data_7HFR
# 
_entry.id   7HFR 
# 
_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   7HFR         pdb_00007hfr 10.2210/pdb7hfr/pdb 
WWPDB D_1001407417 ?            ?                   
# 
_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                        7HFR 
_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 'DIMETHYL SULFOXIDE'                                                                78.133    1   ? ? ? ? 
3 non-polymer syn '(3aS,6S,6aR)-1-(7H-pyrrolo[2,3-d]pyrimidin-4-yl)octahydrocyclopenta[b]pyrrol-6-ol' 244.292   1   ? ? ? ? 
4 water       nat water                                                                               18.015    431 ? ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'nsp3, PL2-PRO, Papain-like protease, Papain-like proteinase, PL-PRO' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;SMVNSFSGYLKLTDNVYIKNADIVEEAKKVKPTVVVNAANVYLKHGGGVAGALNKATNNAMQVESDDYIATNGPLKVGGS
CVLSGHNLAKHCLHVVGPNVNKGEDIQLLKSAYENFNQHEVLLAPLLSAGIFGADPIHSLRVCVDTVRTNVYLAVFDKNL
YDKLVSSFL
;
_entity_poly.pdbx_seq_one_letter_code_can   
;SMVNSFSGYLKLTDNVYIKNADIVEEAKKVKPTVVVNAANVYLKHGGGVAGALNKATNNAMQVESDDYIATNGPLKVGGS
CVLSGHNLAKHCLHVVGPNVNKGEDIQLLKSAYENFNQHEVLLAPLLSAGIFGADPIHSLRVCVDTVRTNVYLAVFDKNL
YDKLVSSFL
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'DIMETHYL SULFOXIDE'                                                                DMS   
3 '(3aS,6S,6aR)-1-(7H-pyrrolo[2,3-d]pyrimidin-4-yl)octahydrocyclopenta[b]pyrrol-6-ol' A1BBS 
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 
A1BBS non-polymer         . '(3aS,6S,6aR)-1-(7H-pyrrolo[2,3-d]pyrimidin-4-yl)octahydrocyclopenta[b]pyrrol-6-ol' ? 'C13 H16 N4 O'   
244.292 
ALA   'L-peptide linking' y ALANINE                                                                             ? 'C3 H7 N O2'     
89.093  
ARG   'L-peptide linking' y ARGININE                                                                            ? 'C6 H15 N4 O2 1' 
175.209 
ASN   'L-peptide linking' y ASPARAGINE                                                                          ? 'C4 H8 N2 O3'    
132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID'                                                                     ? 'C4 H7 N O4'     
133.103 
CYS   'L-peptide linking' y CYSTEINE                                                                            ? 'C3 H7 N O2 S'   
121.158 
DMS   non-polymer         . 'DIMETHYL SULFOXIDE'                                                                ? 'C2 H6 O S'      
78.133  
GLN   'L-peptide linking' y GLUTAMINE                                                                           ? 'C5 H10 N2 O3'   
146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'                                                                     ? 'C5 H9 N O4'     
147.129 
GLY   'peptide linking'   y GLYCINE                                                                             ? 'C2 H5 N O2'     
75.067  
HIS   'L-peptide linking' y HISTIDINE                                                                           ? 'C6 H10 N3 O2 1' 
156.162 
HOH   non-polymer         . WATER                                                                               ? 'H2 O'           
18.015  
ILE   'L-peptide linking' y ISOLEUCINE                                                                          ? 'C6 H13 N O2'    
131.173 
LEU   'L-peptide linking' y LEUCINE                                                                             ? 'C6 H13 N O2'    
131.173 
LYS   'L-peptide linking' y LYSINE                                                                              ? 'C6 H15 N2 O2 1' 
147.195 
MET   'L-peptide linking' y METHIONINE                                                                          ? 'C5 H11 N O2 S'  
149.211 
PHE   'L-peptide linking' y PHENYLALANINE                                                                       ? 'C9 H11 N O2'    
165.189 
PRO   'L-peptide linking' y PROLINE                                                                             ? 'C5 H9 N O2'     
115.130 
SER   'L-peptide linking' y SERINE                                                                              ? 'C3 H7 N O3'     
105.093 
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 DMS   1   301 301  DMS   DMS A . 
D 3 A1BBS 1   302 201  A1BBS LA1 A . 
E 4 HOH   1   401 86   HOH   HOH A . 
E 4 HOH   2   402 109  HOH   HOH A . 
E 4 HOH   3   403 196  HOH   HOH A . 
E 4 HOH   4   404 1309 HOH   HOH A . 
E 4 HOH   5   405 199  HOH   HOH A . 
E 4 HOH   6   406 247  HOH   HOH A . 
E 4 HOH   7   407 292  HOH   HOH A . 
E 4 HOH   8   408 625  HOH   HOH A . 
E 4 HOH   9   409 209  HOH   HOH A . 
E 4 HOH   10  410 155  HOH   HOH A . 
E 4 HOH   11  411 1290 HOH   HOH A . 
E 4 HOH   12  412 151  HOH   HOH A . 
E 4 HOH   13  413 153  HOH   HOH A . 
E 4 HOH   14  414 952  HOH   HOH A . 
E 4 HOH   15  415 662  HOH   HOH A . 
E 4 HOH   16  416 1283 HOH   HOH A . 
E 4 HOH   17  417 964  HOH   HOH A . 
E 4 HOH   18  418 18   HOH   HOH A . 
E 4 HOH   19  419 192  HOH   HOH A . 
E 4 HOH   20  420 93   HOH   HOH A . 
E 4 HOH   21  421 630  HOH   HOH A . 
E 4 HOH   22  422 124  HOH   HOH A . 
E 4 HOH   23  423 76   HOH   HOH A . 
E 4 HOH   24  424 136  HOH   HOH A . 
E 4 HOH   25  425 661  HOH   HOH A . 
E 4 HOH   26  426 461  HOH   HOH A . 
E 4 HOH   27  427 1295 HOH   HOH A . 
E 4 HOH   28  428 236  HOH   HOH A . 
E 4 HOH   29  429 195  HOH   HOH A . 
E 4 HOH   30  430 4    HOH   HOH A . 
E 4 HOH   31  431 36   HOH   HOH A . 
E 4 HOH   32  432 396  HOH   HOH A . 
E 4 HOH   33  433 13   HOH   HOH A . 
E 4 HOH   34  434 225  HOH   HOH A . 
E 4 HOH   35  435 1296 HOH   HOH A . 
E 4 HOH   36  436 7    HOH   HOH A . 
E 4 HOH   37  437 337  HOH   HOH A . 
E 4 HOH   38  438 57   HOH   HOH A . 
E 4 HOH   39  439 26   HOH   HOH A . 
E 4 HOH   40  440 140  HOH   HOH A . 
E 4 HOH   41  441 1310 HOH   HOH A . 
E 4 HOH   42  442 15   HOH   HOH A . 
E 4 HOH   43  443 241  HOH   HOH A . 
E 4 HOH   44  444 229  HOH   HOH A . 
E 4 HOH   45  445 320  HOH   HOH A . 
E 4 HOH   46  446 1300 HOH   HOH A . 
E 4 HOH   47  447 17   HOH   HOH A . 
E 4 HOH   48  448 164  HOH   HOH A . 
E 4 HOH   49  449 162  HOH   HOH A . 
E 4 HOH   50  450 4    HOH   HOH A . 
E 4 HOH   51  451 6    HOH   HOH A . 
E 4 HOH   52  452 469  HOH   HOH A . 
E 4 HOH   53  453 42   HOH   HOH A . 
E 4 HOH   54  454 132  HOH   HOH A . 
E 4 HOH   55  455 165  HOH   HOH A . 
E 4 HOH   56  456 169  HOH   HOH A . 
E 4 HOH   57  457 33   HOH   HOH A . 
E 4 HOH   58  458 81   HOH   HOH A . 
E 4 HOH   59  459 21   HOH   HOH A . 
E 4 HOH   60  460 409  HOH   HOH A . 
E 4 HOH   61  461 105  HOH   HOH A . 
E 4 HOH   62  462 70   HOH   HOH A . 
E 4 HOH   63  463 27   HOH   HOH A . 
E 4 HOH   64  464 1275 HOH   HOH A . 
E 4 HOH   65  465 102  HOH   HOH A . 
E 4 HOH   66  466 78   HOH   HOH A . 
E 4 HOH   67  467 18   HOH   HOH A . 
E 4 HOH   68  468 139  HOH   HOH A . 
E 4 HOH   69  469 39   HOH   HOH A . 
E 4 HOH   70  470 12   HOH   HOH A . 
E 4 HOH   71  471 218  HOH   HOH A . 
E 4 HOH   72  472 939  HOH   HOH A . 
E 4 HOH   73  473 19   HOH   HOH A . 
E 4 HOH   74  474 66   HOH   HOH A . 
E 4 HOH   75  475 2    HOH   HOH A . 
E 4 HOH   76  476 92   HOH   HOH A . 
E 4 HOH   77  477 12   HOH   HOH A . 
E 4 HOH   78  478 56   HOH   HOH A . 
E 4 HOH   79  479 15   HOH   HOH A . 
E 4 HOH   80  480 23   HOH   HOH A . 
E 4 HOH   81  481 68   HOH   HOH A . 
E 4 HOH   82  482 5    HOH   HOH A . 
E 4 HOH   83  483 354  HOH   HOH A . 
E 4 HOH   84  484 138  HOH   HOH A . 
E 4 HOH   85  485 159  HOH   HOH A . 
E 4 HOH   86  486 45   HOH   HOH A . 
E 4 HOH   87  487 46   HOH   HOH A . 
E 4 HOH   88  488 35   HOH   HOH A . 
E 4 HOH   89  489 366  HOH   HOH A . 
E 4 HOH   90  490 134  HOH   HOH A . 
E 4 HOH   91  491 148  HOH   HOH A . 
E 4 HOH   92  492 49   HOH   HOH A . 
E 4 HOH   93  493 393  HOH   HOH A . 
E 4 HOH   94  494 96   HOH   HOH A . 
E 4 HOH   95  495 582  HOH   HOH A . 
E 4 HOH   96  496 405  HOH   HOH A . 
E 4 HOH   97  497 58   HOH   HOH A . 
E 4 HOH   98  498 154  HOH   HOH A . 
E 4 HOH   99  499 351  HOH   HOH A . 
E 4 HOH   100 500 116  HOH   HOH A . 
E 4 HOH   101 501 34   HOH   HOH A . 
E 4 HOH   102 502 85   HOH   HOH A . 
E 4 HOH   103 503 115  HOH   HOH A . 
E 4 HOH   104 504 74   HOH   HOH A . 
E 4 HOH   105 505 3    HOH   HOH A . 
E 4 HOH   106 506 8    HOH   HOH A . 
E 4 HOH   107 507 278  HOH   HOH A . 
E 4 HOH   108 508 281  HOH   HOH A . 
E 4 HOH   109 509 303  HOH   HOH A . 
E 4 HOH   110 510 6    HOH   HOH A . 
E 4 HOH   111 511 122  HOH   HOH A . 
E 4 HOH   112 512 21   HOH   HOH A . 
E 4 HOH   113 513 186  HOH   HOH A . 
E 4 HOH   114 514 1315 HOH   HOH A . 
E 4 HOH   115 515 1308 HOH   HOH A . 
E 4 HOH   116 516 83   HOH   HOH A . 
E 4 HOH   117 517 67   HOH   HOH A . 
E 4 HOH   118 518 1222 HOH   HOH A . 
E 4 HOH   119 519 123  HOH   HOH A . 
E 4 HOH   120 520 1289 HOH   HOH A . 
E 4 HOH   121 521 212  HOH   HOH A . 
E 4 HOH   122 522 24   HOH   HOH A . 
E 4 HOH   123 523 121  HOH   HOH A . 
E 4 HOH   124 524 53   HOH   HOH A . 
E 4 HOH   125 525 7    HOH   HOH A . 
E 4 HOH   126 526 51   HOH   HOH A . 
E 4 HOH   127 527 125  HOH   HOH A . 
E 4 HOH   128 528 493  HOH   HOH A . 
E 4 HOH   129 529 381  HOH   HOH A . 
E 4 HOH   130 530 397  HOH   HOH A . 
E 4 HOH   131 531 95   HOH   HOH A . 
E 4 HOH   132 532 333  HOH   HOH A . 
E 4 HOH   133 533 156  HOH   HOH A . 
E 4 HOH   134 534 944  HOH   HOH A . 
E 4 HOH   135 535 1068 HOH   HOH A . 
E 4 HOH   136 536 25   HOH   HOH A . 
E 4 HOH   137 537 296  HOH   HOH A . 
E 4 HOH   138 538 1313 HOH   HOH A . 
E 4 HOH   139 539 1238 HOH   HOH A . 
E 4 HOH   140 540 16   HOH   HOH A . 
E 4 HOH   141 541 71   HOH   HOH A . 
E 4 HOH   142 542 20   HOH   HOH A . 
E 4 HOH   143 543 16   HOH   HOH A . 
E 4 HOH   144 544 1279 HOH   HOH A . 
E 4 HOH   145 545 24   HOH   HOH A . 
E 4 HOH   146 546 14   HOH   HOH A . 
E 4 HOH   147 547 80   HOH   HOH A . 
E 4 HOH   148 548 73   HOH   HOH A . 
E 4 HOH   149 549 1189 HOH   HOH A . 
E 4 HOH   150 550 10   HOH   HOH A . 
E 4 HOH   151 551 104  HOH   HOH A . 
E 4 HOH   152 552 94   HOH   HOH A . 
E 4 HOH   153 553 576  HOH   HOH A . 
E 4 HOH   154 554 3    HOH   HOH A . 
E 4 HOH   155 555 2    HOH   HOH A . 
E 4 HOH   156 556 5    HOH   HOH A . 
E 4 HOH   157 557 97   HOH   HOH A . 
E 4 HOH   158 558 40   HOH   HOH A . 
E 4 HOH   159 559 79   HOH   HOH A . 
E 4 HOH   160 560 188  HOH   HOH A . 
E 4 HOH   161 561 17   HOH   HOH A . 
E 4 HOH   162 562 330  HOH   HOH A . 
E 4 HOH   163 563 726  HOH   HOH A . 
E 4 HOH   164 564 1094 HOH   HOH A . 
E 4 HOH   165 565 1286 HOH   HOH A . 
E 4 HOH   166 566 1134 HOH   HOH A . 
E 4 HOH   167 567 163  HOH   HOH A . 
E 4 HOH   168 568 1301 HOH   HOH A . 
E 4 HOH   169 569 107  HOH   HOH A . 
E 4 HOH   170 570 1119 HOH   HOH A . 
E 4 HOH   171 571 509  HOH   HOH A . 
E 4 HOH   172 572 361  HOH   HOH A . 
E 4 HOH   173 573 408  HOH   HOH A . 
E 4 HOH   174 574 556  HOH   HOH A . 
E 4 HOH   175 575 319  HOH   HOH A . 
E 4 HOH   176 576 756  HOH   HOH A . 
E 4 HOH   177 577 342  HOH   HOH A . 
E 4 HOH   178 578 1276 HOH   HOH A . 
E 4 HOH   179 579 801  HOH   HOH A . 
E 4 HOH   180 580 22   HOH   HOH A . 
E 4 HOH   181 581 126  HOH   HOH A . 
E 4 HOH   182 582 1307 HOH   HOH A . 
E 4 HOH   183 583 280  HOH   HOH A . 
E 4 HOH   184 584 250  HOH   HOH A . 
E 4 HOH   185 585 370  HOH   HOH A . 
E 4 HOH   186 586 63   HOH   HOH A . 
E 4 HOH   187 587 711  HOH   HOH A . 
E 4 HOH   188 588 224  HOH   HOH A . 
E 4 HOH   189 589 1306 HOH   HOH A . 
E 4 HOH   190 590 1287 HOH   HOH A . 
E 4 HOH   191 591 695  HOH   HOH A . 
E 4 HOH   192 592 674  HOH   HOH A . 
E 4 HOH   193 593 521  HOH   HOH A . 
E 4 HOH   194 594 135  HOH   HOH A . 
E 4 HOH   195 595 202  HOH   HOH A . 
E 4 HOH   196 596 9    HOH   HOH A . 
E 4 HOH   197 597 19   HOH   HOH A . 
E 4 HOH   198 598 919  HOH   HOH A . 
E 4 HOH   199 599 267  HOH   HOH A . 
E 4 HOH   200 600 318  HOH   HOH A . 
E 4 HOH   201 601 326  HOH   HOH A . 
E 4 HOH   202 602 11   HOH   HOH A . 
E 4 HOH   203 603 309  HOH   HOH A . 
E 4 HOH   204 604 331  HOH   HOH A . 
E 4 HOH   205 605 315  HOH   HOH A . 
E 4 HOH   206 606 981  HOH   HOH A . 
E 4 HOH   207 607 941  HOH   HOH A . 
E 4 HOH   208 608 805  HOH   HOH A . 
E 4 HOH   209 609 1299 HOH   HOH A . 
E 4 HOH   210 610 1314 HOH   HOH A . 
E 4 HOH   211 611 263  HOH   HOH A . 
E 4 HOH   212 612 152  HOH   HOH A . 
E 4 HOH   213 613 208  HOH   HOH A . 
E 4 HOH   214 614 180  HOH   HOH A . 
E 4 HOH   215 615 1071 HOH   HOH A . 
E 4 HOH   216 616 350  HOH   HOH A . 
E 4 HOH   217 617 8    HOH   HOH A . 
E 4 HOH   218 618 356  HOH   HOH A . 
E 4 HOH   219 619 363  HOH   HOH A . 
E 4 HOH   220 620 313  HOH   HOH A . 
E 4 HOH   221 621 371  HOH   HOH A . 
E 4 HOH   222 622 25   HOH   HOH A . 
E 4 HOH   223 623 1284 HOH   HOH A . 
E 4 HOH   224 624 185  HOH   HOH A . 
E 4 HOH   225 625 429  HOH   HOH A . 
E 4 HOH   226 626 772  HOH   HOH A . 
E 4 HOH   227 627 376  HOH   HOH A . 
E 4 HOH   228 628 1074 HOH   HOH A . 
E 4 HOH   229 629 1292 HOH   HOH A . 
E 4 HOH   230 630 346  HOH   HOH A . 
E 4 HOH   231 631 1078 HOH   HOH A . 
F 4 HOH   1   201 64   HOH   HOH B . 
F 4 HOH   2   202 398  HOH   HOH B . 
F 4 HOH   3   203 240  HOH   HOH B . 
F 4 HOH   4   204 358  HOH   HOH B . 
F 4 HOH   5   205 531  HOH   HOH B . 
F 4 HOH   6   206 120  HOH   HOH B . 
F 4 HOH   7   207 654  HOH   HOH B . 
F 4 HOH   8   208 549  HOH   HOH B . 
F 4 HOH   9   209 1249 HOH   HOH B . 
F 4 HOH   10  210 364  HOH   HOH B . 
F 4 HOH   11  211 758  HOH   HOH B . 
F 4 HOH   12  212 232  HOH   HOH B . 
F 4 HOH   13  213 900  HOH   HOH B . 
F 4 HOH   14  214 444  HOH   HOH B . 
F 4 HOH   15  215 264  HOH   HOH B . 
F 4 HOH   16  216 50   HOH   HOH B . 
F 4 HOH   17  217 353  HOH   HOH B . 
F 4 HOH   18  218 743  HOH   HOH B . 
F 4 HOH   19  219 332  HOH   HOH B . 
F 4 HOH   20  220 452  HOH   HOH B . 
F 4 HOH   21  221 166  HOH   HOH B . 
F 4 HOH   22  222 54   HOH   HOH B . 
F 4 HOH   23  223 343  HOH   HOH B . 
F 4 HOH   24  224 276  HOH   HOH B . 
F 4 HOH   25  225 282  HOH   HOH B . 
F 4 HOH   26  226 82   HOH   HOH B . 
F 4 HOH   27  227 1278 HOH   HOH B . 
F 4 HOH   28  228 131  HOH   HOH B . 
F 4 HOH   29  229 252  HOH   HOH B . 
F 4 HOH   30  230 110  HOH   HOH B . 
F 4 HOH   31  231 127  HOH   HOH B . 
F 4 HOH   32  232 181  HOH   HOH B . 
F 4 HOH   33  233 272  HOH   HOH B . 
F 4 HOH   34  234 75   HOH   HOH B . 
F 4 HOH   35  235 128  HOH   HOH B . 
F 4 HOH   36  236 205  HOH   HOH B . 
F 4 HOH   37  237 300  HOH   HOH B . 
F 4 HOH   38  238 60   HOH   HOH B . 
F 4 HOH   39  239 325  HOH   HOH B . 
F 4 HOH   40  240 1    HOH   HOH B . 
F 4 HOH   41  241 150  HOH   HOH B . 
F 4 HOH   42  242 341  HOH   HOH B . 
F 4 HOH   43  243 129  HOH   HOH B . 
F 4 HOH   44  244 72   HOH   HOH B . 
F 4 HOH   45  245 62   HOH   HOH B . 
F 4 HOH   46  246 41   HOH   HOH B . 
F 4 HOH   47  247 69   HOH   HOH B . 
F 4 HOH   48  248 391  HOH   HOH B . 
F 4 HOH   49  249 9    HOH   HOH B . 
F 4 HOH   50  250 133  HOH   HOH B . 
F 4 HOH   51  251 14   HOH   HOH B . 
F 4 HOH   52  252 271  HOH   HOH B . 
F 4 HOH   53  253 30   HOH   HOH B . 
F 4 HOH   54  254 103  HOH   HOH B . 
F 4 HOH   55  255 144  HOH   HOH B . 
F 4 HOH   56  256 723  HOH   HOH B . 
F 4 HOH   57  257 47   HOH   HOH B . 
F 4 HOH   58  258 117  HOH   HOH B . 
F 4 HOH   59  259 10   HOH   HOH B . 
