  123  LEU   A H    1 
ATOM   2716 H  HA   . LEU   A 1 123 ? 19.713 -6.771  10.846  1.00 12.92 ?  123  LEU   A HA   1 
ATOM   2717 H  HB2  . LEU   A 1 123 ? 20.158 -5.384  12.661  1.00 13.55 ?  123  LEU   A HB2  1 
ATOM   2718 H  HB3  . LEU   A 1 123 ? 21.235 -4.584  11.823  1.00 13.55 ?  123  LEU   A HB3  1 
ATOM   2719 H  HG   . LEU   A 1 123 ? 19.485 -3.666  10.525  1.00 14.50 ?  123  LEU   A HG   1 
ATOM   2720 H  HD11 . LEU   A 1 123 ? 17.276 -3.912  11.268  1.00 15.85 ?  123  LEU   A HD11 1 
ATOM   2721 H  HD12 . LEU   A 1 123 ? 17.873 -5.302  10.784  1.00 15.85 ?  123  LEU   A HD12 1 
ATOM   2722 H  HD13 . LEU   A 1 123 ? 17.769 -4.979  12.337  1.00 15.85 ?  123  LEU   A HD13 1 
ATOM   2723 H  HD21 . LEU   A 1 123 ? 18.753 -2.159  12.138  1.00 15.47 ?  123  LEU   A HD21 1 
ATOM   2724 H  HD22 . LEU   A 1 123 ? 19.285 -3.127  13.280  1.00 15.47 ?  123  LEU   A HD22 1 
ATOM   2725 H  HD23 . LEU   A 1 123 ? 20.312 -2.424  12.293  1.00 15.47 ?  123  LEU   A HD23 1 
ATOM   2726 N  N    A ALA   A 1 124 ? 19.791 -5.867  8.510   0.62 10.06 ?  124  ALA   A N    1 
ATOM   2727 N  N    B ALA   A 1 124 ? 19.835 -5.971  8.489   0.38 10.65 ?  124  ALA   A N    1 
ATOM   2728 C  CA   A ALA   A 1 124 ? 20.063 -5.567  7.111   0.62 9.83  ?  124  ALA   A CA   1 
ATOM   2729 C  CA   B ALA   A 1 124 ? 20.132 -5.740  7.082   0.38 11.03 ?  124  ALA   A CA   1 
ATOM   2730 C  C    A ALA   A 1 124 ? 18.809 -5.104  6.385   0.62 9.90  ?  124  ALA   A C    1 
ATOM   2731 C  C    B ALA   A 1 124 ? 18.903 -5.274  6.317   0.38 10.68 ?  124  ALA   A C    1 
ATOM   2732 O  O    A ALA   A 1 124 ? 17.685 -5.438  6.783   0.62 10.65 ?  124  ALA   A O    1 
ATOM   2733 O  O    B ALA   A 1 124 ? 17.774 -5.642  6.664   0.38 10.82 ?  124  ALA   A O    1 
ATOM   2734 C  CB   A ALA   A 1 124 ? 20.627 -6.789  6.384   0.62 9.81  ?  124  ALA   A CB   1 
ATOM   2735 C  CB   B ALA   A 1 124 ? 20.703 -7.002  6.418   0.38 11.60 ?  124  ALA   A CB   1 
ATOM   2736 H  H    A ALA   A 1 124 ? 18.990 -6.139  8.683   0.62 12.08 ?  124  ALA   A H    1 
ATOM   2737 H  H    B ALA   A 1 124 ? 19.046 -6.279  8.650   0.38 12.80 ?  124  ALA   A H    1 
ATOM   2738 H  HA   A ALA   A 1 124 ? 20.727 -4.859  7.080   0.62 11.81 ?  124  ALA   A HA   1 
ATOM   2739 H  HA   B ALA   A 1 124 ? 20.803 -5.047  7.024   0.38 13.26 ?  124  ALA   A HA   1 
ATOM   2740 H  HB1  A ALA   A 1 124 ? 20.800 -6.549  5.460   0.62 11.78 ?  124  ALA   A HB1  1 
ATOM   2741 H  HB1  B ALA   A 1 124 ? 20.893 -6.813  5.485   0.38 13.94 ?  124  ALA   A HB1  1 
ATOM   2742 H  HB2  A ALA   A 1 124 ? 21.456 -7.057  6.815   0.62 11.78 ?  124  ALA   A HB2  1 
ATOM   2743 H  HB2  B ALA   A 1 124 ? 21.525 -7.254  6.875   0.38 13.94 ?  124  ALA   A HB2  1 
ATOM   2744 H  HB3  A ALA   A 1 124 ? 19.982 -7.507  6.428   0.62 11.78 ?  124  ALA   A HB3  1 
ATOM   2745 H  HB3  B ALA   A 1 124 ? 20.056 -7.719  6.487   0.38 13.94 ?  124  ALA   A HB3  1 
ATOM   2746 N  N    A PRO   A 1 125 ? 18.978 -4.365  5.290   0.62 10.07 ?  125  PRO   A N    1 
ATOM   2747 N  N    B PRO   A 1 125 ? 19.096 -4.484  5.257   0.38 10.10 ?  125  PRO   A N    1 
ATOM   2748 C  CA   A PRO   A 1 125 ? 17.922 -4.182  4.294   0.62 10.84 ?  125  PRO   A CA   1 
ATOM   2749 C  CA   B PRO   A 1 125 ? 17.990 -4.131  4.364   0.38 10.50 ?  125  PRO   A CA   1 
ATOM   2750 C  C    A PRO   A 1 125 ? 17.993 -5.289  3.247   0.62 10.48 ?  125  PRO   A C    1 
ATOM   2751 C  C    B PRO   A 1 125 ? 17.947 -5.110  3.203   0.38 10.60 ?  125  PRO   A C    1 
ATOM   2752 O  O    A PRO   A 1 125 ? 18.966 -6.042  3.167   0.62 11.09 ?  125  PRO   A O    1 
ATOM   2753 O  O    B PRO   A 1 125 ? 18.848 -5.945  3.076   0.38 10.90 ?  125  PRO   A O    1 
ATOM   2754 C  CB   A PRO   A 1 125 ? 18.348 -2.858  3.644   0.62 11.00 ?  125  PRO   A CB   1 
ATOM   2755 C  CB   B PRO   A 1 125 ? 18.409 -2.745  3.870   0.38 10.35 ?  125  PRO   A CB   1 
ATOM   2756 C  CG   A PRO   A 1 125 ? 19.857 -3.009  3.568   0.62 11.33 ?  125  PRO   A CG   1 
ATOM   2757 C  CG   B PRO   A 1 125 ? 19.922 -2.894  3.727   0.38 10.66 ?  125  PRO   A CG   1 
ATOM   2758 C  CD   A PRO   A 1 125 ? 20.223 -3.678  4.888   0.62 11.21 ?  125  PRO   A CD   1 
ATOM   2759 C  CD   B PRO   A 1 125 ? 20.366 -3.906  4.782   0.38 9.85  ?  125  PRO   A CD   1 
ATOM   2760 H  HA   A PRO   A 1 125 ? 17.039 -4.124  4.691   0.62 13.02 ?  125  PRO   A HA   1 
ATOM   2761 H  HA   B PRO   A 1 125 ? 17.138 -4.095  4.838   0.38 12.61 ?  125  PRO   A HA   1 
ATOM   2762 H  HB2  A PRO   A 1 125 ? 17.951 -2.776  2.762   0.62 13.22 ?  125  PRO   A HB2  1 
ATOM   2763 H  HB2  B PRO   A 1 125 ? 17.986 -2.556  3.015   0.38 12.44 ?  125  PRO   A HB2  1 
ATOM   2764 H  HB3  A PRO   A 1 125 ? 18.093 -2.113  4.213   0.62 13.22 ?  125  PRO   A HB3  1 
ATOM   2765 H  HB3  B PRO   A 1 125 ? 18.176 -2.071  4.530   0.38 12.44 ?  125  PRO   A HB3  1 
ATOM   2766 H  HG2  A PRO   A 1 125 ? 20.098 -3.567  2.811   0.62 13.61 ?  125  PRO   A HG2  1 
ATOM   2767 H  HG2  B PRO   A 1 125 ? 20.127 -3.216  2.837   0.38 12.81 ?  125  PRO   A HG2  1 
ATOM   2768 H  HG3  A PRO   A 1 125 ? 20.270 -2.131  3.491   0.62 13.61 ?  125  PRO   A HG3  1 
ATOM   2769 H  HG3  B PRO   A 1 125 ? 20.341 -2.034  3.882   0.38 12.81 ?  125  PRO   A HG3  1 
ATOM   2770 H  HD2  A PRO   A 1 125 ? 20.942 -4.311  4.754   0.62 13.47 ?  125  PRO   A HD2  1 
ATOM   2771 H  HD2  B PRO   A 1 125 ? 20.928 -4.587  4.379   0.38 11.83 ?  125  PRO   A HD2  1 
ATOM   2772 H  HD3  A PRO   A 1 125 ? 20.460 -3.004  5.549   0.62 13.47 ?  125  PRO   A HD3  1 
ATOM   2773 H  HD3  B PRO   A 1 125 ? 20.823 -3.450  5.507   0.38 11.83 ?  125  PRO   A HD3  1 
ATOM   2774 N  N    A LEU   A 1 126 ? 16.956 -5.346  2.414   0.62 10.36 ?  126  LEU   A N    1 
ATOM   2775 N  N    B LEU   A 1 126 ? 16.944 -5.010  2.335   0.38 10.89 ?  126  LEU   A N    1 
ATOM   2776 C  CA   A LEU   A 1 126 ? 17.019 -6.154  1.205   0.62 11.38 ?  126  LEU   A CA   1 
ATOM   2777 C  CA   B LEU   A 1 126 ? 16.899 -5.846  1.140   0.38 10.61 ?  126  LEU   A CA   1 
ATOM   2778 C  C    A LEU   A 1 126 ? 17.964 -5.509  0.200   0.62 12.44 ?  126  LEU   A C    1 
ATOM   2779 C  C    B LEU   A 1 126 ? 17.821 -5.262  0.074   0.38 10.44 ?  126  LEU   A C    1 
ATOM   2780 O  O    A LEU   A 1 126 ? 17.786 -4.349  -0.185  0.62 14.46 ?  126  LEU   A O    1 
ATOM   2781 O  O    B LEU   A 1 126 ? 17.551 -4.186  -0.468  0.38 10.71 ?  126  LEU   A O    1 
ATOM   2782 C  CB   A LEU   A 1 126 ? 15.629 -6.307  0.599   0.62 12.04 ?  126  LEU   A CB   1 
ATOM   2783 C  CB   B LEU   A 1 126 ? 15.476 -5.920  0.605   0.38 11.47 ?  126  LEU   A CB   1 
ATOM   2784 C  CG   A LEU   A 1 126 ? 14.710 -7.294  1.319   0.62 13.13 ?  126  LEU   A CG   1 
ATOM   2785 C  CG   B LEU   A 1 126 ? 14.499 -6.812  1.360   0.38 11.82 ?  126  LEU   A CG   1 
ATOM   2786 C  CD1  A LEU   A 1 126 ? 13.279 -7.166  0.826   0.62 14.26 ?  126  LEU   A CD1  1 
ATOM   2787 C  CD1  B LEU   A 1 126 ? 13.134 -6.669  0.723   0.38 12.95 ?  126  LEU   A CD1  1 
ATOM   2788 C  CD2  A LEU   A 1 126 ? 15.206 -8.725  1.137   0.62 13.50 ?  126  LEU   A CD2  1 
ATOM   2789 C  CD2  B LEU   A 1 126 ? 14.944 -8.267  1.350   0.38 11.55 ?  126  LEU   A CD2  1 
ATOM   2790 H  H    A LEU   A 1 126 ? 16.218 -4.920  2.516   0.62 12.45 ?  126  LEU   A H    1 
ATOM   2791 H  H    B LEU   A 1 126 ? 16.275 -4.468  2.422   0.38 13.08 ?  126  LEU   A H    1 
ATOM   2792 H  HA   A LEU   A 1 126 ? 17.357 -7.035  1.415   0.62 13.67 ?  126  LEU   A HA   1 
ATOM   2793 H  HA   B LEU   A 1 126 ? 17.199 -6.744  1.366   0.38 12.75 ?  126  LEU   A HA   1 
ATOM   2794 H  HB2  A LEU   A 1 126 ? 15.183 -5.443  0.615   0.62 14.46 ?  126  LEU   A HB2  1 
ATOM   2795 H  HB2  B LEU   A 1 126 ? 15.106 -5.023  0.610   0.38 13.77 ?  126  LEU   A HB2  1 
ATOM   2796 H  HB3  A LEU   A 1 126 ? 15.712 -6.609  -0.319  0.62 14.46 ?  126  LEU   A HB3  1 
ATOM   2797 H  HB3  B LEU   A 1 126 ? 15.516 -6.247  -0.304  0.38 13.77 ?  126  LEU   A HB3  1 
ATOM   2798 H  HG   A LEU   A 1 126 ? 14.713 -7.099  2.267   0.62 15.77 ?  126  LEU   A HG   1 
ATOM   2799 H  HG   B LEU   A 1 126 ? 14.434 -6.515  2.282   0.38 14.21 ?  126  LEU   A HG   1 
ATOM   2800 H  HD11 A LEU   A 1 126 ? 12.720 -7.805  1.300   0.62 17.13 ?  126  LEU   A HD11 1 
ATOM   2801 H  HD11 B LEU   A 1 126 ? 12.505 -7.241  1.189   0.38 15.56 ?  126  LEU   A HD11 1 
ATOM   2802 H  HD12 A LEU   A 1 126 ? 12.965 -6.264  0.998   0.62 17.13 ?  126  LEU   A HD12 1 
ATOM   2803 H  HD12 B LEU   A 1 126 ? 12.849 -5.744  0.785   0.38 15.56 ?  126  LEU   A HD12 1 
ATOM   2804 H  HD13 A LEU   A 1 126 ? 13.252 -7.350  -0.126  0.62 17.13 ?  126  LEU   A HD13 1 
ATOM   2805 H  HD13 B LEU   A 1 126 ? 13.192 -6.934  -0.210  0.38 15.56 ?  126  LEU   A HD13 1 
ATOM   2806 H  HD21 A LEU   A 1 126 ? 14.538 -9.339  1.474   0.62 16.22 ?  126  LEU   A HD21 1 
ATOM   2807 H  HD21 B LEU   A 1 126 ? 14.225 -8.818  1.693   0.38 13.87 ?  126  LEU   A HD21 1 
ATOM   2808 H  HD22 A LEU   A 1 126 ? 15.357 -8.886  0.191   0.62 16.22 ?  126  LEU   A HD22 1 
ATOM   2809 H  HD22 B LEU   A 1 126 ? 15.154 -8.523  0.438   0.38 13.87 ?  126  LEU   A HD22 1 
ATOM   2810 H  HD23 A LEU   A 1 126 ? 16.036 -8.835  1.626   0.62 16.22 ?  126  LEU   A HD23 1 
ATOM   2811 H  HD23 B LEU   A 1 126 ? 15.730 -8.359  1.909   0.38 13.87 ?  126  LEU   A HD23 1 
ATOM   2812 N  N    A LEU   A 1 127 ? 18.956 -6.272  -0.240  0.62 12.31 ?  127  LEU   A N    1 
ATOM   2813 N  N    B LEU   A 1 127 ? 18.882 -5.988  -0.266  0.38 10.23 ?  127  LEU   A N    1 
ATOM   2814 C  CA   A LEU   A 1 127 ? 19.949 -5.756  -1.167  0.62 11.60 ?  127  LEU   A CA   1 
ATOM   2815 C  CA   B LEU   A 1 127 ? 19.864 -5.466  -1.207  0.38 10.65 ?  127  LEU   A CA   1 
ATOM   2816 C  C    A LEU   A 1 127 ? 19.338 -5.538  -2.540  0.62 10.64 ?  127  LEU   A C    1 
ATOM   2817 C  C    B LEU   A 1 127 ? 19.316 -5.437  -2.635  0.38 11.10 ?  127  LEU   A C    1 
ATOM   2818 O  O    A LEU   A 1 127 ? 18.526 -6.335  -3.020  0.62 11.22 ?  127  LEU   A O    1 
ATOM   2819 O  O    B LEU   A 1 127 ? 18.447 -6.226  -3.017  0.38 11.47 ?  127  LEU   A O    1 
ATOM   2820 C  CB   A LEU   A 1 127 ? 21.117 -6.731  -1.280  0.62 11.54 ?  127  LEU   A CB   1 
ATOM   2821 C  CB   B LEU   A 1 127 ? 21.141 -6.305  -1.158  0.38 11.03 ?  127  LEU   A CB   1 
ATOM   2822 C  CG   A LEU   A 1 127 ? 21.925 -6.947  -0.003  0.62 11.50 ?  127  LEU   A CG   1 
ATOM   2823 C  CG   B LEU   A 1 127 ? 21.918 -6.295  0.163   0.38 11.84 ?  127  LEU   A CG   1 
ATOM   2824 C  CD1  A LEU   A 1 127 ? 23.031 -7.944  -0.274  0.62 11.91 ?  127  LEU   A CD1  1 
ATOM   2825 C  CD1  B LEU   A 1 127 ? 23.106 -7.239  0.092   0.38 12.72 ?  127  LEU   A CD1  1 
ATOM   2826 C  CD2  A LEU   A 1 127 ? 22.502 -5.641  0.509   0.62 12.16 ?  127  LEU   A CD2  1 
ATOM   2827 C  CD2  B LEU   A 1 127 ? 22.375 -4.882  0.523   0.38 12.16 ?  127  LEU   A CD2  1 
ATOM   2828 H  H    A LEU   A 1 127 ? 19.076 -7.091  -0.016  0.62 14.79 ?  127  LEU   A H    1 
ATOM   2829 H  H    B LEU   A 1 127 ? 19.059 -6.776  0.045   0.38 12.29 ?  127  LEU   A H    1 
ATOM   2830 H  HA   A LEU   A 1 127 ? 20.282 -4.908  -0.846  0.62 13.93 ?  127  LEU   A HA   1 
ATOM   2831 H  HA   B LEU   A 1 127 ? 20.088 -4.559  -0.945  0.38 12.80 ?  127  LEU   A HA   1 
ATOM   2832 H  HB2  A LEU   A 1 127 ? 20.768 -7.594  -1.557  0.62 13.86 ?  127  LEU   A HB2  1 
ATOM   2833 H  HB2  B LEU   A 1 127 ? 20.906 -7.225  -1.348  0.38 13.25 ?  127  LEU   A HB2  1 
ATOM   2834 H  HB3  A LEU   A 1 127 ? 21.727 -6.399  -1.958  0.62 13.86 ?  127  LEU   A HB3  1 
ATOM   2835 H  HB3  B LEU   A 1 127 ? 21.739 -5.975  -1.846  0.38 13.25 ?  127  LEU   A HB3  1 
ATOM   2836 H  HG   A LEU   A 1 127 ? 21.343 -7.317  0.683   0.62 13.81 ?  127  LEU   A HG   1 
ATOM   2837 H  HG   B LEU   A 1 127 ? 21.336 -6.609  0.873   0.38 14.23 ?  127  LEU   A HG   1 
ATOM   2838 H  HD11 A LEU   A 1 127 ? 23.514 -8.112  0.551   0.62 14.30 ?  127  LEU   A HD11 1 
ATOM   2839 H  HD11 B LEU   A 1 127 ? 23.597 -7.191  0.928   0.38 15.28 ?  127  LEU   A HD11 1 
ATOM   2840 H  HD12 A LEU   A 1 127 ? 22.641 -8.771  -0.602  0.62 14.30 ?  127  LEU   A HD12 1 
ATOM   2841 H  HD12 B LEU   A 1 127 ? 22.783 -8.143  -0.050  0.38 15.28 ?  127  LEU   A HD12 1 
ATOM   2842 H  HD13 A LEU   A 1 127 ? 23.630 -7.575  -0.940  0.62 14.30 ?  127  LEU   A HD13 1 
ATOM   2843 H  HD13 B LEU   A 1 127 ? 23.678 -6.971  -0.643  0.38 15.28 ?  127  LEU   A HD13 1 
ATOM   2844 H  HD21 A LEU   A 1 127 ? 23.134 -5.834  1.218   0.62 14.60 ?  127  LEU   A HD21 1 
ATOM   2845 H  HD21 B LEU   A 1 127 ? 22.968 -4.927  1.289   0.38 14.61 ?  127  LEU   A HD21 1 
ATOM   2846 H  HD22 A LEU   A 1 127 ? 22.955 -5.191  -0.224  0.62 14.60 ?  127  LEU   A HD22 1 
ATOM   2847 H  HD22 B LEU   A 1 127 ? 22.843 -4.499  -0.236  0.38 14.61 ?  127  LEU   A HD22 1 
ATOM   2848 H  HD23 A LEU   A 1 127 ? 21.783 -5.086  0.844   0.62 14.60 ?  127  LEU   A HD23 1 
ATOM   2849 H  HD23 B LEU   A 1 127 ? 21.597 -4.344  0.738   0.38 14.61 ?  127  LEU   A HD23 1 
ATOM   2850 N  N    A SER   A 1 128 ? 19.750 -4.443  -3.171  0.62 10.70 ?  128  SER   A N    1 
ATOM   2851 N  N    B SER   A 1 128 ? 19.849 -4.497  -3.420  0.38 11.42 ?  128  SER   A N    1 
ATOM   2852 C  CA   A SER   A 1 128 ? 19.357 -4.034  -4.512  0.62 10.59 ?  128  SER   A CA   1 
ATOM   2853 C  CA   B SER   A 1 128 ? 19.548 -4.290  -4.837  0.38 11.44 ?  128  SER   A CA   1 
ATOM   2854 C  C    A SER   A 1 128 ? 17.898 -3.603  -4.607  0.62 10.70 ?  128  SER   A C    1 
ATOM   2855 C  C    B SER   A 1 128 ? 18.151 -3.748  -5.131  0.38 11.66 ?  128  SER   A C    1 
ATOM   2856 O  O    A SER   A 1 128 ? 17.426 -3.316  -5.710  0.62 12.00 ?  128  SER   A O    1 
ATOM   2857 O  O    B SER   A 1 128 ? 17.883 -3.320  -6.258  0.38 12.13 ?  128  SER   A O    1 
ATOM   2858 C  CB   A SER   A 1 128 ? 19.715 -5.069  -5.587  0.62 10.35 ?  128  SER   A CB   1 
ATOM   2859 C  CB   B SER   A 1 128 ? 19.870 -5.529  -5.679  0.38 11.69 ?  128  SER   A CB   1 
ATOM   2860 O  OG   A SER   A 1 128 ? 21.120 -5.273  -5.641  0.62 10.86 ?  128  SER   A OG   1 
ATOM   2861 O  OG   B SER   A 1 128 ? 21.273 -5.688  -5.815  0.38 11.73 ?  128  SER   A OG   1 
ATOM   2862 H  H    A SER   A 1 128 ? 20.302 -3.884  -2.811  0.62 12.85 ?  128  SER   A H    1 
ATOM   2863 H  H    B SER   A 1 128 ? 20.442 -3.945  -3.132  0.38 13.72 ?  128  SER   A H    1 
ATOM   2864 H  HA   A SER   A 1 128 ? 19.880 -3.250  -4.719  0.62 12.72 ?  128  SER   A HA   1 
ATOM   2865 H  HA   B SER   A 1 128 ? 20.154 -3.607  -5.143  0.38 13.75 ?  128  SER   A HA   1 
ATOM   2866 H  HB2  A SER   A 1 128 ? 19.271 -5.905  -5.382  0.62 12.44 ?  128  SER   A HB2  1 
ATOM   2867 H  HB2  B SER   A 1 128 ? 19.501 -6.317  -5.253  0.38 14.05 ?  128  SER   A HB2  1 
ATOM   2868 H  HB3  A SER   A 1 128 ? 19.415 -4.736  -6.449  0.62 12.44 ?  128  SER   A HB3  1 
ATOM   2869 H  HB3  B SER   A 1 128 ? 19.484 -5.418  -6.564  0.38 14.05 ?  128  SER   A HB3  1 
ATOM   2870 H  HG   A SER   A 1 128 ? 21.508 -4.547  -5.795  0.62 13.05 ?  128  SER   A HG   1 
ATOM   2871 H  HG   B SER   A 1 128 ? 21.603 -5.004  -6.174  0.38 14.09 ?  128  SER   A HG   1 
ATOM   2872 N  N    A ALA   A 1 129 ? 17.184 -3.526  -3.482  0.62 11.16 ?  129  ALA   A N    1 
ATOM   2873 N  N    B ALA   A 1 129 ? 17.259 -3.747  -4.143  0.38 12.00 ?  129  ALA   A N    1 
ATOM   2874 C  CA   A ALA   A 1 129 ? 15.819 -3.024  -3.469  0.62 11.68 ?  129  ALA   A CA   1 
ATOM   2875 C  CA   B ALA   A 1 129 ? 15.970 -3.088  -4.310  0.38 12.85 ?  129  ALA   A CA   1 
ATOM   2876 C  C    A ALA   A 1 129 ? 15.830 -1.496  -3.483  0.62 10.81 ?  129  ALA   A C    1 
ATOM   2877 C  C    B ALA   A 1 129 ? 16.130 -1.608  -3.973  0.38 13.40 ?  129  ALA   A C    1 
ATOM   2878 O  O    A ALA   A 1 129 ? 16.879 -0.852  -3.583  0.62 10.53 ?  129  ALA   A O    1 
ATOM   2879 O  O    B ALA   A 1 129 ? 17.212 -1.046  -4.170  0.38 13.42 ?  129  ALA   A O    1 
ATOM   2880 C  CB   A ALA   A 1 129 ? 15.062 -3.571  -2.259  0.62 13.75 ?  129  ALA   A CB   1 
ATOM   2881 C  CB   B ALA   A 1 129 ? 14.905 -3.769  -3.448  0.38 13.61 ?  129  ALA   A CB   1 
ATOM   2882 H  H    A ALA   A 1 129 ? 17.470 -3.769  -2.704  0.62 13.41 ?  129  ALA   A H    1 
ATOM   2883 H  H    B ALA   A 1 129 ? 17.370 -4.126  -3.378  0.38 14.41 ?  129  ALA   A H    1 
ATOM   2884 H  HA   A ALA   A 1 129 ? 15.365 -3.324  -4.266  0.62 14.03 ?  129  ALA   A HA   1 
ATOM   2885 H  HA   B ALA   A 1 129 ? 15.695 -3.160  -5.237  0.38 15.44 ?  129  ALA   A HA   1 
ATOM   2886 H  HB1  A ALA   A 1 129 ? 14.151 -3.232  -2.276  0.62 16.51 ?  129  ALA   A HB1  1 
ATOM   2887 H  HB1  B ALA   A 1 129 ? 14.047 -3.350  -3.622  0.38 16.35 ?  129  ALA   A HB1  1 
ATOM   2888 H  HB2  A ALA   A 1 129 ? 15.054 -4.539  -2.302  0.62 16.51 ?  129  ALA   A HB2  1 
ATOM   2889 H  HB2  B ALA   A 1 129 ? 14.864 -4.709  -3.686  0.38 16.35 ?  129  ALA   A HB2  1 
ATOM   2890 H  HB3  A ALA   A 1 129 ? 15.505 -3.279  -1.446  0.62 16.51 ?  129  ALA   A HB3  1 
ATOM   2891 H  HB3  B ALA   A 1 129 ? 15.145 -3.672  -2.517  0.38 16.35 ?  129  ALA   A HB3  1 
ATOM   2892 N  N    A GLY   A 1 130 ? 14.641 -0.906  -3.393  0.62 12.42 ?  130  GLY   A N    1 
ATOM   2893 N  N    B GLY   A 1 130 ? 15.081 -0.960  -3.476  0.38 14.30 ?  130  GLY   A N    1 
ATOM   2894 C  CA   A GLY   A 1 130 ? 14.541 0.543   -3.388  0.62 12.91 ?  130  GLY   A CA   1 
ATOM   2895 C  CA   B GLY   A 1 130 ? 15.218 0.454   -3.168  0.38 14.49 ?  130  GLY   A CA   1 
ATOM   2896 C  C    A GLY   A 1 130 ? 15.174 1.149   -4.623  0.62 13.24 ?  130  GLY   A C    1 
ATOM   2897 C  C    B GLY   A 1 130 ? 15.560 1.223   -4.427  0.38 14.38 ?  130  GLY   A C    1 
ATOM   2898 O  O    A GLY   A 1 130 ? 14.991 0.665   -5.745  0.62 13.17 ?  130  GLY   A O    1 
ATOM   2899 O  O    B GLY   A 1 130 ? 14.985 0.991   -5.496  0.38 14.90 ?  130  GLY   A O    1 
ATOM   2900 H  H    A GLY   A 1 130 ? 13.888 -1.321  -3.336  0.62 14.92 ?  130  GLY   A H    1 
ATOM   2901 H  H    B GLY   A 1 130 ? 14.304 -1.296  -3.333  0.38 17.17 ?  130  GLY   A H    1 
ATOM   2902 H  HA2  A GLY   A 1 130 ? 13.606 0.804   -3.356  0.62 15.50 ?  130  GLY   A HA2  1 
ATOM   2903 H  HA2  B GLY   A 1 130 ? 14.387 0.792   -2.799  0.38 17.41 ?  130  GLY   A HA2  1 
ATOM   2904 H  HA3  A GLY   A 1 130 ? 14.989 0.899   -2.607  0.62 15.50 ?  130  GLY   A HA3  1 
ATOM   2905 H  HA3  B GLY   A 1 130 ? 15.927 0.583   -2.516  0.38 17.41 ?  130  GLY   A HA3  1 
ATOM   2906 N  N    A ILE   A 1 131 ? 15.947 2.220   -4.413  0.62 13.13 ?  131  ILE   A N    1 
ATOM   2907 N  N    B ILE   A 1 131 ? 16.533 2.136   -4.317  0.38 13.62 ?  131  ILE   A N    1 
ATOM   2908 C  CA   A ILE   A 1 131 ? 16.517 2.980   -5.523  0.62 13.03 ?  131  ILE   A CA   1 
ATOM   2909 C  CA   B ILE   A 1 131 ? 16.942 2.939   -5.470  0.38 13.02 ?  131  ILE   A CA   1 
ATOM   2910 C  C    A ILE   A 1 131 ? 17.528 2.193   -6.342  0.62 12.87 ?  131  ILE   A C    1 
ATOM   2911 C  C    B ILE   A 1 131 ? 17.851 2.185   -6.424  0.38 12.91 ?  131  ILE   A C    1 
ATOM   2912 O  O    A ILE   A 1 131 ? 17.941 2.672   -7.405  0.62 14.07 ?  131  ILE   A O    1 
ATOM   2913 O  O    B ILE   A 1 131 ? 18.226 2.743   -7.465  0.38 13.51 ?  131  ILE   A O    1 
ATOM   2914 C  CB   A ILE   A 1 131 ? 17.088 4.337   -5.050  0.62 13.97 ?  131  ILE   A CB   1 
ATOM   2915 C  CB   B ILE   A 1 131 ? 17.577 4.285   -5.059  0.38 13.14 ?  131  ILE   A CB   1 
ATOM   2916 C  CG1  A ILE   A 1 131 ? 18.358 4.153   -4.211  0.62 15.69 ?  131  ILE   A CG1  1 
ATOM   2917 C  CG1  B ILE   A 1 131 ? 18.891 4.063   -4.302  0.38 13.78 ?  131  ILE   A CG1  1 
ATOM   2918 C  CG2  A ILE   A 1 131 ? 16.024 5.110   -4.276  0.62 14.20 ?  131  ILE   A CG2  1 
ATOM   2919 C  CG2  B ILE   A 1 131 ? 16.604 5.087   -4.210  0.38 13.55 ?  131  ILE   A CG2  1 
ATOM   2920 C  CD1  A ILE   A 1 131 ? 19.037 5.472   -3.838  0.62 16.71 ?  131  ILE   A CD1  1 
ATOM   2921 C  CD1  B ILE   A 1 131 ? 19.542 5.349   -3.810  0.38 14.60 ?  131  ILE   A CD1  1 
ATOM   2922 H  H    A ILE   A 1 131 ? 16.143 2.530   -3.639  0.62 15.77 ?  131  ILE   A H    1 
ATOM   2923 H  H    B ILE   A 1 131 ? 16.968 2.307   -3.597  0.38 16.36 ?  131  ILE   A H    1 
ATOM   2924 H  HA   A ILE   A 1 131 ? 15.794 3.184   -6.129  0.62 15.65 ?  131  ILE   A HA   1 
ATOM   2925 H  HA   B ILE   A 1 131 ? 16.150 3.151   -5.976  0.38 15.64 ?  131  ILE   A HA   1 
ATOM   2926 H  HB   A ILE   A 1 131 ? 17.316 4.852   -5.836  0.62 16.78 ?  131  ILE   A HB   1 
ATOM   2927 H  HB   B ILE   A 1 131 ? 17.770 4.790   -5.866  0.38 15.79 ?  131  ILE   A HB   1 
ATOM   2928 H  HG12 A ILE   A 1 131 ? 18.128 3.691   -3.390  0.62 18.84 ?  131  ILE   A HG12 1 
ATOM   2929 H  HG12 B ILE   A 1 131 ? 18.714 3.505   -3.530  0.38 16.55 ?  131  ILE   A HG12 1 
ATOM   2930 H  HG13 A ILE   A 1 131 ? 18.998 3.626   -4.716  0.62 18.84 ?  131  ILE   A HG13 1 
ATOM   2931 H  HG13 B ILE   A 1 131 ? 19.522 3.621   -4.890  0.38 16.55 ?  131  ILE   A HG13 1 
ATOM   2932 H  HG21 A ILE   A 1 131 ? 16.357 5.998   -4.084  0.62 17.06 ?  131  ILE   A HG21 1 
ATOM   2933 H  HG21 B ILE   A 1 131 ? 16.923 5.998   -4.136  0.38 16.27 ?  131  ILE   A HG21 1 
ATOM   2934 H  HG22 A ILE   A 1 131 ? 15.222 5.165   -4.818  0.62 17.06 ?  131  ILE   A HG22 1 
ATOM   2935 H  HG22 B ILE   A 1 131 ? 15.732 5.074   -4.635  0.38 16.27 ?  131  ILE   A HG22 1 
ATOM   2936 H  HG23 A ILE   A 1 131 ? 15.831 4.640   -3.448  0.62 17.06 ?  131  ILE   A HG23 1 
ATOM   2937 H  HG23 B ILE   A 1 131 ? 16.547 4.680   -3.330  0.38 16.27 ?  131  ILE   A HG23 1 
ATOM   2938 H  HD11 A ILE   A 1 131 ? 19.892 5.278   -3.419  0.62 20.07 ?  131  ILE   A HD11 1 
ATOM   2939 H  HD11 B ILE   A 1 131 ? 20.434 5.147   -3.490  0.38 17.54 ?  131  ILE   A HD11 1 
ATOM   2940 H  HD12 A ILE   A 1 131 ? 19.177 5.995   -4.643  0.62 20.07 ?  131  ILE   A HD12 1 
ATOM   2941 H  HD12 B ILE   A 1 131 ? 19.587 5.981   -4.544  0.38 17.54 ?  131  ILE   A HD12 1 
ATOM   2942 H  HD13 A ILE   A 1 131 ? 18.470 5.958   -3.221  0.62 20.07 ?  131  ILE   A HD13 1 
ATOM   2943 H  HD13 B ILE   A 1 131 ? 19.008 5.719   -3.088  0.38 17.54 ?  131  ILE   A HD13 1 
ATOM   2944 N  N    A PHE   A 1 132 ? 17.929 0.997   -5.890  0.62 12.43 ?  132  PHE   A N    1 
ATOM   2945 N  N    B PHE   A 1 132 ? 18.209 0.933   -6.117  0.38 12.68 ?  132  PHE   A N    1 
ATOM   2946 C  CA   A PHE   A 1 132 ? 18.788 0.125   -6.689  0.62 12.59 ?  132  PHE   A CA   1 
ATOM   2947 C  CA   B PHE   A 1 132 ? 19.093 0.153   -6.978  0.38 12.60 ?  132  PHE   A CA   1 
ATOM   2948 C  C    A PHE   A 1 132 ? 18.019 -0.643  -7.768  0.62 12.64 ?  132  PHE   A C    1 
ATOM   2949 C  C    B PHE   A 1 132 ? 18.364 -0.575  -8.108  0.38 13.20 ?  132  PHE   A C    1 
ATOM   2950 O  O    A PHE   A 1 132 ? 18.644 -1.292  -8.614  0.62 13.35 ?  132  PHE   A O    1 
ATOM   2951 O  O    B PHE   A 1 132 ? 19.028 -1.127  -8.994  0.38 14.42 ?  132  PHE   A O    1 
ATOM   2952 C  CB   A PHE   A 1 132 ? 19.559 -0.849  -5.786  0.62 12.36 ?  132  PHE   A CB   1 
ATOM   2953 C  CB   B PHE   A 1 132 ? 19.921 -0.846  -6.153  0.38 11.54 ?  132  PHE   A CB   1 
ATOM   2954 C  CG   A PHE   A 1 132 ? 20.783 -0.254  -5.118  0.62 12.04 ?  132  PHE   A CG   1 
ATOM   2955 C  CG   B PHE   A 1 132 ? 21.119 -0.231  -5.462  0.38 11.58 ?  132  PHE   A CG   1 
ATOM   2956 C  CD1  A PHE   A 1 132 ? 20.665 0.761   -4.179  0.62 12.64 ?  132  PHE   A CD1  1 
ATOM   2957 C  CD1  B PHE   A 1 132 ? 20.968 0.832   -4.585  0.38 12.14 ?  132  PHE   A CD1  1 
ATOM   2958 C  CD2  A PHE   A 1 132 ? 22.048 -0.756  -5.394  0.62 12.25 ?  132  PHE   A CD2  1 
ATOM   2959 C  CD2  B PHE   A 1 132 ? 22.396 -0.731  -5.680  0.38 12.58 ?  132  PHE   A CD2  1 
ATOM   2960 C  CE1  A PHE   A 1 132 ? 21.787 1.288   -3.557  0.62 12.96 ?  132  PHE   A CE1  1 
ATOM   2961 C  CE1  B PHE   A 1 132 ? 22.068 1.393   -3.948  0.38 12.71 ?  132  PHE   A CE1  1 
ATOM   2962 C  CE2  A PHE   A 1 132 ? 23.173 -0.240  -4.770  0.62 12.91 ?  132  PHE   A CE2  1 
ATOM   2963 C  CE2  B PHE   A 1 132 ? 23.498 -0.177  -5.043  0.38 13.33 ?  132  PHE   A CE2  1 
ATOM   2964 C  CZ   A PHE   A 1 132 ? 23.039 0.787   -3.851  0.62 12.68 ?  132  PHE   A CZ   1 
ATOM   2965 C  CZ   B PHE   A 1 132 ? 23.330 0.884   -4.176  0.38 13.22 ?  132  PHE   A CZ   1 
ATOM   2966 H  H    A PHE   A 1 132 ? 17.718 0.666   -5.118  0.62 14.93 ?  132  PHE   A H    1 
ATOM   2967 H  H    B PHE   A 1 132 ? 17.960 0.512   -5.400  0.38 15.23 ?  132  PHE   A H    1 
ATOM   2968 H  HA   A PHE   A 1 132 ? 19.446 0.674   -7.134  0.62 15.12 ?  132  PHE   A HA   1 
ATOM   2969 H  HA   B PHE   A 1 132 ? 19.725 0.764   -7.381  0.38 15.14 ?  132  PHE   A HA   1 
ATOM   2970 H  HB2  A PHE   A 1 132 ? 18.970 -1.158  -5.079  0.62 14.84 ?  132  PHE   A HB2  1 
ATOM   2971 H  HB2  B PHE   A 1 132 ? 19.361 -1.239  -5.469  0.38 13.87 ?  132  PHE   A HB2  1 
ATOM   2972 H  HB3  A PHE   A 1 132 ? 19.857 -1.605  -6.317  0.62 14.84 ?  132  PHE   A HB3  1 
ATOM   2973 H  HB3  B PHE   A 1 132 ? 20.254 -1.543  -6.745  0.38 13.87 ?  132  PHE   A HB3  1 
ATOM   2974 H  HD1  A PHE   A 1 132 ? 19.828 1.103   -3.974  0.62 15.18 ?  132  PHE   A HD1  1 
ATOM   2975 H  HD1  B PHE   A 1 132 ? 20.122 1.178   -4.424  0.38 14.59 ?  132  PHE   A HD1  1 
ATOM   2976 H  HD2  A PHE   A 1 132 ? 22.146 -1.448  -6.011  0.62 14.71 ?  132  PHE   A HD2  1 
ATOM   2977 H  HD2  B PHE   A 1 132 ? 22.520 -1.446  -6.261  0.38 15.11 ?  132  PHE   A HD2  1 
ATOM   2978 H  HE1  A PHE   A 1 132 ? 21.700 1.976   -2.936  0.62 15.57 ?  132  PHE   A HE1  1 
ATOM   2979 H  HE1  B PHE   A 1 132 ? 21.954 2.107   -3.363  0.38 15.26 ?  132  PHE   A HE1  1 
ATOM   2980 H  HE2  A PHE   A 1 132 ? 24.018 -0.579  -4.976  0.62 15.51 ?  132  PHE   A HE2  1 
ATOM   2981 H  HE2  B PHE   A 1 132 ? 24.352 -0.520  -5.202  0.38 16.01 ?  132  PHE   A HE2  1 
ATOM   2982 H  HZ   A PHE   A 1 132 ? 23.795 1.139   -3.436  0.62 15.23 ?  132  PHE   A HZ   1 
ATOM   2983 H  HZ   B PHE   A 1 132 ? 24.071 1.260   -3.751  0.38 15.88 ?  132  PHE   A HZ   1 
ATOM   2984 N  N    A GLY   A 1 133 ? 16.688 -0.613  -7.747  0.62 13.21 ?  133  GLY   A N    1 
ATOM   2985 N  N    B GLY   A 1 133 ? 17.030 -0.618  -8.094  0.38 13.10 ?  133  GLY   A N    1 
ATOM   2986 C  CA   A GLY   A 1 133 ? 15.890 -1.002  -8.897  0.62 13.93 ?  133  GLY   A CA   1 
ATOM   2987 C  CA   B GLY   A 1 133 ? 16.250 -0.983  -9.261  0.38 13.70 ?  133  GLY   A CA   1 
ATOM   2988 C  C    A GLY   A 1 133 ? 15.639 -2.481  -9.117  0.62 14.39 ?  133  GLY   A C    1 
ATOM   2989 C  C    B GLY   A 1 133 ? 15.632 -2.369  -9.248  0.38 14.14 ?  133  GLY   A C    1 
ATOM   2990 O  O    A GLY   A 1 133 ? 15.079 -2.833  -10.162 0.62 15.07 ?  133  GLY   A O    1 
ATOM   2991 O  O    B GLY   A 1 133 ? 14.671 -2.599  -9.995  0.38 14.46 ?  133  GLY   A O    1 
ATOM   2992 H  H    A GLY   A 1 133 ? 16.223 -0.373  -7.067  0.62 15.87 ?  133  GLY   A H    1 
ATOM   2993 H  H    B GLY   A 1 133 ? 16.555 -0.441  -7.399  0.38 15.74 ?  133  GLY   A H    1 
ATOM   2994 H  HA2  A GLY   A 1 133 ? 15.026 -0.572  -8.826  0.62 16.73 ?  133  GLY   A HA2  1 
ATOM   2995 H  HA2  B GLY   A 1 133 ? 15.530 -0.346  -9.363  0.38 16.45 ?  133  GLY   A HA2  1 
ATOM   2996 H  HA3  A GLY   A 1 133 ? 16.323 -0.668  -9.697  0.62 16.73 ?  133  GLY   A HA3  1 
ATOM   2997 H  HA3  B GLY   A 1 133 ? 16.818 -0.920  -10.045 0.38 16.45 ?  133  GLY   A HA3  1 
ATOM   2998 N  N    A ALA   A 1 134 ? 16.025 -3.361  -8.195  0.62 13.91 ?  134  ALA   A N    1 
ATOM   2999 N  N    B ALA   A 1 134 ? 16.142 -3.301  -8.444  0.38 13.98 ?  134  ALA   A N    1 
ATOM   3000 C  CA   A ALA   A 1 134 ? 15.722 -4.776  -8.358  0.62 14.66 ?  134  ALA   A CA   1 
ATOM   3001 C  CA   B ALA   A 1 134 ? 15.686 -4.679  -8.561  0.38 14.08 ?  134  ALA   A CA   1 
ATOM   3002 C  C    A ALA   A 1 134 ? 14.357 -5.114  -7.760  0.62 14.85 ?  134  ALA   A C    1 
ATOM   3003 C  C    B ALA   A 1 134 ? 14.387 -4.912  -7.785  0.38 13.89 ?  134  ALA   A C    1 
ATOM   3004 O  O    A ALA   A 1 134 ? 13.779 -4.349  -6.983  0.62 15.88 ?  134  ALA   A O    1 
ATOM   3005 O  O    B ALA   A 1 134 ? 13.965 -4.107  -6.950  0.38 14.56 ?  134  ALA   A O    1 
ATOM   3006 C  CB   A ALA   A 1 134 ? 16.804 -5.647  -7.714  0.62 15.01 ?  134  ALA   A CB   1 
ATOM   3007 C  CB   B ALA   A 1 134 ? 16.771 -5.651  -8.102  0.38 14.43 ?  134  ALA   A CB   1 
ATOM   3008 H  H    A ALA   A 1 134 ? 16.468 -3.163  -7.480  0.62 16.71 ?  134  ALA   A H    1 
ATOM   3009 H  H    B ALA   A 1 134 ? 16.741 -3.161  -7.840  0.38 16.80 ?  134  ALA   A H    1 
ATOM   3010 H  HA   A ALA   A 1 134 ? 15.701 -4.983  -9.306  0.62 17.61 ?  134  ALA   A HA   1 
ATOM   3011 H  HA   B ALA   A 1 134 ? 15.506 -4.859  -9.494  0.38 16.92 ?  134  ALA   A HA   1 
ATOM   3012 H  HB1  A ALA   A 1 134 ? 16.583 -6.580  -7.859  0.62 18.02 ?  134  ALA   A HB1  1 
ATOM   3013 H  HB1  B ALA   A 1 134 ? 16.438 -6.557  -8.202  0.38 17.33 ?  134  ALA   A HB1  1 
ATOM   3014 H  HB2  A ALA   A 1 134 ? 17.662 -5.445  -8.124  0.62 18.02 ?  134  ALA   A HB2  1 
ATOM   3015 H  HB2  B ALA   A 1 134 ? 17.558 -5.526  -8.655  0.38 17.33 ?  134  ALA   A HB2  1 
ATOM   3016 H  HB3  A ALA   A 1 134 ? 16.840 -5.457  -6.765  0.62 18.02 ?  134  ALA   A HB3  1 
ATOM   3017 H  HB3  B ALA   A 1 134 ? 16.983 -5.475  -7.174  0.38 17.33 ?  134  ALA   A HB3  1 
ATOM   3018 N  N    A ASP   A 1 135 ? 13.848 -6.283  -8.139  0.62 15.43 ?  135  ASP   A N    1 
ATOM   3019 N  N    B ASP   A 1 135 ? 13.762 -6.052  -8.075  0.38 14.56 ?  135  ASP   A N    1 
ATOM   3020 C  CA   A ASP   A 1 135 ? 12.591 -6.790  -7.596  0.62 16.42 ?  135  ASP   A CA   1 
ATOM   3021 C  CA   B ASP   A 1 135 ? 12.495 -6.429  -7.460  0.38 15.23 ?  135  ASP   A CA   1 
ATOM   3022 C  C    A ASP   A 1 135 ? 12.809 -7.233  -6.155  0.62 16.04 ?  135  ASP   A C    1 
ATOM   3023 C  C    B ASP   A 1 135 ? 12.744 -6.911  -6.035  0.38 14.62 ?  135  ASP   A C    1 
ATOM   3024 O  O    A ASP   A 1 135 ? 13.594 -8.160  -5.917  0.62 15.67 ?  135  ASP   A O    1 
ATOM   3025 O  O    B ASP   A 1 135 ? 13.457 -7.904  -5.846  0.38 14.44 ?  135  ASP   A O    1 
ATOM   3026 C  CB   A ASP   A 1 135 ? 12.130 -7.975  -8.440  0.62 18.34 ?  135  ASP   A CB   1 
ATOM   3027 C  CB   B ASP   A 1 135 ? 11.859 -7.549  -8.274  0.38 16.82 ?  135  ASP   A CB   1 
ATOM   3028 C  CG   A ASP   A 1 135 ? 10.895 -8.666  -7.882  0.62 20.11 ?  135  ASP   A CG   1 
ATOM   3029 C  CG   B ASP   A 1 135 ? 10.466 -7.925  -7.781  0.38 18.23 ?  135  ASP   A CG   1 
ATOM   3030 O  OD1  A ASP   A 1 135 ? 10.278 -8.156  -6.925  0.62 20.20 ?  135  ASP   A OD1  1 
ATOM   3031 O  OD1  B ASP   A 1 135 ? 10.066 -7.466  -6.688  0.38 18.57 ?  135  ASP   A OD1  1 
ATOM   3032 O  OD2  A ASP   A 1 135 ? 10.544 -9.738  -8.413  0.62 22.67 -1 135  ASP   A OD2  1 
ATOM   3033 O  OD2  B ASP   A 1 135 ? 9.770  -8.684  -8.489  0.38 19.45 -1 135  ASP   A OD2  1 
ATOM   3034 H  H    A ASP   A 1 135 ? 14.216 -6.800  -8.718  0.62 18.53 ?  135  ASP   A H    1 
ATOM   3035 H  H    B ASP   A 1 135 ? 14.057 -6.631  -8.630  0.38 17.49 ?  135  ASP   A H    1 
ATOM   3036 H  HA   A ASP   A 1 135 ? 11.919 -6.092  -7.633  0.62 19.72 ?  135  ASP   A HA   1 
ATOM   3037 H  HA   B ASP   A 1 135 ? 11.891 -5.669  -7.458  0.38 18.30 ?  135  ASP   A HA   1 
ATOM   3038 H  HB2  A ASP   A 1 135 ? 11.923 -7.661  -9.333  0.62 22.02 ?  135  ASP   A HB2  1 
ATOM   3039 H  HB2  B ASP   A 1 135 ? 11.807 -7.265  -9.203  0.38 20.20 ?  135  ASP   A HB2  1 
ATOM   3040 H  HB3  A ASP   A 1 135 ? 12.838 -8.632  -8.472  0.62 22.02 ?  135  ASP   A HB3  1 
ATOM   3041 H  HB3  B ASP   A 1 135 ? 12.415 -8.341  -8.205  0.38 20.20 ?  135  ASP   A HB3  1 
ATOM   3042 N  N    A PRO   A 1 136 ? 12.147 -6.618  -5.171  0.62 15.85 ?  136  PRO   A N    1 
ATOM   3043 N  N    B PRO   A 1 136 ? 12.184 -6.254  -5.016  0.38 14.21 ?  136  PRO   A N    1 
ATOM   3044 C  CA   A PRO   A 1 136 ? 12.391 -7.019  -3.776  0.62 15.72 ?  136  PRO   A CA   1 
ATOM   3045 C  CA   B PRO   A 1 136 ? 12.428 -6.700  -3.633  0.38 14.47 ?  136  PRO   A CA   1 
ATOM   3046 C  C    A PRO   A 1 136 ? 11.955 -8.436  -3.459  0.62 14.63 ?  136  PRO   A C    1 
ATOM   3047 C  C    B PRO   A 1 136 ? 11.958 -8.119  -3.344  0.38 14.10 ?  136  PRO   A C    1 
ATOM   3048 O  O    A PRO   A 1 136 ? 12.554 -9.065  -2.579  0.62 14.30 ?  136  PRO   A O    1 
ATOM   3049 O  O    B PRO   A 1 136 ? 12.500 -8.768  -2.439  0.38 13.63 ?  136  PRO   A O    1 
ATOM   3050 C  CB   A PRO   A 1 136 ? 11.598 -5.987  -2.965  0.62 16.66 ?  136  PRO   A CB   1 
ATOM   3051 C  CB   B PRO   A 1 136 ? 11.685 -5.651  -2.790  0.38 14.99 ?  136  PRO   A CB   1 
ATOM   3052 C  CG   A PRO   A 1 136 ? 10.561 -5.476  -3.905  0.62 17.50 ?  136  PRO   A CG   1 
ATOM   3053 C  CG   B PRO   A 1 136 ? 10.709 -5.017  -3.733  0.38 15.43 ?  136  PRO   A CG   1 
ATOM   3054 C  CD   A PRO   A 1 136 ? 11.166 -5.523  -5.274  0.62 16.51 ?  136  PRO   A CD   1 
ATOM   3055 C  CD   B PRO   A 1 136 ? 11.358 -5.038  -5.067  0.38 14.39 ?  136  PRO   A CD   1 
ATOM   3056 H  HA   A PRO   A 1 136 ? 13.337 -6.932  -3.563  0.62 18.88 ?  136  PRO   A HA   1 
ATOM   3057 H  HA   B PRO   A 1 136 ? 13.375 -6.640  -3.427  0.38 17.38 ?  136  PRO   A HA   1 
ATOM   3058 H  HB2  A PRO   A 1 136 ? 11.189 -6.425  -2.201  0.62 20.00 ?  136  PRO   A HB2  1 
ATOM   3059 H  HB2  B PRO   A 1 136 ? 11.224 -6.078  -2.054  0.38 18.00 ?  136  PRO   A HB2  1 
ATOM   3060 H  HB3  A PRO   A 1 136 ? 12.192 -5.278  -2.679  0.62 20.00 ?  136  PRO   A HB3  1 
ATOM   3061 H  HB3  B PRO   A 1 136 ? 12.317 -4.989  -2.462  0.38 18.00 ?  136  PRO   A HB3  1 
ATOM   3062 H  HG2  A PRO   A 1 136 ? 9.779  -6.044  -3.860  0.62 21.01 ?  136  PRO   A HG2  1 
ATOM   3063 H  HG2  B PRO   A 1 136 ? 9.891  -5.536  -3.753  0.38 18.53 ?  136  PRO   A HG2  1 
ATOM   3064 H  HG3  A PRO   A 1 136 ? 10.339 -4.565  -3.668  0.62 21.01 ?  136  PRO   A HG3  1 
ATOM   3065 H  HG3  B PRO   A 1 136 ? 10.530 -4.105  -3.461  0.38 18.53 ?  136  PRO   A HG3  1 
ATOM   3066 H  HD2  A PRO   A 1 136 ? 10.493 -5.751  -5.936  0.62 19.83 ?  136  PRO   A HD2  1 
ATOM   3067 H  HD2  B PRO   A 1 136 ? 10.686 -5.109  -5.765  0.38 17.28 ?  136  PRO   A HD2  1 
ATOM   3068 H  HD3  A PRO   A 1 136 ? 11.609 -4.689  -5.488  0.62 19.83 ?  136  PRO   A HD3  1 
ATOM   3069 H  HD3  B PRO   A 1 136 ? 11.917 -4.252  -5.190  0.38 17.28 ?  136  PRO   A HD3  1 
ATOM   3070 N  N    A ILE   A 1 137 ? 10.915 -8.951  -4.118  0.62 15.05 ?  137  ILE   A N    1 
ATOM   3071 N  N    B ILE   A 1 137 ? 10.963 -8.620  -4.078  0.38 14.61 ?  137  ILE   A N    1 
ATOM   3072 C  CA   A ILE   A 1 137 ? 10.546 -10.351 -3.923  0.62 15.17 ?  137  ILE   A CA   1 
ATOM   3073 C  CA   B ILE   A 1 137 ? 10.520 -10.002 -3.895  0.38 15.31 ?  137  ILE   A CA   1 
ATOM   3074 C  C    A ILE   A 1 137 ? 11.707 -11.254 -4.318  0.62 14.50 ?  137  ILE   A C    1 
ATOM   3075 C  C    B ILE   A 1 137 ? 11.652 -10.966 -4.239  0.38 15.40 ?  137  ILE   A C    1 
ATOM   3076 O  O    A ILE   A 1 137 ? 12.041 -12.212 -3.609  0.62 14.30 ?  137  ILE   A O    1 
ATOM   3077 O  O    B ILE   A 1 137 ? 11.926 -11.925 -3.508  0.38 15.47 ?  137  ILE   A O    1 
ATOM   3078 C  CB   A ILE   A 1 137 ? 9.252  -10.684 -4.690  0.62 16.72 ?  137  ILE   A CB   1 
ATOM   3079 C  CB   B ILE   A 1 137 ? 9.264  -10.281 -4.741  0.38 16.40 ?  137  ILE   A CB   1 
ATOM   3080 C  CG1  A ILE   A 1 137 ? 8.085  -9.839  -4.163  0.62 18.51 ?  137  ILE   A CG1  1 
ATOM   3081 C  CG1  B ILE   A 1 137 ? 8.149  -9.275  -4.422  0.38 17.37 ?  137  ILE   A CG1  1 
ATOM   3082 C  CG2  A ILE   A 1 137 ? 8.937  -12.173 -4.579  0.62 17.07 ?  137  ILE   A CG2  1 
ATOM   3083 C  CG2  B ILE   A 1 137 ? 8.790  -11.715 -4.524  0.38 16.66 ?  137  ILE   A CG2  1 
ATOM   3084 C  CD1  A ILE   A 1 137 ? 6.794  -10.022 -4.924  0.62 19.88 ?  137  ILE   A CD1  1 
ATOM   3085 C  CD1  B ILE   A 1 137 ? 6.919  -9.428  -5.295  0.38 18.16 ?  137  ILE   A CD1  1 
ATOM   3086 H  H    A ILE   A 1 137 ? 10.415 -8.522  -4.667  0.62 18.08 ?  137  ILE   A H    1 
ATOM   3087 H  H    B ILE   A 1 137 ? 10.535 -8.179  -4.677  0.38 17.55 ?  137  ILE   A H    1 
ATOM   3088 H  HA   A ILE   A 1 137 ? 10.378 -10.507 -2.986  0.62 18.22 ?  137  ILE   A HA   1 
ATOM   3089 H  HA   B ILE   A 1 137 ? 10.287 -10.137 -2.963  0.38 18.38 ?  137  ILE   A HA   1 
ATOM   3090 H  HB   A ILE   A 1 137 ? 9.382  -10.471 -5.626  0.62 20.08 ?  137  ILE   A HB   1 
ATOM   3091 H  HB   B ILE   A 1 137 ? 9.502  -10.178 -5.674  0.38 19.69 ?  137  ILE   A HB   1 
ATOM   3092 H  HG12 A ILE   A 1 137 ? 7.927  -10.075 -3.236  0.62 22.23 ?  137  ILE   A HG12 1 
ATOM   3093 H  HG12 B ILE   A 1 137 ? 7.875  -9.392  -3.500  0.38 20.86 ?  137  ILE   A HG12 1 
ATOM   3094 H  HG13 A ILE   A 1 137 ? 8.335  -8.900  -4.222  0.62 22.23 ?  137  ILE   A HG13 1 
ATOM   3095 H  HG13 B ILE   A 1 137 ? 8.487  -8.374  -4.552  0.38 20.86 ?  137  ILE   A HG13 1 
ATOM   3096 H  HG21 A ILE   A 1 137 ? 8.042  -12.346 -4.912  0.62 20.50 ?  137  ILE   A HG21 1 
ATOM   3097 H  HG21 B ILE   A 1 137 ? 7.980  -11.863 -5.033  0.38 20.01 ?  137  ILE   A HG21 1 
ATOM   3098 H  HG22 A ILE   A 1 137 ? 9.579  -12.669 -5.107  0.62 20.50 ?  137  ILE   A HG22 1 
ATOM   3099 H  HG22 B ILE   A 1 137 ? 9.480  -12.325 -4.825  0.38 20.01 ?  137  ILE   A HG22 1 
ATOM   3100 H  HG23 A ILE   A 1 137 ? 8.996  -12.434 -3.650  0.62 20.50 ?  137  ILE   A HG23 1 
ATOM   3101 H  HG23 B ILE   A 1 137 ? 8.618  -11.849 -3.579  0.38 20.01 ?  137  ILE   A HG23 1 
ATOM   3102 H  HD11 A ILE   A 1 137 ? 6.101  -10.297 -4.305  0.62 23.88 ?  137  ILE   A HD11 1 
ATOM   3103 H  HD11 B ILE   A 1 137 ? 6.353  -8.650  -5.183  0.38 21.80 ?  137  ILE   A HD11 1 
ATOM   3104 H  HD12 A ILE   A 1 137 ? 6.564  -9.179  -5.336  0.62 23.88 ?  137  ILE   A HD12 1 
ATOM   3105 H  HD12 B ILE   A 1 137 ? 7.197  -9.504  -6.222  0.38 21.80 ?  137  ILE   A HD12 1 
ATOM   3106 H  HD13 A ILE   A 1 137 ? 6.916  -10.696 -5.611  0.62 23.88 ?  137  ILE   A HD13 1 
ATOM   3107 H  HD13 B ILE   A 1 137 ? 6.439  -10.228 -5.029  0.38 21.80 ?  137  ILE   A HD13 1 
ATOM   3108 N  N    A HIS   A 1 138 ? 12.348 -10.951 -5.448  0.62 14.85 ?  138  HIS   A N    1 
ATOM   3109 N  N    B HIS   A 1 138 ? 12.316 -10.725 -5.372  0.38 15.75 ?  138  HIS   A N    1 
ATOM   3110 C  CA   A HIS   A 1 138 ? 13.548 -11.680 -5.841  0.62 14.91 ?  138  HIS   A CA   1 
ATOM   3111 C  CA   B HIS   A 1 138 ? 13.427 -11.575 -5.791  0.38 15.31 ?  138  HIS   A CA   1 
ATOM   3112 C  C    A HIS   A 1 138 ? 14.669 -11.504 -4.821  0.62 14.06 ?  138  HIS   A C    1 
ATOM   3113 C  C    B HIS   A 1 138 ? 14.590 -11.485 -4.811  0.38 14.33 ?  138  HIS   A C    1 
ATOM   3114 O  O    A HIS   A 1 138 ? 15.356 -12.473 -4.471  0.62 14.30 ?  138  HIS   A O    1 
ATOM   3115 O  O    B HIS   A 1 138 ? 15.223 -12.496 -4.483  0.38 14.62 ?  138  HIS   A O    1 
ATOM   3116 C  CB   A HIS   A 1 138 ? 13.995 -11.237 -7.233  0.62 15.96 ?  138  HIS   A CB   1 
ATOM   3117 C  CB   B HIS   A 1 138 ? 13.864 -11.164 -7.198  0.38 15.87 ?  138  HIS   A CB   1 
ATOM   3118 C  CG   A HIS   A 1 138 ? 15.265 -11.888 -7.687  0.62 16.84 ?  138  HIS   A CG   1 
ATOM   3119 C  CG   B HIS   A 1 138 ? 15.139 -11.805 -7.650  0.38 16.62 ?  138  HIS   A CG   1 
ATOM   3120 N  ND1  A HIS   A 1 138 ? 15.370 -13.246 -7.904  0.62 17.66 ?  138  HIS   A ND1  1 
ATOM   3121 N  ND1  B HIS   A 1 138 ? 15.233 -13.148 -7.950  0.38 17.33 ?  138  HIS   A ND1  1 
ATOM   3122 C  CD2  A HIS   A 1 138 ? 16.486 -11.368 -7.951  0.62 17.06 ?  138  HIS   A CD2  1 
ATOM   3123 C  CD2  B HIS   A 1 138 ? 16.372 -11.286 -7.857  0.38 16.78 ?  138  HIS   A CD2  1 
ATOM   3124 C  CE1  A HIS   A 1 138 ? 16.600 -13.532 -8.291  0.62 17.83 ?  138  HIS   A CE1  1 
ATOM   3125 C  CE1  B HIS   A 1 138 ? 16.470 -13.427 -8.321  0.38 17.41 ?  138  HIS   A CE1  1 
ATOM   3126 N  NE2  A HIS   A 1 138 ? 17.298 -12.412 -8.325  0.62 17.36 ?  138  HIS   A NE2  1 
ATOM   3127 N  NE2  B HIS   A 1 138 ? 17.182 -12.315 -8.272  0.38 17.08 ?  138  HIS   A NE2  1 
ATOM   3128 H  H    A HIS   A 1 138 ? 12.109 -10.329 -6.004  0.62 17.84 ?  138  HIS   A H    1 
ATOM   3129 H  H    B HIS   A 1 138 ? 12.143 -10.077 -5.910  0.38 18.91 ?  138  HIS   A H    1 
ATOM   3130 H  HA   A HIS   A 1 138 ? 13.336 -12.622 -5.894  0.62 17.91 ?  138  HIS   A HA   1 
ATOM   3131 H  HA   B HIS   A 1 138 ? 13.129 -12.494 -5.824  0.38 18.38 ?  138  HIS   A HA   1 
ATOM   3132 H  HB2  A HIS   A 1 138 ? 13.298 -11.460 -7.876  0.62 19.16 ?  138  HIS   A HB2  1 
ATOM   3133 H  HB2  B HIS   A 1 138 ? 13.166 -11.413 -7.827  0.38 19.06 ?  138  HIS   A HB2  1 
ATOM   3134 H  HB3  A HIS   A 1 138 ? 14.138 -10.277 -7.232  0.62 19.16 ?  138  HIS   A HB3  1 
ATOM   3135 H  HB3  B HIS   A 1 138 ? 13.992 -10.202 -7.220  0.38 19.06 ?  138  HIS   A HB3  1 
ATOM   3136 H  HD1  B HIS   A 1 138 ? 14.586 -13.714 -7.904  0.38 20.81 ?  138  HIS   A HD1  1 
ATOM   3137 H  HD2  A HIS   A 1 138 ? 16.726 -10.473 -7.891  0.62 20.49 ?  138  HIS   A HD2  1 
ATOM   3138 H  HD2  B HIS   A 1 138 ? 16.622 -10.398 -7.740  0.38 20.15 ?  138  HIS   A HD2  1 
ATOM   3139 H  HE1  A HIS   A 1 138 ? 16.917 -14.380 -8.503  0.62 21.41 ?  138  HIS   A HE1  1 
ATOM   3140 H  HE1  B HIS   A 1 138 ? 16.785 -14.265 -8.573  0.38 20.90 ?  138  HIS   A HE1  1 
ATOM   3141 H  HE2  A HIS   A 1 138 ? 18.122 -12.346 -8.546  0.62 20.84 ?  138  HIS   A HE2  1 
ATOM   3142 N  N    . SER   A 1 139 ? 14.883 -10.275 -4.337  1.00 13.54 ?  139  SER   A N    1 
ATOM   3143 C  CA   . SER   A 1 139 ? 15.959 -10.071 -3.374  1.00 13.26 ?  139  SER   A CA   1 
ATOM   3144 C  C    . SER   A 1 139 ? 15.743 -10.900 -2.114  1.00 12.73 ?  139  SER   A C    1 
ATOM   3145 O  O    . SER   A 1 139 ? 16.691 -11.493 -1.584  1.00 12.81 ?  139  SER   A O    1 
ATOM   3146 C  CB   . SER   A 1 139 ? 16.085 -8.584  -3.039  1.00 13.51 ?  139  SER   A CB   1 
ATOM   3147 O  OG   . SER   A 1 139 ? 17.161 -8.394  -2.140  1.00 13.57 ?  139  SER   A OG   1 
ATOM   3148 H  H    A SER   A 1 139 ? 14.438 -9.571  -4.544  0.62 16.27 ?  139  SER   A H    1 
ATOM   3149 H  H    B SER   A 1 139 ? 14.466 -9.556  -4.554  0.38 16.27 ?  139  SER   A H    1 
ATOM   3150 H  HA   . SER   A 1 139 ? 16.798 -10.354 -3.774  1.00 15.92 ?  139  SER   A HA   1 
ATOM   3151 H  HB2  . SER   A 1 139 ? 16.252 -8.083  -3.854  1.00 16.23 ?  139  SER   A HB2  1 
ATOM   3152 H  HB3  . SER   A 1 139 ? 15.267 -8.278  -2.619  1.00 16.23 ?  139  SER   A HB3  1 
ATOM   3153 H  HG   . SER   A 1 139 ? 17.244 -7.574  -1.956  1.00 16.29 ?  139  SER   A HG   1 
ATOM   3154 N  N    A LEU   A 1 140 ? 14.495 -11.014 -1.657  0.62 13.00 ?  140  LEU   A N    1 
ATOM   3155 N  N    B LEU   A 1 140 ? 14.518 -10.893 -1.576  0.38 11.97 ?  140  LEU   A N    1 
ATOM   3156 C  CA   A LEU   A 1 140 ? 14.229 -11.867 -0.504  0.62 12.66 ?  140  LEU   A CA   1 
ATOM   3157 C  CA   B LEU   A 1 140 ? 14.244 -11.661 -0.362  0.38 11.16 ?  140  LEU   A CA   1 
ATOM   3158 C  C    A LEU   A 1 140 ? 14.517 -13.332 -0.820  0.62 12.69 ?  140  LEU   A C    1 
ATOM   3159 C  C    B LEU   A 1 140 ? 14.497 -13.149 -0.585  0.38 10.75 ?  140  LEU   A C    1 
ATOM   3160 O  O    A LEU   A 1 140 ? 15.101 -14.047 0.001   0.62 12.80 ?  140  LEU   A O    1 
ATOM   3161 O  O    B LEU   A 1 140 ? 15.001 -13.843 0.307   0.38 11.27 ?  140  LEU   A O    1 
ATOM   3162 C  CB   A LEU   A 1 140 ? 12.790 -11.679 -0.029  0.62 12.81 ?  140  LEU   A CB   1 
ATOM   3163 C  CB   B LEU   A 1 140 ? 12.805 -11.415 0.105   0.38 11.05 ?  140  LEU   A CB   1 
ATOM   3164 C  CG   A LEU   A 1 140 ? 12.364 -12.585 1.129   0.62 13.27 ?  140  LEU   A CG   1 
ATOM   3165 C  CG   B LEU   A 1 140 ? 12.304 -12.221 1.311   0.38 11.19 ?  140  LEU   A CG   1 
ATOM   3166 C  CD1  A LEU   A 1 140 ? 13.249 -12.368 2.345   0.62 13.69 ?  140  LEU   A CD1  1 
ATOM   3167 C  CD1  B LEU   A 1 140 ? 13.187 -11.989 2.527   0.38 11.51 ?  140  LEU   A CD1  1 
ATOM   3168 C  CD2  A LEU   A 1 140 ? 10.891 -12.362 1.479   0.62 14.03 ?  140  LEU   A CD2  1 
ATOM   3169 C  CD2  B LEU   A 1 140 ? 10.850 -11.879 1.633   0.38 11.49 ?  140  LEU   A CD2  1 
ATOM   3170 H  H    A LEU   A 1 140 ? 13.808 -10.616 -1.989  0.62 15.61 ?  140  LEU   A H    1 
ATOM   3171 H  H    B LEU   A 1 140 ? 13.847 -10.448 -1.882  0.38 14.38 ?  140  LEU   A H    1 
ATOM   3172 H  HA   A LEU   A 1 140 ? 14.817 -11.604 0.216   0.62 15.21 ?  140  LEU   A HA   1 
ATOM   3173 H  HA   B LEU   A 1 140 ? 14.836 -11.354 0.343   0.38 13.41 ?  140  LEU   A HA   1 
ATOM   3174 H  HB2  A LEU   A 1 140 ? 12.684 -10.761 0.264   0.62 15.38 ?  140  LEU   A HB2  1 
ATOM   3175 H  HB2  B LEU   A 1 140 ? 12.718 -10.477 0.339   0.38 13.27 ?  140  LEU   A HB2  1 
ATOM   3176 H  HB3  A LEU   A 1 140 ? 12.195 -11.855 -0.774  0.62 15.38 ?  140  LEU   A HB3  1 
ATOM   3177 H  HB3  B LEU   A 1 140 ? 12.211 -11.614 -0.633  0.38 13.27 ?  140  LEU   A HB3  1 
ATOM   3178 H  HG   A LEU   A 1 140 ? 12.464 -13.511 0.854   0.62 15.94 ?  140  LEU   A HG   1 
ATOM   3179 H  HG   B LEU   A 1 140 ? 12.338 -13.163 1.095   0.38 13.45 ?  140  LEU   A HG   1 
ATOM   3180 H  HD11 A LEU   A 1 140 ? 12.884 -12.870 3.089   0.62 16.45 ?  140  LEU   A HD11 1 
ATOM   3181 H  HD11 B LEU   A 1 140 ? 12.806 -12.458 3.285   0.38 13.83 ?  140  LEU   A HD11 1 
ATOM   3182 H  HD12 A LEU   A 1 140 ? 14.147 -12.677 2.145   0.62 16.45 ?  140  LEU   A HD12 1 
ATOM   3183 H  HD12 B LEU   A 1 140 ? 14.074 -12.329 2.337   0.38 13.83 ?  140  LEU   A HD12 1 
ATOM   3184 H  HD13 A LEU   A 1 140 ? 13.263 -11.422 2.559   0.62 16.45 ?  140  LEU   A HD13 1 
ATOM   3185 H  HD13 B LEU   A 1 140 ? 13.226 -11.038 2.710   0.38 13.83 ?  140  LEU   A HD13 1 
ATOM   3186 H  HD21 A LEU   A 1 140 ? 10.651 -12.950 2.212   0.62 16.85 ?  140  LEU   A HD21 1 
ATOM   3187 H  HD21 B LEU   A 1 140 ? 10.533 -12.473 2.333   0.38 13.80 ?  140  LEU   A HD21 1 
ATOM   3188 H  HD22 A LEU   A 1 140 ? 10.766 -11.437 1.739   0.62 16.85 ?  140  LEU   A HD22 1 
ATOM   3189 H  HD22 B LEU   A 1 140 ? 10.802 -10.959 1.936   0.38 13.80 ?  140  LEU   A HD22 1 
ATOM   3190 H  HD23 A LEU   A 1 140 ? 10.349 -12.565 0.700   0.62 16.85 ?  140  LEU   A HD23 1 
ATOM   3191 H  HD23 B LEU   A 1 140 ? 10.311 -11.994 0.834   0.38 13.80 ?  140  LEU   A HD23 1 
ATOM   3192 N  N    A ARG   A 1 141 ? 14.102 -13.800 -2.002  0.62 13.08 ?  141  ARG   A N    1 
ATOM   3193 N  N    B ARG   A 1 141 ? 14.145 -13.660 -1.770  0.38 11.35 ?  141  ARG   A N    1 
ATOM   3194 C  CA   A ARG   A 1 141 ? 14.371 -15.181 -2.392  0.62 14.25 ?  141  ARG   A CA   1 
ATOM   3195 C  CA   B ARG   A 1 141 ? 14.374 -15.073 -2.059  0.38 12.29 ?  141  ARG   A CA   1 
ATOM   3196 C  C    A ARG   A 1 141 ? 15.865 -15.478 -2.331  0.62 13.67 ?  141  ARG   A C    1 
ATOM   3197 C  C    B ARG   A 1 141 ? 15.861 -15.370 -2.204  0.38 12.33 ?  141  ARG   A C    1 
ATOM   3198 O  O    A ARG   A 1 141 ? 16.290 -16.475 -1.735  0.62 13.60 ?  141  ARG   A O    1 
ATOM   3199 O  O    B ARG   A 1 141 ? 16.340 -16.404 -1.723  0.38 12.58 ?  141  ARG   A O    1 
ATOM   3200 C  CB   A ARG   A 1 141 ? 13.827 -15.421 -3.802  0.62 16.07 ?  141  ARG   A CB   1 
ATOM   3201 C  CB   B ARG   A 1 141 ? 13.607 -15.494 -3.315  0.38 12.59 ?  141  ARG   A CB   1 
ATOM   3202 C  CG   A ARG   A 1 141 ? 13.782 -16.875 -4.229  0.62 19.02 ?  141  ARG   A CG   1 
ATOM   3203 C  CG   B ARG   A 1 141 ? 13.804 -16.969 -3.700  0.38 13.23 ?  141  ARG   A CG   1 
ATOM   3204 C  CD   A ARG   A 1 141 ? 12.747 -17.631 -3.434  0.62 20.74 ?  141  ARG   A CD   1 
ATOM   3205 C  CD   B ARG   A 1 141 ? 13.209 -17.907 -2.663  0.38 13.73 ?  141  ARG   A CD   1 
ATOM   3206 N  NE   A ARG   A 1 141 ? 13.348 -18.436 -2.381  0.62 21.74 ?  141  ARG   A NE   1 
ATOM   3207 N  NE   B ARG   A 1 141 ? 11.778 -17.672 -2.512  0.38 14.28 ?  141  ARG   A NE   1 
ATOM   3208 C  CZ   A ARG   A 1 141 ? 12.662 -18.996 -1.394  0.62 22.24 ?  141  ARG   A CZ   1 
ATOM   3209 C  CZ   B ARG   A 1 141 ? 11.020 -18.210 -1.568  0.38 14.40 ?  141  ARG   A CZ   1 
ATOM   3210 N  NH1  A ARG   A 1 141 ? 11.362 -18.798 -1.258  0.62 22.65 ?  141  ARG   A NH1  1 
ATOM   3211 N  NH1  B ARG   A 1 141 ? 11.520 -19.039 -0.665  0.38 14.41 ?  141  ARG   A NH1  1 
ATOM   3212 N  NH2  A ARG   A 1 141 ? 13.297 -19.770 -0.520  0.62 22.38 ?  141  ARG   A NH2  1 
ATOM   3213 N  NH2  B ARG   A 1 141 ? 9.724  -17.910 -1.529  0.38 14.68 ?  141  ARG   A NH2  1 
ATOM   3214 H  H    A ARG   A 1 141 ? 13.670 -13.346 -2.591  0.62 15.71 ?  141  ARG   A H    1 
ATOM   3215 H  H    B ARG   A 1 141 ? 13.784 -13.213 -2.408  0.38 13.64 ?  141  ARG   A H    1 
ATOM   3216 H  HA   A ARG   A 1 141 ? 13.920 -15.782 -1.781  0.62 17.12 ?  141  ARG   A HA   1 
ATOM   3217 H  HA   B ARG   A 1 141 ? 14.045 -15.598 -1.320  0.38 14.77 ?  141  ARG   A HA   1 
ATOM   3218 H  HB2  A ARG   A 1 141 ? 12.923 -15.076 -3.848  0.62 19.30 ?  141  ARG   A HB2  1 
ATOM   3219 H  HB2  B ARG   A 1 141 ? 12.653 -15.354 -3.160  0.38 15.12 ?  141  ARG   A HB2  1 
ATOM   3220 H  HB3  A ARG   A 1 141 ? 14.389 -14.954 -4.436  0.62 19.30 ?  141  ARG   A HB3  1 
ATOM   3221 H  HB3  B ARG   A 1 141 ? 13.894 -14.949 -4.062  0.38 15.12 ?  141  ARG   A HB3  1 
ATOM   3222 H  HG2  A ARG   A 1 141 ? 13.545 -16.933 -5.169  0.62 22.84 ?  141  ARG   A HG2  1 
ATOM   3223 H  HG2  B ARG   A 1 141 ? 13.362 -17.136 -4.548  0.38 15.89 ?  141  ARG   A HG2  1 
ATOM   3224 H  HG3  A ARG   A 1 141 ? 14.647 -17.290 -4.075  0.62 22.84 ?  141  ARG   A HG3  1 
ATOM   3225 H  HG3  B ARG   A 1 141 ? 14.753 -17.161 -3.781  0.38 15.89 ?  141  ARG   A HG3  1 
ATOM   3226 H  HD2  A ARG   A 1 141 ? 12.141 -16.999 -3.017  0.62 24.90 ?  141  ARG   A HD2  1 
ATOM   3227 H  HD2  B ARG   A 1 141 ? 13.338 -18.823 -2.947  0.38 16.50 ?  141  ARG   A HD2  1 
ATOM   3228 H  HD3  A ARG   A 1 141 ? 12.255 -18.221 -4.028  0.62 24.90 ?  141  ARG   A HD3  1 
ATOM   3229 H  HD3  B ARG   A 1 141 ? 13.635 -17.755 -1.805  0.38 16.50 ?  141  ARG   A HD3  1 
ATOM   3230 H  HE   A ARG   A 1 141 ? 14.180 -18.640 -2.458  0.62 26.10 ?  141  ARG   A HE   1 
ATOM   3231 H  HE   B ARG   A 1 141 ? 11.393 -17.160 -3.089  0.38 17.15 ?  141  ARG   A HE   1 
ATOM   3232 H  HH11 A ARG   A 1 141 ? 10.937 -18.307 -1.820  0.62 27.20 ?  141  ARG   A HH11 1 
ATOM   3233 H  HH11 B ARG   A 1 141 ? 12.354 -19.241 -0.681  0.38 17.31 ?  141  ARG   A HH11 1 
ATOM   3234 H  HH12 A ARG   A 1 141 ? 10.938 -19.170 -0.608  0.62 27.20 ?  141  ARG   A HH12 1 
ATOM   3235 H  HH12 B ARG   A 1 141 ? 11.006 -19.378 -0.065  0.38 17.31 ?  141  ARG   A HH12 1 
ATOM   3236 H  HH21 A ARG   A 1 141 ? 14.145 -19.899 -0.598  0.62 26.87 ?  141  ARG   A HH21 1 
ATOM   3237 H  HH21 B ARG   A 1 141 ? 9.387  -17.374 -2.112  0.38 17.63 ?  141  ARG   A HH21 1 
ATOM   3238 H  HH22 A ARG   A 1 141 ? 12.866 -20.129 0.130   0.62 26.87 ?  141  ARG   A HH22 1 
ATOM   3239 H  HH22 B ARG   A 1 141 ? 9.220  -18.256 -0.924  0.38 17.63 ?  141  ARG   A HH22 1 
ATOM   3240 N  N    A VAL   A 1 142 ? 16.678 -14.619 -2.947  0.62 12.90 ?  142  VAL   A N    1 
ATOM   3241 N  N    B VAL   A 1 142 ? 16.610 -14.482 -2.865  0.38 12.32 ?  142  VAL   A N    1 
ATOM   3242 C  CA   A VAL   A 1 142 ? 18.124 -14.821 -2.931  0.62 12.60 ?  142  VAL   A CA   1 
ATOM   3243 C  CA   B VAL   A 1 142 ? 18.055 -14.677 -2.956  0.38 12.46 ?  142  VAL   A CA   1 
ATOM   3244 C  C    A VAL   A 1 142 ? 18.665 -14.766 -1.506  0.62 12.08 ?  142  VAL   A C    1 
ATOM   3245 C  C    B VAL   A 1 142 ? 18.662 -14.707 -1.562  0.38 12.04 ?  142  VAL   A C    1 
ATOM   3246 O  O    A VAL   A 1 142 ? 19.512 -15.582 -1.124  0.62 12.40 ?  142  VAL   A O    1 
ATOM   3247 O  O    B VAL   A 1 142 ? 19.547 -15.518 -1.263  0.38 12.24 ?  142  VAL   A O    1 
ATOM   3248 C  CB   A VAL   A 1 142 ? 18.830 -13.823 -3.868  0.62 12.42 ?  142  VAL   A CB   1 
ATOM   3249 C  CB   B VAL   A 1 142 ? 18.698 -13.583 -3.829  0.38 12.90 ?  142  VAL   A CB   1 
ATOM   3250 C  CG1  A VAL   A 1 142 ? 20.334 -14.053 -3.850  0.62 12.01 ?  142  VAL   A CG1  1 
ATOM   3251 C  CG1  B VAL   A 1 142 ? 20.210 -13.725 -3.811  0.38 12.85 ?  142  VAL   A CG1  1 
ATOM   3252 C  CG2  A VAL   A 1 142 ? 18.305 -13.958 -5.290  0.62 13.76 ?  142  VAL   A CG2  1 
ATOM   3253 C  CG2  B VAL   A 1 142 ? 18.189 -13.660 -5.254  0.38 13.80 ?  142  VAL   A CG2  1 
ATOM   3254 H  H    A VAL   A 1 142 ? 16.423 -13.929 -3.390  0.62 15.49 ?  142  VAL   A H    1 
ATOM   3255 H  H    B VAL   A 1 142 ? 16.315 -13.765 -3.251  0.38 14.80 ?  142  VAL   A H    1 
ATOM   3256 H  HA   A VAL   A 1 142 ? 18.318 -15.705 -3.275  0.62 15.13 ?  142  VAL   A HA   1 
ATOM   3257 H  HA   B VAL   A 1 142 ? 18.229 -15.527 -3.383  0.38 14.97 ?  142  VAL   A HA   1 
ATOM   3258 H  HB   A VAL   A 1 142 ? 18.665 -12.914 -3.567  0.62 14.92 ?  142  VAL   A HB   1 
ATOM   3259 H  HB   B VAL   A 1 142 ? 18.473 -12.707 -3.471  0.38 15.50 ?  142  VAL   A HB   1 
ATOM   3260 H  HG11 A VAL   A 1 142 ? 20.742 -13.555 -4.577  0.62 14.43 ?  142  VAL   A HG11 1 
ATOM   3261 H  HG11 B VAL   A 1 142 ? 20.587 -13.152 -4.496  0.38 15.44 ?  142  VAL   A HG11 1 
ATOM   3262 H  HG12 A VAL   A 1 142 ? 20.694 -13.748 -3.002  0.62 14.43 ?  142  VAL   A HG12 1 
ATOM   3263 H  HG12 B VAL   A 1 142 ? 20.546 -13.461 -2.940  0.38 15.44 ?  142  VAL   A HG12 1 
ATOM   3264 H  HG13 A VAL   A 1 142 ? 20.509 -15.001 -3.963  0.62 14.43 ?  142  VAL   A HG13 1 
ATOM   3265 H  HG13 B VAL   A 1 142 ? 20.438 -14.649 -3.989  0.38 15.44 ?  142  VAL   A HG13 1 
ATOM   3266 H  HG21 A VAL   A 1 142 ? 18.811 -13.367 -5.873  0.62 16.53 ?  142  VAL   A HG21 1 
ATOM   3267 H  HG21 B VAL   A 1 142 ? 18.549 -12.914 -5.759  0.38 16.58 ?  142  VAL   A HG21 1 
ATOM   3268 H  HG22 A VAL   A 1 142 ? 18.409 -14.875 -5.578  0.62 16.53 ?  142  VAL   A HG22 1 
ATOM   3269 H  HG22 B VAL   A 1 142 ? 18.484 -14.497 -5.645  0.38 16.58 ?  142  VAL   A HG22 1 
ATOM   3270 H  HG23 A VAL   A 1 142 ? 17.368 -13.708 -5.303  0.62 16.53 ?  142  VAL   A HG23 1 
ATOM   3271 H  HG23 B VAL   A 1 142 ? 17.222 -13.620 -5.247  0.38 16.58 ?  142  VAL   A HG23 1 
ATOM   3272 N  N    . CYS   A 1 143 ? 18.194 -13.814 -0.694  1.00 11.94 ?  143  CYS   A N    1 
ATOM   3273 C  CA   . CYS   A 1 143 ? 18.656 -13.762 0.690   1.00 12.16 ?  143  CYS   A CA   1 
ATOM   3274 C  C    . CYS   A 1 143 ? 18.424 -15.096 1.390   1.00 12.02 ?  143  CYS   A C    1 
ATOM   3275 O  O    . CYS   A 1 143 ? 19.341 -15.678 1.980   1.00 11.98 ?  143  CYS   A O    1 
ATOM   3276 C  CB   . CYS   A 1 143 ? 17.920 -12.645 1.428   1.00 12.65 ?  143  CYS   A CB   1 
ATOM   3277 S  SG   . CYS   A 1 143 ? 18.401 -12.450 3.162   1.00 12.88 ?  143  CYS   A SG   1 
ATOM   3278 H  H    A CYS   A 1 143 ? 17.616 -13.218 -0.911  0.62 14.35 ?  143  CYS   A H    1 
ATOM   3279 H  H    B CYS   A 1 143 ? 17.601 -13.224 -0.885  0.38 14.35 ?  143  CYS   A H    1 
ATOM   3280 H  HA   . CYS   A 1 143 ? 19.606 -13.576 0.705   1.00 14.61 ?  143  CYS   A HA   1 
ATOM   3281 H  HB2  . CYS   A 1 143 ? 18.096 -11.809 0.973   1.00 15.19 ?  143  CYS   A HB2  1 
ATOM   3282 H  HB3  . CYS   A 1 143 ? 16.973 -12.836 1.407   1.00 15.19 ?  143  CYS   A HB3  1 
ATOM   3283 H  HG   . CYS   A 1 143 ? 17.830 -11.495 3.609   1.00 15.47 ?  143  CYS   A HG   1 
ATOM   3284 N  N    . VAL   A 1 144 ? 17.193 -15.603 1.324   1.00 12.51 ?  144  VAL   A N    1 
ATOM   3285 C  CA   . VAL   A 1 144 ? 16.849 -16.841 2.013   1.00 13.71 ?  144  VAL   A CA   1 
ATOM   3286 C  C    . VAL   A 1 144 ? 17.675 -18.010 1.495   1.00 13.14 ?  144  VAL   A C    1 
ATOM   3287 O  O    . VAL   A 1 144 ? 18.047 -18.909 2.261   1.00 13.85 ?  144  VAL   A O    1 
ATOM   3288 C  CB   . VAL   A 1 144 ? 15.335 -17.083 1.871   1.00 16.07 ?  144  VAL   A CB   1 
ATOM   3289 C  CG1  . VAL   A 1 144 ? 14.977 -18.518 2.175   1.00 17.74 ?  144  VAL   A CG1  1 
ATOM   3290 C  CG2  . VAL   A 1 144 ? 14.574 -16.107 2.764   1.00 16.50 ?  144  VAL   A CG2  1 
ATOM   3291 H  H    . VAL   A 1 144 ? 16.538 -15.242 0.890   1.00 15.03 ?  144  VAL   A H    1 
ATOM   3292 H  HA   . VAL   A 1 144 ? 17.034 -16.736 2.954   1.00 16.47 ?  144  VAL   A HA   1 
ATOM   3293 H  HB   . VAL   A 1 144 ? 15.067 -16.902 0.952   1.00 19.29 ?  144  VAL   A HB   1 
ATOM   3294 H  HG11 . VAL   A 1 144 ? 14.018 -18.577 2.340   1.00 21.31 ?  144  VAL   A HG11 1 
ATOM   3295 H  HG12 . VAL   A 1 144 ? 15.210 -19.076 1.418   1.00 21.31 ?  144  VAL   A HG12 1 
ATOM   3296 H  HG13 . VAL   A 1 144 ? 15.459 -18.803 2.965   1.00 21.31 ?  144  VAL   A HG13 1 
ATOM   3297 H  HG21 . VAL   A 1 144 ? 13.617 -16.240 2.649   1.00 19.81 ?  144  VAL   A HG21 1 
ATOM   3298 H  HG22 . VAL   A 1 144 ? 14.817 -16.264 3.690   1.00 19.81 ?  144  VAL   A HG22 1 
ATOM   3299 H  HG23 . VAL   A 1 144 ? 14.806 -15.196 2.514   1.00 19.81 ?  144  VAL   A HG23 1 
ATOM   3300 N  N    . ASP   A 1 145 ? 17.955 -18.034 0.194   1.00 13.51 ?  145  ASP   A N    1 
ATOM   3301 C  CA   . ASP   A 1 145 ? 18.676 -19.138 -0.429  1.00 13.81 ?  145  ASP   A CA   1 
ATOM   3302 C  C    . ASP   A 1 145 ? 20.194 -18.981 -0.373  1.00 13.59 ?  145  ASP   A C    1 
ATOM   3303 O  O    . ASP   A 1 145 ? 20.909 -19.874 -0.846  1.00 16.01 ?  145  ASP   A O    1 
ATOM   3304 C  CB   . ASP   A 1 145 ? 18.243 -19.280 -1.889  1.00 15.28 ?  145  ASP   A CB   1 
ATOM   3305 C  CG   . ASP   A 1 145 ? 16.812 -19.766 -2.036  1.00 17.30 ?  145  ASP   A CG   1 
ATOM   3306 O  OD1  . ASP   A 1 145 ? 16.242 -20.312 -1.064  1.00 18.37 ?  145  ASP   A OD1  1 
ATOM   3307 O  OD2  . ASP   A 1 145 ? 16.267 -19.607 -3.145  1.00 18.81 -1 145  ASP   A OD2  1 
ATOM   3308 H  H    . ASP   A 1 145 ? 17.716 -17.417 -0.361  1.00 16.23 ?  145  ASP   A H    1 
ATOM   3309 H  HA   . ASP   A 1 145 ? 18.443 -19.959 0.028   1.00 16.59 ?  145  ASP   A HA   1 
ATOM   3310 H  HB2  . ASP   A 1 145 ? 18.317 -18.418 -2.329  1.00 18.35 ?  145  ASP   A HB2  1 
ATOM   3311 H  HB3  . ASP   A 1 145 ? 18.822 -19.925 -2.327  1.00 18.35 ?  145  ASP   A HB3  1 
ATOM   3312 N  N    . THR   A 1 146 ? 20.703 -17.881 0.182   1.00 12.11 ?  146  THR   A N    1 
ATOM   3313 C  CA   . THR   A 1 146 ? 22.139 -17.610 0.201   1.00 11.92 ?  146  THR   A CA   1 
ATOM   3314 C  C    . THR   A 1 146 ? 22.694 -17.426 1.603   1.00 12.02 ?  146  THR   A C    1 
ATOM   3315 O  O    . THR   A 1 146 ? 23.772 -17.957 1.917   1.00 12.97 ?  146  THR   A O    1 
ATOM   3316 C  CB   . THR   A 1 146 ? 22.456 -16.360 -0.640  1.00 12.04 ?  146  THR   A CB   1 
ATOM   3317 O  OG1  . THR   A 1 146 ? 21.941 -16.531 -1.961  1.00 12.47 ?  146  THR   A OG1  1 
ATOM   3318 C  CG2  . THR   A 1 146 ? 23.953 -16.109 -0.715  1.00 12.88 ?  146  THR   A CG2  1 
ATOM   3319 H  H    . THR   A 1 146 ? 20.230 -17.261 0.553   1.00 14.54 ?  146  THR   A H    1 
ATOM   3320 H  HA   . THR   A 1 146 ? 22.605 -18.353 -0.199  1.00 14.32 ?  146  THR   A HA   1 
ATOM   3321 H  HB   . THR   A 1 146 ? 22.041 -15.581 -0.236  1.00 14.46 ?  146  THR   A HB   1 
ATOM   3322 H  HG1  . THR   A 1 146 ? 21.108 -16.621 -1.935  1.00 14.98 ?  146  THR   A HG1  1 
ATOM   3323 H  HG21 . THR   A 1 146 ? 24.139 -15.443 -1.395  1.00 15.47 ?  146  THR   A HG21 1 
ATOM   3324 H  HG22 . THR   A 1 146 ? 24.276 -15.783 0.140   1.00 15.47 ?  146  THR   A HG22 1 
ATOM   3325 H  HG23 . THR   A 1 146 ? 24.412 -16.929 -0.939  1.00 15.47 ?  146  THR   A HG23 1 
ATOM   3326 N  N    . VAL   A 1 147 ? 22.014 -16.645 2.439   1.00 11.86 ?  147  VAL   A N    1 
ATOM   3327 C  CA   . VAL   A 1 147 ? 22.502 -16.346 3.778   1.00 11.68 ?  147  VAL   A CA   1 
ATOM   3328 C  C    . VAL   A 1 147 ? 22.184 -17.521 4.694   1.00 12.15 ?  147  VAL   A C    1 
ATOM   3329 O  O    . VAL   A 1 147 ? 21.043 -18.000 4.739   1.00 12.71 ?  147  VAL   A O    1 
ATOM   3330 C  CB   . VAL   A 1 147 ? 21.873 -15.044 4.298   1.00 12.16 ?  147  VAL   A CB   1 
ATOM   3331 C  CG1  . VAL   A 1 147 ? 22.399 -14.722 5.670   1.00 13.01 ?  147  VAL   A CG1  1 
ATOM   3332 C  CG2  . VAL   A 1 147 ? 22.120 -13.893 3.322   1.00 12.09 ?  147  VAL   A CG2  1 
ATOM   3333 H  H    . VAL   A 1 147 ? 21.252 -16.281 2.259   1.00 14.25 ?  147  VAL   A H    1 
ATOM   3334 H  HA   . VAL   A 1 147 ? 23.464 -16.230 3.749   1.00 14.03 ?  147  VAL   A HA   1 
ATOM   3335 H  HB   . VAL   A 1 147 ? 20.914 -15.171 4.374   1.00 14.61 ?  147  VAL   A HB   1 
ATOM   3336 H  HG11 . VAL   A 1 147 ? 22.140 -13.819 5.903   1.00 15.63 ?  147  VAL   A HG11 1 
ATOM   3337 H  HG12 . VAL   A 1 147 ? 22.023 -15.349 6.310   1.00 15.63 ?  147  VAL   A HG12 1 
ATOM   3338 H  HG13 . VAL   A 1 147 ? 23.366 -14.798 5.663   1.00 15.63 ?  147  VAL   A HG13 1 
ATOM   3339 H  HG21 . VAL   A 1 147 ? 21.780 -13.073 3.717   1.00 14.52 ?  147  VAL   A HG21 1 
ATOM   3340 H  HG22 . VAL   A 1 147 ? 23.065 -13.819 3.155   1.00 14.52 ?  147  VAL   A HG22 1 
ATOM   3341 H  HG23 . VAL   A 1 147 ? 21.643 -14.079 2.496   1.00 14.52 ?  147  VAL   A HG23 1 
ATOM   3342 N  N    . ARG   A 1 148 ? 23.200 -17.975 5.432   1.00 12.16 ?  148  ARG   A N    1 
ATOM   3343 C  CA   . ARG   A 1 148 ? 23.071 -19.049 6.403   1.00 12.42 ?  148  ARG   A CA   1 
ATOM   3344 C  C    . ARG   A 1 148 ? 23.193 -18.570 7.838   1.00 12.76 ?  148  ARG   A C    1 
ATOM   3345 O  O    . ARG   A 1 148 ? 22.785 -19.295 8.755   1.00 14.36 ?  148  ARG   A O    1 
ATOM   3346 C  CB   . ARG   A 1 148 ? 24.120 -20.138 6.135   1.00 13.31 ?  148  ARG   A CB   1 
ATOM   3347 C  CG   . ARG   A 1 148 ? 23.966 -20.785 4.775   1.00 14.68 ?  148  ARG   A CG   1 
ATOM   3348 C  CD   . ARG   A 1 148 ? 25.062 -21.810 4.487   1.00 15.76 ?  148  ARG   A CD   1 
ATOM   3349 N  NE   . ARG   A 1 148 ? 26.401 -21.230 4.500   1.00 15.47 ?  148  ARG   A NE   1 
ATOM   3350 C  CZ   . ARG   A 1 148 ? 26.910 -20.506 3.512   1.00 14.81 ?  148  ARG   A CZ   1 
ATOM   3351 N  NH1  . ARG   A 1 148 ? 26.226 -20.271 2.403   1.00 15.07 ?  148  ARG   A NH1  1 
ATOM   3352 N  NH2  . ARG   A 1 148 ? 28.129 -19.983 3.648   1.00 15.14 ?  148  ARG   A NH2  1 
ATOM   3353 H  H    . ARG   A 1 148 ? 24.004 -17.658 5.376   1.00 14.61 ?  148  ARG   A H    1 
ATOM   3354 H  HA   . ARG   A 1 148 ? 22.200 -19.447 6.307   1.00 14.92 ?  148  ARG   A HA   1 
ATOM   3355 H  HB2  . ARG   A 1 148 ? 25.005 -19.754 6.185   1.00 15.99 ?  148  ARG   A HB2  1 
ATOM   3356 H  HB3  . ARG   A 1 148 ? 24.023 -20.838 6.806   1.00 15.99 ?  148  ARG   A HB3  1 
ATOM   3357 H  HG2  . ARG   A 1 148 ? 23.105 -21.233 4.738   1.00 17.63 ?  148  ARG   A HG2  1 
ATOM   3358 H  HG3  . ARG   A 1 148 ? 24.007 -20.091 4.097   1.00 17.63 ?  148  ARG   A HG3  1 
ATOM   3359 H  HD2  . ARG   A 1 148 ? 25.029 -22.502 5.165   1.00 18.93 ?  148  ARG   A HD2  1 
ATOM   3360 H  HD3  . ARG   A 1 148 ? 24.905 -22.196 3.611   1.00 18.93 ?  148  ARG   A HD3  1 
ATOM   3361 H  HE   . ARG   A 1 148 ? 26.893 -21.372 5.186   1.00 18.57 ?  148  ARG   A HE   1 
ATOM   3362 H  HH11 . ARG   A 1 148 ? 25.437 -20.592 2.304   1.00 18.10 ?  148  ARG   A HH11 1 
ATOM   3363 H  HH12 . ARG   A 1 148 ? 26.575 -19.791 1.777   1.00 18.10 ?  148  ARG   A HH12 1 
ATOM   3364 H  HH21 . ARG   A 1 148 ? 28.580 -20.126 4.362   1.00 18.18 ?  148  ARG   A HH21 1 
ATOM   3365 H  HH22 . ARG   A 1 148 ? 28.468 -19.508 3.012   1.00 18.18 ?  148  ARG   A HH22 1 
ATOM   3366 N  N    . THR   A 1 149 ? 23.749 -17.381 8.048   1.00 12.72 ?  149  THR   A N    1 
ATOM   3367 C  CA   . THR   A 1 149 ? 23.821 -16.775 9.362   1.00 12.79 ?  149  THR   A CA   1 
ATOM   3368 C  C    . THR   A 1 149 ? 22.489 -16.086 9.660   1.00 12.34 ?  149  THR   A C    1 
ATOM   3369 O  O    . THR   A 1 149 ? 21.555 -16.088 8.844   1.00 13.17 ?  149  THR   A O    1 
ATOM   3370 C  CB   . THR   A 1 149 ? 25.018 -15.832 9.416   1.00 13.25 ?  149  THR   A CB   1 
ATOM   3371 O  OG1  . THR   A 1 149 ? 24.884 -14.905 8.336   1.00 13.45 ?  149  THR   A OG1  1 
ATOM   3372 C  CG2  . THR   A 1 149 ? 26.328 -16.616 9.287   1.00 13.67 ?  149  THR   A CG2  1 
ATOM   3373 H  H    . THR   A 1 149 ? 24.104 -16.894 7.429   1.00 15.28 ?  149  THR   A H    1 
ATOM   3374 H  HA   . THR   A 1 149 ? 23.951 -17.473 10.024  1.00 15.36 ?  149  THR   A HA   1 
ATOM   3375 H  HB   . THR   A 1 149 ? 25.013 -15.358 10.260  1.00 15.92 ?  149  THR   A HB   1 
ATOM   3376 H  HG1  . THR   A 1 149 ? 25.527 -14.370 8.335   1.00 16.16 ?  149  THR   A HG1  1 
ATOM   3377 H  HG21 . THR   A 1 149 ? 27.083 -16.012 9.344   1.00 16.42 ?  149  THR   A HG21 1 
ATOM   3378 H  HG22 . THR   A 1 149 ? 26.397 -17.275 9.998   1.00 16.42 ?  149  THR   A HG22 1 
ATOM   3379 H  HG23 . THR   A 1 149 ? 26.359 -17.079 8.432   1.00 16.42 ?  149  THR   A HG23 1 
ATOM   3380 N  N    . ASN   A 1 150 ? 22.364 -15.542 10.863  1.00 12.65 ?  150  ASN   A N    1 
ATOM   3381 C  CA   . ASN   A 1 150 ? 21.078 -15.036 11.340  1.00 13.22 ?  150  ASN   A CA   1 
ATOM   3382 C  C    . ASN   A 1 150 ? 20.898 -13.600 10.873  1.00 12.42 ?  150  ASN   A C    1 
ATOM   3383 O  O    . ASN   A 1 150 ? 21.648 -12.706 11.283  1.00 13.83 ?  150  ASN   A O    1 
ATOM   3384 C  CB   . ASN   A 1 150 ? 21.004 -15.145 12.856  1.00 15.73 ?  150  ASN   A CB   1 
ATOM   3385 C  CG   . ASN   A 1 150 ? 20.905 -16.581 13.318  1.00 19.66 ?  150  ASN   A CG   1 
ATOM   3386 O  OD1  . ASN   A 1 150 ? 20.321 -17.419 12.635  1.00 20.64 ?  150  ASN   A OD1  1 
ATOM   3387 N  ND2  . ASN   A 1 150 ? 21.497 -16.879 14.467  1.00 21.90 ?  150  ASN   A ND2  1 
ATOM   3388 H  H    . ASN   A 1 150 ? 23.008 -15.449 11.425  1.00 15.20 ?  150  ASN   A H    1 
ATOM   3389 H  HA   . ASN   A 1 150 ? 20.362 -15.570 10.962  1.00 15.88 ?  150  ASN   A HA   1 
ATOM   3390 H  HB2  . ASN   A 1 150 ? 21.806 -14.758 13.243  1.00 18.89 ?  150  ASN   A HB2  1 
ATOM   3391 H  HB3  . ASN   A 1 150 ? 20.219 -14.674 13.174  1.00 18.89 ?  150  ASN   A HB3  1 
ATOM   3392 H  HD21 . ASN   A 1 150 ? 21.472 -17.686 14.770  1.00 26.30 ?  150  ASN   A HD21 1 
ATOM   3393 H  HD22 . ASN   A 1 150 ? 21.902 -16.268 14.918  1.00 26.30 ?  150  ASN   A HD22 1 
ATOM   3394 N  N    . VAL   A 1 151 ? 19.909 -13.375 10.015  1.00 12.20 ?  151  VAL   A N    1 
ATOM   3395 C  CA   . VAL   A 1 151 ? 19.691 -12.071 9.409   1.00 12.14 ?  151  VAL   A CA   1 
ATOM   3396 C  C    . VAL   A 1 151 ? 18.301 -11.562 9.767   1.00 11.89 ?  151  VAL   A C    1 
ATOM   3397 O  O    . VAL   A 1 151 ? 17.297 -12.276 9.619   1.00 13.40 ?  151  VAL   A O    1 
ATOM   3398 C  CB   . VAL   A 1 151 ? 19.978 -12.071 7.892   1.00 13.43 ?  151  VAL   A CB   1 
ATOM   3399 C  CG1  . VAL   A 1 151 ? 19.149 -13.100 7.149   1.00 14.54 ?  151  VAL   A CG1  1 
ATOM   3400 C  CG2  . VAL   A 1 151 ? 19.798 -10.665 7.312   1.00 13.71 ?  151  VAL   A CG2  1 
ATOM   3401 H  H    . VAL   A 1 151 ? 19.343 -13.971 9.764   1.00 14.66 ?  151  VAL   A H    1 
ATOM   3402 H  HA   . VAL   A 1 151 ? 20.330 -11.452 9.801   1.00 14.59 ?  151  VAL   A HA   1 
ATOM   3403 H  HB   . VAL   A 1 151 ? 20.912 -12.311 7.759   1.00 16.14 ?  151  VAL   A HB   1 
ATOM   3404 H  HG11 . VAL   A 1 151 ? 19.349 -13.057 6.200   1.00 17.47 ?  151  VAL   A HG11 1 
ATOM   3405 H  HG12 . VAL   A 1 151 ? 19.366 -13.990 7.486   1.00 17.47 ?  151  VAL   A HG12 1 
ATOM   3406 H  HG13 . VAL   A 1 151 ? 18.206 -12.921 7.295   1.00 17.47 ?  151  VAL   A HG13 1 
ATOM   3407 H  HG21 . VAL   A 1 151 ? 20.114 -10.661 6.392   1.00 16.47 ?  151  VAL   A HG21 1 
ATOM   3408 H  HG22 . VAL   A 1 151 ? 18.860 -10.430 7.338   1.00 16.47 ?  151  VAL   A HG22 1 
ATOM   3409 H  HG23 . VAL   A 1 151 ? 20.316 -10.038 7.839   1.00 16.47 ?  151  VAL   A HG23 1 
ATOM   3410 N  N    . TYR   A 1 152 ? 18.275 -10.317 10.245  1.00 11.93 ?  152  TYR   A N    1 
ATOM   3411 C  CA   . TYR   A 1 152 ? 17.078 -9.589  10.634  1.00 11.78 ?  152  TYR   A CA   1 
ATOM   3412 C  C    . TYR   A 1 152 ? 16.877 -8.491  9.601   1.00 11.34 ?  152  TYR   A C    1 
ATOM   3413 O  O    . TYR   A 1 152 ? 17.648 -7.524  9.551   1.00 11.95 ?  152  TYR   A O    1 
ATOM   3414 C  CB   . TYR   A 1 152 ? 17.273 -9.037  12.044  1.00 12.60 ?  152  TYR   A CB   1 
ATOM   3415 C  CG   . TYR   A 1 152 ? 17.227 -10.155 13.058  1.00 13.64 ?  152  TYR   A CG   1 
ATOM   3416 C  CD1  . TYR   A 1 152 ? 18.350 -10.916 13.345  1.00 15.27 ?  152  TYR   A CD1  1 
ATOM   3417 C  CD2  . TYR   A 1 152 ? 16.041 -10.492 13.684  1.00 14.10 ?  152  TYR   A CD2  1 
ATOM   3418 C  CE1  . TYR   A 1 152 ? 18.301 -11.969 14.244  1.00 16.62 ?  152  TYR   A CE1  1 
ATOM   3419 C  CE2  . TYR   A 1 152 ? 15.979 -11.546 14.589  1.00 15.56 ?  152  TYR   A CE2  1 
ATOM   3420 C  CZ   . TYR   A 1 152 ? 17.115 -12.281 14.864  1.00 16.73 ?  152  TYR   A CZ   1 
ATOM   3421 O  OH   . TYR   A 1 152 ? 17.070 -13.335 15.756  1.00 19.33 ?  152  TYR   A OH   1 
ATOM   3422 H  H    . TYR   A 1 152 ? 18.996 -9.838  10.339  1.00 14.34 ?  152  TYR   A H    1 
ATOM   3423 H  HA   . TYR   A 1 152 ? 16.316 -10.187 10.626  1.00 14.16 ?  152  TYR   A HA   1 
ATOM   3424 H  HB2  . TYR   A 1 152 ? 18.141 -8.609  12.104  1.00 15.13 ?  152  TYR   A HB2  1 
ATOM   3425 H  HB3  . TYR   A 1 152 ? 16.567 -8.410  12.244  1.00 15.13 ?  152  TYR   A HB3  1 
ATOM   3426 H  HD1  . TYR   A 1 152 ? 19.154 -10.712 12.922  1.00 18.34 ?  152  TYR   A HD1  1 
ATOM   3427 H  HD2  . TYR   A 1 152 ? 15.269 -10.005 13.495  1.00 16.93 ?  152  TYR   A HD2  1 
ATOM   3428 H  HE1  . TYR   A 1 152 ? 19.068 -12.458 14.429  1.00 19.96 ?  152  TYR   A HE1  1 
ATOM   3429 H  HE2  . TYR   A 1 152 ? 15.174 -11.751 15.006  1.00 18.69 ?  152  TYR   A HE2  1 
ATOM   3430 H  HH   . TYR   A 1 152 ? 16.291 -13.401 16.070  1.00 23.21 ?  152  TYR   A HH   1 
ATOM   3431 N  N    A LEU   A 1 153 ? 15.880 -8.689  8.736   0.62 11.55 ?  153  LEU   A N    1 
ATOM   3432 N  N    B LEU   A 1 153 ? 15.832 -8.611  8.801   0.38 11.46 ?  153  LEU   A N    1 
ATOM   3433 C  CA   A LEU   A 1 153 ? 15.610 -7.827  7.589   0.62 11.55 ?  153  LEU   A CA   1 
ATOM   3434 C  CA   B LEU   A 1 153 ? 15.571 -7.657  7.736   0.38 11.22 ?  153  LEU   A CA   1 
ATOM   3435 C  C    A LEU   A 1 153 ? 14.598 -6.752  7.961   0.62 11.62 ?  153  LEU   A C    1 
ATOM   3436 C  C    B LEU   A 1 153 ? 14.586 -6.592  8.199   0.38 11.59 ?  153  LEU   A C    1 
ATOM   3437 O  O    A LEU   A 1 153 ? 13.475 -7.060  8.374   0.62 12.51 ?  153  LEU   A O    1 
ATOM   3438 O  O    B LEU   A 1 153 ? 13.552 -6.910  8.795   0.38 12.04 ?  153  LEU   A O    1 
ATOM   3439 C  CB   A LEU   A 1 153 ? 15.047 -8.651  6.430   0.62 11.55 ?  153  LEU   A CB   1 
ATOM   3440 C  CB   B LEU   A 1 153 ? 15.016 -8.376  6.513   0.38 11.01 ?  153  LEU   A CB   1 
ATOM   3441 C  CG   A LEU   A 1 153 ? 15.999 -9.612  5.718   0.62 11.90 ?  153  LEU   A CG   1 
ATOM   3442 C  CG   B LEU   A 1 153 ? 15.953 -9.438  5.944   0.38 11.04 ?  153  LEU   A CG   1 
ATOM   3443 C  CD1  A LEU   A 1 153 ? 15.213 -10.531 4.786   0.62 12.36 ?  153  LEU   A CD1  1 
ATOM   3444 C  CD1  B LEU   A 1 153 ? 15.211 -10.261 4.911   0.38 11.10 ?  153  LEU   A CD1  1 
ATOM   3445 C  CD2  A LEU   A 1 153 ? 17.048 -8.828  4.944   0.62 11.84 ?  153  LEU   A CD2  1 
ATOM   3446 C  CD2  B LEU   A 1 153 ? 17.202 -8.799  5.343   0.38 11.60 ?  153  LEU   A CD2  1 
ATOM   3447 H  H    A LEU   A 1 153 ? 15.319 -9.346  8.803   0.62 13.88 ?  153  LEU   A H    1 
ATOM   3448 H  H    B LEU   A 1 153 ? 15.248 -9.249  8.859   0.38 13.76 ?  153  LEU   A H    1 
ATOM   3449 H  HA   A LEU   A 1 153 ? 16.428 -7.403  7.303   0.62 13.88 ?  153  LEU   A HA   1 
ATOM   3450 H  HA   B LEU   A 1 153 ? 16.406 -7.228  7.503   0.38 13.48 ?  153  LEU   A HA   1 
ATOM   3451 H  HB2  A LEU   A 1 153 ? 14.307 -9.184  6.765   0.62 13.88 ?  153  LEU   A HB2  1 
ATOM   3452 H  HB2  B LEU   A 1 153 ? 14.187 -8.807  6.765   0.38 13.23 ?  153  LEU   A HB2  1 
ATOM   3453 H  HB3  A LEU   A 1 153 ? 14.716 -8.038  5.756   0.62 13.88 ?  153  LEU   A HB3  1 
ATOM   3454 H  HB3  B LEU   A 1 153 ? 14.854 -7.715  5.825   0.38 13.23 ?  153  LEU   A HB3  1 
ATOM   3455 H  HG   A LEU   A 1 153 ? 16.450 -10.166 6.376   0.62 14.29 ?  153  LEU   A HG   1 
ATOM   3456 H  HG   B LEU   A 1 153 ? 16.233 -10.030 6.661   0.38 13.26 ?  153  LEU   A HG   1 
ATOM   3457 H  HD11 A LEU   A 1 153 ? 15.804 -11.224 4.449   0.62 14.84 ?  153  LEU   A HD11 1 
ATOM   3458 H  HD11 B LEU   A 1 153 ? 15.806 -10.946 4.571   0.38 13.34 ?  153  LEU   A HD11 1 
ATOM   3459 H  HD12 A LEU   A 1 153 ? 14.482 -10.934 5.278   0.62 14.84 ?  153  LEU   A HD12 1 
ATOM   3460 H  HD12 B LEU   A 1 153 ? 14.438 -10.668 5.329   0.38 13.34 ?  153  LEU   A HD12 1 
ATOM   3461 H  HD13 A LEU   A 1 153 ? 14.866 -10.007 4.047   0.62 14.84 ?  153  LEU   A HD13 1 
ATOM   3462 H  HD13 B LEU   A 1 153 ? 14.929 -9.677  4.189   0.38 13.34 ?  153  LEU   A HD13 1 
ATOM   3463 H  HD21 A LEU   A 1 153 ? 17.618 -9.450  4.472   0.62 14.23 ?  153  LEU   A HD21 1 
ATOM   3464 H  HD21 B LEU   A 1 153 ? 17.725 -9.486  4.904   0.38 13.94 ?  153  LEU   A HD21 1 
ATOM   3465 H  HD22 A LEU   A 1 153 ? 16.596 -8.245  4.317   0.62 14.23 ?  153  LEU   A HD22 1 
ATOM   3466 H  HD22 B LEU   A 1 153 ? 16.933 -8.124  4.702   0.38 13.94 ?  153  LEU   A HD22 1 
ATOM   3467 H  HD23 A LEU   A 1 153 ? 17.568 -8.306  5.571   0.62 14.23 ?  153  LEU   A HD23 1 
ATOM   3468 H  HD23 B LEU   A 1 153 ? 17.723 -8.389  6.054   0.38 13.94 ?  153  LEU   A HD23 1 
ATOM   3469 N  N    A ALA   A 1 154 ? 14.985 -5.496  7.774   0.62 11.90 ?  154  ALA   A N    1 
ATOM   3470 N  N    B ALA   A 1 154 ? 14.916 -5.332  7.921   0.38 11.58 ?  154  ALA   A N    1 
ATOM   3471 C  CA   A ALA   A 1 154 ? 14.113 -4.353  7.998   0.62 12.74 ?  154  ALA   A CA   1 
ATOM   3472 C  CA   B ALA   A 1 154 ? 14.037 -4.194  8.165   0.38 12.73 ?  154  ALA   A CA   1 
ATOM   3473 C  C    A ALA   A 1 154 ? 13.619 -3.837  6.654   0.62 12.75 ?  154  ALA   A C    1 
ATOM   3474 C  C    B ALA   A 1 154 ? 13.557 -3.692  6.807   0.38 12.75 ?  154  ALA   A C    1 
ATOM   3475 O  O    A ALA   A 1 154 ? 14.425 -3.516  5.774   0.62 12.83 ?  154  ALA   A O    1 
ATOM   3476 O  O    B ALA   A 1 154 ? 14.351 -3.169  6.018   0.38 12.70 ?  154  ALA   A O    1 
ATOM   3477 C  CB   A ALA   A 1 154 ? 14.865 -3.246  8.733   0.62 13.37 ?  154  ALA   A CB   1 
ATOM   3478 C  CB   B ALA   A 1 154 ? 14.782 -3.097  8.925   0.38 13.38 ?  154  ALA   A CB   1 
ATOM   3479 H  H    A ALA   A 1 154 ? 15.774 -5.286  7.509   0.62 14.30 ?  154  ALA   A H    1 
ATOM   3480 H  H    B ALA   A 1 154 ? 15.675 -5.105  7.581   0.38 13.91 ?  154  ALA   A H    1 
ATOM   3481 H  HA   A ALA   A 1 154 ? 13.350 -4.624  8.527   0.62 15.30 ?  154  ALA   A HA   1 
ATOM   3482 H  HA   B ALA   A 1 154 ? 13.272 -4.473  8.692   0.38 15.29 ?  154  ALA   A HA   1 
ATOM   3483 H  HB1  A ALA   A 1 154 ? 14.264 -2.498  8.866   0.62 16.06 ?  154  ALA   A HB1  1 
ATOM   3484 H  HB1  B ALA   A 1 154 ? 14.181 -2.351  9.075   0.38 16.07 ?  154  ALA   A HB1  1 
ATOM   3485 H  HB2  A ALA   A 1 154 ? 15.169 -3.588  9.586   0.62 16.06 ?  154  ALA   A HB2  1 
ATOM   3486 H  HB2  B ALA   A 1 154 ? 15.089 -3.450  9.777   0.38 16.07 ?  154  ALA   A HB2  1 
ATOM   3487 H  HB3  A ALA   A 1 154 ? 15.623 -2.971  8.194   0.62 16.06 ?  154  ALA   A HB3  1 
ATOM   3488 H  HB3  B ALA   A 1 154 ? 15.543 -2.807  8.397   0.38 16.07 ?  154  ALA   A HB3  1 
ATOM   3489 N  N    A VAL   A 1 155 ? 12.298 -3.761  6.507   0.62 13.81 ?  155  VAL   A N    1 
ATOM   3490 N  N    B VAL   A 1 155 ? 12.262 -3.863  6.536   0.38 13.47 ?  155  VAL   A N    1 
ATOM   3491 C  CA   A VAL   A 1 155 ? 11.646 -3.302  5.286   0.62 15.09 ?  155  VAL   A CA   1 
ATOM   3492 C  CA   B VAL   A 1 155 ? 11.643 -3.467  5.273   0.38 13.92 ?  155  VAL   A CA   1 
ATOM   3493 C  C    A VAL   A 1 155 ? 10.872 -2.038  5.632   0.62 16.30 ?  155  VAL   A C    1 
ATOM   3494 C  C    B VAL   A 1 155 ? 10.964 -2.121  5.475   0.38 14.39 ?  155  VAL   A C    1 
ATOM   3495 O  O    A VAL   A 1 155 ? 9.876  -2.100  6.363   0.62 16.35 ?  155  VAL   A O    1 
ATOM   3496 O  O    B VAL   A 1 155 ? 10.155 -1.963  6.399   0.38 14.56 ?  155  VAL   A O    1 
ATOM   3497 C  CB   A VAL   A 1 155 ? 10.725 -4.377  4.692   0.62 15.27 ?  155  VAL   A CB   1 
ATOM   3498 C  CB   B VAL   A 1 155 ? 10.634 -4.528  4.795   0.38 13.97 ?  155  VAL   A CB   1 
ATOM   3499 C  CG1  A VAL   A 1 155 ? 9.976  -3.833  3.491   0.62 16.18 ?  155  VAL   A CG1  1 
ATOM   3500 C  CG1  B VAL   A 1 155 ? 9.920  -4.070  3.528   0.38 14.52 ?  155  VAL   A CG1  1 
ATOM   3501 C  CG2  A VAL   A 1 155 ? 11.540 -5.605  4.301   0.62 15.75 ?  155  VAL   A CG2  1 
ATOM   3502 C  CG2  B VAL   A 1 155 ? 11.333 -5.851  4.551   0.38 14.40 ?  155  VAL   A CG2  1 
ATOM   3503 H  H    A VAL   A 1 155 ? 11.738 -3.987  7.125   0.62 16.58 ?  155  VAL   A H    1 
ATOM   3504 H  H    B VAL   A 1 155 ? 11.708 -4.214  7.090   0.38 16.18 ?  155  VAL   A H    1 
ATOM   3505 H  HA   A VAL   A 1 155 ? 12.319 -3.080  4.629   0.62 18.13 ?  155  VAL   A HA   1 
ATOM   3506 H  HA   B VAL   A 1 155 ? 12.327 -3.371  4.593   0.38 16.71 ?  155  VAL   A HA   1 
ATOM   3507 H  HB   A VAL   A 1 155 ? 10.074 -4.646  5.361   0.62 18.34 ?  155  VAL   A HB   1 
ATOM   3508 H  HB   B VAL   A 1 155 ? 9.966  -4.666  5.487   0.38 16.79 ?  155  VAL   A HB   1 
ATOM   3509 H  HG11 A VAL   A 1 155 ? 9.565  -4.574  3.017   0.62 19.43 ?  155  VAL   A HG11 1 
ATOM   3510 H  HG11 B VAL   A 1 155 ? 9.456  -4.827  3.134   0.38 17.44 ?  155  VAL   A HG11 1 
ATOM   3511 H  HG12 A VAL   A 1 155 ? 9.289  -3.218  3.796   0.62 19.43 ?  155  VAL   A HG12 1 
ATOM   3512 H  HG12 B VAL   A 1 155 ? 9.280  -3.377  3.754   0.38 17.44 ?  155  VAL   A HG12 1 
ATOM   3513 H  HG13 A VAL   A 1 155 ? 10.600 -3.375  2.910   0.62 19.43 ?  155  VAL   A HG13 1 
ATOM   3514 H  HG13 B VAL   A 1 155 ? 10.573 -3.725  2.901   0.38 17.44 ?  155  VAL   A HG13 1 
ATOM   3515 H  HG21 A VAL   A 1 155 ? 10.947 -6.264  3.906   0.62 18.91 ?  155  VAL   A HG21 1 
ATOM   3516 H  HG21 B VAL   A 1 155 ? 10.711 -6.459  4.124   0.38 17.29 ?  155  VAL   A HG21 1 
ATOM   3517 H  HG22 A VAL   A 1 155 ? 12.218 -5.343  3.659   0.62 18.91 ?  155  VAL   A HG22 1 
ATOM   3518 H  HG22 B VAL   A 1 155 ? 12.098 -5.699  3.974   0.38 17.29 ?  155  VAL   A HG22 1 
ATOM   3519 H  HG23 A VAL   A 1 155 ? 11.960 -5.973  5.094   0.62 18.91 ?  155  VAL   A HG23 1 
ATOM   3520 H  HG23 B VAL   A 1 155 ? 11.627 -6.215  5.400   0.38 17.29 ?  155  VAL   A HG23 1 
ATOM   3521 N  N    A PHE   A 1 156 ? 11.327 -0.895  5.099   0.62 17.03 ?  156  PHE   A N    1 
ATOM   3522 N  N    B PHE   A 1 156 ? 11.282 -1.154  4.606   0.38 14.62 ?  156  PHE   A N    1 
ATOM   3523 C  CA   A PHE   A 1 156 ? 10.787 0.407   5.496   0.62 18.82 ?  156  PHE   A CA   1 
ATOM   3524 C  CA   B PHE   A 1 156 ? 10.824 0.223   4.796   0.38 14.63 ?  156  PHE   A CA   1 
ATOM   3525 C  C    A PHE   A 1 156 ? 9.318  0.561   5.111   0.62 18.55 ?  156  PHE   A C    1 
ATOM   3526 C  C    B PHE   A 1 156 ? 9.357  0.408   4.409   0.38 15.04 ?  156  PHE   A C    1 
ATOM   3527 O  O    A PHE   A 1 156 ? 8.514  1.077   5.897   0.62 19.02 ?  156  PHE   A O    1 
ATOM   3528 O  O    B PHE   A 1 156 ? 8.609  1.091   5.119   0.38 16.33 ?  156  PHE   A O    1 
ATOM   3529 C  CB   A PHE   A 1 156 ? 11.625 1.524   4.861   0.62 20.29 ?  156  PHE   A CB   1 
ATOM   3530 C  CB   B PHE   A 1 156 ? 11.730 1.166   3.994   0.38 13.91 ?  156  PHE   A CB   1 
ATOM   3531 C  CG   A PHE   A 1 156 ? 11.130 2.918   5.171   0.62 22.19 ?  156  PHE   A CG   1 
ATOM   3532 C  CG   B PHE   A 1 156 ? 11.477 2.641   4.230   0.38 14.16 ?  156  PHE   A CG   1 
ATOM   3533 C  CD1  A PHE   A 1 156 ? 11.061 3.362   6.480   0.62 23.40 ?  156  PHE   A CD1  1 
ATOM   3534 C  CD1  B PHE   A 1 156 ? 11.935 3.270   5.381   0.38 15.07 ?  156  PHE   A CD1  1 
ATOM   3535 C  CD2  A PHE   A 1 156 ? 10.758 3.784   4.153   0.62 23.28 ?  156  PHE   A CD2  1 
ATOM   3536 C  CD2  B PHE   A 1 156 ? 10.825 3.403   3.276   0.38 14.32 ?  156  PHE   A CD2  1 
ATOM   3537 C  CE1  A PHE   A 1 156 ? 10.614 4.638   6.773   0.62 24.36 ?  156  PHE   A CE1  1 
ATOM   3538 C  CE1  B PHE   A 1 156 ? 11.714 4.627   5.586   0.38 15.49 ?  156  PHE   A CE1  1 
ATOM   3539 C  CE2  A PHE   A 1 156 ? 10.310 5.065   4.439   0.62 24.15 ?  156  PHE   A CE2  1 
ATOM   3540 C  CE2  B PHE   A 1 156 ? 10.606 4.757   3.472   0.38 14.93 ?  156  PHE   A CE2  1 
ATOM   3541 C  CZ   A PHE   A 1 156 ? 10.241 5.491   5.751   0.62 24.58 ?  156  PHE   A CZ   1 
ATOM   3542 C  CZ   B PHE   A 1 156 ? 11.053 5.371   4.628   0.38 15.48 ?  156  PHE   A CZ   1 
ATOM   3543 H  H    A PHE   A 1 156 ? 11.948 -0.850  4.502   0.62 20.45 ?  156  PHE   A H    1 
ATOM   3544 H  H    B PHE   A 1 156 ? 11.759 -1.275  3.896   0.38 17.56 ?  156  PHE   A H    1 
ATOM   3545 H  HA   A PHE   A 1 156 ? 10.857 0.502   6.456   0.62 22.60 ?  156  PHE   A HA   1 
ATOM   3546 H  HA   B PHE   A 1 156 ? 10.919 0.448   5.733   0.38 17.58 ?  156  PHE   A HA   1 
ATOM   3547 H  HB2  A PHE   A 1 156 ? 12.540 1.456   5.188   0.62 24.37 ?  156  PHE   A HB2  1 
ATOM   3548 H  HB2  B PHE   A 1 156 ? 12.652 0.985   4.235   0.38 16.71 ?  156  PHE   A HB2  1 
ATOM   3549 H  HB3  A PHE   A 1 156 ? 11.619 1.416   3.896   0.62 24.37 ?  156  PHE   A HB3  1 
ATOM   3550 H  HB3  B PHE   A 1 156 ? 11.600 0.993   3.048   0.38 16.71 ?  156  PHE   A HB3  1 
ATOM   3551 H  HD1  A PHE   A 1 156 ? 11.314 2.789   7.172   0.62 28.10 ?  156  PHE   A HD1  1 
ATOM   3552 H  HD1  B PHE   A 1 156 ? 12.381 2.771   6.031   0.38 18.10 ?  156  PHE   A HD1  1 
ATOM   3553 H  HD2  A PHE   A 1 156 ? 10.808 3.496   3.269   0.62 27.95 ?  156  PHE   A HD2  1 
ATOM   3554 H  HD2  B PHE   A 1 156 ? 10.523 2.998   2.499   0.38 17.20 ?  156  PHE   A HD2  1 
ATOM   3555 H  HE1  A PHE   A 1 156 ? 10.570 4.922   7.658   0.62 29.25 ?  156  PHE   A HE1  1 
ATOM   3556 H  HE1  B PHE   A 1 156 ? 12.020 5.031   6.367   0.38 18.60 ?  156  PHE   A HE1  1 
ATOM   3557 H  HE2  A PHE   A 1 156 ? 10.062 5.634   3.749   0.62 28.99 ?  156  PHE   A HE2  1 
ATOM   3558 H  HE2  B PHE   A 1 156 ? 10.159 5.254   2.827   0.38 17.93 ?  156  PHE   A HE2  1 
ATOM   3559 H  HZ   A PHE   A 1 156 ? 9.942  6.348   5.949   0.62 29.52 ?  156  PHE   A HZ   1 
ATOM   3560 H  HZ   B PHE   A 1 156 ? 10.906 6.278   4.766   0.38 18.60 ?  156  PHE   A HZ   1 
ATOM   3561 N  N    A ASP   A 1 157 ? 8.954  0.136   3.906   0.62 17.98 ?  157  ASP   A N    1 
ATOM   3562 N  N    B ASP   A 1 157 ? 8.925  -0.194  3.302   0.38 15.37 ?  157  ASP   A N    1 
ATOM   3563 C  CA   A ASP   A 1 157 ? 7.627  0.389   3.355   0.62 18.44 ?  157  ASP   A CA   1 
ATOM   3564 C  CA   B ASP   A 1 157 ? 7.592  0.046   2.757   0.38 15.37 ?  157  ASP   A CA   1 
ATOM   3565 C  C    A ASP   A 1 157 ? 6.640  -0.651  3.878   0.62 18.36 ?  157  ASP   A C    1 
ATOM   3566 C  C    B ASP   A 1 157 ? 6.599  -0.996  3.267   0.38 14.65 ?  157  ASP   A C    1 
ATOM   3567 O  O    A ASP   A 1 157 ? 6.826  -1.852  3.655   0.62 17.82 ?  157  ASP   A O    1 
ATOM   3568 O  O    B ASP   A 1 157 ? 6.823  -2.200  3.121   0.38 14.09 ?  157  ASP   A O    1 
ATOM   3569 C  CB   A ASP   A 1 157 ? 7.716  0.299   1.836   0.62 19.44 ?  157  ASP   A CB   1 
ATOM   3570 C  CB   B ASP   A 1 157 ? 7.641  0.020   1.229   0.38 16.11 ?  157  ASP   A CB   1 
ATOM   3571 C  CG   A ASP   A 1 157 ? 6.482  0.823   1.148   0.62 21.27 ?  157  ASP   A CG   1 
ATOM   3572 C  CG   B ASP   A 1 157 ? 6.315  0.426   0.594   0.38 17.13 ?  157  ASP   A CG   1 
ATOM   3573 O  OD1  A ASP   A 1 157 ? 6.411  2.049   0.908   0.62 23.03 ?  157  ASP   A OD1  1 
ATOM   3574 O  OD1  B ASP   A 1 157 ? 5.865  1.577   0.804   0.38 18.43 ?  157  ASP   A OD1  1 
ATOM   3575 O  OD2  A ASP   A 1 157 ? 5.582  0.014   0.846   0.62 21.40 -1 157  ASP   A OD2  1 
ATOM   3576 O  OD2  B ASP   A 1 157 ? 5.716  -0.408  -0.116  0.38 17.42 -1 157  ASP   A OD2  1 
ATOM   3577 H  H    A ASP   A 1 157 ? 9.467  -0.309  3.379   0.62 21.59 ?  157  ASP   A H    1 
ATOM   3578 H  H    B ASP   A 1 157 ? 9.390  -0.757  2.848   0.38 18.46 ?  157  ASP   A H    1 
ATOM   3579 H  HA   A ASP   A 1 157 ? 7.322  1.277   3.605   0.62 22.14 ?  157  ASP   A HA   1 
ATOM   3580 H  HA   B ASP   A 1 157 ? 7.282  0.917   3.038   0.38 18.46 ?  157  ASP   A HA   1 
ATOM   3581 H  HB2  A ASP   A 1 157 ? 8.466  0.824   1.530   0.62 23.34 ?  157  ASP   A HB2  1 
ATOM   3582 H  HB2  B ASP   A 1 157 ? 8.347  0.620   0.933   0.38 19.34 ?  157  ASP   A HB2  1 
ATOM   3583 H  HB3  A ASP   A 1 157 ? 7.839  -0.631  1.586   0.62 23.34 ?  157  ASP   A HB3  1 
ATOM   3584 H  HB3  B ASP   A 1 157 ? 7.837  -0.884  0.933   0.38 19.34 ?  157  ASP   A HB3  1 
ATOM   3585 N  N    A LYS   A 1 158 ? 5.579  -0.195  4.553   0.62 19.76 ?  158  LYS   A N    1 
ATOM   3586 N  N    B LYS   A 1 158 ? 5.492  -0.518  3.848   0.38 14.95 ?  158  LYS   A N    1 
ATOM   3587 C  CA   A LYS   A 1 158 ? 4.612  -1.135  5.120   0.62 21.34 ?  158  LYS   A CA   1 
ATOM   3588 C  CA   B LYS   A 1 158 ? 4.504  -1.404  4.466   0.38 15.99 ?  158  LYS   A CA   1 
ATOM   3589 C  C    A LYS   A 1 158 ? 3.899  -1.925  4.028   0.62 20.94 ?  158  LYS   A C    1 
ATOM   3590 C  C    B LYS   A 1 158 ? 3.847  -2.323  3.438   0.38 15.06 ?  158  LYS   A C    1 
ATOM   3591 O  O    A LYS   A 1 158 ? 3.685  -3.134  4.170   0.62 20.95 ?  158  LYS   A O    1 
ATOM   3592 O  O    B LYS   A 1 158 ? 3.736  -3.537  3.652   0.38 14.80 ?  158  LYS   A O    1 
ATOM   3593 C  CB   A LYS   A 1 158 ? 3.606  -0.401  6.012   0.62 23.02 ?  158  LYS   A CB   1 
ATOM   3594 C  CB   B LYS   A 1 158 ? 3.455  -0.557  5.196   0.38 18.28 ?  158  LYS   A CB   1 
ATOM   3595 C  CG   A LYS   A 1 158 ? 2.415  -1.253  6.473   0.62 25.07 ?  158  LYS   A CG   1 
ATOM   3596 C  CG   B LYS   A 1 158 ? 2.207  -1.302  5.656   0.38 20.84 ?  158  LYS   A CG   1 
ATOM   3597 C  CD   A LYS   A 1 158 ? 2.834  -2.500  7.255   0.62 26.61 ?  158  LYS   A CD   1 
ATOM   3598 C  CD   B LYS   A 1 158 ? 2.508  -2.291  6.766   0.38 22.91 ?  158  LYS   A CD   1 
ATOM   3599 C  CE   A LYS   A 1 158 ? 1.615  -3.203  7.846   0.62 27.45 ?  158  LYS   A CE   1 
ATOM   3600 C  CE   B LYS   A 1 158 ? 1.231  -2.953  7.261   0.38 24.05 ?  158  LYS   A CE   1 
ATOM   3601 N  NZ   A LYS   A 1 158 ? 1.918  -4.566  8.373   0.62 27.76 ?  158  LYS   A NZ   1 
ATOM   3602 N  NZ   B LYS   A 1 158 ? 1.501  -4.007  8.275   0.38 24.66 ?  158  LYS   A NZ   1 
ATOM   3603 H  H    A LYS   A 1 158 ? 5.400  0.636   4.691   0.62 23.73 ?  158  LYS   A H    1 
ATOM   3604 H  H    B LYS   A 1 158 ? 5.296  0.314   3.908   0.38 17.96 ?  158  LYS   A H    1 
ATOM   3605 H  HA   A LYS   A 1 158 ? 5.087  -1.765  5.681   0.62 25.62 ?  158  LYS   A HA   1 
ATOM   3606 H  HA   B LYS   A 1 158 ? 4.941  -1.962  5.128   0.38 19.20 ?  158  LYS   A HA   1 
ATOM   3607 H  HB2  A LYS   A 1 158 ? 4.066  -0.088  6.809   0.62 27.64 ?  158  LYS   A HB2  1 
ATOM   3608 H  HB2  B LYS   A 1 158 ? 3.866  -0.170  5.989   0.38 21.96 ?  158  LYS   A HB2  1 
ATOM   3609 H  HB3  A LYS   A 1 158 ? 3.252  0.360   5.524   0.62 27.64 ?  158  LYS   A HB3  1 
ATOM   3610 H  HB3  B LYS   A 1 158 ? 3.165  0.156   4.606   0.38 21.96 ?  158  LYS   A HB3  1 
ATOM   3611 H  HG2  A LYS   A 1 158 ? 1.853  -0.713  7.052   0.62 30.10 ?  158  LYS   A HG2  1 
ATOM   3612 H  HG2  B LYS   A 1 158 ? 1.570  -0.657  6.001   0.38 25.02 ?  158  LYS   A HG2  1 
ATOM   3613 H  HG3  A LYS   A 1 158 ? 1.903  -1.536  5.698   0.62 30.10 ?  158  LYS   A HG3  1 
ATOM   3614 H  HG3  B LYS   A 1 158 ? 1.813  -1.784  4.913   0.38 25.02 ?  158  LYS   A HG3  1 
ATOM   3615 H  HD2  A LYS   A 1 158 ? 3.282  -3.117  6.658   0.62 31.94 ?  158  LYS   A HD2  1 
ATOM   3616 H  HD2  B LYS   A 1 158 ? 3.103  -2.980  6.431   0.38 27.51 ?  158  LYS   A HD2  1 
ATOM   3617 H  HD3  A LYS   A 1 158 ? 3.424  -2.239  7.979   0.62 31.94 ?  158  LYS   A HD3  1 
ATOM   3618 H  HD3  B LYS   A 1 158 ? 2.921  -1.822  7.510   0.38 27.51 ?  158  LYS   A HD3  1 
ATOM   3619 H  HE2  A LYS   A 1 158 ? 1.256  -2.670  8.572   0.62 32.96 ?  158  LYS   A HE2  1 
ATOM   3620 H  HE2  B LYS   A 1 158 ? 0.664  -2.279  7.668   0.38 28.87 ?  158  LYS   A HE2  1 
ATOM   3621 H  HE3  A LYS   A 1 158 ? 0.945  -3.295  7.156   0.62 32.96 ?  158  LYS   A HE3  1 
ATOM   3622 H  HE3  B LYS   A 1 158 ? 0.775  -3.362  6.510   0.38 28.87 ?  158  LYS   A HE3  1 
ATOM   3623 H  HZ1  A LYS   A 1 158 ? 1.179  -4.933  8.709   0.62 33.33 ?  158  LYS   A HZ1  1 
ATOM   3624 H  HZ1  B LYS   A 1 158 ? 0.735  -4.372  8.543   0.38 29.61 ?  158  LYS   A HZ1  1 
ATOM   3625 H  HZ2  A LYS   A 1 158 ? 2.223  -5.082  7.715   0.62 33.33 ?  158  LYS   A HZ2  1 
ATOM   3626 H  HZ2  B LYS   A 1 158 ? 2.018  -4.640  7.925   0.38 29.61 ?  158  LYS   A HZ2  1 
ATOM   3627 H  HZ3  A LYS   A 1 158 ? 2.533  -4.518  9.013   0.62 33.33 ?  158  LYS   A HZ3  1 
ATOM   3628 H  HZ3  B LYS   A 1 158 ? 1.914  -3.652  8.979   0.38 29.61 ?  158  LYS   A HZ3  1 
ATOM   3629 N  N    A ASN   A 1 159 ? 3.520  -1.266  2.932   0.62 21.31 ?  159  ASN   A N    1 
ATOM   3630 N  N    B ASN   A 1 159 ? 3.379  -1.763  2.323   0.38 15.54 ?  159  ASN   A N    1 
ATOM   3631 C  CA   A ASN   A 1 159 ? 2.852  -1.986  1.853   0.62 21.76 ?  159  ASN   A CA   1 
ATOM   3632 C  CA   B ASN   A 1 159 ? 2.719  -2.597  1.324   0.38 16.24 ?  159  ASN   A CA   1 
ATOM   3633 C  C    A ASN   A 1 159 ? 3.760  -3.060  1.263   0.62 20.72 ?  159  ASN   A C    1 
ATOM   3634 C  C    B ASN   A 1 159 ? 3.678  -3.647  0.774   0.38 15.10 ?  159  ASN   A C    1 
ATOM   3635 O  O    A ASN   A 1 159 ? 3.315  -4.183  0.998   0.62 20.56 ?  159  ASN   A O    1 
ATOM   3636 O  O    B ASN   A 1 159 ? 3.281  -4.789  0.511   0.38 15.12 ?  159  ASN   A O    1 
ATOM   3637 C  CB   A ASN   A 1 159 ? 2.378  -1.006  0.778   0.62 23.88 ?  159  ASN   A CB   1 
ATOM   3638 C  CB   B ASN   A 1 159 ? 2.131  -1.721  0.217   0.38 18.84 ?  159  ASN   A CB   1 
ATOM   3639 C  CG   A ASN   A 1 159 ? 1.177  -0.198  1.223   0.62 26.09 ?  159  ASN   A CG   1 
ATOM   3640 C  CG   B ASN   A 1 159 ? 1.101  -0.742  0.743   0.38 21.92 ?  159  ASN   A CG   1 
ATOM   3641 O  OD1  A ASN   A 1 159 ? 0.333  -0.697  1.962   0.62 26.29 ?  159  ASN   A OD1  1 
ATOM   3642 O  OD1  B ASN   A 1 159 ? -0.096 -1.019  0.733   0.38 23.59 ?  159  ASN   A OD1  1 
ATOM   3643 N  ND2  A ASN   A 1 159 ? 1.096  1.055   0.780   0.62 27.08 ?  159  ASN   A ND2  1 
ATOM   3644 N  ND2  B ASN   A 1 159 ? 1.567  0.411   1.220   0.38 22.69 ?  159  ASN   A ND2  1 
ATOM   3645 H  H    A ASN   A 1 159 ? 3.632  -0.427  2.796   0.62 25.59 ?  159  ASN   A H    1 
ATOM   3646 H  H    B ASN   A 1 159 ? 3.425  -0.926  2.132   0.38 18.67 ?  159  ASN   A H    1 
ATOM   3647 H  HA   A ASN   A 1 159 ? 2.066  -2.429  2.214   0.62 26.13 ?  159  ASN   A HA   1 
ATOM   3648 H  HA   B ASN   A 1 159 ? 1.979  -3.061  1.747   0.38 19.50 ?  159  ASN   A HA   1 
ATOM   3649 H  HB2  A ASN   A 1 159 ? 3.092  -0.389  0.571   0.62 28.67 ?  159  ASN   A HB2  1 
ATOM   3650 H  HB2  B ASN   A 1 159 ? 2.837  -1.208  -0.201  0.38 22.63 ?  159  ASN   A HB2  1 
ATOM   3651 H  HB3  A ASN   A 1 159 ? 2.123  -1.504  -0.016  0.62 28.67 ?  159  ASN   A HB3  1 
ATOM   3652 H  HB3  B ASN   A 1 159 ? 1.689  -2.282  -0.438  0.38 22.63 ?  159  ASN   A HB3  1 
ATOM   3653 H  HD21 A ASN   A 1 159 ? 0.434  1.553   1.003   0.62 32.52 ?  159  ASN   A HD21 1 
ATOM   3654 H  HD21 B ASN   A 1 159 ? 1.023  1.004   1.535   0.38 27.25 ?  159  ASN   A HD21 1 
ATOM   3655 H  HD22 A ASN   A 1 159 ? 1.711  1.370   0.271   0.62 32.52 ?  159  ASN   A HD22 1 
ATOM   3656 H  HD22 B ASN   A 1 159 ? 2.412  0.572   1.213   0.38 27.25 ?  159  ASN   A HD22 1 
ATOM   3657 N  N    A LEU   A 1 160 ? 5.040  -2.742  1.068   0.62 19.58 ?  160  LEU   A N    1 
ATOM   3658 N  N    B LEU   A 1 160 ? 4.954  -3.292  0.626   0.38 14.67 ?  160  LEU   A N    1 
ATOM   3659 C  CA   A LEU   A 1 160 ? 5.964  -3.726  0.513   0.62 19.12 ?  160  LEU   A CA   1 
ATOM   3660 C  CA   B LEU   A 1 160 ? 5.945  -4.278  0.206   0.38 14.42 ?  160  LEU   A CA   1 
ATOM   3661 C  C    A LEU   A 1 160 ? 6.153  -4.901  1.461   0.62 18.53 ?  160  LEU   A C    1 
ATOM   3662 C  C    B LEU   A 1 160 ? 6.155  -5.342  1.283   0.38 14.34 ?  160  LEU   A C    1 
ATOM   3663 O  O    A LEU   A 1 160 ? 6.196  -6.058  1.028   0.62 19.19 ?  160  LEU   A O    1 
ATOM   3664 O  O    B LEU   A 1 160 ? 6.194  -6.542  0.985   0.38 14.31 ?  160  LEU   A O    1 
ATOM   3665 C  CB   A LEU   A 1 160 ? 7.308  -3.070  0.207   0.62 19.03 ?  160  LEU   A CB   1 
ATOM   3666 C  CB   B LEU   A 1 160 ? 7.257  -3.576  -0.138  0.38 14.72 ?  160  LEU   A CB   1 
ATOM   3667 C  CG   A LEU   A 1 160 ? 8.383  -4.064  -0.225  0.62 19.35 ?  160  LEU   A CG   1 
ATOM   3668 C  CG   B LEU   A 1 160 ? 8.420  -4.530  -0.396  0.38 15.43 ?  160  LEU   A CG   1 
ATOM   3669 C  CD1  A LEU   A 1 160 ? 7.930  -4.815  -1.465  0.62 19.55 ?  160  LEU   A CD1  1 
ATOM   3670 C  CD1  B LEU   A 1 160 ? 8.099  -5.440  -1.576  0.38 15.94 ?  160  LEU   A CD1  1 
ATOM   3671 C  CD2  A LEU   A 1 160 ? 9.703  -3.365  -0.464  0.62 19.45 ?  160  LEU   A CD2  1 
ATOM   3672 C  CD2  B LEU   A 1 160 ? 9.699  -3.744  -0.607  0.38 15.77 ?  160  LEU   A CD2  1 
ATOM   3673 H  H    A LEU   A 1 160 ? 5.389  -1.981  1.259   0.62 23.51 ?  160  LEU   A H    1 
ATOM   3674 H  H    B LEU   A 1 160 ? 5.265  -2.504  0.762   0.38 17.62 ?  160  LEU   A H    1 
ATOM   3675 H  HA   A LEU   A 1 160 ? 5.594  -4.066  -0.313  0.62 22.96 ?  160  LEU   A HA   1 
ATOM   3676 H  HA   B LEU   A 1 160 ? 5.625  -4.720  -0.597  0.38 17.32 ?  160  LEU   A HA   1 
ATOM   3677 H  HB2  A LEU   A 1 160 ? 7.185  -2.419  -0.506  0.62 22.85 ?  160  LEU   A HB2  1 
ATOM   3678 H  HB2  B LEU   A 1 160 ? 7.124  -3.038  -0.940  0.38 17.67 ?  160  LEU   A HB2  1 
ATOM   3679 H  HB3  A LEU   A 1 160 ? 7.621  -2.628  1.009   0.62 22.85 ?  160  LEU   A HB3  1 
ATOM   3680 H  HB3  B LEU   A 1 160 ? 7.503  -3.002  0.602   0.38 17.67 ?  160  LEU   A HB3  1 
ATOM   3681 H  HG   A LEU   A 1 160 ? 8.520  -4.712  0.484   0.62 23.24 ?  160  LEU   A HG   1 
ATOM   3682 H  HG   B LEU   A 1 160 ? 8.550  -5.090  0.382   0.38 18.53 ?  160  LEU   A HG   1 
ATOM   3683 H  HD11 A LEU   A 1 160 ? 8.681  -5.311  -1.820  0.62 23.48 ?  160  LEU   A HD11 1 
ATOM   3684 H  HD11 B LEU   A 1 160 ? 8.877  -5.979  -1.775  0.38 19.15 ?  160  LEU   A HD11 1 
ATOM   3685 H  HD12 A LEU   A 1 160 ? 7.214  -5.426  -1.225  0.62 23.48 ?  160  LEU   A HD12 1 
ATOM   3686 H  HD12 B LEU   A 1 160 ? 7.351  -6.017  -1.340  0.38 19.15 ?  160  LEU   A HD12 1 
ATOM   3687 H  HD13 A LEU   A 1 160 ? 7.613  -4.176  -2.122  0.62 23.48 ?  160  LEU   A HD13 1 
ATOM   3688 H  HD13 B LEU   A 1 160 ? 7.863  -4.895  -2.343  0.38 19.15 ?  160  LEU   A HD13 1 
ATOM   3689 H  HD21 A LEU   A 1 160 ? 10.361 -4.026  -0.729  0.62 23.36 ?  160  LEU   A HD21 1 
ATOM   3690 H  HD21 B LEU   A 1 160 ? 10.439 -4.365  -0.673  0.38 18.94 ?  160  LEU   A HD21 1 
ATOM   3691 H  HD22 A LEU   A 1 160 ? 9.587  -2.709  -1.167  0.62 23.36 ?  160  LEU   A HD22 1 
ATOM   3692 H  HD22 B LEU   A 1 160 ? 9.621  -3.226  -1.422  0.38 18.94 ?  160  LEU   A HD22 1 
ATOM   3693 H  HD23 A LEU   A 1 160 ? 9.981  -2.931  0.357   0.62 23.36 ?  160  LEU   A HD23 1 
ATOM   3694 H  HD23 B LEU   A 1 160 ? 9.830  -3.152  0.152   0.38 18.94 ?  160  LEU   A HD23 1 
ATOM   3695 N  N    A TYR   A 1 161 ? 6.274  -4.622  2.757   0.62 18.30 ?  161  TYR   A N    1 
ATOM   3696 N  N    B TYR   A 1 161 ? 6.306  -4.919  2.542   0.38 15.12 ?  161  TYR   A N    1 
ATOM   3697 C  CA   A TYR   A 1 161 ? 6.430  -5.694  3.731   0.62 17.92 ?  161  TYR   A CA   1 
ATOM   3698 C  CA   B TYR   A 1 161 ? 6.423  -5.872  3.646   0.38 15.58 ?  161  TYR   A CA   1 
ATOM   3699 C  C    A TYR   A 1 161 ? 5.295  -6.707  3.626   0.62 18.03 ?  161  TYR   A C    1 
ATOM   3700 C  C    B TYR   A 1 161 ? 5.256  -6.850  3.653   0.38 16.18 ?  161  TYR   A C    1 
ATOM   3701 O  O    A TYR   A 1 161 ? 5.531  -7.917  3.553   0.62 17.71 ?  161  TYR   A O    1 
ATOM   3702 O  O    B TYR   A 1 161 ? 5.444  -8.058  3.837   0.38 16.29 ?  161  TYR   A O    1 
ATOM   3703 C  CB   A TYR   A 1 161 ? 6.498  -5.100  5.133   0.62 17.90 ?  161  TYR   A CB   1 
ATOM   3704 C  CB   B TYR   A 1 161 ? 6.499  -5.118  4.982   0.38 15.64 ?  161  TYR   A CB   1 
ATOM   3705 C  CG   A TYR   A 1 161 ? 6.406  -6.141  6.207   0.62 17.34 ?  161  TYR   A CG   1 
ATOM   3706 C  CG   B TYR   A 1 161 ? 6.368  -5.992  6.228   0.38 15.67 ?  161  TYR   A CG   1 
ATOM   3707 C  CD1  A TYR   A 1 161 ? 7.524  -6.861  6.590   0.62 17.04 ?  161  TYR   A CD1  1 
ATOM   3708 C  CD1  B TYR   A 1 161 ? 7.482  -6.593  6.808   0.38 15.77 ?  161  TYR   A CD1  1 
ATOM   3709 C  CD2  A TYR   A 1 161 ? 5.194  -6.422  6.831   0.62 17.41 ?  161  TYR   A CD2  1 
ATOM   3710 C  CD2  B TYR   A 1 161 ? 5.131  -6.188  6.843   0.38 16.09 ?  161  TYR   A CD2  1 
ATOM   3711 C  CE1  A TYR   A 1 161 ? 7.446  -7.821  7.564   0.62 16.75 ?  161  TYR   A CE1  1 
ATOM   3712 C  CE1  B TYR   A 1 161 ? 7.365  -7.386  7.948   0.38 16.46 ?  161  TYR   A CE1  1 
ATOM   3713 C  CE2  A TYR   A 1 161 ? 5.106  -7.384  7.809   0.62 17.26 ?  161  TYR   A CE2  1 
ATOM   3714 C  CE2  B TYR   A 1 161 ? 5.006  -6.978  7.986   0.38 16.51 ?  161  TYR   A CE2  1 
ATOM   3715 C  CZ   A TYR   A 1 161 ? 6.239  -8.080  8.169   0.62 17.02 ?  161  TYR   A CZ   1 
ATOM   3716 C  CZ   B TYR   A 1 161 ? 6.125  -7.572  8.533   0.38 17.11 ?  161  TYR   A CZ   1 
ATOM   3717 O  OH   A TYR   A 1 161 ? 6.170  -9.036  9.148   0.62 17.11 ?  161  TYR   A OH   1 
ATOM   3718 O  OH   B TYR   A 1 161 ? 6.008  -8.359  9.664   0.38 18.17 ?  161  TYR   A OH   1 
ATOM   3719 H  H    A TYR   A 1 161 ? 6.258  -3.837  3.097   0.62 21.97 ?  161  TYR   A H    1 
ATOM   3720 H  H    B TYR   A 1 161 ? 6.337  -4.099  2.776   0.38 18.16 ?  161  TYR   A H    1 
ATOM   3721 H  HA   A TYR   A 1 161 ? 7.254  -6.166  3.564   0.62 21.52 ?  161  TYR   A HA   1 
ATOM   3722 H  HA   B TYR   A 1 161 ? 7.239  -6.383  3.541   0.38 18.71 ?  161  TYR   A HA   1 
ATOM   3723 H  HB2  A TYR   A 1 161 ? 7.344  -4.641  5.237   0.62 21.50 ?  161  TYR   A HB2  1 
ATOM   3724 H  HB2  B TYR   A 1 161 ? 7.355  -4.668  5.031   0.38 18.78 ?  161  TYR   A HB2  1 
ATOM   3725 H  HB3  A TYR   A 1 161 ? 5.762  -4.481  5.255   0.62 21.50 ?  161  TYR   A HB3  1 
ATOM   3726 H  HB3  B TYR   A 1 161 ? 5.784  -4.464  5.007   0.38 18.78 ?  161  TYR   A HB3  1 
ATOM   3727 H  HD1  A TYR   A 1 161 ? 8.339  -6.693  6.179   0.62 20.46 ?  161  TYR   A HD1  1 
ATOM   3728 H  HD1  B TYR   A 1 161 ? 8.318  -6.472  6.424   0.38 18.94 ?  161  TYR   A HD1  1 
ATOM   3729 H  HD2  A TYR   A 1 161 ? 4.429  -5.952  6.584   0.62 20.91 ?  161  TYR   A HD2  1 
ATOM   3730 H  HD2  B TYR   A 1 161 ? 4.370  -5.793  6.486   0.38 19.32 ?  161  TYR   A HD2  1 
ATOM   3731 H  HE1  A TYR   A 1 161 ? 8.202  -8.302  7.812   0.62 20.11 ?  161  TYR   A HE1  1 
ATOM   3732 H  HE1  B TYR   A 1 161 ? 8.121  -7.784  8.324   0.38 19.77 ?  161  TYR   A HE1  1 
ATOM   3733 H  HE2  A TYR   A 1 161 ? 4.287  -7.563  8.220   0.62 20.73 ?  161  TYR   A HE2  1 
ATOM   3734 H  HE2  B TYR   A 1 161 ? 4.170  -7.104  8.385   0.38 19.82 ?  161  TYR   A HE2  1 
ATOM   3735 H  HH   A TYR   A 1 161 ? 5.374  -9.102  9.432   0.62 20.54 ?  161  TYR   A HH   1 
ATOM   3736 H  HH   B TYR   A 1 161 ? 5.205  -8.389  9.920   0.38 21.82 ?  161  TYR   A HH   1 
ATOM   3737 N  N    A ASP   A 1 162 ? 4.047  -6.228  3.612   0.62 18.90 ?  162  ASP   A N    1 
ATOM   3738 N  N    B ASP   A 1 162 ? 4.037  -6.343  3.450   0.38 17.11 ?  162  ASP   A N    1 
ATOM   3739 C  CA   A ASP   A 1 162 ? 2.903  -7.138  3.551   0.62 19.34 ?  162  ASP   A CA   1 
ATOM   3740 C  CA   B ASP   A 1 162 ? 2.865  -7.214  3.435   0.38 17.88 ?  162  ASP   A CA   1 
ATOM   3741 C  C    A ASP   A 1 162 ? 2.944  -7.990  2.289   0.62 19.57 ?  162  ASP   A C    1 
ATOM   3742 C  C    B ASP   A 1 162 ? 2.924  -8.200  2.272   0.38 17.89 ?  162  ASP   A C    1 
ATOM   3743 O  O    A ASP   A 1 162 ? 2.603  -9.178  2.320   0.62 20.11 ?  162  ASP   A O    1 
ATOM   3744 O  O    B ASP   A 1 162 ? 2.517  -9.361  2.409   0.38 18.16 ?  162  ASP   A O    1 
ATOM   3745 C  CB   A ASP   A 1 162 ? 1.585  -6.354  3.606   0.62 20.01 ?  162  ASP   A CB   1 
ATOM   3746 C  CB   B ASP   A 1 162 ? 1.583  -6.375  3.373   0.38 19.00 ?  162  ASP   A CB   1 
ATOM   3747 C  CG   A ASP   A 1 162 ? 1.253  -5.824  4.992   0.62 20.73 ?  162  ASP   A CG   1 
ATOM   3748 C  CG   B ASP   A 1 162 ? 1.352  -5.549  4.624   0.38 20.10 ?  162  ASP   A CG   1 
ATOM   3749 O  OD1  A ASP   A 1 162 ? 1.938  -6.181  5.971   0.62 21.86 ?  162  ASP   A OD1  1 
ATOM   3750 O  OD1  B ASP   A 1 162 ? 1.922  -5.876  5.683   0.38 20.69 ?  162  ASP   A OD1  1 
ATOM   3751 O  OD2  A ASP   A 1 162 ? 0.271  -5.051  5.095   0.62 20.62 -1 162  ASP   A OD2  1 
ATOM   3752 O  OD2  B ASP   A 1 162 ? 0.577  -4.571  4.546   0.38 20.47 -1 162  ASP   A OD2  1 
ATOM   3753 H  H    A ASP   A 1 162 ? 3.830  -5.400  3.631   0.62 22.70 ?  162  ASP   A H    1 
ATOM   3754 H  H    B ASP   A 1 162 ? 3.865  -5.510  3.329   0.38 20.55 ?  162  ASP   A H    1 
ATOM   3755 H  HA   A ASP   A 1 162 ? 2.921  -7.744  4.308   0.62 23.22 ?  162  ASP   A HA   1 
ATOM   3756 H  HA   B ASP   A 1 162 ? 2.840  -7.725  4.256   0.38 21.47 ?  162  ASP   A HA   1 
ATOM   3757 H  HB2  A ASP   A 1 162 ? 1.640  -5.597  3.009   0.62 24.03 ?  162  ASP   A HB2  1 
ATOM   3758 H  HB2  B ASP   A 1 162 ? 1.636  -5.750  2.637   0.38 22.82 ?  162  ASP   A HB2  1 
ATOM   3759 H  HB3  A ASP   A 1 162 ? 0.851  -6.936  3.345   0.62 24.03 ?  162  ASP   A HB3  1 
ATOM   3760 H  HB3  B ASP   A 1 162 ? 0.816  -6.957  3.265   0.38 22.82 ?  162  ASP   A HB3  1 
ATOM   3761 N  N    A LYS   A 1 163 ? 3.349  -7.399  1.164   0.62 20.25 ?  163  LYS   A N    1 
ATOM   3762 N  N    B LYS   A 1 163 ? 3.441  -7.760  1.122   0.38 18.06 ?  163  LYS   A N    1 
ATOM   3763 C  CA   A LYS   A 1 163 ? 3.464  -8.164  -0.073  0.62 20.79 ?  163  LYS   A CA   1 
ATOM   3764 C  CA   B LYS   A 1 163 ? 3.498  -8.622  -0.054  0.38 18.33 ?  163  LYS   A CA   1 
ATOM   3765 C  C    A LYS   A 1 163 ? 4.574  -9.205  0.024   0.62 19.99 ?  163  LYS   A C    1 
ATOM   3766 C  C    B LYS   A 1 163 ? 4.595  -9.676  0.079   0.38 16.87 ?  163  LYS   A C    1 
ATOM   3767 O  O    A LYS   A 1 163 ? 4.442  -10.313 -0.507  0.62 20.62 ?  163  LYS   A O    1 
ATOM   3768 O  O    B LYS   A 1 163 ? 4.397  -10.839 -0.296  0.38 16.91 ?  163  LYS   A O    1 
ATOM   3769 C  CB   A LYS   A 1 163 ? 3.717  -7.212  -1.242  0.62 22.87 ?  163  LYS   A CB   1 
ATOM   3770 C  CB   B LYS   A 1 163 ? 3.704  -7.760  -1.300  0.38 20.39 ?  163  LYS   A CB   1 
ATOM   3771 C  CG   A LYS   A 1 163 ? 3.831  -7.902  -2.587  0.62 25.29 ?  163  LYS   A CG   1 
ATOM   3772 C  CG   B LYS   A 1 163 ? 3.712  -8.526  -2.605  0.38 22.52 ?  163  LYS   A CG   1 
ATOM   3773 C  CD   A LYS   A 1 163 ? 4.220  -6.922  -3.676  0.62 27.53 ?  163  LYS   A CD   1 
ATOM   3774 C  CD   B LYS   A 1 163 ? 3.563  -7.582  -3.785  0.38 24.46 ?  163  LYS   A CD   1 
ATOM   3775 C  CE   A LYS   A 1 163 ? 4.150  -7.567  -5.049  0.62 29.46 ?  163  LYS   A CE   1 
ATOM   3776 C  CE   B LYS   A 1 163 ? 3.317  -8.349  -5.071  0.38 26.00 ?  163  LYS   A CE   1 
ATOM   3777 N  NZ   A LYS   A 1 163 ? 4.765  -6.704  -6.093  0.62 30.54 ?  163  LYS   A NZ   1 
ATOM   3778 N  NZ   B LYS   A 1 163 ? 2.022  -7.977  -5.703  0.38 26.96 ?  163  LYS   A NZ   1 
ATOM   3779 H  H    A LYS   A 1 163 ? 3.553  -6.568  1.093   0.62 24.31 ?  163  LYS   A H    1 
ATOM   3780 H  H    B LYS   A 1 163 ? 3.764  -6.972  1.001   0.38 21.69 ?  163  LYS   A H    1 
ATOM   3781 H  HA   A LYS   A 1 163 ? 2.625  -8.625  -0.243  0.62 24.96 ?  163  LYS   A HA   1 
ATOM   3782 H  HA   B LYS   A 1 163 ? 2.651  -9.082  -0.151  0.38 22.01 ?  163  LYS   A HA   1 
ATOM   3783 H  HB2  A LYS   A 1 163 ? 2.979  -6.580  -1.299  0.62 27.47 ?  163  LYS   A HB2  1 
ATOM   3784 H  HB2  B LYS   A 1 163 ? 2.984  -7.109  -1.349  0.38 24.48 ?  163  LYS   A HB2  1 
ATOM   3785 H  HB3  A LYS   A 1 163 ? 4.544  -6.734  -1.084  0.62 27.47 ?  163  LYS   A HB3  1 
ATOM   3786 H  HB3  B LYS   A 1 163 ? 4.553  -7.300  -1.224  0.38 24.48 ?  163  LYS   A HB3  1 
ATOM   3787 H  HG2  A LYS   A 1 163 ? 4.513  -8.589  -2.543  0.62 30.36 ?  163  LYS   A HG2  1 
ATOM   3788 H  HG2  B LYS   A 1 163 ? 4.556  -8.997  -2.697  0.38 27.04 ?  163  LYS   A HG2  1 
ATOM   3789 H  HG3  A LYS   A 1 163 ? 2.974  -8.294  -2.820  0.62 30.36 ?  163  LYS   A HG3  1 
ATOM   3790 H  HG3  B LYS   A 1 163 ? 2.972  -9.151  -2.618  0.38 27.04 ?  163  LYS   A HG3  1 
ATOM   3791 H  HD2  A LYS   A 1 163 ? 3.610  -6.168  -3.662  0.62 33.05 ?  163  LYS   A HD2  1 
ATOM   3792 H  HD2  B LYS   A 1 163 ? 2.807  -6.991  -3.631  0.38 29.37 ?  163  LYS   A HD2  1 
ATOM   3793 H  HD3  A LYS   A 1 163 ? 5.130  -6.621  -3.525  0.62 33.05 ?  163  LYS   A HD3  1 
ATOM   3794 H  HD3  B LYS   A 1 163 ? 4.377  -7.063  -3.888  0.38 29.37 ?  163  LYS   A HD3  1 
ATOM   3795 H  HE2  A LYS   A 1 163 ? 4.617  -8.416  -5.030  0.62 35.37 ?  163  LYS   A HE2  1 
ATOM   3796 H  HE2  B LYS   A 1 163 ? 4.029  -8.153  -5.698  0.38 31.21 ?  163  LYS   A HE2  1 
ATOM   3797 H  HE3  A LYS   A 1 163 ? 3.220  -7.707  -5.284  0.62 35.37 ?  163  LYS   A HE3  1 
ATOM   3798 H  HE3  B LYS   A 1 163 ? 3.296  -9.299  -4.874  0.38 31.21 ?  163  LYS   A HE3  1 
ATOM   3799 H  HZ1  A LYS   A 1 163 ? 4.712  -7.103  -6.887  0.62 36.67 ?  163  LYS   A HZ1  1 
ATOM   3800 H  HZ1  B LYS   A 1 163 ? 1.905  -8.443  -6.452  0.38 32.37 ?  163  LYS   A HZ1  1 
ATOM   3801 H  HZ2  A LYS   A 1 163 ? 4.338  -5.924  -6.132  0.62 36.67 ?  163  LYS   A HZ2  1 
ATOM   3802 H  HZ2  B LYS   A 1 163 ? 1.350  -8.151  -5.146  0.38 32.37 ?  163  LYS   A HZ2  1 
ATOM   3803 H  HZ3  A LYS   A 1 163 ? 5.621  -6.555  -5.900  0.62 36.67 ?  163  LYS   A HZ3  1 
ATOM   3804 H  HZ3  B LYS   A 1 163 ? 2.018  -7.109  -5.899  0.38 32.37 ?  163  LYS   A HZ3  1 
ATOM   3805 N  N    A LEU   A 1 164 ? 5.681  -8.862  0.688   0.62 18.65 ?  164  LEU   A N    1 
ATOM   3806 N  N    B LEU   A 1 164 ? 5.756  -9.288  0.614   0.38 16.21 ?  164  LEU   A N    1 
ATOM   3807 C  CA   A LEU   A 1 164 ? 6.783  -9.809  0.840   0.62 17.88 ?  164  LEU   A CA   1 
ATOM   3808 C  CA   B LEU   A 1 164 ? 6.842  -10.242 0.818   0.38 15.61 ?  164  LEU   A CA   1 
ATOM   3809 C  C    A LEU   A 1 164 ? 6.350  -11.023 1.648   0.62 18.10 ?  164  LEU   A C    1 
ATOM   3810 C  C    B LEU   A 1 164 ? 6.419  -11.362 1.760   0.38 15.15 ?  164  LEU   A C    1 
ATOM   3811 O  O    A LEU   A 1 164 ? 6.647  -12.167 1.287   0.62 18.66 ?  164  LEU   A O    1 
ATOM   3812 O  O    B LEU   A 1 164 ? 6.779  -12.528 1.558   0.38 14.89 ?  164  LEU   A O    1 
ATOM   3813 C  CB   A LEU   A 1 164 ? 7.966  -9.117  1.518   0.62 17.52 ?  164  LEU   A CB   1 
ATOM   3814 C  CB   B LEU   A 1 164 ? 8.067  -9.524  1.387   0.38 15.48 ?  164  LEU   A CB   1 
ATOM   3815 C  CG   A LEU   A 1 164 ? 8.724  -8.099  0.663   0.62 17.96 ?  164  LEU   A CG   1 
ATOM   3816 C  CG   B LEU   A 1 164 ? 8.784  -8.493  0.515   0.38 15.45 ?  164  LEU   A CG   1 
ATOM   3817 C  CD1  A LEU   A 1 164 ? 9.652  -7.245  1.516   0.62 17.66 ?  164  LEU   A CD1  1 
ATOM   3818 C  CD1  B LEU   A 1 164 ? 9.731  -7.655  1.358   0.38 15.47 ?  164  LEU   A CD1  1 
ATOM   3819 C  CD2  A LEU   A 1 164 ? 9.503  -8.811  -0.429  0.62 18.48 ?  164  LEU   A CD2  1 
ATOM   3820 C  CD2  B LEU   A 1 164 ? 9.537  -9.190  -0.591  0.38 15.62 ?  164  LEU   A CD2  1 
ATOM   3821 H  H    A LEU   A 1 164 ? 5.813  -8.094  1.052   0.62 22.40 ?  164  LEU   A H    1 
ATOM   3822 H  H    B LEU   A 1 164 ? 5.935  -8.492  0.872   0.38 19.46 ?  164  LEU   A H    1 
ATOM   3823 H  HA   A LEU   A 1 164 ? 7.061  -10.114 -0.034  0.62 21.47 ?  164  LEU   A HA   1 
ATOM   3824 H  HA   B LEU   A 1 164 ? 7.087  -10.645 -0.030  0.38 18.75 ?  164  LEU   A HA   1 
ATOM   3825 H  HB2  A LEU   A 1 164 ? 7.635  -8.653  2.303   0.62 21.04 ?  164  LEU   A HB2  1 
ATOM   3826 H  HB2  B LEU   A 1 164 ? 7.791  -9.068  2.193   0.38 18.60 ?  164  LEU   A HB2  1 
ATOM   3827 H  HB3  A LEU   A 1 164 ? 8.598  -9.800  1.789   0.62 21.04 ?  164  LEU   A HB3  1 
ATOM   3828 H  HB3  B LEU   A 1 164 ? 8.723  -10.201 1.616   0.38 18.60 ?  164  LEU   A HB3  1 
ATOM   3829 H  HG   A LEU   A 1 164 ? 8.081  -7.509  0.239   0.62 21.57 ?  164  LEU   A HG   1 
ATOM   3830 H  HG   B LEU   A 1 164 ? 8.128  -7.900  0.115   0.38 18.55 ?  164  LEU   A HG   1 
ATOM   3831 H  HD11 A LEU   A 1 164 ? 10.112 -6.612  0.944   0.62 21.21 ?  164  LEU   A HD11 1 
ATOM   3832 H  HD11 B LEU   A 1 164 ? 10.175 -7.010  0.788   0.38 18.58 ?  164  LEU   A HD11 1 
ATOM   3833 H  HD12 A LEU   A 1 164 ? 9.124  -6.768  2.179   0.62 21.21 ?  164  LEU   A HD12 1 
ATOM   3834 H  HD12 B LEU   A 1 164 ? 9.223  -7.197  2.046   0.38 18.58 ?  164  LEU   A HD12 1 
ATOM   3835 H  HD13 A LEU   A 1 164 ? 10.294 -7.821  1.959   0.62 21.21 ?  164  LEU   A HD13 1 
ATOM   3836 H  HD13 B LEU   A 1 164 ? 10.388 -8.241  1.770   0.38 18.58 ?  164  LEU   A HD13 1 
ATOM   3837 H  HD21 A LEU   A 1 164 ? 10.048 -8.161  -0.899  0.62 22.19 ?  164  LEU   A HD21 1 
ATOM   3838 H  HD21 B LEU   A 1 164 ? 9.987  -8.524  -1.133  0.38 18.76 ?  164  LEU   A HD21 1 
ATOM   3839 H  HD22 A LEU   A 1 164 ? 10.067 -9.488  -0.026  0.62 22.19 ?  164  LEU   A HD22 1 
ATOM   3840 H  HD22 B LEU   A 1 164 ? 10.186 -9.793  -0.198  0.38 18.76 ?  164  LEU   A HD22 1 
ATOM   3841 H  HD23 A LEU   A 1 164 ? 8.878  -9.225  -1.046  0.62 22.19 ?  164  LEU   A HD23 1 
ATOM   3842 H  HD23 B LEU   A 1 164 ? 8.907  -9.689  -1.133  0.38 18.76 ?  164  LEU   A HD23 1 
ATOM   3843 N  N    A VAL   A 1 165 ? 5.649  -10.787 2.755   0.62 17.93 ?  165  VAL   A N    1 
ATOM   3844 N  N    B VAL   A 1 165 ? 5.668  -11.022 2.809   0.38 15.57 ?  165  VAL   A N    1 
ATOM   3845 C  CA   A VAL   A 1 165 ? 5.184  -11.880 3.602   0.62 17.68 ?  165  VAL   A CA   1 
ATOM   3846 C  CA   B VAL   A 1 165 ? 5.189  -12.031 3.750   0.38 15.30 ?  165  VAL   A CA   1 
ATOM   3847 C  C    A VAL   A 1 165 ? 4.121  -12.700 2.884   0.62 17.49 ?  165  VAL   A C    1 
ATOM   3848 C  C    B VAL   A 1 165 ? 4.182  -12.955 3.073   0.38 14.81 ?  165  VAL   A C    1 
ATOM   3849 O  O    A VAL   A 1 165 ? 4.217  -13.929 2.792   0.62 17.35 ?  165  VAL   A O    1 
ATOM   3850 O  O    B VAL   A 1 165 ? 4.254  -14.184 3.200   0.38 14.56 ?  165  VAL   A O    1 
ATOM   3851 C  CB   A VAL   A 1 165 ? 4.663  -11.317 4.937   0.62 18.23 ?  165  VAL   A CB   1 
ATOM   3852 C  CB   B VAL   A 1 165 ? 4.592  -11.347 4.996   0.38 15.78 ?  165  VAL   A CB   1 
ATOM   3853 C  CG1  A VAL   A 1 165 ? 3.888  -12.381 5.706   0.62 18.62 ?  165  VAL   A CG1  1 
ATOM   3854 C  CG1  B VAL   A 1 165 ? 3.931  -12.366 5.916   0.38 16.21 ?  165  VAL   A CG1  1 
ATOM   3855 C  CG2  A VAL   A 1 165 ? 5.815  -10.760 5.758   0.62 18.50 ?  165  VAL   A CG2  1 
ATOM   3856 C  CG2  B VAL   A 1 165 ? 5.661  -10.566 5.749   0.38 15.98 ?  165  VAL   A CG2  1 
ATOM   3857 H  H    A VAL   A 1 165 ? 5.423  -10.013 3.038   0.62 21.54 ?  165  VAL   A H    1 
ATOM   3858 H  H    B VAL   A 1 165 ? 5.426  -10.222 2.998   0.38 18.70 ?  165  VAL   A H    1 
ATOM   3859 H  HA   A VAL   A 1 165 ? 5.925  -12.474 3.798   0.62 21.23 ?  165  VAL   A HA   1 
ATOM   3860 H  HA   B VAL   A 1 165 ? 5.936  -12.572 4.046   0.38 18.37 ?  165  VAL   A HA   1 
ATOM   3861 H  HB   A VAL   A 1 165 ? 4.051  -10.591 4.748   0.62 21.89 ?  165  VAL   A HB   1 
ATOM   3862 H  HB   B VAL   A 1 165 ? 3.908  -10.718 4.716   0.38 18.95 ?  165  VAL   A HB   1 
ATOM   3863 H  HG11 A VAL   A 1 165 ? 3.807  -12.101 6.631   0.62 22.36 ?  165  VAL   A HG11 1 
ATOM   3864 H  HG11 B VAL   A 1 165 ? 3.779  -11.954 6.783   0.38 19.46 ?  165  VAL   A HG11 1 
ATOM   3865 H  HG12 A VAL   A 1 165 ? 3.002  -12.477 5.315   0.62 22.36 ?  165  VAL   A HG12 1 
ATOM   3866 H  HG12 B VAL   A 1 165 ? 3.084  -12.639 5.531   0.38 19.46 ?  165  VAL   A HG12 1 
ATOM   3867 H  HG13 A VAL   A 1 165 ? 4.365  -13.222 5.656   0.62 22.36 ?  165  VAL   A HG13 1 
ATOM   3868 H  HG13 B VAL   A 1 165 ? 4.517  -13.130 6.013   0.38 19.46 ?  165  VAL   A HG13 1 
ATOM   3869 H  HG21 A VAL   A 1 165 ? 5.470  -10.422 6.599   0.62 22.21 ?  165  VAL   A HG21 1 
ATOM   3870 H  HG21 B VAL   A 1 165 ? 5.240  -10.057 6.462   0.38 19.19 ?  165  VAL   A HG21 1 
ATOM   3871 H  HG22 A VAL   A 1 165 ? 6.458  -11.466 5.922   0.62 22.21 ?  165  VAL   A HG22 1 
ATOM   3872 H  HG22 B VAL   A 1 165 ? 6.303  -11.188 6.124   0.38 19.19 ?  165  VAL   A HG22 1 
ATOM   3873 H  HG23 A VAL   A 1 165 ? 6.234  -10.039 5.259   0.62 22.21 ?  165  VAL   A HG23 1 
ATOM   3874 H  HG23 B VAL   A 1 165 ? 6.105  -9.962  5.133   0.38 19.19 ?  165  VAL   A HG23 1 
ATOM   3875 N  N    A SER   A 1 166 ? 3.086  -12.034 2.367   0.62 18.16 ?  166  SER   A N    1 
ATOM   3876 N  N    B SER   A 1 166 ? 3.237  -12.376 2.329   0.38 15.10 ?  166  SER   A N    1 
ATOM   3877 C  CA   A SER   A 1 166 ? 1.957  -12.754 1.790   0.62 19.62 ?  166  SER   A CA   1 
ATOM   3878 C  CA   B SER   A 1 166 ? 2.108  -13.148 1.821   0.38 15.35 ?  166  SER   A CA   1 
ATOM   3879 C  C    A SER   A 1 166 ? 2.358  -13.561 0.567   0.62 19.85 ?  166  SER   A C    1 
ATOM   3880 C  C    B SER   A 1 166 ? 2.530  -14.123 0.728   0.38 15.31 ?  166  SER   A C    1 
ATOM   3881 O  O    A SER   A 1 166 ? 1.665  -14.527 0.223   0.62 20.55 ?  166  SER   A O    1 
ATOM   3882 O  O    B SER   A 1 166 ? 1.983  -15.228 0.637   0.38 15.45 ?  166  SER   A O    1 
ATOM   3883 C  CB   A SER   A 1 166 ? 0.839  -11.778 1.414   0.62 21.47 ?  166  SER   A CB   1 
ATOM   3884 C  CB   B SER   A 1 166 ? 1.026  -12.197 1.307   0.38 16.12 ?  166  SER   A CB   1 
ATOM   3885 O  OG   A SER   A 1 166 ? 0.417  -11.031 2.540   0.62 23.44 ?  166  SER   A OG   1 
ATOM   3886 O  OG   B SER   A 1 166 ? 0.021  -12.891 0.594   0.38 17.42 ?  166  SER   A OG   1 
ATOM   3887 H  H    A SER   A 1 166 ? 3.013  -11.184 2.336   0.62 21.81 ?  166  SER   A H    1 
ATOM   3888 H  H    B SER   A 1 166 ? 3.223  -11.553 2.112   0.38 18.14 ?  166  SER   A H    1 
ATOM   3889 H  HA   A SER   A 1 166 ? 1.594  -13.371 2.447   0.62 23.56 ?  166  SER   A HA   1 
ATOM   3890 H  HA   B SER   A 1 166 ? 1.722  -13.670 2.543   0.38 18.43 ?  166  SER   A HA   1 
ATOM   3891 H  HB2  A SER   A 1 166 ? 1.165  -11.170 0.733   0.62 25.77 ?  166  SER   A HB2  1 
ATOM   3892 H  HB2  B SER   A 1 166 ? 0.626  -11.740 2.065   0.38 19.36 ?  166  SER   A HB2  1 
ATOM   3893 H  HB3  A SER   A 1 166 ? 0.077  -12.277 1.072   0.62 25.77 ?  166  SER   A HB3  1 
ATOM   3894 H  HB3  B SER   A 1 166 ? 1.431  -11.553 0.710   0.38 19.36 ?  166  SER   A HB3  1 
ATOM   3895 H  HG   A SER   A 1 166 ? 1.064  -10.582 2.842   0.62 28.15 ?  166  SER   A HG   1 
ATOM   3896 H  HG   B SER   A 1 166 ? -0.573 -12.352 0.338   0.38 20.92 ?  166  SER   A HG   1 
ATOM   3897 N  N    A SER   A 1 167 ? 3.450  -13.188 -0.097  0.62 19.75 ?  167  SER   A N    1 
ATOM   3898 N  N    B SER   A 1 167 ? 3.487  -13.737 -0.112  0.38 15.85 ?  167  SER   A N    1 
ATOM   3899 C  CA   A SER   A 1 167 ? 3.916  -13.894 -1.280  0.62 20.17 ?  167  SER   A CA   1 
ATOM   3900 C  CA   B SER   A 1 167 ? 3.909  -14.559 -1.237  0.38 16.41 ?  167  SER   A CA   1 
ATOM   3901 C  C    A SER   A 1 167 ? 5.087  -14.826 -1.001  0.62 20.41 ?  167  SER   A C    1 
ATOM   3902 C  C    B SER   A 1 167 ? 5.049  -15.504 -0.882  0.38 16.71 ?  167  SER   A C    1 
ATOM   3903 O  O    A SER   A 1 167 ? 5.594  -15.447 -1.939  0.62 21.02 ?  167  SER   A O    1 
ATOM   3904 O  O    B SER   A 1 167 ? 5.581  -16.175 -1.771  0.38 16.82 ?  167  SER   A O    1 
ATOM   3905 C  CB   A SER   A 1 167 ? 4.309  -12.894 -2.376  0.62 20.45 ?  167  SER   A CB   1 
ATOM   3906 C  CB   B SER   A 1 167 ? 4.312  -13.674 -2.421  0.38 16.90 ?  167  SER   A CB   1 
ATOM   3907 O  OG   A SER   A 1 167 ? 5.383  -12.068 -1.955  0.62 20.56 ?  167  SER   A OG   1 
ATOM   3908 O  OG   B SER   A 1 167 ? 5.484  -12.927 -2.140  0.38 16.93 ?  167  SER   A OG   1 
ATOM   3909 H  H    A SER   A 1 167 ? 3.931  -12.510 0.121   0.62 23.72 ?  167  SER   A H    1 
ATOM   3910 H  H    B SER   A 1 167 ? 3.910  -12.992 -0.047  0.38 19.04 ?  167  SER   A H    1 
ATOM   3911 H  HA   A SER   A 1 167 ? 3.191  -14.432 -1.626  0.62 24.23 ?  167  SER   A HA   1 
ATOM   3912 H  HA   B SER   A 1 167 ? 3.157  -15.099 -1.524  0.38 19.71 ?  167  SER   A HA   1 
ATOM   3913 H  HB2  A SER   A 1 167 ? 4.584  -13.388 -3.166  0.62 24.56 ?  167  SER   A HB2  1 
ATOM   3914 H  HB2  B SER   A 1 167 ? 4.477  -14.237 -3.193  0.38 20.30 ?  167  SER   A HB2  1 
ATOM   3915 H  HB3  A SER   A 1 167 ? 3.541  -12.339 -2.587  0.62 24.56 ?  167  SER   A HB3  1 
ATOM   3916 H  HB3  B SER   A 1 167 ? 3.589  -13.056 -2.613  0.38 20.30 ?  167  SER   A HB3  1 
ATOM   3917 H  HG   A SER   A 1 167 ? 5.165  -11.656 -1.255  0.62 24.69 ?  167  SER   A HG   1 
ATOM   3918 H  HG   B SER   A 1 167 ? 5.360  -12.433 -1.474  0.38 20.33 ?  167  SER   A HG   1 
ATOM   3919 N  N    A PHE   A 1 168 ? 5.528  -14.948 0.251   0.62 20.37 ?  168  PHE   A N    1 
ATOM   3920 N  N    B PHE   A 1 168 ? 5.418  -15.587 0.390   0.38 17.49 ?  168  PHE   A N    1 
ATOM   3921 C  CA   A PHE   A 1 168 ? 6.719  -15.744 0.530   0.62 20.82 ?  168  PHE   A CA   1 
ATOM   3922 C  CA   B PHE   A 1 168 ? 6.594  -16.343 0.781   0.38 19.02 ?  168  PHE   A CA   1 
ATOM   3923 C  C    A PHE   A 1 168 ? 6.421  -17.233 0.413   0.62 23.71 ?  168  PHE   A C    1 
ATOM   3924 C  C    B PHE   A 1 168 ? 6.292  -17.836 0.825   0.38 23.30 ?  168  PHE   A C    1 
ATOM   3925 O  O    A PHE   A 1 168 ? 5.470  -17.744 1.017   0.62 24.57 ?  168  PHE   A O    1 
ATOM   3926 O  O    B PHE   A 1 168 ? 5.142  -18.264 0.946   0.38 23.85 ?  168  PHE   A O    1 
ATOM   3927 C  CB   A PHE   A 1 168 ? 7.280  -15.452 1.921   0.62 19.23 ?  168  PHE   A CB   1 
ATOM   3928 C  CB   B PHE   A 1 168 ? 7.079  -15.893 2.157   0.38 18.05 ?  168  PHE   A CB   1 
ATOM   3929 C  CG   A PHE   A 1 168 ? 8.532  -16.237 2.230   0.62 17.96 ?  168  PHE   A CG   1 
ATOM   3930 C  CG   B PHE   A 1 168 ? 8.447  -16.392 2.504   0.38 17.42 ?  168  PHE   A CG   1 
ATOM   3931 C  CD1  A PHE   A 1 168 ? 9.718  -15.939 1.583   0.62 17.53 ?  168  PHE   A CD1  1 
ATOM   3932 C  CD1  B PHE   A 1 168 ? 9.566  -15.812 1.937   0.38 17.10 ?  168  PHE   A CD1  1 
ATOM   3933 C  CD2  A PHE   A 1 168 ? 8.521  -17.286 3.138   0.62 17.30 ?  168  PHE   A CD2  1 
ATOM   3934 C  CD2  B PHE   A 1 168 ? 8.618  -17.443 3.390   0.38 17.16 ?  168  PHE   A CD2  1 
ATOM   3935 C  CE1  A PHE   A 1 168 ? 10.871 -16.654 1.843   0.62 16.91 ?  168  PHE   A CE1  1 
ATOM   3936 C  CE1  B PHE   A 1 168 ? 10.831 -16.266 2.247   0.38 17.03 ?  168  PHE   A CE1  1 
ATOM   3937 C  CE2  A PHE   A 1 168 ? 9.682  -18.006 3.404   0.62 17.22 ?  168  PHE   A CE2  1 
ATOM   3938 C  CE2  B PHE   A 1 168 ? 9.883  -17.902 3.705   0.38 16.97 ?  168  PHE   A CE2  1 
ATOM   3939 C  CZ   A PHE   A 1 168 ? 10.854 -17.685 2.754   0.62 17.00 ?  168  PHE   A CZ   1 
ATOM   3940 C  CZ   B PHE   A 1 168 ? 10.989 -17.312 3.132   0.38 16.81 ?  168  PHE   A CZ   1 
ATOM   3941 H  H    A PHE   A 1 168 ? 5.169  -14.582 0.942   0.62 24.46 ?  168  PHE   A H    1 
ATOM   3942 H  H    B PHE   A 1 168 ? 5.008  -15.209 1.043   0.38 21.00 ?  168  PHE   A H    1 
ATOM   3943 H  HA   A PHE   A 1 168 ? 7.407  -15.519 -0.121  0.62 25.00 ?  168  PHE   A HA   1 
ATOM   3944 H  HA   B PHE   A 1 168 ? 7.302  -16.191 0.137   0.38 22.83 ?  168  PHE   A HA   1 
ATOM   3945 H  HB2  A PHE   A 1 168 ? 7.497  -14.507 1.984   0.62 23.10 ?  168  PHE   A HB2  1 
ATOM   3946 H  HB2  B PHE   A 1 168 ? 7.101  -14.925 2.178   0.38 21.68 ?  168  PHE   A HB2  1 
ATOM   3947 H  HB3  A PHE   A 1 168 ? 6.612  -15.682 2.584   0.62 23.10 ?  168  PHE   A HB3  1 
ATOM   3948 H  HB3  B PHE   A 1 168 ? 6.462  -16.224 2.829   0.38 21.68 ?  168  PHE   A HB3  1 
ATOM   3949 H  HD1  A PHE   A 1 168 ? 9.743  -15.242 0.968   0.62 21.06 ?  168  PHE   A HD1  1 
ATOM   3950 H  HD1  B PHE   A 1 168 ? 9.466  -15.106 1.338   0.38 20.54 ?  168  PHE   A HD1  1 
ATOM   3951 H  HD2  A PHE   A 1 168 ? 7.733  -17.505 3.580   0.62 20.77 ?  168  PHE   A HD2  1 
ATOM   3952 H  HD2  B PHE   A 1 168 ? 7.872  -17.844 3.777   0.38 20.61 ?  168  PHE   A HD2  1 
ATOM   3953 H  HE1  A PHE   A 1 168 ? 11.663 -16.436 1.403   0.62 20.30 ?  168  PHE   A HE1  1 
ATOM   3954 H  HE1  B PHE   A 1 168 ? 11.578 -15.867 1.861   0.38 20.45 ?  168  PHE   A HE1  1 
ATOM   3955 H  HE2  A PHE   A 1 168 ? 9.666  -18.707 4.018   0.62 20.68 ?  168  PHE   A HE2  1 
ATOM   3956 H  HE2  B PHE   A 1 168 ? 9.986  -18.607 4.302   0.38 20.38 ?  168  PHE   A HE2  1 
ATOM   3957 H  HZ   A PHE   A 1 168 ? 11.632 -18.168 2.927   0.62 20.42 ?  168  PHE   A HZ   1 
ATOM   3958 H  HZ   B PHE   A 1 168 ? 11.840 -17.618 3.343   0.38 20.19 ?  168  PHE   A HZ   1 
ATOM   3959 N  N    A LEU   A 1 169 ? 7.260  -17.932 -0.347  0.62 27.22 ?  169  LEU   A N    1 
ATOM   3960 N  N    B LEU   A 1 169 ? 7.348  -18.636 0.733   0.38 27.07 ?  169  LEU   A N    1 
ATOM   3961 C  CA   A LEU   A 1 169 ? 7.122  -19.366 -0.507  0.62 31.66 ?  169  LEU   A CA   1 
ATOM   3962 C  CA   B LEU   A 1 169 ? 7.205  -20.081 0.848   0.38 30.25 ?  169  LEU   A CA   1 
ATOM   3963 C  C    A LEU   A 1 169 ? 8.059  -20.065 0.468   0.62 34.05 ?  169  LEU   A C    1 
ATOM   3964 C  C    B LEU   A 1 169 ? 8.494  -20.731 1.345   0.38 31.99 ?  169  LEU   A C    1 
ATOM   3965 O  O    A LEU   A 1 169 ? 7.658  -20.441 1.570   0.62 34.88 ?  169  LEU   A O    1 
ATOM   3966 O  O    B LEU   A 1 169 ? 8.467  -21.673 2.139   0.38 32.74 ?  169  LEU   A O    1 
ATOM   3967 C  CB   A LEU   A 1 169 ? 7.443  -19.780 -1.945  0.62 33.05 ?  169  LEU   A CB   1 
ATOM   3968 C  CB   B LEU   A 1 169 ? 6.796  -20.684 -0.497  0.38 31.21 ?  169  LEU   A CB   1 
ATOM   3969 C  CG   A LEU   A 1 169 ? 7.086  -21.221 -2.319  0.62 34.18 ?  169  LEU   A CG   1 
ATOM   3970 C  CG   B LEU   A 1 169 ? 5.650  -21.697 -0.435  0.38 31.72 ?  169  LEU   A CG   1 
ATOM   3971 C  CD1  A LEU   A 1 169 ? 5.651  -21.532 -1.926  0.62 34.75 ?  169  LEU   A CD1  1 
ATOM   3972 C  CD1  B LEU   A 1 169 ? 4.578  -21.352 -1.458  0.38 31.97 ?  169  LEU   A CD1  1 
ATOM   3973 C  CD2  A LEU   A 1 169 ? 7.293  -21.449 -3.808  0.62 34.34 ?  169  LEU   A CD2  1 
ATOM   3974 C  CD2  B LEU   A 1 169 ? 6.174  -23.104 -0.654  0.38 31.86 ?  169  LEU   A CD2  1 
ATOM   3975 O  OXT  A LEU   A 1 169 ? 9.241  -20.252 0.182   0.62 34.60 -1 169  LEU   A OXT  1 
ATOM   3976 O  OXT  B LEU   A 1 169 ? 9.593  -20.329 0.969   0.38 32.08 -1 169  LEU   A OXT  1 
ATOM   3977 H  H    A LEU   A 1 169 ? 7.925  -17.593 -0.781  0.62 32.68 ?  169  LEU   A H    1 
ATOM   3978 H  H    B LEU   A 1 169 ? 8.152  -18.367 0.611   0.38 32.50 ?  169  LEU   A H    1 
ATOM   3979 H  HA   A LEU   A 1 169 ? 6.208  -19.616 -0.304  0.62 38.00 ?  169  LEU   A HA   1 
ATOM   3980 H  HA   B LEU   A 1 169 ? 6.502  -20.264 1.487   0.38 36.32 ?  169  LEU   A HA   1 
ATOM   3981 H  HB2  A LEU   A 1 169 ? 6.957  -19.197 -2.547  0.62 39.67 ?  169  LEU   A HB2  1 
ATOM   3982 H  HB2  B LEU   A 1 169 ? 6.521  -19.968 -1.088  0.38 37.47 ?  169  LEU   A HB2  1 
ATOM   3983 H  HB3  A LEU   A 1 169 ? 8.396  -19.673 -2.089  0.62 39.67 ?  169  LEU   A HB3  1 
ATOM   3984 H  HB3  B LEU   A 1 169 ? 7.568  -21.137 -0.873  0.38 37.47 ?  169  LEU   A HB3  1 
ATOM   3985 H  HG   A LEU   A 1 169 ? 7.670  -21.830 -1.838  0.62 41.03 ?  169  LEU   A HG   1 
ATOM   3986 H  HG   B LEU   A 1 169 ? 5.241  -21.665 0.443   0.38 38.08 ?  169  LEU   A HG   1 
ATOM   3987 H  HD11 A LEU   A 1 169 ? 5.362  -22.327 -2.396  0.62 41.71 ?  169  LEU   A HD11 1 
ATOM   3988 H  HD11 B LEU   A 1 169 ? 3.865  -22.008 -1.399  0.38 38.38 ?  169  LEU   A HD11 1 
ATOM   3989 H  HD12 A LEU   A 1 169 ? 5.611  -21.679 -0.968  0.62 41.71 ?  169  LEU   A HD12 1 
ATOM   3990 H  HD12 B LEU   A 1 169 ? 4.229  -20.467 -1.264  0.38 38.38 ?  169  LEU   A HD12 1 
ATOM   3991 H  HD13 A LEU   A 1 169 ? 5.089  -20.779 -2.171  0.62 41.71 ?  169  LEU   A HD13 1 
ATOM   3992 H  HD13 B LEU   A 1 169 ? 4.970  -21.367 -2.344  0.38 38.38 ?  169  LEU   A HD13 1 
ATOM   3993 H  HD21 A LEU   A 1 169 ? 7.070  -22.369 -4.021  0.62 41.22 ?  169  LEU   A HD21 1 
ATOM   3994 H  HD21 B LEU   A 1 169 ? 5.551  -23.735 -0.264  0.38 38.25 ?  169  LEU   A HD21 1 
ATOM   3995 H  HD22 A LEU   A 1 169 ? 6.714  -20.847 -4.302  0.62 41.22 ?  169  LEU   A HD22 1 
ATOM   3996 H  HD22 B LEU   A 1 169 ? 6.259  -23.265 -1.607  0.38 38.25 ?  169  LEU   A HD22 1 
ATOM   3997 H  HD23 A LEU   A 1 169 ? 8.220  -21.273 -4.030  0.62 41.22 ?  169  LEU   A HD23 1 
ATOM   3998 H  HD23 B LEU   A 1 169 ? 7.037  -23.190 -0.222  0.38 38.25 ?  169  LEU   A HD23 1 
ATOM   3999 N  N    A SER   B 1 1   ? 50.838 -9.224  -23.735 0.62 30.13 ?  1    SER   B N    1 
ATOM   4000 N  N    B SER   B 1 1   ? 50.845 -9.291  -23.796 0.38 24.49 ?  1    SER   B N    1 
ATOM   4001 C  CA   A SER   B 1 1   ? 51.359 -10.280 -22.843 0.62 29.94 ?  1    SER   B CA   1 
ATOM   4002 C  CA   B SER   B 1 1   ? 51.316 -10.245 -22.770 0.38 24.27 ?  1    SER   B CA   1 
ATOM   4003 C  C    A SER   B 1 1   ? 50.299 -11.340 -22.581 0.62 28.52 ?  1    SER   B C    1 
ATOM   4004 C  C    B SER   B 1 1   ? 50.253 -11.298 -22.488 0.38 23.42 ?  1    SER   B C    1 
ATOM   4005 O  O    A SER   B 1 1   ? 49.104 -11.135 -22.824 0.62 28.02 ?  1    SER   B O    1 
ATOM   4006 O  O    B SER   B 1 1   ? 49.067 -11.120 -22.794 0.38 23.26 ?  1    SER   B O    1 
ATOM   4007 C  CB   A SER   B 1 1   ? 51.834 -9.685  -21.520 0.62 30.82 ?  1    SER   B CB   1 
ATOM   4008 C  CB   B SER   B 1 1   ? 51.682 -9.517  -21.480 0.38 24.57 ?  1    SER   B CB   1 
ATOM   4009 O  OG   A SER   B 1 1   ? 50.735 -9.318  -20.708 0.62 32.39 ?  1    SER   B OG   1 
ATOM   4010 O  OG   B SER   B 1 1   ? 50.682 -9.702  -20.496 0.38 25.60 ?  1    SER   B OG   1 
ATOM   4011 H  H1   A SER   B 1 1   ? 50.740 -9.557  -24.552 0.62 36.17 ?  1    SER   B H1   1 
ATOM   4012 H  H1   B SER   B 1 1   ? 51.550 -8.900  -24.169 0.38 29.41 ?  1    SER   B H1   1 
ATOM   4013 H  H2   A SER   B 1 1   ? 50.057 -8.943  -23.426 0.62 36.17 ?  1    SER   B H2   1 
ATOM   4014 H  H2   B SER   B 1 1   ? 50.384 -9.733  -24.412 0.38 29.41 ?  1    SER   B H2   1 
ATOM   4015 H  H3   A SER   B 1 1   ? 51.418 -8.552  -23.752 0.62 36.17 ?  1    SER   B H3   1 
ATOM   4016 H  H3   B SER   B 1 1   ? 50.330 -8.682  -23.410 0.38 29.41 ?  1    SER   B H3   1 
ATOM   4017 H  HA   A SER   B 1 1   ? 52.112 -10.699 -23.280 0.62 35.94 ?  1    SER   B HA   1 
ATOM   4018 H  HA   B SER   B 1 1   ? 52.107 -10.685 -23.108 0.38 29.14 ?  1    SER   B HA   1 
ATOM   4019 H  HB2  A SER   B 1 1   ? 52.369 -10.350 -21.060 0.62 37.00 ?  1    SER   B HB2  1 
ATOM   4020 H  HB2  B SER   B 1 1   ? 52.521 -9.873  -21.152 0.38 29.51 ?  1    SER   B HB2  1 
ATOM   4021 H  HB3  A SER   B 1 1   ? 52.364 -8.895  -21.700 0.62 37.00 ?  1    SER   B HB3  1 
ATOM   4022 H  HB3  B SER   B 1 1   ? 51.775 -8.569  -21.668 0.38 29.51 ?  1    SER   B HB3  1 
ATOM   4023 H  HG   A SER   B 1 1   ? 51.009 -8.898  -20.035 0.62 38.89 ?  1    SER   B HG   1 
ATOM   4024 H  HG   B SER   B 1 1   ? 50.736 -9.090  -19.922 0.38 30.74 ?  1    SER   B HG   1 
ATOM   4025 N  N    A MET   B 1 2   ? 50.758 -12.475 -22.071 0.62 27.41 ?  2    MET   B N    1 
ATOM   4026 N  N    B MET   B 1 2   ? 50.698 -12.397 -21.893 0.38 22.61 ?  2    MET   B N    1 
ATOM   4027 C  CA   A MET   B 1 2   ? 49.939 -13.668 -21.904 0.62 27.02 ?  2    MET   B CA   1 
ATOM   4028 C  CA   B MET   B 1 2   ? 49.876 -13.581 -21.682 0.38 22.39 ?  2    MET   B CA   1 
ATOM   4029 C  C    A MET   B 1 2   ? 49.696 -13.894 -20.420 0.62 24.18 ?  2    MET   B C    1 
ATOM   4030 C  C    B MET   B 1 2   ? 49.603 -13.701 -20.189 0.38 20.70 ?  2    MET   B C    1 
ATOM   4031 O  O    A MET   B 1 2   ? 50.629 -14.202 -19.673 0.62 24.15 ?  2    MET   B O    1 
ATOM   4032 O  O    B MET   B 1 2   ? 50.523 -13.948 -19.402 0.38 20.84 ?  2    MET   B O    1 
ATOM   4033 C  CB   A MET   B 1 2   ? 50.657 -14.862 -22.517 0.62 30.68 ?  2    MET   B CB   1 
ATOM   4034 C  CB   B MET   B 1 2   ? 50.630 -14.800 -22.197 0.38 24.85 ?  2    MET   B CB   1 
ATOM   4035 C  CG   A MET   B 1 2   ? 49.814 -16.121 -22.624 0.62 34.05 ?  2    MET   B CG   1 
ATOM   4036 C  CG   B MET   B 1 2   ? 49.759 -15.931 -22.726 0.38 26.66 ?  2    MET   B CG   1 
ATOM   4037 S  SD   A MET   B 1 2   ? 50.643 -17.368 -23.625 0.62 37.09 ?  2    MET   B SD   1 
ATOM   4038 S  SD   B MET   B 1 2   ? 50.676 -16.966 -23.876 0.38 28.22 ?  2    MET   B SD   1 
ATOM   4039 C  CE   A MET   B 1 2   ? 51.196 -16.330 -24.975 0.62 37.44 ?  2    MET   B CE   1 
ATOM   4040 C  CE   B MET   B 1 2   ? 51.541 -15.719 -24.801 0.38 28.81 ?  2    MET   B CE   1 
ATOM   4041 H  H    A MET   B 1 2   ? 51.572 -12.584 -21.812 0.62 32.91 ?  2    MET   B H    1 
ATOM   4042 H  H    B MET   B 1 2   ? 51.502 -12.493 -21.593 0.38 27.15 ?  2    MET   B H    1 
ATOM   4043 H  HA   A MET   B 1 2   ? 49.095 -13.555 -22.361 0.62 32.44 ?  2    MET   B HA   1 
ATOM   4044 H  HA   B MET   B 1 2   ? 49.046 -13.508 -22.177 0.38 26.88 ?  2    MET   B HA   1 
ATOM   4045 H  HB2  A MET   B 1 2   ? 50.936 -14.579 -23.395 0.62 36.83 ?  2    MET   B HB2  1 
ATOM   4046 H  HB2  B MET   B 1 2   ? 51.237 -14.481 -22.879 0.38 29.84 ?  2    MET   B HB2  1 
ATOM   4047 H  HB3  A MET   B 1 2   ? 51.433 -15.085 -21.983 0.62 36.83 ?  2    MET   B HB3  1 
ATOM   4048 H  HB3  B MET   B 1 2   ? 51.146 -15.187 -21.487 0.38 29.84 ?  2    MET   B HB3  1 
ATOM   4049 H  HG2  A MET   B 1 2   ? 49.666 -16.485 -21.734 0.62 40.88 ?  2    MET   B HG2  1 
ATOM   4050 H  HG2  B MET   B 1 2   ? 49.466 -16.489 -21.981 0.38 32.00 ?  2    MET   B HG2  1 
ATOM   4051 H  HG3  A MET   B 1 2   ? 48.966 -15.909 -23.045 0.62 40.88 ?  2    MET   B HG3  1 
ATOM   4052 H  HG3  B MET   B 1 2   ? 48.990 -15.578 -23.194 0.38 32.00 ?  2    MET   B HG3  1 
ATOM   4053 H  HE1  A MET   B 1 2   ? 51.365 -16.884 -25.737 0.62 44.95 ?  2    MET   B HE1  1 
ATOM   4054 H  HE1  B MET   B 1 2   ? 51.683 -16.067 -25.670 0.38 34.59 ?  2    MET   B HE1  1 
ATOM   4055 H  HE2  A MET   B 1 2   ? 50.496 -15.682 -25.180 0.62 44.95 ?  2    MET   B HE2  1 
ATOM   4056 H  HE2  B MET   B 1 2   ? 50.990 -14.920 -24.857 0.38 34.59 ?  2    MET   B HE2  1 
ATOM   4057 H  HE3  A MET   B 1 2   ? 52.010 -15.859 -24.714 0.62 44.95 ?  2    MET   B HE3  1 
ATOM   4058 H  HE3  B MET   B 1 2   ? 52.388 -15.518 -24.359 0.38 34.59 ?  2    MET   B HE3  1 
ATOM   4059 N  N    A VAL   B 1 3   ? 48.445 -13.744 -19.999 0.62 21.42 ?  3    VAL   B N    1 
ATOM   4060 N  N    B VAL   B 1 3   ? 48.348 -13.503 -19.798 0.38 19.20 ?  3    VAL   B N    1 
ATOM   4061 C  CA   A VAL   B 1 3   ? 48.040 -13.992 -18.624 0.62 20.29 ?  3    VAL   B CA   1 
ATOM   4062 C  CA   B VAL   B 1 3   ? 47.901 -13.746 -18.432 0.38 18.67 ?  3    VAL   B CA   1 
ATOM   4063 C  C    A VAL   B 1 3   ? 46.814 -14.892 -18.643 0.62 17.95 ?  3    VAL   B C    1 
ATOM   4064 C  C    B VAL   B 1 3   ? 46.645 -14.601 -18.469 0.38 17.42 ?  3    VAL   B C    1 
ATOM   4065 O  O    A VAL   B 1 3   ? 46.139 -15.043 -19.664 0.62 17.42 ?  3    VAL   B O    1 
ATOM   4066 O  O    B VAL   B 1 3   ? 45.807 -14.458 -19.365 0.38 17.34 ?  3    VAL   B O    1 
ATOM   4067 C  CB   A VAL   B 1 3   ? 47.734 -12.688 -17.859 0.62 22.04 ?  3    VAL   B CB   1 
ATOM   4068 C  CB   B VAL   B 1 3   ? 47.650 -12.447 -17.637 0.38 19.80 ?  3    VAL   B CB   1 
ATOM   4069 C  CG1  A VAL   B 1 3   ? 48.982 -11.818 -17.757 0.62 22.82 ?  3    VAL   B CG1  1 
ATOM   4070 C  CG1  B VAL   B 1 3   ? 48.927 -11.624 -17.538 0.38 20.36 ?  3    VAL   B CG1  1 
ATOM   4071 C  CG2  A VAL   B 1 3   ? 46.598 -11.930 -18.536 0.62 22.81 ?  3    VAL   B CG2  1 
ATOM   4072 C  CG2  B VAL   B 1 3   ? 46.521 -11.642 -18.260 0.38 20.06 ?  3    VAL   B CG2  1 
ATOM   4073 H  H    A VAL   B 1 3   ? 47.801 -13.493 -20.510 0.62 25.72 ?  3    VAL   B H    1 
ATOM   4074 H  H    B VAL   B 1 3   ? 47.730 -13.217 -20.323 0.38 23.05 ?  3    VAL   B H    1 
ATOM   4075 H  HA   A VAL   B 1 3   ? 48.762 -14.456 -18.163 0.62 24.37 ?  3    VAL   B HA   1 
ATOM   4076 H  HA   B VAL   B 1 3   ? 48.578 -14.251 -17.968 0.38 22.42 ?  3    VAL   B HA   1 
ATOM   4077 H  HB   A VAL   B 1 3   ? 47.451 -12.918 -16.960 0.62 26.46 ?  3    VAL   B HB   1 
ATOM   4078 H  HB   B VAL   B 1 3   ? 47.381 -12.687 -16.736 0.38 23.77 ?  3    VAL   B HB   1 
ATOM   4079 H  HG11 A VAL   B 1 3   ? 48.762 -11.015 -17.259 0.62 27.40 ?  3    VAL   B HG11 1 
ATOM   4080 H  HG11 B VAL   B 1 3   ? 48.744 -10.826 -17.018 0.38 24.44 ?  3    VAL   B HG11 1 
ATOM   4081 H  HG12 A VAL   B 1 3   ? 49.676 -12.315 -17.295 0.62 27.40 ?  3    VAL   B HG12 1 
ATOM   4082 H  HG12 B VAL   B 1 3   ? 49.610 -12.156 -17.101 0.38 24.44 ?  3    VAL   B HG12 1 
ATOM   4083 H  HG13 A VAL   B 1 3   ? 49.278 -11.586 -18.649 0.62 27.40 ?  3    VAL   B HG13 1 
ATOM   4084 H  HG13 B VAL   B 1 3   ? 49.214 -11.381 -18.430 0.38 24.44 ?  3    VAL   B HG13 1 
ATOM   4085 H  HG21 A VAL   B 1 3   ? 46.505 -11.064 -18.113 0.62 27.39 ?  3    VAL   B HG21 1 
ATOM   4086 H  HG21 B VAL   B 1 3   ? 46.504 -10.762 -17.858 0.38 24.09 ?  3    VAL   B HG21 1 
ATOM   4087 H  HG22 A VAL   B 1 3   ? 46.805 -11.820 -19.477 0.62 27.39 ?  3    VAL   B HG22 1 
ATOM   4088 H  HG22 B VAL   B 1 3   ? 46.674 -11.571 -19.214 0.38 24.09 ?  3    VAL   B HG22 1 
ATOM   4089 H  HG23 A VAL   B 1 3   ? 45.774 -12.436 -18.437 0.62 27.39 ?  3    VAL   B HG23 1 
ATOM   4090 H  HG23 B VAL   B 1 3   ? 45.678 -12.098 -18.094 0.38 24.09 ?  3    VAL   B HG23 1 
ATOM   4091 N  N    . ASN   B 1 4   ? 46.525 -15.491 -17.490 1.00 16.57 ?  4    ASN   B N    1 
ATOM   4092 C  CA   . ASN   B 1 4   ? 45.387 -16.399 -17.368 1.00 15.19 ?  4    ASN   B CA   1 
ATOM   4093 C  C    . ASN   B 1 4   ? 45.332 -17.370 -18.546 1.00 15.58 ?  4    ASN   B C    1 
ATOM   4094 O  O    . ASN   B 1 4   ? 44.273 -17.622 -19.115 1.00 16.06 ?  4    ASN   B O    1 
ATOM   4095 C  CB   . ASN   B 1 4   ? 44.062 -15.644 -17.206 1.00 14.60 ?  4    ASN   B CB   1 
ATOM   4096 C  CG   . ASN   B 1 4   ? 44.008 -14.829 -15.924 1.00 14.08 ?  4    ASN   B CG   1 
ATOM   4097 O  OD1  . ASN   B 1 4   ? 44.301 -15.339 -14.845 1.00 13.92 ?  4    ASN   B OD1  1 
ATOM   4098 N  ND2  . ASN   B 1 4   ? 43.659 -13.549 -16.040 1.00 15.10 ?  4    ASN   B ND2  1 
ATOM   4099 H  H    A ASN   B 1 4   ? 46.969 -15.382 -16.769 0.62 19.90 ?  4    ASN   B H    1 
ATOM   4100 H  H    B ASN   B 1 4   ? 47.118 -15.600 -16.882 0.38 19.90 ?  4    ASN   B H    1 
ATOM   4101 H  HA   . ASN   B 1 4   ? 45.515 -16.928 -16.567 1.00 18.24 ?  4    ASN   B HA   1 
ATOM   4102 H  HB2  . ASN   B 1 4   ? 43.941 -15.040 -17.953 1.00 17.53 ?  4    ASN   B HB2  1 
ATOM   4103 H  HB3  . ASN   B 1 4   ? 43.335 -16.288 -17.182 1.00 17.53 ?  4    ASN   B HB3  1 
ATOM   4104 H  HD21 . ASN   B 1 4   ? 43.619 -13.046 -15.340 1.00 18.14 ?  4    ASN   B HD21 1 
ATOM   4105 H  HD22 . ASN   B 1 4   ? 43.468 -13.219 -16.812 1.00 18.14 ?  4    ASN   B HD22 1 
ATOM   4106 N  N    . SER   B 1 5   ? 46.491 -17.906 -18.928 1.00 16.62 ?  5    SER   B N    1 
ATOM   4107 C  CA   . SER   B 1 5   ? 46.585 -18.814 -20.073 1.00 18.68 ?  5    SER   B CA   1 
ATOM   4108 C  C    . SER   B 1 5   ? 46.535 -20.254 -19.576 1.00 20.45 ?  5    SER   B C    1 
ATOM   4109 O  O    . SER   B 1 5   ? 47.511 -20.995 -19.610 1.00 23.23 ?  5    SER   B O    1 
ATOM   4110 C  CB   . SER   B 1 5   ? 47.856 -18.544 -20.873 1.00 19.86 ?  5    SER   B CB   1 
ATOM   4111 O  OG   . SER   B 1 5   ? 49.021 -18.748 -20.086 1.00 22.69 ?  5    SER   B OG   1 
ATOM   4112 H  H    . SER   B 1 5   ? 47.244 -17.764 -18.539 1.00 19.96 ?  5    SER   B H    1 
ATOM   4113 H  HA   . SER   B 1 5   ? 45.823 -18.676 -20.657 1.00 22.44 ?  5    SER   B HA   1 
ATOM   4114 H  HB2  . SER   B 1 5   ? 47.875 -19.147 -21.636 1.00 23.85 ?  5    SER   B HB2  1 
ATOM   4115 H  HB3  . SER   B 1 5   ? 47.825 -17.628 -21.179 1.00 23.85 ?  5    SER   B HB3  1 
ATOM   4116 H  HG   . SER   B 1 5   ? 49.051 -19.548 -19.832 1.00 27.24 ?  5    SER   B HG   1 
ATOM   4117 N  N    . PHE   B 1 6   ? 45.359 -20.627 -19.090 1.00 20.53 ?  6    PHE   B N    1 
ATOM   4118 C  CA   . PHE   B 1 6   ? 45.133 -21.983 -18.614 1.00 20.03 ?  6    PHE   B CA   1 
ATOM   4119 C  C    . PHE   B 1 6   ? 45.019 -22.928 -19.801 1.00 23.73 ?  6    PHE   B C    1 
ATOM   4120 O  O    . PHE   B 1 6   ? 44.359 -22.617 -20.796 1.00 25.63 ?  6    PHE   B O    1 
ATOM   4121 C  CB   . PHE   B 1 6   ? 43.848 -22.027 -17.788 1.00 18.41 ?  6    PHE   B CB   1 
ATOM   4122 C  CG   . PHE   B 1 6   ? 43.894 -21.178 -16.546 1.00 16.63 ?  6    PHE   B CG   1 
ATOM   4123 C  CD1  . PHE   B 1 6   ? 44.403 -21.688 -15.367 1.00 15.52 ?  6    PHE   B CD1  1 
ATOM   4124 C  CD2  . PHE   B 1 6   ? 43.422 -19.873 -16.559 1.00 15.96 ?  6    PHE   B CD2  1 
ATOM   4125 C  CE1  . PHE   B 1 6   ? 44.437 -20.914 -14.217 1.00 14.96 ?  6    PHE   B CE1  1 
ATOM   4126 C  CE2  . PHE   B 1 6   ? 43.456 -19.094 -15.416 1.00 16.39 ?  6    PHE   B CE2  1 
ATOM   4127 C  CZ   . PHE   B 1 6   ? 43.973 -19.608 -14.247 1.00 15.36 ?  6    PHE   B CZ   1 
ATOM   4128 H  H    . PHE   B 1 6   ? 44.668 -20.120 -19.031 1.00 24.65 ?  6    PHE   B H    1 
ATOM   4129 H  HA   . PHE   B 1 6   ? 45.870 -22.273 -18.058 1.00 24.05 ?  6    PHE   B HA   1 
ATOM   4130 H  HB2  . PHE   B 1 6   ? 43.109 -21.712 -18.335 1.00 22.11 ?  6    PHE   B HB2  1 
ATOM   4131 H  HB3  . PHE   B 1 6   ? 43.677 -22.944 -17.512 1.00 22.11 ?  6    PHE   B HB3  1 
ATOM   4132 H  HD1  . PHE   B 1 6   ? 44.724 -22.562 -15.344 1.00 18.64 ?  6    PHE   B HD1  1 
ATOM   4133 H  HD2  . PHE   B 1 6   ? 43.072 -19.523 -17.346 1.00 19.17 ?  6    PHE   B HD2  1 
ATOM   4134 H  HE1  . PHE   B 1 6   ? 44.794 -21.264 -13.430 1.00 17.96 ?  6    PHE   B HE1  1 
ATOM   4135 H  HE2  . PHE   B 1 6   ? 43.138 -18.220 -15.440 1.00 19.68 ?  6    PHE   B HE2  1 
ATOM   4136 H  HZ   . PHE   B 1 6   ? 43.999 -19.089 -13.478 1.00 18.45 ?  6    PHE   B HZ   1 
ATOM   4137 N  N    A SER   B 1 7   ? 45.680 -24.082 -19.692 0.62 24.78 ?  7    SER   B N    1 
ATOM   4138 N  N    B SER   B 1 7   ? 45.669 -24.087 -19.700 0.38 24.63 ?  7    SER   B N    1 
ATOM   4139 C  CA   A SER   B 1 7   ? 45.762 -25.050 -20.774 0.62 27.39 ?  7    SER   B CA   1 
ATOM   4140 C  CA   B SER   B 1 7   ? 45.675 -25.050 -20.791 0.38 26.32 ?  7    SER   B CA   1 
ATOM   4141 C  C    A SER   B 1 7   ? 45.704 -26.460 -20.206 0.62 26.98 ?  7    SER   B C    1 
ATOM   4142 C  C    B SER   B 1 7   ? 45.659 -26.467 -20.238 0.38 26.18 ?  7    SER   B C    1 
ATOM   4143 O  O    A SER   B 1 7   ? 46.313 -26.749 -19.172 0.62 27.94 ?  7    SER   B O    1 
ATOM   4144 O  O    B SER   B 1 7   ? 46.294 -26.755 -19.220 0.38 26.86 ?  7    SER   B O    1 
ATOM   4145 C  CB   A SER   B 1 7   ? 47.067 -24.870 -21.565 0.62 29.87 ?  7    SER   B CB   1 
ATOM   4146 C  CB   B SER   B 1 7   ? 46.906 -24.859 -21.689 0.38 27.79 ?  7    SER   B CB   1 
ATOM   4147 O  OG   A SER   B 1 7   ? 47.192 -25.845 -22.585 0.62 31.68 ?  7    SER   B OG   1 
ATOM   4148 O  OG   B SER   B 1 7   ? 46.797 -25.625 -22.876 0.38 28.84 ?  7    SER   B OG   1 
ATOM   4149 H  H    A SER   B 1 7   ? 46.105 -24.328 -18.983 0.62 29.75 ?  7    SER   B H    1 
ATOM   4150 H  H    B SER   B 1 7   ? 46.119 -24.336 -19.009 0.38 29.57 ?  7    SER   B H    1 
ATOM   4151 H  HA   A SER   B 1 7   ? 45.017 -24.933 -21.379 0.62 32.88 ?  7    SER   B HA   1 
ATOM   4152 H  HA   B SER   B 1 7   ? 44.884 -24.929 -21.333 0.38 31.59 ?  7    SER   B HA   1 
ATOM   4153 H  HB2  A SER   B 1 7   ? 47.070 -23.989 -21.973 0.62 35.86 ?  7    SER   B HB2  1 
ATOM   4154 H  HB2  B SER   B 1 7   ? 46.978 -23.922 -21.931 0.38 33.36 ?  7    SER   B HB2  1 
ATOM   4155 H  HB3  A SER   B 1 7   ? 47.821 -24.952 -20.958 0.62 35.86 ?  7    SER   B HB3  1 
ATOM   4156 H  HB3  B SER   B 1 7   ? 47.700 -25.135 -21.203 0.38 33.36 ?  7    SER   B HB3  1 
ATOM   4157 H  HG   A SER   B 1 7   ? 47.910 -25.732 -23.006 0.62 38.03 ?  7    SER   B HG   1 
ATOM   4158 H  HG   B SER   B 1 7   ? 47.482 -25.515 -23.353 0.38 34.63 ?  7    SER   B HG   1 
ATOM   4159 N  N    A GLY   B 1 8   ? 44.967 -27.333 -20.888 0.62 26.51 ?  8    GLY   B N    1 
ATOM   4160 N  N    B GLY   B 1 8   ? 44.929 -27.348 -20.920 0.38 25.79 ?  8    GLY   B N    1 
ATOM   4161 C  CA   A GLY   B 1 8   ? 44.932 -28.732 -20.520 0.62 25.76 ?  8    GLY   B CA   1 
ATOM   4162 C  CA   B GLY   B 1 8   ? 44.904 -28.747 -20.551 0.38 25.12 ?  8    GLY   B CA   1 
ATOM   4163 C  C    A GLY   B 1 8   ? 44.018 -29.069 -19.369 0.62 24.52 ?  8    GLY   B C    1 
ATOM   4164 C  C    B GLY   B 1 8   ? 43.981 -29.096 -19.410 0.38 24.09 ?  8    GLY   B C    1 
ATOM   4165 O  O    A GLY   B 1 8   ? 44.200 -30.117 -18.738 0.62 26.00 ?  8    GLY   B O    1 
ATOM   4166 O  O    B GLY   B 1 8   ? 44.122 -30.176 -18.826 0.38 24.99 ?  8    GLY   B O    1 
ATOM   4167 H  H    A GLY   B 1 8   ? 44.482 -27.132 -21.566 0.62 31.83 ?  8    GLY   B H    1 
ATOM   4168 H  H    B GLY   B 1 8   ? 44.445 -27.152 -21.602 0.38 30.96 ?  8    GLY   B H    1 
ATOM   4169 H  HA2  A GLY   B 1 8   ? 44.646 -29.251 -21.287 0.62 30.93 ?  8    GLY   B HA2  1 
ATOM   4170 H  HA2  B GLY   B 1 8   ? 44.630 -29.268 -21.321 0.38 30.16 ?  8    GLY   B HA2  1 
ATOM   4171 H  HA3  A GLY   B 1 8   ? 45.825 -29.019 -20.279 0.62 30.93 ?  8    GLY   B HA3  1 
ATOM   4172 H  HA3  B GLY   B 1 8   ? 45.798 -29.023 -20.303 0.38 30.16 ?  8    GLY   B HA3  1 
ATOM   4173 N  N    . TYR   B 1 9   ? 43.028 -28.230 -19.082 1.00 22.56 ?  9    TYR   B N    1 
ATOM   4174 C  CA   . TYR   B 1 9   ? 42.099 -28.503 -18.000 1.00 19.96 ?  9    TYR   B CA   1 
ATOM   4175 C  C    . TYR   B 1 9   ? 40.908 -29.299 -18.499 1.00 19.15 ?  9    TYR   B C    1 
ATOM   4176 O  O    . TYR   B 1 9   ? 40.467 -29.157 -19.645 1.00 21.01 ?  9    TYR   B O    1 
ATOM   4177 C  CB   . TYR   B 1 9   ? 41.605 -27.214 -17.348 1.00 19.03 ?  9    TYR   B CB   1 
ATOM   4178 C  CG   . TYR   B 1 9   ? 42.639 -26.598 -16.442 1.00 18.27 ?  9    TYR   B CG   1 
ATOM   4179 C  CD1  . TYR   B 1 9   ? 43.725 -25.920 -16.971 1.00 18.55 ?  9    TYR   B CD1  1 
ATOM   4180 C  CD2  . TYR   B 1 9   ? 42.548 -26.713 -15.061 1.00 17.29 ?  9    TYR   B CD2  1 
ATOM   4181 C  CE1  . TYR   B 1 9   ? 44.690 -25.364 -16.152 1.00 18.78 ?  9    TYR   B CE1  1 
ATOM   4182 C  CE2  . TYR   B 1 9   ? 43.508 -26.164 -14.233 1.00 17.58 ?  9    TYR   B CE2  1 
ATOM   4183 C  CZ   . TYR   B 1 9   ? 44.578 -25.484 -14.783 1.00 18.30 ?  9    TYR   B CZ   1 
ATOM   4184 O  OH   . TYR   B 1 9   ? 45.540 -24.939 -13.966 1.00 19.31 ?  9    TYR   B OH   1 
ATOM   4185 H  H    A TYR   B 1 9   ? 42.863 -27.501 -19.510 0.62 27.08 ?  9    TYR   B H    1 
ATOM   4186 H  H    B TYR   B 1 9   ? 42.887 -27.482 -19.483 0.38 27.08 ?  9    TYR   B H    1 
ATOM   4187 H  HA   . TYR   B 1 9   ? 42.541 -29.029 -17.320 1.00 23.97 ?  9    TYR   B HA   1 
ATOM   4188 H  HB2  . TYR   B 1 9   ? 41.369 -26.569 -18.035 1.00 22.85 ?  9    TYR   B HB2  1 
ATOM   4189 H  HB3  . TYR   B 1 9   ? 40.830 -27.429 -16.811 1.00 22.85 ?  9    TYR   B HB3  1 
ATOM   4190 H  HD1  . TYR   B 1 9   ? 43.802 -25.834 -17.896 1.00 22.27 ?  9    TYR   B HD1  1 
ATOM   4191 H  HD2  . TYR   B 1 9   ? 41.824 -27.174 -14.691 1.00 20.76 ?  9    TYR   B HD2  1 
ATOM   4192 H  HE1  . TYR   B 1 9   ? 45.408 -24.910 -16.525 1.00 22.55 ?  9    TYR   B HE1  1 
ATOM   4193 H  HE2  . TYR   B 1 9   ? 43.425 -26.254 -13.312 1.00 21.12 ?  9    TYR   B HE2  1 
ATOM   4194 H  HH   . TYR   B 1 9   ? 46.123 -24.565 -14.436 1.00 23.19 ?  9    TYR   B HH   1 
ATOM   4195 N  N    . LEU   B 1 10  ? 40.407 -30.162 -17.623 1.00 17.57 ?  10   LEU   B N    1 
ATOM   4196 C  CA   . LEU   B 1 10  ? 39.201 -30.929 -17.876 1.00 17.48 ?  10   LEU   B CA   1 
ATOM   4197 C  C    . LEU   B 1 10  ? 38.017 -30.164 -17.304 1.00 17.34 ?  10   LEU   B C    1 
ATOM   4198 O  O    . LEU   B 1 10  ? 38.047 -29.736 -16.146 1.00 16.71 ?  10   LEU   B O    1 
ATOM   4199 C  CB   . LEU   B 1 10  ? 39.311 -32.296 -17.200 1.00 18.34 ?  10   LEU   B CB   1 
ATOM   4200 C  CG   . LEU   B 1 10  ? 38.181 -33.276 -17.508 1.00 20.18 ?  10   LEU   B CG   1 
ATOM   4201 C  CD1  . LEU   B 1 10  ? 38.323 -33.831 -18.919 1.00 21.28 ?  10   LEU   B CD1  1 
ATOM   4202 C  CD2  . LEU   B 1 10  ? 38.127 -34.395 -16.480 1.00 21.45 ?  10   LEU   B CD2  1 
ATOM   4203 H  H    . LEU   B 1 10  ? 40.750 -30.322 -16.847 1.00 21.09 ?  10   LEU   B H    1 
ATOM   4204 H  HA   . LEU   B 1 10  ? 39.069 -31.057 -18.827 1.00 20.99 ?  10   LEU   B HA   1 
ATOM   4205 H  HB2  . LEU   B 1 10  ? 40.143 -32.712 -17.482 1.00 22.03 ?  10   LEU   B HB2  1 
ATOM   4206 H  HB3  . LEU   B 1 10  ? 39.330 -32.165 -16.236 1.00 22.03 ?  10   LEU   B HB3  1 
ATOM   4207 H  HG   . LEU   B 1 10  ? 37.337 -32.801 -17.463 1.00 24.23 ?  10   LEU   B HG   1 
ATOM   4208 H  HD11 . LEU   B 1 10  ? 37.610 -34.468 -19.080 1.00 25.55 ?  10   LEU   B HD11 1 
ATOM   4209 H  HD12 . LEU   B 1 10  ? 38.262 -33.098 -19.552 1.00 25.55 ?  10   LEU   B HD12 1 
ATOM   4210 H  HD13 . LEU   B 1 10  ? 39.184 -34.268 -19.000 1.00 25.55 ?  10   LEU   B HD13 1 
ATOM   4211 H  HD21 . LEU   B 1 10  ? 37.402 -34.995 -16.709 1.00 25.75 ?  10   LEU   B HD21 1 
ATOM   4212 H  HD22 . LEU   B 1 10  ? 38.970 -34.868 -16.487 1.00 25.75 ?  10   LEU   B HD22 1 
ATOM   4213 H  HD23 . LEU   B 1 10  ? 37.971 -34.005 -15.604 1.00 25.75 ?  10   LEU   B HD23 1 
ATOM   4214 N  N    . LYS   B 1 11  ? 36.975 -30.007 -18.112 1.00 18.47 ?  11   LYS   B N    1 
ATOM   4215 C  CA   . LYS   B 1 11  ? 35.782 -29.293 -17.690 1.00 20.50 ?  11   LYS   B CA   1 
ATOM   4216 C  C    . LYS   B 1 11  ? 34.927 -30.213 -16.827 1.00 19.45 ?  11   LYS   B C    1 
ATOM   4217 O  O    . LYS   B 1 11  ? 34.547 -31.307 -17.262 1.00 21.11 ?  11   LYS   B O    1 
ATOM   4218 C  CB   . LYS   B 1 11  ? 35.014 -28.841 -18.931 1.00 25.33 ?  11   LYS   B CB   1 
ATOM   4219 C  CG   . LYS   B 1 11  ? 33.908 -27.833 -18.683 1.00 29.32 ?  11   LYS   B CG   1 
ATOM   4220 C  CD   . LYS   B 1 11  ? 33.160 -27.535 -19.978 1.00 32.55 ?  11   LYS   B CD   1 
ATOM   4221 C  CE   . LYS   B 1 11  ? 32.145 -26.416 -19.806 1.00 34.91 ?  11   LYS   B CE   1 
ATOM   4222 N  NZ   . LYS   B 1 11  ? 32.800 -25.091 -19.632 1.00 35.99 ?  11   LYS   B NZ   1 
ATOM   4223 H  H    . LYS   B 1 11  ? 36.927 -30.320 -18.915 1.00 22.17 ?  11   LYS   B H    1 
ATOM   4224 H  HA   . LYS   B 1 11  ? 36.029 -28.513 -17.172 1.00 24.61 ?  11   LYS   B HA   1 
ATOM   4225 H  HB2  . LYS   B 1 11  ? 35.642 -28.432 -19.549 1.00 30.41 ?  11   LYS   B HB2  1 
ATOM   4226 H  HB3  . LYS   B 1 11  ? 34.610 -29.617 -19.346 1.00 30.41 ?  11   LYS   B HB3  1 
ATOM   4227 H  HG2  . LYS   B 1 11  ? 33.278 -28.196 -18.042 1.00 35.19 ?  11   LYS   B HG2  1 
ATOM   4228 H  HG3  . LYS   B 1 11  ? 34.291 -27.006 -18.353 1.00 35.19 ?  11   LYS   B HG3  1 
ATOM   4229 H  HD2  . LYS   B 1 11  ? 33.797 -27.265 -20.659 1.00 39.07 ?  11   LYS   B HD2  1 
ATOM   4230 H  HD3  . LYS   B 1 11  ? 32.687 -28.333 -20.263 1.00 39.07 ?  11   LYS   B HD3  1 
ATOM   4231 H  HE2  . LYS   B 1 11  ? 31.580 -26.372 -20.594 1.00 41.91 ?  11   LYS   B HE2  1 
ATOM   4232 H  HE3  . LYS   B 1 11  ? 31.607 -26.598 -19.020 1.00 41.91 ?  11   LYS   B HE3  1 
ATOM   4233 H  HZ1  . LYS   B 1 11  ? 32.183 -24.456 -19.538 1.00 43.21 ?  11   LYS   B HZ1  1 
ATOM   4234 H  HZ2  . LYS   B 1 11  ? 33.319 -25.100 -18.910 1.00 43.21 ?  11   LYS   B HZ2  1 
ATOM   4235 H  HZ3  . LYS   B 1 11  ? 33.300 -24.903 -20.345 1.00 43.21 ?  11   LYS   B HZ3  1 
ATOM   4236 N  N    . LEU   B 1 12  ? 34.623 -29.777 -15.605 1.00 17.89 ?  12   LEU   B N    1 
ATOM   4237 C  CA   . LEU   B 1 12  ? 33.657 -30.474 -14.759 1.00 17.05 ?  12   LEU   B CA   1 
ATOM   4238 C  C    . LEU   B 1 12  ? 32.270 -29.858 -14.850 1.00 16.88 ?  12   LEU   B C    1 
ATOM   4239 O  O    . LEU   B 1 12  ? 31.282 -30.569 -15.024 1.00 17.77 ?  12   LEU   B O    1 
ATOM   4240 C  CB   . LEU   B 1 12  ? 34.123 -30.494 -13.300 1.00 16.89 ?  12   LEU   B CB   1 
ATOM   4241 C  CG   . LEU   B 1 12  ? 35.468 -31.170 -13.050 1.00 16.65 ?  12   LEU   B CG   1 
ATOM   4242 C  CD1  . LEU   B 1 12  ? 35.842 -31.115 -11.578 1.00 16.90 ?  12   LEU   B CD1  1 
ATOM   4243 C  CD2  . LEU   B 1 12  ? 35.462 -32.610 -13.559 1.00 17.47 ?  12   LEU   B CD2  1 
ATOM   4244 H  H    . LEU   B 1 12  ? 34.964 -29.076 -15.242 1.00 21.49 ?  12   LEU   B H    1 
ATOM   4245 H  HA   . LEU   B 1 12  ? 33.582 -31.390 -15.061 1.00 20.48 ?  12   LEU   B HA   1 
ATOM   4246 H  HB2  . LEU   B 1 12  ? 34.190 -29.580 -12.985 1.00 20.28 ?  12   LEU   B HB2  1 
ATOM   4247 H  HB3  . LEU   B 1 12  ? 33.456 -30.968 -12.774 1.00 20.28 ?  12   LEU   B HB3  1 
ATOM   4248 H  HG   . LEU   B 1 12  ? 36.150 -30.687 -13.543 1.00 19.99 ?  12   LEU   B HG   1 
ATOM   4249 H  HD11 . LEU   B 1 12  ? 36.704 -31.549 -11.456 1.00 20.30 ?  12   LEU   B HD11 1 
ATOM   4250 H  HD12 . LEU   B 1 12  ? 35.899 -30.188 -11.299 1.00 20.30 ?  12   LEU   B HD12 1 
ATOM   4251 H  HD13 . LEU   B 1 12  ? 35.166 -31.577 -11.061 1.00 20.30 ?  12   LEU   B HD13 1 
ATOM   4252 H  HD21 . LEU   B 1 12  ? 36.268 -33.055 -13.254 1.00 20.98 ?  12   LEU   B HD21 1 
ATOM   4253 H  HD22 . LEU   B 1 12  ? 34.679 -33.064 -13.214 1.00 20.98 ?  12   LEU   B HD22 1 
ATOM   4254 H  HD23 . LEU   B 1 12  ? 35.439 -32.601 -14.531 1.00 20.98 ?  12   LEU   B HD23 1 
ATOM   4255 N  N    . THR   B 1 13  ? 32.186 -28.541 -14.735 1.00 16.99 ?  13   THR   B N    1 
ATOM   4256 C  CA   . THR   B 1 13  ? 30.962 -27.787 -14.936 1.00 16.89 ?  13   THR   B CA   1 
ATOM   4257 C  C    . THR   B 1 13  ? 31.299 -26.592 -15.822 1.00 19.06 ?  13   THR   B C    1 
ATOM   4258 O  O    . THR   B 1 13  ? 32.446 -26.406 -16.249 1.00 19.77 ?  13   THR   B O    1 
ATOM   4259 C  CB   . THR   B 1 13  ? 30.377 -27.304 -13.603 1.00 16.50 ?  13   THR   B CB   1 
ATOM   4260 O  OG1  . THR   B 1 13  ? 31.229 -26.282 -13.065 1.00 16.07 ?  13   THR   B OG1  1 
ATOM   4261 C  CG2  . THR   B 1 13  ? 30.257 -28.453 -12.607 1.00 17.27 ?  13   THR   B CG2  1 
ATOM   4262 H  H    . THR   B 1 13  ? 32.855 -28.038 -14.530 1.00 20.41 ?  13   THR   B H    1 
ATOM   4263 H  HA   . THR   B 1 13  ? 30.300 -28.345 -15.379 1.00 20.28 ?  13   THR   B HA   1 
ATOM   4264 H  HB   . THR   B 1 13  ? 29.485 -26.940 -13.751 1.00 19.81 ?  13   THR   B HB   1 
ATOM   4265 H  HG1  . THR   B 1 13  ? 30.920 -25.523 -13.261 1.00 19.30 ?  13   THR   B HG1  1 
ATOM   4266 H  HG21 . THR   B 1 13  ? 29.770 -28.164 -11.820 1.00 20.74 ?  13   THR   B HG21 1 
ATOM   4267 H  HG22 . THR   B 1 13  ? 29.782 -29.196 -13.014 1.00 20.74 ?  13   THR   B HG22 1 
ATOM   4268 H  HG23 . THR   B 1 13  ? 31.139 -28.753 -12.340 1.00 20.74 ?  13   THR   B HG23 1 
ATOM   4269 N  N    A ASP   B 1 14  ? 30.293 -25.759 -16.087 0.62 20.19 ?  14   ASP   B N    1 
ATOM   4270 N  N    B ASP   B 1 14  ? 30.296 -25.750 -16.079 0.38 19.97 ?  14   ASP   B N    1 
ATOM   4271 C  CA   A ASP   B 1 14  ? 30.522 -24.608 -16.951 0.62 21.78 ?  14   ASP   B CA   1 
ATOM   4272 C  CA   B ASP   B 1 14  ? 30.508 -24.599 -16.951 0.38 21.05 ?  14   ASP   B CA   1 
ATOM   4273 C  C    A ASP   B 1 14  ? 31.636 -23.715 -16.417 0.62 19.80 ?  14   ASP   B C    1 
ATOM   4274 C  C    B ASP   B 1 14  ? 31.521 -23.609 -16.392 0.38 19.31 ?  14   ASP   B C    1 
ATOM   4275 O  O    A ASP   B 1 14  ? 32.341 -23.075 -17.206 0.62 20.77 ?  14   ASP   B O    1 
ATOM   4276 O  O    B ASP   B 1 14  ? 31.996 -22.748 -17.140 0.38 19.96 ?  14   ASP   B O    1 
ATOM   4277 C  CB   A ASP   B 1 14  ? 29.228 -23.816 -17.137 0.62 25.57 ?  14   ASP   B CB   1 
ATOM   4278 C  CB   B ASP   B 1 14  ? 29.194 -23.864 -17.202 0.38 23.95 ?  14   ASP   B CB   1 
ATOM   4279 C  CG   A ASP   B 1 14  ? 28.257 -24.491 -18.080 0.62 28.99 ?  14   ASP   B CG   1 
ATOM   4280 C  CG   B ASP   B 1 14  ? 28.287 -24.606 -18.163 0.38 26.53 ?  14   ASP   B CG   1 
ATOM   4281 O  OD1  A ASP   B 1 14  ? 28.615 -25.526 -18.684 0.62 30.10 ?  14   ASP   B OD1  1 
ATOM   4282 O  OD1  B ASP   B 1 14  ? 28.813 -25.290 -19.067 0.38 27.33 ?  14   ASP   B OD1  1 
ATOM   4283 O  OD2  A ASP   B 1 14  ? 27.124 -23.982 -18.214 0.62 30.28 -1 14   ASP   B OD2  1 
ATOM   4284 O  OD2  B ASP   B 1 14  ? 27.051 -24.512 -18.016 0.38 27.46 -1 14   ASP   B OD2  1 
ATOM   4285 H  H    A ASP   B 1 14  ? 29.494 -25.824 -15.774 0.62 24.24 ?  14   ASP   B H    1 
ATOM   4286 H  H    B ASP   B 1 14  ? 29.499 -25.819 -15.764 0.38 23.98 ?  14   ASP   B H    1 
ATOM   4287 H  HA   A ASP   B 1 14  ? 30.808 -24.919 -17.818 0.62 26.15 ?  14   ASP   B HA   1 
ATOM   4288 H  HA   B ASP   B 1 14  ? 30.841 -24.914 -17.805 0.38 25.28 ?  14   ASP   B HA   1 
ATOM   4289 H  HB2  A ASP   B 1 14  ? 28.779 -23.726 -16.286 0.62 30.70 ?  14   ASP   B HB2  1 
ATOM   4290 H  HB2  B ASP   B 1 14  ? 28.726 -23.762 -16.360 0.38 28.76 ?  14   ASP   B HB2  1 
ATOM   4291 H  HB3  A ASP   B 1 14  ? 29.436 -22.944 -17.505 0.62 30.70 ?  14   ASP   B HB3  1 
ATOM   4292 H  HB3  B ASP   B 1 14  ? 29.396 -22.987 -17.575 0.38 28.76 ?  14   ASP   B HB3  1 
ATOM   4293 N  N    . ASN   B 1 15  ? 31.837 -23.682 -15.095 1.00 17.32 ?  15   ASN   B N    1 
ATOM   4294 C  CA   . ASN   B 1 15  ? 32.803 -22.767 -14.491 1.00 15.10 ?  15   ASN   B CA   1 
ATOM   4295 C  C    . ASN   B 1 15  ? 33.899 -23.426 -13.661 1.00 13.66 ?  15   ASN   B C    1 
ATOM   4296 O  O    . ASN   B 1 15  ? 34.761 -22.706 -13.141 1.00 14.17 ?  15   ASN   B O    1 
ATOM   4297 C  CB   . ASN   B 1 15  ? 32.096 -21.715 -13.620 1.00 15.09 ?  15   ASN   B CB   1 
ATOM   4298 C  CG   . ASN   B 1 15  ? 31.474 -22.317 -12.378 1.00 14.85 ?  15   ASN   B CG   1 
ATOM   4299 O  OD1  . ASN   B 1 15  ? 30.529 -23.109 -12.464 1.00 16.77 ?  15   ASN   B OD1  1 
ATOM   4300 N  ND2  . ASN   B 1 15  ? 32.002 -21.970 -11.220 1.00 13.83 ?  15   ASN   B ND2  1 
ATOM   4301 H  H    A ASN   B 1 15  ? 31.428 -24.186 -14.528 0.62 20.80 ?  15   ASN   B H    1 
ATOM   4302 H  H    B ASN   B 1 15  ? 31.477 -24.230 -14.537 0.38 20.80 ?  15   ASN   B H    1 
ATOM   4303 H  HA   . ASN   B 1 15  ? 33.245 -22.279 -15.197 1.00 18.14 ?  15   ASN   B HA   1 
ATOM   4304 H  HB2  . ASN   B 1 15  ? 32.745 -21.041 -13.343 1.00 18.12 ?  15   ASN   B HB2  1 
ATOM   4305 H  HB3  . ASN   B 1 15  ? 31.390 -21.289 -14.136 1.00 18.12 ?  15   ASN   B HB3  1 
ATOM   4306 H  HD21 . ASN   B 1 15  ? 31.681 -22.282 -10.486 1.00 16.61 ?  15   ASN   B HD21 1 
ATOM   4307 H  HD22 . ASN   B 1 15  ? 32.666 -21.414 -11.189 1.00 16.61 ?  15   ASN   B HD22 1 
ATOM   4308 N  N    . VAL   B 1 16  ? 33.899 -24.748 -13.507 1.00 13.70 ?  16   VAL   B N    1 
ATOM   4309 C  CA   . VAL   B 1 16  ? 34.899 -25.443 -12.701 1.00 13.36 ?  16   VAL   B CA   1 
ATOM   4310 C  C    . VAL   B 1 16  ? 35.687 -26.380 -13.601 1.00 13.48 ?  16   VAL   B C    1 
ATOM   4311 O  O    . VAL   B 1 16  ? 35.105 -27.260 -14.258 1.00 14.40 ?  16   VAL   B O    1 
ATOM   4312 C  CB   . VAL   B 1 16  ? 34.276 -26.205 -11.522 1.00 13.54 ?  16   VAL   B CB   1 
ATOM   4313 C  CG1  . VAL   B 1 16  ? 35.362 -26.944 -10.733 1.00 14.04 ?  16   VAL   B CG1  1 
ATOM   4314 C  CG2  . VAL   B 1 16  ? 33.481 -25.256 -10.629 1.00 14.20 ?  16   VAL   B CG2  1 
ATOM   4315 H  H    . VAL   B 1 16  ? 33.307 -25.272 -13.856 1.00 16.45 ?  16   VAL   B H    1 
ATOM   4316 H  HA   . VAL   B 1 16  ? 35.513 -24.789 -12.332 1.00 16.05 ?  16   VAL   B HA   1 
ATOM   4317 H  HB   . VAL   B 1 16  ? 33.660 -26.870 -11.868 1.00 16.26 ?  16   VAL   B HB   1 
ATOM   4318 H  HG11 . VAL   B 1 16  ? 34.987 -27.241 -9.887  1.00 16.86 ?  16   VAL   B HG11 1 
ATOM   4319 H  HG12 . VAL   B 1 16  ? 35.664 -27.707 -11.245 1.00 16.86 ?  16   VAL   B HG12 1 
ATOM   4320 H  HG13 . VAL   B 1 16  ? 36.099 -26.336 -10.568 1.00 16.86 ?  16   VAL   B HG13 1 
ATOM   4321 H  HG21 . VAL   B 1 16  ? 33.146 -25.747 -9.861  1.00 17.06 ?  16   VAL   B HG21 1 
ATOM   4322 H  HG22 . VAL   B 1 16  ? 34.056 -24.536 -10.337 1.00 17.06 ?  16   VAL   B HG22 1 
ATOM   4323 H  HG23 . VAL   B 1 16  ? 32.733 -24.896 -11.138 1.00 17.06 ?  16   VAL   B HG23 1 
ATOM   4324 N  N    . TYR   B 1 17  ? 37.008 -26.206 -13.598 1.00 13.78 ?  17   TYR   B N    1 
ATOM   4325 C  CA   . TYR   B 1 17  ? 37.946 -26.960 -14.411 1.00 14.39 ?  17   TYR   B CA   1 
ATOM   4326 C  C    . TYR   B 1 17  ? 39.003 -27.571 -13.501 1.00 13.38 ?  17   TYR   B C    1 
ATOM   4327 O  O    . TYR   B 1 17  ? 39.290 -27.038 -12.425 1.00 13.96 ?  17   TYR   B O    1 
ATOM   4328 C  CB   . TYR   B 1 17  ? 38.658 -26.036 -15.407 1.00 17.49 ?  17   TYR   B CB   1 
ATOM   4329 C  CG   . TYR   B 1 17  ? 37.734 -25.264 -16.316 1.00 20.90 ?  17   TYR   B CG   1 
ATOM   4330 C  CD1  . TYR   B 1 17  ? 37.187 -24.048 -15.923 1.00 22.53 ?  17   TYR   B CD1  1 
ATOM   4331 C  CD2  . TYR   B 1 17  ? 37.410 -25.753 -17.572 1.00 23.24 ?  17   TYR   B CD2  1 
ATOM   4332 C  CE1  . TYR   B 1 17  ? 36.340 -23.341 -16.758 1.00 24.65 ?  17   TYR   B CE1  1 
ATOM   4333 C  CE2  . TYR   B 1 17  ? 36.569 -25.055 -18.415 1.00 24.97 ?  17   TYR   B CE2  1 
ATOM   4334 C  CZ   . TYR   B 1 17  ? 36.034 -23.850 -18.001 1.00 25.82 ?  17   TYR   B CZ   1 
ATOM   4335 O  OH   . TYR   B 1 17  ? 35.196 -23.152 -18.837 1.00 27.48 ?  17   TYR   B OH   1 
ATOM   4336 H  H    . TYR   B 1 17  ? 37.404 -25.613 -13.107 1.00 16.55 ?  17   TYR   B H    1 
ATOM   4337 H  HA   . TYR   B 1 17  ? 37.483 -27.662 -14.897 1.00 17.28 ?  17   TYR   B HA   1 
ATOM   4338 H  HB2  . TYR   B 1 17  ? 39.199 -25.400 -14.917 1.00 21.01 ?  17   TYR   B HB2  1 
ATOM   4339 H  HB3  . TYR   B 1 17  ? 39.222 -26.580 -15.973 1.00 21.01 ?  17   TYR   B HB3  1 
ATOM   4340 H  HD1  . TYR   B 1 17  ? 37.395 -23.704 -15.086 1.00 27.05 ?  17   TYR   B HD1  1 
ATOM   4341 H  HD2  . TYR   B 1 17  ? 37.763 -26.565 -17.855 1.00 27.91 ?  17   TYR   B HD2  1 
ATOM   4342 H  HE1  . TYR   B 1 17  ? 35.982 -22.527 -16.484 1.00 29.60 ?  17   TYR   B HE1  1 
ATOM   4343 H  HE2  . TYR   B 1 17  ? 36.354 -25.397 -19.255 1.00 29.98 ?  17   TYR   B HE2  1 
ATOM   4344 H  HH   . TYR   B 1 17  ? 35.090 -23.569 -19.559 1.00 32.99 ?  17   TYR   B HH   1 
ATOM   4345 N  N    . ILE   B 1 18  ? 39.608 -28.675 -13.940 1.00 13.34 ?  18   ILE   B N    1 
ATOM   4346 C  CA   . ILE   B 1 18  ? 40.537 -29.406 -13.086 1.00 13.61 ?  18   ILE   B CA   1 
ATOM   4347 C  C    . ILE   B 1 18  ? 41.691 -29.959 -13.915 1.00 14.07 ?  18   ILE   B C    1 
ATOM   4348 O  O    . ILE   B 1 18  ? 41.522 -30.345 -15.076 1.00 15.08 ?  18   ILE   B O    1 
ATOM   4349 C  CB   . ILE   B 1 18  ? 39.788 -30.509 -12.289 1.00 13.98 ?  18   ILE   B CB   1 
ATOM   4350 C  CG1  . ILE   B 1 18  ? 40.643 -31.051 -11.140 1.00 14.62 ?  18   ILE   B CG1  1 
ATOM   4351 C  CG2  . ILE   B 1 18  ? 39.283 -31.621 -13.218 1.00 14.50 ?  18   ILE   B CG2  1 
ATOM   4352 C  CD1  . ILE   B 1 18  ? 39.843 -31.876 -10.146 1.00 16.23 ?  18   ILE   B CD1  1 
ATOM   4353 H  H    . ILE   B 1 18  ? 39.504 -29.014 -14.721 1.00 16.02 ?  18   ILE   B H    1 
ATOM   4354 H  HA   . ILE   B 1 18  ? 40.903 -28.794 -12.428 1.00 16.35 ?  18   ILE   B HA   1 
ATOM   4355 H  HB   . ILE   B 1 18  ? 39.001 -30.103 -11.888 1.00 16.79 ?  18   ILE   B HB   1 
ATOM   4356 H  HG12 . ILE   B 1 18  ? 41.341 -31.610 -11.500 1.00 17.56 ?  18   ILE   B HG12 1 
ATOM   4357 H  HG13 . ILE   B 1 18  ? 41.026 -30.299 -10.658 1.00 17.56 ?  18   ILE   B HG13 1 
ATOM   4358 H  HG21 . ILE   B 1 18  ? 38.691 -32.211 -12.720 1.00 17.42 ?  18   ILE   B HG21 1 
ATOM   4359 H  HG22 . ILE   B 1 18  ? 38.796 -31.217 -13.955 1.00 17.42 ?  18   ILE   B HG22 1 
ATOM   4360 H  HG23 . ILE   B 1 18  ? 40.039 -32.122 -13.556 1.00 17.42 ?  18   ILE   B HG23 1 
ATOM   4361 H  HD11 . ILE   B 1 18  ? 40.422 -32.142 -9.417  1.00 19.49 ?  18   ILE   B HD11 1 
ATOM   4362 H  HD12 . ILE   B 1 18  ? 39.107 -31.340 -9.805  1.00 19.49 ?  18   ILE   B HD12 1 
ATOM   4363 H  HD13 . ILE   B 1 18  ? 39.494 -32.662 -10.597 1.00 19.49 ?  18   ILE   B HD13 1 
ATOM   4364 N  N    . LYS   B 1 19  ? 42.875 -29.994 -13.303 1.00 14.41 ?  19   LYS   B N    1 
ATOM   4365 C  CA   . LYS   B 1 19  ? 44.075 -30.475 -13.972 1.00 15.63 ?  19   LYS   B CA   1 
ATOM   4366 C  C    . LYS   B 1 19  ? 44.977 -31.151 -12.952 1.00 15.10 ?  19   LYS   B C    1 
ATOM   4367 O  O    . LYS   B 1 19  ? 45.065 -30.714 -11.801 1.00 14.89 ?  19   LYS   B O    1 
ATOM   4368 C  CB   . LYS   B 1 19  ? 44.839 -29.312 -14.621 1.00 17.19 ?  19   LYS   B CB   1 
ATOM   4369 C  CG   . LYS   B 1 19  ? 46.032 -29.719 -15.468 1.00 19.48 ?  19   LYS   B CG   1 
ATOM   4370 C  CD   . LYS   B 1 19  ? 46.750 -28.484 -15.998 1.00 21.72 ?  19   LYS   B CD   1 
ATOM   4371 C  CE   . LYS   B 1 19  ? 47.921 -28.839 -16.890 1.00 23.83 ?  19   LYS   B CE   1 
ATOM   4372 N  NZ   . LYS   B 1 19  ? 48.628 -27.625 -17.378 1.00 24.77 ?  19   LYS   B NZ   1 
ATOM   4373 H  H    . LYS   B 1 19  ? 43.003 -29.739 -12.486 1.00 17.31 ?  19   LYS   B H    1 
ATOM   4374 H  HA   . LYS   B 1 19  ? 43.827 -31.118 -14.655 1.00 18.77 ?  19   LYS   B HA   1 
ATOM   4375 H  HB2  . LYS   B 1 19  ? 44.224 -28.828 -15.192 1.00 20.64 ?  19   LYS   B HB2  1 
ATOM   4376 H  HB3  . LYS   B 1 19  ? 45.158 -28.727 -13.915 1.00 20.64 ?  19   LYS   B HB3  1 
ATOM   4377 H  HG2  . LYS   B 1 19  ? 46.649 -30.233 -14.927 1.00 23.40 ?  19   LYS   B HG2  1 
ATOM   4378 H  HG3  . LYS   B 1 19  ? 45.719 -30.246 -16.222 1.00 23.40 ?  19   LYS   B HG3  1 
ATOM   4379 H  HD2  . LYS   B 1 19  ? 46.124 -27.952 -16.514 1.00 26.08 ?  19   LYS   B HD2  1 
ATOM   4380 H  HD3  . LYS   B 1 19  ? 47.085 -27.969 -15.247 1.00 26.08 ?  19   LYS   B HD3  1 
ATOM   4381 H  HE2  . LYS   B 1 19  ? 48.551 -29.379 -16.387 1.00 28.61 ?  19   LYS   B HE2  1 
ATOM   4382 H  HE3  . LYS   B 1 19  ? 47.596 -29.334 -17.659 1.00 28.61 ?  19   LYS   B HE3  1 
ATOM   4383 H  HZ1  . LYS   B 1 19  ? 49.282 -27.857 -17.937 1.00 29.74 ?  19   LYS   B HZ1  1 
ATOM   4384 H  HZ2  . LYS   B 1 19  ? 48.059 -27.091 -17.807 1.00 29.74 ?  19   LYS   B HZ2  1 
ATOM   4385 H  HZ3  . LYS   B 1 19  ? 48.980 -27.180 -16.693 1.00 29.74 ?  19   LYS   B HZ3  1 
ATOM   4386 N  N    . ASN   B 1 20  ? 45.661 -32.206 -13.389 1.00 16.24 ?  20   ASN   B N    1 
ATOM   4387 C  CA   . ASN   B 1 20  ? 46.701 -32.832 -12.581 1.00 17.22 ?  20   ASN   B CA   1 
ATOM   4388 C  C    . ASN   B 1 20  ? 47.972 -32.006 -12.762 1.00 17.77 ?  20   ASN   B C    1 
ATOM   4389 O  O    . ASN   B 1 20  ? 48.600 -32.053 -13.825 1.00 19.76 ?  20   ASN   B O    1 
ATOM   4390 C  CB   . ASN   B 1 20  ? 46.884 -34.282 -13.031 1.00 19.32 ?  20   ASN   B CB   1 
ATOM   4391 C  CG   . ASN   B 1 20  ? 48.055 -34.983 -12.353 1.00 21.01 ?  20   ASN   B CG   1 
ATOM   4392 O  OD1  . ASN   B 1 20  ? 48.735 -35.806 -12.973 1.00 23.39 ?  20   ASN   B OD1  1 
ATOM   4393 N  ND2  . ASN   B 1 20  ? 48.285 -34.680 -11.083 1.00 20.48 ?  20   ASN   B ND2  1 
ATOM   4394 H  H    . ASN   B 1 20  ? 45.535 -32.576 -14.155 1.00 19.51 ?  20   ASN   B H    1 
ATOM   4395 H  HA   . ASN   B 1 20  ? 46.431 -32.824 -11.646 1.00 20.68 ?  20   ASN   B HA   1 
ATOM   4396 H  HB2  . ASN   B 1 20  ? 46.075 -34.783 -12.826 1.00 23.20 ?  20   ASN   B HB2  1 
ATOM   4397 H  HB3  . ASN   B 1 20  ? 47.039 -34.292 -13.989 1.00 23.20 ?  20   ASN   B HB3  1 
ATOM   4398 H  HD21 . ASN   B 1 20  ? 48.938 -35.046 -10.666 1.00 24.59 ?  20   ASN   B HD21 1 
ATOM   4399 H  HD22 . ASN   B 1 20  ? 47.787 -34.102 -10.675 1.00 24.59 ?  20   ASN   B HD22 1 
ATOM   4400 N  N    . ALA   B 1 21  ? 48.338 -31.223 -11.746 1.00 17.22 ?  21   ALA   B N    1 
ATOM   4401 C  CA   . ALA   B 1 21  ? 49.444 -30.291 -11.897 1.00 17.88 ?  21   ALA   B CA   1 
ATOM   4402 C  C    . ALA   B 1 21  ? 49.906 -29.797 -10.534 1.00 17.09 ?  21   ALA   B C    1 
ATOM   4403 O  O    . ALA   B 1 21  ? 49.163 -29.828 -9.546  1.00 16.72 ?  21   ALA   B O    1 
ATOM   4404 C  CB   . ALA   B 1 21  ? 49.033 -29.116 -12.782 1.00 19.36 ?  21   ALA   B CB   1 
ATOM   4405 H  H    . ALA   B 1 21  ? 47.957 -31.219 -10.971 1.00 20.68 ?  21   ALA   B H    1 
ATOM   4406 H  HA   . ALA   B 1 21  ? 50.180 -30.757 -12.323 1.00 21.47 ?  21   ALA   B HA   1 
ATOM   4407 H  HB1  . ALA   B 1 21  ? 49.821 -28.594 -12.969 1.00 23.25 ?  21   ALA   B HB1  1 
ATOM   4408 H  HB2  . ALA   B 1 21  ? 48.661 -29.467 -13.607 1.00 23.25 ?  21   ALA   B HB2  1 
ATOM   4409 H  HB3  . ALA   B 1 21  ? 48.369 -28.590 -12.316 1.00 23.25 ?  21   ALA   B HB3  1 
ATOM   4410 N  N    . ASP   B 1 22  ? 51.165 -29.355 -10.512 1.00 16.17 ?  22   ASP   B N    1 
ATOM   4411 C  CA   . ASP   B 1 22  ? 51.787 -28.676 -9.379  1.00 15.43 ?  22   ASP   B CA   1 
ATOM   4412 C  C    . ASP   B 1 22  ? 51.393 -27.202 -9.444  1.00 13.88 ?  22   ASP   B C    1 
ATOM   4413 O  O    . ASP   B 1 22  ? 51.715 -26.520 -10.422 1.00 14.36 ?  22   ASP   B O    1 
ATOM   4414 C  CB   . ASP   B 1 22  ? 53.304 -28.858 -9.539  1.00 17.06 ?  22   ASP   B CB   1 
ATOM   4415 C  CG   . ASP   B 1 22  ? 54.141 -28.110 -8.505  1.00 18.75 ?  22   ASP   B CG   1 
ATOM   4416 O  OD1  . ASP   B 1 22  ? 53.783 -26.993 -8.100  1.00 18.75 ?  22   ASP   B OD1  1 
ATOM   4417 O  OD2  . ASP   B 1 22  ? 55.214 -28.636 -8.130  1.00 21.69 -1 22   ASP   B OD2  1 
ATOM   4418 H  H    . ASP   B 1 22  ? 51.703 -29.447 -11.182 1.00 19.42 ?  22   ASP   B H    1 
ATOM   4419 H  HA   . ASP   B 1 22  ? 51.491 -29.071 -8.540  1.00 18.54 ?  22   ASP   B HA   1 
ATOM   4420 H  HB2  . ASP   B 1 22  ? 53.519 -29.797 -9.466  1.00 20.49 ?  22   ASP   B HB2  1 
ATOM   4421 H  HB3  . ASP   B 1 22  ? 53.562 -28.524 -10.412 1.00 20.49 ?  22   ASP   B HB3  1 
ATOM   4422 N  N    . ILE   B 1 23  ? 50.679 -26.719 -8.421  1.00 13.40 ?  23   ILE   B N    1 
ATOM   4423 C  CA   . ILE   B 1 23  ? 50.097 -25.375 -8.472  1.00 12.68 ?  23   ILE   B CA   1 
ATOM   4424 C  C    . ILE   B 1 23  ? 51.160 -24.288 -8.607  1.00 12.41 ?  23   ILE   B C    1 
ATOM   4425 O  O    . ILE   B 1 23  ? 50.899 -23.242 -9.210  1.00 11.96 ?  23   ILE   B O    1 
ATOM   4426 C  CB   . ILE   B 1 23  ? 49.169 -25.134 -7.264  1.00 12.80 ?  23   ILE   B CB   1 
ATOM   4427 C  CG1  . ILE   B 1 23  ? 48.351 -23.850 -7.445  1.00 13.49 ?  23   ILE   B CG1  1 
ATOM   4428 C  CG2  . ILE   B 1 23  ? 49.947 -25.118 -5.959  1.00 13.47 ?  23   ILE   B CG2  1 
ATOM   4429 C  CD1  . ILE   B 1 23  ? 47.213 -23.710 -6.436  1.00 14.20 ?  23   ILE   B CD1  1 
ATOM   4430 H  H    . ILE   B 1 23  ? 50.511 -27.151 -7.696  1.00 16.09 ?  23   ILE   B H    1 
ATOM   4431 H  HA   . ILE   B 1 23  ? 49.543 -25.319 -9.263  1.00 15.23 ?  23   ILE   B HA   1 
ATOM   4432 H  HB   . ILE   B 1 23  ? 48.542 -25.870 -7.225  1.00 15.37 ?  23   ILE   B HB   1 
ATOM   4433 H  HG12 . ILE   B 1 23  ? 48.940 -23.082 -7.340  1.00 16.20 ?  23   ILE   B HG12 1 
ATOM   4434 H  HG13 . ILE   B 1 23  ? 47.965 -23.843 -8.337  1.00 16.20 ?  23   ILE   B HG13 1 
ATOM   4435 H  HG21 . ILE   B 1 23  ? 49.321 -25.110 -5.220  1.00 16.18 ?  23   ILE   B HG21 1 
ATOM   4436 H  HG22 . ILE   B 1 23  ? 50.499 -25.915 -5.917  1.00 16.18 ?  23   ILE   B HG22 1 
ATOM   4437 H  HG23 . ILE   B 1 23  ? 50.505 -24.327 -5.932  1.00 16.18 ?  23   ILE   B HG23 1 
ATOM   4438 H  HD11 . ILE   B 1 23  ? 46.696 -22.920 -6.650  1.00 17.05 ?  23   ILE   B HD11 1 
ATOM   4439 H  HD12 . ILE   B 1 23  ? 46.652 -24.499 -6.489  1.00 17.05 ?  23   ILE   B HD12 1 
ATOM   4440 H  HD13 . ILE   B 1 23  ? 47.591 -23.630 -5.546  1.00 17.05 ?  23   ILE   B HD13 1 
ATOM   4441 N  N    . VAL   B 1 24  ? 52.354 -24.499 -8.049  1.00 12.62 ?  24   VAL   B N    1 
ATOM   4442 C  CA   . VAL   B 1 24  ? 53.434 -23.520 -8.205  1.00 13.19 ?  24   VAL   B CA   1 
ATOM   4443 C  C    . VAL   B 1 24  ? 53.891 -23.464 -9.656  1.00 13.21 ?  24   VAL   B C    1 
ATOM   4444 O  O    . VAL   B 1 24  ? 54.026 -22.383 -10.244 1.00 13.90 ?  24   VAL   B O    1 
ATOM   4445 C  CB   . VAL   B 1 24  ? 54.609 -23.843 -7.260  1.00 14.12 ?  24   VAL   B CB   1 
ATOM   4446 C  CG1  . VAL   B 1 24  ? 55.821 -22.951 -7.571  1.00 14.93 ?  24   VAL   B CG1  1 
ATOM   4447 C  CG2  . VAL   B 1 24  ? 54.182 -23.678 -5.820  1.00 15.16 ?  24   VAL   B CG2  1 
ATOM   4448 H  H    . VAL   B 1 24  ? 52.566 -25.190 -7.583  1.00 15.16 ?  24   VAL   B H    1 
ATOM   4449 H  HA   . VAL   B 1 24  ? 53.095 -22.642 -7.964  1.00 15.85 ?  24   VAL   B HA   1 
ATOM   4450 H  HB   . VAL   B 1 24  ? 54.872 -24.767 -7.386  1.00 16.97 ?  24   VAL   B HB   1 
ATOM   4451 H  HG11 . VAL   B 1 24  ? 56.415 -22.957 -6.806  1.00 17.94 ?  24   VAL   B HG11 1 
ATOM   4452 H  HG12 . VAL   B 1 24  ? 56.275 -23.305 -8.349  1.00 17.94 ?  24   VAL   B HG12 1 
ATOM   4453 H  HG13 . VAL   B 1 24  ? 55.509 -22.050 -7.743  1.00 17.94 ?  24   VAL   B HG13 1 
ATOM   4454 H  HG21 . VAL   B 1 24  ? 54.899 -23.973 -5.239  1.00 18.21 ?  24   VAL   B HG21 1 
ATOM   4455 H  HG22 . VAL   B 1 24  ? 53.987 -22.741 -5.654  1.00 18.21 ?  24   VAL   B HG22 1 
ATOM   4456 H  HG23 . VAL   B 1 24  ? 53.386 -24.212 -5.659  1.00 18.21 ?  24   VAL   B HG23 1 
ATOM   4457 N  N    . GLU   B 1 25  ? 54.151 -24.631 -10.252 1.00 14.25 ?  25   GLU   B N    1 
ATOM   4458 C  CA   . GLU   B 1 25  ? 54.544 -24.664 -11.656 1.00 15.68 ?  25   GLU   B CA   1 
ATOM   4459 C  C    . GLU   B 1 25  ? 53.435 -24.117 -12.542 1.00 14.71 ?  25   GLU   B C    1 
ATOM   4460 O  O    . GLU   B 1 25  ? 53.704 -23.402 -13.517 1.00 15.82 ?  25   GLU   B O    1 
ATOM   4461 C  CB   . GLU   B 1 25  ? 54.937 -26.084 -12.058 1.00 20.01 ?  25   GLU   B CB   1 
ATOM   4462 C  CG   . GLU   B 1 25  ? 56.238 -26.538 -11.408 1.00 26.03 ?  25   GLU   B CG   1 
ATOM   4463 C  CD   . GLU   B 1 25  ? 57.349 -25.502 -11.497 1.00 31.25 ?  25   GLU   B CD   1 
ATOM   4464 O  OE1  . GLU   B 1 25  ? 57.705 -25.097 -12.624 1.00 33.16 ?  25   GLU   B OE1  1 
ATOM   4465 O  OE2  . GLU   B 1 25  ? 57.856 -25.075 -10.434 1.00 33.10 -1 25   GLU   B OE2  1 
ATOM   4466 H  H    . GLU   B 1 25  ? 54.111 -25.396 -9.868  1.00 17.12 ?  25   GLU   B H    1 
ATOM   4467 H  HA   . GLU   B 1 25  ? 55.304 -24.080 -11.782 1.00 18.83 ?  25   GLU   B HA   1 
ATOM   4468 H  HB2  . GLU   B 1 25  ? 54.236 -26.699 -11.780 1.00 24.02 ?  25   GLU   B HB2  1 
ATOM   4469 H  HB3  . GLU   B 1 25  ? 55.047 -26.124 -13.021 1.00 24.02 ?  25   GLU   B HB3  1 
ATOM   4470 H  HG2  . GLU   B 1 25  ? 56.085 -26.698 -10.470 1.00 31.25 ?  25   GLU   B HG2  1 
ATOM   4471 H  HG3  . GLU   B 1 25  ? 56.543 -27.347 -11.848 1.00 31.25 ?  25   GLU   B HG3  1 
ATOM   4472 N  N    A GLU   B 1 26  ? 52.180 -24.437 -12.216 0.62 14.00 ?  26   GLU   B N    1 
ATOM   4473 N  N    B GLU   B 1 26  ? 52.179 -24.437 -12.215 0.38 14.16 ?  26   GLU   B N    1 
ATOM   4474 C  CA   A GLU   B 1 26  ? 51.055 -23.907 -12.980 0.62 14.63 ?  26   GLU   B CA   1 
ATOM   4475 C  CA   B GLU   B 1 26  ? 51.052 -23.910 -12.978 0.38 14.35 ?  26   GLU   B CA   1 
ATOM   4476 C  C    A GLU   B 1 26  ? 51.003 -22.389 -12.898 0.62 13.58 ?  26   GLU   B C    1 
ATOM   4477 C  C    B GLU   B 1 26  ? 50.999 -22.391 -12.897 0.38 13.46 ?  26   GLU   B C    1 
ATOM   4478 O  O    A GLU   B 1 26  ? 50.801 -21.709 -13.910 0.62 15.04 ?  26   GLU   B O    1 
ATOM   4479 O  O    B GLU   B 1 26  ? 50.801 -21.711 -13.910 0.38 14.42 ?  26   GLU   B O    1 
ATOM   4480 C  CB   A GLU   B 1 26  ? 49.743 -24.494 -12.463 0.62 16.48 ?  26   GLU   B CB   1 
ATOM   4481 C  CB   B GLU   B 1 26  ? 49.740 -24.506 -12.462 0.38 15.61 ?  26   GLU   B CB   1 
ATOM   4482 C  CG   A GLU   B 1 26  ? 49.359 -25.815 -13.082 0.62 19.80 ?  26   GLU   B CG   1 
ATOM   4483 C  CG   B GLU   B 1 26  ? 49.254 -25.724 -13.222 0.38 17.92 ?  26   GLU   B CG   1 
ATOM   4484 C  CD   A GLU   B 1 26  ? 49.131 -25.730 -14.586 0.62 21.05 ?  26   GLU   B CD   1 
ATOM   4485 C  CD   B GLU   B 1 26  ? 48.896 -25.402 -14.675 0.38 18.12 ?  26   GLU   B CD   1 
ATOM   4486 O  OE1  A GLU   B 1 26  ? 48.301 -24.912 -15.036 0.62 20.99 ?  26   GLU   B OE1  1 
ATOM   4487 O  OE1  B GLU   B 1 26  ? 47.769 -24.917 -14.941 0.38 18.91 ?  26   GLU   B OE1  1 
ATOM   4488 O  OE2  A GLU   B 1 26  ? 49.795 -26.484 -15.319 0.62 22.08 -1 26   GLU   B OE2  1 
ATOM   4489 O  OE2  B GLU   B 1 26  ? 49.754 -25.623 -15.547 0.38 17.80 -1 26   GLU   B OE2  1 
ATOM   4490 H  H    A GLU   B 1 26  ? 51.955 -24.952 -11.562 0.62 16.81 ?  26   GLU   B H    1 
ATOM   4491 H  H    B GLU   B 1 26  ? 51.956 -24.952 -11.561 0.38 17.00 ?  26   GLU   B H    1 
ATOM   4492 H  HA   A GLU   B 1 26  ? 51.158 -24.152 -13.910 0.62 17.57 ?  26   GLU   B HA   1 
ATOM   4493 H  HA   B GLU   B 1 26  ? 51.158 -24.154 -13.908 0.38 17.24 ?  26   GLU   B HA   1 
ATOM   4494 H  HB2  A GLU   B 1 26  ? 49.820 -24.625 -11.503 0.62 19.79 ?  26   GLU   B HB2  1 
ATOM   4495 H  HB2  B GLU   B 1 26  ? 49.859 -24.760 -11.534 0.38 18.75 ?  26   GLU   B HB2  1 
ATOM   4496 H  HB3  A GLU   B 1 26  ? 49.029 -23.859 -12.643 0.62 19.79 ?  26   GLU   B HB3  1 
ATOM   4497 H  HB3  B GLU   B 1 26  ? 49.048 -23.828 -12.527 0.38 18.75 ?  26   GLU   B HB3  1 
ATOM   4498 H  HG2  A GLU   B 1 26  ? 50.078 -26.435 -12.925 0.62 23.78 ?  26   GLU   B HG2  1 
ATOM   4499 H  HG2  B GLU   B 1 26  ? 49.950 -26.404 -13.175 0.38 21.51 ?  26   GLU   B HG2  1 
ATOM   4500 H  HG3  A GLU   B 1 26  ? 48.542 -26.120 -12.664 0.62 23.78 ?  26   GLU   B HG3  1 
ATOM   4501 H  HG3  B GLU   B 1 26  ? 48.446 -26.049 -12.805 0.38 21.51 ?  26   GLU   B HG3  1 
ATOM   4502 N  N    . ALA   B 1 27  ? 51.152 -21.839 -11.690 1.00 12.66 ?  27   ALA   B N    1 
ATOM   4503 C  CA   . ALA   B 1 27  ? 51.114 -20.392 -11.536 1.00 13.10 ?  27   ALA   B CA   1 
ATOM   4504 C  C    . ALA   B 1 27  ? 52.185 -19.728 -12.395 1.00 13.89 ?  27   ALA   B C    1 
ATOM   4505 O  O    . ALA   B 1 27  ? 51.922 -18.732 -13.081 1.00 14.75 ?  27   ALA   B O    1 
ATOM   4506 C  CB   . ALA   B 1 27  ? 51.277 -20.020 -10.061 1.00 13.16 ?  27   ALA   B CB   1 
ATOM   4507 H  H    A ALA   B 1 27  ? 51.269 -22.275 -10.957 0.62 15.20 ?  27   ALA   B H    1 
ATOM   4508 H  H    B ALA   B 1 27  ? 51.273 -22.275 -10.957 0.38 15.20 ?  27   ALA   B H    1 
ATOM   4509 H  HA   . ALA   B 1 27  ? 50.253 -20.060 -11.826 1.00 15.74 ?  27   ALA   B HA   1 
ATOM   4510 H  HB1  . ALA   B 1 27  ? 51.245 -19.053 -9.969  1.00 15.81 ?  27   ALA   B HB1  1 
ATOM   4511 H  HB2  . ALA   B 1 27  ? 50.551 -20.419 -9.552  1.00 15.81 ?  27   ALA   B HB2  1 
ATOM   4512 H  HB3  . ALA   B 1 27  ? 52.127 -20.354 -9.738  1.00 15.81 ?  27   ALA   B HB3  1 
ATOM   4513 N  N    . LYS   B 1 28  ? 53.400 -20.278 -12.390 1.00 15.43 ?  28   LYS   B N    1 
ATOM   4514 C  CA   . LYS   B 1 28  ? 54.477 -19.653 -13.148 1.00 17.43 ?  28   LYS   B CA   1 
ATOM   4515 C  C    . LYS   B 1 28  ? 54.230 -19.730 -14.650 1.00 18.04 ?  28   LYS   B C    1 
ATOM   4516 O  O    . LYS   B 1 28  ? 54.644 -18.828 -15.391 1.00 19.43 ?  28   LYS   B O    1 
ATOM   4517 C  CB   . LYS   B 1 28  ? 55.829 -20.252 -12.747 1.00 21.08 ?  28   LYS   B CB   1 
ATOM   4518 C  CG   . LYS   B 1 28  ? 56.225 -19.910 -11.311 1.00 25.11 ?  28   LYS   B CG   1 
ATOM   4519 C  CD   . LYS   B 1 28  ? 57.651 -20.322 -10.976 1.00 30.21 ?  28   LYS   B CD   1 
ATOM   4520 C  CE   . LYS   B 1 28  ? 57.752 -21.802 -10.696 1.00 34.05 ?  28   LYS   B CE   1 
ATOM   4521 N  NZ   . LYS   B 1 28  ? 59.112 -22.177 -10.219 1.00 35.86 ?  28   LYS   B NZ   1 
ATOM   4522 H  H    . LYS   B 1 28  ? 53.617 -20.997 -11.970 1.00 18.53 ?  28   LYS   B H    1 
ATOM   4523 H  HA   . LYS   B 1 28  ? 54.505 -18.715 -12.917 1.00 20.94 ?  28   LYS   B HA   1 
ATOM   4524 H  HB2  . LYS   B 1 28  ? 55.789 -21.217 -12.821 1.00 25.31 ?  28   LYS   B HB2  1 
ATOM   4525 H  HB3  . LYS   B 1 28  ? 56.520 -19.903 -13.335 1.00 25.31 ?  28   LYS   B HB3  1 
ATOM   4526 H  HG2  . LYS   B 1 28  ? 56.150 -18.949 -11.185 1.00 30.15 ?  28   LYS   B HG2  1 
ATOM   4527 H  HG3  . LYS   B 1 28  ? 55.627 -20.370 -10.702 1.00 30.15 ?  28   LYS   B HG3  1 
ATOM   4528 H  HD2  . LYS   B 1 28  ? 58.227 -20.111 -11.728 1.00 36.27 ?  28   LYS   B HD2  1 
ATOM   4529 H  HD3  . LYS   B 1 28  ? 57.942 -19.839 -10.186 1.00 36.27 ?  28   LYS   B HD3  1 
ATOM   4530 H  HE2  . LYS   B 1 28  ? 57.110 -22.040 -10.008 1.00 40.87 ?  28   LYS   B HE2  1 
ATOM   4531 H  HE3  . LYS   B 1 28  ? 57.567 -22.294 -11.511 1.00 40.87 ?  28   LYS   B HE3  1 
ATOM   4532 H  HZ1  . LYS   B 1 28  ? 59.148 -23.051 -10.060 1.00 43.04 ?  28   LYS   B HZ1  1 
ATOM   4533 H  HZ2  . LYS   B 1 28  ? 59.718 -21.969 -10.837 1.00 43.04 ?  28   LYS   B HZ2  1 
ATOM   4534 H  HZ3  . LYS   B 1 28  ? 59.302 -21.738 -9.468  1.00 43.04 ?  28   LYS   B HZ3  1 
ATOM   4535 N  N    . LYS   B 1 29  ? 53.538 -20.770 -15.116 1.00 19.13 ?  29   LYS   B N    1 
ATOM   4536 C  CA   . LYS   B 1 29  ? 53.252 -20.911 -16.541 1.00 21.93 ?  29   LYS   B CA   1 
ATOM   4537 C  C    . LYS   B 1 29  ? 52.005 -20.147 -16.976 1.00 21.04 ?  29   LYS   B C    1 
ATOM   4538 O  O    . LYS   B 1 29  ? 52.009 -19.512 -18.037 1.00 22.72 ?  29   LYS   B O    1 
ATOM   4539 C  CB   . LYS   B 1 29  ? 53.102 -22.393 -16.901 1.00 26.77 ?  29   LYS   B CB   1 
ATOM   4540 C  CG   . LYS   B 1 29  ? 52.944 -22.654 -18.393 1.00 31.33 ?  29   LYS   B CG   1 
ATOM   4541 C  CD   . LYS   B 1 29  ? 53.133 -24.129 -18.731 1.00 34.88 ?  29   LYS   B CD   1 
ATOM   4542 C  CE   . LYS   B 1 29  ? 52.010 -24.987 -18.170 1.00 37.21 ?  29   LYS   B CE   1 
ATOM   4543 N  NZ   . LYS   B 1 29  ? 52.211 -26.433 -18.479 1.00 38.59 ?  29   LYS   B NZ   1 
ATOM   4544 H  H    . LYS   B 1 29  ? 53.222 -21.409 -14.625 1.00 22.97 ?  29   LYS   B H    1 
ATOM   4545 H  HA   . LYS   B 1 29  ? 54.002 -20.560 -17.042 1.00 26.33 ?  29   LYS   B HA   1 
ATOM   4546 H  HB2  . LYS   B 1 29  ? 53.895 -22.867 -16.601 1.00 32.14 ?  29   LYS   B HB2  1 
ATOM   4547 H  HB3  . LYS   B 1 29  ? 52.320 -22.745 -16.454 1.00 32.14 ?  29   LYS   B HB3  1 
ATOM   4548 H  HG2  . LYS   B 1 29  ? 52.052 -22.392 -18.670 1.00 37.62 ?  29   LYS   B HG2  1 
ATOM   4549 H  HG3  . LYS   B 1 29  ? 53.610 -22.144 -18.880 1.00 37.62 ?  29   LYS   B HG3  1 
ATOM   4550 H  HD2  . LYS   B 1 29  ? 53.143 -24.238 -19.695 1.00 41.87 ?  29   LYS   B HD2  1 
ATOM   4551 H  HD3  . LYS   B 1 29  ? 53.970 -24.440 -18.351 1.00 41.87 ?  29   LYS   B HD3  1 
ATOM   4552 H  HE2  . LYS   B 1 29  ? 51.980 -24.887 -17.206 1.00 44.66 ?  29   LYS   B HE2  1 
ATOM   4553 H  HE3  . LYS   B 1 29  ? 51.168 -24.707 -18.562 1.00 44.66 ?  29   LYS   B HE3  1 
ATOM   4554 H  HZ1  . LYS   B 1 29  ? 51.542 -26.912 -18.140 1.00 46.32 ?  29   LYS   B HZ1  1 
ATOM   4555 H  HZ2  . LYS   B 1 29  ? 52.237 -26.555 -19.360 1.00 46.32 ?  29   LYS   B HZ2  1 
ATOM   4556 H  HZ3  . LYS   B 1 29  ? 52.977 -26.716 -18.125 1.00 46.32 ?  29   LYS   B HZ3  1 
ATOM   4557 N  N    . VAL   B 1 30  ? 50.938 -20.204 -16.173 1.00 19.11 ?  30   VAL   B N    1 
ATOM   4558 C  CA   . VAL   B 1 30  ? 49.646 -19.623 -16.547 1.00 19.73 ?  30   VAL   B CA   1 
ATOM   4559 C  C    . VAL   B 1 30  ? 49.642 -18.111 -16.388 1.00 18.45 ?  30   VAL   B C    1 
ATOM   4560 O  O    . VAL   B 1 30  ? 48.904 -17.401 -17.090 1.00 19.20 ?  30   VAL   B O    1 
ATOM   4561 C  CB   . VAL   B 1 30  ? 48.541 -20.252 -15.673 1.00 21.46 ?  30   VAL   B CB   1 
ATOM   4562 C  CG1  . VAL   B 1 30  ? 47.247 -19.444 -15.741 1.00 21.99 ?  30   VAL   B CG1  1 
ATOM   4563 C  CG2  . VAL   B 1 30  ? 48.306 -21.705 -16.067 1.00 22.66 ?  30   VAL   B CG2  1 
ATOM   4564 H  H    . VAL   B 1 30  ? 50.932 -20.594 -15.396 1.00 22.94 ?  30   VAL   B H    1 
ATOM   4565 H  HA   . VAL   B 1 30  ? 49.455 -19.856 -17.470 1.00 23.70 ?  30   VAL   B HA   1 
ATOM   4566 H  HB   . VAL   B 1 30  ? 48.833 -20.259 -14.748 1.00 25.77 ?  30   VAL   B HB   1 
ATOM   4567 H  HG11 . VAL   B 1 30  ? 46.507 -20.025 -15.500 1.00 26.40 ?  30   VAL   B HG11 1 
ATOM   4568 H  HG12 . VAL   B 1 30  ? 47.300 -18.708 -15.115 1.00 26.40 ?  30   VAL   B HG12 1 
ATOM   4569 H  HG13 . VAL   B 1 30  ? 47.121 -19.121 -16.641 1.00 26.40 ?  30   VAL   B HG13 1 
ATOM   4570 H  HG21 . VAL   B 1 30  ? 47.613 -22.086 -15.497 1.00 27.21 ?  30   VAL   B HG21 1 
ATOM   4571 H  HG22 . VAL   B 1 30  ? 48.018 -21.741 -16.994 1.00 27.21 ?  30   VAL   B HG22 1 
ATOM   4572 H  HG23 . VAL   B 1 30  ? 49.129 -22.204 -15.957 1.00 27.21 ?  30   VAL   B HG23 1 
ATOM   4573 N  N    . LYS   B 1 31  ? 50.424 -17.609 -15.450 1.00 18.21 ?  31   LYS   B N    1 
ATOM   4574 C  CA   . LYS   B 1 31  ? 50.446 -16.199 -15.096 1.00 18.71 ?  31   LYS   B CA   1 
ATOM   4575 C  C    . LYS   B 1 31  ? 49.049 -15.720 -14.703 1.00 16.22 ?  31   LYS   B C    1 
ATOM   4576 O  O    . LYS   B 1 31  ? 48.512 -14.799 -15.329 1.00 17.24 ?  31   LYS   B O    1 
ATOM   4577 C  CB   . LYS   B 1 31  ? 51.073 -15.384 -16.233 1.00 21.88 ?  31   LYS   B CB   1 
ATOM   4578 C  CG   . LYS   B 1 31  ? 52.513 -15.807 -16.540 1.00 25.34 ?  31   LYS   B CG   1 
ATOM   4579 C  CD   . LYS   B 1 31  ? 53.101 -15.042 -17.713 1.00 28.79 ?  31   LYS   B CD   1 
ATOM   4580 C  CE   . LYS   B 1 31  ? 54.593 -15.272 -17.832 1.00 31.31 ?  31   LYS   B CE   1 
ATOM   4581 N  NZ   . LYS   B 1 31  ? 55.299 -14.836 -16.597 1.00 32.60 ?  31   LYS   B NZ   1 
ATOM   4582 H  H    . LYS   B 1 31  ? 50.972 -18.099 -15.000 1.00 21.87 ?  31   LYS   B H    1 
ATOM   4583 H  HA   . LYS   B 1 31  ? 51.009 -16.115 -14.330 1.00 22.46 ?  31   LYS   B HA   1 
ATOM   4584 H  HB2  . LYS   B 1 31  ? 50.547 -15.500 -17.041 1.00 26.27 ?  31   LYS   B HB2  1 
ATOM   4585 H  HB3  . LYS   B 1 31  ? 51.080 -14.456 -15.967 1.00 26.27 ?  31   LYS   B HB3  1 
ATOM   4586 H  HG2  . LYS   B 1 31  ? 53.059 -15.642 -15.755 1.00 30.42 ?  31   LYS   B HG2  1 
ATOM   4587 H  HG3  . LYS   B 1 31  ? 52.527 -16.756 -16.757 1.00 30.42 ?  31   LYS   B HG3  1 
ATOM   4588 H  HD2  . LYS   B 1 31  ? 52.677 -15.345 -18.530 1.00 34.57 ?  31   LYS   B HD2  1 
ATOM   4589 H  HD3  . LYS   B 1 31  ? 52.946 -14.097 -17.580 1.00 34.57 ?  31   LYS   B HD3  1 
ATOM   4590 H  HE2  . LYS   B 1 31  ? 54.766 -16.219 -17.966 1.00 37.59 ?  31   LYS   B HE2  1 
ATOM   4591 H  HE3  . LYS   B 1 31  ? 54.938 -14.759 -18.580 1.00 37.59 ?  31   LYS   B HE3  1 
ATOM   4592 H  HZ1  . LYS   B 1 31  ? 56.177 -14.833 -16.732 1.00 39.13 ?  31   LYS   B HZ1  1 
ATOM   4593 H  HZ2  . LYS   B 1 31  ? 55.037 -14.016 -16.372 1.00 39.13 ?  31   LYS   B HZ2  1 
ATOM   4594 H  HZ3  . LYS   B 1 31  ? 55.112 -15.392 -15.926 1.00 39.13 ?  31   LYS   B HZ3  1 
ATOM   4595 N  N    . PRO   B 1 32  ? 48.437 -16.311 -13.670 1.00 14.00 ?  32   PRO   B N    1 
ATOM   4596 C  CA   . PRO   B 1 32  ? 47.062 -15.948 -13.311 1.00 13.02 ?  32   PRO   B CA   1 
ATOM   4597 C  C    . PRO   B 1 32  ? 46.988 -14.604 -12.604 1.00 13.28 ?  32   PRO   B C    1 
ATOM   4598 O  O    . PRO   B 1 32  ? 47.915 -14.190 -11.903 1.00 14.76 ?  32   PRO   B O    1 
ATOM   4599 C  CB   . PRO   B 1 32  ? 46.663 -17.066 -12.340 1.00 13.37 ?  32   PRO   B CB   1 
ATOM   4600 C  CG   . PRO   B 1 32  ? 47.962 -17.398 -11.651 1.00 13.41 ?  32   PRO   B CG   1 
ATOM   4601 C  CD   . PRO   B 1 32  ? 49.012 -17.286 -12.724 1.00 13.90 ?  32   PRO   B CD   1 
ATOM   4602 H  HA   . PRO   B 1 32  ? 46.477 -15.962 -14.096 1.00 15.64 ?  32   PRO   B HA   1 
ATOM   4603 H  HB2  . PRO   B 1 32  ? 46.007 -16.735 -11.707 1.00 16.06 ?  32   PRO   B HB2  1 
ATOM   4604 H  HB3  . PRO   B 1 32  ? 46.323 -17.833 -12.828 1.00 16.06 ?  32   PRO   B HB3  1 
ATOM   4605 H  HG2  . PRO   B 1 32  ? 48.127 -16.755 -10.941 1.00 16.11 ?  32   PRO   B HG2  1 
ATOM   4606 H  HG3  . PRO   B 1 32  ? 47.927 -18.298 -11.299 1.00 16.11 ?  32   PRO   B HG3  1 
ATOM   4607 H  HD2  . PRO   B 1 32  ? 49.837 -16.938 -12.357 1.00 16.70 ?  32   PRO   B HD2  1 
ATOM   4608 H  HD3  . PRO   B 1 32  ? 49.142 -18.139 -13.160 1.00 16.70 ?  32   PRO   B HD3  1 
ATOM   4609 N  N    . THR   B 1 33  ? 45.836 -13.943 -12.763 1.00 12.73 ?  33   THR   B N    1 
ATOM   4610 C  CA   . THR   B 1 33  ? 45.553 -12.767 -11.947 1.00 13.20 ?  33   THR   B CA   1 
ATOM   4611 C  C    . THR   B 1 33  ? 45.510 -13.124 -10.465 1.00 12.59 ?  33   THR   B C    1 
ATOM   4612 O  O    . THR   B 1 33  ? 45.982 -12.348 -9.622  1.00 13.75 ?  33   THR   B O    1 
ATOM   4613 C  CB   . THR   B 1 33  ? 44.231 -12.131 -12.386 1.00 13.81 ?  33   THR   B CB   1 
ATOM   4614 O  OG1  . THR   B 1 33  ? 44.261 -11.880 -13.793 1.00 14.22 ?  33   THR   B OG1  1 
ATOM   4615 C  CG2  . THR   B 1 33  ? 43.993 -10.835 -11.645 1.00 15.11 ?  33   THR   B CG2  1 
ATOM   4616 H  H    . THR   B 1 33  ? 45.212 -14.162 -13.321 1.00 15.29 ?  33   THR   B H    1 
ATOM   4617 H  HA   . THR   B 1 33  ? 46.258 -12.121 -12.085 1.00 15.85 ?  33   THR   B HA   1 
ATOM   4618 H  HB   . THR   B 1 33  ? 43.499 -12.740 -12.187 1.00 16.59 ?  33   THR   B HB   1 
ATOM   4619 H  HG1  . THR   B 1 33  ? 43.538 -11.514 -14.037 1.00 17.07 ?  33   THR   B HG1  1 
ATOM   4620 H  HG21 . THR   B 1 33  ? 43.239 -10.368 -12.028 1.00 18.15 ?  33   THR   B HG21 1 
ATOM   4621 H  HG22 . THR   B 1 33  ? 43.815 -11.015 -10.708 1.00 18.15 ?  33   THR   B HG22 1 
ATOM   4622 H  HG23 . THR   B 1 33  ? 44.782 -10.270 -11.711 1.00 18.15 ?  33   THR   B HG23 1 
ATOM   4623 N  N    . VAL   B 1 34  ? 44.950 -14.290 -10.126 1.00 11.84 ?  34   VAL   B N    1 
ATOM   4624 C  CA   . VAL   B 1 34  ? 44.759 -14.690 -8.736  1.00 11.27 ?  34   VAL   B CA   1 
ATOM   4625 C  C    . VAL   B 1 34  ? 45.182 -16.141 -8.571  1.00 10.37 ?  34   VAL   B C    1 
ATOM   4626 O  O    . VAL   B 1 34  ? 44.653 -17.024 -9.255  1.00 11.35 ?  34   VAL   B O    1 
ATOM   4627 C  CB   . VAL   B 1 34  ? 43.289 -14.542 -8.285  1.00 12.52 ?  34   VAL   B CB   1 
ATOM   4628 C  CG1  . VAL   B 1 34  ? 43.127 -14.992 -6.835  1.00 12.78 ?  34   VAL   B CG1  1 
ATOM   4629 C  CG2  . VAL   B 1 34  ? 42.793 -13.125 -8.488  1.00 13.66 ?  34   VAL   B CG2  1 
ATOM   4630 H  H    . VAL   B 1 34  ? 44.680 -14.879 -10.695 1.00 14.22 ?  34   VAL   B H    1 
ATOM   4631 H  HA   . VAL   B 1 34  ? 45.316 -14.141 -8.161  1.00 13.54 ?  34   VAL   B HA   1 
ATOM   4632 H  HB   . VAL   B 1 34  ? 42.741 -15.123 -8.838  1.00 15.04 ?  34   VAL   B HB   1 
ATOM   4633 H  HG11 . VAL   B 1 34  ? 42.274 -14.676 -6.502  1.00 15.35 ?  34   VAL   B HG11 1 
ATOM   4634 H  HG12 . VAL   B 1 34  ? 43.157 -15.962 -6.798  1.00 15.35 ?  34   VAL   B HG12 1 
ATOM   4635 H  HG13 . VAL   B 1 34  ? 43.849 -14.617 -6.307  1.00 15.35 ?  34   VAL   B HG13 1 
ATOM   4636 H  HG21 . VAL   B 1 34  ? 41.879 -13.062 -8.170  1.00 16.41 ?  34   VAL   B HG21 1 
ATOM   4637 H  HG22 . VAL   B 1 34  ? 43.361 -12.517 -7.995  1.00 16.41 ?  34   VAL   B HG22 1 
ATOM   4638 H  HG23 . VAL   B 1 34  ? 42.825 -12.911 -9.438  1.00 16.41 ?  34   VAL   B HG23 1 
ATOM   4639 N  N    . VAL   B 1 35  ? 46.088 -16.393 -7.632  1.00 10.04 ?  35   VAL   B N    1 
ATOM   4640 C  CA   . VAL   B 1 35  ? 46.321 -17.737 -7.114  1.00 9.87  ?  35   VAL   B CA   1 
ATOM   4641 C  C    . VAL   B 1 35  ? 45.778 -17.795 -5.695  1.00 9.53  ?  35   VAL   B C    1 
ATOM   4642 O  O    . VAL   B 1 35  ? 46.008 -16.878 -4.897  1.00 10.00 ?  35   VAL   B O    1 
ATOM   4643 C  CB   . VAL   B 1 35  ? 47.804 -18.172 -7.193  1.00 10.51 ?  35   VAL   B CB   1 
ATOM   4644 C  CG1  . VAL   B 1 35  ? 48.714 -17.335 -6.285  1.00 11.34 ?  35   VAL   B CG1  1 
ATOM   4645 C  CG2  . VAL   B 1 35  ? 47.942 -19.661 -6.873  1.00 11.22 ?  35   VAL   B CG2  1 
ATOM   4646 H  H    . VAL   B 1 35  ? 46.590 -15.791 -7.272  1.00 12.06 ?  35   VAL   B H    1 
ATOM   4647 H  HA   . VAL   B 1 35  ? 45.807 -18.364 -7.640  1.00 11.86 ?  35   VAL   B HA   1 
ATOM   4648 H  HB   . VAL   B 1 35  ? 48.108 -18.052 -8.108  1.00 12.63 ?  35   VAL   B HB   1 
ATOM   4649 H  HG11 . VAL   B 1 35  ? 49.634 -17.579 -6.459  1.00 13.62 ?  35   VAL   B HG11 1 
ATOM   4650 H  HG12 . VAL   B 1 35  ? 48.567 -16.402 -6.478  1.00 13.62 ?  35   VAL   B HG12 1 
ATOM   4651 H  HG13 . VAL   B 1 35  ? 48.488 -17.527 -5.360  1.00 13.62 ?  35   VAL   B HG13 1 
ATOM   4652 H  HG21 . VAL   B 1 35  ? 48.862 -19.935 -6.981  1.00 13.48 ?  35   VAL   B HG21 1 
ATOM   4653 H  HG22 . VAL   B 1 35  ? 47.658 -19.819 -5.952  1.00 13.48 ?  35   VAL   B HG22 1 
ATOM   4654 H  HG23 . VAL   B 1 35  ? 47.372 -20.177 -7.473  1.00 13.48 ?  35   VAL   B HG23 1 
ATOM   4655 N  N    . VAL   B 1 36  ? 45.063 -18.877 -5.378  1.00 9.46  ?  36   VAL   B N    1 
ATOM   4656 C  CA   . VAL   B 1 36  ? 44.520 -19.081 -4.045  1.00 9.36  ?  36   VAL   B CA   1 
ATOM   4657 C  C    . VAL   B 1 36  ? 45.531 -19.837 -3.195  1.00 9.10  ?  36   VAL   B C    1 
ATOM   4658 O  O    . VAL   B 1 36  ? 46.063 -20.872 -3.613  1.00 10.15 ?  36   VAL   B O    1 
ATOM   4659 C  CB   . VAL   B 1 36  ? 43.187 -19.843 -4.117  1.00 9.69  ?  36   VAL   B CB   1 
ATOM   4660 C  CG1  . VAL   B 1 36  ? 42.681 -20.196 -2.722  1.00 10.37 ?  36   VAL   B CG1  1 
ATOM   4661 C  CG2  . VAL   B 1 36  ? 42.158 -19.023 -4.874  1.00 10.58 ?  36   VAL   B CG2  1 
ATOM   4662 H  H    . VAL   B 1 36  ? 44.893 -19.517 -5.927  1.00 11.37 ?  36   VAL   B H    1 
ATOM   4663 H  HA   . VAL   B 1 36  ? 44.355 -18.222 -3.629  1.00 11.25 ?  36   VAL   B HA   1 
ATOM   4664 H  HB   . VAL   B 1 36  ? 43.319 -20.671 -4.602  1.00 11.65 ?  36   VAL   B HB   1 
ATOM   4665 H  HG11 . VAL   B 1 36  ? 41.744 -20.436 -2.774  1.00 12.47 ?  36   VAL   B HG11 1 
ATOM   4666 H  HG12 . VAL   B 1 36  ? 43.195 -20.938 -2.373  1.00 12.47 ?  36   VAL   B HG12 1 
ATOM   4667 H  HG13 . VAL   B 1 36  ? 42.786 -19.418 -2.143  1.00 12.47 ?  36   VAL   B HG13 1 
ATOM   4668 H  HG21 . VAL   B 1 36  ? 41.314 -19.501 -4.890  1.00 12.71 ?  36   VAL   B HG21 1 
ATOM   4669 H  HG22 . VAL   B 1 36  ? 42.045 -18.166 -4.435  1.00 12.71 ?  36   VAL   B HG22 1 
ATOM   4670 H  HG23 . VAL   B 1 36  ? 42.472 -18.884 -5.786  1.00 12.71 ?  36   VAL   B HG23 1 
ATOM   4671 N  N    . ASN   B 1 37  ? 45.757 -19.343 -1.980  1.00 9.28  ?  37   ASN   B N    1 
ATOM   4672 C  CA   . ASN   B 1 37  ? 46.506 -20.070 -0.967  1.00 9.94  ?  37   ASN   B CA   1 
ATOM   4673 C  C    . ASN   B 1 37  ? 45.554 -20.739 0.018   1.00 9.75  ?  37   ASN   B C    1 
ATOM   4674 O  O    . ASN   B 1 37  ? 44.542 -20.157 0.425   1.00 10.31 ?  37   ASN   B O    1 
ATOM   4675 C  CB   . ASN   B 1 37  ? 47.429 -19.124 -0.204  1.00 9.73  ?  37   ASN   B CB   1 
ATOM   4676 C  CG   . ASN   B 1 37  ? 48.285 -19.839 0.805   1.00 9.83  ?  37   ASN   B CG   1 
ATOM   4677 O  OD1  . ASN   B 1 37  ? 48.620 -21.014 0.631   1.00 10.74 ?  37   ASN   B OD1  1 
ATOM   4678 N  ND2  . ASN   B 1 37  ? 48.639 -19.140 1.877   1.00 10.21 ?  37   ASN   B ND2  1 
ATOM   4679 H  H    . ASN   B 1 37  ? 45.488 -18.569 -1.714  1.00 11.15 ?  37   ASN   B H    1 
ATOM   4680 H  HA   . ASN   B 1 37  ? 47.042 -20.762 -1.380  1.00 11.94 ?  37   ASN   B HA   1 
ATOM   4681 H  HB2  . ASN   B 1 37  ? 48.019 -18.690 -0.833  1.00 11.69 ?  37   ASN   B HB2  1 
ATOM   4682 H  HB3  . ASN   B 1 37  ? 46.895 -18.470 0.270   1.00 11.69 ?  37   ASN   B HB3  1 
ATOM   4683 H  HD21 . ASN   B 1 37  ? 49.129 -19.505 2.486   1.00 12.27 ?  37   ASN   B HD21 1 
ATOM   4684 H  HD22 . ASN   B 1 37  ? 48.380 -18.333 1.971   1.00 12.27 ?  37   ASN   B HD22 1 
ATOM   4685 N  N    . ALA   B 1 38  ? 45.899 -21.971 0.397   1.00 9.99  ?  38   ALA   B N    1 
ATOM   4686 C  CA   . ALA   B 1 38  ? 45.251 -22.710 1.481   1.00 10.40 ?  38   ALA   B CA   1 
ATOM   4687 C  C    . ALA   B 1 38  ? 45.846 -22.228 2.803   1.00 10.30 ?  38   ALA   B C    1 
ATOM   4688 O  O    . ALA   B 1 38  ? 46.746 -22.843 3.386   1.00 11.14 ?  38   ALA   B O    1 
ATOM   4689 C  CB   . ALA   B 1 38  ? 45.466 -24.204 1.290   1.00 11.83 ?  38   ALA   B CB   1 
ATOM   4690 H  H    . ALA   B 1 38  ? 46.542 -22.410 0.038   1.00 12.00 ?  38   ALA   B H    1 
ATOM   4691 H  HA   . ALA   B 1 38  ? 44.297 -22.525 1.481   1.00 12.50 ?  38   ALA   B HA   1 
ATOM   4692 H  HB1  . ALA   B 1 38  ? 45.024 -24.680 2.019   1.00 14.21 ?  38   ALA   B HB1  1 
ATOM   4693 H  HB2  . ALA   B 1 38  ? 45.078 -24.472 0.445   1.00 14.21 ?  38   ALA   B HB2  1 
ATOM   4694 H  HB3  . ALA   B 1 38  ? 46.413 -24.392 1.303   1.00 14.21 ?  38   ALA   B HB3  1 
ATOM   4695 N  N    . ALA   B 1 39  ? 45.333 -21.089 3.267   1.00 9.89  ?  39   ALA   B N    1 
ATOM   4696 C  CA   . ALA   B 1 39  ? 45.881 -20.356 4.397   1.00 10.35 ?  39   ALA   B CA   1 
ATOM   4697 C  C    . ALA   B 1 39  ? 45.265 -20.804 5.719   1.00 10.45 ?  39   ALA   B C    1 
ATOM   4698 O  O    . ALA   B 1 39  ? 44.234 -21.477 5.769   1.00 11.11 ?  39   ALA   B O    1 
ATOM   4699 C  CB   . ALA   B 1 39  ? 45.640 -18.855 4.202   1.00 11.20 ?  39   ALA   B CB   1 
ATOM   4700 H  H    . ALA   B 1 39  ? 44.635 -20.712 2.926   1.00 11.89 ?  39   ALA   B H    1 
ATOM   4701 H  HA   . ALA   B 1 39  ? 46.837 -20.506 4.436   1.00 12.43 ?  39   ALA   B HA   1 
ATOM   4702 H  HB1  . ALA   B 1 39  ? 46.012 -18.376 4.958   1.00 13.45 ?  39   ALA   B HB1  1 
ATOM   4703 H  HB2  . ALA   B 1 39  ? 46.074 -18.567 3.382   1.00 13.45 ?  39   ALA   B HB2  1 
ATOM   4704 H  HB3  . ALA   B 1 39  ? 44.685 -18.692 4.144   1.00 13.45 ?  39   ALA   B HB3  1 
ATOM   4705 N  N    . ASN   B 1 40  ? 45.915 -20.394 6.802   1.00 11.22 ?  40   ASN   B N    1 
ATOM   4706 C  CA   . ASN   B 1 40  ? 45.356 -20.434 8.144   1.00 11.72 ?  40   ASN   B CA   1 
ATOM   4707 C  C    . ASN   B 1 40  ? 45.171 -19.004 8.659   1.00 11.53 ?  40   ASN   B C    1 
ATOM   4708 O  O    . ASN   B 1 40  ? 45.585 -18.027 8.025   1.00 11.55 ?  40   ASN   B O    1 
ATOM   4709 C  CB   . ASN   B 1 40  ? 46.213 -21.301 9.083   1.00 12.53 ?  40   ASN   B CB   1 
ATOM   4710 C  CG   . ASN   B 1 40  ? 47.667 -20.890 9.101   1.00 13.57 ?  40   ASN   B CG   1 
ATOM   4711 O  OD1  . ASN   B 1 40  ? 47.983 -19.706 9.180   1.00 15.70 ?  40   ASN   B OD1  1 
ATOM   4712 N  ND2  . ASN   B 1 40  ? 48.563 -21.864 9.031   1.00 13.89 ?  40   ASN   B ND2  1 
ATOM   4713 H  H    . ASN   B 1 40  ? 46.717 -20.073 6.784   1.00 13.48 ?  40   ASN   B H    1 
ATOM   4714 H  HA   . ASN   B 1 40  ? 44.475 -20.838 8.100   1.00 14.08 ?  40   ASN   B HA   1 
ATOM   4715 H  HB2  . ASN   B 1 40  ? 45.865 -21.223 9.988   1.00 15.05 ?  40   ASN   B HB2  1 
ATOM   4716 H  HB3  . ASN   B 1 40  ? 46.161 -22.224 8.790   1.00 15.05 ?  40   ASN   B HB3  1 
ATOM   4717 H  HD21 . ASN   B 1 40  ? 49.403 -21.680 9.042   1.00 16.68 ?  40   ASN   B HD21 1 
ATOM   4718 H  HD22 . ASN   B 1 40  ? 48.304 -22.684 8.976   1.00 16.68 ?  40   ASN   B HD22 1 
ATOM   4719 N  N    . VAL   B 1 41  ? 44.520 -18.874 9.819   1.00 11.97 ?  41   VAL   B N    1 
ATOM   4720 C  CA   . VAL   B 1 41  ? 44.062 -17.553 10.267  1.00 12.34 ?  41   VAL   B CA   1 
ATOM   4721 C  C    . VAL   B 1 41  ? 45.211 -16.592 10.558  1.00 12.03 ?  41   VAL   B C    1 
ATOM   4722 O  O    . VAL   B 1 41  ? 45.027 -15.372 10.472  1.00 12.29 ?  41   VAL   B O    1 
ATOM   4723 C  CB   . VAL   B 1 41  ? 43.092 -17.633 11.464  1.00 13.91 ?  41   VAL   B CB   1 
ATOM   4724 C  CG1  . VAL   B 1 41  ? 41.791 -18.320 11.072  1.00 14.36 ?  41   VAL   B CG1  1 
ATOM   4725 C  CG2  . VAL   B 1 41  ? 43.750 -18.312 12.655  1.00 14.92 ?  41   VAL   B CG2  1 
ATOM   4726 H  H    . VAL   B 1 41  ? 44.325 -19.520 10.352  1.00 14.38 ?  41   VAL   B H    1 
ATOM   4727 H  HA   . VAL   B 1 41  ? 43.553 -17.162 9.537   1.00 14.82 ?  41   VAL   B HA   1 
ATOM   4728 H  HB   . VAL   B 1 41  ? 42.864 -16.729 11.737  1.00 16.71 ?  41   VAL   B HB   1 
ATOM   4729 H  HG11 . VAL   B 1 41  ? 41.194 -18.332 11.839  1.00 17.25 ?  41   VAL   B HG11 1 
ATOM   4730 H  HG12 . VAL   B 1 41  ? 41.380 -17.831 10.343  1.00 17.25 ?  41   VAL   B HG12 1 
ATOM   4731 H  HG13 . VAL   B 1 41  ? 41.986 -19.229 10.793  1.00 17.25 ?  41   VAL   B HG13 1 
ATOM   4732 H  HG21 . VAL   B 1 41  ? 43.119 -18.348 13.388  1.00 17.92 ?  41   VAL   B HG21 1 
ATOM   4733 H  HG22 . VAL   B 1 41  ? 44.009 -19.213 12.398  1.00 17.92 ?  41   VAL   B HG22 1 
ATOM   4734 H  HG23 . VAL   B 1 41  ? 44.533 -17.805 12.913  1.00 17.92 ?  41   VAL   B HG23 1 
ATOM   4735 N  N    . TYR   B 1 42  ? 46.384 -17.103 10.940  1.00 12.52 ?  42   TYR   B N    1 
ATOM   4736 C  CA   . TYR   B 1 42  ? 47.541 -16.257 11.210  1.00 12.94 ?  42   TYR   B CA   1 
ATOM   4737 C  C    . TYR   B 1 42  ? 48.503 -16.187 10.030  1.00 12.05 ?  42   TYR   B C    1 
ATOM   4738 O  O    . TYR   B 1 42  ? 49.593 -15.619 10.162  1.00 13.28 ?  42   TYR   B O    1 
ATOM   4739 C  CB   . TYR   B 1 42  ? 48.238 -16.667 12.515  1.00 14.79 ?  42   TYR   B CB   1 
ATOM   4740 C  CG   . TYR   B 1 42  ? 47.637 -15.973 13.736  1.00 15.20 ?  42   TYR   B CG   1 
ATOM   4741 C  CD1  . TYR   B 1 42  ? 47.857 -14.617 13.958  1.00 14.24 ?  42   TYR   B CD1  1 
ATOM   4742 C  CD2  . TYR   B 1 42  ? 46.848 -16.659 14.653  1.00 16.96 ?  42   TYR   B CD2  1 
ATOM   4743 C  CE1  . TYR   B 1 42  ? 47.322 -13.964 15.048  1.00 15.51 ?  42   TYR   B CE1  1 
ATOM   4744 C  CE2  . TYR   B 1 42  ? 46.304 -16.008 15.757  1.00 17.23 ?  42   TYR   B CE2  1 
ATOM   4745 C  CZ   . TYR   B 1 42  ? 46.548 -14.657 15.947  1.00 17.36 ?  42   TYR   B CZ   1 
ATOM   4746 O  OH   . TYR   B 1 42  ? 46.030 -13.989 17.037  1.00 19.95 ?  42   TYR   B OH   1 
ATOM   4747 H  H    . TYR   B 1 42  ? 46.530 -17.950 11.044  1.00 15.05 ?  42   TYR   B H    1 
ATOM   4748 H  HA   . TYR   B 1 42  ? 47.213 -15.357 11.341  1.00 15.55 ?  42   TYR   B HA   1 
ATOM   4749 H  HB2  . TYR   B 1 42  ? 48.144 -17.623 12.636  1.00 17.77 ?  42   TYR   B HB2  1 
ATOM   4750 H  HB3  . TYR   B 1 42  ? 49.173 -16.424 12.459  1.00 17.77 ?  42   TYR   B HB3  1 
ATOM   4751 H  HD1  . TYR   B 1 42  ? 48.384 -14.139 13.350  1.00 17.11 ?  42   TYR   B HD1  1 
ATOM   4752 H  HD2  . TYR   B 1 42  ? 46.680 -17.567 14.522  1.00 20.37 ?  42   TYR   B HD2  1 
ATOM   4753 H  HE1  . TYR   B 1 42  ? 47.492 -13.059 15.175  1.00 18.62 ?  42   TYR   B HE1  1 
ATOM   4754 H  HE2  . TYR   B 1 42  ? 45.780 -16.481 16.361  1.00 20.69 ?  42   TYR   B HE2  1 
ATOM   4755 H  HH   . TYR   B 1 42  ? 46.264 -13.186 17.012  1.00 23.96 ?  42   TYR   B HH   1 
ATOM   4756 N  N    . LEU   B 1 43  ? 48.104 -16.708 8.870   1.00 11.14 ?  43   LEU   B N    1 
ATOM   4757 C  CA   . LEU   B 1 43  ? 48.915 -16.643 7.658   1.00 11.16 ?  43   LEU   B CA   1 
ATOM   4758 C  C    . LEU   B 1 43  ? 50.331 -17.146 7.916   1.00 11.45 ?  43   LEU   B C    1 
ATOM   4759 O  O    . LEU   B 1 43  ? 51.307 -16.553 7.462   1.00 12.14 ?  43   LEU   B O    1 
ATOM   4760 C  CB   . LEU   B 1 43  ? 48.933 -15.243 7.043   1.00 11.42 ?  43   LEU   B CB   1 
ATOM   4761 C  CG   . LEU   B 1 43  ? 47.576 -14.626 6.677   1.00 11.35 ?  43   LEU   B CG   1 
ATOM   4762 C  CD1  . LEU   B 1 43  ? 47.794 -13.240 6.104   1.00 12.92 ?  43   LEU   B CD1  1 
ATOM   4763 C  CD2  . LEU   B 1 43  ? 46.802 -15.507 5.709   1.00 11.70 ?  43   LEU   B CD2  1 
ATOM   4764 H  H    . LEU   B 1 43  ? 47.357 -17.125 8.760   1.00 13.39 ?  43   LEU   B H    1 
ATOM   4765 H  HA   . LEU   B 1 43  ? 48.517 -17.239 6.999   1.00 13.41 ?  43   LEU   B HA   1 
ATOM   4766 H  HB2  . LEU   B 1 43  ? 49.360 -14.644 7.674   1.00 13.72 ?  43   LEU   B HB2  1 