F 4 HOH   60  260 20   HOH   HOH B . 
F 4 HOH   61  261 31   HOH   HOH B . 
F 4 HOH   62  262 52   HOH   HOH B . 
F 4 HOH   63  263 143  HOH   HOH B . 
F 4 HOH   64  264 84   HOH   HOH B . 
F 4 HOH   65  265 1140 HOH   HOH B . 
F 4 HOH   66  266 1106 HOH   HOH B . 
F 4 HOH   67  267 242  HOH   HOH B . 
F 4 HOH   68  268 147  HOH   HOH B . 
F 4 HOH   69  269 175  HOH   HOH B . 
F 4 HOH   70  270 347  HOH   HOH B . 
F 4 HOH   71  271 172  HOH   HOH B . 
F 4 HOH   72  272 114  HOH   HOH B . 
F 4 HOH   73  273 416  HOH   HOH B . 
F 4 HOH   74  274 1277 HOH   HOH B . 
F 4 HOH   75  275 59   HOH   HOH B . 
F 4 HOH   76  276 11   HOH   HOH B . 
F 4 HOH   77  277 231  HOH   HOH B . 
F 4 HOH   78  278 1312 HOH   HOH B . 
F 4 HOH   79  279 77   HOH   HOH B . 
F 4 HOH   80  280 61   HOH   HOH B . 
F 4 HOH   81  281 635  HOH   HOH B . 
F 4 HOH   82  282 220  HOH   HOH B . 
F 4 HOH   83  283 88   HOH   HOH B . 
F 4 HOH   84  284 1305 HOH   HOH B . 
F 4 HOH   85  285 287  HOH   HOH B . 
F 4 HOH   86  286 43   HOH   HOH B . 
F 4 HOH   87  287 1066 HOH   HOH B . 
F 4 HOH   88  288 22   HOH   HOH B . 
F 4 HOH   89  289 387  HOH   HOH B . 
F 4 HOH   90  290 106  HOH   HOH B . 
F 4 HOH   91  291 243  HOH   HOH B . 
F 4 HOH   92  292 311  HOH   HOH B . 
F 4 HOH   93  293 235  HOH   HOH B . 
F 4 HOH   94  294 89   HOH   HOH B . 
F 4 HOH   95  295 13   HOH   HOH B . 
F 4 HOH   96  296 137  HOH   HOH B . 
F 4 HOH   97  297 302  HOH   HOH B . 
F 4 HOH   98  298 170  HOH   HOH B . 
F 4 HOH   99  299 215  HOH   HOH B . 
F 4 HOH   100 300 316  HOH   HOH B . 
F 4 HOH   101 301 297  HOH   HOH B . 
F 4 HOH   102 302 160  HOH   HOH B . 
F 4 HOH   103 303 99   HOH   HOH B . 
F 4 HOH   104 304 299  HOH   HOH B . 
F 4 HOH   105 305 23   HOH   HOH B . 
F 4 HOH   106 306 142  HOH   HOH B . 
F 4 HOH   107 307 216  HOH   HOH B . 
F 4 HOH   108 308 221  HOH   HOH B . 
F 4 HOH   109 309 101  HOH   HOH B . 
F 4 HOH   110 310 1126 HOH   HOH B . 
F 4 HOH   111 311 48   HOH   HOH B . 
F 4 HOH   112 312 32   HOH   HOH B . 
F 4 HOH   113 313 112  HOH   HOH B . 
F 4 HOH   114 314 91   HOH   HOH B . 
F 4 HOH   115 315 1291 HOH   HOH B . 
F 4 HOH   116 316 37   HOH   HOH B . 
F 4 HOH   117 317 141  HOH   HOH B . 
F 4 HOH   118 318 118  HOH   HOH B . 
F 4 HOH   119 319 38   HOH   HOH B . 
F 4 HOH   120 320 100  HOH   HOH B . 
F 4 HOH   121 321 44   HOH   HOH B . 
F 4 HOH   122 322 177  HOH   HOH B . 
F 4 HOH   123 323 1294 HOH   HOH B . 
F 4 HOH   124 324 334  HOH   HOH B . 
F 4 HOH   125 325 197  HOH   HOH B . 
F 4 HOH   126 326 182  HOH   HOH B . 
F 4 HOH   127 327 1285 HOH   HOH B . 
F 4 HOH   128 328 161  HOH   HOH B . 
F 4 HOH   129 329 28   HOH   HOH B . 
F 4 HOH   130 330 29   HOH   HOH B . 
F 4 HOH   131 331 55   HOH   HOH B . 
F 4 HOH   132 332 717  HOH   HOH B . 
F 4 HOH   133 333 98   HOH   HOH B . 
F 4 HOH   134 334 207  HOH   HOH B . 
F 4 HOH   135 335 445  HOH   HOH B . 
F 4 HOH   136 336 704  HOH   HOH B . 
F 4 HOH   137 337 1274 HOH   HOH B . 
F 4 HOH   138 338 65   HOH   HOH B . 
F 4 HOH   139 339 234  HOH   HOH B . 
F 4 HOH   140 340 1293 HOH   HOH B . 
F 4 HOH   141 341 960  HOH   HOH B . 
F 4 HOH   142 342 339  HOH   HOH B . 
F 4 HOH   143 343 619  HOH   HOH B . 
F 4 HOH   144 344 362  HOH   HOH B . 
F 4 HOH   145 345 87   HOH   HOH B . 
F 4 HOH   146 346 1304 HOH   HOH B . 
F 4 HOH   147 347 90   HOH   HOH B . 
F 4 HOH   148 348 203  HOH   HOH B . 
F 4 HOH   149 349 191  HOH   HOH B . 
F 4 HOH   150 350 178  HOH   HOH B . 
F 4 HOH   151 351 463  HOH   HOH B . 
F 4 HOH   152 352 1046 HOH   HOH B . 
F 4 HOH   153 353 1280 HOH   HOH B . 
F 4 HOH   154 354 335  HOH   HOH B . 
F 4 HOH   155 355 623  HOH   HOH B . 
F 4 HOH   156 356 304  HOH   HOH B . 
F 4 HOH   157 357 1077 HOH   HOH B . 
F 4 HOH   158 358 541  HOH   HOH B . 
F 4 HOH   159 359 290  HOH   HOH B . 
F 4 HOH   160 360 389  HOH   HOH B . 
F 4 HOH   161 361 718  HOH   HOH B . 
F 4 HOH   162 362 283  HOH   HOH B . 
F 4 HOH   163 363 479  HOH   HOH B . 
F 4 HOH   164 364 1072 HOH   HOH B . 
F 4 HOH   165 365 291  HOH   HOH B . 
F 4 HOH   166 366 340  HOH   HOH B . 
F 4 HOH   167 367 373  HOH   HOH B . 
F 4 HOH   168 368 898  HOH   HOH B . 
F 4 HOH   169 369 615  HOH   HOH B . 
F 4 HOH   170 370 310  HOH   HOH B . 
F 4 HOH   171 371 667  HOH   HOH B . 
F 4 HOH   172 372 1303 HOH   HOH B . 
F 4 HOH   173 373 1316 HOH   HOH B . 
F 4 HOH   174 374 190  HOH   HOH B . 
F 4 HOH   175 375 149  HOH   HOH B . 
F 4 HOH   176 376 431  HOH   HOH B . 
F 4 HOH   177 377 183  HOH   HOH B . 
F 4 HOH   178 378 418  HOH   HOH B . 
F 4 HOH   179 379 1173 HOH   HOH B . 
F 4 HOH   180 380 1311 HOH   HOH B . 
F 4 HOH   181 381 1163 HOH   HOH B . 
F 4 HOH   182 382 424  HOH   HOH B . 
F 4 HOH   183 383 176  HOH   HOH B . 
F 4 HOH   184 384 1000 HOH   HOH B . 
F 4 HOH   185 385 470  HOH   HOH B . 
F 4 HOH   186 386 491  HOH   HOH B . 
F 4 HOH   187 387 1298 HOH   HOH B . 
F 4 HOH   188 388 265  HOH   HOH B . 
F 4 HOH   189 389 248  HOH   HOH B . 
F 4 HOH   190 390 184  HOH   HOH B . 
F 4 HOH   191 391 410  HOH   HOH B . 
F 4 HOH   192 392 355  HOH   HOH B . 
F 4 HOH   193 393 360  HOH   HOH B . 
F 4 HOH   194 394 792  HOH   HOH B . 
F 4 HOH   195 395 566  HOH   HOH B . 
F 4 HOH   196 396 157  HOH   HOH B . 
F 4 HOH   197 397 314  HOH   HOH B . 
F 4 HOH   198 398 274  HOH   HOH B . 
F 4 HOH   199 399 321  HOH   HOH B . 
F 4 HOH   200 400 558  HOH   HOH B . 
# 
loop_
_software.pdbx_ordinal 
_software.name 
_software.version 
_software.date 
_software.type 
_software.contact_author 
_software.contact_author_email 
_software.classification 
_software.location 
_software.language 
_software.citation_id 
1 PHENIX      1.21.1_5286    ?               package 'Paul D. Adams'   PDAdams@lbl.gov                         refinement        
http://www.phenix-online.org/                                                C++ ? 
2 Aimless     0.7.15         02/11/23        program 'Phil Evans'      ?                                       'data scaling'    
http://www.mrc-lmb.cam.ac.uk/harry/pre/aimless.html                          ?   ? 
3 PDB_EXTRACT 3.28           'Apr. 15, 2021' package PDB               deposit@deposit.rcsb.org                'data extraction' 
http://sw-tools.pdb.org/apps/PDB_EXTRACT/                                    C++ ? 
4 XDS         'Jun 30, 2023' 'Jun. 30, 2023' program 'Wolfgang Kabsch' Wolfgang.Kabsch@mpimf-heidelberg.mpg.de 'data reduction'  
http://xds.mpimf-heidelberg.mpg.de                                           ?   ? 
5 PHASER      2.8.3          'May 17, 2020'  program 'Randy J. Read'   cimr-phaser@lists.cam.ac.uk             phasing           
https://www.phaser.cimr.cam.ac.uk/index.php/Phaser_Crystallographic_Software ?   ? 
# 
_cell.entry_id           7HFR 
_cell.length_a           88.572 
_cell.length_b           88.572 
_cell.length_c           39.634 
_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                         7HFR 
_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          7HFR 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_Matthews      2.14 
_exptl_crystal.density_percent_sol   42.56 
_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                     7HFR 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             44.290 
_reflns.d_resolution_high            0.970 
_reflns.number_obs                   180411 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         99.400 
_reflns.pdbx_Rmerge_I_obs            0.054 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        14.000 
_reflns.B_iso_Wilson_estimate        11.440 
_reflns.pdbx_redundancy              6.200 
_reflns.pdbx_Rrim_I_all              0.059 
_reflns.pdbx_Rpim_I_all              0.023 
_reflns.pdbx_CC_half                 0.999 
_reflns.pdbx_netI_over_av_sigmaI     ? 
_reflns.pdbx_number_measured_all     1114315 
_reflns.pdbx_scaling_rejects         ? 
_reflns.pdbx_chi_squared             ? 
_reflns.Rmerge_F_all                 ? 
_reflns.Rmerge_F_obs                 ? 
_reflns.observed_criterion_F_max     ? 
_reflns.observed_criterion_F_min     ? 
_reflns.observed_criterion_I_max     ? 
_reflns.observed_criterion_I_min     ? 
_reflns.pdbx_d_res_high_opt          ? 
_reflns.pdbx_d_res_low_opt           ? 
_reflns.details                      ? 
# 
loop_
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_ordinal 
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.number_measured_obs 
_reflns_shell.number_measured_all 
_reflns_shell.number_unique_obs 
_reflns_shell.pdbx_rejects 
_reflns_shell.Rmerge_I_obs 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.pdbx_Rsym_value 
_reflns_shell.pdbx_chi_squared 
_reflns_shell.pdbx_redundancy 
_reflns_shell.percent_possible_obs 
_reflns_shell.pdbx_netI_over_sigmaI_obs 
_reflns_shell.number_possible 
_reflns_shell.number_unique_all 
_reflns_shell.Rmerge_F_all 
_reflns_shell.Rmerge_F_obs 
_reflns_shell.Rmerge_I_all 
_reflns_shell.meanI_over_sigI_all 
_reflns_shell.percent_possible_all 
_reflns_shell.pdbx_Rrim_I_all 
_reflns_shell.pdbx_Rpim_I_all 
_reflns_shell.pdbx_CC_half 
1 1 0.970 0.990  ? 25876 8124 ? 0.809 ? ? ? 3.200 ? 0.900  ? ? ? ? ? ? 91.300 0.964 0.506 0.670 
1 2 5.310 44.290 ? 8287  1200 ? 0.046 ? ? ? 6.900 ? 38.900 ? ? ? ? ? ? 99.800 0.050 0.019 0.998 
# 
_refine.entry_id                                 7HFR 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_d_res_high                            0.9700 
_refine.ls_d_res_low                             44.2900 
_refine.pdbx_ls_sigma_F                          1.360 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.ls_percent_reflns_obs                    99.2900 
_refine.ls_number_reflns_obs                     180319 
_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                          0.1433 
_refine.ls_R_factor_R_work                       0.1426 
_refine.ls_wR_factor_R_work                      ? 
_refine.ls_R_factor_R_free                       0.1567 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_percent_reflns_R_free                 4.8200 
_refine.ls_number_reflns_R_free                  8699 
_refine.ls_number_reflns_R_work                  171620 
_refine.ls_R_factor_R_free_error                 ? 
_refine.B_iso_mean                               18.9189 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.overall_SU_R_free                        ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.overall_SU_ML                            0.1100 
_refine.overall_SU_B                             ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.pdbx_solvent_vdw_probe_radii             1.1000 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.B_iso_max                                74.290 
_refine.B_iso_min                                7.680 
_refine.pdbx_overall_phase_error                 17.1500 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_R_factor_R_free_error_details         ? 
# 
_refine_hist.cycle_id                         final 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.d_res_high                       0.9700 
_refine_hist.d_res_low                        44.2900 
_refine_hist.pdbx_number_atoms_ligand         44 
_refine_hist.number_atoms_solvent             431 
_refine_hist.number_atoms_total               3017 
_refine_hist.pdbx_number_residues_total       336 
_refine_hist.pdbx_B_iso_mean_ligand           19.90 
_refine_hist.pdbx_B_iso_mean_solvent          31.01 
_refine_hist.pdbx_number_atoms_protein        2542 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
# 
loop_
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.R_factor_R_free 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.pdbx_refine_id 
0.9700 0.9800  30 89.0000  5038 . 0.4055 0.4072 . 276 0.0000 5314 . 'X-RAY DIFFRACTION' 
0.9800 0.9900  30 95.0000  5524 . 0.3428 0.3457 . 264 0.0000 5788 . 'X-RAY DIFFRACTION' 
0.9900 1.0000  30 97.0000  5528 . 0.2995 0.3264 . 287 0.0000 5815 . 'X-RAY DIFFRACTION' 
1.0000 1.0200  30 99.0000  5705 . 0.2623 0.2414 . 278 0.0000 5983 . 'X-RAY DIFFRACTION' 
1.0200 1.0300  30 100.0000 5746 . 0.2254 0.2520 . 243 0.0000 5989 . 'X-RAY DIFFRACTION' 
1.0300 1.0400  30 100.0000 5731 . 0.2051 0.2055 . 327 0.0000 6058 . 'X-RAY DIFFRACTION' 
1.0400 1.0600  30 100.0000 5640 . 0.1890 0.1945 . 316 0.0000 5956 . 'X-RAY DIFFRACTION' 
1.0600 1.0800  30 100.0000 5748 . 0.1821 0.2207 . 299 0.0000 6047 . 'X-RAY DIFFRACTION' 
1.0800 1.0900  30 100.0000 5732 . 0.1630 0.2044 . 289 0.0000 6021 . 'X-RAY DIFFRACTION' 
1.0900 1.1100  30 100.0000 5746 . 0.1580 0.1732 . 284 0.0000 6030 . 'X-RAY DIFFRACTION' 
1.1100 1.1300  30 100.0000 5759 . 0.1437 0.1640 . 276 0.0000 6035 . 'X-RAY DIFFRACTION' 
1.1300 1.1500  30 100.0000 5727 . 0.1355 0.1578 . 278 0.0000 6005 . 'X-RAY DIFFRACTION' 
1.1500 1.1700  30 100.0000 5737 . 0.1238 0.1488 . 299 0.0000 6036 . 'X-RAY DIFFRACTION' 
1.1700 1.2000  30 100.0000 5792 . 0.1188 0.1447 . 284 0.0000 6076 . 'X-RAY DIFFRACTION' 
1.2000 1.2200  30 100.0000 5644 . 0.1137 0.1450 . 306 0.0000 5950 . 'X-RAY DIFFRACTION' 
1.2200 1.2500  30 100.0000 5784 . 0.1174 0.1331 . 287 0.0000 6071 . 'X-RAY DIFFRACTION' 
1.2500 1.2800  30 100.0000 5727 . 0.1191 0.1280 . 279 0.0000 6006 . 'X-RAY DIFFRACTION' 
1.2800 1.3200  30 100.0000 5757 . 0.1224 0.1478 . 307 0.0000 6064 . 'X-RAY DIFFRACTION' 
1.3200 1.3600  30 100.0000 5715 . 0.1286 0.1425 . 299 0.0000 6014 . 'X-RAY DIFFRACTION' 
1.3600 1.4000  30 100.0000 5784 . 0.1246 0.1533 . 273 0.0000 6057 . 'X-RAY DIFFRACTION' 
1.4000 1.4500  30 100.0000 5774 . 0.1228 0.1444 . 293 0.0000 6067 . 'X-RAY DIFFRACTION' 
1.4500 1.5100  30 100.0000 5774 . 0.1166 0.1191 . 283 0.0000 6057 . 'X-RAY DIFFRACTION' 
1.5100 1.5800  30 100.0000 5774 . 0.1162 0.1290 . 291 0.0000 6065 . 'X-RAY DIFFRACTION' 
1.5800 1.6600  30 100.0000 5745 . 0.1183 0.1274 . 308 0.0000 6053 . 'X-RAY DIFFRACTION' 
1.6600 1.7600  30 100.0000 5846 . 0.1277 0.1263 . 262 0.0000 6108 . 'X-RAY DIFFRACTION' 
1.7600 1.9000  30 100.0000 5755 . 0.1337 0.1370 . 307 0.0000 6062 . 'X-RAY DIFFRACTION' 
1.9000 2.0900  30 100.0000 5820 . 0.1346 0.1399 . 296 0.0000 6116 . 'X-RAY DIFFRACTION' 
2.0900 2.3900  30 100.0000 5736 . 0.1372 0.1354 . 320 0.0000 6056 . 'X-RAY DIFFRACTION' 
2.3900 3.0100  30 100.0000 5867 . 0.1478 0.1625 . 297 0.0000 6164 . 'X-RAY DIFFRACTION' 
3.0100 44.2900 30 100.0000 5965 . 0.1507 0.1807 . 291 0.0000 6256 . 'X-RAY DIFFRACTION' 
# 
_struct.entry_id                  7HFR 
_struct.title                     
'PanDDA analysis group deposition -- Crystal structure of SARS-CoV-2 NSP3 macrodomain in complex with AVI-0005997' 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_details        ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HFR 
_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 7HFR A 3 ? 169 ? P0DTD1 1025 ? 1191 ? 3 169 
2 1 7HFR 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 7HFR SER A 1 ? UNP P0DTD1 ? ? 'expression tag' 1 1 
1 7HFR MET A 2 ? UNP P0DTD1 ? ? 'expression tag' 2 2 
2 7HFR SER B 1 ? UNP P0DTD1 ? ? 'expression tag' 1 3 
2 7HFR 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 TYR A 17  ? N TYR A 17  O LEU A 153 ? O LEU A 153 
AA1 3 4 O TYR A 152 ? O TYR A 152 N LEU A 122 ? N LEU A 122 
AA2 1 2 N ASN A 37  ? N ASN A 37  O LEU A 93  ? O LEU A 93  
AA2 2 3 O CYS A 92  ? O CYS A 92  N LEU A 83  ? N LEU A 83  
AA3 1 2 N LEU B 10  ? N LEU B 10  O ILE B 18  ? O ILE B 18  
AA3 2 3 N TYR B 17  ? N TYR B 17  O LEU B 153 ? O LEU B 153 
AA3 3 4 O TYR B 152 ? O TYR B 152 N LEU B 122 ? N LEU B 122 
AA4 1 2 N ASN B 37  ? N ASN B 37  O VAL B 95  ? O VAL B 95  
AA4 2 3 O CYS B 92  ? O CYS B 92  N LEU B 83  ? N LEU B 83  
# 
_pdbx_entry_details.entry_id                   7HFR 
_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 ? ? 55.06 -130.68 
2 1 HIS A 86 ? ? 55.06 -133.71 
3 1 HIS B 86 ? ? 57.24 -128.60 
# 
_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 630 ? 5.95 . 
2 1 O ? A HOH 631 ? 7.66 . 
3 1 O ? B HOH 400 ? 6.33 . 
# 
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 
A1BBS N2   N Y N 1   
A1BBS C3   C N N 2   
A1BBS C6   C N N 3   
A1BBS C9   C Y N 4   
A1BBS C12  C Y N 5   
A1BBS C1   C N S 6   
A1BBS C10  C Y N 7   
A1BBS C11  C Y N 8   
A1BBS C13  C N R 9   
A1BBS C2   C N N 10  
A1BBS C4   C N S 11  
A1BBS C5   C N N 12  
A1BBS C7   C Y N 13  
A1BBS C8   C Y N 14  
A1BBS N1   N N N 15  
A1BBS N3   N Y N 16  
A1BBS N4   N Y N 17  
A1BBS O1   O N N 18  
A1BBS H8   H N N 19  
A1BBS H7   H N N 20  
A1BBS H11  H N N 21  
A1BBS H12  H N N 22  
A1BBS H15  H N N 23  
A1BBS H1   H N N 24  
A1BBS H14  H N N 25  
A1BBS H3   H N N 26  
A1BBS H6   H N N 27  
A1BBS H5   H N N 28  
A1BBS H2   H N N 29  
A1BBS H10  H N N 30  
A1BBS H9   H N N 31  
A1BBS H13  H N N 32  
A1BBS H16  H N N 33  
A1BBS H4   H N N 34  
ALA   N    N N N 35  
ALA   CA   C N S 36  
ALA   C    C N N 37  
ALA   O    O N N 38  
ALA   CB   C N N 39  
ALA   OXT  O N N 40  
ALA   H    H N N 41  
ALA   H2   H N N 42  
ALA   HA   H N N 43  
ALA   HB1  H N N 44  
ALA   HB2  H N N 45  
ALA   HB3  H N N 46  
ALA   HXT  H N N 47  
ARG   N    N N N 48  
ARG   CA   C N S 49  
ARG   C    C N N 50  
ARG   O    O N N 51  
ARG   CB   C N N 52  
ARG   CG   C N N 53  
ARG   CD   C N N 54  
ARG   NE   N N N 55  
ARG   CZ   C N N 56  
ARG   NH1  N N N 57  
ARG   NH2  N N N 58  
ARG   OXT  O N N 59  
ARG   H    H N N 60  
ARG   H2   H N N 61  
ARG   HA   H N N 62  
ARG   HB2  H N N 63  
ARG   HB3  H N N 64  
ARG   HG2  H N N 65  
ARG   HG3  H N N 66  
ARG   HD2  H N N 67  
ARG   HD3  H N N 68  
ARG   HE   H N N 69  
ARG   HH11 H N N 70  
ARG   HH12 H N N 71  
ARG   HH21 H N N 72  
ARG   HH22 H N N 73  
ARG   HXT  H N N 74  
ASN   N    N N N 75  
ASN   CA   C N S 76  
ASN   C    C N N 77  
ASN   O    O N N 78  
ASN   CB   C N N 79  
ASN   CG   C N N 80  
ASN   OD1  O N N 81  
ASN   ND2  N N N 82  
ASN   OXT  O N N 83  
ASN   H    H N N 84  
ASN   H2   H N N 85  
ASN   HA   H N N 86  
ASN   HB2  H N N 87  
ASN   HB3  H N N 88  
ASN   HD21 H N N 89  
ASN   HD22 H N N 90  
ASN   HXT  H N N 91  
ASP   N    N N N 92  
ASP   CA   C N S 93  
ASP   C    C N N 94  
ASP   O    O N N 95  
ASP   CB   C N N 96  
ASP   CG   C N N 97  
ASP   OD1  O N N 98  
ASP   OD2  O N N 99  
ASP   OXT  O N N 100 
ASP   H    H N N 101 
ASP   H2   H N N 102 
ASP   HA   H N N 103 
ASP   HB2  H N N 104 
ASP   HB3  H N N 105 
ASP   HD2  H N N 106 
ASP   HXT  H N N 107 
CYS   N    N N N 108 
CYS   CA   C N R 109 
CYS   C    C N N 110 
CYS   O    O N N 111 
CYS   CB   C N N 112 
CYS   SG   S N N 113 
CYS   OXT  O N N 114 
CYS   H    H N N 115 
CYS   H2   H N N 116 
CYS   HA   H N N 117 
CYS   HB2  H N N 118 
CYS   HB3  H N N 119 
CYS   HG   H N N 120 
CYS   HXT  H N N 121 
DMS   S    S N N 122 
DMS   O    O N N 123 
DMS   C1   C N N 124 
DMS   C2   C N N 125 
DMS   H11  H N N 126 
DMS   H12  H N N 127 
DMS   H13  H N N 128 
DMS   H21  H N N 129 
DMS   H22  H N N 130 
DMS   H23  H N N 131 
GLN   N    N N N 132 
GLN   CA   C N S 133 
GLN   C    C N N 134 
GLN   O    O N N 135 
GLN   CB   C N N 136 
GLN   CG   C N N 137 
GLN   CD   C N N 138 
GLN   OE1  O N N 139 
GLN   NE2  N N N 140 
GLN   OXT  O N N 141 
GLN   H    H N N 142 
GLN   H2   H N N 143 
GLN   HA   H N N 144 
GLN   HB2  H N N 145 
GLN   HB3  H N N 146 
GLN   HG2  H N N 147 
GLN   HG3  H N N 148 
GLN   HE21 H N N 149 
GLN   HE22 H N N 150 
GLN   HXT  H N N 151 
GLU   N    N N N 152 
GLU   CA   C N S 153 
GLU   C    C N N 154 
GLU   O    O N N 155 
GLU   CB   C N N 156 
GLU   CG   C N N 157 
GLU   CD   C N N 158 
GLU   OE1  O N N 159 
GLU   OE2  O N N 160 
GLU   OXT  O N N 161 
GLU   H    H N N 162 
GLU   H2   H N N 163 
GLU   HA   H N N 164 
GLU   HB2  H N N 165 
GLU   HB3  H N N 166 
GLU   HG2  H N N 167 
GLU   HG3  H N N 168 
GLU   HE2  H N N 169 
GLU   HXT  H N N 170 
GLY   N    N N N 171 
GLY   CA   C N N 172 
GLY   C    C N N 173 
GLY   O    O N N 174 
GLY   OXT  O N N 175 
GLY   H    H N N 176 
GLY   H2   H N N 177 
GLY   HA2  H N N 178 
GLY   HA3  H N N 179 
GLY   HXT  H N N 180 
HIS   N    N N N 181 
HIS   CA   C N S 182 
HIS   C    C N N 183 
HIS   O    O N N 184 
HIS   CB   C N N 185 
HIS   CG   C Y N 186 
HIS   ND1  N Y N 187 
HIS   CD2  C Y N 188 
HIS   CE1  C Y N 189 
HIS   NE2  N Y N 190 
HIS   OXT  O N N 191 
HIS   H    H N N 192 
HIS   H2   H N N 193 
HIS   HA   H N N 194 
HIS   HB2  H N N 195 
HIS   HB3  H N N 196 
HIS   HD1  H N N 197 
HIS   HD2  H N N 198 
HIS   HE1  H N N 199 
HIS   HE2  H N N 200 
HIS   HXT  H N N 201 
HOH   O    O N N 202 
HOH   H1   H N N 203 
HOH   H2   H N N 204 
ILE   N    N N N 205 
ILE   CA   C N S 206 
ILE   C    C N N 207 
ILE   O    O N N 208 
ILE   CB   C N S 209 
ILE   CG1  C N N 210 
ILE   CG2  C N N 211 
ILE   CD1  C N N 212 
ILE   OXT  O N N 213 
ILE   H    H N N 214 
ILE   H2   H N N 215 
ILE   HA   H N N 216 
ILE   HB   H N N 217 
ILE   HG12 H N N 218 
ILE   HG13 H N N 219 
ILE   HG21 H N N 220 
ILE   HG22 H N N 221 
ILE   HG23 H N N 222 
ILE   HD11 H N N 223 
ILE   HD12 H N N 224 
ILE   HD13 H N N 225 
ILE   HXT  H N N 226 
LEU   N    N N N 227 
LEU   CA   C N S 228 
LEU   C    C N N 229 
LEU   O    O N N 230 
LEU   CB   C N N 231 
LEU   CG   C N N 232 
LEU   CD1  C N N 233 
LEU   CD2  C N N 234 
LEU   OXT  O N N 235 
LEU   H    H N N 236 
LEU   H2   H N N 237 
LEU   HA   H N N 238 
LEU   HB2  H N N 239 
LEU   HB3  H N N 240 
LEU   HG   H N N 241 
LEU   HD11 H N N 242 
LEU   HD12 H N N 243 
LEU   HD13 H N N 244 
LEU   HD21 H N N 245 
LEU   HD22 H N N 246 
LEU   HD23 H N N 247 
LEU   HXT  H N N 248 
LYS   N    N N N 249 
LYS   CA   C N S 250 
LYS   C    C N N 251 
LYS   O    O N N 252 
LYS   CB   C N N 253 
LYS   CG   C N N 254 
LYS   CD   C N N 255 
LYS   CE   C N N 256 
LYS   NZ   N N N 257 
LYS   OXT  O N N 258 
LYS   H    H N N 259 
LYS   H2   H N N 260 
LYS   HA   H N N 261 
LYS   HB2  H N N 262 
LYS   HB3  H N N 263 
LYS   HG2  H N N 264 
LYS   HG3  H N N 265 
LYS   HD2  H N N 266 
LYS   HD3  H N N 267 
LYS   HE2  H N N 268 
LYS   HE3  H N N 269 
LYS   HZ1  H N N 270 
LYS   HZ2  H N N 271 
LYS   HZ3  H N N 272 
LYS   HXT  H N N 273 
MET   N    N N N 274 
MET   CA   C N S 275 
MET   C    C N N 276 
MET   O    O N N 277 
MET   CB   C N N 278 
MET   CG   C N N 279 
MET   SD   S N N 280 
MET   CE   C N N 281 
MET   OXT  O N N 282 
MET   H    H N N 283 
MET   H2   H N N 284 
MET   HA   H N N 285 
MET   HB2  H N N 286 
MET   HB3  H N N 287 
MET   HG2  H N N 288 
MET   HG3  H N N 289 
MET   HE1  H N N 290 
MET   HE2  H N N 291 
MET   HE3  H N N 292 
MET   HXT  H N N 293 
PHE   N    N N N 294 
PHE   CA   C N S 295 
PHE   C    C N N 296 
PHE   O    O N N 297 
PHE   CB   C N N 298 
PHE   CG   C Y N 299 
PHE   CD1  C Y N 300 
PHE   CD2  C Y N 301 
PHE   CE1  C Y N 302 
PHE   CE2  C Y N 303 
PHE   CZ   C Y N 304 
PHE   OXT  O N N 305 
PHE   H    H N N 306 
PHE   H2   H N N 307 
PHE   HA   H N N 308 
PHE   HB2  H N N 309 
PHE   HB3  H N N 310 
PHE   HD1  H N N 311 
PHE   HD2  H N N 312 
PHE   HE1  H N N 313 
PHE   HE2  H N N 314 
PHE   HZ   H N N 315 
PHE   HXT  H N N 316 
PRO   N    N N N 317 
PRO   CA   C N S 318 
PRO   C    C N N 319 
PRO   O    O N N 320 
PRO   CB   C N N 321 
PRO   CG   C N N 322 
PRO   CD   C N N 323 
PRO   OXT  O N N 324 
PRO   H    H N N 325 
PRO   HA   H N N 326 
PRO   HB2  H N N 327 
PRO   HB3  H N N 328 
PRO   HG2  H N N 329 
PRO   HG3  H N N 330 
PRO   HD2  H N N 331 
PRO   HD3  H N N 332 
PRO   HXT  H N N 333 
SER   N    N N N 334 
SER   CA   C N S 335 
SER   C    C N N 336 
SER   O    O N N 337 
SER   CB   C N N 338 
SER   OG   O N N 339 
SER   OXT  O N N 340 
SER   H    H N N 341 
SER   H2   H N N 342 
SER   HA   H N N 343 
SER   HB2  H N N 344 
SER   HB3  H N N 345 
SER   HG   H N N 346 
SER   HXT  H N N 347 
THR   N    N N N 348 
THR   CA   C N S 349 
THR   C    C N N 350 
THR   O    O N N 351 
THR   CB   C N R 352 
THR   OG1  O N N 353 
THR   CG2  C N N 354 
THR   OXT  O N N 355 
THR   H    H N N 356 
THR   H2   H N N 357 
THR   HA   H N N 358 
THR   HB   H N N 359 
THR   HG1  H N N 360 
THR   HG21 H N N 361 
THR   HG22 H N N 362 
THR   HG23 H N N 363 
THR   HXT  H N N 364 
TYR   N    N N N 365 
TYR   CA   C N S 366 
TYR   C    C N N 367 
TYR   O    O N N 368 
TYR   CB   C N N 369 
TYR   CG   C Y N 370 
TYR   CD1  C Y N 371 
TYR   CD2  C Y N 372 
TYR   CE1  C Y N 373 
TYR   CE2  C Y N 374 
TYR   CZ   C Y N 375 
TYR   OH   O N N 376 
TYR   OXT  O N N 377 
TYR   H    H N N 378 
TYR   H2   H N N 379 
TYR   HA   H N N 380 
TYR   HB2  H N N 381 
TYR   HB3  H N N 382 
TYR   HD1  H N N 383 
TYR   HD2  H N N 384 
TYR   HE1  H N N 385 
TYR   HE2  H N N 386 
TYR   HH   H N N 387 
TYR   HXT  H N N 388 
VAL   N    N N N 389 
VAL   CA   C N S 390 
VAL   C    C N N 391 
VAL   O    O N N 392 
VAL   CB   C N N 393 
VAL   CG1  C N N 394 
VAL   CG2  C N N 395 
VAL   OXT  O N N 396 
VAL   H    H N N 397 
VAL   H2   H N N 398 
VAL   HA   H N N 399 
VAL   HB   H N N 400 
VAL   HG11 H N N 401 
VAL   HG12 H N N 402 
VAL   HG13 H N N 403 
VAL   HG21 H N N 404 
VAL   HG22 H N N 405 
VAL   HG23 H N N 406 
VAL   HXT  H N N 407 
# 
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 
A1BBS C3  C4   sing N N 1   
A1BBS C3  C2   sing N N 2   
A1BBS C5  C4   sing N N 3   
A1BBS C5  C6   sing N N 4   
A1BBS C4  C13  sing N N 5   
A1BBS C2  C1   sing N N 6   
A1BBS C6  N1   sing N N 7   
A1BBS C13 C1   sing N N 8   
A1BBS C13 N1   sing N N 9   
A1BBS C1  O1   sing N N 10  
A1BBS N1  C7   sing N N 11  
A1BBS C7  N2   doub Y N 12  
A1BBS C7  C10  sing Y N 13  
A1BBS C11 C10  sing Y N 14  
A1BBS C11 C12  doub Y N 15  
A1BBS N2  C8   sing Y N 16  
A1BBS C10 C9   doub Y N 17  
A1BBS C12 N4   sing Y N 18  
A1BBS C8  N3   doub Y N 19  
A1BBS C9  N4   sing Y N 20  
A1BBS C9  N3   sing Y N 21  
A1BBS C3  H8   sing N N 22  
A1BBS C3  H7   sing N N 23  
A1BBS C6  H11  sing N N 24  
A1BBS C6  H12  sing N N 25  
A1BBS C12 H15  sing N N 26  
A1BBS C1  H1   sing N N 27  
A1BBS C11 H14  sing N N 28  
A1BBS C13 H3   sing N N 29  
A1BBS C2  H6   sing N N 30  
A1BBS C2  H5   sing N N 31  
A1BBS C4  H2   sing N N 32  
A1BBS C5  H10  sing N N 33  
A1BBS C5  H9   sing N N 34  
A1BBS C8  H13  sing N N 35  
A1BBS N4  H16  sing N N 36  
A1BBS O1  H4   sing N N 37  
ALA   N   CA   sing N N 38  
ALA   N   H    sing N N 39  
ALA   N   H2   sing N N 40  
ALA   CA  C    sing N N 41  
ALA   CA  CB   sing N N 42  
ALA   CA  HA   sing N N 43  
ALA   C   O    doub N N 44  
ALA   C   OXT  sing N N 45  
ALA   CB  HB1  sing N N 46  
ALA   CB  HB2  sing N N 47  
ALA   CB  HB3  sing N N 48  
ALA   OXT HXT  sing N N 49  
ARG   N   CA   sing N N 50  
ARG   N   H    sing N N 51  
ARG   N   H2   sing N N 52  
ARG   CA  C    sing N N 53  
ARG   CA  CB   sing N N 54  
ARG   CA  HA   sing N N 55  
ARG   C   O    doub N N 56  
ARG   C   OXT  sing N N 57  
ARG   CB  CG   sing N N 58  
ARG   CB  HB2  sing N N 59  
ARG   CB  HB3  sing N N 60  
ARG   CG  CD   sing N N 61  
ARG   CG  HG2  sing N N 62  
ARG   CG  HG3  sing N N 63  
ARG   CD  NE   sing N N 64  
ARG   CD  HD2  sing N N 65  
ARG   CD  HD3  sing N N 66  
ARG   NE  CZ   sing N N 67  
ARG   NE  HE   sing N N 68  
ARG   CZ  NH1  sing N N 69  
ARG   CZ  NH2  doub N N 70  
ARG   NH1 HH11 sing N N 71  
ARG   NH1 HH12 sing N N 72  
ARG   NH2 HH21 sing N N 73  
ARG   NH2 HH22 sing N N 74  
ARG   OXT HXT  sing N N 75  
ASN   N   CA   sing N N 76  
ASN   N   H    sing N N 77  
ASN   N   H2   sing N N 78  
ASN   CA  C    sing N N 79  
ASN   CA  CB   sing N N 80  
ASN   CA  HA   sing N N 81  
ASN   C   O    doub N N 82  
ASN   C   OXT  sing N N 83  
ASN   CB  CG   sing N N 84  
ASN   CB  HB2  sing N N 85  
ASN   CB  HB3  sing N N 86  
ASN   CG  OD1  doub N N 87  
ASN   CG  ND2  sing N N 88  
ASN   ND2 HD21 sing N N 89  
ASN   ND2 HD22 sing N N 90  
ASN   OXT HXT  sing N N 91  
ASP   N   CA   sing N N 92  
ASP   N   H    sing N N 93  
ASP   N   H2   sing N N 94  
ASP   CA  C    sing N N 95  
ASP   CA  CB   sing N N 96  
ASP   CA  HA   sing N N 97  
ASP   C   O    doub N N 98  
ASP   C   OXT  sing N N 99  
ASP   CB  CG   sing N N 100 
ASP   CB  HB2  sing N N 101 
ASP   CB  HB3  sing N N 102 
ASP   CG  OD1  doub N N 103 
ASP   CG  OD2  sing N N 104 
ASP   OD2 HD2  sing N N 105 
ASP   OXT HXT  sing N N 106 
CYS   N   CA   sing N N 107 
CYS   N   H    sing N N 108 
CYS   N   H2   sing N N 109 
CYS   CA  C    sing N N 110 
CYS   CA  CB   sing N N 111 
CYS   CA  HA   sing N N 112 
CYS   C   O    doub N N 113 
CYS   C   OXT  sing N N 114 
CYS   CB  SG   sing N N 115 
CYS   CB  HB2  sing N N 116 
CYS   CB  HB3  sing N N 117 
CYS   SG  HG   sing N N 118 
CYS   OXT HXT  sing N N 119 
DMS   S   O    doub N N 120 
DMS   S   C1   sing N N 121 
DMS   S   C2   sing N N 122 
DMS   C1  H11  sing N N 123 
DMS   C1  H12  sing N N 124 
DMS   C1  H13  sing N N 125 
DMS   C2  H21  sing N N 126 
DMS   C2  H22  sing N N 127 
DMS   C2  H23  sing N N 128 
GLN   N   CA   sing N N 129 
GLN   N   H    sing N N 130 
GLN   N   H2   sing N N 131 
GLN   CA  C    sing N N 132 
GLN   CA  CB   sing N N 133 
GLN   CA  HA   sing N N 134 
GLN   C   O    doub N N 135 
GLN   C   OXT  sing N N 136 
GLN   CB  CG   sing N N 137 
GLN   CB  HB2  sing N N 138 
GLN   CB  HB3  sing N N 139 
GLN   CG  CD   sing N N 140 
GLN   CG  HG2  sing N N 141 
GLN   CG  HG3  sing N N 142 
GLN   CD  OE1  doub N N 143 
GLN   CD  NE2  sing N N 144 
GLN   NE2 HE21 sing N N 145 
GLN   NE2 HE22 sing N N 146 
GLN   OXT HXT  sing N N 147 
GLU   N   CA   sing N N 148 
GLU   N   H    sing N N 149 
GLU   N   H2   sing N N 150 
GLU   CA  C    sing N N 151 
GLU   CA  CB   sing N N 152 
GLU   CA  HA   sing N N 153 
GLU   C   O    doub N N 154 
GLU   C   OXT  sing N N 155 
GLU   CB  CG   sing N N 156 
GLU   CB  HB2  sing N N 157 
GLU   CB  HB3  sing N N 158 
GLU   CG  CD   sing N N 159 
GLU   CG  HG2  sing N N 160 
GLU   CG  HG3  sing N N 161 
GLU   CD  OE1  doub N N 162 
GLU   CD  OE2  sing N N 163 
GLU   OE2 HE2  sing N N 164 
GLU   OXT HXT  sing N N 165 
GLY   N   CA   sing N N 166 
GLY   N   H    sing N N 167 