ATOM   4767 H  HB3  . LEU   B 1 43  ? 49.459 -15.281 6.229   1.00 13.72 ?  43   LEU   B HB3  1 
ATOM   4768 H  HG   . LEU   B 1 43  ? 47.047 -14.536 7.481   1.00 13.64 ?  43   LEU   B HG   1 
ATOM   4769 H  HD11 . LEU   B 1 43  ? 46.935 -12.850 5.873   1.00 15.52 ?  43   LEU   B HD11 1 
ATOM   4770 H  HD12 . LEU   B 1 43  ? 48.235 -12.685 6.772   1.00 15.52 ?  43   LEU   B HD12 1 
ATOM   4771 H  HD13 . LEU   B 1 43  ? 48.351 -13.301 5.312   1.00 15.52 ?  43   LEU   B HD13 1 
ATOM   4772 H  HD21 . LEU   B 1 43  ? 45.995 -15.045 5.434   1.00 14.05 ?  43   LEU   B HD21 1 
ATOM   4773 H  HD22 . LEU   B 1 43  ? 47.356 -15.694 4.934   1.00 14.05 ?  43   LEU   B HD22 1 
ATOM   4774 H  HD23 . LEU   B 1 43  ? 46.569 -16.339 6.154   1.00 14.05 ?  43   LEU   B HD23 1 
ATOM   4775 N  N    . LYS   B 1 44  ? 50.436 -18.272 8.625   1.00 11.73 ?  44   LYS   B N    1 
ATOM   4776 C  CA   . LYS   B 1 44  ? 51.704 -18.949 8.865   1.00 12.25 ?  44   LYS   B CA   1 
ATOM   4777 C  C    . LYS   B 1 44  ? 51.818 -20.064 7.834   1.00 11.77 ?  44   LYS   B C    1 
ATOM   4778 O  O    . LYS   B 1 44  ? 51.121 -21.080 7.920   1.00 13.17 ?  44   LYS   B O    1 
ATOM   4779 C  CB   . LYS   B 1 44  ? 51.754 -19.468 10.300  1.00 13.96 ?  44   LYS   B CB   1 
ATOM   4780 C  CG   . LYS   B 1 44  ? 51.925 -18.355 11.329  1.00 16.71 ?  44   LYS   B CG   1 
ATOM   4781 C  CD   . LYS   B 1 44  ? 53.114 -17.471 10.943  1.00 20.14 ?  44   LYS   B CD   1 
ATOM   4782 C  CE   . LYS   B 1 44  ? 53.650 -16.647 12.084  1.00 23.16 ?  44   LYS   B CE   1 
ATOM   4783 N  NZ   . LYS   B 1 44  ? 54.792 -15.792 11.675  1.00 24.41 ?  44   LYS   B NZ   1 
ATOM   4784 H  H    . LYS   B 1 44  ? 49.762 -18.661 8.997   1.00 14.09 ?  44   LYS   B H    1 
ATOM   4785 H  HA   . LYS   B 1 44  ? 52.433 -18.332 8.709   1.00 14.72 ?  44   LYS   B HA   1 
ATOM   4786 H  HB2  . LYS   B 1 44  ? 50.917 -19.926 10.497  1.00 16.77 ?  44   LYS   B HB2  1 
ATOM   4787 H  HB3  . LYS   B 1 44  ? 52.495 -20.077 10.390  1.00 16.77 ?  44   LYS   B HB3  1 
ATOM   4788 H  HG2  . LYS   B 1 44  ? 51.125 -17.809 11.359  1.00 20.07 ?  44   LYS   B HG2  1 
ATOM   4789 H  HG3  . LYS   B 1 44  ? 52.103 -18.748 12.201  1.00 20.07 ?  44   LYS   B HG3  1 
ATOM   4790 H  HD2  . LYS   B 1 44  ? 53.828 -18.042 10.606  1.00 24.18 ?  44   LYS   B HD2  1 
ATOM   4791 H  HD3  . LYS   B 1 44  ? 52.828 -16.860 10.244  1.00 24.18 ?  44   LYS   B HD3  1 
ATOM   4792 H  HE2  . LYS   B 1 44  ? 52.955 -16.049 12.360  1.00 27.81 ?  44   LYS   B HE2  1 
ATOM   4793 H  HE3  . LYS   B 1 44  ? 53.926 -17.231 12.812  1.00 27.81 ?  44   LYS   B HE3  1 
ATOM   4794 H  HZ1  . LYS   B 1 44  ? 55.081 -15.320 12.372  1.00 29.31 ?  44   LYS   B HZ1  1 
ATOM   4795 H  HZ2  . LYS   B 1 44  ? 55.457 -16.293 11.366  1.00 29.31 ?  44   LYS   B HZ2  1 
ATOM   4796 H  HZ3  . LYS   B 1 44  ? 54.532 -15.228 11.034  1.00 29.31 ?  44   LYS   B HZ3  1 
ATOM   4797 N  N    . HIS   B 1 45  ? 52.664 -19.846 6.831   1.00 11.35 ?  45   HIS   B N    1 
ATOM   4798 C  CA   . HIS   B 1 45  ? 52.680 -20.681 5.629   1.00 11.84 ?  45   HIS   B CA   1 
ATOM   4799 C  C    . HIS   B 1 45  ? 53.700 -21.803 5.783   1.00 13.86 ?  45   HIS   B C    1 
ATOM   4800 O  O    . HIS   B 1 45  ? 54.768 -21.811 5.176   1.00 16.64 ?  45   HIS   B O    1 
ATOM   4801 C  CB   . HIS   B 1 45  ? 52.995 -19.827 4.415   1.00 11.61 ?  45   HIS   B CB   1 
ATOM   4802 C  CG   . HIS   B 1 45  ? 52.128 -18.622 4.307   1.00 11.40 ?  45   HIS   B CG   1 
ATOM   4803 N  ND1  . HIS   B 1 45  ? 50.749 -18.697 4.283   1.00 11.64 ?  45   HIS   B ND1  1 
ATOM   4804 C  CD2  . HIS   B 1 45  ? 52.447 -17.309 4.223   1.00 12.46 ?  45   HIS   B CD2  1 
ATOM   4805 C  CE1  . HIS   B 1 45  ? 50.265 -17.473 4.180   1.00 11.24 ?  45   HIS   B CE1  1 
ATOM   4806 N  NE2  . HIS   B 1 45  ? 51.269 -16.614 4.141   1.00 11.74 ?  45   HIS   B NE2  1 
ATOM   4807 H  H    . HIS   B 1 45  ? 53.232 -19.204 6.816   1.00 13.64 ?  45   HIS   B H    1 
ATOM   4808 H  HA   . HIS   B 1 45  ? 51.800 -21.075 5.501   1.00 14.22 ?  45   HIS   B HA   1 
ATOM   4809 H  HB2  . HIS   B 1 45  ? 53.915 -19.533 4.462   1.00 13.94 ?  45   HIS   B HB2  1 
ATOM   4810 H  HB3  . HIS   B 1 45  ? 52.861 -20.363 3.611   1.00 13.94 ?  45   HIS   B HB3  1 
ATOM   4811 H  HD2  . HIS   B 1 45  ? 53.305 -16.943 4.220   1.00 14.96 ?  45   HIS   B HD2  1 
ATOM   4812 H  HE1  . HIS   B 1 45  ? 49.362 -17.252 4.135   1.00 13.50 ?  45   HIS   B HE1  1 
ATOM   4813 H  HE2  . HIS   B 1 45  ? 51.193 -15.758 4.083   1.00 14.10 ?  45   HIS   B HE2  1 
ATOM   4814 N  N    A GLY   B 1 46  ? 53.329 -22.787 6.596   0.62 14.52 ?  46   GLY   B N    1 
ATOM   4815 N  N    B GLY   B 1 46  ? 53.340 -22.771 6.617   0.38 14.68 ?  46   GLY   B N    1 
ATOM   4816 C  CA   A GLY   B 1 46  ? 54.258 -23.837 6.968   0.62 16.31 ?  46   GLY   B CA   1 
ATOM   4817 C  CA   B GLY   B 1 46  ? 54.263 -23.838 6.944   0.38 15.96 ?  46   GLY   B CA   1 
ATOM   4818 C  C    A GLY   B 1 46  ? 54.291 -25.068 6.083   0.62 18.08 ?  46   GLY   B C    1 
ATOM   4819 C  C    B GLY   B 1 46  ? 54.273 -24.990 5.960   0.38 17.35 ?  46   GLY   B C    1 
ATOM   4820 O  O    A GLY   B 1 46  ? 55.367 -25.517 5.676   0.62 20.70 ?  46   GLY   B O    1 
ATOM   4821 O  O    B GLY   B 1 46  ? 55.298 -25.279 5.336   0.38 18.23 ?  46   GLY   B O    1 
ATOM   4822 H  H    A GLY   B 1 46  ? 52.550 -22.848 6.964   0.62 17.44 ?  46   GLY   B H    1 
ATOM   4823 H  H    B GLY   B 1 46  ? 52.574 -22.818 7.013   0.38 17.63 ?  46   GLY   B H    1 
ATOM   4824 H  HA2  A GLY   B 1 46  ? 55.151 -23.461 6.990   0.62 19.59 ?  46   GLY   B HA2  1 
ATOM   4825 H  HA2  B GLY   B 1 46  ? 55.159 -23.471 6.989   0.38 19.17 ?  46   GLY   B HA2  1 
ATOM   4826 H  HA3  A GLY   B 1 46  ? 54.039 -24.137 7.862   0.62 19.59 ?  46   GLY   B HA3  1 
ATOM   4827 H  HA3  B GLY   B 1 46  ? 54.036 -24.186 7.820   0.38 19.17 ?  46   GLY   B HA3  1 
ATOM   4828 N  N    . GLY   B 1 47  ? 53.127 -25.650 5.795   1.00 17.79 ?  47   GLY   B N    1 
ATOM   4829 C  CA   . GLY   B 1 47  ? 53.059 -26.919 5.101   1.00 15.42 ?  47   GLY   B CA   1 
ATOM   4830 C  C    . GLY   B 1 47  ? 52.152 -26.889 3.885   1.00 13.53 ?  47   GLY   B C    1 
ATOM   4831 O  O    . GLY   B 1 47  ? 51.501 -25.888 3.592   1.00 13.70 ?  47   GLY   B O    1 
ATOM   4832 H  H    A GLY   B 1 47  ? 52.357 -25.333 6.018   0.62 21.36 ?  47   GLY   B H    1 
ATOM   4833 H  H    B GLY   B 1 47  ? 52.364 -25.374 6.087   0.38 21.36 ?  47   GLY   B H    1 
ATOM   4834 H  HA2  . GLY   B 1 47  ? 53.946 -27.180 4.808   1.00 18.52 ?  47   GLY   B HA2  1 
ATOM   4835 H  HA3  . GLY   B 1 47  ? 52.733 -27.599 5.715   1.00 18.52 ?  47   GLY   B HA3  1 
ATOM   4836 N  N    . GLY   B 1 48  ? 52.100 -28.028 3.199   1.00 12.84 ?  48   GLY   B N    1 
ATOM   4837 C  CA   . GLY   B 1 48  ? 51.176 -28.175 2.091   1.00 12.77 ?  48   GLY   B CA   1 
ATOM   4838 C  C    . GLY   B 1 48  ? 51.316 -27.063 1.077   1.00 11.99 ?  48   GLY   B C    1 
ATOM   4839 O  O    . GLY   B 1 48  ? 52.422 -26.602 0.763   1.00 12.31 ?  48   GLY   B O    1 
ATOM   4840 H  H    . GLY   B 1 48  ? 52.583 -28.718 3.356   1.00 15.42 ?  48   GLY   B H    1 
ATOM   4841 H  HA2  . GLY   B 1 48  ? 51.338 -29.023 1.645   1.00 15.34 ?  48   GLY   B HA2  1 
ATOM   4842 H  HA3  . GLY   B 1 48  ? 50.263 -28.175 2.421   1.00 15.34 ?  48   GLY   B HA3  1 
ATOM   4843 N  N    . VAL   B 1 49  ? 50.170 -26.627 0.548   1.00 11.95 ?  49   VAL   B N    1 
ATOM   4844 C  CA   . VAL   B 1 49  ? 50.159 -25.599 -0.489  1.00 11.80 ?  49   VAL   B CA   1 
ATOM   4845 C  C    . VAL   B 1 49  ? 50.823 -24.314 0.004   1.00 10.83 ?  49   VAL   B C    1 
ATOM   4846 O  O    . VAL   B 1 49  ? 51.611 -23.692 -0.719  1.00 11.56 ?  49   VAL   B O    1 
ATOM   4847 C  CB   . VAL   B 1 49  ? 48.718 -25.346 -0.975  1.00 13.09 ?  49   VAL   B CB   1 
ATOM   4848 C  CG1  . VAL   B 1 49  ? 48.647 -24.091 -1.837  1.00 13.20 ?  49   VAL   B CG1  1 
ATOM   4849 C  CG2  . VAL   B 1 49  ? 48.189 -26.555 -1.734  1.00 14.82 ?  49   VAL   B CG2  1 
ATOM   4850 H  H    . VAL   B 1 49  ? 49.385 -26.905 0.775   1.00 14.36 ?  49   VAL   B H    1 
ATOM   4851 H  HA   . VAL   B 1 49  ? 50.668 -25.919 -1.249  1.00 14.18 ?  49   VAL   B HA   1 
ATOM   4852 H  HB   . VAL   B 1 49  ? 48.147 -25.206 -0.207  1.00 15.73 ?  49   VAL   B HB   1 
ATOM   4853 H  HG11 . VAL   B 1 49  ? 47.819 -24.101 -2.344  1.00 15.86 ?  49   VAL   B HG11 1 
ATOM   4854 H  HG12 . VAL   B 1 49  ? 48.669 -23.307 -1.263  1.00 15.86 ?  49   VAL   B HG12 1 
ATOM   4855 H  HG13 . VAL   B 1 49  ? 49.403 -24.078 -2.445  1.00 15.86 ?  49   VAL   B HG13 1 
ATOM   4856 H  HG21 . VAL   B 1 49  ? 47.284 -26.373 -2.029  1.00 17.80 ?  49   VAL   B HG21 1 
ATOM   4857 H  HG22 . VAL   B 1 49  ? 48.760 -26.721 -2.502  1.00 17.80 ?  49   VAL   B HG22 1 
ATOM   4858 H  HG23 . VAL   B 1 49  ? 48.198 -27.324 -1.144  1.00 17.80 ?  49   VAL   B HG23 1 
ATOM   4859 N  N    . ALA   B 1 50  ? 50.482 -23.871 1.219   1.00 10.55 ?  50   ALA   B N    1 
ATOM   4860 C  CA   . ALA   B 1 50  ? 51.003 -22.592 1.700   1.00 10.50 ?  50   ALA   B CA   1 
ATOM   4861 C  C    . ALA   B 1 50  ? 52.521 -22.626 1.806   1.00 10.71 ?  50   ALA   B C    1 
ATOM   4862 O  O    . ALA   B 1 50  ? 53.204 -21.664 1.436   1.00 10.79 ?  50   ALA   B O    1 
ATOM   4863 C  CB   . ALA   B 1 50  ? 50.378 -22.239 3.048   1.00 10.87 ?  50   ALA   B CB   1 
ATOM   4864 H  H    . ALA   B 1 50  ? 49.972 -24.288 1.773   1.00 12.68 ?  50   ALA   B H    1 
ATOM   4865 H  HA   . ALA   B 1 50  ? 50.773 -21.901 1.070   1.00 12.61 ?  50   ALA   B HA   1 
ATOM   4866 H  HB1  . ALA   B 1 50  ? 50.733 -21.389 3.350   1.00 13.06 ?  50   ALA   B HB1  1 
ATOM   4867 H  HB2  . ALA   B 1 50  ? 49.414 -22.174 2.939   1.00 13.06 ?  50   ALA   B HB2  1 
ATOM   4868 H  HB3  . ALA   B 1 50  ? 50.590 -22.934 3.691   1.00 13.06 ?  50   ALA   B HB3  1 
ATOM   4869 N  N    . GLY   B 1 51  ? 53.072 -23.719 2.324   1.00 11.45 ?  51   GLY   B N    1 
ATOM   4870 C  CA   . GLY   B 1 51  ? 54.515 -23.833 2.389   1.00 12.26 ?  51   GLY   B CA   1 
ATOM   4871 C  C    . GLY   B 1 51  ? 55.160 -23.780 1.019   1.00 11.96 ?  51   GLY   B C    1 
ATOM   4872 O  O    . GLY   B 1 51  ? 56.204 -23.147 0.839   1.00 12.81 ?  51   GLY   B O    1 
ATOM   4873 H  H    . GLY   B 1 51  ? 52.644 -24.399 2.635   1.00 13.75 ?  51   GLY   B H    1 
ATOM   4874 H  HA2  . GLY   B 1 51  ? 54.877 -23.106 2.924   1.00 14.73 ?  51   GLY   B HA2  1 
ATOM   4875 H  HA3  . GLY   B 1 51  ? 54.761 -24.673 2.814   1.00 14.73 ?  51   GLY   B HA3  1 
ATOM   4876 N  N    . ALA   B 1 52  ? 54.554 -24.444 0.036   1.00 11.64 ?  52   ALA   B N    1 
ATOM   4877 C  CA   . ALA   B 1 52  ? 55.118 -24.452 -1.307  1.00 11.94 ?  52   ALA   B CA   1 
ATOM   4878 C  C    . ALA   B 1 52  ? 55.041 -23.070 -1.956  1.00 11.34 ?  52   ALA   B C    1 
ATOM   4879 O  O    . ALA   B 1 52  ? 56.015 -22.621 -2.587  1.00 12.10 ?  52   ALA   B O    1 
ATOM   4880 C  CB   . ALA   B 1 52  ? 54.406 -25.495 -2.160  1.00 12.62 ?  52   ALA   B CB   1 
ATOM   4881 H  H    . ALA   B 1 52  ? 53.814 -24.880 0.121   1.00 13.99 ?  52   ALA   B H    1 
ATOM   4882 H  HA   . ALA   B 1 52  ? 56.054 -24.701 -1.243  1.00 14.34 ?  52   ALA   B HA   1 
ATOM   4883 H  HB1  . ALA   B 1 52  ? 54.798 -25.490 -3.047  1.00 15.16 ?  52   ALA   B HB1  1 
ATOM   4884 H  HB2  . ALA   B 1 52  ? 54.523 -26.367 -1.751  1.00 15.16 ?  52   ALA   B HB2  1 
ATOM   4885 H  HB3  . ALA   B 1 52  ? 53.466 -25.272 -2.208  1.00 15.16 ?  52   ALA   B HB3  1 
ATOM   4886 N  N    . LEU   B 1 53  ? 53.892 -22.393 -1.834  1.00 11.23 ?  53   LEU   B N    1 
ATOM   4887 C  CA   . LEU   B 1 53  ? 53.784 -21.053 -2.401  1.00 11.43 ?  53   LEU   B CA   1 
ATOM   4888 C  C    . LEU   B 1 53  ? 54.795 -20.116 -1.755  1.00 11.37 ?  53   LEU   B C    1 
ATOM   4889 O  O    . LEU   B 1 53  ? 55.494 -19.363 -2.445  1.00 12.01 ?  53   LEU   B O    1 
ATOM   4890 C  CB   . LEU   B 1 53  ? 52.359 -20.509 -2.233  1.00 11.55 ?  53   LEU   B CB   1 
ATOM   4891 C  CG   . LEU   B 1 53  ? 51.232 -21.233 -2.977  1.00 12.03 ?  53   LEU   B CG   1 
ATOM   4892 C  CD1  . LEU   B 1 53  ? 49.883 -20.637 -2.620  1.00 13.63 ?  53   LEU   B CD1  1 
ATOM   4893 C  CD2  . LEU   B 1 53  ? 51.441 -21.213 -4.487  1.00 14.01 ?  53   LEU   B CD2  1 
ATOM   4894 H  H    . LEU   B 1 53  ? 53.187 -22.681 -1.436  1.00 13.49 ?  53   LEU   B H    1 
ATOM   4895 H  HA   . LEU   B 1 53  ? 53.984 -21.100 -3.352  1.00 13.73 ?  53   LEU   B HA   1 
ATOM   4896 H  HB2  . LEU   B 1 53  ? 52.143 -20.542 -1.291  1.00 13.87 ?  53   LEU   B HB2  1 
ATOM   4897 H  HB3  . LEU   B 1 53  ? 52.355 -19.595 -2.537  1.00 13.87 ?  53   LEU   B HB3  1 
ATOM   4898 H  HG   . LEU   B 1 53  ? 51.217 -22.163 -2.695  1.00 14.45 ?  53   LEU   B HG   1 
ATOM   4899 H  HD11 . LEU   B 1 53  ? 49.183 -21.118 -3.100  1.00 16.37 ?  53   LEU   B HD11 1 
ATOM   4900 H  HD12 . LEU   B 1 53  ? 49.735 -20.731 -1.662  1.00 16.37 ?  53   LEU   B HD12 1 
ATOM   4901 H  HD13 . LEU   B 1 53  ? 49.868 -19.704 -2.866  1.00 16.37 ?  53   LEU   B HD13 1 
ATOM   4902 H  HD21 . LEU   B 1 53  ? 50.717 -21.697 -4.915  1.00 16.83 ?  53   LEU   B HD21 1 
ATOM   4903 H  HD22 . LEU   B 1 53  ? 51.451 -20.295 -4.793  1.00 16.83 ?  53   LEU   B HD22 1 
ATOM   4904 H  HD23 . LEU   B 1 53  ? 52.287 -21.642 -4.694  1.00 16.83 ?  53   LEU   B HD23 1 
ATOM   4905 N  N    . ASN   B 1 54  ? 54.892 -20.146 -0.426  1.00 10.86 ?  54   ASN   B N    1 
ATOM   4906 C  CA   . ASN   B 1 54  ? 55.812 -19.238 0.241   1.00 11.36 ?  54   ASN   B CA   1 
ATOM   4907 C  C    . ASN   B 1 54  ? 57.252 -19.520 -0.164  1.00 11.76 ?  54   ASN   B C    1 
ATOM   4908 O  O    . ASN   B 1 54  ? 58.031 -18.587 -0.401  1.00 12.28 ?  54   ASN   B O    1 
ATOM   4909 C  CB   . ASN   B 1 54  ? 55.656 -19.312 1.753   1.00 12.26 ?  54   ASN   B CB   1 
ATOM   4910 C  CG   . ASN   B 1 54  ? 56.627 -18.390 2.456   1.00 12.26 ?  54   ASN   B CG   1 
ATOM   4911 O  OD1  . ASN   B 1 54  ? 56.648 -17.188 2.192   1.00 12.65 ?  54   ASN   B OD1  1 
ATOM   4912 N  ND2  . ASN   B 1 54  ? 57.468 -18.950 3.316   1.00 14.23 ?  54   ASN   B ND2  1 
ATOM   4913 H  H    . ASN   B 1 54  ? 54.452 -20.672 0.095   1.00 13.05 ?  54   ASN   B H    1 
ATOM   4914 H  HA   . ASN   B 1 54  ? 55.601 -18.332 -0.033  1.00 13.65 ?  54   ASN   B HA   1 
ATOM   4915 H  HB2  . ASN   B 1 54  ? 54.754 -19.041 1.995   1.00 14.73 ?  54   ASN   B HB2  1 
ATOM   4916 H  HB3  . ASN   B 1 54  ? 55.825 -20.216 2.051   1.00 14.73 ?  54   ASN   B HB3  1 
ATOM   4917 H  HD21 . ASN   B 1 54  ? 58.043 -18.464 3.736   1.00 17.09 ?  54   ASN   B HD21 1 
ATOM   4918 H  HD22 . ASN   B 1 54  ? 57.437 -19.797 3.464   1.00 17.09 ?  54   ASN   B HD22 1 
ATOM   4919 N  N    . LYS   B 1 55  ? 57.632 -20.797 -0.235  1.00 12.42 ?  55   LYS   B N    1 
ATOM   4920 C  CA   . LYS   B 1 55  ? 58.986 -21.139 -0.655  1.00 13.45 ?  55   LYS   B CA   1 
ATOM   4921 C  C    . LYS   B 1 55  ? 59.282 -20.597 -2.047  1.00 13.60 ?  55   LYS   B C    1 
ATOM   4922 O  O    . LYS   B 1 55  ? 60.385 -20.100 -2.301  1.00 13.93 ?  55   LYS   B O    1 
ATOM   4923 C  CB   . LYS   B 1 55  ? 59.177 -22.656 -0.602  1.00 15.17 ?  55   LYS   B CB   1 
ATOM   4924 C  CG   . LYS   B 1 55  ? 60.558 -23.124 -1.018  1.00 19.67 ?  55   LYS   B CG   1 
ATOM   4925 C  CD   . LYS   B 1 55  ? 60.725 -24.626 -0.828  1.00 23.47 ?  55   LYS   B CD   1 
ATOM   4926 C  CE   . LYS   B 1 55  ? 60.682 -25.020 0.647   1.00 26.59 ?  55   LYS   B CE   1 
ATOM   4927 N  NZ   . LYS   B 1 55  ? 61.103 -26.424 0.875   1.00 28.35 ?  55   LYS   B NZ   1 
ATOM   4928 H  H    . LYS   B 1 55  ? 57.130 -21.468 -0.046  1.00 14.92 ?  55   LYS   B H    1 
ATOM   4929 H  HA   . LYS   B 1 55  ? 59.618 -20.739 -0.042  1.00 16.15 ?  55   LYS   B HA   1 
ATOM   4930 H  HB2  . LYS   B 1 55  ? 59.021 -22.950 0.309   1.00 18.22 ?  55   LYS   B HB2  1 
ATOM   4931 H  HB3  . LYS   B 1 55  ? 58.533 -23.074 -1.195  1.00 18.22 ?  55   LYS   B HB3  1 
ATOM   4932 H  HG2  . LYS   B 1 55  ? 60.697 -22.921 -1.958  1.00 23.62 ?  55   LYS   B HG2  1 
ATOM   4933 H  HG3  . LYS   B 1 55  ? 61.226 -22.672 -0.477  1.00 23.62 ?  55   LYS   B HG3  1 
ATOM   4934 H  HD2  . LYS   B 1 55  ? 60.005 -25.090 -1.286  1.00 28.18 ?  55   LYS   B HD2  1 
ATOM   4935 H  HD3  . LYS   B 1 55  ? 61.583 -24.904 -1.187  1.00 28.18 ?  55   LYS   B HD3  1 
ATOM   4936 H  HE2  . LYS   B 1 55  ? 61.275 -24.433 1.145   1.00 31.93 ?  55   LYS   B HE2  1 
ATOM   4937 H  HE3  . LYS   B 1 55  ? 59.770 -24.917 0.972   1.00 31.93 ?  55   LYS   B HE3  1 
ATOM   4938 H  HZ1  . LYS   B 1 55  ? 61.050 -26.616 1.742   1.00 34.04 ?  55   LYS   B HZ1  1 
ATOM   4939 H  HZ2  . LYS   B 1 55  ? 60.570 -26.974 0.423   1.00 34.04 ?  55   LYS   B HZ2  1 
ATOM   4940 H  HZ3  . LYS   B 1 55  ? 61.939 -26.536 0.600   1.00 34.04 ?  55   LYS   B HZ3  1 
ATOM   4941 N  N    . ALA   B 1 56  ? 58.310 -20.671 -2.960  1.00 13.10 ?  56   ALA   B N    1 
ATOM   4942 C  CA   . ALA   B 1 56  ? 58.538 -20.176 -4.311  1.00 13.86 ?  56   ALA   B CA   1 
ATOM   4943 C  C    . ALA   B 1 56  ? 58.814 -18.679 -4.314  1.00 13.45 ?  56   ALA   B C    1 
ATOM   4944 O  O    . ALA   B 1 56  ? 59.543 -18.185 -5.186  1.00 14.42 ?  56   ALA   B O    1 
ATOM   4945 C  CB   . ALA   B 1 56  ? 57.349 -20.515 -5.211  1.00 14.90 ?  56   ALA   B CB   1 
ATOM   4946 H  H    . ALA   B 1 56  ? 57.515 -20.978 -2.817  1.00 15.73 ?  56   ALA   B H    1 
ATOM   4947 H  HA   . ALA   B 1 56  ? 59.317 -20.614 -4.673  1.00 16.65 ?  56   ALA   B HA   1 
ATOM   4948 H  HB1  . ALA   B 1 56  ? 57.526 -20.187 -6.108  1.00 17.90 ?  56   ALA   B HB1  1 
ATOM   4949 H  HB2  . ALA   B 1 56  ? 57.236 -21.480 -5.231  1.00 17.90 ?  56   ALA   B HB2  1 
ATOM   4950 H  HB3  . ALA   B 1 56  ? 56.549 -20.098 -4.858  1.00 17.90 ?  56   ALA   B HB3  1 
ATOM   4951 N  N    . THR   B 1 57  ? 58.245 -17.942 -3.355  1.00 13.16 ?  57   THR   B N    1 
ATOM   4952 C  CA   . THR   B 1 57  ? 58.489 -16.508 -3.224  1.00 13.15 ?  57   THR   B CA   1 
ATOM   4953 C  C    . THR   B 1 57  ? 59.743 -16.188 -2.416  1.00 13.90 ?  57   THR   B C    1 
ATOM   4954 O  O    . THR   B 1 57  ? 59.980 -15.016 -2.107  1.00 14.25 ?  57   THR   B O    1 
ATOM   4955 C  CB   . THR   B 1 57  ? 57.287 -15.784 -2.582  1.00 12.49 ?  57   THR   B CB   1 
ATOM   4956 O  OG1  . THR   B 1 57  ? 57.274 -15.998 -1.163  1.00 12.56 ?  57   THR   B OG1  1 
ATOM   4957 C  CG2  . THR   B 1 57  ? 55.968 -16.207 -3.224  1.00 12.62 ?  57   THR   B CG2  1 
ATOM   4958 H  H    . THR   B 1 57  ? 57.697 -18.251 -2.766  1.00 15.81 ?  57   THR   B H    1 
ATOM   4959 H  HA   . THR   B 1 57  ? 58.606 -16.134 -4.111  1.00 15.80 ?  57   THR   B HA   1 
ATOM   4960 H  HB   . THR   B 1 57  ? 57.385 -14.830 -2.746  1.00 15.00 ?  57   THR   B HB   1 
ATOM   4961 H  HG1  . THR   B 1 57  ? 57.199 -16.820 -1.000  1.00 15.08 ?  57   THR   B HG1  1 
ATOM   4962 H  HG21 . THR   B 1 57  ? 55.241 -15.665 -2.884  1.00 15.15 ?  57   THR   B HG21 1 
ATOM   4963 H  HG22 . THR   B 1 57  ? 56.017 -16.099 -4.188  1.00 15.15 ?  57   THR   B HG22 1 
ATOM   4964 H  HG23 . THR   B 1 57  ? 55.787 -17.138 -3.025  1.00 15.15 ?  57   THR   B HG23 1 
ATOM   4965 N  N    . ASN   B 1 58  ? 60.539 -17.190 -2.054  1.00 14.80 ?  58   ASN   B N    1 
ATOM   4966 C  CA   . ASN   B 1 58  ? 61.733 -16.974 -1.242  1.00 17.29 ?  58   ASN   B CA   1 
ATOM   4967 C  C    . ASN   B 1 58  ? 61.392 -16.258 0.065   1.00 15.12 ?  58   ASN   B C    1 
ATOM   4968 O  O    . ASN   B 1 58  ? 62.124 -15.379 0.526   1.00 15.74 ?  58   ASN   B O    1 
ATOM   4969 C  CB   . ASN   B 1 58  ? 62.816 -16.223 -2.022  1.00 24.37 ?  58   ASN   B CB   1 
ATOM   4970 C  CG   . ASN   B 1 58  ? 64.191 -16.377 -1.402  1.00 33.14 ?  58   ASN   B CG   1 
ATOM   4971 O  OD1  . ASN   B 1 58  ? 64.497 -17.398 -0.787  1.00 35.98 ?  58   ASN   B OD1  1 
ATOM   4972 N  ND2  . ASN   B 1 58  ? 65.027 -15.360 -1.560  1.00 37.44 ?  58   ASN   B ND2  1 
ATOM   4973 H  H    . ASN   B 1 58  ? 60.400 -18.015 -2.263  1.00 17.77 ?  58   ASN   B H    1 
ATOM   4974 H  HA   . ASN   B 1 58  ? 62.097 -17.844 -1.016  1.00 20.76 ?  58   ASN   B HA   1 
ATOM   4975 H  HB2  . ASN   B 1 58  ? 62.852 -16.570 -2.929  1.00 29.26 ?  58   ASN   B HB2  1 
ATOM   4976 H  HB3  . ASN   B 1 58  ? 62.597 -15.279 -2.038  1.00 29.26 ?  58   ASN   B HB3  1 
ATOM   4977 H  HD21 . ASN   B 1 58  ? 65.818 -15.401 -1.227  1.00 44.95 ?  58   ASN   B HD21 1 
ATOM   4978 H  HD22 . ASN   B 1 58  ? 64.777 -14.662 -1.995  1.00 44.95 ?  58   ASN   B HD22 1 
ATOM   4979 N  N    . ASN   B 1 59  ? 60.269 -16.643 0.670   1.00 13.96 ?  59   ASN   B N    1 
ATOM   4980 C  CA   . ASN   B 1 59  ? 59.798 -16.171 1.971   1.00 13.66 ?  59   ASN   B CA   1 
ATOM   4981 C  C    . ASN   B 1 59  ? 59.203 -14.765 1.915   1.00 12.95 ?  59   ASN   B C    1 
ATOM   4982 O  O    . ASN   B 1 59  ? 58.772 -14.261 2.956   1.00 13.15 ?  59   ASN   B O    1 
ATOM   4983 C  CB   . ASN   B 1 59  ? 60.874 -16.234 3.070   1.00 15.09 ?  59   ASN   B CB   1 
ATOM   4984 C  CG   . ASN   B 1 59  ? 60.291 -16.395 4.454   1.00 15.98 ?  59   ASN   B CG   1 
ATOM   4985 O  OD1  . ASN   B 1 59  ? 59.456 -17.268 4.689   1.00 16.11 ?  59   ASN   B OD1  1 
ATOM   4986 N  ND2  . ASN   B 1 59  ? 60.720 -15.551 5.380   1.00 16.72 ?  59   ASN   B ND2  1 
ATOM   4987 H  H    . ASN   B 1 59  ? 59.731 -17.223 0.327   1.00 16.76 ?  59   ASN   B H    1 
ATOM   4988 H  HA   . ASN   B 1 59  ? 59.090 -16.766 2.259   1.00 16.41 ?  59   ASN   B HA   1 
ATOM   4989 H  HB2  . ASN   B 1 59  ? 61.458 -16.994 2.912   1.00 18.13 ?  59   ASN   B HB2  1 
ATOM   4990 H  HB3  . ASN   B 1 59  ? 61.390 -15.414 3.067   1.00 18.13 ?  59   ASN   B HB3  1 
ATOM   4991 H  HD21 . ASN   B 1 59  ? 60.417 -15.605 6.186   1.00 20.08 ?  59   ASN   B HD21 1 
ATOM   4992 H  HD22 . ASN   B 1 59  ? 61.305 -14.955 5.181   1.00 20.08 ?  59   ASN   B HD22 1 
ATOM   4993 N  N    . ALA   B 1 60  ? 59.136 -14.126 0.743   1.00 12.94 ?  60   ALA   B N    1 
ATOM   4994 C  CA   . ALA   B 1 60  ? 58.543 -12.791 0.671   1.00 12.94 ?  60   ALA   B CA   1 
ATOM   4995 C  C    . ALA   B 1 60  ? 57.074 -12.813 1.070   1.00 12.16 ?  60   ALA   B C    1 
ATOM   4996 O  O    . ALA   B 1 60  ? 56.572 -11.859 1.677   1.00 13.08 ?  60   ALA   B O    1 
ATOM   4997 C  CB   . ALA   B 1 60  ? 58.706 -12.214 -0.735  1.00 14.16 ?  60   ALA   B CB   1 
ATOM   4998 H  H    . ALA   B 1 60  ? 59.428 -14.440 -0.000  1.00 15.55 ?  60   ALA   B H    1 
ATOM   4999 H  HA   . ALA   B 1 60  ? 59.013 -12.210 1.289   1.00 15.54 ?  60   ALA   B HA   1 
ATOM   5000 H  HB1  . ALA   B 1 60  ? 58.308 -11.333 -0.758  1.00 17.01 ?  60   ALA   B HB1  1 
ATOM   5001 H  HB2  . ALA   B 1 60  ? 59.653 -12.157 -0.946  1.00 17.01 ?  60   ALA   B HB2  1 
ATOM   5002 H  HB3  . ALA   B 1 60  ? 58.262 -12.799 -1.368  1.00 17.01 ?  60   ALA   B HB3  1 
ATOM   5003 N  N    . MET   B 1 61  ? 56.364 -13.889 0.724   1.00 11.91 ?  61   MET   B N    1 
ATOM   5004 C  CA   . MET   B 1 61  ? 54.968 -14.014 1.121   1.00 11.46 ?  61   MET   B CA   1 
ATOM   5005 C  C    . MET   B 1 61  ? 54.833 -14.019 2.642   1.00 11.57 ?  61   MET   B C    1 
ATOM   5006 O  O    . MET   B 1 61  ? 53.936 -13.366 3.191   1.00 11.32 ?  61   MET   B O    1 
ATOM   5007 C  CB   . MET   B 1 61  ? 54.379 -15.280 0.490   1.00 11.14 ?  61   MET   B CB   1 
ATOM   5008 C  CG   . MET   B 1 61  ? 52.943 -15.579 0.903   1.00 10.95 ?  61   MET   B CG   1 
ATOM   5009 S  SD   . MET   B 1 61  ? 52.297 -17.077 0.141   1.00 12.07 ?  61   MET   B SD   1 
ATOM   5010 C  CE   . MET   B 1 61  ? 52.031 -16.478 -1.524  1.00 13.28 ?  61   MET   B CE   1 
ATOM   5011 H  H    . MET   B 1 61  ? 56.668 -14.555 0.260   1.00 14.30 ?  61   MET   B H    1 
ATOM   5012 H  HA   . MET   B 1 61  ? 54.478 -13.259 0.762   1.00 13.77 ?  61   MET   B HA   1 
ATOM   5013 H  HB2  . MET   B 1 61  ? 54.390 -15.183 -0.478  1.00 13.38 ?  61   MET   B HB2  1 
ATOM   5014 H  HB3  . MET   B 1 61  ? 54.926 -16.041 0.744   1.00 13.38 ?  61   MET   B HB3  1 
ATOM   5015 H  HG2  . MET   B 1 61  ? 52.915 -15.704 1.865   1.00 13.15 ?  61   MET   B HG2  1 
ATOM   5016 H  HG3  . MET   B 1 61  ? 52.382 -14.839 0.644   1.00 13.15 ?  61   MET   B HG3  1 
ATOM   5017 H  HE1  . MET   B 1 61  ? 51.639 -17.185 -2.054  1.00 15.95 ?  61   MET   B HE1  1 
ATOM   5018 H  HE2  . MET   B 1 61  ? 51.433 -15.713 -1.493  1.00 15.95 ?  61   MET   B HE2  1 
ATOM   5019 H  HE3  . MET   B 1 61  ? 52.885 -16.211 -1.903  1.00 15.95 ?  61   MET   B HE3  1 
ATOM   5020 N  N    . GLN   B 1 62  ? 55.711 -14.737 3.346   1.00 11.74 ?  62   GLN   B N    1 
ATOM   5021 C  CA   . GLN   B 1 62  ? 55.605 -14.785 4.802   1.00 12.00 ?  62   GLN   B CA   1 
ATOM   5022 C  C    . GLN   B 1 62  ? 55.888 -13.424 5.426   1.00 11.85 ?  62   GLN   B C    1 
ATOM   5023 O  O    . GLN   B 1 62  ? 55.206 -13.017 6.374   1.00 12.55 ?  62   GLN   B O    1 
ATOM   5024 C  CB   . GLN   B 1 62  ? 56.563 -15.830 5.372   1.00 12.39 ?  62   GLN   B CB   1 
ATOM   5025 C  CG   . GLN   B 1 62  ? 56.342 -16.107 6.851   1.00 12.46 ?  62   GLN   B CG   1 
ATOM   5026 C  CD   . GLN   B 1 62  ? 54.963 -16.698 7.093   1.00 11.90 ?  62   GLN   B CD   1 
ATOM   5027 O  OE1  . GLN   B 1 62  ? 54.705 -17.845 6.728   1.00 12.67 ?  62   GLN   B OE1  1 
ATOM   5028 N  NE2  . GLN   B 1 62  ? 54.051 -15.907 7.655   1.00 12.62 ?  62   GLN   B NE2  1 
ATOM   5029 H  H    . GLN   B 1 62  ? 56.353 -15.195 3.009   1.00 14.10 ?  62   GLN   B H    1 
ATOM   5030 H  HA   . GLN   B 1 62  ? 54.701 -15.037 5.040   1.00 14.42 ?  62   GLN   B HA   1 
ATOM   5031 H  HB2  . GLN   B 1 62  ? 56.444 -16.662 4.889   1.00 14.88 ?  62   GLN   B HB2  1 
ATOM   5032 H  HB3  . GLN   B 1 62  ? 57.474 -15.513 5.261   1.00 14.88 ?  62   GLN   B HB3  1 
ATOM   5033 H  HG2  . GLN   B 1 62  ? 57.006 -16.746 7.155   1.00 14.96 ?  62   GLN   B HG2  1 
ATOM   5034 H  HG3  . GLN   B 1 62  ? 56.413 -15.282 7.348   1.00 14.96 ?  62   GLN   B HG3  1 
ATOM   5035 H  HE21 . GLN   B 1 62  ? 54.257 -15.107 7.883   1.00 15.16 ?  62   GLN   B HE21 1 
ATOM   5036 H  HE22 . GLN   B 1 62  ? 53.256 -16.208 7.801   1.00 15.16 ?  62   GLN   B HE22 1 
ATOM   5037 N  N    . VAL   B 1 63  ? 56.900 -12.708 4.925   1.00 12.58 ?  63   VAL   B N    1 
ATOM   5038 C  CA   . VAL   B 1 63  ? 57.213 -11.394 5.481   1.00 13.46 ?  63   VAL   B CA   1 
ATOM   5039 C  C    . VAL   B 1 63  ? 56.022 -10.458 5.305   1.00 12.76 ?  63   VAL   B C    1 
ATOM   5040 O  O    . VAL   B 1 63  ? 55.617 -9.749  6.235   1.00 13.19 ?  63   VAL   B O    1 
ATOM   5041 C  CB   . VAL   B 1 63  ? 58.500 -10.832 4.851   1.00 14.63 ?  63   VAL   B CB   1 
ATOM   5042 C  CG1  . VAL   B 1 63  ? 58.715 -9.390  5.291   1.00 15.34 ?  63   VAL   B CG1  1 
ATOM   5043 C  CG2  . VAL   B 1 63  ? 59.696 -11.702 5.233   1.00 15.45 ?  63   VAL   B CG2  1 
ATOM   5044 H  H    . VAL   B 1 63  ? 57.405 -12.958 4.269   1.00 15.11 ?  63   VAL   B H    1 
ATOM   5045 H  HA   . VAL   B 1 63  ? 57.373 -11.494 6.427   1.00 16.17 ?  63   VAL   B HA   1 
ATOM   5046 H  HB   . VAL   B 1 63  ? 58.423 -10.846 3.885   1.00 17.57 ?  63   VAL   B HB   1 
ATOM   5047 H  HG11 . VAL   B 1 63  ? 59.634 -9.140  5.115   1.00 18.42 ?  63   VAL   B HG11 1 
ATOM   5048 H  HG12 . VAL   B 1 63  ? 58.113 -8.816  4.796   1.00 18.42 ?  63   VAL   B HG12 1 
ATOM   5049 H  HG13 . VAL   B 1 63  ? 58.533 -9.324  6.243   1.00 18.42 ?  63   VAL   B HG13 1 
ATOM   5050 H  HG21 . VAL   B 1 63  ? 60.502 -11.325 4.844   1.00 18.55 ?  63   VAL   B HG21 1 
ATOM   5051 H  HG22 . VAL   B 1 63  ? 59.778 -11.718 6.203   1.00 18.55 ?  63   VAL   B HG22 1 
ATOM   5052 H  HG23 . VAL   B 1 63  ? 59.557 -12.601 4.900   1.00 18.55 ?  63   VAL   B HG23 1 
ATOM   5053 N  N    . GLU   B 1 64  ? 55.444 -10.453 4.103   1.00 12.16 ?  64   GLU   B N    1 
ATOM   5054 C  CA   . GLU   B 1 64  ? 54.274 -9.623  3.831   1.00 11.75 ?  64   GLU   B CA   1 
ATOM   5055 C  C    . GLU   B 1 64  ? 53.095 -10.023 4.708   1.00 11.60 ?  64   GLU   B C    1 
ATOM   5056 O  O    . GLU   B 1 64  ? 52.357 -9.164  5.217   1.00 12.08 ?  64   GLU   B O    1 
ATOM   5057 C  CB   . GLU   B 1 64  ? 53.907 -9.767  2.353   1.00 11.96 ?  64   GLU   B CB   1 
ATOM   5058 C  CG   . GLU   B 1 64  ? 52.635 -9.039  1.928   1.00 12.45 ?  64   GLU   B CG   1 
ATOM   5059 C  CD   . GLU   B 1 64  ? 52.117 -9.524  0.583   1.00 13.32 ?  64   GLU   B CD   1 
ATOM   5060 O  OE1  . GLU   B 1 64  ? 52.299 -10.730 0.261   1.00 14.06 ?  64   GLU   B OE1  1 
ATOM   5061 O  OE2  . GLU   B 1 64  ? 51.498 -8.704  -0.142  1.00 14.21 -1 64   GLU   B OE2  1 
ATOM   5062 H  H    . GLU   B 1 64  ? 55.713 -10.922 3.427   1.00 14.61 ?  64   GLU   B H    1 
ATOM   5063 H  HA   . GLU   B 1 64  ? 54.489 -8.697  4.005   1.00 14.12 ?  64   GLU   B HA   1 
ATOM   5064 H  HB2  . GLU   B 1 64  ? 54.632 -9.404  1.814   1.00 14.37 ?  64   GLU   B HB2  1 
ATOM   5065 H  HB3  . GLU   B 1 64  ? 53.789 -10.704 2.149   1.00 14.37 ?  64   GLU   B HB3  1 
ATOM   5066 H  HG2  . GLU   B 1 64  ? 51.933 -9.191  2.587   1.00 14.95 ?  64   GLU   B HG2  1 
ATOM   5067 H  HG3  . GLU   B 1 64  ? 52.817 -8.090  1.859   1.00 14.95 ?  64   GLU   B HG3  1 
ATOM   5068 N  N    . SER   B 1 65  ? 52.910 -11.329 4.892   1.00 11.65 ?  65   SER   B N    1 
ATOM   5069 C  CA   . SER   B 1 65  ? 51.803 -11.835 5.693   1.00 11.61 ?  65   SER   B CA   1 
ATOM   5070 C  C    . SER   B 1 65  ? 51.937 -11.429 7.154   1.00 11.45 ?  65   SER   B C    1 
ATOM   5071 O  O    . SER   B 1 65  ? 50.940 -11.061 7.791   1.00 11.74 ?  65   SER   B O    1 
ATOM   5072 C  CB   . SER   B 1 65  ? 51.727 -13.356 5.564   1.00 11.75 ?  65   SER   B CB   1 
ATOM   5073 O  OG   . SER   B 1 65  ? 51.375 -13.748 4.246   1.00 11.85 ?  65   SER   B OG   1 
ATOM   5074 H  H    . SER   B 1 65  ? 53.417 -11.952 4.569   1.00 14.00 ?  65   SER   B H    1 
ATOM   5075 H  HA   . SER   B 1 65  ? 50.971 -11.470 5.354   1.00 13.94 ?  65   SER   B HA   1 
ATOM   5076 H  HB2  . SER   B 1 65  ? 52.591 -13.737 5.784   1.00 14.11 ?  65   SER   B HB2  1 
ATOM   5077 H  HB3  . SER   B 1 65  ? 51.053 -13.694 6.180   1.00 14.11 ?  65   SER   B HB3  1 
ATOM   5078 H  HG   . SER   B 1 65  ? 51.950 -13.454 3.698   1.00 14.24 ?  65   SER   B HG   1 
ATOM   5079 N  N    . ASP   B 1 66  ? 53.146 -11.525 7.719   1.00 12.01 ?  66   ASP   B N    1 
ATOM   5080 C  CA   . ASP   B 1 66  ? 53.332 -11.128 9.113   1.00 12.39 ?  66   ASP   B CA   1 
ATOM   5081 C  C    . ASP   B 1 66  ? 53.013 -9.650  9.308   1.00 12.55 ?  66   ASP   B C    1 
ATOM   5082 O  O    . ASP   B 1 66  ? 52.440 -9.258  10.331  1.00 13.01 ?  66   ASP   B O    1 
ATOM   5083 C  CB   . ASP   B 1 66  ? 54.762 -11.427 9.563   1.00 13.34 ?  66   ASP   B CB   1 
ATOM   5084 C  CG   . ASP   B 1 66  ? 55.044 -12.920 9.714   1.00 15.33 ?  66   ASP   B CG   1 
ATOM   5085 O  OD1  . ASP   B 1 66  ? 54.092 -13.733 9.642   1.00 15.97 ?  66   ASP   B OD1  1 
ATOM   5086 O  OD2  . ASP   B 1 66  ? 56.232 -13.277 9.917   1.00 18.20 -1 66   ASP   B OD2  1 
ATOM   5087 H  H    . ASP   B 1 66  ? 53.848 -11.821 7.330   1.00 14.43 ?  66   ASP   B H    1 
ATOM   5088 H  HA   . ASP   B 1 66  ? 52.729 -11.635 9.678   1.00 14.88 ?  66   ASP   B HA   1 
ATOM   5089 H  HB2  . ASP   B 1 66  ? 55.381 -11.072 8.908   1.00 16.03 ?  66   ASP   B HB2  1 
ATOM   5090 H  HB3  . ASP   B 1 66  ? 54.917 -11.001 10.426  1.00 16.03 ?  66   ASP   B HB3  1 
ATOM   5091 N  N    . ASP   B 1 67  ? 53.386 -8.811  8.341   1.00 12.16 ?  67   ASP   B N    1 
ATOM   5092 C  CA   . ASP   B 1 67  ? 53.039 -7.399  8.422   1.00 12.78 ?  67   ASP   B CA   1 
ATOM   5093 C  C    . ASP   B 1 67  ? 51.526 -7.195  8.350   1.00 12.71 ?  67   ASP   B C    1 
ATOM   5094 O  O    . ASP   B 1 67  ? 50.966 -6.384  9.099   1.00 13.69 ?  67   ASP   B O    1 
ATOM   5095 C  CB   . ASP   B 1 67  ? 53.756 -6.637  7.312   1.00 13.94 ?  67   ASP   B CB   1 
ATOM   5096 C  CG   . ASP   B 1 67  ? 53.336 -5.190  7.261   1.00 15.28 ?  67   ASP   B CG   1 
ATOM   5097 O  OD1  . ASP   B 1 67  ? 53.844 -4.373  8.063   1.00 16.70 ?  67   ASP   B OD1  1 
ATOM   5098 O  OD2  . ASP   B 1 67  ? 52.449 -4.893  6.444   1.00 16.52 -1 67   ASP   B OD2  1 
ATOM   5099 H  H    . ASP   B 1 67  ? 53.847 -9.032  7.649   1.00 14.61 ?  67   ASP   B H    1 
ATOM   5100 H  HA   . ASP   B 1 67  ? 53.347 -7.044  9.269   1.00 15.35 ?  67   ASP   B HA   1 
ATOM   5101 H  HB2  . ASP   B 1 67  ? 54.715 -6.673  7.466   1.00 16.74 ?  67   ASP   B HB2  1 
ATOM   5102 H  HB3  . ASP   B 1 67  ? 53.548 -7.052  6.454   1.00 16.74 ?  67   ASP   B HB3  1 
ATOM   5103 N  N    . TYR   B 1 68  ? 50.849 -7.932  7.461   1.00 12.57 ?  68   TYR   B N    1 
ATOM   5104 C  CA   . TYR   B 1 68  ? 49.391 -7.862  7.386   1.00 13.17 ?  68   TYR   B CA   1 
ATOM   5105 C  C    . TYR   B 1 68  ? 48.755 -8.206  8.730   1.00 13.09 ?  68   TYR   B C    1 
ATOM   5106 O  O    . TYR   B 1 68  ? 47.821 -7.525  9.180   1.00 13.33 ?  68   TYR   B O    1 
ATOM   5107 C  CB   . TYR   B 1 68  ? 48.861 -8.796  6.287   1.00 13.85 ?  68   TYR   B CB   1 
ATOM   5108 C  CG   . TYR   B 1 68  ? 47.352 -8.945  6.341   1.00 14.85 ?  68   TYR   B CG   1 
ATOM   5109 C  CD1  . TYR   B 1 68  ? 46.764 -9.888  7.174   1.00 15.63 ?  68   TYR   B CD1  1 
ATOM   5110 C  CD2  . TYR   B 1 68  ? 46.520 -8.118  5.603   1.00 15.87 ?  68   TYR   B CD2  1 
ATOM   5111 C  CE1  . TYR   B 1 68  ? 45.399 -10.011 7.271   1.00 16.59 ?  68   TYR   B CE1  1 
ATOM   5112 C  CE2  . TYR   B 1 68  ? 45.134 -8.244  5.685   1.00 16.13 ?  68   TYR   B CE2  1 
ATOM   5113 C  CZ   . TYR   B 1 68  ? 44.593 -9.192  6.525   1.00 16.59 ?  68   TYR   B CZ   1 
ATOM   5114 O  OH   . TYR   B 1 68  ? 43.225 -9.314  6.629   1.00 17.60 ?  68   TYR   B OH   1 
ATOM   5115 H  H    . TYR   B 1 68  ? 51.207 -8.486  6.900   1.00 15.10 ?  68   TYR   B H    1 
ATOM   5116 H  HA   . TYR   B 1 68  ? 49.135 -6.957  7.162   1.00 15.81 ?  68   TYR   B HA   1 
ATOM   5117 H  HB2  . TYR   B 1 68  ? 49.092 -8.427  5.422   1.00 16.64 ?  68   TYR   B HB2  1 
ATOM   5118 H  HB3  . TYR   B 1 68  ? 49.254 -9.673  6.397   1.00 16.64 ?  68   TYR   B HB3  1 
ATOM   5119 H  HD1  . TYR   B 1 68  ? 47.305 -10.450 7.684   1.00 18.77 ?  68   TYR   B HD1  1 
ATOM   5120 H  HD2  . TYR   B 1 68  ? 46.891 -7.469  5.055   1.00 19.06 ?  68   TYR   B HD2  1 
ATOM   5121 H  HE1  . TYR   B 1 68  ? 45.021 -10.664 7.820   1.00 19.92 ?  68   TYR   B HE1  1 
ATOM   5122 H  HE2  . TYR   B 1 68  ? 44.577 -7.685  5.191   1.00 19.38 ?  68   TYR   B HE2  1 
ATOM   5123 H  HH   . TYR   B 1 68  ? 42.837 -8.772  6.107   1.00 21.13 ?  68   TYR   B HH   1 
ATOM   5124 N  N    . ILE   B 1 69  ? 49.246 -9.267  9.380   1.00 12.71 ?  69   ILE   B N    1 
ATOM   5125 C  CA   . ILE   B 1 69  ? 48.694 -9.692  10.664  1.00 12.93 ?  69   ILE   B CA   1 
ATOM   5126 C  C    . ILE   B 1 69  ? 48.942 -8.637  11.735  1.00 12.63 ?  69   ILE   B C    1 
ATOM   5127 O  O    . ILE   B 1 69  ? 48.074 -8.361  12.568  1.00 12.95 ?  69   ILE   B O    1 
ATOM   5128 C  CB   . ILE   B 1 69  ? 49.277 -11.063 11.063  1.00 13.80 ?  69   ILE   B CB   1 
ATOM   5129 C  CG1  . ILE   B 1 69  ? 48.756 -12.169 10.138  1.00 14.34 ?  69   ILE   B CG1  1 
ATOM   5130 C  CG2  . ILE   B 1 69  ? 48.979 -11.387 12.524  1.00 14.92 ?  69   ILE   B CG2  1 
ATOM   5131 C  CD1  . ILE   B 1 69  ? 47.276 -12.481 10.296  1.00 14.76 ?  69   ILE   B CD1  1 
ATOM   5132 H  H    . ILE   B 1 69  ? 49.903 -9.750  9.102   1.00 15.27 ?  69   ILE   B H    1 
ATOM   5133 H  HA   . ILE   B 1 69  ? 47.740 -9.791  10.572  1.00 15.53 ?  69   ILE   B HA   1 
ATOM   5134 H  HB   . ILE   B 1 69  ? 50.243 -11.021 10.961  1.00 16.57 ?  69   ILE   B HB   1 
ATOM   5135 H  HG12 . ILE   B 1 69  ? 48.905 -11.897 9.217   1.00 17.22 ?  69   ILE   B HG12 1 
ATOM   5136 H  HG13 . ILE   B 1 69  ? 49.253 -12.984 10.319  1.00 17.22 ?  69   ILE   B HG13 1 
ATOM   5137 H  HG21 . ILE   B 1 69  ? 49.132 -12.334 12.671  1.00 17.92 ?  69   ILE   B HG21 1 
ATOM   5138 H  HG22 . ILE   B 1 69  ? 49.567 -10.868 13.093  1.00 17.92 ?  69   ILE   B HG22 1 
ATOM   5139 H  HG23 . ILE   B 1 69  ? 48.053 -11.170 12.711  1.00 17.92 ?  69   ILE   B HG23 1 
ATOM   5140 H  HD11 . ILE   B 1 69  ? 47.041 -13.189 9.678   1.00 17.72 ?  69   ILE   B HD11 1 
ATOM   5141 H  HD12 . ILE   B 1 69  ? 47.109 -12.771 11.207  1.00 17.72 ?  69   ILE   B HD12 1 
ATOM   5142 H  HD13 . ILE   B 1 69  ? 46.761 -11.686 10.100  1.00 17.72 ?  69   ILE   B HD13 1 
ATOM   5143 N  N    . ALA   B 1 70  ? 50.132 -8.045  11.752  1.00 12.76 ?  70   ALA   B N    1 
ATOM   5144 C  CA   . ALA   B 1 70  ? 50.410 -7.004  12.736  1.00 12.66 ?  70   ALA   B CA   1 
ATOM   5145 C  C    . ALA   B 1 70  ? 49.408 -5.867  12.624  1.00 12.89 ?  70   ALA   B C    1 
ATOM   5146 O  O    . ALA   B 1 70  ? 48.962 -5.323  13.638  1.00 13.65 ?  70   ALA   B O    1 
ATOM   5147 C  CB   . ALA   B 1 70  ? 51.838 -6.482  12.565  1.00 13.42 ?  70   ALA   B CB   1 
ATOM   5148 H  H    . ALA   B 1 70  ? 50.782 -8.224  11.224  1.00 15.33 ?  70   ALA   B H    1 
ATOM   5149 H  HA   . ALA   B 1 70  ? 50.342 -7.379  13.632  1.00 15.20 ?  70   ALA   B HA   1 
ATOM   5150 H  HB1  . ALA   B 1 70  ? 52.024 -5.825  13.259  1.00 16.11 ?  70   ALA   B HB1  1 
ATOM   5151 H  HB2  . ALA   B 1 70  ? 52.462 -7.222  12.644  1.00 16.11 ?  70   ALA   B HB2  1 
ATOM   5152 H  HB3  . ALA   B 1 70  ? 51.925 -6.070  11.691  1.00 16.11 ?  70   ALA   B HB3  1 
ATOM   5153 N  N    . THR   B 1 71  ? 49.042 -5.499  11.400  1.00 13.32 ?  71   THR   B N    1 
ATOM   5154 C  CA   . THR   B 1 71  ? 48.145 -4.370  11.182  1.00 14.34 ?  71   THR   B CA   1 
ATOM   5155 C  C    . THR   B 1 71  ? 46.676 -4.736  11.392  1.00 15.04 ?  71   THR   B C    1 
ATOM   5156 O  O    . THR   B 1 71  ? 45.897 -3.918  11.901  1.00 16.76 ?  71   THR   B O    1 
ATOM   5157 C  CB   . THR   B 1 71  ? 48.360 -3.819  9.771   1.00 16.33 ?  71   THR   B CB   1 
ATOM   5158 O  OG1  . THR   B 1 71  ? 49.683 -3.282  9.667   1.00 18.50 ?  71   THR   B OG1  1 
ATOM   5159 C  CG2  . THR   B 1 71  ? 47.344 -2.739  9.444   1.00 17.69 ?  71   THR   B CG2  1 
ATOM   5160 H  H    . THR   B 1 71  ? 49.304 -5.893  10.681  1.00 16.00 ?  71   THR   B H    1 
ATOM   5161 H  HA   . THR   B 1 71  ? 48.368 -3.671  11.811  1.00 17.22 ?  71   THR   B HA   1 
ATOM   5162 H  HB   . THR   B 1 71  ? 48.268 -4.535  9.124   1.00 19.61 ?  71   THR   B HB   1 
ATOM   5163 H  HG1  . THR   B 1 71  ? 49.810 -2.959  8.897   1.00 22.21 ?  71   THR   B HG1  1 
ATOM   5164 H  HG21 . THR   B 1 71  ? 47.649 -2.216  8.685   1.00 21.24 ?  71   THR   B HG21 1 
ATOM   5165 H  HG22 . THR   B 1 71  ? 46.490 -3.141  9.226   1.00 21.24 ?  71   THR   B HG22 1 
ATOM   5166 H  HG23 . THR   B 1 71  ? 47.233 -2.147  10.205  1.00 21.24 ?  71   THR   B HG23 1 
ATOM   5167 N  N    . ASN   B 1 72  ? 46.278 -5.953  11.007  1.00 14.59 ?  72   ASN   B N    1 
ATOM   5168 C  CA   . ASN   B 1 72  ? 44.871 -6.309  10.891  1.00 15.23 ?  72   ASN   B CA   1 
ATOM   5169 C  C    . ASN   B 1 72  ? 44.402 -7.405  11.837  1.00 15.61 ?  72   ASN   B C    1 
ATOM   5170 O  O    . ASN   B 1 72  ? 43.186 -7.567  12.001  1.00 16.80 ?  72   ASN   B O    1 
ATOM   5171 C  CB   . ASN   B 1 72  ? 44.550 -6.741  9.451   1.00 16.17 ?  72   ASN   B CB   1 
ATOM   5172 C  CG   . ASN   B 1 72  ? 44.832 -5.648  8.449   1.00 17.22 ?  72   ASN   B CG   1 
ATOM   5173 O  OD1  . ASN   B 1 72  ? 45.862 -5.653  7.769   1.00 18.35 ?  72   ASN   B OD1  1 
ATOM   5174 N  ND2  . ASN   B 1 72  ? 43.944 -4.676  8.384   1.00 19.11 ?  72   ASN   B ND2  1 
ATOM   5175 H  H    . ASN   B 1 72  ? 46.817 -6.603  10.805  1.00 17.53 ?  72   ASN   B H    1 
ATOM   5176 H  HA   . ASN   B 1 72  ? 44.344 -5.520  11.081  1.00 18.29 ?  72   ASN   B HA   1 
ATOM   5177 H  HB2  . ASN   B 1 72  ? 45.095 -7.509  9.220   1.00 19.42 ?  72   ASN   B HB2  1 
ATOM   5178 H  HB3  . ASN   B 1 72  ? 43.610 -6.968  9.392   1.00 19.42 ?  72   ASN   B HB3  1 
ATOM   5179 H  HD21 . ASN   B 1 72  ? 44.050 -4.027  7.829   1.00 22.95 ?  72   ASN   B HD21 1 
ATOM   5180 H  HD22 . ASN   B 1 72  ? 43.234 -4.705  8.874   1.00 22.95 ?  72   ASN   B HD22 1 
ATOM   5181 N  N    . GLY   B 1 73  ? 45.305 -8.158  12.456  1.00 15.14 ?  73   GLY   B N    1 
ATOM   5182 C  CA   . GLY   B 1 73  ? 44.911 -9.296  13.248  1.00 14.76 ?  73   GLY   B CA   1 
ATOM   5183 C  C    . GLY   B 1 73  ? 44.562 -10.490 12.384  1.00 13.24 ?  73   GLY   B C    1 
ATOM   5184 O  O    . GLY   B 1 73  ? 44.563 -10.417 11.153  1.00 13.27 ?  73   GLY   B O    1 
ATOM   5185 H  H    . GLY   B 1 73  ? 46.157 -8.024  12.427  1.00 18.18 ?  73   GLY   B H    1 
ATOM   5186 H  HA2  . GLY   B 1 73  ? 45.635 -9.543  13.844  1.00 17.73 ?  73   GLY   B HA2  1 
ATOM   5187 H  HA3  . GLY   B 1 73  ? 44.136 -9.063  13.786  1.00 17.73 ?  73   GLY   B HA3  1 
ATOM   5188 N  N    . PRO   B 1 74  ? 44.259 -11.615 13.027  1.00 13.58 ?  74   PRO   B N    1 
ATOM   5189 C  CA   . PRO   B 1 74  ? 44.008 -12.849 12.283  1.00 13.26 ?  74   PRO   B CA   1 
ATOM   5190 C  C    . PRO   B 1 74  ? 42.707 -12.793 11.495  1.00 12.52 ?  74   PRO   B C    1 
ATOM   5191 O  O    . PRO   B 1 74  ? 41.765 -12.058 11.816  1.00 13.89 ?  74   PRO   B O    1 
ATOM   5192 C  CB   . PRO   B 1 74  ? 43.934 -13.912 13.386  1.00 14.23 ?  74   PRO   B CB   1 
ATOM   5193 C  CG   . PRO   B 1 74  ? 43.485 -13.160 14.592  1.00 15.94 ?  74   PRO   B CG   1 
ATOM   5194 C  CD   . PRO   B 1 74  ? 44.148 -11.815 14.481  1.00 15.22 ?  74   PRO   B CD   1 
ATOM   5195 H  HA   . PRO   B 1 74  ? 44.750 -13.041 11.682  1.00 15.93 ?  74   PRO   B HA   1 
ATOM   5196 H  HB2  . PRO   B 1 74  ? 43.288 -14.593 13.135  1.00 17.10 ?  74   PRO   B HB2  1 
ATOM   5197 H  HB3  . PRO   B 1 74  ? 44.811 -14.301 13.521  1.00 17.10 ?  74   PRO   B HB3  1 
ATOM   5198 H  HG2  . PRO   B 1 74  ? 42.517 -13.070 14.577  1.00 19.14 ?  74   PRO   B HG2  1 
ATOM   5199 H  HG3  . PRO   B 1 74  ? 43.775 -13.623 15.390  1.00 19.14 ?  74   PRO   B HG3  1 
ATOM   5200 H  HD2  . PRO   B 1 74  ? 43.584 -11.130 14.881  1.00 18.28 ?  74   PRO   B HD2  1 
ATOM   5201 H  HD3  . PRO   B 1 74  ? 45.025 -11.836 14.887  1.00 18.28 ?  74   PRO   B HD3  1 
ATOM   5202 N  N    . LEU   B 1 75  ? 42.675 -13.605 10.443  1.00 12.04 ?  75   LEU   B N    1 
ATOM   5203 C  CA   . LEU   B 1 75  ? 41.462 -13.821 9.676   1.00 12.16 ?  75   LEU   B CA   1 
ATOM   5204 C  C    . LEU   B 1 75  ? 40.490 -14.680 10.477  1.00 12.68 ?  75   LEU   B C    1 
ATOM   5205 O  O    . LEU   B 1 75  ? 40.840 -15.272 11.501  1.00 13.87 ?  75   LEU   B O    1 
ATOM   5206 C  CB   . LEU   B 1 75  ? 41.790 -14.540 8.368   1.00 12.00 ?  75   LEU   B CB   1 
ATOM   5207 C  CG   . LEU   B 1 75  ? 42.637 -13.794 7.333   1.00 13.97 ?  75   LEU   B CG   1 
ATOM   5208 C  CD1  . LEU   B 1 75  ? 42.870 -14.662 6.097   1.00 15.59 ?  75   LEU   B CD1  1 
ATOM   5209 C  CD2  . LEU   B 1 75  ? 42.016 -12.480 6.947   1.00 17.58 ?  75   LEU   B CD2  1 
ATOM   5210 H  H    . LEU   B 1 75  ? 43.353 -14.047 10.143  1.00 14.47 ?  75   LEU   B H    1 
ATOM   5211 H  HA   . LEU   B 1 75  ? 41.040 -12.972 9.467   1.00 14.61 ?  75   LEU   B HA   1 
ATOM   5212 H  HB2  . LEU   B 1 75  ? 42.269 -15.358 8.587   1.00 14.41 ?  75   LEU   B HB2  1 
ATOM   5213 H  HB3  . LEU   B 1 75  ? 40.956 -14.774 7.932   1.00 14.41 ?  75   LEU   B HB3  1 
ATOM   5214 H  HG   . LEU   B 1 75  ? 43.506 -13.609 7.722   1.00 16.78 ?  75   LEU   B HG   1 
ATOM   5215 H  HD11 . LEU   B 1 75  ? 43.415 -14.167 5.459   1.00 18.72 ?  75   LEU   B HD11 1 
ATOM   5216 H  HD12 . LEU   B 1 75  ? 43.338 -15.474 6.358   1.00 18.72 ?  75   LEU   B HD12 1 
ATOM   5217 H  HD13 . LEU   B 1 75  ? 42.018 -14.887 5.696   1.00 18.72 ?  75   LEU   B HD13 1 
ATOM   5218 H  HD21 . LEU   B 1 75  ? 42.539 -12.083 6.236   1.00 21.11 ?  75   LEU   B HD21 1 
ATOM   5219 H  HD22 . LEU   B 1 75  ? 41.108 -12.638 6.648   1.00 21.11 ?  75   LEU   B HD22 1 
ATOM   5220 H  HD23 . LEU   B 1 75  ? 42.014 -11.897 7.723   1.00 21.11 ?  75   LEU   B HD23 1 
ATOM   5221 N  N    . LYS   B 1 76  ? 39.250 -14.746 9.992   1.00 13.64 ?  76   LYS   B N    1 
ATOM   5222 C  CA   . LYS   B 1 76  ? 38.268 -15.710 10.463  1.00 14.70 ?  76   LYS   B CA   1 
ATOM   5223 C  C    . LYS   B 1 76  ? 38.376 -16.989 9.636   1.00 13.37 ?  76   LYS   B C    1 
ATOM   5224 O  O    . LYS   B 1 76  ? 38.654 -16.945 8.439   1.00 13.09 ?  76   LYS   B O    1 
ATOM   5225 C  CB   . LYS   B 1 76  ? 36.848 -15.151 10.267  1.00 17.21 ?  76   LYS   B CB   1 
ATOM   5226 C  CG   . LYS   B 1 76  ? 36.557 -13.771 10.884  1.00 19.02 ?  76   LYS   B CG   1 
ATOM   5227 C  CD   . LYS   B 1 76  ? 35.156 -13.248 10.503  1.00 20.18 ?  76   LYS   B CD   1 
ATOM   5228 C  CE   . LYS   B 1 76  ? 34.882 -11.883 11.110  1.00 22.22 ?  76   LYS   B CE   1 
ATOM   5229 N  NZ   . LYS   B 1 76  ? 33.598 -11.286 10.650  1.00 22.94 ?  76   LYS   B NZ   1 
ATOM   5230 H  H    . LYS   B 1 76  ? 38.951 -14.234 9.366   1.00 16.38 ?  76   LYS   B H    1 
ATOM   5231 H  HA   . LYS   B 1 76  ? 38.411 -15.918 11.401  1.00 17.65 ?  76   LYS   B HA   1 
ATOM   5232 H  HB2  . LYS   B 1 76  ? 36.681 -15.080 9.315   1.00 20.67 ?  76   LYS   B HB2  1 
ATOM   5233 H  HB3  . LYS   B 1 76  ? 36.219 -15.775 10.659  1.00 20.67 ?  76   LYS   B HB3  1 
ATOM   5234 H  HG2  . LYS   B 1 76  ? 36.605 -13.836 11.851  1.00 22.84 ?  76   LYS   B HG2  1 
ATOM   5235 H  HG3  . LYS   B 1 76  ? 37.217 -13.132 10.562  1.00 22.84 ?  76   LYS   B HG3  1 
ATOM   5236 H  HD2  . LYS   B 1 76  ? 35.098 -13.169 9.536   1.00 24.23 ?  76   LYS   B HD2  1 
ATOM   5237 H  HD3  . LYS   B 1 76  ? 34.486 -13.868 10.829  1.00 24.23 ?  76   LYS   B HD3  1 
ATOM   5238 H  HE2  . LYS   B 1 76  ? 34.845 -11.971 12.074  1.00 26.67 ?  76   LYS   B HE2  1 
ATOM   5239 H  HE3  . LYS   B 1 76  ? 35.600 -11.279 10.860  1.00 26.67 ?  76   LYS   B HE3  1 
ATOM   5240 H  HZ1  . LYS   B 1 76  ? 33.479 -10.490 11.029  1.00 27.54 ?  76   LYS   B HZ1  1 
ATOM   5241 H  HZ2  . LYS   B 1 76  ? 33.607 -11.186 9.765   1.00 27.54 ?  76   LYS   B HZ2  1 
ATOM   5242 H  HZ3  . LYS   B 1 76  ? 32.918 -11.817 10.872  1.00 27.54 ?  76   LYS   B HZ3  1 
ATOM   5243 N  N    . VAL   B 1 77  ? 38.134 -18.139 10.275  1.00 14.14 ?  77   VAL   B N    1 
ATOM   5244 C  CA   . VAL   B 1 77  ? 37.918 -19.357 9.500   1.00 14.50 ?  77   VAL   B CA   1 
ATOM   5245 C  C    . VAL   B 1 77  ? 36.724 -19.131 8.582   1.00 13.50 ?  77   VAL   B C    1 
ATOM   5246 O  O    . VAL   B 1 77  ? 35.658 -18.684 9.026   1.00 13.40 ?  77   VAL   B O    1 
ATOM   5247 C  CB   . VAL   B 1 77  ? 37.721 -20.569 10.423  1.00 15.96 ?  77   VAL   B CB   1 
ATOM   5248 C  CG1  . VAL   B 1 77  ? 37.431 -21.810 9.590   1.00 16.69 ?  77   VAL   B CG1  1 
ATOM   5249 C  CG2  . VAL   B 1 77  ? 38.955 -20.789 11.306  1.00 17.08 ?  77   VAL   B CG2  1 
ATOM   5250 H  H    . VAL   B 1 77  ? 38.100 -18.237 11.125  1.00 16.99 ?  77   VAL   B H    1 
ATOM   5251 H  HA   . VAL   B 1 77  ? 38.696 -19.524 8.942   1.00 17.41 ?  77   VAL   B HA   1 
ATOM   5252 H  HB   . VAL   B 1 77  ? 36.957 -20.406 11.000  1.00 19.17 ?  77   VAL   B HB   1 
ATOM   5253 H  HG11 . VAL   B 1 77  ? 37.471 -22.588 10.166  1.00 20.04 ?  77   VAL   B HG11 1 
ATOM   5254 H  HG12 . VAL   B 1 77  ? 36.544 -21.733 9.202   1.00 20.04 ?  77   VAL   B HG12 1 
ATOM   5255 H  HG13 . VAL   B 1 77  ? 38.095 -21.880 8.889   1.00 20.04 ?  77   VAL   B HG13 1 
ATOM   5256 H  HG21 . VAL   B 1 77  ? 38.815 -21.582 11.843  1.00 20.51 ?  77   VAL   B HG21 1 
ATOM   5257 H  HG22 . VAL   B 1 77  ? 39.729 -20.901 10.736  1.00 20.51 ?  77   VAL   B HG22 1 
ATOM   5258 H  HG23 . VAL   B 1 77  ? 39.071 -20.014 11.878  1.00 20.51 ?  77   VAL   B HG23 1 
ATOM   5259 N  N    . GLY   B 1 78  ? 36.905 -19.414 7.291   1.00 12.76 ?  78   GLY   B N    1 
ATOM   5260 C  CA   . GLY   B 1 78  ? 35.931 -19.092 6.273   1.00 12.74 ?  78   GLY   B CA   1 
ATOM   5261 C  C    . GLY   B 1 78  ? 36.167 -17.771 5.577   1.00 12.01 ?  78   GLY   B C    1 
ATOM   5262 O  O    . GLY   B 1 78  ? 35.477 -17.481 4.594   1.00 12.42 ?  78   GLY   B O    1 
ATOM   5263 H  H    . GLY   B 1 78  ? 37.605 -19.809 6.978   1.00 15.33 ?  78   GLY   B H    1 
ATOM   5264 H  HA2  . GLY   B 1 78  ? 35.929 -19.786 5.599   1.00 15.30 ?  78   GLY   B HA2  1 
ATOM   5265 H  HA3  . GLY   B 1 78  ? 35.049 -19.060 6.677   1.00 15.30 ?  78   GLY   B HA3  1 
ATOM   5266 N  N    . GLY   B 1 79  ? 37.116 -16.964 6.057   1.00 12.00 ?  79   GLY   B N    1 
ATOM   5267 C  CA   . GLY   B 1 79  ? 37.409 -15.671 5.474   1.00 11.77 ?  79   GLY   B CA   1 
ATOM   5268 C  C    . GLY   B 1 79  ? 38.648 -15.688 4.591   1.00 11.14 ?  79   GLY   B C    1 
ATOM   5269 O  O    . GLY   B 1 79  ? 39.265 -16.721 4.348   1.00 11.68 ?  79   GLY   B O    1 
ATOM   5270 H  H    . GLY   B 1 79  ? 37.612 -17.152 6.730   1.00 14.41 ?  79   GLY   B H    1 
ATOM   5271 H  HA2  . GLY   B 1 79  ? 36.655 -15.378 4.934   1.00 14.14 ?  79   GLY   B HA2  1 
ATOM   5272 H  HA3  . GLY   B 1 79  ? 37.549 -15.022 6.178   1.00 14.14 ?  79   GLY   B HA3  1 
ATOM   5273 N  N    . SER   B 1 80  ? 39.012 -14.494 4.112   1.00 11.13 ?  80   SER   B N    1 
ATOM   5274 C  CA   . SER   B 1 80  ? 40.120 -14.367 3.175   1.00 11.00 ?  80   SER   B CA   1 
ATOM   5275 C  C    . SER   B 1 80  ? 40.703 -12.963 3.224   1.00 10.79 ?  80   SER   B C    1 
ATOM   5276 O  O    . SER   B 1 80  ? 40.088 -12.028 3.738   1.00 12.17 ?  80   SER   B O    1 
ATOM   5277 C  CB   . SER   B 1 80  ? 39.680 -14.673 1.739   1.00 11.24 ?  80   SER   B CB   1 
ATOM   5278 O  OG   . SER   B 1 80  ? 38.843 -13.651 1.216   1.00 12.57 ?  80   SER   B OG   1 
ATOM   5279 H  H    . SER   B 1 80  ? 38.634 -13.750 4.317   1.00 13.37 ?  80   SER   B H    1 
ATOM   5280 H  HA   . SER   B 1 80  ? 40.811 -14.996 3.426   1.00 13.21 ?  80   SER   B HA   1 
ATOM   5281 H  HB2  . SER   B 1 80  ? 40.466 -14.749 1.175   1.00 13.50 ?  80   SER   B HB2  1 
ATOM   5282 H  HB3  . SER   B 1 80  ? 39.189 -15.512 1.731   1.00 13.50 ?  80   SER   B HB3  1 
ATOM   5283 H  HG   . SER   B 1 80  ? 38.152 -13.575 1.690   1.00 15.10 ?  80   SER   B HG   1 
ATOM   5284 N  N    . CYS   B 1 81  ? 41.893 -12.821 2.641   1.00 10.79 ?  81   CYS   B N    1 
ATOM   5285 C  CA   . CYS   B 1 81  ? 42.441 -11.508 2.330   1.00 10.91 ?  81   CYS   B CA   1 
ATOM   5286 C  C    . CYS   B 1 81  ? 43.207 -11.592 1.017   1.00 10.22 ?  81   CYS   B C    1 
ATOM   5287 O  O    . CYS   B 1 81  ? 43.708 -12.657 0.637   1.00 11.26 ?  81   CYS   B O    1 
ATOM   5288 C  CB   . CYS   B 1 81  ? 43.330 -10.965 3.457   1.00 11.93 ?  81   CYS   B CB   1 
ATOM   5289 S  SG   . CYS   B 1 81  ? 44.857 -11.897 3.683   1.00 12.00 ?  81   CYS   B SG   1 
ATOM   5290 H  H    . CYS   B 1 81  ? 42.403 -13.473 2.410   1.00 12.97 ?  81   CYS   B H    1 
ATOM   5291 H  HA   . CYS   B 1 81  ? 41.711 -10.883 2.207   1.00 13.11 ?  81   CYS   B HA   1 
ATOM   5292 H  HB2  . CYS   B 1 81  ? 43.571 -10.046 3.260   1.00 14.33 ?  81   CYS   B HB2  1 
ATOM   5293 H  HB3  . CYS   B 1 81  ? 42.833 -10.996 4.295   1.00 14.33 ?  81   CYS   B HB3  1 
ATOM   5294 H  HG   . CYS   B 1 81  ? 45.487 -11.412 4.585   1.00 14.42 ?  81   CYS   B HG   1 
ATOM   5295 N  N    . VAL   B 1 82  ? 43.314 -10.449 0.342   1.00 10.83 ?  82   VAL   B N    1 
ATOM   5296 C  CA   . VAL   B 1 82  ? 44.070 -10.321 -0.901  1.00 11.01 ?  82   VAL   B CA   1 
ATOM   5297 C  C    . VAL   B 1 82  ? 45.415 -9.680  -0.593  1.00 11.12 ?  82   VAL   B C    1 
ATOM   5298 O  O    . VAL   B 1 82  ? 45.472 -8.557  -0.075  1.00 12.20 ?  82   VAL   B O    1 
ATOM   5299 C  CB   . VAL   B 1 82  ? 43.317 -9.477  -1.941  1.00 12.02 ?  82   VAL   B CB   1 
ATOM   5300 C  CG1  . VAL   B 1 82  ? 44.158 -9.325  -3.206  1.00 13.32 ?  82   VAL   B CG1  1 
ATOM   5301 C  CG2  . VAL   B 1 82  ? 41.957 -10.080 -2.255  1.00 13.15 ?  82   VAL   B CG2  1 
ATOM   5302 H  H    . VAL   B 1 82  ? 42.944 -9.706  0.593   1.00 13.02 ?  82   VAL   B H    1 
ATOM   5303 H  HA   . VAL   B 1 82  ? 44.224 -11.197 -1.276  1.00 13.22 ?  82   VAL   B HA   1 
ATOM   5304 H  HB   . VAL   B 1 82  ? 43.169 -8.589  -1.579  1.00 14.44 ?  82   VAL   B HB   1 
ATOM   5305 H  HG11 . VAL   B 1 82  ? 43.592 -9.010  -3.929  1.00 16.00 ?  82   VAL   B HG11 1 
ATOM   5306 H  HG12 . VAL   B 1 82  ? 44.867 -8.676  -3.044  1.00 16.00 ?  82   VAL   B HG12 1 
ATOM   5307 H  HG13 . VAL   B 1 82  ? 44.543 -10.182 -3.438  1.00 16.00 ?  82   VAL   B HG13 1 
ATOM   5308 H  HG21 . VAL   B 1 82  ? 41.519 -9.545  -2.939  1.00 15.79 ?  82   VAL   B HG21 1 
ATOM   5309 H  HG22 . VAL   B 1 82  ? 42.077 -10.988 -2.578  1.00 15.79 ?  82   VAL   B HG22 1 
ATOM   5310 H  HG23 . VAL   B 1 82  ? 41.416 -10.086 -1.449  1.00 15.79 ?  82   VAL   B HG23 1 
ATOM   5311 N  N    . LEU   B 1 83  ? 46.493 -10.372 -0.955  1.00 10.79 ?  83   LEU   B N    1 
ATOM   5312 C  CA   . LEU   B 1 83  ? 47.853 -9.858  -0.844  1.00 10.59 ?  83   LEU   B CA   1 
ATOM   5313 C  C    . LEU   B 1 83  ? 48.549 -10.002 -2.197  1.00 10.66 ?  83   LEU   B C    1 
ATOM   5314 O  O    . LEU   B 1 83  ? 47.946 -10.429 -3.184  1.00 10.69 ?  83   LEU   B O    1 
ATOM   5315 C  CB   . LEU   B 1 83  ? 48.604 -10.531 0.313   1.00 11.29 ?  83   LEU   B CB   1 
ATOM   5316 C  CG   . LEU   B 1 83  ? 48.102 -10.162 1.719   1.00 12.48 ?  83   LEU   B CG   1 
ATOM   5317 C  CD1  . LEU   B 1 83  ? 48.739 -11.027 2.794   1.00 12.85 ?  83   LEU   B CD1  1 
ATOM   5318 C  CD2  . LEU   B 1 83  ? 48.309 -8.674  2.021   1.00 13.68 ?  83   LEU   B CD2  1 
ATOM   5319 H  H    . LEU   B 1 83  ? 46.454 -11.172 -1.282  1.00 12.97 ?  83   LEU   B H    1 
ATOM   5320 H  HA   . LEU   B 1 83  ? 47.802 -8.915  -0.653  1.00 12.73 ?  83   LEU   B HA   1 
ATOM   5321 H  HB2  . LEU   B 1 83  ? 48.528 -11.490 0.215   1.00 13.56 ?  83   LEU   B HB2  1 
ATOM   5322 H  HB3  . LEU   B 1 83  ? 49.537 -10.270 0.259   1.00 13.56 ?  83   LEU   B HB3  1 
ATOM   5323 H  HG   . LEU   B 1 83  ? 47.148 -10.328 1.747   1.00 15.00 ?  83   LEU   B HG   1 
ATOM   5324 H  HD11 . LEU   B 1 83  ? 48.385 -10.765 3.661   1.00 15.43 ?  83   LEU   B HD11 1 
ATOM   5325 H  HD12 . LEU   B 1 83  ? 48.519 -11.959 2.621   1.00 15.43 ?  83   LEU   B HD12 1 
ATOM   5326 H  HD13 . LEU   B 1 83  ? 49.698 -10.905 2.776   1.00 15.43 ?  83   LEU   B HD13 1 
ATOM   5327 H  HD21 . LEU   B 1 83  ? 48.117 -8.514  2.956   1.00 16.43 ?  83   LEU   B HD21 1 
ATOM   5328 H  HD22 . LEU   B 1 83  ? 49.228 -8.438  1.823   1.00 16.43 ?  83   LEU   B HD22 1 
ATOM   5329 H  HD23 . LEU   B 1 83  ? 47.707 -8.154  1.465   1.00 16.43 ?  83   LEU   B HD23 1 
ATOM   5330 N  N    . SER   B 1 84  ? 49.824 -9.623  -2.259  1.00 11.69 ?  84   SER   B N    1 
ATOM   5331 C  CA   . SER   B 1 84  ? 50.558 -9.742  -3.511  1.00 11.98 ?  84   SER   B CA   1 
ATOM   5332 C  C    . SER   B 1 84  ? 50.715 -11.204 -3.917  1.00 11.19 ?  84   SER   B C    1 
ATOM   5333 O  O    . SER   B 1 84  ? 50.832 -12.097 -3.078  1.00 11.09 ?  84   SER   B O    1 
ATOM   5334 C  CB   . SER   B 1 84  ? 51.953 -9.132  -3.370  1.00 14.04 ?  84   SER   B CB   1 
ATOM   5335 O  OG   . SER   B 1 84  ? 52.704 -9.361  -4.549  1.00 15.36 ?  84   SER   B OG   1 
ATOM   5336 H  H    . SER   B 1 84  ? 50.269 -9.294  -1.602  1.00 14.04 ?  84   SER   B H    1 
ATOM   5337 H  HA   . SER   B 1 84  ? 50.081 -9.279  -4.213  1.00 14.39 ?  84   SER   B HA   1 
ATOM   5338 H  HB2  . SER   B 1 84  ? 51.864 -8.173  -3.220  1.00 16.86 ?  84   SER   B HB2  1 
ATOM   5339 H  HB3  . SER   B 1 84  ? 52.408 -9.541  -2.619  1.00 16.86 ?  84   SER   B HB3  1 
ATOM   5340 H  HG   . SER   B 1 84  ? 53.470 -9.010  -4.473  1.00 18.45 ?  84   SER   B HG   1 
ATOM   5341 N  N    . GLY   B 1 85  ? 50.785 -11.435 -5.222  1.00 12.19 ?  85   GLY   B N    1 
ATOM   5342 C  CA   . GLY   B 1 85  ? 51.132 -12.735 -5.740  1.00 12.92 ?  85   GLY   B CA   1 
ATOM   5343 C  C    . GLY   B 1 85  ? 52.598 -12.921 -6.055  1.00 12.07 ?  85   GLY   B C    1 
ATOM   5344 O  O    . GLY   B 1 85  ? 52.977 -13.999 -6.516  1.00 12.49 ?  85   GLY   B O    1 
ATOM   5345 H  H    . GLY   B 1 85  ? 50.633 -10.852 -5.828  1.00 14.64 ?  85   GLY   B H    1 
ATOM   5346 H  HA2  . GLY   B 1 85  ? 50.880 -13.418 -5.092  1.00 15.51 ?  85   GLY   B HA2  1 
ATOM   5347 H  HA3  . GLY   B 1 85  ? 50.633 -12.901 -6.551  1.00 15.51 ?  85   GLY   B HA3  1 
ATOM   5348 N  N    . HIS   B 1 86  ? 53.448 -11.920 -5.834  1.00 11.96 ?  86   HIS   B N    1 
ATOM   5349 C  CA   . HIS   B 1 86  ? 54.913 -12.088 -5.928  1.00 12.02 ?  86   HIS   B CA   1 
ATOM   5350 C  C    . HIS   B 1 86  ? 55.288 -12.595 -7.318  1.00 12.14 ?  86   HIS   B C    1 
ATOM   5351 O  O    . HIS   B 1 86  ? 54.897 -11.979 -8.321  1.00 12.97 ?  86   HIS   B O    1 
ATOM   5352 C  CB   . HIS   B 1 86  ? 55.422 -12.925 -4.756  1.00 12.37 ?  86   HIS   B CB   1 
ATOM   5353 C  CG   . HIS   B 1 86  ? 55.108 -12.323 -3.430  1.00 12.74 ?  86   HIS   B CG   1 
ATOM   5354 N  ND1  . HIS   B 1 86  ? 55.925 -11.394 -2.822  1.00 14.10 ?  86   HIS   B ND1  1 
ATOM   5355 C  CD2  . HIS   B 1 86  ? 54.034 -12.472 -2.619  1.00 12.85 ?  86   HIS   B CD2  1 
ATOM   5356 C  CE1  . HIS   B 1 86  ? 55.366 -11.002 -1.691  1.00 13.93 ?  86   HIS   B CE1  1 
ATOM   5357 N  NE2  . HIS   B 1 86  ? 54.219 -11.640 -1.544  1.00 13.25 ?  86   HIS   B NE2  1 
ATOM   5358 H  H    . HIS   B 1 86  ? 53.204 -11.124 -5.629  1.00 14.36 ?  86   HIS   B H    1 
ATOM   5359 H  HA   . HIS   B 1 86  ? 55.315 -11.215 -5.835  1.00 14.44 ?  86   HIS   B HA   1 
ATOM   5360 H  HB2  . HIS   B 1 86  ? 55.017 -13.805 -4.789  1.00 14.86 ?  86   HIS   B HB2  1 
ATOM   5361 H  HB3  . HIS   B 1 86  ? 56.390 -13.006 -4.823  1.00 14.86 ?  86   HIS   B HB3  1 
ATOM   5362 H  HD2  . HIS   B 1 86  ? 53.304 -13.032 -2.769  1.00 15.43 ?  86   HIS   B HD2  1 
ATOM   5363 H  HE1  . HIS   B 1 86  ? 55.728 -10.397 -1.086  1.00 16.73 ?  86   HIS   B HE1  1 
ATOM   5364 H  HE2  . HIS   B 1 86  ? 53.683 -11.569 -0.875  1.00 15.92 ?  86   HIS   B HE2  1 
ATOM   5365 N  N    . ASN   B 1 87  ? 56.056 -13.677 -7.430  1.00 12.61 ?  87   ASN   B N    1 
ATOM   5366 C  CA   . ASN   B 1 87  ? 56.445 -14.254 -8.707  1.00 13.31 ?  87   ASN   B CA   1 
ATOM   5367 C  C    . ASN   B 1 87  ? 55.461 -15.294 -9.210  1.00 13.03 ?  87   ASN   B C    1 
ATOM   5368 O  O    . ASN   B 1 87  ? 55.773 -15.998 -10.176 1.00 14.68 ?  87   ASN   B O    1 
ATOM   5369 C  CB   . ASN   B 1 87  ? 57.838 -14.887 -8.598  1.00 15.39 ?  87   ASN   B CB   1 
ATOM   5370 C  CG   . ASN   B 1 87  ? 57.908 -15.986 -7.545  1.00 16.33 ?  87   ASN   B CG   1 
ATOM   5371 O  OD1  . ASN   B 1 87  ? 57.262 -15.905 -6.495  1.00 15.29 ?  87   ASN   B OD1  1 
ATOM   5372 N  ND2  . ASN   B 1 87  ? 58.684 -17.034 -7.833  1.00 18.63 ?  87   ASN   B ND2  1 
ATOM   5373 H  H    . ASN   B 1 87  ? 56.358 -14.116 -6.758  1.00 15.14 ?  87   ASN   B H    1 
ATOM   5374 H  HA   . ASN   B 1 87  ? 56.488 -13.550 -9.368  1.00 15.98 ?  87   ASN   B HA   1 
ATOM   5375 H  HB2  . ASN   B 1 87  ? 58.077 -15.277 -9.458  1.00 18.49 ?  87   ASN   B HB2  1 
ATOM   5376 H  HB3  . ASN   B 1 87  ? 58.477 -14.200 -8.359  1.00 18.49 ?  87   ASN   B HB3  1 
ATOM   5377 H  HD21 . ASN   B 1 87  ? 58.764 -17.679 -7.273  1.00 22.37 ?  87   ASN   B HD21 1 
ATOM   5378 H  HD22 . ASN   B 1 87  ? 59.120 -17.059 -8.579  1.00 22.37 ?  87   ASN   B HD22 1 
ATOM   5379 N  N    . LEU   B 1 88  ? 54.287 -15.401 -8.588  1.00 12.36 ?  88   LEU   B N    1 
ATOM   5380 C  CA   . LEU   B 1 88  ? 53.305 -16.428 -8.916  1.00 12.54 ?  88   LEU   B CA   1 
ATOM   5381 C  C    . LEU   B 1 88  ? 52.067 -15.905 -9.630  1.00 12.43 ?  88   LEU   B C    1 
ATOM   5382 O  O    . LEU   B 1 88  ? 51.463 -16.644 -10.417 1.00 13.97 ?  88   LEU   B O    1 
ATOM   5383 C  CB   . LEU   B 1 88  ? 52.841 -17.118 -7.630  1.00 13.40 ?  88   LEU   B CB   1 
ATOM   5384 C  CG   . LEU   B 1 88  ? 53.964 -17.778 -6.843  1.00 15.70 ?  88   LEU   B CG   1 
ATOM   5385 C  CD1  . LEU   B 1 88  ? 53.487 -18.105 -5.441  1.00 17.15 ?  88   LEU   B CD1  1 
ATOM   5386 C  CD2  . LEU   B 1 88  ? 54.415 -19.025 -7.573  1.00 19.25 ?  88   LEU   B CD2  1 
ATOM   5387 H  H    . LEU   B 1 88  ? 54.033 -14.881 -7.945  1.00 14.85 ?  88   LEU   B H    1 
ATOM   5388 H  HA   . LEU   B 1 88  ? 53.720 -17.092 -9.480  1.00 15.06 ?  88   LEU   B HA   1 
ATOM   5389 H  HB2  . LEU   B 1 88  ? 52.422 -16.461 -7.052  1.00 16.09 ?  88   LEU   B HB2  1 
ATOM   5390 H  HB3  . LEU   B 1 88  ? 52.196 -17.807 -7.861  1.00 16.09 ?  88   LEU   B HB3  1 
ATOM   5391 H  HG   . LEU   B 1 88  ? 54.716 -17.167 -6.783  1.00 18.86 ?  88   LEU   B HG   1 
ATOM   5392 H  HD11 . LEU   B 1 88  ? 54.152 -18.659 -5.007  1.00 20.60 ?  88   LEU   B HD11 1 
ATOM   5393 H  HD12 . LEU   B 1 88  ? 53.371 -17.277 -4.949  1.00 20.60 ?  88   LEU   B HD12 1 
ATOM   5394 H  HD13 . LEU   B 1 88  ? 52.645 -18.577 -5.500  1.00 20.60 ?  88   LEU   B HD13 1 
ATOM   5395 H  HD21 . LEU   B 1 88  ? 55.077 -19.481 -7.031  1.00 23.11 ?  88   LEU   B HD21 1 
ATOM   5396 H  HD22 . LEU   B 1 88  ? 53.649 -19.602 -7.715  1.00 23.11 ?  88   LEU   B HD22 1 
ATOM   5397 H  HD23 . LEU   B 1 88  ? 54.803 -18.774 -8.426  1.00 23.11 ?  88   LEU   B HD23 1 
ATOM   5398 N  N    . ALA   B 1 89  ? 51.663 -14.670 -9.358  1.00 11.48 ?  89   ALA   B N    1 
ATOM   5399 C  CA   . ALA   B 1 89  ? 50.367 -14.173 -9.798  1.00 11.00 ?  89   ALA   B CA   1 
ATOM   5400 C  C    . ALA   B 1 89  ? 50.343 -12.684 -9.511  1.00 11.28 ?  89   ALA   B C    1 
ATOM   5401 O  O    . ALA   B 1 89  ? 51.183 -12.175 -8.771  1.00 12.22 ?  89   ALA   B O    1 
ATOM   5402 C  CB   . ALA   B 1 89  ? 49.241 -14.857 -9.032  1.00 11.28 ?  89   ALA   B CB   1 
ATOM   5403 H  H    . ALA   B 1 89  ? 52.123 -14.091 -8.916  1.00 13.80 ?  89   ALA   B H    1 
ATOM   5404 H  HA   . ALA   B 1 89  ? 50.251 -14.322 -10.755 1.00 13.21 ?  89   ALA   B HA   1 
ATOM   5405 H  HB1  . ALA   B 1 89  ? 48.391 -14.524 -9.357  1.00 13.55 ?  89   ALA   B HB1  1 
ATOM   5406 H  HB2  . ALA   B 1 89  ? 49.298 -15.817 -9.185  1.00 13.55 ?  89   ALA   B HB2  1 
ATOM   5407 H  HB3  . ALA   B 1 89  ? 49.342 -14.665 -8.092  1.00 13.55 ?  89   ALA   B HB3  1 
ATOM   5408 N  N    . LYS   B 1 90  ? 49.358 -11.984 -10.073 1.00 12.45 ?  90   LYS   B N    1 
ATOM   5409 C  CA   . LYS   B 1 90  ? 49.172 -10.594 -9.669  1.00 12.57 ?  90   LYS   B CA   1 
ATOM   5410 C  C    . LYS   B 1 90  ? 48.858 -10.518 -8.180  1.00 12.28 ?  90   LYS   B C    1 
ATOM   5411 O  O    . LYS   B 1 90  ? 49.513 -9.780  -7.429  1.00 13.17 ?  90   LYS   B O    1 
ATOM   5412 C  CB   . LYS   B 1 90  ? 48.092 -9.931  -10.526 1.00 14.02 ?  90   LYS   B CB   1 
ATOM   5413 C  CG   . LYS   B 1 90  ? 47.788 -8.486  -10.148 1.00 14.87 ?  90   LYS   B CG   1 
ATOM   5414 C  CD   . LYS   B 1 90  ? 49.000 -7.586  -10.219 1.00 17.55 ?  90   LYS   B CD   1 
ATOM   5415 C  CE   . LYS   B 1 90  ? 48.554 -6.166  -9.964  1.00 20.11 ?  90   LYS   B CE   1 
ATOM   5416 N  NZ   . LYS   B 1 90  ? 49.697 -5.237  -9.822  1.00 20.23 ?  90   LYS   B NZ   1 
ATOM   5417 H  H    . LYS   B 1 90  ? 48.806 -12.282 -10.662 1.00 14.95 ?  90   LYS   B H    1 
ATOM   5418 H  HA   . LYS   B 1 90  ? 49.999 -10.116 -9.822  1.00 15.09 ?  90   LYS   B HA   1 
ATOM   5419 H  HB2  . LYS   B 1 90  ? 48.382 -9.935  -11.456 1.00 16.84 ?  90   LYS   B HB2  1 
ATOM   5420 H  HB3  . LYS   B 1 90  ? 47.268 -10.438 -10.446 1.00 16.84 ?  90   LYS   B HB3  1 
ATOM   5421 H  HG2  . LYS   B 1 90  ? 47.119 -8.135  -10.759 1.00 17.85 ?  90   LYS   B HG2  1 
ATOM   5422 H  HG3  . LYS   B 1 90  ? 47.444 -8.462  -9.240  1.00 17.85 ?  90   LYS   B HG3  1 
ATOM   5423 H  HD2  . LYS   B 1 90  ? 49.640 -7.840  -9.534  1.00 21.07 ?  90   LYS   B HD2  1 
ATOM   5424 H  HD3  . LYS   B 1 90  ? 49.400 -7.638  -11.101 1.00 21.07 ?  90   LYS   B HD3  1 
ATOM   5425 H  HE2  . LYS   B 1 90  ? 48.013 -5.858  -10.710 1.00 24.14 ?  90   LYS   B HE2  1 
ATOM   5426 H  HE3  . LYS   B 1 90  ? 48.039 -6.128  -9.143  1.00 24.14 ?  90   LYS   B HE3  1 
ATOM   5427 H  HZ1  . LYS   B 1 90  ? 49.407 -4.406  -9.675  1.00 24.29 ?  90   LYS   B HZ1  1 
ATOM   5428 H  HZ2  . LYS   B 1 90  ? 50.213 -5.485  -9.140  1.00 24.29 ?  90   LYS   B HZ2  1 
ATOM   5429 H  HZ3  . LYS   B 1 90  ? 50.189 -5.238  -10.567 1.00 24.29 ?  90   LYS   B HZ3  1 
ATOM   5430 N  N    . HIS   B 1 91  ? 47.897 -11.333 -7.728  1.00 10.61 ?  91   HIS   B N    1 
ATOM   5431 C  CA   . HIS   B 1 91  ? 47.431 -11.368 -6.354  1.00 10.83 ?  91   HIS   B CA   1 
ATOM   5432 C  C    . HIS   B 1 91  ? 47.427 -12.797 -5.838  1.00 10.31 ?  91   HIS   B C    1 
ATOM   5433 O  O    . HIS   B 1 91  ? 47.191 -13.745 -6.595  1.00 10.74 ?  91   HIS   B O    1 
ATOM   5434 C  CB   . HIS   B 1 91  ? 45.978 -10.880 -6.235  1.00 12.45 ?  91   HIS   B CB   1 
ATOM   5435 C  CG   . HIS   B 1 91  ? 45.771 -9.470  -6.667  1.00 15.95 ?  91   HIS   B CG   1 
ATOM   5436 N  ND1  . HIS   B 1 91  ? 46.380 -8.399  -6.048  1.00 18.50 ?  91   HIS   B ND1  1 
ATOM   5437 C  CD2  . HIS   B 1 91  ? 44.986 -8.948  -7.635  1.00 18.05 ?  91   HIS   B CD2  1 
ATOM   5438 C  CE1  . HIS   B 1 91  ? 45.998 -7.276  -6.633  1.00 19.46 ?  91   HIS   B CE1  1 
ATOM   5439 N  NE2  . HIS   B 1 91  ? 45.145 -7.582  -7.595  1.00 19.70 ?  91   HIS   B NE2  1 
ATOM   5440 H  H    . HIS   B 1 91  ? 47.481 -11.893 -8.233  1.00 12.75 ?  91   HIS   B H    1 
ATOM   5441 H  HA   . HIS   B 1 91  ? 48.003 -10.812 -5.790  1.00 13.02 ?  91   HIS   B HA   1 
ATOM   5442 H  HB2  . HIS   B 1 91  ? 45.416 -11.444 -6.790  1.00 14.96 ?  91   HIS   B HB2  1 
ATOM   5443 H  HB3  . HIS   B 1 91  ? 45.698 -10.952 -5.307  1.00 14.96 ?  91   HIS   B HB3  1 
ATOM   5444 H  HD1  . HIS   B 1 91  ? 46.931 -8.452  -5.387  1.00 22.22 ?  91   HIS   B HD1  1 
ATOM   5445 H  HD2  . HIS   B 1 91  ? 44.446 -9.417  -8.226  1.00 21.67 ?  91   HIS   B HD2  1 
ATOM   5446 H  HE1  . HIS   B 1 91  ? 46.275 -6.418  -6.398  1.00 23.37 ?  91   HIS   B HE1  1 
ATOM   5447 N  N    . CYS   B 1 92  ? 47.621 -12.931 -4.533  1.00 9.90  ?  92   CYS   B N    1 
ATOM   5448 C  CA   . CYS   B 1 92  ? 47.323 -14.164 -3.821  1.00 9.89  ?  92   CYS   B CA   1 
ATOM   5449 C  C    . CYS   B 1 92  ? 46.097 -13.930 -2.943  1.00 9.57  ?  92   CYS   B C    1 
ATOM   5450 O  O    . CYS   B 1 92  ? 46.091 -13.024 -2.097  1.00 10.36 ?  92   CYS   B O    1 
ATOM   5451 C  CB   . CYS   B 1 92  ? 48.505 -14.624 -2.974  1.00 10.31 ?  92   CYS   B CB   1 
ATOM   5452 S  SG   . CYS   B 1 92  ? 48.140 -16.165 -2.074  1.00 10.53 ?  92   CYS   B SG   1 
ATOM   5453 H  H    . CYS   B 1 92  ? 47.942 -12.306 -4.027  1.00 11.90 ?  92   CYS   B H    1 
ATOM   5454 H  HA   . CYS   B 1 92  ? 47.119 -14.857 -4.467  1.00 11.88 ?  92   CYS   B HA   1 
ATOM   5455 H  HB2  . CYS   B 1 92  ? 49.265 -14.782 -3.551  1.00 12.38 ?  92   CYS   B HB2  1 
ATOM   5456 H  HB3  . CYS   B 1 92  ? 48.710 -13.935 -2.324  1.00 12.38 ?  92   CYS   B HB3  1 
ATOM   5457 H  HG   . CYS   B 1 92  ? 49.114 -16.480 -1.446  1.00 12.65 ?  92   CYS   B HG   1 
ATOM   5458 N  N    . LEU   B 1 93  ? 45.063 -14.741 -3.156  1.00 9.42  ?  93   LEU   B N    1 
ATOM   5459 C  CA   . LEU   B 1 93  ? 43.886 -14.757 -2.295  1.00 9.79  ?  93   LEU   B CA   1 
ATOM   5460 C  C    . LEU   B 1 93  ? 44.114 -15.818 -1.228  1.00 9.37  ?  93   LEU   B C    1 
ATOM   5461 O  O    . LEU   B 1 93  ? 44.068 -17.016 -1.520  1.00 9.76  ?  93   LEU   B O    1 
ATOM   5462 C  CB   . LEU   B 1 93  ? 42.620 -15.045 -3.100  1.00 10.00 ?  93   LEU   B CB   1 
ATOM   5463 C  CG   . LEU   B 1 93  ? 41.326 -15.062 -2.282  1.00 10.75 ?  93   LEU   B CG   1 
ATOM   5464 C  CD1  . LEU   B 1 93  ? 40.963 -13.673 -1.778  1.00 11.24 ?  93   LEU   B CD1  1 
ATOM   5465 C  CD2  . LEU   B 1 93  ? 40.191 -15.656 -3.105  1.00 11.19 ?  93   LEU   B CD2  1 
ATOM   5466 H  H    . LEU   B 1 93  ? 45.020 -15.312 -3.811  1.00 11.32 ?  93   LEU   B H    1 
ATOM   5467 H  HA   . LEU   B 1 93  ? 43.793 -13.895 -1.867  1.00 11.77 ?  93   LEU   B HA   1 
ATOM   5468 H  HB2  . LEU   B 1 93  ? 42.524 -14.355 -3.780  1.00 12.01 ?  93   LEU   B HB2  1 
ATOM   5469 H  HB3  . LEU   B 1 93  ? 42.708 -15.908 -3.524  1.00 12.01 ?  93   LEU   B HB3  1 
ATOM   5470 H  HG   . LEU   B 1 93  ? 41.454 -15.625 -1.508  1.00 12.92 ?  93   LEU   B HG   1 
ATOM   5471 H  HD11 . LEU   B 1 93  ? 40.117 -13.718 -1.311  1.00 13.50 ?  93   LEU   B HD11 1 
ATOM   5472 H  HD12 . LEU   B 1 93  ? 41.660 -13.363 -1.178  1.00 13.50 ?  93   LEU   B HD12 1 
ATOM   5473 H  HD13 . LEU   B 1 93  ? 40.891 -13.071 -2.538  1.00 13.50 ?  93   LEU   B HD13 1 
ATOM   5474 H  HD21 . LEU   B 1 93  ? 39.377 -15.649 -2.575  1.00 13.44 ?  93   LEU   B HD21 1 
ATOM   5475 H  HD22 . LEU   B 1 93  ? 40.064 -15.125 -3.907  1.00 13.44 ?  93   LEU   B HD22 1 
ATOM   5476 H  HD23 . LEU   B 1 93  ? 40.418 -16.568 -3.346  1.00 13.44 ?  93   LEU   B HD23 1 
ATOM   5477 N  N    . HIS   B 1 94  ? 44.392 -15.379 -0.006  1.00 9.41  ?  94   HIS   B N    1 
ATOM   5478 C  CA   . HIS   B 1 94  ? 44.607 -16.282 1.117   1.00 9.50  ?  94   HIS   B CA   1 
ATOM   5479 C  C    . HIS   B 1 94  ? 43.244 -16.633 1.697   1.00 9.82  ?  94   HIS   B C    1 
ATOM   5480 O  O    . HIS   B 1 94  ? 42.578 -15.757 2.249   1.00 11.13 ?  94   HIS   B O    1 
ATOM   5481 C  CB   . HIS   B 1 94  ? 45.478 -15.609 2.175   1.00 9.98  ?  94   HIS   B CB   1 
ATOM   5482 C  CG   . HIS   B 1 94  ? 46.860 -15.308 1.703   1.00 9.60  ?  94   HIS   B CG   1 
ATOM   5483 N  ND1  . HIS   B 1 94  ? 47.888 -16.220 1.788   1.00 9.96  ?  94   HIS   B ND1  1 
ATOM   5484 C  CD2  . HIS   B 1 94  ? 47.368 -14.199 1.109   1.00 10.17 ?  94   HIS   B CD2  1 
ATOM   5485 C  CE1  . HIS   B 1 94  ? 48.976 -15.671 1.277   1.00 10.16 ?  94   HIS   B CE1  1 
ATOM   5486 N  NE2  . HIS   B 1 94  ? 48.689 -14.449 0.855   1.00 10.37 ?  94   HIS   B NE2  1 
ATOM   5487 H  H    . HIS   B 1 94  ? 44.458 -14.541 0.199   1.00 11.31 ?  94   HIS   B H    1 
ATOM   5488 H  HA   . HIS   B 1 94  ? 45.041 -17.089 0.811   1.00 11.42 ?  94   HIS   B HA   1 
ATOM   5489 H  HB2  . HIS   B 1 94  ? 45.065 -14.772 2.437   1.00 11.99 ?  94   HIS   B HB2  1 
ATOM   5490 H  HB3  . HIS   B 1 94  ? 45.548 -16.198 2.940   1.00 11.99 ?  94   HIS   B HB3  1 
ATOM   5491 H  HD2  . HIS   B 1 94  ? 46.909 -13.418 0.910   1.00 12.21 ?  94   HIS   B HD2  1 
ATOM   5492 H  HE1  . HIS   B 1 94  ? 49.809 -16.089 1.224   1.00 12.21 ?  94   HIS   B HE1  1 
ATOM   5493 H  HE2  . HIS   B 1 94  ? 49.245 -13.910 0.491   1.00 12.46 ?  94   HIS   B HE2  1 
ATOM   5494 N  N    . VAL   B 1 95  ? 42.808 -17.888 1.549   1.00 9.63  ?  95   VAL   B N    1 
ATOM   5495 C  CA   . VAL   B 1 95  ? 41.483 -18.326 1.985   1.00 9.84  ?  95   VAL   B CA   1 
ATOM   5496 C  C    . VAL   B 1 95  ? 41.650 -19.363 3.080   1.00 10.02 ?  95   VAL   B C    1 
ATOM   5497 O  O    . VAL   B 1 95  ? 42.420 -20.315 2.918   1.00 10.51 ?  95   VAL   B O    1 
ATOM   5498 C  CB   . VAL   B 1 95  ? 40.662 -18.927 0.828   1.00 10.10 ?  95   VAL   B CB   1 
ATOM   5499 C  CG1  . VAL   B 1 95  ? 39.295 -19.374 1.324   1.00 11.02 ?  95   VAL   B CG1  1 
ATOM   5500 C  CG2  . VAL   B 1 95  ? 40.530 -17.950 -0.302  1.00 10.22 ?  95   VAL   B CG2  1 
ATOM   5501 H  H    . VAL   B 1 95  ? 43.270 -18.512 1.181   1.00 11.57 ?  95   VAL   B H    1 
ATOM   5502 H  HA   . VAL   B 1 95  ? 40.991 -17.571 2.349   1.00 11.82 ?  95   VAL   B HA   1 
ATOM   5503 H  HB   . VAL   B 1 95  ? 41.121 -19.708 0.491   1.00 12.14 ?  95   VAL   B HB   1 
ATOM   5504 H  HG11 . VAL   B 1 95  ? 38.719 -19.557 0.558   1.00 13.23 ?  95   VAL   B HG11 1 
ATOM   5505 H  HG12 . VAL   B 1 95  ? 39.388 -20.184 1.854   1.00 13.23 ?  95   VAL   B HG12 1 
ATOM   5506 H  HG13 . VAL   B 1 95  ? 38.897 -18.672 1.864   1.00 13.23 ?  95   VAL   B HG13 1 
ATOM   5507 H  HG21 . VAL   B 1 95  ? 39.951 -18.332 -0.981  1.00 12.28 ?  95   VAL   B HG21 1 
ATOM   5508 H  HG22 . VAL   B 1 95  ? 40.141 -17.128 0.037   1.00 12.28 ?  95   VAL   B HG22 1 
ATOM   5509 H  HG23 . VAL   B 1 95  ? 41.407 -17.777 -0.669  1.00 12.28 ?  95   VAL   B HG23 1 
ATOM   5510 N  N    . VAL   B 1 96  ? 40.928 -19.188 4.180   1.00 10.43 ?  96   VAL   B N    1 
ATOM   5511 C  CA   . VAL   B 1 96  ? 41.013 -20.104 5.316   1.00 10.76 ?  96   VAL   B CA   1 
ATOM   5512 C  C    . VAL   B 1 96  ? 39.823 -21.065 5.272   1.00 11.22 ?  96   VAL   B C    1 
ATOM   5513 O  O    . VAL   B 1 96  ? 38.707 -20.709 5.656   1.00 12.09 ?  96   VAL   B O    1 
ATOM   5514 C  CB   . VAL   B 1 96  ? 41.064 -19.355 6.650   1.00 11.52 ?  96   VAL   B CB   1 
ATOM   5515 C  CG1  . VAL   B 1 96  ? 41.217 -20.349 7.794   1.00 12.34 ?  96   VAL   B CG1  1 
ATOM   5516 C  CG2  . VAL   B 1 96  ? 42.189 -18.334 6.667   1.00 12.46 ?  96   VAL   B CG2  1 
ATOM   5517 H  H    . VAL   B 1 96  ? 40.376 -18.541 4.300   1.00 12.53 ?  96   VAL   B H    1 
ATOM   5518 H  HA   . VAL   B 1 96  ? 41.827 -20.631 5.241   1.00 12.93 ?  96   VAL   B HA   1 
ATOM   5519 H  HB   . VAL   B 1 96  ? 40.225 -18.887 6.782   1.00 13.84 ?  96   VAL   B HB   1 
ATOM   5520 H  HG11 . VAL   B 1 96  ? 41.417 -19.864 8.614   1.00 14.82 ?  96   VAL   B HG11 1 
ATOM   5521 H  HG12 . VAL   B 1 96  ? 40.391 -20.847 7.906   1.00 14.82 ?  96   VAL   B HG12 1 
ATOM   5522 H  HG13 . VAL   B 1 96  ? 41.945 -20.960 7.594   1.00 14.82 ?  96   VAL   B HG13 1 
ATOM   5523 H  HG21 . VAL   B 1 96  ? 42.233 -17.923 7.547   1.00 14.97 ?  96   VAL   B HG21 1 
ATOM   5524 H  HG22 . VAL   B 1 96  ? 43.025 -18.776 6.466   1.00 14.97 ?  96   VAL   B HG22 1 
ATOM   5525 H  HG23 . VAL   B 1 96  ? 42.004 -17.652 5.999   1.00 14.97 ?  96   VAL   B HG23 1 
ATOM   5526 N  N    . GLY   B 1 97  ? 40.051 -22.295 4.823   1.00 11.27 ?  97   GLY   B N    1 
ATOM   5527 C  CA   . GLY   B 1 97  ? 39.079 -23.351 4.999   1.00 12.10 ?  97   GLY   B CA   1 
ATOM   5528 C  C    . GLY   B 1 97  ? 39.224 -23.963 6.375   1.00 13.11 ?  97   GLY   B C    1 
ATOM   5529 O  O    . GLY   B 1 97  ? 40.271 -23.837 7.019   1.00 13.56 ?  97   GLY   B O    1 
ATOM   5530 H  H    . GLY   B 1 97  ? 40.768 -22.536 4.406   1.00 13.54 ?  97   GLY   B H    1 
ATOM   5531 H  HA2  . GLY   B 1 97  ? 38.183 -22.983 4.897   1.00 14.53 ?  97   GLY   B HA2  1 
ATOM   5532 H  HA3  . GLY   B 1 97  ? 39.211 -24.036 4.326   1.00 14.53 ?  97   GLY   B HA3  1 
ATOM   5533 N  N    . PRO   B 1 98  ? 38.179 -24.638 6.856   1.00 14.12 ?  98   PRO   B N    1 
ATOM   5534 C  CA   . PRO   B 1 98  ? 38.279 -25.326 8.147   1.00 15.15 ?  98   PRO   B CA   1 
ATOM   5535 C  C    . PRO   B 1 98  ? 39.303 -26.449 8.096   1.00 15.10 ?  98   PRO   B C    1 
ATOM   5536 O  O    . PRO   B 1 98  ? 39.401 -27.186 7.115   1.00 15.27 ?  98   PRO   B O    1 
ATOM   5537 C  CB   . PRO   B 1 98  ? 36.862 -25.867 8.367   1.00 15.94 ?  98   PRO   B CB   1 
ATOM   5538 C  CG   . PRO   B 1 98  ? 36.292 -26.004 7.000   1.00 15.71 ?  98   PRO   B CG   1 
ATOM   5539 C  CD   . PRO   B 1 98  ? 36.856 -24.832 6.233   1.00 14.61 ?  98   PRO   B CD   1 
ATOM   5540 H  HA   . PRO   B 1 98  ? 38.510 -24.700 8.847   1.00 18.20 ?  98   PRO   B HA   1 
ATOM   5541 H  HB2  . PRO   B 1 98  ? 36.908 -26.730 8.809   1.00 19.15 ?  98   PRO   B HB2  1 
ATOM   5542 H  HB3  . PRO   B 1 98  ? 36.348 -25.237 8.891   1.00 19.15 ?  98   PRO   B HB3  1 
ATOM   5543 H  HG2  . PRO   B 1 98  ? 36.580 -26.848 6.609   1.00 18.86 ?  98   PRO   B HG2  1 
ATOM   5544 H  HG3  . PRO   B 1 98  ? 35.325 -25.960 7.043   1.00 18.86 ?  98   PRO   B HG3  1 
ATOM   5545 H  HD2  . PRO   B 1 98  ? 36.947 -25.059 5.289   1.00 17.55 ?  98   PRO   B HD2  1 
ATOM   5546 H  HD3  . PRO   B 1 98  ? 36.304 -24.047 6.355   1.00 17.55 ?  98   PRO   B HD3  1 
ATOM   5547 N  N    . ASN   B 1 99  ? 40.060 -26.577 9.176   1.00 16.29 ?  99   ASN   B N    1 
ATOM   5548 C  CA   . ASN   B 1 99  ? 41.034 -27.653 9.336   1.00 17.16 ?  99   ASN   B CA   1 
ATOM   5549 C  C    . ASN   B 1 99  ? 40.405 -28.730 10.218  1.00 19.88 ?  99   ASN   B C    1 
ATOM   5550 O  O    . ASN   B 1 99  ? 40.333 -28.580 11.441  1.00 20.55 ?  99   ASN   B O    1 
ATOM   5551 C  CB   . ASN   B 1 99  ? 42.315 -27.098 9.946   1.00 17.42 ?  99   ASN   B CB   1 
ATOM   5552 C  CG   . ASN   B 1 99  ? 43.445 -28.103 9.940   1.00 18.06 ?  99   ASN   B CG   1 
ATOM   5553 O  OD1  . ASN   B 1 99  ? 43.226 -29.291 10.128  1.00 18.94 ?  99   ASN   B OD1  1 
ATOM   5554 N  ND2  . ASN   B 1 99  ? 44.659 -27.632 9.713   1.00 18.22 ?  99   ASN   B ND2  1 
ATOM   5555 H  H    . ASN   B 1 99  ? 40.024 -26.041 9.844   1.00 19.57 ?  99   ASN   B H    1 
ATOM   5556 H  HA   . ASN   B 1 99  ? 41.236 -28.044 8.472   1.00 20.60 ?  99   ASN   B HA   1 
ATOM   5557 H  HB2  . ASN   B 1 99  ? 42.592 -26.327 9.442   1.00 20.92 ?  99   ASN   B HB2  1 
ATOM   5558 H  HB3  . ASN   B 1 99  ? 42.136 -26.854 10.870  1.00 20.92 ?  99   ASN   B HB3  1 
ATOM   5559 H  HD21 . ASN   B 1 99  ? 45.329 -28.166 9.698   1.00 21.87 ?  99   ASN   B HD21 1 
ATOM   5560 H  HD22 . ASN   B 1 99  ? 44.768 -26.791 9.591   1.00 21.87 ?  99   ASN   B HD22 1 
ATOM   5561 N  N    A VAL   B 1 100 ? 39.934 -29.812 9.591   0.62 22.09 ?  100  VAL   B N    1 
ATOM   5562 N  N    B VAL   B 1 100 ? 39.952 -29.818 9.585   0.38 22.10 ?  100  VAL   B N    1 
ATOM   5563 C  CA   A VAL   B 1 100 ? 39.325 -30.905 10.347  0.62 24.63 ?  100  VAL   B CA   1 
ATOM   5564 C  CA   B VAL   B 1 100 ? 39.330 -30.918 10.319  0.38 24.44 ?  100  VAL   B CA   1 
ATOM   5565 C  C    A VAL   B 1 100 ? 40.343 -31.562 11.271  0.62 24.83 ?  100  VAL   B C    1 
ATOM   5566 C  C    B VAL   B 1 100 ? 40.336 -31.594 11.244  0.38 24.88 ?  100  VAL   B C    1 
ATOM   5567 O  O    A VAL   B 1 100 ? 39.991 -32.034 12.359  0.62 25.81 ?  100  VAL   B O    1 
ATOM   5568 O  O    B VAL   B 1 100 ? 39.966 -32.113 12.304  0.38 25.50 ?  100  VAL   B O    1 
ATOM   5569 C  CB   A VAL   B 1 100 ? 38.657 -31.916 9.391   0.62 27.31 ?  100  VAL   B CB   1 
ATOM   5570 C  CB   B VAL   B 1 100 ? 38.679 -31.910 9.336   0.38 26.41 ?  100  VAL   B CB   1 
ATOM   5571 C  CG1  A VAL   B 1 100 ? 38.170 -33.137 10.157  0.62 28.21 ?  100  VAL   B CG1  1 
ATOM   5572 C  CG1  B VAL   B 1 100 ? 38.178 -33.149 10.066  0.38 27.04 ?  100  VAL   B CG1  1 
ATOM   5573 C  CG2  A VAL   B 1 100 ? 37.496 -31.259 8.655   0.62 28.04 ?  100  VAL   B CG2  1 
ATOM   5574 C  CG2  B VAL   B 1 100 ? 37.536 -31.238 8.590   0.38 27.01 ?  100  VAL   B CG2  1 
ATOM   5575 H  H    A VAL   B 1 100 ? 39.946 -29.929 8.734   0.62 26.52 ?  100  VAL   B H    1 
ATOM   5576 H  H    B VAL   B 1 100 ? 39.992 -29.941 8.731   0.38 26.53 ?  100  VAL   B H    1 
ATOM   5577 H  HA   A VAL   B 1 100 ? 38.618 -30.535 10.899  0.62 29.58 ?  100  VAL   B HA   1 
ATOM   5578 H  HA   B VAL   B 1 100 ? 38.621 -30.558 10.871  0.38 29.34 ?  100  VAL   B HA   1 
ATOM   5579 H  HB   A VAL   B 1 100 ? 39.304 -32.215 8.731   0.62 32.79 ?  100  VAL   B HB   1 
ATOM   5580 H  HB   B VAL   B 1 100 ? 39.337 -32.196 8.683   0.38 31.71 ?  100  VAL   B HB   1 
ATOM   5581 H  HG11 A VAL   B 1 100 ? 37.565 -33.645 9.592   0.62 33.87 ?  100  VAL   B HG11 1 
ATOM   5582 H  HG11 B VAL   B 1 100 ? 37.586 -33.646 9.477   0.38 32.46 ?  100  VAL   B HG11 1 
ATOM   5583 H  HG12 A VAL   B 1 100 ? 38.931 -33.688 10.399  0.62 33.87 ?  100  VAL   B HG12 1 
ATOM   5584 H  HG12 B VAL   B 1 100 ? 38.935 -33.703 10.313  0.38 32.46 ?  100  VAL   B HG12 1 
ATOM   5585 H  HG13 A VAL   B 1 100 ? 37.704 -32.844 10.956  0.62 33.87 ?  100  VAL   B HG13 1 
ATOM   5586 H  HG13 B VAL   B 1 100 ? 37.694 -32.874 10.860  0.38 32.46 ?  100  VAL   B HG13 1 
ATOM   5587 H  HG21 A VAL   B 1 100 ? 37.085 -31.910 8.063   0.62 33.66 ?  100  VAL   B HG21 1 
ATOM   5588 H  HG21 B VAL   B 1 100 ? 37.127 -31.882 7.991   0.38 32.42 ?  100  VAL   B HG21 1 
ATOM   5589 H  HG22 A VAL   B 1 100 ? 36.845 -30.950 9.305   0.62 33.66 ?  100  VAL   B HG22 1 
ATOM   5590 H  HG22 B VAL   B 1 100 ? 36.882 -30.925 9.235   0.38 32.42 ?  100  VAL   B HG22 1 
ATOM   5591 H  HG23 A VAL   B 1 100 ? 37.832 -30.510 8.140   0.62 33.66 ?  100  VAL   B HG23 1 
ATOM   5592 H  HG23 B VAL   B 1 100 ? 37.888 -30.491 8.084   0.38 32.42 ?  100  VAL   B HG23 1 
ATOM   5593 N  N    . ASN   B 1 101 ? 41.615 -31.613 10.861  1.00 25.19 ?  101  ASN   B N    1 
ATOM   5594 C  CA   . ASN   B 1 101 ? 42.654 -32.152 11.738  1.00 27.15 ?  101  ASN   B CA   1 
ATOM   5595 C  C    . ASN   B 1 101 ? 42.840 -31.310 12.995  1.00 30.27 ?  101  ASN   B C    1 
ATOM   5596 O  O    . ASN   B 1 101 ? 43.463 -31.780 13.956  1.00 31.01 ?  101  ASN   B O    1 
ATOM   5597 C  CB   . ASN   B 1 101 ? 43.977 -32.292 10.980  1.00 26.76 ?  101  ASN   B CB   1 
ATOM   5598 C  CG   . ASN   B 1 101 ? 43.953 -33.431 9.977   1.00 25.99 ?  101  ASN   B CG   1 
ATOM   5599 O  OD1  . ASN   B 1 101 ? 43.250 -34.420 10.166  1.00 26.63 ?  101  ASN   B OD1  1 
ATOM   5600 N  ND2  . ASN   B 1 101 ? 44.713 -33.291 8.899   1.00 25.56 ?  101  ASN   B ND2  1 
ATOM   5601 H  H    A ASN   B 1 101 ? 41.891 -31.354 10.087  0.62 30.25 ?  101  ASN   B H    1 
ATOM   5602 H  H    B ASN   B 1 101 ? 41.898 -31.329 10.098  0.38 30.25 ?  101  ASN   B H    1 
ATOM   5603 H  HA   . ASN   B 1 101 ? 42.385 -33.034 12.022  1.00 32.59 ?  101  ASN   B HA   1 
ATOM   5604 H  HB2  . ASN   B 1 101 ? 44.162 -31.473 10.496  1.00 32.12 ?  101  ASN   B HB2  1 
ATOM   5605 H  HB3  . ASN   B 1 101 ? 44.688 -32.470 11.615  1.00 32.12 ?  101  ASN   B HB3  1 
ATOM   5606 H  HD21 . ASN   B 1 101 ? 44.730 -33.911 8.304   1.00 30.69 ?  101  ASN   B HD21 1 
ATOM   5607 H  HD22 . ASN   B 1 101 ? 45.192 -32.585 8.799   1.00 30.69 ?  101  ASN   B HD22 1 
ATOM   5608 N  N    A LYS   B 1 102 ? 42.320 -30.081 13.005  0.62 32.09 ?  102  LYS   B N    1 
ATOM   5609 N  N    B LYS   B 1 102 ? 42.319 -30.083 13.008  0.38 32.11 ?  102  LYS   B N    1 
ATOM   5610 C  CA   A LYS   B 1 102 ? 42.303 -29.228 14.186  0.62 34.51 ?  102  LYS   B CA   1 
ATOM   5611 C  CA   B LYS   B 1 102 ? 42.308 -29.241 14.196  0.38 34.27 ?  102  LYS   B CA   1 
ATOM   5612 C  C    A LYS   B 1 102 ? 40.934 -29.187 14.852  0.62 33.90 ?  102  LYS   B C    1 
ATOM   5613 C  C    B LYS   B 1 102 ? 40.934 -29.186 14.852  0.38 33.89 ?  102  LYS   B C    1 
ATOM   5614 O  O    A LYS   B 1 102 ? 40.726 -28.385 15.767  0.62 34.45 ?  102  LYS   B O    1 
ATOM   5615 O  O    B LYS   B 1 102 ? 40.726 -28.380 15.764  0.38 34.29 ?  102  LYS   B O    1 
ATOM   5616 C  CB   A LYS   B 1 102 ? 42.715 -27.800 13.821  0.62 37.55 ?  102  LYS   B CB   1 
ATOM   5617 C  CB   B LYS   B 1 102 ? 42.769 -27.824 13.852  0.38 36.76 ?  102  LYS   B CB   1 
ATOM   5618 C  CG   A LYS   B 1 102 ? 44.176 -27.612 13.458  0.62 40.34 ?  102  LYS   B CG   1 
ATOM   5619 C  CG   B LYS   B 1 102 ? 44.238 -27.705 13.485  0.38 39.00 ?  102  LYS   B CG   1 
ATOM   5620 C  CD   A LYS   B 1 102 ? 44.426 -26.161 13.069  0.62 42.86 ?  102  LYS   B CD   1 
ATOM   5621 C  CD   B LYS   B 1 102 ? 44.562 -26.285 13.046  0.38 41.00 ?  102  LYS   B CD   1 
ATOM   5622 C  CE   A LYS   B 1 102 ? 45.893 -25.878 12.801  0.62 44.70 ?  102  LYS   B CE   1 
ATOM   5623 C  CE   B LYS   B 1 102 ? 46.053 -26.079 12.841  0.38 42.46 ?  102  LYS   B CE   1 
ATOM   5624 N  NZ   A LYS   B 1 102 ? 46.103 -24.455 12.400  0.62 45.73 ?  102  LYS   B NZ   1 
ATOM   5625 N  NZ   B LYS   B 1 102 ? 46.355 -24.688 12.398  0.38 43.30 ?  102  LYS   B NZ   1 
ATOM   5626 H  H    A LYS   B 1 102 ? 41.958 -29.708 12.317  0.62 38.52 ?  102  LYS   B H    1 
ATOM   5627 H  H    B LYS   B 1 102 ? 41.952 -29.709 12.324  0.38 38.55 ?  102  LYS   B H    1 
ATOM   5628 H  HA   A LYS   B 1 102 ? 42.945 -29.567 14.827  0.62 41.43 ?  102  LYS   B HA   1 
ATOM   5629 H  HA   B LYS   B 1 102 ? 42.936 -29.603 14.839  0.38 41.14 ?  102  LYS   B HA   1 
ATOM   5630 H  HB2  A LYS   B 1 102 ? 42.187 -27.512 13.061  0.62 45.08 ?  102  LYS   B HB2  1 
ATOM   5631 H  HB2  B LYS   B 1 102 ? 42.252 -27.502 13.099  0.38 44.13 ?  102  LYS   B HB2  1 
ATOM   5632 H  HB3  A LYS   B 1 102 ? 42.529 -27.224 14.580  0.62 45.08 ?  102  LYS   B HB3  1 
ATOM   5633 H  HB3  B LYS   B 1 102 ? 42.614 -27.252 14.622  0.38 44.13 ?  102  LYS   B HB3  1 
ATOM   5634 H  HG2  A LYS   B 1 102 ? 44.732 -27.826 14.224  0.62 48.42 ?  102  LYS   B HG2  1 
ATOM   5635 H  HG2  B LYS   B 1 102 ? 44.785 -27.919 14.258  0.38 46.82 ?  102  LYS   B HG2  1 
ATOM   5636 H  HG3  A LYS   B 1 102 ? 44.400 -28.178 12.704  0.62 48.42 ?  102  LYS   B HG3  1 
ATOM   5637 H  HG3  B LYS   B 1 102 ? 44.438 -28.307 12.751  0.38 46.82 ?  102  LYS   B HG3  1 
ATOM   5638 H  HD2  A LYS   B 1 102 ? 43.927 -25.960 12.261  0.62 51.44 ?  102  LYS   B HD2  1 
ATOM   5639 H  HD2  B LYS   B 1 102 ? 44.112 -26.102 12.206  0.38 49.22 ?  102  LYS   B HD2  1 
ATOM   5640 H  HD3  A LYS   B 1 102 ? 44.134 -25.584 13.792  0.62 51.44 ?  102  LYS   B HD3  1 
ATOM   5641 H  HD3  B LYS   B 1 102 ? 44.261 -25.664 13.728  0.38 49.22 ?  102  LYS   B HD3  1 
ATOM   5642 H  HE2  A LYS   B 1 102 ? 46.405 -26.046 13.607  0.62 53.66 ?  102  LYS   B HE2  1 
ATOM   5643 H  HE2  B LYS   B 1 102 ? 46.516 -26.239 13.679  0.38 50.97 ?  102  LYS   B HE2  1 
ATOM   5644 H  HE3  A LYS   B 1 102 ? 46.204 -26.447 12.080  0.62 53.66 ?  102  LYS   B HE3  1 
ATOM   5645 H  HE3  B LYS   B 1 102 ? 46.371 -26.692 12.160  0.38 50.97 ?  102  LYS   B HE3  1 
ATOM   5646 H  HZ1  A LYS   B 1 102 ? 46.966 -24.306 12.247  0.62 54.90 ?  102  LYS   B HZ1  1 
ATOM   5647 H  HZ1  B LYS   B 1 102 ? 47.231 -24.588 12.284  0.38 51.97 ?  102  LYS   B HZ1  1 
ATOM   5648 H  HZ2  A LYS   B 1 102 ? 45.642 -24.277 11.659  0.62 54.90 ?  102  LYS   B HZ2  1 
ATOM   5649 H  HZ2  B LYS   B 1 102 ? 45.941 -24.519 11.628  0.38 51.97 ?  102  LYS   B HZ2  1 
ATOM   5650 H  HZ3  A LYS   B 1 102 ? 45.826 -23.913 13.049  0.62 54.90 ?  102  LYS   B HZ3  1 
ATOM   5651 H  HZ3  B LYS   B 1 102 ? 46.074 -24.106 13.010  0.38 51.97 ?  102  LYS   B HZ3  1 
ATOM   5652 N  N    . GLY   B 1 103 ? 39.990 -30.009 14.399  1.00 33.34 ?  103  GLY   B N    1 
ATOM   5653 C  CA   . GLY   B 1 103 ? 38.668 -30.052 14.989  1.00 33.12 ?  103  GLY   B CA   1 
ATOM   5654 C  C    . GLY   B 1 103 ? 37.712 -28.978 14.523  1.00 32.29 ?  103  GLY   B C    1 
ATOM   5655 O  O    . GLY   B 1 103 ? 36.626 -28.847 15.101  1.00 33.05 ?  103  GLY   B O    1 
ATOM   5656 H  H    A GLY   B 1 103 ? 40.095 -30.549 13.740  0.62 40.02 ?  103  GLY   B H    1 
ATOM   5657 H  H    B GLY   B 1 103 ? 40.095 -30.550 13.741  0.38 40.02 ?  103  GLY   B H    1 
ATOM   5658 H  HA2  . GLY   B 1 103 ? 38.267 -30.913 14.794  1.00 39.76 ?  103  GLY   B HA2  1 
ATOM   5659 H  HA3  . GLY   B 1 103 ? 38.750 -29.972 15.952  1.00 39.76 ?  103  GLY   B HA3  1 
ATOM   5660 N  N    A GLU   B 1 104 ? 38.082 -28.196 13.512  0.62 30.96 ?  104  GLU   B N    1 
ATOM   5661 N  N    B GLU   B 1 104 ? 38.062 -28.216 13.492  0.38 31.76 ?  104  GLU   B N    1 
ATOM   5662 C  CA   A GLU   B 1 104 ? 37.238 -27.104 13.054  0.62 29.48 ?  104  GLU   B CA   1 
ATOM   5663 C  CA   B GLU   B 1 104 ? 37.196 -27.144 13.026  0.38 31.00 ?  104  GLU   B CA   1 
ATOM   5664 C  C    A GLU   B 1 104 ? 36.050 -27.638 12.254  0.62 29.91 ?  104  GLU   B C    1 
ATOM   5665 C  C    B GLU   B 1 104 ? 36.036 -27.698 12.205  0.38 31.26 ?  104  GLU   B C    1 
ATOM   5666 O  O    A GLU   B 1 104 ? 36.083 -28.736 11.689  0.62 30.88 ?  104  GLU   B O    1 
ATOM   5667 O  O    B GLU   B 1 104 ? 36.118 -28.783 11.621  0.38 31.68 ?  104  GLU   B O    1 
ATOM   5668 C  CB   A GLU   B 1 104 ? 38.064 -26.110 12.235  0.62 28.48 ?  104  GLU   B CB   1 
ATOM   5669 C  CB   B GLU   B 1 104 ? 38.008 -26.125 12.225  0.38 30.26 ?  104  GLU   B CB   1 
ATOM   5670 C  CG   A GLU   B 1 104 ? 39.168 -25.457 13.061  0.62 27.46 ?  104  GLU   B CG   1 
ATOM   5671 C  CG   B GLU   B 1 104 ? 39.094 -25.471 13.068  0.38 29.53 ?  104  GLU   B CG   1 
ATOM   5672 C  CD   A GLU   B 1 104 ? 40.090 -24.560 12.262  0.62 26.44 ?  104  GLU   B CD   1 
ATOM   5673 C  CD   B GLU   B 1 104 ? 40.040 -24.598 12.268  0.38 28.86 ?  104  GLU   B CD   1 
ATOM   5674 O  OE1  A GLU   B 1 104 ? 40.100 -24.643 11.017  0.62 24.41 ?  104  GLU   B OE1  1 
ATOM   5675 O  OE1  B GLU   B 1 104 ? 39.996 -24.642 11.021  0.38 28.07 ?  104  GLU   B OE1  1 
ATOM   5676 O  OE2  A GLU   B 1 104 ? 40.817 -23.765 12.893  0.62 26.93 -1 104  GLU   B OE2  1 
ATOM   5677 O  OE2  B GLU   B 1 104 ? 40.833 -23.867 12.896  0.38 28.87 -1 104  GLU   B OE2  1 
ATOM   5678 H  H    A GLU   B 1 104 ? 38.822 -28.272 13.081  0.62 37.17 ?  104  GLU   B H    1 
ATOM   5679 H  H    B GLU   B 1 104 ? 38.799 -28.292 13.053  0.38 38.13 ?  104  GLU   B H    1 
ATOM   5680 H  HA   A GLU   B 1 104 ? 36.890 -26.631 13.827  0.62 35.39 ?  104  GLU   B HA   1 
ATOM   5681 H  HA   B GLU   B 1 104 ? 36.824 -26.686 13.793  0.38 37.22 ?  104  GLU   B HA   1 
ATOM   5682 H  HB2  A GLU   B 1 104 ? 38.479 -26.575 11.493  0.62 34.19 ?  104  GLU   B HB2  1 
ATOM   5683 H  HB2  B GLU   B 1 104 ? 38.434 -26.570 11.477  0.38 36.32 ?  104  GLU   B HB2  1 
ATOM   5684 H  HB3  A GLU   B 1 104 ? 37.482 -25.407 11.904  0.62 34.19 ?  104  GLU   B HB3  1 
ATOM   5685 H  HB3  B GLU   B 1 104 ? 37.415 -25.426 11.904  0.38 36.32 ?  104  GLU   B HB3  1 
ATOM   5686 H  HG2  A GLU   B 1 104 ? 38.764 -24.914 13.755  0.62 32.97 ?  104  GLU   B HG2  1 
ATOM   5687 H  HG2  B GLU   B 1 104 ? 38.675 -24.912 13.742  0.38 35.45 ?  104  GLU   B HG2  1 
ATOM   5688 H  HG3  A GLU   B 1 104 ? 39.715 -26.150 13.461  0.62 32.97 ?  104  GLU   B HG3  1 
ATOM   5689 H  HG3  B GLU   B 1 104 ? 39.620 -26.164 13.498  0.38 35.45 ?  104  GLU   B HG3  1 
ATOM   5690 N  N    A ASP   B 1 105 ? 34.988 -26.837 12.216  0.62 29.49 ?  105  ASP   B N    1 
ATOM   5691 N  N    B ASP   B 1 105 ? 34.945 -26.935 12.173  0.38 30.97 ?  105  ASP   B N    1 
ATOM   5692 C  CA   A ASP   B 1 105 ? 33.711 -27.280 11.669  0.62 29.98 ?  105  ASP   B CA   1 
ATOM   5693 C  CA   B ASP   B 1 105 ? 33.688 -27.411 11.605  0.38 31.08 ?  105  ASP   B CA   1 
ATOM   5694 C  C    A ASP   B 1 105 ? 33.775 -27.336 10.148  0.62 27.64 ?  105  ASP   B C    1 
ATOM   5695 C  C    B ASP   B 1 105 ? 33.768 -27.423 10.083  0.38 29.56 ?  105  ASP   B C    1 
ATOM   5696 O  O    A ASP   B 1 105 ? 33.944 -26.306 9.487   0.62 26.76 ?  105  ASP   B O    1 
ATOM   5697 O  O    B ASP   B 1 105 ? 33.965 -26.378 9.454   0.38 29.06 ?  105  ASP   B O    1 
ATOM   5698 C  CB   A ASP   B 1 105 ? 32.605 -26.325 12.113  0.62 33.32 ?  105  ASP   B CB   1 
ATOM   5699 C  CB   B ASP   B 1 105 ? 32.541 -26.514 12.070  0.38 32.71 ?  105  ASP   B CB   1 
ATOM   5700 C  CG   A ASP   B 1 105 ? 31.226 -26.791 11.693  0.62 36.15 ?  105  ASP   B CG   1 
ATOM   5701 C  CG   B ASP   B 1 105 ? 31.178 -27.086 11.727  0.38 34.20 ?  105  ASP   B CG   1 
ATOM   5702 O  OD1  A ASP   B 1 105 ? 31.111 -27.908 11.145  0.62 36.62 ?  105  ASP   B OD1  1 
ATOM   5703 O  OD1  B ASP   B 1 105 ? 31.122 -28.112 11.017  0.38 34.59 ?  105  ASP   B OD1  1 
ATOM   5704 O  OD2  A ASP   B 1 105 ? 30.253 -26.036 11.909  0.62 37.76 -1 105  ASP   B OD2  1 
ATOM   5705 O  OD2  B ASP   B 1 105 ? 30.161 -26.516 12.177  0.38 34.83 -1 105  ASP   B OD2  1 
ATOM   5706 H  H    A ASP   B 1 105 ? 34.984 -26.026 12.498  0.62 35.40 ?  105  ASP   B H    1 
ATOM   5707 H  H    B ASP   B 1 105 ? 34.910 -26.135 12.472  0.38 37.17 ?  105  ASP   B H    1 
ATOM   5708 H  HA   A ASP   B 1 105 ? 33.505 -28.166 12.002  0.62 35.99 ?  105  ASP   B HA   1 
ATOM   5709 H  HA   B ASP   B 1 105 ? 33.508 -28.313 11.910  0.38 37.31 ?  105  ASP   B HA   1 
ATOM   5710 H  HB2  A ASP   B 1 105 ? 32.627 -26.243 13.080  0.62 40.00 ?  105  ASP   B HB2  1 
ATOM   5711 H  HB2  B ASP   B 1 105 ? 32.586 -26.412 13.034  0.38 39.26 ?  105  ASP   B HB2  1 
ATOM   5712 H  HB3  A ASP   B 1 105 ? 32.749 -25.458 11.704  0.62 40.00 ?  105  ASP   B HB3  1 
ATOM   5713 H  HB3  B ASP   B 1 105 ? 32.623 -25.644 11.643  0.38 39.26 ?  105  ASP   B HB3  1 
ATOM   5714 N  N    A ILE   B 1 106 ? 33.603 -28.540 9.594   0.62 26.83 ?  106  ILE   B N    1 
ATOM   5715 N  N    B ILE   B 1 106 ? 33.600 -28.611 9.494   0.38 28.68 ?  106  ILE   B N    1 
ATOM   5716 C  CA   A ILE   B 1 106 ? 33.601 -28.726 8.149   0.62 26.00 ?  106  ILE   B CA   1 
ATOM   5717 C  CA   B ILE   B 1 106 ? 33.606 -28.755 8.044   0.38 27.96 ?  106  ILE   B CA   1 
ATOM   5718 C  C    A ILE   B 1 106 ? 32.507 -27.905 7.476   0.62 24.45 ?  106  ILE   B C    1 
ATOM   5719 C  C    B ILE   B 1 106 ? 32.501 -27.933 7.390   0.38 27.09 ?  106  ILE   B C    1 
ATOM   5720 O  O    A ILE   B 1 106 ? 32.614 -27.590 6.287   0.62 23.26 ?  106  ILE   B O    1 
ATOM   5721 O  O    B ILE   B 1 106 ? 32.572 -27.644 6.191   0.38 26.85 ?  106  ILE   B O    1 
ATOM   5722 C  CB   A ILE   B 1 106 ? 33.494 -30.235 7.821   0.62 26.78 ?  106  ILE   B CB   1 
ATOM   5723 C  CB   B ILE   B 1 106 ? 33.515 -30.255 7.675   0.38 28.24 ?  106  ILE   B CB   1 
ATOM   5724 C  CG1  A ILE   B 1 106 ? 33.726 -30.493 6.331   0.62 27.29 ?  106  ILE   B CG1  1 
ATOM   5725 C  CG1  B ILE   B 1 106 ? 33.783 -30.473 6.184   0.38 28.38 ?  106  ILE   B CG1  1 
ATOM   5726 C  CG2  A ILE   B 1 106 ? 32.140 -30.784 8.258   0.62 27.40 ?  106  ILE   B CG2  1 
ATOM   5727 C  CG2  B ILE   B 1 106 ? 32.155 -30.822 8.063   0.38 28.59 ?  106  ILE   B CG2  1 
ATOM   5728 C  CD1  A ILE   B 1 106 ? 35.077 -30.027 5.840   0.62 27.31 ?  106  ILE   B CD1  1 
ATOM   5729 C  CD1  B ILE   B 1 106 ? 35.131 -29.965 5.729   0.38 28.43 ?  106  ILE   B CD1  1 
ATOM   5730 H  H    A ILE   B 1 106 ? 33.481 -29.263 10.041  0.62 32.22 ?  106  ILE   B H    1 
ATOM   5731 H  H    B ILE   B 1 106 ? 33.488 -29.348 9.918   0.38 34.43 ?  106  ILE   B H    1 
ATOM   5732 H  HA   A ILE   B 1 106 ? 34.446 -28.412 7.805   0.62 31.21 ?  106  ILE   B HA   1 
ATOM   5733 H  HA   B ILE   B 1 106 ? 34.448 -28.419 7.711   0.38 33.57 ?  106  ILE   B HA   1 
ATOM   5734 H  HB   A ILE   B 1 106 ? 34.181 -30.704 8.320   0.62 32.15 ?  106  ILE   B HB   1 
ATOM   5735 H  HB   B ILE   B 1 106 ? 34.193 -30.732 8.177   0.38 33.90 ?  106  ILE   B HB   1 
ATOM   5736 H  HG12 A ILE   B 1 106 ? 33.667 -31.449 6.166   0.62 32.76 ?  106  ILE   B HG12 1 
ATOM   5737 H  HG12 B ILE   B 1 106 ? 33.749 -31.427 5.997   0.38 34.08 ?  106  ILE   B HG12 1 
ATOM   5738 H  HG13 A ILE   B 1 106 ? 33.046 -30.031 5.819   0.62 32.76 ?  106  ILE   B HG13 1 
ATOM   5739 H  HG13 B ILE   B 1 106 ? 33.102 -30.016 5.669   0.38 34.08 ?  106  ILE   B HG13 1 
ATOM   5740 H  HG21 A ILE   B 1 106 ? 32.145 -31.749 8.161   0.62 32.90 ?  106  ILE   B HG21 1 
ATOM   5741 H  HG21 B ILE   B 1 106 ? 32.176 -31.787 7.963   0.38 34.33 ?  106  ILE   B HG21 1 
ATOM   5742 H  HG22 A ILE   B 1 106 ? 31.988 -30.548 9.187   0.62 32.90 ?  106  ILE   B HG22 1 
ATOM   5743 H  HG22 B ILE   B 1 106 ? 31.968 -30.589 8.986   0.38 34.33 ?  106  ILE   B HG22 1 
ATOM   5744 H  HG23 A ILE   B 1 106 ? 31.446 -30.399 7.702   0.62 32.90 ?  106  ILE   B HG23 1 
ATOM   5745 H  HG23 B ILE   B 1 106 ? 31.476 -30.445 7.483   0.38 34.33 ?  106  ILE   B HG23 1 
ATOM   5746 H  HD11 A ILE   B 1 106 ? 35.256 -30.433 4.979   0.62 32.79 ?  106  ILE   B HD11 1 
ATOM   5747 H  HD11 B ILE   B 1 106 ? 35.343 -30.361 4.871   0.38 34.13 ?  106  ILE   B HD11 1 
ATOM   5748 H  HD12 A ILE   B 1 106 ? 35.066 -29.060 5.754   0.62 32.79 ?  106  ILE   B HD12 1 
ATOM   5749 H  HD12 B ILE   B 1 106 ? 35.092 -28.999 5.649   0.38 34.13 ?  106  ILE   B HD12 1 
ATOM   5750 H  HD13 A ILE   B 1 106 ? 35.755 -30.295 6.480   0.62 32.79 ?  106  ILE   B HD13 1 
ATOM   5751 H  HD13 B ILE   B 1 106 ? 35.800 -30.218 6.385   0.38 34.13 ?  106  ILE   B HD13 1 
ATOM   5752 N  N    A GLN   B 1 107 ? 31.456 -27.535 8.212   0.62 24.85 ?  107  GLN   B N    1 
ATOM   5753 N  N    B GLN   B 1 107 ? 31.477 -27.544 8.154   0.38 26.85 ?  107  GLN   B N    1 
ATOM   5754 C  CA   A GLN   B 1 107 ? 30.382 -26.735 7.633   0.62 24.96 ?  107  GLN   B CA   1 
ATOM   5755 C  CA   B GLN   B 1 107 ? 30.392 -26.741 7.602   0.38 26.43 ?  107  GLN   B CA   1 
ATOM   5756 C  C    A GLN   B 1 107 ? 30.869 -25.381 7.133   0.62 22.93 ?  107  GLN   B C    1 
ATOM   5757 C  C    B GLN   B 1 107 ? 30.865 -25.369 7.135   0.38 23.81 ?  107  GLN   B C    1 
ATOM   5758 O  O    A GLN   B 1 107 ? 30.226 -24.797 6.257   0.62 23.58 ?  107  GLN   B O    1 
ATOM   5759 O  O    B GLN   B 1 107 ? 30.201 -24.756 6.293   0.38 24.26 ?  107  GLN   B O    1 
ATOM   5760 C  CB   A GLN   B 1 107 ? 29.264 -26.539 8.660   0.62 28.65 ?  107  GLN   B CB   1 
ATOM   5761 C  CB   B GLN   B 1 107 ? 29.278 -26.594 8.642   0.38 29.08 ?  107  GLN   B CB   1 
ATOM   5762 C  CG   A GLN   B 1 107 ? 27.937 -26.055 8.077   0.62 32.25 ?  107  GLN   B CG   1 
ATOM   5763 C  CG   B GLN   B 1 107 ? 27.941 -26.119 8.085   0.38 31.55 ?  107  GLN   B CG   1 
ATOM   5764 C  CD   A GLN   B 1 107 ? 27.855 -24.543 7.952   0.62 34.95 ?  107  GLN   B CD   1 
ATOM   5765 C  CD   B GLN   B 1 107 ? 27.817 -24.606 8.051   0.38 33.48 ?  107  GLN   B CD   1 
ATOM   5766 O  OE1  A GLN   B 1 107 ? 28.677 -23.815 8.512   0.62 35.96 ?  107  GLN   B OE1  1 
ATOM   5767 O  OE1  B GLN   B 1 107 ? 28.636 -23.889 8.628   0.38 34.16 ?  107  GLN   B OE1  1 
ATOM   5768 N  NE2  A GLN   B 1 107 ? 26.855 -24.062 7.216   0.62 35.93 ?  107  GLN   B NE2  1 
ATOM   5769 N  NE2  B GLN   B 1 107 ? 26.785 -24.113 7.374   0.38 34.22 ?  107  GLN   B NE2  1 
ATOM   5770 H  H    A GLN   B 1 107 ? 31.347 -27.726 9.036   0.62 29.84 ?  107  GLN   B H    1 
ATOM   5771 H  H    B GLN   B 1 107 ? 31.386 -27.734 8.984   0.38 32.23 ?  107  GLN   B H    1 
ATOM   5772 H  HA   A GLN   B 1 107 ? 30.010 -27.212 6.873   0.62 29.96 ?  107  GLN   B HA   1 
ATOM   5773 H  HA   B GLN   B 1 107 ? 30.019 -27.204 6.835   0.38 31.74 ?  107  GLN   B HA   1 
ATOM   5774 H  HB2  A GLN   B 1 107 ? 29.100 -27.386 9.094   0.62 34.39 ?  107  GLN   B HB2  1 
ATOM   5775 H  HB2  B GLN   B 1 107 ? 29.130 -27.455 9.056   0.38 34.91 ?  107  GLN   B HB2  1 
ATOM   5776 H  HB3  A GLN   B 1 107 ? 29.556 -25.885 9.313   0.62 34.39 ?  107  GLN   B HB3  1 
ATOM   5777 H  HB3  B GLN   B 1 107 ? 29.563 -25.955 9.314   0.38 34.91 ?  107  GLN   B HB3  1 
ATOM   5778 H  HG2  A GLN   B 1 107 ? 27.821 -26.431 7.192   0.62 38.72 ?  107  GLN   B HG2  1 
ATOM   5779 H  HG2  B GLN   B 1 107 ? 27.840 -26.446 7.178   0.38 37.88 ?  107  GLN   B HG2  1 
ATOM   5780 H  HG3  A GLN   B 1 107 ? 27.214 -26.349 8.657   0.62 38.72 ?  107  GLN   B HG3  1 
ATOM   5781 H  HG3  B GLN   B 1 107 ? 27.226 -26.468 8.643   0.38 37.88 ?  107  GLN   B HG3  1 
ATOM   5782 H  HE21 A GLN   B 1 107 ? 26.299 -24.600 6.838   0.62 43.13 ?  107  GLN   B HE21 1 
ATOM   5783 H  HE21 B GLN   B 1 107 ? 26.233 -24.644 6.982   0.38 41.07 ?  107  GLN   B HE21 1 
ATOM   5784 H  HE22 A GLN   B 1 107 ? 26.761 -23.212 7.118   0.62 43.13 ?  107  GLN   B HE22 1 
ATOM   5785 H  HE22 B GLN   B 1 107 ? 26.668 -23.262 7.328   0.38 41.07 ?  107  GLN   B HE22 1 
ATOM   5786 N  N    . LEU   B 1 108 ? 31.996 -24.877 7.650   1.00 21.06 ?  108  LEU   B N    1 
ATOM   5787 C  CA   . LEU   B 1 108 ? 32.540 -23.579 7.241   1.00 18.60 ?  108  LEU   B CA   1 
ATOM   5788 C  C    . LEU   B 1 108 ? 33.177 -23.605 5.861   1.00 16.03 ?  108  LEU   B C    1 
ATOM   5789 O  O    . LEU   B 1 108 ? 33.597 -22.553 5.367   1.00 15.33 ?  108  LEU   B O    1 
ATOM   5790 C  CB   . LEU   B 1 108 ? 33.551 -23.086 8.276   1.00 19.19 ?  108  LEU   B CB   1 
ATOM   5791 C  CG   . LEU   B 1 108 ? 32.933 -22.529 9.559   1.00 20.68 ?  108  LEU   B CG   1 