GLY   N   H2   sing N N 168 
GLY   CA  C    sing N N 169 
GLY   CA  HA2  sing N N 170 
GLY   CA  HA3  sing N N 171 
GLY   C   O    doub N N 172 
GLY   C   OXT  sing N N 173 
GLY   OXT HXT  sing N N 174 
HIS   N   CA   sing N N 175 
HIS   N   H    sing N N 176 
HIS   N   H2   sing N N 177 
HIS   CA  C    sing N N 178 
HIS   CA  CB   sing N N 179 
HIS   CA  HA   sing N N 180 
HIS   C   O    doub N N 181 
HIS   C   OXT  sing N N 182 
HIS   CB  CG   sing N N 183 
HIS   CB  HB2  sing N N 184 
HIS   CB  HB3  sing N N 185 
HIS   CG  ND1  sing Y N 186 
HIS   CG  CD2  doub Y N 187 
HIS   ND1 CE1  doub Y N 188 
HIS   ND1 HD1  sing N N 189 
HIS   CD2 NE2  sing Y N 190 
HIS   CD2 HD2  sing N N 191 
HIS   CE1 NE2  sing Y N 192 
HIS   CE1 HE1  sing N N 193 
HIS   NE2 HE2  sing N N 194 
HIS   OXT HXT  sing N N 195 
HOH   O   H1   sing N N 196 
HOH   O   H2   sing N N 197 
ILE   N   CA   sing N N 198 
ILE   N   H    sing N N 199 
ILE   N   H2   sing N N 200 
ILE   CA  C    sing N N 201 
ILE   CA  CB   sing N N 202 
ILE   CA  HA   sing N N 203 
ILE   C   O    doub N N 204 
ILE   C   OXT  sing N N 205 
ILE   CB  CG1  sing N N 206 
ILE   CB  CG2  sing N N 207 
ILE   CB  HB   sing N N 208 
ILE   CG1 CD1  sing N N 209 
ILE   CG1 HG12 sing N N 210 
ILE   CG1 HG13 sing N N 211 
ILE   CG2 HG21 sing N N 212 
ILE   CG2 HG22 sing N N 213 
ILE   CG2 HG23 sing N N 214 
ILE   CD1 HD11 sing N N 215 
ILE   CD1 HD12 sing N N 216 
ILE   CD1 HD13 sing N N 217 
ILE   OXT HXT  sing N N 218 
LEU   N   CA   sing N N 219 
LEU   N   H    sing N N 220 
LEU   N   H2   sing N N 221 
LEU   CA  C    sing N N 222 
LEU   CA  CB   sing N N 223 
LEU   CA  HA   sing N N 224 
LEU   C   O    doub N N 225 
LEU   C   OXT  sing N N 226 
LEU   CB  CG   sing N N 227 
LEU   CB  HB2  sing N N 228 
LEU   CB  HB3  sing N N 229 
LEU   CG  CD1  sing N N 230 
LEU   CG  CD2  sing N N 231 
LEU   CG  HG   sing N N 232 
LEU   CD1 HD11 sing N N 233 
LEU   CD1 HD12 sing N N 234 
LEU   CD1 HD13 sing N N 235 
LEU   CD2 HD21 sing N N 236 
LEU   CD2 HD22 sing N N 237 
LEU   CD2 HD23 sing N N 238 
LEU   OXT HXT  sing N N 239 
LYS   N   CA   sing N N 240 
LYS   N   H    sing N N 241 
LYS   N   H2   sing N N 242 
LYS   CA  C    sing N N 243 
LYS   CA  CB   sing N N 244 
LYS   CA  HA   sing N N 245 
LYS   C   O    doub N N 246 
LYS   C   OXT  sing N N 247 
LYS   CB  CG   sing N N 248 
LYS   CB  HB2  sing N N 249 
LYS   CB  HB3  sing N N 250 
LYS   CG  CD   sing N N 251 
LYS   CG  HG2  sing N N 252 
LYS   CG  HG3  sing N N 253 
LYS   CD  CE   sing N N 254 
LYS   CD  HD2  sing N N 255 
LYS   CD  HD3  sing N N 256 
LYS   CE  NZ   sing N N 257 
LYS   CE  HE2  sing N N 258 
LYS   CE  HE3  sing N N 259 
LYS   NZ  HZ1  sing N N 260 
LYS   NZ  HZ2  sing N N 261 
LYS   NZ  HZ3  sing N N 262 
LYS   OXT HXT  sing N N 263 
MET   N   CA   sing N N 264 
MET   N   H    sing N N 265 
MET   N   H2   sing N N 266 
MET   CA  C    sing N N 267 
MET   CA  CB   sing N N 268 
MET   CA  HA   sing N N 269 
MET   C   O    doub N N 270 
MET   C   OXT  sing N N 271 
MET   CB  CG   sing N N 272 
MET   CB  HB2  sing N N 273 
MET   CB  HB3  sing N N 274 
MET   CG  SD   sing N N 275 
MET   CG  HG2  sing N N 276 
MET   CG  HG3  sing N N 277 
MET   SD  CE   sing N N 278 
MET   CE  HE1  sing N N 279 
MET   CE  HE2  sing N N 280 
MET   CE  HE3  sing N N 281 
MET   OXT HXT  sing N N 282 
PHE   N   CA   sing N N 283 
PHE   N   H    sing N N 284 
PHE   N   H2   sing N N 285 
PHE   CA  C    sing N N 286 
PHE   CA  CB   sing N N 287 
PHE   CA  HA   sing N N 288 
PHE   C   O    doub N N 289 
PHE   C   OXT  sing N N 290 
PHE   CB  CG   sing N N 291 
PHE   CB  HB2  sing N N 292 
PHE   CB  HB3  sing N N 293 
PHE   CG  CD1  doub Y N 294 
PHE   CG  CD2  sing Y N 295 
PHE   CD1 CE1  sing Y N 296 
PHE   CD1 HD1  sing N N 297 
PHE   CD2 CE2  doub Y N 298 
PHE   CD2 HD2  sing N N 299 
PHE   CE1 CZ   doub Y N 300 
PHE   CE1 HE1  sing N N 301 
PHE   CE2 CZ   sing Y N 302 
PHE   CE2 HE2  sing N N 303 
PHE   CZ  HZ   sing N N 304 
PHE   OXT HXT  sing N N 305 
PRO   N   CA   sing N N 306 
PRO   N   CD   sing N N 307 
PRO   N   H    sing N N 308 
PRO   CA  C    sing N N 309 
PRO   CA  CB   sing N N 310 
PRO   CA  HA   sing N N 311 
PRO   C   O    doub N N 312 
PRO   C   OXT  sing N N 313 
PRO   CB  CG   sing N N 314 
PRO   CB  HB2  sing N N 315 
PRO   CB  HB3  sing N N 316 
PRO   CG  CD   sing N N 317 
PRO   CG  HG2  sing N N 318 
PRO   CG  HG3  sing N N 319 
PRO   CD  HD2  sing N N 320 
PRO   CD  HD3  sing N N 321 
PRO   OXT HXT  sing N N 322 
SER   N   CA   sing N N 323 
SER   N   H    sing N N 324 
SER   N   H2   sing N N 325 
SER   CA  C    sing N N 326 
SER   CA  CB   sing N N 327 
SER   CA  HA   sing N N 328 
SER   C   O    doub N N 329 
SER   C   OXT  sing N N 330 
SER   CB  OG   sing N N 331 
SER   CB  HB2  sing N N 332 
SER   CB  HB3  sing N N 333 
SER   OG  HG   sing N N 334 
SER   OXT HXT  sing N N 335 
THR   N   CA   sing N N 336 
THR   N   H    sing N N 337 
THR   N   H2   sing N N 338 
THR   CA  C    sing N N 339 
THR   CA  CB   sing N N 340 
THR   CA  HA   sing N N 341 
THR   C   O    doub N N 342 
THR   C   OXT  sing N N 343 
THR   CB  OG1  sing N N 344 
THR   CB  CG2  sing N N 345 
THR   CB  HB   sing N N 346 
THR   OG1 HG1  sing N N 347 
THR   CG2 HG21 sing N N 348 
THR   CG2 HG22 sing N N 349 
THR   CG2 HG23 sing N N 350 
THR   OXT HXT  sing N N 351 
TYR   N   CA   sing N N 352 
TYR   N   H    sing N N 353 
TYR   N   H2   sing N N 354 
TYR   CA  C    sing N N 355 
TYR   CA  CB   sing N N 356 
TYR   CA  HA   sing N N 357 
TYR   C   O    doub N N 358 
TYR   C   OXT  sing N N 359 
TYR   CB  CG   sing N N 360 
TYR   CB  HB2  sing N N 361 
TYR   CB  HB3  sing N N 362 
TYR   CG  CD1  doub Y N 363 
TYR   CG  CD2  sing Y N 364 
TYR   CD1 CE1  sing Y N 365 
TYR   CD1 HD1  sing N N 366 
TYR   CD2 CE2  doub Y N 367 
TYR   CD2 HD2  sing N N 368 
TYR   CE1 CZ   doub Y N 369 
TYR   CE1 HE1  sing N N 370 
TYR   CE2 CZ   sing Y N 371 
TYR   CE2 HE2  sing N N 372 
TYR   CZ  OH   sing N N 373 
TYR   OH  HH   sing N N 374 
TYR   OXT HXT  sing N N 375 
VAL   N   CA   sing N N 376 
VAL   N   H    sing N N 377 
VAL   N   H2   sing N N 378 
VAL   CA  C    sing N N 379 
VAL   CA  CB   sing N N 380 
VAL   CA  HA   sing N N 381 
VAL   C   O    doub N N 382 
VAL   C   OXT  sing N N 383 
VAL   CB  CG1  sing N N 384 
VAL   CB  CG2  sing N N 385 
VAL   CB  HB   sing N N 386 
VAL   CG1 HG11 sing N N 387 
VAL   CG1 HG12 sing N N 388 
VAL   CG1 HG13 sing N N 389 
VAL   CG2 HG21 sing N N 390 
VAL   CG2 HG22 sing N N 391 
VAL   CG2 HG23 sing N N 392 
VAL   OXT HXT  sing N N 393 
# 
_pdbx_audit_support.funding_organization   
'National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)' 
_pdbx_audit_support.country                'United States' 
_pdbx_audit_support.grant_number           U19AI171110 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_deposit_group.group_title         
'PanDDA analysis group deposition of SARS-CoV-2 NSP3 macrodomain ligand screen - FrankenROCS hits and analogues of AVI-313' 
_pdbx_deposit_group.group_description   
'SARS-CoV-2 NSP3 macrodomain in complex with ligands identified by X-ray diffraction using ALS 8.3.1,  SSRL 9-2, and SSRL 12-2' 
_pdbx_deposit_group.group_type          'changed state' 
_pdbx_deposit_group.group_id            G_1002304 
# 
_atom_sites.entry_id                    7HFR 
_atom_sites.fract_transf_matrix[1][1]   0.011290 
_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]   0.011290 
_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]   0.025231 
_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 
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   ? 19.586 -16.324 22.218  0.30 54.69 ?  3   VAL   A N    1 
ATOM   2    N N    B VAL   A 1 3   ? 19.617 -15.919 22.331  0.70 57.48 ?  3   VAL   A N    1 
ATOM   3    C CA   A VAL   A 1 3   ? 18.608 -15.254 22.374  0.30 54.25 ?  3   VAL   A CA   1 
ATOM   4    C CA   B VAL   A 1 3   ? 18.592 -14.896 22.498  0.70 56.88 ?  3   VAL   A CA   1 
ATOM   5    C C    A VAL   A 1 3   ? 19.258 -13.902 22.098  0.30 52.18 ?  3   VAL   A C    1 
ATOM   6    C C    B VAL   A 1 3   ? 19.182 -13.517 22.213  0.70 54.58 ?  3   VAL   A C    1 
ATOM   7    O O    A VAL   A 1 3   ? 20.363 -13.629 22.566  0.30 52.62 ?  3   VAL   A O    1 
ATOM   8    O O    B VAL   A 1 3   ? 20.297 -13.213 22.638  0.70 55.25 ?  3   VAL   A O    1 
ATOM   9    C CB   A VAL   A 1 3   ? 17.959 -15.288 23.773  0.30 55.48 ?  3   VAL   A CB   1 
ATOM   10   C CB   B VAL   A 1 3   ? 17.960 -14.963 23.905  0.70 58.06 ?  3   VAL   A CB   1 
ATOM   11   C CG1  A VAL   A 1 3   ? 16.924 -14.179 23.910  0.30 55.86 ?  3   VAL   A CG1  1 
ATOM   12   C CG1  B VAL   A 1 3   ? 16.828 -13.952 24.032  0.70 58.38 ?  3   VAL   A CG1  1 
ATOM   13   C CG2  A VAL   A 1 3   ? 17.326 -16.647 24.035  0.30 55.86 ?  3   VAL   A CG2  1 
ATOM   14   C CG2  B VAL   A 1 3   ? 17.457 -16.371 24.198  0.70 58.40 ?  3   VAL   A CG2  1 
ATOM   15   H HA   A VAL   A 1 3   ? 17.903 -15.378 21.723  0.30 65.10 ?  3   VAL   A HA   1 
ATOM   16   H HA   B VAL   A 1 3   ? 17.885 -15.057 21.857  0.70 68.26 ?  3   VAL   A HA   1 
ATOM   17   H HB   A VAL   A 1 3   ? 18.643 -15.143 24.445  0.30 66.58 ?  3   VAL   A HB   1 
ATOM   18   H HB   B VAL   A 1 3   ? 18.633 -14.743 24.567  0.70 69.67 ?  3   VAL   A HB   1 
ATOM   19   H HG11 A VAL   A 1 3   ? 16.411 -14.325 24.720  0.30 67.03 ?  3   VAL   A HG11 1 
ATOM   20   H HG11 B VAL   A 1 3   ? 16.364 -14.103 24.871  0.70 70.05 ?  3   VAL   A HG11 1 
ATOM   21   H HG12 A VAL   A 1 3   ? 17.379 -13.324 23.958  0.30 67.03 ?  3   VAL   A HG12 1 
ATOM   22   H HG12 B VAL   A 1 3   ? 17.199 -13.057 24.016  0.70 70.05 ?  3   VAL   A HG12 1 
ATOM   23   H HG13 A VAL   A 1 3   ? 16.336 -14.200 23.139  0.30 67.03 ?  3   VAL   A HG13 1 
ATOM   24   H HG13 B VAL   A 1 3   ? 16.215 -14.072 23.290  0.70 70.05 ?  3   VAL   A HG13 1 
ATOM   25   H HG21 A VAL   A 1 3   ? 16.862 -16.621 24.886  0.30 67.03 ?  3   VAL   A HG21 1 
ATOM   26   H HG21 B VAL   A 1 3   ? 16.969 -16.364 25.037  0.70 70.07 ?  3   VAL   A HG21 1 
ATOM   27   H HG22 A VAL   A 1 3   ? 16.699 -16.845 23.322  0.30 67.03 ?  3   VAL   A HG22 1 
ATOM   28   H HG22 B VAL   A 1 3   ? 16.870 -16.652 23.478  0.70 70.07 ?  3   VAL   A HG22 1 
ATOM   29   H HG23 A VAL   A 1 3   ? 18.023 -17.321 24.059  0.30 67.03 ?  3   VAL   A HG23 1 
ATOM   30   H HG23 B VAL   A 1 3   ? 18.215 -16.972 24.261  0.70 70.07 ?  3   VAL   A HG23 1 
ATOM   31   N N    A ASN   A 1 4   ? 18.569 -13.062 21.328  0.30 49.32 ?  4   ASN   A N    1 
ATOM   32   N N    B ASN   A 1 4   ? 18.434 -12.688 21.484  0.70 51.11 ?  4   ASN   A N    1 
ATOM   33   C CA   A ASN   A 1 4   ? 19.010 -11.700 21.053  0.30 46.21 ?  4   ASN   A CA   1 
ATOM   34   C CA   B ASN   A 1 4   ? 18.837 -11.320 21.176  0.70 47.27 ?  4   ASN   A CA   1 
ATOM   35   C C    A ASN   A 1 4   ? 17.857 -10.737 21.320  0.30 43.26 ?  4   ASN   A C    1 
ATOM   36   C C    B ASN   A 1 4   ? 17.669 -10.374 21.437  0.70 43.79 ?  4   ASN   A C    1 
ATOM   37   O O    A ASN   A 1 4   ? 16.749 -11.143 21.683  0.30 43.27 ?  4   ASN   A O    1 
ATOM   38   O O    B ASN   A 1 4   ? 16.604 -10.780 21.914  0.70 43.60 ?  4   ASN   A O    1 
ATOM   39   C CB   A ASN   A 1 4   ? 19.569 -11.557 19.631  0.30 45.88 ?  4   ASN   A CB   1 
ATOM   40   C CB   B ASN   A 1 4   ? 19.375 -11.191 19.744  0.70 46.73 ?  4   ASN   A CB   1 
ATOM   41   C CG   A ASN   A 1 4   ? 18.578 -11.971 18.562  0.30 45.53 ?  4   ASN   A CG   1 
ATOM   42   C CG   B ASN   A 1 4   ? 18.400 -11.689 18.701  0.70 46.12 ?  4   ASN   A CG   1 
ATOM   43   O OD1  A ASN   A 1 4   ? 17.424 -11.542 18.566  0.30 45.43 ?  4   ASN   A OD1  1 
ATOM   44   O OD1  B ASN   A 1 4   ? 17.230 -11.305 18.691  0.70 45.93 ?  4   ASN   A OD1  1 
ATOM   45   N ND2  A ASN   A 1 4   ? 19.027 -12.814 17.638  0.30 45.41 ?  4   ASN   A ND2  1 
ATOM   46   N ND2  B ASN   A 1 4   ? 18.880 -12.553 17.813  0.70 45.94 ?  4   ASN   A ND2  1 
ATOM   47   H H    A ASN   A 1 4   ? 17.825 -13.266 20.947  0.30 59.19 ?  4   ASN   A H    1 
ATOM   48   H H    B ASN   A 1 4   ? 17.672 -12.908 21.154  0.70 61.33 ?  4   ASN   A H    1 
ATOM   49   H HA   A ASN   A 1 4   ? 19.724 -11.480 21.666  0.30 55.45 ?  4   ASN   A HA   1 
ATOM   50   H HA   B ASN   A 1 4   ? 19.554 -11.072 21.772  0.70 56.73 ?  4   ASN   A HA   1 
ATOM   51   H HB2  A ASN   A 1 4   ? 19.806 -10.627 19.477  0.30 55.06 ?  4   ASN   A HB2  1 
ATOM   52   H HB2  B ASN   A 1 4   ? 19.562 -10.256 19.557  0.70 56.08 ?  4   ASN   A HB2  1 
ATOM   53   H HB3  A ASN   A 1 4   ? 20.356 -12.116 19.543  0.30 55.06 ?  4   ASN   A HB3  1 
ATOM   54   H HB3  B ASN   A 1 4   ? 20.188 -11.711 19.664  0.70 56.08 ?  4   ASN   A HB3  1 
ATOM   55   H HD21 A ASN   A 1 4   ? 18.507 -13.079 17.006  0.30 54.50 ?  4   ASN   A HD21 1 
ATOM   56   H HD21 B ASN   A 1 4   ? 18.370 -12.867 17.197  0.70 55.13 ?  4   ASN   A HD21 1 
ATOM   57   H HD22 A ASN   A 1 4   ? 19.840 -13.095 17.671  0.30 54.50 ?  4   ASN   A HD22 1 
ATOM   58   H HD22 B ASN   A 1 4   ? 19.704 -12.799 17.856  0.70 55.13 ?  4   ASN   A HD22 1 
ATOM   59   N N    A SER   A 1 5   ? 18.126 -9.445  21.137  0.30 40.17 ?  5   SER   A N    1 
ATOM   60   N N    B SER   A 1 5   ? 17.874 -9.095  21.119  0.70 40.42 ?  5   SER   A N    1 
ATOM   61   C CA   A SER   A 1 5   ? 17.194 -8.389  21.510  0.30 37.02 ?  5   SER   A CA   1 
ATOM   62   C CA   B SER   A 1 5   ? 16.938 -8.038  21.484  0.70 37.07 ?  5   SER   A CA   1 
ATOM   63   C C    A SER   A 1 5   ? 16.326 -7.914  20.349  0.30 33.66 ?  5   SER   A C    1 
ATOM   64   C C    B SER   A 1 5   ? 16.069 -7.565  20.320  0.70 33.13 ?  5   SER   A C    1 
ATOM   65   O O    A SER   A 1 5   ? 15.583 -6.941  20.506  0.30 33.67 ?  5   SER   A O    1 
ATOM   66   O O    B SER   A 1 5   ? 15.371 -6.555  20.457  0.70 33.05 ?  5   SER   A O    1 
ATOM   67   C CB   A SER   A 1 5   ? 17.948 -7.208  22.127  0.30 37.29 ?  5   SER   A CB   1 
ATOM   68   C CB   B SER   A 1 5   ? 17.686 -6.854  22.104  0.70 37.84 ?  5   SER   A CB   1 
ATOM   69   O OG   A SER   A 1 5   ? 18.963 -6.736  21.259  0.30 37.44 ?  5   SER   A OG   1 
ATOM   70   O OG   B SER   A 1 5   ? 18.620 -6.301  21.193  0.70 38.35 ?  5   SER   A OG   1 
ATOM   71   H H    A SER   A 1 5   ? 18.855 -9.154  20.787  0.30 48.20 ?  5   SER   A H    1 
ATOM   72   H H    B SER   A 1 5   ? 18.562 -8.815  20.683  0.70 48.51 ?  5   SER   A H    1 
ATOM   73   H HA   A SER   A 1 5   ? 16.600 -8.736  22.191  0.30 44.42 ?  5   SER   A HA   1 
ATOM   74   H HA   B SER   A 1 5   ? 16.348 -8.388  22.168  0.70 44.48 ?  5   SER   A HA   1 
ATOM   75   H HB2  A SER   A 1 5   ? 17.319 -6.488  22.298  0.30 44.74 ?  5   SER   A HB2  1 
ATOM   76   H HB2  B SER   A 1 5   ? 17.043 -6.170  22.346  0.70 45.40 ?  5   SER   A HB2  1 
ATOM   77   H HB3  A SER   A 1 5   ? 18.353 -7.496  22.961  0.30 44.74 ?  5   SER   A HB3  1 
ATOM   78   H HB3  B SER   A 1 5   ? 18.158 -7.159  22.897  0.70 45.40 ?  5   SER   A HB3  1 
ATOM   79   H HG   A SER   A 1 5   ? 19.366 -6.090  21.614  0.30 44.92 ?  5   SER   A HG   1 
ATOM   80   H HG   B SER   A 1 5   ? 19.024 -5.657  21.552  0.70 46.02 ?  5   SER   A HG   1 
ATOM   81   N N    A PHE   A 1 6   ? 16.398 -8.571  19.194  0.30 30.15 ?  6   PHE   A N    1 
ATOM   82   N N    B PHE   A 1 6   ? 16.092 -8.260  19.185  0.70 29.11 ?  6   PHE   A N    1 
ATOM   83   C CA   A PHE   A 1 6   ? 15.505 -8.234  18.094  0.30 26.72 ?  6   PHE   A CA   1 
ATOM   84   C CA   B PHE   A 1 6   ? 15.178 -7.934  18.098  0.70 25.23 ?  6   PHE   A CA   1 
ATOM   85   C C    A PHE   A 1 6   ? 14.077 -8.615  18.461  0.30 25.72 ?  6   PHE   A C    1 
ATOM   86   C C    B PHE   A 1 6   ? 13.756 -8.323  18.488  0.70 24.73 ?  6   PHE   A C    1 
ATOM   87   O O    A PHE   A 1 6   ? 13.806 -9.760  18.835  0.30 25.74 ?  6   PHE   A O    1 
ATOM   88   O O    B PHE   A 1 6   ? 13.541 -9.341  19.148  0.70 25.16 ?  6   PHE   A O    1 
ATOM   89   C CB   A PHE   A 1 6   ? 15.932 -8.964  16.822  0.30 24.48 ?  6   PHE   A CB   1 
ATOM   90   C CB   B PHE   A 1 6   ? 15.586 -8.679  16.828  0.70 22.89 ?  6   PHE   A CB   1 
ATOM   91   C CG   A PHE   A 1 6   ? 17.196 -8.428  16.210  0.30 22.54 ?  6   PHE   A CG   1 
ATOM   92   C CG   B PHE   A 1 6   ? 16.894 -8.209  16.240  0.70 21.22 ?  6   PHE   A CG   1 
ATOM   93   C CD1  A PHE   A 1 6   ? 17.185 -7.240  15.496  0.30 21.65 ?  6   PHE   A CD1  1 
ATOM   94   C CD1  B PHE   A 1 6   ? 16.948 -7.050  15.486  0.70 20.24 ?  6   PHE   A CD1  1 
ATOM   95   C CD2  A PHE   A 1 6   ? 18.393 -9.113  16.341  0.30 21.92 ?  6   PHE   A CD2  1 
ATOM   96   C CD2  B PHE   A 1 6   ? 18.060 -8.930  16.436  0.70 21.13 ?  6   PHE   A CD2  1 
ATOM   97   C CE1  A PHE   A 1 6   ? 18.345 -6.744  14.930  0.30 21.20 ?  6   PHE   A CE1  1 
ATOM   98   C CE1  B PHE   A 1 6   ? 18.144 -6.615  14.943  0.70 19.89 ?  6   PHE   A CE1  1 
ATOM   99   C CE2  A PHE   A 1 6   ? 19.555 -8.622  15.776  0.30 21.57 ?  6   PHE   A CE2  1 
ATOM   100  C CE2  B PHE   A 1 6   ? 19.256 -8.503  15.895  0.70 21.24 ?  6   PHE   A CE2  1 
ATOM   101  C CZ   A PHE   A 1 6   ? 19.531 -7.437  15.070  0.30 21.26 ?  6   PHE   A CZ   1 
ATOM   102  C CZ   B PHE   A 1 6   ? 19.297 -7.343  15.148  0.70 20.56 ?  6   PHE   A CZ   1 
ATOM   103  H H    A PHE   A 1 6   ? 16.949 -9.208  19.024  0.30 36.18 ?  6   PHE   A H    1 
ATOM   104  H H    B PHE   A 1 6   ? 16.619 -8.920  19.023  0.70 34.93 ?  6   PHE   A H    1 
ATOM   105  H HA   A PHE   A 1 6   ? 15.537 -7.280  17.930  0.30 32.06 ?  6   PHE   A HA   1 
ATOM   106  H HA   B PHE   A 1 6   ? 15.199 -6.986  17.931  0.70 30.28 ?  6   PHE   A HA   1 
ATOM   107  H HB2  A PHE   A 1 6   ? 16.078 -9.900  17.034  0.30 29.38 ?  6   PHE   A HB2  1 
ATOM   108  H HB2  B PHE   A 1 6   ? 15.671 -9.625  17.037  0.70 27.47 ?  6   PHE   A HB2  1 
ATOM   109  H HB3  A PHE   A 1 6   ? 15.225 -8.884  16.163  0.30 29.38 ?  6   PHE   A HB3  1 
ATOM   110  H HB3  B PHE   A 1 6   ? 14.893 -8.554  16.162  0.70 27.47 ?  6   PHE   A HB3  1 
ATOM   111  H HD1  A PHE   A 1 6   ? 16.389 -6.770  15.400  0.30 25.99 ?  6   PHE   A HD1  1 
ATOM   112  H HD1  B PHE   A 1 6   ? 16.169 -6.557  15.349  0.70 24.29 ?  6   PHE   A HD1  1 
ATOM   113  H HD2  A PHE   A 1 6   ? 18.414 -9.913  16.817  0.30 26.30 ?  6   PHE   A HD2  1 
ATOM   114  H HD2  B PHE   A 1 6   ? 18.034 -9.714  16.944  0.70 25.35 ?  6   PHE   A HD2  1 
ATOM   115  H HE1  A PHE   A 1 6   ? 18.327 -5.945  14.454  0.30 25.44 ?  6   PHE   A HE1  1 
ATOM   116  H HE1  B PHE   A 1 6   ? 18.167 -5.833  14.441  0.70 23.86 ?  6   PHE   A HE1  1 
ATOM   117  H HE2  A PHE   A 1 6   ? 20.353 -9.090  15.872  0.30 25.88 ?  6   PHE   A HE2  1 
ATOM   118  H HE2  B PHE   A 1 6   ? 20.032 -8.994  16.038  0.70 25.49 ?  6   PHE   A HE2  1 
ATOM   119  H HZ   A PHE   A 1 6   ? 20.312 -7.104  14.689  0.30 25.51 ?  6   PHE   A HZ   1 
ATOM   120  H HZ   B PHE   A 1 6   ? 20.099 -7.050  14.785  0.70 24.67 ?  6   PHE   A HZ   1 
ATOM   121  N N    A SER   A 1 7   ? 13.161 -7.656  18.347  0.30 24.80 ?  7   SER   A N    1 
ATOM   122  N N    B SER   A 1 7   ? 12.777 -7.515  18.073  0.70 24.30 ?  7   SER   A N    1 
ATOM   123  C CA   A SER   A 1 7   ? 11.797 -7.820  18.823  0.30 24.08 ?  7   SER   A CA   1 
ATOM   124  C CA   B SER   A 1 7   ? 11.399 -7.686  18.521  0.70 24.33 ?  7   SER   A CA   1 
ATOM   125  C C    A SER   A 1 7   ? 10.808 -7.530  17.705  0.30 22.26 ?  7   SER   A C    1 
ATOM   126  C C    B SER   A 1 7   ? 10.422 -7.446  17.378  0.70 22.26 ?  7   SER   A C    1 
ATOM   127  O O    A SER   A 1 7   ? 11.039 -6.666  16.855  0.30 22.31 ?  7   SER   A O    1 
ATOM   128  O O    B SER   A 1 7   ? 10.608 -6.532  16.572  0.70 22.16 ?  7   SER   A O    1 
ATOM   129  C CB   A SER   A 1 7   ? 11.509 -6.873  19.992  0.30 24.90 ?  7   SER   A CB   1 
ATOM   130  C CB   B SER   A 1 7   ? 11.082 -6.718  19.673  0.70 26.23 ?  7   SER   A CB   1 
ATOM   131  O OG   A SER   A 1 7   ? 10.148 -6.939  20.373  0.30 25.61 ?  7   SER   A OG   1 
ATOM   132  O OG   B SER   A 1 7   ? 9.763  -6.906  20.157  0.70 27.71 ?  7   SER   A OG   1 
ATOM   133  H H    A SER   A 1 7   ? 13.311 -6.889  17.984  0.30 29.76 ?  7   SER   A H    1 
ATOM   134  H H    B SER   A 1 7   ? 12.892 -6.859  17.530  0.70 29.15 ?  7   SER   A H    1 
ATOM   135  H HA   A SER   A 1 7   ? 11.661 -8.731  19.123  0.30 28.89 ?  7   SER   A HA   1 
ATOM   136  H HA   B SER   A 1 7   ? 11.273 -8.589  18.844  0.70 29.19 ?  7   SER   A HA   1 
ATOM   137  H HB2  A SER   A 1 7   ? 12.056 -7.132  20.747  0.30 29.88 ?  7   SER   A HB2  1 
ATOM   138  H HB2  B SER   A 1 7   ? 11.717 -6.869  20.394  0.70 31.47 ?  7   SER   A HB2  1 
ATOM   139  H HB3  A SER   A 1 7   ? 11.721 -5.966  19.721  0.30 29.88 ?  7   SER   A HB3  1 
ATOM   140  H HB3  B SER   A 1 7   ? 11.166 -5.806  19.351  0.70 31.47 ?  7   SER   A HB3  1 
ATOM   141  H HG   A SER   A 1 7   ? 9.999  -6.410  21.008  0.30 30.73 ?  7   SER   A HG   1 
ATOM   142  H HG   B SER   A 1 7   ? 9.619  -6.378  20.795  0.70 33.26 ?  7   SER   A HG   1 
ATOM   143  N N    A GLY   A 1 8   ? 9.698  -8.267  17.718  0.30 20.52 ?  8   GLY   A N    1 
ATOM   144  N N    B GLY   A 1 8   ? 9.372  -8.266  17.319  0.70 20.75 ?  8   GLY   A N    1 
ATOM   145  C CA   A GLY   A 1 8   ? 8.615  -8.011  16.794  0.30 18.93 ?  8   GLY   A CA   1 
ATOM   146  C CA   B GLY   A 1 8   ? 8.304  -8.055  16.362  0.70 19.76 ?  8   GLY   A CA   1 
ATOM   147  C C    A GLY   A 1 8   ? 8.857  -8.466  15.377  0.30 17.17 ?  8   GLY   A C    1 
ATOM   148  C C    B GLY   A 1 8   ? 8.540  -8.591  14.967  0.70 17.83 ?  8   GLY   A C    1 
ATOM   149  O O    A GLY   A 1 8   ? 8.185  -7.979  14.463  0.30 17.35 ?  8   GLY   A O    1 
ATOM   150  O O    B GLY   A 1 8   ? 7.782  -8.244  14.055  0.70 18.47 ?  8   GLY   A O    1 
ATOM   151  H H    A GLY   A 1 8   ? 9.553  -8.926  18.251  0.30 24.63 ?  8   GLY   A H    1 
ATOM   152  H H    B GLY   A 1 8   ? 9.264  -8.948  17.830  0.70 24.90 ?  8   GLY   A H    1 
ATOM   153  H HA2  A GLY   A 1 8   ? 7.810  -8.448  17.120  0.30 22.72 ?  8   GLY   A HA2  1 
ATOM   154  H HA2  B GLY   A 1 8   ? 7.501  -8.474  16.702  0.70 23.71 ?  8   GLY   A HA2  1 
ATOM   155  H HA3  A GLY   A 1 8   ? 8.445  -7.059  16.760  0.30 22.72 ?  8   GLY   A HA3  1 
ATOM   156  H HA3  B GLY   A 1 8   ? 8.137  -7.102  16.293  0.70 23.71 ?  8   GLY   A HA3  1 
ATOM   157  N N    A TYR   A 1 9   ? 9.801  -9.378  15.156  0.30 15.40 ?  9   TYR   A N    1 
ATOM   158  N N    B TYR   A 1 9   ? 9.548  -9.436  14.766  0.70 16.17 ?  9   TYR   A N    1 
ATOM   159  C CA   A TYR   A 1 9   ? 10.072 -9.887  13.821  0.30 13.75 ?  9   TYR   A CA   1 
ATOM   160  C CA   B TYR   A 1 9   ? 9.860  -9.948  13.441  0.70 14.92 ?  9   TYR   A CA   1 
ATOM   161  C C    A TYR   A 1 9   ? 9.191  -11.087 13.506  0.30 12.82 ?  9   TYR   A C    1 
ATOM   162  C C    B TYR   A 1 9   ? 9.019  -11.177 13.106  0.70 14.65 ?  9   TYR   A C    1 
ATOM   163  O O    A TYR   A 1 9   ? 8.930  -11.935 14.366  0.30 12.92 ?  9   TYR   A O    1 
ATOM   164  O O    B TYR   A 1 9   ? 8.679  -11.985 13.976  0.70 15.42 ?  9   TYR   A O    1 
ATOM   165  C CB   A TYR   A 1 9   ? 11.541 -10.292 13.672  0.30 13.56 ?  9   TYR   A CB   1 
ATOM   166  C CB   B TYR   A 1 9   ? 11.347 -10.309 13.334  0.70 14.79 ?  9   TYR   A CB   1 
ATOM   167  C CG   A TYR   A 1 9   ? 12.471 -9.114  13.499  0.30 13.03 ?  9   TYR   A CG   1 
ATOM   168  C CG   B TYR   A 1 9   ? 12.242 -9.098  13.164  0.70 15.25 ?  9   TYR   A CG   1 
ATOM   169  C CD1  A TYR   A 1 9   ? 12.811 -8.318  14.579  0.30 13.36 ?  9   TYR   A CD1  1 
ATOM   170  C CD1  B TYR   A 1 9   ? 12.506 -8.252  14.232  0.70 15.49 ?  9   TYR   A CD1  1 
ATOM   171  C CD2  A TYR   A 1 9   ? 12.998 -8.790  12.254  0.30 12.72 ?  9   TYR   A CD2  1 
ATOM   172  C CD2  B TYR   A 1 9   ? 12.802 -8.789  11.933  0.70 14.79 ?  9   TYR   A CD2  1 
ATOM   173  C CE1  A TYR   A 1 9   ? 13.647 -7.234  14.434  0.30 13.54 ?  9   TYR   A CE1  1 
ATOM   174  C CE1  B TYR   A 1 9   ? 13.301 -7.125  14.081  0.70 15.59 ?  9   TYR   A CE1  1 
ATOM   175  C CE2  A TYR   A 1 9   ? 13.838 -7.702  12.096  0.30 13.00 ?  9   TYR   A CE2  1 
ATOM   176  C CE2  B TYR   A 1 9   ? 13.601 -7.663  11.768  0.70 14.55 ?  9   TYR   A CE2  1 
ATOM   177  C CZ   A TYR   A 1 9   ? 14.158 -6.929  13.192  0.30 13.61 ?  9   TYR   A CZ   1 
ATOM   178  C CZ   B TYR   A 1 9   ? 13.850 -6.835  12.844  0.70 14.80 ?  9   TYR   A CZ   1 
ATOM   179  O OH   A TYR   A 1 9   ? 14.997 -5.850  13.049  0.30 14.52 ?  9   TYR   A OH   1 
ATOM   180  O OH   B TYR   A 1 9   ? 14.638 -5.715  12.675  0.70 15.60 ?  9   TYR   A OH   1 
ATOM   181  H H    A TYR   A 1 9   ? 10.307 -9.710  15.769  0.30 18.48 ?  9   TYR   A H    1 
ATOM   182  H H    B TYR   A 1 9   ? 10.049 -9.747  15.389  0.70 19.40 ?  9   TYR   A H    1 
ATOM   183  H HA   A TYR   A 1 9   ? 9.890  -9.186  13.172  0.30 16.50 ?  9   TYR   A HA   1 
ATOM   184  H HA   B TYR   A 1 9   ? 9.664  -9.266  12.782  0.70 17.90 ?  9   TYR   A HA   1 
ATOM   185  H HB2  A TYR   A 1 9   ? 11.822 -10.778 14.462  0.30 16.27 ?  9   TYR   A HB2  1 
ATOM   186  H HB2  B TYR   A 1 9   ? 11.621 -10.775 14.137  0.70 17.75 ?  9   TYR   A HB2  1 
ATOM   187  H HB3  A TYR   A 1 9   ? 11.630 -10.855 12.888  0.30 16.27 ?  9   TYR   A HB3  1 
ATOM   188  H HB3  B TYR   A 1 9   ? 11.466 -10.876 12.560  0.70 17.75 ?  9   TYR   A HB3  1 
ATOM   189  H HD1  A TYR   A 1 9   ? 12.464 -8.515  15.417  0.30 16.03 ?  9   TYR   A HD1  1 
ATOM   190  H HD1  B TYR   A 1 9   ? 12.130 -8.440  15.066  0.70 18.58 ?  9   TYR   A HD1  1 
ATOM   191  H HD2  A TYR   A 1 9   ? 12.785 -9.309  11.513  0.30 15.26 ?  9   TYR   A HD2  1 
ATOM   192  H HD2  B TYR   A 1 9   ? 12.631 -9.337  11.201  0.70 17.75 ?  9   TYR   A HD2  1 
ATOM   193  H HE1  A TYR   A 1 9   ? 13.864 -6.707  15.169  0.30 16.25 ?  9   TYR   A HE1  1 
ATOM   194  H HE1  B TYR   A 1 9   ? 13.470 -6.572  14.810  0.70 18.71 ?  9   TYR   A HE1  1 
ATOM   195  H HE2  A TYR   A 1 9   ? 14.191 -7.494  11.257  0.30 15.60 ?  9   TYR   A HE2  1 
ATOM   196  H HE2  B TYR   A 1 9   ? 13.972 -7.471  10.938  0.70 17.46 ?  9   TYR   A HE2  1 
ATOM   197  H HH   A TYR   A 1 9   ? 15.105 -5.468  13.789  0.30 17.43 ?  9   TYR   A HH   1 
ATOM   198  H HH   B TYR   A 1 9   ? 14.716 -5.313  13.406  0.70 18.72 ?  9   TYR   A HH   1 
ATOM   199  N N    A LEU   A 1 10  ? 8.732  -11.140 12.261  0.30 12.08 ?  10  LEU   A N    1 
ATOM   200  N N    B LEU   A 1 10  ? 8.716  -11.316 11.816  0.70 14.84 ?  10  LEU   A N    1 
ATOM   201  C CA   A LEU   A 1 10  ? 8.159  -12.350 11.700  0.30 12.24 ?  10  LEU   A CA   1 
ATOM   202  C CA   B LEU   A 1 10  ? 8.135  -12.526 11.254  0.70 14.18 ?  10  LEU   A CA   1 
ATOM   203  C C    A LEU   A 1 10  ? 9.293  -13.271 11.260  0.30 11.83 ?  10  LEU   A C    1 
ATOM   204  C C    B LEU   A 1 10  ? 9.274  -13.465 10.897  0.70 14.37 ?  10  LEU   A C    1 
ATOM   205  O O    A LEU   A 1 10  ? 10.308 -12.811 10.733  0.30 11.05 ?  10  LEU   A O    1 
ATOM   206  O O    B LEU   A 1 10  ? 10.215 -13.061 10.208  0.70 14.36 ?  10  LEU   A O    1 
ATOM   207  C CB   A LEU   A 1 10  ? 7.309  -11.974 10.489  0.30 12.90 ?  10  LEU   A CB   1 
ATOM   208  C CB   B LEU   A 1 10  ? 7.350  -12.180 9.987   0.70 14.58 ?  10  LEU   A CB   1 
ATOM   209  C CG   A LEU   A 1 10  ? 6.596  -13.126 9.790   0.30 13.70 ?  10  LEU   A CG   1 
ATOM   210  C CG   B LEU   A 1 10  ? 6.802  -13.333 9.145   0.70 14.62 ?  10  LEU   A CG   1 
ATOM   211  C CD1  A LEU   A 1 10  ? 5.520  -13.696 10.692  0.30 14.26 ?  10  LEU   A CD1  1 
ATOM   212  C CD1  B LEU   A 1 10  ? 5.716  -14.060 9.911   0.70 14.40 ?  10  LEU   A CD1  1 
ATOM   213  C CD2  A LEU   A 1 10  ? 6.015  -12.673 8.465   0.30 14.22 ?  10  LEU   A CD2  1 
ATOM   214  C CD2  B LEU   A 1 10  ? 6.283  -12.815 7.828   0.70 15.69 ?  10  LEU   A CD2  1 
ATOM   215  H H    A LEU   A 1 10  ? 8.739  -10.466 11.718  0.30 14.50 ?  10  LEU   A H    1 