ATOM   5792 C  CD1  . LEU   B 1 108 ? 33.939 -22.533 10.696  1.00 21.22 ?  108  LEU   B CD1  1 
ATOM   5793 C  CD2  . LEU   B 1 108 ? 32.427 -21.117 9.313   1.00 21.20 ?  108  LEU   B CD2  1 
ATOM   5794 H  H    A LEU   B 1 108 ? 32.458 -25.271 8.253   0.62 25.29 ?  108  LEU   B H    1 
ATOM   5795 H  H    B LEU   B 1 108 ? 32.461 -25.276 8.248   0.38 25.29 ?  108  LEU   B H    1 
ATOM   5796 H  HA   . LEU   B 1 108 ? 31.816 -22.938 7.215   1.00 22.33 ?  108  LEU   B HA   1 
ATOM   5797 H  HB2  . LEU   B 1 108 ? 34.122 -23.829 8.531   1.00 23.04 ?  108  LEU   B HB2  1 
ATOM   5798 H  HB3  . LEU   B 1 108 ? 34.084 -22.383 7.881   1.00 23.04 ?  108  LEU   B HB3  1 
ATOM   5799 H  HG   . LEU   B 1 108 ? 32.176 -23.079 9.821   1.00 24.83 ?  108  LEU   B HG   1 
ATOM   5800 H  HD11 . LEU   B 1 108 ? 33.500 -22.227 11.507  1.00 25.48 ?  108  LEU   B HD11 1 
ATOM   5801 H  HD12 . LEU   B 1 108 ? 34.271 -23.435 10.820  1.00 25.48 ?  108  LEU   B HD12 1 
ATOM   5802 H  HD13 . LEU   B 1 108 ? 34.670 -21.937 10.472  1.00 25.48 ?  108  LEU   B HD13 1 
ATOM   5803 H  HD21 . LEU   B 1 108 ? 32.056 -20.765 10.137  1.00 25.45 ?  108  LEU   B HD21 1 
ATOM   5804 H  HD22 . LEU   B 1 108 ? 33.169 -20.563 9.022   1.00 25.45 ?  108  LEU   B HD22 1 
ATOM   5805 H  HD23 . LEU   B 1 108 ? 31.743 -21.141 8.626   1.00 25.45 ?  108  LEU   B HD23 1 
ATOM   5806 N  N    . LEU   B 1 109 ? 33.242 -24.771 5.229   1.00 14.86 ?  109  LEU   B N    1 
ATOM   5807 C  CA   . LEU   B 1 109 ? 33.870 -24.879 3.919   1.00 13.95 ?  109  LEU   B CA   1 
ATOM   5808 C  C    . LEU   B 1 109 ? 33.100 -24.098 2.858   1.00 13.55 ?  109  LEU   B C    1 
ATOM   5809 O  O    . LEU   B 1 109 ? 33.714 -23.508 1.960   1.00 13.20 ?  109  LEU   B O    1 
ATOM   5810 C  CB   . LEU   B 1 109 ? 33.990 -26.354 3.544   1.00 14.13 ?  109  LEU   B CB   1 
ATOM   5811 C  CG   . LEU   B 1 109 ? 34.765 -26.697 2.275   1.00 13.89 ?  109  LEU   B CG   1 
ATOM   5812 C  CD1  . LEU   B 1 109 ? 36.145 -26.042 2.286   1.00 13.30 ?  109  LEU   B CD1  1 
ATOM   5813 C  CD2  . LEU   B 1 109 ? 34.874 -28.217 2.111   1.00 15.00 ?  109  LEU   B CD2  1 
ATOM   5814 H  H    . LEU   B 1 109 ? 32.938 -25.509 5.532   1.00 17.85 ?  109  LEU   B H    1 
ATOM   5815 H  HA   . LEU   B 1 109 ? 34.768 -24.509 3.965   1.00 16.76 ?  109  LEU   B HA   1 
ATOM   5816 H  HB2  . LEU   B 1 109 ? 34.430 -26.816 4.275   1.00 16.97 ?  109  LEU   B HB2  1 
ATOM   5817 H  HB3  . LEU   B 1 109 ? 33.095 -26.711 3.434   1.00 16.97 ?  109  LEU   B HB3  1 
ATOM   5818 H  HG   . LEU   B 1 109 ? 34.278 -26.363 1.506   1.00 16.68 ?  109  LEU   B HG   1 
ATOM   5819 H  HD11 . LEU   B 1 109 ? 36.678 -26.410 1.563   1.00 15.98 ?  109  LEU   B HD11 1 
ATOM   5820 H  HD12 . LEU   B 1 109 ? 36.038 -25.087 2.166   1.00 15.98 ?  109  LEU   B HD12 1 
ATOM   5821 H  HD13 . LEU   B 1 109 ? 36.574 -26.227 3.137   1.00 15.98 ?  109  LEU   B HD13 1 
ATOM   5822 H  HD21 . LEU   B 1 109 ? 35.441 -28.414 1.344   1.00 18.01 ?  109  LEU   B HD21 1 
ATOM   5823 H  HD22 . LEU   B 1 109 ? 35.265 -28.596 2.913   1.00 18.01 ?  109  LEU   B HD22 1 
ATOM   5824 H  HD23 . LEU   B 1 109 ? 33.989 -28.588 1.967   1.00 18.01 ?  109  LEU   B HD23 1 
ATOM   5825 N  N    . LYS   B 1 110 ? 31.765 -24.066 2.943   1.00 12.89 ?  110  LYS   B N    1 
ATOM   5826 C  CA   . LYS   B 1 110 ? 31.004 -23.311 1.951   1.00 12.85 ?  110  LYS   B CA   1 
ATOM   5827 C  C    . LYS   B 1 110 ? 31.339 -21.823 2.033   1.00 12.81 ?  110  LYS   B C    1 
ATOM   5828 O  O    . LYS   B 1 110 ? 31.595 -21.175 1.012   1.00 12.64 ?  110  LYS   B O    1 
ATOM   5829 C  CB   . LYS   B 1 110 ? 29.502 -23.560 2.102   1.00 13.30 ?  110  LYS   B CB   1 
ATOM   5830 C  CG   . LYS   B 1 110 ? 28.694 -22.929 0.965   1.00 13.64 ?  110  LYS   B CG   1 
ATOM   5831 C  CD   . LYS   B 1 110 ? 27.223 -23.359 0.989   1.00 14.09 ?  110  LYS   B CD   1 
ATOM   5832 C  CE   . LYS   B 1 110 ? 26.457 -22.824 -0.223  1.00 15.08 ?  110  LYS   B CE   1 
ATOM   5833 N  NZ   . LYS   B 1 110 ? 26.786 -23.547 -1.484  1.00 15.21 ?  110  LYS   B NZ   1 
ATOM   5834 H  H    . LYS   B 1 110 ? 31.298 -24.461 3.546   1.00 15.49 ?  110  LYS   B H    1 
ATOM   5835 H  HA   . LYS   B 1 110 ? 31.265 -23.617 1.070   1.00 15.43 ?  110  LYS   B HA   1 
ATOM   5836 H  HB2  . LYS   B 1 110 ? 29.339 -24.517 2.095   1.00 15.97 ?  110  LYS   B HB2  1 
ATOM   5837 H  HB3  . LYS   B 1 110 ? 29.198 -23.176 2.938   1.00 15.97 ?  110  LYS   B HB3  1 
ATOM   5838 H  HG2  . LYS   B 1 110 ? 28.723 -21.967 1.048   1.00 16.38 ?  110  LYS   B HG2  1 
ATOM   5839 H  HG3  . LYS   B 1 110 ? 29.069 -23.207 0.115   1.00 16.38 ?  110  LYS   B HG3  1 
ATOM   5840 H  HD2  . LYS   B 1 110 ? 27.171 -24.330 0.978   1.00 16.92 ?  110  LYS   B HD2  1 
ATOM   5841 H  HD3  . LYS   B 1 110 ? 26.801 -23.013 1.793   1.00 16.92 ?  110  LYS   B HD3  1 
ATOM   5842 H  HE2  . LYS   B 1 110 ? 25.506 -22.918 -0.065  1.00 18.11 ?  110  LYS   B HE2  1 
ATOM   5843 H  HE3  . LYS   B 1 110 ? 26.682 -21.889 -0.350  1.00 18.11 ?  110  LYS   B HE3  1 
ATOM   5844 H  HZ1  . LYS   B 1 110 ? 26.326 -23.208 -2.162  1.00 18.27 ?  110  LYS   B HZ1  1 
ATOM   5845 H  HZ2  . LYS   B 1 110 ? 27.658 -23.473 -1.658  1.00 18.27 ?  110  LYS   B HZ2  1 
ATOM   5846 H  HZ3  . LYS   B 1 110 ? 26.586 -24.412 -1.399  1.00 18.27 ?  110  LYS   B HZ3  1 
ATOM   5847 N  N    . SER   B 1 111 ? 31.353 -21.266 3.249   1.00 12.78 ?  111  SER   B N    1 
ATOM   5848 C  CA   . SER   B 1 111 ? 31.751 -19.870 3.422   1.00 12.77 ?  111  SER   B CA   1 
ATOM   5849 C  C    . SER   B 1 111 ? 33.130 -19.613 2.825   1.00 12.05 ?  111  SER   B C    1 
ATOM   5850 O  O    . SER   B 1 111 ? 33.353 -18.582 2.174   1.00 12.57 ?  111  SER   B O    1 
ATOM   5851 C  CB   . SER   B 1 111 ? 31.754 -19.507 4.906   1.00 13.88 ?  111  SER   B CB   1 
ATOM   5852 O  OG   . SER   B 1 111 ? 30.452 -19.498 5.443   1.00 15.50 ?  111  SER   B OG   1 
ATOM   5853 H  H    . SER   B 1 111 ? 31.149 -21.677 3.979   1.00 15.35 ?  111  SER   B H    1 
ATOM   5854 H  HA   . SER   B 1 111 ? 31.116 -19.302 2.972   1.00 15.34 ?  111  SER   B HA   1 
ATOM   5855 H  HB2  . SER   B 1 111 ? 32.281 -20.161 5.395   1.00 16.67 ?  111  SER   B HB2  1 
ATOM   5856 H  HB3  . SER   B 1 111 ? 32.139 -18.627 5.017   1.00 16.67 ?  111  SER   B HB3  1 
ATOM   5857 H  HG   . SER   B 1 111 ? 30.472 -19.294 6.268   1.00 18.61 ?  111  SER   B HG   1 
ATOM   5858 N  N    . ALA   B 1 112 ? 34.069 -20.536 3.041   1.00 12.23 ?  112  ALA   B N    1 
ATOM   5859 C  CA   . ALA   B 1 112 ? 35.413 -20.358 2.501   1.00 11.88 ?  112  ALA   B CA   1 
ATOM   5860 C  C    . ALA   B 1 112 ? 35.383 -20.263 0.978   1.00 11.26 ?  112  ALA   B C    1 
ATOM   5861 O  O    . ALA   B 1 112 ? 36.002 -19.369 0.386   1.00 11.71 ?  112  ALA   B O    1 
ATOM   5862 C  CB   . ALA   B 1 112 ? 36.324 -21.494 2.977   1.00 12.26 ?  112  ALA   B CB   1 
ATOM   5863 H  H    . ALA   B 1 112 ? 33.958 -21.263 3.494   1.00 14.69 ?  112  ALA   B H    1 
ATOM   5864 H  HA   . ALA   B 1 112 ? 35.779 -19.526 2.844   1.00 14.27 ?  112  ALA   B HA   1 
ATOM   5865 H  HB1  . ALA   B 1 112 ? 37.216 -21.356 2.617   1.00 14.73 ?  112  ALA   B HB1  1 
ATOM   5866 H  HB2  . ALA   B 1 112 ? 36.360 -21.485 3.949   1.00 14.73 ?  112  ALA   B HB2  1 
ATOM   5867 H  HB3  . ALA   B 1 112 ? 35.968 -22.338 2.668   1.00 14.73 ?  112  ALA   B HB3  1 
ATOM   5868 N  N    . TYR   B 1 113 ? 34.646 -21.166 0.324   1.00 11.35 ?  113  TYR   B N    1 
ATOM   5869 C  CA   . TYR   B 1 113 ? 34.562 -21.121 -1.132  1.00 11.08 ?  113  TYR   B CA   1 
ATOM   5870 C  C    . TYR   B 1 113 ? 33.851 -19.873 -1.646  1.00 10.72 ?  113  TYR   B C    1 
ATOM   5871 O  O    . TYR   B 1 113 ? 34.122 -19.442 -2.770  1.00 10.95 ?  113  TYR   B O    1 
ATOM   5872 C  CB   . TYR   B 1 113 ? 33.895 -22.385 -1.679  1.00 11.36 ?  113  TYR   B CB   1 
ATOM   5873 C  CG   . TYR   B 1 113 ? 34.861 -23.529 -1.940  1.00 11.83 ?  113  TYR   B CG   1 
ATOM   5874 C  CD1  . TYR   B 1 113 ? 35.851 -23.431 -2.910  1.00 11.97 ?  113  TYR   B CD1  1 
ATOM   5875 C  CD2  . TYR   B 1 113 ? 34.771 -24.714 -1.227  1.00 12.08 ?  113  TYR   B CD2  1 
ATOM   5876 C  CE1  . TYR   B 1 113 ? 36.727 -24.462 -3.155  1.00 12.36 ?  113  TYR   B CE1  1 
ATOM   5877 C  CE2  . TYR   B 1 113 ? 35.638 -25.767 -1.468  1.00 12.25 ?  113  TYR   B CE2  1 
ATOM   5878 C  CZ   . TYR   B 1 113 ? 36.612 -25.636 -2.437  1.00 12.42 ?  113  TYR   B CZ   1 
ATOM   5879 O  OH   . TYR   B 1 113 ? 37.497 -26.648 -2.710  1.00 13.08 ?  113  TYR   B OH   1 
ATOM   5880 H  H    . TYR   B 1 113 ? 34.180 -21.790 0.701   1.00 13.63 ?  113  TYR   B H    1 
ATOM   5881 H  HA   . TYR   B 1 113 ? 35.459 -21.101 -1.473  1.00 13.31 ?  113  TYR   B HA   1 
ATOM   5882 H  HB2  . TYR   B 1 113 ? 33.235 -22.704 -1.038  1.00 13.65 ?  113  TYR   B HB2  1 
ATOM   5883 H  HB3  . TYR   B 1 113 ? 33.457 -22.174 -2.517  1.00 13.65 ?  113  TYR   B HB3  1 
ATOM   5884 H  HD1  . TYR   B 1 113 ? 35.932 -22.643 -3.401  1.00 14.38 ?  113  TYR   B HD1  1 
ATOM   5885 H  HD2  . TYR   B 1 113 ? 34.110 -24.806 -0.581  1.00 14.51 ?  113  TYR   B HD2  1 
ATOM   5886 H  HE1  . TYR   B 1 113 ? 37.384 -24.378 -3.812  1.00 14.85 ?  113  TYR   B HE1  1 
ATOM   5887 H  HE2  . TYR   B 1 113 ? 35.561 -26.558 -0.983  1.00 14.72 ?  113  TYR   B HE2  1 
ATOM   5888 H  HH   . TYR   B 1 113 ? 37.331 -27.316 -2.228  1.00 15.71 ?  113  TYR   B HH   1 
ATOM   5889 N  N    . GLU   B 1 114 ? 32.932 -19.294 -0.866  1.00 11.20 ?  114  GLU   B N    1 
ATOM   5890 C  CA   . GLU   B 1 114 ? 32.250 -18.087 -1.322  1.00 10.95 ?  114  GLU   B CA   1 
ATOM   5891 C  C    . GLU   B 1 114 ? 33.235 -16.964 -1.620  1.00 10.70 ?  114  GLU   B C    1 
ATOM   5892 O  O    . GLU   B 1 114 ? 32.959 -16.107 -2.459  1.00 11.06 ?  114  GLU   B O    1 
ATOM   5893 C  CB   . GLU   B 1 114 ? 31.192 -17.657 -0.299  1.00 11.43 ?  114  GLU   B CB   1 
ATOM   5894 C  CG   . GLU   B 1 114 ? 29.984 -18.581 -0.358  1.00 11.67 ?  114  GLU   B CG   1 
ATOM   5895 C  CD   . GLU   B 1 114 ? 28.955 -18.387 0.745   1.00 11.93 ?  114  GLU   B CD   1 
ATOM   5896 O  OE1  . GLU   B 1 114 ? 29.247 -17.775 1.791   1.00 12.19 ?  114  GLU   B OE1  1 
ATOM   5897 O  OE2  . GLU   B 1 114 ? 27.834 -18.932 0.581   1.00 13.16 -1 114  GLU   B OE2  1 
ATOM   5898 H  H    . GLU   B 1 114 ? 32.686 -19.579 -0.090  1.00 13.45 ?  114  GLU   B H    1 
ATOM   5899 H  HA   . GLU   B 1 114 ? 31.783 -18.290 -2.144  1.00 13.15 ?  114  GLU   B HA   1 
ATOM   5900 H  HB2  . GLU   B 1 114 ? 31.567 -17.705 0.598   1.00 13.73 ?  114  GLU   B HB2  1 
ATOM   5901 H  HB3  . GLU   B 1 114 ? 30.895 -16.757 -0.492  1.00 13.73 ?  114  GLU   B HB3  1 
ATOM   5902 H  HG2  . GLU   B 1 114 ? 29.530 -18.438 -1.199  1.00 14.02 ?  114  GLU   B HG2  1 
ATOM   5903 H  HG3  . GLU   B 1 114 ? 30.298 -19.500 -0.309  1.00 14.02 ?  114  GLU   B HG3  1 
ATOM   5904 N  N    . ASN   B 1 115 ? 34.400 -16.957 -0.970  1.00 10.75 ?  115  ASN   B N    1 
ATOM   5905 C  CA   . ASN   B 1 115 ? 35.393 -15.925 -1.269  1.00 10.55 ?  115  ASN   B CA   1 
ATOM   5906 C  C    . ASN   B 1 115 ? 35.804 -15.945 -2.736  1.00 10.56 ?  115  ASN   B C    1 
ATOM   5907 O  O    . ASN   B 1 115 ? 36.191 -14.901 -3.290  1.00 10.91 ?  115  ASN   B O    1 
ATOM   5908 C  CB   . ASN   B 1 115 ? 36.636 -16.104 -0.387  1.00 11.29 ?  115  ASN   B CB   1 
ATOM   5909 C  CG   . ASN   B 1 115 ? 36.369 -15.830 1.077   1.00 11.79 ?  115  ASN   B CG   1 
ATOM   5910 O  OD1  . ASN   B 1 115 ? 36.370 -14.683 1.511   1.00 13.59 ?  115  ASN   B OD1  1 
ATOM   5911 N  ND2  . ASN   B 1 115 ? 36.196 -16.890 1.861   1.00 11.90 ?  115  ASN   B ND2  1 
ATOM   5912 H  H    . ASN   B 1 115 ? 34.632 -17.520 -0.358  1.00 12.91 ?  115  ASN   B H    1 
ATOM   5913 H  HA   . ASN   B 1 115 ? 35.011 -15.054 -1.076  1.00 12.68 ?  115  ASN   B HA   1 
ATOM   5914 H  HB2  . ASN   B 1 115 ? 36.953 -17.014 -0.469  1.00 13.56 ?  115  ASN   B HB2  1 
ATOM   5915 H  HB3  . ASN   B 1 115 ? 37.321 -15.484 -0.682  1.00 13.56 ?  115  ASN   B HB3  1 
ATOM   5916 H  HD21 . ASN   B 1 115 ? 36.054 -16.781 2.705   1.00 14.30 ?  115  ASN   B HD21 1 
ATOM   5917 H  HD22 . ASN   B 1 115 ? 36.219 -17.681 1.529   1.00 14.30 ?  115  ASN   B HD22 1 
ATOM   5918 N  N    . PHE   B 1 116 ? 35.777 -17.126 -3.374  1.00 10.34 ?  116  PHE   B N    1 
ATOM   5919 C  CA   . PHE   B 1 116 ? 36.203 -17.221 -4.767  1.00 10.66 ?  116  PHE   B CA   1 
ATOM   5920 C  C    . PHE   B 1 116 ? 35.298 -16.395 -5.678  1.00 10.32 ?  116  PHE   B C    1 
ATOM   5921 O  O    . PHE   B 1 116 ? 35.730 -15.963 -6.751  1.00 11.02 ?  116  PHE   B O    1 
ATOM   5922 C  CB   . PHE   B 1 116 ? 36.163 -18.668 -5.287  1.00 10.41 ?  116  PHE   B CB   1 
ATOM   5923 C  CG   . PHE   B 1 116 ? 37.240 -19.624 -4.741  1.00 10.31 ?  116  PHE   B CG   1 
ATOM   5924 C  CD1  . PHE   B 1 116 ? 37.890 -19.438 -3.530  1.00 10.92 ?  116  PHE   B CD1  1 
ATOM   5925 C  CD2  . PHE   B 1 116 ? 37.544 -20.761 -5.478  1.00 10.64 ?  116  PHE   B CD2  1 
ATOM   5926 C  CE1  . PHE   B 1 116 ? 38.821 -20.376 -3.079  1.00 11.28 ?  116  PHE   B CE1  1 
ATOM   5927 C  CE2  . PHE   B 1 116 ? 38.471 -21.689 -5.039  1.00 10.93 ?  116  PHE   B CE2  1 
ATOM   5928 C  CZ   . PHE   B 1 116 ? 39.105 -21.505 -3.840  1.00 10.84 ?  116  PHE   B CZ   1 
ATOM   5929 H  H    . PHE   B 1 116 ? 35.519 -17.873 -3.023  1.00 12.43 ?  116  PHE   B H    1 
ATOM   5930 H  HA   . PHE   B 1 116 ? 37.109 -16.895 -4.850  1.00 12.81 ?  116  PHE   B HA   1 
ATOM   5931 H  HB2  . PHE   B 1 116 ? 35.293 -19.049 -5.060  1.00 12.50 ?  116  PHE   B HB2  1 
ATOM   5932 H  HB3  . PHE   B 1 116 ? 36.257 -18.649 -6.250  1.00 12.50 ?  116  PHE   B HB3  1 
ATOM   5933 H  HD1  . PHE   B 1 116 ? 37.684 -18.693 -3.006  1.00 13.13 ?  116  PHE   B HD1  1 
ATOM   5934 H  HD2  . PHE   B 1 116 ? 37.105 -20.907 -6.286  1.00 12.79 ?  116  PHE   B HD2  1 
ATOM   5935 H  HE1  . PHE   B 1 116 ? 39.254 -20.240 -2.268  1.00 13.56 ?  116  PHE   B HE1  1 
ATOM   5936 H  HE2  . PHE   B 1 116 ? 38.660 -22.437 -5.555  1.00 13.13 ?  116  PHE   B HE2  1 
ATOM   5937 H  HZ   . PHE   B 1 116 ? 39.741 -22.115 -3.546  1.00 13.02 ?  116  PHE   B HZ   1 
ATOM   5938 N  N    . ASN   B 1 117 ? 34.031 -16.190 -5.288  1.00 10.89 ?  117  ASN   B N    1 
ATOM   5939 C  CA   . ASN   B 1 117 ? 33.080 -15.482 -6.143  1.00 11.20 ?  117  ASN   B CA   1 
ATOM   5940 C  C    . ASN   B 1 117 ? 33.396 -14.001 -6.290  1.00 11.51 ?  117  ASN   B C    1 
ATOM   5941 O  O    . ASN   B 1 117 ? 32.794 -13.347 -7.145  1.00 12.58 ?  117  ASN   B O    1 
ATOM   5942 C  CB   . ASN   B 1 117 ? 31.653 -15.699 -5.655  1.00 11.25 ?  117  ASN   B CB   1 
ATOM   5943 C  CG   . ASN   B 1 117 ? 31.207 -17.113 -5.897  1.00 11.60 ?  117  ASN   B CG   1 
ATOM   5944 O  OD1  . ASN   B 1 117 ? 31.561 -17.708 -6.917  1.00 12.26 ?  117  ASN   B OD1  1 
ATOM   5945 N  ND2  . ASN   B 1 117 ? 30.469 -17.682 -4.956  1.00 11.62 ?  117  ASN   B ND2  1 
ATOM   5946 H  H    . ASN   B 1 117 ? 33.706 -16.441 -4.521  1.00 13.08 ?  117  ASN   B H    1 
ATOM   5947 H  HA   . ASN   B 1 117 ? 33.139 -15.870 -7.019  1.00 13.45 ?  117  ASN   B HA   1 
ATOM   5948 H  HB2  . ASN   B 1 117 ? 31.603 -15.521 -4.698  1.00 13.52 ?  117  ASN   B HB2  1 
ATOM   5949 H  HB3  . ASN   B 1 117 ? 31.056 -15.098 -6.132  1.00 13.52 ?  117  ASN   B HB3  1 
ATOM   5950 H  HD21 . ASN   B 1 117 ? 30.198 -18.490 -5.051  1.00 13.96 ?  117  ASN   B HD21 1 
ATOM   5951 H  HD22 . ASN   B 1 117 ? 30.249 -17.234 -4.252  1.00 13.96 ?  117  ASN   B HD22 1 
ATOM   5952 N  N    . GLN   B 1 118 ? 34.335 -13.477 -5.511  1.00 11.18 ?  118  GLN   B N    1 
ATOM   5953 C  CA   . GLN   B 1 118 ? 34.766 -12.091 -5.649  1.00 11.48 ?  118  GLN   B CA   1 
ATOM   5954 C  C    . GLN   B 1 118 ? 35.825 -11.899 -6.729  1.00 11.74 ?  118  GLN   B C    1 
ATOM   5955 O  O    . GLN   B 1 118 ? 36.301 -10.772 -6.905  1.00 13.30 ?  118  GLN   B O    1 
ATOM   5956 C  CB   . GLN   B 1 118 ? 35.251 -11.566 -4.293  1.00 12.42 ?  118  GLN   B CB   1 
ATOM   5957 C  CG   . GLN   B 1 118 ? 34.159 -11.605 -3.227  1.00 12.50 ?  118  GLN   B CG   1 
ATOM   5958 C  CD   . GLN   B 1 118 ? 32.988 -10.697 -3.570  1.00 12.32 ?  118  GLN   B CD   1 
ATOM   5959 O  OE1  . GLN   B 1 118 ? 33.178 -9.561  -4.014  1.00 13.39 ?  118  GLN   B OE1  1 
ATOM   5960 N  NE2  . GLN   B 1 118 ? 31.777 -11.186 -3.372  1.00 12.84 ?  118  GLN   B NE2  1 
ATOM   5961 H  H    . GLN   B 1 118 ? 34.758 -13.910 -4.891  1.00 13.43 ?  118  GLN   B H    1 
ATOM   5962 H  HA   . GLN   B 1 118 ? 34.002 -11.562 -5.913  1.00 13.79 ?  118  GLN   B HA   1 
ATOM   5963 H  HB2  . GLN   B 1 118 ? 35.993 -12.103 -3.984  1.00 14.92 ?  118  GLN   B HB2  1 
ATOM   5964 H  HB3  . GLN   B 1 118 ? 35.532 -10.638 -4.393  1.00 14.92 ?  118  GLN   B HB3  1 
ATOM   5965 H  HG2  . GLN   B 1 118 ? 33.828 -12.514 -3.150  1.00 15.02 ?  118  GLN   B HG2  1 
ATOM   5966 H  HG3  . GLN   B 1 118 ? 34.534 -11.315 -2.380  1.00 15.02 ?  118  GLN   B HG3  1 
ATOM   5967 H  HE21 . GLN   B 1 118 ? 31.681 -11.982 -3.061  1.00 15.42 ?  118  GLN   B HE21 1 
ATOM   5968 H  HE22 . GLN   B 1 118 ? 31.092 -10.707 -3.557  1.00 15.42 ?  118  GLN   B HE22 1 
ATOM   5969 N  N    . HIS   B 1 119 ? 36.186 -12.952 -7.465  1.00 11.16 ?  119  HIS   B N    1 
ATOM   5970 C  CA   . HIS   B 1 119 ? 37.226 -12.904 -8.486  1.00 11.78 ?  119  HIS   B CA   1 
ATOM   5971 C  C    . HIS   B 1 119 ? 36.744 -13.632 -9.730  1.00 11.54 ?  119  HIS   B C    1 
ATOM   5972 O  O    . HIS   B 1 119 ? 36.238 -14.750 -9.639  1.00 12.35 ?  119  HIS   B O    1 
ATOM   5973 C  CB   . HIS   B 1 119 ? 38.509 -13.541 -7.946  1.00 11.99 ?  119  HIS   B CB   1 
ATOM   5974 C  CG   . HIS   B 1 119 ? 38.988 -12.859 -6.712  1.00 12.89 ?  119  HIS   B CG   1 
ATOM   5975 N  ND1  . HIS   B 1 119 ? 39.780 -11.732 -6.750  1.00 14.85 ?  119  HIS   B ND1  1 
ATOM   5976 C  CD2  . HIS   B 1 119 ? 38.691 -13.072 -5.411  1.00 14.15 ?  119  HIS   B CD2  1 
ATOM   5977 C  CE1  . HIS   B 1 119 ? 39.985 -11.307 -5.516  1.00 15.81 ?  119  HIS   B CE1  1 
ATOM   5978 N  NE2  . HIS   B 1 119 ? 39.328 -12.097 -4.686  1.00 15.54 ?  119  HIS   B NE2  1 
ATOM   5979 H  H    . HIS   B 1 119 ? 35.822 -13.733 -7.395  1.00 13.41 ?  119  HIS   B H    1 
ATOM   5980 H  HA   . HIS   B 1 119 ? 37.412 -11.979 -8.717  1.00 14.15 ?  119  HIS   B HA   1 
ATOM   5981 H  HB2  . HIS   B 1 119 ? 38.343 -14.469 -7.733  1.00 14.40 ?  119  HIS   B HB2  1 
ATOM   5982 H  HB3  . HIS   B 1 119 ? 39.208 -13.470 -8.619  1.00 14.40 ?  119  HIS   B HB3  1 
ATOM   5983 H  HD2  . HIS   B 1 119 ? 38.164 -13.759 -5.069  1.00 17.00 ?  119  HIS   B HD2  1 
ATOM   5984 H  HE1  . HIS   B 1 119 ? 40.511 -10.579 -5.266  1.00 18.98 ?  119  HIS   B HE1  1 
ATOM   5985 H  HE2  . HIS   B 1 119 ? 39.330 -12.034 -3.824  1.00 18.66 ?  119  HIS   B HE2  1 
ATOM   5986 N  N    . GLU   B 1 120 ? 36.898 -13.001 -10.894 1.00 12.29 ?  120  GLU   B N    1 
ATOM   5987 C  CA   . GLU   B 1 120 ? 36.308 -13.572 -12.102 1.00 13.77 ?  120  GLU   B CA   1 
ATOM   5988 C  C    . GLU   B 1 120 ? 36.975 -14.878 -12.517 1.00 12.52 ?  120  GLU   B C    1 
ATOM   5989 O  O    . GLU   B 1 120 ? 36.309 -15.752 -13.085 1.00 12.61 ?  120  GLU   B O    1 
ATOM   5990 C  CB   . GLU   B 1 120 ? 36.345 -12.555 -13.239 1.00 18.06 ?  120  GLU   B CB   1 
ATOM   5991 C  CG   . GLU   B 1 120 ? 35.372 -11.406 -13.030 1.00 23.99 ?  120  GLU   B CG   1 
ATOM   5992 C  CD   . GLU   B 1 120 ? 35.181 -10.552 -14.264 1.00 29.48 ?  120  GLU   B CD   1 
ATOM   5993 O  OE1  . GLU   B 1 120 ? 36.175 -10.298 -14.976 1.00 31.55 ?  120  GLU   B OE1  1 
ATOM   5994 O  OE2  . GLU   B 1 120 ? 34.032 -10.133 -14.517 1.00 32.05 -1 120  GLU   B OE2  1 
ATOM   5995 H  H    . GLU   B 1 120 ? 37.324 -12.260 -11.011 1.00 14.77 ?  120  GLU   B H    1 
ATOM   5996 H  HA   . GLU   B 1 120 ? 35.380 -13.770 -11.923 1.00 16.55 ?  120  GLU   B HA   1 
ATOM   5997 H  HB2  . GLU   B 1 120 ? 37.237 -12.179 -13.304 1.00 21.69 ?  120  GLU   B HB2  1 
ATOM   5998 H  HB3  . GLU   B 1 120 ? 36.111 -12.997 -14.070 1.00 21.69 ?  120  GLU   B HB3  1 
ATOM   5999 H  HG2  . GLU   B 1 120 ? 34.505 -11.765 -12.786 1.00 28.80 ?  120  GLU   B HG2  1 
ATOM   6000 H  HG3  . GLU   B 1 120 ? 35.705 -10.829 -12.328 1.00 28.80 ?  120  GLU   B HG3  1 
ATOM   6001 N  N    . VAL   B 1 121 ? 38.273 -15.028 -12.251 1.00 12.05 ?  121  VAL   B N    1 
ATOM   6002 C  CA   . VAL   B 1 121 ? 39.018 -16.232 -12.610 1.00 11.89 ?  121  VAL   B CA   1 
ATOM   6003 C  C    . VAL   B 1 121 ? 40.135 -16.444 -11.594 1.00 11.44 ?  121  VAL   B C    1 
ATOM   6004 O  O    . VAL   B 1 121 ? 40.818 -15.494 -11.197 1.00 12.18 ?  121  VAL   B O    1 
ATOM   6005 C  CB   . VAL   B 1 121 ? 39.522 -16.176 -14.073 1.00 13.88 ?  121  VAL   B CB   1 
ATOM   6006 C  CG1  . VAL   B 1 121 ? 40.369 -14.930 -14.329 1.00 15.42 ?  121  VAL   B CG1  1 
ATOM   6007 C  CG2  . VAL   B 1 121 ? 40.279 -17.445 -14.441 1.00 15.23 ?  121  VAL   B CG2  1 
ATOM   6008 H  H    . VAL   B 1 121 ? 38.756 -14.434 -11.855 1.00 14.47 ?  121  VAL   B H    1 
ATOM   6009 H  HA   . VAL   B 1 121 ? 38.413 -16.988 -12.546 1.00 14.29 ?  121  VAL   B HA   1 
ATOM   6010 H  HB   . VAL   B 1 121 ? 38.748 -16.122 -14.660 1.00 16.67 ?  121  VAL   B HB   1 
ATOM   6011 H  HG11 . VAL   B 1 121 ? 40.681 -14.942 -15.249 1.00 18.51 ?  121  VAL   B HG11 1 
ATOM   6012 H  HG12 . VAL   B 1 121 ? 39.826 -14.139 -14.177 1.00 18.51 ?  121  VAL   B HG12 1 
ATOM   6013 H  HG13 . VAL   B 1 121 ? 41.126 -14.932 -13.724 1.00 18.51 ?  121  VAL   B HG13 1 
ATOM   6014 H  HG21 . VAL   B 1 121 ? 40.475 -17.429 -15.393 1.00 18.30 ?  121  VAL   B HG21 1 
ATOM   6015 H  HG22 . VAL   B 1 121 ? 41.106 -17.477 -13.936 1.00 18.30 ?  121  VAL   B HG22 1 
ATOM   6016 H  HG23 . VAL   B 1 121 ? 39.729 -18.214 -14.231 1.00 18.30 ?  121  VAL   B HG23 1 
ATOM   6017 N  N    . LEU   B 1 122 ? 40.320 -17.700 -11.175 1.00 10.72 ?  122  LEU   B N    1 
ATOM   6018 C  CA   . LEU   B 1 122 ? 41.297 -18.059 -10.150 1.00 10.46 ?  122  LEU   B CA   1 
ATOM   6019 C  C    . LEU   B 1 122 ? 41.950 -19.392 -10.473 1.00 10.57 ?  122  LEU   B C    1 
ATOM   6020 O  O    . LEU   B 1 122 ? 41.289 -20.312 -10.974 1.00 12.01 ?  122  LEU   B O    1 
ATOM   6021 C  CB   . LEU   B 1 122 ? 40.644 -18.293 -8.772  1.00 12.65 ?  122  LEU   B CB   1 
ATOM   6022 C  CG   . LEU   B 1 122 ? 39.611 -17.277 -8.274  1.00 12.63 ?  122  LEU   B CG   1 
ATOM   6023 C  CD1  . LEU   B 1 122 ? 38.217 -17.639 -8.756  1.00 13.39 ?  122  LEU   B CD1  1 
ATOM   6024 C  CD2  . LEU   B 1 122 ? 39.655 -17.183 -6.761  1.00 11.74 ?  122  LEU   B CD2  1 
ATOM   6025 H  H    . LEU   B 1 122 ? 39.889 -18.382 -11.483 1.00 12.88 ?  122  LEU   B H    1 
ATOM   6026 H  HA   . LEU   B 1 122 ? 41.977 -17.370 -10.070 1.00 12.57 ?  122  LEU   B HA   1 
ATOM   6027 H  HB2  . LEU   B 1 122 ? 40.200 -19.154 -8.797  1.00 15.20 ?  122  LEU   B HB2  1 
ATOM   6028 H  HB3  . LEU   B 1 122 ? 41.349 -18.319 -8.108  1.00 15.20 ?  122  LEU   B HB3  1 
ATOM   6029 H  HG   . LEU   B 1 122 ? 39.829 -16.404 -8.635  1.00 15.17 ?  122  LEU   B HG   1 
ATOM   6030 H  HD11 . LEU   B 1 122 ? 37.583 -16.996 -8.401  1.00 16.08 ?  122  LEU   B HD11 1 
ATOM   6031 H  HD12 . LEU   B 1 122 ? 38.199 -17.612 -9.728  1.00 16.08 ?  122  LEU   B HD12 1 
ATOM   6032 H  HD13 . LEU   B 1 122 ? 37.994 -18.529 -8.447  1.00 16.08 ?  122  LEU   B HD13 1 
ATOM   6033 H  HD21 . LEU   B 1 122 ? 38.974 -16.562 -6.458  1.00 14.11 ?  122  LEU   B HD21 1 
ATOM   6034 H  HD22 . LEU   B 1 122 ? 39.494 -18.062 -6.381  1.00 14.11 ?  122  LEU   B HD22 1 
ATOM   6035 H  HD23 . LEU   B 1 122 ? 40.533 -16.866 -6.489  1.00 14.11 ?  122  LEU   B HD23 1 
ATOM   6036 N  N    . LEU   B 1 123 ? 43.236 -19.505 -10.110 1.00 10.26 ?  123  LEU   B N    1 
ATOM   6037 C  CA   . LEU   B 1 123 ? 43.950 -20.775 -9.996  1.00 10.56 ?  123  LEU   B CA   1 
ATOM   6038 C  C    . LEU   B 1 123 ? 43.921 -21.173 -8.524  1.00 10.32 ?  123  LEU   B C    1 
ATOM   6039 O  O    . LEU   B 1 123 ? 44.277 -20.354 -7.666  1.00 10.71 ?  123  LEU   B O    1 
ATOM   6040 C  CB   . LEU   B 1 123 ? 45.399 -20.596 -10.462 1.00 10.84 ?  123  LEU   B CB   1 
ATOM   6041 C  CG   . LEU   B 1 123 ? 46.340 -21.781 -10.225 1.00 11.54 ?  123  LEU   B CG   1 
ATOM   6042 C  CD1  . LEU   B 1 123 ? 45.900 -23.033 -10.979 1.00 12.15 ?  123  LEU   B CD1  1 
ATOM   6043 C  CD2  . LEU   B 1 123 ? 47.756 -21.394 -10.615 1.00 12.24 ?  123  LEU   B CD2  1 
ATOM   6044 H  H    . LEU   B 1 123 ? 43.732 -18.828 -9.903  1.00 12.32 ?  123  LEU   B H    1 
ATOM   6045 H  HA   . LEU   B 1 123 ? 43.511 -21.461 -10.527 1.00 12.68 ?  123  LEU   B HA   1 
ATOM   6046 H  HB2  . LEU   B 1 123 ? 45.387 -20.424 -11.416 1.00 13.02 ?  123  LEU   B HB2  1 
ATOM   6047 H  HB3  . LEU   B 1 123 ? 45.774 -19.837 -9.998  1.00 13.02 ?  123  LEU   B HB3  1 
ATOM   6048 H  HG   . LEU   B 1 123 ? 46.342 -22.000 -9.281  1.00 13.86 ?  123  LEU   B HG   1 
ATOM   6049 H  HD11 . LEU   B 1 123 ? 46.536 -23.743 -10.811 1.00 14.59 ?  123  LEU   B HD11 1 
ATOM   6050 H  HD12 . LEU   B 1 123 ? 45.018 -23.298 -10.664 1.00 14.59 ?  123  LEU   B HD12 1 
ATOM   6051 H  HD13 . LEU   B 1 123 ? 45.862 -22.834 -11.927 1.00 14.59 ?  123  LEU   B HD13 1 
ATOM   6052 H  HD21 . LEU   B 1 123 ? 48.344 -22.152 -10.466 1.00 14.70 ?  123  LEU   B HD21 1 
ATOM   6053 H  HD22 . LEU   B 1 123 ? 47.769 -21.148 -11.555 1.00 14.70 ?  123  LEU   B HD22 1 
ATOM   6054 H  HD23 . LEU   B 1 123 ? 48.037 -20.643 -10.072 1.00 14.70 ?  123  LEU   B HD23 1 
ATOM   6055 N  N    . ALA   B 1 124 ? 43.477 -22.401 -8.217  1.00 10.04 ?  124  ALA   B N    1 
ATOM   6056 C  CA   . ALA   B 1 124 ? 43.228 -22.726 -6.820  1.00 10.22 ?  124  ALA   B CA   1 
ATOM   6057 C  C    . ALA   B 1 124 ? 43.504 -24.184 -6.493  1.00 10.03 ?  124  ALA   B C    1 
ATOM   6058 O  O    . ALA   B 1 124 ? 43.373 -25.055 -7.364  1.00 10.70 ?  124  ALA   B O    1 
ATOM   6059 C  CB   . ALA   B 1 124 ? 41.774 -22.416 -6.435  1.00 10.89 ?  124  ALA   B CB   1 
ATOM   6060 H  H    . ALA   B 1 124 ? 43.313 -23.040 -8.778  1.00 12.07 ?  124  ALA   B H    1 
ATOM   6061 H  HA   . ALA   B 1 124 ? 43.803 -22.177 -6.274  1.00 12.28 ?  124  ALA   B HA   1 
ATOM   6062 H  HB1  . ALA   B 1 124 ? 41.635 -22.637 -5.501  1.00 13.08 ?  124  ALA   B HB1  1 
ATOM   6063 H  HB2  . ALA   B 1 124 ? 41.609 -21.466 -6.575  1.00 13.08 ?  124  ALA   B HB2  1 
ATOM   6064 H  HB3  . ALA   B 1 124 ? 41.177 -22.937 -6.993  1.00 13.08 ?  124  ALA   B HB3  1 
ATOM   6065 N  N    . PRO   B 1 125 ? 43.808 -24.481 -5.231  1.00 10.21 ?  125  PRO   B N    1 
ATOM   6066 C  CA   . PRO   B 1 125 ? 43.745 -25.848 -4.712  1.00 11.00 ?  125  PRO   B CA   1 
ATOM   6067 C  C    . PRO   B 1 125 ? 42.345 -26.118 -4.158  1.00 10.81 ?  125  PRO   B C    1 
ATOM   6068 O  O    . PRO   B 1 125 ? 41.548 -25.205 -3.950  1.00 11.69 ?  125  PRO   B O    1 
ATOM   6069 C  CB   . PRO   B 1 125 ? 44.748 -25.779 -3.553  1.00 12.29 ?  125  PRO   B CB   1 
ATOM   6070 C  CG   . PRO   B 1 125 ? 44.514 -24.394 -2.977  1.00 11.90 ?  125  PRO   B CG   1 
ATOM   6071 C  CD   . PRO   B 1 125 ? 44.148 -23.517 -4.166  1.00 11.04 ?  125  PRO   B CD   1 
ATOM   6072 H  HA   . PRO   B 1 125 ? 44.010 -26.513 -5.369  1.00 13.21 ?  125  PRO   B HA   1 
ATOM   6073 H  HB2  . PRO   B 1 125 ? 44.547 -26.468 -2.898  1.00 14.77 ?  125  PRO   B HB2  1 
ATOM   6074 H  HB3  . PRO   B 1 125 ? 45.654 -25.873 -3.888  1.00 14.77 ?  125  PRO   B HB3  1 
ATOM   6075 H  HG2  . PRO   B 1 125 ? 43.787 -24.418 -2.337  1.00 14.29 ?  125  PRO   B HG2  1 
ATOM   6076 H  HG3  . PRO   B 1 125 ? 45.330 -24.072 -2.551  1.00 14.29 ?  125  PRO   B HG3  1 
ATOM   6077 H  HD2  . PRO   B 1 125 ? 43.386 -22.960 -3.962  1.00 13.26 ?  125  PRO   B HD2  1 
ATOM   6078 H  HD3  . PRO   B 1 125 ? 44.917 -22.975 -4.434  1.00 13.26 ?  125  PRO   B HD3  1 
ATOM   6079 N  N    . LEU   B 1 126 ? 42.072 -27.396 -3.876  1.00 11.68 ?  126  LEU   B N    1 
ATOM   6080 C  CA   . LEU   B 1 126 ? 40.858 -27.766 -3.155  1.00 12.29 ?  126  LEU   B CA   1 
ATOM   6081 C  C    . LEU   B 1 126 ? 40.982 -27.368 -1.691  1.00 12.59 ?  126  LEU   B C    1 
ATOM   6082 O  O    . LEU   B 1 126 ? 41.869 -27.840 -0.973  1.00 14.55 ?  126  LEU   B O    1 
ATOM   6083 C  CB   . LEU   B 1 126 ? 40.612 -29.265 -3.269  1.00 13.59 ?  126  LEU   B CB   1 
ATOM   6084 C  CG   . LEU   B 1 126 ? 40.080 -29.749 -4.620  1.00 14.67 ?  126  LEU   B CG   1 
ATOM   6085 C  CD1  . LEU   B 1 126 ? 40.118 -31.252 -4.692  1.00 16.46 ?  126  LEU   B CD1  1 
ATOM   6086 C  CD2  . LEU   B 1 126 ? 38.664 -29.232 -4.889  1.00 14.82 ?  126  LEU   B CD2  1 
ATOM   6087 H  H    . LEU   B 1 126 ? 42.580 -28.062 -4.085  1.00 14.03 ?  126  LEU   B H    1 
ATOM   6088 H  HA   . LEU   B 1 126 ? 40.106 -27.292 -3.540  1.00 14.76 ?  126  LEU   B HA   1 
ATOM   6089 H  HB2  . LEU   B 1 126 ? 41.448 -29.722 -3.105  1.00 16.32 ?  126  LEU   B HB2  1 
ATOM   6090 H  HB3  . LEU   B 1 126 ? 39.963 -29.514 -2.596  1.00 16.32 ?  126  LEU   B HB3  1 
ATOM   6091 H  HG   . LEU   B 1 126 ? 40.659 -29.397 -5.321  1.00 17.62 ?  126  LEU   B HG   1 
ATOM   6092 H  HD11 . LEU   B 1 126 ? 39.777 -31.534 -5.554  1.00 19.77 ?  126  LEU   B HD11 1 
ATOM   6093 H  HD12 . LEU   B 1 126 ? 41.033 -31.551 -4.581  1.00 19.77 ?  126  LEU   B HD12 1 
ATOM   6094 H  HD13 . LEU   B 1 126 ? 39.563 -31.613 -3.982  1.00 19.77 ?  126  LEU   B HD13 1 
ATOM   6095 H  HD21 . LEU   B 1 126 ? 38.326 -29.647 -5.698  1.00 17.80 ?  126  LEU   B HD21 1 
ATOM   6096 H  HD22 . LEU   B 1 126 ? 38.096 -29.457 -4.138  1.00 17.80 ?  126  LEU   B HD22 1 
ATOM   6097 H  HD23 . LEU   B 1 126 ? 38.689 -28.265 -5.004  1.00 17.80 ?  126  LEU   B HD23 1 
ATOM   6098 N  N    . LEU   B 1 127 ? 40.057 -26.535 -1.231  1.00 12.46 ?  127  LEU   B N    1 
ATOM   6099 C  CA   . LEU   B 1 127 ? 40.114 -26.043 0.135   1.00 12.77 ?  127  LEU   B CA   1 
ATOM   6100 C  C    . LEU   B 1 127 ? 39.835 -27.160 1.129   1.00 12.51 ?  127  LEU   B C    1 
ATOM   6101 O  O    . LEU   B 1 127 ? 39.007 -28.047 0.898   1.00 12.80 ?  127  LEU   B O    1 
ATOM   6102 C  CB   . LEU   B 1 127 ? 39.103 -24.918 0.346   1.00 13.05 ?  127  LEU   B CB   1 
ATOM   6103 C  CG   . LEU   B 1 127 ? 39.288 -23.651 -0.479  1.00 13.97 ?  127  LEU   B CG   1 
ATOM   6104 C  CD1  . LEU   B 1 127 ? 38.159 -22.683 -0.141  1.00 14.21 ?  127  LEU   B CD1  1 
ATOM   6105 C  CD2  . LEU   B 1 127 ? 40.654 -23.012 -0.238  1.00 14.67 ?  127  LEU   B CD2  1 
ATOM   6106 H  H    . LEU   B 1 127 ? 39.389 -26.227 -1.693  1.00 14.97 ?  127  LEU   B H    1 
ATOM   6107 H  HA   . LEU   B 1 127 ? 41.001 -25.685 0.307   1.00 15.33 ?  127  LEU   B HA   1 
ATOM   6108 H  HB2  . LEU   B 1 127 ? 38.220 -25.263 0.143   1.00 15.67 ?  127  LEU   B HB2  1 
ATOM   6109 H  HB3  . LEU   B 1 127 ? 39.135 -24.655 1.280   1.00 15.67 ?  127  LEU   B HB3  1 
ATOM   6110 H  HG   . LEU   B 1 127 ? 39.214 -23.865 -1.419  1.00 16.77 ?  127  LEU   B HG   1 
ATOM   6111 H  HD11 . LEU   B 1 127 ? 38.271 -21.866 -0.658  1.00 17.07 ?  127  LEU   B HD11 1 
ATOM   6112 H  HD12 . LEU   B 1 127 ? 37.308 -23.092 -0.354  1.00 17.07 ?  127  LEU   B HD12 1 
ATOM   6113 H  HD13 . LEU   B 1 127 ? 38.194 -22.471 0.809   1.00 17.07 ?  127  LEU   B HD13 1 
ATOM   6114 H  HD21 . LEU   B 1 127 ? 40.693 -22.156 -0.692  1.00 17.62 ?  127  LEU   B HD21 1 
ATOM   6115 H  HD22 . LEU   B 1 127 ? 40.779 -22.882 0.718   1.00 17.62 ?  127  LEU   B HD22 1 
ATOM   6116 H  HD23 . LEU   B 1 127 ? 41.341 -23.602 -0.581  1.00 17.62 ?  127  LEU   B HD23 1 
ATOM   6117 N  N    . SER   B 1 128 ? 40.518 -27.084 2.263   1.00 12.23 ?  128  SER   B N    1 
ATOM   6118 C  CA   . SER   B 1 128 ? 40.395 -27.994 3.391   1.00 13.18 ?  128  SER   B CA   1 
ATOM   6119 C  C    . SER   B 1 128 ? 40.878 -29.408 3.078   1.00 14.12 ?  128  SER   B C    1 
ATOM   6120 O  O    . SER   B 1 128 ? 40.787 -30.282 3.942   1.00 15.73 ?  128  SER   B O    1 
ATOM   6121 C  CB   . SER   B 1 128 ? 38.994 -27.982 4.019   1.00 13.08 ?  128  SER   B CB   1 
ATOM   6122 O  OG   . SER   B 1 128 ? 38.707 -26.706 4.586   1.00 13.98 ?  128  SER   B OG   1 
ATOM   6123 H  H    . SER   B 1 128 ? 41.090 -26.455 2.407   1.00 14.69 ?  128  SER   B H    1 
ATOM   6124 H  HA   . SER   B 1 128 ? 40.988 -27.657 4.072   1.00 15.83 ?  128  SER   B HA   1 
ATOM   6125 H  HB2  . SER   B 1 128 ? 38.331 -28.192 3.341   1.00 15.71 ?  128  SER   B HB2  1 
ATOM   6126 H  HB3  . SER   B 1 128 ? 38.962 -28.661 4.724   1.00 15.71 ?  128  SER   B HB3  1 
ATOM   6127 H  HG   . SER   B 1 128 ? 39.282 -26.525 5.174   1.00 16.79 ?  128  SER   B HG   1 
ATOM   6128 N  N    . ALA   B 1 129 ? 41.447 -29.642 1.891   1.00 15.57 ?  129  ALA   B N    1 
ATOM   6129 C  CA   . ALA   B 1 129 ? 41.991 -30.943 1.539   1.00 16.63 ?  129  ALA   B CA   1 
ATOM   6130 C  C    . ALA   B 1 129 ? 43.395 -31.111 2.117   1.00 15.28 ?  129  ALA   B C    1 
ATOM   6131 O  O    . ALA   B 1 129 ? 43.952 -30.217 2.768   1.00 14.76 ?  129  ALA   B O    1 
ATOM   6132 C  CB   . ALA   B 1 129 ? 42.014 -31.116 0.021   1.00 18.54 ?  129  ALA   B CB   1 
ATOM   6133 H  H    . ALA   B 1 129 ? 41.520 -29.057 1.259   1.00 18.69 ?  129  ALA   B H    1 
ATOM   6134 H  HA   . ALA   B 1 129 ? 41.426 -31.636 1.909   1.00 19.97 ?  129  ALA   B HA   1 
ATOM   6135 H  HB1  . ALA   B 1 129 ? 42.370 -31.995 -0.193  1.00 22.26 ?  129  ALA   B HB1  1 
ATOM   6136 H  HB2  . ALA   B 1 129 ? 41.109 -31.037 -0.320  1.00 22.26 ?  129  ALA   B HB2  1 
ATOM   6137 H  HB3  . ALA   B 1 129 ? 42.576 -30.429 -0.370  1.00 22.26 ?  129  ALA   B HB3  1 
ATOM   6138 N  N    . GLY   B 1 130 ? 43.973 -32.282 1.866   1.00 15.13 ?  130  GLY   B N    1 
ATOM   6139 C  CA   . GLY   B 1 130 ? 45.364 -32.511 2.216   1.00 15.65 ?  130  GLY   B CA   1 
ATOM   6140 C  C    . GLY   B 1 130 ? 45.580 -32.421 3.709   1.00 15.82 ?  130  GLY   B C    1 
ATOM   6141 O  O    . GLY   B 1 130 ? 44.882 -33.067 4.505   1.00 16.55 ?  130  GLY   B O    1 
ATOM   6142 H  H    . GLY   B 1 130 ? 43.589 -32.953 1.486   1.00 18.18 ?  130  GLY   B H    1 
ATOM   6143 H  HA2  . GLY   B 1 130 ? 45.638 -33.393 1.914   1.00 18.79 ?  130  GLY   B HA2  1 
ATOM   6144 H  HA3  . GLY   B 1 130 ? 45.927 -31.851 1.779   1.00 18.79 ?  130  GLY   B HA3  1 
ATOM   6145 N  N    . ILE   B 1 131 ? 46.553 -31.590 4.099   1.00 16.05 ?  131  ILE   B N    1 
ATOM   6146 C  CA   . ILE   B 1 131 ? 46.922 -31.471 5.504   1.00 17.11 ?  131  ILE   B CA   1 
ATOM   6147 C  C    . ILE   B 1 131 ? 45.810 -30.881 6.354   1.00 16.14 ?  131  ILE   B C    1 
ATOM   6148 O  O    . ILE   B 1 131 ? 45.890 -30.959 7.584   1.00 17.42 ?  131  ILE   B O    1 
ATOM   6149 C  CB   . ILE   B 1 131 ? 48.245 -30.695 5.696   1.00 19.01 ?  131  ILE   B CB   1 
ATOM   6150 C  CG1  . ILE   B 1 131 ? 48.069 -29.215 5.332   1.00 19.94 ?  131  ILE   B CG1  1 
ATOM   6151 C  CG2  . ILE   B 1 131 ? 49.361 -31.317 4.861   1.00 20.28 ?  131  ILE   B CG2  1 
ATOM   6152 C  CD1  . ILE   B 1 131 ? 49.272 -28.345 5.660   1.00 21.49 ?  131  ILE   B CD1  1 
ATOM   6153 H  H    . ILE   B 1 131 ? 47.007 -31.083 3.569   1.00 19.28 ?  131  ILE   B H    1 
ATOM   6154 H  HA   . ILE   B 1 131 ? 47.078 -32.366 5.838   1.00 20.55 ?  131  ILE   B HA   1 
ATOM   6155 H  HB   . ILE   B 1 131 ? 48.494 -30.749 6.631   1.00 22.82 ?  131  ILE   B HB   1 
ATOM   6156 H  HG12 . ILE   B 1 131 ? 47.901 -29.148 4.379   1.00 23.94 ?  131  ILE   B HG12 1 
ATOM   6157 H  HG13 . ILE   B 1 131 ? 47.309 -28.852 5.820   1.00 23.94 ?  131  ILE   B HG13 1 
ATOM   6158 H  HG21 . ILE   B 1 131 ? 50.203 -30.906 5.108   1.00 24.35 ?  131  ILE   B HG21 1 
ATOM   6159 H  HG22 . ILE   B 1 131 ? 49.388 -32.267 5.035   1.00 24.35 ?  131  ILE   B HG22 1 
ATOM   6160 H  HG23 . ILE   B 1 131 ? 49.175 -31.154 3.922   1.00 24.35 ?  131  ILE   B HG23 1 
ATOM   6161 H  HD11 . ILE   B 1 131 ? 49.044 -27.417 5.490   1.00 25.81 ?  131  ILE   B HD11 1 
ATOM   6162 H  HD12 . ILE   B 1 131 ? 49.499 -28.463 6.596   1.00 25.81 ?  131  ILE   B HD12 1 
ATOM   6163 H  HD13 . ILE   B 1 131 ? 50.016 -28.613 5.101   1.00 25.81 ?  131  ILE   B HD13 1 
ATOM   6164 N  N    . PHE   B 1 132 ? 44.774 -30.303 5.736   1.00 15.24 ?  132  PHE   B N    1 
ATOM   6165 C  CA   . PHE   B 1 132 ? 43.625 -29.787 6.476   1.00 15.49 ?  132  PHE   B CA   1 
ATOM   6166 C  C    . PHE   B 1 132 ? 42.597 -30.870 6.803   1.00 16.69 ?  132  PHE   B C    1 
ATOM   6167 O  O    . PHE   B 1 132 ? 41.695 -30.615 7.608   1.00 18.46 ?  132  PHE   B O    1 
ATOM   6168 C  CB   . PHE   B 1 132 ? 42.951 -28.654 5.690   1.00 14.35 ?  132  PHE   B CB   1 
ATOM   6169 C  CG   . PHE   B 1 132 ? 43.650 -27.310 5.790   1.00 14.00 ?  132  PHE   B CG   1 
ATOM   6170 C  CD1  . PHE   B 1 132 ? 44.947 -27.130 5.327   1.00 15.64 ?  132  PHE   B CD1  1 
ATOM   6171 C  CD2  . PHE   B 1 132 ? 42.967 -26.209 6.291   1.00 13.80 ?  132  PHE   B CD2  1 
ATOM   6172 C  CE1  . PHE   B 1 132 ? 45.563 -25.888 5.406   1.00 15.76 ?  132  PHE   B CE1  1 
ATOM   6173 C  CE2  . PHE   B 1 132 ? 43.571 -24.969 6.369   1.00 14.17 ?  132  PHE   B CE2  1 
ATOM   6174 C  CZ   . PHE   B 1 132 ? 44.867 -24.808 5.923   1.00 15.10 ?  132  PHE   B CZ   1 
ATOM   6175 H  H    . PHE   B 1 132 ? 44.712 -30.205 4.884   1.00 18.30 ?  132  PHE   B H    1 
ATOM   6176 H  HA   . PHE   B 1 132 ? 43.943 -29.419 7.315   1.00 18.60 ?  132  PHE   B HA   1 
ATOM   6177 H  HB2  . PHE   B 1 132 ? 42.929 -28.908 4.756   1.00 17.23 ?  132  PHE   B HB2  1 
ATOM   6178 H  HB3  . PHE   B 1 132 ? 42.047 -28.550 6.025   1.00 17.23 ?  132  PHE   B HB3  1 
ATOM   6179 H  HD1  . PHE   B 1 132 ? 45.417 -27.862 4.985   1.00 18.79 ?  132  PHE   B HD1  1 
ATOM   6180 H  HD2  . PHE   B 1 132 ? 42.090 -26.316 6.593   1.00 16.57 ?  132  PHE   B HD2  1 
ATOM   6181 H  HE1  . PHE   B 1 132 ? 46.436 -25.785 5.109   1.00 18.93 ?  132  PHE   B HE1  1 
ATOM   6182 H  HE2  . PHE   B 1 132 ? 43.101 -24.244 6.719   1.00 17.02 ?  132  PHE   B HE2  1 
ATOM   6183 H  HZ   . PHE   B 1 132 ? 45.275 -23.971 5.980   1.00 18.14 ?  132  PHE   B HZ   1 
ATOM   6184 N  N    . GLY   B 1 133 ? 42.692 -32.062 6.197   1.00 16.37 ?  133  GLY   B N    1 
ATOM   6185 C  CA   . GLY   B 1 133 ? 41.982 -33.235 6.682   1.00 17.61 ?  133  GLY   B CA   1 
ATOM   6186 C  C    . GLY   B 1 133 ? 40.588 -33.501 6.145   1.00 18.25 ?  133  GLY   B C    1 
ATOM   6187 O  O    . GLY   B 1 133 ? 40.005 -34.530 6.505   1.00 20.44 ?  133  GLY   B O    1 
ATOM   6188 H  H    . GLY   B 1 133 ? 43.177 -32.209 5.498   1.00 19.66 ?  133  GLY   B H    1 
ATOM   6189 H  HA2  . GLY   B 1 133 ? 42.522 -34.016 6.488   1.00 21.14 ?  133  GLY   B HA2  1 
ATOM   6190 H  HA3  . GLY   B 1 133 ? 41.906 -33.163 7.644   1.00 21.14 ?  133  GLY   B HA3  1 
ATOM   6191 N  N    . ALA   B 1 134 ? 40.023 -32.627 5.316   1.00 17.24 ?  134  ALA   B N    1 
ATOM   6192 C  CA   . ALA   B 1 134 ? 38.702 -32.916 4.776   1.00 17.23 ?  134  ALA   B CA   1 
ATOM   6193 C  C    . ALA   B 1 134 ? 38.806 -33.896 3.612   1.00 16.96 ?  134  ALA   B C    1 
ATOM   6194 O  O    . ALA   B 1 134 ? 39.868 -34.070 3.006   1.00 17.80 ?  134  ALA   B O    1 
ATOM   6195 C  CB   . ALA   B 1 134 ? 38.007 -31.634 4.318   1.00 17.84 ?  134  ALA   B CB   1 
ATOM   6196 H  H    . ALA   B 1 134 ? 40.368 -31.875 5.063   1.00 20.70 ?  134  ALA   B H    1 
ATOM   6197 H  HA   . ALA   B 1 134 ? 38.160 -33.323 5.466   1.00 20.69 ?  134  ALA   B HA   1 
ATOM   6198 H  HB1  . ALA   B 1 134 ? 37.123 -31.859 3.981   1.00 21.42 ?  134  ALA   B HB1  1 
ATOM   6199 H  HB2  . ALA   B 1 134 ? 37.927 -31.031 5.074   1.00 21.42 ?  134  ALA   B HB2  1 
ATOM   6200 H  HB3  . ALA   B 1 134 ? 38.531 -31.219 3.617   1.00 21.42 ?  134  ALA   B HB3  1 
ATOM   6201 N  N    . ASP   B 1 135 ? 37.683 -34.537 3.309   1.00 17.49 ?  135  ASP   B N    1 
ATOM   6202 C  CA   . ASP   B 1 135 ? 37.592 -35.426 2.158   1.00 18.26 ?  135  ASP   B CA   1 
ATOM   6203 C  C    . ASP   B 1 135 ? 37.677 -34.585 0.890   1.00 16.86 ?  135  ASP   B C    1 
ATOM   6204 O  O    . ASP   B 1 135 ? 36.813 -33.721 0.674   1.00 16.87 ?  135  ASP   B O    1 
ATOM   6205 C  CB   . ASP   B 1 135 ? 36.255 -36.164 2.218   1.00 20.23 ?  135  ASP   B CB   1 
ATOM   6206 C  CG   . ASP   B 1 135 ? 36.068 -37.156 1.084   1.00 22.20 ?  135  ASP   B CG   1 
ATOM   6207 O  OD1  . ASP   B 1 135 ? 36.926 -37.205 0.180   1.00 22.00 ?  135  ASP   B OD1  1 
ATOM   6208 O  OD2  . ASP   B 1 135 ? 35.060 -37.903 1.108   1.00 25.35 -1 135  ASP   B OD2  1 
ATOM   6209 H  H    . ASP   B 1 135 ? 36.955 -34.474 3.759   1.00 21.00 ?  135  ASP   B H    1 
ATOM   6210 H  HA   . ASP   B 1 135 ? 38.316 -36.073 2.181   1.00 21.93 ?  135  ASP   B HA   1 
ATOM   6211 H  HB2  . ASP   B 1 135 ? 36.209 -36.653 3.052   1.00 24.30 ?  135  ASP   B HB2  1 
ATOM   6212 H  HB3  . ASP   B 1 135 ? 35.540 -35.518 2.166   1.00 24.30 ?  135  ASP   B HB3  1 
ATOM   6213 N  N    . PRO   B 1 136 ? 38.685 -34.782 0.036   1.00 16.99 ?  136  PRO   B N    1 
ATOM   6214 C  CA   . PRO   B 1 136 ? 38.766 -33.964 -1.184  1.00 16.29 ?  136  PRO   B CA   1 
ATOM   6215 C  C    . PRO   B 1 136 ? 37.565 -34.116 -2.094  1.00 15.44 ?  136  PRO   B C    1 
ATOM   6216 O  O    . PRO   B 1 136 ? 37.235 -33.169 -2.814  1.00 14.63 ?  136  PRO   B O    1 
ATOM   6217 C  CB   . PRO   B 1 136 ? 40.066 -34.441 -1.850  1.00 17.33 ?  136  PRO   B CB   1 
ATOM   6218 C  CG   . PRO   B 1 136 ? 40.274 -35.828 -1.311  1.00 18.68 ?  136  PRO   B CG   1 
ATOM   6219 C  CD   . PRO   B 1 136 ? 39.767 -35.778 0.101   1.00 18.29 ?  136  PRO   B CD   1 
ATOM   6220 H  HA   . PRO   B 1 136 ? 38.852 -33.028 -0.957  1.00 19.56 ?  136  PRO   B HA   1 
ATOM   6221 H  HB2  . PRO   B 1 136 ? 39.959 -34.457 -2.818  1.00 20.81 ?  136  PRO   B HB2  1 
ATOM   6222 H  HB3  . PRO   B 1 136 ? 40.794 -33.855 -1.597  1.00 20.81 ?  136  PRO   B HB3  1 
ATOM   6223 H  HG2  . PRO   B 1 136 ? 39.763 -36.465 -1.836  1.00 22.43 ?  136  PRO   B HG2  1 
ATOM   6224 H  HG3  . PRO   B 1 136 ? 41.218 -36.047 -1.328  1.00 22.43 ?  136  PRO   B HG3  1 
ATOM   6225 H  HD2  . PRO   B 1 136 ? 39.418 -36.643 0.364   1.00 21.97 ?  136  PRO   B HD2  1 
ATOM   6226 H  HD3  . PRO   B 1 136 ? 40.463 -35.473 0.703   1.00 21.97 ?  136  PRO   B HD3  1 
ATOM   6227 N  N    . ILE   B 1 137 ? 36.904 -35.280 -2.090  1.00 15.72 ?  137  ILE   B N    1 
ATOM   6228 C  CA   . ILE   B 1 137 ? 35.682 -35.448 -2.874  1.00 16.29 ?  137  ILE   B CA   1 
ATOM   6229 C  C    . ILE   B 1 137 ? 34.612 -34.480 -2.388  1.00 15.93 ?  137  ILE   B C    1 
ATOM   6230 O  O    . ILE   B 1 137 ? 33.891 -33.867 -3.185  1.00 15.67 ?  137  ILE   B O    1 
ATOM   6231 C  CB   . ILE   B 1 137 ? 35.208 -36.917 -2.820  1.00 18.30 ?  137  ILE   B CB   1 
ATOM   6232 C  CG1  . ILE   B 1 137 ? 36.179 -37.814 -3.585  1.00 20.62 ?  137  ILE   B CG1  1 
ATOM   6233 C  CG2  . ILE   B 1 137 ? 33.801 -37.059 -3.393  1.00 18.66 ?  137  ILE   B CG2  1 
ATOM   6234 C  CD1  . ILE   B 1 137 ? 35.900 -39.300 -3.427  1.00 22.95 ?  137  ILE   B CD1  1 
ATOM   6235 H  H    . ILE   B 1 137 ? 37.140 -35.981 -1.653  1.00 18.87 ?  137  ILE   B H    1 
ATOM   6236 H  HA   . ILE   B 1 137 ? 35.868 -35.239 -3.805  1.00 19.57 ?  137  ILE   B HA   1 
ATOM   6237 H  HB   . ILE   B 1 137 ? 35.186 -37.203 -1.898  1.00 21.97 ?  137  ILE   B HB   1 
ATOM   6238 H  HG12 . ILE   B 1 137 ? 36.125 -37.609 -4.532  1.00 24.76 ?  137  ILE   B HG12 1 
ATOM   6239 H  HG13 . ILE   B 1 137 ? 37.077 -37.651 -3.263  1.00 24.76 ?  137  ILE   B HG13 1 
ATOM   6240 H  HG21 . ILE   B 1 137 ? 33.557 -37.999 -3.429  1.00 22.41 ?  137  ILE   B HG21 1 
ATOM   6241 H  HG22 . ILE   B 1 137 ? 33.173 -36.593 -2.823  1.00 22.41 ?  137  ILE   B HG22 1 
ATOM   6242 H  HG23 . ILE   B 1 137 ? 33.784 -36.684 -4.287  1.00 22.41 ?  137  ILE   B HG23 1 
ATOM   6243 H  HD11 . ILE   B 1 137 ? 36.524 -39.787 -3.984  1.00 27.55 ?  137  ILE   B HD11 1 
ATOM   6244 H  HD12 . ILE   B 1 137 ? 36.019 -39.549 -2.496  1.00 27.55 ?  137  ILE   B HD12 1 
ATOM   6245 H  HD13 . ILE   B 1 137 ? 34.995 -39.500 -3.710  1.00 27.55 ?  137  ILE   B HD13 1 
ATOM   6246 N  N    . HIS   B 1 138 ? 34.493 -34.332 -1.072  1.00 15.87 ?  138  HIS   B N    1 
ATOM   6247 C  CA   . HIS   B 1 138 ? 33.545 -33.367 -0.528  1.00 16.34 ?  138  HIS   B CA   1 
ATOM   6248 C  C    . HIS   B 1 138 ? 33.958 -31.938 -0.851  1.00 15.16 ?  138  HIS   B C    1 
ATOM   6249 O  O    . HIS   B 1 138 ? 33.108 -31.097 -1.160  1.00 15.91 ?  138  HIS   B O    1 
ATOM   6250 C  CB   . HIS   B 1 138 ? 33.436 -33.553 0.978   1.00 17.65 ?  138  HIS   B CB   1 
ATOM   6251 C  CG   . HIS   B 1 138 ? 32.516 -32.572 1.626   1.00 19.18 ?  138  HIS   B CG   1 
ATOM   6252 N  ND1  . HIS   B 1 138 ? 31.174 -32.503 1.322   1.00 20.98 ?  138  HIS   B ND1  1 
ATOM   6253 C  CD2  . HIS   B 1 138 ? 32.749 -31.598 2.535   1.00 19.78 ?  138  HIS   B CD2  1 
ATOM   6254 C  CE1  . HIS   B 1 138 ? 30.614 -31.540 2.032   1.00 20.94 ?  138  HIS   B CE1  1 
ATOM   6255 N  NE2  . HIS   B 1 138 ? 31.548 -30.974 2.776   1.00 20.14 ?  138  HIS   B NE2  1 
ATOM   6256 H  H    . HIS   B 1 138 ? 34.949 -34.769 -0.486  1.00 19.06 ?  138  HIS   B H    1 
ATOM   6257 H  HA   . HIS   B 1 138 ? 32.673 -33.535 -0.922  1.00 19.62 ?  138  HIS   B HA   1 
ATOM   6258 H  HB2  . HIS   B 1 138 ? 33.096 -34.446 1.159   1.00 21.19 ?  138  HIS   B HB2  1 
ATOM   6259 H  HB3  . HIS   B 1 138 ? 34.313 -33.448 1.371   1.00 21.19 ?  138  HIS   B HB3  1 
ATOM   6260 H  HD1  . HIS   B 1 138 ? 30.761 -33.019 0.763   1.00 25.19 ?  138  HIS   B HD1  1 
ATOM   6261 H  HD2  . HIS   B 1 138 ? 33.558 -31.399 2.935   1.00 23.75 ?  138  HIS   B HD2  1 
ATOM   6262 H  HE1  . HIS   B 1 138 ? 29.709 -31.310 2.013   1.00 25.15 ?  138  HIS   B HE1  1 
ATOM   6263 N  N    . SER   B 1 139 ? 35.253 -31.639 -0.783  1.00 14.63 ?  139  SER   B N    1 
ATOM   6264 C  CA   . SER   B 1 139 ? 35.690 -30.289 -1.101  1.00 14.09 ?  139  SER   B CA   1 
ATOM   6265 C  C    . SER   B 1 139 ? 35.352 -29.933 -2.541  1.00 13.09 ?  139  SER   B C    1 
ATOM   6266 O  O    . SER   B 1 139 ? 34.911 -28.814 -2.818  1.00 13.69 ?  139  SER   B O    1 
ATOM   6267 C  CB   . SER   B 1 139 ? 37.181 -30.144 -0.831  1.00 14.23 ?  139  SER   B CB   1 
ATOM   6268 O  OG   . SER   B 1 139 ? 37.592 -28.812 -1.098  1.00 14.29 ?  139  SER   B OG   1 
ATOM   6269 H  H    . SER   B 1 139 ? 35.880 -32.185 -0.574  1.00 17.57 ?  139  SER   B H    1 
ATOM   6270 H  HA   . SER   B 1 139 ? 35.216 -29.667 -0.531  1.00 16.93 ?  139  SER   B HA   1 
ATOM   6271 H  HB2  . SER   B 1 139 ? 37.355 -30.351 0.100   1.00 17.09 ?  139  SER   B HB2  1 
ATOM   6272 H  HB3  . SER   B 1 139 ? 37.673 -30.745 -1.408  1.00 17.09 ?  139  SER   B HB3  1 
ATOM   6273 H  HG   . SER   B 1 139 ? 38.417 -28.726 -0.939  1.00 17.17 ?  139  SER   B HG   1 
ATOM   6274 N  N    . LEU   B 1 140 ? 35.535 -30.876 -3.467  1.00 13.30 ?  140  LEU   B N    1 
ATOM   6275 C  CA   . LEU   B 1 140 ? 35.164 -30.627 -4.856  1.00 13.48 ?  140  LEU   B CA   1 
ATOM   6276 C  C    . LEU   B 1 140 ? 33.659 -30.400 -4.980  1.00 13.59 ?  140  LEU   B C    1 
ATOM   6277 O  O    . LEU   B 1 140 ? 33.218 -29.511 -5.716  1.00 13.43 ?  140  LEU   B O    1 
ATOM   6278 C  CB   . LEU   B 1 140 ? 35.634 -31.787 -5.736  1.00 13.71 ?  140  LEU   B CB   1 
ATOM   6279 C  CG   . LEU   B 1 140 ? 35.265 -31.681 -7.209  1.00 13.79 ?  140  LEU   B CG   1 
ATOM   6280 C  CD1  . LEU   B 1 140 ? 35.827 -30.403 -7.797  1.00 14.80 ?  140  LEU   B CD1  1 
ATOM   6281 C  CD2  . LEU   B 1 140 ? 35.744 -32.903 -7.968  1.00 14.63 ?  140  LEU   B CD2  1 
ATOM   6282 H  H    . LEU   B 1 140 ? 35.857 -31.655 -3.322  1.00 15.98 ?  140  LEU   B H    1 
ATOM   6283 H  HA   . LEU   B 1 140 ? 35.612 -29.823 -5.161  1.00 16.19 ?  140  LEU   B HA   1 
ATOM   6284 H  HB2  . LEU   B 1 140 ? 36.603 -31.844 -5.684  1.00 16.47 ?  140  LEU   B HB2  1 
ATOM   6285 H  HB3  . LEU   B 1 140 ? 35.244 -32.610 -5.403  1.00 16.47 ?  140  LEU   B HB3  1 
ATOM   6286 H  HG   . LEU   B 1 140 ? 34.303 -31.639 -7.290  1.00 16.56 ?  140  LEU   B HG   1 
ATOM   6287 H  HD11 . LEU   B 1 140 ? 35.727 -30.427 -8.760  1.00 17.77 ?  140  LEU   B HD11 1 
ATOM   6288 H  HD12 . LEU   B 1 140 ? 35.336 -29.645 -7.434  1.00 17.77 ?  140  LEU   B HD12 1 
ATOM   6289 H  HD13 . LEU   B 1 140 ? 36.765 -30.330 -7.562  1.00 17.77 ?  140  LEU   B HD13 1 
ATOM   6290 H  HD21 . LEU   B 1 140 ? 35.495 -32.807 -8.902  1.00 17.57 ?  140  LEU   B HD21 1 
ATOM   6291 H  HD22 . LEU   B 1 140 ? 36.705 -32.970 -7.885  1.00 17.57 ?  140  LEU   B HD22 1 
ATOM   6292 H  HD23 . LEU   B 1 140 ? 35.318 -33.687 -7.591  1.00 17.57 ?  140  LEU   B HD23 1 
ATOM   6293 N  N    . ARG   B 1 141 ? 32.860 -31.189 -4.256  1.00 14.11 ?  141  ARG   B N    1 
ATOM   6294 C  CA   . ARG   B 1 141 ? 31.409 -31.015 -4.237  1.00 14.89 ?  141  ARG   B CA   1 
ATOM   6295 C  C    . ARG   B 1 141 ? 31.032 -29.601 -3.808  1.00 14.04 ?  141  ARG   B C    1 
ATOM   6296 O  O    . ARG   B 1 141 ? 30.225 -28.923 -4.463  1.00 14.16 ?  141  ARG   B O    1 
ATOM   6297 C  CB   . ARG   B 1 141 ? 30.823 -32.048 -3.265  1.00 16.14 ?  141  ARG   B CB   1 
ATOM   6298 C  CG   . ARG   B 1 141 ? 29.353 -31.929 -2.955  1.00 18.11 ?  141  ARG   B CG   1 
ATOM   6299 C  CD   . ARG   B 1 141 ? 28.567 -32.569 -4.025  1.00 20.24 ?  141  ARG   B CD   1 
ATOM   6300 N  NE   . ARG   B 1 141 ? 28.283 -31.652 -5.116  1.00 20.23 ?  141  ARG   B NE   1 
ATOM   6301 C  CZ   . ARG   B 1 141 ? 28.263 -31.992 -6.398  1.00 19.18 ?  141  ARG   B CZ   1 
ATOM   6302 N  NH1  . ARG   B 1 141 ? 28.697 -33.174 -6.811  1.00 19.00 ?  141  ARG   B NH1  1 
ATOM   6303 N  NH2  . ARG   B 1 141 ? 27.783 -31.126 -7.287  1.00 20.24 ?  141  ARG   B NH2  1 
ATOM   6304 H  H    . ARG   B 1 141 ? 33.145 -31.830 -3.762  1.00 16.95 ?  141  ARG   B H    1 
ATOM   6305 H  HA   . ARG   B 1 141 ? 31.051 -31.178 -5.119  1.00 17.88 ?  141  ARG   B HA   1 
ATOM   6306 H  HB2  . ARG   B 1 141 ? 30.983 -32.934 -3.633  1.00 19.39 ?  141  ARG   B HB2  1 
ATOM   6307 H  HB3  . ARG   B 1 141 ? 31.301 -31.973 -2.424  1.00 19.39 ?  141  ARG   B HB3  1 
ATOM   6308 H  HG2  . ARG   B 1 141 ? 29.173 -32.373 -2.117  1.00 21.74 ?  141  ARG   B HG2  1 
ATOM   6309 H  HG3  . ARG   B 1 141 ? 29.102 -30.989 -2.898  1.00 21.74 ?  141  ARG   B HG3  1 
ATOM   6310 H  HD2  . ARG   B 1 141 ? 29.065 -33.330 -4.373  1.00 24.30 ?  141  ARG   B HD2  1 
ATOM   6311 H  HD3  . ARG   B 1 141 ? 27.731 -32.874 -3.653  1.00 24.30 ?  141  ARG   B HD3  1 
ATOM   6312 H  HE   . ARG   B 1 141 ? 28.098 -30.837 -4.912  1.00 24.30 ?  141  ARG   B HE   1 
ATOM   6313 H  HH11 . ARG   B 1 141 ? 29.000 -33.750 -6.249  1.00 22.82 ?  141  ARG   B HH11 1 
ATOM   6314 H  HH12 . ARG   B 1 141 ? 28.682 -33.365 -7.647  1.00 22.82 ?  141  ARG   B HH12 1 
ATOM   6315 H  HH21 . ARG   B 1 141 ? 27.504 -30.353 -7.030  1.00 24.31 ?  141  ARG   B HH21 1 
ATOM   6316 H  HH22 . ARG   B 1 141 ? 27.783 -31.324 -8.124  1.00 24.31 ?  141  ARG   B HH22 1 
ATOM   6317 N  N    . VAL   B 1 142 ? 31.582 -29.155 -2.682  1.00 13.97 ?  142  VAL   B N    1 
ATOM   6318 C  CA   . VAL   B 1 142 ? 31.249 -27.823 -2.194  1.00 13.51 ?  142  VAL   B CA   1 
ATOM   6319 C  C    . VAL   B 1 142 ? 31.717 -26.765 -3.187  1.00 13.33 ?  142  VAL   B C    1 
ATOM   6320 O  O    . VAL   B 1 142 ? 31.019 -25.778 -3.439  1.00 13.68 ?  142  VAL   B O    1 
ATOM   6321 C  CB   . VAL   B 1 142 ? 31.804 -27.598 -0.773  1.00 14.20 ?  142  VAL   B CB   1 
ATOM   6322 C  CG1  . VAL   B 1 142 ? 31.493 -26.179 -0.282  1.00 14.30 ?  142  VAL   B CG1  1 
ATOM   6323 C  CG2  . VAL   B 1 142 ? 31.247 -28.634 0.188   1.00 15.21 ?  142  VAL   B CG2  1 
ATOM   6324 H  H    . VAL   B 1 142 ? 32.144 -29.589 -2.196  1.00 16.78 ?  142  VAL   B H    1 
ATOM   6325 H  HA   . VAL   B 1 142 ? 30.289 -27.751 -2.133  1.00 16.22 ?  142  VAL   B HA   1 
ATOM   6326 H  HB   . VAL   B 1 142 ? 32.770 -27.699 -0.788  1.00 17.06 ?  142  VAL   B HB   1 
ATOM   6327 H  HG11 . VAL   B 1 142 ? 31.697 -26.121 0.664   1.00 17.17 ?  142  VAL   B HG11 1 
ATOM   6328 H  HG12 . VAL   B 1 142 ? 32.043 -25.547 -0.775  1.00 17.17 ?  142  VAL   B HG12 1 
ATOM   6329 H  HG13 . VAL   B 1 142 ? 30.556 -25.993 -0.433  1.00 17.17 ?  142  VAL   B HG13 1 
ATOM   6330 H  HG21 . VAL   B 1 142 ? 31.574 -28.445 1.082   1.00 18.26 ?  142  VAL   B HG21 1 
ATOM   6331 H  HG22 . VAL   B 1 142 ? 30.280 -28.591 0.171   1.00 18.26 ?  142  VAL   B HG22 1 
ATOM   6332 H  HG23 . VAL   B 1 142 ? 31.545 -29.515 -0.092  1.00 18.26 ?  142  VAL   B HG23 1 
ATOM   6333 N  N    . CYS   B 1 143 ? 32.896 -26.961 -3.780  1.00 12.87 ?  143  CYS   B N    1 
ATOM   6334 C  CA   . CYS   B 1 143 ? 33.391 -26.020 -4.782  1.00 12.85 ?  143  CYS   B CA   1 
ATOM   6335 C  C    . CYS   B 1 143 ? 32.385 -25.871 -5.919  1.00 13.08 ?  143  CYS   B C    1 
ATOM   6336 O  O    . CYS   B 1 143 ? 31.979 -24.759 -6.272  1.00 13.07 ?  143  CYS   B O    1 
ATOM   6337 C  CB   . CYS   B 1 143 ? 34.743 -26.512 -5.315  1.00 12.96 ?  143  CYS   B CB   1 
ATOM   6338 S  SG   . CYS   B 1 143 ? 35.496 -25.406 -6.536  1.00 13.39 ?  143  CYS   B SG   1 
ATOM   6339 H  H    . CYS   B 1 143 ? 33.423 -27.617 -3.620  1.00 15.46 ?  143  CYS   B H    1 
ATOM   6340 H  HA   . CYS   B 1 143 ? 33.520 -25.147 -4.376  1.00 15.44 ?  143  CYS   B HA   1 
ATOM   6341 H  HB2  . CYS   B 1 143 ? 35.364 -26.591 -4.576  1.00 15.57 ?  143  CYS   B HB2  1 
ATOM   6342 H  HB3  . CYS   B 1 143 ? 34.619 -27.370 -5.735  1.00 15.57 ?  143  CYS   B HB3  1 
ATOM   6343 H  HG   . CYS   B 1 143 ? 36.563 -25.848 -6.866  1.00 16.09 ?  143  CYS   B HG   1 
ATOM   6344 N  N    . VAL   B 1 144 ? 31.978 -26.994 -6.513  1.00 13.31 ?  144  VAL   B N    1 
ATOM   6345 C  CA   . VAL   B 1 144 ? 31.065 -26.938 -7.650  1.00 14.60 ?  144  VAL   B CA   1 
ATOM   6346 C  C    . VAL   B 1 144 ? 29.727 -26.323 -7.267  1.00 14.63 ?  144  VAL   B C    1 
ATOM   6347 O  O    . VAL   B 1 144 ? 29.112 -25.609 -8.070  1.00 15.81 ?  144  VAL   B O    1 
ATOM   6348 C  CB   . VAL   B 1 144 ? 30.907 -28.352 -8.215  1.00 17.02 ?  144  VAL   B CB   1 
ATOM   6349 C  CG1  . VAL   B 1 144 ? 29.622 -28.497 -9.030  1.00 19.29 ?  144  VAL   B CG1  1 
ATOM   6350 C  CG2  . VAL   B 1 144 ? 32.149 -28.749 -9.016  1.00 17.42 ?  144  VAL   B CG2  1 
ATOM   6351 H  H    . VAL   B 1 144 ? 32.222 -27.784 -6.289  1.00 15.98 ?  144  VAL   B H    1 
ATOM   6352 H  HA   . VAL   B 1 144 ? 31.451 -26.385 -8.347  1.00 17.53 ?  144  VAL   B HA   1 
ATOM   6353 H  HB   . VAL   B 1 144 ? 30.842 -28.973 -7.471  1.00 20.44 ?  144  VAL   B HB   1 
ATOM   6354 H  HG11 . VAL   B 1 144 ? 29.693 -29.295 -9.585  1.00 23.16 ?  144  VAL   B HG11 1 
ATOM   6355 H  HG12 . VAL   B 1 144 ? 28.870 -28.590 -8.426  1.00 23.16 ?  144  VAL   B HG12 1 
ATOM   6356 H  HG13 . VAL   B 1 144 ? 29.512 -27.718 -9.592  1.00 23.16 ?  144  VAL   B HG13 1 
ATOM   6357 H  HG21 . VAL   B 1 144 ? 32.032 -29.650 -9.360  1.00 20.92 ?  144  VAL   B HG21 1 
ATOM   6358 H  HG22 . VAL   B 1 144 ? 32.259 -28.128 -9.754  1.00 20.92 ?  144  VAL   B HG22 1 
ATOM   6359 H  HG23 . VAL   B 1 144 ? 32.924 -28.715 -8.436  1.00 20.92 ?  144  VAL   B HG23 1 
ATOM   6360 N  N    . ASP   B 1 145 ? 29.264 -26.571 -6.047  1.00 14.69 ?  145  ASP   B N    1 
ATOM   6361 C  CA   . ASP   B 1 145 ? 27.957 -26.101 -5.608  1.00 15.42 ?  145  ASP   B CA   1 
ATOM   6362 C  C    . ASP   B 1 145 ? 27.992 -24.679 -5.062  1.00 14.74 ?  145  ASP   B C    1 
ATOM   6363 O  O    . ASP   B 1 145 ? 26.937 -24.137 -4.722  1.00 16.64 ?  145  ASP   B O    1 
ATOM   6364 C  CB   . ASP   B 1 145 ? 27.381 -27.024 -4.529  1.00 16.87 ?  145  ASP   B CB   1 
ATOM   6365 C  CG   . ASP   B 1 145 ? 27.008 -28.396 -5.048  1.00 19.14 ?  145  ASP   B CG   1 
ATOM   6366 O  OD1  . ASP   B 1 145 ? 26.881 -28.585 -6.276  1.00 19.67 ?  145  ASP   B OD1  1 
ATOM   6367 O  OD2  . ASP   B 1 145 ? 26.828 -29.286 -4.196  1.00 21.26 -1 145  ASP   B OD2  1 
ATOM   6368 H  H    . ASP   B 1 145 ? 29.709 -26.987 -5.444  1.00 17.65 ?  145  ASP   B H    1 
ATOM   6369 H  HA   . ASP   B 1 145 ? 27.359 -26.094 -6.364  1.00 18.52 ?  145  ASP   B HA   1 
ATOM   6370 H  HB2  . ASP   B 1 145 ? 28.039 -27.146 -3.836  1.00 20.26 ?  145  ASP   B HB2  1 
ATOM   6371 H  HB3  . ASP   B 1 145 ? 26.580 -26.612 -4.167  1.00 20.26 ?  145  ASP   B HB3  1 
ATOM   6372 N  N    . THR   B 1 146 ? 29.168 -24.064 -4.959  1.00 12.93 ?  146  THR   B N    1 
ATOM   6373 C  CA   . THR   B 1 146 ? 29.312 -22.742 -4.354  1.00 12.81 ?  146  THR   B CA   1 
ATOM   6374 C  C    . THR   B 1 146 ? 29.937 -21.712 -5.278  1.00 12.43 ?  146  THR   B C    1 
ATOM   6375 O  O    . THR   B 1 146 ? 29.480 -20.555 -5.324  1.00 12.74 ?  146  THR   B O    1 
ATOM   6376 C  CB   . THR   B 1 146 ? 30.146 -22.849 -3.071  1.00 13.16 ?  146  THR   B CB   1 
ATOM   6377 O  OG1  . THR   B 1 146 ? 29.571 -23.840 -2.208  1.00 13.34 ?  146  THR   B OG1  1 
ATOM   6378 C  CG2  . THR   B 1 146 ? 30.230 -21.508 -2.351  1.00 13.32 ?  146  THR   B CG2  1 
ATOM   6379 H  H    . THR   B 1 146 ? 29.919 -24.390 -5.243  1.00 15.53 ?  146  THR   B H    1 
ATOM   6380 H  HA   . THR   B 1 146 ? 28.441 -22.413 -4.106  1.00 15.39 ?  146  THR   B HA   1 
ATOM   6381 H  HB   . THR   B 1 146 ? 31.056 -23.112 -3.302  1.00 15.80 ?  146  THR   B HB   1 
ATOM   6382 H  HG1  . THR   B 1 146 ? 29.606 -24.600 -2.587  1.00 16.02 ?  146  THR   B HG1  1 
ATOM   6383 H  HG21 . THR   B 1 146 ? 30.590 -21.629 -1.460  1.00 15.99 ?  146  THR   B HG21 1 
ATOM   6384 H  HG22 . THR   B 1 146 ? 30.810 -20.900 -2.842  1.00 15.99 ?  146  THR   B HG22 1 
ATOM   6385 H  HG23 . THR   B 1 146 ? 29.347 -21.114 -2.285  1.00 15.99 ?  146  THR   B HG23 1 
ATOM   6386 N  N    . VAL   B 1 147 ? 31.001 -22.086 -5.983  1.00 12.41 ?  147  VAL   B N    1 
ATOM   6387 C  CA   . VAL   B 1 147 ? 31.720 -21.148 -6.832  1.00 12.17 ?  147  VAL   B CA   1 
ATOM   6388 C  C    . VAL   B 1 147 ? 30.978 -21.011 -8.150  1.00 12.75 ?  147  VAL   B C    1 
ATOM   6389 O  O    . VAL   B 1 147 ? 30.605 -22.012 -8.779  1.00 13.28 ?  147  VAL   B O    1 
ATOM   6390 C  CB   . VAL   B 1 147 ? 33.173 -21.602 -7.045  1.00 12.08 ?  147  VAL   B CB   1 
ATOM   6391 C  CG1  . VAL   B 1 147 ? 33.930 -20.568 -7.862  1.00 12.29 ?  147  VAL   B CG1  1 
ATOM   6392 C  CG2  . VAL   B 1 147 ? 33.852 -21.819 -5.712  1.00 12.33 ?  147  VAL   B CG2  1 
ATOM   6393 H  H    . VAL   B 1 147 ? 31.329 -22.886 -5.991  1.00 14.91 ?  147  VAL   B H    1 
ATOM   6394 H  HA   . VAL   B 1 147 ? 31.740 -20.281 -6.402  1.00 14.63 ?  147  VAL   B HA   1 
ATOM   6395 H  HB   . VAL   B 1 147 ? 33.186 -22.438 -7.538  1.00 14.51 ?  147  VAL   B HB   1 
ATOM   6396 H  HG11 . VAL   B 1 147 ? 34.872 -20.792 -7.864  1.00 14.76 ?  147  VAL   B HG11 1 
ATOM   6397 H  HG12 . VAL   B 1 147 ? 33.588 -20.563 -8.769  1.00 14.76 ?  147  VAL   B HG12 1 
ATOM   6398 H  HG13 . VAL   B 1 147 ? 33.801 -19.693 -7.456  1.00 14.76 ?  147  VAL   B HG13 1 
ATOM   6399 H  HG21 . VAL   B 1 147 ? 34.794 -21.992 -5.861  1.00 14.81 ?  147  VAL   B HG21 1 
ATOM   6400 H  HG22 . VAL   B 1 147 ? 33.743 -21.019 -5.173  1.00 14.81 ?  147  VAL   B HG22 1 
ATOM   6401 H  HG23 . VAL   B 1 147 ? 33.440 -22.575 -5.271  1.00 14.81 ?  147  VAL   B HG23 1 
ATOM   6402 N  N    . ARG   B 1 148 ? 30.771 -19.759 -8.567  1.00 12.35 ?  148  ARG   B N    1 
ATOM   6403 C  CA   . ARG   B 1 148 ? 30.149 -19.426 -9.838  1.00 12.51 ?  148  ARG   B CA   1 
ATOM   6404 C  C    . ARG   B 1 148 ? 31.104 -18.747 -10.810 1.00 12.56 ?  148  ARG   B C    1 
ATOM   6405 O  O    . ARG   B 1 148 ? 30.812 -18.717 -12.013 1.00 13.96 ?  148  ARG   B O    1 
ATOM   6406 C  CB   . ARG   B 1 148 ? 28.909 -18.543 -9.611  1.00 13.07 ?  148  ARG   B CB   1 
ATOM   6407 C  CG   . ARG   B 1 148 ? 27.839 -19.263 -8.809  1.00 14.05 ?  148  ARG   B CG   1 
ATOM   6408 C  CD   . ARG   B 1 148 ? 26.622 -18.395 -8.489  1.00 15.04 ?  148  ARG   B CD   1 
ATOM   6409 N  NE   . ARG   B 1 148 ? 26.985 -17.194 -7.747  1.00 14.63 ?  148  ARG   B NE   1 
ATOM   6410 C  CZ   . ARG   B 1 148 ? 27.294 -17.164 -6.457  1.00 13.76 ?  148  ARG   B CZ   1 
ATOM   6411 N  NH1  . ARG   B 1 148 ? 27.260 -18.258 -5.709  1.00 13.98 ?  148  ARG   B NH1  1 
ATOM   6412 N  NH2  . ARG   B 1 148 ? 27.674 -16.012 -5.910  1.00 13.69 ?  148  ARG   B NH2  1 
ATOM   6413 H  H    . ARG   B 1 148 ? 30.991 -19.059 -8.102  1.00 14.84 ?  148  ARG   B H    1 
ATOM   6414 H  HA   . ARG   B 1 148 ? 29.848 -20.246 -10.249 1.00 15.02 ?  148  ARG   B HA   1 
ATOM   6415 H  HB2  . ARG   B 1 148 ? 29.171 -17.745 -9.120  1.00 15.71 ?  148  ARG   B HB2  1 
ATOM   6416 H  HB3  . ARG   B 1 148 ? 28.535 -18.296 -10.470 1.00 15.71 ?  148  ARG   B HB3  1 
ATOM   6417 H  HG2  . ARG   B 1 148 ? 27.527 -20.029 -9.321  1.00 16.88 ?  148  ARG   B HG2  1 
ATOM   6418 H  HG3  . ARG   B 1 148 ? 28.218 -19.562 -7.969  1.00 16.88 ?  148  ARG   B HG3  1 
ATOM   6419 H  HD2  . ARG   B 1 148 ? 26.198 -18.120 -9.318  1.00 18.06 ?  148  ARG   B HD2  1 
ATOM   6420 H  HD3  . ARG   B 1 148 ? 25.997 -18.905 -7.949  1.00 18.06 ?  148  ARG   B HD3  1 
ATOM   6421 H  HE   . ARG   B 1 148 ? 27.013 -16.451 -8.180  1.00 17.57 ?  148  ARG   B HE   1 
ATOM   6422 H  HH11 . ARG   B 1 148 ? 27.016 -19.009 -6.048  1.00 16.79 ?  148  ARG   B HH11 1 
ATOM   6423 H  HH12 . ARG   B 1 148 ? 27.462 -18.213 -4.872  1.00 16.79 ?  148  ARG   B HH12 1 
ATOM   6424 H  HH21 . ARG   B 1 148 ? 27.712 -15.301 -6.389  1.00 16.44 ?  148  ARG   B HH21 1 
ATOM   6425 H  HH22 . ARG   B 1 148 ? 27.881 -15.980 -5.076  1.00 16.44 ?  148  ARG   B HH22 1 
ATOM   6426 N  N    . THR   B 1 149 ? 32.211 -18.192 -10.323 1.00 12.42 ?  149  THR   B N    1 
ATOM   6427 C  CA   . THR   B 1 149 ? 33.252 -17.635 -11.172 1.00 12.51 ?  149  THR   B CA   1 
ATOM   6428 C  C    . THR   B 1 149 ? 34.127 -18.774 -11.695 1.00 11.96 ?  149  THR   B C    1 
ATOM   6429 O  O    . THR   B 1 149 ? 33.931 -19.946 -11.362 1.00 12.65 ?  149  THR   B O    1 
ATOM   6430 C  CB   . THR   B 1 149 ? 34.027 -16.585 -10.387 1.00 12.60 ?  149  THR   B CB   1 
ATOM   6431 O  OG1  . THR   B 1 149 ? 34.481 -17.190 -9.177  1.00 12.30 ?  149  THR   B OG1  1 
ATOM   6432 C  CG2  . THR   B 1 149 ? 33.134 -15.383 -10.081 1.00 13.46 ?  149  THR   B CG2  1 
ATOM   6433 H  H    . THR   B 1 149 ? 32.373 -18.109 -9.481  1.00 14.92 ?  149  THR   B H    1 
ATOM   6434 H  HA   . THR   B 1 149 ? 32.839 -17.194 -11.933 1.00 15.03 ?  149  THR   B HA   1 
ATOM   6435 H  HB   . THR   B 1 149 ? 34.787 -16.288 -10.903 1.00 15.14 ?  149  THR   B HB   1 
ATOM   6436 H  HG1  . THR   B 1 149 ? 34.902 -16.622 -8.711  1.00 14.77 ?  149  THR   B HG1  1 
ATOM   6437 H  HG21 . THR   B 1 149 ? 33.638 -14.709 -9.601  1.00 16.17 ?  149  THR   B HG21 1 
ATOM   6438 H  HG22 . THR   B 1 149 ? 32.801 -14.999 -10.908 1.00 16.17 ?  149  THR   B HG22 1 
ATOM   6439 H  HG23 . THR   B 1 149 ? 32.378 -15.657 -9.537  1.00 16.17 ?  149  THR   B HG23 1 
ATOM   6440 N  N    . ASN   B 1 150 ? 35.092 -18.446 -12.541 1.00 12.01 ?  150  ASN   B N    1 
ATOM   6441 C  CA   . ASN   B 1 150 ? 35.851 -19.467 -13.250 1.00 12.75 ?  150  ASN   B CA   1 
ATOM   6442 C  C    . ASN   B 1 150 ? 37.020 -19.921 -12.389 1.00 12.14 ?  150  ASN   B C    1 
ATOM   6443 O  O    . ASN   B 1 150 ? 37.959 -19.157 -12.147 1.00 13.00 ?  150  ASN   B O    1 
ATOM   6444 C  CB   . ASN   B 1 150 ? 36.320 -18.935 -14.595 1.00 14.83 ?  150  ASN   B CB   1 
ATOM   6445 C  CG   . ASN   B 1 150 ? 35.171 -18.720 -15.546 1.00 17.44 ?  150  ASN   B CG   1 
ATOM   6446 O  OD1  . ASN   B 1 150 ? 34.264 -19.543 -15.622 1.00 18.18 ?  150  ASN   B OD1  1 
ATOM   6447 N  ND2  . ASN   B 1 150 ? 35.182 -17.601 -16.251 1.00 19.41 ?  150  ASN   B ND2  1 
ATOM   6448 H  H    . ASN   B 1 150 ? 35.334 -17.637 -12.714 1.00 14.42 ?  150  ASN   B H    1 
ATOM   6449 H  HA   . ASN   B 1 150 ? 35.269 -20.233 -13.410 1.00 15.31 ?  150  ASN   B HA   1 
ATOM   6450 H  HB2  . ASN   B 1 150 ? 36.763 -18.081 -14.457 1.00 17.81 ?  150  ASN   B HB2  1 
ATOM   6451 H  HB3  . ASN   B 1 150 ? 36.930 -19.570 -14.991 1.00 17.81 ?  150  ASN   B HB3  1 
ATOM   6452 H  HD21 . ASN   B 1 150 ? 34.547 -17.434 -16.807 1.00 23.31 ?  150  ASN   B HD21 1 
ATOM   6453 H  HD22 . ASN   B 1 150 ? 35.832 -17.041 -16.164 1.00 23.31 ?  150  ASN   B HD22 1 
ATOM   6454 N  N    . VAL   B 1 151 ? 36.974 -21.166 -11.932 1.00 11.98 ?  151  VAL   B N    1 
ATOM   6455 C  CA   . VAL   B 1 151 ? 37.993 -21.703 -11.042 1.00 12.12 ?  151  VAL   B CA   1 
ATOM   6456 C  C    . VAL   B 1 151 ? 38.697 -22.870 -11.721 1.00 11.77 ?  151  VAL   B C    1 
ATOM   6457 O  O    . VAL   B 1 151 ? 38.053 -23.802 -12.225 1.00 12.91 ?  151  VAL   B O    1 
ATOM   6458 C  CB   . VAL   B 1 151 ? 37.434 -22.050 -9.648  1.00 13.03 ?  151  VAL   B CB   1 
ATOM   6459 C  CG1  . VAL   B 1 151 ? 36.261 -23.034 -9.730  1.00 14.03 ?  151  VAL   B CG1  1 
ATOM   6460 C  CG2  . VAL   B 1 151 ? 38.543 -22.572 -8.747  1.00 13.50 ?  151  VAL   B CG2  1 
ATOM   6461 H  H    . VAL   B 1 151 ? 36.349 -21.730 -12.127 1.00 14.39 ?  151  VAL   B H    1 
ATOM   6462 H  HA   . VAL   B 1 151 ? 38.661 -21.012 -10.905 1.00 14.56 ?  151  VAL   B HA   1 
ATOM   6463 H  HB   . VAL   B 1 151 ? 37.096 -21.237 -9.243  1.00 15.66 ?  151  VAL   B HB   1 
ATOM   6464 H  HG11 . VAL   B 1 151 ? 35.946 -23.232 -8.833  1.00 16.86 ?  151  VAL   B HG11 1 
ATOM   6465 H  HG12 . VAL   B 1 151 ? 35.542 -22.632 -10.248 1.00 16.86 ?  151  VAL   B HG12 1 
ATOM   6466 H  HG13 . VAL   B 1 151 ? 36.558 -23.851 -10.162 1.00 16.86 ?  151  VAL   B HG13 1 
ATOM   6467 H  HG21 . VAL   B 1 151 ? 38.202 -22.645 -7.839  1.00 16.21 ?  151  VAL   B HG21 1 
ATOM   6468 H  HG22 . VAL   B 1 151 ? 38.820 -23.450 -9.060  1.00 16.21 ?  151  VAL   B HG22 1 
ATOM   6469 H  HG23 . VAL   B 1 151 ? 39.288 -21.958 -8.771  1.00 16.21 ?  151  VAL   B HG23 1 
ATOM   6470 N  N    . TYR   B 1 152 ? 40.029 -22.784 -11.745 1.00 11.34 ?  152  TYR   B N    1 
ATOM   6471 C  CA   . TYR   B 1 152 ? 40.928 -23.767 -12.330 1.00 11.74 ?  152  TYR   B CA   1 
ATOM   6472 C  C    . TYR   B 1 152 ? 41.650 -24.455 -11.174 1.00 10.85 ?  152  TYR   B C    1 
ATOM   6473 O  O    . TYR   B 1 152 ? 42.499 -23.848 -10.513 1.00 11.61 ?  152  TYR   B O    1 
ATOM   6474 C  CB   . TYR   B 1 152 ? 41.898 -23.062 -13.283 1.00 12.36 ?  152  TYR   B CB   1 
ATOM   6475 C  CG   . TYR   B 1 152 ? 41.220 -22.593 -14.546 1.00 12.95 ?  152  TYR   B CG   1 
ATOM   6476 C  CD1  . TYR   B 1 152 ? 40.573 -21.362 -14.608 1.00 13.21 ?  152  TYR   B CD1  1 
ATOM   6477 C  CD2  . TYR   B 1 152 ? 41.207 -23.395 -15.673 1.00 14.43 ?  152  TYR   B CD2  1 
ATOM   6478 C  CE1  . TYR   B 1 152 ? 39.931 -20.947 -15.768 1.00 14.93 ?  152  TYR   B CE1  1 
ATOM   6479 C  CE2  . TYR   B 1 152 ? 40.572 -22.997 -16.827 1.00 15.15 ?  152  TYR   B CE2  1 
ATOM   6480 C  CZ   . TYR   B 1 152 ? 39.939 -21.770 -16.875 1.00 15.54 ?  152  TYR   B CZ   1 
ATOM   6481 O  OH   . TYR   B 1 152 ? 39.309 -21.383 -18.035 1.00 18.19 ?  152  TYR   B OH   1 
ATOM   6482 H  H    . TYR   B 1 152 ? 40.461 -22.111 -11.408 1.00 13.62 ?  152  TYR   B H    1 
ATOM   6483 H  HA   . TYR   B 1 152 ? 40.419 -24.425 -12.826 1.00 14.11 ?  152  TYR   B HA   1 
ATOM   6484 H  HB2  . TYR   B 1 152 ? 42.276 -22.288 -12.835 1.00 14.85 ?  152  TYR   B HB2  1 
ATOM   6485 H  HB3  . TYR   B 1 152 ? 42.607 -23.679 -13.529 1.00 14.85 ?  152  TYR   B HB3  1 
ATOM   6486 H  HD1  . TYR   B 1 152 ? 40.566 -20.809 -13.858 1.00 15.86 ?  152  TYR   B HD1  1 
ATOM   6487 H  HD2  . TYR   B 1 152 ? 41.627 -24.228 -15.645 1.00 17.33 ?  152  TYR   B HD2  1 
ATOM   6488 H  HE1  . TYR   B 1 152 ? 39.501 -20.122 -15.803 1.00 17.93 ?  152  TYR   B HE1  1 
ATOM   6489 H  HE2  . TYR   B 1 152 ? 40.576 -23.556 -17.573 1.00 18.19 ?  152  TYR   B HE2  1 
ATOM   6490 H  HH   . TYR   B 1 152 ? 39.393 -21.983 -18.620 1.00 21.84 ?  152  TYR   B HH   1 
ATOM   6491 N  N    . LEU   B 1 153 ? 41.281 -25.711 -10.912 1.00 11.30 ?  153  LEU   B N    1 
ATOM   6492 C  CA   . LEU   B 1 153 ? 41.786 -26.462 -9.772  1.00 11.11 ?  153  LEU   B CA   1 
ATOM   6493 C  C    . LEU   B 1 153 ? 43.013 -27.266 -10.175 1.00 11.69 ?  153  LEU   B C    1 
ATOM   6494 O  O    . LEU   B 1 153 ? 42.989 -27.986 -11.177 1.00 12.91 ?  153  LEU   B O    1 
ATOM   6495 C  CB   . LEU   B 1 153 ? 40.709 -27.422 -9.256  1.00 11.70 ?  153  LEU   B CB   1 
ATOM   6496 C  CG   . LEU   B 1 153 ? 39.452 -26.770 -8.676  1.00 12.08 ?  153  LEU   B CG   1 
ATOM   6497 C  CD1  . LEU   B 1 153 ? 38.363 -27.818 -8.512  1.00 13.03 ?  153  LEU   B CD1  1 
ATOM   6498 C  CD2  . LEU   B 1 153 ? 39.756 -26.097 -7.344  1.00 12.81 ?  153  LEU   B CD2  1 
ATOM   6499 H  H    . LEU   B 1 153 ? 40.718 -26.156 -11.395 1.00 13.58 ?  153  LEU   B H    1 
ATOM   6500 H  HA   . LEU   B 1 153 ? 42.023 -25.849 -9.064  1.00 13.34 ?  153  LEU   B HA   1 
ATOM   6501 H  HB2  . LEU   B 1 153 ? 40.427 -27.990 -9.987  1.00 14.06 ?  153  LEU   B HB2  1 
ATOM   6502 H  HB3  . LEU   B 1 153 ? 41.099 -27.966 -8.554  1.00 14.06 ?  153  LEU   B HB3  1 
ATOM   6503 H  HG   . LEU   B 1 153 ? 39.126 -26.089 -9.288  1.00 14.51 ?  153  LEU   B HG   1 
ATOM   6504 H  HD11 . LEU   B 1 153 ? 37.560 -27.386 -8.181  1.00 15.65 ?  153  LEU   B HD11 1 
ATOM   6505 H  HD12 . LEU   B 1 153 ? 38.192 -28.224 -9.372  1.00 15.65 ?  153  LEU   B HD12 1 
ATOM   6506 H  HD13 . LEU   B 1 153 ? 38.667 -28.484 -7.879  1.00 15.65 ?  153  LEU   B HD13 1 
ATOM   6507 H  HD21 . LEU   B 1 153 ? 38.939 -25.729 -6.978  1.00 15.39 ?  153  LEU   B HD21 1 
ATOM   6508 H  HD22 . LEU   B 1 153 ? 40.123 -26.760 -6.736  1.00 15.39 ?  153  LEU   B HD22 1 
ATOM   6509 H  HD23 . LEU   B 1 153 ? 40.404 -25.390 -7.490  1.00 15.39 ?  153  LEU   B HD23 1 
ATOM   6510 N  N    . ALA   B 1 154 ? 44.071 -27.160 -9.375  1.00 11.76 ?  154  ALA   B N    1 
ATOM   6511 C  CA   . ALA   B 1 154 ? 45.300 -27.919 -9.568  1.00 12.65 ?  154  ALA   B CA   1 
ATOM   6512 C  C    . ALA   B 1 154 ? 45.377 -28.995 -8.492  1.00 13.23 ?  154  ALA   B C    1 
ATOM   6513 O  O    . ALA   B 1 154 ? 45.304 -28.697 -7.292  1.00 14.83 ?  154  ALA   B O    1 
ATOM   6514 C  CB   . ALA   B 1 154 ? 46.521 -27.003 -9.513  1.00 13.92 ?  154  ALA   B CB   1 
ATOM   6515 H  H    . ALA   B 1 154 ? 44.095 -26.632 -8.690  1.00 14.13 ?  154  ALA   B H    1 
ATOM   6516 H  HA   . ALA   B 1 154 ? 45.277 -28.346 -10.434 1.00 15.19 ?  154  ALA   B HA   1 
ATOM   6517 H  HB1  . ALA   B 1 154 ? 47.321 -27.534 -9.645  1.00 16.72 ?  154  ALA   B HB1  1 
ATOM   6518 H  HB2  . ALA   B 1 154 ? 46.449 -26.334 -10.217 1.00 16.72 ?  154  ALA   B HB2  1 
ATOM   6519 H  HB3  . ALA   B 1 154 ? 46.554 -26.563 -8.648  1.00 16.72 ?  154  ALA   B HB3  1 
ATOM   6520 N  N    . VAL   B 1 155 ? 45.485 -30.245 -8.926  1.00 12.64 ?  155  VAL   B N    1 
ATOM   6521 C  CA   . VAL   B 1 155 ? 45.588 -31.393 -8.036  1.00 12.98 ?  155  VAL   B CA   1 
ATOM   6522 C  C    . VAL   B 1 155 ? 46.927 -32.065 -8.322  1.00 13.17 ?  155  VAL   B C    1 
ATOM   6523 O  O    . VAL   B 1 155 ? 47.160 -32.551 -9.436  1.00 14.73 ?  155  VAL   B O    1 
ATOM   6524 C  CB   . VAL   B 1 155 ? 44.425 -32.382 -8.232  1.00 14.22 ?  155  VAL   B CB   1 
ATOM   6525 C  CG1  . VAL   B 1 155 ? 44.602 -33.577 -7.320  1.00 14.33 ?  155  VAL   B CG1  1 
ATOM   6526 C  CG2  . VAL   B 1 155 ? 43.077 -31.678 -7.975  1.00 15.50 ?  155  VAL   B CG2  1 
ATOM   6527 H  H    . VAL   B 1 155 ? 45.511 -30.459 -9.761  1.00 15.18 ?  155  VAL   B H    1 
ATOM   6528 H  HA   . VAL   B 1 155 ? 45.579 -31.096 -7.115  1.00 15.59 ?  155  VAL   B HA   1 
ATOM   6529 H  HB   . VAL   B 1 155 ? 44.423 -32.694 -9.151  1.00 17.08 ?  155  VAL   B HB   1 
ATOM   6530 H  HG11 . VAL   B 1 155 ? 43.769 -34.075 -7.286  1.00 17.21 ?  155  VAL   B HG11 1 
ATOM   6531 H  HG12 . VAL   B 1 155 ? 45.307 -34.142 -7.671  1.00 17.21 ?  155  VAL   B HG12 1 
ATOM   6532 H  HG13 . VAL   B 1 155 ? 44.834 -33.266 -6.432  1.00 17.21 ?  155  VAL   B HG13 1 
ATOM   6533 H  HG21 . VAL   B 1 155 ? 42.358 -32.325 -8.068  1.00 18.61 ?  155  VAL   B HG21 1 
ATOM   6534 H  HG22 . VAL   B 1 155 ? 43.076 -31.312 -7.076  1.00 18.61 ?  155  VAL   B HG22 1 
ATOM   6535 H  HG23 . VAL   B 1 155 ? 42.960 -30.963 -8.622  1.00 18.61 ?  155  VAL   B HG23 1 
ATOM   6536 N  N    . PHE   B 1 156 ? 47.796 -32.106 -7.311  1.00 13.71 ?  156  PHE   B N    1 
ATOM   6537 C  CA   . PHE   B 1 156 ? 49.177 -32.557 -7.519  1.00 14.64 ?  156  PHE   B CA   1 
ATOM   6538 C  C    . PHE   B 1 156 ? 49.276 -34.055 -7.811  1.00 16.00 ?  156  PHE   B C    1 
ATOM   6539 O  O    . PHE   B 1 156 ? 49.998 -34.478 -8.725  1.00 17.61 ?  156  PHE   B O    1 
ATOM   6540 C  CB   . PHE   B 1 156 ? 50.003 -32.201 -6.289  1.00 14.34 ?  156  PHE   B CB   1 
ATOM   6541 C  CG   . PHE   B 1 156 ? 51.430 -32.664 -6.353  1.00 15.06 ?  156  PHE   B CG   1 
ATOM   6542 C  CD1  . PHE   B 1 156 ? 52.308 -32.127 -7.278  1.00 17.02 ?  156  PHE   B CD1  1 
ATOM   6543 C  CD2  . PHE   B 1 156 ? 51.896 -33.620 -5.473  1.00 15.26 ?  156  PHE   B CD2  1 
ATOM   6544 C  CE1  . PHE   B 1 156 ? 53.630 -32.540 -7.331  1.00 17.71 ?  156  PHE   B CE1  1 
ATOM   6545 C  CE2  . PHE   B 1 156 ? 53.216 -34.032 -5.520  1.00 16.77 ?  156  PHE   B CE2  1 
ATOM   6546 C  CZ   . PHE   B 1 156 ? 54.077 -33.491 -6.456  1.00 17.39 ?  156  PHE   B CZ   1 
ATOM   6547 H  H    . PHE   B 1 156 ? 47.611 -31.883 -6.497  1.00 16.46 ?  156  PHE   B H    1 
ATOM   6548 H  HA   . PHE   B 1 156 ? 49.543 -32.079 -8.273  1.00 17.58 ?  156  PHE   B HA   1 
ATOM   6549 H  HB2  . PHE   B 1 156 ? 50.013 -31.236 -6.188  1.00 17.23 ?  156  PHE   B HB2  1 
ATOM   6550 H  HB3  . PHE   B 1 156 ? 49.597 -32.607 -5.506  1.00 17.23 ?  156  PHE   B HB3  1 
ATOM   6551 H  HD1  . PHE   B 1 156 ? 52.003 -31.473 -7.872  1.00 20.44 ?  156  PHE   B HD1  1 
ATOM   6552 H  HD2  . PHE   B 1 156 ? 51.316 -33.991 -4.845  1.00 18.32 ?  156  PHE   B HD2  1 
ATOM   6553 H  HE1  . PHE   B 1 156 ? 54.209 -32.167 -7.960  1.00 21.27 ?  156  PHE   B HE1  1 
ATOM   6554 H  HE2  . PHE   B 1 156 ? 53.521 -34.686 -4.931  1.00 20.14 ?  156  PHE   B HE2  1 
ATOM   6555 H  HZ   . PHE   B 1 156 ? 54.964 -33.771 -6.491  1.00 20.88 ?  156  PHE   B HZ   1 
ATOM   6556 N  N    . ASP   B 1 157 ? 48.597 -34.875 -7.023  1.00 16.10 ?  157  ASP   B N    1 
ATOM   6557 C  CA   . ASP   B 1 157 ? 48.748 -36.322 -7.122  1.00 17.15 ?  157  ASP   B CA   1 
ATOM   6558 C  C    . ASP   B 1 157 ? 47.829 -36.874 -8.207  1.00 17.48 ?  157  ASP   B C    1 
ATOM   6559 O  O    . ASP   B 1 157 ? 46.604 -36.752 -8.106  1.00 16.84 ?  157  ASP   B O    1 
ATOM   6560 C  CB   . ASP   B 1 157 ? 48.403 -36.944 -5.774  1.00 18.60 ?  157  ASP   B CB   1 
ATOM   6561 C  CG   . ASP   B 1 157 ? 48.542 -38.454 -5.767  1.00 20.87 ?  157  ASP   B CG   1 
ATOM   6562 O  OD1  . ASP   B 1 157 ? 48.879 -39.056 -6.814  1.00 21.46 ?  157  ASP   B OD1  1 
ATOM   6563 O  OD2  . ASP   B 1 157 ? 48.326 -39.044 -4.691  1.00 23.02 -1 157  ASP   B OD2  1 
ATOM   6564 H  H    . ASP   B 1 157 ? 48.043 -34.624 -6.424  1.00 19.34 ?  157  ASP   B H    1 
ATOM   6565 H  HA   . ASP   B 1 157 ? 49.664 -36.550 -7.347  1.00 20.59 ?  157  ASP   B HA   1 
ATOM   6566 H  HB2  . ASP   B 1 157 ? 48.986 -36.568 -5.099  1.00 22.34 ?  157  ASP   B HB2  1 
ATOM   6567 H  HB3  . ASP   B 1 157 ? 47.477 -36.731 -5.562  1.00 22.34 ?  157  ASP   B HB3  1 
ATOM   6568 N  N    A LYS   B 1 158 ? 48.419 -37.530 -9.212  0.62 18.26 ?  158  LYS   B N    1 
ATOM   6569 N  N    B LYS   B 1 158 ? 48.425 -37.465 -9.250  0.38 18.12 ?  158  LYS   B N    1 
ATOM   6570 C  CA   A LYS   B 1 158 ? 47.640 -38.150 -10.283 0.62 19.47 ?  158  LYS   B CA   1 
ATOM   6571 C  CA   B LYS   B 1 158 ? 47.650 -38.026 -10.356 0.38 19.18 ?  158  LYS   B CA   1 
ATOM   6572 C  C    A LYS   B 1 158 ? 46.579 -39.104 -9.738  0.62 19.36 ?  158  LYS   B C    1 
ATOM   6573 C  C    B LYS   B 1 158 ? 46.595 -39.010 -9.868  0.38 19.07 ?  158  LYS   B C    1 
ATOM   6574 O  O    A LYS   B 1 158 ? 45.463 -39.175 -10.268 0.62 19.15 ?  158  LYS   B O    1 
ATOM   6575 O  O    B LYS   B 1 158 ? 45.511 -39.104 -10.456 0.38 19.04 ?  158  LYS   B O    1 
ATOM   6576 C  CB   A LYS   B 1 158 ? 48.587 -38.883 -11.241 0.62 21.05 ?  158  LYS   B CB   1 
ATOM   6577 C  CB   B LYS   B 1 158 ? 48.602 -38.703 -11.352 0.38 20.49 ?  158  LYS   B CB   1 
ATOM   6578 C  CG   A LYS   B 1 158 ? 47.909 -39.776 -12.273 0.62 22.90 ?  158  LYS   B CG   1 
ATOM   6579 C  CG   B LYS   B 1 158 ? 47.934 -39.600 -12.393 0.38 21.91 ?  158  LYS   B CG   1 
ATOM   6580 C  CD   A LYS   B 1 158 ? 47.043 -38.987 -13.233 0.62 24.89 ?  158  LYS   B CD   1 
ATOM   6581 C  CD   B LYS   B 1 158 ? 47.029 -38.816 -13.327 0.38 23.54 ?  158  LYS   B CD   1 
ATOM   6582 C  CE   A LYS   B 1 158 ? 46.452 -39.894 -14.299 0.62 26.27 ?  158  LYS   B CE   1 
ATOM   6583 C  CE   B LYS   B 1 158 ? 46.447 -39.716 -14.408 0.38 24.71 ?  158  LYS   B CE   1 
ATOM   6584 N  NZ   A LYS   B 1 158 ? 45.387 -39.212 -15.086 0.62 26.33 ?  158  LYS   B NZ   1 
ATOM   6585 N  NZ   B LYS   B 1 158 ? 45.400 -39.022 -15.210 0.38 25.02 ?  158  LYS   B NZ   1 
ATOM   6586 H  H    A LYS   B 1 158 ? 49.270 -37.633 -9.292  0.62 21.93 ?  158  LYS   B H    1 
ATOM   6587 H  H    B LYS   B 1 158 ? 49.275 -37.556 -9.340  0.38 21.76 ?  158  LYS   B H    1 
ATOM   6588 H  HA   A LYS   B 1 158 ? 47.189 -37.459 -10.789 0.62 23.38 ?  158  LYS   B HA   1 
ATOM   6589 H  HA   B LYS   B 1 158 ? 47.197 -37.309 -10.825 0.38 23.03 ?  158  LYS   B HA   1 
ATOM   6590 H  HB2  A LYS   B 1 158 ? 49.106 -38.222 -11.730 0.62 25.28 ?  158  LYS   B HB2  1 
ATOM   6591 H  HB2  B LYS   B 1 158 ? 49.086 -38.014 -11.838 0.38 24.60 ?  158  LYS   B HB2  1 
ATOM   6592 H  HB3  A LYS   B 1 158 ? 49.186 -39.442 -10.722 0.62 25.28 ?  158  LYS   B HB3  1 
ATOM   6593 H  HB3  B LYS   B 1 158 ? 49.231 -39.251 -10.859 0.38 24.60 ?  158  LYS   B HB3  1 
ATOM   6594 H  HG2  A LYS   B 1 158 ? 48.592 -40.228 -12.794 0.62 27.49 ?  158  LYS   B HG2  1 
ATOM   6595 H  HG2  B LYS   B 1 158 ? 48.625 -40.018 -12.932 0.38 26.30 ?  158  LYS   B HG2  1 
ATOM   6596 H  HG3  A LYS   B 1 158 ? 47.352 -40.435 -11.827 0.62 27.49 ?  158  LYS   B HG3  1 
ATOM   6597 H  HG3  B LYS   B 1 158 ? 47.406 -40.285 -11.953 0.38 26.30 ?  158  LYS   B HG3  1 
ATOM   6598 H  HD2  A LYS   B 1 158 ? 46.314 -38.572 -12.745 0.62 29.88 ?  158  LYS   B HD2  1 
ATOM   6599 H  HD2  B LYS   B 1 158 ? 46.296 -38.434 -12.821 0.38 28.26 ?  158  LYS   B HD2  1 
ATOM   6600 H  HD3  A LYS   B 1 158 ? 47.582 -38.310 -13.673 0.62 29.88 ?  158  LYS   B HD3  1 
ATOM   6601 H  HD3  B LYS   B 1 158 ? 47.542 -38.115 -13.759 0.38 28.26 ?  158  LYS   B HD3  1 
ATOM   6602 H  HE2  A LYS   B 1 158 ? 47.152 -40.164 -14.912 0.62 31.54 ?  158  LYS   B HE2  1 
ATOM   6603 H  HE2  B LYS   B 1 158 ? 47.155 -39.993 -15.010 0.38 29.67 ?  158  LYS   B HE2  1 
ATOM   6604 H  HE3  A LYS   B 1 158 ? 46.061 -40.674 -13.875 0.62 31.54 ?  158  LYS   B HE3  1 
ATOM   6605 H  HE3  B LYS   B 1 158 ? 46.041 -40.493 -13.991 0.38 29.67 ?  158  LYS   B HE3  1 
ATOM   6606 H  HZ1  A LYS   B 1 158 ? 45.059 -39.766 -15.700 0.62 31.61 ?  158  LYS   B HZ1  1 
ATOM   6607 H  HZ1  B LYS   B 1 158 ? 45.078 -39.572 -15.832 0.38 30.04 ?  158  LYS   B HZ1  1 
ATOM   6608 H  HZ2  A LYS   B 1 158 ? 44.726 -38.955 -14.547 0.62 31.61 ?  158  LYS   B HZ2  1 
ATOM   6609 H  HZ2  B LYS   B 1 158 ? 44.733 -38.763 -14.680 0.38 30.04 ?  158  LYS   B HZ2  1 
ATOM   6610 H  HZ3  A LYS   B 1 158 ? 45.722 -38.494 -15.493 0.62 31.61 ?  158  LYS   B HZ3  1 
ATOM   6611 H  HZ3  B LYS   B 1 158 ? 45.748 -38.306 -15.609 0.38 30.04 ?  158  LYS   B HZ3  1 
ATOM   6612 N  N    A ASN   B 1 159 ? 46.910 -39.868 -8.695  0.62 19.58 ?  159  ASN   B N    1 
ATOM   6613 N  N    B ASN   B 1 159 ? 46.891 -39.758 -8.805  0.38 19.20 ?  159  ASN   B N    1 
ATOM   6614 C  CA   A ASN   B 1 159 ? 45.951 -40.840 -8.175  0.62 20.18 ?  159  ASN   B CA   1 
ATOM   6615 C  CA   B ASN   B 1 159 ? 45.938 -40.748 -8.313  0.38 19.45 ?  159  ASN   B CA   1 
ATOM   6616 C  C    A ASN   B 1 159 ? 44.760 -40.158 -7.506  0.62 19.15 ?  159  ASN   B C    1 
ATOM   6617 C  C    B ASN   B 1 159 ? 44.744 -40.082 -7.631  0.38 18.80 ?  159  ASN   B C    1 
ATOM   6618 O  O    A ASN   B 1 159 ? 43.636 -40.673 -7.570  0.62 19.45 ?  159  ASN   B O    1 
ATOM   6619 O  O    B ASN   B 1 159 ? 43.602 -40.533 -7.793  0.38 18.78 ?  159  ASN   B O    1 
ATOM   6620 C  CB   A ASN   B 1 159 ? 46.649 -41.808 -7.222  0.62 22.04 ?  159  ASN   B CB   1 
ATOM   6621 C  CB   B ASN   B 1 159 ? 46.644 -41.739 -7.387  0.38 20.26 ?  159  ASN   B CB   1 
ATOM   6622 C  CG   A ASN   B 1 159 ? 47.676 -42.672 -7.924  0.62 24.01 ?  159  ASN   B CG   1 
ATOM   6623 C  CG   B ASN   B 1 159 ? 47.666 -42.591 -8.120  0.38 21.29 ?  159  ASN   B CG   1 
ATOM   6624 O  OD1  A ASN   B 1 159 ? 47.428 -43.190 -9.017  0.62 24.87 ?  159  ASN   B OD1  1 
ATOM   6625 O  OD1  B ASN   B 1 159 ? 47.433 -43.021 -9.253  0.38 21.68 ?  159  ASN   B OD1  1 
ATOM   6626 N  ND2  A ASN   B 1 159 ? 48.840 -42.832 -7.302  0.62 24.79 ?  159  ASN   B ND2  1 
ATOM   6627 N  ND2  B ASN   B 1 159 ? 48.806 -42.838 -7.479  0.38 21.83 ?  159  ASN   B ND2  1 
ATOM   6628 H  H    A ASN   B 1 159 ? 47.659 -39.836 -8.280  0.62 23.51 ?  159  ASN   B H    1 
ATOM   6629 H  H    B ASN   B 1 159 ? 47.626 -39.712 -8.366  0.38 23.05 ?  159  ASN   B H    1 
ATOM   6630 H  HA   A ASN   B 1 159 ? 45.607 -41.358 -8.920  0.62 24.24 ?  159  ASN   B HA   1 
ATOM   6631 H  HA   B ASN   B 1 159 ? 45.603 -41.252 -9.072  0.38 23.36 ?  159  ASN   B HA   1 
ATOM   6632 H  HB2  A ASN   B 1 159 ? 47.101 -41.303 -6.531  0.62 26.46 ?  159  ASN   B HB2  1 
ATOM   6633 H  HB2  B ASN   B 1 159 ? 47.109 -41.254 -6.691  0.38 24.33 ?  159  ASN   B HB2  1 
ATOM   6634 H  HB3  A ASN   B 1 159 ? 45.984 -42.395 -6.829  0.62 26.46 ?  159  ASN   B HB3  1 
ATOM   6635 H  HB3  B ASN   B 1 159 ? 45.985 -42.335 -6.998  0.38 24.33 ?  159  ASN   B HB3  1 
ATOM   6636 H  HD21 A ASN   B 1 159 ? 49.456 -43.317 -7.659  0.62 29.77 ?  159  ASN   B HD21 1 
ATOM   6637 H  HD21 B ASN   B 1 159 ? 49.418 -43.320 -7.851  0.38 26.21 ?  159  ASN   B HD21 1 
ATOM   6638 H  HD22 A ASN   B 1 159 ? 48.975 -42.463 -6.538  0.62 29.77 ?  159  ASN   B HD22 1 
ATOM   6639 H  HD22 B ASN   B 1 159 ? 48.933 -42.524 -6.689  0.38 26.21 ?  159  ASN   B HD22 1 
ATOM   6640 N  N    . LEU   B 1 160 ? 44.975 -39.002 -6.874  1.00 18.40 ?  160  LEU   B N    1 
ATOM   6641 C  CA   . LEU   B 1 160 ? 43.850 -38.264 -6.308  1.00 17.16 ?  160  LEU   B CA   1 
ATOM   6642 C  C    . LEU   B 1 160 ? 43.048 -37.596 -7.413  1.00 16.72 ?  160  LEU   B C    1 
ATOM   6643 O  O    . LEU   B 1 160 ? 41.810 -37.601 -7.380  1.00 16.49 ?  160  LEU   B O    1 
ATOM   6644 C  CB   . LEU   B 1 160 ? 44.323 -37.235 -5.284  1.00 16.73 ?  160  LEU   B CB   1 
ATOM   6645 C  CG   . LEU   B 1 160 ? 43.192 -36.347 -4.742  1.00 16.59 ?  160  LEU   B CG   1 
ATOM   6646 C  CD1  . LEU   B 1 160 ? 42.087 -37.187 -4.105  1.00 17.27 ?  160  LEU   B CD1  1 
ATOM   6647 C  CD2  . LEU   B 1 160 ? 43.727 -35.322 -3.747  1.00 16.80 ?  160  LEU   B CD2  1 
ATOM   6648 H  H    A LEU   B 1 160 ? 45.747 -38.633 -6.768  0.62 22.09 ?  160  LEU   B H    1 
ATOM   6649 H  H    B LEU   B 1 160 ? 45.754 -38.684 -6.688  0.38 22.09 ?  160  LEU   B H    1 
ATOM   6650 H  HA   . LEU   B 1 160 ? 43.269 -38.892 -5.857  1.00 20.60 ?  160  LEU   B HA   1 
ATOM   6651 H  HB2  . LEU   B 1 160 ? 44.723 -37.704 -4.533  1.00 20.10 ?  160  LEU   B HB2  1 
ATOM   6652 H  HB3  . LEU   B 1 160 ? 44.985 -36.659 -5.700  1.00 20.10 ?  160  LEU   B HB3  1 
ATOM   6653 H  HG   . LEU   B 1 160 ? 42.797 -35.857 -5.481  1.00 19.92 ?  160  LEU   B HG   1 
ATOM   6654 H  HD11 . LEU   B 1 160 ? 41.457 -36.596 -3.669  1.00 20.74 ?  160  LEU   B HD11 1 
ATOM   6655 H  HD12 . LEU   B 1 160 ? 41.636 -37.701 -4.794  1.00 20.74 ?  160  LEU   B HD12 1 
ATOM   6656 H  HD13 . LEU   B 1 160 ? 42.485 -37.787 -3.453  1.00 20.74 ?  160  LEU   B HD13 1 
ATOM   6657 H  HD21 . LEU   B 1 160 ? 42.990 -34.765 -3.447  1.00 20.18 ?  160  LEU   B HD21 1 
ATOM   6658 H  HD22 . LEU   B 1 160 ? 44.119 -35.787 -2.995  1.00 20.18 ?  160  LEU   B HD22 1 
ATOM   6659 H  HD23 . LEU   B 1 160 ? 44.395 -34.774 -4.188  1.00 20.18 ?  160  LEU   B HD23 1 
ATOM   6660 N  N    A TYR   B 1 161 ? 43.738 -37.031 -8.406  0.62 16.53 ?  161  TYR   B N    1 
ATOM   6661 N  N    B TYR   B 1 161 ? 43.733 -37.033 -8.413  0.38 16.60 ?  161  TYR   B N    1 
ATOM   6662 C  CA   A TYR   B 1 161 ? 43.065 -36.464 -9.567  0.62 16.31 ?  161  TYR   B CA   1 
ATOM   6663 C  CA   B TYR   B 1 161 ? 43.044 -36.457 -9.565  0.38 16.46 ?  161  TYR   B CA   1 
ATOM   6664 C  C    A TYR   B 1 161 ? 42.115 -37.482 -10.183 0.62 16.25 ?  161  TYR   B C    1 
ATOM   6665 C  C    B TYR   B 1 161 ? 42.112 -37.478 -10.202 0.38 16.36 ?  161  TYR   B C    1 
ATOM   6666 O  O    A TYR   B 1 161 ? 40.941 -37.187 -10.433 0.62 16.11 ?  161  TYR   B O    1 
ATOM   6667 O  O    B TYR   B 1 161 ? 40.948 -37.181 -10.494 0.38 16.24 ?  161  TYR   B O    1 
ATOM   6668 C  CB   A TYR   B 1 161 ? 44.110 -36.007 -10.591 0.62 16.71 ?  161  TYR   B CB   1 
ATOM   6669 C  CB   B TYR   B 1 161 ? 44.068 -35.949 -10.589 0.38 16.76 ?  161  TYR   B CB   1 
ATOM   6670 C  CG   A TYR   B 1 161 ? 43.530 -35.527 -11.901 0.62 17.22 ?  161  TYR   B CG   1 
ATOM   6671 C  CG   B TYR   B 1 161 ? 43.464 -35.481 -11.900 0.38 17.18 ?  161  TYR   B CG   1 
ATOM   6672 C  CD1  A TYR   B 1 161 ? 43.143 -34.204 -12.062 0.62 17.00 ?  161  TYR   B CD1  1 
ATOM   6673 C  CD1  B TYR   B 1 161 ? 43.054 -34.163 -12.066 0.38 17.07 ?  161  TYR   B CD1  1 
ATOM   6674 C  CD2  A TYR   B 1 161 ? 43.360 -36.396 -12.974 0.62 18.09 ?  161  TYR   B CD2  1 
ATOM   6675 C  CD2  B TYR   B 1 161 ? 43.304 -36.355 -12.971 0.38 17.66 ?  161  TYR   B CD2  1 
ATOM   6676 C  CE1  A TYR   B 1 161 ? 42.611 -33.757 -13.250 0.62 18.20 ?  161  TYR   B CE1  1 
ATOM   6677 C  CE1  B TYR   B 1 161 ? 42.503 -33.729 -13.256 0.38 17.77 ?  161  TYR   B CE1  1 
ATOM   6678 C  CE2  A TYR   B 1 161 ? 42.825 -35.959 -14.166 0.62 19.22 ?  161  TYR   B CE2  1 
ATOM   6679 C  CE2  B TYR   B 1 161 ? 42.751 -35.929 -14.165 0.38 18.35 ?  161  TYR   B CE2  1 
ATOM   6680 C  CZ   A TYR   B 1 161 ? 42.455 -34.639 -14.300 0.62 19.27 ?  161  TYR   B CZ   1 
ATOM   6681 C  CZ   B TYR   B 1 161 ? 42.356 -34.615 -14.303 0.38 18.41 ?  161  TYR   B CZ   1 
ATOM   6682 O  OH   A TYR   B 1 161 ? 41.921 -34.194 -15.484 0.62 21.18 ?  161  TYR   B OH   1 
ATOM   6683 O  OH   B TYR   B 1 161 ? 41.803 -34.183 -15.486 0.38 19.63 ?  161  TYR   B OH   1 
ATOM   6684 H  H    A TYR   B 1 161 ? 44.593 -36.970 -8.432  0.62 19.85 ?  161  TYR   B H    1 
ATOM   6685 H  H    B TYR   B 1 161 ? 44.588 -36.976 -8.449  0.38 19.93 ?  161  TYR   B H    1 
ATOM   6686 H  HA   A TYR   B 1 161 ? 42.547 -35.692 -9.295  0.62 19.59 ?  161  TYR   B HA   1 
ATOM   6687 H  HA   B TYR   B 1 161 ? 42.509 -35.703 -9.276  0.38 19.77 ?  161  TYR   B HA   1 
ATOM   6688 H  HB2  A TYR   B 1 161 ? 44.619 -35.275 -10.210 0.62 20.06 ?  161  TYR   B HB2  1 
ATOM   6689 H  HB2  B TYR   B 1 161 ? 44.546 -35.198 -10.203 0.38 20.13 ?  161  TYR   B HB2  1 
ATOM   6690 H  HB3  A TYR   B 1 161 ? 44.700 -36.750 -10.788 0.62 20.06 ?  161  TYR   B HB3  1 
ATOM   6691 H  HB3  B TYR   B 1 161 ? 44.689 -36.664 -10.792 0.38 20.13 ?  161  TYR   B HB3  1 
ATOM   6692 H  HD1  A TYR   B 1 161 ? 43.251 -33.604 -11.355 0.62 20.42 ?  161  TYR   B HD1  1 
ATOM   6693 H  HD1  B TYR   B 1 161 ? 43.153 -33.560 -11.364 0.38 20.50 ?  161  TYR   B HD1  1 
ATOM   6694 H  HD2  A TYR   B 1 161 ? 43.607 -37.287 -12.887 0.62 21.73 ?  161  TYR   B HD2  1 
ATOM   6695 H  HD2  B TYR   B 1 161 ? 43.568 -37.241 -12.884 0.38 21.21 ?  161  TYR   B HD2  1 
ATOM   6696 H  HE1  A TYR   B 1 161 ? 42.360 -32.862 -13.341 0.62 21.85 ?  161  TYR   B HE1  1 
ATOM   6697 H  HE1  B TYR   B 1 161 ? 42.235 -32.841 -13.351 0.38 21.34 ?  161  TYR   B HE1  1 
ATOM   6698 H  HE2  A TYR   B 1 161 ? 42.714 -36.545 -14.877 0.62 23.08 ?  161  TYR   B HE2  1 
ATOM   6699 H  HE2  B TYR   B 1 161 ? 42.649 -36.522 -14.874 0.38 22.04 ?  161  TYR   B HE2  1 
ATOM   6700 H  HH   A TYR   B 1 161 ? 41.885 -34.826 -16.035 0.62 25.44 ?  161  TYR   B HH   1 
ATOM   6701 H  HH   B TYR   B 1 161 ? 41.773 -34.816 -16.037 0.38 23.57 ?  161  TYR   B HH   1 
ATOM   6702 N  N    . ASP   B 1 162 ? 42.610 -38.697 -10.419 1.00 16.55 ?  162  ASP   B N    1 
ATOM   6703 C  CA   . ASP   B 1 162 ? 41.777 -39.732 -11.021 1.00 17.30 ?  162  ASP   B CA   1 
ATOM   6704 C  C    . ASP   B 1 162 ? 40.576 -40.066 -10.142 1.00 16.97 ?  162  ASP   B C    1 
ATOM   6705 O  O    . ASP   B 1 162 ? 39.471 -40.278 -10.651 1.00 17.35 ?  162  ASP   B O    1 
ATOM   6706 C  CB   . ASP   B 1 162 ? 42.603 -40.995 -11.283 1.00 19.05 ?  162  ASP   B CB   1 
ATOM   6707 C  CG   . ASP   B 1 162 ? 43.601 -40.833 -12.416 1.00 20.40 ?  162  ASP   B CG   1 
ATOM   6708 O  OD1  . ASP   B 1 162 ? 43.470 -39.890 -13.219 1.00 20.71 ?  162  ASP   B OD1  1 
ATOM   6709 O  OD2  . ASP   B 1 162 ? 44.506 -41.692 -12.523 1.00 21.91 -1 162  ASP   B OD2  1 
ATOM   6710 H  H    A ASP   B 1 162 ? 43.412 -38.944 -10.241 0.62 19.88 ?  162  ASP   B H    1 
ATOM   6711 H  H    B ASP   B 1 162 ? 43.409 -38.946 -10.228 0.38 19.88 ?  162  ASP   B H    1 
ATOM   6712 H  HA   . ASP   B 1 162 ? 41.439 -39.414 -11.870 1.00 20.77 ?  162  ASP   B HA   1 
ATOM   6713 H  HB2  . ASP   B 1 162 ? 43.103 -41.220 -10.485 1.00 22.87 ?  162  ASP   B HB2  1 
ATOM   6714 H  HB3  . ASP   B 1 162 ? 42.006 -41.722 -11.519 1.00 22.87 ?  162  ASP   B HB3  1 
ATOM   6715 N  N    . LYS   B 1 163 ? 40.773 -40.145 -8.824  1.00 16.36 ?  163  LYS   B N    1 
ATOM   6716 C  CA   . LYS   B 1 163 ? 39.652 -40.418 -7.929  1.00 17.14 ?  163  LYS   B CA   1 
ATOM   6717 C  C    . LYS   B 1 163 ? 38.609 -39.308 -7.988  1.00 15.88 ?  163  LYS   B C    1 
ATOM   6718 O  O    . LYS   B 1 163 ? 37.399 -39.575 -7.994  1.00 17.00 ?  163  LYS   B O    1 
ATOM   6719 C  CB   . LYS   B 1 163 ? 40.145 -40.606 -6.496  1.00 19.87 ?  163  LYS   B CB   1 
ATOM   6720 C  CG   . LYS   B 1 163 ? 39.055 -41.071 -5.553  1.00 25.52 ?  163  LYS   B CG   1 
ATOM   6721 C  CD   . LYS   B 1 163 ? 39.545 -41.238 -4.127  1.00 30.33 ?  163  LYS   B CD   1 
ATOM   6722 C  CE   . LYS   B 1 163 ? 38.464 -41.882 -3.269  1.00 33.70 ?  163  LYS   B CE   1 
ATOM   6723 N  NZ   . LYS   B 1 163 ? 38.672 -41.653 -1.813  1.00 36.03 ?  163  LYS   B NZ   1 
ATOM   6724 H  H    . LYS   B 1 163 ? 41.531 -40.039 -8.432  1.00 19.64 ?  163  LYS   B H    1 
ATOM   6725 H  HA   . LYS   B 1 163 ? 39.223 -41.241 -8.207  1.00 20.59 ?  163  LYS   B HA   1 
ATOM   6726 H  HB2  . LYS   B 1 163 ? 40.850 -41.276 -6.491  1.00 23.86 ?  163  LYS   B HB2  1 
ATOM   6727 H  HB3  . LYS   B 1 163 ? 40.488 -39.764 -6.165  1.00 23.86 ?  163  LYS   B HB3  1 
ATOM   6728 H  HG2  . LYS   B 1 163 ? 38.340 -40.419 -5.548  1.00 30.63 ?  163  LYS   B HG2  1 
ATOM   6729 H  HG3  . LYS   B 1 163 ? 38.720 -41.931 -5.858  1.00 30.63 ?  163  LYS   B HG3  1 
ATOM   6730 H  HD2  . LYS   B 1 163 ? 40.327 -41.814 -4.118  1.00 36.41 ?  163  LYS   B HD2  1 
ATOM   6731 H  HD3  . LYS   B 1 163 ? 39.759 -40.369 -3.755  1.00 36.41 ?  163  LYS   B HD3  1 
ATOM   6732 H  HE2  . LYS   B 1 163 ? 37.599 -41.519 -3.515  1.00 40.45 ?  163  LYS   B HE2  1 
ATOM   6733 H  HE3  . LYS   B 1 163 ? 38.471 -42.839 -3.424  1.00 40.45 ?  163  LYS   B HE3  1 
ATOM   6734 H  HZ1  . LYS   B 1 163 ? 38.019 -42.042 -1.349  1.00 43.25 ?  163  LYS   B HZ1  1 
ATOM   6735 H  HZ2  . LYS   B 1 163 ? 39.452 -41.997 -1.561  1.00 43.25 ?  163  LYS   B HZ2  1 
ATOM   6736 H  HZ3  . LYS   B 1 163 ? 38.669 -40.780 -1.640  1.00 43.25 ?  163  LYS   B HZ3  1 
ATOM   6737 N  N    . LEU   B 1 164 ? 39.066 -38.055 -8.028  1.00 14.45 ?  164  LEU   B N    1 
ATOM   6738 C  CA   . LEU   B 1 164 ? 38.162 -36.913 -8.086  1.00 14.23 ?  164  LEU   B CA   1 
ATOM   6739 C  C    . LEU   B 1 164 ? 37.369 -36.898 -9.388  1.00 14.52 ?  164  LEU   B C    1 
ATOM   6740 O  O    . LEU   B 1 164 ? 36.148 -36.700 -9.381  1.00 15.75 ?  164  LEU   B O    1 
ATOM   6741 C  CB   . LEU   B 1 164 ? 38.965 -35.620 -7.929  1.00 13.88 ?  164  LEU   B CB   1 
ATOM   6742 C  CG   . LEU   B 1 164 ? 39.512 -35.358 -6.529  1.00 14.72 ?  164  LEU   B CG   1 
ATOM   6743 C  CD1  . LEU   B 1 164 ? 40.590 -34.289 -6.577  1.00 14.78 ?  164  LEU   B CD1  1 
ATOM   6744 C  CD2  . LEU   B 1 164 ? 38.406 -34.939 -5.584  1.00 16.64 ?  164  LEU   B CD2  1 
ATOM   6745 H  H    . LEU   B 1 164 ? 39.904 -37.841 -8.027  1.00 17.36 ?  164  LEU   B H    1 
ATOM   6746 H  HA   . LEU   B 1 164 ? 37.536 -36.969 -7.354  1.00 17.09 ?  164  LEU   B HA   1 
ATOM   6747 H  HB2  . LEU   B 1 164 ? 39.725 -35.654 -8.537  1.00 16.68 ?  164  LEU   B HB2  1 
ATOM   6748 H  HB3  . LEU   B 1 164 ? 38.397 -34.874 -8.166  1.00 16.68 ?  164  LEU   B HB3  1 
ATOM   6749 H  HG   . LEU   B 1 164 ? 39.915 -36.169 -6.187  1.00 17.69 ?  164  LEU   B HG   1 
ATOM   6750 H  HD11 . LEU   B 1 164 ? 40.924 -34.131 -5.677  1.00 17.75 ?  164  LEU   B HD11 1 
ATOM   6751 H  HD12 . LEU   B 1 164 ? 41.321 -34.595 -7.144  1.00 17.75 ?  164  LEU   B HD12 1 
ATOM   6752 H  HD13 . LEU   B 1 164 ? 40.218 -33.470 -6.938  1.00 17.75 ?  164  LEU   B HD13 1 
ATOM   6753 H  HD21 . LEU   B 1 164 ? 38.793 -34.711 -4.725  1.00 19.98 ?  164  LEU   B HD21 1 
ATOM   6754 H  HD22 . LEU   B 1 164 ? 37.947 -34.169 -5.955  1.00 19.98 ?  164  LEU   B HD22 1 
ATOM   6755 H  HD23 . LEU   B 1 164 ? 37.785 -35.677 -5.482  1.00 19.98 ?  164  LEU   B HD23 1 
ATOM   6756 N  N    . VAL   B 1 165 ? 38.049 -37.075 -10.521 1.00 15.94 ?  165  VAL   B N    1 
ATOM   6757 C  CA   . VAL   B 1 165 ? 37.385 -36.998 -11.818 1.00 17.40 ?  165  VAL   B CA   1 
ATOM   6758 C  C    . VAL   B 1 165 ? 36.465 -38.195 -12.012 1.00 19.38 ?  165  VAL   B C    1 
ATOM   6759 O  O    . VAL   B 1 165 ? 35.298 -38.055 -12.405 1.00 20.48 ?  165  VAL   B O    1 
ATOM   6760 C  CB   . VAL   B 1 165 ? 38.429 -36.911 -12.946 1.00 18.34 ?  165  VAL   B CB   1 
ATOM   6761 C  CG1  . VAL   B 1 165 ? 37.767 -37.037 -14.297 1.00 19.64 ?  165  VAL   B CG1  1 
ATOM   6762 C  CG2  . VAL   B 1 165 ? 39.212 -35.621 -12.849 1.00 18.43 ?  165  VAL   B CG2  1 
ATOM   6763 H  H    . VAL   B 1 165 ? 38.893 -37.237 -10.566 1.00 19.15 ?  165  VAL   B H    1 
ATOM   6764 H  HA   . VAL   B 1 165 ? 36.843 -36.198 -11.854 1.00 20.89 ?  165  VAL   B HA   1 
ATOM   6765 H  HB   . VAL   B 1 165 ? 39.060 -37.643 -12.851 1.00 22.03 ?  165  VAL   B HB   1 
ATOM   6766 H  HG11 . VAL   B 1 165 ? 38.375 -36.718 -14.978 1.00 23.58 ?  165  VAL   B HG11 1 
ATOM   6767 H  HG12 . VAL   B 1 165 ? 37.560 -37.974 -14.456 1.00 23.58 ?  165  VAL   B HG12 1 
ATOM   6768 H  HG13 . VAL   B 1 165 ? 36.954 -36.513 -14.300 1.00 23.58 ?  165  VAL   B HG13 1 
ATOM   6769 H  HG21 . VAL   B 1 165 ? 39.837 -35.573 -13.590 1.00 22.13 ?  165  VAL   B HG21 1 
ATOM   6770 H  HG22 . VAL   B 1 165 ? 38.594 -34.873 -12.890 1.00 22.13 ?  165  VAL   B HG22 1 
ATOM   6771 H  HG23 . VAL   B 1 165 ? 39.695 -35.603 -12.008 1.00 22.13 ?  165  VAL   B HG23 1 
ATOM   6772 N  N    . SER   B 1 166 ? 36.986 -39.396 -11.744 1.00 20.40 ?  166  SER   B N    1 
ATOM   6773 C  CA   . SER   B 1 166 ? 36.234 -40.612 -12.027 1.00 21.97 ?  166  SER   B CA   1 
ATOM   6774 C  C    . SER   B 1 166 ? 34.973 -40.701 -11.182 1.00 21.88 ?  166  SER   B C    1 
ATOM   6775 O  O    . SER   B 1 166 ? 34.000 -41.324 -11.606 1.00 23.55 ?  166  SER   B O    1 
ATOM   6776 C  CB   . SER   B 1 166 ? 37.107 -41.864 -11.841 1.00 23.44 ?  166  SER   B CB   1 
ATOM   6777 O  OG   . SER   B 1 166 ? 37.450 -42.078 -10.482 1.00 23.65 ?  166  SER   B OG   1 
ATOM   6778 H  H    . SER   B 1 166 ? 37.771 -39.532 -11.417 1.00 24.50 ?  166  SER   B H    1 
ATOM   6779 H  HA   . SER   B 1 166 ? 35.961 -40.598 -12.958 1.00 26.37 ?  166  SER   B HA   1 
ATOM   6780 H  HB2  . SER   B 1 166 ? 36.620 -42.639 -12.164 1.00 28.14 ?  166  SER   B HB2  1 
ATOM   6781 H  HB3  . SER   B 1 166 ? 37.926 -41.756 -12.355 1.00 28.14 ?  166  SER   B HB3  1 
ATOM   6782 H  HG   . SER   B 1 166 ? 37.873 -41.408 -10.191 1.00 28.40 ?  166  SER   B HG   1 
ATOM   6783 N  N    . SER   B 1 167 ? 34.955 -40.086 -10.001 1.00 20.32 ?  167  SER   B N    1 
ATOM   6784 C  CA   . SER   B 1 167 ? 33.805 -40.156 -9.107  1.00 19.91 ?  167  SER   B CA   1 
ATOM   6785 C  C    . SER   B 1 167 ? 32.885 -38.938 -9.191  1.00 19.28 ?  167  SER   B C    1 
ATOM   6786 O  O    . SER   B 1 167 ? 31.811 -38.948 -8.581  1.00 19.45 ?  167  SER   B O    1 
ATOM   6787 C  CB   . SER   B 1 167 ? 34.268 -40.351 -7.655  1.00 19.57 ?  167  SER   B CB   1 
ATOM   6788 O  OG   . SER   B 1 167 ? 34.927 -39.187 -7.169  1.00 19.20 ?  167  SER   B OG   1 
ATOM   6789 H  H    . SER   B 1 167 ? 35.605 -39.627 -9.695  1.00 24.40 ?  167  SER   B H    1 
ATOM   6790 H  HA   . SER   B 1 167 ? 33.278 -40.936 -9.349  1.00 23.91 ?  167  SER   B HA   1 
ATOM   6791 H  HB2  . SER   B 1 167 ? 33.492 -40.539 -7.101  1.00 23.50 ?  167  SER   B HB2  1 
ATOM   6792 H  HB3  . SER   B 1 167 ? 34.881 -41.110 -7.620  1.00 23.50 ?  167  SER   B HB3  1 
ATOM   6793 H  HG   . SER   B 1 167 ? 35.599 -39.033 -7.641  1.00 23.06 ?  167  SER   B HG   1 
ATOM   6794 N  N    . PHE   B 1 168 ? 33.267 -37.890 -9.924  1.00 19.12 ?  168  PHE   B N    1 
ATOM   6795 C  CA   . PHE   B 1 168 ? 32.432 -36.688 -9.979  1.00 18.48 ?  168  PHE   B CA   1 
ATOM   6796 C  C    . PHE   B 1 168 ? 31.115 -36.949 -10.707 1.00 15.80 ?  168  PHE   B C    1 
ATOM   6797 O  O    . PHE   B 1 168 ? 30.071 -36.358 -10.363 1.00 16.24 ?  168  PHE   B O    1 
ATOM   6798 C  CB   . PHE   B 1 168 ? 33.188 -35.548 -10.659 1.00 19.00 ?  168  PHE   B CB   1 
ATOM   6799 C  CG   . PHE   B 1 168 ? 32.381 -34.299 -10.781 1.00 18.95 ?  168  PHE   B CG   1 
ATOM   6800 C  CD1  . PHE   B 1 168 ? 32.058 -33.568 -9.648  1.00 19.75 ?  168  PHE   B CD1  1 
ATOM   6801 C  CD2  . PHE   B 1 168 ? 31.928 -33.863 -12.010 1.00 18.40 ?  168  PHE   B CD2  1 
ATOM   6802 C  CE1  . PHE   B 1 168 ? 31.298 -32.424 -9.735  1.00 20.21 ?  168  PHE   B CE1  1 
ATOM   6803 C  CE2  . PHE   B 1 168 ? 31.179 -32.698 -12.111 1.00 19.58 ?  168  PHE   B CE2  1 
ATOM   6804 C  CZ   . PHE   B 1 168 ? 30.855 -31.980 -10.968 1.00 19.75 ?  168  PHE   B CZ   1 
ATOM   6805 H  H    . PHE   B 1 168 ? 33.995 -37.848 -10.384 1.00 22.95 ?  168  PHE   B H    1 
ATOM   6806 H  HA   . PHE   B 1 168 ? 32.221 -36.414 -9.076  1.00 22.19 ?  168  PHE   B HA   1 
ATOM   6807 H  HB2  . PHE   B 1 168 ? 33.980 -35.344 -10.139 1.00 22.82 ?  168  PHE   B HB2  1 
ATOM   6808 H  HB3  . PHE   B 1 168 ? 33.441 -35.827 -11.553 1.00 22.82 ?  168  PHE   B HB3  1 
ATOM   6809 H  HD1  . PHE   B 1 168 ? 32.346 -33.867 -8.817  1.00 23.71 ?  168  PHE   B HD1  1 
ATOM   6810 H  HD2  . PHE   B 1 168 ? 32.140 -34.338 -12.778 1.00 22.09 ?  168  PHE   B HD2  1 
ATOM   6811 H  HE1  . PHE   B 1 168 ? 31.086 -31.946 -8.967  1.00 24.27 ?  168  PHE   B HE1  1 
ATOM   6812 H  HE2  . PHE   B 1 168 ? 30.873 -32.406 -12.943 1.00 23.51 ?  168  PHE   B HE2  1 
ATOM   6813 H  HZ   . PHE   B 1 168 ? 30.342 -31.204 -11.033 1.00 23.71 ?  168  PHE   B HZ   1 
ATOM   6814 N  N    . LEU   B 1 169 ? 31.149 -37.830 -11.705 1.00 16.51 ?  169  LEU   B N    1 
ATOM   6815 C  CA   . LEU   B 1 169 ? 29.971 -38.153 -12.502 1.00 19.31 ?  169  LEU   B CA   1 
ATOM   6816 C  C    . LEU   B 1 169 ? 29.950 -39.598 -12.972 1.00 22.48 ?  169  LEU   B C    1 