ATOM   216  H H    B LEU   A 1 10  ? 8.872  -10.711 11.217  0.70 17.80 ?  10  LEU   A H    1 
ATOM   217  H HA   A LEU   A 1 10  ? 7.607  -12.795 12.365  0.30 14.69 ?  10  LEU   A HA   1 
ATOM   218  H HA   B LEU   A 1 10  ? 7.562  -12.959 11.888  0.70 17.02 ?  10  LEU   A HA   1 
ATOM   219  H HB2  A LEU   A 1 10  ? 6.631  -11.340 10.771  0.30 15.48 ?  10  LEU   A HB2  1 
ATOM   220  H HB2  B LEU   A 1 10  ? 6.594  -11.641 10.246  0.70 17.49 ?  10  LEU   A HB2  1 
ATOM   221  H HB3  A LEU   A 1 10  ? 7.890  -11.549 9.834   0.30 15.48 ?  10  LEU   A HB3  1 
ATOM   222  H HB3  B LEU   A 1 10  ? 7.929  -11.663 9.401   0.70 17.49 ?  10  LEU   A HB3  1 
ATOM   223  H HG   A LEU   A 1 10  ? 7.242  -13.827 9.608   0.30 16.45 ?  10  LEU   A HG   1 
ATOM   224  H HG   B LEU   A 1 10  ? 7.516  -13.975 8.961   0.70 17.55 ?  10  LEU   A HG   1 
ATOM   225  H HD11 A LEU   A 1 10  ? 5.070  -14.414 10.225  0.30 17.11 ?  10  LEU   A HD11 1 
ATOM   226  H HD11 B LEU   A 1 10  ? 5.355  -14.767 9.356   0.70 17.28 ?  10  LEU   A HD11 1 
ATOM   227  H HD12 A LEU   A 1 10  ? 5.932  -14.035 11.503  0.30 17.11 ?  10  LEU   A HD12 1 
ATOM   228  H HD12 B LEU   A 1 10  ? 6.098  -14.440 10.722  0.70 17.28 ?  10  LEU   A HD12 1 
ATOM   229  H HD13 A LEU   A 1 10  ? 4.889  -12.993 10.912  0.30 17.11 ?  10  LEU   A HD13 1 
ATOM   230  H HD13 B LEU   A 1 10  ? 5.024  -13.424 10.138  0.70 17.28 ?  10  LEU   A HD13 1 
ATOM   231  H HD21 A LEU   A 1 10  ? 5.570  -13.427 8.049   0.30 17.07 ?  10  LEU   A HD21 1 
ATOM   232  H HD21 B LEU   A 1 10  ? 5.933  -13.559 7.316   0.70 18.82 ?  10  LEU   A HD21 1 
ATOM   233  H HD22 A LEU   A 1 10  ? 5.381  -11.959 8.628   0.30 17.07 ?  10  LEU   A HD22 1 
ATOM   234  H HD22 B LEU   A 1 10  ? 5.584  -12.171 8.006   0.70 18.82 ?  10  LEU   A HD22 1 
ATOM   235  H HD23 A LEU   A 1 10  ? 6.735  -12.356 7.897   0.30 17.07 ?  10  LEU   A HD23 1 
ATOM   236  H HD23 B LEU   A 1 10  ? 7.014  -12.395 7.352   0.70 18.82 ?  10  LEU   A HD23 1 
ATOM   237  N N    A LYS   A 1 11  ? 9.121  -14.573 11.471  0.30 12.25 ?  11  LYS   A N    1 
ATOM   238  N N    B LYS   A 1 11  ? 9.209  -14.695 11.389  0.70 14.48 ?  11  LYS   A N    1 
ATOM   239  C CA   A LYS   A 1 11  ? 10.167 -15.556 11.204  0.30 12.54 ?  11  LYS   A CA   1 
ATOM   240  C CA   B LYS   A 1 11  ? 10.169 -15.708 10.985  0.70 14.69 ?  11  LYS   A CA   1 
ATOM   241  C C    A LYS   A 1 11  ? 9.891  -16.222 9.861   0.30 12.85 ?  11  LYS   A C    1 
ATOM   242  C C    B LYS   A 1 11  ? 9.806  -16.163 9.579   0.70 14.21 ?  11  LYS   A C    1 
ATOM   243  O O    A LYS   A 1 11  ? 8.881  -16.918 9.708   0.30 13.25 ?  11  LYS   A O    1 
ATOM   244  O O    B LYS   A 1 11  ? 8.664  -16.567 9.324   0.70 14.69 ?  11  LYS   A O    1 
ATOM   245  C CB   A LYS   A 1 11  ? 10.219 -16.599 12.324  0.30 12.58 ?  11  LYS   A CB   1 
ATOM   246  C CB   B LYS   A 1 11  ? 10.111 -16.867 11.978  0.70 15.43 ?  11  LYS   A CB   1 
ATOM   247  C CG   A LYS   A 1 11  ? 11.200 -17.746 12.079  0.30 13.05 ?  11  LYS   A CG   1 
ATOM   248  C CG   B LYS   A 1 11  ? 11.253 -17.867 11.928  0.70 15.94 ?  11  LYS   A CG   1 
ATOM   249  C CD   A LYS   A 1 11  ? 11.292 -18.671 13.288  0.30 13.76 ?  11  LYS   A CD   1 
ATOM   250  C CD   B LYS   A 1 11  ? 11.243 -18.697 13.212  0.70 16.89 ?  11  LYS   A CD   1 
ATOM   251  C CE   A LYS   A 1 11  ? 12.248 -19.841 13.051  0.30 14.28 ?  11  LYS   A CE   1 
ATOM   252  C CE   B LYS   A 1 11  ? 12.292 -19.799 13.214  0.70 17.40 ?  11  LYS   A CE   1 
ATOM   253  N NZ   A LYS   A 1 11  ? 13.661 -19.412 12.831  0.30 14.42 ?  11  LYS   A NZ   1 
ATOM   254  N NZ   B LYS   A 1 11  ? 13.670 -19.263 13.061  0.70 17.49 ?  11  LYS   A NZ   1 
ATOM   255  H H    A LYS   A 1 11  ? 8.389  -14.910 11.765  0.30 14.70 ?  11  LYS   A H    1 
ATOM   256  H H    B LYS   A 1 11  ? 8.628  -14.961 11.964  0.70 17.37 ?  11  LYS   A H    1 
ATOM   257  H HA   A LYS   A 1 11  ? 11.026 -15.109 11.163  0.30 15.05 ?  11  LYS   A HA   1 
ATOM   258  H HA   B LYS   A 1 11  ? 11.067 -15.344 10.982  0.70 17.63 ?  11  LYS   A HA   1 
ATOM   259  H HB2  A LYS   A 1 11  ? 10.480 -16.154 13.149  0.30 15.09 ?  11  LYS   A HB2  1 
ATOM   260  H HB2  B LYS   A 1 11  ? 10.093 -16.501 12.878  0.70 18.51 ?  11  LYS   A HB2  1 
ATOM   261  H HB3  A LYS   A 1 11  ? 9.332  -16.981 12.431  0.30 15.09 ?  11  LYS   A HB3  1 
ATOM   262  H HB3  B LYS   A 1 11  ? 9.291  -17.365 11.823  0.70 18.51 ?  11  LYS   A HB3  1 
ATOM   263  H HG2  A LYS   A 1 11  ? 10.898 -18.270 11.321  0.30 15.66 ?  11  LYS   A HG2  1 
ATOM   264  H HG2  B LYS   A 1 11  ? 11.138 -18.467 11.174  0.70 19.12 ?  11  LYS   A HG2  1 
ATOM   265  H HG3  A LYS   A 1 11  ? 12.081 -17.381 11.907  0.30 15.66 ?  11  LYS   A HG3  1 
ATOM   266  H HG3  B LYS   A 1 11  ? 12.101 -17.400 11.871  0.70 19.12 ?  11  LYS   A HG3  1 
ATOM   267  H HD2  A LYS   A 1 11  ? 11.615 -18.169 14.051  0.30 16.52 ?  11  LYS   A HD2  1 
ATOM   268  H HD2  B LYS   A 1 11  ? 11.420 -18.114 13.969  0.70 20.27 ?  11  LYS   A HD2  1 
ATOM   269  H HD3  A LYS   A 1 11  ? 10.413 -19.037 13.477  0.30 16.52 ?  11  LYS   A HD3  1 
ATOM   270  H HD3  B LYS   A 1 11  ? 10.371 -19.113 13.315  0.70 20.27 ?  11  LYS   A HD3  1 
ATOM   271  H HE2  A LYS   A 1 11  ? 12.231 -20.425 13.826  0.30 17.13 ?  11  LYS   A HE2  1 
ATOM   272  H HE2  B LYS   A 1 11  ? 12.245 -20.281 14.056  0.70 20.88 ?  11  LYS   A HE2  1 
ATOM   273  H HE3  A LYS   A 1 11  ? 11.960 -20.329 12.264  0.30 17.13 ?  11  LYS   A HE3  1 
ATOM   274  H HE3  B LYS   A 1 11  ? 12.116 -20.402 12.475  0.70 20.88 ?  11  LYS   A HE3  1 
ATOM   275  H HZ1  A LYS   A 1 11  ? 14.185 -20.128 12.739  0.30 17.31 ?  11  LYS   A HZ1  1 
ATOM   276  H HZ1  B LYS   A 1 11  ? 14.245 -19.936 12.971  0.70 20.98 ?  11  LYS   A HZ1  1 
ATOM   277  H HZ2  A LYS   A 1 11  ? 13.719 -18.916 12.096  0.30 17.31 ?  11  LYS   A HZ2  1 
ATOM   278  H HZ2  B LYS   A 1 11  ? 13.715 -18.744 12.342  0.70 20.98 ?  11  LYS   A HZ2  1 
ATOM   279  H HZ3  A LYS   A 1 11  ? 13.946 -18.936 13.527  0.30 17.31 ?  11  LYS   A HZ3  1 
ATOM   280  H HZ3  B LYS   A 1 11  ? 13.891 -18.788 13.779  0.70 20.98 ?  11  LYS   A HZ3  1 
ATOM   281  N N    A LEU   A 1 12  ? 10.793 -16.026 8.894   0.30 12.75 ?  12  LEU   A N    1 
ATOM   282  N N    B LEU   A 1 12  ? 10.752 -16.063 8.654   0.70 14.06 ?  12  LEU   A N    1 
ATOM   283  C CA   A LEU   A 1 12  ? 10.571 -16.557 7.551   0.30 13.36 ?  12  LEU   A CA   1 
ATOM   284  C CA   B LEU   A 1 12  ? 10.544 -16.651 7.340   0.70 15.07 ?  12  LEU   A CA   1 
ATOM   285  C C    A LEU   A 1 12  ? 11.091 -17.987 7.386   0.30 13.50 ?  12  LEU   A C    1 
ATOM   286  C C    B LEU   A 1 12  ? 11.135 -18.045 7.255   0.70 14.55 ?  12  LEU   A C    1 
ATOM   287  O O    A LEU   A 1 12  ? 10.389 -18.850 6.849   0.30 13.32 ?  12  LEU   A O    1 
ATOM   288  O O    B LEU   A 1 12  ? 10.528 -18.938 6.654   0.70 14.80 ?  12  LEU   A O    1 
ATOM   289  C CB   A LEU   A 1 12  ? 11.185 -15.621 6.500   0.30 13.92 ?  12  LEU   A CB   1 
ATOM   290  C CB   B LEU   A 1 12  ? 11.167 -15.780 6.252   0.70 15.76 ?  12  LEU   A CB   1 
ATOM   291  C CG   A LEU   A 1 12  ? 10.488 -14.269 6.296   0.30 14.36 ?  12  LEU   A CG   1 
ATOM   292  C CG   B LEU   A 1 12  ? 10.554 -14.391 6.093   0.70 17.05 ?  12  LEU   A CG   1 
ATOM   293  C CD1  A LEU   A 1 12  ? 11.189 -13.446 5.219   0.30 14.70 ?  12  LEU   A CD1  1 
ATOM   294  C CD1  B LEU   A 1 12  ? 11.330 -13.614 5.043   0.70 17.76 ?  12  LEU   A CD1  1 
ATOM   295  C CD2  A LEU   A 1 12  ? 9.020  -14.467 5.942   0.30 14.80 ?  12  LEU   A CD2  1 
ATOM   296  C CD2  B LEU   A 1 12  ? 9.076  -14.486 5.728   0.70 18.03 ?  12  LEU   A CD2  1 
ATOM   297  H H    A LEU   A 1 12  ? 11.534 -15.581 8.988   0.30 15.29 ?  12  LEU   A H    1 
ATOM   298  H H    B LEU   A 1 12  ? 11.499 -15.650 8.760   0.70 16.88 ?  12  LEU   A H    1 
ATOM   299  H HA   A LEU   A 1 12  ? 9.620  -16.584 7.397   0.30 16.03 ?  12  LEU   A HA   1 
ATOM   300  H HA   B LEU   A 1 12  ? 9.594  -16.718 7.169   0.70 18.08 ?  12  LEU   A HA   1 
ATOM   301  H HB2  A LEU   A 1 12  ? 12.102 -15.428 6.756   0.30 16.70 ?  12  LEU   A HB2  1 
ATOM   302  H HB2  B LEU   A 1 12  ? 12.109 -15.665 6.456   0.70 18.91 ?  12  LEU   A HB2  1 
ATOM   303  H HB3  A LEU   A 1 12  ? 11.178 -16.073 5.645   0.30 16.70 ?  12  LEU   A HB3  1 
ATOM   304  H HB3  B LEU   A 1 12  ? 11.072 -16.242 5.406   0.70 18.91 ?  12  LEU   A HB3  1 
ATOM   305  H HG   A LEU   A 1 12  ? 10.531 -13.761 7.122   0.30 17.23 ?  12  LEU   A HG   1 
ATOM   306  H HG   B LEU   A 1 12  ? 10.630 -13.916 6.935   0.70 20.46 ?  12  LEU   A HG   1 
ATOM   307  H HD11 A LEU   A 1 12  ? 10.730 -12.595 5.118   0.30 17.64 ?  12  LEU   A HD11 1 
ATOM   308  H HD11 B LEU   A 1 12  ? 10.935 -12.734 4.945   0.70 21.31 ?  12  LEU   A HD11 1 
ATOM   309  H HD12 A LEU   A 1 12  ? 12.110 -13.292 5.484   0.30 17.64 ?  12  LEU   A HD12 1 
ATOM   310  H HD12 B LEU   A 1 12  ? 12.256 -13.528 5.330   0.70 21.31 ?  12  LEU   A HD12 1 
ATOM   311  H HD13 A LEU   A 1 12  ? 11.164 -13.933 4.380   0.30 17.64 ?  12  LEU   A HD13 1 
ATOM   312  H HD13 B LEU   A 1 12  ? 11.291 -14.091 4.200   0.70 21.31 ?  12  LEU   A HD13 1 
ATOM   313  H HD21 A LEU   A 1 12  ? 8.662  -13.636 5.598   0.30 17.76 ?  12  LEU   A HD21 1 
ATOM   314  H HD21 B LEU   A 1 12  ? 8.758  -13.608 5.475   0.70 21.63 ?  12  LEU   A HD21 1 
ATOM   315  H HD22 A LEU   A 1 12  ? 8.954  -15.162 5.268   0.30 17.76 ?  12  LEU   A HD22 1 
ATOM   316  H HD22 B LEU   A 1 12  ? 8.974  -15.104 4.987   0.70 21.63 ?  12  LEU   A HD22 1 
ATOM   317  H HD23 A LEU   A 1 12  ? 8.540  -14.733 6.740   0.30 17.76 ?  12  LEU   A HD23 1 
ATOM   318  H HD23 B LEU   A 1 12  ? 8.582  -14.811 6.498   0.70 21.63 ?  12  LEU   A HD23 1 
ATOM   319  N N    . THR   A 1 13  ? 12.321 -18.238 7.827   1.00 14.19 ?  13  THR   A N    1 
ATOM   320  C CA   . THR   A 1 13  ? 12.985 -19.530 7.770   1.00 14.44 ?  13  THR   A CA   1 
ATOM   321  C C    . THR   A 1 13  ? 13.746 -19.733 9.077   1.00 14.72 ?  13  THR   A C    1 
ATOM   322  O O    . THR   A 1 13  ? 13.647 -18.939 10.016  1.00 14.82 ?  13  THR   A O    1 
ATOM   323  C CB   . THR   A 1 13  ? 13.977 -19.599 6.600   1.00 15.37 ?  13  THR   A CB   1 
ATOM   324  O OG1  . THR   A 1 13  ? 15.029 -18.666 6.833   1.00 15.95 ?  13  THR   A OG1  1 
ATOM   325  C CG2  . THR   A 1 13  ? 13.330 -19.295 5.262   1.00 16.58 ?  13  THR   A CG2  1 
ATOM   326  H H    A THR   A 1 13  ? 12.822 -17.633 8.183   0.30 17.02 ?  13  THR   A H    1 
ATOM   327  H H    B THR   A 1 13  ? 12.768 -17.632 8.247   0.70 17.02 ?  13  THR   A H    1 
ATOM   328  H HA   . THR   A 1 13  ? 12.331 -20.238 7.665   1.00 17.33 ?  13  THR   A HA   1 
ATOM   329  H HB   . THR   A 1 13  ? 14.360 -20.487 6.553   1.00 18.45 ?  13  THR   A HB   1 
ATOM   330  H HG1  . THR   A 1 13  ? 15.590 -18.685 6.202   1.00 19.14 ?  13  THR   A HG1  1 
ATOM   331  H HG21 . THR   A 1 13  ? 13.958 -19.490 4.543   1.00 19.89 ?  13  THR   A HG21 1 
ATOM   332  H HG22 . THR   A 1 13  ? 12.544 -19.846 5.148   1.00 19.89 ?  13  THR   A HG22 1 
ATOM   333  H HG23 . THR   A 1 13  ? 13.080 -18.362 5.216   1.00 19.89 ?  13  THR   A HG23 1 
ATOM   334  N N    A ASP   A 1 14  ? 14.566 -20.786 9.104   0.30 15.15 ?  14  ASP   A N    1 
ATOM   335  N N    B ASP   A 1 14  ? 14.522 -20.815 9.137   0.70 15.27 ?  14  ASP   A N    1 
ATOM   336  C CA   A ASP   A 1 14  ? 15.369 -21.090 10.284  0.30 15.63 ?  14  ASP   A CA   1 
ATOM   337  C CA   B ASP   A 1 14  ? 15.351 -21.062 10.310  0.70 16.15 ?  14  ASP   A CA   1 
ATOM   338  C C    A ASP   A 1 14  ? 16.281 -19.932 10.674  0.30 14.64 ?  14  ASP   A C    1 
ATOM   339  C C    B ASP   A 1 14  ? 16.159 -19.827 10.701  0.70 15.24 ?  14  ASP   A C    1 
ATOM   340  O O    A ASP   A 1 14  ? 16.638 -19.800 11.850  0.30 14.36 ?  14  ASP   A O    1 
ATOM   341  O O    B ASP   A 1 14  ? 16.314 -19.529 11.891  0.70 16.23 ?  14  ASP   A O    1 
ATOM   342  C CB   A ASP   A 1 14  ? 16.204 -22.345 10.022  0.30 17.59 ?  14  ASP   A CB   1 
ATOM   343  C CB   B ASP   A 1 14  ? 16.294 -22.233 10.042  0.70 19.07 ?  14  ASP   A CB   1 
ATOM   344  C CG   A ASP   A 1 14  ? 17.093 -22.712 11.194  0.30 19.47 ?  14  ASP   A CG   1 
ATOM   345  C CG   B ASP   A 1 14  ? 17.274 -22.450 11.176  0.70 23.53 ?  14  ASP   A CG   1 
ATOM   346  O OD1  A ASP   A 1 14  ? 16.553 -23.155 12.231  0.30 19.53 ?  14  ASP   A OD1  1 
ATOM   347  O OD1  B ASP   A 1 14  ? 16.817 -22.723 12.307  0.70 24.88 ?  14  ASP   A OD1  1 
ATOM   348  O OD2  A ASP   A 1 14  ? 18.327 -22.571 11.076  0.30 20.99 -1 14  ASP   A OD2  1 
ATOM   349  O OD2  B ASP   A 1 14  ? 18.495 -22.328 10.940  0.70 25.52 -1 14  ASP   A OD2  1 
ATOM   350  H H    A ASP   A 1 14  ? 14.683 -21.328 8.450   0.30 18.18 ?  14  ASP   A H    1 
ATOM   351  H H    B ASP   A 1 14  ? 14.600 -21.398 8.513   0.70 18.33 ?  14  ASP   A H    1 
ATOM   352  H HA   A ASP   A 1 14  ? 14.780 -21.273 11.029  0.30 18.76 ?  14  ASP   A HA   1 
ATOM   353  H HA   B ASP   A 1 14  ? 14.779 -21.301 11.055  0.70 19.38 ?  14  ASP   A HA   1 
ATOM   354  H HB2  A ASP   A 1 14  ? 15.610 -23.097 9.877   0.30 21.10 ?  14  ASP   A HB2  1 
ATOM   355  H HB2  B ASP   A 1 14  ? 15.757 -23.042 9.897   0.70 22.88 ?  14  ASP   A HB2  1 
ATOM   356  H HB3  A ASP   A 1 14  ? 16.755 -22.201 9.234   0.30 21.10 ?  14  ASP   A HB3  1 
ATOM   357  H HB3  B ASP   A 1 14  ? 16.819 -22.051 9.250   0.70 22.88 ?  14  ASP   A HB3  1 
ATOM   358  N N    . ASN   A 1 15  ? 16.671 -19.088 9.715   1.00 14.31 ?  15  ASN   A N    1 
ATOM   359  C CA   . ASN   A 1 15  ? 17.655 -18.047 9.976   1.00 14.69 ?  15  ASN   A CA   1 
ATOM   360  C C    . ASN   A 1 15  ? 17.298 -16.664 9.439   1.00 14.91 ?  15  ASN   A C    1 
ATOM   361  O O    . ASN   A 1 15  ? 18.083 -15.734 9.650   1.00 16.16 ?  15  ASN   A O    1 
ATOM   362  C CB   . ASN   A 1 15  ? 19.029 -18.455 9.417   1.00 14.73 ?  15  ASN   A CB   1 
ATOM   363  C CG   . ASN   A 1 15  ? 19.028 -18.569 7.910   1.00 14.90 ?  15  ASN   A CG   1 
ATOM   364  O OD1  . ASN   A 1 15  ? 18.329 -19.414 7.335   1.00 16.21 ?  15  ASN   A OD1  1 
ATOM   365  N ND2  . ASN   A 1 15  ? 19.810 -17.714 7.255   1.00 15.52 ?  15  ASN   A ND2  1 
ATOM   366  H H    A ASN   A 1 15  ? 16.376 -19.099 8.914   0.30 17.17 ?  15  ASN   A H    1 
ATOM   367  H H    B ASN   A 1 15  ? 16.460 -19.172 8.892   0.70 17.17 ?  15  ASN   A H    1 
ATOM   368  H HA   . ASN   A 1 15  ? 17.759 -17.951 10.938  1.00 17.63 ?  15  ASN   A HA   1 
ATOM   369  H HB2  . ASN   A 1 15  ? 19.686 -17.779 9.674   1.00 17.68 ?  15  ASN   A HB2  1 
ATOM   370  H HB3  . ASN   A 1 15  ? 19.282 -19.313 9.787   1.00 17.68 ?  15  ASN   A HB3  1 
ATOM   371  H HD21 . ASN   A 1 15  ? 19.835 -17.735 6.400   1.00 18.63 ?  15  ASN   A HD21 1 
ATOM   372  H HD22 . ASN   A 1 15  ? 20.277 -17.132 7.688   1.00 18.63 ?  15  ASN   A HD22 1 
ATOM   373  N N    . VAL   A 1 16  ? 16.165 -16.489 8.760   1.00 14.63 ?  16  VAL   A N    1 
ATOM   374  C CA   . VAL   A 1 16  ? 15.785 -15.205 8.177   1.00 14.45 ?  16  VAL   A CA   1 
ATOM   375  C C    . VAL   A 1 16  ? 14.500 -14.709 8.826   1.00 13.76 ?  16  VAL   A C    1 
ATOM   376  O O    . VAL   A 1 16  ? 13.506 -15.443 8.907   1.00 14.01 ?  16  VAL   A O    1 
ATOM   377  C CB   . VAL   A 1 16  ? 15.643 -15.268 6.645   1.00 15.37 ?  16  VAL   A CB   1 
ATOM   378  C CG1  . VAL   A 1 16  ? 15.238 -13.895 6.084   1.00 16.14 ?  16  VAL   A CG1  1 
ATOM   379  C CG2  . VAL   A 1 16  ? 16.932 -15.758 6.004   1.00 16.02 ?  16  VAL   A CG2  1 
ATOM   380  H H    . VAL   A 1 16  ? 15.588 -17.119 8.634   1.00 17.56 ?  16  VAL   A H    1 
ATOM   381  H HA   . VAL   A 1 16  ? 16.480 -14.565 8.379   1.00 17.34 ?  16  VAL   A HA   1 
ATOM   382  H HB   . VAL   A 1 16  ? 14.942 -15.905 6.427   1.00 18.44 ?  16  VAL   A HB   1 
ATOM   383  H HG11 . VAL   A 1 16  ? 15.309 -13.923 5.118   1.00 19.37 ?  16  VAL   A HG11 1 
ATOM   384  H HG12 . VAL   A 1 16  ? 14.319 -13.708 6.340   1.00 19.37 ?  16  VAL   A HG12 1 
ATOM   385  H HG13 . VAL   A 1 16  ? 15.829 -13.221 6.444   1.00 19.37 ?  16  VAL   A HG13 1 
ATOM   386  H HG21 . VAL   A 1 16  ? 16.841 -15.708 5.041   1.00 19.23 ?  16  VAL   A HG21 1 
ATOM   387  H HG22 . VAL   A 1 16  ? 17.664 -15.190 6.296   1.00 19.23 ?  16  VAL   A HG22 1 
ATOM   388  H HG23 . VAL   A 1 16  ? 17.097 -16.673 6.277   1.00 19.23 ?  16  VAL   A HG23 1 
ATOM   389  N N    A TYR   A 1 17  ? 14.527 -13.440 9.262   0.30 13.07 ?  17  TYR   A N    1 
ATOM   390  N N    B TYR   A 1 17  ? 14.525 -13.453 9.248   0.70 13.52 ?  17  TYR   A N    1 
ATOM   391  C CA   A TYR   A 1 17  ? 13.460 -12.769 9.996   0.30 12.33 ?  17  TYR   A CA   1 
ATOM   392  C CA   B TYR   A 1 17  ? 13.414 -12.771 9.884   0.70 13.27 ?  17  TYR   A CA   1 
ATOM   393  C C    A TYR   A 1 17  ? 13.209 -11.409 9.357   0.30 12.08 ?  17  TYR   A C    1 
ATOM   394  C C    B TYR   A 1 17  ? 13.134 -11.482 9.117   0.70 13.14 ?  17  TYR   A C    1 
ATOM   395  O O    A TYR   A 1 17  ? 14.126 -10.807 8.794   0.30 11.69 ?  17  TYR   A O    1 
ATOM   396  O O    B TYR   A 1 17  ? 14.021 -10.938 8.457   0.70 13.32 ?  17  TYR   A O    1 
ATOM   397  C CB   A TYR   A 1 17  ? 13.874 -12.545 11.460  0.30 12.74 ?  17  TYR   A CB   1 
ATOM   398  C CB   B TYR   A 1 17  ? 13.776 -12.456 11.340  0.70 14.42 ?  17  TYR   A CB   1 
ATOM   399  C CG   A TYR   A 1 17  ? 14.079 -13.816 12.246  0.30 13.66 ?  17  TYR   A CG   1 
ATOM   400  C CG   B TYR   A 1 17  ? 13.971 -13.698 12.183  0.70 16.04 ?  17  TYR   A CG   1 
ATOM   401  C CD1  A TYR   A 1 17  ? 15.266 -14.531 12.163  0.30 14.34 ?  17  TYR   A CD1  1 
ATOM   402  C CD1  B TYR   A 1 17  ? 15.172 -14.406 12.174  0.70 17.33 ?  17  TYR   A CD1  1 
ATOM   403  C CD2  A TYR   A 1 17  ? 13.081 -14.302 13.078  0.30 14.09 ?  17  TYR   A CD2  1 
ATOM   404  C CD2  B TYR   A 1 17  ? 12.942 -14.178 12.977  0.70 16.82 ?  17  TYR   A CD2  1 
ATOM   405  C CE1  A TYR   A 1 17  ? 15.448 -15.702 12.883  0.30 15.00 ?  17  TYR   A CE1  1 
ATOM   406  C CE1  B TYR   A 1 17  ? 15.332 -15.564 12.945  0.70 18.31 ?  17  TYR   A CE1  1 
ATOM   407  C CE2  A TYR   A 1 17  ? 13.255 -15.472 13.801  0.30 14.76 ?  17  TYR   A CE2  1 
ATOM   408  C CE2  B TYR   A 1 17  ? 13.091 -15.332 13.744  0.70 18.12 ?  17  TYR   A CE2  1 
ATOM   409  C CZ   A TYR   A 1 17  ? 14.439 -16.168 13.703  0.30 15.14 ?  17  TYR   A CZ   1 
ATOM   410  C CZ   B TYR   A 1 17  ? 14.284 -16.019 13.729  0.70 18.71 ?  17  TYR   A CZ   1 
ATOM   411  O OH   A TYR   A 1 17  ? 14.619 -17.330 14.423  0.30 15.56 ?  17  TYR   A OH   1 
ATOM   412  O OH   B TYR   A 1 17  ? 14.424 -17.156 14.498  0.70 19.80 ?  17  TYR   A OH   1 
ATOM   413  H H    A TYR   A 1 17  ? 15.197 -12.911 9.119   0.30 15.69 ?  17  TYR   A H    1 
ATOM   414  H H    B TYR   A 1 17  ? 15.221 -12.944 9.167   0.70 16.22 ?  17  TYR   A H    1 
ATOM   415  H HA   A TYR   A 1 17  ? 12.642 -13.277 9.970   0.30 14.80 ?  17  TYR   A HA   1 
ATOM   416  H HA   B TYR   A 1 17  ? 12.628 -13.336 9.859   0.70 15.93 ?  17  TYR   A HA   1 
ATOM   417  H HB2  A TYR   A 1 17  ? 14.709 -12.054 11.479  0.30 15.29 ?  17  TYR   A HB2  1 
ATOM   418  H HB2  B TYR   A 1 17  ? 14.597 -11.945 11.355  0.70 17.31 ?  17  TYR   A HB2  1 
ATOM   419  H HB3  A TYR   A 1 17  ? 13.183 -12.035 11.908  0.30 15.29 ?  17  TYR   A HB3  1 
ATOM   420  H HB3  B TYR   A 1 17  ? 13.056 -11.939 11.729  0.70 17.31 ?  17  TYR   A HB3  1 
ATOM   421  H HD1  A TYR   A 1 17  ? 15.948 -14.220 11.610  0.30 17.21 ?  17  TYR   A HD1  1 
ATOM   422  H HD1  B TYR   A 1 17  ? 15.880 -14.108 11.646  0.70 20.79 ?  17  TYR   A HD1  1 
ATOM   423  H HD2  A TYR   A 1 17  ? 12.277 -13.838 13.145  0.30 16.90 ?  17  TYR   A HD2  1 
ATOM   424  H HD2  B TYR   A 1 17  ? 12.129 -13.732 12.994  0.70 20.19 ?  17  TYR   A HD2  1 
ATOM   425  H HE1  A TYR   A 1 17  ? 16.251 -16.166 12.817  0.30 18.00 ?  17  TYR   A HE1  1 
ATOM   426  H HE1  B TYR   A 1 17  ? 16.146 -16.028 12.935  0.70 21.97 ?  17  TYR   A HE1  1 
ATOM   427  H HE2  A TYR   A 1 17  ? 12.574 -15.780 14.352  0.30 17.71 ?  17  TYR   A HE2  1 
ATOM   428  H HE2  B TYR   A 1 17  ? 12.391 -15.637 14.274  0.70 21.74 ?  17  TYR   A HE2  1 
ATOM   429  H HH   A TYR   A 1 17  ? 15.380 -17.637 14.267  0.30 18.67 ?  17  TYR   A HH   1 
ATOM   430  H HH   B TYR   A 1 17  ? 13.711 -17.309 14.911  0.70 23.75 ?  17  TYR   A HH   1 
ATOM   431  N N    A ILE   A 1 18  ? 11.974 -10.903 9.457   0.30 11.96 ?  18  ILE   A N    1 
ATOM   432  N N    B ILE   A 1 18  ? 11.908 -10.968 9.215   0.70 13.66 ?  18  ILE   A N    1 
ATOM   433  C CA   A ILE   A 1 18  ? 11.612 -9.660  8.779   0.30 11.66 ?  18  ILE   A CA   1 
ATOM   434  C CA   B ILE   A 1 18  ? 11.542 -9.751  8.482   0.70 13.63 ?  18  ILE   A CA   1 
ATOM   435  C C    A ILE   A 1 18  ? 10.665 -8.824  9.629   0.30 11.63 ?  18  ILE   A C    1 
ATOM   436  C C    B ILE   A 1 18  ? 10.544 -8.930  9.291   0.70 14.25 ?  18  ILE   A C    1 
ATOM   437  O O    A ILE   A 1 18  ? 9.874  -9.350  10.421  0.30 11.83 ?  18  ILE   A O    1 
ATOM   438  O O    B ILE   A 1 18  ? 9.678  -9.479  9.979   0.70 13.97 ?  18  ILE   A O    1 
ATOM   439  C CB   A ILE   A 1 18  ? 11.003 -9.958  7.395   0.30 11.45 ?  18  ILE   A CB   1 
ATOM   440  C CB   B ILE   A 1 18  ? 11.034 -10.083 7.062   0.70 14.23 ?  18  ILE   A CB   1 
ATOM   441  C CG1  A ILE   A 1 18  ? 11.034 -8.728  6.485   0.30 12.22 ?  18  ILE   A CG1  1 
ATOM   442  C CG1  B ILE   A 1 18  ? 10.924 -8.810  6.229   0.70 14.87 ?  18  ILE   A CG1  1 
ATOM   443  C CG2  A ILE   A 1 18  ? 9.594  -10.530 7.535   0.30 11.79 ?  18  ILE   A CG2  1 
ATOM   444  C CG2  B ILE   A 1 18  ? 9.717  -10.863 7.118   0.70 14.43 ?  18  ILE   A CG2  1 
ATOM   445  C CD1  A ILE   A 1 18  ? 10.702 -9.069  5.045   0.30 13.10 ?  18  ILE   A CD1  1 
ATOM   446  C CD1  B ILE   A 1 18  ? 10.686 -9.075  4.774   0.70 16.53 ?  18  ILE   A CD1  1 
ATOM   447  H H    A ILE   A 1 18  ? 11.327 -11.268 9.897   0.30 14.35 ?  18  ILE   A H    1 
ATOM   448  H H    B ILE   A 1 18  ? 11.283 -11.304 9.694   0.70 16.39 ?  18  ILE   A H    1 
ATOM   449  H HA   A ILE   A 1 18  ? 12.420 -9.136  8.650   0.30 13.99 ?  18  ILE   A HA   1 
ATOM   450  H HA   B ILE   A 1 18  ? 12.343 -9.216  8.378   0.70 16.36 ?  18  ILE   A HA   1 
ATOM   451  H HB   A ILE   A 1 18  ? 11.558 -10.630 6.991   0.30 13.74 ?  18  ILE   A HB   1 
ATOM   452  H HB   B ILE   A 1 18  ? 11.695 -10.656 6.632   0.70 17.07 ?  18  ILE   A HB   1 
ATOM   453  H HG12 A ILE   A 1 18  ? 10.387 -8.077  6.796   0.30 14.67 ?  18  ILE   A HG12 1 
ATOM   454  H HG12 B ILE   A 1 18  ? 10.188 -8.281  6.563   0.70 17.84 ?  18  ILE   A HG12 1 
ATOM   455  H HG13 A ILE   A 1 18  ? 11.927 -8.340  6.499   0.30 14.67 ?  18  ILE   A HG13 1 
ATOM   456  H HG13 B ILE   A 1 18  ? 11.755 -8.313  6.307   0.70 17.84 ?  18  ILE   A HG13 1 
ATOM   457  H HG21 A ILE   A 1 18  ? 9.324  -10.891 6.678   0.30 14.14 ?  18  ILE   A HG21 1 
ATOM   458  H HG21 B ILE   A 1 18  ? 9.499  -11.182 6.226   0.70 17.32 ?  18  ILE   A HG21 1 
ATOM   459  H HG22 A ILE   A 1 18  ? 9.609  -11.233 8.202   0.30 14.14 ?  18  ILE   A HG22 1 
ATOM   460  H HG22 B ILE   A 1 18  ? 9.823  -11.615 7.719   0.70 17.32 ?  18  ILE   A HG22 1 
ATOM   461  H HG23 A ILE   A 1 18  ? 8.987  -9.827  7.808   0.30 14.14 ?  18  ILE   A HG23 1 
ATOM   462  H HG23 B ILE   A 1 18  ? 9.017  -10.275 7.439   0.70 17.32 ?  18  ILE   A HG23 1 
ATOM   463  H HD11 A ILE   A 1 18  ? 10.830 -8.284  4.492   0.30 15.72 ?  18  ILE   A HD11 1 
ATOM   464  H HD11 B ILE   A 1 18  ? 10.696 -8.229  4.298   0.70 19.84 ?  18  ILE   A HD11 1 
ATOM   465  H HD12 A ILE   A 1 18  ? 11.288 -9.783  4.745   0.30 15.72 ?  18  ILE   A HD12 1 
ATOM   466  H HD12 B ILE   A 1 18  ? 11.385 -9.653  4.439   0.70 19.84 ?  18  ILE   A HD12 1 
ATOM   467  H HD13 A ILE   A 1 18  ? 9.777  -9.362  4.995   0.30 15.72 ?  18  ILE   A HD13 1 
ATOM   468  H HD13 B ILE   A 1 18  ? 9.821  -9.501  4.671   0.70 19.84 ?  18  ILE   A HD13 1 
ATOM   469  N N    A LYS   A 1 19  ? 10.730 -7.504  9.430   0.30 11.94 ?  19  LYS   A N    1 
ATOM   470  N N    B LYS   A 1 19  ? 10.660 -7.604  9.183   0.70 14.54 ?  19  LYS   A N    1 
ATOM   471  C CA   A LYS   A 1 19  ? 9.960  -6.563  10.228  0.30 12.62 ?  19  LYS   A CA   1 
ATOM   472  C CA   B LYS   A 1 19  ? 9.796  -6.668  9.894   0.70 14.99 ?  19  LYS   A CA   1 
ATOM   473  C C    A LYS   A 1 19  ? 9.756  -5.291  9.419   0.30 12.69 ?  19  LYS   A C    1 
ATOM   474  C C    B LYS   A 1 19  ? 9.590  -5.419  9.050   0.70 14.41 ?  19  LYS   A C    1 
ATOM   475  O O    A LYS   A 1 19  ? 10.685 -4.818  8.761   0.30 12.29 ?  19  LYS   A O    1 
ATOM   476  O O    B LYS   A 1 19  ? 10.487 -5.002  8.308   0.70 13.63 ?  19  LYS   A O    1 
ATOM   477  C CB   A LYS   A 1 19  ? 10.706 -6.252  11.531  0.30 13.29 ?  19  LYS   A CB   1 
ATOM   478  C CB   B LYS   A 1 19  ? 10.450 -6.246  11.213  0.70 15.73 ?  19  LYS   A CB   1 
ATOM   479  C CG   A LYS   A 1 19  ? 9.986  -5.332  12.481  0.30 13.81 ?  19  LYS   A CG   1 
ATOM   480  C CG   B LYS   A 1 19  ? 9.612  -5.366  12.136  0.70 16.59 ?  19  LYS   A CG   1 
ATOM   481  C CD   A LYS   A 1 19  ? 10.849 -5.089  13.697  0.30 14.32 ?  19  LYS   A CD   1 
ATOM   482  C CD   B LYS   A 1 19  ? 10.416 -5.035  13.386  0.70 17.34 ?  19  LYS   A CD   1 
ATOM   483  C CE   A LYS   A 1 19  ? 10.155 -4.205  14.701  0.30 14.66 ?  19  LYS   A CE   1 
ATOM   484  C CE   B LYS   A 1 19  ? 9.652  -4.165  14.365  0.70 18.21 ?  19  LYS   A CE   1 
ATOM   485  N NZ   A LYS   A 1 19  ? 11.022 -3.969  15.883  0.30 14.93 ?  19  LYS   A NZ   1 
ATOM   486  N NZ   B LYS   A 1 19  ? 10.511 -3.816  15.531  0.70 18.80 ?  19  LYS   A NZ   1 
ATOM   487  H H    A LYS   A 1 19  ? 11.219 -7.112  8.827   0.30 14.33 ?  19  LYS   A H    1 
ATOM   488  H H    B LYS   A 1 19  ? 11.256 -7.221  8.703   0.70 17.45 ?  19  LYS   A H    1 
ATOM   489  H HA   A LYS   A 1 19  ? 9.095  -6.931  10.446  0.30 15.15 ?  19  LYS   A HA   1 
ATOM   490  H HA   B LYS   A 1 19  ? 8.934  -7.091  10.078  0.70 17.99 ?  19  LYS   A HA   1 
ATOM   491  H HB2  A LYS   A 1 19  ? 10.856 -7.085  12.004  0.30 15.95 ?  19  LYS   A HB2  1 
ATOM   492  H HB2  B LYS   A 1 19  ? 10.674 -7.043  11.709  0.70 18.88 ?  19  LYS   A HB2  1 
ATOM   493  H HB3  A LYS   A 1 19  ? 11.557 -5.839  11.320  0.30 15.95 ?  19  LYS   A HB3  1 
ATOM   494  H HB3  B LYS   A 1 19  ? 11.255 -5.754  11.001  0.70 18.88 ?  19  LYS   A HB3  1 
ATOM   495  H HG2  A LYS   A 1 19  ? 9.816  -4.480  12.050  0.30 16.57 ?  19  LYS   A HG2  1 
ATOM   496  H HG2  B LYS   A 1 19  ? 9.385  -4.532  11.691  0.70 19.91 ?  19  LYS   A HG2  1 
ATOM   497  H HG3  A LYS   A 1 19  ? 9.155  -5.742  12.769  0.30 16.57 ?  19  LYS   A HG3  1 
ATOM   498  H HG3  B LYS   A 1 19  ? 8.807  -5.835  12.408  0.70 19.91 ?  19  LYS   A HG3  1 
ATOM   499  H HD2  A LYS   A 1 19  ? 11.048 -5.938  14.122  0.30 17.18 ?  19  LYS   A HD2  1 
ATOM   500  H HD2  B LYS   A 1 19  ? 10.652 -5.859  13.840  0.70 20.81 ?  19  LYS   A HD2  1 
ATOM   501  H HD3  A LYS   A 1 19  ? 11.672 -4.653  13.421  0.30 17.18 ?  19  LYS   A HD3  1 
ATOM   502  H HD3  B LYS   A 1 19  ? 11.221 -4.556  13.129  0.70 20.81 ?  19  LYS   A HD3  1 
ATOM   503  H HE2  A LYS   A 1 19  ? 9.954  -3.349  14.290  0.30 17.59 ?  19  LYS   A HE2  1 
ATOM   504  H HE2  B LYS   A 1 19  ? 9.380  -3.343  13.929  0.70 21.85 ?  19  LYS   A HE2  1 
ATOM   505  H HE3  A LYS   A 1 19  ? 9.339  -4.636  14.999  0.30 17.59 ?  19  LYS   A HE3  1 
ATOM   506  H HE3  B LYS   A 1 19  ? 8.876  -4.648  14.693  0.70 21.85 ?  19  LYS   A HE3  1 
ATOM   507  H HZ1  A LYS   A 1 19  ? 10.588 -3.478  16.482  0.30 17.92 ?  19  LYS   A HZ1  1 
ATOM   508  H HZ1  B LYS   A 1 19  ? 10.060 -3.306  16.103  0.70 22.55 ?  19  LYS   A HZ1  1 
ATOM   509  H HZ2  A LYS   A 1 19  ? 11.250 -4.746  16.250  0.30 17.92 ?  19  LYS   A HZ2  1 
ATOM   510  H HZ2  B LYS   A 1 19  ? 10.774 -4.557  15.948  0.70 22.55 ?  19  LYS   A HZ2  1 
ATOM   511  H HZ3  A LYS   A 1 19  ? 11.760 -3.539  15.634  0.30 17.92 ?  19  LYS   A HZ3  1 