ATOM   6817 O  O    . LEU   B 1 169 ? 29.033 -40.021 -13.680 1.00 24.93 ?  169  LEU   B O    1 
ATOM   6818 C  CB   . LEU   B 1 169 ? 29.904 -37.240 -13.723 1.00 21.23 ?  169  LEU   B CB   1 
ATOM   6819 C  CG   . LEU   B 1 169 ? 28.674 -36.341 -13.812 1.00 24.59 ?  169  LEU   B CG   1 
ATOM   6820 C  CD1  . LEU   B 1 169 ? 28.608 -35.707 -15.184 1.00 25.36 ?  169  LEU   B CD1  1 
ATOM   6821 C  CD2  . LEU   B 1 169 ? 27.398 -37.110 -13.511 1.00 25.11 ?  169  LEU   B CD2  1 
ATOM   6822 O  OXT  . LEU   B 1 169 ? 30.851 -40.366 -12.666 1.00 23.76 -1 169  LEU   B OXT  1 
ATOM   6823 H  H    . LEU   B 1 169 ? 31.859 -38.255 -11.953 1.00 19.82 ?  169  LEU   B H    1 
ATOM   6824 H  HA   . LEU   B 1 169 ? 29.188 -38.003 -11.954 1.00 23.19 ?  169  LEU   B HA   1 
ATOM   6825 H  HB2  . LEU   B 1 169 ? 30.683 -36.664 -13.724 1.00 25.49 ?  169  LEU   B HB2  1 
ATOM   6826 H  HB3  . LEU   B 1 169 ? 29.911 -37.793 -14.522 1.00 25.49 ?  169  LEU   B HB3  1 
ATOM   6827 H  HG   . LEU   B 1 169 ? 28.755 -35.628 -13.158 1.00 29.52 ?  169  LEU   B HG   1 
ATOM   6828 H  HD11 . LEU   B 1 169 ? 27.841 -35.115 -15.220 1.00 30.45 ?  169  LEU   B HD11 1 
ATOM   6829 H  HD12 . LEU   B 1 169 ? 29.423 -35.205 -15.336 1.00 30.45 ?  169  LEU   B HD12 1 
ATOM   6830 H  HD13 . LEU   B 1 169 ? 28.520 -36.408 -15.848 1.00 30.45 ?  169  LEU   B HD13 1 
ATOM   6831 H  HD21 . LEU   B 1 169 ? 26.655 -36.682 -13.957 1.00 30.15 ?  169  LEU   B HD21 1 
ATOM   6832 H  HD22 . LEU   B 1 169 ? 27.499 -38.022 -13.833 1.00 30.15 ?  169  LEU   B HD22 1 
ATOM   6833 H  HD23 . LEU   B 1 169 ? 27.253 -37.115 -12.552 1.00 30.15 ?  169  LEU   B HD23 1 
HETATM 6834 N  N2   B A1BBT C 2 .   ? 15.012 -0.138  3.770   0.38 13.44 ?  201  A1BBT A N2   1 
HETATM 6835 C  C3   B A1BBT C 2 .   ? 13.638 0.035   -0.016  0.38 14.17 ?  201  A1BBT A C3   1 
HETATM 6836 C  C6   B A1BBT C 2 .   ? 15.210 2.176   0.851   0.38 13.76 ?  201  A1BBT A C6   1 
HETATM 6837 C  C9   B A1BBT C 2 .   ? 15.325 2.063   5.306   0.38 11.94 ?  201  A1BBT A C9   1 
HETATM 6838 C  C12  B A1BBT C 2 .   ? 15.641 4.266   4.952   0.38 11.57 ?  201  A1BBT A C12  1 
HETATM 6839 C  C1   B A1BBT C 2 .   ? 15.898 -0.874  0.375   0.38 13.68 ?  201  A1BBT A C1   1 
HETATM 6840 C  C10  B A1BBT C 2 .   ? 15.337 2.238   3.905   0.38 12.48 ?  201  A1BBT A C10  1 
HETATM 6841 C  C11  B A1BBT C 2 .   ? 15.545 3.661   3.719   0.38 11.77 ?  201  A1BBT A C11  1 
HETATM 6842 C  C2   B A1BBT C 2 .   ? 14.666 -0.234  1.037   0.38 13.39 ?  201  A1BBT A C2   1 
HETATM 6843 C  C4   B A1BBT C 2 .   ? 13.293 1.250   -0.425  0.38 14.89 ?  201  A1BBT A C4   1 
HETATM 6844 C  C5   B A1BBT C 2 .   ? 13.975 2.468   0.022   0.38 14.98 ?  201  A1BBT A C5   1 
HETATM 6845 C  C7   B A1BBT C 2 .   ? 15.161 1.054   3.138   0.38 12.94 ?  201  A1BBT A C7   1 
HETATM 6846 C  C8   B A1BBT C 2 .   ? 15.010 -0.165  5.136   0.38 13.20 ?  201  A1BBT A C8   1 
HETATM 6847 N  N1   B A1BBT C 2 .   ? 15.143 0.994   1.706   0.38 12.96 ?  201  A1BBT A N1   1 
HETATM 6848 N  N3   B A1BBT C 2 .   ? 15.164 0.877   5.963   0.38 12.49 ?  201  A1BBT A N3   1 
HETATM 6849 N  N4   B A1BBT C 2 .   ? 15.511 3.278   5.929   0.38 11.76 ?  201  A1BBT A N4   1 
HETATM 6850 O  O1   B A1BBT C 2 .   ? 15.443 -2.071  -0.189  0.38 14.72 ?  201  A1BBT A O1   1 
HETATM 6851 H  H5   B A1BBT C 2 .   ? 13.088 -0.853  -0.344  0.38 17.02 ?  201  A1BBT A H5   1 
HETATM 6852 H  H9   B A1BBT C 2 .   ? 15.422 3.027   1.436   0.38 16.52 ?  201  A1BBT A H9   1 
HETATM 6853 H  H10  B A1BBT C 2 .   ? 16.069 2.102   0.199   0.38 16.52 ?  201  A1BBT A H10  1 
HETATM 6854 H  H13  B A1BBT C 2 .   ? 15.789 5.303   5.202   0.38 13.89 ?  201  A1BBT A H13  1 
HETATM 6855 H  H4   B A1BBT C 2 .   ? 16.326 -0.180  -0.388  0.38 16.43 ?  201  A1BBT A H4   1 
HETATM 6856 H  H3   B A1BBT C 2 .   ? 16.705 -1.051  1.111   0.38 16.43 ?  201  A1BBT A H3   1 
HETATM 6857 H  H12  B A1BBT C 2 .   ? 15.609 4.180   2.774   0.38 14.14 ?  201  A1BBT A H12  1 
HETATM 6858 H  H1   B A1BBT C 2 .   ? 14.187 -0.958  1.748   0.38 16.08 ?  201  A1BBT A H1   1 
HETATM 6859 H  H6   B A1BBT C 2 .   ? 12.470 1.396   -1.132  0.38 17.88 ?  201  A1BBT A H6   1 
HETATM 6860 H  H7   B A1BBT C 2 .   ? 13.273 3.184   0.502   0.38 17.99 ?  201  A1BBT A H7   1 
HETATM 6861 H  H8   B A1BBT C 2 .   ? 14.294 3.001   -0.893  0.38 17.99 ?  201  A1BBT A H8   1 
HETATM 6862 H  H11  B A1BBT C 2 .   ? 14.873 -1.132  5.636   0.38 15.85 ?  201  A1BBT A H11  1 
HETATM 6863 H  H14  B A1BBT C 2 .   ? 15.537 3.425   6.921   0.38 14.12 ?  201  A1BBT A H14  1 
HETATM 6864 H  H2   B A1BBT C 2 .   ? 16.147 -2.395  -0.742  0.38 17.68 ?  201  A1BBT A H2   1 
HETATM 6865 CL CL   B CL    D 3 .   ? 18.332 2.078   -1.186  0.38 13.92 ?  202  CL    A CL   1 
HETATM 6866 O  O    . HOH   E 4 .   ? 11.762 -10.863 -10.010 1.00 45.94 ?  1301 HOH   A O    1 
HETATM 6867 O  O    . HOH   E 4 .   ? -0.449 -3.152  3.000   1.00 44.13 ?  1302 HOH   A O    1 
HETATM 6868 O  O    . HOH   E 4 .   ? 18.558 -2.486  -16.482 1.00 43.32 ?  1303 HOH   A O    1 
HETATM 6869 O  O    . HOH   E 4 .   ? 14.641 -4.644  20.485  1.00 45.63 ?  1304 HOH   A O    1 
HETATM 6870 O  O    . HOH   E 4 .   ? 24.584 1.953   -7.095  1.00 22.45 ?  1305 HOH   A O    1 
HETATM 6871 O  O    . HOH   E 4 .   ? 17.268 -18.094 15.019  1.00 28.17 ?  1306 HOH   A O    1 
HETATM 6872 O  O    . HOH   E 4 .   ? 15.237 -12.312 18.695  1.00 44.71 ?  1307 HOH   A O    1 
HETATM 6873 O  O    . HOH   E 4 .   ? 28.942 0.420   -9.764  1.00 21.14 ?  1308 HOH   A O    1 
HETATM 6874 O  O    . HOH   E 4 .   ? 26.820 11.378  1.650   1.00 15.31 ?  1309 HOH   A O    1 
HETATM 6875 O  O    A HOH   E 4 .   ? 4.724  3.855   0.617   0.62 26.16 ?  1310 HOH   A O    1 
HETATM 6876 O  O    . HOH   E 4 .   ? 9.266  -10.155 19.432  1.00 47.95 ?  1311 HOH   A O    1 
HETATM 6877 O  O    . HOH   E 4 .   ? 34.416 -1.822  12.540  1.00 40.01 ?  1312 HOH   A O    1 
HETATM 6878 O  O    . HOH   E 4 .   ? 12.003 0.320   14.756  1.00 35.37 ?  1313 HOH   A O    1 
HETATM 6879 O  O    . HOH   E 4 .   ? 18.988 -22.036 6.924   1.00 31.91 ?  1314 HOH   A O    1 
HETATM 6880 O  O    . HOH   E 4 .   ? 0.750  -4.859  0.077   1.00 35.22 ?  1315 HOH   A O    1 
HETATM 6881 O  O    . HOH   E 4 .   ? 28.347 -6.290  19.563  1.00 42.94 ?  1316 HOH   A O    1 
HETATM 6882 O  O    . HOH   E 4 .   ? 30.302 -13.306 -8.444  1.00 25.15 ?  1317 HOH   A O    1 
HETATM 6883 O  O    . HOH   E 4 .   ? 14.761 -13.961 16.743  1.00 27.94 ?  1318 HOH   A O    1 
HETATM 6884 O  O    . HOH   E 4 .   ? 42.413 10.552  5.127   1.00 20.20 ?  1319 HOH   A O    1 
HETATM 6885 O  O    B HOH   E 4 .   ? 12.788 -0.391  -5.431  0.38 32.90 ?  1320 HOH   A O    1 
HETATM 6886 O  O    . HOH   E 4 .   ? 30.869 6.239   -12.294 1.00 27.82 ?  1321 HOH   A O    1 
HETATM 6887 O  O    . HOH   E 4 .   ? 20.174 4.465   -7.547  1.00 25.69 ?  1322 HOH   A O    1 
HETATM 6888 O  O    . HOH   E 4 .   ? 7.711  -6.354  -6.625  1.00 41.30 ?  1323 HOH   A O    1 
HETATM 6889 O  O    . HOH   E 4 .   ? 28.385 -0.186  -13.445 1.00 35.64 ?  1324 HOH   A O    1 
HETATM 6890 O  O    . HOH   E 4 .   ? 17.097 -19.350 4.911   1.00 14.30 ?  1325 HOH   A O    1 
HETATM 6891 O  O    A HOH   E 4 .   ? 3.653  -9.527  9.733   0.62 29.84 ?  1326 HOH   A O    1 
HETATM 6892 O  O    . HOH   E 4 .   ? 14.938 3.892   17.578  1.00 39.97 ?  1327 HOH   A O    1 
HETATM 6893 O  O    . HOH   E 4 .   ? 14.149 -4.620  -11.873 1.00 35.80 ?  1328 HOH   A O    1 
HETATM 6894 O  O    . HOH   E 4 .   ? 37.513 2.832   10.251  1.00 28.35 ?  1329 HOH   A O    1 
HETATM 6895 O  O    . HOH   E 4 .   ? 28.697 -10.583 -14.093 1.00 39.63 ?  1330 HOH   A O    1 
HETATM 6896 O  O    . HOH   E 4 .   ? 14.452 -24.708 11.558  1.00 34.27 ?  1331 HOH   A O    1 
HETATM 6897 O  O    . HOH   E 4 .   ? 36.192 -5.105  -0.543  1.00 29.32 ?  1332 HOH   A O    1 
HETATM 6898 O  O    . HOH   E 4 .   ? 9.972  -21.439 5.702   1.00 18.12 ?  1333 HOH   A O    1 
HETATM 6899 O  O    . HOH   E 4 .   ? -0.716 -8.662  2.105   1.00 45.33 ?  1334 HOH   A O    1 
HETATM 6900 O  O    . HOH   E 4 .   ? 10.984 1.586   12.491  1.00 24.07 ?  1335 HOH   A O    1 
HETATM 6901 O  O    . HOH   E 4 .   ? 22.375 5.295   19.046  1.00 45.15 ?  1336 HOH   A O    1 
HETATM 6902 O  O    . HOH   E 4 .   ? 31.091 -18.142 7.812   1.00 18.37 ?  1337 HOH   A O    1 
HETATM 6903 O  O    . HOH   E 4 .   ? 18.761 -19.368 13.600  1.00 33.02 ?  1338 HOH   A O    1 
HETATM 6904 O  O    A HOH   E 4 .   ? 17.534 -1.758  0.437   0.62 17.89 ?  1339 HOH   A O    1 
HETATM 6905 O  O    . HOH   E 4 .   ? 38.280 10.213  7.062   1.00 43.69 ?  1340 HOH   A O    1 
HETATM 6906 O  O    . HOH   E 4 .   ? 44.333 7.178   6.366   1.00 26.70 ?  1341 HOH   A O    1 
HETATM 6907 O  O    . HOH   E 4 .   ? 25.765 -0.904  -7.434  1.00 16.43 ?  1342 HOH   A O    1 
HETATM 6908 O  O    A HOH   E 4 .   ? 8.256  -21.455 3.993   0.62 41.96 ?  1343 HOH   A O    1 
HETATM 6909 O  O    . HOH   E 4 .   ? 22.649 -12.017 21.953  1.00 50.57 ?  1344 HOH   A O    1 
HETATM 6910 O  O    . HOH   E 4 .   ? 20.023 -12.684 -8.814  1.00 25.78 ?  1345 HOH   A O    1 
HETATM 6911 O  O    A HOH   E 4 .   ? 14.677 -3.703  3.094   0.62 17.58 ?  1346 HOH   A O    1 
HETATM 6912 O  O    . HOH   E 4 .   ? 27.918 0.784   -7.195  1.00 14.39 ?  1347 HOH   A O    1 
HETATM 6913 O  O    . HOH   E 4 .   ? 22.222 -19.327 11.395  1.00 32.86 ?  1348 HOH   A O    1 
HETATM 6914 O  O    A HOH   E 4 .   ? 14.313 0.525   6.797   0.62 24.51 ?  1349 HOH   A O    1 
HETATM 6915 O  O    . HOH   E 4 .   ? 27.333 13.767  2.817   1.00 28.36 ?  1350 HOH   A O    1 
HETATM 6916 O  O    . HOH   E 4 .   ? 23.893 -15.790 -9.146  1.00 36.03 ?  1351 HOH   A O    1 
HETATM 6917 O  O    . HOH   E 4 .   ? 31.665 8.247   14.773  1.00 24.50 ?  1352 HOH   A O    1 
HETATM 6918 O  O    . HOH   E 4 .   ? 20.682 -19.803 -5.039  1.00 27.37 ?  1353 HOH   A O    1 
HETATM 6919 O  O    . HOH   E 4 .   ? 21.316 -2.412  -2.309  1.00 17.10 ?  1354 HOH   A O    1 
HETATM 6920 O  O    . HOH   E 4 .   ? 38.565 4.989   6.980   1.00 15.44 ?  1355 HOH   A O    1 
HETATM 6921 O  O    . HOH   E 4 .   ? 15.307 -21.608 14.258  1.00 17.96 ?  1356 HOH   A O    1 
HETATM 6922 O  O    . HOH   E 4 .   ? 7.980  -12.939 -0.947  1.00 23.59 ?  1357 HOH   A O    1 
HETATM 6923 O  O    . HOH   E 4 .   ? 8.880  -11.965 17.334  1.00 41.41 ?  1358 HOH   A O    1 
HETATM 6924 O  O    . HOH   E 4 .   ? 22.757 12.517  1.588   1.00 13.95 ?  1359 HOH   A O    1 
HETATM 6925 O  O    . HOH   E 4 .   ? 34.046 -1.112  -8.966  1.00 26.38 ?  1360 HOH   A O    1 
HETATM 6926 O  O    A HOH   E 4 .   ? 7.001  -8.220  11.849  0.62 19.91 ?  1361 HOH   A O    1 
HETATM 6927 O  O    . HOH   E 4 .   ? 10.420 -22.253 -1.248  1.00 56.89 ?  1362 HOH   A O    1 
HETATM 6928 O  O    . HOH   E 4 .   ? 14.460 -21.313 -4.277  1.00 27.35 ?  1363 HOH   A O    1 
HETATM 6929 O  O    B HOH   E 4 .   ? 14.992 -2.892  3.377   0.38 13.64 ?  1364 HOH   A O    1 
HETATM 6930 O  O    . HOH   E 4 .   ? 39.770 -1.022  -5.224  1.00 20.19 ?  1365 HOH   A O    1 
HETATM 6931 O  O    . HOH   E 4 .   ? 14.176 -23.117 7.409   1.00 18.70 ?  1366 HOH   A O    1 
HETATM 6932 O  O    . HOH   E 4 .   ? 37.315 11.949  4.934   1.00 30.07 ?  1367 HOH   A O    1 
HETATM 6933 O  O    . HOH   E 4 .   ? 35.846 -12.667 6.864   1.00 15.25 ?  1368 HOH   A O    1 
HETATM 6934 O  O    . HOH   E 4 .   ? 42.519 4.243   5.335   1.00 32.83 ?  1369 HOH   A O    1 
HETATM 6935 O  O    B HOH   E 4 .   ? 9.229  2.166   7.568   0.38 26.00 ?  1370 HOH   A O    1 
HETATM 6936 O  O    . HOH   E 4 .   ? 24.071 -2.163  -2.125  1.00 10.90 ?  1371 HOH   A O    1 
HETATM 6937 O  O    . HOH   E 4 .   ? 17.244 -17.830 -5.002  1.00 25.81 ?  1372 HOH   A O    1 
HETATM 6938 O  O    . HOH   E 4 .   ? 33.697 -7.161  4.316   1.00 15.98 ?  1373 HOH   A O    1 
HETATM 6939 O  O    . HOH   E 4 .   ? 11.797 -10.774 17.073  1.00 29.34 ?  1374 HOH   A O    1 
HETATM 6940 O  O    . HOH   E 4 .   ? 21.937 -21.899 8.452   1.00 29.10 ?  1375 HOH   A O    1 
HETATM 6941 O  O    B HOH   E 4 .   ? 13.163 -3.402  -0.993  0.38 30.31 ?  1376 HOH   A O    1 
HETATM 6942 O  O    . HOH   E 4 .   ? 30.801 3.100   8.273   1.00 12.13 ?  1377 HOH   A O    1 
HETATM 6943 O  O    . HOH   E 4 .   ? 43.339 7.796   2.639   1.00 29.33 ?  1378 HOH   A O    1 
HETATM 6944 O  O    . HOH   E 4 .   ? 31.172 -13.968 -2.414  1.00 13.60 ?  1379 HOH   A O    1 
HETATM 6945 O  O    . HOH   E 4 .   ? 27.509 -10.583 14.091  1.00 16.69 ?  1380 HOH   A O    1 
HETATM 6946 O  O    . HOH   E 4 .   ? 37.291 -2.877  9.696   1.00 45.80 ?  1381 HOH   A O    1 
HETATM 6947 O  O    . HOH   E 4 .   ? 43.970 8.492   -3.077  1.00 28.00 ?  1382 HOH   A O    1 
HETATM 6948 O  O    . HOH   E 4 .   ? 18.504 9.437   8.902   1.00 20.95 ?  1383 HOH   A O    1 
HETATM 6949 O  O    . HOH   E 4 .   ? 21.174 10.274  14.945  1.00 34.47 ?  1384 HOH   A O    1 
HETATM 6950 O  O    . HOH   E 4 .   ? 33.625 -16.998 8.098   1.00 18.83 ?  1385 HOH   A O    1 
HETATM 6951 O  O    . HOH   E 4 .   ? 5.141  2.522   4.992   1.00 32.09 ?  1386 HOH   A O    1 
HETATM 6952 O  O    . HOH   E 4 .   ? 16.637 -22.158 0.989   1.00 29.44 ?  1387 HOH   A O    1 
HETATM 6953 O  O    . HOH   E 4 .   ? 13.578 -15.355 -7.473  1.00 27.45 ?  1388 HOH   A O    1 
HETATM 6954 O  O    . HOH   E 4 .   ? 24.430 3.538   -1.875  1.00 14.68 ?  1389 HOH   A O    1 
HETATM 6955 O  O    . HOH   E 4 .   ? 31.931 -7.323  -9.800  1.00 21.85 ?  1390 HOH   A O    1 
HETATM 6956 O  O    . HOH   E 4 .   ? 15.838 2.095   24.686  1.00 46.45 ?  1391 HOH   A O    1 
HETATM 6957 O  O    . HOH   E 4 .   ? 32.010 -9.373  -6.610  1.00 23.27 ?  1392 HOH   A O    1 
HETATM 6958 O  O    . HOH   E 4 .   ? 24.018 3.930   -4.896  1.00 25.17 ?  1393 HOH   A O    1 
HETATM 6959 O  O    . HOH   E 4 .   ? 15.452 11.935  7.781   1.00 33.10 ?  1394 HOH   A O    1 
HETATM 6960 O  O    . HOH   E 4 .   ? 19.030 -0.727  -1.779  1.00 15.66 ?  1395 HOH   A O    1 
HETATM 6961 O  O    . HOH   E 4 .   ? 24.259 -7.751  14.469  1.00 15.86 ?  1396 HOH   A O    1 
HETATM 6962 O  O    . HOH   E 4 .   ? 24.791 -17.533 12.734  1.00 22.94 ?  1397 HOH   A O    1 
HETATM 6963 O  O    . HOH   E 4 .   ? 26.947 4.131   -0.684  1.00 12.24 ?  1398 HOH   A O    1 
HETATM 6964 O  O    A HOH   E 4 .   ? 13.343 -1.487  -6.526  0.62 15.84 ?  1399 HOH   A O    1 
HETATM 6965 O  O    B HOH   E 4 .   ? 10.881 -1.203  1.537   0.38 15.88 ?  1400 HOH   A O    1 
HETATM 6966 O  O    . HOH   E 4 .   ? 32.825 -9.253  6.007   1.00 19.97 ?  1401 HOH   A O    1 
HETATM 6967 O  O    . HOH   E 4 .   ? 30.642 1.914   16.713  1.00 20.77 ?  1402 HOH   A O    1 
HETATM 6968 O  O    . HOH   E 4 .   ? 37.564 -2.037  5.819   1.00 27.02 ?  1403 HOH   A O    1 
HETATM 6969 O  O    . HOH   E 4 .   ? 27.530 -6.178  -14.019 1.00 35.87 ?  1404 HOH   A O    1 
HETATM 6970 O  O    . HOH   E 4 .   ? 21.368 3.033   -0.338  1.00 12.71 ?  1405 HOH   A O    1 
HETATM 6971 O  O    . HOH   E 4 .   ? 15.227 -8.157  -9.797  1.00 24.72 ?  1406 HOH   A O    1 
HETATM 6972 O  O    . HOH   E 4 .   ? 20.625 -20.059 2.798   1.00 18.13 ?  1407 HOH   A O    1 
HETATM 6973 O  O    . HOH   E 4 .   ? 23.453 11.387  4.053   1.00 11.87 ?  1408 HOH   A O    1 
HETATM 6974 O  O    . HOH   E 4 .   ? 27.277 2.364   18.718  1.00 31.77 ?  1409 HOH   A O    1 
HETATM 6975 O  O    . HOH   E 4 .   ? 16.361 -14.157 20.151  1.00 54.01 ?  1410 HOH   A O    1 
HETATM 6976 O  O    . HOH   E 4 .   ? 30.117 -10.076 13.056  1.00 21.00 ?  1411 HOH   A O    1 
HETATM 6977 O  O    . HOH   E 4 .   ? 6.650  -3.483  12.805  1.00 33.03 ?  1412 HOH   A O    1 
HETATM 6978 O  O    . HOH   E 4 .   ? 16.076 6.948   2.912   1.00 18.14 ?  1413 HOH   A O    1 
HETATM 6979 O  O    . HOH   E 4 .   ? 14.565 -0.618  -12.087 1.00 29.80 ?  1414 HOH   A O    1 
HETATM 6980 O  O    . HOH   E 4 .   ? 13.955 -4.909  17.428  1.00 26.15 ?  1415 HOH   A O    1 
HETATM 6981 O  O    . HOH   E 4 .   ? 41.631 1.444   4.951   1.00 36.07 ?  1416 HOH   A O    1 
HETATM 6982 O  O    B HOH   E 4 .   ? 4.757  4.247   0.984   0.38 33.93 ?  1417 HOH   A O    1 
HETATM 6983 O  O    . HOH   E 4 .   ? 16.230 16.709  8.710   1.00 34.86 ?  1418 HOH   A O    1 
HETATM 6984 O  O    A HOH   E 4 .   ? 6.515  -5.664  11.179  0.62 19.00 ?  1419 HOH   A O    1 
HETATM 6985 O  O    . HOH   E 4 .   ? 38.107 -1.335  -1.951  1.00 19.05 ?  1420 HOH   A O    1 
HETATM 6986 O  O    . HOH   E 4 .   ? 30.385 -12.926 13.579  1.00 19.19 ?  1421 HOH   A O    1 
HETATM 6987 O  O    . HOH   E 4 .   ? 21.885 -13.946 -8.106  1.00 48.02 ?  1422 HOH   A O    1 
HETATM 6988 O  O    . HOH   E 4 .   ? 35.136 -5.246  -3.078  1.00 17.63 ?  1423 HOH   A O    1 
HETATM 6989 O  O    . HOH   E 4 .   ? 41.009 -8.300  -6.726  1.00 36.83 ?  1424 HOH   A O    1 
HETATM 6990 O  O    . HOH   E 4 .   ? 32.581 -10.643 3.248   1.00 31.97 ?  1425 HOH   A O    1 
HETATM 6991 O  O    . HOH   E 4 .   ? 27.043 -3.194  19.436  1.00 37.94 ?  1426 HOH   A O    1 
HETATM 6992 O  O    . HOH   E 4 .   ? 24.022 -20.325 -1.307  1.00 16.46 ?  1427 HOH   A O    1 
HETATM 6993 O  O    A HOH   E 4 .   ? 15.839 -0.992  5.266   0.62 29.70 ?  1428 HOH   A O    1 
HETATM 6994 O  O    . HOH   E 4 .   ? 32.773 -4.388  -9.904  1.00 27.52 ?  1429 HOH   A O    1 
HETATM 6995 O  O    . HOH   E 4 .   ? 36.750 -4.987  5.388   1.00 24.73 ?  1430 HOH   A O    1 
HETATM 6996 O  O    . HOH   E 4 .   ? 22.633 8.175   18.332  1.00 45.93 ?  1431 HOH   A O    1 
HETATM 6997 O  O    . HOH   E 4 .   ? 10.461 -13.870 -1.755  1.00 17.56 ?  1432 HOH   A O    1 
HETATM 6998 O  O    B HOH   E 4 .   ? 7.619  3.740   4.248   0.38 19.81 ?  1433 HOH   A O    1 
HETATM 6999 O  O    . HOH   E 4 .   ? 19.084 -11.022 24.070  1.00 76.19 ?  1434 HOH   A O    1 
HETATM 7000 O  O    . HOH   E 4 .   ? 45.037 -0.556  2.958   1.00 41.54 ?  1435 HOH   A O    1 
HETATM 7001 O  O    A HOH   E 4 .   ? 11.104 -0.434  1.932   0.62 21.01 ?  1436 HOH   A O    1 
HETATM 7002 O  O    A HOH   E 4 .   ? 18.895 1.990   -0.757  0.62 12.61 ?  1437 HOH   A O    1 
HETATM 7003 O  O    . HOH   E 4 .   ? 21.403 -9.174  21.347  1.00 52.79 ?  1438 HOH   A O    1 
HETATM 7004 O  O    . HOH   E 4 .   ? 23.503 -7.985  17.090  1.00 20.99 ?  1439 HOH   A O    1 
HETATM 7005 O  O    . HOH   E 4 .   ? -1.420 -4.992  7.630   1.00 39.01 ?  1440 HOH   A O    1 
HETATM 7006 O  O    B HOH   E 4 .   ? 7.950  3.737   1.336   0.38 22.39 ?  1441 HOH   A O    1 
HETATM 7007 O  O    . HOH   E 4 .   ? 23.444 -20.995 1.369   1.00 18.71 ?  1442 HOH   A O    1 
HETATM 7008 O  O    . HOH   E 4 .   ? 37.793 -8.832  -3.405  1.00 22.75 ?  1443 HOH   A O    1 
HETATM 7009 O  O    A HOH   E 4 .   ? 16.289 2.901   -1.445  0.62 17.12 ?  1444 HOH   A O    1 
HETATM 7010 O  O    . HOH   E 4 .   ? 34.439 -8.121  -0.474  1.00 28.95 ?  1445 HOH   A O    1 
HETATM 7011 O  O    . HOH   E 4 .   ? 31.408 -12.801 0.041   1.00 20.48 ?  1446 HOH   A O    1 
HETATM 7012 O  O    . HOH   E 4 .   ? 18.446 -16.060 16.291  1.00 38.70 ?  1447 HOH   A O    1 
HETATM 7013 O  O    . HOH   E 4 .   ? 20.619 -17.764 24.827  1.00 61.83 ?  1448 HOH   A O    1 
HETATM 7014 O  O    . HOH   E 4 .   ? 23.250 7.644   -3.325  1.00 27.68 ?  1449 HOH   A O    1 
HETATM 7015 O  O    . HOH   E 4 .   ? 30.584 14.765  2.767   1.00 18.63 ?  1450 HOH   A O    1 
HETATM 7016 O  O    B HOH   E 4 .   ? 12.064 -1.592  -3.000  0.38 15.85 ?  1451 HOH   A O    1 
HETATM 7017 O  O    A HOH   E 4 .   ? 9.444  -16.382 -1.983  0.62 42.43 ?  1452 HOH   A O    1 
HETATM 7018 O  O    . HOH   E 4 .   ? 18.585 4.968   -15.107 1.00 56.60 ?  1453 HOH   A O    1 
HETATM 7019 O  O    . HOH   E 4 .   ? 21.610 -14.810 17.856  1.00 53.59 ?  1454 HOH   A O    1 
HETATM 7020 O  O    A HOH   E 4 .   ? 14.065 -0.388  3.459   0.62 35.00 ?  1455 HOH   A O    1 
HETATM 7021 O  O    . HOH   E 4 .   ? 29.877 -16.077 10.790  1.00 31.72 ?  1456 HOH   A O    1 
HETATM 7022 O  O    . HOH   E 4 .   ? 27.742 7.017   -6.513  1.00 36.52 ?  1457 HOH   A O    1 
HETATM 7023 O  O    . HOH   E 4 .   ? 29.895 -1.979  -12.696 1.00 49.25 ?  1458 HOH   A O    1 
HETATM 7024 O  O    . HOH   E 4 .   ? 32.463 -15.969 10.850  1.00 31.93 ?  1459 HOH   A O    1 
HETATM 7025 O  O    . HOH   E 4 .   ? 25.436 8.303   -4.872  1.00 22.80 ?  1460 HOH   A O    1 
HETATM 7026 O  O    . HOH   E 4 .   ? 19.970 -17.440 -5.025  1.00 24.49 ?  1461 HOH   A O    1 
HETATM 7027 O  O    . HOH   E 4 .   ? 12.025 -13.426 16.388  1.00 54.80 ?  1462 HOH   A O    1 
HETATM 7028 O  O    . HOH   E 4 .   ? 23.267 -22.336 -3.344  1.00 38.62 ?  1463 HOH   A O    1 
HETATM 7029 O  O    . HOH   E 4 .   ? 24.776 5.638   20.734  1.00 55.26 ?  1464 HOH   A O    1 
HETATM 7030 O  O    . HOH   E 4 .   ? 24.596 14.567  7.812   1.00 35.60 ?  1465 HOH   A O    1 
HETATM 7031 O  O    B HOH   E 4 .   ? 12.602 -3.238  1.855   0.38 23.79 ?  1466 HOH   A O    1 
HETATM 7032 O  O    . HOH   E 4 .   ? 26.970 11.593  -1.286  1.00 30.53 ?  1467 HOH   A O    1 
HETATM 7033 O  O    . HOH   E 4 .   ? 22.088 5.179   -6.147  1.00 34.85 ?  1468 HOH   A O    1 
HETATM 7034 O  O    . HOH   E 4 .   ? 18.768 10.906  11.183  1.00 29.95 ?  1469 HOH   A O    1 
HETATM 7035 O  O    . HOH   E 4 .   ? 39.762 -7.074  -3.529  1.00 45.96 ?  1470 HOH   A O    1 
HETATM 7036 O  O    . HOH   E 4 .   ? 15.821 -21.577 3.729   1.00 21.93 ?  1471 HOH   A O    1 
HETATM 7037 O  O    . HOH   E 4 .   ? 23.442 13.704  5.520   1.00 18.85 ?  1472 HOH   A O    1 
HETATM 7038 O  O    . HOH   E 4 .   ? 27.584 -11.404 16.579  1.00 37.39 ?  1473 HOH   A O    1 
HETATM 7039 O  O    . HOH   E 4 .   ? 25.943 10.810  -3.637  1.00 23.20 ?  1474 HOH   A O    1 
HETATM 7040 O  O    . HOH   E 4 .   ? 12.310 1.650   17.301  1.00 40.94 ?  1475 HOH   A O    1 
HETATM 7041 O  O    . HOH   E 4 .   ? 11.109 -15.146 -6.114  1.00 33.57 ?  1476 HOH   A O    1 
HETATM 7042 O  O    . HOH   E 4 .   ? 16.916 -20.562 16.172  1.00 29.94 ?  1477 HOH   A O    1 
HETATM 7043 O  O    . HOH   E 4 .   ? 23.250 11.936  -4.016  1.00 21.25 ?  1478 HOH   A O    1 
HETATM 7044 O  O    . HOH   E 4 .   ? 28.767 8.993   17.499  1.00 36.48 ?  1479 HOH   A O    1 
HETATM 7045 O  O    . HOH   E 4 .   ? 18.230 -16.342 -8.863  1.00 45.82 ?  1480 HOH   A O    1 
HETATM 7046 O  O    . HOH   E 4 .   ? 35.144 7.474   12.246  1.00 51.00 ?  1481 HOH   A O    1 
HETATM 7047 O  O    . HOH   E 4 .   ? 15.741 -17.305 -6.955  1.00 31.50 ?  1482 HOH   A O    1 
HETATM 7048 O  O    . HOH   E 4 .   ? 14.096 -10.388 -10.902 1.00 35.50 ?  1483 HOH   A O    1 
HETATM 7049 O  O    . HOH   E 4 .   ? 41.072 -3.993  -0.364  1.00 39.94 ?  1484 HOH   A O    1 
HETATM 7050 O  O    . HOH   E 4 .   ? 28.603 -4.756  -12.315 1.00 40.35 ?  1485 HOH   A O    1 
HETATM 7051 O  O    . HOH   E 4 .   ? 17.422 -18.792 19.702  1.00 51.83 ?  1486 HOH   A O    1 
HETATM 7052 O  O    . HOH   E 4 .   ? 30.990 0.717   19.085  1.00 41.76 ?  1487 HOH   A O    1 
HETATM 7053 O  O    . HOH   E 4 .   ? 44.452 10.466  -1.614  1.00 34.21 ?  1488 HOH   A O    1 
HETATM 7054 O  O    . HOH   E 4 .   ? 23.223 -12.986 19.252  1.00 53.40 ?  1489 HOH   A O    1 
HETATM 7055 O  O    . HOH   E 4 .   ? 41.712 9.394   -3.989  1.00 31.06 ?  1490 HOH   A O    1 
HETATM 7056 O  O    . HOH   E 4 .   ? 16.060 -6.951  -11.802 1.00 45.94 ?  1491 HOH   A O    1 
HETATM 7057 O  O    . HOH   E 4 .   ? 31.525 -0.603  -10.576 1.00 25.75 ?  1492 HOH   A O    1 
HETATM 7058 O  O    . HOH   E 4 .   ? 39.199 2.385   7.419   1.00 31.71 ?  1493 HOH   A O    1 
HETATM 7059 O  O    . HOH   E 4 .   ? 20.140 -22.391 4.207   1.00 29.76 ?  1494 HOH   A O    1 
HETATM 7060 O  O    . HOH   E 4 .   ? 18.597 -23.260 1.939   1.00 44.80 ?  1495 HOH   A O    1 
HETATM 7061 O  O    . HOH   E 4 .   ? 16.232 -23.440 5.750   1.00 29.42 ?  1496 HOH   A O    1 
HETATM 7062 O  O    . HOH   E 4 .   ? 30.717 5.800   -14.773 1.00 36.10 ?  1497 HOH   A O    1 
HETATM 7063 O  O    . HOH   E 4 .   ? 14.011 -25.345 8.889   1.00 36.69 ?  1498 HOH   A O    1 
HETATM 7064 O  O    . HOH   E 4 .   ? 40.551 -0.264  -7.843  1.00 31.12 ?  1499 HOH   A O    1 
HETATM 7065 O  O    . HOH   E 4 .   ? 20.650 -16.082 -7.385  1.00 29.56 ?  1500 HOH   A O    1 
HETATM 7066 O  O    . HOH   E 4 .   ? 28.881 -7.985  -15.222 1.00 49.62 ?  1501 HOH   A O    1 
HETATM 7067 O  O    . HOH   E 4 .   ? 30.753 -5.884  -11.873 1.00 52.56 ?  1502 HOH   A O    1 
HETATM 7068 O  O    B HOH   E 4 .   ? 14.783 8.304   5.107   0.38 18.22 ?  1503 HOH   A O    1 
HETATM 7069 O  O    . HOH   E 4 .   ? 37.465 -6.643  7.569   1.00 24.49 ?  1504 HOH   A O    1 
HETATM 7070 O  O    . HOH   E 4 .   ? 39.555 -0.060  6.590   1.00 32.11 ?  1505 HOH   A O    1 
HETATM 7071 O  O    . HOH   E 4 .   ? 28.970 14.446  0.849   1.00 49.61 ?  1506 HOH   A O    1 
HETATM 7072 O  O    B HOH   E 4 .   ? 8.904  5.011   7.853   0.38 24.89 ?  1507 HOH   A O    1 
HETATM 7073 O  O    B HOH   E 4 .   ? 10.373 -0.331  -1.269  0.38 22.80 ?  1508 HOH   A O    1 
HETATM 7074 O  O    . HOH   E 4 .   ? 37.987 14.006  6.676   1.00 40.67 ?  1509 HOH   A O    1 
HETATM 7075 O  O    B HOH   E 4 .   ? 7.503  5.829   5.748   0.38 25.58 ?  1510 HOH   A O    1 
HETATM 7076 O  O    . HOH   E 4 .   ? 8.273  -2.979  -5.701  1.00 54.41 ?  1511 HOH   A O    1 
HETATM 7077 O  O    . HOH   E 4 .   ? 36.577 -6.464  10.213  1.00 44.70 ?  1512 HOH   A O    1 
HETATM 7078 O  O    . HOH   E 4 .   ? 22.115 -24.086 4.485   1.00 26.43 ?  1513 HOH   A O    1 
HETATM 7079 O  O    B HOH   E 4 .   ? 5.758  6.756   1.637   0.38 33.06 ?  1514 HOH   A O    1 
HETATM 7080 O  O    . HOH   E 4 .   ? 17.461 -6.811  -14.163 1.00 43.97 ?  1515 HOH   A O    1 
HETATM 7081 O  O    A HOH   E 4 .   ? 14.876 8.603   4.885   0.62 33.24 ?  1516 HOH   A O    1 
HETATM 7082 O  O    . HOH   E 4 .   ? 24.132 9.189   -7.187  1.00 40.35 ?  1517 HOH   A O    1 
HETATM 7083 O  O    . HOH   E 4 .   ? 16.259 -21.159 18.725  1.00 43.43 ?  1518 HOH   A O    1 
HETATM 7084 O  O    . HOH   E 4 .   ? 15.817 -12.456 27.487  1.00 44.69 ?  1519 HOH   A O    1 
HETATM 7085 O  O    B HOH   E 4 .   ? 8.353  7.254   2.379   0.38 27.50 ?  1520 HOH   A O    1 
HETATM 7086 O  O    . HOH   E 4 .   ? 14.708 -22.769 19.823  1.00 35.31 ?  1521 HOH   A O    1 
HETATM 7087 O  O    . HOH   F 4 .   ? 29.944 -22.451 5.528   1.00 18.83 ?  201  HOH   B O    1 
HETATM 7088 O  O    . HOH   F 4 .   ? 41.654 -36.029 -17.222 1.00 33.66 ?  202  HOH   B O    1 
HETATM 7089 O  O    . HOH   F 4 .   ? 27.741 -29.146 -1.817  1.00 36.41 ?  203  HOH   B O    1 
HETATM 7090 O  O    . HOH   F 4 .   ? 27.896 -41.739 -15.192 1.00 37.68 ?  204  HOH   B O    1 
HETATM 7091 O  O    . HOH   F 4 .   ? 59.243 -18.651 6.841   1.00 36.60 ?  205  HOH   B O    1 
HETATM 7092 O  O    . HOH   F 4 .   ? 49.380 -22.768 -19.796 1.00 51.98 ?  206  HOH   B O    1 
HETATM 7093 O  O    . HOH   F 4 .   ? 38.126 -39.495 -0.158  1.00 40.68 ?  207  HOH   B O    1 
HETATM 7094 O  O    . HOH   F 4 .   ? 48.157 -6.950  15.515  1.00 31.47 ?  208  HOH   B O    1 
HETATM 7095 O  O    . HOH   F 4 .   ? 53.060 -13.453 -20.305 1.00 33.50 ?  209  HOH   B O    1 
HETATM 7096 O  O    . HOH   F 4 .   ? 54.559 -9.413  -8.746  1.00 19.08 ?  210  HOH   B O    1 
HETATM 7097 O  O    . HOH   F 4 .   ? 31.043 -28.784 4.390   1.00 28.21 ?  211  HOH   B O    1 
HETATM 7098 O  O    . HOH   F 4 .   ? 57.801 -24.535 5.066   1.00 39.66 ?  212  HOH   B O    1 
HETATM 7099 O  O    . HOH   F 4 .   ? 30.056 -26.329 4.129   1.00 25.48 ?  213  HOH   B O    1 
HETATM 7100 O  O    . HOH   F 4 .   ? 41.378 -7.839  5.469   1.00 40.14 ?  214  HOH   B O    1 
HETATM 7101 O  O    . HOH   F 4 .   ? 30.256 -41.023 -8.100  1.00 16.45 ?  215  HOH   B O    1 
HETATM 7102 O  O    . HOH   F 4 .   ? 58.336 -12.977 8.350   1.00 28.22 ?  216  HOH   B O    1 
HETATM 7103 O  O    . HOH   F 4 .   ? 47.475 -7.353  -3.883  1.00 40.69 ?  217  HOH   B O    1 
HETATM 7104 O  O    . HOH   F 4 .   ? 55.474 -16.534 -14.360 1.00 34.37 ?  218  HOH   B O    1 
HETATM 7105 O  O    . HOH   F 4 .   ? 26.567 -19.367 -1.718  1.00 13.99 ?  219  HOH   B O    1 
HETATM 7106 O  O    . HOH   F 4 .   ? 50.263 -3.448  7.071   1.00 33.72 ?  220  HOH   B O    1 
HETATM 7107 O  O    . HOH   F 4 .   ? 44.561 -7.191  2.025   1.00 38.21 ?  221  HOH   B O    1 
HETATM 7108 O  O    . HOH   F 4 .   ? 56.498 -19.798 7.058   1.00 28.85 ?  222  HOH   B O    1 
HETATM 7109 O  O    . HOH   F 4 .   ? 56.770 -30.797 -7.799  1.00 30.90 ?  223  HOH   B O    1 
HETATM 7110 O  O    . HOH   F 4 .   ? 41.537 -39.190 -14.948 1.00 21.34 ?  224  HOH   B O    1 
HETATM 7111 O  O    . HOH   F 4 .   ? 34.586 -36.398 -7.206  1.00 18.19 ?  225  HOH   B O    1 
HETATM 7112 O  O    . HOH   F 4 .   ? 57.489 -16.282 -12.236 1.00 17.74 ?  226  HOH   B O    1 
HETATM 7113 O  O    . HOH   F 4 .   ? 40.611 -16.131 14.048  1.00 24.22 ?  227  HOH   B O    1 
HETATM 7114 O  O    . HOH   F 4 .   ? 48.664 -36.558 -15.572 1.00 43.23 ?  228  HOH   B O    1 
HETATM 7115 O  O    . HOH   F 4 .   ? 50.856 -6.092  0.164   1.00 27.16 ?  229  HOH   B O    1 
HETATM 7116 O  O    . HOH   F 4 .   ? 37.147 -19.735 -18.105 1.00 44.57 ?  230  HOH   B O    1 
HETATM 7117 O  O    . HOH   F 4 .   ? 41.466 -9.643  13.039  1.00 21.27 ?  231  HOH   B O    1 
HETATM 7118 O  O    . HOH   F 4 .   ? 44.984 -43.578 -10.617 1.00 26.72 ?  232  HOH   B O    1 
HETATM 7119 O  O    . HOH   F 4 .   ? 43.119 -43.263 -8.241  1.00 28.34 ?  233  HOH   B O    1 
HETATM 7120 O  O    . HOH   F 4 .   ? 35.180 -8.031  -2.975  1.00 17.78 ?  234  HOH   B O    1 
HETATM 7121 O  O    . HOH   F 4 .   ? 51.732 -6.514  4.372   1.00 19.84 ?  235  HOH   B O    1 
HETATM 7122 O  O    . HOH   F 4 .   ? 46.459 -1.577  13.182  1.00 27.23 ?  236  HOH   B O    1 
HETATM 7123 O  O    . HOH   F 4 .   ? 25.446 -25.914 -1.273  1.00 34.36 ?  237  HOH   B O    1 
HETATM 7124 O  O    . HOH   F 4 .   ? 39.426 -10.866 6.117   1.00 22.69 ?  238  HOH   B O    1 
HETATM 7125 O  O    . HOH   F 4 .   ? 29.840 -34.121 -0.431  1.00 34.88 ?  239  HOH   B O    1 
HETATM 7126 O  O    . HOH   F 4 .   ? 35.005 -24.640 13.852  1.00 31.59 ?  240  HOH   B O    1 
HETATM 7127 O  O    . HOH   F 4 .   ? 32.769 -43.763 -11.370 1.00 21.33 ?  241  HOH   B O    1 
HETATM 7128 O  O    . HOH   F 4 .   ? 57.239 -26.842 -7.667  1.00 40.47 ?  242  HOH   B O    1 
HETATM 7129 O  O    . HOH   F 4 .   ? 28.486 -19.677 -13.120 1.00 24.01 ?  243  HOH   B O    1 
HETATM 7130 O  O    . HOH   F 4 .   ? 41.971 -23.564 9.312   1.00 17.40 ?  244  HOH   B O    1 
HETATM 7131 O  O    . HOH   F 4 .   ? 42.744 -22.885 3.868   1.00 11.32 ?  245  HOH   B O    1 
HETATM 7132 O  O    . HOH   F 4 .   ? 58.270 -10.645 -4.068  1.00 20.04 ?  246  HOH   B O    1 
HETATM 7133 O  O    . HOH   F 4 .   ? 43.203 -32.392 -17.134 1.00 23.54 ?  247  HOH   B O    1 
HETATM 7134 O  O    . HOH   F 4 .   ? 57.736 -24.380 -3.835  1.00 21.19 ?  248  HOH   B O    1 
HETATM 7135 O  O    . HOH   F 4 .   ? 42.666 -25.399 2.669   1.00 14.63 ?  249  HOH   B O    1 
HETATM 7136 O  O    . HOH   F 4 .   ? 39.612 -11.152 0.325   1.00 16.62 ?  250  HOH   B O    1 
HETATM 7137 O  O    . HOH   F 4 .   ? 44.617 -27.818 -0.692  1.00 21.77 ?  251  HOH   B O    1 
HETATM 7138 O  O    . HOH   F 4 .   ? 40.426 -12.777 -11.508 1.00 14.69 ?  252  HOH   B O    1 
HETATM 7139 O  O    . HOH   F 4 .   ? 50.846 -13.003 -0.464  1.00 11.72 ?  253  HOH   B O    1 
HETATM 7140 O  O    . HOH   F 4 .   ? 45.219 -35.033 6.806   1.00 37.58 ?  254  HOH   B O    1 
HETATM 7141 O  O    . HOH   F 4 .   ? 34.403 -18.464 11.486  1.00 25.20 ?  255  HOH   B O    1 
HETATM 7142 O  O    . HOH   F 4 .   ? 38.529 -11.079 -2.235  1.00 18.54 ?  256  HOH   B O    1 
HETATM 7143 O  O    . HOH   F 4 .   ? 36.112 -43.429 -8.463  1.00 38.99 ?  257  HOH   B O    1 
HETATM 7144 O  O    . HOH   F 4 .   ? 28.531 -30.859 -14.791 1.00 29.42 ?  258  HOH   B O    1 
HETATM 7145 O  O    . HOH   F 4 .   ? 29.767 -25.209 -10.740 1.00 16.20 ?  259  HOH   B O    1 
HETATM 7146 O  O    . HOH   F 4 .   ? 39.033 -11.946 12.324  1.00 34.95 ?  260  HOH   B O    1 
HETATM 7147 O  O    . HOH   F 4 .   ? 31.859 -17.945 -14.477 1.00 29.16 ?  261  HOH   B O    1 
HETATM 7148 O  O    . HOH   F 4 .   ? 51.035 -39.996 -8.316  1.00 32.98 ?  262  HOH   B O    1 
HETATM 7149 O  O    . HOH   F 4 .   ? 30.509 -42.278 -10.660 1.00 30.00 ?  263  HOH   B O    1 
HETATM 7150 O  O    . HOH   F 4 .   ? 46.974 -29.622 9.789   1.00 32.29 ?  264  HOH   B O    1 
HETATM 7151 O  O    . HOH   F 4 .   ? 30.940 -15.745 2.708   1.00 13.41 ?  265  HOH   B O    1 
HETATM 7152 O  O    . HOH   F 4 .   ? 57.059 -8.651  8.375   1.00 19.07 ?  266  HOH   B O    1 
HETATM 7153 O  O    . HOH   F 4 .   ? 41.251 -5.590  11.524  1.00 49.40 ?  267  HOH   B O    1 
HETATM 7154 O  O    . HOH   F 4 .   ? 48.132 -22.782 5.835   1.00 16.38 ?  268  HOH   B O    1 
HETATM 7155 O  O    . HOH   F 4 .   ? 51.636 -13.836 11.014  1.00 25.61 ?  269  HOH   B O    1 
HETATM 7156 O  O    . HOH   F 4 .   ? 34.983 -33.282 -19.221 1.00 29.32 ?  270  HOH   B O    1 
HETATM 7157 O  O    . HOH   F 4 .   ? 57.606 -9.254  1.399   1.00 18.97 ?  271  HOH   B O    1 
HETATM 7158 O  O    . HOH   F 4 .   ? 49.365 -28.745 -6.952  1.00 15.30 ?  272  HOH   B O    1 
HETATM 7159 O  O    . HOH   F 4 .   ? 34.590 -12.837 2.689   1.00 25.93 ?  273  HOH   B O    1 
HETATM 7160 O  O    . HOH   F 4 .   ? 56.242 -23.541 -14.743 1.00 26.90 ?  274  HOH   B O    1 
HETATM 7161 O  O    . HOH   F 4 .   ? 42.884 -20.213 -20.699 1.00 40.76 ?  275  HOH   B O    1 
HETATM 7162 O  O    . HOH   F 4 .   ? 42.459 -9.949  9.330   1.00 20.01 ?  276  HOH   B O    1 
HETATM 7163 O  O    . HOH   F 4 .   ? 46.688 -31.279 -4.848  1.00 20.49 ?  277  HOH   B O    1 
HETATM 7164 O  O    . HOH   F 4 .   ? 49.803 -0.506  10.214  1.00 30.68 ?  278  HOH   B O    1 
HETATM 7165 O  O    . HOH   F 4 .   ? 43.472 -15.804 -12.177 1.00 14.14 ?  279  HOH   B O    1 
HETATM 7166 O  O    . HOH   F 4 .   ? 42.509 -34.711 3.811   1.00 24.44 ?  280  HOH   B O    1 
HETATM 7167 O  O    . HOH   F 4 .   ? 27.178 -31.815 -9.973  1.00 19.60 ?  281  HOH   B O    1 
HETATM 7168 O  O    . HOH   F 4 .   ? 28.315 -34.341 -9.404  1.00 18.81 ?  282  HOH   B O    1 
HETATM 7169 O  O    . HOH   F 4 .   ? 28.019 -22.904 -7.954  1.00 16.93 ?  283  HOH   B O    1 
HETATM 7170 O  O    . HOH   F 4 .   ? 57.254 -12.102 12.314  1.00 36.94 ?  284  HOH   B O    1 
HETATM 7171 O  O    . HOH   F 4 .   ? 48.499 -25.082 3.091   1.00 13.15 ?  285  HOH   B O    1 
HETATM 7172 O  O    . HOH   F 4 .   ? 48.827 -20.041 5.922   1.00 13.43 ?  286  HOH   B O    1 
HETATM 7173 O  O    . HOH   F 4 .   ? 52.647 -10.379 12.959  1.00 21.22 ?  287  HOH   B O    1 
HETATM 7174 O  O    . HOH   F 4 .   ? 47.143 -34.016 -4.693  1.00 17.64 ?  288  HOH   B O    1 
HETATM 7175 O  O    . HOH   F 4 .   ? 36.938 -12.787 -1.485  1.00 26.80 ?  289  HOH   B O    1 
HETATM 7176 O  O    . HOH   F 4 .   ? 33.586 -15.324 -13.934 1.00 20.86 ?  290  HOH   B O    1 
HETATM 7177 O  O    . HOH   F 4 .   ? 45.782 -36.311 -16.124 1.00 37.59 ?  291  HOH   B O    1 
HETATM 7178 O  O    . HOH   F 4 .   ? 27.624 -26.757 -15.615 1.00 33.23 ?  292  HOH   B O    1 
HETATM 7179 O  O    . HOH   F 4 .   ? 51.283 -37.592 -9.672  1.00 25.27 ?  293  HOH   B O    1 
HETATM 7180 O  O    . HOH   F 4 .   ? 42.823 -12.202 -18.466 1.00 27.49 ?  294  HOH   B O    1 
HETATM 7181 O  O    . HOH   F 4 .   ? 51.754 -5.954  -7.909  1.00 46.79 ?  295  HOH   B O    1 
HETATM 7182 O  O    . HOH   F 4 .   ? 45.376 -33.379 -16.027 1.00 23.03 ?  296  HOH   B O    1 
HETATM 7183 O  O    . HOH   F 4 .   ? 47.915 -24.478 -17.884 1.00 33.67 ?  297  HOH   B O    1 
HETATM 7184 O  O    . HOH   F 4 .   ? 44.712 -27.508 2.017   1.00 14.90 ?  298  HOH   B O    1 
HETATM 7185 O  O    . HOH   F 4 .   ? 59.905 -15.381 8.171   1.00 30.68 ?  299  HOH   B O    1 
HETATM 7186 O  O    . HOH   F 4 .   ? 40.337 -10.860 -9.479  1.00 17.04 ?  300  HOH   B O    1 
HETATM 7187 O  O    . HOH   F 4 .   ? 42.420 -9.882  -14.878 1.00 34.93 ?  301  HOH   B O    1 
HETATM 7188 O  O    . HOH   F 4 .   ? 52.566 -29.250 -13.079 1.00 24.80 ?  302  HOH   B O    1 
HETATM 7189 O  O    . HOH   F 4 .   ? 26.018 -21.515 -3.446  1.00 16.85 ?  303  HOH   B O    1 
HETATM 7190 O  O    . HOH   F 4 .   ? 52.672 -35.671 -8.786  1.00 30.76 ?  304  HOH   B O    1 
HETATM 7191 O  O    . HOH   F 4 .   ? 35.162 -33.681 4.550   1.00 31.69 ?  305  HOH   B O    1 
HETATM 7192 O  O    . HOH   F 4 .   ? 53.527 -30.247 4.492   1.00 18.63 ?  306  HOH   B O    1 
HETATM 7193 O  O    . HOH   F 4 .   ? 62.806 -13.580 4.741   1.00 27.67 ?  307  HOH   B O    1 
HETATM 7194 O  O    . HOH   F 4 .   ? 53.165 -16.031 -12.736 1.00 26.76 ?  308  HOH   B O    1 
HETATM 7195 O  O    . HOH   F 4 .   ? 37.585 -18.067 13.164  1.00 30.42 ?  309  HOH   B O    1 
HETATM 7196 O  O    . HOH   F 4 .   ? 44.085 -29.393 -4.670  1.00 21.94 ?  310  HOH   B O    1 
HETATM 7197 O  O    . HOH   F 4 .   ? 41.858 -8.092  1.340   1.00 22.67 ?  311  HOH   B O    1 
HETATM 7198 O  O    . HOH   F 4 .   ? 37.928 -10.242 -10.703 1.00 17.26 ?  312  HOH   B O    1 
HETATM 7199 O  O    . HOH   F 4 .   ? 62.949 -20.158 -0.831  1.00 40.89 ?  313  HOH   B O    1 
HETATM 7200 O  O    . HOH   F 4 .   ? 45.934 -40.437 -3.652  1.00 29.42 ?  314  HOH   B O    1 
HETATM 7201 O  O    . HOH   F 4 .   ? 37.091 -30.590 -21.012 1.00 30.22 ?  315  HOH   B O    1 
HETATM 7202 O  O    . HOH   F 4 .   ? 50.104 -24.621 5.888   1.00 36.52 ?  316  HOH   B O    1 
HETATM 7203 O  O    . HOH   F 4 .   ? 43.332 -21.450 10.708  1.00 15.22 ?  317  HOH   B O    1 
HETATM 7204 O  O    . HOH   F 4 .   ? 38.423 -12.709 7.986   1.00 17.37 ?  318  HOH   B O    1 
HETATM 7205 O  O    . HOH   F 4 .   ? 32.886 -34.611 -5.887  1.00 16.38 ?  319  HOH   B O    1 
HETATM 7206 O  O    . HOH   F 4 .   ? 43.631 -15.377 18.126  1.00 28.73 ?  320  HOH   B O    1 
HETATM 7207 O  O    . HOH   F 4 .   ? 53.738 -12.546 -22.268 1.00 34.69 ?  321  HOH   B O    1 
HETATM 7208 O  O    . HOH   F 4 .   ? 26.418 -21.082 -6.208  1.00 16.34 ?  322  HOH   B O    1 
HETATM 7209 O  O    . HOH   F 4 .   ? 51.469 -33.025 -10.886 1.00 41.37 ?  323  HOH   B O    1 
HETATM 7210 O  O    . HOH   F 4 .   ? 37.360 -35.705 7.280   1.00 34.05 ?  324  HOH   B O    1 
HETATM 7211 O  O    . HOH   F 4 .   ? 38.459 -9.363  -13.269 1.00 29.44 ?  325  HOH   B O    1 
HETATM 7212 O  O    . HOH   F 4 .   ? 48.125 -32.684 -16.721 1.00 43.79 ?  326  HOH   B O    1 
HETATM 7213 O  O    . HOH   F 4 .   ? 44.751 -24.627 9.604   1.00 19.87 ?  327  HOH   B O    1 
HETATM 7214 O  O    . HOH   F 4 .   ? 43.219 -34.588 0.064   1.00 21.95 ?  328  HOH   B O    1 
HETATM 7215 O  O    . HOH   F 4 .   ? 36.822 -12.418 4.308   1.00 18.12 ?  329  HOH   B O    1 
HETATM 7216 O  O    . HOH   F 4 .   ? 33.794 -31.160 11.113  1.00 36.56 ?  330  HOH   B O    1 
HETATM 7217 O  O    . HOH   F 4 .   ? 57.620 -21.975 3.370   1.00 31.13 ?  331  HOH   B O    1 
HETATM 7218 O  O    . HOH   F 4 .   ? 47.314 -24.493 8.180   1.00 25.75 ?  332  HOH   B O    1 
HETATM 7219 O  O    . HOH   F 4 .   ? 48.688 -12.004 -14.134 1.00 26.94 ?  333  HOH   B O    1 
HETATM 7220 O  O    . HOH   F 4 .   ? 60.001 -17.288 -10.570 1.00 35.76 ?  334  HOH   B O    1 
HETATM 7221 O  O    . HOH   F 4 .   ? 41.382 -24.513 15.835  1.00 43.72 ?  335  HOH   B O    1 
HETATM 7222 O  O    . HOH   F 4 .   ? 42.910 -43.525 -14.396 1.00 46.62 ?  336  HOH   B O    1 
HETATM 7223 O  O    . HOH   F 4 .   ? 44.234 -1.707  7.603   1.00 48.57 ?  337  HOH   B O    1 
HETATM 7224 O  O    . HOH   F 4 .   ? 47.566 -27.469 2.000   1.00 14.52 ?  338  HOH   B O    1 
HETATM 7225 O  O    . HOH   F 4 .   ? 27.722 -14.741 -9.509  1.00 37.58 ?  339  HOH   B O    1 
HETATM 7226 O  O    . HOH   F 4 .   ? 28.913 -42.849 -12.370 1.00 39.21 ?  340  HOH   B O    1 
HETATM 7227 O  O    . HOH   F 4 .   ? 37.165 -15.161 -16.566 1.00 39.43 ?  341  HOH   B O    1 
HETATM 7228 O  O    . HOH   F 4 .   ? 46.944 -19.954 12.278  1.00 30.66 ?  342  HOH   B O    1 
HETATM 7229 O  O    . HOH   F 4 .   ? 39.661 -23.552 -20.375 1.00 38.61 ?  343  HOH   B O    1 
HETATM 7230 O  O    . HOH   F 4 .   ? 37.091 -45.194 -9.726  1.00 37.86 ?  344  HOH   B O    1 
HETATM 7231 O  O    . HOH   F 4 .   ? 34.613 -10.357 7.657   1.00 23.06 ?  345  HOH   B O    1 
HETATM 7232 O  O    . HOH   F 4 .   ? 38.505 -12.237 -16.273 1.00 47.16 ?  346  HOH   B O    1 
HETATM 7233 O  O    . HOH   F 4 .   ? 39.857 -44.240 -11.212 1.00 44.78 ?  347  HOH   B O    1 
HETATM 7234 O  O    . HOH   F 4 .   ? 33.068 -14.703 1.074   1.00 20.52 ?  348  HOH   B O    1 
HETATM 7235 O  O    . HOH   F 4 .   ? 44.172 -37.364 -17.848 1.00 34.83 ?  349  HOH   B O    1 
HETATM 7236 O  O    . HOH   F 4 .   ? 33.706 -9.742  -8.792  1.00 30.61 ?  350  HOH   B O    1 
HETATM 7237 O  O    . HOH   F 4 .   ? 40.431 -43.500 -9.149  1.00 27.34 ?  351  HOH   B O    1 
HETATM 7238 O  O    . HOH   F 4 .   ? 38.631 -22.359 15.067  1.00 42.29 ?  352  HOH   B O    1 
HETATM 7239 O  O    . HOH   F 4 .   ? 27.861 -26.641 -0.543  1.00 29.41 ?  353  HOH   B O    1 
HETATM 7240 O  O    . HOH   F 4 .   ? 62.647 -20.114 -4.872  1.00 47.47 ?  354  HOH   B O    1 
HETATM 7241 O  O    . HOH   F 4 .   ? 55.748 -8.257  10.769  1.00 24.46 ?  355  HOH   B O    1 
HETATM 7242 O  O    . HOH   F 4 .   ? 23.350 -23.728 6.846   1.00 35.02 ?  356  HOH   B O    1 
HETATM 7243 O  O    . HOH   F 4 .   ? 56.733 -7.307  2.994   1.00 27.14 ?  357  HOH   B O    1 
HETATM 7244 O  O    . HOH   F 4 .   ? 43.272 -12.741 -21.220 1.00 42.96 ?  358  HOH   B O    1 
HETATM 7245 O  O    . HOH   F 4 .   ? 34.043 -7.813  11.509  1.00 41.64 ?  359  HOH   B O    1 
HETATM 7246 O  O    . HOH   F 4 .   ? 61.565 -19.873 1.665   1.00 36.80 ?  360  HOH   B O    1 
HETATM 7247 O  O    . HOH   F 4 .   ? 36.275 -8.493  -9.729  1.00 34.96 ?  361  HOH   B O    1 
HETATM 7248 O  O    . HOH   F 4 .   ? 56.958 -21.544 -16.451 1.00 40.74 ?  362  HOH   B O    1 
HETATM 7249 O  O    . HOH   F 4 .   ? 27.239 -25.957 -11.345 1.00 33.51 ?  363  HOH   B O    1 
HETATM 7250 O  O    . HOH   F 4 .   ? 40.305 -8.875  9.866   1.00 36.67 ?  364  HOH   B O    1 
HETATM 7251 O  O    . HOH   F 4 .   ? 40.340 -11.344 -13.909 1.00 33.01 ?  365  HOH   B O    1 
HETATM 7252 O  O    . HOH   F 4 .   ? 32.655 -23.589 14.004  1.00 41.36 ?  366  HOH   B O    1 
HETATM 7253 O  O    . HOH   F 4 .   ? 54.274 -5.782  2.924   1.00 38.79 ?  367  HOH   B O    1 
HETATM 7254 O  O    . HOH   F 4 .   ? 59.118 -10.511 9.142   1.00 44.17 ?  368  HOH   B O    1 
HETATM 7255 O  O    . HOH   F 4 .   ? 36.275 -8.691  8.973   1.00 36.82 ?  369  HOH   B O    1 
HETATM 7256 O  O    . HOH   F 4 .   ? 48.470 -26.479 8.747   1.00 39.80 ?  370  HOH   B O    1 
HETATM 7257 O  O    . HOH   F 4 .   ? 39.895 -7.096  7.800   1.00 39.41 ?  371  HOH   B O    1 
HETATM 7258 O  O    . HOH   F 4 .   ? 52.157 -12.910 13.271  1.00 28.84 ?  372  HOH   B O    1 
HETATM 7259 O  O    . HOH   F 4 .   ? 56.112 -7.821  -0.623  1.00 35.22 ?  373  HOH   B O    1 
HETATM 7260 O  O    . HOH   F 4 .   ? 41.864 -9.982  -17.425 1.00 55.01 ?  374  HOH   B O    1 
HETATM 7261 O  O    . HOH   F 4 .   ? 41.891 -6.800  -4.912  1.00 47.10 ?  375  HOH   B O    1 
HETATM 7262 O  O    . HOH   F 4 .   ? 63.130 -12.381 7.006   1.00 36.40 ?  376  HOH   B O    1 
HETATM 7263 O  O    . HOH   F 4 .   ? 36.608 -22.889 13.288  1.00 26.39 ?  377  HOH   B O    1 
HETATM 7264 O  O    . HOH   F 4 .   ? 44.162 -5.653  -3.536  1.00 39.80 ?  378  HOH   B O    1 
HETATM 7265 O  O    . HOH   F 4 .   ? 38.130 -10.517 10.023  1.00 27.62 ?  379  HOH   B O    1 
HETATM 7266 O  O    . HOH   F 4 .   ? 42.771 -17.149 -23.165 1.00 43.81 ?  380  HOH   B O    1 
HETATM 7267 O  O    . HOH   F 4 .   ? 40.240 -7.678  3.154   1.00 39.23 ?  381  HOH   B O    1 
HETATM 7268 O  O    . HOH   F 4 .   ? 39.670 -14.089 15.626  1.00 50.16 ?  382  HOH   B O    1 
HETATM 7269 O  O    . HOH   F 4 .   ? 52.951 -29.936 7.192   1.00 22.62 ?  383  HOH   B O    1 
HETATM 7270 O  O    . HOH   F 4 .   ? 60.544 -22.341 2.841   1.00 50.83 ?  384  HOH   B O    1 
HETATM 7271 O  O    . HOH   F 4 .   ? 46.907 -5.400  2.940   1.00 42.30 ?  385  HOH   B O    1 
HETATM 7272 O  O    . HOH   F 4 .   ? 41.104 -9.740  15.816  1.00 46.68 ?  386  HOH   B O    1 
HETATM 7273 O  O    . HOH   F 4 .   ? 25.856 -18.987 -11.849 1.00 39.13 ?  387  HOH   B O    1 
HETATM 7274 O  O    . HOH   F 4 .   ? 23.995 -20.937 -7.635  1.00 27.54 ?  388  HOH   B O    1 
HETATM 7275 O  O    . HOH   F 4 .   ? 35.518 -33.733 7.398   1.00 43.03 ?  389  HOH   B O    1 
HETATM 7276 O  O    . HOH   F 4 .   ? 35.332 -20.412 13.328  1.00 31.89 ?  390  HOH   B O    1 
HETATM 7277 O  O    . HOH   F 4 .   ? 23.388 -23.900 1.680   1.00 31.13 ?  391  HOH   B O    1 
HETATM 7278 O  O    . HOH   F 4 .   ? 40.817 -6.634  -0.787  1.00 25.82 ?  392  HOH   B O    1 
HETATM 7279 O  O    . HOH   F 4 .   ? 44.198 -31.773 -3.850  1.00 35.45 ?  393  HOH   B O    1 
HETATM 7280 O  O    . HOH   F 4 .   ? 28.061 -27.095 2.356   1.00 29.64 ?  394  HOH   B O    1 
HETATM 7281 O  O    . HOH   F 4 .   ? 26.652 -27.927 -13.401 1.00 36.63 ?  395  HOH   B O    1 
HETATM 7282 O  O    . HOH   F 4 .   ? 24.693 -20.603 -10.460 1.00 37.84 ?  396  HOH   B O    1 
HETATM 7283 O  O    . HOH   F 4 .   ? 50.727 -30.929 8.697   1.00 29.09 ?  397  HOH   B O    1 
HETATM 7284 O  O    . HOH   F 4 .   ? 34.471 -33.513 9.648   1.00 34.41 ?  398  HOH   B O    1 
HETATM 7285 O  O    . HOH   F 4 .   ? 26.859 -30.612 -12.637 1.00 27.99 ?  399  HOH   B O    1 
HETATM 7286 O  O    . HOH   F 4 .   ? 57.703 -6.496  -2.345  1.00 33.08 ?  400  HOH   B O    1 
HETATM 7287 O  O    . HOH   F 4 .   ? 45.765 -20.087 15.284  1.00 49.38 ?  401  HOH   B O    1 
HETATM 7288 O  O    . HOH   F 4 .   ? 40.933 -11.819 -22.313 1.00 42.02 ?  402  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   ? 0.6849 0.6735 0.7865 0.0149  -0.0271 0.0933  3    VAL   A N   
2    N  N   B VAL   A 3   ? 0.6639 0.6557 0.7539 0.0047  -0.0205 0.0547  3    VAL   A N   
3    C  CA  A VAL   A 3   ? 0.6823 0.6712 0.7772 0.0131  -0.0260 0.0928  3    VAL   A CA  
4    C  CA  B VAL   A 3   ? 0.6613 0.6533 0.7453 0.0034  -0.0198 0.0546  3    VAL   A CA  
5    C  C   A VAL   A 3   ? 0.6677 0.6597 0.7422 0.0061  -0.0268 0.0958  3    VAL   A C   
6    C  C   B VAL   A 3   ? 0.6470 0.6423 0.7128 -0.0020 -0.0203 0.0561  3    VAL   A C   
7    O  O   A VAL   A 3   ? 0.6703 0.6620 0.7534 0.0074  -0.0292 0.0987  3    VAL   A O   
8    O  O   B VAL   A 3   ? 0.6496 0.6445 0.7211 -0.0010 -0.0218 0.0575  3    VAL   A O   
9    C  CB  A VAL   A 3   ? 0.6916 0.6783 0.7948 0.0166  -0.0233 0.0898  3    VAL   A CB  
10   C  CB  B VAL   A 3   ? 0.6704 0.6601 0.7620 0.0064  -0.0182 0.0532  3    VAL   A CB  
11   C  CG1 A VAL   A 3   ? 0.6946 0.6805 0.7999 0.0179  -0.0225 0.0889  3    VAL   A CG1 
12   C  CG1 B VAL   A 3   ? 0.6734 0.6621 0.7671 0.0074  -0.0177 0.0527  3    VAL   A CG1 
13   C  CG2 A VAL   A 3   ? 0.6945 0.6807 0.8001 0.0178  -0.0221 0.0892  3    VAL   A CG2 
14   C  CG2 B VAL   A 3   ? 0.6734 0.6623 0.7674 0.0075  -0.0175 0.0531  3    VAL   A CG2 
31   N  N   A ASN   A 4   ? 0.6481 0.6439 0.6865 -0.0031 -0.0232 0.0947  4    ASN   A N   
32   N  N   B ASN   A 4   ? 0.6279 0.6273 0.6649 -0.0093 -0.0179 0.0555  4    ASN   A N   
33   C  CA  A ASN   A 4   ? 0.6260 0.6260 0.6238 -0.0129 -0.0181 0.0914  4    ASN   A CA  
34   C  CA  B ASN   A 4   ? 0.6065 0.6104 0.6117 -0.0171 -0.0142 0.0535  4    ASN   A CA  
35   C  C   A ASN   A 4   ? 0.5910 0.6029 0.5832 -0.0269 -0.0020 0.0714  4    ASN   A C   
36   C  C   B ASN   A 4   ? 0.5744 0.5890 0.5765 -0.0286 -0.0006 0.0432  4    ASN   A C   
37   O  O   A ASN   A 4   ? 0.5930 0.6045 0.5853 -0.0280 -0.0026 0.0722  4    ASN   A O   
38   O  O   B ASN   A 4   ? 0.5761 0.5905 0.5791 -0.0289 -0.0012 0.0441  4    ASN   A O   
39   C  CB  A ASN   A 4   ? 0.6358 0.6291 0.5955 -0.0095 -0.0278 0.1066  4    ASN   A CB  
40   C  CB  B ASN   A 4   ? 0.6146 0.6132 0.5893 -0.0141 -0.0230 0.0610  4    ASN   A CB  
41   C  CG  A ASN   A 4   ? 0.6431 0.6308 0.5678 -0.0069 -0.0362 0.1199  4    ASN   A CG  
42   C  CG  B ASN   A 4   ? 0.6207 0.6148 0.5679 -0.0120 -0.0303 0.0674  4    ASN   A CG  
43   O  OD1 A ASN   A 4   ? 0.6464 0.6316 0.5570 -0.0062 -0.0397 0.1244  4    ASN   A OD1 
44   O  OD1 B ASN   A 4   ? 0.6233 0.6153 0.5598 -0.0113 -0.0333 0.0696  4    ASN   A OD1 
45   N  ND2 A ASN   A 4   ? 0.6450 0.6311 0.5610 -0.0056 -0.0389 0.1257  4    ASN   A ND2 
46   N  ND2 B ASN   A 4   ? 0.6224 0.6152 0.5628 -0.0110 -0.0327 0.0704  4    ASN   A ND2 
59   N  N   A SER   A 5   ? 0.5511 0.5750 0.5335 -0.0405 0.0147  0.0511  5    SER   A N   
60   N  N   B SER   A 5   ? 0.5382 0.5637 0.5335 -0.0405 0.0141  0.0322  5    SER   A N   
61   C  CA  A SER   A 5   ? 0.5098 0.5457 0.4842 -0.0535 0.0337  0.0319  5    SER   A CA  
62   C  CA  B SER   A 5   ? 0.5007 0.5371 0.4891 -0.0522 0.0311  0.0224  5    SER   A CA  
63   C  C   A SER   A 5   ? 0.4636 0.5075 0.4251 -0.0617 0.0506  0.0227  5    SER   A C   
64   C  C   B SER   A 5   ? 0.4587 0.5027 0.4336 -0.0617 0.0495  0.0197  5    SER   A C   
65   O  O   A SER   A 5   ? 0.4660 0.5111 0.4104 -0.0596 0.0531  0.0153  5    SER   A O   
66   O  O   B SER   A 5   ? 0.4608 0.5048 0.4294 -0.0615 0.0517  0.0149  5    SER   A O   
67   C  CB  A SER   A 5   ? 0.5141 0.5531 0.4983 -0.0573 0.0351  0.0246  5    SER   A CB  
68   C  CB  B SER   A 5   ? 0.5045 0.5430 0.5012 -0.0538 0.0297  0.0175  5    SER   A CB  
69   O  OG  A SER   A 5   ? 0.5163 0.5567 0.5063 -0.0592 0.0358  0.0203  5    SER   A OG  
70   O  OG  B SER   A 5   ? 0.5062 0.5462 0.5076 -0.0545 0.0288  0.0145  5    SER   A OG  
81   N  N   . PHE   A 6   ? 0.4138 0.4647 0.3790 -0.0714 0.0653  0.0251  6    PHE   A N   
82   C  CA  . PHE   A 6   ? 0.3243 0.3831 0.2933 -0.0845 0.0840  0.0391  6    PHE   A CA  
83   C  C   . PHE   A 6   ? 0.2986 0.3653 0.2970 -0.0849 0.1046  0.0326  6    PHE   A C   
84   O  O   . PHE   A 6   ? 0.3077 0.3702 0.3358 -0.0876 0.0984  0.0473  6    PHE   A O   
85   C  CB  . PHE   A 6   ? 0.2746 0.3270 0.2356 -0.0801 0.0622  0.0440  6    PHE   A CB  
86   C  CG  . PHE   A 6   ? 0.2391 0.2859 0.2063 -0.0676 0.0366  0.0438  6    PHE   A CG  
87   C  CD1 . PHE   A 6   ? 0.2271 0.2721 0.2061 -0.0574 0.0196  0.0454  6    PHE   A CD1 
88   C  CD2 . PHE   A 6   ? 0.2386 0.2732 0.2314 -0.0470 0.0287  0.0392  6    PHE   A CD2 
89   C  CE1 . PHE   A 6   ? 0.2221 0.2613 0.2165 -0.0537 0.0188  0.0526  6    PHE   A CE1 
90   C  CE2 . PHE   A 6   ? 0.2357 0.2657 0.2458 -0.0410 0.0253  0.0329  6    PHE   A CE2 
91   C  CZ  . PHE   A 6   ? 0.2272 0.2591 0.2312 -0.0455 0.0223  0.0374  6    PHE   A CZ  
102  N  N   A SER   A 7   ? 0.2798 0.3480 0.2695 -0.0864 0.1118  0.0261  7    SER   A N   
103  N  N   B SER   A 7   ? 0.2842 0.3542 0.2940 -0.0782 0.1086  0.0178  7    SER   A N   
104  C  CA  A SER   A 7   ? 0.2717 0.3403 0.2643 -0.0758 0.1041  0.0041  7    SER   A CA  
105  C  CA  B SER   A 7   ? 0.2763 0.3458 0.3034 -0.0665 0.1034  -0.0015 7    SER   A CA  
106  C  C   A SER   A 7   ? 0.2475 0.3027 0.2371 -0.0742 0.1118  -0.0033 7    SER   A C   
107  C  C   B SER   A 7   ? 0.2557 0.3208 0.2765 -0.0649 0.1087  -0.0047 7    SER   A C   
108  O  O   A SER   A 7   ? 0.2556 0.2936 0.2180 -0.0765 0.1139  -0.0093 7    SER   A O   
109  O  O   B SER   A 7   ? 0.2557 0.3192 0.2797 -0.0679 0.1103  -0.0045 7    SER   A O   
110  C  CB  A SER   A 7   ? 0.2911 0.3654 0.2853 -0.0610 0.0860  -0.0002 7    SER   A CB  
111  C  CB  B SER   A 7   ? 0.2900 0.3594 0.3369 -0.0546 0.0916  -0.0100 7    SER   A CB  
112  O  OG  A SER   A 7   ? 0.3035 0.3744 0.2989 -0.0522 0.0763  -0.0012 7    SER   A OG  
113  O  OG  B SER   A 7   ? 0.2984 0.3662 0.3636 -0.0469 0.0845  -0.0119 7    SER   A OG  
124  N  N   A GLY   A 8   ? 0.2255 0.2780 0.2473 -0.0698 0.0992  -0.0110 8    GLY   A N   
125  N  N   B GLY   A 8   ? 0.2384 0.2996 0.2536 -0.0628 0.1079  -0.0045 8    GLY   A N   
126  C  CA  A GLY   A 8   ? 0.2096 0.2551 0.2586 -0.0494 0.0859  -0.0097 8    GLY   A CA  
127  C  CA  B GLY   A 8   ? 0.2286 0.2795 0.2433 -0.0527 0.0905  -0.0040 8    GLY   A CA  
128  C  C   A GLY   A 8   ? 0.1871 0.2329 0.2542 -0.0329 0.0642  -0.0076 8    GLY   A C   
129  C  C   B GLY   A 8   ? 0.2118 0.2580 0.2234 -0.0483 0.0770  -0.0002 8    GLY   A C   
130  O  O   A GLY   A 8   ? 0.1855 0.2349 0.2823 -0.0223 0.0651  -0.0215 8    GLY   A O   
131  O  O   B GLY   A 8   ? 0.2123 0.2528 0.2380 -0.0469 0.0753  -0.0056 8    GLY   A O   
138  N  N   A TYR   A 9   ? 0.1675 0.2109 0.2197 -0.0210 0.0467  0.0118  9    TYR   A N   
139  N  N   B TYR   A 9   ? 0.1928 0.2409 0.2027 -0.0414 0.0591  0.0152  9    TYR   A N   
140  C  CA  A TYR   A 9   ? 0.1478 0.1869 0.1903 -0.0235 0.0343  0.0189  9    TYR   A CA  
141  C  CA  B TYR   A 9   ? 0.1747 0.2185 0.1931 -0.0315 0.0339  0.0281  9    TYR   A CA  
142  C  C   A TYR   A 9   ? 0.1444 0.1762 0.1942 -0.0204 0.0350  0.0444  9    TYR   A C   
143  C  C   B TYR   A 9   ? 0.1718 0.2051 0.1878 -0.0276 0.0236  0.0461  9    TYR   A C   
144  O  O   A TYR   A 9   ? 0.1635 0.2005 0.2248 -0.0195 0.0146  0.0393  9    TYR   A O   
145  O  O   B TYR   A 9   ? 0.1735 0.2113 0.1984 -0.0273 0.0102  0.0573  9    TYR   A O   
146  C  CB  A TYR   A 9   ? 0.1477 0.1872 0.1820 -0.0152 0.0231  0.0069  9    TYR   A CB  
147  C  CB  B TYR   A 9   ? 0.1619 0.2131 0.1910 -0.0232 0.0210  0.0180  9    TYR   A CB  
148  C  CG  A TYR   A 9   ? 0.1538 0.1905 0.1942 -0.0105 0.0356  -0.0155 9    TYR   A CG  
149  C  CG  B TYR   A 9   ? 0.1521 0.2043 0.1726 -0.0200 0.0251  0.0102  9    TYR   A CG  
150  C  CD1 A TYR   A 9   ? 0.1643 0.1974 0.2075 -0.0163 0.0459  -0.0279 9    TYR   A CD1 
151  C  CD1 B TYR   A 9   ? 0.1556 0.2035 0.1749 -0.0259 0.0322  0.0033  9    TYR   A CD1 
152  C  CD2 A TYR   A 9   ? 0.1571 0.1829 0.1986 -0.0101 0.0298  -0.0075 9    TYR   A CD2 
153  C  CD2 B TYR   A 9   ? 0.1462 0.1965 0.1619 -0.0135 0.0230  0.0112  9    TYR   A CD2 
154  C  CE1 A TYR   A 9   ? 0.1652 0.1995 0.2259 -0.0127 0.0479  -0.0352 9    TYR   A CE1 
155  C  CE1 B TYR   A 9   ? 0.1527 0.1953 0.1758 -0.0223 0.0379  -0.0060 9    TYR   A CE1 
156  C  CE2 A TYR   A 9   ? 0.1586 0.1853 0.2182 -0.0094 0.0394  -0.0160 9    TYR   A CE2 
157  C  CE2 B TYR   A 9   ? 0.1440 0.1928 0.1645 -0.0111 0.0346  0.0051  9    TYR   A CE2 
158  C  CZ  A TYR   A 9   ? 0.1612 0.1930 0.2390 -0.0191 0.0529  -0.0237 9    TYR   A CZ  
159  C  CZ  B TYR   A 9   ? 0.1465 0.1892 0.1851 -0.0163 0.0450  0.0025  9    TYR   A CZ  
160  O  OH  A TYR   A 9   ? 0.1736 0.1961 0.2632 -0.0283 0.0565  -0.0292 9    TYR   A OH  
161  O  OH  B TYR   A 9   ? 0.1480 0.1863 0.2062 -0.0158 0.0558  0.0052  9    TYR   A OH  
180  N  N   A LEU   A 10  ? 0.1428 0.1603 0.1921 -0.0181 0.0229  0.0349  10   LEU   A N   
181  N  N   B LEU   A 10  ? 0.1694 0.1893 0.1746 -0.0238 0.0167  0.0490  10   LEU   A N   
182  C  CA  A LEU   A 10  ? 0.1445 0.1574 0.1895 -0.0229 0.0280  0.0399  10   LEU   A CA  
183  C  CA  B LEU   A 10  ? 0.1674 0.1866 0.1818 -0.0277 0.0203  0.0380  10   LEU   A CA  
184  C  C   A LEU   A 10  ? 0.1408 0.1540 0.1920 -0.0225 0.0235  0.0487  10   LEU   A C   
185  C  C   B LEU   A 10  ? 0.1533 0.1773 0.1688 -0.0291 0.0189  0.0411  10   LEU   A C   
186  O  O   A LEU   A 10  ? 0.1365 0.1466 0.2073 -0.0256 0.0249  0.0457  10   LEU   A O   
187  O  O   B LEU   A 10  ? 0.1512 0.1717 0.1743 -0.0309 0.0224  0.0383  10   LEU   A O   
188  C  CB  A LEU   A 10  ? 0.1543 0.1656 0.2181 -0.0233 0.0294  0.0399  10   LEU   A CB  
189  C  CB  B LEU   A 10  ? 0.1797 0.1894 0.1968 -0.0330 0.0216  0.0357  10   LEU   A CB  
190  C  CG  A LEU   A 10  ? 0.1822 0.1749 0.2708 -0.0169 0.0129  0.0359  10   LEU   A CG  
191  C  CG  B LEU   A 10  ? 0.2001 0.1952 0.2191 -0.0349 0.0131  0.0288  10   LEU   A CG  
192  C  CD1 A LEU   A 10  ? 0.2069 0.1834 0.3001 -0.0216 0.0154  0.0279  10   LEU   A CD1 
193  C  CD1 B LEU   A 10  ? 0.2108 0.2042 0.2409 -0.0446 0.0058  0.0244  10   LEU   A CD1 
194  C  CD2 A LEU   A 10  ? 0.1870 0.1850 0.2897 0.0011  0.0239  0.0166  10   LEU   A CD2 
195  C  CD2 B LEU   A 10  ? 0.2131 0.2034 0.2395 -0.0316 0.0069  0.0269  10   LEU   A CD2 
218  N  N   A LYS   A 11  ? 0.1506 0.1482 0.1787 -0.0223 0.0163  0.0420  11   LYS   A N   
219  N  N   B LYS   A 11  ? 0.1450 0.1651 0.1501 -0.0334 0.0108  0.0418  11   LYS   A N   
220  C  CA  A LYS   A 11  ? 0.1527 0.1468 0.1952 -0.0308 0.0217  0.0407  11   LYS   A CA  
221  C  CA  B LYS   A 11  ? 0.1437 0.1534 0.1544 -0.0314 0.0090  0.0387  11   LYS   A CA  
222  C  C   A LYS   A 11  ? 0.1459 0.1516 0.2103 -0.0302 0.0308  0.0222  11   LYS   A C   
223  C  C   B LYS   A 11  ? 0.1349 0.1406 0.1612 -0.0395 0.0062  0.0233  11   LYS   A C   
224  O  O   A LYS   A 11  ? 0.1436 0.1688 0.2457 -0.0425 0.0369  0.0067  11   LYS   A O   
225  O  O   B LYS   A 11  ? 0.1326 0.1380 0.1768 -0.0475 0.0160  -0.0013 11   LYS   A O   
226  C  CB  A LYS   A 11  ? 0.1659 0.1482 0.1951 -0.0252 0.0174  0.0333  11   LYS   A CB  
227  C  CB  B LYS   A 11  ? 0.1522 0.1538 0.1550 -0.0205 0.0131  0.0369  11   LYS   A CB  
228  C  CG  A LYS   A 11  ? 0.1808 0.1414 0.1833 -0.0322 0.0234  0.0359  11   LYS   A CG  
229  C  CG  B LYS   A 11  ? 0.1594 0.1508 0.1632 -0.0170 0.0169  0.0300  11   LYS   A CG  
230  C  CD  A LYS   A 11  ? 0.1976 0.1428 0.1744 -0.0215 0.0238  0.0264  11   LYS   A CD  
231  C  CD  B LYS   A 11  ? 0.1689 0.1479 0.1674 -0.0023 0.0179  0.0262  11   LYS   A CD  
232  C  CE  A LYS   A 11  ? 0.2008 0.1467 0.1800 -0.0137 0.0318  0.0302  11   LYS   A CE  
233  C  CE  B LYS   A 11  ? 0.1719 0.1458 0.1788 0.0032  0.0261  0.0325  11   LYS   A CE  
234  N  NZ  A LYS   A 11  ? 0.1946 0.1540 0.1924 -0.0077 0.0193  0.0394  11   LYS   A NZ  
235  N  NZ  B LYS   A 11  ? 0.1674 0.1509 0.1916 0.0040  0.0167  0.0379  11   LYS   A NZ  
262  N  N   A LEU   A 12  ? 0.1401 0.1476 0.1918 -0.0279 0.0319  0.0131  12   LEU   A N   
263  N  N   B LEU   A 12  ? 0.1299 0.1526 0.1673 -0.0313 0.0026  0.0225  12   LEU   A N   
264  C  CA  A LEU   A 12  ? 0.1431 0.1527 0.1908 -0.0262 0.0182  0.0258  12   LEU   A CA  
265  C  CA  B LEU   A 12  ? 0.1237 0.1674 0.1707 -0.0259 0.0074  0.0263  12   LEU   A CA  
266  C  C   A LEU   A 12  ? 0.1453 0.1475 0.1929 -0.0259 0.0142  0.0350  12   LEU   A C   
267  C  C   B LEU   A 12  ? 0.1291 0.1679 0.1734 -0.0204 0.0180  0.0354  12   LEU   A C   
268  O  O   A LEU   A 12  ? 0.1437 0.1465 0.1976 -0.0162 0.0107  0.0196  12   LEU   A O   
269  O  O   B LEU   A 12  ? 0.1313 0.1551 0.1640 -0.0037 0.0148  0.0387  12   LEU   A O   
270  C  CB  A LEU   A 12  ? 0.1513 0.1421 0.1922 -0.0140 0.0072  0.0271  12   LEU   A CB  
271  C  CB  B LEU   A 12  ? 0.1265 0.1793 0.1857 -0.0200 0.0084  0.0279  12   LEU   A CB  
272  C  CG  A LEU   A 12  ? 0.1536 0.1441 0.2068 0.0016  0.0201  0.0260  12   LEU   A CG  
273  C  CG  B LEU   A 12  ? 0.1309 0.1889 0.2128 -0.0145 0.0185  0.0233  12   LEU   A CG  
274  C  CD1 A LEU   A 12  ? 0.1628 0.1508 0.2185 0.0156  0.0227  0.0358  12   LEU   A CD1 
275  C  CD1 B LEU   A 12  ? 0.1357 0.1975 0.2233 -0.0032 0.0341  0.0219  12   LEU   A CD1 
276  C  CD2 A LEU   A 12  ? 0.1598 0.1473 0.2269 0.0111  0.0199  0.0248  12   LEU   A CD2 
277  C  CD2 B LEU   A 12  ? 0.1354 0.1933 0.2330 -0.0082 0.0122  0.0059  12   LEU   A CD2 
300  N  N   A THR   A 13  ? 0.1438 0.1489 0.1934 -0.0281 0.0049  0.0346  13   THR   A N   
301  N  N   B THR   A 13  ? 0.1295 0.1687 0.1783 -0.0214 0.0227  0.0295  13   THR   A N   
302  C  CA  A THR   A 13  ? 0.1464 0.1457 0.1811 -0.0239 0.0026  0.0340  13   THR   A CA  
303  C  CA  B THR   A 13  ? 0.1345 0.1661 0.1789 -0.0211 0.0270  0.0276  13   THR   A CA  
304  C  C   A THR   A 13  ? 0.1548 0.1453 0.1833 -0.0275 0.0068  0.0450  13   THR   A C   
305  C  C   B THR   A 13  ? 0.1388 0.1631 0.1796 -0.0287 0.0318  0.0140  13   THR   A C   
306  O  O   A THR   A 13  ? 0.1602 0.1451 0.2008 -0.0242 0.0042  0.0435  13   THR   A O   
307  O  O   B THR   A 13  ? 0.1424 0.1623 0.1863 -0.0237 0.0365  0.0087  13   THR   A O   
308  C  CB  A THR   A 13  ? 0.1440 0.1549 0.1801 -0.0132 -0.0027 0.0432  13   THR   A CB  
309  C  CB  B THR   A 13  ? 0.1283 0.1718 0.1761 -0.0076 0.0157  0.0466  13   THR   A CB  
310  O  OG1 A THR   A 13  ? 0.1429 0.1514 0.1596 -0.0185 -0.0150 0.0521  13   THR   A OG1 
311  O  OG1 B THR   A 13  ? 0.1251 0.1748 0.1802 -0.0143 0.0173  0.0501  13   THR   A OG1 
312  C  CG2 A THR   A 13  ? 0.1357 0.1700 0.1890 -0.0155 0.0084  0.0222  13   THR   A CG2 
313  C  CG2 B THR   A 13  ? 0.1236 0.1832 0.1917 -0.0002 0.0161  0.0424  13   THR   A CG2 
328  N  N   A ASP   A 14  ? 0.1594 0.1482 0.1730 -0.0275 0.0056  0.0508  14   ASP   A N   
329  N  N   B ASP   A 14  ? 0.1443 0.1626 0.1832 -0.0313 0.0169  0.0060  14   ASP   A N   
330  C  CA  A ASP   A 14  ? 0.1544 0.1539 0.1703 -0.0217 -0.0007 0.0433  14   ASP   A CA  
331  C  CA  B ASP   A 14  ? 0.1494 0.1643 0.1835 -0.0254 0.0138  0.0129  14   ASP   A CA  
332  C  C   A ASP   A 14  ? 0.1529 0.1595 0.1490 -0.0208 0.0004  0.0373  14   ASP   A C   
333  C  C   B ASP   A 14  ? 0.1495 0.1494 0.1436 -0.0159 0.0194  0.0185  14   ASP   A C   
334  O  O   A ASP   A 14  ? 0.1640 0.1618 0.1533 -0.0327 0.0047  0.0231  14   ASP   A O   
335  O  O   B ASP   A 14  ? 0.1598 0.1430 0.1369 -0.0094 0.0300  0.0126  14   ASP   A O   
336  C  CB  A ASP   A 14  ? 0.1750 0.1606 0.2287 -0.0280 -0.0057 0.0521  14   ASP   A CB  
337  C  CB  B ASP   A 14  ? 0.1636 0.1899 0.2265 -0.0268 0.0133  0.0191  14   ASP   A CB  
338  C  CG  A ASP   A 14  ? 0.1976 0.2054 0.3163 -0.0356 -0.0133 0.0346  14   ASP   A CG  
339  C  CG  B ASP   A 14  ? 0.1753 0.2204 0.2788 -0.0322 0.0054  0.0085  14   ASP   A CG  
340  O  OD1 A ASP   A 14  ? 0.2091 0.2306 0.3436 -0.0220 -0.0333 0.0355  14   ASP   A OD1 
341  O  OD1 B ASP   A 14  ? 0.1855 0.2267 0.2965 -0.0298 -0.0016 0.0081  14   ASP   A OD1 
342  O  OD2 A ASP   A 14  ? 0.2168 0.2329 0.3709 -0.0372 -0.0197 0.0078  14   ASP   A OD2 
343  O  OD2 B ASP   A 14  ? 0.1828 0.2359 0.3068 -0.0284 -0.0028 -0.0040 14   ASP   A OD2 
352  N  N   A ASN   A 15  ? 0.1466 0.1599 0.1492 -0.0233 0.0011  0.0415  15   ASN   A N   
353  N  N   B ASN   A 15  ? 0.1359 0.1347 0.1184 -0.0211 0.0146  0.0280  15   ASN   A N   
354  C  CA  A ASN   A 15  ? 0.1477 0.1563 0.1689 -0.0227 -0.0147 0.0317  15   ASN   A CA  
355  C  CA  B ASN   A 15  ? 0.1298 0.1341 0.1424 -0.0163 0.0123  0.0214  15   ASN   A CA  
356  C  C   A ASN   A 15  ? 0.1375 0.1519 0.1820 -0.0200 0.0048  0.0302  15   ASN   A C   
357  C  C   B ASN   A 15  ? 0.1290 0.1410 0.1751 -0.0140 0.0228  0.0200  15   ASN   A C   
358  O  O   A ASN   A 15  ? 0.1414 0.1459 0.1785 -0.0141 -0.0004 0.0286  15   ASN   A O   
359  O  O   B ASN   A 15  ? 0.1299 0.1401 0.1852 -0.0126 0.0238  0.0097  15   ASN   A O   
360  C  CB  A ASN   A 15  ? 0.1574 0.1586 0.1645 -0.0186 -0.0158 0.0326  15   ASN   A CB  
361  C  CB  B ASN   A 15  ? 0.1220 0.1309 0.1274 -0.0134 0.0126  0.0132  15   ASN   A CB  
362  C  CG  A ASN   A 15  ? 0.1542 0.1647 0.1613 -0.0110 0.0014  0.0237  15   ASN   A CG  
363  C  CG  B ASN   A 15  ? 0.1121 0.1431 0.1397 -0.0155 0.0143  0.0120  15   ASN   A CG  
364  O  OD1 A ASN   A 15  ? 0.1579 0.1645 0.1696 -0.0155 0.0311  0.0130  15   ASN   A OD1 
365  O  OD1 B ASN   A 15  ? 0.1163 0.1484 0.1430 -0.0218 0.0275  -0.0002 15   ASN   A OD1 
366  N  ND2 A ASN   A 15  ? 0.1544 0.1785 0.1676 -0.0132 -0.0089 0.0314  15   ASN   A ND2 
367  N  ND2 B ASN   A 15  ? 0.1080 0.1516 0.1351 -0.0235 0.0134  0.0187  15   ASN   A ND2 
380  N  N   A VAL   A 16  ? 0.1349 0.1446 0.2007 -0.0184 0.0080  0.0371  16   VAL   A N   
381  N  N   B VAL   A 16  ? 0.1294 0.1437 0.1978 -0.0069 0.0095  0.0371  16   VAL   A N   
382  C  CA  A VAL   A 16  ? 0.1331 0.1425 0.2039 -0.0170 0.0145  0.0361  16   VAL   A CA  
383  C  CA  B VAL   A 16  ? 0.1332 0.1491 0.1980 -0.0065 0.0173  0.0466  16   VAL   A CA  
384  C  C   A VAL   A 16  ? 0.1310 0.1346 0.1910 -0.0165 0.0122  0.0372  16   VAL   A C   
385  C  C   B VAL   A 16  ? 0.1320 0.1577 0.1881 -0.0034 0.0202  0.0504  16   VAL   A C   
386  O  O   A VAL   A 16  ? 0.1233 0.1380 0.1914 -0.0232 0.0172  0.0203  16   VAL   A O   
387  O  O   B VAL   A 16  ? 0.1336 0.1622 0.1942 -0.0013 0.0310  0.0376  16   VAL   A O   
388  C  CB  A VAL   A 16  ? 0.1369 0.1592 0.1977 0.0014  0.0263  0.0410  16   VAL   A CB  
389  C  CB  B VAL   A 16  ? 0.1413 0.1556 0.1960 0.0043  0.0244  0.0492  16   VAL   A CB  
390  C  CG1 A VAL   A 16  ? 0.1506 0.1693 0.1901 0.0096  0.0294  0.0339  16   VAL   A CG1 
391  C  CG1 B VAL   A 16  ? 0.1488 0.1604 0.1931 0.0115  0.0213  0.0464  16   VAL   A CG1 
392  C  CG2 A VAL   A 16  ? 0.1396 0.1715 0.2113 0.0062  0.0395  0.0437  16   VAL   A CG2 
393  C  CG2 B VAL   A 16  ? 0.1424 0.1639 0.2065 0.0042  0.0304  0.0453  16   VAL   A CG2 
412  N  N   A TYR   A 17  ? 0.1312 0.1266 0.1891 -0.0146 0.0251  0.0348  17   TYR   A N   
413  N  N   B TYR   A 17  ? 0.1292 0.1571 0.1808 -0.0067 0.0170  0.0467  17   TYR   A N   
414  C  CA  A TYR   A 17  ? 0.1401 0.1356 0.1777 -0.0221 0.0219  0.0298  17   TYR   A CA  
415  C  CA  B TYR   A 17  ? 0.1300 0.1580 0.1600 -0.0122 0.0139  0.0402  17   TYR   A CA  
416  C  C   A TYR   A 17  ? 0.1390 0.1262 0.1758 -0.0187 0.0222  0.0219  17   TYR   A C   
417  C  C   B TYR   A 17  ? 0.1281 0.1505 0.1450 -0.0144 0.0079  0.0367  17   TYR   A C   
418  O  O   A TYR   A 17  ? 0.1333 0.1272 0.1669 -0.0128 0.0195  0.0183  17   TYR   A O   
419  O  O   B TYR   A 17  ? 0.1214 0.1515 0.1390 -0.0194 -0.0024 0.0319  17   TYR   A O   
420  C  CB  A TYR   A 17  ? 0.1540 0.1366 0.1827 -0.0254 0.0069  0.0408  17   TYR   A CB  
421  C  CB  B TYR   A 17  ? 0.1347 0.1612 0.1636 -0.0039 0.0044  0.0337  17   TYR   A CB  
422  C  CG  A TYR   A 17  ? 0.1651 0.1468 0.1988 -0.0196 -0.0014 0.0420  17   TYR   A CG  
423  C  CG  B TYR   A 17  ? 0.1344 0.1674 0.1642 0.0034  0.0004  0.0316  17   TYR   A CG  
424  C  CD1 A TYR   A 17  ? 0.1674 0.1598 0.2027 -0.0141 0.0030  0.0419  17   TYR   A CD1 
425  C  CD1 B TYR   A 17  ? 0.1383 0.1722 0.1665 0.0102  0.0026  0.0316  17   TYR   A CD1 
426  C  CD2 A TYR   A 17  ? 0.1693 0.1443 0.2005 -0.0253 0.0006  0.0427  17   TYR   A CD2 
427  C  CD2 B TYR   A 17  ? 0.1321 0.1666 0.1639 0.0046  0.0026  0.0378  17   TYR   A CD2 
428  C  CE1 A TYR   A 17  ? 0.1700 0.1586 0.2128 -0.0117 -0.0021 0.0417  17   TYR   A CE1 
429  C  CE1 B TYR   A 17  ? 0.1478 0.1714 0.1703 0.0107  0.0158  0.0304  17   TYR   A CE1 
430  C  CE2 A TYR   A 17  ? 0.1724 0.1474 0.2052 -0.0151 -0.0022 0.0312  17   TYR   A CE2 
431  C  CE2 B TYR   A 17  ? 0.1361 0.1625 0.1663 0.0058  0.0117  0.0303  17   TYR   A CE2 
432  C  CZ  A TYR   A 17  ? 0.1767 0.1493 0.2050 -0.0171 0.0000  0.0388  17   TYR   A CZ  
433  C  CZ  B TYR   A 17  ? 0.1381 0.1606 0.1660 0.0125  0.0125  0.0317  17   TYR   A CZ  
434  O  OH  A TYR   A 17  ? 0.1917 0.1485 0.2116 -0.0112 0.0063  0.0352  17   TYR   A OH  
435  O  OH  B TYR   A 17  ? 0.1327 0.1570 0.1661 0.0198  0.0279  0.0270  17   TYR   A OH  
454  N  N   A ILE   A 18  ? 0.1430 0.1356 0.1706 -0.0173 0.0278  0.0326  18   ILE   A N   
455  N  N   B ILE   A 18  ? 0.1271 0.1491 0.1429 -0.0152 0.0137  0.0339  18   ILE   A N   
456  C  CA  A ILE   A 18  ? 0.1466 0.1403 0.1805 -0.0160 0.0274  0.0230  18   ILE   A CA  
457  C  CA  B ILE   A 18  ? 0.1262 0.1469 0.1351 -0.0060 0.0214  0.0233  18   ILE   A CA  
458  C  C   A ILE   A 18  ? 0.1496 0.1417 0.2038 -0.0199 0.0339  0.0241  18   ILE   A C   
459  C  C   B ILE   A 18  ? 0.1304 0.1560 0.1371 -0.0095 0.0155  0.0243  18   ILE   A C   
460  O  O   A ILE   A 18  ? 0.1462 0.1531 0.1950 -0.0265 0.0337  0.0284  18   ILE   A O   
461  O  O   B ILE   A 18  ? 0.1326 0.1667 0.1514 -0.0167 0.0230  0.0236  18   ILE   A O   
462  C  CB  A ILE   A 18  ? 0.1575 0.1467 0.1617 -0.0058 0.0310  0.0220  18   ILE   A CB  
463  C  CB  B ILE   A 18  ? 0.1338 0.1486 0.1227 0.0040  0.0185  0.0226  18   ILE   A CB  
464  C  CG1 A ILE   A 18  ? 0.1655 0.1541 0.1551 0.0041  0.0136  0.0272  18   ILE   A CG1 
465  C  CG1 B ILE   A 18  ? 0.1495 0.1570 0.1363 0.0036  0.0176  0.0353  18   ILE   A CG1 
466  C  CG2 A ILE   A 18  ? 0.1529 0.1393 0.1699 0.0008  0.0279  0.0057  18   ILE   A CG2 
467  C  CG2 B ILE   A 18  ? 0.1369 0.1488 0.1149 -0.0017 0.0091  0.0252  18   ILE   A CG2 
468  C  CD1 A ILE   A 18  ? 0.1880 0.1697 0.1742 0.0206  0.0219  0.0269  18   ILE   A CD1 
469  C  CD1 B ILE   A 18  ? 0.1667 0.1690 0.1411 0.0111  0.0254  0.0295  18   ILE   A CD1 
492  N  N   A LYS   A 19  ? 0.1562 0.1415 0.2266 -0.0144 0.0526  0.0273  19   LYS   A N   
493  N  N   B LYS   A 19  ? 0.1377 0.1565 0.1470 -0.0032 0.0303  0.0192  19   LYS   A N   
494  C  CA  A LYS   A 19  ? 0.1690 0.1515 0.2502 -0.0059 0.0505  0.0234  19   LYS   A CA  
495  C  CA  B LYS   A 19  ? 0.1518 0.1699 0.1860 0.0079  0.0326  0.0093  19   LYS   A CA  
496  C  C   A LYS   A 19  ? 0.1499 0.1456 0.2732 -0.0029 0.0446  0.0347  19   LYS   A C   
497  C  C   B LYS   A 19  ? 0.1422 0.1719 0.2207 0.0130  0.0291  0.0160  19   LYS   A C   
498  O  O   A LYS   A 19  ? 0.1329 0.1363 0.2589 -0.0054 0.0289  0.0384  19   LYS   A O   
499  O  O   B LYS   A 19  ? 0.1369 0.1712 0.2219 0.0090  0.0174  0.0204  19   LYS   A O   
500  C  CB  A LYS   A 19  ? 0.1845 0.1709 0.2553 -0.0121 0.0647  0.0212  19   LYS   A CB  
501  C  CB  B LYS   A 19  ? 0.1637 0.1805 0.1934 0.0118  0.0480  -0.0051 19   LYS   A CB  
502  C  CG  A LYS   A 19  ? 0.2155 0.1888 0.2652 -0.0179 0.0671  0.0080  19   LYS   A CG  
503  C  CG  B LYS   A 19  ? 0.1936 0.1976 0.2063 0.0126  0.0527  -0.0097 19   LYS   A CG  
504  C  CD  A LYS   A 19  ? 0.2427 0.2117 0.2623 -0.0179 0.0741  0.0027  19   LYS   A CD  
505  C  CD  B LYS   A 19  ? 0.2184 0.2171 0.2177 0.0131  0.0574  -0.0065 19   LYS   A CD  
506  C  CE  A LYS   A 19  ? 0.2644 0.2253 0.2769 -0.0257 0.0749  -0.0024 19   LYS   A CE  
507  C  CE  B LYS   A 19  ? 0.2337 0.2301 0.2237 0.0076  0.0614  -0.0094 19   LYS   A CE  
508  N  NZ  A LYS   A 19  ? 0.2757 0.2374 0.2773 -0.0366 0.0874  -0.0087 19   LYS   A NZ  
509  N  NZ  B LYS   A 19  ? 0.2464 0.2382 0.2266 -0.0001 0.0701  -0.0161 19   LYS   A NZ  
536  N  N   A ASN   A 20  ? 0.1602 0.1564 0.3157 -0.0057 0.0503  0.0518  20   ASN   A N   
537  N  N   B ASN   A 20  ? 0.1455 0.1818 0.2614 0.0123  0.0324  0.0186  20   ASN   A N   
538  C  CA  A ASN   A 20  ? 0.1665 0.1699 0.3333 0.0170  0.0507  0.0512  20   ASN   A CA  
539  C  CA  B ASN   A 20  ? 0.1448 0.1897 0.2779 0.0218  0.0321  0.0143  20   ASN   A CA  
540  C  C   A ASN   A 20  ? 0.1841 0.1712 0.3263 0.0196  0.0528  0.0524  20   ASN   A C   
541  C  C   B ASN   A 20  ? 0.1607 0.1842 0.2828 0.0056  0.0470  0.0213  20   ASN   A C   
542  O  O   A ASN   A 20  ? 0.1996 0.1747 0.3209 0.0174  0.0516  0.0561  20   ASN   A O   
543  O  O   B ASN   A 20  ? 0.1757 0.1865 0.2904 0.0047  0.0482  0.0255  20   ASN   A O   
544  C  CB  A ASN   A 20  ? 0.1777 0.1870 0.3506 0.0218  0.0529  0.0566  20   ASN   A CB  
545  C  CB  B ASN   A 20  ? 0.1474 0.2068 0.2866 0.0370  0.0196  0.0093  20   ASN   A CB  
546  C  CG  A ASN   A 20  ? 0.1925 0.1960 0.3702 0.0335  0.0455  0.0594  20   ASN   A CG  
547  C  CG  B ASN   A 20  ? 0.1544 0.2144 0.2965 0.0521  0.0036  0.0108  20   ASN   A CG  
548  O  OD1 A ASN   A 20  ? 0.2193 0.2175 0.3903 0.0324  0.0446  0.0348  20   ASN   A OD1 
549  O  OD1 B ASN   A 20  ? 0.1665 0.2199 0.3127 0.0580  0.0075  0.0012  20   ASN   A OD1 
550  N  ND2 A ASN   A 20  ? 0.1982 0.1956 0.3783 0.0403  0.0386  0.0682  20   ASN   A ND2 
551  N  ND2 B ASN   A 20  ? 0.1661 0.2168 0.3111 0.0529  -0.0001 0.0135  20   ASN   A ND2 
564  N  N   A ALA   A 21  ? 0.1830 0.1743 0.3240 0.0241  0.0386  0.0342  21   ALA   A N   
565  N  N   B ALA   A 21  ? 0.1596 0.1772 0.2765 -0.0102 0.0426  0.0166  21   ALA   A N   
566  C  CA  A ALA   A 21  ? 0.1954 0.1780 0.3033 0.0257  0.0299  0.0366  21   ALA   A CA  
567  C  CA  B ALA   A 21  ? 0.1710 0.1731 0.2640 -0.0198 0.0408  0.0286  21   ALA   A CA  
568  C  C   A ALA   A 21  ? 0.1912 0.1846 0.2814 0.0234  0.0257  0.0301  21   ALA   A C   
569  C  C   B ALA   A 21  ? 0.1612 0.1654 0.2418 -0.0218 0.0371  0.0227  21   ALA   A C   
570  O  O   A ALA   A 21  ? 0.1984 0.1848 0.2822 0.0205  0.0313  0.0237  21   ALA   A O   
571  O  O   B ALA   A 21  ? 0.1543 0.1588 0.2457 -0.0247 0.0264  0.0037  21   ALA   A O   
572  C  CB  A ALA   A 21  ? 0.2065 0.1847 0.3186 0.0204  0.0254  0.0360  21   ALA   A CB  
573  C  CB  B ALA   A 21  ? 0.1839 0.1817 0.2814 -0.0241 0.0314  0.0324  21   ALA   A CB  
584  N  N   A ASP   A 22  ? 0.1881 0.1806 0.2633 0.0178  0.0213  0.0352  22   ASP   A N   
585  N  N   B ASP   A 22  ? 0.1651 0.1586 0.2257 -0.0195 0.0409  0.0273  22   ASP   A N   
586  C  CA  A ASP   A 22  ? 0.1868 0.1838 0.2525 0.0103  0.0135  0.0274  22   ASP   A CA  
587  C  CA  B ASP   A 22  ? 0.1697 0.1569 0.2047 -0.0111 0.0358  0.0222  22   ASP   A CA  
588  C  C   A ASP   A 22  ? 0.1750 0.1848 0.2118 0.0006  0.0155  0.0251  22   ASP   A C   
589  C  C   B ASP   A 22  ? 0.1559 0.1605 0.1741 -0.0182 0.0359  0.0148  22   ASP   A C   
590  O  O   A ASP   A 22  ? 0.1786 0.1934 0.2146 -0.0037 0.0211  0.0164  22   ASP   A O   
591  O  O   B ASP   A 22  ? 0.1568 0.1675 0.1684 -0.0236 0.0386  -0.0035 22   ASP   A O   
592  C  CB  A ASP   A 22  ? 0.2028 0.1910 0.2991 0.0092  0.0142  0.0124  22   ASP   A CB  
593  C  CB  B ASP   A 22  ? 0.1914 0.1600 0.2209 0.0008  0.0406  0.0198  22   ASP   A CB  
594  C  CG  A ASP   A 22  ? 0.2172 0.1936 0.3339 0.0034  0.0023  0.0150  22   ASP   A CG  
595  C  CG  B ASP   A 22  ? 0.2052 0.1611 0.2317 0.0084  0.0466  0.0219  22   ASP   A CG  
596  O  OD1 A ASP   A 22  ? 0.2070 0.1883 0.3531 -0.0169 -0.0187 0.0358  22   ASP   A OD1 
597  O  OD1 B ASP   A 22  ? 0.1984 0.1512 0.2114 0.0036  0.0536  0.0238  22   ASP   A OD1 
598  O  OD2 A ASP   A 22  ? 0.2431 0.2039 0.3536 0.0164  0.0170  0.0022  22   ASP   A OD2 
599  O  OD2 B ASP   A 22  ? 0.2224 0.1767 0.2639 0.0113  0.0523  0.0240  22   ASP   A OD2 
608  N  N   A ILE   A 23  ? 0.1770 0.1814 0.1785 0.0048  0.0209  0.0288  23   ILE   A N   
609  N  N   B ILE   A 23  ? 0.1524 0.1545 0.1625 -0.0142 0.0306  0.0215  23   ILE   A N   
610  C  CA  A ILE   A 23  ? 0.1720 0.1754 0.1647 0.0012  0.0241  0.0232  23   ILE   A CA  
611  C  CA  B ILE   A 23  ? 0.1469 0.1565 0.1450 -0.0133 0.0196  0.0221  23   ILE   A CA  
612  C  C   A ILE   A 23  ? 0.1673 0.1811 0.1620 -0.0006 0.0356  0.0191  23   ILE   A C   
613  C  C   B ILE   A 23  ? 0.1515 0.1653 0.1517 -0.0192 0.0190  0.0192  23   ILE   A C   
614  O  O   A ILE   A 23  ? 0.1714 0.1861 0.1734 0.0029  0.0331  0.0150  23   ILE   A O   
615  O  O   B ILE   A 23  ? 0.1522 0.1665 0.1532 -0.0173 0.0136  0.0162  23   ILE   A O   
616  C  CB  A ILE   A 23  ? 0.1839 0.1747 0.1543 0.0039  0.0210  0.0216  23   ILE   A CB  
617  C  CB  B ILE   A 23  ? 0.1463 0.1509 0.1288 -0.0043 0.0165  0.0236  23   ILE   A CB  
618  C  CG1 A ILE   A 23  ? 0.1911 0.1773 0.1541 0.0097  0.0284  0.0136  23   ILE   A CG1 
619  C  CG1 B ILE   A 23  ? 0.1519 0.1534 0.1292 -0.0030 0.0051  0.0114  23   ILE   A CG1 
620  C  CG2 A ILE   A 23  ? 0.1821 0.1770 0.1561 0.0053  0.0133  0.0266  23   ILE   A CG2 
621  C  CG2 B ILE   A 23  ? 0.1369 0.1469 0.1293 0.0033  0.0131  0.0250  23   ILE   A CG2 
622  C  CD1 A ILE   A 23  ? 0.1934 0.1800 0.1655 0.0075  0.0190  0.0081  23   ILE   A CD1 
623  C  CD1 B ILE   A 23  ? 0.1421 0.1527 0.1235 0.0010  -0.0013 -0.0005 23   ILE   A CD1 
646  N  N   A VAL   A 24  ? 0.1644 0.1820 0.1736 -0.0099 0.0258  0.0114  24   VAL   A N   
647  N  N   B VAL   A 24  ? 0.1623 0.1752 0.1672 -0.0219 0.0107  0.0170  24   VAL   A N   
648  C  CA  A VAL   A 24  ? 0.1790 0.1885 0.1917 -0.0179 0.0205  -0.0017 24   VAL   A CA  
649  C  CA  B VAL   A 24  ? 0.1785 0.1805 0.1859 -0.0232 0.0109  0.0090  24   VAL   A CA  
650  C  C   A VAL   A 24  ? 0.1879 0.2025 0.1984 -0.0209 0.0197  -0.0023 24   VAL   A C   
651  C  C   B VAL   A 24  ? 0.1857 0.1976 0.1939 -0.0210 0.0168  -0.0010 24   VAL   A C   
652  O  O   A VAL   A 24  ? 0.1981 0.2028 0.2008 -0.0181 0.0214  -0.0004 24   VAL   A O   
653  O  O   B VAL   A 24  ? 0.1923 0.1993 0.2016 -0.0235 0.0183  -0.0025 24   VAL   A O   
654  C  CB  A VAL   A 24  ? 0.1873 0.1875 0.2148 -0.0234 0.0326  0.0090  24   VAL   A CB  
655  C  CB  B VAL   A 24  ? 0.1855 0.1788 0.2084 -0.0287 0.0095  0.0174  24   VAL   A CB  
656  C  CG1 A VAL   A 24  ? 0.1954 0.1965 0.2208 -0.0156 0.0365  -0.0078 24   VAL   A CG1 
657  C  CG1 B VAL   A 24  ? 0.1974 0.1872 0.2318 -0.0238 0.0005  0.0172  24   VAL   A CG1 
658  C  CG2 A VAL   A 24  ? 0.2027 0.1888 0.2250 -0.0218 0.0466  0.0189  24   VAL   A CG2 
659  C  CG2 B VAL   A 24  ? 0.1922 0.1739 0.2130 -0.0411 0.0187  0.0191  24   VAL   A CG2 
678  N  N   A GLU   A 25  ? 0.1940 0.2290 0.1990 -0.0246 0.0357  -0.0096 25   GLU   A N   
679  N  N   B GLU   A 25  ? 0.1870 0.2200 0.1926 -0.0157 0.0376  -0.0122 25   GLU   A N   
680  C  CA  A GLU   A 25  ? 0.2094 0.2536 0.2207 -0.0189 0.0468  -0.0079 25   GLU   A CA  
681  C  CA  B GLU   A 25  ? 0.1938 0.2437 0.1999 -0.0162 0.0432  -0.0095 25   GLU   A CA  
682  C  C   A GLU   A 25  ? 0.1955 0.2525 0.1866 -0.0302 0.0562  -0.0108 25   GLU   A C   
683  C  C   B GLU   A 25  ? 0.1929 0.2577 0.1879 -0.0136 0.0401  -0.0091 25   GLU   A C   
684  O  O   A GLU   A 25  ? 0.2001 0.2677 0.1814 -0.0312 0.0531  -0.0077 25   GLU   A O   
685  O  O   B GLU   A 25  ? 0.1986 0.2665 0.1958 -0.0134 0.0363  -0.0121 25   GLU   A O   
686  C  CB  A GLU   A 25  ? 0.2372 0.2778 0.2776 -0.0112 0.0429  -0.0064 25   GLU   A CB  
687  C  CB  B GLU   A 25  ? 0.2062 0.2547 0.2308 -0.0176 0.0456  -0.0056 25   GLU   A CB  
688  C  CG  A GLU   A 25  ? 0.2699 0.3025 0.3512 -0.0117 0.0287  -0.0075 25   GLU   A CG  
689  C  CG  B GLU   A 25  ? 0.2318 0.2679 0.2873 -0.0211 0.0371  -0.0016 25   GLU   A CG  
690  C  CD  A GLU   A 25  ? 0.2949 0.3231 0.4127 -0.0128 0.0181  -0.0080 25   GLU   A CD  
691  C  CD  B GLU   A 25  ? 0.2501 0.2794 0.3382 -0.0281 0.0276  0.0039  25   GLU   A CD  
692  O  OE1 A GLU   A 25  ? 0.3081 0.3318 0.4315 -0.0128 0.0059  -0.0172 25   GLU   A OE1 
693  O  OE1 B GLU   A 25  ? 0.2602 0.2863 0.3652 -0.0290 0.0238  0.0047  25   GLU   A OE1 
694  O  OE2 A GLU   A 25  ? 0.2999 0.3323 0.4442 -0.0107 0.0150  -0.0102 25   GLU   A OE2 
695  O  OE2 B GLU   A 25  ? 0.2562 0.2799 0.3551 -0.0331 0.0245  0.0063  25   GLU   A OE2 
708  N  N   A GLU   A 26  ? 0.1863 0.2347 0.1933 -0.0483 0.0644  -0.0143 26   GLU   A N   
709  N  N   B GLU   A 26  ? 0.1940 0.2583 0.1877 -0.0163 0.0419  -0.0097 26   GLU   A N   
710  C  CA  A GLU   A 26  ? 0.2080 0.2283 0.1809 -0.0622 0.0609  -0.0082 26   GLU   A CA  
711  C  CA  B GLU   A 26  ? 0.2024 0.2574 0.1903 -0.0190 0.0356  -0.0033 26   GLU   A CA  
712  C  C   A GLU   A 26  ? 0.2076 0.2186 0.1568 -0.0580 0.0513  -0.0032 26   GLU   A C   
713  C  C   B GLU   A 26  ? 0.1975 0.2418 0.1751 -0.0066 0.0316  0.0048  26   GLU   A C   
714  O  O   A GLU   A 26  ? 0.2187 0.2209 0.1463 -0.0614 0.0524  -0.0011 26   GLU   A O   
715  O  O   B GLU   A 26  ? 0.2008 0.2438 0.1763 -0.0119 0.0390  0.0023  26   GLU   A O   
716  C  CB  A GLU   A 26  ? 0.2356 0.2314 0.2248 -0.0717 0.0621  -0.0020 26   GLU   A CB  
717  C  CB  B GLU   A 26  ? 0.2150 0.2694 0.2097 -0.0296 0.0167  -0.0081 26   GLU   A CB  
718  C  CG  A GLU   A 26  ? 0.2566 0.2404 0.2955 -0.0722 0.0765  -0.0139 26   GLU   A CG  
719  C  CG  B GLU   A 26  ? 0.2229 0.2782 0.2306 -0.0340 0.0172  -0.0127 26   GLU   A CG  
720  C  CD  A GLU   A 26  ? 0.2686 0.2453 0.3236 -0.0747 0.1098  -0.0219 26   GLU   A CD  
721  C  CD  B GLU   A 26  ? 0.2263 0.2831 0.2404 -0.0417 0.0230  -0.0131 26   GLU   A CD  
722  O  OE1 A GLU   A 26  ? 0.2614 0.2563 0.3183 -0.0651 0.1407  -0.0690 26   GLU   A OE1 
723  O  OE1 B GLU   A 26  ? 0.2320 0.2920 0.2371 -0.0361 0.0347  -0.0209 26   GLU   A OE1 
724  O  OE2 A GLU   A 26  ? 0.2822 0.2505 0.3229 -0.0704 0.1201  -0.0140 26   GLU   A OE2 
725  O  OE2 B GLU   A 26  ? 0.2198 0.2783 0.2279 -0.0515 0.0232  -0.0185 26   GLU   A OE2 
738  N  N   A ALA   A 27  ? 0.1894 0.2061 0.1537 -0.0604 0.0487  0.0031  27   ALA   A N   
739  N  N   B ALA   A 27  ? 0.1849 0.2234 0.1619 0.0091  0.0247  0.0203  27   ALA   A N   
740  C  CA  A ALA   A 27  ? 0.1935 0.2103 0.1444 -0.0533 0.0453  -0.0022 27   ALA   A CA  
741  C  CA  B ALA   A 27  ? 0.1885 0.2158 0.1436 0.0167  0.0185  0.0308  27   ALA   A CA  
742  C  C   A ALA   A 27  ? 0.2139 0.2316 0.1601 -0.0588 0.0504  -0.0197 27   ALA   A C   
743  C  C   B ALA   A 27  ? 0.2012 0.2230 0.1399 0.0225  0.0167  0.0242  27   ALA   A C   
744  O  O   A ALA   A 27  ? 0.2233 0.2370 0.1710 -0.0607 0.0386  -0.0236 27   ALA   A O   
745  O  O   B ALA   A 27  ? 0.1952 0.2183 0.1306 0.0285  0.0146  0.0239  27   ALA   A O   
746  C  CB  A ALA   A 27  ? 0.1817 0.2041 0.1403 -0.0491 0.0342  0.0012  27   ALA   A CB  
747  C  CB  B ALA   A 27  ? 0.1795 0.2066 0.1385 0.0107  0.0215  0.0315  27   ALA   A CB  
758  N  N   A LYS   A 28  ? 0.2437 0.2646 0.1915 -0.0455 0.0472  -0.0459 28   LYS   A N   
759  N  N   B LYS   A 28  ? 0.2226 0.2397 0.1592 0.0291  0.0109  0.0095  28   LYS   A N   
760  C  CA  A LYS   A 28  ? 0.2774 0.3030 0.2247 -0.0353 0.0506  -0.0568 28   LYS   A CA  
761  C  CA  B LYS   A 28  ? 0.2486 0.2660 0.1850 0.0353  0.0108  -0.0107 28   LYS   A CA  
762  C  C   A LYS   A 28  ? 0.2962 0.3363 0.2154 -0.0367 0.0680  -0.0450 28   LYS   A C   
763  C  C   B LYS   A 28  ? 0.2732 0.2887 0.1844 0.0335  0.0106  -0.0051 28   LYS   A C   
764  O  O   A LYS   A 28  ? 0.3002 0.3439 0.2488 -0.0308 0.0445  -0.0422 28   LYS   A O   
765  O  O   B LYS   A 28  ? 0.2827 0.2931 0.1930 0.0352  -0.0017 -0.0087 28   LYS   A O   
766  C  CB  A LYS   A 28  ? 0.2929 0.3137 0.2859 -0.0203 0.0471  -0.0618 28   LYS   A CB  
767  C  CB  B LYS   A 28  ? 0.2568 0.2745 0.2214 0.0384  0.0107  -0.0220 28   LYS   A CB  
768  C  CG  A LYS   A 28  ? 0.3076 0.3252 0.3346 -0.0089 0.0489  -0.0613 28   LYS   A CG  
769  C  CG  B LYS   A 28  ? 0.2648 0.2867 0.2540 0.0353  0.0174  -0.0214 28   LYS   A CG  
770  C  CD  A LYS   A 28  ? 0.3188 0.3403 0.3877 -0.0040 0.0503  -0.0527 28   LYS   A CD  
771  C  CD  B LYS   A 28  ? 0.2750 0.2992 0.2907 0.0335  0.0194  -0.0195 28   LYS   A CD  
772  C  CE  A LYS   A 28  ? 0.3274 0.3506 0.4218 -0.0033 0.0523  -0.0504 28   LYS   A CE  
773  C  CE  B LYS   A 28  ? 0.2828 0.3054 0.3166 0.0305  0.0250  -0.0218 28   LYS   A CE  
774  N  NZ  A LYS   A 28  ? 0.3339 0.3553 0.4420 -0.0011 0.0564  -0.0523 28   LYS   A NZ  
775  N  NZ  B LYS   A 28  ? 0.2883 0.3094 0.3292 0.0300  0.0273  -0.0248 28   LYS   A NZ  
802  N  N   A LYS   A 29  ? 0.3092 0.3632 0.1978 -0.0438 0.1043  -0.0241 29   LYS   A N   
803  N  N   B LYS   A 29  ? 0.2866 0.3088 0.1890 0.0271  0.0334  0.0078  29   LYS   A N   
804  C  CA  A LYS   A 29  ? 0.3308 0.3897 0.2081 -0.0500 0.1278  -0.0063 29   LYS   A CA  
805  C  CA  B LYS   A 29  ? 0.3056 0.3308 0.2179 0.0185  0.0487  0.0184  29   LYS   A CA  
806  C  C   A LYS   A 29  ? 0.3274 0.3817 0.1853 -0.0640 0.1110  0.0084  29   LYS   A C   
807  C  C   B LYS   A 29  ? 0.3035 0.3255 0.1955 0.0079  0.0391  0.0301  29   LYS   A C   
808  O  O   A LYS   A 29  ? 0.3398 0.3939 0.1994 -0.0559 0.0998  0.0064  29   LYS   A O   
809  O  O   B LYS   A 29  ? 0.3110 0.3339 0.2000 0.0104  0.0354  0.0316  29   LYS   A O   
810  C  CB  A LYS   A 29  ? 0.3505 0.4205 0.2689 -0.0419 0.1532  -0.0005 29   LYS   A CB  
811  C  CB  B LYS   A 29  ? 0.3259 0.3564 0.2803 0.0195  0.0678  0.0190  29   LYS   A CB  
812  C  CG  A LYS   A 29  ? 0.3712 0.4472 0.3485 -0.0338 0.1593  0.0024  29   LYS   A CG  
813  C  CG  B LYS   A 29  ? 0.3464 0.3792 0.3504 0.0205  0.0785  0.0164  29   LYS   A CG  
814  C  CD  A LYS   A 29  ? 0.3914 0.4692 0.4254 -0.0268 0.1571  -0.0010 29   LYS   A CD  
815  C  CD  B LYS   A 29  ? 0.3626 0.3969 0.4121 0.0220  0.0852  0.0121  29   LYS   A CD  
816  C  CE  A LYS   A 29  ? 0.4039 0.4843 0.4751 -0.0223 0.1600  -0.0036 29   LYS   A CE  
817  C  CE  B LYS   A 29  ? 0.3735 0.4094 0.4543 0.0228  0.0918  0.0077  29   LYS   A CE  
818  N  NZ  A LYS   A 29  ? 0.4092 0.4923 0.5063 -0.0191 0.1620  -0.0065 29   LYS   A NZ  
819  N  NZ  B LYS   A 29  ? 0.3786 0.4160 0.4801 0.0238  0.0951  0.0049  29   LYS   A NZ  
846  N  N   A VAL   A 30  ? 0.3087 0.3586 0.1712 -0.0813 0.0935  0.0150  30   VAL   A N   
847  N  N   B VAL   A 30  ? 0.2939 0.3108 0.1837 -0.0041 0.0330  0.0325  30   VAL   A N   
848  C  CA  A VAL   A 30  ? 0.3033 0.3363 0.1582 -0.0973 0.0584  0.0297  30   VAL   A CA  
849  C  CA  B VAL   A 30  ? 0.2857 0.2960 0.1743 -0.0173 0.0180  0.0382  30   VAL   A CA  
850  C  C   A VAL   A 30  ? 0.2962 0.3071 0.1236 -0.0849 0.0397  0.0406  30   VAL   A C   
851  C  C   B VAL   A 30  ? 0.2860 0.2882 0.1561 -0.0175 0.0092  0.0323  30   VAL   A C   
852  O  O   A VAL   A 30  ? 0.3067 0.3106 0.1246 -0.0860 0.0330  0.0466  30   VAL   A O   
853  O  O   B VAL   A 30  ? 0.2901 0.2859 0.1528 -0.0191 0.0044  0.0374  30   VAL   A O   
854  C  CB  A VAL   A 30  ? 0.3005 0.3364 0.1985 -0.1092 0.0385  0.0269  30   VAL   A CB  
855  C  CB  B VAL   A 30  ? 0.2807 0.2903 0.1927 -0.0276 0.0081  0.0416  30   VAL   A CB  
856  C  CG1 A VAL   A 30  ? 0.3055 0.3365 0.2175 -0.1138 0.0263  0.0282  30   VAL   A CG1 
857  C  CG1 B VAL   A 30  ? 0.2826 0.2886 0.2074 -0.0293 0.0012  0.0415  30   VAL   A CG1 
858  C  CG2 A VAL   A 30  ? 0.2984 0.3403 0.2267 -0.1179 0.0401  0.0269  30   VAL   A CG2 
859  C  CG2 B VAL   A 30  ? 0.2796 0.2908 0.2075 -0.0332 0.0108  0.0457  30   VAL   A CG2 
878  N  N   A LYS   A 31  ? 0.2861 0.2894 0.1080 -0.0843 0.0240  0.0333  31   LYS   A N   
879  N  N   B LYS   A 31  ? 0.2835 0.2834 0.1650 -0.0143 -0.0000 0.0214  31   LYS   A N   
880  C  CA  A LYS   A 31  ? 0.2977 0.2862 0.1116 -0.0720 -0.0042 0.0221  31   LYS   A CA  
881  C  CA  B LYS   A 31  ? 0.2868 0.2824 0.1869 -0.0102 -0.0091 0.0105  31   LYS   A CA  
882  C  C   A LYS   A 31  ? 0.2712 0.2576 0.0966 -0.0501 -0.0045 0.0526  31   LYS   A C   
883  C  C   B LYS   A 31  ? 0.2632 0.2675 0.1667 -0.0015 -0.0048 0.0265  31   LYS   A C   
884  O  O   A LYS   A 31  ? 0.2800 0.2703 0.1175 -0.0427 -0.0227 0.0623  31   LYS   A O   
885  O  O   B LYS   A 31  ? 0.2688 0.2704 0.1807 0.0052  -0.0138 0.0271  31   LYS   A O   
886  C  CB  A LYS   A 31  ? 0.3344 0.3160 0.2198 -0.0615 -0.0219 -0.0048 31   LYS   A CB  
887  C  CB  B LYS   A 31  ? 0.3147 0.3009 0.2537 -0.0108 -0.0184 -0.0107 31   LYS   A CB  
888  C  CG  A LYS   A 31  ? 0.3761 0.3450 0.3474 -0.0480 -0.0333 -0.0229 31   LYS   A CG  
889  C  CG  B LYS   A 31  ? 0.3429 0.3228 0.3382 -0.0094 -0.0264 -0.0268 31   LYS   A CG  
890  C  CD  A LYS   A 31  ? 0.4064 0.3643 0.4389 -0.0355 -0.0438 -0.0378 31   LYS   A CD  
891  C  CD  B LYS   A 31  ? 0.3640 0.3403 0.4049 -0.0086 -0.0351 -0.0396 31   LYS   A CD  
892  C  CE  A LYS   A 31  ? 0.4255 0.3780 0.4961 -0.0261 -0.0524 -0.0498 31   LYS   A CE  
893  C  CE  B LYS   A 31  ? 0.3775 0.3527 0.4510 -0.0086 -0.0411 -0.0479 31   LYS   A CE  
894  N  NZ  A LYS   A 31  ? 0.4365 0.3850 0.5273 -0.0203 -0.0582 -0.0572 31   LYS   A NZ  
895  N  NZ  B LYS   A 31  ? 0.3861 0.3600 0.4781 -0.0080 -0.0439 -0.0541 31   LYS   A NZ  
922  N  N   A PRO   A 32  ? 0.2393 0.2313 0.0868 -0.0503 0.0041  0.0442  32   PRO   A N   
923  N  N   B PRO   A 32  ? 0.2350 0.2498 0.1419 -0.0019 0.0106  0.0263  32   PRO   A N   
924  C  CA  A PRO   A 32  ? 0.2377 0.2181 0.1251 -0.0537 -0.0034 0.0477  32   PRO   A CA  
925  C  CA  B PRO   A 32  ? 0.2241 0.2381 0.1432 -0.0019 0.0095  0.0333  32   PRO   A CA  
926  C  C   A PRO   A 32  ? 0.2367 0.2112 0.1311 -0.0402 -0.0129 0.0489  32   PRO   A C   
927  C  C   B PRO   A 32  ? 0.2195 0.2289 0.1365 0.0015  -0.0008 0.0403  32   PRO   A C   
928  O  O   A PRO   A 32  ? 0.2364 0.2063 0.1277 -0.0474 -0.0177 0.0422  32   PRO   A O   
929  O  O   B PRO   A 32  ? 0.2197 0.2257 0.1527 0.0037  -0.0104 0.0386  32   PRO   A O   
930  C  CB  A PRO   A 32  ? 0.2334 0.2258 0.1394 -0.0491 -0.0111 0.0371  32   PRO   A CB  
931  C  CB  B PRO   A 32  ? 0.2191 0.2424 0.1483 0.0011  0.0114  0.0238  32   PRO   A CB  
932  C  CG  A PRO   A 32  ? 0.2285 0.2310 0.0981 -0.0453 -0.0160 0.0328  32   PRO   A CG  
933  C  CG  B PRO   A 32  ? 0.2192 0.2462 0.1358 0.0048  0.0081  0.0170  32   PRO   A CG  
934  C  CD  A PRO   A 32  ? 0.2301 0.2297 0.0811 -0.0499 -0.0086 0.0390  32   PRO   A CD  
935  C  CD  B PRO   A 32  ? 0.2242 0.2482 0.1362 0.0019  0.0103  0.0170  32   PRO   A CD  
950  N  N   A THR   A 33  ? 0.2375 0.2086 0.1290 -0.0300 -0.0189 0.0534  33   THR   A N   
951  N  N   B THR   A 33  ? 0.2191 0.2211 0.1323 -0.0000 -0.0052 0.0457  33   THR   A N   
952  C  CA  A THR   A 33  ? 0.2354 0.2120 0.1455 -0.0183 -0.0248 0.0507  33   THR   A CA  
953  C  CA  B THR   A 33  ? 0.2164 0.2127 0.1339 0.0013  -0.0137 0.0505  33   THR   A CA  
954  C  C   A THR   A 33  ? 0.2026 0.2018 0.1362 -0.0175 -0.0305 0.0415  33   THR   A C   
955  C  C   B THR   A 33  ? 0.1949 0.1953 0.1354 -0.0095 -0.0185 0.0401  33   THR   A C   
956  O  O   A THR   A 33  ? 0.1887 0.1989 0.1372 -0.0132 -0.0461 0.0401  33   THR   A O   
957  O  O   B THR   A 33  ? 0.1898 0.1879 0.1542 -0.0114 -0.0156 0.0288  33   THR   A O   
958  C  CB  A THR   A 33  ? 0.2609 0.2319 0.1716 -0.0091 -0.0306 0.0587  33   THR   A CB  
959  C  CB  B THR   A 33  ? 0.2354 0.2256 0.1407 0.0091  -0.0170 0.0661  33   THR   A CB  
960  O  OG1 A THR   A 33  ? 0.2796 0.2487 0.2046 -0.0021 -0.0203 0.0649  33   THR   A OG1 
961  O  OG1 B THR   A 33  ? 0.2492 0.2398 0.1586 0.0160  -0.0151 0.0754  33   THR   A OG1 
962  C  CG2 A THR   A 33  ? 0.2672 0.2378 0.1813 -0.0038 -0.0374 0.0559  33   THR   A CG2 
963  C  CG2 B THR   A 33  ? 0.2394 0.2292 0.1524 0.0101  -0.0178 0.0620  33   THR   A CG2 
978  N  N   . VAL   A 34  ? 0.1876 0.1900 0.1251 -0.0237 -0.0200 0.0409  34   VAL   A N   
979  C  CA  . VAL   A 34  ? 0.1756 0.1766 0.1110 -0.0184 -0.0108 0.0407  34   VAL   A CA  
980  C  C   . VAL   A 34  ? 0.1640 0.1672 0.1071 -0.0175 -0.0068 0.0276  34   VAL   A C   
981  O  O   . VAL   A 34  ? 0.1626 0.1722 0.1368 -0.0289 -0.0045 0.0334  34   VAL   A O   
982  C  CB  . VAL   A 34  ? 0.1743 0.1750 0.1397 -0.0175 -0.0040 0.0311  34   VAL   A CB  
983  C  CG1 . VAL   A 34  ? 0.1847 0.1772 0.1377 -0.0129 0.0025  0.0144  34   VAL   A CG1 
984  C  CG2 . VAL   A 34  ? 0.1794 0.1904 0.1764 -0.0129 -0.0101 0.0235  34   VAL   A CG2 
995  N  N   . VAL   A 35  ? 0.1517 0.1558 0.1139 -0.0213 -0.0118 0.0271  35   VAL   A N   
996  C  CA  . VAL   A 35  ? 0.1431 0.1529 0.1115 -0.0182 -0.0002 0.0215  35   VAL   A CA  
997  C  C   . VAL   A 35  ? 0.1371 0.1374 0.1159 -0.0147 0.0057  0.0222  35   VAL   A C   
998  O  O   . VAL   A 35  ? 0.1345 0.1517 0.1289 -0.0234 0.0059  0.0112  35   VAL   A O   
999  C  CB  . VAL   A 35  ? 0.1469 0.1597 0.1170 -0.0088 0.0064  0.0105  35   VAL   A CB  
1000 C  CG1 . VAL   A 35  ? 0.1577 0.1626 0.1319 -0.0005 0.0050  0.0022  35   VAL   A CG1 
1001 C  CG2 . VAL   A 35  ? 0.1453 0.1666 0.1500 -0.0073 0.0074  0.0051  35   VAL   A CG2 
1011 N  N   . VAL   A 36  ? 0.1290 0.1395 0.0980 -0.0143 0.0054  0.0232  36   VAL   A N   
1012 C  CA  . VAL   A 36  ? 0.1248 0.1309 0.1082 -0.0087 0.0027  0.0148  36   VAL   A CA  
1013 C  C   . VAL   A 36  ? 0.1200 0.1321 0.1096 -0.0171 0.0114  0.0148  36   VAL   A C   
1014 O  O   . VAL   A 36  ? 0.1239 0.1354 0.1282 -0.0039 0.0155  0.0177  36   VAL   A O   
1015 C  CB  . VAL   A 36  ? 0.1221 0.1272 0.1177 -0.0104 -0.0018 0.0189  36   VAL   A CB  
1016 C  CG1 . VAL   A 36  ? 0.1251 0.1275 0.1310 -0.0105 0.0046  0.0119  36   VAL   A CG1 
1017 C  CG2 . VAL   A 36  ? 0.1340 0.1325 0.1344 -0.0049 0.0024  0.0297  36   VAL   A CG2 
1027 N  N   . ASN   A 37  ? 0.1125 0.1272 0.1071 -0.0015 0.0034  0.0202  37   ASN   A N   
1028 C  CA  . ASN   A 37  ? 0.1139 0.1254 0.1074 -0.0017 0.0034  0.0230  37   ASN   A CA  
1029 C  C   . ASN   A 37  ? 0.1216 0.1203 0.1094 -0.0056 0.0093  0.0266  37   ASN   A C   
1030 O  O   . ASN   A 37  ? 0.1275 0.1308 0.1056 0.0037  0.0045  0.0139  37   ASN   A O   
1031 C  CB  . ASN   A 37  ? 0.1176 0.1246 0.1283 0.0033  0.0091  0.0210  37   ASN   A CB  
1032 C  CG  . ASN   A 37  ? 0.1185 0.1239 0.1281 0.0025  0.0069  0.0159  37   ASN   A CG  
1033 O  OD1 . ASN   A 37  ? 0.1241 0.1272 0.1454 -0.0017 0.0047  0.0222  37   ASN   A OD1 
1034 N  ND2 . ASN   A 37  ? 0.1257 0.1221 0.1385 0.0036  -0.0004 0.0260  37   ASN   A ND2 
1041 N  N   A ALA   A 38  ? 0.1188 0.1336 0.1149 0.0001  0.0057  0.0165  38   ALA   A N   
1042 N  N   B ALA   A 38  ? 0.1244 0.1271 0.1197 -0.0038 0.0015  0.0228  38   ALA   A N   
1043 C  CA  A ALA   A 38  ? 0.1223 0.1355 0.1177 -0.0052 -0.0003 0.0107  38   ALA   A CA  
1044 C  CA  B ALA   A 38  ? 0.1319 0.1309 0.1283 -0.0097 -0.0067 0.0264  38   ALA   A CA  
1045 C  C   A ALA   A 38  ? 0.1178 0.1340 0.1082 0.0037  0.0002  0.0016  38   ALA   A C   
1046 C  C   B ALA   A 38  ? 0.1303 0.1300 0.1262 -0.0078 -0.0162 0.0123  38   ALA   A C   
1047 O  O   A ALA   A 38  ? 0.1118 0.1232 0.1123 -0.0007 -0.0116 -0.0063 38   ALA   A O   
1048 O  O   B ALA   A 38  ? 0.1321 0.1224 0.1345 -0.0047 -0.0301 0.0121  38   ALA   A O   
1049 C  CB  A ALA   A 38  ? 0.1226 0.1435 0.1284 -0.0150 -0.0068 0.0112  38   ALA   A CB  
1050 C  CB  B ALA   A 38  ? 0.1381 0.1305 0.1288 -0.0075 -0.0115 0.0165  38   ALA   A CB  
1061 N  N   A ALA   A 39  ? 0.1224 0.1317 0.1128 0.0074  0.0113  0.0124  39   ALA   A N   
1062 N  N   B ALA   A 39  ? 0.1346 0.1372 0.1325 -0.0079 -0.0079 0.0245  39   ALA   A N   
1063 C  CA  A ALA   A 39  ? 0.1154 0.1266 0.1180 0.0112  0.0090  0.0105  39   ALA   A CA  
1064 C  CA  B ALA   A 39  ? 0.1330 0.1411 0.1285 -0.0106 -0.0102 0.0223  39   ALA   A CA  
1065 C  C   A ALA   A 39  ? 0.1177 0.1296 0.1163 0.0022  0.0033  0.0062  39   ALA   A C   
1066 C  C   B ALA   A 39  ? 0.1283 0.1334 0.1292 -0.0101 -0.0048 0.0182  39   ALA   A C   
1067 O  O   A ALA   A 39  ? 0.1358 0.1285 0.1131 -0.0054 0.0099  0.0142  39   ALA   A O   
1068 O  O   B ALA   A 39  ? 0.1428 0.1310 0.1342 -0.0084 -0.0124 0.0109  39   ALA   A O   
1069 C  CB  A ALA   A 39  ? 0.1092 0.1244 0.1360 0.0115  -0.0025 0.0065  39   ALA   A CB  
1070 C  CB  B ALA   A 39  ? 0.1454 0.1451 0.1285 -0.0097 -0.0144 0.0167  39   ALA   A CB  
1081 N  N   A ASN   A 40  ? 0.1202 0.1319 0.1180 -0.0090 0.0064  0.0008  40   ASN   A N   
1082 N  N   B ASN   A 40  ? 0.1256 0.1271 0.1187 -0.0067 0.0105  0.0269  40   ASN   A N   
1083 C  CA  A ASN   A 40  ? 0.1264 0.1314 0.1148 -0.0076 0.0005  0.0001  40   ASN   A CA  
1084 C  CA  B ASN   A 40  ? 0.1256 0.1207 0.1181 -0.0028 -0.0086 0.0224  40   ASN   A CA  
1085 C  C   A ASN   A 40  ? 0.1271 0.1193 0.1022 -0.0012 0.0075  0.0062  40   ASN   A C   
1086 C  C   B ASN   A 40  ? 0.1226 0.1180 0.1175 -0.0088 0.0004  0.0261  40   ASN   A C   
1087 O  O   A ASN   A 40  ? 0.1284 0.1223 0.0985 -0.0038 0.0067  0.0080  40   ASN   A O   
1088 O  O   B ASN   A 40  ? 0.1151 0.1244 0.1232 -0.0146 -0.0046 0.0309  40   ASN   A O   
1089 C  CB  A ASN   A 40  ? 0.1297 0.1443 0.1277 0.0012  -0.0143 0.0073  40   ASN   A CB  
1090 C  CB  B ASN   A 40  ? 0.1337 0.1174 0.1280 0.0038  -0.0068 0.0172  40   ASN   A CB  
1091 C  CG  A ASN   A 40  ? 0.1428 0.1453 0.1565 0.0021  -0.0085 0.0191  40   ASN   A CG  
1092 C  CG  B ASN   A 40  ? 0.1353 0.1150 0.1314 0.0011  -0.0090 0.0068  40   ASN   A CG  
1093 O  OD1 A ASN   A 40  ? 0.1557 0.1421 0.1677 0.0020  -0.0100 0.0307  40   ASN   A OD1 
1094 O  OD1 B ASN   A 40  ? 0.1391 0.1146 0.1421 0.0001  0.0006  -0.0069 40   ASN   A OD1 
1095 N  ND2 A ASN   A 40  ? 0.1487 0.1613 0.1824 0.0053  0.0080  0.0043  40   ASN   A ND2 
1096 N  ND2 B ASN   A 40  ? 0.1362 0.1206 0.1448 -0.0057 0.0028  -0.0091 40   ASN   A ND2 
1109 N  N   A VAL   A 41  ? 0.1241 0.1268 0.1035 -0.0028 0.0097  0.0099  41   VAL   A N   
1110 N  N   B VAL   A 41  ? 0.1255 0.1290 0.1236 -0.0022 0.0025  0.0275  41   VAL   A N   
1111 C  CA  A VAL   A 41  ? 0.1250 0.1285 0.1184 -0.0012 0.0096  0.0130  41   VAL   A CA  
1112 C  CA  B VAL   A 41  ? 0.1251 0.1375 0.1161 -0.0036 0.0094  0.0222  41   VAL   A CA  
1113 C  C   A VAL   A 41  ? 0.1231 0.1222 0.1190 -0.0005 0.0064  0.0144  41   VAL   A C   
1114 C  C   B VAL   A 41  ? 0.1192 0.1316 0.1112 -0.0080 0.0139  0.0176  41   VAL   A C   
1115 O  O   A VAL   A 41  ? 0.1355 0.1231 0.1256 0.0053  -0.0034 0.0079  41   VAL   A O   
1116 O  O   B VAL   A 41  ? 0.1301 0.1258 0.1107 -0.0031 0.0022  0.0132  41   VAL   A O   
1117 C  CB  A VAL   A 41  ? 0.1299 0.1351 0.1183 -0.0005 0.0081  0.0071  41   VAL   A CB  
1118 C  CB  B VAL   A 41  ? 0.1341 0.1486 0.1237 0.0009  0.0149  0.0259  41   VAL   A CB  
1119 C  CG1 A VAL   A 41  ? 0.1430 0.1381 0.1413 0.0010  0.0031  0.0113  41   VAL   A CG1 
1120 C  CG1 B VAL   A 41  ? 0.1500 0.1576 0.1317 -0.0057 0.0198  0.0215  41   VAL   A CG1 
1121 C  CG2 A VAL   A 41  ? 0.1384 0.1399 0.1082 -0.0021 0.0164  0.0116  41   VAL   A CG2 
1122 C  CG2 B VAL   A 41  ? 0.1304 0.1516 0.1243 0.0029  0.0045  0.0277  41   VAL   A CG2 
1141 N  N   A TYR   A 42  ? 0.1107 0.1181 0.1467 -0.0043 0.0092  0.0180  42   TYR   A N   
1142 N  N   B TYR   A 42  ? 0.1155 0.1317 0.1188 -0.0033 0.0154  0.0219  42   TYR   A N   
1143 C  CA  A TYR   A 42  ? 0.1167 0.1177 0.1479 -0.0082 0.0098  0.0209  42   TYR   A CA  
1144 C  CA  B TYR   A 42  ? 0.1137 0.1343 0.1195 -0.0000 0.0185  0.0321  42   TYR   A CA  
1145 C  C   A TYR   A 42  ? 0.1151 0.1096 0.1413 0.0021  0.0059  0.0201  42   TYR   A C   
1146 C  C   B TYR   A 42  ? 0.1149 0.1418 0.1215 -0.0085 0.0084  0.0372  42   TYR   A C   
1147 O  O   A TYR   A 42  ? 0.1148 0.1128 0.1655 -0.0071 0.0087  -0.0074 42   TYR   A O   
1148 O  O   B TYR   A 42  ? 0.1136 0.1474 0.1219 -0.0162 0.0063  0.0274  42   TYR   A O   
1149 C  CB  A TYR   A 42  ? 0.1312 0.1350 0.1438 -0.0092 0.0211  0.0328  42   TYR   A CB  
1150 C  CB  B TYR   A 42  ? 0.1187 0.1337 0.1296 0.0026  0.0118  0.0391  42   TYR   A CB  
1151 C  CG  A TYR   A 42  ? 0.1396 0.1439 0.1416 -0.0055 0.0068  0.0369  42   TYR   A CG  
1152 C  CG  B TYR   A 42  ? 0.1293 0.1407 0.1343 0.0098  -0.0011 0.0400  42   TYR   A CG  
1153 C  CD1 A TYR   A 42  ? 0.1420 0.1568 0.1371 -0.0077 0.0030  0.0318  42   TYR   A CD1 
1154 C  CD1 B TYR   A 42  ? 0.1288 0.1463 0.1289 0.0049  0.0033  0.0469  42   TYR   A CD1 
1155 C  CD2 A TYR   A 42  ? 0.1396 0.1638 0.1574 0.0086  0.0040  0.0300  42   TYR   A CD2 
1156 C  CD2 B TYR   A 42  ? 0.1452 0.1595 0.1596 0.0179  -0.0055 0.0292  42   TYR   A CD2 
1157 C  CE1 A TYR   A 42  ? 0.1525 0.1662 0.1346 -0.0053 0.0007  0.0297  42   TYR   A CE1 
1158 C  CE1 B TYR   A 42  ? 0.1327 0.1552 0.1348 0.0026  0.0038  0.0431  42   TYR   A CE1 
1159 C  CE2 A TYR   A 42  ? 0.1523 0.1731 0.1744 -0.0038 0.0038  0.0339  42   TYR   A CE2 
1160 C  CE2 B TYR   A 42  ? 0.1496 0.1688 0.1624 0.0129  -0.0036 0.0353  42   TYR   A CE2 
1161 C  CZ  A TYR   A 42  ? 0.1604 0.1735 0.1440 -0.0067 0.0058  0.0341  42   TYR   A CZ  
1162 C  CZ  B TYR   A 42  ? 0.1450 0.1635 0.1451 0.0069  0.0014  0.0329  42   TYR   A CZ  
1163 O  OH  A TYR   A 42  ? 0.1736 0.1920 0.1568 -0.0083 0.0016  0.0298  42   TYR   A OH  
1164 O  OH  B TYR   A 42  ? 0.1480 0.1739 0.1522 0.0004  -0.0010 0.0248  42   TYR   A OH  
1183 N  N   A LEU   A 43  ? 0.1205 0.1117 0.1305 -0.0063 0.0108  -0.0009 43   LEU   A N   
1184 N  N   B LEU   A 43  ? 0.1176 0.1417 0.1301 -0.0101 0.0009  0.0362  43   LEU   A N   
1185 C  CA  A LEU   A 43  ? 0.1095 0.1163 0.1235 -0.0099 0.0054  0.0031  43   LEU   A CA  
1186 C  CA  B LEU   A 43  ? 0.1229 0.1366 0.1324 -0.0058 0.0015  0.0340  43   LEU   A CA  
1187 C  C   A LEU   A 43  ? 0.1111 0.1227 0.1181 -0.0018 0.0027  0.0002  43   LEU   A C   
1188 C  C   B LEU   A 43  ? 0.1234 0.1339 0.1340 -0.0068 -0.0038 0.0266  43   LEU   A C   
1189 O  O   A LEU   A 43  ? 0.1279 0.1285 0.1343 0.0093  -0.0091 0.0025  43   LEU   A O   
1190 O  O   B LEU   A 43  ? 0.1293 0.1367 0.1364 -0.0090 -0.0175 0.0187  43   LEU   A O   
1191 C  CB  A LEU   A 43  ? 0.1217 0.1163 0.1422 -0.0125 -0.0045 0.0004  43   LEU   A CB  
1192 C  CB  B LEU   A 43  ? 0.1217 0.1272 0.1328 -0.0059 0.0064  0.0326  43   LEU   A CB  
1193 C  CG  A LEU   A 43  ? 0.1267 0.1249 0.1552 -0.0059 -0.0080 -0.0018 43   LEU   A CG  
1194 C  CG  B LEU   A 43  ? 0.1229 0.1229 0.1386 0.0052  0.0128  0.0242  43   LEU   A CG  
1195 C  CD1 A LEU   A 43  ? 0.1264 0.1363 0.1800 -0.0052 -0.0092 0.0100  43   LEU   A CD1 
1196 C  CD1 B LEU   A 43  ? 0.1295 0.1309 0.1456 0.0064  0.0191  0.0346  43   LEU   A CD1 
1197 C  CD2 A LEU   A 43  ? 0.1327 0.1308 0.1534 -0.0088 -0.0110 0.0142  43   LEU   A CD2 
1198 C  CD2 B LEU   A 43  ? 0.1289 0.1161 0.1451 0.0074  0.0098  0.0355  43   LEU   A CD2 
1221 N  N   A LYS   A 44  ? 0.1206 0.1249 0.1218 -0.0043 0.0090  0.0023  44   LYS   A N   
1222 N  N   B LYS   A 44  ? 0.1208 0.1351 0.1282 0.0002  -0.0036 0.0305  44   LYS   A N   
1223 C  CA  A LYS   A 44  ? 0.1304 0.1205 0.1332 -0.0040 0.0179  0.0125  44   LYS   A CA  
1224 C  CA  B LYS   A 44  ? 0.1321 0.1355 0.1187 0.0015  -0.0056 0.0297  44   LYS   A CA  
1225 C  C   A LYS   A 44  ? 0.1193 0.1187 0.1310 0.0014  0.0128  0.0130  44   LYS   A C   
1226 C  C   B LYS   A 44  ? 0.1299 0.1340 0.1116 0.0001  -0.0044 0.0141  44   LYS   A C   
1227 O  O   A LYS   A 44  ? 0.1230 0.1391 0.1574 0.0035  0.0033  0.0043  44   LYS   A O   
1228 O  O   B LYS   A 44  ? 0.1278 0.1382 0.1033 -0.0034 -0.0019 0.0015  44   LYS   A O   
1229 C  CB  A LYS   A 44  ? 0.1602 0.1287 0.1757 -0.0042 0.0215  0.0203  44   LYS   A CB  
1230 C  CB  B LYS   A 44  ? 0.1579 0.1539 0.1646 0.0042  0.0062  0.0371  44   LYS   A CB  
1231 C  CG  A LYS   A 44  ? 0.1897 0.1500 0.2387 -0.0138 0.0454  0.0384  44   LYS   A CG  
1232 C  CG  B LYS   A 44  ? 0.1737 0.1779 0.2235 0.0100  0.0194  0.0423  44   LYS   A CG  
1233 C  CD  A LYS   A 44  ? 0.2247 0.2064 0.3552 -0.0201 0.0453  0.0243  44   LYS   A CD  
1234 C  CD  B LYS   A 44  ? 0.1959 0.2174 0.3058 0.0059  0.0130  0.0323  44   LYS   A CD  
1235 C  CE  A LYS   A 44  ? 0.2466 0.2392 0.4314 -0.0209 0.0452  0.0096  44   LYS   A CE  
1236 C  CE  B LYS   A 44  ? 0.2080 0.2405 0.3599 -0.0031 0.0097  0.0282  44   LYS   A CE  
1237 N  NZ  A LYS   A 44  ? 0.2584 0.2613 0.4668 -0.0175 0.0433  0.0036  44   LYS   A NZ  
1238 N  NZ  B LYS   A 44  ? 0.2177 0.2558 0.3874 -0.0173 0.0084  0.0225  44   LYS   A NZ  
1265 N  N   A HIS   A 45  ? 0.1142 0.1141 0.1204 -0.0023 0.0111  0.0155  45   HIS   A N   
1266 N  N   B HIS   A 45  ? 0.1368 0.1357 0.1246 -0.0052 -0.0126 0.0145  45   HIS   A N   
1267 C  CA  A HIS   A 45  ? 0.1106 0.1152 0.1117 0.0037  0.0067  0.0077  45   HIS   A CA  
1268 C  CA  B HIS   A 45  ? 0.1394 0.1391 0.1405 -0.0030 -0.0182 0.0097  45   HIS   A CA  
1269 C  C   A HIS   A 45  ? 0.1154 0.1271 0.1237 0.0060  0.0048  0.0127  45   HIS   A C   
1270 C  C   B HIS   A 45  ? 0.1460 0.1451 0.1485 -0.0064 -0.0119 0.0100  45   HIS   A C   
1271 O  O   A HIS   A 45  ? 0.1132 0.1188 0.1419 -0.0040 0.0062  0.0078  45   HIS   A O   
1272 O  O   B HIS   A 45  ? 0.1517 0.1464 0.1654 -0.0038 -0.0129 0.0037  45   HIS   A O   
1273 C  CB  A HIS   A 45  ? 0.1117 0.1186 0.1057 -0.0040 0.0080  0.0139  45   HIS   A CB  
1274 C  CB  B HIS   A 45  ? 0.1323 0.1392 0.1503 0.0011  -0.0258 0.0048  45   HIS   A CB  
1275 C  CG  A HIS   A 45  ? 0.1230 0.1098 0.1045 -0.0036 0.0077  0.0128  45   HIS   A CG  
1276 C  CG  B HIS   A 45  ? 0.1218 0.1306 0.1426 -0.0009 -0.0063 0.0052  45   HIS   A CG  
1277 N  ND1 A HIS   A 45  ? 0.1227 0.1172 0.1109 -0.0003 0.0066  0.0118  45   HIS   A ND1 
1278 N  ND1 B HIS   A 45  ? 0.1182 0.1330 0.1499 0.0022  -0.0113 0.0169  45   HIS   A ND1 
1279 C  CD2 A HIS   A 45  ? 0.1272 0.1175 0.1098 -0.0064 0.0009  0.0223  45   HIS   A CD2 
1280 C  CD2 B HIS   A 45  ? 0.1102 0.1226 0.1250 -0.0011 -0.0010 -0.0036 45   HIS   A CD2 
1281 C  CE1 A HIS   A 45  ? 0.1294 0.1238 0.1156 -0.0042 0.0102  0.0203  45   HIS   A CE1 
1282 C  CE1 B HIS   A 45  ? 0.1091 0.1212 0.1186 -0.0058 -0.0129 0.0061  45   HIS   A CE1 
1283 N  NE2 A HIS   A 45  ? 0.1336 0.1221 0.1143 0.0050  0.0089  0.0249  45   HIS   A NE2 
1284 N  NE2 B HIS   A 45  ? 0.1041 0.1160 0.1103 -0.0081 -0.0100 -0.0086 45   HIS   A NE2 
1299 N  N   A GLY   A 46  ? 0.1186 0.1404 0.1392 0.0184  -0.0083 0.0252  46   GLY   A N   
1300 N  N   B GLY   A 46  ? 0.1447 0.1458 0.1447 -0.0128 -0.0076 0.0148  46   GLY   A N   
1301 C  CA  A GLY   A 46  ? 0.1261 0.1509 0.1666 0.0183  -0.0041 0.0325  46   GLY   A CA  
1302 C  CA  B GLY   A 46  ? 0.1389 0.1490 0.1418 -0.0106 0.0006  0.0186  46   GLY   A CA  
1303 C  C   A GLY   A 46  ? 0.1293 0.1431 0.1508 0.0163  -0.0116 0.0465  46   GLY   A C   
1304 C  C   B GLY   A 46  ? 0.1354 0.1413 0.1220 -0.0008 0.0051  0.0256  46   GLY   A C   
1305 O  O   A GLY   A 46  ? 0.1395 0.1433 0.1538 0.0142  -0.0160 0.0456  46   GLY   A O   
1306 O  O   B GLY   A 46  ? 0.1427 0.1430 0.1313 0.0037  0.0040  0.0098  46   GLY   A O   
1313 N  N   A GLY   A 47  ? 0.1270 0.1435 0.1382 0.0154  -0.0117 0.0255  47   GLY   A N   
1314 N  N   B GLY   A 47  ? 0.1374 0.1457 0.1279 0.0035  0.0117  0.0103  47   GLY   A N   
1315 C  CA  A GLY   A 47  ? 0.1330 0.1477 0.1415 0.0211  -0.0158 0.0236  47   GLY   A CA  
1316 C  CA  B GLY   A 47  ? 0.1354 0.1518 0.1341 0.0046  0.0055  0.0142  47   GLY   A CA  
1317 C  C   A GLY   A 47  ? 0.1325 0.1341 0.1445 0.0194  -0.0111 0.0169  47   GLY   A C   
1318 C  C   B GLY   A 47  ? 0.1248 0.1398 0.1148 0.0031  0.0029  0.0079  47   GLY   A C   
1319 O  O   A GLY   A 47  ? 0.1321 0.1257 0.1580 0.0226  -0.0075 0.0133  47   GLY   A O   
1320 O  O   B GLY   A 47  ? 0.1192 0.1392 0.1269 0.0028  -0.0079 0.0129  47   GLY   A O   
1327 N  N   A GLY   A 48  ? 0.1251 0.1375 0.1332 0.0198  -0.0096 0.0126  48   GLY   A N   
1328 N  N   B GLY   A 48  ? 0.1281 0.1458 0.1181 0.0015  0.0065  0.0035  48   GLY   A N   
1329 C  CA  A GLY   A 48  ? 0.1193 0.1406 0.1481 0.0130  -0.0117 0.0048  48   GLY   A CA  
1330 C  CA  B GLY   A 48  ? 0.1248 0.1312 0.1115 -0.0030 0.0026  -0.0080 48   GLY   A CA  
1331 C  C   A GLY   A 48  ? 0.1210 0.1380 0.1366 0.0042  0.0019  0.0017  48   GLY   A C   
1332 C  C   B GLY   A 48  ? 0.1265 0.1241 0.1152 -0.0077 0.0000  0.0020  48   GLY   A C   
1333 O  O   A GLY   A 48  ? 0.1314 0.1380 0.1335 -0.0011 0.0078  0.0133  48   GLY   A O   
1334 O  O   B GLY   A 48  ? 0.1391 0.1205 0.1015 -0.0081 0.0066  -0.0038 48   GLY   A O   
1341 N  N   A VAL   A 49  ? 0.1287 0.1317 0.1494 0.0014  -0.0138 0.0065  49   VAL   A N   
1342 N  N   B VAL   A 49  ? 0.1210 0.1227 0.1447 -0.0076 -0.0060 0.0014  49   VAL   A N   
1343 C  CA  A VAL   A 49  ? 0.1315 0.1185 0.1491 -0.0016 0.0038  0.0042  49   VAL   A CA  
1344 C  CA  B VAL   A 49  ? 0.1107 0.1212 0.1474 -0.0042 -0.0025 0.0099  49   VAL   A CA  
1345 C  C   A VAL   A 49  ? 0.1284 0.1152 0.1241 -0.0033 -0.0028 0.0151  49   VAL   A C   
1346 C  C   B VAL   A 49  ? 0.1176 0.1134 0.1216 0.0056  0.0050  0.0072  49   VAL   A C   
1347 O  O   A VAL   A 49  ? 0.1330 0.1278 0.1279 -0.0100 -0.0044 0.0051  49   VAL   A O   
1348 O  O   B VAL   A 49  ? 0.1179 0.1095 0.1111 0.0116  0.0096  0.0119  49   VAL   A O   
1349 C  CB  A VAL   A 49  ? 0.1452 0.1310 0.1612 -0.0013 0.0036  0.0027  49   VAL   A CB  
1350 C  CB  B VAL   A 49  ? 0.1052 0.1226 0.1663 -0.0016 -0.0139 0.0071  49   VAL   A CB  
1351 C  CG1 A VAL   A 49  ? 0.1489 0.1263 0.1693 0.0057  0.0159  0.0078  49   VAL   A CG1 
1352 C  CG1 B VAL   A 49  ? 0.0999 0.1174 0.1595 0.0115  -0.0100 0.0017  49   VAL   A CG1 
1353 C  CG2 A VAL   A 49  ? 0.1584 0.1455 0.2058 -0.0132 0.0147  -0.0070 49   VAL   A CG2 
1354 C  CG2 B VAL   A 49  ? 0.1059 0.1251 0.1822 -0.0047 -0.0126 0.0082  49   VAL   A CG2 
1373 N  N   A ALA   A 50  ? 0.1197 0.1205 0.1271 -0.0102 -0.0157 0.0159  50   ALA   A N   
1374 N  N   B ALA   A 50  ? 0.1204 0.1152 0.1068 0.0095  0.0038  0.0040  50   ALA   A N   
1375 C  CA  A ALA   A 50  ? 0.1139 0.1201 0.1284 -0.0162 -0.0084 0.0132  50   ALA   A CA  
1376 C  CA  B ALA   A 50  ? 0.1223 0.1160 0.0972 0.0068  0.0008  0.0050  50   ALA   A CA  
1377 C  C   A ALA   A 50  ? 0.1087 0.1241 0.1234 -0.0159 -0.0058 0.0134  50   ALA   A C   
1378 C  C   B ALA   A 50  ? 0.1269 0.1225 0.1022 0.0007  -0.0066 0.0037  50   ALA   A C   
1379 O  O   A ALA   A 50  ? 0.1087 0.1245 0.1375 -0.0067 0.0016  0.0058  50   ALA   A O   
1380 O  O   B ALA   A 50  ? 0.1343 0.1224 0.1010 0.0028  -0.0046 0.0040  50   ALA   A O   
1381 C  CB  A ALA   A 50  ? 0.1110 0.1273 0.1419 -0.0178 -0.0111 0.0098  50   ALA   A CB  
1382 C  CB  B ALA   A 50  ? 0.1250 0.1123 0.0940 0.0106  0.0124  -0.0040 50   ALA   A CB  
1393 N  N   A GLY   A 51  ? 0.1197 0.1157 0.1251 -0.0030 -0.0137 0.0183  51   GLY   A N   
1394 N  N   B GLY   A 51  ? 0.1337 0.1210 0.1197 0.0041  -0.0104 0.0019  51   GLY   A N   
1395 C  CA  A GLY   A 51  ? 0.1265 0.1116 0.1352 0.0045  -0.0132 0.0122  51   GLY   A CA  
1396 C  CA  B GLY   A 51  ? 0.1359 0.1207 0.1267 0.0038  -0.0095 -0.0026 51   GLY   A CA  
1397 C  C   A GLY   A 51  ? 0.1160 0.1221 0.1364 0.0086  -0.0058 0.0012  51   GLY   A C   
1398 C  C   B GLY   A 51  ? 0.1274 0.1282 0.1292 0.0037  -0.0033 -0.0071 51   GLY   A C   
1399 O  O   A GLY   A 51  ? 0.1185 0.1315 0.1470 0.0062  -0.0118 0.0005  51   GLY   A O   
1400 O  O   B GLY   A 51  ? 0.1357 0.1333 0.1290 0.0002  -0.0063 -0.0135 51   GLY   A O   
1407 N  N   . ALA   A 52  ? 0.1201 0.1338 0.1248 -0.0002 0.0004  -0.0076 52   ALA   A N   
1408 C  CA  . ALA   A 52  ? 0.1200 0.1516 0.1391 -0.0026 -0.0010 -0.0058 52   ALA   A CA  
1409 C  C   . ALA   A 52  ? 0.1217 0.1473 0.1240 -0.0083 0.0009  0.0011  52   ALA   A C   
1410 O  O   . ALA   A 52  ? 0.1310 0.1511 0.1379 -0.0055 -0.0004 -0.0071 52   ALA   A O   
1411 C  CB  . ALA   A 52  ? 0.1251 0.1817 0.1584 -0.0022 -0.0039 0.0038  52   ALA   A CB  
1418 N  N   A LEU   A 53  ? 0.1206 0.1402 0.1253 -0.0074 0.0009  -0.0019 53   LEU   A N   
1419 N  N   B LEU   A 53  ? 0.1172 0.1390 0.1205 -0.0043 -0.0005 0.0019  53   LEU   A N   
1420 C  CA  A LEU   A 53  ? 0.1340 0.1471 0.1271 -0.0095 0.0001  0.0027  53   LEU   A CA  
1421 C  CA  B LEU   A 53  ? 0.1231 0.1397 0.1159 -0.0021 -0.0038 0.0065  53   LEU   A CA  
1422 C  C   A LEU   A 53  ? 0.1288 0.1437 0.1049 -0.0011 0.0047  -0.0036 53   LEU   A C   
1423 C  C   B LEU   A 53  ? 0.1188 0.1358 0.0929 0.0049  0.0006  0.0049  53   LEU   A C   
1424 O  O   A LEU   A 53  ? 0.1395 0.1451 0.1249 -0.0131 0.0044  0.0013  53   LEU   A O   
1425 O  O   B LEU   A 53  ? 0.1268 0.1366 0.0999 0.0047  -0.0045 0.0076  53   LEU   A O   
1426 C  CB  A LEU   A 53  ? 0.1426 0.1495 0.1386 -0.0125 0.0041  0.0136  53   LEU   A CB  
1427 C  CB  B LEU   A 53  ? 0.1247 0.1375 0.1215 -0.0015 -0.0076 0.0124  53   LEU   A CB  
1428 C  CG  A LEU   A 53  ? 0.1456 0.1498 0.1379 -0.0186 0.0071  0.0099  53   LEU   A CG  
1429 C  CG  B LEU   A 53  ? 0.1261 0.1367 0.1225 -0.0026 -0.0147 0.0074  53   LEU   A CG  
1430 C  CD1 A LEU   A 53  ? 0.1425 0.1545 0.1374 -0.0029 0.0050  0.0155  53   LEU   A CD1 
1431 C  CD1 B LEU   A 53  ? 0.1379 0.1390 0.1403 -0.0014 -0.0103 -0.0026 53   LEU   A CD1 
1432 C  CD2 A LEU   A 53  ? 0.1626 0.1673 0.1437 -0.0263 0.0072  0.0069  53   LEU   A CD2 
1433 C  CD2 B LEU   A 53  ? 0.1304 0.1427 0.1310 -0.0094 -0.0038 0.0010  53   LEU   A CD2 
1456 N  N   A ASN   A 54  ? 0.1246 0.1366 0.1230 -0.0061 -0.0055 0.0007  54   ASN   A N   
1457 N  N   B ASN   A 54  ? 0.1181 0.1359 0.0992 -0.0001 0.0011  0.0088  54   ASN   A N   
1458 C  CA  A ASN   A 54  ? 0.1108 0.1298 0.1420 -0.0054 -0.0021 -0.0051 54   ASN   A CA  
1459 C  CA  B ASN   A 54  ? 0.1113 0.1343 0.1055 0.0028  0.0007  0.0002  54   ASN   A CA  
1460 C  C   A ASN   A 54  ? 0.1209 0.1305 0.1321 -0.0149 0.0007  -0.0023 54   ASN   A C   
1461 C  C   B ASN   A 54  ? 0.1227 0.1351 0.1115 -0.0059 -0.0006 -0.0009 54   ASN   A C   
1462 O  O   A ASN   A 54  ? 0.1240 0.1410 0.1429 -0.0104 -0.0061 -0.0054 54   ASN   A O   
1463 O  O   B ASN   A 54  ? 0.1289 0.1429 0.1160 -0.0032 -0.0081 -0.0030 54   ASN   A O   
1464 C  CB  A ASN   A 54  ? 0.1101 0.1242 0.1512 -0.0118 -0.0101 -0.0051 54   ASN   A CB  
1465 C  CB  B ASN   A 54  ? 0.1111 0.1327 0.0923 0.0096  -0.0004 0.0014  54   ASN   A CB  
1466 C  CG  A ASN   A 54  ? 0.1155 0.1303 0.1526 -0.0092 -0.0053 -0.0014 54   ASN   A CG  
1467 C  CG  B ASN   A 54  ? 0.1159 0.1273 0.0859 0.0099  0.0037  -0.0034 54   ASN   A CG  
1468 O  OD1 A ASN   A 54  ? 0.1197 0.1217 0.1684 -0.0105 -0.0166 0.0143  54   ASN   A OD1 
1469 O  OD1 B ASN   A 54  ? 0.1144 0.1193 0.0905 0.0128  -0.0002 -0.0138 54   ASN   A OD1 
1470 N  ND2 A ASN   A 54  ? 0.1148 0.1368 0.1694 -0.0009 -0.0138 0.0018  54   ASN   A ND2 
1471 N  ND2 B ASN   A 54  ? 0.1251 0.1237 0.0993 0.0070  -0.0018 0.0054  54   ASN   A ND2 
1484 N  N   . LYS   A 55  ? 0.1234 0.1355 0.1273 -0.0042 -0.0026 -0.0014 55   LYS   A N   
1485 C  CA  . LYS   A 55  ? 0.1349 0.1398 0.1342 0.0048  -0.0125 -0.0062 55   LYS   A CA  
1486 C  C   . LYS   A 55  ? 0.1288 0.1487 0.1385 0.0002  -0.0061 -0.0125 55   LYS   A C   
1487 O  O   . LYS   A 55  ? 0.1399 0.1618 0.1427 0.0057  -0.0109 -0.0223 55   LYS   A O   
1488 C  CB  . LYS   A 55  ? 0.1400 0.1506 0.1457 0.0135  -0.0080 -0.0118 55   LYS   A CB  
1489 C  CG  . LYS   A 55  ? 0.1597 0.1762 0.1633 0.0243  -0.0253 -0.0262 55   LYS   A CG  
1490 C  CD  . LYS   A 55  ? 0.1702 0.2038 0.1864 0.0400  -0.0218 -0.0167 55   LYS   A CD  
1491 C  CE  . LYS   A 55  ? 0.1956 0.2398 0.2088 0.0578  -0.0290 -0.0190 55   LYS   A CE  
1492 N  NZ  . LYS   A 55  ? 0.2096 0.2570 0.2133 0.0634  -0.0256 -0.0208 55   LYS   A NZ  
1507 N  N   . ALA   A 56  ? 0.1342 0.1573 0.1333 -0.0094 0.0043  -0.0096 56   ALA   A N   
1508 C  CA  . ALA   A 56  ? 0.1444 0.1754 0.1362 -0.0094 0.0127  -0.0062 56   ALA   A CA  
1509 C  C   . ALA   A 56  ? 0.1475 0.1798 0.1107 -0.0136 0.0057  -0.0160 56   ALA   A C   
1510 O  O   . ALA   A 56  ? 0.1609 0.2190 0.1256 -0.0000 0.0100  -0.0129 56   ALA   A O   
1511 C  CB  . ALA   A 56  ? 0.1461 0.2000 0.1425 -0.0164 0.0078  0.0025  56   ALA   A CB  
1517 N  N   . THR   A 57  ? 0.1315 0.1591 0.1125 -0.0070 0.0096  -0.0108 57   THR   A N   
1518 C  CA  . THR   A 57  ? 0.1403 0.1602 0.1208 -0.0083 -0.0032 -0.0077 57   THR   A CA  
1519 C  C   . THR   A 57  ? 0.1433 0.1628 0.1270 -0.0067 -0.0034 -0.0191 57   THR   A C   
1520 O  O   . THR   A 57  ? 0.1449 0.1687 0.1392 -0.0137 -0.0143 -0.0228 57   THR   A O   
1521 C  CB  . THR   A 57  ? 0.1392 0.1613 0.1268 -0.0091 -0.0016 -0.0042 57   THR   A CB  
1522 O  OG1 . THR   A 57  ? 0.1307 0.1577 0.1185 -0.0044 -0.0030 -0.0029 57   THR   A OG1 
1523 C  CG2 . THR   A 57  ? 0.1428 0.1558 0.1264 -0.0062 -0.0015 0.0072  57   THR   A CG2 
1531 N  N   . ASN   A 58  ? 0.1437 0.1555 0.1451 -0.0028 0.0008  -0.0220 58   ASN   A N   
1532 C  CA  . ASN   A 58  ? 0.1608 0.1542 0.1697 -0.0041 0.0060  -0.0339 58   ASN   A CA  
1533 C  C   . ASN   A 58  ? 0.1393 0.1403 0.1541 0.0046  -0.0038 -0.0204 58   ASN   A C   
1534 O  O   . ASN   A 58  ? 0.1465 0.1548 0.1623 -0.0115 -0.0067 -0.0232 58   ASN   A O   
1535 C  CB  . ASN   A 58  ? 0.2061 0.1718 0.2044 -0.0187 0.0280  -0.0416 58   ASN   A CB  
1536 C  CG  . ASN   A 58  ? 0.2509 0.1982 0.2754 -0.0161 0.0287  -0.0301 58   ASN   A CG  
1537 O  OD1 . ASN   A 58  ? 0.2783 0.1979 0.3197 0.0207  0.0590  -0.0233 58   ASN   A OD1 
1538 N  ND2 . ASN   A 58  ? 0.2623 0.2080 0.2985 -0.0171 0.0074  -0.0341 58   ASN   A ND2 
1545 N  N   . ASN   A 59  ? 0.1340 0.1336 0.1374 -0.0025 -0.0103 -0.0114 59   ASN   A N   
1546 C  CA  . ASN   A 59  ? 0.1368 0.1222 0.1337 -0.0065 -0.0063 -0.0012 59   ASN   A CA  
1547 C  C   . ASN   A 59  ? 0.1335 0.1321 0.1285 -0.0122 -0.0077 0.0024  59   ASN   A C   
1548 O  O   . ASN   A 59  ? 0.1317 0.1424 0.1307 -0.0043 -0.0008 0.0091  59   ASN   A O   
1549 C  CB  . ASN   A 59  ? 0.1426 0.1255 0.1450 0.0018  -0.0204 -0.0136 59   ASN   A CB  
1550 C  CG  . ASN   A 59  ? 0.1389 0.1309 0.1443 -0.0031 -0.0293 -0.0019 59   ASN   A CG  
1551 O  OD1 . ASN   A 59  ? 0.1511 0.1394 0.1398 -0.0094 -0.0253 0.0081  59   ASN   A OD1 
1552 N  ND2 . ASN   A 59  ? 0.1505 0.1363 0.1567 -0.0179 -0.0209 0.0027  59   ASN   A ND2 
1559 N  N   . ALA   A 60  ? 0.1218 0.1346 0.1315 -0.0057 -0.0062 -0.0023 60   ALA   A N   
1560 C  CA  . ALA   A 60  ? 0.1265 0.1347 0.1418 -0.0013 -0.0092 -0.0006 60   ALA   A CA  
1561 C  C   . ALA   A 60  ? 0.1256 0.1344 0.1473 -0.0043 -0.0014 0.0074  60   ALA   A C   
1562 O  O   . ALA   A 60  ? 0.1249 0.1352 0.1630 -0.0038 -0.0110 0.0003  60   ALA   A O   
1563 C  CB  . ALA   A 60  ? 0.1435 0.1500 0.1475 -0.0003 -0.0175 -0.0166 60   ALA   A CB  
1569 N  N   . MET   A 61  ? 0.1200 0.1270 0.1321 -0.0080 0.0027  -0.0017 61   MET   A N   
1570 C  CA  . MET   A 61  ? 0.1237 0.1268 0.1287 0.0001  -0.0003 0.0058  61   MET   A CA  
1571 C  C   . MET   A 61  ? 0.1182 0.1224 0.1395 -0.0047 -0.0096 0.0018  61   MET   A C   
1572 O  O   . MET   A 61  ? 0.1255 0.1235 0.1404 0.0004  0.0006  0.0082  61   MET   A O   
1573 C  CB  . MET   A 61  ? 0.1291 0.1275 0.1258 -0.0014 0.0028  0.0054  61   MET   A CB  
1574 C  CG  . MET   A 61  ? 0.1336 0.1387 0.1409 0.0034  -0.0040 0.0044  61   MET   A CG  
1575 S  SD  . MET   A 61  ? 0.1335 0.1402 0.1676 -0.0107 -0.0041 -0.0137 61   MET   A SD  
1576 C  CE  . MET   A 61  ? 0.1529 0.1570 0.1922 -0.0112 0.0176  -0.0131 61   MET   A CE  
1586 N  N   . GLN   A 62  ? 0.1201 0.1220 0.1351 -0.0035 -0.0021 -0.0024 62   GLN   A N   
1587 C  CA  . GLN   A 62  ? 0.1268 0.1220 0.1367 -0.0016 0.0051  0.0036  62   GLN   A CA  
1588 C  C   . GLN   A 62  ? 0.1275 0.1138 0.1433 -0.0016 0.0072  0.0086  62   GLN   A C   
1589 O  O   . GLN   A 62  ? 0.1299 0.1278 0.1438 -0.0053 0.0029  0.0008  62   GLN   A O   
1590 C  CB  . GLN   A 62  ? 0.1260 0.1186 0.1429 -0.0052 -0.0019 0.0048  62   GLN   A CB  
1591 C  CG  . GLN   A 62  ? 0.1325 0.1175 0.1416 -0.0085 -0.0039 0.0143  62   GLN   A CG  
1592 C  CD  . GLN   A 62  ? 0.1324 0.1224 0.1382 -0.0047 0.0040  0.0179  62   GLN   A CD  
1593 O  OE1 . GLN   A 62  ? 0.1342 0.1372 0.1388 -0.0012 -0.0042 0.0088  62   GLN   A OE1 
1594 N  NE2 . GLN   A 62  ? 0.1422 0.1264 0.1515 0.0016  0.0030  0.0004  62   GLN   A NE2 
1603 N  N   . VAL   A 63  ? 0.1220 0.1220 0.1528 -0.0078 0.0061  -0.0122 63   VAL   A N   
1604 C  CA  . VAL   A 63  ? 0.1248 0.1352 0.1718 -0.0104 0.0028  -0.0059 63   VAL   A CA  
1605 C  C   . VAL   A 63  ? 0.1192 0.1375 0.1614 -0.0138 -0.0066 -0.0093 63   VAL   A C   
1606 O  O   . VAL   A 63  ? 0.1185 0.1372 0.1760 -0.0151 -0.0021 -0.0057 63   VAL   A O   
1607 C  CB  . VAL   A 63  ? 0.1377 0.1495 0.2058 -0.0163 -0.0022 -0.0364 63   VAL   A CB  
1608 C  CG1 . VAL   A 63  ? 0.1468 0.1703 0.2415 -0.0144 -0.0098 -0.0589 63   VAL   A CG1 
1609 C  CG2 . VAL   A 63  ? 0.1423 0.1432 0.2279 -0.0157 0.0098  -0.0316 63   VAL   A CG2 
1619 N  N   . GLU   A 64  ? 0.1184 0.1437 0.1526 -0.0035 -0.0057 -0.0049 64   GLU   A N   
1620 C  CA  . GLU   A 64  ? 0.1190 0.1385 0.1556 -0.0091 -0.0134 0.0007  64   GLU   A CA  
1621 C  C   . GLU   A 64  ? 0.1150 0.1315 0.1530 -0.0068 -0.0003 0.0024  64   GLU   A C   
1622 O  O   . GLU   A 64  ? 0.1250 0.1442 0.1504 -0.0001 0.0003  0.0050  64   GLU   A O   
1623 C  CB  . GLU   A 64  ? 0.1342 0.1506 0.1525 -0.0114 -0.0029 -0.0028 64   GLU   A CB  
1624 C  CG  . GLU   A 64  ? 0.1385 0.1569 0.1695 -0.0106 -0.0074 -0.0027 64   GLU   A CG  
1625 C  CD  . GLU   A 64  ? 0.1529 0.1630 0.1768 -0.0124 0.0021  0.0015  64   GLU   A CD  
1626 O  OE1 . GLU   A 64  ? 0.1540 0.1753 0.2002 -0.0236 0.0078  0.0057  64   GLU   A OE1 
1627 O  OE2 . GLU   A 64  ? 0.1685 0.1572 0.1802 -0.0183 -0.0060 0.0090  64   GLU   A OE2 
1634 N  N   . SER   A 65  ? 0.1117 0.1331 0.1406 -0.0002 -0.0034 0.0068  65   SER   A N   
1635 C  CA  . SER   A 65  ? 0.1188 0.1290 0.1424 -0.0028 -0.0028 -0.0062 65   SER   A CA  
1636 C  C   . SER   A 65  ? 0.1174 0.1317 0.1410 -0.0028 -0.0060 -0.0052 65   SER   A C   
1637 O  O   . SER   A 65  ? 0.1308 0.1418 0.1641 0.0001  0.0151  0.0010  65   SER   A O   
1638 C  CB  . SER   A 65  ? 0.1224 0.1293 0.1380 -0.0058 0.0030  0.0056  65   SER   A CB  
1639 O  OG  . SER   A 65  ? 0.1202 0.1353 0.1535 -0.0088 -0.0004 0.0143  65   SER   A OG  
1645 N  N   . ASP   A 66  ? 0.1201 0.1366 0.1446 -0.0057 0.0113  0.0034  66   ASP   A N   
1646 C  CA  . ASP   A 66  ? 0.1340 0.1410 0.1614 -0.0003 0.0098  0.0157  66   ASP   A CA  
1647 C  C   . ASP   A 66  ? 0.1309 0.1356 0.1677 -0.0030 0.0100  0.0198  66   ASP   A C   
1648 O  O   . ASP   A 66  ? 0.1371 0.1486 0.1880 -0.0028 0.0237  0.0232  66   ASP   A O   
1649 C  CB  . ASP   A 66  ? 0.1409 0.1491 0.1912 0.0094  0.0116  0.0288  66   ASP   A CB  
1650 C  CG  . ASP   A 66  ? 0.1660 0.1649 0.2146 0.0039  0.0075  0.0454  66   ASP   A CG  
1651 O  OD1 . ASP   A 66  ? 0.1679 0.1961 0.1919 -0.0111 -0.0046 0.0483  66   ASP   A OD1 
1652 O  OD2 . ASP   A 66  ? 0.1803 0.1769 0.2901 0.0221  -0.0103 0.0202  66   ASP   A OD2 
1657 N  N   . ASP   A 67  ? 0.1233 0.1383 0.1827 -0.0052 0.0077  0.0220  67   ASP   A N   
1658 C  CA  . ASP   A 67  ? 0.1209 0.1552 0.1989 -0.0031 -0.0007 0.0325  67   ASP   A CA  
1659 C  C   . ASP   A 67  ? 0.1271 0.1613 0.1878 -0.0003 0.0094  0.0344  67   ASP   A C   
1660 O  O   . ASP   A 67  ? 0.1203 0.1677 0.2135 -0.0007 0.0277  0.0383  67   ASP   A O   
1661 C  CB  . ASP   A 67  ? 0.1313 0.1647 0.2289 -0.0060 -0.0156 0.0397  67   ASP   A CB  
1662 C  CG  . ASP   A 67  ? 0.1313 0.1813 0.2666 -0.0107 -0.0294 0.0512  67   ASP   A CG  
1663 O  OD1 . ASP   A 67  ? 0.1401 0.2075 0.3549 -0.0168 -0.0394 0.0668  67   ASP   A OD1 
1664 O  OD2 . ASP   A 67  ? 0.1330 0.1832 0.2488 0.0020  -0.0161 0.0390  67   ASP   A OD2 
1669 N  N   . TYR   A 68  ? 0.1289 0.1474 0.1779 0.0056  0.0167  0.0328  68   TYR   A N   
1670 C  CA  . TYR   A 68  ? 0.1376 0.1399 0.1811 0.0078  0.0247  0.0288  68   TYR   A CA  
1671 C  C   . TYR   A 68  ? 0.1362 0.1426 0.1840 0.0045  0.0254  0.0241  68   TYR   A C   
1672 O  O   . TYR   A 68  ? 0.1399 0.1481 0.1922 0.0118  0.0307  0.0249  68   TYR   A O   
1673 C  CB  . TYR   A 68  ? 0.1488 0.1407 0.1928 0.0102  0.0450  0.0347  68   TYR   A CB  
1674 C  CG  . TYR   A 68  ? 0.1495 0.1568 0.2230 0.0073  0.0603  0.0385  68   TYR   A CG  
1675 C  CD1 . TYR   A 68  ? 0.1586 0.1681 0.2665 -0.0166 0.0538  0.0027  68   TYR   A CD1 
1676 C  CD2 . TYR   A 68  ? 0.1700 0.1630 0.2807 0.0166  0.0635  0.0515  68   TYR   A CD2 
1677 C  CE1 . TYR   A 68  ? 0.1620 0.1750 0.3120 -0.0114 0.0559  -0.0074 68   TYR   A CE1 
1678 C  CE2 . TYR   A 68  ? 0.1696 0.1699 0.3132 0.0025  0.0689  0.0248  68   TYR   A CE2 
1679 C  CZ  . TYR   A 68  ? 0.1702 0.1717 0.3338 -0.0138 0.0587  -0.0100 68   TYR   A CZ  
1680 O  OH  . TYR   A 68  ? 0.2020 0.1737 0.3662 -0.0134 0.0435  -0.0474 68   TYR   A OH  
1690 N  N   . ILE   A 69  ? 0.1248 0.1339 0.1747 -0.0000 0.0230  0.0235  69   ILE   A N   
1691 C  CA  . ILE   A 69  ? 0.1336 0.1347 0.1667 0.0029  0.0153  0.0080  69   ILE   A CA  
1692 C  C   . ILE   A 69  ? 0.1371 0.1400 0.1562 0.0074  0.0135  0.0174  69   ILE   A C   
1693 O  O   . ILE   A 69  ? 0.1429 0.1482 0.1616 -0.0006 0.0239  0.0172  69   ILE   A O   
1694 C  CB  . ILE   A 69  ? 0.1430 0.1564 0.1761 0.0038  0.0092  -0.0003 69   ILE   A CB  
1695 C  CG1 . ILE   A 69  ? 0.1433 0.1665 0.1773 0.0065  0.0206  -0.0142 69   ILE   A CG1 
1696 C  CG2 . ILE   A 69  ? 0.1573 0.1777 0.1890 0.0114  0.0048  -0.0081 69   ILE   A CG2 
1697 C  CD1 . ILE   A 69  ? 0.1484 0.1775 0.2036 -0.0048 0.0146  -0.0165 69   ILE   A CD1 
1709 N  N   . ALA   A 70  ? 0.1429 0.1439 0.1688 -0.0019 0.0199  0.0222  70   ALA   A N   
1710 C  CA  . ALA   A 70  ? 0.1449 0.1520 0.1874 -0.0118 0.0251  0.0312  70   ALA   A CA  
1711 C  C   . ALA   A 70  ? 0.1412 0.1716 0.1897 -0.0145 0.0227  0.0326  70   ALA   A C   
1712 O  O   . ALA   A 70  ? 0.1581 0.2067 0.2112 0.0115  0.0432  0.0453  70   ALA   A O   
1713 C  CB  . ALA   A 70  ? 0.1507 0.1488 0.2072 -0.0131 0.0235  0.0180  70   ALA   A CB  
1719 N  N   . THR   A 71  ? 0.1393 0.1673 0.1815 0.0012  0.0136  0.0288  71   THR   A N   
1720 C  CA  . THR   A 71  ? 0.1495 0.1814 0.2088 0.0088  0.0229  0.0375  71   THR   A CA  
1721 C  C   . THR   A 71  ? 0.1356 0.1766 0.2343 0.0160  0.0346  0.0264  71   THR   A C   
1722 O  O   . THR   A 71  ? 0.1457 0.2020 0.2823 0.0131  0.0538  0.0022  71   THR   A O   
1723 C  CB  . THR   A 71  ? 0.1788 0.2090 0.2460 0.0147  -0.0131 0.0404  71   THR   A CB  
1724 O  OG1 . THR   A 71  ? 0.2071 0.2305 0.2571 0.0053  -0.0416 0.0354  71   THR   A OG1 
1725 C  CG2 . THR   A 71  ? 0.1921 0.2275 0.2725 0.0234  -0.0193 0.0581  71   THR   A CG2 
1733 N  N   . ASN   A 72  ? 0.1396 0.1600 0.2033 0.0184  0.0298  0.0321  72   ASN   A N   
1734 C  CA  . ASN   A 72  ? 0.1441 0.1618 0.2149 0.0226  0.0391  0.0304  72   ASN   A CA  
1735 C  C   . ASN   A 72  ? 0.1607 0.1564 0.2039 0.0224  0.0513  0.0217  72   ASN   A C   
1736 O  O   . ASN   A 72  ? 0.1839 0.1563 0.2264 0.0237  0.0453  0.0102  72   ASN   A O   
1737 C  CB  . ASN   A 72  ? 0.1663 0.1702 0.2209 0.0226  0.0475  0.0344  72   ASN   A CB  
1738 C  CG  . ASN   A 72  ? 0.1908 0.1808 0.2269 0.0296  0.0362  0.0373  72   ASN   A CG  
1739 O  OD1 . ASN   A 72  ? 0.2104 0.2087 0.2452 0.0287  0.0477  0.0360  72   ASN   A OD1 
1740 N  ND2 . ASN   A 72  ? 0.2046 0.1811 0.2373 0.0529  0.0189  0.0242  72   ASN   A ND2 
1747 N  N   . GLY   A 73  ? 0.1664 0.1502 0.1878 0.0106  0.0468  0.0163  73   GLY   A N   
1748 C  CA  . GLY   A 73  ? 0.1695 0.1486 0.1812 -0.0029 0.0423  0.0102  73   GLY   A CA  
1749 C  C   . GLY   A 73  ? 0.1628 0.1412 0.1691 0.0018  0.0538  0.0268  73   GLY   A C   
1750 O  O   . GLY   A 73  ? 0.1603 0.1402 0.1882 0.0049  0.0419  0.0288  73   GLY   A O   
1754 N  N   . PRO   A 74  ? 0.1730 0.1427 0.1725 -0.0084 0.0514  0.0134  74   PRO   A N   
1755 C  CA  . PRO   A 74  ? 0.1718 0.1389 0.1836 0.0008  0.0470  0.0177  74   PRO   A CA  
1756 C  C   . PRO   A 74  ? 0.1667 0.1241 0.1768 0.0015  0.0356  0.0096  74   PRO   A C   
1757 O  O   . PRO   A 74  ? 0.1765 0.1286 0.2083 0.0040  0.0423  0.0050  74   PRO   A O   
1758 C  CB  . PRO   A 74  ? 0.1869 0.1643 0.1968 0.0007  0.0479  0.0299  74   PRO   A CB  
1759 C  CG  . PRO   A 74  ? 0.2116 0.1965 0.2488 -0.0150 0.0331  0.0157  74   PRO   A CG  
1760 C  CD  . PRO   A 74  ? 0.1892 0.1723 0.1961 -0.0204 0.0384  0.0091  74   PRO   A CD  
1768 N  N   . LEU   A 75  ? 0.1649 0.1229 0.1574 -0.0007 0.0306  0.0096  75   LEU   A N   
1769 C  CA  . LEU   A 75  ? 0.1657 0.1258 0.1457 -0.0009 0.0107  0.0152  75   LEU   A CA  
1770 C  C   . LEU   A 75  ? 0.1803 0.1340 0.1332 0.0060  0.0150  0.0177  75   LEU   A C   
1771 O  O   . LEU   A 75  ? 0.2208 0.1466 0.1483 0.0122  0.0115  0.0128  75   LEU   A O   
1772 C  CB  . LEU   A 75  ? 0.1637 0.1293 0.1378 -0.0054 0.0120  0.0203  75   LEU   A CB  
1773 C  CG  . LEU   A 75  ? 0.1775 0.1693 0.1484 -0.0351 0.0074  0.0133  75   LEU   A CG  
1774 C  CD1 . LEU   A 75  ? 0.1897 0.2214 0.1515 -0.0354 0.0100  0.0050  75   LEU   A CD1 
1775 C  CD2 . LEU   A 75  ? 0.2043 0.2081 0.2137 -0.0147 0.0043  0.0189  75   LEU   A CD2 
1787 N  N   . LYS   A 76  ? 0.1754 0.1320 0.1471 -0.0019 0.0143  0.0059  76   LYS   A N   
1788 C  CA  . LYS   A 76  ? 0.1648 0.1483 0.1541 -0.0066 0.0115  -0.0018 76   LYS   A CA  
1789 C  C   . LYS   A 76  ? 0.1648 0.1379 0.1237 -0.0025 0.0139  0.0066  76   LYS   A C   
1790 O  O   . LYS   A 76  ? 0.1720 0.1342 0.1258 -0.0010 0.0188  0.0108  76   LYS   A O   
1791 C  CB  . LYS   A 76  ? 0.1712 0.1696 0.1899 0.0001  0.0100  -0.0124 76   LYS   A CB  
1792 C  CG  . LYS   A 76  ? 0.1765 0.1676 0.2356 0.0100  0.0039  -0.0144 76   LYS   A CG  
1793 C  CD  . LYS   A 76  ? 0.1880 0.1651 0.2798 0.0110  -0.0045 -0.0283 76   LYS   A CD  
1794 C  CE  . LYS   A 76  ? 0.2020 0.1832 0.3535 0.0052  -0.0036 -0.0341 76   LYS   A CE  
1795 N  NZ  . LYS   A 76  ? 0.2014 0.1797 0.4067 -0.0041 -0.0134 -0.0413 76   LYS   A NZ  
1809 N  N   . VAL   A 77  ? 0.1815 0.1408 0.1214 -0.0038 0.0220  0.0146  77   VAL   A N   
1810 C  CA  . VAL   A 77  ? 0.1680 0.1422 0.1272 0.0094  0.0101  0.0101  77   VAL   A CA  
1811 C  C   . VAL   A 77  ? 0.1633 0.1351 0.1212 0.0089  0.0147  0.0091  77   VAL   A C   
1812 O  O   . VAL   A 77  ? 0.1785 0.1402 0.1313 0.0098  0.0299  0.0090  77   VAL   A O   
1813 C  CB  . VAL   A 77  ? 0.1788 0.1585 0.1460 0.0030  0.0055  0.0228  77   VAL   A CB  
1814 C  CG1 . VAL   A 77  ? 0.1816 0.1692 0.1772 0.0174  -0.0032 0.0121  77   VAL   A CG1 
1815 C  CG2 . VAL   A 77  ? 0.2058 0.1699 0.1612 0.0009  -0.0029 0.0310  77   VAL   A CG2 
1825 N  N   . GLY   A 78  ? 0.1584 0.1334 0.1224 -0.0002 0.0171  0.0092  78   GLY   A N   
1826 C  CA  . GLY   A 78  ? 0.1590 0.1332 0.1379 -0.0003 0.0263  0.0146  78   GLY   A CA  
1827 C  C   . GLY   A 78  ? 0.1466 0.1330 0.1373 0.0049  0.0239  0.0202  78   GLY   A C   
1828 O  O   . GLY   A 78  ? 0.1505 0.1371 0.1418 -0.0002 0.0167  0.0235  78   GLY   A O   
1832 N  N   . GLY   A 79  ? 0.1478 0.1296 0.1349 -0.0021 0.0131  0.0177  79   GLY   A N   
1833 C  CA  . GLY   A 79  ? 0.1470 0.1337 0.1424 -0.0044 0.0169  0.0144  79   GLY   A CA  
1834 C  C   . GLY   A 79  ? 0.1301 0.1266 0.1379 -0.0032 0.0187  0.0052  79   GLY   A C   
1835 O  O   . GLY   A 79  ? 0.1414 0.1368 0.1405 0.0187  0.0091  0.0063  79   GLY   A O   
1839 N  N   . SER   A 80  ? 0.1293 0.1436 0.1551 -0.0012 0.0134  -0.0032 80   SER   A N   
1840 C  CA  . SER   A 80  ? 0.1242 0.1363 0.1439 -0.0026 0.0099  0.0027  80   SER   A CA  
1841 C  C   . SER   A 80  ? 0.1254 0.1355 0.1468 0.0024  0.0140  0.0144  80   SER   A C   
1842 O  O   . SER   A 80  ? 0.1263 0.1575 0.1753 0.0093  0.0149  0.0023  80   SER   A O   
1843 C  CB  . SER   A 80  ? 0.1376 0.1377 0.1671 -0.0054 0.0123  0.0036  80   SER   A CB  
1844 O  OG  . SER   A 80  ? 0.1636 0.1380 0.2100 0.0031  -0.0004 0.0258  80   SER   A OG  
1850 N  N   . CYS   A 81  ? 0.1172 0.1341 0.1476 0.0030  0.0021  0.0122  81   CYS   A N   
1851 C  CA  . CYS   A 81  ? 0.1182 0.1398 0.1490 -0.0034 -0.0086 0.0264  81   CYS   A CA  
1852 C  C   . CYS   A 81  ? 0.1177 0.1434 0.1352 -0.0117 -0.0012 0.0261  81   CYS   A C   
1853 O  O   . CYS   A 81  ? 0.1198 0.1670 0.1487 0.0008  0.0004  0.0365  81   CYS   A O   
1854 C  CB  . CYS   A 81  ? 0.1306 0.1532 0.1542 -0.0147 0.0004  0.0277  81   CYS   A CB  
1855 S  SG  . CYS   A 81  ? 0.1420 0.1376 0.1556 -0.0142 0.0003  0.0182  81   CYS   A SG  
1861 N  N   . VAL   A 82  ? 0.1250 0.1488 0.1363 -0.0015 -0.0094 0.0225  82   VAL   A N   
1862 C  CA  . VAL   A 82  ? 0.1356 0.1485 0.1442 0.0011  -0.0106 0.0317  82   VAL   A CA  
1863 C  C   . VAL   A 82  ? 0.1295 0.1490 0.1494 0.0023  -0.0074 0.0251  82   VAL   A C   
1864 O  O   . VAL   A 82  ? 0.1266 0.1566 0.1773 -0.0018 -0.0031 0.0039  82   VAL   A O   
1865 C  CB  . VAL   A 82  ? 0.1656 0.1606 0.1596 0.0017  -0.0073 0.0307  82   VAL   A CB  
1866 C  CG1 . VAL   A 82  ? 0.1971 0.1726 0.1745 0.0066  0.0055  0.0283  82   VAL   A CG1 
1867 C  CG2 . VAL   A 82  ? 0.1766 0.1604 0.1883 -0.0039 -0.0065 0.0390  82   VAL   A CG2 
1877 N  N   . LEU   A 83  ? 0.1265 0.1433 0.1438 -0.0066 -0.0085 0.0195  83   LEU   A N   
1878 C  CA  . LEU   A 83  ? 0.1309 0.1460 0.1377 -0.0077 -0.0123 0.0129  83   LEU   A CA  
1879 C  C   . LEU   A 83  ? 0.1349 0.1524 0.1278 -0.0099 -0.0137 0.0164  83   LEU   A C   
1880 O  O   . LEU   A 83  ? 0.1432 0.1569 0.1430 -0.0107 -0.0056 0.0216  83   LEU   A O   
1881 C  CB  . LEU   A 83  ? 0.1393 0.1542 0.1399 -0.0126 -0.0142 0.0128  83   LEU   A CB  
1882 C  CG  . LEU   A 83  ? 0.1523 0.1639 0.1503 -0.0139 -0.0042 0.0111  83   LEU   A CG  
1883 C  CD1 . LEU   A 83  ? 0.1623 0.1678 0.1620 -0.0236 -0.0027 0.0276  83   LEU   A CD1 
1884 C  CD2 . LEU   A 83  ? 0.1472 0.1841 0.1646 -0.0139 0.0102  0.0189  83   LEU   A CD2 
1896 N  N   . SER   A 84  ? 0.1523 0.1587 0.1402 -0.0141 -0.0137 0.0215  84   SER   A N   
1897 C  CA  . SER   A 84  ? 0.1601 0.1621 0.1263 -0.0149 -0.0142 0.0257  84   SER   A CA  
1898 C  C   . SER   A 84  ? 0.1624 0.1569 0.1215 -0.0161 -0.0044 0.0144  84   SER   A C   
1899 O  O   . SER   A 84  ? 0.1542 0.1699 0.1220 -0.0062 -0.0094 0.0147  84   SER   A O   
1900 C  CB  . SER   A 84  ? 0.1687 0.1879 0.1451 -0.0136 -0.0130 0.0100  84   SER   A CB  
1901 O  OG  . SER   A 84  ? 0.1746 0.2135 0.1508 -0.0131 -0.0254 -0.0001 84   SER   A OG  
1907 N  N   . GLY   A 85  ? 0.1682 0.1728 0.1322 -0.0161 0.0049  0.0185  85   GLY   A N   
1908 C  CA  . GLY   A 85  ? 0.1762 0.1797 0.1425 -0.0242 0.0088  0.0015  85   GLY   A CA  
1909 C  C   . GLY   A 85  ? 0.1728 0.1864 0.1201 -0.0136 -0.0072 0.0057  85   GLY   A C   
1910 O  O   . GLY   A 85  ? 0.1695 0.1966 0.1286 -0.0196 0.0065  -0.0083 85   GLY   A O   
1914 N  N   . HIS   A 86  ? 0.1760 0.1753 0.1214 -0.0067 -0.0123 0.0131  86   HIS   A N   
1915 C  CA  . HIS   A 86  ? 0.1973 0.1769 0.1165 -0.0135 -0.0116 0.0130  86   HIS   A CA  
1916 C  C   . HIS   A 86  ? 0.2220 0.1896 0.0994 -0.0185 -0.0178 0.0088  86   HIS   A C   
1917 O  O   . HIS   A 86  ? 0.2327 0.2164 0.1141 -0.0129 -0.0047 0.0060  86   HIS   A O   
1918 C  CB  . HIS   A 86  ? 0.1976 0.1707 0.1337 -0.0073 -0.0042 0.0038  86   HIS   A CB  
1919 C  CG  . HIS   A 86  ? 0.1887 0.1722 0.1314 -0.0033 -0.0012 0.0186  86   HIS   A CG  
1920 N  ND1 . HIS   A 86  ? 0.1938 0.1812 0.1753 -0.0165 -0.0050 0.0179  86   HIS   A ND1 
1921 C  CD2 . HIS   A 86  ? 0.1926 0.1701 0.1252 0.0101  0.0043  0.0217  86   HIS   A CD2 
1922 C  CE1 . HIS   A 86  ? 0.1935 0.1812 0.1743 -0.0122 0.0166  0.0230  86   HIS   A CE1 
1923 N  NE2 . HIS   A 86  ? 0.1947 0.1740 0.1479 0.0061  0.0163  0.0313  86   HIS   A NE2 
1931 N  N   . ASN   A 87  ? 0.2352 0.1962 0.1186 -0.0034 0.0048  0.0018  87   ASN   A N   
1932 C  CA  . ASN   A 87  ? 0.2548 0.2127 0.1176 -0.0024 0.0266  -0.0011 87   ASN   A CA  
1933 C  C   . ASN   A 87  ? 0.2556 0.2294 0.1536 -0.0085 0.0553  -0.0008 87   ASN   A C   
1934 O  O   . ASN   A 87  ? 0.2831 0.2476 0.1938 -0.0281 0.0922  -0.0081 87   ASN   A O   
1935 C  CB  . ASN   A 87  ? 0.2696 0.2158 0.1365 0.0055  0.0257  -0.0052 87   ASN   A CB  
1936 C  CG  . ASN   A 87  ? 0.2872 0.2194 0.1414 0.0172  0.0368  -0.0001 87   ASN   A CG  
1937 O  OD1 . ASN   A 87  ? 0.3060 0.2154 0.1440 0.0389  0.0393  0.0087  87   ASN   A OD1 
1938 N  ND2 . ASN   A 87  ? 0.2895 0.2473 0.1584 0.0107  0.0380  0.0040  87   ASN   A ND2 
1945 N  N   . LEU   A 88  ? 0.2223 0.2185 0.1441 -0.0088 0.0285  0.0181  88   LEU   A N   
1946 C  CA  . LEU   A 88  ? 0.1971 0.2136 0.1599 -0.0177 0.0305  0.0330  88   LEU   A CA  
1947 C  C   . LEU   A 88  ? 0.1848 0.2167 0.1550 -0.0162 0.0196  0.0460  88   LEU   A C   
1948 O  O   . LEU   A 88  ? 0.1855 0.2236 0.1993 -0.0177 0.0269  0.0608  88   LEU   A O   
1949 C  CB  . LEU   A 88  ? 0.2000 0.2241 0.1707 -0.0272 -0.0015 0.0450  88   LEU   A CB  
1950 C  CG  . LEU   A 88  ? 0.2145 0.2365 0.1986 -0.0334 -0.0172 0.0443  88   LEU   A CG  
1951 C  CD1 . LEU   A 88  ? 0.2258 0.2472 0.1917 -0.0409 -0.0205 0.0335  88   LEU   A CD1 
1952 C  CD2 . LEU   A 88  ? 0.2322 0.2475 0.2432 -0.0201 -0.0146 0.0299  88   LEU   A CD2 
1964 N  N   . ALA   A 89  ? 0.1852 0.2118 0.1378 -0.0191 0.0111  0.0174  89   ALA   A N   
1965 C  CA  . ALA   A 89  ? 0.1916 0.2098 0.1226 -0.0139 0.0049  0.0197  89   ALA   A CA  
1966 C  C   . ALA   A 89  ? 0.1980 0.2112 0.1341 -0.0076 -0.0098 0.0253  89   ALA   A C   
1967 O  O   . ALA   A 89  ? 0.1896 0.2046 0.1726 -0.0197 -0.0170 -0.0002 89   ALA   A O   
1968 C  CB  . ALA   A 89  ? 0.1841 0.2074 0.1131 -0.0123 0.0067  0.0207  89   ALA   A CB  
1974 N  N   A LYS   A 90  ? 0.2037 0.2196 0.1259 -0.0146 -0.0194 0.0312  90   LYS   A N   
1975 N  N   B LYS   A 90  ? 0.2056 0.2199 0.1435 -0.0136 -0.0155 0.0248  90   LYS   A N   
1976 C  CA  A LYS   A 90  ? 0.2095 0.2308 0.1224 -0.0112 -0.0337 0.0348  90   LYS   A CA  
1977 C  CA  B LYS   A 90  ? 0.2123 0.2299 0.1565 -0.0129 -0.0237 0.0230  90   LYS   A CA  
1978 C  C   A LYS   A 90  ? 0.1925 0.2185 0.1290 -0.0144 -0.0341 0.0214  90   LYS   A C   
1979 C  C   B LYS   A 90  ? 0.1946 0.2184 0.1434 -0.0158 -0.0279 0.0158  90   LYS   A C   
1980 O  O   A LYS   A 90  ? 0.2008 0.2314 0.1570 -0.0175 -0.0368 0.0137  90   LYS   A O   
1981 O  O   B LYS   A 90  ? 0.1974 0.2310 0.1644 -0.0201 -0.0292 0.0036  90   LYS   A O   
1982 C  CB  A LYS   A 90  ? 0.2325 0.2633 0.1516 -0.0068 -0.0420 0.0567  90   LYS   A CB  
1983 C  CB  B LYS   A 90  ? 0.2363 0.2568 0.2022 -0.0112 -0.0259 0.0320  90   LYS   A CB  
1984 C  CG  A LYS   A 90  ? 0.2604 0.2926 0.2534 -0.0026 -0.0424 0.0680  90   LYS   A CG  
1985 C  CG  B LYS   A 90  ? 0.2614 0.2811 0.2757 -0.0095 -0.0255 0.0366  90   LYS   A CG  
1986 C  CD  A LYS   A 90  ? 0.2855 0.3180 0.3442 -0.0026 -0.0323 0.0730  90   LYS   A CD  
1987 C  CD  B LYS   A 90  ? 0.2826 0.3015 0.3419 -0.0092 -0.0202 0.0389  90   LYS   A CD  
1988 C  CE  A LYS   A 90  ? 0.3101 0.3409 0.4162 -0.0035 -0.0207 0.0689  90   LYS   A CE  
1989 C  CE  B LYS   A 90  ? 0.3015 0.3182 0.3943 -0.0089 -0.0145 0.0362  90   LYS   A CE  
1990 N  NZ  A LYS   A 90  ? 0.3240 0.3555 0.4636 -0.0058 -0.0110 0.0639  90   LYS   A NZ  
1991 N  NZ  B LYS   A 90  ? 0.3131 0.3275 0.4265 -0.0096 -0.0100 0.0343  90   LYS   A NZ  
2018 N  N   . HIS   A 91  ? 0.1830 0.1961 0.1155 -0.0150 -0.0328 0.0257  91   HIS   A N   
2019 C  CA  . HIS   A 91  ? 0.1690 0.1742 0.1200 -0.0094 -0.0290 0.0230  91   HIS   A CA  
2020 C  C   . HIS   A 91  ? 0.1509 0.1631 0.1087 -0.0109 -0.0144 0.0212  91   HIS   A C   
2021 O  O   . HIS   A 91  ? 0.1485 0.1778 0.1252 -0.0185 -0.0047 0.0255  91   HIS   A O   
2022 C  CB  . HIS   A 91  ? 0.1870 0.1954 0.1688 0.0139  -0.0348 0.0179  91   HIS   A CB  
2023 C  CG  . HIS   A 91  ? 0.2217 0.2460 0.2217 0.0236  -0.0705 0.0121  91   HIS   A CG  
2024 N  ND1 . HIS   A 91  ? 0.2326 0.2792 0.2663 0.0203  -0.0739 -0.0137 91   HIS   A ND1 
2025 C  CD2 . HIS   A 91  ? 0.2514 0.2657 0.2550 0.0298  -0.0869 0.0307  91   HIS   A CD2 
2026 C  CE1 . HIS   A 91  ? 0.2463 0.2861 0.2878 0.0271  -0.0721 0.0023  91   HIS   A CE1 
2027 N  NE2 . HIS   A 91  ? 0.2612 0.2818 0.2853 0.0366  -0.0840 0.0175  91   HIS   A NE2 
2036 N  N   . CYS   A 92  ? 0.1460 0.1586 0.1118 -0.0162 -0.0149 0.0188  92   CYS   A N   
2037 C  CA  . CYS   A 92  ? 0.1374 0.1498 0.1238 -0.0141 0.0008  0.0225  92   CYS   A CA  
2038 C  C   . CYS   A 92  ? 0.1305 0.1440 0.1164 -0.0160 -0.0017 0.0265  92   CYS   A C   
2039 O  O   . CYS   A 92  ? 0.1390 0.1521 0.1340 -0.0216 -0.0036 0.0156  92   CYS   A O   
2040 C  CB  . CYS   A 92  ? 0.1415 0.1526 0.1322 -0.0070 -0.0087 0.0181  92   CYS   A CB  
2041 S  SG  . CYS   A 92  ? 0.1395 0.1407 0.1296 -0.0110 -0.0053 0.0154  92   CYS   A SG  
2047 N  N   . LEU   A 93  ? 0.1273 0.1345 0.1237 -0.0108 0.0075  0.0217  93   LEU   A N   
2048 C  CA  . LEU   A 93  ? 0.1200 0.1314 0.1247 -0.0062 0.0055  0.0160  93   LEU   A CA  
2049 C  C   . LEU   A 93  ? 0.1178 0.1190 0.1297 -0.0023 0.0026  0.0167  93   LEU   A C   
2050 O  O   . LEU   A 93  ? 0.1194 0.1303 0.1175 0.0004  0.0021  0.0165  93   LEU   A O   
2051 C  CB  . LEU   A 93  ? 0.1275 0.1282 0.1401 -0.0014 0.0058  0.0168  93   LEU   A CB  
2052 C  CG  . LEU   A 93  ? 0.1304 0.1289 0.1415 -0.0026 0.0014  0.0292  93   LEU   A CG  
2053 C  CD1 . LEU   A 93  ? 0.1410 0.1392 0.1625 0.0018  0.0074  0.0218  93   LEU   A CD1 
2054 C  CD2 . LEU   A 93  ? 0.1491 0.1310 0.1654 -0.0041 0.0052  0.0223  93   LEU   A CD2 
2066 N  N   . HIS   A 94  ? 0.1167 0.1159 0.1278 -0.0041 0.0051  0.0165  94   HIS   A N   
2067 C  CA  . HIS   A 94  ? 0.1139 0.1219 0.1259 -0.0031 -0.0007 0.0202  94   HIS   A CA  
2068 C  C   . HIS   A 94  ? 0.1137 0.1207 0.1244 -0.0052 0.0006  0.0172  94   HIS   A C   
2069 O  O   . HIS   A 94  ? 0.1217 0.1393 0.1540 0.0015  0.0012  -0.0042 94   HIS   A O   
2070 C  CB  . HIS   A 94  ? 0.1183 0.1203 0.1368 -0.0070 -0.0018 0.0146  94   HIS   A CB  
2071 C  CG  . HIS   A 94  ? 0.1216 0.1180 0.1217 -0.0046 -0.0078 0.0149  94   HIS   A CG  
2072 N  ND1 . HIS   A 94  ? 0.1208 0.1185 0.1329 -0.0049 -0.0046 0.0171  94   HIS   A ND1 
2073 C  CD2 . HIS   A 94  ? 0.1285 0.1316 0.1298 -0.0026 -0.0079 0.0103  94   HIS   A CD2 
2074 C  CE1 . HIS   A 94  ? 0.1292 0.1209 0.1228 -0.0073 -0.0076 0.0109  94   HIS   A CE1 
2075 N  NE2 . HIS   A 94  ? 0.1332 0.1269 0.1378 -0.0091 -0.0133 0.0083  94   HIS   A NE2 
2083 N  N   . VAL   A 95  ? 0.1150 0.1125 0.1096 -0.0039 0.0055  0.0109  95   VAL   A N   
2084 C  CA  . VAL   A 95  ? 0.1226 0.1219 0.1137 -0.0032 0.0090  0.0180  95   VAL   A CA  
2085 C  C   . VAL   A 95  ? 0.1167 0.1195 0.1123 -0.0092 0.0064  0.0079  95   VAL   A C   
2086 O  O   . VAL   A 95  ? 0.1281 0.1304 0.1178 0.0058  0.0017  0.0124  95   VAL   A O   
2087 C  CB  . VAL   A 95  ? 0.1237 0.1272 0.1309 -0.0130 0.0080  0.0127  95   VAL   A CB  
2088 C  CG1 . VAL   A 95  ? 0.1348 0.1271 0.1428 -0.0108 0.0016  0.0026  95   VAL   A CG1 
2089 C  CG2 . VAL   A 95  ? 0.1273 0.1207 0.1347 -0.0084 0.0055  0.0224  95   VAL   A CG2 
2099 N  N   . VAL   A 96  ? 0.1209 0.1229 0.1093 -0.0026 0.0038  0.0141  96   VAL   A N   
2100 C  CA  . VAL   A 96  ? 0.1347 0.1227 0.1266 -0.0031 0.0074  0.0240  96   VAL   A CA  
2101 C  C   . VAL   A 96  ? 0.1364 0.1292 0.1243 -0.0048 0.0114  0.0189  96   VAL   A C   
2102 O  O   . VAL   A 96  ? 0.1466 0.1330 0.1418 -0.0069 0.0131  -0.0005 96   VAL   A O   
2103 C  CB  . VAL   A 96  ? 0.1401 0.1287 0.1271 -0.0054 0.0134  0.0179  96   VAL   A CB  
2104 C  CG1 . VAL   A 96  ? 0.1514 0.1323 0.1215 -0.0022 0.0088  0.0162  96   VAL   A CG1 
2105 C  CG2 . VAL   A 96  ? 0.1366 0.1389 0.1410 -0.0158 0.0163  0.0147  96   VAL   A CG2 
2115 N  N   . GLY   A 97  ? 0.1322 0.1339 0.1201 -0.0117 0.0055  0.0142  97   GLY   A N   
2116 C  CA  . GLY   A 97  ? 0.1401 0.1423 0.1223 -0.0106 -0.0026 0.0223  97   GLY   A CA  
2117 C  C   . GLY   A 97  ? 0.1470 0.1535 0.1177 -0.0098 -0.0065 0.0170  97   GLY   A C   
2118 O  O   . GLY   A 97  ? 0.1586 0.1565 0.1332 -0.0130 -0.0034 0.0202  97   GLY   A O   
2122 N  N   A PRO   A 98  ? 0.1552 0.1591 0.1096 -0.0065 -0.0080 0.0257  98   PRO   A N   
2123 N  N   B PRO   A 98  ? 0.1552 0.1524 0.1263 -0.0039 -0.0057 0.0213  98   PRO   A N   
2124 C  CA  A PRO   A 98  ? 0.1561 0.1758 0.1210 -0.0048 -0.0040 0.0204  98   PRO   A CA  
2125 C  CA  B PRO   A 98  ? 0.1609 0.1574 0.1356 -0.0031 -0.0091 0.0166  98   PRO   A CA  
2126 C  C   A PRO   A 98  ? 0.1570 0.1854 0.1141 -0.0100 0.0004  0.0266  98   PRO   A C   
2127 C  C   B PRO   A 98  ? 0.1763 0.1510 0.1304 -0.0044 -0.0108 0.0223  98   PRO   A C   
2128 O  O   A PRO   A 98  ? 0.1503 0.1718 0.1246 -0.0050 0.0051  0.0230  98   PRO   A O   
2129 O  O   B PRO   A 98  ? 0.1802 0.1491 0.1449 -0.0077 -0.0059 0.0250  98   PRO   A O   
2130 C  CB  A PRO   A 98  ? 0.1596 0.1774 0.1158 0.0057  -0.0119 0.0044  98   PRO   A CB  
2131 C  CB  B PRO   A 98  ? 0.1576 0.1574 0.1348 0.0036  -0.0121 0.0190  98   PRO   A CB  
2132 C  CG  A PRO   A 98  ? 0.1570 0.1647 0.1105 0.0078  -0.0133 0.0011  98   PRO   A CG  
2133 C  CG  B PRO   A 98  ? 0.1631 0.1573 0.1520 0.0036  -0.0095 0.0189  98   PRO   A CG  
2134 C  CD  A PRO   A 98  ? 0.1538 0.1570 0.1051 0.0049  -0.0093 0.0161  98   PRO   A CD  
2135 C  CD  B PRO   A 98  ? 0.1551 0.1508 0.1346 0.0016  -0.0091 0.0217  98   PRO   A CD  
2150 N  N   A ASN   A 99  ? 0.1647 0.2064 0.1151 -0.0068 0.0099  0.0374  99   ASN   A N   
2151 N  N   B ASN   A 99  ? 0.1930 0.1449 0.1141 0.0045  -0.0079 0.0272  99   ASN   A N   
2152 C  CA  A ASN   A 99  ? 0.1846 0.2223 0.1105 -0.0086 0.0066  0.0435  99   ASN   A CA  
2153 C  CA  B ASN   A 99  ? 0.2140 0.1409 0.1152 0.0139  -0.0019 0.0396  99   ASN   A CA  
2154 C  C   A ASN   A 99  ? 0.2098 0.2484 0.1088 -0.0145 0.0075  0.0385  99   ASN   A C   
2155 C  C   B ASN   A 99  ? 0.2240 0.1400 0.1110 0.0106  -0.0095 0.0472  99   ASN   A C   
2156 O  O   A ASN   A 99  ? 0.2188 0.2675 0.1235 -0.0031 0.0018  0.0280  99   ASN   A O   
2157 O  O   B ASN   A 99  ? 0.2242 0.1319 0.1140 0.0216  -0.0187 0.0267  99   ASN   A O   
2158 C  CB  A ASN   A 99  ? 0.1846 0.2202 0.1265 -0.0073 -0.0038 0.0531  99   ASN   A CB  
2159 C  CB  B ASN   A 99  ? 0.2269 0.1426 0.1284 0.0215  0.0004  0.0283  99   ASN   A CB  
2160 C  CG  A ASN   A 99  ? 0.1892 0.2246 0.1543 -0.0033 -0.0026 0.0467  99   ASN   A CG  
2161 C  CG  B ASN   A 99  ? 0.2371 0.1451 0.1251 0.0256  0.0032  0.0298  99   ASN   A CG  
2162 O  OD1 A ASN   A 99  ? 0.2002 0.2294 0.1531 0.0078  -0.0019 0.0345  99   ASN   A OD1 
2163 O  OD1 B ASN   A 99  ? 0.2327 0.1499 0.1157 0.0302  0.0079  0.0365  99   ASN   A OD1 
2164 N  ND2 A ASN   A 99  ? 0.1902 0.2247 0.1678 -0.0018 -0.0013 0.0583  99   ASN   A ND2 
2165 N  ND2 B ASN   A 99  ? 0.2453 0.1482 0.1567 0.0300  -0.0070 0.0167  99   ASN   A ND2 
2178 N  N   A VAL   A 100 ? 0.2275 0.2587 0.1196 -0.0290 -0.0166 0.0357  100  VAL   A N   
2179 N  N   B VAL   A 100 ? 0.2373 0.1676 0.1262 0.0020  -0.0159 0.0466  100  VAL   A N   
2180 C  CA  A VAL   A 100 ? 0.2518 0.2805 0.1420 -0.0296 -0.0214 0.0324  100  VAL   A CA  
2181 C  CA  B VAL   A 100 ? 0.2577 0.1881 0.1690 -0.0030 -0.0401 0.0360  100  VAL   A CA  
2182 C  C   A VAL   A 100 ? 0.2692 0.3016 0.1486 -0.0335 -0.0248 0.0551  100  VAL   A C   
2183 C  C   B VAL   A 100 ? 0.2599 0.1899 0.1585 0.0073  -0.0579 0.0257  100  VAL   A C   
2184 O  O   A VAL   A 100 ? 0.2712 0.3102 0.1420 -0.0316 -0.0072 0.0527  100  VAL   A O   
2185 O  O   B VAL   A 100 ? 0.2680 0.1926 0.1626 0.0085  -0.0634 0.0032  100  VAL   A O   
2186 C  CB  A VAL   A 100 ? 0.2639 0.2825 0.1765 -0.0282 -0.0255 0.0104  100  VAL   A CB  
2187 C  CB  B VAL   A 100 ? 0.2736 0.2092 0.2197 -0.0144 -0.0354 0.0325  100  VAL   A CB  
2188 C  CG1 A VAL   A 100 ? 0.2675 0.2873 0.2020 -0.0311 -0.0117 0.0015  100  VAL   A CG1 
2189 C  CG1 B VAL   A 100 ? 0.2764 0.2114 0.2460 -0.0163 -0.0284 0.0309  100  VAL   A CG1 
2190 C  CG2 A VAL   A 100 ? 0.2702 0.2813 0.1733 -0.0320 -0.0219 0.0051  100  VAL   A CG2 
2191 C  CG2 B VAL   A 100 ? 0.2796 0.2192 0.2376 -0.0155 -0.0369 0.0326  100  VAL   A CG2 
2210 N  N   A ASN   A 101 ? 0.2858 0.3098 0.1815 -0.0356 -0.0339 0.0899  101  ASN   A N   
2211 N  N   B ASN   A 101 ? 0.2575 0.1964 0.1488 0.0125  -0.0670 0.0301  101  ASN   A N   
2212 C  CA  A ASN   A 101 ? 0.3119 0.3216 0.2163 -0.0357 -0.0325 0.1123  101  ASN   A CA  
2213 C  CA  B ASN   A 101 ? 0.2652 0.2066 0.1545 0.0177  -0.0535 0.0371  101  ASN   A CA  
2214 C  C   A ASN   A 101 ? 0.3335 0.3459 0.2339 -0.0416 -0.0079 0.1400  101  ASN   A C   
2215 C  C   B ASN   A 101 ? 0.2820 0.2207 0.1460 0.0232  -0.0321 0.0577  101  ASN   A C   
2216 O  O   A ASN   A 101 ? 0.3447 0.3537 0.2707 -0.0385 -0.0097 0.1352  101  ASN   A O   
2217 O  O   B ASN   A 101 ? 0.2894 0.2241 0.1535 0.0192  -0.0199 0.0613  101  ASN   A O   
2218 C  CB  A ASN   A 101 ? 0.3122 0.3059 0.2078 -0.0281 -0.0636 0.1047  101  ASN   A CB  
2219 C  CB  B ASN   A 101 ? 0.2527 0.2030 0.1650 0.0138  -0.0597 0.0350  101  ASN   A CB  
2220 C  CG  A ASN   A 101 ? 0.3121 0.2944 0.2013 -0.0239 -0.0840 0.0790  101  ASN   A CG  
2221 C  CG  B ASN   A 101 ? 0.2444 0.2090 0.2010 0.0070  -0.0665 0.0257  101  ASN   A CG  
2222 O  OD1 A ASN   A 101 ? 0.3092 0.2927 0.2186 -0.0145 -0.0878 0.0448  101  ASN   A OD1 
2223 O  OD1 B ASN   A 101 ? 0.2532 0.2213 0.2315 -0.0053 -0.0638 0.0208  101  ASN   A OD1 
2224 N  ND2 A ASN   A 101 ? 0.3188 0.2898 0.2106 -0.0278 -0.0845 0.0756  101  ASN   A ND2 
2225 N  ND2 B ASN   A 101 ? 0.2380 0.2044 0.2211 0.0114  -0.0593 0.0179  101  ASN   A ND2 
2238 N  N   A LYS   A 102 ? 0.3404 0.3675 0.2535 -0.0510 0.0088  0.1360  102  LYS   A N   
2239 N  N   B LYS   A 102 ? 0.2889 0.2335 0.1748 0.0304  -0.0162 0.0599  102  LYS   A N   
2240 C  CA  A LYS   A 102 ? 0.3547 0.3869 0.2647 -0.0530 0.0033  0.1205  102  LYS   A CA  
2241 C  CA  B LYS   A 102 ? 0.3025 0.2520 0.1925 0.0272  -0.0028 0.0648  102  LYS   A CA  
2242 C  C   A LYS   A 102 ? 0.3619 0.3992 0.2380 -0.0426 0.0004  0.1118  102  LYS   A C   
2243 C  C   B LYS   A 102 ? 0.3050 0.2558 0.1872 0.0359  -0.0096 0.0706  102  LYS   A C   
2244 O  O   A LYS   A 102 ? 0.3672 0.4085 0.2427 -0.0373 0.0022  0.1072  102  LYS   A O   
2245 O  O   B LYS   A 102 ? 0.3086 0.2566 0.1966 0.0358  -0.0013 0.0738  102  LYS   A O   
2246 C  CB  A LYS   A 102 ? 0.3632 0.3953 0.3158 -0.0620 -0.0085 0.0937  102  LYS   A CB  
2247 C  CB  B LYS   A 102 ? 0.3134 0.2694 0.2466 0.0201  -0.0021 0.0482  102  LYS   A CB  
2248 C  CG  A LYS   A 102 ? 0.3715 0.4007 0.3612 -0.0684 -0.0233 0.0641  102  LYS   A CG  
2249 C  CG  B LYS   A 102 ? 0.3239 0.2869 0.3048 0.0131  -0.0022 0.0295  102  LYS   A CG  
2250 C  CD  A LYS   A 102 ? 0.3822 0.4080 0.4073 -0.0702 -0.0365 0.0346  102  LYS   A CD  
2251 C  CD  B LYS   A 102 ? 0.3342 0.3055 0.3595 0.0084  -0.0025 0.0135  102  LYS   A CD  
2252 C  CE  A LYS   A 102 ? 0.3908 0.4127 0.4442 -0.0709 -0.0442 0.0179  102  LYS   A CE  
2253 C  CE  B LYS   A 102 ? 0.3424 0.3199 0.4017 0.0070  -0.0038 0.0057  102  LYS   A CE  
2254 N  NZ  A LYS   A 102 ? 0.3942 0.4144 0.4626 -0.0736 -0.0468 0.0073  102  LYS   A NZ  
2255 N  NZ  B LYS   A 102 ? 0.3476 0.3288 0.4279 0.0069  -0.0043 -0.0007 102  LYS   A NZ  
2282 N  N   A GLY   A 103 ? 0.3620 0.4036 0.2376 -0.0328 -0.0089 0.0864  103  GLY   A N   
2283 N  N   B GLY   A 103 ? 0.3047 0.2618 0.1763 0.0426  -0.0257 0.0592  103  GLY   A N   
2284 C  CA  A GLY   A 103 ? 0.3616 0.4048 0.2330 -0.0256 -0.0104 0.0656  103  GLY   A CA  
2285 C  CA  B GLY   A 103 ? 0.3021 0.2620 0.1881 0.0434  -0.0332 0.0510  103  GLY   A CA  
2286 C  C   A GLY   A 103 ? 0.3538 0.4024 0.2276 -0.0227 -0.0029 0.0472  103  GLY   A C   
2287 C  C   B GLY   A 103 ? 0.2928 0.2570 0.1769 0.0414  -0.0345 0.0442  103  GLY   A C   
2288 O  O   A GLY   A 103 ? 0.3635 0.4104 0.2519 -0.0179 -0.0028 0.0312  103  GLY   A O   
2289 O  O   B GLY   A 103 ? 0.3006 0.2592 0.1853 0.0479  -0.0371 0.0502  103  GLY   A O   
2296 N  N   A GLU   A 104 ? 0.3307 0.3867 0.1919 -0.0281 0.0071  0.0427  104  GLU   A N   
2297 N  N   B GLU   A 104 ? 0.2701 0.2426 0.1519 0.0345  -0.0396 0.0510  104  GLU   A N   
2298 C  CA  A GLU   A 104 ? 0.3056 0.3684 0.1682 -0.0386 0.0141  0.0356  104  GLU   A CA  
2299 C  CA  B GLU   A 104 ? 0.2478 0.2274 0.1293 0.0261  -0.0374 0.0433  104  GLU   A CA  
2300 C  C   A GLU   A 104 ? 0.3038 0.3686 0.1679 -0.0336 0.0067  0.0159  104  GLU   A C   
2301 C  C   B GLU   A 104 ? 0.2369 0.2260 0.1402 0.0297  -0.0294 0.0253  104  GLU   A C   
2302 O  O   A GLU   A 104 ? 0.3039 0.3688 0.1895 -0.0356 0.0055  0.0012  104  GLU   A O   
2303 O  O   B GLU   A 104 ? 0.2338 0.2247 0.1755 0.0347  -0.0293 0.0170  104  GLU   A O   
2304 C  CB  A GLU   A 104 ? 0.2809 0.3510 0.1580 -0.0538 0.0315  0.0508  104  GLU   A CB  
2305 C  CB  B GLU   A 104 ? 0.2424 0.2163 0.1279 0.0120  -0.0270 0.0485  104  GLU   A CB  
2306 C  CG  A GLU   A 104 ? 0.2649 0.3372 0.1743 -0.0635 0.0233  0.0585  104  GLU   A CG  
2307 C  CG  B GLU   A 104 ? 0.2434 0.2202 0.1457 0.0039  -0.0324 0.0531  104  GLU   A CG  
2308 C  CD  A GLU   A 104 ? 0.2485 0.3220 0.1722 -0.0747 0.0197  0.0640  104  GLU   A CD  
2309 C  CD  B GLU   A 104 ? 0.2438 0.2252 0.1442 -0.0006 -0.0409 0.0551  104  GLU   A CD  
2310 O  OE1 A GLU   A 104 ? 0.2321 0.3107 0.1417 -0.0795 0.0100  0.0653  104  GLU   A OE1 
2311 O  OE1 B GLU   A 104 ? 0.2432 0.2307 0.1607 0.0035  -0.0391 0.0470  104  GLU   A OE1 
2312 O  OE2 A GLU   A 104 ? 0.2607 0.3232 0.2008 -0.0781 0.0188  0.0646  104  GLU   A OE2 
2313 O  OE2 B GLU   A 104 ? 0.2534 0.2300 0.1390 -0.0107 -0.0353 0.0520  104  GLU   A OE2 
2326 N  N   A ASP   A 105 ? 0.3032 0.3699 0.1704 -0.0260 0.0037  0.0079  105  ASP   A N   
2327 N  N   B ASP   A 105 ? 0.2366 0.2227 0.1540 0.0290  -0.0179 0.0177  105  ASP   A N   
2328 C  CA  A ASP   A 105 ? 0.3007 0.3704 0.1873 -0.0170 0.0029  -0.0165 105  ASP   A CA  
2329 C  CA  B ASP   A 105 ? 0.2380 0.2170 0.1801 0.0380  -0.0039 -0.0105 105  ASP   A CA  
2330 C  C   A ASP   A 105 ? 0.2725 0.3483 0.1525 -0.0273 -0.0051 -0.0249 105  ASP   A C   
2331 C  C   B ASP   A 105 ? 0.2354 0.1983 0.1708 0.0343  -0.0007 -0.0134 105  ASP   A C   
2332 O  O   A ASP   A 105 ? 0.2617 0.3489 0.1065 -0.0373 -0.0038 -0.0229 105  ASP   A O   
2333 O  O   B ASP   A 105 ? 0.2269 0.1809 0.1629 0.0340  0.0024  -0.0043 105  ASP   A O   
2334 C  CB  A ASP   A 105 ? 0.3236 0.3914 0.2532 -0.0018 0.0106  -0.0263 105  ASP   A CB  
2335 C  CB  B ASP   A 105 ? 0.2426 0.2336 0.2187 0.0487  0.0072  -0.0325 105  ASP   A CB  
2336 C  CG  A ASP   A 105 ? 0.3440 0.4088 0.3201 0.0105  0.0120  -0.0349 105  ASP   A CG  
2337 C  CG  B ASP   A 105 ? 0.2482 0.2443 0.2569 0.0585  0.0131  -0.0559 105  ASP   A CG  
2338 O  OD1 A ASP   A 105 ? 0.3491 0.4154 0.3302 0.0118  0.0071  -0.0469 105  ASP   A OD1 
2339 O  OD1 B ASP   A 105 ? 0.2519 0.2445 0.2515 0.0556  0.0015  -0.0664 105  ASP   A OD1 
2340 O  OD2 A ASP   A 105 ? 0.3566 0.4158 0.3655 0.0157  0.0142  -0.0281 105  ASP   A OD2 
2341 O  OD2 B ASP   A 105 ? 0.2514 0.2514 0.2982 0.0642  0.0177  -0.0533 105  ASP   A OD2 
2350 N  N   A ILE   A 106 ? 0.2526 0.3237 0.1703 -0.0296 -0.0227 -0.0349 106  ILE   A N   
2351 N  N   B ILE   A 106 ? 0.2406 0.2108 0.1857 0.0338  -0.0113 -0.0142 106  ILE   A N   
2352 C  CA  A ILE   A 106 ? 0.2236 0.3012 0.1959 -0.0363 -0.0345 -0.0546 106  ILE   A CA  
2353 C  CA  B ILE   A 106 ? 0.2419 0.2224 0.2031 0.0246  -0.0173 -0.0239 106  ILE   A CA  
2354 C  C   A ILE   A 106 ? 0.2009 0.2809 0.2072 -0.0538 -0.0308 -0.0628 106  ILE   A C   
2355 C  C   B ILE   A 106 ? 0.2460 0.2161 0.2055 0.0270  -0.0098 -0.0033 106  ILE   A C   
2356 O  O   A ILE   A 106 ? 0.1769 0.2698 0.2135 -0.0593 -0.0089 -0.0566 106  ILE   A O   
2357 O  O   B ILE   A 106 ? 0.2409 0.2185 0.2116 0.0273  -0.0059 0.0030  106  ILE   A O   
2358 C  CB  A ILE   A 106 ? 0.2292 0.3054 0.2329 -0.0216 -0.0485 -0.0460 106  ILE   A CB  
2359 C  CB  B ILE   A 106 ? 0.2460 0.2467 0.2269 0.0114  -0.0345 -0.0392 106  ILE   A CB  
2360 C  CG1 A ILE   A 106 ? 0.2264 0.3034 0.2490 -0.0097 -0.0510 -0.0365 106  ILE   A CG1 
2361 C  CG1 B ILE   A 106 ? 0.2436 0.2589 0.2314 0.0060  -0.0435 -0.0498 106  ILE   A CG1 
2362 C  CG2 A ILE   A 106 ? 0.2347 0.3087 0.2428 -0.0164 -0.0573 -0.0510 106  ILE   A CG2 
2363 C  CG2 B ILE   A 106 ? 0.2520 0.2564 0.2364 0.0092  -0.0365 -0.0425 106  ILE   A CG2 
2364 C  CD1 A ILE   A 106 ? 0.2234 0.2982 0.2525 0.0003  -0.0464 -0.0282 106  ILE   A CD1 
2365 C  CD1 B ILE   A 106 ? 0.2405 0.2652 0.2376 0.0017  -0.0492 -0.0553 106  ILE   A CD1 
2388 N  N   A GLN   A 107 ? 0.2171 0.2734 0.2373 -0.0543 -0.0277 -0.0744 107  GLN   A N   
2389 N  N   B GLN   A 107 ? 0.2558 0.2068 0.2174 0.0290  -0.0100 0.0109  107  GLN   A N   
2390 C  CA  A GLN   A 107 ? 0.2406 0.2672 0.2997 -0.0417 -0.0154 -0.0813 107  GLN   A CA  
2391 C  CA  B GLN   A 107 ? 0.2697 0.2116 0.2597 0.0226  -0.0102 0.0203  107  GLN   A CA  
2392 C  C   A GLN   A 107 ? 0.2138 0.2314 0.2767 -0.0378 0.0097  -0.0557 107  GLN   A C   
2393 C  C   B GLN   A 107 ? 0.2464 0.1821 0.2267 0.0229  -0.0067 0.0415  107  GLN   A C   
2394 O  O   A GLN   A 107 ? 0.2242 0.2372 0.3302 -0.0344 0.0259  -0.0427 107  GLN   A O   
2395 O  O   B GLN   A 107 ? 0.2518 0.1772 0.2337 0.0223  -0.0165 0.0474  107  GLN   A O   
2396 C  CB  A GLN   A 107 ? 0.2895 0.3031 0.3992 -0.0422 -0.0290 -0.0895 107  GLN   A CB  
2397 C  CB  B GLN   A 107 ? 0.3034 0.2519 0.3322 0.0104  -0.0209 0.0153  107  GLN   A CB  
2398 C  CG  A GLN   A 107 ? 0.3385 0.3425 0.5107 -0.0386 -0.0390 -0.0816 107  GLN   A CG  
2399 C  CG  B GLN   A 107 ? 0.3333 0.2885 0.4041 0.0025  -0.0338 0.0232  107  GLN   A CG  
2400 C  CD  A GLN   A 107 ? 0.3773 0.3722 0.6045 -0.0356 -0.0448 -0.0723 107  GLN   A CD  
2401 C  CD  B GLN   A 107 ? 0.3570 0.3187 0.4665 -0.0023 -0.0426 0.0319  107  GLN   A CD  
2402 O  OE1 A GLN   A 107 ? 0.3896 0.3839 0.6420 -0.0343 -0.0461 -0.0663 107  GLN   A OE1 
2403 O  OE1 B GLN   A 107 ? 0.3659 0.3281 0.4843 -0.0029 -0.0454 0.0373  107  GLN   A OE1 
2404 N  NE2 A GLN   A 107 ? 0.3883 0.3818 0.6356 -0.0358 -0.0481 -0.0734 107  GLN   A NE2 
2405 N  NE2 B GLN   A 107 ? 0.3634 0.3271 0.4866 -0.0041 -0.0488 0.0352  107  GLN   A NE2 
2422 N  N   A LEU   A 108 ? 0.1830 0.1973 0.1987 -0.0404 0.0157  -0.0465 108  LEU   A N   
2423 N  N   B LEU   A 108 ? 0.2244 0.1744 0.1895 0.0098  0.0070  0.0418  108  LEU   A N   
2424 C  CA  A LEU   A 108 ? 0.1730 0.1799 0.1754 -0.0210 0.0176  -0.0128 108  LEU   A CA  
2425 C  CA  B LEU   A 108 ? 0.2062 0.1725 0.1827 0.0051  0.0157  0.0311  108  LEU   A CA  
2426 C  C   A LEU   A 108 ? 0.1563 0.1513 0.1689 -0.0121 0.0147  0.0089  108  LEU   A C   
2427 C  C   B LEU   A 108 ? 0.1798 0.1559 0.1777 0.0022  0.0160  0.0284  108  LEU   A C   
2428 O  O   A LEU   A 108 ? 0.1553 0.1515 0.1850 -0.0078 0.0243  0.0127  108  LEU   A O   
2429 O  O   B LEU   A 108 ? 0.1840 0.1584 0.1923 0.0035  0.0251  0.0262  108  LEU   A O   
2430 C  CB  A LEU   A 108 ? 0.1801 0.1950 0.1543 -0.0311 0.0272  -0.0110 108  LEU   A CB  
2431 C  CB  B LEU   A 108 ? 0.2141 0.1907 0.1769 -0.0037 0.0235  0.0216  108  LEU   A CB  
2432 C  CG  A LEU   A 108 ? 0.1939 0.2137 0.1837 -0.0292 0.0317  -0.0120 108  LEU   A CG  
2433 C  CG  B LEU   A 108 ? 0.2237 0.2058 0.1938 -0.0027 0.0296  0.0165  108  LEU   A CG  
2434 C  CD1 A LEU   A 108 ? 0.2066 0.2212 0.1870 -0.0364 0.0395  -0.0137 108  LEU   A CD1 
2435 C  CD1 B LEU   A 108 ? 0.2305 0.2126 0.1959 -0.0062 0.0365  0.0149  108  LEU   A CD1 
2436 C  CD2 A LEU   A 108 ? 0.1946 0.2309 0.2261 -0.0198 0.0315  -0.0088 108  LEU   A CD2 
2437 C  CD2 B LEU   A 108 ? 0.2248 0.2160 0.2180 0.0036  0.0295  0.0155  108  LEU   A CD2 
2460 N  N   . LEU   A 109 ? 0.1561 0.1514 0.1744 0.0034  0.0149  0.0268  109  LEU   A N   
2461 C  CA  . LEU   A 109 ? 0.1508 0.1461 0.1644 -0.0020 0.0031  0.0263  109  LEU   A CA  
2462 C  C   . LEU   A 109 ? 0.1383 0.1406 0.1611 -0.0045 0.0151  0.0150  109  LEU   A C   
2463 O  O   . LEU   A 109 ? 0.1436 0.1326 0.1786 -0.0039 0.0001  0.0105  109  LEU   A O   
2464 C  CB  . LEU   A 109 ? 0.1561 0.1596 0.1837 0.0087  -0.0014 0.0384  109  LEU   A CB  
2465 C  CG  . LEU   A 109 ? 0.1509 0.1671 0.2002 0.0033  0.0060  0.0400  109  LEU   A CG  
2466 C  CD1 . LEU   A 109 ? 0.1560 0.1570 0.2092 -0.0037 0.0096  0.0280  109  LEU   A CD1 
2467 C  CD2 . LEU   A 109 ? 0.1406 0.1798 0.2342 0.0066  0.0058  0.0446  109  LEU   A CD2 
2480 N  N   . LYS   A 110 ? 0.1380 0.1395 0.1554 -0.0008 0.0001  0.0101  110  LYS   A N   
2481 C  CA  . LYS   A 110 ? 0.1376 0.1300 0.1631 -0.0092 0.0018  0.0119  110  LYS   A CA  
2482 C  C   . LYS   A 110 ? 0.1373 0.1269 0.1477 -0.0111 0.0037  -0.0006 110  LYS   A C   
2483 O  O   . LYS   A 110 ? 0.1373 0.1318 0.1597 -0.0097 0.0073  0.0016  110  LYS   A O   
2484 C  CB  . LYS   A 110 ? 0.1446 0.1404 0.1915 -0.0070 0.0004  -0.0010 110  LYS   A CB  
2485 C  CG  . LYS   A 110 ? 0.1444 0.1330 0.1911 -0.0019 0.0011  -0.0074 110  LYS   A CG  
2486 C  CD  . LYS   A 110 ? 0.1501 0.1410 0.2157 -0.0118 0.0004  -0.0081 110  LYS   A CD  
2487 C  CE  . LYS   A 110 ? 0.1603 0.1447 0.2402 -0.0114 0.0100  -0.0111 110  LYS   A CE  
2488 N  NZ  . LYS   A 110 ? 0.1556 0.1445 0.2567 -0.0183 0.0233  -0.0028 110  LYS   A NZ  
2502 N  N   . SER   A 111 ? 0.1438 0.1292 0.1468 -0.0031 0.0019  0.0022  111  SER   A N   
2503 C  CA  . SER   A 111 ? 0.1331 0.1385 0.1524 -0.0004 0.0088  0.0041  111  SER   A CA  
2504 C  C   . SER   A 111 ? 0.1268 0.1244 0.1583 -0.0071 0.0059  0.0159  111  SER   A C   
2505 O  O   . SER   A 111 ? 0.1398 0.1188 0.1788 -0.0051 0.0091  0.0125  111  SER   A O   
2506 C  CB  . SER   A 111 ? 0.1493 0.1579 0.1747 -0.0003 0.0244  -0.0102 111  SER   A CB  
2507 O  OG  . SER   A 111 ? 0.1967 0.1792 0.1789 0.0037  0.0303  -0.0181 111  SER   A OG  
2513 N  N   . ALA   A 112 ? 0.1328 0.1219 0.1505 -0.0022 0.0116  0.0096  112  ALA   A N   
2514 C  CA  . ALA   A 112 ? 0.1378 0.1190 0.1441 -0.0066 0.0141  0.0059  112  ALA   A CA  
2515 C  C   . ALA   A 112 ? 0.1275 0.1174 0.1389 -0.0000 0.0080  0.0117  112  ALA   A C   
2516 O  O   . ALA   A 112 ? 0.1315 0.1168 0.1580 -0.0098 0.0124  0.0119  112  ALA   A O   
2517 C  CB  . ALA   A 112 ? 0.1493 0.1247 0.1489 -0.0010 0.0134  0.0175  112  ALA   A CB  
2523 N  N   . TYR   A 113 ? 0.1161 0.1260 0.1547 -0.0033 0.0076  0.0179  113  TYR   A N   
2524 C  CA  . TYR   A 113 ? 0.1245 0.1168 0.1470 -0.0012 0.0097  0.0156  113  TYR   A CA  
2525 C  C   . TYR   A 113 ? 0.1249 0.1180 0.1456 -0.0074 0.0094  0.0116  113  TYR   A C   
2526 O  O   . TYR   A 113 ? 0.1272 0.1211 0.1582 -0.0042 0.0170  0.0057  113  TYR   A O   
2527 C  CB  . TYR   A 113 ? 0.1261 0.1252 0.1613 -0.0023 0.0028  0.0239  113  TYR   A CB  
2528 C  CG  . TYR   A 113 ? 0.1248 0.1308 0.1548 -0.0082 0.0110  0.0275  113  TYR   A CG  
2529 C  CD1 . TYR   A 113 ? 0.1223 0.1425 0.1571 -0.0031 0.0094  0.0285  113  TYR   A CD1 
2530 C  CD2 . TYR   A 113 ? 0.1309 0.1388 0.1579 -0.0078 0.0036  0.0269  113  TYR   A CD2 
2531 C  CE1 . TYR   A 113 ? 0.1277 0.1567 0.1669 -0.0011 0.0058  0.0209  113  TYR   A CE1 
2532 C  CE2 . TYR   A 113 ? 0.1337 0.1479 0.1622 -0.0093 0.0039  0.0295  113  TYR   A CE2 
2533 C  CZ  . TYR   A 113 ? 0.1234 0.1492 0.1671 0.0034  0.0097  0.0319  113  TYR   A CZ  
2534 O  OH  . TYR   A 113 ? 0.1262 0.1617 0.1837 0.0116  0.0026  0.0296  113  TYR   A OH  
2544 N  N   . GLU   A 114 ? 0.1211 0.1169 0.1528 -0.0021 0.0167  0.0143  114  GLU   A N   
2545 C  CA  . GLU   A 114 ? 0.1266 0.1144 0.1669 0.0050  0.0052  0.0184  114  GLU   A CA  
2546 C  C   . GLU   A 114 ? 0.1130 0.1105 0.1694 0.0035  0.0112  0.0149  114  GLU   A C   
2547 O  O   . GLU   A 114 ? 0.1342 0.1180 0.1625 0.0039  0.0054  0.0158  114  GLU   A O   
2548 C  CB  . GLU   A 114 ? 0.1232 0.1212 0.1639 -0.0023 0.0039  0.0147  114  GLU   A CB  
2549 C  CG  . GLU   A 114 ? 0.1304 0.1272 0.1824 0.0007  0.0057  0.0019  114  GLU   A CG  
2550 C  CD  . GLU   A 114 ? 0.1366 0.1279 0.1838 -0.0004 0.0020  0.0099  114  GLU   A CD  
2551 O  OE1 . GLU   A 114 ? 0.1472 0.1276 0.1849 -0.0067 0.0163  -0.0099 114  GLU   A OE1 
2552 O  OE2 . GLU   A 114 ? 0.1624 0.1304 0.2038 -0.0091 0.0120  -0.0100 114  GLU   A OE2 
2559 N  N   . ASN   A 115 ? 0.1172 0.1228 0.1483 -0.0040 0.0089  0.0076  115  ASN   A N   
2560 C  CA  . ASN   A 115 ? 0.1221 0.1246 0.1583 -0.0036 0.0113  0.0188  115  ASN   A CA  
2561 C  C   . ASN   A 115 ? 0.1242 0.1199 0.1467 -0.0101 0.0062  0.0103  115  ASN   A C   
2562 O  O   . ASN   A 115 ? 0.1300 0.1330 0.1494 -0.0078 0.0110  0.0147  115  ASN   A O   
2563 C  CB  . ASN   A 115 ? 0.1349 0.1346 0.1547 -0.0081 0.0175  0.0206  115  ASN   A CB  
2564 C  CG  . ASN   A 115 ? 0.1313 0.1521 0.1674 -0.0150 0.0186  0.0158  115  ASN   A CG  
2565 O  OD1 . ASN   A 115 ? 0.1370 0.2474 0.1841 -0.0201 0.0298  0.0338  115  ASN   A OD1 
2566 N  ND2 . ASN   A 115 ? 0.1312 0.1374 0.1713 -0.0106 0.0251  0.0225  115  ASN   A ND2 
2573 N  N   . PHE   A 116 ? 0.1185 0.1208 0.1519 -0.0006 0.0119  0.0214  116  PHE   A N   
2574 C  CA  . PHE   A 116 ? 0.1220 0.1326 0.1384 -0.0025 0.0095  0.0151  116  PHE   A CA  
2575 C  C   . PHE   A 116 ? 0.1207 0.1346 0.1533 -0.0041 0.0167  0.0249  116  PHE   A C   
2576 O  O   . PHE   A 116 ? 0.1298 0.1401 0.1641 0.0060  0.0202  0.0293  116  PHE   A O   
2577 C  CB  . PHE   A 116 ? 0.1268 0.1209 0.1572 0.0007  0.0201  0.0178  116  PHE   A CB  
2578 C  CG  . PHE   A 116 ? 0.1253 0.1239 0.1507 -0.0036 0.0134  0.0145  116  PHE   A CG  
2579 C  CD1 . PHE   A 116 ? 0.1202 0.1265 0.1521 -0.0013 0.0129  0.0169  116  PHE   A CD1 
2580 C  CD2 . PHE   A 116 ? 0.1249 0.1287 0.1724 -0.0006 0.0233  0.0209  116  PHE   A CD2 
2581 C  CE1 . PHE   A 116 ? 0.1258 0.1236 0.1591 -0.0141 0.0078  0.0112  116  PHE   A CE1 
2582 C  CE2 . PHE   A 116 ? 0.1297 0.1274 0.1853 -0.0012 0.0172  0.0089  116  PHE   A CE2 
2583 C  CZ  . PHE   A 116 ? 0.1352 0.1137 0.1566 -0.0041 0.0060  0.0175  116  PHE   A CZ  
2593 N  N   . ASN   A 117 ? 0.1197 0.1289 0.1643 -0.0010 0.0171  0.0196  117  ASN   A N   
2594 C  CA  . ASN   A 117 ? 0.1265 0.1265 0.1712 0.0026  0.0160  0.0315  117  ASN   A CA  
2595 C  C   . ASN   A 117 ? 0.1256 0.1321 0.1761 -0.0013 0.0128  0.0204  117  ASN   A C   
2596 O  O   . ASN   A 117 ? 0.1376 0.1392 0.1876 -0.0029 -0.0026 0.0414  117  ASN   A O   
2597 C  CB  . ASN   A 117 ? 0.1278 0.1299 0.1683 -0.0028 0.0160  0.0288  117  ASN   A CB  
2598 C  CG  . ASN   A 117 ? 0.1263 0.1309 0.1821 -0.0037 0.0122  0.0311  117  ASN   A CG  
2599 O  OD1 . ASN   A 117 ? 0.1281 0.1518 0.1889 -0.0157 0.0191  0.0186  117  ASN   A OD1 
2600 N  ND2 . ASN   A 117 ? 0.1188 0.1297 0.1873 -0.0042 0.0124  0.0274  117  ASN   A ND2 
2607 N  N   . GLN   A 118 ? 0.1181 0.1343 0.1845 -0.0024 0.0050  0.0257  118  GLN   A N   
2608 C  CA  . GLN   A 118 ? 0.1311 0.1442 0.1902 -0.0027 0.0030  0.0202  118  GLN   A CA  
2609 C  C   . GLN   A 118 ? 0.1291 0.1524 0.1756 -0.0020 0.0024  0.0312  118  GLN   A C   
2610 O  O   . GLN   A 118 ? 0.1312 0.1818 0.1951 0.0022  -0.0100 0.0089  118  GLN   A O   
2611 C  CB  . GLN   A 118 ? 0.1282 0.1478 0.1998 -0.0025 0.0109  0.0240  118  GLN   A CB  
2612 C  CG  . GLN   A 118 ? 0.1296 0.1481 0.2009 0.0043  0.0136  0.0330  118  GLN   A CG  
2613 C  CD  . GLN   A 118 ? 0.1277 0.1510 0.1994 0.0035  0.0111  0.0203  118  GLN   A CD  
2614 O  OE1 . GLN   A 118 ? 0.1352 0.1677 0.2120 0.0153  0.0032  0.0167  118  GLN   A OE1 
2615 N  NE2 . GLN   A 118 ? 0.1373 0.1506 0.2062 0.0025  0.0076  0.0232  118  GLN   A NE2 
2624 N  N   . HIS   A 119 ? 0.1347 0.1431 0.1665 0.0007  0.0025  0.0318  119  HIS   A N   
2625 C  CA  . HIS   A 119 ? 0.1431 0.1553 0.1649 0.0002  0.0052  0.0307  119  HIS   A CA  
2626 C  C   . HIS   A 119 ? 0.1557 0.1641 0.1599 -0.0045 0.0109  0.0343  119  HIS   A C   
2627 O  O   . HIS   A 119 ? 0.1539 0.1694 0.1667 -0.0200 0.0006  0.0324  119  HIS   A O   
2628 C  CB  . HIS   A 119 ? 0.1431 0.1508 0.1793 0.0062  0.0217  0.0339  119  HIS   A CB  
2629 C  CG  . HIS   A 119 ? 0.1455 0.1529 0.2177 0.0102  0.0163  0.0380  119  HIS   A CG  
2630 N  ND1 . HIS   A 119 ? 0.1601 0.1710 0.2798 -0.0039 0.0095  0.0299  119  HIS   A ND1 
2631 C  CD2 . HIS   A 119 ? 0.1562 0.1628 0.2412 0.0129  0.0335  0.0584  119  HIS   A CD2 
2632 C  CE1 . HIS   A 119 ? 0.1556 0.1716 0.3011 -0.0064 0.0282  0.0471  119  HIS   A CE1 
2633 N  NE2 . HIS   A 119 ? 0.1709 0.1639 0.2893 0.0025  0.0440  0.0618  119  HIS   A NE2 
2641 N  N   A GLU   A 120 ? 0.1575 0.1784 0.1538 0.0002  -0.0014 0.0583  120  GLU   A N   
2642 N  N   B GLU   A 120 ? 0.1686 0.1869 0.1709 0.0002  0.0087  0.0462  120  GLU   A N   
2643 C  CA  A GLU   A 120 ? 0.1670 0.2017 0.1749 0.0055  -0.0019 0.0879  120  GLU   A CA  
2644 C  CA  B GLU   A 120 ? 0.1837 0.2126 0.1975 0.0049  0.0127  0.0620  120  GLU   A CA  
2645 C  C   A GLU   A 120 ? 0.1544 0.1929 0.1570 -0.0102 0.0046  0.0761  120  GLU   A C   
2646 C  C   B GLU   A 120 ? 0.1688 0.2039 0.1670 -0.0021 0.0082  0.0585  120  GLU   A C   
2647 O  O   A GLU   A 120 ? 0.1531 0.1850 0.1732 -0.0118 -0.0012 0.0791  120  GLU   A O   
2648 O  O   B GLU   A 120 ? 0.1717 0.2052 0.1744 0.0012  -0.0028 0.0508  120  GLU   A O   
2649 C  CB  A GLU   A 120 ? 0.2087 0.2427 0.2276 0.0174  -0.0069 0.1267  120  GLU   A CB  
2650 C  CB  B GLU   A 120 ? 0.2209 0.2493 0.2630 0.0128  0.0187  0.0804  120  GLU   A CB  
2651 C  CG  A GLU   A 120 ? 0.2654 0.2835 0.3403 0.0283  -0.0086 0.1223  120  GLU   A CG  
2652 C  CG  B GLU   A 120 ? 0.2627 0.2837 0.3453 0.0217  0.0235  0.0823  120  GLU   A CG  
2653 C  CD  A GLU   A 120 ? 0.3125 0.3158 0.4407 0.0393  -0.0005 0.1107  120  GLU   A CD  
2654 C  CD  B GLU   A 120 ? 0.2952 0.3116 0.4132 0.0310  0.0316  0.0810  120  GLU   A CD  
2655 O  OE1 A GLU   A 120 ? 0.3299 0.3336 0.4672 0.0384  0.0042  0.1029  120  GLU   A OE1 
2656 O  OE1 B GLU   A 120 ? 0.3063 0.3240 0.4319 0.0330  0.0350  0.0774  120  GLU   A OE1 
2657 O  OE2 A GLU   A 120 ? 0.3291 0.3226 0.4813 0.0373  -0.0001 0.1111  120  GLU   A OE2 
2658 O  OE2 B GLU   A 120 ? 0.3038 0.3180 0.4410 0.0295  0.0318  0.0839  120  GLU   A OE2 
2671 N  N   . VAL   A 121 ? 0.1549 0.1948 0.1474 -0.0030 0.0116  0.0606  121  VAL   A N   
2672 C  CA  . VAL   A 121 ? 0.1616 0.2018 0.1287 -0.0010 0.0186  0.0590  121  VAL   A CA  
2673 C  C   . VAL   A 121 ? 0.1543 0.1840 0.1227 -0.0128 0.0108  0.0470  121  VAL   A C   
2674 O  O   . VAL   A 121 ? 0.1575 0.1863 0.1516 -0.0225 -0.0057 0.0367  121  VAL   A O   
2675 C  CB  . VAL   A 121 ? 0.2012 0.2446 0.1800 0.0078  0.0293  0.0702  121  VAL   A CB  
2676 C  CG1 . VAL   A 121 ? 0.2000 0.2608 0.1840 0.0195  0.0380  0.0778  121  VAL   A CG1 
2677 C  CG2 . VAL   A 121 ? 0.2326 0.2650 0.2335 -0.0008 0.0267  0.0590  121  VAL   A CG2 
2688 N  N   . LEU   A 122 ? 0.1458 0.1565 0.1383 -0.0143 0.0138  0.0427  122  LEU   A N   
2689 C  CA  . LEU   A 122 ? 0.1500 0.1457 0.1418 -0.0145 0.0320  0.0324  122  LEU   A CA  
2690 C  C   . LEU   A 122 ? 0.1485 0.1507 0.1311 -0.0152 0.0140  0.0337  122  LEU   A C   
2691 O  O   . LEU   A 122 ? 0.1419 0.1549 0.1748 -0.0216 0.0100  0.0363  122  LEU   A O   
2692 C  CB  . LEU   A 122 ? 0.1642 0.1518 0.1791 -0.0069 0.0195  0.0421  122  LEU   A CB  
2693 C  CG  . LEU   A 122 ? 0.1632 0.1598 0.1676 -0.0041 0.0256  0.0326  122  LEU   A CG  
2694 C  CD1 . LEU   A 122 ? 0.1793 0.1689 0.1790 -0.0044 0.0188  0.0365  122  LEU   A CD1 
2695 C  CD2 . LEU   A 122 ? 0.1577 0.1519 0.1631 -0.0009 0.0363  0.0202  122  LEU   A CD2 
2707 N  N   . LEU   A 123 ? 0.1421 0.1436 0.1382 -0.0153 0.0065  0.0286  123  LEU   A N   
2708 C  CA  . LEU   A 123 ? 0.1350 0.1424 0.1313 -0.0141 0.0104  0.0316  123  LEU   A CA  
2709 C  C   . LEU   A 123 ? 0.1339 0.1466 0.1219 -0.0092 0.0081  0.0277  123  LEU   A C   
2710 O  O   . LEU   A 123 ? 0.1335 0.1563 0.1351 -0.0249 0.0037  0.0312  123  LEU   A O   
2711 C  CB  . LEU   A 123 ? 0.1474 0.1493 0.1319 -0.0124 0.0187  0.0346  123  LEU   A CB  
2712 C  CG  . LEU   A 123 ? 0.1524 0.1597 0.1466 -0.0104 0.0137  0.0248  123  LEU   A CG  
2713 C  CD1 . LEU   A 123 ? 0.1573 0.1709 0.1731 0.0038  0.0127  0.0166  123  LEU   A CD1 
2714 C  CD2 . LEU   A 123 ? 0.1634 0.1711 0.1550 -0.0063 0.0097  0.0139  123  LEU   A CD2 
2726 N  N   A ALA   A 124 ? 0.1285 0.1377 0.1159 -0.0093 0.0114  0.0284  124  ALA   A N   
2727 N  N   B ALA   A 124 ? 0.1356 0.1416 0.1275 -0.0179 0.0061  0.0226  124  ALA   A N   
2728 C  CA  A ALA   A 124 ? 0.1182 0.1302 0.1252 0.0003  0.0071  0.0309  124  ALA   A CA  
2729 C  CA  B ALA   A 124 ? 0.1379 0.1402 0.1412 -0.0224 0.0018  0.0206  124  ALA   A CA  
2730 C  C   A ALA   A 124 ? 0.1182 0.1233 0.1346 -0.0076 0.0151  0.0258  124  ALA   A C   
2731 C  C   B ALA   A 124 ? 0.1350 0.1311 0.1396 -0.0194 0.0022  0.0238  124  ALA   A C   
2732 O  O   A ALA   A 124 ? 0.1204 0.1351 0.1493 -0.0111 0.0237  0.0252  124  ALA   A O   
2733 O  O   B ALA   A 124 ? 0.1317 0.1271 0.1522 -0.0047 0.0078  0.0238  124  ALA   A O   
2734 C  CB  A ALA   A 124 ? 0.1112 0.1241 0.1372 0.0082  0.0040  0.0313  124  ALA   A CB  
2735 C  CB  B ALA   A 124 ? 0.1465 0.1425 0.1519 -0.0240 0.0012  0.0197  124  ALA   A CB  
2746 N  N   A PRO   A 125 ? 0.1162 0.1239 0.1424 -0.0002 0.0160  0.0318  125  PRO   A N   
2747 N  N   B PRO   A 125 ? 0.1320 0.1305 0.1214 -0.0136 0.0006  0.0311  125  PRO   A N   
2748 C  CA  A PRO   A 125 ? 0.1243 0.1287 0.1588 -0.0031 0.0060  0.0244  125  PRO   A CA  
2749 C  CA  B PRO   A 125 ? 0.1367 0.1361 0.1261 -0.0119 -0.0004 0.0286  125  PRO   A CA  
2750 C  C   A PRO   A 125 ? 0.1174 0.1267 0.1542 -0.0026 0.0069  0.0293  125  PRO   A C   
2751 C  C   B PRO   A 125 ? 0.1344 0.1419 0.1266 -0.0115 -0.0018 0.0259  125  PRO   A C   
2752 O  O   A PRO   A 125 ? 0.1238 0.1300 0.1676 0.0034  -0.0021 0.0194  125  PRO   A O   
2753 O  O   B PRO   A 125 ? 0.1410 0.1384 0.1349 -0.0126 -0.0049 0.0303  125  PRO   A O   
2754 C  CB  A PRO   A 125 ? 0.1382 0.1332 0.1467 -0.0077 0.0047  0.0219  125  PRO   A CB  
2755 C  CB  B PRO   A 125 ? 0.1401 0.1341 0.1191 -0.0109 0.0021  0.0322  125  PRO   A CB  
2756 C  CG  A PRO   A 125 ? 0.1398 0.1361 0.1545 -0.0174 0.0096  0.0183  125  PRO   A CG  
2757 C  CG  B PRO   A 125 ? 0.1397 0.1331 0.1322 -0.0157 0.0004  0.0301  125  PRO   A CG  
2758 C  CD  A PRO   A 125 ? 0.1307 0.1391 0.1561 -0.0128 0.0145  0.0199  125  PRO   A CD  
2759 C  CD  B PRO   A 125 ? 0.1325 0.1242 0.1175 -0.0188 0.0049  0.0321  125  PRO   A CD  
2774 N  N   A LEU   A 126 ? 0.1144 0.1269 0.1524 0.0013  0.0127  0.0326  126  LEU   A N   
2775 N  N   B LEU   A 126 ? 0.1359 0.1461 0.1318 -0.0051 -0.0062 0.0171  126  LEU   A N   
2776 C  CA  A LEU   A 126 ? 0.1326 0.1401 0.1598 0.0053  0.0100  0.0353  126  LEU   A CA  
2777 C  CA  B LEU   A 126 ? 0.1362 0.1347 0.1323 -0.0117 0.0024  0.0212  126  LEU   A CA  
2778 C  C   A LEU   A 126 ? 0.1503 0.1521 0.1701 0.0172  0.0110  0.0349  126  LEU   A C   
2779 C  C   B LEU   A 126 ? 0.1320 0.1313 0.1334 -0.0032 0.0025  0.0087  126  LEU   A C   
2780 O  O   A LEU   A 126 ? 0.1754 0.1639 0.2102 0.0265  0.0318  0.0535  126  LEU   A O   
2781 O  O   B LEU   A 126 ? 0.1367 0.1372 0.1329 0.0034  -0.0088 0.0284  126  LEU   A O   
2782 C  CB  A LEU   A 126 ? 0.1420 0.1414 0.1739 0.0033  -0.0094 0.0267  126  LEU   A CB  
2783 C  CB  B LEU   A 126 ? 0.1429 0.1433 0.1495 -0.0105 0.0027  0.0157  126  LEU   A CB  
2784 C  CG  A LEU   A 126 ? 0.1359 0.1529 0.2099 0.0100  -0.0028 0.0190  126  LEU   A CG  
2785 C  CG  B LEU   A 126 ? 0.1344 0.1380 0.1769 -0.0053 0.0061  0.0148  126  LEU   A CG  
2786 C  CD1 A LEU   A 126 ? 0.1391 0.1608 0.2419 0.0151  -0.0101 0.0292  126  LEU   A CD1 
2787 C  CD1 B LEU   A 126 ? 0.1362 0.1404 0.2156 -0.0045 -0.0042 0.0084  126  LEU   A CD1 
2788 C  CD2 A LEU   A 126 ? 0.1470 0.1549 0.2110 0.0014  0.0087  0.0188  126  LEU   A CD2 
2789 C  CD2 B LEU   A 126 ? 0.1274 0.1336 0.1777 -0.0060 0.0200  0.0209  126  LEU   A CD2 
2812 N  N   A LEU   A 127 ? 0.1471 0.1516 0.1691 0.0057  0.0113  0.0256  127  LEU   A N   
2813 N  N   B LEU   A 127 ? 0.1208 0.1306 0.1373 0.0004  0.0084  0.0229  127  LEU   A N   
2814 C  CA  A LEU   A 127 ? 0.1382 0.1477 0.1547 0.0035  0.0054  0.0226  127  LEU   A CA  
2815 C  CA  B LEU   A 127 ? 0.1207 0.1426 0.1413 -0.0016 0.0078  0.0295  127  LEU   A CA  
2816 C  C   A LEU   A 127 ? 0.1358 0.1333 0.1351 0.0097  0.0026  0.0238  127  LEU   A C   
2817 C  C   B LEU   A 127 ? 0.1272 0.1424 0.1520 -0.0056 0.0020  0.0200  127  LEU   A C   
2818 O  O   A LEU   A 127 ? 0.1415 0.1374 0.1475 0.0009  -0.0048 0.0230  127  LEU   A O   
2819 O  O   B LEU   A 127 ? 0.1325 0.1495 0.1538 -0.0181 0.0092  0.0176  127  LEU   A O   
2820 C  CB  A LEU   A 127 ? 0.1362 0.1457 0.1564 0.0063  0.0014  0.0150  127  LEU   A CB  
2821 C  CB  B LEU   A 127 ? 0.1195 0.1587 0.1409 0.0016  0.0106  0.0251  127  LEU   A CB  
2822 C  CG  A LEU   A 127 ? 0.1410 0.1425 0.1533 0.0087  -0.0038 0.0182  127  LEU   A CG  
2823 C  CG  B LEU   A 127 ? 0.1273 0.1732 0.1496 0.0047  0.0052  0.0260  127  LEU   A CG  
2824 C  CD1 A LEU   A 127 ? 0.1441 0.1362 0.1721 -0.0008 -0.0086 0.0136  127  LEU   A CD1 
2825 C  CD1 B LEU   A 127 ? 0.1327 0.1781 0.1725 0.0126  0.0097  0.0222  127  LEU   A CD1 
2826 C  CD2 A LEU   A 127 ? 0.1497 0.1451 0.1671 0.0171  -0.0178 0.0214  127  LEU   A CD2 
2827 C  CD2 B LEU   A 127 ? 0.1353 0.1813 0.1454 0.0050  -0.0091 0.0124  127  LEU   A CD2 
2850 N  N   A SER   A 128 ? 0.1439 0.1387 0.1239 0.0017  0.0023  0.0190  128  SER   A N   
2851 N  N   B SER   A 128 ? 0.1368 0.1389 0.1582 -0.0083 -0.0001 0.0153  128  SER   A N   
2852 C  CA  A SER   A 128 ? 0.1476 0.1397 0.1149 0.0033  -0.0033 0.0177  128  SER   A CA  
2853 C  CA  B SER   A 128 ? 0.1410 0.1360 0.1578 -0.0062 -0.0047 0.0098  128  SER   A CA  
2854 C  C   A SER   A 128 ? 0.1485 0.1410 0.1172 0.0035  -0.0035 0.0238  128  SER   A C   
2855 C  C   B SER   A 128 ? 0.1434 0.1403 0.1596 -0.0052 -0.0203 0.0169  128  SER   A C   
2856 O  O   A SER   A 128 ? 0.1558 0.1660 0.1340 0.0063  0.0071  0.0154  128  SER   A O   
2857 O  O   B SER   A 128 ? 0.1384 0.1552 0.1674 -0.0065 -0.0241 0.0276  128  SER   A O   
2858 C  CB  A SER   A 128 ? 0.1528 0.1327 0.1077 -0.0080 -0.0119 0.0212  128  SER   A CB  
2859 C  CB  B SER   A 128 ? 0.1484 0.1346 0.1614 -0.0057 -0.0110 0.0147  128  SER   A CB  
2860 O  OG  A SER   A 128 ? 0.1518 0.1422 0.1186 -0.0038 -0.0025 0.0113  128  SER   A OG  
2861 O  OG  B SER   A 128 ? 0.1451 0.1352 0.1653 -0.0044 0.0008  0.0153  128  SER   A OG  
2872 N  N   A ALA   A 129 ? 0.1464 0.1433 0.1343 0.0015  -0.0100 0.0211  129  ALA   A N   
2873 N  N   B ALA   A 129 ? 0.1454 0.1401 0.1704 0.0016  -0.0204 0.0163  129  ALA   A N   
2874 C  CA  A ALA   A 129 ? 0.1416 0.1539 0.1484 0.0041  -0.0015 0.0232  129  ALA   A CA  
2875 C  CA  B ALA   A 129 ? 0.1532 0.1481 0.1871 -0.0037 -0.0157 0.0046  129  ALA   A CA  
2876 C  C   A ALA   A 129 ? 0.1347 0.1476 0.1285 0.0128  -0.0097 0.0087  129  ALA   A C   
2877 C  C   B ALA   A 129 ? 0.1586 0.1548 0.1958 0.0022  -0.0056 0.0085  129  ALA   A C   
2878 O  O   A ALA   A 129 ? 0.1353 0.1471 0.1176 0.0085  0.0003  0.0127  129  ALA   A O   
2879 O  O   B ALA   A 129 ? 0.1589 0.1632 0.1877 0.0019  0.0029  0.0046  129  ALA   A O   
2880 C  CB  A ALA   A 129 ? 0.1565 0.1780 0.1879 0.0155  -0.0010 0.0428  129  ALA   A CB  
2881 C  CB  B ALA   A 129 ? 0.1549 0.1571 0.2052 -0.0092 -0.0116 -0.0132 129  ALA   A CB  
2892 N  N   A GLY   A 130 ? 0.1445 0.1564 0.1708 0.0124  -0.0001 0.0106  130  GLY   A N   
2893 N  N   B GLY   A 130 ? 0.1689 0.1627 0.2117 0.0074  0.0022  0.0140  130  GLY   A N   
2894 C  CA  A GLY   A 130 ? 0.1594 0.1510 0.1799 0.0119  -0.0145 0.0138  130  GLY   A CA  
2895 C  CA  B GLY   A 130 ? 0.1755 0.1615 0.2137 0.0099  0.0023  0.0174  130  GLY   A CA  
2896 C  C   A GLY   A 130 ? 0.1756 0.1489 0.1788 0.0059  -0.0231 0.0111  130  GLY   A C   
2897 C  C   B GLY   A 130 ? 0.1832 0.1555 0.2078 0.0084  -0.0075 0.0205  130  GLY   A C   
2898 O  O   A GLY   A 130 ? 0.1862 0.1394 0.1747 0.0066  -0.0334 0.0048  130  GLY   A O   
2899 O  O   B GLY   A 130 ? 0.1955 0.1621 0.2086 0.0107  -0.0138 0.0153  130  GLY   A O   
2906 N  N   A ILE   A 131 ? 0.1765 0.1450 0.1774 -0.0037 -0.0243 0.0133  131  ILE   A N   
2907 N  N   B ILE   A 131 ? 0.1744 0.1443 0.1988 0.0080  -0.0098 0.0238  131  ILE   A N   
2908 C  CA  A ILE   A 131 ? 0.1893 0.1468 0.1590 -0.0046 -0.0386 0.0157  131  ILE   A CA  
2909 C  CA  B ILE   A 131 ? 0.1616 0.1419 0.1912 0.0107  -0.0227 0.0217  131  ILE   A CA  
2910 C  C   A ILE   A 131 ? 0.1829 0.1575 0.1485 -0.0113 -0.0316 0.0237  131  ILE   A C   
2911 C  C   B ILE   A 131 ? 0.1638 0.1487 0.1780 0.0045  -0.0210 0.0143  131  ILE   A C   
2912 O  O   A ILE   A 131 ? 0.1931 0.1740 0.1675 -0.0105 -0.0322 0.0340  131  ILE   A O   
2913 O  O   B ILE   A 131 ? 0.1729 0.1578 0.1828 -0.0059 -0.0164 0.0083  131  ILE   A O   
2914 C  CB  A ILE   A 131 ? 0.2015 0.1547 0.1745 -0.0001 -0.0481 0.0017  131  ILE   A CB  
2915 C  CB  B ILE   A 131 ? 0.1546 0.1489 0.1959 0.0171  -0.0364 0.0179  131  ILE   A CB  
2916 C  CG1 A ILE   A 131 ? 0.2116 0.1871 0.1973 0.0014  -0.0619 -0.0083 131  ILE   A CG1 
2917 C  CG1 B ILE   A 131 ? 0.1596 0.1653 0.1987 0.0173  -0.0314 0.0195  131  ILE   A CG1 
2918 C  CG2 A ILE   A 131 ? 0.2031 0.1417 0.1949 0.0040  -0.0467 -0.0078 131  ILE   A CG2 
2919 C  CG2 B ILE   A 131 ? 0.1562 0.1516 0.2070 0.0163  -0.0329 0.0090  131  ILE   A CG2 
2920 C  CD1 A ILE   A 131 ? 0.2158 0.1965 0.2226 -0.0005 -0.0666 -0.0189 131  ILE   A CD1 
2921 C  CD1 B ILE   A 131 ? 0.1659 0.1755 0.2135 0.0090  -0.0381 0.0052  131  ILE   A CD1 
2944 N  N   A PHE   A 132 ? 0.1741 0.1546 0.1436 -0.0021 -0.0154 0.0225  132  PHE   A N   
2945 N  N   B PHE   A 132 ? 0.1549 0.1487 0.1780 0.0152  -0.0242 0.0124  132  PHE   A N   
2946 C  CA  A PHE   A 132 ? 0.1781 0.1676 0.1327 -0.0043 0.0008  0.0046  132  PHE   A CA  
2947 C  CA  B PHE   A 132 ? 0.1468 0.1552 0.1768 0.0139  -0.0212 0.0147  132  PHE   A CA  
2948 C  C   A PHE   A 132 ? 0.1791 0.1762 0.1249 -0.0126 -0.0015 0.0075  132  PHE   A C   
2949 C  C   B PHE   A 132 ? 0.1539 0.1664 0.1814 0.0201  -0.0259 0.0145  132  PHE   A C   
2950 O  O   A PHE   A 132 ? 0.1854 0.1844 0.1375 -0.0245 -0.0067 0.0083  132  PHE   A O   
2951 O  O   B PHE   A 132 ? 0.1721 0.1869 0.1887 0.0115  -0.0094 0.0128  132  PHE   A O   
2952 C  CB  A PHE   A 132 ? 0.1747 0.1657 0.1290 -0.0058 -0.0043 0.0042  132  PHE   A CB  
2953 C  CB  B PHE   A 132 ? 0.1339 0.1494 0.1552 0.0111  -0.0150 0.0375  132  PHE   A CB  
2954 C  CG  A PHE   A 132 ? 0.1744 0.1648 0.1181 -0.0019 -0.0002 0.0065  132  PHE   A CG  
2955 C  CG  B PHE   A 132 ? 0.1381 0.1502 0.1519 0.0126  -0.0156 0.0426  132  PHE   A CG  
2956 C  CD1 A PHE   A 132 ? 0.1798 0.1711 0.1294 0.0022  -0.0073 -0.0047 132  PHE   A CD1 
2957 C  CD1 B PHE   A 132 ? 0.1421 0.1553 0.1639 0.0148  -0.0169 0.0316  132  PHE   A CD1 
2958 C  CD2 A PHE   A 132 ? 0.1694 0.1756 0.1203 -0.0012 -0.0009 0.0001  132  PHE   A CD2 
2959 C  CD2 B PHE   A 132 ? 0.1422 0.1668 0.1689 0.0119  -0.0187 0.0306  132  PHE   A CD2 
2960 C  CE1 A PHE   A 132 ? 0.1758 0.1809 0.1358 0.0021  -0.0067 -0.0041 132  PHE   A CE1 
2961 C  CE1 B PHE   A 132 ? 0.1478 0.1620 0.1730 0.0141  -0.0207 0.0260  132  PHE   A CE1 
2962 C  CE2 A PHE   A 132 ? 0.1692 0.1833 0.1381 0.0026  -0.0048 0.0021  132  PHE   A CE2 
2963 C  CE2 B PHE   A 132 ? 0.1459 0.1770 0.1835 0.0131  -0.0211 0.0246  132  PHE   A CE2 
2964 C  CZ  A PHE   A 132 ? 0.1658 0.1811 0.1348 0.0001  -0.0060 0.0027  132  PHE   A CZ  
2965 C  CZ  B PHE   A 132 ? 0.1480 0.1698 0.1845 0.0087  -0.0281 0.0269  132  PHE   A CZ  
2984 N  N   A GLY   A 133 ? 0.1820 0.1794 0.1405 -0.0060 -0.0176 0.0114  133  GLY   A N   
2985 N  N   B GLY   A 133 ? 0.1577 0.1629 0.1773 0.0202  -0.0320 0.0202  133  GLY   A N   
2986 C  CA  A GLY   A 133 ? 0.1929 0.1835 0.1527 -0.0102 -0.0257 0.0031  133  GLY   A CA  
2987 C  CA  B GLY   A 133 ? 0.1684 0.1668 0.1852 0.0113  -0.0356 0.0084  133  GLY   A CA  
2988 C  C   A GLY   A 133 ? 0.1947 0.1909 0.1611 -0.0098 -0.0453 0.0014  133  GLY   A C   
2989 C  C   B GLY   A 133 ? 0.1752 0.1720 0.1902 0.0028  -0.0474 -0.0001 133  GLY   A C   
2990 O  O   A GLY   A 133 ? 0.1965 0.2023 0.1740 -0.0003 -0.0485 -0.0202 133  GLY   A O   
2991 O  O   B GLY   A 133 ? 0.1790 0.1787 0.1918 0.0005  -0.0527 -0.0170 133  GLY   A O   
2998 N  N   A ALA   A 134 ? 0.1944 0.1817 0.1524 -0.0164 -0.0295 0.0075  134  ALA   A N   
2999 N  N   B ALA   A 134 ? 0.1757 0.1674 0.1883 0.0009  -0.0369 0.0030  134  ALA   A N   
3000 C  CA  A ALA   A 134 ? 0.1918 0.1819 0.1832 -0.0165 -0.0297 0.0025  134  ALA   A CA  
3001 C  CA  B ALA   A 134 ? 0.1764 0.1655 0.1932 -0.0006 -0.0399 0.0115  134  ALA   A CA  
3002 C  C   A ALA   A 134 ? 0.1917 0.1893 0.1832 -0.0161 -0.0284 0.0056  134  ALA   A C   
3003 C  C   B ALA   A 134 ? 0.1772 0.1651 0.1855 -0.0061 -0.0340 0.0210  134  ALA   A C   
3004 O  O   A ALA   A 134 ? 0.2029 0.1947 0.2059 -0.0167 -0.0137 0.0089  134  ALA   A O   
3005 O  O   B ALA   A 134 ? 0.1791 0.1666 0.2075 -0.0166 -0.0196 0.0247  134  ALA   A O   
3006 C  CB  A ALA   A 134 ? 0.1913 0.1751 0.2038 -0.0168 -0.0246 -0.0042 134  ALA   A CB  
3007 C  CB  B ALA   A 134 ? 0.1771 0.1626 0.2085 -0.0017 -0.0399 0.0045  134  ALA   A CB  
3018 N  N   A ASP   A 135 ? 0.1924 0.1930 0.2007 -0.0173 -0.0302 0.0155  135  ASP   A N   
3019 N  N   B ASP   A 135 ? 0.1857 0.1725 0.1950 -0.0107 -0.0339 0.0216  135  ASP   A N   
3020 C  CA  A ASP   A 135 ? 0.1894 0.2038 0.2307 -0.0274 -0.0432 0.0363  135  ASP   A CA  
3021 C  CA  B ASP   A 135 ? 0.1869 0.1764 0.2156 -0.0180 -0.0397 0.0194  135  ASP   A CA  
3022 C  C   A ASP   A 135 ? 0.1812 0.1964 0.2319 -0.0153 -0.0349 0.0570  135  ASP   A C   
3023 C  C   B ASP   A 135 ? 0.1769 0.1662 0.2122 -0.0190 -0.0354 0.0289  135  ASP   A C   
3024 O  O   A ASP   A 135 ? 0.1745 0.1947 0.2264 -0.0125 -0.0418 0.0572  135  ASP   A O   
3025 O  O   B ASP   A 135 ? 0.1737 0.1637 0.2114 -0.0212 -0.0348 0.0402  135  ASP   A O   
3026 C  CB  A ASP   A 135 ? 0.2044 0.2257 0.2666 -0.0434 -0.0566 0.0279  135  ASP   A CB  
3027 C  CB  B ASP   A 135 ? 0.2020 0.1926 0.2445 -0.0218 -0.0414 0.0155  135  ASP   A CB  
3028 C  CG  A ASP   A 135 ? 0.2168 0.2446 0.3025 -0.0561 -0.0611 0.0194  135  ASP   A CG  
3029 C  CG  B ASP   A 135 ? 0.2136 0.2095 0.2694 -0.0253 -0.0397 0.0134  135  ASP   A CG  
3030 O  OD1 A ASP   A 135 ? 0.2148 0.2484 0.3041 -0.0635 -0.0697 0.0318  135  ASP   A OD1 
3031 O  OD1 B ASP   A 135 ? 0.2186 0.2055 0.2817 -0.0210 -0.0336 0.0120  135  ASP   A OD1 
3032 O  OD2 A ASP   A 135 ? 0.2455 0.2609 0.3549 -0.0509 -0.0272 0.0114  135  ASP   A OD2 
3033 O  OD2 B ASP   A 135 ? 0.2189 0.2292 0.2908 -0.0307 -0.0454 0.0145  135  ASP   A OD2 
3042 N  N   A PRO   A 136 ? 0.1744 0.1898 0.2379 -0.0018 -0.0212 0.0733  136  PRO   A N   
3043 N  N   B PRO   A 136 ? 0.1679 0.1592 0.2129 -0.0111 -0.0347 0.0307  136  PRO   A N   
3044 C  CA  A PRO   A 136 ? 0.1671 0.1848 0.2452 -0.0049 -0.0108 0.0603  136  PRO   A CA  
3045 C  CA  B PRO   A 136 ? 0.1625 0.1667 0.2207 -0.0126 -0.0278 0.0244  136  PRO   A CA  
3046 C  C   A PRO   A 136 ? 0.1410 0.1761 0.2388 -0.0043 -0.0015 0.0577  136  PRO   A C   
3047 C  C   B PRO   A 136 ? 0.1491 0.1703 0.2164 -0.0100 -0.0202 0.0269  136  PRO   A C   
3048 O  O   A PRO   A 136 ? 0.1320 0.1764 0.2349 0.0031  0.0085  0.0556  136  PRO   A O   
3049 O  O   B PRO   A 136 ? 0.1445 0.1644 0.2091 -0.0016 -0.0123 0.0234  136  PRO   A O   
3050 C  CB  A PRO   A 136 ? 0.1842 0.1876 0.2611 -0.0026 -0.0113 0.0582  136  PRO   A CB  
3051 C  CB  B PRO   A 136 ? 0.1755 0.1643 0.2298 -0.0108 -0.0277 0.0209  136  PRO   A CB  
3052 C  CG  A PRO   A 136 ? 0.1936 0.1946 0.2765 0.0004  -0.0135 0.0578  136  PRO   A CG  
3053 C  CG  B PRO   A 136 ? 0.1856 0.1606 0.2400 -0.0059 -0.0296 0.0214  136  PRO   A CG  
3054 C  CD  A PRO   A 136 ? 0.1862 0.1901 0.2509 0.0021  -0.0109 0.0795  136  PRO   A CD  
3055 C  CD  B PRO   A 136 ? 0.1737 0.1521 0.2209 -0.0078 -0.0326 0.0339  136  PRO   A CD  
3070 N  N   A ILE   A 137 ? 0.1376 0.1814 0.2530 -0.0060 -0.0231 0.0585  137  ILE   A N   
3071 N  N   B ILE   A 137 ? 0.1496 0.1760 0.2296 -0.0160 -0.0231 0.0245  137  ILE   A N   
3072 C  CA  A ILE   A 137 ? 0.1346 0.1895 0.2525 -0.0167 -0.0320 0.0594  137  ILE   A CA  
3073 C  CA  B ILE   A 137 ? 0.1555 0.1904 0.2356 -0.0177 -0.0215 0.0191  137  ILE   A CA  
3074 C  C   A ILE   A 137 ? 0.1342 0.1907 0.2262 -0.0216 -0.0335 0.0557  137  ILE   A C   
3075 C  C   B ILE   A 137 ? 0.1575 0.1978 0.2300 -0.0160 -0.0118 0.0206  137  ILE   A C   
3076 O  O   A ILE   A 137 ? 0.1393 0.1808 0.2234 -0.0282 -0.0158 0.0401  137  ILE   A O   
3077 O  O   B ILE   A 137 ? 0.1582 0.1979 0.2317 -0.0135 -0.0058 0.0205  137  ILE   A O   
3078 C  CB  A ILE   A 137 ? 0.1445 0.2040 0.2867 -0.0230 -0.0446 0.0680  137  ILE   A CB  
3079 C  CB  B ILE   A 137 ? 0.1663 0.1946 0.2622 -0.0232 -0.0333 0.0205  137  ILE   A CB  
3080 C  CG1 A ILE   A 137 ? 0.1613 0.2249 0.3173 -0.0218 -0.0369 0.0702  137  ILE   A CG1 
3081 C  CG1 B ILE   A 137 ? 0.1814 0.1992 0.2794 -0.0138 -0.0439 0.0364  137  ILE   A CG1 
3082 C  CG2 A ILE   A 137 ? 0.1497 0.2036 0.2953 -0.0199 -0.0498 0.0591  137  ILE   A CG2 
3083 C  CG2 B ILE   A 137 ? 0.1703 0.1939 0.2688 -0.0220 -0.0289 0.0167  137  ILE   A CG2 
3084 C  CD1 A ILE   A 137 ? 0.1794 0.2357 0.3404 -0.0178 -0.0258 0.0700  137  ILE   A CD1 
3085 C  CD1 B ILE   A 137 ? 0.1906 0.2030 0.2963 -0.0088 -0.0397 0.0467  137  ILE   A CD1 
3108 N  N   A HIS   A 138 ? 0.1391 0.2060 0.2193 -0.0136 -0.0207 0.0520  138  HIS   A N   
3109 N  N   B HIS   A 138 ? 0.1621 0.2122 0.2240 -0.0140 -0.0018 0.0193  138  HIS   A N   
3110 C  CA  A HIS   A 138 ? 0.1441 0.2162 0.2062 -0.0147 -0.0180 0.0463  138  HIS   A CA  
3111 C  CA  B HIS   A 138 ? 0.1614 0.2149 0.2053 -0.0161 -0.0015 0.0261  138  HIS   A CA  
3112 C  C   A HIS   A 138 ? 0.1357 0.2054 0.1930 -0.0102 -0.0136 0.0483  138  HIS   A C   
3113 C  C   B HIS   A 138 ? 0.1494 0.2046 0.1903 -0.0132 0.0009  0.0383  138  HIS   A C   
3114 O  O   A HIS   A 138 ? 0.1356 0.2062 0.2014 -0.0099 -0.0084 0.0397  138  HIS   A O   
3115 O  O   B HIS   A 138 ? 0.1562 0.2066 0.1927 -0.0151 0.0070  0.0308  138  HIS   A O   
3116 C  CB  A HIS   A 138 ? 0.1676 0.2371 0.2016 -0.0142 -0.0300 0.0403  138  HIS   A CB  
3117 C  CB  B HIS   A 138 ? 0.1725 0.2299 0.2006 -0.0157 -0.0060 0.0181  138  HIS   A CB  
3118 C  CG  A HIS   A 138 ? 0.1845 0.2447 0.2108 -0.0204 -0.0283 0.0299  138  HIS   A CG  
3119 C  CG  B HIS   A 138 ? 0.1837 0.2377 0.2099 -0.0190 -0.0092 0.0095  138  HIS   A CG  
3120 N  ND1 A HIS   A 138 ? 0.1943 0.2529 0.2240 -0.0220 -0.0214 0.0173  138  HIS   A ND1 
3121 N  ND1 B HIS   A 138 ? 0.1916 0.2440 0.2230 -0.0213 -0.0079 0.0020  138  HIS   A ND1 
3122 C  CD2 A HIS   A 138 ? 0.1872 0.2501 0.2109 -0.0190 -0.0312 0.0293  138  HIS   A CD2 
3123 C  CD2 B HIS   A 138 ? 0.1850 0.2416 0.2109 -0.0178 -0.0100 0.0105  138  HIS   A CD2 
3124 C  CE1 A HIS   A 138 ? 0.1980 0.2567 0.2227 -0.0213 -0.0195 0.0180  138  HIS   A CE1 
3125 C  CE1 B HIS   A 138 ? 0.1931 0.2459 0.2224 -0.0189 -0.0063 0.0051  138  HIS   A CE1 
3126 N  NE2 A HIS   A 138 ? 0.1948 0.2559 0.2089 -0.0181 -0.0212 0.0247  138  HIS   A NE2 
3127 N  NE2 B HIS   A 138 ? 0.1906 0.2458 0.2127 -0.0174 -0.0033 0.0094  138  HIS   A NE2 
3142 N  N   . SER   A 139 ? 0.1360 0.1918 0.1868 -0.0061 -0.0080 0.0487  139  SER   A N   
3143 C  CA  . SER   A 139 ? 0.1345 0.1844 0.1848 -0.0099 -0.0037 0.0490  139  SER   A CA  
3144 C  C   . SER   A 139 ? 0.1243 0.1661 0.1932 -0.0102 0.0028  0.0369  139  SER   A C   
3145 O  O   . SER   A 139 ? 0.1270 0.1591 0.2008 -0.0095 -0.0021 0.0398  139  SER   A O   
3146 C  CB  . SER   A 139 ? 0.1372 0.1829 0.1932 -0.0151 -0.0090 0.0497  139  SER   A CB  
3147 O  OG  . SER   A 139 ? 0.1381 0.1747 0.2026 -0.0188 -0.0160 0.0570  139  SER   A OG  
3154 N  N   A LEU   A 140 ? 0.1285 0.1715 0.1938 -0.0034 -0.0029 0.0350  140  LEU   A N   
3155 N  N   B LEU   A 140 ? 0.1226 0.1606 0.1718 -0.0176 0.0043  0.0475  140  LEU   A N   
3156 C  CA  A LEU   A 140 ? 0.1244 0.1669 0.1899 -0.0030 -0.0046 0.0239  140  LEU   A CA  
3157 C  CA  B LEU   A 140 ? 0.1168 0.1486 0.1586 -0.0238 0.0082  0.0447  140  LEU   A CA  
3158 C  C   A LEU   A 140 ? 0.1201 0.1752 0.1866 -0.0023 0.0002  0.0146  140  LEU   A C   
3159 C  C   B LEU   A 140 ? 0.1153 0.1496 0.1434 -0.0219 0.0105  0.0458  140  LEU   A C   
3160 O  O   A LEU   A 140 ? 0.1273 0.1713 0.1878 0.0032  0.0101  0.0113  140  LEU   A O   
3161 O  O   B LEU   A 140 ? 0.1206 0.1453 0.1622 -0.0097 0.0072  0.0364  140  LEU   A O   
3162 C  CB  A LEU   A 140 ? 0.1292 0.1573 0.2001 -0.0038 -0.0070 0.0118  140  LEU   A CB  
3163 C  CB  B LEU   A 140 ? 0.1160 0.1433 0.1603 -0.0276 0.0037  0.0383  140  LEU   A CB  
3164 C  CG  A LEU   A 140 ? 0.1365 0.1484 0.2195 -0.0073 0.0070  0.0097  140  LEU   A CG  
3165 C  CG  B LEU   A 140 ? 0.1169 0.1392 0.1692 -0.0274 0.0103  0.0365  140  LEU   A CG  
3166 C  CD1 A LEU   A 140 ? 0.1356 0.1480 0.2367 0.0045  -0.0017 0.0051  140  LEU   A CD1 
3167 C  CD1 B LEU   A 140 ? 0.1185 0.1409 0.1780 -0.0197 0.0161  0.0393  140  LEU   A CD1 
3168 C  CD2 A LEU   A 140 ? 0.1487 0.1502 0.2341 -0.0047 0.0138  0.0066  140  LEU   A CD2 
3169 C  CD2 B LEU   A 140 ? 0.1184 0.1387 0.1795 -0.0220 0.0083  0.0350  140  LEU   A CD2 
3192 N  N   A ARG   A 141 ? 0.1220 0.1841 0.1909 -0.0036 -0.0123 0.0087  141  ARG   A N   
3193 N  N   B ARG   A 141 ? 0.1233 0.1585 0.1495 -0.0184 -0.0023 0.0440  141  ARG   A N   
3194 C  CA  A ARG   A 141 ? 0.1390 0.1985 0.2041 -0.0238 -0.0090 -0.0043 141  ARG   A CA  
3195 C  CA  B ARG   A 141 ? 0.1294 0.1723 0.1654 -0.0254 -0.0009 0.0309  141  ARG   A CA  
3196 C  C   A ARG   A 141 ? 0.1388 0.1787 0.2020 -0.0192 -0.0026 0.0043  141  ARG   A C   
3197 C  C   B ARG   A 141 ? 0.1342 0.1629 0.1714 -0.0181 -0.0020 0.0288  141  ARG   A C   
3198 O  O   A ARG   A 141 ? 0.1376 0.1707 0.2086 -0.0226 0.0129  0.0046  141  ARG   A O   
3199 O  O   B ARG   A 141 ? 0.1334 0.1609 0.1837 -0.0169 0.0044  0.0244  141  ARG   A O   
3200 C  CB  A ARG   A 141 ? 0.1585 0.2303 0.2219 -0.0355 -0.0050 -0.0143 141  ARG   A CB  
3201 C  CB  B ARG   A 141 ? 0.1311 0.1897 0.1574 -0.0311 0.0158  0.0250  141  ARG   A CB  
3202 C  CG  A ARG   A 141 ? 0.1993 0.2648 0.2586 -0.0367 -0.0221 -0.0225 141  ARG   A CG  
3203 C  CG  B ARG   A 141 ? 0.1462 0.2001 0.1564 -0.0309 0.0194  0.0154  141  ARG   A CG  
3204 C  CD  A ARG   A 141 ? 0.2190 0.2873 0.2817 -0.0477 -0.0339 -0.0160 141  ARG   A CD  
3205 C  CD  B ARG   A 141 ? 0.1555 0.1947 0.1716 -0.0315 0.0023  0.0131  141  ARG   A CD  
3206 N  NE  A ARG   A 141 ? 0.2197 0.3049 0.3012 -0.0545 -0.0316 -0.0093 141  ARG   A NE  
3207 N  NE  B ARG   A 141 ? 0.1611 0.2046 0.1769 -0.0231 0.0082  0.0173  141  ARG   A NE  
3208 C  CZ  A ARG   A 141 ? 0.2148 0.3241 0.3062 -0.0680 -0.0282 -0.0027 141  ARG   A CZ  
3209 C  CZ  B ARG   A 141 ? 0.1649 0.2100 0.1723 -0.0241 0.0222  0.0256  141  ARG   A CZ  
3210 N  NH1 A ARG   A 141 ? 0.2146 0.3323 0.3137 -0.0646 -0.0284 0.0016  141  ARG   A NH1 
3211 N  NH1 B ARG   A 141 ? 0.1675 0.2179 0.1623 -0.0304 0.0311  0.0161  141  ARG   A NH1 
3212 N  NH2 A ARG   A 141 ? 0.2121 0.3333 0.3047 -0.0719 -0.0224 -0.0012 141  ARG   A NH2 
3213 N  NH2 B ARG   A 141 ? 0.1656 0.2136 0.1786 -0.0111 0.0207  0.0295  141  ARG   A NH2 
3240 N  N   A VAL   A 142 ? 0.1268 0.1704 0.1928 -0.0127 -0.0062 0.0043  142  VAL   A N   
3241 N  N   B VAL   A 142 ? 0.1320 0.1639 0.1722 -0.0100 0.0017  0.0245  142  VAL   A N   
3242 C  CA  A VAL   A 142 ? 0.1243 0.1610 0.1932 -0.0102 0.0138  0.0122  142  VAL   A CA  
3243 C  CA  B VAL   A 142 ? 0.1383 0.1628 0.1724 -0.0047 0.0062  0.0230  142  VAL   A CA  
3244 C  C   A VAL   A 142 ? 0.1166 0.1576 0.1846 -0.0127 0.0088  0.0154  142  VAL   A C   
3245 C  C   B VAL   A 142 ? 0.1258 0.1572 0.1745 -0.0095 0.0026  0.0234  142  VAL   A C   
3246 O  O   A VAL   A 142 ? 0.1246 0.1607 0.1859 -0.0007 0.0062  0.0157  142  VAL   A O   
3247 O  O   B VAL   A 142 ? 0.1304 0.1591 0.1756 -0.0027 -0.0023 0.0272  142  VAL   A O   
3248 C  CB  A VAL   A 142 ? 0.1272 0.1519 0.1928 -0.0077 0.0113  0.0179  142  VAL   A CB  
3249 C  CB  B VAL   A 142 ? 0.1523 0.1711 0.1667 0.0020  0.0050  0.0246  142  VAL   A CB  
3250 C  CG1 A VAL   A 142 ? 0.1255 0.1283 0.2024 -0.0124 0.0188  0.0163  142  VAL   A CG1 
3251 C  CG1 B VAL   A 142 ? 0.1567 0.1675 0.1640 0.0047  0.0035  0.0152  142  VAL   A CG1 
3252 C  CG2 A VAL   A 142 ? 0.1396 0.1690 0.2142 -0.0023 0.0057  0.0100  142  VAL   A CG2 
3253 C  CG2 B VAL   A 142 ? 0.1629 0.1822 0.1793 0.0110  -0.0063 0.0303  142  VAL   A CG2 
3272 N  N   . CYS   A 143 ? 0.1216 0.1532 0.1790 -0.0133 0.0020  0.0165  143  CYS   A N   
3273 C  CA  . CYS   A 143 ? 0.1268 0.1479 0.1874 -0.0065 0.0069  0.0183  143  CYS   A CA  
3274 C  C   . CYS   A 143 ? 0.1291 0.1408 0.1866 -0.0079 0.0087  0.0246  143  CYS   A C   
3275 O  O   . CYS   A 143 ? 0.1247 0.1451 0.1852 -0.0068 0.0034  0.0260  143  CYS   A O   
3276 C  CB  . CYS   A 143 ? 0.1382 0.1524 0.1899 -0.0074 0.0186  0.0307  143  CYS   A CB  
3277 S  SG  . CYS   A 143 ? 0.1559 0.1593 0.1741 0.0039  0.0135  0.0219  143  CYS   A SG  
3284 N  N   . VAL   A 144 ? 0.1288 0.1473 0.1994 -0.0097 0.0109  0.0325  144  VAL   A N   
3285 C  CA  . VAL   A 144 ? 0.1357 0.1578 0.2274 -0.0180 0.0217  0.0316  144  VAL   A CA  
3286 C  C   . VAL   A 144 ? 0.1348 0.1483 0.2164 -0.0207 0.0003  0.0298  144  VAL   A C   
3287 O  O   . VAL   A 144 ? 0.1537 0.1558 0.2168 -0.0072 -0.0011 0.0344  144  VAL   A O   
3288 C  CB  . VAL   A 144 ? 0.1532 0.1784 0.2789 -0.0055 0.0402  0.0277  144  VAL   A CB  
3289 C  CG1 . VAL   A 144 ? 0.1637 0.1977 0.3126 -0.0186 0.0212  0.0189  144  VAL   A CG1 
3290 C  CG2 . VAL   A 144 ? 0.1512 0.1803 0.2952 -0.0100 0.0438  0.0404  144  VAL   A CG2 
3300 N  N   . ASP   A 145 ? 0.1379 0.1455 0.2300 -0.0203 0.0113  0.0172  145  ASP   A N   
3301 C  CA  . ASP   A 145 ? 0.1483 0.1518 0.2246 -0.0189 0.0054  0.0119  145  ASP   A CA  
3302 C  C   . ASP   A 145 ? 0.1455 0.1468 0.2241 -0.0165 0.0107  0.0017  145  ASP   A C   
3303 O  O   . ASP   A 145 ? 0.1627 0.1559 0.2896 -0.0153 0.0078  -0.0268 145  ASP   A O   
3304 C  CB  . ASP   A 145 ? 0.1587 0.1858 0.2361 -0.0275 -0.0035 0.0011  145  ASP   A CB  
3305 C  CG  . ASP   A 145 ? 0.1720 0.2223 0.2628 -0.0436 -0.0058 -0.0014 145  ASP   A CG  
3306 O  OD1 . ASP   A 145 ? 0.1693 0.2367 0.2919 -0.0519 0.0048  0.0058  145  ASP   A OD1 
3307 O  OD2 . ASP   A 145 ? 0.1929 0.2466 0.2751 -0.0481 -0.0285 -0.0002 145  ASP   A OD2 
3312 N  N   . THR   A 146 ? 0.1329 0.1380 0.1891 -0.0166 0.0099  0.0039  146  THR   A N   
3313 C  CA  . THR   A 146 ? 0.1274 0.1390 0.1864 -0.0042 0.0075  0.0114  146  THR   A CA  
3314 C  C   . THR   A 146 ? 0.1236 0.1351 0.1979 0.0009  0.0115  0.0192  146  THR   A C   
3315 O  O   . THR   A 146 ? 0.1397 0.1484 0.2048 0.0024  0.0037  0.0148  146  THR   A O   
3316 C  CB  . THR   A 146 ? 0.1323 0.1426 0.1825 -0.0028 0.0089  0.0290  146  THR   A CB  
3317 O  OG1 . THR   A 146 ? 0.1321 0.1542 0.1877 -0.0021 0.0028  0.0163  146  THR   A OG1 
3318 C  CG2 . THR   A 146 ? 0.1329 0.1458 0.2108 -0.0119 0.0020  0.0194  146  THR   A CG2 
3326 N  N   . VAL   A 147 ? 0.1244 0.1371 0.1892 -0.0043 0.0141  0.0250  147  VAL   A N   
3327 C  CA  . VAL   A 147 ? 0.1209 0.1435 0.1793 -0.0103 0.0166  0.0295  147  VAL   A CA  
3328 C  C   . VAL   A 147 ? 0.1312 0.1400 0.1906 -0.0095 0.0174  0.0284  147  VAL   A C   
3329 O  O   . VAL   A 147 ? 0.1348 0.1423 0.2056 -0.0136 0.0117  0.0300  147  VAL   A O   
3330 C  CB  . VAL   A 147 ? 0.1398 0.1401 0.1822 -0.0100 0.0134  0.0331  147  VAL   A CB  
3331 C  CG1 . VAL   A 147 ? 0.1697 0.1443 0.1806 -0.0066 0.0068  0.0392  147  VAL   A CG1 
3332 C  CG2 . VAL   A 147 ? 0.1420 0.1384 0.1788 -0.0129 0.0060  0.0289  147  VAL   A CG2 
3342 N  N   . ARG   A 148 ? 0.1360 0.1404 0.1856 -0.0064 0.0169  0.0445  148  ARG   A N   
3343 C  CA  . ARG   A 148 ? 0.1426 0.1348 0.1946 -0.0118 0.0167  0.0418  148  ARG   A CA  
3344 C  C   . ARG   A 148 ? 0.1503 0.1389 0.1955 -0.0158 0.0191  0.0593  148  ARG   A C   
3345 O  O   . ARG   A 148 ? 0.1769 0.1558 0.2130 -0.0184 0.0227  0.0535  148  ARG   A O   
3346 C  CB  . ARG   A 148 ? 0.1497 0.1380 0.2180 -0.0062 0.0271  0.0370  148  ARG   A CB  
3347 C  CG  . ARG   A 148 ? 0.1650 0.1403 0.2524 -0.0095 0.0448  0.0350  148  ARG   A CG  
3348 C  CD  . ARG   A 148 ? 0.1800 0.1424 0.2765 -0.0022 0.0493  0.0490  148  ARG   A CD  
3349 N  NE  . ARG   A 148 ? 0.1715 0.1440 0.2721 0.0100  0.0487  0.0595  148  ARG   A NE  
3350 C  CZ  . ARG   A 148 ? 0.1700 0.1383 0.2543 0.0106  0.0518  0.0479  148  ARG   A CZ  
3351 N  NH1 . ARG   A 148 ? 0.1737 0.1378 0.2612 0.0000  0.0472  0.0168  148  ARG   A NH1 
3352 N  NH2 . ARG   A 148 ? 0.1667 0.1609 0.2474 0.0208  0.0526  0.0520  148  ARG   A NH2 
3366 N  N   . THR   A 149 ? 0.1515 0.1457 0.1860 -0.0152 0.0067  0.0503  149  THR   A N   
3367 C  CA  . THR   A 149 ? 0.1478 0.1552 0.1827 -0.0110 0.0057  0.0448  149  THR   A CA  
3368 C  C   . THR   A 149 ? 0.1407 0.1559 0.1723 -0.0142 0.0103  0.0465  149  THR   A C   
3369 O  O   . THR   A 149 ? 0.1437 0.1614 0.1952 -0.0162 0.0149  0.0475  149  THR   A O   
3370 C  CB  . THR   A 149 ? 0.1456 0.1658 0.1921 -0.0133 0.0092  0.0379  149  THR   A CB  
3371 O  OG1 . THR   A 149 ? 0.1522 0.1586 0.2003 -0.0236 0.0102  0.0423  149  THR   A OG1 
3372 C  CG2 . THR   A 149 ? 0.1449 0.1733 0.2011 -0.0051 0.0016  0.0390  149  THR   A CG2 
3380 N  N   . ASN   A 150 ? 0.1427 0.1526 0.1854 -0.0118 -0.0030 0.0526  150  ASN   A N   
3381 C  CA  . ASN   A 150 ? 0.1559 0.1624 0.1841 -0.0107 0.0164  0.0523  150  ASN   A CA  
3382 C  C   . ASN   A 150 ? 0.1374 0.1557 0.1790 -0.0154 0.0076  0.0497  150  ASN   A C   
3383 O  O   . ASN   A 150 ? 0.1519 0.1633 0.2102 -0.0134 -0.0089 0.0443  150  ASN   A O   
3384 C  CB  . ASN   A 150 ? 0.2012 0.1871 0.2094 -0.0153 0.0253  0.0657  150  ASN   A CB  
3385 C  CG  . ASN   A 150 ? 0.2577 0.2218 0.2674 -0.0115 0.0109  0.0707  150  ASN   A CG  
3386 O  OD1 . ASN   A 150 ? 0.2793 0.2322 0.2727 -0.0185 0.0143  0.0884  150  ASN   A OD1 
3387 N  ND2 . ASN   A 150 ? 0.2883 0.2425 0.3014 -0.0047 0.0034  0.0761  150  ASN   A ND2 
3394 N  N   . VAL   A 151 ? 0.1398 0.1422 0.1817 -0.0124 0.0069  0.0466  151  VAL   A N   
3395 C  CA  . VAL   A 151 ? 0.1452 0.1422 0.1739 -0.0163 0.0134  0.0383  151  VAL   A CA  
3396 C  C   . VAL   A 151 ? 0.1365 0.1393 0.1761 -0.0166 0.0173  0.0476  151  VAL   A C   
3397 O  O   . VAL   A 151 ? 0.1415 0.1534 0.2144 -0.0166 0.0177  0.0389  151  VAL   A O   
3398 C  CB  . VAL   A 151 ? 0.1700 0.1648 0.1756 -0.0053 0.0151  0.0333  151  VAL   A CB  
3399 C  CG1 . VAL   A 151 ? 0.1651 0.1851 0.2024 -0.0090 0.0083  0.0306  151  VAL   A CG1 
3400 C  CG2 . VAL   A 151 ? 0.1799 0.1627 0.1783 -0.0030 0.0281  0.0344  151  VAL   A CG2 
3410 N  N   . TYR   A 152 ? 0.1394 0.1438 0.1703 -0.0125 0.0125  0.0428  152  TYR   A N   
3411 C  CA  . TYR   A 152 ? 0.1359 0.1515 0.1603 -0.0121 0.0125  0.0406  152  TYR   A CA  
3412 C  C   . TYR   A 152 ? 0.1302 0.1440 0.1565 -0.0140 0.0213  0.0359  152  TYR   A C   
3413 O  O   . TYR   A 152 ? 0.1448 0.1462 0.1631 -0.0247 0.0187  0.0289  152  TYR   A O   
3414 C  CB  . TYR   A 152 ? 0.1571 0.1525 0.1691 -0.0139 0.0213  0.0418  152  TYR   A CB  
3415 C  CG  . TYR   A 152 ? 0.1738 0.1766 0.1678 -0.0171 0.0300  0.0406  152  TYR   A CG  
3416 C  CD1 . TYR   A 152 ? 0.1878 0.1998 0.1926 0.0005  0.0401  0.0549  152  TYR   A CD1 
3417 C  CD2 . TYR   A 152 ? 0.1760 0.1915 0.1681 -0.0268 0.0304  0.0378  152  TYR   A CD2 
3418 C  CE1 . TYR   A 152 ? 0.2167 0.2126 0.2021 0.0099  0.0256  0.0641  152  TYR   A CE1 
3419 C  CE2 . TYR   A 152 ? 0.2045 0.2073 0.1795 -0.0284 0.0308  0.0462  152  TYR   A CE2 
3420 C  CZ  . TYR   A 152 ? 0.2348 0.2111 0.1897 -0.0123 0.0281  0.0730  152  TYR   A CZ  
3421 O  OH  . TYR   A 152 ? 0.2686 0.2349 0.2310 -0.0052 0.0296  0.0934  152  TYR   A OH  
3431 N  N   A LEU   A 153 ? 0.1290 0.1396 0.1703 -0.0175 0.0186  0.0309  153  LEU   A N   
3432 N  N   B LEU   A 153 ? 0.1354 0.1476 0.1523 -0.0166 0.0179  0.0324  153  LEU   A N   
3433 C  CA  A LEU   A 153 ? 0.1267 0.1331 0.1791 -0.0092 0.0164  0.0369  153  LEU   A CA  
3434 C  CA  B LEU   A 153 ? 0.1341 0.1483 0.1440 -0.0036 0.0194  0.0326  153  LEU   A CA  
3435 C  C   A LEU   A 153 ? 0.1283 0.1286 0.1844 -0.0065 0.0242  0.0289  153  LEU   A C   
3436 C  C   B LEU   A 153 ? 0.1348 0.1585 0.1470 0.0005  0.0258  0.0296  153  LEU   A C   
3437 O  O   A LEU   A 153 ? 0.1377 0.1343 0.2033 -0.0143 0.0402  0.0139  153  LEU   A O   
3438 O  O   B LEU   A 153 ? 0.1405 0.1690 0.1480 -0.0001 0.0355  0.0275  153  LEU   A O   
3439 C  CB  A LEU   A 153 ? 0.1254 0.1276 0.1859 -0.0102 0.0065  0.0333  153  LEU   A CB  
3440 C  CB  B LEU   A 153 ? 0.1314 0.1431 0.1438 0.0004  0.0084  0.0377  153  LEU   A CB  
3441 C  CG  A LEU   A 153 ? 0.1307 0.1354 0.1860 -0.0100 0.0131  0.0231  153  LEU   A CG  
3442 C  CG  B LEU   A 153 ? 0.1399 0.1468 0.1326 -0.0010 0.0016  0.0315  153  LEU   A CG  
3443 C  CD1 A LEU   A 153 ? 0.1349 0.1362 0.1984 -0.0130 0.0106  0.0190  153  LEU   A CD1 
3444 C  CD1 B LEU   A 153 ? 0.1409 0.1457 0.1352 0.0016  0.0048  0.0305  153  LEU   A CD1 
3445 C  CD2 A LEU   A 153 ? 0.1358 0.1469 0.1672 -0.0147 0.0208  0.0019  153  LEU   A CD2 
3446 C  CD2 B LEU   A 153 ? 0.1461 0.1568 0.1378 -0.0113 -0.0062 0.0213  153  LEU   A CD2 
3469 N  N   A ALA   A 154 ? 0.1269 0.1261 0.1992 -0.0027 0.0281  0.0373  154  ALA   A N   
3470 N  N   B ALA   A 154 ? 0.1326 0.1547 0.1525 -0.0026 0.0342  0.0353  154  ALA   A N   
3471 C  CA  A ALA   A 154 ? 0.1364 0.1360 0.2115 0.0016  0.0235  0.0352  154  ALA   A CA  
3472 C  CA  B ALA   A 154 ? 0.1413 0.1565 0.1858 -0.0031 0.0223  0.0314  154  ALA   A CA  
3473 C  C   A ALA   A 154 ? 0.1299 0.1340 0.2205 0.0059  0.0263  0.0437  154  ALA   A C   
3474 C  C   B ALA   A 154 ? 0.1396 0.1536 0.1912 -0.0093 0.0236  0.0332  154  ALA   A C   
3475 O  O   A ALA   A 154 ? 0.1400 0.1307 0.2167 0.0098  0.0256  0.0402  154  ALA   A O   
3476 O  O   B ALA   A 154 ? 0.1427 0.1545 0.1855 -0.0120 0.0228  0.0305  154  ALA   A O   
3477 C  CB  A ALA   A 154 ? 0.1515 0.1447 0.2116 0.0131  0.0240  0.0215  154  ALA   A CB  
3478 C  CB  B ALA   A 154 ? 0.1503 0.1576 0.2005 0.0024  0.0166  0.0209  154  ALA   A CB  
3489 N  N   A VAL   A 155 ? 0.1387 0.1536 0.2323 0.0143  0.0185  0.0689  155  VAL   A N   
3490 N  N   B VAL   A 155 ? 0.1458 0.1592 0.2068 -0.0069 0.0199  0.0362  155  VAL   A N   
3491 C  CA  A VAL   A 155 ? 0.1521 0.1707 0.2507 0.0131  0.0057  0.0768  155  VAL   A CA  
3492 C  CA  B VAL   A 155 ? 0.1514 0.1616 0.2158 -0.0138 0.0198  0.0453  155  VAL   A CA  
3493 C  C   A VAL   A 155 ? 0.1650 0.1750 0.2792 0.0140  -0.0102 0.0700  155  VAL   A C   
3494 C  C   B VAL   A 155 ? 0.1556 0.1648 0.2263 -0.0124 0.0239  0.0536  155  VAL   A C   
3495 O  O   A VAL   A 155 ? 0.1531 0.1671 0.3009 0.0102  -0.0008 0.0456  155  VAL   A O   
3496 O  O   B VAL   A 155 ? 0.1513 0.1704 0.2315 -0.0002 0.0249  0.0597  155  VAL   A O   
3497 C  CB  A VAL   A 155 ? 0.1611 0.1852 0.2338 0.0140  0.0036  0.0724  155  VAL   A CB  
3498 C  CB  B VAL   A 155 ? 0.1591 0.1593 0.2126 -0.0149 0.0072  0.0345  155  VAL   A CB  
3499 C  CG1 A VAL   A 155 ? 0.1747 0.1963 0.2438 0.0152  -0.0072 0.0734  155  VAL   A CG1 
3500 C  CG1 B VAL   A 155 ? 0.1685 0.1650 0.2182 -0.0138 -0.0039 0.0348  155  VAL   A CG1 
3501 C  CG2 A VAL   A 155 ? 0.1748 0.1950 0.2285 0.0193  0.0023  0.0792  155  VAL   A CG2 
3502 C  CG2 B VAL   A 155 ? 0.1704 0.1601 0.2165 -0.0122 0.0125  0.0385  155  VAL   A CG2 
3521 N  N   A PHE   A 156 ? 0.1884 0.1810 0.2776 0.0157  -0.0308 0.0809  156  PHE   A N   
3522 N  N   B PHE   A 156 ? 0.1665 0.1601 0.2289 -0.0180 0.0217  0.0494  156  PHE   A N   
3523 C  CA  A PHE   A 156 ? 0.2251 0.1944 0.2954 0.0284  -0.0295 0.0805  156  PHE   A CA  
3524 C  CA  B PHE   A 156 ? 0.1760 0.1617 0.2183 -0.0155 0.0156  0.0546  156  PHE   A CA  
3525 C  C   A PHE   A 156 ? 0.2218 0.1949 0.2880 0.0392  -0.0168 0.0861  156  PHE   A C   
3526 C  C   B PHE   A 156 ? 0.1796 0.1677 0.2241 -0.0136 0.0247  0.0598  156  PHE   A C   
3527 O  O   A PHE   A 156 ? 0.2242 0.2054 0.2932 0.0384  -0.0032 0.0856  156  PHE   A O   
3528 O  O   B PHE   A 156 ? 0.1937 0.1845 0.2424 -0.0040 0.0243  0.0613  156  PHE   A O   
3529 C  CB  A PHE   A 156 ? 0.2549 0.2048 0.3114 0.0369  -0.0476 0.0801  156  PHE   A CB  
3530 C  CB  B PHE   A 156 ? 0.1752 0.1538 0.1998 -0.0120 0.0042  0.0589  156  PHE   A CB  
3531 C  CG  A PHE   A 156 ? 0.2876 0.2144 0.3412 0.0505  -0.0555 0.0648  156  PHE   A CG  
3532 C  CG  B PHE   A 156 ? 0.1833 0.1564 0.1985 -0.0045 0.0053  0.0583  156  PHE   A CG  
3533 C  CD1 A PHE   A 156 ? 0.3036 0.2228 0.3628 0.0551  -0.0531 0.0501  156  PHE   A CD1 
3534 C  CD1 B PHE   A 156 ? 0.1884 0.1657 0.2185 0.0052  0.0098  0.0525  156  PHE   A CD1 
3535 C  CD2 A PHE   A 156 ? 0.3042 0.2251 0.3553 0.0586  -0.0592 0.0562  156  PHE   A CD2 
3536 C  CD2 B PHE   A 156 ? 0.1909 0.1536 0.1996 -0.0019 0.0047  0.0604  156  PHE   A CD2 
3537 C  CE1 A PHE   A 156 ? 0.3160 0.2313 0.3783 0.0577  -0.0521 0.0365  156  PHE   A CE1 
3538 C  CE1 B PHE   A 156 ? 0.1918 0.1675 0.2292 0.0077  0.0132  0.0428  156  PHE   A CE1 
3539 C  CE2 A PHE   A 156 ? 0.3157 0.2333 0.3686 0.0624  -0.0592 0.0405  156  PHE   A CE2 
3540 C  CE2 B PHE   A 156 ? 0.1966 0.1569 0.2137 0.0002  0.0037  0.0545  156  PHE   A CE2 
3541 C  CZ  A PHE   A 156 ? 0.3196 0.2356 0.3789 0.0625  -0.0542 0.0305  156  PHE   A CZ  
3542 C  CZ  B PHE   A 156 ? 0.1930 0.1617 0.2336 -0.0001 0.0132  0.0427  156  PHE   A CZ  
3561 N  N   A ASP   A 157 ? 0.2126 0.1942 0.2763 0.0421  -0.0168 0.0901  157  ASP   A N   
3562 N  N   B ASP   A 157 ? 0.1795 0.1675 0.2369 -0.0193 0.0099  0.0493  157  ASP   A N   
3563 C  CA  A ASP   A 157 ? 0.2115 0.2080 0.2810 0.0387  -0.0179 0.0917  157  ASP   A CA  
3564 C  CA  B ASP   A 157 ? 0.1742 0.1683 0.2414 -0.0228 -0.0080 0.0273  157  ASP   A CA  
3565 C  C   A ASP   A 157 ? 0.2009 0.2164 0.2805 0.0466  0.0012  0.0971  157  ASP   A C   
3566 C  C   B ASP   A 157 ? 0.1595 0.1657 0.2315 -0.0183 -0.0027 0.0175  157  ASP   A C   
3567 O  O   A ASP   A 157 ? 0.1979 0.2103 0.2691 0.0401  0.0036  0.0966  157  ASP   A O   
3568 O  O   B ASP   A 157 ? 0.1534 0.1612 0.2209 -0.0196 0.0079  0.0156  157  ASP   A O   
3569 C  CB  A ASP   A 157 ? 0.2221 0.2147 0.3018 0.0277  -0.0353 0.0901  157  ASP   A CB  
3570 C  CB  B ASP   A 157 ? 0.1854 0.1729 0.2536 -0.0242 -0.0114 0.0235  157  ASP   A CB  
3571 C  CG  A ASP   A 157 ? 0.2423 0.2259 0.3399 0.0238  -0.0527 0.0894  157  ASP   A CG  
3572 C  CG  B ASP   A 157 ? 0.2035 0.1758 0.2715 -0.0217 -0.0306 0.0170  157  ASP   A CG  
3573 O  OD1 A ASP   A 157 ? 0.2633 0.2303 0.3813 0.0070  -0.0642 0.0832  157  ASP   A OD1 
3574 O  OD1 B ASP   A 157 ? 0.2180 0.1834 0.2986 -0.0185 -0.0532 0.0103  157  ASP   A OD1 
3575 O  OD2 A ASP   A 157 ? 0.2380 0.2274 0.3479 0.0230  -0.0556 0.0828  157  ASP   A OD2 
3576 O  OD2 B ASP   A 157 ? 0.2080 0.1834 0.2705 -0.0146 -0.0257 0.0099  157  ASP   A OD2 
3585 N  N   A LYS   A 158 ? 0.2054 0.2354 0.3101 0.0545  0.0184  0.0944  158  LYS   A N   
3586 N  N   B LYS   A 158 ? 0.1578 0.1695 0.2409 -0.0139 0.0016  0.0080  158  LYS   A N   
3587 C  CA  A LYS   A 158 ? 0.2105 0.2579 0.3424 0.0588  0.0348  0.1003  158  LYS   A CA  
3588 C  CA  B LYS   A 158 ? 0.1619 0.1846 0.2610 -0.0098 0.0077  0.0134  158  LYS   A CA  
3589 C  C   A LYS   A 158 ? 0.1963 0.2633 0.3359 0.0566  0.0225  0.1044  158  LYS   A C   
3590 C  C   B LYS   A 158 ? 0.1458 0.1721 0.2541 -0.0131 -0.0035 0.0130  158  LYS   A C   
3591 O  O   A LYS   A 158 ? 0.1988 0.2651 0.3320 0.0488  0.0371  0.1019  158  LYS   A O   
3592 O  O   B LYS   A 158 ? 0.1343 0.1700 0.2581 -0.0164 -0.0025 0.0229  158  LYS   A O   
3593 C  CB  A LYS   A 158 ? 0.2274 0.2729 0.3743 0.0627  0.0659  0.1123  158  LYS   A CB  
3594 C  CB  B LYS   A 158 ? 0.1789 0.2180 0.2978 -0.0029 0.0274  0.0252  158  LYS   A CB  
3595 C  CG  A LYS   A 158 ? 0.2482 0.2893 0.4152 0.0622  0.0899  0.1223  158  LYS   A CG  
3596 C  CG  B LYS   A 158 ? 0.2053 0.2463 0.3402 0.0056  0.0393  0.0401  158  LYS   A CG  
3597 C  CD  A LYS   A 158 ? 0.2636 0.2994 0.4479 0.0621  0.1157  0.1382  158  LYS   A CD  
3598 C  CD  B LYS   A 158 ? 0.2268 0.2645 0.3792 0.0130  0.0490  0.0540  158  LYS   A CD  
3599 C  CE  A LYS   A 158 ? 0.2692 0.3029 0.4710 0.0580  0.1393  0.1586  158  LYS   A CE  
3600 C  CE  B LYS   A 158 ? 0.2375 0.2717 0.4046 0.0211  0.0583  0.0736  158  LYS   A CE  
3601 N  NZ  A LYS   A 158 ? 0.2657 0.3037 0.4855 0.0556  0.1563  0.1661  158  LYS   A NZ  
3602 N  NZ  B LYS   A 158 ? 0.2418 0.2745 0.4208 0.0236  0.0657  0.0854  158  LYS   A NZ  
3629 N  N   A ASN   A 159 ? 0.1863 0.2703 0.3532 0.0563  -0.0058 0.1019  159  ASN   A N   
3630 N  N   B ASN   A 159 ? 0.1567 0.1740 0.2599 -0.0115 -0.0164 0.0040  159  ASN   A N   
3631 C  CA  A ASN   A 159 ? 0.1862 0.2797 0.3609 0.0494  -0.0262 0.1020  159  ASN   A CA  
3632 C  CA  B ASN   A 159 ? 0.1638 0.1754 0.2778 -0.0080 -0.0316 0.0149  159  ASN   A CA  
3633 C  C   A ASN   A 159 ? 0.1751 0.2730 0.3391 0.0365  -0.0117 0.0926  159  ASN   A C   
3634 C  C   B ASN   A 159 ? 0.1502 0.1644 0.2592 -0.0136 -0.0293 0.0179  159  ASN   A C   
3635 O  O   A ASN   A 159 ? 0.1724 0.2778 0.3310 0.0339  -0.0154 0.0783  159  ASN   A O   
3636 O  O   B ASN   A 159 ? 0.1455 0.1688 0.2601 -0.0182 -0.0346 0.0134  159  ASN   A O   
3637 C  CB  A ASN   A 159 ? 0.2012 0.2984 0.4078 0.0457  -0.0375 0.1003  159  ASN   A CB  
3638 C  CB  B ASN   A 159 ? 0.1917 0.1983 0.3260 -0.0022 -0.0422 0.0196  159  ASN   A CB  
3639 C  CG  A ASN   A 159 ? 0.2202 0.3149 0.4560 0.0388  -0.0326 0.0920  159  ASN   A CG  
3640 C  CG  B ASN   A 159 ? 0.2249 0.2278 0.3804 0.0011  -0.0432 0.0229  159  ASN   A CG  
3641 O  OD1 A ASN   A 159 ? 0.2143 0.3251 0.4597 0.0323  -0.0324 0.0919  159  ASN   A OD1 
3642 O  OD1 B ASN   A 159 ? 0.2441 0.2434 0.4087 -0.0009 -0.0403 0.0178  159  ASN   A OD1 
3643 N  ND2 A ASN   A 159 ? 0.2293 0.3204 0.4794 0.0410  -0.0322 0.0871  159  ASN   A ND2 
3644 N  ND2 B ASN   A 159 ? 0.2323 0.2311 0.3988 0.0014  -0.0471 0.0274  159  ASN   A ND2 
3657 N  N   A LEU   A 160 ? 0.1622 0.2571 0.3247 0.0306  -0.0145 0.1032  160  LEU   A N   
3658 N  N   B LEU   A 160 ? 0.1471 0.1565 0.2537 -0.0146 -0.0320 0.0305  160  LEU   A N   
3659 C  CA  A LEU   A 160 ? 0.1591 0.2521 0.3153 0.0171  0.0010  0.1065  160  LEU   A CA  
3660 C  CA  B LEU   A 160 ? 0.1524 0.1488 0.2468 -0.0146 -0.0192 0.0385  160  LEU   A CA  
3661 C  C   A LEU   A 160 ? 0.1417 0.2501 0.3123 0.0126  0.0093  0.1104  160  LEU   A C   
3662 C  C   B LEU   A 160 ? 0.1500 0.1526 0.2424 -0.0084 -0.0101 0.0429  160  LEU   A C   
3663 O  O   A LEU   A 160 ? 0.1437 0.2535 0.3319 0.0109  0.0157  0.1109  160  LEU   A O   
3664 O  O   B LEU   A 160 ? 0.1514 0.1424 0.2499 -0.0168 -0.0033 0.0426  160  LEU   A O   
3665 C  CB  A LEU   A 160 ? 0.1723 0.2503 0.3006 0.0008  0.0072  0.1036  160  LEU   A CB  
3666 C  CB  B LEU   A 160 ? 0.1662 0.1482 0.2447 -0.0165 -0.0131 0.0495  160  LEU   A CB  
3667 C  CG  A LEU   A 160 ? 0.1811 0.2525 0.3016 -0.0120 0.0113  0.0910  160  LEU   A CG  
3668 C  CG  B LEU   A 160 ? 0.1740 0.1597 0.2525 -0.0218 -0.0033 0.0519  160  LEU   A CG  
3669 C  CD1 A LEU   A 160 ? 0.1851 0.2527 0.3050 -0.0099 0.0096  0.0827  160  LEU   A CD1 
3670 C  CD1 B LEU   A 160 ? 0.1767 0.1652 0.2639 -0.0202 0.0031  0.0567  160  LEU   A CD1 
3671 C  CD2 A LEU   A 160 ? 0.1846 0.2547 0.2999 -0.0155 0.0196  0.0736  160  LEU   A CD2 
3672 C  CD2 B LEU   A 160 ? 0.1811 0.1639 0.2543 -0.0244 0.0014  0.0463  160  LEU   A CD2 
3695 N  N   A TYR   A 161 ? 0.1379 0.2462 0.3111 0.0119  0.0118  0.1111  161  TYR   A N   
3696 N  N   B TYR   A 161 ? 0.1531 0.1738 0.2478 0.0011  -0.0009 0.0522  161  TYR   A N   
3697 C  CA  A TYR   A 161 ? 0.1407 0.2401 0.3001 0.0085  0.0085  0.1074  161  TYR   A CA  
3698 C  CA  B TYR   A 161 ? 0.1579 0.1867 0.2473 0.0001  0.0078  0.0691  161  TYR   A CA  
3699 C  C   A TYR   A 161 ? 0.1302 0.2572 0.2974 0.0105  0.0110  0.1066  161  TYR   A C   
3700 C  C   B TYR   A 161 ? 0.1578 0.2023 0.2546 -0.0039 0.0178  0.0675  161  TYR   A C   
3701 O  O   A TYR   A 161 ? 0.1228 0.2635 0.2866 0.0014  0.0120  0.1155  161  TYR   A O   
3702 O  O   B TYR   A 161 ? 0.1568 0.2093 0.2529 -0.0042 0.0299  0.0668  161  TYR   A O   
3703 C  CB  A TYR   A 161 ? 0.1479 0.2230 0.3093 0.0095  0.0061  0.0881  161  TYR   A CB  
3704 C  CB  B TYR   A 161 ? 0.1588 0.1838 0.2515 0.0068  0.0160  0.0749  161  TYR   A CB  
3705 C  CG  A TYR   A 161 ? 0.1520 0.2047 0.3021 0.0055  0.0014  0.0708  161  TYR   A CG  
3706 C  CG  B TYR   A 161 ? 0.1573 0.1816 0.2565 0.0121  0.0230  0.0704  161  TYR   A CG  
3707 C  CD1 A TYR   A 161 ? 0.1490 0.1960 0.3023 0.0025  0.0009  0.0614  161  TYR   A CD1 
3708 C  CD1 B TYR   A 161 ? 0.1541 0.1812 0.2639 0.0115  0.0232  0.0600  161  TYR   A CD1 
3709 C  CD2 A TYR   A 161 ? 0.1591 0.2062 0.2962 -0.0009 -0.0080 0.0639  161  TYR   A CD2 
3710 C  CD2 B TYR   A 161 ? 0.1613 0.1887 0.2614 0.0171  0.0227  0.0683  161  TYR   A CD2 
3711 C  CE1 A TYR   A 161 ? 0.1632 0.1811 0.2921 -0.0067 -0.0015 0.0606  161  TYR   A CE1 
3712 C  CE1 B TYR   A 161 ? 0.1651 0.1858 0.2746 0.0120  0.0133  0.0593  161  TYR   A CE1 
3713 C  CE2 A TYR   A 161 ? 0.1699 0.1942 0.2916 -0.0048 -0.0079 0.0656  161  TYR   A CE2 
3714 C  CE2 B TYR   A 161 ? 0.1678 0.1885 0.2709 0.0148  0.0206  0.0717  161  TYR   A CE2 
3715 C  CZ  A TYR   A 161 ? 0.1776 0.1790 0.2902 -0.0118 -0.0101 0.0703  161  TYR   A CZ  
3716 C  CZ  B TYR   A 161 ? 0.1787 0.1866 0.2849 0.0089  0.0167  0.0667  161  TYR   A CZ  
3717 O  OH  A TYR   A 161 ? 0.1924 0.1635 0.2941 -0.0157 -0.0237 0.0813  161  TYR   A OH  
3718 O  OH  B TYR   A 161 ? 0.1951 0.1871 0.3081 0.0044  0.0100  0.0590  161  TYR   A OH  
3737 N  N   A ASP   A 162 ? 0.1276 0.2718 0.3188 0.0166  0.0161  0.0970  162  ASP   A N   
3738 N  N   B ASP   A 162 ? 0.1592 0.2123 0.2788 -0.0098 0.0164  0.0641  162  ASP   A N   
3739 C  CA  A ASP   A 162 ? 0.1220 0.2918 0.3210 0.0123  0.0156  0.0997  162  ASP   A CA  
3740 C  CA  B ASP   A 162 ? 0.1594 0.2302 0.2899 -0.0215 0.0132  0.0648  162  ASP   A CA  
3741 C  C   A ASP   A 162 ? 0.1207 0.3092 0.3136 0.0036  0.0188  0.1061  162  ASP   A C   
3742 C  C   B ASP   A 162 ? 0.1593 0.2367 0.2839 -0.0326 0.0073  0.0523  162  ASP   A C   
3743 O  O   A ASP   A 162 ? 0.1226 0.3149 0.3266 -0.0069 0.0267  0.1004  162  ASP   A O   
3744 O  O   B ASP   A 162 ? 0.1601 0.2397 0.2901 -0.0453 0.0096  0.0444  162  ASP   A O   
3745 C  CB  A ASP   A 162 ? 0.1309 0.2990 0.3304 0.0114  0.0261  0.0953  162  ASP   A CB  
3746 C  CB  B ASP   A 162 ? 0.1650 0.2474 0.3096 -0.0187 0.0168  0.0720  162  ASP   A CB  
3747 C  CG  A ASP   A 162 ? 0.1468 0.3039 0.3370 0.0129  0.0353  0.0875  162  ASP   A CG  
3748 C  CG  B ASP   A 162 ? 0.1770 0.2618 0.3248 -0.0112 0.0189  0.0774  162  ASP   A CG  
3749 O  OD1 A ASP   A 162 ? 0.1654 0.3112 0.3539 0.0147  0.0335  0.0764  162  ASP   A OD1 
3750 O  OD1 B ASP   A 162 ? 0.1824 0.2684 0.3354 -0.0084 0.0149  0.0766  162  ASP   A OD1 
3751 O  OD2 A ASP   A 162 ? 0.1510 0.3031 0.3292 0.0087  0.0574  0.0871  162  ASP   A OD2 
3752 O  OD2 B ASP   A 162 ? 0.1855 0.2654 0.3270 -0.0081 0.0326  0.0812  162  ASP   A OD2 
3761 N  N   A LYS   A 163 ? 0.1372 0.3201 0.3121 0.0090  -0.0065 0.1108  163  LYS   A N   
3762 N  N   B LYS   A 163 ? 0.1658 0.2386 0.2820 -0.0309 -0.0091 0.0502  163  LYS   A N   
3763 C  CA  A LYS   A 163 ? 0.1557 0.3253 0.3089 -0.0001 -0.0103 0.1093  163  LYS   A CA  
3764 C  CA  B LYS   A 163 ? 0.1736 0.2405 0.2824 -0.0362 -0.0144 0.0437  163  LYS   A CA  
3765 C  C   A LYS   A 163 ? 0.1508 0.3108 0.2978 -0.0067 0.0082  0.1061  163  LYS   A C   
3766 C  C   B LYS   A 163 ? 0.1651 0.2124 0.2636 -0.0411 -0.0075 0.0380  163  LYS   A C   
3767 O  O   A LYS   A 163 ? 0.1517 0.3216 0.3102 -0.0157 0.0129  0.1055  163  LYS   A O   
3768 O  O   B LYS   A 163 ? 0.1705 0.2027 0.2693 -0.0467 -0.0031 0.0434  163  LYS   A O   
3769 C  CB  A LYS   A 163 ? 0.1881 0.3469 0.3341 0.0018  -0.0228 0.1006  163  LYS   A CB  
3770 C  CB  B LYS   A 163 ? 0.1968 0.2681 0.3098 -0.0377 -0.0181 0.0389  163  LYS   A CB  
3771 C  CG  A LYS   A 163 ? 0.2222 0.3669 0.3717 -0.0037 -0.0130 0.0922  163  LYS   A CG  
3772 C  CG  B LYS   A 163 ? 0.2201 0.2919 0.3438 -0.0395 -0.0123 0.0360  163  LYS   A CG  
3773 C  CD  A LYS   A 163 ? 0.2475 0.3829 0.4157 -0.0096 -0.0088 0.0837  163  LYS   A CD  
3774 C  CD  B LYS   A 163 ? 0.2386 0.3118 0.3790 -0.0420 -0.0119 0.0317  163  LYS   A CD  
3775 C  CE  A LYS   A 163 ? 0.2711 0.3938 0.4546 -0.0122 -0.0015 0.0812  163  LYS   A CE  
3776 C  CE  B LYS   A 163 ? 0.2533 0.3249 0.4096 -0.0423 -0.0103 0.0247  163  LYS   A CE  
3777 N  NZ  A LYS   A 163 ? 0.2841 0.3999 0.4764 -0.0129 0.0019  0.0817  163  LYS   A NZ  
3778 N  NZ  B LYS   A 163 ? 0.2626 0.3326 0.4293 -0.0432 -0.0088 0.0197  163  LYS   A NZ  
3805 N  N   A LEU   A 164 ? 0.1445 0.2830 0.2812 -0.0152 0.0096  0.1014  164  LEU   A N   
3806 N  N   B LEU   A 164 ? 0.1579 0.2043 0.2536 -0.0341 -0.0072 0.0293  164  LEU   A N   
3807 C  CA  A LEU   A 164 ? 0.1441 0.2624 0.2729 -0.0198 0.0225  0.0897  164  LEU   A CA  
3808 C  CA  B LEU   A 164 ? 0.1556 0.1950 0.2425 -0.0217 0.0094  0.0352  164  LEU   A CA  
3809 C  C   A LEU   A 164 ? 0.1465 0.2628 0.2784 -0.0200 0.0225  0.0855  164  LEU   A C   
3810 C  C   B LEU   A 164 ? 0.1562 0.1874 0.2321 -0.0144 0.0100  0.0288  164  LEU   A C   
3811 O  O   A LEU   A 164 ? 0.1574 0.2695 0.2821 -0.0235 0.0490  0.0757  164  LEU   A O   
3812 O  O   B LEU   A 164 ? 0.1635 0.1828 0.2196 -0.0074 0.0130  0.0244  164  LEU   A O   
3813 C  CB  A LEU   A 164 ? 0.1447 0.2524 0.2685 -0.0200 0.0268  0.0774  164  LEU   A CB  
3814 C  CB  B LEU   A 164 ? 0.1537 0.1941 0.2406 -0.0243 0.0227  0.0377  164  LEU   A CB  
3815 C  CG  A LEU   A 164 ? 0.1611 0.2487 0.2726 -0.0191 0.0220  0.0674  164  LEU   A CG  
3816 C  CG  B LEU   A 164 ? 0.1553 0.1944 0.2372 -0.0271 0.0318  0.0374  164  LEU   A CG  
3817 C  CD1 A LEU   A 164 ? 0.1572 0.2445 0.2694 -0.0059 0.0076  0.0622  164  LEU   A CD1 
3818 C  CD1 B LEU   A 164 ? 0.1536 0.1946 0.2395 -0.0259 0.0238  0.0353  164  LEU   A CD1 
3819 C  CD2 A LEU   A 164 ? 0.1740 0.2510 0.2769 -0.0222 0.0172  0.0578  164  LEU   A CD2 
3820 C  CD2 B LEU   A 164 ? 0.1642 0.1971 0.2322 -0.0229 0.0401  0.0417  164  LEU   A CD2 
3843 N  N   A VAL   A 165 ? 0.1435 0.2640 0.2739 -0.0197 0.0266  0.0842  165  VAL   A N   
3844 N  N   B VAL   A 165 ? 0.1529 0.1950 0.2437 -0.0099 0.0127  0.0267  165  VAL   A N   
3845 C  CA  A VAL   A 165 ? 0.1526 0.2641 0.2551 -0.0205 0.0320  0.0821  165  VAL   A CA  
3846 C  CA  B VAL   A 165 ? 0.1509 0.1975 0.2328 -0.0122 0.0212  0.0298  165  VAL   A CA  
3847 C  C   A VAL   A 165 ? 0.1474 0.2716 0.2454 -0.0136 0.0332  0.0892  165  VAL   A C   
3848 C  C   B VAL   A 165 ? 0.1422 0.1929 0.2276 -0.0189 0.0136  0.0275  165  VAL   A C   
3849 O  O   A VAL   A 165 ? 0.1540 0.2746 0.2305 -0.0143 0.0419  0.1027  165  VAL   A O   
3850 O  O   B VAL   A 165 ? 0.1451 0.1904 0.2179 -0.0239 0.0126  0.0403  165  VAL   A O   
3851 C  CB  A VAL   A 165 ? 0.1711 0.2623 0.2592 -0.0220 0.0299  0.0659  165  VAL   A CB  
3852 C  CB  B VAL   A 165 ? 0.1635 0.2066 0.2295 -0.0071 0.0257  0.0299  165  VAL   A CB  
3853 C  CG1 A VAL   A 165 ? 0.1751 0.2687 0.2638 -0.0237 0.0351  0.0588  165  VAL   A CG1 
3854 C  CG1 B VAL   A 165 ? 0.1666 0.2157 0.2335 -0.0088 0.0319  0.0292  165  VAL   A CG1 
3855 C  CG2 A VAL   A 165 ? 0.1828 0.2568 0.2632 -0.0238 0.0225  0.0686  165  VAL   A CG2 
3856 C  CG2 B VAL   A 165 ? 0.1702 0.2063 0.2306 -0.0035 0.0213  0.0412  165  VAL   A CG2 
3875 N  N   A SER   A 166 ? 0.1430 0.2778 0.2692 -0.0034 0.0308  0.0804  166  SER   A N   
3876 N  N   B SER   A 166 ? 0.1386 0.1963 0.2391 -0.0222 0.0083  0.0197  166  SER   A N   
3877 C  CA  A SER   A 166 ? 0.1541 0.2955 0.2960 -0.0047 0.0141  0.0655  166  SER   A CA  
3878 C  CA  B SER   A 166 ? 0.1386 0.2032 0.2414 -0.0218 0.0032  0.0226  166  SER   A CA  
3879 C  C   A SER   A 166 ? 0.1563 0.3071 0.2907 -0.0086 0.0022  0.0594  166  SER   A C   
3880 C  C   B SER   A 166 ? 0.1366 0.2044 0.2408 -0.0253 0.0047  0.0276  166  SER   A C   
3881 O  O   A SER   A 166 ? 0.1626 0.3094 0.3090 -0.0125 0.0007  0.0504  166  SER   A O   
3882 O  O   B SER   A 166 ? 0.1399 0.1964 0.2508 -0.0287 0.0006  0.0383  166  SER   A O   
3883 C  CB  A SER   A 166 ? 0.1769 0.3054 0.3332 0.0073  0.0037  0.0503  166  SER   A CB  
3884 C  CB  B SER   A 166 ? 0.1542 0.2128 0.2454 -0.0165 0.0038  0.0332  166  SER   A CB  
3885 O  OG  A SER   A 166 ? 0.2078 0.3158 0.3671 0.0042  -0.0010 0.0490  166  SER   A OG  
3886 O  OG  B SER   A 166 ? 0.1711 0.2263 0.2644 -0.0113 -0.0084 0.0237  166  SER   A OG  
3897 N  N   A SER   A 167 ? 0.1652 0.3140 0.2712 -0.0027 -0.0003 0.0565  167  SER   A N   
3898 N  N   B SER   A 167 ? 0.1451 0.2134 0.2437 -0.0241 0.0240  0.0234  167  SER   A N   
3899 C  CA  A SER   A 167 ? 0.1873 0.3173 0.2619 -0.0051 -0.0091 0.0441  167  SER   A CA  
3900 C  CA  B SER   A 167 ? 0.1648 0.2271 0.2315 -0.0212 0.0272  0.0162  167  SER   A CA  
3901 C  C   A SER   A 167 ? 0.1920 0.3222 0.2614 -0.0054 -0.0037 0.0400  167  SER   A C   
3902 C  C   B SER   A 167 ? 0.1677 0.2392 0.2280 -0.0167 0.0304  0.0121  167  SER   A C   
3903 O  O   A SER   A 167 ? 0.2066 0.3195 0.2725 -0.0016 -0.0175 0.0401  167  SER   A O   
3904 O  O   B SER   A 167 ? 0.1797 0.2374 0.2221 -0.0188 0.0346  0.0141  167  SER   A O   
3905 C  CB  A SER   A 167 ? 0.1974 0.3173 0.2624 0.0005  -0.0036 0.0407  167  SER   A CB  
3906 C  CB  B SER   A 167 ? 0.1747 0.2317 0.2358 -0.0174 0.0413  0.0099  167  SER   A CB  
3907 O  OG  A SER   A 167 ? 0.1990 0.3177 0.2645 0.0040  0.0120  0.0443  167  SER   A OG  
3908 O  OG  B SER   A 167 ? 0.1761 0.2316 0.2356 -0.0108 0.0588  0.0007  167  SER   A OG  
3919 N  N   A PHE   A 168 ? 0.1887 0.3311 0.2543 -0.0025 0.0035  0.0340  168  PHE   A N   
3920 N  N   B PHE   A 168 ? 0.1704 0.2562 0.2377 -0.0111 0.0231  0.0074  168  PHE   A N   
3921 C  CA  A PHE   A 168 ? 0.1896 0.3374 0.2640 -0.0085 0.0164  0.0184  168  PHE   A CA  
3922 C  CA  B PHE   A 168 ? 0.1889 0.2800 0.2537 -0.0103 0.0269  0.0082  168  PHE   A CA  
3923 C  C   A PHE   A 168 ? 0.2134 0.3707 0.3168 -0.0240 0.0429  0.0105  168  PHE   A C   
3924 C  C   B PHE   A 168 ? 0.2411 0.3122 0.3319 -0.0189 0.0142  -0.0018 168  PHE   A C   
3925 O  O   A PHE   A 168 ? 0.2065 0.3811 0.3461 -0.0366 0.0482  0.0124  168  PHE   A O   
3926 O  O   B PHE   A 168 ? 0.2492 0.3140 0.3432 -0.0312 0.0245  -0.0015 168  PHE   A O   
3927 C  CB  A PHE   A 168 ? 0.1796 0.3124 0.2388 -0.0092 -0.0001 0.0157  168  PHE   A CB  
3928 C  CB  B PHE   A 168 ? 0.1775 0.2788 0.2296 -0.0113 0.0277  0.0233  168  PHE   A CB  
3929 C  CG  A PHE   A 168 ? 0.1747 0.2903 0.2175 -0.0092 -0.0008 0.0091  168  PHE   A CG  
3930 C  CG  B PHE   A 168 ? 0.1720 0.2771 0.2128 -0.0127 0.0232  0.0396  168  PHE   A CG  
3931 C  CD1 A PHE   A 168 ? 0.1698 0.2822 0.2143 -0.0112 -0.0155 0.0127  168  PHE   A CD1 
3932 C  CD1 B PHE   A 168 ? 0.1694 0.2782 0.2023 -0.0137 0.0220  0.0542  168  PHE   A CD1 
3933 C  CD2 A PHE   A 168 ? 0.1720 0.2792 0.2060 -0.0106 0.0158  -0.0031 168  PHE   A CD2 
3934 C  CD2 B PHE   A 168 ? 0.1686 0.2737 0.2096 -0.0174 0.0159  0.0436  168  PHE   A CD2 
3935 C  CE1 A PHE   A 168 ? 0.1598 0.2775 0.2051 -0.0158 -0.0165 0.0065  168  PHE   A CE1 
3936 C  CE1 B PHE   A 168 ? 0.1673 0.2778 0.2019 -0.0187 0.0152  0.0627  168  PHE   A CE1 
3937 C  CE2 A PHE   A 168 ? 0.1757 0.2733 0.2052 -0.0145 0.0113  -0.0011 168  PHE   A CE2 
3938 C  CE2 B PHE   A 168 ? 0.1666 0.2728 0.2055 -0.0228 0.0089  0.0555  168  PHE   A CE2 
3939 C  CZ  A PHE   A 168 ? 0.1689 0.2750 0.2021 -0.0140 -0.0032 0.0038  168  PHE   A CZ  
3940 C  CZ  B PHE   A 168 ? 0.1670 0.2731 0.1987 -0.0255 0.0135  0.0640  168  PHE   A CZ  
3959 N  N   A LEU   A 169 ? 0.2666 0.3941 0.3736 -0.0279 0.0356  -0.0039 169  LEU   A N   
3960 N  N   B LEU   A 169 ? 0.2872 0.3430 0.3984 -0.0227 -0.0090 -0.0040 169  LEU   A N   
3961 C  CA  A LEU   A 169 ? 0.3320 0.4222 0.4486 -0.0210 0.0113  -0.0064 169  LEU   A CA  
3962 C  CA  B LEU   A 169 ? 0.3310 0.3714 0.4470 -0.0292 -0.0156 0.0040  169  LEU   A CA  
3963 C  C   A LEU   A 169 ? 0.3552 0.4301 0.5086 -0.0193 0.0023  0.0044  169  LEU   A C   
3964 C  C   B LEU   A 169 ? 0.3506 0.3809 0.4839 -0.0298 -0.0162 0.0123  169  LEU   A C   
3965 O  O   A LEU   A 169 ? 0.3639 0.4333 0.5281 -0.0161 -0.0014 0.0077  169  LEU   A O   
3966 O  O   B LEU   A 169 ? 0.3586 0.3858 0.4997 -0.0270 -0.0185 0.0171  169  LEU   A O   
3967 C  CB  A LEU   A 169 ? 0.3652 0.4386 0.4518 -0.0199 0.0006  -0.0196 169  LEU   A CB  
3968 C  CB  B LEU   A 169 ? 0.3502 0.3878 0.4479 -0.0353 -0.0164 0.0064  169  LEU   A CB  
3969 C  CG  A LEU   A 169 ? 0.3915 0.4516 0.4555 -0.0198 -0.0052 -0.0351 169  LEU   A CG  
3970 C  CG  B LEU   A 169 ? 0.3639 0.3993 0.4421 -0.0399 -0.0176 0.0096  169  LEU   A CG  
3971 C  CD1 A LEU   A 169 ? 0.4007 0.4562 0.4633 -0.0184 -0.0070 -0.0391 169  LEU   A CD1 
3972 C  CD1 B LEU   A 169 ? 0.3689 0.4038 0.4420 -0.0414 -0.0184 0.0112  169  LEU   A CD1 
3973 C  CD2 A LEU   A 169 ? 0.3995 0.4556 0.4497 -0.0205 -0.0049 -0.0412 169  LEU   A CD2 
3974 C  CD2 B LEU   A 169 ? 0.3687 0.4021 0.4400 -0.0426 -0.0161 0.0121  169  LEU   A CD2 
3975 O  OXT A LEU   A 169 ? 0.3563 0.4315 0.5268 -0.0211 0.0068  0.0050  169  LEU   A OXT 
3976 O  OXT B LEU   A 169 ? 0.3524 0.3811 0.4853 -0.0324 -0.0106 0.0135  169  LEU   A OXT 
3999 N  N   A SER   B 1   ? 0.3974 0.3720 0.3753 -0.1008 -0.0804 0.0443  1    SER   B N   
4000 N  N   B SER   B 1   ? 0.3251 0.2878 0.3177 -0.1090 -0.0497 0.0101  1    SER   B N   
4001 C  CA  A SER   B 1   ? 0.3881 0.3738 0.3756 -0.1040 -0.0875 0.0443  1    SER   B CA  
4002 C  CA  B SER   B 1   ? 0.3152 0.2929 0.3141 -0.1128 -0.0589 0.0082  1    SER   B CA  
4003 C  C   A SER   B 1   ? 0.3609 0.3702 0.3524 -0.1035 -0.0929 0.0604  1    SER   B C   
4004 C  C   B SER   B 1   ? 0.2908 0.2991 0.3000 -0.1156 -0.0654 0.0357  1    SER   B C   
4005 O  O   A SER   B 1   ? 0.3673 0.3709 0.3262 -0.1006 -0.0880 0.0584  1    SER   B O   
4006 O  O   B SER   B 1   ? 0.2967 0.3022 0.2851 -0.1096 -0.0604 0.0341  1    SER   B O   
4007 C  CB  A SER   B 1   ? 0.4012 0.3750 0.3948 -0.1059 -0.0808 0.0329  1    SER   B CB  
4008 C  CB  B SER   B 1   ? 0.3260 0.2861 0.3216 -0.1120 -0.0500 -0.0158 1    SER   B CB  
4009 O  OG  A SER   B 1   ? 0.4145 0.3825 0.4338 -0.1048 -0.0700 0.0303  1    SER   B OG  
4010 O  OG  B SER   B 1   ? 0.3390 0.2873 0.3465 -0.1076 -0.0398 -0.0290 1    SER   B OG  
4025 N  N   A MET   B 2   ? 0.3291 0.3630 0.3495 -0.1026 -0.0929 0.0923  2    MET   B N   
4026 N  N   B MET   B 2   ? 0.2669 0.2999 0.2924 -0.1171 -0.0630 0.0824  2    MET   B N   
4027 C  CA  A MET   B 2   ? 0.3034 0.3605 0.3627 -0.0847 -0.0914 0.1089  2    MET   B CA  
4028 C  CA  B MET   B 2   ? 0.2526 0.3065 0.2916 -0.0960 -0.0630 0.1074  2    MET   B CA  
4029 C  C   A MET   B 2   ? 0.2595 0.3360 0.3233 -0.0740 -0.1057 0.1289  2    MET   B C   
4030 C  C   B MET   B 2   ? 0.2288 0.2939 0.2638 -0.0810 -0.0552 0.1190  2    MET   B C   
4031 O  O   A MET   B 2   ? 0.2511 0.3482 0.3183 -0.0595 -0.1287 0.1304  2    MET   B O   
4032 O  O   B MET   B 2   ? 0.2248 0.3017 0.2654 -0.0695 -0.0538 0.1076  2    MET   B O   
4033 C  CB  A MET   B 2   ? 0.3307 0.3881 0.4468 -0.0647 -0.0658 0.0902  2    MET   B CB  
4034 C  CB  B MET   B 2   ? 0.2728 0.3313 0.3402 -0.0770 -0.0634 0.1065  2    MET   B CB  
4035 C  CG  A MET   B 2   ? 0.3567 0.4111 0.5260 -0.0439 -0.0388 0.0790  2    MET   B CG  
4036 C  CG  B MET   B 2   ? 0.2902 0.3517 0.3710 -0.0583 -0.0587 0.1218  2    MET   B CG  
4037 S  SD  A MET   B 2   ? 0.3801 0.4323 0.5970 -0.0276 -0.0210 0.0699  2    MET   B SD  
4038 S  SD  B MET   B 2   ? 0.3070 0.3733 0.3921 -0.0403 -0.0635 0.1332  2    MET   B SD  
4039 C  CE  A MET   B 2   ? 0.3828 0.4362 0.6036 -0.0269 -0.0134 0.0705  2    MET   B CE  
4040 C  CE  B MET   B 2   ? 0.3081 0.3766 0.4101 -0.0412 -0.0575 0.1211  2    MET   B CE  
4059 N  N   A VAL   B 3   ? 0.2235 0.2942 0.2963 -0.0846 -0.0973 0.1378  3    VAL   B N   
4060 N  N   B VAL   B 3   ? 0.2096 0.2727 0.2471 -0.0826 -0.0491 0.1312  3    VAL   B N   
4061 C  CA  A VAL   B 3   ? 0.2115 0.2652 0.2943 -0.0732 -0.0836 0.1216  3    VAL   B CA  
4062 C  CA  B VAL   B 3   ? 0.2056 0.2556 0.2482 -0.0683 -0.0423 0.1187  3    VAL   B CA  
4063 C  C   A VAL   B 3   ? 0.1885 0.2432 0.2503 -0.0681 -0.0759 0.1075  3    VAL   B C   
4064 C  C   B VAL   B 3   ? 0.1937 0.2452 0.2229 -0.0556 -0.0464 0.1075  3    VAL   B C   
4065 O  O   A VAL   B 3   ? 0.1767 0.2385 0.2468 -0.0661 -0.0779 0.1128  3    VAL   B O   
4066 O  O   B VAL   B 3   ? 0.1945 0.2534 0.2108 -0.0349 -0.0475 0.1067  3    VAL   B O   
4067 C  CB  A VAL   B 3   ? 0.2271 0.2675 0.3429 -0.0698 -0.0722 0.1007  3    VAL   B CB  
4068 C  CB  B VAL   B 3   ? 0.2169 0.2531 0.2822 -0.0673 -0.0335 0.1043  3    VAL   B CB  
4069 C  CG1 A VAL   B 3   ? 0.2354 0.2654 0.3662 -0.0704 -0.0680 0.0949  3    VAL   B CG1 
4070 C  CG1 B VAL   B 3   ? 0.2228 0.2494 0.3012 -0.0693 -0.0310 0.0974  3    VAL   B CG1 
4071 C  CG2 A VAL   B 3   ? 0.2325 0.2725 0.3617 -0.0643 -0.0586 0.1046  3    VAL   B CG2 
4072 C  CG2 B VAL   B 3   ? 0.2194 0.2528 0.2901 -0.0682 -0.0272 0.1074  3    VAL   B CG2 
4091 N  N   . ASN   B 4   ? 0.1837 0.2293 0.2165 -0.0643 -0.0561 0.0949  4    ASN   B N   
4092 C  CA  . ASN   B 4   ? 0.1839 0.2280 0.1652 -0.0560 -0.0468 0.0556  4    ASN   B CA  
4093 C  C   . ASN   B 4   ? 0.1927 0.2430 0.1563 -0.0575 -0.0361 0.0383  4    ASN   B C   
4094 O  O   . ASN   B 4   ? 0.1899 0.2451 0.1752 -0.0556 -0.0339 0.0193  4    ASN   B O   
4095 C  CB  . ASN   B 4   ? 0.1790 0.2208 0.1548 -0.0536 -0.0535 0.0388  4    ASN   B CB  
4096 C  CG  . ASN   B 4   ? 0.1874 0.2033 0.1443 -0.0523 -0.0443 0.0358  4    ASN   B CG  
4097 O  OD1 . ASN   B 4   ? 0.1823 0.1924 0.1543 -0.0532 -0.0479 0.0370  4    ASN   B OD1 
4098 N  ND2 . ASN   B 4   ? 0.2108 0.2095 0.1536 -0.0311 -0.0346 0.0268  4    ASN   B ND2 
4106 N  N   . SER   B 5   ? 0.2029 0.2584 0.1702 -0.0598 -0.0266 0.0365  5    SER   B N   
4107 C  CA  . SER   B 5   ? 0.2228 0.2943 0.1928 -0.0454 -0.0093 0.0381  5    SER   B CA  
4108 C  C   . SER   B 5   ? 0.2453 0.2975 0.2342 -0.0640 0.0208  0.0312  5    SER   B C   
4109 O  O   . SER   B 5   ? 0.2615 0.2926 0.3287 -0.0590 0.0642  0.0387  5    SER   B O   
4110 C  CB  . SER   B 5   ? 0.2252 0.3121 0.2174 -0.0359 -0.0005 0.0496  5    SER   B CB  
4111 O  OG  . SER   B 5   ? 0.2486 0.3374 0.2759 -0.0221 -0.0089 0.0547  5    SER   B OG  
4117 N  N   . PHE   B 6   ? 0.2671 0.3144 0.1985 -0.0682 0.0367  0.0315  6    PHE   B N   
4118 C  CA  . PHE   B 6   ? 0.2792 0.3151 0.1668 -0.0926 0.0425  0.0131  6    PHE   B CA  
4119 C  C   . PHE   B 6   ? 0.3374 0.3420 0.2222 -0.1011 0.0787  -0.0165 6    PHE   B C   
4120 O  O   . PHE   B 6   ? 0.3522 0.3675 0.2543 -0.0937 0.0554  -0.0272 6    PHE   B O   
4121 C  CB  . PHE   B 6   ? 0.2458 0.2949 0.1588 -0.0860 0.0140  0.0129  6    PHE   B CB  
4122 C  CG  . PHE   B 6   ? 0.2118 0.2681 0.1519 -0.0804 0.0009  0.0129  6    PHE   B CG  
4123 C  CD1 . PHE   B 6   ? 0.2132 0.2366 0.1398 -0.0695 -0.0073 0.0155  6    PHE   B CD1 
4124 C  CD2 . PHE   B 6   ? 0.1865 0.2675 0.1526 -0.0689 0.0025  0.0429  6    PHE   B CD2 
4125 C  CE1 . PHE   B 6   ? 0.2048 0.2174 0.1461 -0.0563 -0.0070 0.0104  6    PHE   B CE1 
4126 C  CE2 . PHE   B 6   ? 0.1873 0.2528 0.1826 -0.0474 0.0032  0.0358  6    PHE   B CE2 
4127 C  CZ  . PHE   B 6   ? 0.1934 0.2278 0.1625 -0.0492 -0.0004 0.0195  6    PHE   B CZ  
4137 N  N   A SER   B 7   ? 0.3646 0.3372 0.2398 -0.1127 0.1149  -0.0353 7    SER   B N   
4138 N  N   B SER   B 7   ? 0.3542 0.3357 0.2458 -0.1091 0.0978  -0.0329 7    SER   B N   
4139 C  CA  A SER   B 7   ? 0.3920 0.3462 0.3024 -0.1091 0.1335  -0.0444 7    SER   B CA  
4140 C  CA  B SER   B 7   ? 0.3707 0.3372 0.2920 -0.1072 0.1076  -0.0423 7    SER   B CA  
4141 C  C   A SER   B 7   ? 0.3883 0.3373 0.2994 -0.1101 0.1500  -0.0537 7    SER   B C   
4142 C  C   B SER   B 7   ? 0.3683 0.3279 0.2986 -0.1077 0.1194  -0.0502 7    SER   B C   
4143 O  O   A SER   B 7   ? 0.3949 0.3400 0.3266 -0.1125 0.1479  -0.0537 7    SER   B O   
4144 O  O   B SER   B 7   ? 0.3727 0.3298 0.3181 -0.1098 0.1168  -0.0504 7    SER   B O   
4145 C  CB  A SER   B 7   ? 0.4115 0.3591 0.3644 -0.1056 0.1408  -0.0438 7    SER   B CB  
4146 C  CB  B SER   B 7   ? 0.3820 0.3445 0.3293 -0.1056 0.1094  -0.0414 7    SER   B CB  
4147 O  OG  A SER   B 7   ? 0.4234 0.3697 0.4106 -0.1029 0.1408  -0.0401 7    SER   B OG  
4148 O  OG  B SER   B 7   ? 0.3892 0.3500 0.3568 -0.1040 0.1078  -0.0387 7    SER   B OG  
4159 N  N   A GLY   B 8   ? 0.3823 0.3267 0.2982 -0.0978 0.1565  -0.0632 8    GLY   B N   
4160 N  N   B GLY   B 8   ? 0.3646 0.3165 0.2987 -0.0990 0.1266  -0.0587 8    GLY   B N   
4161 C  CA  A GLY   B 8   ? 0.3664 0.3096 0.3029 -0.0910 0.1551  -0.0721 8    GLY   B CA  
4162 C  CA  B GLY   B 8   ? 0.3542 0.3012 0.2990 -0.0930 0.1310  -0.0667 8    GLY   B CA  
4163 C  C   A GLY   B 8   ? 0.3477 0.2877 0.2961 -0.0874 0.1497  -0.0717 8    GLY   B C   
4164 C  C   B GLY   B 8   ? 0.3416 0.2823 0.2916 -0.0887 0.1339  -0.0698 8    GLY   B C   
4165 O  O   A GLY   B 8   ? 0.3596 0.2968 0.3313 -0.0742 0.1470  -0.0766 8    GLY   B O   
4166 O  O   B GLY   B 8   ? 0.3490 0.2846 0.3159 -0.0832 0.1323  -0.0713 8    GLY   B O   
4173 N  N   . TYR   B 9   ? 0.3257 0.2651 0.2664 -0.0830 0.1245  -0.0825 9    TYR   B N   
4174 C  CA  . TYR   B 9   ? 0.2939 0.2336 0.2308 -0.0692 0.0842  -0.0672 9    TYR   B CA  
4175 C  C   . TYR   B 9   ? 0.2860 0.2252 0.2165 -0.0698 0.0456  -0.0543 9    TYR   B C   
4176 O  O   . TYR   B 9   ? 0.2998 0.2417 0.2569 -0.0740 0.0544  -0.0334 9    TYR   B O   
4177 C  CB  . TYR   B 9   ? 0.2812 0.2111 0.2307 -0.0575 0.0715  -0.0634 9    TYR   B CB  
4178 C  CG  . TYR   B 9   ? 0.2730 0.1926 0.2286 -0.0648 0.0581  -0.0580 9    TYR   B CG  
4179 C  CD1 . TYR   B 9   ? 0.2763 0.1874 0.2409 -0.0782 0.0654  -0.0511 9    TYR   B CD1 
4180 C  CD2 . TYR   B 9   ? 0.2568 0.1839 0.2162 -0.0638 0.0525  -0.0598 9    TYR   B CD2 
4181 C  CE1 . TYR   B 9   ? 0.2727 0.1989 0.2421 -0.0812 0.0713  -0.0549 9    TYR   B CE1 
4182 C  CE2 . TYR   B 9   ? 0.2552 0.1906 0.2222 -0.0636 0.0563  -0.0506 9    TYR   B CE2 
4183 C  CZ  . TYR   B 9   ? 0.2630 0.2003 0.2319 -0.0758 0.0667  -0.0644 9    TYR   B CZ  
4184 O  OH  . TYR   B 9   ? 0.2637 0.2223 0.2479 -0.0844 0.0616  -0.0817 9    TYR   B OH  
4195 N  N   . LEU   B 10  ? 0.2628 0.2031 0.2015 -0.0659 0.0242  -0.0452 10   LEU   B N   
4196 C  CA  . LEU   B 10  ? 0.2655 0.2015 0.1972 -0.0741 -0.0058 -0.0357 10   LEU   B CA  
4197 C  C   . LEU   B 10  ? 0.2537 0.2022 0.2028 -0.0642 -0.0226 -0.0344 10   LEU   B C   
4198 O  O   . LEU   B 10  ? 0.2376 0.1993 0.1980 -0.0554 -0.0092 -0.0283 10   LEU   B O   
4199 C  CB  . LEU   B 10  ? 0.2902 0.1969 0.2098 -0.0790 -0.0189 -0.0206 10   LEU   B CB  
4200 C  CG  . LEU   B 10  ? 0.3146 0.2036 0.2485 -0.0737 -0.0529 -0.0038 10   LEU   B CG  
4201 C  CD1 . LEU   B 10  ? 0.3319 0.2057 0.2708 -0.0676 -0.0501 -0.0057 10   LEU   B CD1 
4202 C  CD2 . LEU   B 10  ? 0.3230 0.2150 0.2769 -0.0725 -0.0513 0.0158  10   LEU   B CD2 
4214 N  N   . LYS   B 11  ? 0.2689 0.2246 0.2081 -0.0575 -0.0338 -0.0196 11   LYS   B N   
4215 C  CA  . LYS   B 11  ? 0.2959 0.2449 0.2380 -0.0497 -0.0405 -0.0246 11   LYS   B CA  
4216 C  C   . LYS   B 11  ? 0.2777 0.2238 0.2375 -0.0681 -0.0259 -0.0297 11   LYS   B C   
4217 O  O   . LYS   B 11  ? 0.2965 0.2437 0.2617 -0.0852 -0.0221 -0.0603 11   LYS   B O   
4218 C  CB  . LYS   B 11  ? 0.3443 0.2997 0.3185 -0.0258 -0.0514 -0.0273 11   LYS   B CB  
4219 C  CG  . LYS   B 11  ? 0.3827 0.3325 0.3986 -0.0114 -0.0597 -0.0344 11   LYS   B CG  
4220 C  CD  . LYS   B 11  ? 0.4169 0.3544 0.4654 -0.0034 -0.0646 -0.0407 11   LYS   B CD  
4221 C  CE  . LYS   B 11  ? 0.4430 0.3701 0.5134 -0.0014 -0.0701 -0.0463 11   LYS   B CE  
4222 N  NZ  . LYS   B 11  ? 0.4506 0.3799 0.5371 -0.0010 -0.0732 -0.0469 11   LYS   B NZ  
4236 N  N   . LEU   B 12  ? 0.2392 0.2016 0.2390 -0.0586 -0.0283 -0.0410 12   LEU   B N   
4237 C  CA  . LEU   B 12  ? 0.2199 0.1794 0.2485 -0.0535 -0.0164 -0.0428 12   LEU   B CA  
4238 C  C   . LEU   B 12  ? 0.2058 0.1816 0.2539 -0.0519 -0.0310 -0.0427 12   LEU   B C   
4239 O  O   . LEU   B 12  ? 0.2081 0.1852 0.2818 -0.0576 -0.0550 -0.0315 12   LEU   B O   
4240 C  CB  . LEU   B 12  ? 0.2227 0.1640 0.2550 -0.0363 -0.0051 -0.0365 12   LEU   B CB  
4241 C  CG  . LEU   B 12  ? 0.2272 0.1558 0.2496 -0.0366 -0.0008 -0.0269 12   LEU   B CG  
4242 C  CD1 . LEU   B 12  ? 0.2375 0.1665 0.2382 -0.0210 -0.0115 -0.0035 12   LEU   B CD1 
4243 C  CD2 . LEU   B 12  ? 0.2362 0.1614 0.2661 -0.0383 0.0030  -0.0364 12   LEU   B CD2 
4255 N  N   . THR   B 13  ? 0.2027 0.1875 0.2555 -0.0522 -0.0383 -0.0497 13   THR   B N   
4256 C  CA  . THR   B 13  ? 0.2023 0.1948 0.2445 -0.0579 -0.0429 -0.0297 13   THR   B CA  
4257 C  C   . THR   B 13  ? 0.2477 0.2147 0.2619 -0.0696 -0.0629 -0.0248 13   THR   B C   
4258 O  O   . THR   B 13  ? 0.2676 0.2174 0.2662 -0.0624 -0.0321 -0.0322 13   THR   B O   
4259 C  CB  . THR   B 13  ? 0.1878 0.1951 0.2439 -0.0492 -0.0410 -0.0179 13   THR   B CB  
4260 O  OG1 . THR   B 13  ? 0.1814 0.1891 0.2400 -0.0474 -0.0311 -0.0187 13   THR   B OG1 
4261 C  CG2 . THR   B 13  ? 0.2005 0.1991 0.2567 -0.0406 -0.0297 -0.0108 13   THR   B CG2 
4269 N  N   A ASP   B 14  ? 0.2634 0.2254 0.2782 -0.0783 -0.0942 -0.0112 14   ASP   B N   
4270 N  N   B ASP   B 14  ? 0.2601 0.2240 0.2747 -0.0696 -0.0807 -0.0074 14   ASP   B N   
4271 C  CA  A ASP   B 14  ? 0.2755 0.2405 0.3116 -0.0778 -0.1042 0.0053  14   ASP   B CA  
4272 C  CA  B ASP   B 14  ? 0.2692 0.2354 0.2954 -0.0649 -0.0883 0.0089  14   ASP   B CA  
4273 C  C   A ASP   B 14  ? 0.2617 0.2239 0.2666 -0.0757 -0.0855 0.0139  14   ASP   B C   
4274 C  C   B ASP   B 14  ? 0.2531 0.2198 0.2609 -0.0636 -0.0822 0.0140  14   ASP   B C   
4275 O  O   A ASP   B 14  ? 0.2863 0.2369 0.2661 -0.0781 -0.0805 0.0211  14   ASP   B O   
4276 O  O   B ASP   B 14  ? 0.2674 0.2261 0.2647 -0.0579 -0.0799 0.0183  14   ASP   B O   
4277 C  CB  A ASP   B 14  ? 0.2974 0.2754 0.3987 -0.0729 -0.1205 0.0047  14   ASP   B CB  
4278 C  CB  B ASP   B 14  ? 0.2909 0.2639 0.3552 -0.0571 -0.0940 0.0142  14   ASP   B CB  
4279 C  CG  A ASP   B 14  ? 0.3202 0.3031 0.4781 -0.0669 -0.1217 -0.0071 14   ASP   B CG  
4280 C  CG  B ASP   B 14  ? 0.3123 0.2873 0.4083 -0.0488 -0.0920 0.0102  14   ASP   B CG  
4281 O  OD1 A ASP   B 14  ? 0.3336 0.3129 0.4970 -0.0677 -0.1229 -0.0202 14   ASP   B OD1 
4282 O  OD1 B ASP   B 14  ? 0.3217 0.2971 0.4197 -0.0463 -0.0899 0.0025  14   ASP   B OD1 
4283 O  OD2 A ASP   B 14  ? 0.3222 0.3129 0.5153 -0.0689 -0.1174 -0.0048 14   ASP   B OD2 
4284 O  OD2 B ASP   B 14  ? 0.3178 0.2946 0.4308 -0.0512 -0.0905 0.0129  14   ASP   B OD2 
4293 N  N   . ASN   B 15  ? 0.2267 0.1990 0.2322 -0.0606 -0.0798 0.0142  15   ASN   B N   
4294 C  CA  . ASN   B 15  ? 0.1838 0.1727 0.2174 -0.0409 -0.0498 0.0019  15   ASN   B CA  
4295 C  C   . ASN   B 15  ? 0.1619 0.1560 0.2011 -0.0256 -0.0343 -0.0054 15   ASN   B C   
4296 O  O   . ASN   B 15  ? 0.1672 0.1457 0.2256 -0.0235 -0.0478 -0.0163 15   ASN   B O   
4297 C  CB  . ASN   B 15  ? 0.1723 0.1686 0.2324 -0.0172 -0.0556 0.0098  15   ASN   B CB  
4298 C  CG  . ASN   B 15  ? 0.1591 0.1695 0.2356 -0.0261 -0.0265 0.0091  15   ASN   B CG  
4299 O  OD1 . ASN   B 15  ? 0.1680 0.2019 0.2671 -0.0430 -0.0311 0.0149  15   ASN   B OD1 
4300 N  ND2 . ASN   B 15  ? 0.1584 0.1486 0.2183 -0.0178 0.0032  -0.0063 15   ASN   B ND2 
4308 N  N   . VAL   B 16  ? 0.1632 0.1530 0.2044 -0.0309 -0.0436 -0.0056 16   VAL   B N   
4309 C  CA  . VAL   B 16  ? 0.1630 0.1532 0.1915 -0.0325 -0.0290 -0.0268 16   VAL   B CA  
4310 C  C   . VAL   B 16  ? 0.1625 0.1653 0.1845 -0.0388 -0.0291 -0.0154 16   VAL   B C   
4311 O  O   . VAL   B 16  ? 0.1640 0.1759 0.2072 -0.0319 -0.0250 -0.0290 16   VAL   B O   
4312 C  CB  . VAL   B 16  ? 0.1696 0.1498 0.1950 -0.0176 -0.0169 -0.0267 16   VAL   B CB  
4313 C  CG1 . VAL   B 16  ? 0.1765 0.1566 0.2002 -0.0025 -0.0116 -0.0128 16   VAL   B CG1 
4314 C  CG2 . VAL   B 16  ? 0.1739 0.1517 0.2141 -0.0086 -0.0144 -0.0190 16   VAL   B CG2 
4324 N  N   . TYR   B 17  ? 0.1672 0.1753 0.1811 -0.0326 -0.0202 -0.0210 17   TYR   B N   
4325 C  CA  . TYR   B 17  ? 0.1736 0.1896 0.1836 -0.0361 -0.0217 -0.0040 17   TYR   B CA  
4326 C  C   . TYR   B 17  ? 0.1690 0.1579 0.1817 -0.0391 -0.0119 -0.0153 17   TYR   B C   
4327 O  O   . TYR   B 17  ? 0.1707 0.1678 0.1918 -0.0344 -0.0192 -0.0418 17   TYR   B O   
4328 C  CB  . TYR   B 17  ? 0.2119 0.2383 0.2144 -0.0222 -0.0202 0.0321  17   TYR   B CB  
4329 C  CG  . TYR   B 17  ? 0.2455 0.2868 0.2618 -0.0114 -0.0422 0.0460  17   TYR   B CG  
4330 C  CD1 . TYR   B 17  ? 0.2652 0.3033 0.2875 -0.0081 -0.0580 0.0519  17   TYR   B CD1 
4331 C  CD2 . TYR   B 17  ? 0.2711 0.3160 0.2959 -0.0023 -0.0522 0.0460  17   TYR   B CD2 
4332 C  CE1 . TYR   B 17  ? 0.2892 0.3300 0.3175 0.0024  -0.0700 0.0523  17   TYR   B CE1 
4333 C  CE2 . TYR   B 17  ? 0.2916 0.3349 0.3223 0.0114  -0.0739 0.0545  17   TYR   B CE2 
4334 C  CZ  . TYR   B 17  ? 0.3025 0.3456 0.3331 0.0145  -0.0821 0.0575  17   TYR   B CZ  
4335 O  OH  . TYR   B 17  ? 0.3202 0.3653 0.3586 0.0218  -0.0920 0.0569  17   TYR   B OH  
4345 N  N   . ILE   B 18  ? 0.1765 0.1624 0.1679 -0.0331 -0.0025 -0.0203 18   ILE   B N   
4346 C  CA  . ILE   B 18  ? 0.1804 0.1606 0.1762 -0.0382 0.0046  -0.0264 18   ILE   B CA  
4347 C  C   . ILE   B 18  ? 0.1906 0.1625 0.1816 -0.0490 0.0055  -0.0386 18   ILE   B C   
4348 O  O   . ILE   B 18  ? 0.2114 0.1758 0.1858 -0.0376 0.0189  -0.0434 18   ILE   B O   
4349 C  CB  . ILE   B 18  ? 0.1848 0.1579 0.1883 -0.0415 0.0002  -0.0206 18   ILE   B CB  
4350 C  CG1 . ILE   B 18  ? 0.1896 0.1630 0.2030 -0.0429 0.0103  -0.0142 18   ILE   B CG1 
4351 C  CG2 . ILE   B 18  ? 0.1903 0.1605 0.2002 -0.0425 -0.0005 -0.0243 18   ILE   B CG2 
4352 C  CD1 . ILE   B 18  ? 0.2011 0.1877 0.2280 -0.0356 -0.0117 0.0171  18   ILE   B CD1 
4364 N  N   . LYS   B 19  ? 0.1945 0.1635 0.1896 -0.0293 0.0388  -0.0424 19   LYS   B N   
4365 C  CA  . LYS   B 19  ? 0.2035 0.1704 0.2198 -0.0287 0.0354  -0.0515 19   LYS   B CA  
4366 C  C   . LYS   B 19  ? 0.1872 0.1598 0.2265 -0.0239 0.0390  -0.0644 19   LYS   B C   
4367 O  O   . LYS   B 19  ? 0.1860 0.1696 0.2101 -0.0178 0.0327  -0.0543 19   LYS   B O   
4368 C  CB  . LYS   B 19  ? 0.2280 0.1927 0.2324 -0.0345 0.0584  -0.0475 19   LYS   B CB  
4369 C  CG  . LYS   B 19  ? 0.2583 0.2164 0.2657 -0.0456 0.0780  -0.0499 19   LYS   B CG  
4370 C  CD  . LYS   B 19  ? 0.2957 0.2473 0.2824 -0.0540 0.0917  -0.0416 19   LYS   B CD  
4371 C  CE  . LYS   B 19  ? 0.3308 0.2725 0.3020 -0.0588 0.0906  -0.0491 19   LYS   B CE  
4372 N  NZ  . LYS   B 19  ? 0.3459 0.2896 0.3056 -0.0648 0.0908  -0.0510 19   LYS   B NZ  
4386 N  N   . ASN   B 20  ? 0.1851 0.1740 0.2580 -0.0161 0.0385  -0.0666 20   ASN   B N   
4387 C  CA  . ASN   B 20  ? 0.1900 0.1875 0.2770 -0.0136 0.0499  -0.0831 20   ASN   B CA  
4388 C  C   . ASN   B 20  ? 0.1853 0.2106 0.2795 -0.0206 0.0551  -0.0953 20   ASN   B C   
4389 O  O   . ASN   B 20  ? 0.2050 0.2475 0.2985 -0.0321 0.0480  -0.0944 20   ASN   B O   
4390 C  CB  . ASN   B 20  ? 0.2238 0.1900 0.3201 0.0071  0.0437  -0.0865 20   ASN   B CB  
4391 C  CG  . ASN   B 20  ? 0.2529 0.1982 0.3473 0.0343  0.0424  -0.0928 20   ASN   B CG  
4392 O  OD1 . ASN   B 20  ? 0.2841 0.2301 0.3746 0.0490  0.0344  -0.0964 20   ASN   B OD1 
4393 N  ND2 . ASN   B 20  ? 0.2439 0.1998 0.3344 0.0322  0.0356  -0.0817 20   ASN   B ND2 
4400 N  N   . ALA   B 21  ? 0.1859 0.1944 0.2740 -0.0285 0.0599  -0.0817 21   ALA   B N   
4401 C  CA  . ALA   B 21  ? 0.1939 0.1979 0.2875 -0.0335 0.0431  -0.0700 21   ALA   B CA  
4402 C  C   . ALA   B 21  ? 0.1939 0.1812 0.2744 -0.0247 0.0494  -0.0513 21   ALA   B C   
4403 O  O   . ALA   B 21  ? 0.2048 0.1671 0.2633 -0.0346 0.0491  -0.0417 21   ALA   B O   
4404 C  CB  . ALA   B 21  ? 0.2057 0.2280 0.3019 -0.0467 0.0403  -0.0550 21   ALA   B CB  
4410 N  N   . ASP   B 22  ? 0.1841 0.1703 0.2599 -0.0253 0.0384  -0.0452 22   ASP   B N   
4411 C  CA  . ASP   B 22  ? 0.1820 0.1620 0.2424 -0.0144 0.0297  -0.0376 22   ASP   B CA  
4412 C  C   . ASP   B 22  ? 0.1796 0.1566 0.1912 -0.0159 0.0280  -0.0214 22   ASP   B C   
4413 O  O   . ASP   B 22  ? 0.1881 0.1651 0.1924 -0.0166 0.0185  -0.0158 22   ASP   B O   
4414 C  CB  . ASP   B 22  ? 0.1934 0.1688 0.2861 -0.0028 0.0300  -0.0206 22   ASP   B CB  
4415 C  CG  . ASP   B 22  ? 0.1908 0.1887 0.3329 0.0086  0.0059  -0.0224 22   ASP   B CG  
4416 O  OD1 . ASP   B 22  ? 0.2026 0.1864 0.3232 0.0095  -0.0254 -0.0163 22   ASP   B OD1 
4417 O  OD2 . ASP   B 22  ? 0.2019 0.2164 0.4059 0.0134  -0.0104 -0.0326 22   ASP   B OD2 
4422 N  N   . ILE   B 23  ? 0.1839 0.1519 0.1731 -0.0084 0.0057  0.0089  23   ILE   B N   
4423 C  CA  . ILE   B 23  ? 0.1704 0.1475 0.1638 -0.0092 0.0017  0.0009  23   ILE   B CA  
4424 C  C   . ILE   B 23  ? 0.1621 0.1504 0.1590 -0.0071 -0.0022 -0.0017 23   ILE   B C   
4425 O  O   . ILE   B 23  ? 0.1532 0.1491 0.1520 -0.0087 -0.0006 -0.0009 23   ILE   B O   
4426 C  CB  . ILE   B 23  ? 0.1671 0.1455 0.1736 -0.0225 0.0086  0.0134  23   ILE   B CB  
4427 C  CG1 . ILE   B 23  ? 0.1682 0.1590 0.1852 -0.0143 0.0122  0.0268  23   ILE   B CG1 
4428 C  CG2 . ILE   B 23  ? 0.1816 0.1679 0.1623 -0.0155 -0.0040 0.0034  23   ILE   B CG2 
4429 C  CD1 . ILE   B 23  ? 0.1714 0.1727 0.1953 -0.0083 0.0147  0.0219  23   ILE   B CD1 
4441 N  N   . VAL   B 24  ? 0.1668 0.1488 0.1640 -0.0116 -0.0050 -0.0031 24   VAL   B N   
4442 C  CA  . VAL   B 24  ? 0.1639 0.1519 0.1855 -0.0038 -0.0154 -0.0035 24   VAL   B CA  
4443 C  C   . VAL   B 24  ? 0.1588 0.1554 0.1876 -0.0120 -0.0070 0.0011  24   VAL   B C   
4444 O  O   . VAL   B 24  ? 0.1581 0.1661 0.2040 -0.0162 -0.0023 0.0087  24   VAL   B O   
4445 C  CB  . VAL   B 24  ? 0.1719 0.1692 0.1956 0.0057  -0.0201 -0.0067 24   VAL   B CB  
4446 C  CG1 . VAL   B 24  ? 0.1744 0.1693 0.2238 -0.0088 -0.0185 -0.0112 24   VAL   B CG1 
4447 C  CG2 . VAL   B 24  ? 0.1833 0.2009 0.1919 0.0105  -0.0232 -0.0122 24   VAL   B CG2 
4457 N  N   . GLU   B 25  ? 0.1836 0.1729 0.1849 -0.0102 0.0062  -0.0130 25   GLU   B N   
4458 C  CA  . GLU   B 25  ? 0.1934 0.1977 0.2045 -0.0018 0.0209  -0.0175 25   GLU   B CA  
4459 C  C   . GLU   B 25  ? 0.1924 0.1918 0.1746 -0.0156 0.0148  -0.0063 25   GLU   B C   
4460 O  O   . GLU   B 25  ? 0.1948 0.2102 0.1963 -0.0146 0.0304  -0.0009 25   GLU   B O   
4461 C  CB  . GLU   B 25  ? 0.2315 0.2425 0.2862 0.0295  0.0322  -0.0266 25   GLU   B CB  
4462 C  CG  . GLU   B 25  ? 0.2735 0.3065 0.4090 0.0352  0.0284  -0.0298 25   GLU   B CG  
4463 C  CD  . GLU   B 25  ? 0.3158 0.3625 0.5092 0.0275  0.0192  -0.0321 25   GLU   B CD  
4464 O  OE1 . GLU   B 25  ? 0.3372 0.3826 0.5402 0.0303  0.0225  -0.0279 25   GLU   B OE1 
4465 O  OE2 . GLU   B 25  ? 0.3333 0.3789 0.5454 0.0228  0.0088  -0.0387 25   GLU   B OE2 
4472 N  N   A GLU   B 26  ? 0.1930 0.1814 0.1574 -0.0313 0.0124  -0.0021 26   GLU   B N   
4473 N  N   B GLU   B 26  ? 0.1858 0.1822 0.1699 -0.0265 0.0067  -0.0002 26   GLU   B N   
4474 C  CA  A GLU   B 26  ? 0.1930 0.1937 0.1690 -0.0385 0.0016  -0.0027 26   GLU   B CA  
4475 C  CA  B GLU   B 26  ? 0.1774 0.1858 0.1821 -0.0324 -0.0060 0.0025  26   GLU   B CA  
4476 C  C   A GLU   B 26  ? 0.1720 0.1888 0.1553 -0.0282 0.0082  0.0098  26   GLU   B C   
4477 C  C   B GLU   B 26  ? 0.1663 0.1832 0.1618 -0.0253 0.0031  0.0121  26   GLU   B C   
4478 O  O   A GLU   B 26  ? 0.1865 0.2114 0.1735 -0.0226 -0.0004 0.0186  26   GLU   B O   
4479 O  O   B GLU   B 26  ? 0.1769 0.1993 0.1718 -0.0213 -0.0024 0.0185  26   GLU   B O   
4480 C  CB  A GLU   B 26  ? 0.2244 0.2130 0.1886 -0.0477 0.0182  0.0162  26   GLU   B CB  
4481 C  CB  B GLU   B 26  ? 0.1866 0.1938 0.2129 -0.0398 -0.0077 0.0140  26   GLU   B CB  
4482 C  CG  A GLU   B 26  ? 0.2632 0.2382 0.2509 -0.0470 0.0362  0.0057  26   GLU   B CG  
4483 C  CG  B GLU   B 26  ? 0.2022 0.2067 0.2717 -0.0402 -0.0022 -0.0001 26   GLU   B CG  
4484 C  CD  A GLU   B 26  ? 0.2822 0.2491 0.2683 -0.0599 0.0641  -0.0071 26   GLU   B CD  
4485 C  CD  B GLU   B 26  ? 0.1948 0.2049 0.2888 -0.0534 -0.0011 -0.0255 26   GLU   B CD  
4486 O  OE1 A GLU   B 26  ? 0.2895 0.2440 0.2641 -0.0628 0.1087  -0.0002 26   GLU   B OE1 
4487 O  OE1 B GLU   B 26  ? 0.1841 0.2078 0.3266 -0.0761 0.0170  -0.0375 26   GLU   B OE1 
4488 O  OE2 A GLU   B 26  ? 0.2870 0.2591 0.2930 -0.0665 0.0635  0.0055  26   GLU   B OE2 
4489 O  OE2 B GLU   B 26  ? 0.1960 0.1972 0.2832 -0.0436 0.0055  -0.0324 26   GLU   B OE2 
4502 N  N   . ALA   B 27  ? 0.1561 0.1734 0.1514 -0.0207 0.0107  0.0154  27   ALA   B N   
4503 C  CA  . ALA   B 27  ? 0.1573 0.1662 0.1742 -0.0131 0.0069  0.0259  27   ALA   B CA  
4504 C  C   . ALA   B 27  ? 0.1546 0.1739 0.1992 -0.0201 0.0099  0.0385  27   ALA   B C   
4505 O  O   . ALA   B 27  ? 0.1652 0.1890 0.2064 -0.0104 0.0092  0.0438  27   ALA   B O   
4506 C  CB  . ALA   B 27  ? 0.1705 0.1567 0.1728 -0.0097 0.0087  0.0241  27   ALA   B CB  
4513 N  N   . LYS   B 28  ? 0.1492 0.1929 0.2440 -0.0234 0.0146  0.0585  28   LYS   B N   
4514 C  CA  . LYS   B 28  ? 0.1674 0.2365 0.2584 -0.0151 0.0476  0.0946  28   LYS   B CA  
4515 C  C   . LYS   B 28  ? 0.1904 0.2576 0.2373 -0.0036 0.0575  0.0758  28   LYS   B C   
4516 O  O   . LYS   B 28  ? 0.2195 0.2700 0.2486 -0.0024 0.0621  0.0754  28   LYS   B O   
4517 C  CB  . LYS   B 28  ? 0.1927 0.2808 0.3274 -0.0038 0.0741  0.1172  28   LYS   B CB  
4518 C  CG  . LYS   B 28  ? 0.2316 0.3315 0.3910 0.0089  0.0830  0.1358  28   LYS   B CG  
4519 C  CD  . LYS   B 28  ? 0.2898 0.3942 0.4638 0.0169  0.1007  0.1431  28   LYS   B CD  
4520 C  CE  . LYS   B 28  ? 0.3350 0.4402 0.5185 0.0259  0.1054  0.1541  28   LYS   B CE  
4521 N  NZ  . LYS   B 28  ? 0.3659 0.4507 0.5458 0.0336  0.1017  0.1618  28   LYS   B NZ  
4535 N  N   . LYS   B 29  ? 0.2103 0.2825 0.2340 0.0146  0.0535  0.0585  29   LYS   B N   
4536 C  CA  . LYS   B 29  ? 0.2578 0.3199 0.2556 0.0154  0.0557  0.0558  29   LYS   B CA  
4537 C  C   . LYS   B 29  ? 0.2541 0.3255 0.2200 0.0132  0.0367  0.0646  29   LYS   B C   
4538 O  O   . LYS   B 29  ? 0.2767 0.3513 0.2352 0.0217  0.0342  0.0641  29   LYS   B O   
4539 C  CB  . LYS   B 29  ? 0.3144 0.3556 0.3472 0.0162  0.0573  0.0411  29   LYS   B CB  
4540 C  CG  . LYS   B 29  ? 0.3611 0.3847 0.4448 0.0146  0.0587  0.0368  29   LYS   B CG  
4541 C  CD  . LYS   B 29  ? 0.4022 0.4054 0.5175 0.0109  0.0683  0.0319  29   LYS   B CD  
4542 C  CE  . LYS   B 29  ? 0.4298 0.4191 0.5648 0.0073  0.0788  0.0288  29   LYS   B CE  
4543 N  NZ  . LYS   B 29  ? 0.4429 0.4283 0.5950 0.0048  0.0828  0.0265  29   LYS   B NZ  
4557 N  N   . VAL   B 30  ? 0.2204 0.3040 0.2015 -0.0053 0.0281  0.0728  30   VAL   B N   
4558 C  CA  . VAL   B 30  ? 0.2063 0.2914 0.2521 -0.0170 -0.0088 0.0775  30   VAL   B CA  
4559 C  C   . VAL   B 30  ? 0.1794 0.2840 0.2376 -0.0216 -0.0119 0.0992  30   VAL   B C   
4560 O  O   . VAL   B 30  ? 0.1880 0.2997 0.2419 -0.0184 -0.0026 0.1086  30   VAL   B O   
4561 C  CB  . VAL   B 30  ? 0.2133 0.2817 0.3204 -0.0337 -0.0387 0.0691  30   VAL   B CB  
4562 C  CG1 . VAL   B 30  ? 0.2215 0.2890 0.3249 -0.0311 -0.0272 0.0657  30   VAL   B CG1 
4563 C  CG2 . VAL   B 30  ? 0.2284 0.2810 0.3517 -0.0413 -0.0477 0.0463  30   VAL   B CG2 
4573 N  N   . LYS   B 31  ? 0.1705 0.2445 0.2770 -0.0347 -0.0079 0.1136  31   LYS   B N   
4574 C  CA  . LYS   B 31  ? 0.1607 0.2322 0.3179 -0.0400 -0.0149 0.1171  31   LYS   B CA  
4575 C  C   . LYS   B 31  ? 0.1546 0.1938 0.2678 -0.0463 -0.0283 0.0926  31   LYS   B C   
4576 O  O   . LYS   B 31  ? 0.1584 0.2146 0.2820 -0.0297 -0.0219 0.1040  31   LYS   B O   
4577 C  CB  . LYS   B 31  ? 0.1712 0.2786 0.3816 -0.0328 0.0170  0.1282  31   LYS   B CB  
4578 C  CG  . LYS   B 31  ? 0.2046 0.3214 0.4367 -0.0362 0.0387  0.1208  31   LYS   B CG  
4579 C  CD  . LYS   B 31  ? 0.2411 0.3689 0.4840 -0.0318 0.0434  0.1062  31   LYS   B CD  
4580 C  CE  . LYS   B 31  ? 0.2660 0.3948 0.5290 -0.0283 0.0361  0.0906  31   LYS   B CE  
4581 N  NZ  . LYS   B 31  ? 0.2835 0.4106 0.5445 -0.0186 0.0280  0.0748  31   LYS   B NZ  
4595 N  N   . PRO   B 32  ? 0.1673 0.1679 0.1968 -0.0430 -0.0433 0.0551  32   PRO   B N   
4596 C  CA  . PRO   B 32  ? 0.1753 0.1642 0.1551 -0.0411 -0.0458 0.0347  32   PRO   B CA  
4597 C  C   . PRO   B 32  ? 0.1875 0.1523 0.1647 -0.0457 -0.0553 0.0385  32   PRO   B C   
4598 O  O   . PRO   B 32  ? 0.1992 0.1538 0.2080 -0.0445 -0.0728 0.0398  32   PRO   B O   
4599 C  CB  . PRO   B 32  ? 0.1967 0.1596 0.1516 -0.0483 -0.0325 0.0154  32   PRO   B CB  
4600 C  CG  . PRO   B 32  ? 0.2148 0.1428 0.1519 -0.0351 -0.0508 0.0299  32   PRO   B CG  
4601 C  CD  . PRO   B 32  ? 0.1952 0.1526 0.1804 -0.0271 -0.0459 0.0336  32   PRO   B CD  
4609 N  N   . THR   B 33  ? 0.1906 0.1435 0.1496 -0.0371 -0.0514 0.0215  33   THR   B N   
4610 C  CA  . THR   B 33  ? 0.2012 0.1500 0.1503 -0.0432 -0.0473 0.0290  33   THR   B CA  
4611 C  C   . THR   B 33  ? 0.1969 0.1358 0.1456 -0.0363 -0.0490 0.0146  33   THR   B C   
4612 O  O   . THR   B 33  ? 0.2197 0.1407 0.1620 -0.0467 -0.0574 0.0258  33   THR   B O   
4613 C  CB  . THR   B 33  ? 0.2140 0.1551 0.1558 -0.0263 -0.0627 0.0388  33   THR   B CB  
4614 O  OG1 . THR   B 33  ? 0.2075 0.1670 0.1656 -0.0297 -0.0576 0.0386  33   THR   B OG1 
4615 C  CG2 . THR   B 33  ? 0.2368 0.1581 0.1793 -0.0164 -0.0602 0.0297  33   THR   B CG2 
4623 N  N   . VAL   B 34  ? 0.1801 0.1384 0.1313 -0.0355 -0.0403 0.0146  34   VAL   B N   
4624 C  CA  . VAL   B 34  ? 0.1675 0.1352 0.1255 -0.0320 -0.0392 0.0072  34   VAL   B CA  
4625 C  C   . VAL   B 34  ? 0.1509 0.1332 0.1098 -0.0299 -0.0235 0.0076  34   VAL   B C   
4626 O  O   . VAL   B 34  ? 0.1707 0.1375 0.1232 -0.0280 -0.0312 0.0100  34   VAL   B O   
4627 C  CB  . VAL   B 34  ? 0.1788 0.1440 0.1529 -0.0128 -0.0370 0.0023  34   VAL   B CB  
4628 C  CG1 . VAL   B 34  ? 0.1740 0.1618 0.1496 -0.0121 -0.0231 0.0003  34   VAL   B CG1 
4629 C  CG2 . VAL   B 34  ? 0.1887 0.1496 0.1810 -0.0071 -0.0307 0.0022  34   VAL   B CG2 
4639 N  N   . VAL   B 35  ? 0.1452 0.1267 0.1095 -0.0271 -0.0116 0.0067  35   VAL   B N   
4640 C  CA  . VAL   B 35  ? 0.1429 0.1249 0.1074 -0.0186 -0.0093 0.0069  35   VAL   B CA  
4641 C  C   . VAL   B 35  ? 0.1291 0.1178 0.1151 -0.0125 -0.0103 -0.0006 35   VAL   B C   
4642 O  O   . VAL   B 35  ? 0.1400 0.1234 0.1164 -0.0193 0.0010  -0.0053 35   VAL   B O   
4643 C  CB  . VAL   B 35  ? 0.1418 0.1464 0.1111 -0.0156 0.0060  0.0062  35   VAL   B CB  
4644 C  CG1 . VAL   B 35  ? 0.1359 0.1542 0.1408 -0.0242 0.0049  -0.0008 35   VAL   B CG1 
4645 C  CG2 . VAL   B 35  ? 0.1452 0.1443 0.1368 -0.0144 0.0037  0.0037  35   VAL   B CG2 
4655 N  N   . VAL   B 36  ? 0.1317 0.1168 0.1111 -0.0152 -0.0109 0.0062  36   VAL   B N   
4656 C  CA  . VAL   B 36  ? 0.1344 0.1150 0.1064 -0.0125 -0.0010 0.0038  36   VAL   B CA  
4657 C  C   . VAL   B 36  ? 0.1268 0.1207 0.0984 -0.0084 -0.0006 0.0038  36   VAL   B C   
4658 O  O   . VAL   B 36  ? 0.1356 0.1297 0.1205 -0.0096 0.0010  -0.0036 36   VAL   B O   
4659 C  CB  . VAL   B 36  ? 0.1302 0.1238 0.1143 -0.0159 0.0013  0.0044  36   VAL   B CB  
4660 C  CG1 . VAL   B 36  ? 0.1299 0.1363 0.1280 -0.0164 0.0007  0.0158  36   VAL   B CG1 
4661 C  CG2 . VAL   B 36  ? 0.1382 0.1326 0.1310 -0.0173 -0.0160 0.0140  36   VAL   B CG2 
4671 N  N   . ASN   B 37  ? 0.1335 0.1199 0.0992 -0.0021 -0.0066 0.0085  37   ASN   B N   
4672 C  CA  . ASN   B 37  ? 0.1342 0.1252 0.1183 0.0013  -0.0041 0.0049  37   ASN   B CA  
4673 C  C   . ASN   B 37  ? 0.1293 0.1285 0.1129 0.0060  -0.0063 0.0099  37   ASN   B C   
4674 O  O   . ASN   B 37  ? 0.1396 0.1363 0.1158 0.0046  0.0053  0.0110  37   ASN   B O   
4675 C  CB  . ASN   B 37  ? 0.1302 0.1241 0.1152 0.0035  -0.0112 -0.0011 37   ASN   B CB  
4676 C  CG  . ASN   B 37  ? 0.1283 0.1286 0.1164 0.0010  -0.0037 0.0022  37   ASN   B CG  
4677 O  OD1 . ASN   B 37  ? 0.1432 0.1323 0.1325 0.0139  -0.0112 -0.0020 37   ASN   B OD1 
4678 N  ND2 . ASN   B 37  ? 0.1340 0.1272 0.1268 0.0017  -0.0103 0.0055  37   ASN   B ND2 
4685 N  N   . ALA   B 38  ? 0.1400 0.1269 0.1125 0.0144  0.0061  0.0073  38   ALA   B N   
4686 C  CA  . ALA   B 38  ? 0.1494 0.1282 0.1176 0.0001  0.0115  0.0064  38   ALA   B CA  
4687 C  C   . ALA   B 38  ? 0.1427 0.1268 0.1220 -0.0027 0.0107  0.0081  38   ALA   B C   
4688 O  O   . ALA   B 38  ? 0.1561 0.1347 0.1323 0.0080  0.0050  0.0065  38   ALA   B O   
4689 C  CB  . ALA   B 38  ? 0.1675 0.1434 0.1386 -0.0105 0.0142  0.0099  38   ALA   B CB  
4695 N  N   . ALA   B 39  ? 0.1387 0.1312 0.1060 0.0111  0.0028  0.0062  39   ALA   B N   
4696 C  CA  . ALA   B 39  ? 0.1475 0.1322 0.1135 0.0052  -0.0067 0.0009  39   ALA   B CA  
4697 C  C   . ALA   B 39  ? 0.1538 0.1395 0.1040 0.0089  -0.0075 0.0032  39   ALA   B C   
4698 O  O   . ALA   B 39  ? 0.1545 0.1446 0.1228 -0.0020 -0.0007 0.0078  39   ALA   B O   
4699 C  CB  . ALA   B 39  ? 0.1551 0.1416 0.1289 -0.0024 -0.0032 -0.0002 39   ALA   B CB  
4705 N  N   . ASN   B 40  ? 0.1538 0.1616 0.1108 -0.0003 0.0062  -0.0023 40   ASN   B N   
4706 C  CA  . ASN   B 40  ? 0.1619 0.1617 0.1217 0.0061  0.0018  -0.0009 40   ASN   B CA  
4707 C  C   . ASN   B 40  ? 0.1665 0.1640 0.1076 0.0069  -0.0013 0.0036  40   ASN   B C   
4708 O  O   . ASN   B 40  ? 0.1695 0.1560 0.1135 0.0031  -0.0109 0.0057  40   ASN   B O   
4709 C  CB  . ASN   B 40  ? 0.1738 0.1622 0.1402 0.0156  -0.0042 0.0165  40   ASN   B CB  
4710 C  CG  . ASN   B 40  ? 0.1828 0.1683 0.1643 0.0103  -0.0163 0.0185  40   ASN   B CG  
4711 O  OD1 . ASN   B 40  ? 0.1802 0.1637 0.2527 0.0063  -0.0236 0.0192  40   ASN   B OD1 
4712 N  ND2 . ASN   B 40  ? 0.1900 0.1646 0.1730 0.0057  -0.0153 0.0153  40   ASN   B ND2 
4719 N  N   . VAL   B 41  ? 0.1767 0.1707 0.1072 0.0145  0.0085  0.0074  41   VAL   B N   
4720 C  CA  . VAL   B 41  ? 0.1802 0.1786 0.1100 0.0104  0.0054  -0.0027 41   VAL   B CA  
4721 C  C   . VAL   B 41  ? 0.1764 0.1787 0.1019 0.0177  0.0028  -0.0093 41   VAL   B C   
4722 O  O   . VAL   B 41  ? 0.1762 0.1764 0.1144 0.0141  -0.0079 -0.0098 41   VAL   B O   
4723 C  CB  . VAL   B 41  ? 0.1971 0.1929 0.1387 -0.0058 0.0246  -0.0156 41   VAL   B CB  
4724 C  CG1 . VAL   B 41  ? 0.1935 0.1945 0.1578 -0.0090 0.0401  -0.0192 41   VAL   B CG1 
4725 C  CG2 . VAL   B 41  ? 0.2110 0.2111 0.1447 -0.0131 0.0291  -0.0123 41   VAL   B CG2 
4735 N  N   . TYR   B 42  ? 0.1851 0.1762 0.1146 0.0200  -0.0093 -0.0027 42   TYR   B N   
4736 C  CA  . TYR   B 42  ? 0.1887 0.1801 0.1230 0.0162  -0.0247 -0.0113 42   TYR   B CA  
4737 C  C   . TYR   B 42  ? 0.1698 0.1633 0.1248 0.0186  -0.0195 -0.0105 42   TYR   B C   
4738 O  O   . TYR   B 42  ? 0.1725 0.1749 0.1570 0.0180  -0.0243 -0.0127 42   TYR   B O   
4739 C  CB  . TYR   B 42  ? 0.2104 0.2130 0.1387 0.0119  -0.0343 -0.0009 42   TYR   B CB  
4740 C  CG  . TYR   B 42  ? 0.2149 0.2276 0.1350 0.0008  -0.0317 0.0110  42   TYR   B CG  
4741 C  CD1 . TYR   B 42  ? 0.2064 0.2260 0.1087 -0.0062 -0.0170 -0.0028 42   TYR   B CD1 
4742 C  CD2 . TYR   B 42  ? 0.2246 0.2404 0.1794 0.0040  -0.0186 0.0201  42   TYR   B CD2 
4743 C  CE1 . TYR   B 42  ? 0.2237 0.2505 0.1150 -0.0033 -0.0202 -0.0054 42   TYR   B CE1 
4744 C  CE2 . TYR   B 42  ? 0.2275 0.2558 0.1713 0.0025  0.0088  0.0318  42   TYR   B CE2 
4745 C  CZ  . TYR   B 42  ? 0.2423 0.2700 0.1472 0.0138  0.0093  0.0057  42   TYR   B CZ  
4746 O  OH  . TYR   B 42  ? 0.2784 0.2949 0.1847 0.0288  0.0234  0.0080  42   TYR   B OH  
4756 N  N   . LEU   B 43  ? 0.1553 0.1538 0.1143 0.0105  -0.0084 -0.0080 43   LEU   B N   
4757 C  CA  . LEU   B 43  ? 0.1560 0.1536 0.1145 0.0041  -0.0148 0.0017  43   LEU   B CA  
4758 C  C   . LEU   B 43  ? 0.1607 0.1539 0.1204 0.0071  -0.0153 -0.0005 43   LEU   B C   
4759 O  O   . LEU   B 43  ? 0.1568 0.1583 0.1461 0.0061  -0.0173 0.0037  43   LEU   B O   
4760 C  CB  . LEU   B 43  ? 0.1532 0.1470 0.1337 -0.0015 -0.0233 -0.0099 43   LEU   B CB  
4761 C  CG  . LEU   B 43  ? 0.1593 0.1434 0.1286 0.0046  -0.0156 -0.0034 43   LEU   B CG  
4762 C  CD1 . LEU   B 43  ? 0.1730 0.1557 0.1624 0.0000  -0.0318 -0.0021 43   LEU   B CD1 
4763 C  CD2 . LEU   B 43  ? 0.1592 0.1456 0.1396 -0.0051 -0.0253 -0.0074 43   LEU   B CD2 
4775 N  N   . LYS   B 44  ? 0.1605 0.1537 0.1315 0.0071  -0.0077 -0.0023 44   LYS   B N   
4776 C  CA  . LYS   B 44  ? 0.1757 0.1633 0.1265 0.0139  -0.0134 0.0029  44   LYS   B CA  
4777 C  C   . LYS   B 44  ? 0.1689 0.1547 0.1238 0.0208  -0.0153 -0.0001 44   LYS   B C   
4778 O  O   . LYS   B 44  ? 0.1938 0.1538 0.1528 0.0085  0.0011  0.0004  44   LYS   B O   
4779 C  CB  . LYS   B 44  ? 0.2027 0.1887 0.1390 0.0248  -0.0284 0.0026  44   LYS   B CB  
4780 C  CG  . LYS   B 44  ? 0.2368 0.2159 0.1823 0.0217  -0.0497 0.0034  44   LYS   B CG  
4781 C  CD  . LYS   B 44  ? 0.2750 0.2392 0.2510 0.0050  -0.0534 -0.0035 44   LYS   B CD  
4782 C  CE  . LYS   B 44  ? 0.3114 0.2639 0.3046 -0.0062 -0.0570 0.0092  44   LYS   B CE  
4783 N  NZ  . LYS   B 44  ? 0.3261 0.2720 0.3295 -0.0059 -0.0669 0.0300  44   LYS   B NZ  
4797 N  N   . HIS   B 45  ? 0.1547 0.1585 0.1182 0.0100  -0.0057 0.0031  45   HIS   B N   
4798 C  CA  . HIS   B 45  ? 0.1659 0.1579 0.1260 0.0100  -0.0072 -0.0015 45   HIS   B CA  
4799 C  C   . HIS   B 45  ? 0.1849 0.1742 0.1676 0.0230  -0.0207 -0.0015 45   HIS   B C   
4800 O  O   . HIS   B 45  ? 0.2040 0.2048 0.2234 0.0475  0.0144  0.0034  45   HIS   B O   
4801 C  CB  . HIS   B 45  ? 0.1625 0.1560 0.1224 0.0002  -0.0051 -0.0021 45   HIS   B CB  
4802 C  CG  . HIS   B 45  ? 0.1563 0.1520 0.1248 -0.0026 -0.0075 -0.0036 45   HIS   B CG  
4803 N  ND1 . HIS   B 45  ? 0.1612 0.1503 0.1308 0.0033  -0.0184 -0.0022 45   HIS   B ND1 
4804 C  CD2 . HIS   B 45  ? 0.1684 0.1567 0.1482 -0.0064 -0.0129 -0.0025 45   HIS   B CD2 
4805 C  CE1 . HIS   B 45  ? 0.1676 0.1386 0.1206 0.0014  -0.0224 -0.0073 45   HIS   B CE1 
4806 N  NE2 . HIS   B 45  ? 0.1739 0.1461 0.1260 0.0033  -0.0187 -0.0025 45   HIS   B NE2 
4814 N  N   A GLY   B 46  ? 0.1872 0.1689 0.1956 0.0301  -0.0373 0.0106  46   GLY   B N   
4815 N  N   B GLY   B 46  ? 0.1919 0.1773 0.1886 0.0237  -0.0283 0.0100  46   GLY   B N   
4816 C  CA  A GLY   B 46  ? 0.2009 0.1827 0.2360 0.0247  -0.0390 0.0056  46   GLY   B CA  
4817 C  CA  B GLY   B 46  ? 0.2036 0.1898 0.2131 0.0181  -0.0296 0.0117  46   GLY   B CA  
4818 C  C   A GLY   B 46  ? 0.2055 0.2013 0.2802 0.0286  -0.0360 0.0077  46   GLY   B C   
4819 C  C   B GLY   B 46  ? 0.2114 0.2055 0.2422 0.0181  -0.0266 0.0184  46   GLY   B C   
4820 O  O   A GLY   B 46  ? 0.2090 0.2145 0.3630 0.0315  -0.0192 -0.0133 46   GLY   B O   
4821 O  O   B GLY   B 46  ? 0.2183 0.2153 0.2589 0.0167  -0.0181 0.0321  46   GLY   B O   
4828 N  N   . GLY   B 47  ? 0.2116 0.2117 0.2525 0.0090  -0.0181 -0.0004 47   GLY   B N   
4829 C  CA  . GLY   B 47  ? 0.2012 0.1842 0.2006 -0.0011 -0.0096 -0.0040 47   GLY   B CA  
4830 C  C   . GLY   B 47  ? 0.1779 0.1659 0.1704 0.0025  0.0036  -0.0018 47   GLY   B C   
4831 O  O   . GLY   B 47  ? 0.1850 0.1534 0.1822 0.0050  -0.0012 0.0034  47   GLY   B O   
4836 N  N   . GLY   B 48  ? 0.1601 0.1513 0.1764 0.0049  -0.0065 0.0140  48   GLY   B N   
4837 C  CA  . GLY   B 48  ? 0.1596 0.1498 0.1757 -0.0007 -0.0056 0.0075  48   GLY   B CA  
4838 C  C   . GLY   B 48  ? 0.1525 0.1407 0.1625 0.0020  0.0033  0.0024  48   GLY   B C   
4839 O  O   . GLY   B 48  ? 0.1479 0.1440 0.1759 0.0039  -0.0118 0.0034  48   GLY   B O   
4843 N  N   . VAL   B 49  ? 0.1509 0.1467 0.1566 0.0058  0.0020  0.0009  49   VAL   B N   
4844 C  CA  . VAL   B 49  ? 0.1499 0.1543 0.1442 0.0088  -0.0085 -0.0097 49   VAL   B CA  
4845 C  C   . VAL   B 49  ? 0.1381 0.1446 0.1288 0.0117  -0.0034 0.0025  49   VAL   B C   
4846 O  O   . VAL   B 49  ? 0.1513 0.1503 0.1377 0.0064  -0.0026 0.0046  49   VAL   B O   
4847 C  CB  . VAL   B 49  ? 0.1522 0.1690 0.1763 -0.0000 -0.0192 -0.0079 49   VAL   B CB  
4848 C  CG1 . VAL   B 49  ? 0.1519 0.1748 0.1751 0.0028  -0.0278 0.0010  49   VAL   B CG1 
4849 C  CG2 . VAL   B 49  ? 0.1709 0.1927 0.1995 -0.0074 -0.0385 -0.0122 49   VAL   B CG2 
4859 N  N   . ALA   B 50  ? 0.1365 0.1403 0.1242 0.0038  -0.0002 0.0051  50   ALA   B N   
4860 C  CA  . ALA   B 50  ? 0.1355 0.1305 0.1327 0.0098  -0.0020 0.0035  50   ALA   B CA  
4861 C  C   . ALA   B 50  ? 0.1412 0.1412 0.1245 0.0043  -0.0036 0.0076  50   ALA   B C   
4862 O  O   . ALA   B 50  ? 0.1451 0.1437 0.1212 0.0078  0.0013  0.0018  50   ALA   B O   
4863 C  CB  . ALA   B 50  ? 0.1417 0.1345 0.1368 -0.0024 -0.0096 0.0073  50   ALA   B CB  
4869 N  N   . GLY   B 51  ? 0.1465 0.1504 0.1380 0.0117  -0.0072 0.0125  51   GLY   B N   
4870 C  CA  . GLY   B 51  ? 0.1513 0.1558 0.1588 0.0165  -0.0105 0.0099  51   GLY   B CA  
4871 C  C   . GLY   B 51  ? 0.1463 0.1486 0.1596 0.0199  -0.0101 0.0033  51   GLY   B C   
4872 O  O   . GLY   B 51  ? 0.1481 0.1583 0.1804 0.0109  -0.0039 -0.0014 51   GLY   B O   
4876 N  N   . ALA   B 52  ? 0.1503 0.1421 0.1499 0.0127  -0.0048 0.0019  52   ALA   B N   
4877 C  CA  . ALA   B 52  ? 0.1495 0.1478 0.1564 0.0140  0.0007  -0.0027 52   ALA   B CA  
4878 C  C   . ALA   B 52  ? 0.1412 0.1434 0.1464 0.0074  0.0016  -0.0063 52   ALA   B C   
4879 O  O   . ALA   B 52  ? 0.1427 0.1504 0.1666 0.0117  0.0048  -0.0016 52   ALA   B O   
4880 C  CB  . ALA   B 52  ? 0.1694 0.1501 0.1599 0.0024  0.0109  -0.0075 52   ALA   B CB  
4886 N  N   . LEU   B 53  ? 0.1347 0.1419 0.1501 0.0146  0.0000  0.0033  53   LEU   B N   
4887 C  CA  . LEU   B 53  ? 0.1400 0.1584 0.1358 0.0125  -0.0003 -0.0001 53   LEU   B CA  
4888 C  C   . LEU   B 53  ? 0.1470 0.1483 0.1368 0.0089  0.0069  -0.0029 53   LEU   B C   
4889 O  O   . LEU   B 53  ? 0.1511 0.1553 0.1500 -0.0006 0.0091  0.0123  53   LEU   B O   
4890 C  CB  . LEU   B 53  ? 0.1365 0.1585 0.1438 0.0111  0.0022  0.0123  53   LEU   B CB  
4891 C  CG  . LEU   B 53  ? 0.1340 0.1702 0.1528 0.0040  -0.0034 0.0250  53   LEU   B CG  
4892 C  CD1 . LEU   B 53  ? 0.1466 0.1937 0.1775 0.0143  0.0006  0.0064  53   LEU   B CD1 
4893 C  CD2 . LEU   B 53  ? 0.1517 0.2023 0.1783 -0.0024 -0.0095 -0.0082 53   LEU   B CD2 
4905 N  N   . ASN   B 54  ? 0.1446 0.1364 0.1318 0.0049  0.0031  0.0022  54   ASN   B N   
4906 C  CA  . ASN   B 54  ? 0.1438 0.1524 0.1356 0.0055  -0.0080 -0.0060 54   ASN   B CA  
4907 C  C   . ASN   B 54  ? 0.1414 0.1576 0.1478 -0.0004 0.0018  -0.0034 54   ASN   B C   
4908 O  O   . ASN   B 54  ? 0.1415 0.1572 0.1679 -0.0012 0.0054  -0.0029 54   ASN   B O   
4909 C  CB  . ASN   B 54  ? 0.1504 0.1624 0.1531 0.0080  0.0007  -0.0019 54   ASN   B CB  
4910 C  CG  . ASN   B 54  ? 0.1490 0.1688 0.1482 0.0063  -0.0050 0.0007  54   ASN   B CG  
4911 O  OD1 . ASN   B 54  ? 0.1469 0.1685 0.1653 0.0040  -0.0068 -0.0185 54   ASN   B OD1 
4912 N  ND2 . ASN   B 54  ? 0.1654 0.1913 0.1839 0.0047  -0.0232 0.0184  54   ASN   B ND2 
4919 N  N   . LYS   B 55  ? 0.1416 0.1619 0.1684 0.0106  0.0054  -0.0029 55   LYS   B N   
4920 C  CA  . LYS   B 55  ? 0.1497 0.1729 0.1883 0.0187  0.0027  -0.0108 55   LYS   B CA  
4921 C  C   . LYS   B 55  ? 0.1454 0.1754 0.1958 0.0134  0.0093  -0.0154 55   LYS   B C   
4922 O  O   . LYS   B 55  ? 0.1451 0.1859 0.1983 0.0103  0.0084  -0.0154 55   LYS   B O   
4923 C  CB  . LYS   B 55  ? 0.1632 0.1820 0.2312 0.0293  0.0118  -0.0079 55   LYS   B CB  
4924 C  CG  . LYS   B 55  ? 0.2073 0.2156 0.3246 0.0322  0.0277  0.0106  55   LYS   B CG  
4925 C  CD  . LYS   B 55  ? 0.2465 0.2424 0.4029 0.0419  0.0429  0.0239  55   LYS   B CD  
4926 C  CE  . LYS   B 55  ? 0.2727 0.2644 0.4734 0.0435  0.0541  0.0361  55   LYS   B CE  
4927 N  NZ  . LYS   B 55  ? 0.2842 0.2814 0.5116 0.0409  0.0414  0.0498  55   LYS   B NZ  
4941 N  N   . ALA   B 56  ? 0.1429 0.1753 0.1795 0.0123  0.0020  -0.0189 56   ALA   B N   
4942 C  CA  . ALA   B 56  ? 0.1616 0.1915 0.1734 0.0041  0.0042  -0.0128 56   ALA   B CA  
4943 C  C   . ALA   B 56  ? 0.1569 0.1883 0.1657 0.0053  0.0137  -0.0085 56   ALA   B C   
4944 O  O   . ALA   B 56  ? 0.1704 0.2004 0.1770 0.0075  0.0362  -0.0000 56   ALA   B O   
4945 C  CB  . ALA   B 56  ? 0.1777 0.2067 0.1818 -0.0123 0.0054  -0.0142 56   ALA   B CB  
4951 N  N   . THR   B 57  ? 0.1521 0.1757 0.1723 0.0063  0.0213  -0.0036 57   THR   B N   
4952 C  CA  . THR   B 57  ? 0.1600 0.1752 0.1645 0.0001  0.0302  -0.0001 57   THR   B CA  
4953 C  C   . THR   B 57  ? 0.1613 0.1821 0.1849 -0.0036 0.0280  -0.0036 57   THR   B C   
4954 O  O   . THR   B 57  ? 0.1665 0.1812 0.1938 -0.0152 0.0211  -0.0038 57   THR   B O   
4955 C  CB  . THR   B 57  ? 0.1670 0.1636 0.1440 -0.0029 0.0247  0.0126  57   THR   B CB  
4956 O  OG1 . THR   B 57  ? 0.1582 0.1576 0.1613 -0.0039 0.0182  0.0079  57   THR   B OG1 
4957 C  CG2 . THR   B 57  ? 0.1557 0.1654 0.1583 -0.0010 0.0245  0.0116  57   THR   B CG2 
4965 N  N   . ASN   B 58  ? 0.1480 0.2028 0.2114 -0.0141 0.0162  -0.0269 58   ASN   B N   
4966 C  CA  . ASN   B 58  ? 0.1562 0.2440 0.2566 -0.0254 0.0439  -0.0332 58   ASN   B CA  
4967 C  C   . ASN   B 58  ? 0.1437 0.2252 0.2055 -0.0171 0.0125  -0.0240 58   ASN   B C   
4968 O  O   . ASN   B 58  ? 0.1511 0.2391 0.2081 -0.0161 0.0066  -0.0285 58   ASN   B O   
4969 C  CB  . ASN   B 58  ? 0.2390 0.3130 0.3741 -0.0403 0.1069  -0.0339 58   ASN   B CB  
4970 C  CG  . ASN   B 58  ? 0.3429 0.3810 0.5354 -0.0455 0.1259  -0.0050 58   ASN   B CG  
4971 O  OD1 . ASN   B 58  ? 0.3694 0.4027 0.5948 -0.0460 0.1275  0.0020  58   ASN   B OD1 
4972 N  ND2 . ASN   B 58  ? 0.4152 0.4152 0.5923 -0.0487 0.1322  0.0035  58   ASN   B ND2 
4979 N  N   . ASN   B 59  ? 0.1414 0.2081 0.1807 -0.0137 0.0088  -0.0130 59   ASN   B N   
4980 C  CA  . ASN   B 59  ? 0.1406 0.2032 0.1754 -0.0114 -0.0086 -0.0030 59   ASN   B CA  
4981 C  C   . ASN   B 59  ? 0.1410 0.1902 0.1609 -0.0125 -0.0140 -0.0102 59   ASN   B C   
4982 O  O   . ASN   B 59  ? 0.1486 0.1916 0.1594 -0.0123 -0.0084 -0.0058 59   ASN   B O   
4983 C  CB  . ASN   B 59  ? 0.1514 0.2228 0.1993 -0.0022 -0.0159 0.0048  59   ASN   B CB  
4984 C  CG  . ASN   B 59  ? 0.1676 0.2344 0.2051 0.0019  -0.0284 0.0055  59   ASN   B CG  
4985 O  OD1 . ASN   B 59  ? 0.1720 0.2344 0.2055 0.0021  -0.0209 0.0202  59   ASN   B OD1 
4986 N  ND2 . ASN   B 59  ? 0.1816 0.2466 0.2071 -0.0017 -0.0248 -0.0082 59   ASN   B ND2 
4993 N  N   . ALA   B 60  ? 0.1473 0.1840 0.1606 -0.0118 0.0036  -0.0150 60   ALA   B N   
4994 C  CA  . ALA   B 60  ? 0.1569 0.1670 0.1678 -0.0201 0.0044  -0.0052 60   ALA   B CA  
4995 C  C   . ALA   B 60  ? 0.1563 0.1627 0.1431 -0.0088 -0.0022 0.0001  60   ALA   B C   
4996 O  O   . ALA   B 60  ? 0.1602 0.1667 0.1699 -0.0133 -0.0013 -0.0057 60   ALA   B O   
4997 C  CB  . ALA   B 60  ? 0.1739 0.1693 0.1949 -0.0209 0.0126  0.0034  60   ALA   B CB  
5003 N  N   . MET   B 61  ? 0.1466 0.1529 0.1529 -0.0081 -0.0000 0.0055  61   MET   B N   
5004 C  CA  . MET   B 61  ? 0.1432 0.1485 0.1438 -0.0074 -0.0096 -0.0012 61   MET   B CA  
5005 C  C   . MET   B 61  ? 0.1475 0.1435 0.1485 -0.0097 -0.0074 -0.0002 61   MET   B C   
5006 O  O   . MET   B 61  ? 0.1502 0.1413 0.1387 -0.0024 -0.0072 -0.0099 61   MET   B O   
5007 C  CB  . MET   B 61  ? 0.1375 0.1517 0.1341 0.0016  -0.0060 -0.0002 61   MET   B CB  
5008 C  CG  . MET   B 61  ? 0.1332 0.1526 0.1302 -0.0001 -0.0101 0.0015  61   MET   B CG  
5009 S  SD  . MET   B 61  ? 0.1414 0.1535 0.1636 -0.0029 -0.0014 -0.0133 61   MET   B SD  
5010 C  CE  . MET   B 61  ? 0.1436 0.1800 0.1809 -0.0012 -0.0042 -0.0165 61   MET   B CE  
5020 N  N   . GLN   B 62  ? 0.1493 0.1518 0.1449 -0.0030 -0.0152 0.0078  62   GLN   B N   
5021 C  CA  . GLN   B 62  ? 0.1512 0.1582 0.1468 0.0006  -0.0132 0.0026  62   GLN   B CA  
5022 C  C   . GLN   B 62  ? 0.1491 0.1617 0.1396 -0.0005 -0.0235 -0.0075 62   GLN   B C   
5023 O  O   . GLN   B 62  ? 0.1596 0.1695 0.1475 -0.0022 -0.0185 -0.0141 62   GLN   B O   
5024 C  CB  . GLN   B 62  ? 0.1537 0.1596 0.1573 0.0060  -0.0077 0.0015  62   GLN   B CB  
5025 C  CG  . GLN   B 62  ? 0.1577 0.1650 0.1506 0.0049  -0.0207 -0.0020 62   GLN   B CG  
5026 C  CD  . GLN   B 62  ? 0.1564 0.1585 0.1372 0.0106  -0.0235 0.0137  62   GLN   B CD  
5027 O  OE1 . GLN   B 62  ? 0.1605 0.1591 0.1620 0.0065  -0.0233 -0.0026 62   GLN   B OE1 
5028 N  NE2 . GLN   B 62  ? 0.1598 0.1704 0.1493 0.0086  -0.0239 -0.0038 62   GLN   B NE2 
5037 N  N   . VAL   B 63  ? 0.1467 0.1673 0.1641 -0.0071 -0.0224 -0.0149 63   VAL   B N   
5038 C  CA  . VAL   B 63  ? 0.1625 0.1692 0.1799 -0.0120 -0.0254 -0.0053 63   VAL   B CA  
5039 C  C   . VAL   B 63  ? 0.1633 0.1612 0.1606 -0.0161 -0.0222 -0.0127 63   VAL   B C   
5040 O  O   . VAL   B 63  ? 0.1673 0.1576 0.1761 -0.0073 -0.0339 -0.0110 63   VAL   B O   
5041 C  CB  . VAL   B 63  ? 0.1657 0.1822 0.2080 -0.0175 -0.0224 -0.0062 63   VAL   B CB  
5042 C  CG1 . VAL   B 63  ? 0.1717 0.1865 0.2245 -0.0283 -0.0138 -0.0114 63   VAL   B CG1 
5043 C  CG2 . VAL   B 63  ? 0.1542 0.2057 0.2271 -0.0063 -0.0286 -0.0123 63   VAL   B CG2 
5053 N  N   . GLU   B 64  ? 0.1549 0.1519 0.1553 -0.0047 -0.0175 -0.0096 64   GLU   B N   
5054 C  CA  . GLU   B 64  ? 0.1555 0.1433 0.1478 -0.0104 -0.0205 -0.0100 64   GLU   B CA  
5055 C  C   . GLU   B 64  ? 0.1542 0.1464 0.1401 -0.0014 -0.0273 -0.0126 64   GLU   B C   
5056 O  O   . GLU   B 64  ? 0.1689 0.1566 0.1334 -0.0085 -0.0199 -0.0174 64   GLU   B O   
5057 C  CB  . GLU   B 64  ? 0.1562 0.1500 0.1483 -0.0123 -0.0146 -0.0010 64   GLU   B CB  
5058 C  CG  . GLU   B 64  ? 0.1686 0.1586 0.1458 -0.0263 -0.0149 -0.0072 64   GLU   B CG  
5059 C  CD  . GLU   B 64  ? 0.1705 0.1769 0.1586 -0.0273 -0.0228 -0.0077 64   GLU   B CD  
5060 O  OE1 . GLU   B 64  ? 0.1708 0.1945 0.1689 -0.0345 -0.0115 -0.0287 64   GLU   B OE1 
5061 O  OE2 . GLU   B 64  ? 0.1833 0.1856 0.1712 -0.0292 -0.0304 -0.0079 64   GLU   B OE2 
5068 N  N   . SER   B 65  ? 0.1580 0.1451 0.1395 -0.0056 -0.0092 -0.0189 65   SER   B N   
5069 C  CA  . SER   B 65  ? 0.1525 0.1442 0.1442 -0.0047 -0.0126 -0.0183 65   SER   B CA  
5070 C  C   . SER   B 65  ? 0.1549 0.1438 0.1363 0.0001  -0.0118 -0.0147 65   SER   B C   
5071 O  O   . SER   B 65  ? 0.1627 0.1562 0.1271 0.0035  -0.0148 -0.0206 65   SER   B O   
5072 C  CB  . SER   B 65  ? 0.1549 0.1493 0.1422 -0.0120 -0.0132 -0.0101 65   SER   B CB  
5073 O  OG  . SER   B 65  ? 0.1544 0.1489 0.1471 -0.0066 -0.0113 -0.0203 65   SER   B OG  
5079 N  N   . ASP   B 66  ? 0.1645 0.1531 0.1386 -0.0005 -0.0211 -0.0182 66   ASP   B N   
5080 C  CA  . ASP   B 66  ? 0.1759 0.1625 0.1324 0.0058  -0.0284 -0.0108 66   ASP   B CA  
5081 C  C   . ASP   B 66  ? 0.1767 0.1658 0.1345 -0.0039 -0.0259 -0.0168 66   ASP   B C   
5082 O  O   . ASP   B 66  ? 0.1830 0.1612 0.1503 0.0029  -0.0294 -0.0234 66   ASP   B O   
5083 C  CB  . ASP   B 66  ? 0.1865 0.1731 0.1472 0.0095  -0.0398 -0.0193 66   ASP   B CB  
5084 C  CG  . ASP   B 66  ? 0.2141 0.1944 0.1741 0.0180  -0.0567 -0.0066 66   ASP   B CG  
5085 O  OD1 . ASP   B 66  ? 0.2384 0.1856 0.1827 0.0145  -0.0479 -0.0058 66   ASP   B OD1 
5086 O  OD2 . ASP   B 66  ? 0.2283 0.2202 0.2429 0.0388  -0.0534 -0.0049 66   ASP   B OD2 
5091 N  N   . ASP   B 67  ? 0.1687 0.1589 0.1346 -0.0013 -0.0254 -0.0226 67   ASP   B N   
5092 C  CA  . ASP   B 67  ? 0.1826 0.1548 0.1480 -0.0101 -0.0185 -0.0141 67   ASP   B CA  
5093 C  C   . ASP   B 67  ? 0.1791 0.1508 0.1529 -0.0004 -0.0220 -0.0193 67   ASP   B C   
5094 O  O   . ASP   B 67  ? 0.1896 0.1588 0.1717 0.0004  -0.0186 -0.0235 67   ASP   B O   
5095 C  CB  . ASP   B 67  ? 0.2031 0.1613 0.1651 -0.0133 -0.0366 -0.0112 67   ASP   B CB  
5096 C  CG  . ASP   B 67  ? 0.2409 0.1684 0.1714 -0.0080 -0.0676 -0.0122 67   ASP   B CG  
5097 O  OD1 . ASP   B 67  ? 0.2656 0.1773 0.1914 -0.0068 -0.0672 -0.0125 67   ASP   B OD1 
5098 O  OD2 . ASP   B 67  ? 0.2535 0.1763 0.1978 0.0104  -0.0675 -0.0086 67   ASP   B OD2 
5103 N  N   . TYR   B 68  ? 0.1758 0.1563 0.1454 0.0023  -0.0325 -0.0223 68   TYR   B N   
5104 C  CA  . TYR   B 68  ? 0.1689 0.1672 0.1641 0.0064  -0.0250 -0.0351 68   TYR   B CA  
5105 C  C   . TYR   B 68  ? 0.1661 0.1629 0.1683 0.0054  -0.0266 -0.0357 68   TYR   B C   
5106 O  O   . TYR   B 68  ? 0.1755 0.1715 0.1595 0.0084  -0.0276 -0.0449 68   TYR   B O   
5107 C  CB  . TYR   B 68  ? 0.1726 0.1872 0.1664 0.0069  -0.0392 -0.0396 68   TYR   B CB  
5108 C  CG  . TYR   B 68  ? 0.1872 0.2057 0.1712 0.0178  -0.0301 -0.0609 68   TYR   B CG  
5109 C  CD1 . TYR   B 68  ? 0.1880 0.2120 0.1938 -0.0041 -0.0227 -0.0721 68   TYR   B CD1 
5110 C  CD2 . TYR   B 68  ? 0.1960 0.2249 0.1822 0.0262  -0.0395 -0.0472 68   TYR   B CD2 
5111 C  CE1 . TYR   B 68  ? 0.1940 0.2274 0.2089 0.0015  -0.0216 -0.0627 68   TYR   B CE1 
5112 C  CE2 . TYR   B 68  ? 0.1975 0.2295 0.1861 0.0243  -0.0308 -0.0635 68   TYR   B CE2 
5113 C  CZ  . TYR   B 68  ? 0.1937 0.2310 0.2057 0.0090  -0.0278 -0.0635 68   TYR   B CZ  
5114 O  OH  . TYR   B 68  ? 0.1864 0.2463 0.2359 0.0024  -0.0243 -0.0336 68   TYR   B OH  
5124 N  N   . ILE   B 69  ? 0.1631 0.1594 0.1605 0.0063  -0.0283 -0.0377 69   ILE   B N   
5125 C  CA  . ILE   B 69  ? 0.1724 0.1620 0.1568 0.0018  -0.0146 -0.0329 69   ILE   B CA  
5126 C  C   . ILE   B 69  ? 0.1715 0.1585 0.1501 0.0108  -0.0285 -0.0289 69   ILE   B C   
5127 O  O   . ILE   B 69  ? 0.1770 0.1673 0.1478 0.0067  -0.0157 -0.0296 69   ILE   B O   
5128 C  CB  . ILE   B 69  ? 0.1794 0.1686 0.1764 -0.0012 0.0055  -0.0283 69   ILE   B CB  
5129 C  CG1 . ILE   B 69  ? 0.1834 0.1721 0.1893 -0.0047 0.0138  -0.0293 69   ILE   B CG1 
5130 C  CG2 . ILE   B 69  ? 0.1920 0.1772 0.1978 0.0011  0.0080  -0.0255 69   ILE   B CG2 
5131 C  CD1 . ILE   B 69  ? 0.1766 0.1792 0.2049 -0.0202 0.0092  -0.0378 69   ILE   B CD1 
5143 N  N   . ALA   B 70  ? 0.1644 0.1628 0.1577 0.0104  -0.0337 -0.0271 70   ALA   B N   
5144 C  CA  . ALA   B 70  ? 0.1690 0.1654 0.1465 0.0044  -0.0294 -0.0252 70   ALA   B CA  
5145 C  C   . ALA   B 70  ? 0.1792 0.1662 0.1444 -0.0012 -0.0364 -0.0352 70   ALA   B C   
5146 O  O   . ALA   B 70  ? 0.1903 0.1670 0.1614 0.0013  -0.0322 -0.0402 70   ALA   B O   
5147 C  CB  . ALA   B 70  ? 0.1740 0.1748 0.1609 0.0020  -0.0328 -0.0321 70   ALA   B CB  
5153 N  N   . THR   B 71  ? 0.1873 0.1659 0.1529 0.0021  -0.0383 -0.0326 71   THR   B N   
5154 C  CA  . THR   B 71  ? 0.1957 0.1634 0.1858 0.0099  -0.0589 -0.0334 71   THR   B CA  
5155 C  C   . THR   B 71  ? 0.1908 0.1654 0.2154 0.0288  -0.0572 -0.0439 71   THR   B C   
5156 O  O   . THR   B 71  ? 0.2055 0.1783 0.2528 0.0260  -0.0458 -0.0609 71   THR   B O   
5157 C  CB  . THR   B 71  ? 0.2194 0.1921 0.2088 0.0023  -0.0675 -0.0153 71   THR   B CB  
5158 O  OG1 . THR   B 71  ? 0.2379 0.2244 0.2404 -0.0206 -0.0620 0.0163  71   THR   B OG1 
5159 C  CG2 . THR   B 71  ? 0.2405 0.1952 0.2364 0.0122  -0.0606 -0.0031 71   THR   B CG2 
5167 N  N   . ASN   B 72  ? 0.1783 0.1703 0.2060 0.0207  -0.0530 -0.0630 72   ASN   B N   
5168 C  CA  . ASN   B 72  ? 0.1815 0.1883 0.2088 0.0228  -0.0413 -0.0738 72   ASN   B CA  
5169 C  C   . ASN   B 72  ? 0.1750 0.2039 0.2141 0.0042  -0.0167 -0.0698 72   ASN   B C   
5170 O  O   . ASN   B 72  ? 0.1759 0.2189 0.2436 0.0062  -0.0124 -0.0675 72   ASN   B O   
5171 C  CB  . ASN   B 72  ? 0.1917 0.2053 0.2174 0.0175  -0.0524 -0.0638 72   ASN   B CB  
5172 C  CG  . ASN   B 72  ? 0.2064 0.2191 0.2288 0.0308  -0.0570 -0.0416 72   ASN   B CG  
5173 O  OD1 . ASN   B 72  ? 0.2302 0.2360 0.2312 0.0163  -0.0427 -0.0471 72   ASN   B OD1 
5174 N  ND2 . ASN   B 72  ? 0.2178 0.2289 0.2794 0.0447  -0.0398 -0.0113 72   ASN   B ND2 
5181 N  N   . GLY   B 73  ? 0.1786 0.2001 0.1966 -0.0002 -0.0279 -0.0668 73   GLY   B N   
5182 C  CA  . GLY   B 73  ? 0.1733 0.2105 0.1769 -0.0034 -0.0118 -0.0579 73   GLY   B CA  
5183 C  C   . GLY   B 73  ? 0.1693 0.2046 0.1291 0.0034  -0.0106 -0.0465 73   GLY   B C   
5184 O  O   . GLY   B 73  ? 0.1688 0.1897 0.1458 0.0070  -0.0165 -0.0284 73   GLY   B O   
5188 N  N   . PRO   B 74  ? 0.1780 0.2128 0.1250 -0.0011 -0.0167 -0.0379 74   PRO   B N   
5189 C  CA  . PRO   B 74  ? 0.1713 0.2106 0.1219 -0.0002 -0.0141 -0.0293 74   PRO   B CA  
5190 C  C   . PRO   B 74  ? 0.1568 0.1926 0.1265 0.0012  -0.0094 -0.0198 74   PRO   B C   
5191 O  O   . PRO   B 74  ? 0.1609 0.2003 0.1666 0.0045  -0.0059 -0.0297 74   PRO   B O   
5192 C  CB  . PRO   B 74  ? 0.1895 0.2334 0.1179 -0.0043 -0.0091 -0.0112 74   PRO   B CB  
5193 C  CG  . PRO   B 74  ? 0.2111 0.2449 0.1497 -0.0025 -0.0075 -0.0117 74   PRO   B CG  
5194 C  CD  . PRO   B 74  ? 0.2063 0.2369 0.1353 0.0006  -0.0031 -0.0207 74   PRO   B CD  
5202 N  N   . LEU   B 75  ? 0.1585 0.1821 0.1170 0.0063  -0.0173 -0.0205 75   LEU   B N   
5203 C  CA  . LEU   B 75  ? 0.1584 0.1796 0.1242 0.0020  -0.0157 -0.0053 75   LEU   B CA  
5204 C  C   . LEU   B 75  ? 0.1637 0.1861 0.1319 0.0094  -0.0051 -0.0071 75   LEU   B C   
5205 O  O   . LEU   B 75  ? 0.1869 0.1999 0.1402 0.0009  -0.0086 0.0092  75   LEU   B O   
5206 C  CB  . LEU   B 75  ? 0.1614 0.1790 0.1154 -0.0045 -0.0167 0.0078  75   LEU   B CB  
5207 C  CG  . LEU   B 75  ? 0.1937 0.2011 0.1362 -0.0296 -0.0047 0.0064  75   LEU   B CG  
5208 C  CD1 . LEU   B 75  ? 0.2264 0.2196 0.1462 -0.0390 0.0196  -0.0077 75   LEU   B CD1 
5209 C  CD2 . LEU   B 75  ? 0.2359 0.2210 0.2111 -0.0178 0.0128  0.0122  75   LEU   B CD2 
5221 N  N   . LYS   B 76  ? 0.1574 0.2082 0.1526 0.0019  0.0011  0.0017  76   LYS   B N   
5222 C  CA  . LYS   B 76  ? 0.1712 0.2159 0.1715 -0.0009 0.0161  -0.0030 76   LYS   B CA  
5223 C  C   . LYS   B 76  ? 0.1682 0.1999 0.1398 0.0060  0.0077  0.0205  76   LYS   B C   
5224 O  O   . LYS   B 76  ? 0.1749 0.1834 0.1391 0.0013  0.0103  0.0158  76   LYS   B O   
5225 C  CB  . LYS   B 76  ? 0.1908 0.2212 0.2420 -0.0066 0.0379  -0.0298 76   LYS   B CB  
5226 C  CG  . LYS   B 76  ? 0.2032 0.2362 0.2832 0.0036  0.0262  -0.0305 76   LYS   B CG  
5227 C  CD  . LYS   B 76  ? 0.2034 0.2427 0.3207 0.0116  0.0163  -0.0521 76   LYS   B CD  
5228 C  CE  . LYS   B 76  ? 0.2116 0.2570 0.3754 0.0154  0.0031  -0.0611 76   LYS   B CE  
5229 N  NZ  . LYS   B 76  ? 0.2097 0.2630 0.3990 0.0101  -0.0141 -0.0773 76   LYS   B NZ  
5243 N  N   . VAL   B 77  ? 0.1767 0.2138 0.1468 0.0179  0.0132  0.0268  77   VAL   B N   
5244 C  CA  . VAL   B 77  ? 0.1809 0.2054 0.1645 0.0200  0.0175  0.0541  77   VAL   B CA  
5245 C  C   . VAL   B 77  ? 0.1672 0.1864 0.1594 0.0169  0.0328  0.0361  77   VAL   B C   
5246 O  O   . VAL   B 77  ? 0.1684 0.1817 0.1591 0.0243  0.0330  0.0286  77   VAL   B O   
5247 C  CB  . VAL   B 77  ? 0.1877 0.2168 0.2019 0.0187  0.0340  0.0714  77   VAL   B CB  
5248 C  CG1 . VAL   B 77  ? 0.1828 0.2101 0.2411 0.0109  0.0335  0.0847  77   VAL   B CG1 
5249 C  CG2 . VAL   B 77  ? 0.1955 0.2363 0.2173 0.0146  0.0167  0.0720  77   VAL   B CG2 
5259 N  N   . GLY   B 78  ? 0.1563 0.1692 0.1594 0.0141  0.0204  0.0298  78   GLY   B N   
5260 C  CA  . GLY   B 78  ? 0.1591 0.1669 0.1581 0.0129  0.0323  0.0133  78   GLY   B CA  
5261 C  C   . GLY   B 78  ? 0.1565 0.1570 0.1427 0.0086  0.0253  0.0255  78   GLY   B C   
5262 O  O   . GLY   B 78  ? 0.1617 0.1583 0.1521 0.0159  0.0221  0.0198  78   GLY   B O   
5266 N  N   . GLY   B 79  ? 0.1465 0.1578 0.1515 0.0112  0.0224  0.0141  79   GLY   B N   
5267 C  CA  . GLY   B 79  ? 0.1487 0.1543 0.1441 0.0162  0.0122  0.0079  79   GLY   B CA  
5268 C  C   . GLY   B 79  ? 0.1366 0.1454 0.1413 0.0165  0.0146  0.0069  79   GLY   B C   
5269 O  O   . GLY   B 79  ? 0.1444 0.1462 0.1533 0.0122  0.0189  0.0155  79   GLY   B O   
5273 N  N   . SER   B 80  ? 0.1407 0.1388 0.1434 0.0093  0.0193  0.0058  80   SER   B N   
5274 C  CA  . SER   B 80  ? 0.1394 0.1361 0.1423 0.0028  0.0131  0.0036  80   SER   B CA  
5275 C  C   . SER   B 80  ? 0.1389 0.1338 0.1372 0.0029  0.0009  0.0012  80   SER   B C   
5276 O  O   . SER   B 80  ? 0.1540 0.1374 0.1709 0.0076  0.0064  -0.0055 80   SER   B O   
5277 C  CB  . SER   B 80  ? 0.1439 0.1374 0.1459 -0.0020 0.0095  0.0032  80   SER   B CB  
5278 O  OG  . SER   B 80  ? 0.1523 0.1565 0.1687 -0.0005 -0.0104 0.0078  80   SER   B OG  
5284 N  N   . CYS   B 81  ? 0.1371 0.1275 0.1455 0.0049  0.0020  -0.0025 81   CYS   B N   
5285 C  CA  . CYS   B 81  ? 0.1424 0.1272 0.1451 0.0030  -0.0099 -0.0054 81   CYS   B CA  
5286 C  C   . CYS   B 81  ? 0.1378 0.1221 0.1285 0.0004  -0.0141 -0.0006 81   CYS   B C   
5287 O  O   . CYS   B 81  ? 0.1610 0.1240 0.1427 0.0083  -0.0008 -0.0039 81   CYS   B O   
5288 C  CB  . CYS   B 81  ? 0.1555 0.1442 0.1536 -0.0034 -0.0101 -0.0028 81   CYS   B CB  
5289 S  SG  . CYS   B 81  ? 0.1580 0.1596 0.1385 -0.0012 -0.0237 -0.0115 81   CYS   B SG  
5295 N  N   . VAL   B 82  ? 0.1423 0.1244 0.1449 0.0028  -0.0084 -0.0005 82   VAL   B N   
5296 C  CA  . VAL   B 82  ? 0.1521 0.1303 0.1358 -0.0014 -0.0060 0.0047  82   VAL   B CA  
5297 C  C   . VAL   B 82  ? 0.1605 0.1205 0.1414 -0.0036 -0.0083 -0.0009 82   VAL   B C   
5298 O  O   . VAL   B 82  ? 0.1651 0.1214 0.1769 -0.0030 0.0025  -0.0184 82   VAL   B O   
5299 C  CB  . VAL   B 82  ? 0.1558 0.1458 0.1552 -0.0017 -0.0122 0.0066  82   VAL   B CB  
5300 C  CG1 . VAL   B 82  ? 0.1704 0.1647 0.1710 0.0024  -0.0160 0.0164  82   VAL   B CG1 
5301 C  CG2 . VAL   B 82  ? 0.1574 0.1657 0.1765 -0.0019 -0.0297 0.0135  82   VAL   B CG2 
5311 N  N   . LEU   B 83  ? 0.1485 0.1235 0.1382 -0.0124 -0.0204 -0.0071 83   LEU   B N   
5312 C  CA  . LEU   B 83  ? 0.1448 0.1297 0.1280 -0.0120 -0.0189 -0.0053 83   LEU   B CA  
5313 C  C   . LEU   B 83  ? 0.1496 0.1269 0.1286 -0.0191 -0.0221 -0.0012 83   LEU   B C   
5314 O  O   . LEU   B 83  ? 0.1481 0.1369 0.1213 -0.0191 -0.0103 0.0038  83   LEU   B O   
5315 C  CB  . LEU   B 83  ? 0.1517 0.1436 0.1335 -0.0106 -0.0207 -0.0097 83   LEU   B CB  
5316 C  CG  . LEU   B 83  ? 0.1687 0.1659 0.1398 -0.0128 -0.0105 -0.0138 83   LEU   B CG  
5317 C  CD1 . LEU   B 83  ? 0.1746 0.1738 0.1398 -0.0132 -0.0237 -0.0051 83   LEU   B CD1 
5318 C  CD2 . LEU   B 83  ? 0.1940 0.1651 0.1607 -0.0054 -0.0148 -0.0212 83   LEU   B CD2 
5330 N  N   . SER   B 84  ? 0.1501 0.1453 0.1488 -0.0251 -0.0214 0.0043  84   SER   B N   
5331 C  CA  . SER   B 84  ? 0.1573 0.1627 0.1352 -0.0300 -0.0124 0.0213  84   SER   B CA  
5332 C  C   . SER   B 84  ? 0.1442 0.1739 0.1071 -0.0183 -0.0147 0.0207  84   SER   B C   
5333 O  O   . SER   B 84  ? 0.1581 0.1600 0.1033 -0.0205 -0.0077 -0.0002 84   SER   B O   
5334 C  CB  . SER   B 84  ? 0.1754 0.1705 0.1874 -0.0303 0.0131  0.0142  84   SER   B CB  
5335 O  OG  . SER   B 84  ? 0.1760 0.1812 0.2265 -0.0390 0.0067  0.0172  84   SER   B OG  
5341 N  N   . GLY   B 85  ? 0.1488 0.1945 0.1196 -0.0239 -0.0107 0.0234  85   GLY   B N   
5342 C  CA  . GLY   B 85  ? 0.1467 0.2032 0.1408 -0.0348 0.0024  -0.0097 85   GLY   B CA  
5343 C  C   . GLY   B 85  ? 0.1478 0.1874 0.1234 -0.0431 -0.0005 0.0068  85   GLY   B C   
5344 O  O   . GLY   B 85  ? 0.1609 0.1851 0.1287 -0.0513 0.0170  -0.0084 85   GLY   B O   
5348 N  N   . HIS   B 86  ? 0.1402 0.1688 0.1453 -0.0295 -0.0146 0.0150  86   HIS   B N   
5349 C  CA  . HIS   B 86  ? 0.1541 0.1658 0.1368 -0.0311 -0.0172 0.0131  86   HIS   B CA  
5350 C  C   . HIS   B 86  ? 0.1527 0.1793 0.1292 -0.0416 -0.0068 0.0242  86   HIS   B C   
5351 O  O   . HIS   B 86  ? 0.1640 0.1940 0.1346 -0.0309 0.0059  0.0262  86   HIS   B O   
5352 C  CB  . HIS   B 86  ? 0.1582 0.1657 0.1462 -0.0198 -0.0222 0.0013  86   HIS   B CB  
5353 C  CG  . HIS   B 86  ? 0.1578 0.1795 0.1469 -0.0068 -0.0145 0.0077  86   HIS   B CG  
5354 N  ND1 . HIS   B 86  ? 0.1663 0.2033 0.1659 -0.0166 -0.0130 -0.0089 86   HIS   B ND1 
5355 C  CD2 . HIS   B 86  ? 0.1595 0.1796 0.1491 -0.0044 -0.0195 0.0056  86   HIS   B CD2 
5356 C  CE1 . HIS   B 86  ? 0.1791 0.1983 0.1517 -0.0122 -0.0044 -0.0220 86   HIS   B CE1 
5357 N  NE2 . HIS   B 86  ? 0.1732 0.1866 0.1437 0.0048  -0.0059 -0.0084 86   HIS   B NE2 
5365 N  N   . ASN   B 87  ? 0.1561 0.1807 0.1422 -0.0314 0.0037  0.0177  87   ASN   B N   
5366 C  CA  . ASN   B 87  ? 0.1599 0.2026 0.1431 -0.0302 0.0282  0.0137  87   ASN   B CA  
5367 C  C   . ASN   B 87  ? 0.1756 0.1823 0.1371 -0.0313 0.0318  0.0154  87   ASN   B C   
5368 O  O   . ASN   B 87  ? 0.2052 0.1873 0.1652 -0.0245 0.0515  0.0060  87   ASN   B O   
5369 C  CB  . ASN   B 87  ? 0.1619 0.2374 0.1856 -0.0278 0.0365  0.0131  87   ASN   B CB  
5370 C  CG  . ASN   B 87  ? 0.1681 0.2558 0.1965 0.0046  0.0419  0.0299  87   ASN   B CG  
5371 O  OD1 . ASN   B 87  ? 0.1645 0.2401 0.1762 0.0173  0.0510  0.0450  87   ASN   B OD1 
5372 N  ND2 . ASN   B 87  ? 0.2099 0.2656 0.2324 0.0158  0.0458  0.0256  87   ASN   B ND2 
5379 N  N   . LEU   B 88  ? 0.1672 0.1731 0.1294 -0.0333 0.0131  0.0110  88   LEU   B N   
5380 C  CA  . LEU   B 88  ? 0.1789 0.1642 0.1333 -0.0369 0.0039  -0.0069 88   LEU   B CA  
5381 C  C   . LEU   B 88  ? 0.1782 0.1585 0.1355 -0.0395 -0.0014 -0.0057 88   LEU   B C   
5382 O  O   . LEU   B 88  ? 0.2042 0.1655 0.1612 -0.0222 -0.0268 -0.0094 88   LEU   B O   
5383 C  CB  . LEU   B 88  ? 0.1948 0.1716 0.1427 -0.0492 -0.0130 0.0088  88   LEU   B CB  
5384 C  CG  . LEU   B 88  ? 0.2294 0.2013 0.1659 -0.0401 -0.0344 0.0325  88   LEU   B CG  
5385 C  CD1 . LEU   B 88  ? 0.2371 0.2354 0.1792 -0.0547 -0.0274 0.0498  88   LEU   B CD1 
5386 C  CD2 . LEU   B 88  ? 0.2650 0.2267 0.2395 0.0016  -0.0566 0.0125  88   LEU   B CD2 
5398 N  N   . ALA   B 89  ? 0.1589 0.1570 0.1204 -0.0395 0.0189  -0.0062 89   ALA   B N   
5399 C  CA  . ALA   B 89  ? 0.1570 0.1558 0.1050 -0.0390 0.0039  0.0040  89   ALA   B CA  
5400 C  C   . ALA   B 89  ? 0.1703 0.1541 0.1043 -0.0444 0.0141  0.0025  89   ALA   B C   
5401 O  O   . ALA   B 89  ? 0.1502 0.1667 0.1474 -0.0424 0.0141  -0.0309 89   ALA   B O   
5402 C  CB  . ALA   B 89  ? 0.1475 0.1517 0.1294 -0.0342 0.0067  0.0145  89   ALA   B CB  
5408 N  N   . LYS   B 90  ? 0.2068 0.1470 0.1193 -0.0485 -0.0091 0.0150  90   LYS   B N   
5409 C  CA  . LYS   B 90  ? 0.2202 0.1446 0.1127 -0.0498 -0.0166 0.0150  90   LYS   B CA  
5410 C  C   . LYS   B 90  ? 0.1982 0.1382 0.1303 -0.0433 -0.0102 0.0018  90   LYS   B C   
5411 O  O   . LYS   B 90  ? 0.2008 0.1521 0.1476 -0.0529 -0.0026 0.0058  90   LYS   B O   
5412 C  CB  . LYS   B 90  ? 0.2372 0.1512 0.1441 -0.0451 -0.0083 0.0227  90   LYS   B CB  
5413 C  CG  . LYS   B 90  ? 0.2363 0.1707 0.1578 -0.0290 0.0218  0.0107  90   LYS   B CG  
5414 C  CD  . LYS   B 90  ? 0.2627 0.1940 0.2100 -0.0165 0.0523  -0.0021 90   LYS   B CD  
5415 C  CE  . LYS   B 90  ? 0.2759 0.2114 0.2766 -0.0209 0.0689  -0.0122 90   LYS   B CE  
5416 N  NZ  . LYS   B 90  ? 0.2865 0.2014 0.2805 -0.0344 0.0848  -0.0106 90   LYS   B NZ  
5430 N  N   . HIS   B 91  ? 0.1691 0.1273 0.1068 -0.0287 -0.0153 0.0066  91   HIS   B N   
5431 C  CA  . HIS   B 91  ? 0.1614 0.1249 0.1253 -0.0209 -0.0148 0.0016  91   HIS   B CA  
5432 C  C   . HIS   B 91  ? 0.1481 0.1300 0.1136 -0.0245 -0.0103 0.0029  91   HIS   B C   
5433 O  O   . HIS   B 91  ? 0.1650 0.1352 0.1078 -0.0257 -0.0145 0.0027  91   HIS   B O   
5434 C  CB  . HIS   B 91  ? 0.1755 0.1268 0.1709 -0.0098 -0.0109 0.0149  91   HIS   B CB  
5435 C  CG  . HIS   B 91  ? 0.2162 0.1517 0.2381 0.0029  0.0204  0.0226  91   HIS   B CG  
5436 N  ND1 . HIS   B 91  ? 0.2476 0.1568 0.2986 0.0014  0.0336  0.0132  91   HIS   B ND1 
5437 C  CD2 . HIS   B 91  ? 0.2273 0.1783 0.2801 0.0189  0.0033  0.0550  91   HIS   B CD2 
5438 C  CE1 . HIS   B 91  ? 0.2521 0.1702 0.3172 0.0182  0.0265  0.0207  91   HIS   B CE1 
5439 N  NE2 . HIS   B 91  ? 0.2456 0.1869 0.3160 0.0273  0.0195  0.0588  91   HIS   B NE2 
5447 N  N   . CYS   B 92  ? 0.1443 0.1265 0.1054 -0.0211 -0.0102 -0.0004 92   CYS   B N   
5448 C  CA  . CYS   B 92  ? 0.1396 0.1261 0.1099 -0.0199 -0.0022 -0.0003 92   CYS   B CA  
5449 C  C   . CYS   B 92  ? 0.1410 0.1228 0.0997 -0.0135 -0.0065 0.0012  92   CYS   B C   
5450 O  O   . CYS   B 92  ? 0.1500 0.1303 0.1133 -0.0128 0.0006  -0.0005 92   CYS   B O   
5451 C  CB  . CYS   B 92  ? 0.1399 0.1348 0.1170 -0.0155 -0.0098 0.0035  92   CYS   B CB  
5452 S  SG  . CYS   B 92  ? 0.1413 0.1375 0.1213 -0.0091 -0.0074 0.0052  92   CYS   B SG  
5458 N  N   . LEU   B 93  ? 0.1332 0.1221 0.1026 -0.0125 -0.0029 -0.0046 93   LEU   B N   
5459 C  CA  . LEU   B 93  ? 0.1322 0.1220 0.1179 -0.0018 -0.0087 0.0029  93   LEU   B CA  
5460 C  C   . LEU   B 93  ? 0.1286 0.1167 0.1109 -0.0039 -0.0052 0.0095  93   LEU   B C   
5461 O  O   . LEU   B 93  ? 0.1359 0.1217 0.1130 -0.0057 -0.0060 0.0016  93   LEU   B O   
5462 C  CB  . LEU   B 93  ? 0.1389 0.1148 0.1261 -0.0013 -0.0069 0.0071  93   LEU   B CB  
5463 C  CG  . LEU   B 93  ? 0.1301 0.1337 0.1447 -0.0033 -0.0069 0.0225  93   LEU   B CG  
5464 C  CD1 . LEU   B 93  ? 0.1335 0.1503 0.1432 0.0077  0.0014  0.0069  93   LEU   B CD1 
5465 C  CD2 . LEU   B 93  ? 0.1315 0.1382 0.1555 0.0011  -0.0076 0.0115  93   LEU   B CD2 
5477 N  N   . HIS   B 94  ? 0.1304 0.1187 0.1085 -0.0066 -0.0106 0.0054  94   HIS   B N   
5478 C  CA  . HIS   B 94  ? 0.1329 0.1204 0.1078 -0.0027 -0.0012 0.0085  94   HIS   B CA  
5479 C  C   . HIS   B 94  ? 0.1330 0.1227 0.1174 -0.0020 -0.0039 0.0071  94   HIS   B C   
5480 O  O   . HIS   B 94  ? 0.1301 0.1297 0.1629 -0.0048 0.0199  -0.0030 94   HIS   B O   
5481 C  CB  . HIS   B 94  ? 0.1308 0.1284 0.1199 0.0007  -0.0029 0.0055  94   HIS   B CB  
5482 C  CG  . HIS   B 94  ? 0.1336 0.1226 0.1086 -0.0066 -0.0154 0.0015  94   HIS   B CG  
5483 N  ND1 . HIS   B 94  ? 0.1399 0.1264 0.1123 -0.0018 -0.0184 0.0007  94   HIS   B ND1 
5484 C  CD2 . HIS   B 94  ? 0.1292 0.1293 0.1277 -0.0033 -0.0122 0.0058  94   HIS   B CD2 
5485 C  CE1 . HIS   B 94  ? 0.1385 0.1286 0.1191 -0.0084 -0.0174 0.0050  94   HIS   B CE1 
5486 N  NE2 . HIS   B 94  ? 0.1309 0.1351 0.1282 -0.0149 -0.0125 0.0043  94   HIS   B NE2 
5494 N  N   . VAL   B 95  ? 0.1238 0.1215 0.1205 -0.0012 0.0011  0.0094  95   VAL   B N   
5495 C  CA  . VAL   B 95  ? 0.1267 0.1275 0.1195 0.0025  -0.0018 0.0099  95   VAL   B CA  
5496 C  C   . VAL   B 95  ? 0.1371 0.1301 0.1134 0.0001  0.0107  0.0083  95   VAL   B C   
5497 O  O   . VAL   B 95  ? 0.1350 0.1270 0.1371 0.0086  0.0089  0.0158  95   VAL   B O   
5498 C  CB  . VAL   B 95  ? 0.1343 0.1267 0.1229 -0.0049 -0.0088 0.0056  95   VAL   B CB  
5499 C  CG1 . VAL   B 95  ? 0.1466 0.1360 0.1359 -0.0107 -0.0010 0.0078  95   VAL   B CG1 
5500 C  CG2 . VAL   B 95  ? 0.1356 0.1277 0.1249 0.0033  -0.0121 0.0061  95   VAL   B CG2 
5510 N  N   . VAL   B 96  ? 0.1506 0.1294 0.1161 0.0094  0.0086  0.0174  96   VAL   B N   
5511 C  CA  . VAL   B 96  ? 0.1528 0.1454 0.1108 0.0097  0.0065  0.0199  96   VAL   B CA  
5512 C  C   . VAL   B 96  ? 0.1531 0.1456 0.1275 0.0126  0.0180  0.0155  96   VAL   B C   
5513 O  O   . VAL   B 96  ? 0.1521 0.1545 0.1527 0.0021  0.0164  0.0021  96   VAL   B O   
5514 C  CB  . VAL   B 96  ? 0.1529 0.1685 0.1163 0.0110  0.0149  0.0096  96   VAL   B CB  
5515 C  CG1 . VAL   B 96  ? 0.1571 0.1808 0.1308 0.0166  0.0171  0.0159  96   VAL   B CG1 
5516 C  CG2 . VAL   B 96  ? 0.1679 0.1721 0.1335 0.0107  0.0091  0.0041  96   VAL   B CG2 
5526 N  N   . GLY   B 97  ? 0.1571 0.1493 0.1219 0.0096  0.0101  0.0214  97   GLY   B N   
5527 C  CA  . GLY   B 97  ? 0.1787 0.1484 0.1325 0.0043  0.0087  0.0207  97   GLY   B CA  
5528 C  C   . GLY   B 97  ? 0.1975 0.1554 0.1451 0.0168  0.0117  0.0218  97   GLY   B C   
5529 O  O   . GLY   B 97  ? 0.2115 0.1631 0.1406 0.0143  0.0130  0.0156  97   GLY   B O   
5533 N  N   . PRO   B 98  ? 0.2099 0.1607 0.1657 0.0159  0.0448  0.0334  98   PRO   B N   
5534 C  CA  . PRO   B 98  ? 0.2270 0.1754 0.1733 0.0279  0.0608  0.0314  98   PRO   B CA  
5535 C  C   . PRO   B 98  ? 0.2426 0.1796 0.1515 0.0462  0.0602  0.0574  98   PRO   B C   
5536 O  O   . PRO   B 98  ? 0.2291 0.1792 0.1720 0.0410  0.0592  0.0505  98   PRO   B O   
5537 C  CB  . PRO   B 98  ? 0.2158 0.1852 0.2048 0.0180  0.0711  0.0345  98   PRO   B CB  
5538 C  CG  . PRO   B 98  ? 0.2070 0.1830 0.2068 0.0166  0.0657  0.0439  98   PRO   B CG  
5539 C  CD  . PRO   B 98  ? 0.1907 0.1670 0.1975 0.0214  0.0578  0.0485  98   PRO   B CD  
5547 N  N   . ASN   B 99  ? 0.2614 0.2022 0.1555 0.0656  0.0611  0.0432  99   ASN   B N   
5548 C  CA  . ASN   B 99  ? 0.2817 0.2142 0.1560 0.0783  0.0574  0.0600  99   ASN   B CA  
5549 C  C   . ASN   B 99  ? 0.3060 0.2468 0.2024 0.0805  0.0909  0.0844  99   ASN   B C   
5550 O  O   . ASN   B 99  ? 0.3238 0.2488 0.2082 0.0871  0.0820  0.0828  99   ASN   B O   
5551 C  CB  . ASN   B 99  ? 0.2878 0.2096 0.1646 0.0802  0.0410  0.0502  99   ASN   B CB  
5552 C  CG  . ASN   B 99  ? 0.2891 0.2171 0.1802 0.0730  0.0342  0.0466  99   ASN   B CG  
5553 O  OD1 . ASN   B 99  ? 0.2924 0.2153 0.2121 0.0770  0.0327  0.0583  99   ASN   B OD1 
5554 N  ND2 . ASN   B 99  ? 0.2847 0.2176 0.1897 0.0738  0.0049  0.0312  99   ASN   B ND2 
5561 N  N   A VAL   B 100 ? 0.3196 0.2610 0.2587 0.0660  0.0955  0.1155  100  VAL   B N   
5562 N  N   B VAL   B 100 ? 0.3225 0.2610 0.2562 0.0669  0.0840  0.1059  100  VAL   B N   
5563 C  CA  A VAL   B 100 ? 0.3401 0.2786 0.3173 0.0538  0.0912  0.1342  100  VAL   B CA  
5564 C  CA  B VAL   B 100 ? 0.3427 0.2769 0.3089 0.0550  0.0734  0.1202  100  VAL   B CA  
5565 C  C   A VAL   B 100 ? 0.3597 0.2853 0.2985 0.0580  0.0883  0.1529  100  VAL   B C   
5566 C  C   B VAL   B 100 ? 0.3608 0.2839 0.3008 0.0579  0.0713  0.1401  100  VAL   B C   
5567 O  O   A VAL   B 100 ? 0.3676 0.3026 0.3103 0.0553  0.1015  0.1413  100  VAL   B O   
5568 O  O   B VAL   B 100 ? 0.3660 0.2941 0.3086 0.0544  0.0760  0.1309  100  VAL   B O   
5569 C  CB  A VAL   B 100 ? 0.3477 0.2935 0.3963 0.0309  0.0794  0.1372  100  VAL   B CB  
5570 C  CB  B VAL   B 100 ? 0.3481 0.2877 0.3677 0.0371  0.0615  0.1183  100  VAL   B CB  
5571 C  CG1 A VAL   B 100 ? 0.3513 0.2986 0.4219 0.0272  0.0747  0.1396  100  VAL   B CG1 
5572 C  CG1 B VAL   B 100 ? 0.3505 0.2913 0.3857 0.0337  0.0574  0.1202  100  VAL   B CG1 
5573 C  CG2 A VAL   B 100 ? 0.3493 0.2993 0.4166 0.0206  0.0786  0.1407  100  VAL   B CG2 
5574 C  CG2 B VAL   B 100 ? 0.3496 0.2918 0.3848 0.0294  0.0592  0.1181  100  VAL   B CG2 
5593 N  N   . ASN   B 101 ? 0.3749 0.2868 0.2956 0.0662  0.0620  0.1532  101  ASN   B N   
5594 C  CA  . ASN   B 101 ? 0.4180 0.3098 0.3036 0.0627  0.0299  0.1556  101  ASN   B CA  
5595 C  C   . ASN   B 101 ? 0.4770 0.3608 0.3122 0.0537  0.0177  0.1515  101  ASN   B C   
5596 O  O   . ASN   B 101 ? 0.4808 0.3692 0.3284 0.0606  0.0235  0.1248  101  ASN   B O   
5597 C  CB  . ASN   B 101 ? 0.4058 0.2938 0.3170 0.0547  0.0238  0.1345  101  ASN   B CB  
5598 C  CG  . ASN   B 101 ? 0.3943 0.2739 0.3192 0.0474  0.0244  0.1302  101  ASN   B CG  
5599 O  OD1 . ASN   B 101 ? 0.3924 0.2750 0.3445 0.0351  0.0439  0.1203  101  ASN   B OD1 
5600 N  ND2 . ASN   B 101 ? 0.3894 0.2719 0.3099 0.0469  0.0185  0.1167  101  ASN   B ND2 
5608 N  N   A LYS   B 102 ? 0.5051 0.3858 0.3282 0.0422  0.0186  0.1468  102  LYS   B N   
5609 N  N   B LYS   B 102 ? 0.5013 0.3866 0.3322 0.0439  0.0151  0.1414  102  LYS   B N   
5610 C  CA  A LYS   B 102 ? 0.5302 0.4182 0.3627 0.0285  0.0226  0.1209  102  LYS   B CA  
5611 C  CA  B LYS   B 102 ? 0.5228 0.4158 0.3635 0.0333  0.0163  0.1194  102  LYS   B CA  
5612 C  C   A LYS   B 102 ? 0.5289 0.4234 0.3358 0.0312  0.0258  0.1272  102  LYS   B C   
5613 C  C   B LYS   B 102 ? 0.5239 0.4219 0.3419 0.0330  0.0245  0.1263  102  LYS   B C   
5614 O  O   A LYS   B 102 ? 0.5368 0.4281 0.3440 0.0323  0.0122  0.1233  102  LYS   B O   
5615 O  O   B LYS   B 102 ? 0.5298 0.4259 0.3473 0.0334  0.0147  0.1251  102  LYS   B O   
5616 C  CB  A LYS   B 102 ? 0.5523 0.4434 0.4311 0.0131  0.0331  0.0815  102  LYS   B CB  
5617 C  CB  B LYS   B 102 ? 0.5395 0.4368 0.4204 0.0238  0.0170  0.0852  102  LYS   B CB  
5618 C  CG  A LYS   B 102 ? 0.5705 0.4651 0.4970 0.0006  0.0444  0.0432  102  LYS   B CG  
5619 C  CG  B LYS   B 102 ? 0.5528 0.4545 0.4747 0.0165  0.0190  0.0522  102  LYS   B CG  
5620 C  CD  A LYS   B 102 ? 0.5864 0.4830 0.5590 -0.0088 0.0551  0.0133  102  LYS   B CD  
5621 C  CD  B LYS   B 102 ? 0.5641 0.4690 0.5249 0.0112  0.0221  0.0257  102  LYS   B CD  
5622 C  CE  A LYS   B 102 ? 0.5975 0.4954 0.6056 -0.0159 0.0622  -0.0088 102  LYS   B CE  
5623 C  CE  B LYS   B 102 ? 0.5720 0.4792 0.5622 0.0074  0.0238  0.0061  102  LYS   B CE  
5624 N  NZ  A LYS   B 102 ? 0.6036 0.5024 0.6317 -0.0191 0.0647  -0.0218 102  LYS   B NZ  
5625 N  NZ  B LYS   B 102 ? 0.5763 0.4849 0.5839 0.0056  0.0239  -0.0050 102  LYS   B NZ  
5652 N  N   . GLY   B 103 ? 0.5164 0.4217 0.3285 0.0329  0.0456  0.1253  103  GLY   B N   
5653 C  CA  . GLY   B 103 ? 0.4952 0.4212 0.3420 0.0383  0.0789  0.1036  103  GLY   B CA  
5654 C  C   . GLY   B 103 ? 0.4696 0.4160 0.3412 0.0410  0.1082  0.0832  103  GLY   B C   
5655 O  O   . GLY   B 103 ? 0.4772 0.4228 0.3557 0.0394  0.1156  0.0828  103  GLY   B O   
5660 N  N   A GLU   B 104 ? 0.4485 0.4067 0.3214 0.0509  0.1316  0.0703  104  GLU   B N   
5661 N  N   B GLU   B 104 ? 0.4551 0.4103 0.3415 0.0362  0.1020  0.0666  104  GLU   B N   
5662 C  CA  A GLU   B 104 ? 0.4259 0.3957 0.2986 0.0648  0.1457  0.0538  104  GLU   B CA  
5663 C  CA  B GLU   B 104 ? 0.4394 0.4031 0.3355 0.0330  0.0923  0.0471  104  GLU   B CA  
5664 C  C   A GLU   B 104 ? 0.4259 0.3954 0.3150 0.0457  0.1784  0.0612  104  GLU   B C   
5665 C  C   B GLU   B 104 ? 0.4349 0.4013 0.3514 0.0243  0.1068  0.0458  104  GLU   B C   
5666 O  O   A GLU   B 104 ? 0.4281 0.3991 0.3460 0.0407  0.1760  0.0654  104  GLU   B O   
5667 O  O   B GLU   B 104 ? 0.4357 0.4026 0.3653 0.0225  0.1067  0.0462  104  GLU   B O   
5668 C  CB  A GLU   B 104 ? 0.4106 0.3826 0.2890 0.0990  0.1053  0.0186  104  GLU   B CB  
5669 C  CB  B GLU   B 104 ? 0.4311 0.3959 0.3227 0.0383  0.0626  0.0228  104  GLU   B CB  
5670 C  CG  A GLU   B 104 ? 0.3965 0.3741 0.2729 0.1293  0.0574  -0.0192 104  GLU   B CG  
5671 C  CG  B GLU   B 104 ? 0.4236 0.3905 0.3078 0.0430  0.0306  -0.0038 104  GLU   B CG  
5672 C  CD  A GLU   B 104 ? 0.3857 0.3685 0.2503 0.1512  0.0154  -0.0390 104  GLU   B CD  
5673 C  CD  B GLU   B 104 ? 0.4180 0.3863 0.2922 0.0450  0.0049  -0.0224 104  GLU   B CD  
5674 O  OE1 A GLU   B 104 ? 0.3729 0.3595 0.1953 0.1637  0.0154  -0.0438 104  GLU   B OE1 
5675 O  OE1 B GLU   B 104 ? 0.4130 0.3820 0.2715 0.0445  0.0005  -0.0267 104  GLU   B OE1 
5676 O  OE2 A GLU   B 104 ? 0.3874 0.3744 0.2616 0.1535  -0.0133 -0.0489 104  GLU   B OE2 
5677 O  OE2 B GLU   B 104 ? 0.4183 0.3875 0.2910 0.0454  -0.0110 -0.0327 104  GLU   B OE2 
5690 N  N   A ASP   B 105 ? 0.4192 0.3899 0.3114 0.0320  0.2036  0.0638  105  ASP   B N   
5691 N  N   B ASP   B 105 ? 0.4278 0.3972 0.3516 0.0169  0.1181  0.0438  105  ASP   B N   
5692 C  CA  A ASP   B 105 ? 0.4159 0.3852 0.3379 0.0211  0.2155  0.0477  105  ASP   B CA  
5693 C  CA  B ASP   B 105 ? 0.4223 0.3932 0.3653 0.0108  0.1232  0.0350  105  ASP   B CA  
5694 C  C   A ASP   B 105 ? 0.3942 0.3502 0.3059 0.0083  0.2003  0.0463  105  ASP   B C   
5695 C  C   B ASP   B 105 ? 0.4104 0.3755 0.3372 0.0023  0.1255  0.0309  105  ASP   B C   
5696 O  O   A ASP   B 105 ? 0.3796 0.3418 0.2954 0.0105  0.1931  0.0463  105  ASP   B O   
5697 O  O   B ASP   B 105 ? 0.4083 0.3722 0.3234 0.0025  0.1304  0.0345  105  ASP   B O   
5698 C  CB  A ASP   B 105 ? 0.4286 0.4092 0.4283 0.0269  0.2201  0.0259  105  ASP   B CB  
5699 C  CB  B ASP   B 105 ? 0.4265 0.4043 0.4119 0.0145  0.1230  0.0288  105  ASP   B CB  
5700 C  CG  A ASP   B 105 ? 0.4375 0.4278 0.5082 0.0288  0.2303  0.0098  105  ASP   B CG  
5701 C  CG  B ASP   B 105 ? 0.4300 0.4129 0.4566 0.0156  0.1261  0.0250  105  ASP   B CG  
5702 O  OD1 A ASP   B 105 ? 0.4368 0.4338 0.5209 0.0227  0.2449  0.0150  105  ASP   B OD1 
5703 O  OD1 B ASP   B 105 ? 0.4301 0.4161 0.4682 0.0128  0.1291  0.0276  105  ASP   B OD1 
5704 O  OD2 A ASP   B 105 ? 0.4435 0.4356 0.5557 0.0340  0.2196  -0.0030 105  ASP   B OD2 
5705 O  OD2 B ASP   B 105 ? 0.4308 0.4167 0.4758 0.0166  0.1261  0.0233  105  ASP   B OD2 
5714 N  N   A ILE   B 106 ? 0.3888 0.3191 0.3117 -0.0039 0.1964  0.0549  106  ILE   B N   
5715 N  N   B ILE   B 106 ? 0.3989 0.3586 0.3321 -0.0040 0.1182  0.0258  106  ILE   B N   
5716 C  CA  A ILE   B 106 ? 0.3695 0.2872 0.3312 -0.0175 0.1938  0.0466  106  ILE   B CA  
5717 C  CA  B ILE   B 106 ? 0.3832 0.3424 0.3369 -0.0103 0.1142  0.0171  106  ILE   B CA  
5718 C  C   A ILE   B 106 ? 0.3367 0.2667 0.3254 -0.0135 0.1920  0.0329  106  ILE   B C   
5719 C  C   B ILE   B 106 ? 0.3614 0.3300 0.3376 -0.0080 0.1134  0.0081  106  ILE   B C   
5720 O  O   A ILE   B 106 ? 0.3275 0.2337 0.3224 -0.0171 0.1843  0.0356  106  ILE   B O   
5721 O  O   B ILE   B 106 ? 0.3601 0.3221 0.3382 -0.0105 0.1098  0.0052  106  ILE   B O   
5722 C  CB  A ILE   B 106 ? 0.3853 0.2826 0.3497 -0.0332 0.1859  0.0504  106  ILE   B CB  
5723 C  CB  B ILE   B 106 ? 0.3896 0.3416 0.3418 -0.0181 0.1105  0.0162  106  ILE   B CB  
5724 C  CG1 A ILE   B 106 ? 0.3936 0.2852 0.3580 -0.0304 0.1712  0.0367  106  ILE   B CG1 
5725 C  CG1 B ILE   B 106 ? 0.3929 0.3418 0.3438 -0.0176 0.1039  0.0137  106  ILE   B CG1 
5726 C  CG2 A ILE   B 106 ? 0.3888 0.2847 0.3676 -0.0429 0.1873  0.0537  106  ILE   B CG2 
5727 C  CG2 B ILE   B 106 ? 0.3915 0.3436 0.3512 -0.0222 0.1104  0.0160  106  ILE   B CG2 
5728 C  CD1 A ILE   B 106 ? 0.3974 0.2859 0.3544 -0.0282 0.1640  0.0341  106  ILE   B CD1 
5729 C  CD1 B ILE   B 106 ? 0.3944 0.3413 0.3445 -0.0169 0.0994  0.0135  106  ILE   B CD1 
5752 N  N   A GLN   B 107 ? 0.3195 0.2820 0.3428 -0.0150 0.1882  0.0278  107  GLN   B N   
5753 N  N   B GLN   B 107 ? 0.3433 0.3267 0.3501 -0.0059 0.1119  0.0058  107  GLN   B N   
5754 C  CA  A GLN   B 107 ? 0.2956 0.2959 0.3567 -0.0232 0.1780  0.0276  107  GLN   B CA  
5755 C  CA  B GLN   B 107 ? 0.3233 0.3217 0.3594 -0.0058 0.1079  0.0089  107  GLN   B CA  
5756 C  C   A GLN   B 107 ? 0.2680 0.2732 0.3301 -0.0104 0.1410  0.0172  107  GLN   B C   
5757 C  C   B GLN   B 107 ? 0.2873 0.2911 0.3264 0.0023  0.1082  0.0085  107  GLN   B C   
5758 O  O   A GLN   B 107 ? 0.2576 0.2681 0.3703 0.0011  0.1076  -0.0097 107  GLN   B O   
5759 O  O   B GLN   B 107 ? 0.2839 0.2917 0.3460 0.0068  0.0911  -0.0067 107  GLN   B O   
5760 C  CB  A GLN   B 107 ? 0.3223 0.3356 0.4305 -0.0287 0.1551  0.0302  107  GLN   B CB  
5761 C  CB  B GLN   B 107 ? 0.3437 0.3469 0.4141 -0.0089 0.0926  0.0117  107  GLN   B CB  
5762 C  CG  A GLN   B 107 ? 0.3529 0.3711 0.5015 -0.0277 0.1175  0.0277  107  GLN   B CG  
5763 C  CG  B GLN   B 107 ? 0.3632 0.3691 0.4665 -0.0095 0.0732  0.0128  107  GLN   B CG  
5764 C  CD  A GLN   B 107 ? 0.3750 0.3970 0.5558 -0.0291 0.0902  0.0294  107  GLN   B CD  
5765 C  CD  B GLN   B 107 ? 0.3779 0.3856 0.5086 -0.0109 0.0582  0.0152  107  GLN   B CD  
5766 O  OE1 A GLN   B 107 ? 0.3837 0.4070 0.5757 -0.0281 0.0863  0.0279  107  GLN   B OE1 
5767 O  OE1 B GLN   B 107 ? 0.3832 0.3919 0.5228 -0.0110 0.0575  0.0156  107  GLN   B OE1 
5768 N  NE2 A GLN   B 107 ? 0.3851 0.4050 0.5751 -0.0279 0.0765  0.0325  107  GLN   B NE2 
5769 N  NE2 B GLN   B 107 ? 0.3844 0.3911 0.5246 -0.0103 0.0506  0.0170  107  GLN   B NE2 
5786 N  N   . LEU   B 108 ? 0.2524 0.2596 0.2883 0.0157  0.1185  0.0193  108  LEU   B N   
5787 C  CA  . LEU   B 108 ? 0.2303 0.2364 0.2399 0.0323  0.0822  0.0357  108  LEU   B CA  
5788 C  C   . LEU   B 108 ? 0.1929 0.1932 0.2230 0.0309  0.0536  0.0349  108  LEU   B C   
5789 O  O   . LEU   B 108 ? 0.1926 0.1833 0.2065 0.0250  0.0346  0.0282  108  LEU   B O   
5790 C  CB  . LEU   B 108 ? 0.2522 0.2638 0.2130 0.0337  0.0858  0.0394  108  LEU   B CB  
5791 C  CG  . LEU   B 108 ? 0.2635 0.2965 0.2259 0.0382  0.0703  0.0165  108  LEU   B CG  
5792 C  CD1 . LEU   B 108 ? 0.2700 0.3137 0.2226 0.0344  0.0684  0.0178  108  LEU   B CD1 
5793 C  CD2 . LEU   B 108 ? 0.2710 0.3044 0.2300 0.0430  0.0586  0.0016  108  LEU   B CD2 
5806 N  N   . LEU   B 109 ? 0.1791 0.1671 0.2185 0.0223  0.0458  0.0259  109  LEU   B N   
5807 C  CA  . LEU   B 109 ? 0.1605 0.1444 0.2253 0.0126  0.0406  0.0264  109  LEU   B CA  
5808 C  C   . LEU   B 109 ? 0.1541 0.1348 0.2260 0.0041  0.0415  0.0222  109  LEU   B C   
5809 O  O   . LEU   B 109 ? 0.1492 0.1353 0.2172 0.0026  0.0350  0.0307  109  LEU   B O   
5810 C  CB  . LEU   B 109 ? 0.1716 0.1409 0.2244 0.0058  0.0319  0.0357  109  LEU   B CB  
5811 C  CG  . LEU   B 109 ? 0.1681 0.1391 0.2205 0.0071  0.0211  0.0209  109  LEU   B CG  
5812 C  CD1 . LEU   B 109 ? 0.1601 0.1504 0.1949 0.0062  0.0200  0.0173  109  LEU   B CD1 
5813 C  CD2 . LEU   B 109 ? 0.1862 0.1424 0.2413 0.0042  0.0173  0.0213  109  LEU   B CD2 
5825 N  N   . LYS   B 110 ? 0.1476 0.1320 0.2103 -0.0024 0.0319  0.0188  110  LYS   B N   
5826 C  CA  . LYS   B 110 ? 0.1470 0.1277 0.2136 -0.0053 0.0373  0.0123  110  LYS   B CA  
5827 C  C   . LYS   B 110 ? 0.1380 0.1304 0.2184 -0.0015 0.0337  0.0089  110  LYS   B C   
5828 O  O   . LYS   B 110 ? 0.1368 0.1292 0.2142 -0.0037 0.0243  0.0067  110  LYS   B O   
5829 C  CB  . LYS   B 110 ? 0.1482 0.1288 0.2283 -0.0018 0.0358  0.0102  110  LYS   B CB  
5830 C  CG  . LYS   B 110 ? 0.1475 0.1360 0.2346 -0.0076 0.0210  0.0238  110  LYS   B CG  
5831 C  CD  . LYS   B 110 ? 0.1532 0.1398 0.2423 -0.0057 0.0156  0.0169  110  LYS   B CD  
5832 C  CE  . LYS   B 110 ? 0.1522 0.1582 0.2623 -0.0015 0.0138  0.0044  110  LYS   B CE  
5833 N  NZ  . LYS   B 110 ? 0.1495 0.1711 0.2574 0.0030  0.0056  -0.0021 110  LYS   B NZ  
5847 N  N   . SER   B 111 ? 0.1460 0.1308 0.2089 -0.0019 0.0268  0.0094  111  SER   B N   
5848 C  CA  . SER   B 111 ? 0.1527 0.1360 0.1965 0.0011  0.0266  0.0122  111  SER   B CA  
5849 C  C   . SER   B 111 ? 0.1503 0.1282 0.1792 -0.0005 0.0216  0.0061  111  SER   B C   
5850 O  O   . SER   B 111 ? 0.1445 0.1326 0.2005 -0.0020 0.0132  0.0086  111  SER   B O   
5851 C  CB  . SER   B 111 ? 0.1659 0.1595 0.2019 0.0025  0.0414  0.0215  111  SER   B CB  
5852 O  OG  . SER   B 111 ? 0.1881 0.1926 0.2080 0.0063  0.0473  0.0234  111  SER   B OG  
5858 N  N   . ALA   B 112 ? 0.1394 0.1336 0.1916 0.0067  0.0283  0.0179  112  ALA   B N   
5859 C  CA  . ALA   B 112 ? 0.1362 0.1417 0.1734 0.0011  0.0096  0.0045  112  ALA   B CA  
5860 C  C   . ALA   B 112 ? 0.1276 0.1329 0.1674 0.0030  0.0100  0.0048  112  ALA   B C   
5861 O  O   . ALA   B 112 ? 0.1298 0.1339 0.1811 -0.0005 0.0163  0.0033  112  ALA   B O   
5862 C  CB  . ALA   B 112 ? 0.1386 0.1458 0.1815 0.0016  0.0115  0.0184  112  ALA   B CB  
5868 N  N   . TYR   B 113 ? 0.1288 0.1239 0.1783 -0.0020 0.0189  0.0086  113  TYR   B N   
5869 C  CA  . TYR   B 113 ? 0.1226 0.1242 0.1741 -0.0002 0.0177  0.0019  113  TYR   B CA  
5870 C  C   . TYR   B 113 ? 0.1256 0.1148 0.1669 -0.0068 0.0094  0.0001  113  TYR   B C   
5871 O  O   . TYR   B 113 ? 0.1316 0.1195 0.1650 -0.0057 0.0102  -0.0012 113  TYR   B O   
5872 C  CB  . TYR   B 113 ? 0.1310 0.1120 0.1886 -0.0030 0.0173  0.0088  113  TYR   B CB  
5873 C  CG  . TYR   B 113 ? 0.1349 0.1178 0.1967 -0.0053 0.0103  0.0151  113  TYR   B CG  
5874 C  CD1 . TYR   B 113 ? 0.1367 0.1208 0.1974 -0.0060 0.0100  0.0180  113  TYR   B CD1 
5875 C  CD2 . TYR   B 113 ? 0.1436 0.1209 0.1944 -0.0065 0.0090  0.0089  113  TYR   B CD2 
5876 C  CE1 . TYR   B 113 ? 0.1387 0.1300 0.2010 -0.0029 0.0174  0.0072  113  TYR   B CE1 
5877 C  CE2 . TYR   B 113 ? 0.1469 0.1147 0.2040 0.0028  0.0164  0.0138  113  TYR   B CE2 
5878 C  CZ  . TYR   B 113 ? 0.1377 0.1242 0.2100 0.0039  0.0163  0.0060  113  TYR   B CZ  
5879 O  OH  . TYR   B 113 ? 0.1466 0.1197 0.2304 0.0140  0.0230  0.0041  113  TYR   B OH  
5889 N  N   . GLU   B 114 ? 0.1230 0.1149 0.1876 -0.0042 0.0217  0.0035  114  GLU   B N   
5890 C  CA  . GLU   B 114 ? 0.1223 0.1138 0.1799 0.0040  0.0071  0.0053  114  GLU   B CA  
5891 C  C   . GLU   B 114 ? 0.1247 0.1155 0.1663 -0.0019 0.0083  0.0093  114  GLU   B C   
5892 O  O   . GLU   B 114 ? 0.1191 0.1200 0.1810 0.0024  0.0036  0.0102  114  GLU   B O   
5893 C  CB  . GLU   B 114 ? 0.1260 0.1198 0.1886 0.0022  0.0174  0.0008  114  GLU   B CB  
5894 C  CG  . GLU   B 114 ? 0.1306 0.1183 0.1944 -0.0001 0.0169  0.0055  114  GLU   B CG  
5895 C  CD  . GLU   B 114 ? 0.1284 0.1248 0.2000 -0.0104 0.0169  0.0102  114  GLU   B CD  
5896 O  OE1 . GLU   B 114 ? 0.1262 0.1422 0.1949 -0.0066 0.0214  0.0128  114  GLU   B OE1 
5897 O  OE2 . GLU   B 114 ? 0.1350 0.1461 0.2189 -0.0155 0.0218  0.0066  114  GLU   B OE2 
5904 N  N   . ASN   B 115 ? 0.1274 0.1176 0.1632 -0.0059 0.0008  0.0066  115  ASN   B N   
5905 C  CA  . ASN   B 115 ? 0.1278 0.1205 0.1526 -0.0091 0.0082  0.0077  115  ASN   B CA  
5906 C  C   . ASN   B 115 ? 0.1246 0.1165 0.1601 -0.0084 0.0013  0.0013  115  ASN   B C   
5907 O  O   . ASN   B 115 ? 0.1365 0.1209 0.1569 -0.0097 0.0036  0.0004  115  ASN   B O   
5908 C  CB  . ASN   B 115 ? 0.1410 0.1314 0.1566 -0.0152 0.0092  0.0025  115  ASN   B CB  
5909 C  CG  . ASN   B 115 ? 0.1494 0.1416 0.1569 0.0022  0.0082  0.0020  115  ASN   B CG  
5910 O  OD1 . ASN   B 115 ? 0.1887 0.1501 0.1778 -0.0008 0.0104  -0.0108 115  ASN   B OD1 
5911 N  ND2 . ASN   B 115 ? 0.1400 0.1528 0.1594 -0.0014 0.0019  0.0108  115  ASN   B ND2 
5918 N  N   . PHE   B 116 ? 0.1260 0.1188 0.1482 -0.0044 0.0036  0.0022  116  PHE   B N   
5919 C  CA  . PHE   B 116 ? 0.1284 0.1222 0.1546 -0.0121 0.0002  0.0024  116  PHE   B CA  
5920 C  C   . PHE   B 116 ? 0.1307 0.1083 0.1529 -0.0094 -0.0010 0.0045  116  PHE   B C   
5921 O  O   . PHE   B 116 ? 0.1335 0.1259 0.1595 -0.0021 -0.0038 0.0055  116  PHE   B O   
5922 C  CB  . PHE   B 116 ? 0.1250 0.1139 0.1565 -0.0061 -0.0008 0.0044  116  PHE   B CB  
5923 C  CG  . PHE   B 116 ? 0.1181 0.1224 0.1513 -0.0065 0.0046  0.0059  116  PHE   B CG  
5924 C  CD1 . PHE   B 116 ? 0.1282 0.1264 0.1605 0.0004  0.0007  0.0044  116  PHE   B CD1 
5925 C  CD2 . PHE   B 116 ? 0.1270 0.1331 0.1444 -0.0039 0.0045  0.0007  116  PHE   B CD2 
5926 C  CE1 . PHE   B 116 ? 0.1323 0.1301 0.1663 -0.0025 -0.0075 0.0120  116  PHE   B CE1 
5927 C  CE2 . PHE   B 116 ? 0.1307 0.1257 0.1588 -0.0021 0.0045  0.0052  116  PHE   B CE2 
5928 C  CZ  . PHE   B 116 ? 0.1224 0.1315 0.1579 0.0030  -0.0034 0.0132  116  PHE   B CZ  
5938 N  N   . ASN   B 117 ? 0.1305 0.1147 0.1685 -0.0040 -0.0064 0.0053  117  ASN   B N   
5939 C  CA  . ASN   B 117 ? 0.1404 0.1182 0.1669 -0.0012 -0.0136 0.0002  117  ASN   B CA  
5940 C  C   . ASN   B 117 ? 0.1386 0.1197 0.1790 -0.0018 -0.0097 0.0032  117  ASN   B C   
5941 O  O   . ASN   B 117 ? 0.1411 0.1302 0.2067 -0.0088 -0.0265 0.0118  117  ASN   B O   
5942 C  CB  . ASN   B 117 ? 0.1333 0.1211 0.1731 -0.0045 -0.0040 0.0002  117  ASN   B CB  
5943 C  CG  . ASN   B 117 ? 0.1282 0.1259 0.1866 -0.0037 0.0041  -0.0109 117  ASN   B CG  
5944 O  OD1 . ASN   B 117 ? 0.1521 0.1298 0.1838 -0.0150 0.0055  -0.0073 117  ASN   B OD1 
5945 N  ND2 . ASN   B 117 ? 0.1319 0.1279 0.1816 -0.0061 0.0017  -0.0087 117  ASN   B ND2 
5952 N  N   . GLN   B 118 ? 0.1420 0.1140 0.1688 -0.0034 -0.0157 0.0051  118  GLN   B N   
5953 C  CA  . GLN   B 118 ? 0.1393 0.1177 0.1792 -0.0016 -0.0155 0.0010  118  GLN   B CA  
5954 C  C   . GLN   B 118 ? 0.1417 0.1161 0.1882 -0.0028 -0.0068 -0.0010 118  GLN   B C   
5955 O  O   . GLN   B 118 ? 0.1597 0.1230 0.2225 -0.0059 0.0035  0.0044  118  GLN   B O   
5956 C  CB  . GLN   B 118 ? 0.1492 0.1275 0.1954 0.0009  -0.0190 -0.0007 118  GLN   B CB  
5957 C  CG  . GLN   B 118 ? 0.1580 0.1250 0.1919 0.0064  -0.0128 -0.0083 118  GLN   B CG  
5958 C  CD  . GLN   B 118 ? 0.1653 0.1211 0.1818 0.0080  -0.0027 -0.0129 118  GLN   B CD  
5959 O  OE1 . GLN   B 118 ? 0.1723 0.1239 0.2124 0.0078  0.0101  0.0024  118  GLN   B OE1 
5960 N  NE2 . GLN   B 118 ? 0.1704 0.1251 0.1923 0.0009  -0.0122 0.0078  118  GLN   B NE2 
5969 N  N   . HIS   B 119 ? 0.1436 0.1243 0.1561 -0.0100 -0.0107 0.0109  119  HIS   B N   
5970 C  CA  . HIS   B 119 ? 0.1565 0.1324 0.1587 -0.0057 -0.0166 0.0134  119  HIS   B CA  
5971 C  C   . HIS   B 119 ? 0.1548 0.1342 0.1495 -0.0066 -0.0296 0.0092  119  HIS   B C   
5972 O  O   . HIS   B 119 ? 0.1656 0.1373 0.1664 -0.0303 -0.0191 0.0102  119  HIS   B O   
5973 C  CB  . HIS   B 119 ? 0.1614 0.1442 0.1498 -0.0008 -0.0195 0.0031  119  HIS   B CB  
5974 C  CG  . HIS   B 119 ? 0.1636 0.1631 0.1631 0.0083  -0.0348 -0.0095 119  HIS   B CG  
5975 N  ND1 . HIS   B 119 ? 0.1796 0.1810 0.2036 0.0013  -0.0462 -0.0348 119  HIS   B ND1 
5976 C  CD2 . HIS   B 119 ? 0.1822 0.1841 0.1715 0.0365  -0.0401 -0.0164 119  HIS   B CD2 
5977 C  CE1 . HIS   B 119 ? 0.1938 0.1969 0.2099 0.0187  -0.0573 -0.0422 119  HIS   B CE1 
5978 N  NE2 . HIS   B 119 ? 0.1981 0.2058 0.1865 0.0359  -0.0470 -0.0355 119  HIS   B NE2 
5986 N  N   . GLU   B 120 ? 0.1735 0.1400 0.1536 -0.0125 -0.0372 0.0193  120  GLU   B N   
5987 C  CA  . GLU   B 120 ? 0.2033 0.1527 0.1674 -0.0051 -0.0489 0.0267  120  GLU   B CA  
5988 C  C   . GLU   B 120 ? 0.1812 0.1447 0.1497 -0.0134 -0.0389 0.0233  120  GLU   B C   
5989 O  O   . GLU   B 120 ? 0.1704 0.1563 0.1524 -0.0130 -0.0337 0.0123  120  GLU   B O   
5990 C  CB  . GLU   B 120 ? 0.2641 0.1797 0.2424 0.0107  -0.0678 0.0459  120  GLU   B CB  
5991 C  CG  . GLU   B 120 ? 0.3137 0.2537 0.3441 0.0199  -0.0924 0.0599  120  GLU   B CG  
5992 C  CD  . GLU   B 120 ? 0.3541 0.3162 0.4498 0.0186  -0.0984 0.0712  120  GLU   B CD  
5993 O  OE1 . GLU   B 120 ? 0.3728 0.3383 0.4875 0.0103  -0.0936 0.0831  120  GLU   B OE1 
5994 O  OE2 . GLU   B 120 ? 0.3743 0.3392 0.5042 0.0179  -0.0998 0.0659  120  GLU   B OE2 
6001 N  N   . VAL   B 121 ? 0.1685 0.1382 0.1510 -0.0216 -0.0201 0.0189  121  VAL   B N   
6002 C  CA  . VAL   B 121 ? 0.1671 0.1502 0.1345 -0.0192 -0.0194 0.0131  121  VAL   B CA  
6003 C  C   . VAL   B 121 ? 0.1600 0.1462 0.1283 -0.0241 -0.0194 0.0134  121  VAL   B C   
6004 O  O   . VAL   B 121 ? 0.1695 0.1443 0.1491 -0.0352 -0.0271 0.0140  121  VAL   B O   
6005 C  CB  . VAL   B 121 ? 0.1886 0.1919 0.1469 -0.0088 -0.0245 0.0200  121  VAL   B CB  
6006 C  CG1 . VAL   B 121 ? 0.1944 0.2061 0.1853 -0.0198 -0.0155 0.0245  121  VAL   B CG1 
6007 C  CG2 . VAL   B 121 ? 0.2180 0.2165 0.1443 0.0006  -0.0220 0.0117  121  VAL   B CG2 
6017 N  N   . LEU   B 122 ? 0.1498 0.1375 0.1202 -0.0191 -0.0191 0.0062  122  LEU   B N   
6018 C  CA  . LEU   B 122 ? 0.1426 0.1450 0.1099 -0.0221 -0.0153 0.0053  122  LEU   B CA  
6019 C  C   . LEU   B 122 ? 0.1384 0.1356 0.1274 -0.0317 -0.0133 0.0074  122  LEU   B C   
6020 O  O   . LEU   B 122 ? 0.1520 0.1388 0.1656 -0.0322 -0.0212 0.0028  122  LEU   B O   
6021 C  CB  . LEU   B 122 ? 0.1686 0.1594 0.1527 0.0009  -0.0219 0.0104  122  LEU   B CB  
6022 C  CG  . LEU   B 122 ? 0.1523 0.1665 0.1610 -0.0112 -0.0077 0.0073  122  LEU   B CG  
6023 C  CD1 . LEU   B 122 ? 0.1608 0.1923 0.1555 -0.0217 -0.0112 0.0038  122  LEU   B CD1 
6024 C  CD2 . LEU   B 122 ? 0.1527 0.1635 0.1300 -0.0093 -0.0050 -0.0062 122  LEU   B CD2 
6036 N  N   . LEU   B 123 ? 0.1422 0.1266 0.1209 -0.0266 -0.0148 0.0090  123  LEU   B N   
6037 C  CA  . LEU   B 123 ? 0.1450 0.1297 0.1264 -0.0260 -0.0168 -0.0009 123  LEU   B CA  
6038 C  C   . LEU   B 123 ? 0.1397 0.1294 0.1232 -0.0242 -0.0082 0.0033  123  LEU   B C   
6039 O  O   . LEU   B 123 ? 0.1507 0.1286 0.1278 -0.0300 -0.0138 0.0039  123  LEU   B O   
6040 C  CB  . LEU   B 123 ? 0.1481 0.1327 0.1311 -0.0268 -0.0131 -0.0023 123  LEU   B CB  
6041 C  CG  . LEU   B 123 ? 0.1501 0.1390 0.1492 -0.0165 -0.0016 0.0064  123  LEU   B CG  
6042 C  CD1 . LEU   B 123 ? 0.1611 0.1396 0.1609 -0.0181 0.0071  -0.0125 123  LEU   B CD1 
6043 C  CD2 . LEU   B 123 ? 0.1578 0.1447 0.1624 -0.0178 0.0038  0.0133  123  LEU   B CD2 
6055 N  N   . ALA   B 124 ? 0.1393 0.1240 0.1183 -0.0195 -0.0002 -0.0016 124  ALA   B N   
6056 C  CA  . ALA   B 124 ? 0.1309 0.1186 0.1390 -0.0138 -0.0063 -0.0092 124  ALA   B CA  
6057 C  C   . ALA   B 124 ? 0.1271 0.1208 0.1331 -0.0152 -0.0073 -0.0064 124  ALA   B C   
6058 O  O   . ALA   B 124 ? 0.1417 0.1273 0.1375 -0.0160 -0.0061 -0.0025 124  ALA   B O   
6059 C  CB  . ALA   B 124 ? 0.1349 0.1278 0.1510 -0.0032 0.0066  -0.0029 124  ALA   B CB  
6065 N  N   . PRO   B 125 ? 0.1378 0.1234 0.1269 -0.0107 -0.0122 0.0072  125  PRO   B N   
6066 C  CA  . PRO   B 125 ? 0.1477 0.1245 0.1456 -0.0134 -0.0100 0.0162  125  PRO   B CA  
6067 C  C   . PRO   B 125 ? 0.1417 0.1179 0.1510 -0.0103 -0.0016 0.0119  125  PRO   B C   
6068 O  O   . PRO   B 125 ? 0.1436 0.1213 0.1792 -0.0082 0.0038  0.0152  125  PRO   B O   
6069 C  CB  . PRO   B 125 ? 0.1543 0.1520 0.1608 -0.0197 -0.0253 0.0347  125  PRO   B CB  
6070 C  CG  . PRO   B 125 ? 0.1627 0.1547 0.1347 -0.0257 -0.0262 0.0172  125  PRO   B CG  
6071 C  CD  . PRO   B 125 ? 0.1545 0.1371 0.1278 -0.0265 -0.0082 0.0054  125  PRO   B CD  
6079 N  N   . LEU   B 126 ? 0.1460 0.1199 0.1780 -0.0102 0.0157  0.0121  126  LEU   B N   
6080 C  CA  . LEU   B 126 ? 0.1556 0.1259 0.1853 -0.0117 0.0202  0.0141  126  LEU   B CA  
6081 C  C   . LEU   B 126 ? 0.1550 0.1377 0.1857 0.0026  0.0249  0.0157  126  LEU   B C   
6082 O  O   . LEU   B 126 ? 0.1758 0.1742 0.2027 0.0183  0.0012  -0.0069 126  LEU   B O   
6083 C  CB  . LEU   B 126 ? 0.1719 0.1289 0.2155 -0.0193 0.0282  0.0093  126  LEU   B CB  
6084 C  CG  . LEU   B 126 ? 0.1911 0.1406 0.2257 -0.0244 0.0292  -0.0049 126  LEU   B CG  
6085 C  CD1 . LEU   B 126 ? 0.2016 0.1458 0.2782 -0.0218 0.0196  -0.0189 126  LEU   B CD1 
6086 C  CD2 . LEU   B 126 ? 0.1893 0.1542 0.2195 -0.0331 0.0245  -0.0017 126  LEU   B CD2 
6098 N  N   . LEU   B 127 ? 0.1539 0.1265 0.1931 -0.0002 0.0315  0.0080  127  LEU   B N   
6099 C  CA  . LEU   B 127 ? 0.1513 0.1362 0.1976 -0.0051 0.0289  0.0229  127  LEU   B CA  
6100 C  C   . LEU   B 127 ? 0.1413 0.1314 0.2025 -0.0019 0.0236  0.0179  127  LEU   B C   
6101 O  O   . LEU   B 127 ? 0.1493 0.1325 0.2047 -0.0117 0.0111  0.0142  127  LEU   B O   
6102 C  CB  . LEU   B 127 ? 0.1659 0.1299 0.2000 0.0017  0.0228  0.0241  127  LEU   B CB  
6103 C  CG  . LEU   B 127 ? 0.1774 0.1290 0.2242 0.0041  0.0295  0.0123  127  LEU   B CG  
6104 C  CD1 . LEU   B 127 ? 0.1788 0.1353 0.2258 0.0103  0.0239  0.0089  127  LEU   B CD1 
6105 C  CD2 . LEU   B 127 ? 0.1788 0.1394 0.2392 -0.0053 0.0372  0.0234  127  LEU   B CD2 
6117 N  N   . SER   B 128 ? 0.1473 0.1268 0.1907 -0.0005 0.0083  0.0130  128  SER   B N   
6118 C  CA  . SER   B 128 ? 0.1574 0.1398 0.2037 0.0105  -0.0005 0.0230  128  SER   B CA  
6119 C  C   . SER   B 128 ? 0.1713 0.1433 0.2217 0.0106  -0.0246 0.0229  128  SER   B C   
6120 O  O   . SER   B 128 ? 0.1830 0.1473 0.2671 0.0057  -0.0224 0.0343  128  SER   B O   
6121 C  CB  . SER   B 128 ? 0.1625 0.1442 0.1903 0.0045  0.0100  0.0317  128  SER   B CB  
6122 O  OG  . SER   B 128 ? 0.1729 0.1608 0.1973 0.0138  0.0166  0.0328  128  SER   B OG  
6128 N  N   . ALA   B 129 ? 0.1935 0.1498 0.2481 0.0280  -0.0150 0.0054  129  ALA   B N   
6129 C  CA  . ALA   B 129 ? 0.2146 0.1564 0.2608 0.0338  -0.0132 -0.0105 129  ALA   B CA  
6130 C  C   . ALA   B 129 ? 0.1955 0.1488 0.2361 0.0244  0.0089  0.0019  129  ALA   B C   
6131 O  O   . ALA   B 129 ? 0.1794 0.1554 0.2259 0.0187  0.0072  0.0089  129  ALA   B O   
6132 C  CB  . ALA   B 129 ? 0.2367 0.1791 0.2888 0.0388  -0.0015 -0.0216 129  ALA   B CB  
6138 N  N   . GLY   B 130 ? 0.1871 0.1443 0.2437 0.0288  0.0160  -0.0048 130  GLY   B N   
6139 C  CA  . GLY   B 130 ? 0.1908 0.1561 0.2477 0.0270  0.0320  -0.0041 130  GLY   B CA  
6140 C  C   . GLY   B 130 ? 0.1961 0.1552 0.2499 0.0194  0.0213  0.0094  130  GLY   B C   
6141 O  O   . GLY   B 130 ? 0.2035 0.1678 0.2577 0.0204  0.0133  0.0191  130  GLY   B O   
6145 N  N   . ILE   B 131 ? 0.1817 0.1735 0.2548 0.0350  0.0171  0.0077  131  ILE   B N   
6146 C  CA  . ILE   B 131 ? 0.2075 0.1835 0.2591 0.0247  0.0117  0.0282  131  ILE   B CA  
6147 C  C   . ILE   B 131 ? 0.2144 0.1767 0.2221 0.0144  0.0095  0.0374  131  ILE   B C   
6148 O  O   . ILE   B 131 ? 0.2379 0.1954 0.2286 0.0183  -0.0083 0.0390  131  ILE   B O   
6149 C  CB  . ILE   B 131 ? 0.2070 0.2151 0.3000 0.0253  0.0066  0.0279  131  ILE   B CB  
6150 C  CG1 . ILE   B 131 ? 0.2136 0.2337 0.3103 0.0014  0.0057  0.0329  131  ILE   B CG1 
6151 C  CG2 . ILE   B 131 ? 0.2076 0.2369 0.3260 0.0326  0.0136  0.0164  131  ILE   B CG2 
6152 C  CD1 . ILE   B 131 ? 0.2277 0.2568 0.3320 -0.0155 -0.0049 0.0332  131  ILE   B CD1 
6164 N  N   . PHE   B 132 ? 0.2015 0.1621 0.2152 0.0146  0.0227  0.0231  132  PHE   B N   
6165 C  CA  . PHE   B 132 ? 0.2088 0.1656 0.2141 0.0058  0.0500  0.0175  132  PHE   B CA  
6166 C  C   . PHE   B 132 ? 0.2243 0.1770 0.2329 0.0065  0.0578  0.0180  132  PHE   B C   
6167 O  O   . PHE   B 132 ? 0.2414 0.2001 0.2600 0.0047  0.0675  0.0208  132  PHE   B O   
6168 C  CB  . PHE   B 132 ? 0.1960 0.1581 0.1909 0.0144  0.0468  0.0182  132  PHE   B CB  
6169 C  CG  . PHE   B 132 ? 0.1895 0.1597 0.1827 0.0166  0.0314  0.0240  132  PHE   B CG  
6170 C  CD1 . PHE   B 132 ? 0.2000 0.1661 0.2283 0.0103  0.0317  0.0207  132  PHE   B CD1 
6171 C  CD2 . PHE   B 132 ? 0.1974 0.1647 0.1623 0.0261  0.0220  0.0251  132  PHE   B CD2 
6172 C  CE1 . PHE   B 132 ? 0.1985 0.1674 0.2330 0.0103  0.0190  0.0242  132  PHE   B CE1 
6173 C  CE2 . PHE   B 132 ? 0.2068 0.1715 0.1602 0.0215  0.0160  0.0223  132  PHE   B CE2 
6174 C  CZ  . PHE   B 132 ? 0.2037 0.1697 0.2003 0.0175  -0.0013 0.0392  132  PHE   B CZ  
6184 N  N   . GLY   B 133 ? 0.2229 0.1665 0.2325 0.0086  0.0436  0.0357  133  GLY   B N   
6185 C  CA  . GLY   B 133 ? 0.2350 0.1773 0.2567 -0.0114 0.0440  0.0507  133  GLY   B CA  
6186 C  C   . GLY   B 133 ? 0.2409 0.1890 0.2634 -0.0296 0.0548  0.0519  133  GLY   B C   
6187 O  O   . GLY   B 133 ? 0.2597 0.2070 0.3100 -0.0449 0.0479  0.0618  133  GLY   B O   
6191 N  N   . ALA   B 134 ? 0.2200 0.1857 0.2492 -0.0242 0.0608  0.0262  134  ALA   B N   
6192 C  CA  . ALA   B 134 ? 0.2147 0.1783 0.2616 -0.0179 0.0615  0.0116  134  ALA   B CA  
6193 C  C   . ALA   B 134 ? 0.2261 0.1623 0.2560 -0.0129 0.0521  0.0282  134  ALA   B C   
6194 O  O   . ALA   B 134 ? 0.2278 0.1856 0.2628 -0.0045 0.0352  0.0237  134  ALA   B O   
6195 C  CB  . ALA   B 134 ? 0.2101 0.1789 0.2887 -0.0059 0.0464  0.0011  134  ALA   B CB  
6201 N  N   . ASP   B 135 ? 0.2462 0.1606 0.2578 -0.0147 0.0297  0.0333  135  ASP   B N   
6202 C  CA  . ASP   B 135 ? 0.2659 0.1538 0.2742 -0.0111 0.0173  0.0336  135  ASP   B CA  
6203 C  C   . ASP   B 135 ? 0.2397 0.1418 0.2592 -0.0042 0.0138  0.0333  135  ASP   B C   
6204 O  O   . ASP   B 135 ? 0.2283 0.1464 0.2662 -0.0041 0.0157  0.0348  135  ASP   B O   
6205 C  CB  . ASP   B 135 ? 0.3005 0.1683 0.3000 -0.0324 0.0105  0.0339  135  ASP   B CB  
6206 C  CG  . ASP   B 135 ? 0.3276 0.1725 0.3435 -0.0502 0.0065  0.0290  135  ASP   B CG  
6207 O  OD1 . ASP   B 135 ? 0.3326 0.1625 0.3407 -0.0334 0.0030  0.0245  135  ASP   B OD1 
6208 O  OD2 . ASP   B 135 ? 0.3500 0.2147 0.3982 -0.0686 0.0045  0.0125  135  ASP   B OD2 
6213 N  N   . PRO   B 136 ? 0.2311 0.1529 0.2613 0.0187  -0.0019 0.0279  136  PRO   B N   
6214 C  CA  . PRO   B 136 ? 0.2083 0.1472 0.2634 0.0151  -0.0042 0.0096  136  PRO   B CA  
6215 C  C   . PRO   B 136 ? 0.1856 0.1333 0.2677 0.0124  0.0026  0.0104  136  PRO   B C   
6216 O  O   . PRO   B 136 ? 0.1658 0.1303 0.2599 0.0071  0.0002  0.0141  136  PRO   B O   
6217 C  CB  . PRO   B 136 ? 0.2133 0.1683 0.2768 0.0312  -0.0088 0.0026  136  PRO   B CB  
6218 C  CG  . PRO   B 136 ? 0.2343 0.1760 0.2993 0.0339  -0.0042 0.0017  136  PRO   B CG  
6219 C  CD  . PRO   B 136 ? 0.2409 0.1664 0.2877 0.0360  0.0006  0.0140  136  PRO   B CD  
6227 N  N   . ILE   B 137 ? 0.2020 0.1236 0.2715 0.0071  -0.0053 0.0063  137  ILE   B N   
6228 C  CA  . ILE   B 137 ? 0.2097 0.1202 0.2891 -0.0027 -0.0017 0.0006  137  ILE   B CA  
6229 C  C   . ILE   B 137 ? 0.1943 0.1274 0.2837 -0.0084 0.0100  0.0086  137  ILE   B C   
6230 O  O   . ILE   B 137 ? 0.1809 0.1367 0.2777 -0.0088 0.0092  0.0092  137  ILE   B O   
6231 C  CB  . ILE   B 137 ? 0.2386 0.1277 0.3289 -0.0019 0.0015  0.0016  137  ILE   B CB  
6232 C  CG1 . ILE   B 137 ? 0.2669 0.1460 0.3707 0.0031  0.0031  -0.0119 137  ILE   B CG1 
6233 C  CG2 . ILE   B 137 ? 0.2467 0.1347 0.3277 -0.0299 -0.0009 0.0075  137  ILE   B CG2 
6234 C  CD1 . ILE   B 137 ? 0.2916 0.1752 0.4050 0.0109  -0.0030 -0.0073 137  ILE   B CD1 
6246 N  N   . HIS   B 138 ? 0.2003 0.1275 0.2752 -0.0121 0.0146  0.0142  138  HIS   B N   
6247 C  CA  . HIS   B 138 ? 0.2092 0.1403 0.2712 -0.0032 0.0371  0.0200  138  HIS   B CA  
6248 C  C   . HIS   B 138 ? 0.1915 0.1323 0.2521 -0.0019 0.0395  0.0259  138  HIS   B C   
6249 O  O   . HIS   B 138 ? 0.1845 0.1475 0.2726 -0.0002 0.0441  0.0339  138  HIS   B O   
6250 C  CB  . HIS   B 138 ? 0.2396 0.1482 0.2827 -0.0084 0.0626  0.0252  138  HIS   B CB  
6251 C  CG  . HIS   B 138 ? 0.2646 0.1697 0.2944 -0.0084 0.0843  0.0453  138  HIS   B CG  
6252 N  ND1 . HIS   B 138 ? 0.2740 0.1911 0.3320 -0.0065 0.0931  0.0347  138  HIS   B ND1 
6253 C  CD2 . HIS   B 138 ? 0.2818 0.1772 0.2927 -0.0030 0.0898  0.0314  138  HIS   B CD2 
6254 C  CE1 . HIS   B 138 ? 0.2813 0.1894 0.3251 -0.0023 0.0953  0.0346  138  HIS   B CE1 
6255 N  NE2 . HIS   B 138 ? 0.2895 0.1742 0.3015 0.0037  0.0948  0.0234  138  HIS   B NE2 
6263 N  N   . SER   B 139 ? 0.1852 0.1205 0.2499 0.0041  0.0280  0.0152  139  SER   B N   
6264 C  CA  . SER   B 139 ? 0.1781 0.1175 0.2400 0.0014  0.0263  0.0065  139  SER   B CA  
6265 C  C   . SER   B 139 ? 0.1466 0.1157 0.2352 0.0020  0.0310  0.0073  139  SER   B C   
6266 O  O   . SER   B 139 ? 0.1556 0.1206 0.2440 -0.0001 0.0132  0.0059  139  SER   B O   
6267 C  CB  . SER   B 139 ? 0.1807 0.1226 0.2374 0.0039  0.0087  0.0038  139  SER   B CB  
6268 O  OG  . SER   B 139 ? 0.1774 0.1255 0.2401 -0.0004 -0.0083 0.0168  139  SER   B OG  
6274 N  N   . LEU   B 140 ? 0.1509 0.1139 0.2407 -0.0022 0.0243  -0.0022 140  LEU   B N   
6275 C  CA  . LEU   B 140 ? 0.1523 0.1184 0.2415 -0.0035 0.0183  0.0032  140  LEU   B CA  
6276 C  C   . LEU   B 140 ? 0.1481 0.1187 0.2494 -0.0064 0.0123  -0.0060 140  LEU   B C   
6277 O  O   . LEU   B 140 ? 0.1491 0.1266 0.2348 -0.0048 0.0051  0.0028  140  LEU   B O   
6278 C  CB  . LEU   B 140 ? 0.1543 0.1188 0.2479 -0.0098 0.0247  -0.0020 140  LEU   B CB  
6279 C  CG  . LEU   B 140 ? 0.1567 0.1226 0.2447 -0.0078 0.0130  0.0068  140  LEU   B CG  
6280 C  CD1 . LEU   B 140 ? 0.1649 0.1390 0.2583 -0.0137 0.0265  0.0002  140  LEU   B CD1 
6281 C  CD2 . LEU   B 140 ? 0.1765 0.1307 0.2488 -0.0075 0.0115  -0.0064 140  LEU   B CD2 
6293 N  N   . ARG   B 141 ? 0.1434 0.1273 0.2655 -0.0124 0.0153  -0.0057 141  ARG   B N   
6294 C  CA  . ARG   B 141 ? 0.1415 0.1274 0.2967 -0.0167 0.0301  -0.0069 141  ARG   B CA  
6295 C  C   . ARG   B 141 ? 0.1338 0.1210 0.2785 -0.0112 0.0210  -0.0012 141  ARG   B C   
6296 O  O   . ARG   B 141 ? 0.1455 0.1264 0.2660 -0.0136 0.0179  -0.0122 141  ARG   B O   
6297 C  CB  . ARG   B 141 ? 0.1527 0.1414 0.3193 -0.0236 0.0360  -0.0061 141  ARG   B CB  
6298 C  CG  . ARG   B 141 ? 0.1862 0.1658 0.3360 -0.0282 0.0352  -0.0026 141  ARG   B CG  
6299 C  CD  . ARG   B 141 ? 0.2327 0.1927 0.3435 -0.0226 0.0142  -0.0099 141  ARG   B CD  
6300 N  NE  . ARG   B 141 ? 0.2479 0.1870 0.3339 -0.0334 0.0212  -0.0151 141  ARG   B NE  
6301 C  CZ  . ARG   B 141 ? 0.2566 0.1660 0.3061 -0.0265 0.0254  -0.0303 141  ARG   B CZ  
6302 N  NH1 . ARG   B 141 ? 0.2673 0.1595 0.2951 -0.0186 0.0230  -0.0197 141  ARG   B NH1 
6303 N  NH2 . ARG   B 141 ? 0.2689 0.1788 0.3214 -0.0135 0.0098  -0.0207 141  ARG   B NH2 
6317 N  N   . VAL   B 142 ? 0.1473 0.1217 0.2618 -0.0074 0.0177  -0.0052 142  VAL   B N   
6318 C  CA  . VAL   B 142 ? 0.1376 0.1234 0.2521 -0.0027 0.0251  0.0033  142  VAL   B CA  
6319 C  C   . VAL   B 142 ? 0.1351 0.1241 0.2475 -0.0032 0.0189  -0.0048 142  VAL   B C   
6320 O  O   . VAL   B 142 ? 0.1457 0.1193 0.2549 0.0001  0.0215  0.0009  142  VAL   B O   
6321 C  CB  . VAL   B 142 ? 0.1544 0.1336 0.2516 0.0009  0.0319  0.0099  142  VAL   B CB  
6322 C  CG1 . VAL   B 142 ? 0.1552 0.1287 0.2593 0.0024  0.0375  0.0031  142  VAL   B CG1 
6323 C  CG2 . VAL   B 142 ? 0.1788 0.1348 0.2642 0.0105  0.0287  0.0152  142  VAL   B CG2 
6333 N  N   . CYS   B 143 ? 0.1339 0.1217 0.2335 -0.0018 0.0148  0.0094  143  CYS   B N   
6334 C  CA  . CYS   B 143 ? 0.1336 0.1242 0.2306 -0.0091 0.0124  0.0037  143  CYS   B CA  
6335 C  C   . CYS   B 143 ? 0.1372 0.1275 0.2322 -0.0079 0.0136  -0.0044 143  CYS   B C   
6336 O  O   . CYS   B 143 ? 0.1331 0.1247 0.2388 -0.0047 0.0015  -0.0004 143  CYS   B O   
6337 C  CB  . CYS   B 143 ? 0.1399 0.1233 0.2292 -0.0097 0.0064  -0.0007 143  CYS   B CB  
6338 S  SG  . CYS   B 143 ? 0.1439 0.1443 0.2207 -0.0074 0.0138  0.0025  143  CYS   B SG  
6344 N  N   . VAL   B 144 ? 0.1410 0.1258 0.2388 -0.0054 0.0076  -0.0196 144  VAL   B N   
6345 C  CA  . VAL   B 144 ? 0.1469 0.1354 0.2724 -0.0152 -0.0042 -0.0208 144  VAL   B CA  
6346 C  C   . VAL   B 144 ? 0.1412 0.1332 0.2814 -0.0110 0.0006  -0.0055 144  VAL   B C   
6347 O  O   . VAL   B 144 ? 0.1518 0.1517 0.2973 0.0024  0.0026  0.0160  144  VAL   B O   
6348 C  CB  . VAL   B 144 ? 0.1679 0.1455 0.3335 -0.0124 -0.0173 -0.0313 144  VAL   B CB  
6349 C  CG1 . VAL   B 144 ? 0.1915 0.1809 0.3605 -0.0063 -0.0225 -0.0279 144  VAL   B CG1 
6350 C  CG2 . VAL   B 144 ? 0.1817 0.1512 0.3289 -0.0025 -0.0302 -0.0371 144  VAL   B CG2 
6360 N  N   . ASP   B 145 ? 0.1402 0.1300 0.2880 -0.0090 0.0088  -0.0177 145  ASP   B N   
6361 C  CA  . ASP   B 145 ? 0.1424 0.1341 0.3096 -0.0051 0.0194  -0.0111 145  ASP   B CA  
6362 C  C   . ASP   B 145 ? 0.1362 0.1399 0.2838 -0.0103 0.0149  -0.0058 145  ASP   B C   
6363 O  O   . ASP   B 145 ? 0.1353 0.1538 0.3433 -0.0149 0.0174  -0.0247 145  ASP   B O   
6364 C  CB  . ASP   B 145 ? 0.1495 0.1424 0.3490 -0.0153 0.0300  0.0036  145  ASP   B CB  
6365 C  CG  . ASP   B 145 ? 0.1724 0.1513 0.4035 -0.0290 0.0318  0.0047  145  ASP   B CG  
6366 O  OD1 . ASP   B 145 ? 0.1756 0.1566 0.4150 -0.0243 0.0006  0.0009  145  ASP   B OD1 
6367 O  OD2 . ASP   B 145 ? 0.1968 0.1618 0.4491 -0.0341 0.0520  0.0100  145  ASP   B OD2 
6372 N  N   . THR   B 146 ? 0.1274 0.1271 0.2367 -0.0099 0.0129  -0.0033 146  THR   B N   
6373 C  CA  . THR   B 146 ? 0.1345 0.1247 0.2276 -0.0034 0.0164  -0.0041 146  THR   B CA  
6374 C  C   . THR   B 146 ? 0.1351 0.1257 0.2114 -0.0026 0.0035  -0.0004 146  THR   B C   
6375 O  O   . THR   B 146 ? 0.1443 0.1230 0.2168 -0.0063 0.0015  0.0034  146  THR   B O   
6376 C  CB  . THR   B 146 ? 0.1374 0.1298 0.2327 -0.0031 0.0234  0.0003  146  THR   B CB  
6377 O  OG1 . THR   B 146 ? 0.1429 0.1274 0.2364 -0.0088 0.0225  0.0123  146  THR   B OG1 
6378 C  CG2 . THR   B 146 ? 0.1468 0.1368 0.2223 -0.0002 0.0169  -0.0012 146  THR   B CG2 
6386 N  N   . VAL   B 147 ? 0.1417 0.1306 0.1993 -0.0011 0.0166  0.0017  147  VAL   B N   
6387 C  CA  . VAL   B 147 ? 0.1383 0.1249 0.1994 -0.0116 0.0052  0.0008  147  VAL   B CA  
6388 C  C   . VAL   B 147 ? 0.1427 0.1300 0.2117 -0.0164 -0.0051 -0.0052 147  VAL   B C   
6389 O  O   . VAL   B 147 ? 0.1488 0.1373 0.2182 -0.0185 -0.0237 -0.0040 147  VAL   B O   
6390 C  CB  . VAL   B 147 ? 0.1393 0.1378 0.1819 -0.0086 -0.0026 -0.0013 147  VAL   B CB  
6391 C  CG1 . VAL   B 147 ? 0.1360 0.1514 0.1794 -0.0132 -0.0072 0.0010  147  VAL   B CG1 
6392 C  CG2 . VAL   B 147 ? 0.1462 0.1327 0.1895 -0.0143 0.0035  -0.0045 147  VAL   B CG2 
6402 N  N   . ARG   B 148 ? 0.1354 0.1280 0.2061 -0.0064 -0.0158 -0.0064 148  ARG   B N   
6403 C  CA  . ARG   B 148 ? 0.1398 0.1345 0.2010 -0.0107 -0.0221 -0.0155 148  ARG   B CA  
6404 C  C   . ARG   B 148 ? 0.1415 0.1450 0.1908 -0.0089 -0.0248 -0.0082 148  ARG   B C   
6405 O  O   . ARG   B 148 ? 0.1649 0.1740 0.1915 -0.0265 -0.0342 0.0039  148  ARG   B O   
6406 C  CB  . ARG   B 148 ? 0.1422 0.1461 0.2084 -0.0025 -0.0271 -0.0158 148  ARG   B CB  
6407 C  CG  . ARG   B 148 ? 0.1500 0.1616 0.2224 -0.0104 -0.0217 -0.0343 148  ARG   B CG  
6408 C  CD  . ARG   B 148 ? 0.1561 0.1788 0.2365 0.0073  -0.0200 -0.0348 148  ARG   B CD  
6409 N  NE  . ARG   B 148 ? 0.1600 0.1749 0.2210 0.0190  -0.0283 -0.0308 148  ARG   B NE  
6410 C  CZ  . ARG   B 148 ? 0.1527 0.1665 0.2037 0.0183  -0.0192 -0.0240 148  ARG   B CZ  
6411 N  NH1 . ARG   B 148 ? 0.1447 0.1710 0.2153 0.0017  0.0027  -0.0238 148  ARG   B NH1 
6412 N  NH2 . ARG   B 148 ? 0.1738 0.1516 0.1947 0.0211  -0.0171 -0.0150 148  ARG   B NH2 
6426 N  N   . THR   B 149 ? 0.1461 0.1351 0.1905 -0.0140 -0.0265 0.0023  149  THR   B N   
6427 C  CA  . THR   B 149 ? 0.1552 0.1387 0.1816 -0.0174 -0.0244 0.0095  149  THR   B CA  
6428 C  C   . THR   B 149 ? 0.1490 0.1385 0.1668 -0.0198 -0.0203 0.0063  149  THR   B C   
6429 O  O   . THR   B 149 ? 0.1623 0.1414 0.1771 -0.0236 -0.0136 0.0029  149  THR   B O   
6430 C  CB  . THR   B 149 ? 0.1580 0.1379 0.1829 -0.0182 -0.0225 -0.0003 149  THR   B CB  
6431 O  OG1 . THR   B 149 ? 0.1596 0.1399 0.1678 -0.0236 -0.0231 0.0034  149  THR   B OG1 
6432 C  CG2 . THR   B 149 ? 0.1692 0.1391 0.2031 -0.0129 -0.0189 0.0045  149  THR   B CG2 
6440 N  N   . ASN   B 150 ? 0.1580 0.1354 0.1627 -0.0152 -0.0274 -0.0034 150  ASN   B N   
6441 C  CA  . ASN   B 150 ? 0.1673 0.1517 0.1653 -0.0226 -0.0287 -0.0009 150  ASN   B CA  
6442 C  C   . ASN   B 150 ? 0.1558 0.1457 0.1597 -0.0133 -0.0308 -0.0022 150  ASN   B C   
6443 O  O   . ASN   B 150 ? 0.1606 0.1474 0.1860 -0.0244 -0.0386 -0.0020 150  ASN   B O   
6444 C  CB  . ASN   B 150 ? 0.1912 0.1908 0.1813 -0.0222 -0.0435 0.0104  150  ASN   B CB  
6445 C  CG  . ASN   B 150 ? 0.2185 0.2280 0.2162 -0.0271 -0.0429 0.0263  150  ASN   B CG  
6446 O  OD1 . ASN   B 150 ? 0.2262 0.2519 0.2129 -0.0373 -0.0592 0.0243  150  ASN   B OD1 
6447 N  ND2 . ASN   B 150 ? 0.2318 0.2467 0.2591 -0.0155 -0.0524 0.0700  150  ASN   B ND2 
6454 N  N   . VAL   B 151 ? 0.1481 0.1405 0.1666 -0.0190 -0.0266 0.0020  151  VAL   B N   
6455 C  CA  . VAL   B 151 ? 0.1496 0.1427 0.1681 -0.0250 -0.0172 0.0017  151  VAL   B CA  
6456 C  C   . VAL   B 151 ? 0.1500 0.1361 0.1611 -0.0328 -0.0197 -0.0042 151  VAL   B C   
6457 O  O   . VAL   B 151 ? 0.1572 0.1493 0.1841 -0.0265 -0.0022 -0.0169 151  VAL   B O   
6458 C  CB  . VAL   B 151 ? 0.1705 0.1535 0.1713 -0.0118 -0.0142 -0.0016 151  VAL   B CB  
6459 C  CG1 . VAL   B 151 ? 0.1789 0.1574 0.1969 -0.0176 0.0024  -0.0137 151  VAL   B CG1 
6460 C  CG2 . VAL   B 151 ? 0.1846 0.1720 0.1562 -0.0016 -0.0126 0.0122  151  VAL   B CG2 
6470 N  N   . TYR   B 152 ? 0.1491 0.1303 0.1514 -0.0254 -0.0153 -0.0045 152  TYR   B N   
6471 C  CA  . TYR   B 152 ? 0.1499 0.1516 0.1446 -0.0267 -0.0074 -0.0047 152  TYR   B CA  
6472 C  C   . TYR   B 152 ? 0.1466 0.1336 0.1321 -0.0235 -0.0069 -0.0113 152  TYR   B C   
6473 O  O   . TYR   B 152 ? 0.1569 0.1353 0.1488 -0.0263 -0.0105 -0.0028 152  TYR   B O   
6474 C  CB  . TYR   B 152 ? 0.1587 0.1628 0.1482 -0.0271 -0.0040 -0.0037 152  TYR   B CB  
6475 C  CG  . TYR   B 152 ? 0.1768 0.1720 0.1431 -0.0433 -0.0080 -0.0039 152  TYR   B CG  
6476 C  CD1 . TYR   B 152 ? 0.1843 0.1786 0.1389 -0.0319 -0.0218 0.0067  152  TYR   B CD1 
6477 C  CD2 . TYR   B 152 ? 0.2014 0.1902 0.1566 -0.0390 -0.0049 -0.0076 152  TYR   B CD2 
6478 C  CE1 . TYR   B 152 ? 0.2033 0.2017 0.1623 -0.0271 -0.0243 0.0205  152  TYR   B CE1 
6479 C  CE2 . TYR   B 152 ? 0.2121 0.2141 0.1493 -0.0400 -0.0132 -0.0150 152  TYR   B CE2 
6480 C  CZ  . TYR   B 152 ? 0.2179 0.2252 0.1474 -0.0342 -0.0328 0.0079  152  TYR   B CZ  
6481 O  OH  . TYR   B 152 ? 0.2470 0.2654 0.1786 -0.0225 -0.0343 0.0128  152  TYR   B OH  
6491 N  N   . LEU   B 153 ? 0.1494 0.1281 0.1519 -0.0275 -0.0041 -0.0099 153  LEU   B N   
6492 C  CA  . LEU   B 153 ? 0.1518 0.1229 0.1474 -0.0245 0.0048  -0.0071 153  LEU   B CA  
6493 C  C   . LEU   B 153 ? 0.1536 0.1258 0.1650 -0.0237 0.0005  -0.0121 153  LEU   B C   
6494 O  O   . LEU   B 153 ? 0.1594 0.1547 0.1764 -0.0157 -0.0009 -0.0386 153  LEU   B O   
6495 C  CB  . LEU   B 153 ? 0.1548 0.1273 0.1625 -0.0264 0.0047  -0.0097 153  LEU   B CB  
6496 C  CG  . LEU   B 153 ? 0.1469 0.1393 0.1728 -0.0222 0.0016  -0.0091 153  LEU   B CG  
6497 C  CD1 . LEU   B 153 ? 0.1563 0.1532 0.1854 -0.0311 0.0041  0.0053  153  LEU   B CD1 
6498 C  CD2 . LEU   B 153 ? 0.1501 0.1499 0.1868 -0.0270 0.0117  0.0026  153  LEU   B CD2 
6510 N  N   . ALA   B 154 ? 0.1500 0.1217 0.1751 -0.0079 -0.0021 -0.0096 154  ALA   B N   
6511 C  CA  . ALA   B 154 ? 0.1598 0.1401 0.1805 -0.0044 -0.0084 -0.0271 154  ALA   B CA  
6512 C  C   . ALA   B 154 ? 0.1778 0.1411 0.1839 0.0044  -0.0207 -0.0281 154  ALA   B C   
6513 O  O   . ALA   B 154 ? 0.2097 0.1453 0.2084 0.0065  -0.0086 -0.0051 154  ALA   B O   
6514 C  CB  . ALA   B 154 ? 0.1580 0.1638 0.2070 -0.0039 -0.0059 -0.0384 154  ALA   B CB  
6520 N  N   . VAL   B 155 ? 0.1423 0.1326 0.2054 0.0022  -0.0011 -0.0229 155  VAL   B N   
6521 C  CA  . VAL   B 155 ? 0.1419 0.1306 0.2207 0.0000  -0.0067 -0.0180 155  VAL   B CA  
6522 C  C   . VAL   B 155 ? 0.1438 0.1355 0.2213 -0.0040 -0.0037 -0.0332 155  VAL   B C   
6523 O  O   . VAL   B 155 ? 0.1561 0.1535 0.2501 0.0043  -0.0039 -0.0455 155  VAL   B O   
6524 C  CB  . VAL   B 155 ? 0.1426 0.1479 0.2499 -0.0075 -0.0105 -0.0041 155  VAL   B CB  
6525 C  CG1 . VAL   B 155 ? 0.1515 0.1465 0.2463 -0.0083 -0.0137 -0.0046 155  VAL   B CG1 
6526 C  CG2 . VAL   B 155 ? 0.1373 0.1679 0.2836 -0.0096 -0.0218 0.0235  155  VAL   B CG2 
6536 N  N   . PHE   B 156 ? 0.1365 0.1469 0.2374 -0.0003 -0.0027 -0.0281 156  PHE   B N   
6537 C  CA  . PHE   B 156 ? 0.1394 0.1522 0.2645 0.0081  -0.0026 -0.0313 156  PHE   B CA  
6538 C  C   . PHE   B 156 ? 0.1354 0.1656 0.3070 0.0165  -0.0004 -0.0458 156  PHE   B C   
6539 O  O   . PHE   B 156 ? 0.1633 0.1820 0.3238 0.0200  0.0066  -0.0531 156  PHE   B O   
6540 C  CB  . PHE   B 156 ? 0.1434 0.1463 0.2553 -0.0005 -0.0139 -0.0107 156  PHE   B CB  
6541 C  CG  . PHE   B 156 ? 0.1440 0.1564 0.2720 0.0011  -0.0108 0.0027  156  PHE   B CG  
6542 C  CD1 . PHE   B 156 ? 0.1482 0.1856 0.3128 0.0074  -0.0018 0.0339  156  PHE   B CD1 
6543 C  CD2 . PHE   B 156 ? 0.1504 0.1661 0.2633 0.0089  -0.0145 -0.0012 156  PHE   B CD2 
6544 C  CE1 . PHE   B 156 ? 0.1504 0.1996 0.3231 0.0096  -0.0038 0.0344  156  PHE   B CE1 
6545 C  CE2 . PHE   B 156 ? 0.1584 0.1890 0.2897 0.0152  -0.0101 0.0082  156  PHE   B CE2 
6546 C  CZ  . PHE   B 156 ? 0.1467 0.1979 0.3161 0.0155  -0.0136 0.0176  156  PHE   B CZ  
6556 N  N   . ASP   B 157 ? 0.1393 0.1509 0.3216 0.0136  -0.0143 -0.0335 157  ASP   B N   
6557 C  CA  . ASP   B 157 ? 0.1523 0.1551 0.3440 0.0126  -0.0198 -0.0373 157  ASP   B CA  
6558 C  C   . ASP   B 157 ? 0.1562 0.1569 0.3511 0.0073  -0.0162 -0.0550 157  ASP   B C   
6559 O  O   . ASP   B 157 ? 0.1429 0.1536 0.3434 0.0033  -0.0175 -0.0428 157  ASP   B O   
6560 C  CB  . ASP   B 157 ? 0.1790 0.1737 0.3542 0.0124  -0.0459 -0.0214 157  ASP   B CB  
6561 C  CG  . ASP   B 157 ? 0.2202 0.1900 0.3827 0.0076  -0.0364 -0.0212 157  ASP   B CG  
6562 O  OD1 . ASP   B 157 ? 0.2287 0.1865 0.4002 0.0210  -0.0232 -0.0228 157  ASP   B OD1 
6563 O  OD2 . ASP   B 157 ? 0.2548 0.2085 0.4113 -0.0016 -0.0251 -0.0125 157  ASP   B OD2 
6568 N  N   A LYS   B 158 ? 0.1525 0.1745 0.3669 0.0071  -0.0058 -0.0780 158  LYS   B N   
6569 N  N   B LYS   B 158 ? 0.1683 0.1792 0.3411 0.0084  -0.0101 -0.0685 158  LYS   B N   
6570 C  CA  A LYS   B 158 ? 0.1689 0.1916 0.3792 0.0117  -0.0036 -0.0942 158  LYS   B CA  
6571 C  CA  B LYS   B 158 ? 0.1918 0.2008 0.3361 0.0123  -0.0082 -0.0773 158  LYS   B CA  
6572 C  C   A LYS   B 158 ? 0.1646 0.1730 0.3979 0.0099  -0.0183 -0.0873 158  LYS   B C   
6573 C  C   B LYS   B 158 ? 0.1925 0.1975 0.3347 0.0126  -0.0177 -0.0719 158  LYS   B C   
6574 O  O   A LYS   B 158 ? 0.1606 0.1660 0.4010 -0.0014 -0.0186 -0.0943 158  LYS   B O   
6575 O  O   B LYS   B 158 ? 0.1939 0.2004 0.3290 0.0096  -0.0154 -0.0706 158  LYS   B O   
6576 C  CB  A LYS   B 158 ? 0.1947 0.2294 0.3757 0.0169  0.0073  -0.1100 158  LYS   B CB  
6577 C  CB  B LYS   B 158 ? 0.2162 0.2257 0.3366 0.0167  0.0010  -0.0897 158  LYS   B CB  
6578 C  CG  A LYS   B 158 ? 0.2281 0.2662 0.3757 0.0185  0.0142  -0.1165 158  LYS   B CG  
6579 C  CG  B LYS   B 158 ? 0.2419 0.2497 0.3408 0.0188  0.0095  -0.0957 158  LYS   B CG  
6580 C  CD  A LYS   B 158 ? 0.2529 0.3062 0.3864 0.0157  0.0126  -0.1062 158  LYS   B CD  
6581 C  CD  B LYS   B 158 ? 0.2635 0.2769 0.3538 0.0185  0.0113  -0.0902 158  LYS   B CD  
6582 C  CE  A LYS   B 158 ? 0.2697 0.3338 0.3949 0.0182  0.0089  -0.0990 158  LYS   B CE  
6583 C  CE  B LYS   B 158 ? 0.2784 0.2953 0.3652 0.0218  0.0114  -0.0850 158  LYS   B CE  
6584 N  NZ  A LYS   B 158 ? 0.2688 0.3419 0.3898 0.0168  0.0069  -0.0970 158  LYS   B NZ  
6585 N  NZ  B LYS   B 158 ? 0.2817 0.3031 0.3659 0.0225  0.0130  -0.0828 158  LYS   B NZ  
6612 N  N   A ASN   B 159 ? 0.1682 0.1584 0.4174 0.0098  -0.0303 -0.0701 159  ASN   B N   
6613 N  N   B ASN   B 159 ? 0.1925 0.1910 0.3458 0.0101  -0.0287 -0.0631 159  ASN   B N   
6614 C  CA  A ASN   B 159 ? 0.1856 0.1505 0.4308 0.0271  -0.0452 -0.0562 159  ASN   B CA  
6615 C  CA  B ASN   B 159 ? 0.1967 0.1830 0.3594 0.0190  -0.0369 -0.0582 159  ASN   B CA  
6616 C  C   A ASN   B 159 ? 0.1740 0.1418 0.4118 0.0236  -0.0615 -0.0456 159  ASN   B C   
6617 C  C   B ASN   B 159 ? 0.1815 0.1620 0.3707 0.0215  -0.0489 -0.0518 159  ASN   B C   
6618 O  O   A ASN   B 159 ? 0.1739 0.1366 0.4285 -0.0008 -0.0688 -0.0322 159  ASN   B O   
6619 O  O   B ASN   B 159 ? 0.1800 0.1586 0.3749 0.0168  -0.0495 -0.0462 159  ASN   B O   
6620 C  CB  A ASN   B 159 ? 0.2073 0.1696 0.4605 0.0328  -0.0540 -0.0527 159  ASN   B CB  
6621 C  CB  B ASN   B 159 ? 0.2099 0.1976 0.3624 0.0216  -0.0395 -0.0551 159  ASN   B CB  
6622 C  CG  A ASN   B 159 ? 0.2350 0.1903 0.4868 0.0289  -0.0604 -0.0657 159  ASN   B CG  
6623 C  CG  B ASN   B 159 ? 0.2259 0.2124 0.3706 0.0237  -0.0440 -0.0542 159  ASN   B CG  
6624 O  OD1 A ASN   B 159 ? 0.2512 0.1970 0.4968 0.0307  -0.0568 -0.0739 159  ASN   B OD1 
6625 O  OD1 B ASN   B 159 ? 0.2341 0.2180 0.3716 0.0270  -0.0439 -0.0488 159  ASN   B OD1 
6626 N  ND2 A ASN   B 159 ? 0.2380 0.2042 0.5000 0.0276  -0.0670 -0.0604 159  ASN   B ND2 
6627 N  ND2 B ASN   B 159 ? 0.2284 0.2221 0.3790 0.0255  -0.0471 -0.0496 159  ASN   B ND2 
6640 N  N   . LEU   B 160 ? 0.1666 0.1513 0.3811 0.0168  -0.0546 -0.0458 160  LEU   B N   
6641 C  CA  . LEU   B 160 ? 0.1581 0.1490 0.3448 0.0184  -0.0384 -0.0272 160  LEU   B CA  
6642 C  C   . LEU   B 160 ? 0.1551 0.1467 0.3333 0.0006  -0.0199 -0.0380 160  LEU   B C   
6643 O  O   . LEU   B 160 ? 0.1416 0.1507 0.3342 -0.0009 -0.0247 -0.0179 160  LEU   B O   
6644 C  CB  . LEU   B 160 ? 0.1562 0.1569 0.3228 0.0104  -0.0386 -0.0189 160  LEU   B CB  
6645 C  CG  . LEU   B 160 ? 0.1567 0.1675 0.3061 0.0116  -0.0379 -0.0068 160  LEU   B CG  
6646 C  CD1 . LEU   B 160 ? 0.1686 0.1852 0.3026 0.0016  -0.0231 -0.0070 160  LEU   B CD1 
6647 C  CD2 . LEU   B 160 ? 0.1583 0.1715 0.3087 0.0223  -0.0368 -0.0146 160  LEU   B CD2 
6660 N  N   A TYR   B 161 ? 0.1523 0.1450 0.3309 -0.0120 0.0027  -0.0491 161  TYR   B N   
6661 N  N   B TYR   B 161 ? 0.1589 0.1493 0.3225 -0.0073 -0.0023 -0.0458 161  TYR   B N   
6662 C  CA  A TYR   B 161 ? 0.1541 0.1464 0.3192 -0.0176 0.0200  -0.0472 161  TYR   B CA  
6663 C  CA  B TYR   B 161 ? 0.1652 0.1535 0.3068 -0.0102 0.0118  -0.0451 161  TYR   B CA  
6664 C  C   A TYR   B 161 ? 0.1610 0.1461 0.3102 -0.0126 0.0238  -0.0461 161  TYR   B C   
6665 C  C   B TYR   B 161 ? 0.1657 0.1503 0.3055 -0.0079 0.0171  -0.0497 161  TYR   B C   
6666 O  O   A TYR   B 161 ? 0.1639 0.1427 0.3056 -0.0223 0.0143  -0.0346 161  TYR   B O   
6667 O  O   B TYR   B 161 ? 0.1680 0.1487 0.3002 -0.0117 0.0133  -0.0447 161  TYR   B O   
6668 C  CB  A TYR   B 161 ? 0.1666 0.1510 0.3172 -0.0281 0.0351  -0.0566 161  TYR   B CB  
6669 C  CB  B TYR   B 161 ? 0.1802 0.1624 0.2944 -0.0152 0.0216  -0.0457 161  TYR   B CB  
6670 C  CG  A TYR   B 161 ? 0.1919 0.1580 0.3045 -0.0378 0.0445  -0.0600 161  TYR   B CG  
6671 C  CG  B TYR   B 161 ? 0.2022 0.1731 0.2776 -0.0225 0.0263  -0.0435 161  TYR   B CG  
6672 C  CD1 A TYR   B 161 ? 0.1970 0.1565 0.2925 -0.0465 0.0478  -0.0616 161  TYR   B CD1 
6673 C  CD1 B TYR   B 161 ? 0.2078 0.1753 0.2656 -0.0281 0.0282  -0.0436 161  TYR   B CD1 
6674 C  CD2 A TYR   B 161 ? 0.2166 0.1701 0.3008 -0.0294 0.0363  -0.0618 161  TYR   B CD2 
6675 C  CD2 B TYR   B 161 ? 0.2187 0.1821 0.2702 -0.0192 0.0232  -0.0419 161  TYR   B CD2 
6676 C  CE1 A TYR   B 161 ? 0.2142 0.1770 0.3002 -0.0453 0.0468  -0.0533 161  TYR   B CE1 
6677 C  CE1 B TYR   B 161 ? 0.2203 0.1881 0.2668 -0.0299 0.0271  -0.0378 161  TYR   B CE1 
6678 C  CE2 A TYR   B 161 ? 0.2323 0.1866 0.3115 -0.0321 0.0381  -0.0539 161  TYR   B CE2 
6679 C  CE2 B TYR   B 161 ? 0.2302 0.1929 0.2742 -0.0217 0.0256  -0.0379 161  TYR   B CE2 
6680 C  CZ  A TYR   B 161 ? 0.2336 0.1902 0.3086 -0.0451 0.0343  -0.0491 161  TYR   B CZ  
6681 C  CZ  B TYR   B 161 ? 0.2330 0.1957 0.2709 -0.0299 0.0216  -0.0352 161  TYR   B CZ  
6682 O  OH  A TYR   B 161 ? 0.2607 0.2161 0.3280 -0.0500 0.0286  -0.0515 161  TYR   B OH  
6683 O  OH  B TYR   B 161 ? 0.2516 0.2115 0.2827 -0.0347 0.0217  -0.0369 161  TYR   B OH  
6702 N  N   . ASP   B 162 ? 0.1639 0.1492 0.3159 -0.0067 0.0092  -0.0620 162  ASP   B N   
6703 C  CA  . ASP   B 162 ? 0.1747 0.1555 0.3270 -0.0075 -0.0004 -0.0558 162  ASP   B CA  
6704 C  C   . ASP   B 162 ? 0.1739 0.1441 0.3268 -0.0133 -0.0074 -0.0483 162  ASP   B C   
6705 O  O   . ASP   B 162 ? 0.1789 0.1477 0.3327 -0.0206 -0.0241 -0.0258 162  ASP   B O   
6706 C  CB  . ASP   B 162 ? 0.1993 0.1743 0.3502 -0.0002 -0.0077 -0.0693 162  ASP   B CB  
6707 C  CG  . ASP   B 162 ? 0.2050 0.1992 0.3708 0.0087  -0.0085 -0.0835 162  ASP   B CG  
6708 O  OD1 . ASP   B 162 ? 0.2018 0.2208 0.3642 -0.0029 0.0089  -0.0845 162  ASP   B OD1 
6709 O  OD2 . ASP   B 162 ? 0.2201 0.2182 0.3940 0.0250  -0.0100 -0.0831 162  ASP   B OD2 
6715 N  N   . LYS   B 163 ? 0.1707 0.1341 0.3167 -0.0086 -0.0200 -0.0361 163  LYS   B N   
6716 C  CA  . LYS   B 163 ? 0.1802 0.1418 0.3293 -0.0164 -0.0102 -0.0226 163  LYS   B CA  
6717 C  C   . LYS   B 163 ? 0.1503 0.1416 0.3115 -0.0154 -0.0091 -0.0032 163  LYS   B C   
6718 O  O   . LYS   B 163 ? 0.1574 0.1471 0.3413 -0.0232 -0.0092 0.0077  163  LYS   B O   
6719 C  CB  . LYS   B 163 ? 0.2231 0.1713 0.3608 -0.0103 -0.0136 -0.0048 163  LYS   B CB  
6720 C  CG  . LYS   B 163 ? 0.2998 0.2567 0.4130 -0.0144 -0.0044 0.0074  163  LYS   B CG  
6721 C  CD  . LYS   B 163 ? 0.3605 0.3220 0.4700 -0.0224 -0.0042 0.0123  163  LYS   B CD  
6722 C  CE  . LYS   B 163 ? 0.4046 0.3686 0.5072 -0.0294 -0.0017 0.0183  163  LYS   B CE  
6723 N  NZ  . LYS   B 163 ? 0.4333 0.4031 0.5324 -0.0333 0.0003  0.0174  163  LYS   B NZ  
6737 N  N   . LEU   B 164 ? 0.1406 0.1391 0.2694 -0.0123 -0.0082 -0.0053 164  LEU   B N   
6738 C  CA  . LEU   B 164 ? 0.1430 0.1367 0.2610 -0.0127 -0.0153 -0.0002 164  LEU   B CA  
6739 C  C   . LEU   B 164 ? 0.1520 0.1383 0.2612 -0.0187 -0.0273 -0.0038 164  LEU   B C   
6740 O  O   . LEU   B 164 ? 0.1571 0.1632 0.2782 -0.0202 -0.0238 -0.0005 164  LEU   B O   
6741 C  CB  . LEU   B 164 ? 0.1400 0.1340 0.2536 -0.0116 -0.0095 -0.0068 164  LEU   B CB  
6742 C  CG  . LEU   B 164 ? 0.1516 0.1504 0.2574 -0.0143 -0.0054 0.0037  164  LEU   B CG  
6743 C  CD1 . LEU   B 164 ? 0.1592 0.1526 0.2498 -0.0176 -0.0093 -0.0053 164  LEU   B CD1 
6744 C  CD2 . LEU   B 164 ? 0.1682 0.1843 0.2797 -0.0111 0.0045  -0.0093 164  LEU   B CD2 
6756 N  N   . VAL   B 165 ? 0.1805 0.1468 0.2786 -0.0223 -0.0309 -0.0114 165  VAL   B N   
6757 C  CA  . VAL   B 165 ? 0.2137 0.1548 0.2925 -0.0368 -0.0479 -0.0055 165  VAL   B CA  
6758 C  C   . VAL   B 165 ? 0.2409 0.1710 0.3243 -0.0430 -0.0710 -0.0033 165  VAL   B C   
6759 O  O   . VAL   B 165 ? 0.2580 0.1926 0.3274 -0.0471 -0.0759 -0.0024 165  VAL   B O   
6760 C  CB  . VAL   B 165 ? 0.2390 0.1708 0.2871 -0.0217 -0.0200 -0.0175 165  VAL   B CB  
6761 C  CG1 . VAL   B 165 ? 0.2568 0.1821 0.3073 -0.0203 -0.0121 -0.0242 165  VAL   B CG1 
6762 C  CG2 . VAL   B 165 ? 0.2348 0.1809 0.2843 -0.0193 -0.0032 -0.0088 165  VAL   B CG2 
6772 N  N   . SER   B 166 ? 0.2528 0.1594 0.3632 -0.0396 -0.0840 -0.0299 166  SER   B N   
6773 C  CA  . SER   B 166 ? 0.2503 0.1588 0.4255 -0.0386 -0.0678 -0.0380 166  SER   B CA  
6774 C  C   . SER   B 166 ? 0.2339 0.1624 0.4349 -0.0470 -0.0710 -0.0125 166  SER   B C   
6775 O  O   . SER   B 166 ? 0.2393 0.1924 0.4630 -0.0573 -0.0826 -0.0375 166  SER   B O   
6776 C  CB  . SER   B 166 ? 0.2490 0.1757 0.4658 -0.0308 -0.0642 -0.0414 166  SER   B CB  
6777 O  OG  . SER   B 166 ? 0.2395 0.1760 0.4831 -0.0195 -0.0690 -0.0226 166  SER   B OG  
6783 N  N   . SER   B 167 ? 0.2120 0.1591 0.4011 -0.0423 -0.0747 0.0263  167  SER   B N   
6784 C  CA  . SER   B 167 ? 0.2062 0.1670 0.3833 -0.0337 -0.0448 0.0277  167  SER   B CA  
6785 C  C   . SER   B 167 ? 0.1944 0.1772 0.3609 -0.0454 -0.0358 0.0504  167  SER   B C   
6786 O  O   . SER   B 167 ? 0.1981 0.1924 0.3485 -0.0462 -0.0263 0.0513  167  SER   B O   
6787 C  CB  . SER   B 167 ? 0.1974 0.1733 0.3729 -0.0324 -0.0138 0.0274  167  SER   B CB  
6788 O  OG  . SER   B 167 ? 0.1906 0.1832 0.3560 -0.0221 -0.0008 0.0240  167  SER   B OG  
6794 N  N   . PHE   B 168 ? 0.1920 0.1781 0.3563 -0.0397 -0.0250 0.0547  168  PHE   B N   
6795 C  CA  . PHE   B 168 ? 0.2002 0.1771 0.3249 -0.0433 -0.0186 0.0366  168  PHE   B CA  
6796 C  C   . PHE   B 168 ? 0.1784 0.1581 0.2640 -0.0231 -0.0051 0.0203  168  PHE   B C   
6797 O  O   . PHE   B 168 ? 0.2125 0.1526 0.2520 -0.0010 -0.0029 0.0020  168  PHE   B O   
6798 C  CB  . PHE   B 168 ? 0.2104 0.1829 0.3286 -0.0554 -0.0366 0.0499  168  PHE   B CB  
6799 C  CG  . PHE   B 168 ? 0.2353 0.1685 0.3161 -0.0482 -0.0440 0.0274  168  PHE   B CG  
6800 C  CD1 . PHE   B 168 ? 0.2590 0.1656 0.3258 -0.0508 -0.0531 0.0190  168  PHE   B CD1 
6801 C  CD2 . PHE   B 168 ? 0.2259 0.1601 0.3129 -0.0412 -0.0439 0.0349  168  PHE   B CD2 
6802 C  CE1 . PHE   B 168 ? 0.2702 0.1745 0.3234 -0.0404 -0.0422 0.0304  168  PHE   B CE1 
6803 C  CE2 . PHE   B 168 ? 0.2502 0.1699 0.3237 -0.0314 -0.0476 0.0257  168  PHE   B CE2 
6804 C  CZ  . PHE   B 168 ? 0.2598 0.1624 0.3281 -0.0216 -0.0500 0.0366  168  PHE   B CZ  
6814 N  N   . LEU   B 169 ? 0.1885 0.1730 0.2657 0.0017  0.0055  0.0029  169  LEU   B N   
6815 C  CA  . LEU   B 169 ? 0.2211 0.1988 0.3137 -0.0104 0.0011  -0.0265 169  LEU   B CA  
6816 C  C   . LEU   B 169 ? 0.2562 0.2235 0.3744 0.0034  -0.0002 -0.0568 169  LEU   B C   
6817 O  O   . LEU   B 169 ? 0.2772 0.2457 0.4242 -0.0023 0.0030  -0.0771 169  LEU   B O   
6818 C  CB  . LEU   B 169 ? 0.2410 0.2366 0.3291 -0.0185 -0.0097 -0.0034 169  LEU   B CB  
6819 C  CG  . LEU   B 169 ? 0.2827 0.2794 0.3720 -0.0079 -0.0068 0.0048  169  LEU   B CG  
6820 C  CD1 . LEU   B 169 ? 0.2946 0.2927 0.3764 -0.0065 -0.0136 0.0201  169  LEU   B CD1 
6821 C  CD2 . LEU   B 169 ? 0.2843 0.2903 0.3795 0.0027  0.0073  -0.0060 169  LEU   B CD2 
6822 O  OXT . LEU   B 169 ? 0.2775 0.2426 0.3825 0.0366  0.0058  -0.0589 169  LEU   B OXT 
6834 N  N2  B A1BBT C .   ? 0.1586 0.1675 0.1846 0.0023  -0.0167 0.0278  201  A1BBT A N2  
6835 C  C3  B A1BBT C .   ? 0.1812 0.1814 0.1759 -0.0149 -0.0178 0.0321  201  A1BBT A C3  
6836 C  C6  B A1BBT C .   ? 0.1860 0.1551 0.1815 -0.0165 0.0231  0.0391  201  A1BBT A C6  
6837 C  C9  B A1BBT C .   ? 0.1479 0.1498 0.1558 0.0043  -0.0007 0.0326  201  A1BBT A C9  
6838 C  C12 B A1BBT C .   ? 0.1217 0.1542 0.1636 0.0016  0.0048  0.0448  201  A1BBT A C12 
6839 C  C1  B A1BBT C .   ? 0.1874 0.1811 0.1511 -0.0252 -0.0248 0.0228  201  A1BBT A C1  
6840 C  C10 B A1BBT C .   ? 0.1485 0.1631 0.1625 0.0115  0.0046  0.0247  201  A1BBT A C10 
6841 C  C11 B A1BBT C .   ? 0.1326 0.1638 0.1509 0.0140  0.0187  0.0383  201  A1BBT A C11 
6842 C  C2  B A1BBT C .   ? 0.1813 0.1714 0.1560 -0.0248 -0.0111 0.0376  201  A1BBT A C2  
6843 C  C4  B A1BBT C .   ? 0.1902 0.1857 0.1897 -0.0088 -0.0186 0.0311  201  A1BBT A C4  
6844 C  C5  B A1BBT C .   ? 0.1984 0.1799 0.1908 -0.0135 0.0021  0.0334  201  A1BBT A C5  
6845 C  C7  B A1BBT C .   ? 0.1583 0.1616 0.1719 0.0003  -0.0041 0.0325  201  A1BBT A C7  
6846 C  C8  B A1BBT C .   ? 0.1554 0.1671 0.1789 0.0031  -0.0147 0.0348  201  A1BBT A C8  
6847 N  N1  B A1BBT C .   ? 0.1687 0.1546 0.1692 -0.0120 0.0095  0.0459  201  A1BBT A N1  
6848 N  N3  B A1BBT C .   ? 0.1536 0.1566 0.1646 -0.0078 0.0067  0.0441  201  A1BBT A N3  
6849 N  N4  B A1BBT C .   ? 0.1407 0.1409 0.1650 0.0115  -0.0090 0.0401  201  A1BBT A N4  
6850 O  O1  B A1BBT C .   ? 0.1897 0.1909 0.1785 -0.0221 -0.0280 0.0146  201  A1BBT A O1  
6865 CL CL  B CL    D .   ? 0.1736 0.1423 0.2132 -0.0141 0.0017  0.0045  202  CL    A CL  
6866 O  O   . HOH   E .   ? 0.6087 0.6092 0.5277 -0.0604 -0.1273 -0.1191 1301 HOH   A O   
6867 O  O   . HOH   E .   ? 0.3325 0.6438 0.7006 0.0902  0.1144  0.1577  1302 HOH   A O   
6868 O  O   . HOH   E .   ? 0.7994 0.5109 0.3356 -0.1519 -0.0049 0.1515  1303 HOH   A O   
6869 O  O   . HOH   E .   ? 0.4278 0.8392 0.4669 -0.1179 0.0677  0.0444  1304 HOH   A O   
6870 O  O   . HOH   E .   ? 0.2545 0.2419 0.3566 0.0338  -0.1007 0.0222  1305 HOH   A O   
6871 O  O   . HOH   E .   ? 0.3195 0.2528 0.4980 -0.0376 -0.1087 0.1267  1306 HOH   A O   
6872 O  O   . HOH   E .   ? 0.5990 0.4562 0.6436 -0.0460 0.1573  0.2249  1307 HOH   A O   
6873 O  O   . HOH   E .   ? 0.3348 0.3130 0.1553 -0.0731 0.0453  0.0357  1308 HOH   A O   
6874 O  O   . HOH   E .   ? 0.1934 0.1713 0.2173 0.0177  -0.0289 0.0061  1309 HOH   A O   
6875 O  O   A HOH   E .   ? 0.4123 0.1849 0.3967 -0.0257 -0.0421 -0.0014 1310 HOH   A O   
6876 O  O   . HOH   E .   ? 0.6891 0.5317 0.6011 -0.1305 0.2343  0.2023  1311 HOH   A O   
6877 O  O   . HOH   E .   ? 0.6422 0.5368 0.3413 0.2585  -0.1107 0.0608  1312 HOH   A O   
6878 O  O   . HOH   E .   ? 0.4087 0.3229 0.6124 0.0155  0.1269  -0.0266 1313 HOH   A O   
6879 O  O   . HOH   E .   ? 0.4631 0.2052 0.5440 0.0609  -0.0236 -0.0132 1314 HOH   A O   
6880 O  O   . HOH   E .   ? 0.2430 0.7013 0.3940 -0.0323 -0.0514 0.1228  1315 HOH   A O   
6881 O  O   . HOH   E .   ? 0.6541 0.6276 0.3498 -0.1067 -0.0458 0.0850  1316 HOH   A O   
6882 O  O   . HOH   E .   ? 0.1752 0.4610 0.3194 0.0760  -0.0085 0.0520  1317 HOH   A O   
6883 O  O   . HOH   E .   ? 0.3655 0.3297 0.3662 -0.1459 0.0085  0.0900  1318 HOH   A O   
6884 O  O   . HOH   E .   ? 0.2096 0.2004 0.3576 -0.0457 0.0132  -0.0115 1319 HOH   A O   
6885 O  O   B HOH   E .   ? 0.4097 0.4473 0.3931 -0.1167 -0.0366 -0.1395 1320 HOH   A O   
6886 O  O   . HOH   E .   ? 0.4886 0.2727 0.2959 -0.1155 0.0221  0.0421  1321 HOH   A O   
6887 O  O   . HOH   E .   ? 0.2717 0.3389 0.3657 0.0589  -0.0078 0.0825  1322 HOH   A O   
6888 O  O   . HOH   E .   ? 0.3136 0.6801 0.5757 -0.0279 -0.0896 0.2127  1323 HOH   A O   
6889 O  O   . HOH   E .   ? 0.4437 0.5907 0.3197 -0.1272 0.1468  0.0670  1324 HOH   A O   
6890 O  O   . HOH   E .   ? 0.1711 0.1628 0.2092 -0.0141 0.0150  0.0314  1325 HOH   A O   
6891 O  O   A HOH   E .   ? 0.2480 0.3918 0.4939 -0.0493 0.0596  0.2048  1326 HOH   A O   
6892 O  O   . HOH   E .   ? 0.4512 0.5902 0.4774 0.1950  0.0749  -0.1169 1327 HOH   A O   
6893 O  O   . HOH   E .   ? 0.5091 0.4647 0.3864 -0.1381 -0.1166 -0.0116 1328 HOH   A O   
6894 O  O   . HOH   E .   ? 0.2194 0.4230 0.4346 -0.0528 -0.0903 0.1828  1329 HOH   A O   
6895 O  O   . HOH   E .   ? 0.4468 0.6676 0.3914 0.2020  -0.0594 -0.0853 1330 HOH   A O   
6896 O  O   . HOH   E .   ? 0.2860 0.4447 0.5715 0.0982  0.0152  -0.1528 1331 HOH   A O   
6897 O  O   . HOH   E .   ? 0.3147 0.4214 0.3778 -0.0443 0.1310  0.0631  1332 HOH   A O   
6898 O  O   . HOH   E .   ? 0.2697 0.2043 0.2146 -0.0384 0.0226  -0.0082 1333 HOH   A O   
6899 O  O   . HOH   E .   ? 0.6184 0.5384 0.5655 -0.0452 -0.1226 0.0075  1334 HOH   A O   
6900 O  O   . HOH   E .   ? 0.2502 0.3110 0.3534 -0.0026 0.0845  -0.0402 1335 HOH   A O   
6901 O  O   . HOH   E .   ? 0.6236 0.5139 0.5779 -0.0082 0.2881  -0.1173 1336 HOH   A O   
6902 O  O   . HOH   E .   ? 0.2354 0.2090 0.2535 0.0435  0.0376  0.0450  1337 HOH   A O   
6903 O  O   . HOH   E .   ? 0.3769 0.4067 0.4710 -0.1586 -0.0488 0.2086  1338 HOH   A O   
6904 O  O   A HOH   E .   ? 0.3403 0.1586 0.1808 0.0173  0.0347  0.0155  1339 HOH   A O   
6905 O  O   . HOH   E .   ? 0.6362 0.5634 0.4606 0.0674  -0.0960 -0.1023 1340 HOH   A O   
6906 O  O   . HOH   E .   ? 0.2581 0.4374 0.3190 0.0942  -0.0709 -0.0047 1341 HOH   A O   
6907 O  O   . HOH   E .   ? 0.1856 0.2362 0.2025 -0.0317 -0.0103 0.0855  1342 HOH   A O   
6908 O  O   A HOH   E .   ? 0.7505 0.4353 0.4085 -0.0383 -0.1233 0.0017  1343 HOH   A O   
6909 O  O   . HOH   E .   ? 0.6091 0.5692 0.7432 -0.1063 -0.0511 0.1524  1344 HOH   A O   
6910 O  O   . HOH   E .   ? 0.2006 0.3379 0.4410 -0.0344 0.0386  -0.0709 1345 HOH   A O   
6911 O  O   A HOH   E .   ? 0.1796 0.2670 0.2213 0.0766  0.0525  0.0777  1346 HOH   A O   
6912 O  O   . HOH   E .   ? 0.2177 0.1706 0.1586 -0.0185 0.0186  0.0150  1347 HOH   A O   
6913 O  O   . HOH   E .   ? 0.5823 0.3653 0.3008 0.0761  0.1042  0.1225  1348 HOH   A O   
6914 O  O   A HOH   E .   ? 0.2163 0.4698 0.2453 0.1159  0.0050  -0.0167 1349 HOH   A O   
6915 O  O   . HOH   E .   ? 0.4585 0.2003 0.4186 0.0424  -0.0620 0.0698  1350 HOH   A O   
6916 O  O   . HOH   E .   ? 0.4642 0.3495 0.5552 0.0916  -0.0119 0.0765  1351 HOH   A O   
6917 O  O   . HOH   E .   ? 0.3309 0.3873 0.2126 -0.1006 -0.0353 -0.0549 1352 HOH   A O   
6918 O  O   . HOH   E .   ? 0.2666 0.4034 0.3700 -0.0979 -0.0581 -0.0317 1353 HOH   A O   
6919 O  O   . HOH   E .   ? 0.1566 0.1869 0.3061 0.0041  -0.0467 -0.0461 1354 HOH   A O   
6920 O  O   . HOH   E .   ? 0.1518 0.2182 0.2167 0.0075  -0.0117 0.0557  1355 HOH   A O   
6921 O  O   . HOH   E .   ? 0.2058 0.2156 0.2610 -0.0211 -0.0082 0.0813  1356 HOH   A O   
6922 O  O   . HOH   E .   ? 0.1526 0.4522 0.2914 -0.0316 0.0308  0.0476  1357 HOH   A O   
6923 O  O   . HOH   E .   ? 0.6004 0.4202 0.5529 -0.1258 0.0777  0.0585  1358 HOH   A O   
6924 O  O   . HOH   E .   ? 0.1706 0.1624 0.1970 0.0129  -0.0234 0.0286  1359 HOH   A O   
6925 O  O   . HOH   E .   ? 0.3402 0.4474 0.2145 -0.0392 0.0698  0.0497  1360 HOH   A O   
6926 O  O   A HOH   E .   ? 0.2311 0.2078 0.3177 -0.0337 0.0887  0.0660  1361 HOH   A O   
6927 O  O   . HOH   E .   ? 0.7825 0.7191 0.6602 -0.0827 0.0258  -0.0765 1362 HOH   A O   
6928 O  O   . HOH   E .   ? 0.2957 0.3170 0.4265 -0.0399 -0.0893 -0.0745 1363 HOH   A O   
6929 O  O   B HOH   E .   ? 0.1452 0.1684 0.2045 0.0158  -0.0001 0.0334  1364 HOH   A O   
6930 O  O   . HOH   E .   ? 0.2006 0.2007 0.3656 0.0203  0.1010  -0.0059 1365 HOH   A O   
6931 O  O   . HOH   E .   ? 0.2736 0.1909 0.2462 -0.0055 0.0134  0.0312  1366 HOH   A O   
6932 O  O   . HOH   E .   ? 0.5080 0.2811 0.3534 -0.1841 0.1673  -0.0802 1367 HOH   A O   
6933 O  O   . HOH   E .   ? 0.1441 0.1912 0.2442 0.0033  -0.0067 0.0075  1368 HOH   A O   
6934 O  O   . HOH   E .   ? 0.3503 0.4981 0.3989 0.2042  0.0520  0.0496  1369 HOH   A O   
6935 O  O   B HOH   E .   ? 0.2912 0.3193 0.3774 0.0944  -0.0357 -0.0025 1370 HOH   A O   
6936 O  O   . HOH   E .   ? 0.1344 0.1374 0.1425 -0.0056 0.0076  0.0147  1371 HOH   A O   
6937 O  O   . HOH   E .   ? 0.2643 0.3996 0.3167 -0.0284 0.0265  0.0067  1372 HOH   A O   
6938 O  O   . HOH   E .   ? 0.1888 0.1975 0.2208 -0.0253 0.0032  0.0335  1373 HOH   A O   
6939 O  O   . HOH   E .   ? 0.5134 0.3097 0.2915 -0.0772 0.0595  0.0065  1374 HOH   A O   
6940 O  O   . HOH   E .   ? 0.4052 0.2097 0.4907 -0.1017 0.1076  0.0051  1375 HOH   A O   
6941 O  O   B HOH   E .   ? 0.4026 0.3332 0.4159 -0.0283 -0.0055 -0.0524 1376 HOH   A O   
6942 O  O   . HOH   E .   ? 0.1478 0.1573 0.1558 -0.0047 -0.0167 0.0018  1377 HOH   A O   
6943 O  O   . HOH   E .   ? 0.3341 0.4214 0.3590 0.0072  -0.0245 0.0843  1378 HOH   A O   
6944 O  O   . HOH   E .   ? 0.1611 0.1348 0.2210 -0.0110 0.0220  -0.0025 1379 HOH   A O   
6945 O  O   . HOH   E .   ? 0.1942 0.2156 0.2245 -0.0210 -0.0421 0.0447  1380 HOH   A O   
6946 O  O   . HOH   E .   ? 0.3805 0.7643 0.5955 -0.0887 -0.1536 0.0453  1381 HOH   A O   
6947 O  O   . HOH   E .   ? 0.2759 0.4638 0.3242 0.0682  0.0861  0.2085  1382 HOH   A O   
6948 O  O   . HOH   E .   ? 0.1871 0.2611 0.3477 0.0302  0.0642  -0.0547 1383 HOH   A O   
6949 O  O   . HOH   E .   ? 0.3521 0.6692 0.2884 0.1733  0.0477  -0.0708 1384 HOH   A O   
6950 O  O   . HOH   E .   ? 0.1841 0.2716 0.2597 0.0433  0.0521  0.0969  1385 HOH   A O   
6951 O  O   . HOH   E .   ? 0.3046 0.2864 0.6284 0.0737  0.0841  0.0678  1386 HOH   A O   
6952 O  O   . HOH   E .   ? 0.3551 0.2440 0.5196 -0.0856 0.0051  -0.0067 1387 HOH   A O   
6953 O  O   . HOH   E .   ? 0.3528 0.3163 0.3737 -0.1016 -0.0050 -0.0238 1388 HOH   A O   
6954 O  O   . HOH   E .   ? 0.1970 0.1854 0.1756 -0.0036 0.0098  0.0164  1389 HOH   A O   
6955 O  O   . HOH   E .   ? 0.3285 0.2980 0.2036 0.0358  0.0753  0.0207  1390 HOH   A O   
6956 O  O   . HOH   E .   ? 0.4812 0.6948 0.5890 0.1313  -0.0113 0.0344  1391 HOH   A O   
6957 O  O   . HOH   E .   ? 0.4104 0.2192 0.2544 0.1182  0.0336  0.0289  1392 HOH   A O   
6958 O  O   . HOH   E .   ? 0.3474 0.2398 0.3690 -0.0468 0.0822  -0.0452 1393 HOH   A O   
6959 O  O   . HOH   E .   ? 0.2540 0.4589 0.5447 0.0338  -0.0130 0.0904  1394 HOH   A O   
6960 O  O   . HOH   E .   ? 0.1789 0.1699 0.2464 0.0057  -0.0564 -0.0013 1395 HOH   A O   
6961 O  O   . HOH   E .   ? 0.2346 0.1907 0.1772 -0.0453 0.0210  0.0189  1396 HOH   A O   
6962 O  O   . HOH   E .   ? 0.3074 0.2373 0.3268 -0.0015 -0.0366 0.0798  1397 HOH   A O   
6963 O  O   . HOH   E .   ? 0.1750 0.1423 0.1479 -0.0203 0.0168  0.0050  1398 HOH   A O   
6964 O  O   A HOH   E .   ? 0.2049 0.1633 0.2338 0.0091  -0.0722 -0.0121 1399 HOH   A O   
6965 O  O   B HOH   E .   ? 0.1778 0.1999 0.2255 -0.0135 0.0133  0.0257  1400 HOH   A O   
6966 O  O   . HOH   E .   ? 0.1848 0.1922 0.3816 0.0393  0.1014  0.1046  1401 HOH   A O   
6967 O  O   . HOH   E .   ? 0.3120 0.2507 0.2267 -0.0562 -0.1091 0.0331  1402 HOH   A O   
6968 O  O   . HOH   E .   ? 0.2461 0.3914 0.3891 -0.0440 0.1139  -0.0989 1403 HOH   A O   
6969 O  O   . HOH   E .   ? 0.3918 0.6005 0.3705 -0.0688 -0.0143 0.1387  1404 HOH   A O   
6970 O  O   . HOH   E .   ? 0.1386 0.1698 0.1746 0.0121  -0.0212 -0.0217 1405 HOH   A O   
6971 O  O   . HOH   E .   ? 0.2496 0.3087 0.3811 -0.0159 -0.0193 -0.0562 1406 HOH   A O   
6972 O  O   . HOH   E .   ? 0.2200 0.1676 0.3011 0.0094  -0.0299 0.0082  1407 HOH   A O   
6973 O  O   . HOH   E .   ? 0.1356 0.1474 0.1681 0.0019  -0.0195 0.0064  1408 HOH   A O   
6974 O  O   . HOH   E .   ? 0.4946 0.4853 0.2273 0.0199  0.0857  0.1062  1409 HOH   A O   
6975 O  O   . HOH   E .   ? 0.6048 0.7087 0.7387 -0.0026 -0.0203 -0.0741 1410 HOH   A O   
6976 O  O   . HOH   E .   ? 0.1911 0.2748 0.3320 -0.0132 -0.0165 0.0305  1411 HOH   A O   
6977 O  O   . HOH   E .   ? 0.3086 0.3755 0.5707 0.0020  0.0683  -0.0406 1412 HOH   A O   
6978 O  O   . HOH   E .   ? 0.2110 0.1959 0.2822 0.0249  -0.0423 0.0360  1413 HOH   A O   
6979 O  O   . HOH   E .   ? 0.4012 0.4995 0.2315 -0.0969 -0.1317 0.0659  1414 HOH   A O   
6980 O  O   . HOH   E .   ? 0.3026 0.3109 0.3799 -0.1144 0.1163  -0.0189 1415 HOH   A O   
6981 O  O   . HOH   E .   ? 0.4094 0.6572 0.3039 -0.0877 -0.0102 0.1105  1416 HOH   A O   
6982 O  O   B HOH   E .   ? 0.3733 0.4991 0.4167 0.0923  -0.0280 0.0679  1417 HOH   A O   
6983 O  O   . HOH   E .   ? 0.4801 0.4928 0.3515 0.1428  -0.0977 -0.1678 1418 HOH   A O   
6984 O  O   A HOH   E .   ? 0.1497 0.2336 0.3387 -0.0100 0.0663  0.0747  1419 HOH   A O   
6985 O  O   . HOH   E .   ? 0.2471 0.2190 0.2579 -0.0488 -0.0069 0.0581  1420 HOH   A O   
6986 O  O   . HOH   E .   ? 0.2155 0.2698 0.2440 -0.0070 -0.0562 0.0601  1421 HOH   A O   
6987 O  O   . HOH   E .   ? 0.5336 0.6213 0.6696 0.2447  0.0748  0.2171  1422 HOH   A O   
6988 O  O   . HOH   E .   ? 0.3359 0.1360 0.1980 -0.0011 -0.0587 0.0196  1423 HOH   A O   
6989 O  O   . HOH   E .   ? 0.2751 0.3434 0.7809 -0.0372 0.0401  -0.0684 1424 HOH   A O   
6990 O  O   . HOH   E .   ? 0.4019 0.2465 0.5663 -0.0666 -0.2468 0.1079  1425 HOH   A O   
6991 O  O   . HOH   E .   ? 0.5920 0.4630 0.3866 -0.0401 -0.1718 0.0240  1426 HOH   A O   
6992 O  O   . HOH   E .   ? 0.1613 0.1743 0.2898 -0.0005 0.0097  0.0212  1427 HOH   A O   
6993 O  O   A HOH   E .   ? 0.2857 0.3944 0.4483 -0.0691 0.0685  0.1268  1428 HOH   A O   
6994 O  O   . HOH   E .   ? 0.2829 0.5868 0.1760 -0.0403 0.0576  0.0204  1429 HOH   A O   
6995 O  O   . HOH   E .   ? 0.2592 0.4137 0.2669 0.1694  0.0030  0.0391  1430 HOH   A O   
6996 O  O   . HOH   E .   ? 0.5777 0.7506 0.4167 0.0690  0.2732  -0.0543 1431 HOH   A O   
6997 O  O   . HOH   E .   ? 0.1755 0.2350 0.2566 -0.0248 -0.0001 0.0486  1432 HOH   A O   
6998 O  O   B HOH   E .   ? 0.2361 0.1794 0.3374 0.0144  -0.0156 0.0660  1433 HOH   A O   
6999 O  O   . HOH   E .   ? 1.0651 1.0094 0.8203 -0.1090 -0.1258 0.0087  1434 HOH   A O   
7000 O  O   . HOH   E .   ? 0.6398 0.4247 0.5137 0.1636  -0.0512 0.1544  1435 HOH   A O   
7001 O  O   A HOH   E .   ? 0.2708 0.2232 0.3044 0.0274  0.0429  0.0727  1436 HOH   A O   
7002 O  O   A HOH   E .   ? 0.1521 0.1641 0.1631 0.0129  -0.0231 -0.0232 1437 HOH   A O   
7003 O  O   . HOH   E .   ? 0.6970 0.6742 0.6346 -0.1425 0.0341  -0.1256 1438 HOH   A O   
7004 O  O   . HOH   E .   ? 0.3758 0.2503 0.1712 -0.0770 0.0377  0.0439  1439 HOH   A O   
7005 O  O   . HOH   E .   ? 0.3942 0.5396 0.5483 0.0356  0.0359  0.2914  1440 HOH   A O   
7006 O  O   B HOH   E .   ? 0.4045 0.1873 0.2589 0.0453  -0.0590 0.0552  1441 HOH   A O   
7007 O  O   . HOH   E .   ? 0.2691 0.1730 0.2687 0.0137  0.0095  0.0077  1442 HOH   A O   
7008 O  O   . HOH   E .   ? 0.1906 0.2119 0.4619 -0.0176 -0.0848 0.0512  1443 HOH   A O   
7009 O  O   A HOH   E .   ? 0.3124 0.1354 0.2025 0.0065  -0.1286 -0.0042 1444 HOH   A O   
7010 O  O   . HOH   E .   ? 0.4367 0.3597 0.3036 0.2329  -0.0522 -0.0457 1445 HOH   A O   
7011 O  O   . HOH   E .   ? 0.2206 0.2985 0.2589 -0.0044 0.0013  -0.0530 1446 HOH   A O   
7012 O  O   . HOH   E .   ? 0.4652 0.4798 0.5253 -0.0476 -0.1011 -0.1365 1447 HOH   A O   
7013 O  O   . HOH   E .   ? 0.8888 0.7414 0.7193 0.0072  -0.0271 -0.0027 1448 HOH   A O   
7014 O  O   . HOH   E .   ? 0.2527 0.3342 0.4649 0.0189  0.0590  -0.1262 1449 HOH   A O   
7015 O  O   . HOH   E .   ? 0.2394 0.2176 0.2507 0.0187  0.0456  0.0486  1450 HOH   A O   
7016 O  O   B HOH   E .   ? 0.1077 0.2377 0.2569 0.0027  0.0089  0.0802  1451 HOH   A O   
7017 O  O   A HOH   E .   ? 0.5936 0.3421 0.6766 0.1183  -0.0176 -0.1255 1452 HOH   A O   
7018 O  O   . HOH   E .   ? 0.8193 0.8149 0.5164 0.2481  -0.1221 0.2177  1453 HOH   A O   
7019 O  O   . HOH   E .   ? 0.5984 0.6111 0.8267 0.0679  -0.1124 0.2200  1454 HOH   A O   
7020 O  O   A HOH   E .   ? 0.3869 0.5146 0.4285 0.2126  0.1170  0.2060  1455 HOH   A O   
7021 O  O   . HOH   E .   ? 0.4090 0.4364 0.3598 0.1030  0.0855  0.0928  1456 HOH   A O   
7022 O  O   . HOH   E .   ? 0.4788 0.4204 0.4886 -0.0108 -0.0041 0.1031  1457 HOH   A O   
7023 O  O   . HOH   E .   ? 0.6835 0.6581 0.5295 -0.0375 0.1882  0.1510  1458 HOH   A O   
7024 O  O   . HOH   E .   ? 0.4999 0.2979 0.4153 0.0516  0.0506  0.0073  1459 HOH   A O   
7025 O  O   . HOH   E .   ? 0.2686 0.2538 0.3440 0.0509  -0.0774 -0.0142 1460 HOH   A O   
7026 O  O   . HOH   E .   ? 0.2760 0.3005 0.3541 -0.0625 0.0325  -0.0706 1461 HOH   A O   
7027 O  O   . HOH   E .   ? 0.7030 0.6898 0.6893 0.1836  0.2251  0.2402  1462 HOH   A O   
7028 O  O   . HOH   E .   ? 0.3418 0.5447 0.5808 -0.1357 0.1511  -0.1177 1463 HOH   A O   
7029 O  O   . HOH   E .   ? 0.8307 0.7671 0.5017 -0.0293 -0.0692 -0.0096 1464 HOH   A O   
7030 O  O   . HOH   E .   ? 0.3426 0.5060 0.5040 0.0801  -0.1229 0.1547  1465 HOH   A O   
7031 O  O   B HOH   E .   ? 0.1872 0.3732 0.3435 0.0159  -0.0668 -0.1063 1466 HOH   A O   
7032 O  O   . HOH   E .   ? 0.3611 0.4585 0.3405 -0.1164 -0.0273 0.0269  1467 HOH   A O   
7033 O  O   . HOH   E .   ? 0.2811 0.3366 0.7064 -0.0094 -0.0700 -0.0602 1468 HOH   A O   
7034 O  O   . HOH   E .   ? 0.2579 0.4312 0.4489 0.0393  0.0082  -0.1815 1469 HOH   A O   
7035 O  O   . HOH   E .   ? 0.6136 0.3645 0.7683 0.0739  0.0523  0.2631  1470 HOH   A O   
7036 O  O   . HOH   E .   ? 0.2744 0.2496 0.3093 -0.0736 0.0465  -0.0337 1471 HOH   A O   
7037 O  O   . HOH   E .   ? 0.2839 0.1808 0.2514 0.0400  -0.0965 -0.0329 1472 HOH   A O   
7038 O  O   . HOH   E .   ? 0.3558 0.6762 0.3885 -0.0618 -0.0679 0.2312  1473 HOH   A O   
7039 O  O   . HOH   E .   ? 0.2781 0.2650 0.3383 0.0054  0.0599  0.0059  1474 HOH   A O   
7040 O  O   . HOH   E .   ? 0.6130 0.4687 0.4740 0.0009  0.1386  0.0314  1475 HOH   A O   
7041 O  O   . HOH   E .   ? 0.4183 0.5167 0.3405 0.0455  -0.0699 -0.0515 1476 HOH   A O   
7042 O  O   . HOH   E .   ? 0.5148 0.2561 0.3665 -0.0506 -0.1163 0.0622  1477 HOH   A O   
7043 O  O   . HOH   E .   ? 0.2763 0.2747 0.2564 0.0580  0.0023  0.0305  1478 HOH   A O   
7044 O  O   . HOH   E .   ? 0.4126 0.4582 0.5153 -0.1999 -0.0523 0.0063  1479 HOH   A O   
7045 O  O   . HOH   E .   ? 0.6219 0.6487 0.4703 0.1876  -0.0941 -0.0856 1480 HOH   A O   
7046 O  O   . HOH   E .   ? 0.5600 0.7313 0.6464 -0.1469 -0.1364 -0.0361 1481 HOH   A O   
7047 O  O   . HOH   E .   ? 0.4310 0.4920 0.2740 0.0205  -0.0078 0.0392  1482 HOH   A O   
7048 O  O   . HOH   E .   ? 0.5362 0.4544 0.3583 -0.0802 -0.0534 -0.0561 1483 HOH   A O   
7049 O  O   . HOH   E .   ? 0.5576 0.4880 0.4720 -0.0255 -0.0521 -0.1175 1484 HOH   A O   
7050 O  O   . HOH   E .   ? 0.6378 0.3938 0.5016 -0.0507 0.0667  0.0271  1485 HOH   A O   
7051 O  O   . HOH   E .   ? 0.6920 0.5182 0.7589 -0.0356 0.1155  -0.0990 1486 HOH   A O   
7052 O  O   . HOH   E .   ? 0.8514 0.4001 0.3351 -0.0675 -0.1354 -0.0058 1487 HOH   A O   
7053 O  O   . HOH   E .   ? 0.3321 0.4317 0.5360 0.0385  0.1816  0.1407  1488 HOH   A O   
7054 O  O   . HOH   E .   ? 0.7650 0.7280 0.5361 -0.1165 0.1811  0.1775  1489 HOH   A O   
7055 O  O   . HOH   E .   ? 0.2593 0.5245 0.3962 0.1009  0.0958  0.2563  1490 HOH   A O   
7056 O  O   . HOH   E .   ? 0.6759 0.4931 0.5766 -0.1129 -0.1109 -0.1092 1491 HOH   A O   
7057 O  O   . HOH   E .   ? 0.3878 0.3309 0.2596 -0.0689 0.1125  -0.0505 1492 HOH   A O   
7058 O  O   . HOH   E .   ? 0.2752 0.2253 0.7044 0.0075  -0.1243 0.0052  1493 HOH   A O   
7059 O  O   . HOH   E .   ? 0.3283 0.2077 0.5948 0.0166  0.1153  0.0709  1494 HOH   A O   
7060 O  O   . HOH   E .   ? 0.5258 0.6422 0.5343 0.0572  -0.1295 0.0696  1495 HOH   A O   
7061 O  O   . HOH   E .   ? 0.2669 0.2730 0.5778 0.0081  0.0969  -0.0487 1496 HOH   A O   
7062 O  O   . HOH   E .   ? 0.6360 0.2932 0.4426 -0.0581 0.1151  0.0406  1497 HOH   A O   
7063 O  O   . HOH   E .   ? 0.4680 0.3731 0.5528 -0.1275 0.1096  0.1086  1498 HOH   A O   
7064 O  O   . HOH   E .   ? 0.4821 0.3120 0.3882 -0.0193 0.1994  0.0212  1499 HOH   A O   
7065 O  O   . HOH   E .   ? 0.2915 0.4900 0.3416 -0.0371 -0.0375 -0.0445 1500 HOH   A O   
7066 O  O   . HOH   E .   ? 0.5885 0.5575 0.7393 0.0945  0.2549  -0.1037 1501 HOH   A O   
7067 O  O   . HOH   E .   ? 0.4263 0.9490 0.6216 -0.1334 -0.0780 0.2378  1502 HOH   A O   
7068 O  O   B HOH   E .   ? 0.1902 0.3016 0.2006 0.0178  -0.0096 -0.0616 1503 HOH   A O   
7069 O  O   . HOH   E .   ? 0.2418 0.3300 0.3587 0.0412  -0.0610 0.0622  1504 HOH   A O   
7070 O  O   . HOH   E .   ? 0.3466 0.3907 0.4826 0.0743  -0.1114 -0.0145 1505 HOH   A O   
7071 O  O   . HOH   E .   ? 0.6216 0.7322 0.5312 0.1183  -0.0179 0.2202  1506 HOH   A O   
7072 O  O   B HOH   E .   ? 0.3111 0.3432 0.2915 0.0017  -0.0034 -0.0314 1507 HOH   A O   
7073 O  O   B HOH   E .   ? 0.4415 0.2192 0.2054 -0.0431 0.0392  0.0084  1508 HOH   A O   
7074 O  O   . HOH   E .   ? 0.6323 0.3999 0.5132 0.0628  -0.0863 0.2102  1509 HOH   A O   
7075 O  O   B HOH   E .   ? 0.3452 0.2765 0.3501 -0.0531 0.1208  -0.0200 1510 HOH   A O   
7076 O  O   . HOH   E .   ? 0.7610 0.7627 0.5437 0.1488  -0.1459 0.0482  1511 HOH   A O   
7077 O  O   . HOH   E .   ? 0.4961 0.7309 0.4716 0.3186  -0.0186 0.1192  1512 HOH   A O   
7078 O  O   . HOH   E .   ? 0.3005 0.2122 0.4916 -0.0101 0.0052  0.0227  1513 HOH   A O   
7079 O  O   B HOH   E .   ? 0.4306 0.3850 0.4405 0.0336  0.0919  0.1502  1514 HOH   A O   
7080 O  O   . HOH   E .   ? 0.5854 0.6632 0.4221 -0.0539 -0.1257 -0.1262 1515 HOH   A O   
7081 O  O   A HOH   E .   ? 0.3233 0.6920 0.2477 0.1165  0.0108  0.0082  1516 HOH   A O   
7082 O  O   . HOH   E .   ? 0.3015 0.8202 0.4116 0.1546  0.0015  0.0162  1517 HOH   A O   
7083 O  O   . HOH   E .   ? 0.6007 0.5418 0.5075 0.1690  0.0616  0.1269  1518 HOH   A O   
7084 O  O   . HOH   E .   ? 0.5102 0.6559 0.5317 -0.0237 -0.0673 0.1184  1519 HOH   A O   
7085 O  O   B HOH   E .   ? 0.3517 0.3286 0.3647 0.0800  0.0839  0.0940  1520 HOH   A O   
7086 O  O   . HOH   E .   ? 0.3012 0.4846 0.5558 -0.0479 -0.0913 0.2911  1521 HOH   A O   
7087 O  O   . HOH   F .   ? 0.2328 0.2003 0.2824 0.0246  0.0763  0.0258  201  HOH   B O   
7088 O  O   . HOH   F .   ? 0.4857 0.3829 0.4103 -0.0198 -0.0345 -0.1833 202  HOH   B O   
7089 O  O   . HOH   F .   ? 0.3626 0.2839 0.7370 -0.0318 0.1002  0.0143  203  HOH   B O   
7090 O  O   . HOH   F .   ? 0.3532 0.5880 0.4905 -0.0386 0.1941  -0.1880 204  HOH   B O   
7091 O  O   . HOH   F .   ? 0.2833 0.6963 0.4112 0.1044  0.0252  0.2593  205  HOH   B O   
7092 O  O   . HOH   F .   ? 0.6724 0.6901 0.6127 0.3210  -0.0295 -0.0286 206  HOH   B O   
7093 O  O   . HOH   F .   ? 0.7500 0.3275 0.4682 0.0020  0.1165  -0.0319 207  HOH   B O   
7094 O  O   . HOH   F .   ? 0.4207 0.5054 0.2697 0.0401  -0.0206 -0.1293 208  HOH   B O   
7095 O  O   . HOH   F .   ? 0.3203 0.4271 0.5257 -0.1127 0.0194  -0.1638 209  HOH   B O   
7096 O  O   . HOH   F .   ? 0.1975 0.2270 0.3003 0.0109  0.0177  -0.0288 210  HOH   B O   
7097 O  O   . HOH   F .   ? 0.3165 0.2160 0.5393 0.0041  0.1952  0.0205  211  HOH   B O   
7098 O  O   . HOH   F .   ? 0.4210 0.5855 0.5004 0.2608  0.0234  -0.0918 212  HOH   B O   
7099 O  O   . HOH   F .   ? 0.2868 0.2004 0.4811 0.0209  0.1726  0.0701  213  HOH   B O   
7100 O  O   . HOH   F .   ? 0.5023 0.6059 0.4170 0.3080  -0.1131 -0.0438 214  HOH   B O   
7101 O  O   . HOH   F .   ? 0.1598 0.2035 0.2615 -0.0262 -0.0086 0.0149  215  HOH   B O   
7102 O  O   . HOH   F .   ? 0.3427 0.3784 0.3510 0.0375  -0.1004 0.0424  216  HOH   B O   
7103 O  O   . HOH   F .   ? 0.5779 0.3831 0.5849 0.0791  -0.0844 0.2433  217  HOH   B O   
7104 O  O   . HOH   F .   ? 0.5511 0.3066 0.4483 -0.1843 -0.0211 -0.0255 218  HOH   B O   
7105 O  O   . HOH   F .   ? 0.1588 0.1581 0.2146 -0.0279 0.0051  0.0105  219  HOH   B O   
7106 O  O   . HOH   F .   ? 0.3671 0.4819 0.4322 0.1724  -0.0229 -0.0302 220  HOH   B O   
7107 O  O   . HOH   F .   ? 0.5133 0.4692 0.4692 0.0521  0.1584  -0.1575 221  HOH   B O   
7108 O  O   . HOH   F .   ? 0.2523 0.2678 0.5759 0.0548  -0.0674 0.0348  222  HOH   B O   
7109 O  O   . HOH   F .   ? 0.4096 0.2992 0.4652 0.0672  -0.0926 -0.0767 223  HOH   B O   
7110 O  O   . HOH   F .   ? 0.2249 0.2239 0.3619 -0.0245 -0.0001 -0.0616 224  HOH   B O   
7111 O  O   . HOH   F .   ? 0.1809 0.2121 0.2981 -0.0181 0.0220  -0.0235 225  HOH   B O   
7112 O  O   . HOH   F .   ? 0.2419 0.1769 0.2551 -0.0229 0.1022  -0.0045 226  HOH   B O   
7113 O  O   . HOH   F .   ? 0.3843 0.3386 0.1974 0.0230  0.0774  0.0470  227  HOH   B O   
7114 O  O   . HOH   F .   ? 0.6531 0.4726 0.5170 0.1313  0.0089  -0.0468 228  HOH   B O   
7115 O  O   . HOH   F .   ? 0.5149 0.2173 0.2997 -0.0021 -0.0881 0.0187  229  HOH   B O   
7116 O  O   . HOH   F .   ? 0.5294 0.7687 0.3953 0.3351  0.0449  0.0410  230  HOH   B O   
7117 O  O   . HOH   F .   ? 0.2355 0.2677 0.3048 0.0203  0.0374  -0.0805 231  HOH   B O   
7118 O  O   . HOH   F .   ? 0.3624 0.2691 0.3838 0.0585  -0.0301 -0.0478 232  HOH   B O   
7119 O  O   . HOH   F .   ? 0.2812 0.1865 0.6092 -0.0027 -0.1361 -0.0339 233  HOH   B O   
7120 O  O   . HOH   F .   ? 0.2139 0.1350 0.3268 0.0132  -0.0551 -0.0167 234  HOH   B O   
7121 O  O   . HOH   F .   ? 0.3817 0.1902 0.1818 0.0308  -0.0851 -0.0198 235  HOH   B O   
7122 O  O   . HOH   F .   ? 0.3795 0.2406 0.4144 0.0211  -0.0646 -0.1233 236  HOH   B O   
7123 O  O   . HOH   F .   ? 0.5923 0.3137 0.3994 -0.2253 0.0633  0.0076  237  HOH   B O   
7124 O  O   . HOH   F .   ? 0.2515 0.3492 0.2613 -0.0660 0.0337  -0.0483 238  HOH   B O   
7125 O  O   . HOH   F .   ? 0.4179 0.3782 0.5293 -0.1535 -0.0434 0.0739  239  HOH   B O   
7126 O  O   . HOH   F .   ? 0.5916 0.3351 0.2734 -0.0035 0.0758  -0.0589 240  HOH   B O   
7127 O  O   . HOH   F .   ? 0.2286 0.2645 0.3172 -0.0566 0.0077  -0.0205 241  HOH   B O   
7128 O  O   . HOH   F .   ? 0.4252 0.4544 0.6582 0.0178  -0.1564 -0.1431 242  HOH   B O   
7129 O  O   . HOH   F .   ? 0.2179 0.3559 0.3386 -0.0454 -0.0583 -0.0717 243  HOH   B O   
7130 O  O   . HOH   F .   ? 0.2581 0.2149 0.1883 0.0155  -0.0101 0.0058  244  HOH   B O   
7131 O  O   . HOH   F .   ? 0.1448 0.1346 0.1509 -0.0030 -0.0022 0.0119  245  HOH   B O   
7132 O  O   . HOH   F .   ? 0.2407 0.3218 0.1990 -0.0620 0.0340  0.0350  246  HOH   B O   
7133 O  O   . HOH   F .   ? 0.3297 0.2725 0.2924 -0.0396 0.0420  -0.0586 247  HOH   B O   
7134 O  O   . HOH   F .   ? 0.2833 0.2378 0.2841 0.0868  0.0791  -0.0057 248  HOH   B O   
7135 O  O   . HOH   F .   ? 0.1584 0.1512 0.2461 -0.0063 0.0155  -0.0137 249  HOH   B O   
7136 O  O   . HOH   F .   ? 0.2250 0.1876 0.2189 -0.0249 -0.0436 0.0126  250  HOH   B O   
7137 O  O   . HOH   F .   ? 0.2189 0.3709 0.2372 -0.0439 -0.0174 0.0617  251  HOH   B O   
7138 O  O   . HOH   F .   ? 0.2168 0.1590 0.1823 -0.0280 -0.0375 0.0273  252  HOH   B O   
7139 O  O   . HOH   F .   ? 0.1552 0.1436 0.1466 -0.0101 -0.0039 -0.0044 253  HOH   B O   
7140 O  O   . HOH   F .   ? 0.5185 0.5965 0.3131 -0.0003 -0.0417 -0.0215 254  HOH   B O   
7141 O  O   . HOH   F .   ? 0.3579 0.3821 0.2175 0.0250  0.0980  -0.0037 255  HOH   B O   
7142 O  O   . HOH   F .   ? 0.2445 0.2181 0.2417 0.0745  -0.0888 -0.0648 256  HOH   B O   
7143 O  O   . HOH   F .   ? 0.3687 0.4111 0.7015 0.0075  0.0994  -0.0357 257  HOH   B O   
7144 O  O   . HOH   F .   ? 0.2211 0.4357 0.4610 -0.0602 -0.0104 -0.1572 258  HOH   B O   
7145 O  O   . HOH   F .   ? 0.1592 0.1709 0.2854 -0.0224 -0.0091 0.0060  259  HOH   B O   
7146 O  O   . HOH   F .   ? 0.2543 0.4569 0.6166 0.0059  -0.0195 -0.1419 260  HOH   B O   
7147 O  O   . HOH   F .   ? 0.3147 0.5082 0.2851 -0.0177 -0.0893 0.0756  261  HOH   B O   
7148 O  O   . HOH   F .   ? 0.2503 0.4424 0.5603 0.1170  -0.0519 -0.0523 262  HOH   B O   
7149 O  O   . HOH   F .   ? 0.4310 0.4271 0.2820 0.0478  0.0164  -0.0924 263  HOH   B O   
7150 O  O   . HOH   F .   ? 0.3331 0.3679 0.5259 0.1303  -0.0696 -0.1076 264  HOH   B O   
7151 O  O   . HOH   F .   ? 0.1398 0.1724 0.1971 -0.0090 0.0054  0.0137  265  HOH   B O   
7152 O  O   . HOH   F .   ? 0.2365 0.2844 0.2038 -0.0551 -0.0549 -0.0466 266  HOH   B O   
7153 O  O   . HOH   F .   ? 0.3365 0.8099 0.7308 0.1841  -0.0609 -0.1174 267  HOH   B O   
7154 O  O   . HOH   F .   ? 0.2319 0.2222 0.1685 0.0152  0.0051  0.0010  268  HOH   B O   
7155 O  O   . HOH   F .   ? 0.2678 0.4143 0.2910 -0.0811 -0.0289 -0.0643 269  HOH   B O   
7156 O  O   . HOH   F .   ? 0.4020 0.3163 0.3957 -0.0718 0.0125  -0.0485 270  HOH   B O   
7157 O  O   . HOH   F .   ? 0.2497 0.1940 0.2771 -0.0516 0.0240  -0.0132 271  HOH   B O   
7158 O  O   . HOH   F .   ? 0.2097 0.1529 0.2188 -0.0233 -0.0147 0.0112  272  HOH   B O   
7159 O  O   . HOH   F .   ? 0.2499 0.4154 0.3201 -0.0723 0.0669  -0.1683 273  HOH   B O   
7160 O  O   . HOH   F .   ? 0.2651 0.4142 0.3429 0.0301  0.1228  0.0020  274  HOH   B O   
7161 O  O   . HOH   F .   ? 0.5387 0.7423 0.2676 0.0804  -0.1410 0.0267  275  HOH   B O   
7162 O  O   . HOH   F .   ? 0.2496 0.2777 0.2328 -0.0380 -0.0732 0.0137  276  HOH   B O   
7163 O  O   . HOH   F .   ? 0.2326 0.3092 0.2368 0.0840  -0.0382 -0.0304 277  HOH   B O   
7164 O  O   . HOH   F .   ? 0.3930 0.2798 0.4927 -0.0319 -0.1114 -0.0907 278  HOH   B O   
7165 O  O   . HOH   F .   ? 0.1952 0.1812 0.1609 -0.0505 -0.0453 0.0170  279  HOH   B O   
7166 O  O   . HOH   F .   ? 0.3046 0.2165 0.4074 0.0193  0.0299  0.0667  280  HOH   B O   
7167 O  O   . HOH   F .   ? 0.2235 0.1872 0.3340 0.0050  -0.0373 -0.0421 281  HOH   B O   
7168 O  O   . HOH   F .   ? 0.1818 0.1465 0.3865 -0.0106 -0.0171 -0.0158 282  HOH   B O   
7169 O  O   . HOH   F .   ? 0.1666 0.1595 0.3171 -0.0101 0.0133  -0.0080 283  HOH   B O   
7170 O  O   . HOH   F .   ? 0.4504 0.4751 0.4782 0.0082  -0.1537 0.0543  284  HOH   B O   
7171 O  O   . HOH   F .   ? 0.1678 0.1593 0.1724 -0.0003 0.0086  -0.0018 285  HOH   B O   
7172 O  O   . HOH   F .   ? 0.1645 0.1991 0.1468 -0.0153 -0.0143 0.0063  286  HOH   B O   
7173 O  O   . HOH   F .   ? 0.3428 0.2624 0.2008 0.0251  -0.0708 -0.0122 287  HOH   B O   
7174 O  O   . HOH   F .   ? 0.1805 0.2040 0.2857 0.0201  -0.0160 -0.0101 288  HOH   B O   
7175 O  O   . HOH   F .   ? 0.3892 0.2133 0.4158 -0.0878 -0.2102 0.0862  289  HOH   B O   
7176 O  O   . HOH   F .   ? 0.2517 0.2601 0.2809 0.0164  -0.0679 0.0291  290  HOH   B O   
7177 O  O   . HOH   F .   ? 0.5542 0.3971 0.4771 0.0299  0.1319  -0.1724 291  HOH   B O   
7178 O  O   . HOH   F .   ? 0.2825 0.4542 0.5258 -0.1054 -0.1276 0.1008  292  HOH   B O   
7179 O  O   . HOH   F .   ? 0.1740 0.3447 0.4416 0.0360  -0.0159 -0.1427 293  HOH   B O   
7180 O  O   . HOH   F .   ? 0.4447 0.3659 0.2341 0.0939  -0.0660 0.0647  294  HOH   B O   
7181 O  O   . HOH   F .   ? 0.6298 0.6241 0.5239 0.3024  0.0262  0.0473  295  HOH   B O   
7182 O  O   . HOH   F .   ? 0.3003 0.3104 0.2644 -0.0143 0.0088  -0.1343 296  HOH   B O   
7183 O  O   . HOH   F .   ? 0.4284 0.4194 0.4317 -0.1173 0.1606  -0.1060 297  HOH   B O   
7184 O  O   . HOH   F .   ? 0.1862 0.1670 0.2128 0.0117  0.0240  0.0219  298  HOH   B O   
7185 O  O   . HOH   F .   ? 0.2734 0.6652 0.2270 0.1026  -0.0328 -0.0656 299  HOH   B O   
7186 O  O   . HOH   F .   ? 0.2232 0.1652 0.2591 -0.0313 -0.0357 -0.0093 300  HOH   B O   
7187 O  O   . HOH   F .   ? 0.3239 0.6411 0.3623 0.1716  -0.0678 -0.0093 301  HOH   B O   
7188 O  O   . HOH   F .   ? 0.2939 0.2937 0.3547 -0.0451 0.1183  -0.0865 302  HOH   B O   
7189 O  O   . HOH   F .   ? 0.1693 0.1537 0.3172 0.0024  0.0051  0.0021  303  HOH   B O   
7190 O  O   . HOH   F .   ? 0.2156 0.3112 0.6422 0.0570  -0.0839 -0.1544 304  HOH   B O   
7191 O  O   . HOH   F .   ? 0.3782 0.4272 0.3986 -0.1763 0.1432  -0.0621 305  HOH   B O   
7192 O  O   . HOH   F .   ? 0.2114 0.1522 0.3442 0.0319  -0.0940 -0.0024 306  HOH   B O   
7193 O  O   . HOH   F .   ? 0.2299 0.3184 0.5029 -0.0195 -0.0776 -0.0426 307  HOH   B O   
7194 O  O   . HOH   F .   ? 0.4788 0.2884 0.2497 -0.1776 0.0682  -0.0280 308  HOH   B O   
7195 O  O   . HOH   F .   ? 0.4428 0.5013 0.2119 0.0147  0.0825  0.0749  309  HOH   B O   
7196 O  O   . HOH   F .   ? 0.3219 0.1879 0.3239 0.0668  0.1051  0.0326  310  HOH   B O   
7197 O  O   . HOH   F .   ? 0.3724 0.2225 0.2665 0.1210  0.0849  0.0173  311  HOH   B O   
7198 O  O   . HOH   F .   ? 0.2535 0.1543 0.2480 -0.0197 -0.0131 0.0341  312  HOH   B O   
7199 O  O   . HOH   F .   ? 0.5485 0.4440 0.5611 0.0576  0.0544  0.0164  313  HOH   B O   
7200 O  O   . HOH   F .   ? 0.3220 0.2943 0.5013 -0.0210 -0.0783 0.1062  314  HOH   B O   
7201 O  O   . HOH   F .   ? 0.4956 0.3980 0.2548 0.0248  -0.0428 -0.0662 315  HOH   B O   
7202 O  O   . HOH   F .   ? 0.6248 0.3919 0.3710 0.2667  0.1576  0.0992  316  HOH   B O   
7203 O  O   . HOH   F .   ? 0.2209 0.1919 0.1654 -0.0066 0.0189  0.0127  317  HOH   B O   
7204 O  O   . HOH   F .   ? 0.1710 0.2779 0.2111 -0.0100 -0.0166 0.0639  318  HOH   B O   
7205 O  O   . HOH   F .   ? 0.1626 0.1962 0.2635 -0.0294 -0.0077 0.0014  319  HOH   B O   
7206 O  O   . HOH   F .   ? 0.4988 0.3789 0.2140 0.1042  -0.0820 -0.0085 320  HOH   B O   
7207 O  O   . HOH   F .   ? 0.2046 0.5937 0.5198 -0.0700 -0.0055 -0.0095 321  HOH   B O   
7208 O  O   . HOH   F .   ? 0.1576 0.1686 0.2947 -0.0174 0.0062  -0.0122 322  HOH   B O   
7209 O  O   . HOH   F .   ? 0.3448 0.4431 0.7840 -0.0329 -0.0961 0.2304  323  HOH   B O   
7210 O  O   . HOH   F .   ? 0.4211 0.3832 0.4896 -0.0546 0.0330  0.1326  324  HOH   B O   
7211 O  O   . HOH   F .   ? 0.5198 0.2657 0.3331 0.0476  0.0924  0.0949  325  HOH   B O   
7212 O  O   . HOH   F .   ? 0.6517 0.4624 0.5496 0.1564  0.1601  0.0439  326  HOH   B O   
7213 O  O   . HOH   F .   ? 0.2842 0.2359 0.2350 0.0316  -0.0247 0.0304  327  HOH   B O   
7214 O  O   . HOH   F .   ? 0.1999 0.3217 0.3125 0.0566  -0.0254 -0.0973 328  HOH   B O   
7215 O  O   . HOH   F .   ? 0.1965 0.1998 0.2923 0.0349  0.0499  0.0242  329  HOH   B O   
7216 O  O   . HOH   F .   ? 0.6402 0.3490 0.4001 0.0317  0.1647  0.1349  330  HOH   B O   
7217 O  O   . HOH   F .   ? 0.2906 0.2924 0.5996 -0.0598 -0.1940 0.1649  331  HOH   B O   
7218 O  O   . HOH   F .   ? 0.2568 0.2049 0.5169 0.0157  0.0056  0.0344  332  HOH   B O   
7219 O  O   . HOH   F .   ? 0.2296 0.2486 0.5455 -0.0518 -0.0137 0.1599  333  HOH   B O   
7220 O  O   . HOH   F .   ? 0.4692 0.3305 0.5590 0.1529  0.2368  0.1909  334  HOH   B O   
7221 O  O   . HOH   F .   ? 0.5643 0.5835 0.5133 -0.1231 -0.0605 0.1389  335  HOH   B O   
7222 O  O   . HOH   F .   ? 0.6167 0.5317 0.6229 -0.1224 -0.1239 -0.1405 336  HOH   B O   
7223 O  O   . HOH   F .   ? 0.5989 0.5742 0.6723 0.1032  -0.1085 0.2575  337  HOH   B O   
7224 O  O   . HOH   F .   ? 0.1785 0.1516 0.2217 0.0076  -0.0129 0.0108  338  HOH   B O   
7225 O  O   . HOH   F .   ? 0.7807 0.2747 0.3725 0.0680  -0.0987 -0.0562 339  HOH   B O   
7226 O  O   . HOH   F .   ? 0.2730 0.5519 0.6648 -0.0127 -0.0725 0.0168  340  HOH   B O   
7227 O  O   . HOH   F .   ? 0.4015 0.6975 0.3991 -0.0297 -0.0728 0.2013  341  HOH   B O   
7228 O  O   . HOH   F .   ? 0.5178 0.3362 0.3108 0.0709  -0.1228 -0.0795 342  HOH   B O   
7229 O  O   . HOH   F .   ? 0.4934 0.6198 0.3539 0.0423  -0.1055 0.0321  343  HOH   B O   
7230 O  O   . HOH   F .   ? 0.4432 0.5488 0.4463 -0.1239 -0.0795 -0.0702 344  HOH   B O   
7231 O  O   . HOH   F .   ? 0.2926 0.1895 0.3939 0.0407  -0.1100 -0.0506 345  HOH   B O   
7232 O  O   . HOH   F .   ? 0.7401 0.6826 0.3693 0.0307  -0.0589 0.2218  346  HOH   B O   
7233 O  O   . HOH   F .   ? 0.4440 0.6654 0.5922 0.0014  -0.1055 0.0437  347  HOH   B O   
7234 O  O   . HOH   F .   ? 0.2171 0.2085 0.3542 -0.0152 0.0842  -0.0089 348  HOH   B O   
7235 O  O   . HOH   F .   ? 0.3207 0.4731 0.5296 -0.1404 0.0535  -0.0444 349  HOH   B O   
7236 O  O   . HOH   F .   ? 0.2389 0.6340 0.2901 0.1545  -0.0561 -0.1431 350  HOH   B O   
7237 O  O   . HOH   F .   ? 0.3036 0.2228 0.5124 -0.0388 -0.0771 -0.0546 351  HOH   B O   
7238 O  O   . HOH   F .   ? 0.5270 0.5480 0.5319 -0.1313 0.0623  0.0621  352  HOH   B O   
7239 O  O   . HOH   F .   ? 0.2388 0.4110 0.4677 0.0084  0.0518  0.0039  353  HOH   B O   
7240 O  O   . HOH   F .   ? 0.4270 0.6484 0.7282 0.0227  0.1053  -0.0605 354  HOH   B O   
7241 O  O   . HOH   F .   ? 0.3767 0.2275 0.3253 -0.0611 0.0232  -0.0827 355  HOH   B O   
7242 O  O   . HOH   F .   ? 0.4822 0.2850 0.5632 -0.1297 0.1768  0.0166  356  HOH   B O   
7243 O  O   . HOH   F .   ? 0.3791 0.2681 0.3841 -0.0831 -0.0179 -0.0623 357  HOH   B O   
7244 O  O   . HOH   F .   ? 0.5659 0.5168 0.5496 0.0555  0.1011  0.0495  358  HOH   B O   
7245 O  O   . HOH   F .   ? 0.4843 0.5841 0.5139 0.2114  -0.1124 0.1657  359  HOH   B O   
7246 O  O   . HOH   F .   ? 0.5211 0.3620 0.5153 0.0159  -0.1712 -0.0791 360  HOH   B O   
7247 O  O   . HOH   F .   ? 0.5091 0.3483 0.4708 0.0095  0.1524  -0.0287 361  HOH   B O   
7248 O  O   . HOH   F .   ? 0.5763 0.3880 0.5835 0.0657  0.1299  0.0938  362  HOH   B O   
7249 O  O   . HOH   F .   ? 0.2191 0.3779 0.6764 -0.0763 -0.0563 -0.0790 363  HOH   B O   
7250 O  O   . HOH   F .   ? 0.4098 0.6590 0.3245 0.2107  -0.0449 0.0319  364  HOH   B O   
7251 O  O   . HOH   F .   ? 0.6417 0.2504 0.3623 -0.0061 0.0559  0.0811  365  HOH   B O   
7252 O  O   . HOH   F .   ? 0.6605 0.4761 0.4349 0.1215  0.0866  0.0668  366  HOH   B O   
7253 O  O   . HOH   F .   ? 0.5700 0.3118 0.5922 -0.1276 0.0227  0.0201  367  HOH   B O   
7254 O  O   . HOH   F .   ? 0.6369 0.6628 0.3786 0.2085  -0.1440 0.1279  368  HOH   B O   
7255 O  O   . HOH   F .   ? 0.4772 0.3849 0.5368 0.1534  -0.1611 -0.0200 369  HOH   B O   
7256 O  O   . HOH   F .   ? 0.5058 0.5390 0.4672 0.0021  -0.0279 -0.1108 370  HOH   B O   
7257 O  O   . HOH   F .   ? 0.4325 0.5670 0.4980 0.2629  0.0281  0.0993  371  HOH   B O   
7258 O  O   . HOH   F .   ? 0.4509 0.3220 0.3230 0.0602  -0.1520 -0.0208 372  HOH   B O   
7259 O  O   . HOH   F .   ? 0.6402 0.3975 0.3005 -0.0860 -0.0982 -0.0856 373  HOH   B O   
7260 O  O   . HOH   F .   ? 0.8045 0.7565 0.5292 0.2923  -0.1233 0.1344  374  HOH   B O   
7261 O  O   . HOH   F .   ? 0.4843 0.7227 0.5824 0.1831  0.0752  0.2748  375  HOH   B O   
7262 O  O   . HOH   F .   ? 0.4300 0.4943 0.4585 -0.0751 -0.0716 0.0022  376  HOH   B O   
7263 O  O   . HOH   F .   ? 0.3010 0.4959 0.2059 0.0258  -0.0118 0.0238  377  HOH   B O   
7264 O  O   . HOH   F .   ? 0.6864 0.3459 0.4801 -0.0859 -0.0511 -0.0079 378  HOH   B O   
7265 O  O   . HOH   F .   ? 0.2270 0.3943 0.4281 0.0339  -0.0431 -0.0613 379  HOH   B O   
7266 O  O   . HOH   F .   ? 0.5184 0.7767 0.3693 -0.1399 0.0546  -0.1590 380  HOH   B O   
7267 O  O   . HOH   F .   ? 0.3695 0.5896 0.5316 0.0561  0.0168  -0.0368 381  HOH   B O   
7268 O  O   . HOH   F .   ? 0.5833 0.6961 0.6266 0.0024  0.2923  0.1125  382  HOH   B O   
7269 O  O   . HOH   F .   ? 0.2700 0.2545 0.3351 0.0071  0.0068  0.0266  383  HOH   B O   
7270 O  O   . HOH   F .   ? 0.4785 0.8685 0.5843 0.1372  0.1988  0.0537  384  HOH   B O   
7271 O  O   . HOH   F .   ? 0.8148 0.3904 0.4021 0.0803  0.0705  -0.0786 385  HOH   B O   
7272 O  O   . HOH   F .   ? 0.7300 0.6296 0.4140 0.2468  0.0130  0.0149  386  HOH   B O   
7273 O  O   . HOH   F .   ? 0.4713 0.5678 0.4478 0.0184  -0.0107 -0.0454 387  HOH   B O   
7274 O  O   . HOH   F .   ? 0.2178 0.4432 0.3855 -0.0517 -0.0647 -0.0656 388  HOH   B O   
7275 O  O   . HOH   F .   ? 0.6028 0.4046 0.6275 -0.0819 0.0518  0.0116  389  HOH   B O   
7276 O  O   . HOH   F .   ? 0.5569 0.3917 0.2629 0.0558  0.0773  -0.0087 390  HOH   B O   
7277 O  O   . HOH   F .   ? 0.4441 0.3016 0.4373 -0.1459 0.0100  0.0582  391  HOH   B O   
7278 O  O   . HOH   F .   ? 0.4408 0.2435 0.2968 0.1035  -0.0473 0.0170  392  HOH   B O   
7279 O  O   . HOH   F .   ? 0.5420 0.4234 0.3817 0.0515  0.0209  0.0934  393  HOH   B O   
7280 O  O   . HOH   F .   ? 0.4605 0.2222 0.4436 -0.0653 0.0051  0.0677  394  HOH   B O   
7281 O  O   . HOH   F .   ? 0.2398 0.4497 0.7023 -0.1226 -0.0537 -0.0205 395  HOH   B O   
7282 O  O   . HOH   F .   ? 0.4441 0.6293 0.3644 0.1038  -0.0083 -0.0948 396  HOH   B O   
7283 O  O   . HOH   F .   ? 0.3321 0.3676 0.4055 0.0130  0.0241  -0.0857 397  HOH   B O   
7284 O  O   . HOH   F .   ? 0.4679 0.4034 0.4362 0.0539  0.1151  0.0643  398  HOH   B O   
7285 O  O   . HOH   F .   ? 0.2183 0.2495 0.5956 -0.0500 -0.0810 0.0131  399  HOH   B O   
7286 O  O   . HOH   F .   ? 0.5367 0.4058 0.3144 -0.1940 -0.0377 0.1045  400  HOH   B O   
7287 O  O   . HOH   F .   ? 0.5786 0.6451 0.6524 0.0991  -0.1148 0.3153  401  HOH   B O   
7288 O  O   . HOH   F .   ? 0.6311 0.5828 0.3826 0.1956  -0.0613 -0.0610 402  HOH   B O   
# 