ATOM   512  H HZ3  B LYS   A 1 19  ? 11.232 -3.371  15.254  0.70 22.55 ?  19  LYS   A HZ3  1 
ATOM   513  N N    A ASN   A 1 20  ? 8.538  -4.752  9.454   0.30 13.28 ?  20  ASN   A N    1 
ATOM   514  N N    B ASN   A 1 20  ? 8.417  -4.798  9.197   0.70 15.15 ?  20  ASN   A N    1 
ATOM   515  C CA   A ASN   A 1 20  ? 8.270  -3.438  8.876   0.30 13.45 ?  20  ASN   A CA   1 
ATOM   516  C CA   B ASN   A 1 20  ? 8.125  -3.518  8.553   0.70 15.18 ?  20  ASN   A CA   1 
ATOM   517  C C    A ASN   A 1 20  ? 8.843  -2.414  9.842   0.30 13.23 ?  20  ASN   A C    1 
ATOM   518  C C    B ASN   A 1 20  ? 8.639  -2.422  9.482   0.70 15.48 ?  20  ASN   A C    1 
ATOM   519  O O    A ASN   A 1 20  ? 8.284  -2.170  10.914  0.30 13.44 ?  20  ASN   A O    1 
ATOM   520  O O    B ASN   A 1 20  ? 7.952  -2.023  10.426  0.70 16.80 ?  20  ASN   A O    1 
ATOM   521  C CB   A ASN   A 1 20  ? 6.775  -3.236  8.661   0.30 14.23 ?  20  ASN   A CB   1 
ATOM   522  C CB   B ASN   A 1 20  ? 6.623  -3.395  8.302   0.70 15.09 ?  20  ASN   A CB   1 
ATOM   523  C CG   A ASN   A 1 20  ? 6.418  -1.811  8.263   0.30 15.03 ?  20  ASN   A CG   1 
ATOM   524  C CG   B ASN   A 1 20  ? 6.213  -2.089  7.624   0.70 14.97 ?  20  ASN   A CG   1 
ATOM   525  O OD1  A ASN   A 1 20  ? 5.433  -1.257  8.749   0.30 16.25 ?  20  ASN   A OD1  1 
ATOM   526  O OD1  B ASN   A 1 20  ? 5.060  -1.663  7.760   0.70 15.56 ?  20  ASN   A OD1  1 
ATOM   527  N ND2  A ASN   A 1 20  ? 7.214  -1.214  7.381   0.30 14.58 ?  20  ASN   A ND2  1 
ATOM   528  N ND2  B ASN   A 1 20  ? 7.133  -1.460  6.885   0.70 15.46 ?  20  ASN   A ND2  1 
ATOM   529  H H    A ASN   A 1 20  ? 7.848  -5.126  9.800   0.30 15.93 ?  20  ASN   A H    1 
ATOM   530  H H    B ASN   A 1 20  ? 7.765  -5.103  9.675   0.70 18.18 ?  20  ASN   A H    1 
ATOM   531  H HA   A ASN   A 1 20  ? 8.722  -3.352  8.024   0.30 16.14 ?  20  ASN   A HA   1 
ATOM   532  H HA   B ASN   A 1 20  ? 8.590  -3.472  7.705   0.70 18.22 ?  20  ASN   A HA   1 
ATOM   533  H HB2  A ASN   A 1 20  ? 6.476  -3.826  7.952   0.30 17.07 ?  20  ASN   A HB2  1 
ATOM   534  H HB2  B ASN   A 1 20  ? 6.329  -4.123  7.741   0.70 18.11 ?  20  ASN   A HB2  1 
ATOM   535  H HB3  A ASN   A 1 20  ? 6.304  -3.441  9.482   0.30 17.07 ?  20  ASN   A HB3  1 
ATOM   536  H HB3  B ASN   A 1 20  ? 6.162  -3.440  9.153   0.70 18.11 ?  20  ASN   A HB3  1 
ATOM   537  H HD21 A ASN   A 1 20  ? 7.045  -0.410  7.124   0.30 17.50 ?  20  ASN   A HD21 1 
ATOM   538  H HD21 B ASN   A 1 20  ? 6.935  -0.727  6.487   0.70 18.56 ?  20  ASN   A HD21 1 
ATOM   539  H HD22 A ASN   A 1 20  ? 7.897  -1.629  7.067   0.30 17.50 ?  20  ASN   A HD22 1 
ATOM   540  H HD22 B ASN   A 1 20  ? 7.920  -1.797  6.794   0.70 18.56 ?  20  ASN   A HD22 1 
ATOM   541  N N    A ALA   A 1 21  ? 9.986  -1.835  9.480   0.30 13.09 ?  21  ALA   A N    1 
ATOM   542  N N    B ALA   A 1 21  ? 9.858  -1.938  9.223   0.70 15.65 ?  21  ALA   A N    1 
ATOM   543  C CA   A ALA   A 1 21  ? 10.676 -0.942  10.393  0.30 13.23 ?  21  ALA   A CA   1 
ATOM   544  C CA   B ALA   A 1 21  ? 10.493 -0.960  10.101  0.70 15.75 ?  21  ALA   A CA   1 
ATOM   545  C C    A ALA   A 1 21  ? 11.698 -0.119  9.631   0.30 13.77 ?  21  ALA   A C    1 
ATOM   546  C C    B ALA   A 1 21  ? 11.611 -0.239  9.360   0.70 14.73 ?  21  ALA   A C    1 
ATOM   547  O O    A ALA   A 1 21  ? 12.251 -0.563  8.622   0.30 14.29 ?  21  ALA   A O    1 
ATOM   548  O O    B ALA   A 1 21  ? 12.134 -0.734  8.358   0.70 14.74 ?  21  ALA   A O    1 
ATOM   549  C CB   A ALA   A 1 21  ? 11.384 -1.732  11.494  0.30 13.38 ?  21  ALA   A CB   1 
ATOM   550  C CB   B ALA   A 1 21  ? 11.042 -1.628  11.366  0.70 17.49 ?  21  ALA   A CB   1 
ATOM   551  H H    A ALA   A 1 21  ? 10.379 -1.943  8.720   0.30 15.71 ?  21  ALA   A H    1 
ATOM   552  H H    B ALA   A 1 21  ? 10.334 -2.154  8.539   0.70 18.78 ?  21  ALA   A H    1 
ATOM   553  H HA   A ALA   A 1 21  ? 10.033 -0.337  10.804  0.30 15.88 ?  21  ALA   A HA   1 
ATOM   554  H HA   B ALA   A 1 21  ? 9.836  -0.297  10.372  0.70 18.90 ?  21  ALA   A HA   1 
ATOM   555  H HB1  A ALA   A 1 21  ? 11.788 -1.108  12.111  0.30 16.06 ?  21  ALA   A HB1  1 
ATOM   556  H HB1  B ALA   A 1 21  ? 11.454 -0.956  11.930  0.70 20.99 ?  21  ALA   A HB1  1 
ATOM   557  H HB2  A ALA   A 1 21  ? 10.727 -2.278  11.953  0.30 16.06 ?  21  ALA   A HB2  1 
ATOM   558  H HB2  B ALA   A 1 21  ? 10.307 -2.052  11.844  0.70 20.99 ?  21  ALA   A HB2  1 
ATOM   559  H HB3  A ALA   A 1 21  ? 12.059 -2.294  11.087  0.30 16.06 ?  21  ALA   A HB3  1 
ATOM   560  H HB3  B ALA   A 1 21  ? 11.697 -2.297  11.114  0.70 20.99 ?  21  ALA   A HB3  1 
ATOM   561  N N    A ASP   A 1 22  ? 11.932 1.087   10.137  0.30 13.97 ?  22  ASP   A N    1 
ATOM   562  N N    B ASP   A 1 22  ? 11.946 0.956   9.867   0.70 14.44 ?  22  ASP   A N    1 
ATOM   563  C CA   A ASP   A 1 22  ? 13.015 1.933   9.658   0.30 13.75 ?  22  ASP   A CA   1 
ATOM   564  C CA   B ASP   A 1 22  ? 13.101 1.732   9.416   0.70 14.11 ?  22  ASP   A CA   1 
ATOM   565  C C    A ASP   A 1 22  ? 14.330 1.383   10.193  0.30 13.36 ?  22  ASP   A C    1 
ATOM   566  C C    B ASP   A 1 22  ? 14.365 1.132   10.025  0.70 12.77 ?  22  ASP   A C    1 
ATOM   567  O O    A ASP   A 1 22  ? 14.550 1.361   11.408  0.30 13.21 ?  22  ASP   A O    1 
ATOM   568  O O    B ASP   A 1 22  ? 14.485 1.051   11.251  0.70 13.45 ?  22  ASP   A O    1 
ATOM   569  C CB   A ASP   A 1 22  ? 12.786 3.347   10.182  0.30 13.94 ?  22  ASP   A CB   1 
ATOM   570  C CB   B ASP   A 1 22  ? 12.924 3.186   9.872   0.70 15.44 ?  22  ASP   A CB   1 
ATOM   571  C CG   A ASP   A 1 22  ? 13.785 4.351   9.634   0.30 13.55 ?  22  ASP   A CG   1 
ATOM   572  C CG   B ASP   A 1 22  ? 14.042 4.119   9.395   0.70 16.39 ?  22  ASP   A CG   1 
ATOM   573  O OD1  A ASP   A 1 22  ? 14.867 3.947   9.161   0.30 13.17 ?  22  ASP   A OD1  1 
ATOM   574  O OD1  B ASP   A 1 22  ? 15.060 3.649   8.839   0.70 16.04 ?  22  ASP   A OD1  1 
ATOM   575  O OD2  A ASP   A 1 22  ? 13.482 5.561   9.686   0.30 14.04 -1 22  ASP   A OD2  1 
ATOM   576  O OD2  B ASP   A 1 22  ? 13.883 5.345   9.589   0.70 18.67 -1 22  ASP   A OD2  1 
ATOM   577  H H    A ASP   A 1 22  ? 11.472 1.440   10.770  0.30 16.77 ?  22  ASP   A H    1 
ATOM   578  H H    B ASP   A 1 22  ? 11.494 1.358   10.490  0.70 17.33 ?  22  ASP   A H    1 
ATOM   579  H HA   A ASP   A 1 22  ? 13.035 1.945   8.686   0.30 16.50 ?  22  ASP   A HA   1 
ATOM   580  H HA   B ASP   A 1 22  ? 13.165 1.713   8.452   0.70 16.93 ?  22  ASP   A HA   1 
ATOM   581  H HB2  A ASP   A 1 22  ? 11.893 3.637   9.932   0.30 16.72 ?  22  ASP   A HB2  1 
ATOM   582  H HB2  B ASP   A 1 22  ? 12.087 3.534   9.524   0.70 18.53 ?  22  ASP   A HB2  1 
ATOM   583  H HB3  A ASP   A 1 22  ? 12.864 3.335   11.153  0.30 16.72 ?  22  ASP   A HB3  1 
ATOM   584  H HB3  B ASP   A 1 22  ? 12.910 3.220   10.844  0.70 18.53 ?  22  ASP   A HB3  1 
ATOM   585  N N    A ILE   A 1 23  ? 15.207 0.936   9.290   0.30 13.30 ?  23  ILE   A N    1 
ATOM   586  N N    B ILE   A 1 23  ? 15.313 0.722   9.174   0.70 12.35 ?  23  ILE   A N    1 
ATOM   587  C CA   A ILE   A 1 23  ? 16.466 0.332   9.718   0.30 13.08 ?  23  ILE   A CA   1 
ATOM   588  C CA   B ILE   A 1 23  ? 16.549 0.110   9.657   0.70 12.46 ?  23  ILE   A CA   1 
ATOM   589  C C    A ILE   A 1 23  ? 17.263 1.293   10.592  0.30 13.02 ?  23  ILE   A C    1 
ATOM   590  C C    B ILE   A 1 23  ? 17.287 1.036   10.619  0.70 12.66 ?  23  ILE   A C    1 
ATOM   591  O O    A ILE   A 1 23  ? 18.034 0.864   11.461  0.30 13.28 ?  23  ILE   A O    1 
ATOM   592  O O    B ILE   A 1 23  ? 17.938 0.570   11.564  0.70 13.11 ?  23  ILE   A O    1 
ATOM   593  C CB   A ILE   A 1 23  ? 17.271 -0.161  8.497   0.30 13.01 ?  23  ILE   A CB   1 
ATOM   594  C CB   B ILE   A 1 23  ? 17.439 -0.355  8.477   0.70 12.04 ?  23  ILE   A CB   1 
ATOM   595  C CG1  A ILE   A 1 23  ? 18.466 -1.006  8.952   0.30 13.12 ?  23  ILE   A CG1  1 
ATOM   596  C CG1  B ILE   A 1 23  ? 18.509 -1.330  8.976   0.70 12.26 ?  23  ILE   A CG1  1 
ATOM   597  C CG2  A ILE   A 1 23  ? 17.705 1.017   7.626   0.30 13.01 ?  23  ILE   A CG2  1 
ATOM   598  C CG2  B ILE   A 1 23  ? 18.082 0.828   7.755   0.70 11.83 ?  23  ILE   A CG2  1 
ATOM   599  C CD1  A ILE   A 1 23  ? 19.191 -1.704  7.820   0.30 13.16 ?  23  ILE   A CD1  1 
ATOM   600  C CD1  B ILE   A 1 23  ? 19.358 -1.932  7.872   0.70 12.73 ?  23  ILE   A CD1  1 
ATOM   601  H H    A ILE   A 1 23  ? 15.090 0.970   8.440   0.30 15.96 ?  23  ILE   A H    1 
ATOM   602  H H    B ILE   A 1 23  ? 15.259 0.778   8.331   0.70 14.82 ?  23  ILE   A H    1 
ATOM   603  H HA   A ILE   A 1 23  ? 16.258 -0.448  10.256  0.30 15.70 ?  23  ILE   A HA   1 
ATOM   604  H HA   B ILE   A 1 23  ? 16.311 -0.688  10.153  0.70 14.96 ?  23  ILE   A HA   1 
ATOM   605  H HB   A ILE   A 1 23  ? 16.692 -0.727  7.965   0.30 15.61 ?  23  ILE   A HB   1 
ATOM   606  H HB   B ILE   A 1 23  ? 16.878 -0.831  7.839   0.70 14.44 ?  23  ILE   A HB   1 
ATOM   607  H HG12 A ILE   A 1 23  ? 19.105 -0.431  9.401   0.30 15.74 ?  23  ILE   A HG12 1 
ATOM   608  H HG12 B ILE   A 1 23  ? 19.104 -0.855  9.578   0.70 14.71 ?  23  ILE   A HG12 1 
ATOM   609  H HG13 A ILE   A 1 23  ? 18.151 -1.689  9.566   0.30 15.74 ?  23  ILE   A HG13 1 
ATOM   610  H HG13 B ILE   A 1 23  ? 18.077 -2.058  9.445   0.70 14.71 ?  23  ILE   A HG13 1 
ATOM   611  H HG21 A ILE   A 1 23  ? 18.090 0.675   6.804   0.30 15.62 ?  23  ILE   A HG21 1 
ATOM   612  H HG21 B ILE   A 1 23  ? 18.452 0.514   6.911   0.70 14.19 ?  23  ILE   A HG21 1 
ATOM   613  H HG22 A ILE   A 1 23  ? 16.928 1.561   7.424   0.30 15.62 ?  23  ILE   A HG22 1 
ATOM   614  H HG22 B ILE   A 1 23  ? 17.405 1.497   7.591   0.70 14.19 ?  23  ILE   A HG22 1 
ATOM   615  H HG23 A ILE   A 1 23  ? 18.361 1.542   8.107   0.30 15.62 ?  23  ILE   A HG23 1 
ATOM   616  H HG23 B ILE   A 1 23  ? 18.786 1.187   8.312   0.70 14.19 ?  23  ILE   A HG23 1 
ATOM   617  H HD11 A ILE   A 1 23  ? 19.889 -2.267  8.193   0.30 15.80 ?  23  ILE   A HD11 1 
ATOM   618  H HD11 B ILE   A 1 23  ? 19.938 -2.611  8.255   0.70 15.28 ?  23  ILE   A HD11 1 
ATOM   619  H HD12 A ILE   A 1 23  ? 18.557 -2.246  7.326   0.30 15.80 ?  23  ILE   A HD12 1 
ATOM   620  H HD12 B ILE   A 1 23  ? 18.777 -2.331  7.207   0.70 15.28 ?  23  ILE   A HD12 1 
ATOM   621  H HD13 A ILE   A 1 23  ? 19.583 -1.036  7.237   0.30 15.80 ?  23  ILE   A HD13 1 
ATOM   622  H HD13 B ILE   A 1 23  ? 19.895 -1.233  7.465   0.70 15.28 ?  23  ILE   A HD13 1 
ATOM   623  N N    A VAL   A 1 24  ? 17.097 2.601   10.382  0.30 13.31 ?  24  VAL   A N    1 
ATOM   624  N N    B VAL   A 1 24  ? 17.195 2.352   10.406  0.70 13.83 ?  24  VAL   A N    1 
ATOM   625  C CA   A VAL   A 1 24  ? 17.769 3.584   11.228  0.30 13.85 ?  24  VAL   A CA   1 
ATOM   626  C CA   B VAL   A 1 24  ? 17.867 3.301   11.291  0.70 14.87 ?  24  VAL   A CA   1 
ATOM   627  C C    A VAL   A 1 24  ? 17.265 3.486   12.661  0.30 14.55 ?  24  VAL   A C    1 
ATOM   628  C C    B VAL   A 1 24  ? 17.277 3.227   12.693  0.70 15.36 ?  24  VAL   A C    1 
ATOM   629  O O    A VAL   A 1 24  ? 18.050 3.388   13.611  0.30 14.87 ?  24  VAL   A O    1 
ATOM   630  O O    B VAL   A 1 24  ? 18.002 3.262   13.695  0.70 16.21 ?  24  VAL   A O    1 
ATOM   631  C CB   A VAL   A 1 24  ? 17.585 5.002   10.657  0.30 13.97 ?  24  VAL   A CB   1 
ATOM   632  C CB   B VAL   A 1 24  ? 17.785 4.723   10.704  0.70 16.21 ?  24  VAL   A CB   1 
ATOM   633  C CG1  A VAL   A 1 24  ? 18.058 6.042   11.662  0.30 14.07 ?  24  VAL   A CG1  1 
ATOM   634  C CG1  B VAL   A 1 24  ? 18.489 5.709   11.610  0.70 17.43 ?  24  VAL   A CG1  1 
ATOM   635  C CG2  A VAL   A 1 24  ? 18.331 5.145   9.344   0.30 13.90 ?  24  VAL   A CG2  1 
ATOM   636  C CG2  B VAL   A 1 24  ? 18.380 4.758   9.305   0.70 16.78 ?  24  VAL   A CG2  1 
ATOM   637  H H    A VAL   A 1 24  ? 16.614 2.939   9.756   0.30 15.97 ?  24  VAL   A H    1 
ATOM   638  H H    B VAL   A 1 24  ? 16.755 2.712   9.764   0.70 16.60 ?  24  VAL   A H    1 
ATOM   639  H HA   A VAL   A 1 24  ? 18.716 3.391   11.238  0.30 16.62 ?  24  VAL   A HA   1 
ATOM   640  H HA   B VAL   A 1 24  ? 18.806 3.062   11.350  0.70 17.85 ?  24  VAL   A HA   1 
ATOM   641  H HB   A VAL   A 1 24  ? 16.641 5.157   10.486  0.30 16.76 ?  24  VAL   A HB   1 
ATOM   642  H HB   B VAL   A 1 24  ? 16.853 4.987   10.641  0.70 19.45 ?  24  VAL   A HB   1 
ATOM   643  H HG11 A VAL   A 1 24  ? 18.211 6.879   11.196  0.30 16.89 ?  24  VAL   A HG11 1 
ATOM   644  H HG11 B VAL   A 1 24  ? 18.607 6.545   11.132  0.70 20.92 ?  24  VAL   A HG11 1 
ATOM   645  H HG12 A VAL   A 1 24  ? 17.379 6.161   12.343  0.30 16.89 ?  24  VAL   A HG12 1 
ATOM   646  H HG12 B VAL   A 1 24  ? 17.944 5.852   12.394  0.70 20.92 ?  24  VAL   A HG12 1 
ATOM   647  H HG13 A VAL   A 1 24  ? 18.886 5.734   12.064  0.30 16.89 ?  24  VAL   A HG13 1 
ATOM   648  H HG13 B VAL   A 1 24  ? 19.352 5.347   11.862  0.70 20.92 ?  24  VAL   A HG13 1 
ATOM   649  H HG21 A VAL   A 1 24  ? 18.024 5.947   8.894   0.30 16.67 ?  24  VAL   A HG21 1 
ATOM   650  H HG21 B VAL   A 1 24  ? 18.403 5.675   8.995   0.70 20.13 ?  24  VAL   A HG21 1 
ATOM   651  H HG22 A VAL   A 1 24  ? 19.280 5.211   9.528   0.30 16.67 ?  24  VAL   A HG22 1 
ATOM   652  H HG22 B VAL   A 1 24  ? 19.279 4.396   9.338   0.70 20.13 ?  24  VAL   A HG22 1 
ATOM   653  H HG23 A VAL   A 1 24  ? 18.151 4.368   8.791   0.30 16.67 ?  24  VAL   A HG23 1 
ATOM   654  H HG23 B VAL   A 1 24  ? 17.829 4.222   8.714   0.70 20.13 ?  24  VAL   A HG23 1 
ATOM   655  N N    A GLU   A 1 25  ? 15.942 3.530   12.838  0.30 15.13 ?  25  GLU   A N    1 
ATOM   656  N N    B GLU   A 1 25  ? 15.950 3.121   12.787  0.70 15.67 ?  25  GLU   A N    1 
ATOM   657  C CA   A GLU   A 1 25  ? 15.378 3.466   14.181  0.30 16.02 ?  25  GLU   A CA   1 
ATOM   658  C CA   B GLU   A 1 25  ? 15.305 3.012   14.091  0.70 16.81 ?  25  GLU   A CA   1 
ATOM   659  C C    A GLU   A 1 25  ? 15.595 2.099   14.815  0.30 15.18 ?  25  GLU   A C    1 
ATOM   660  C C    B GLU   A 1 25  ? 15.597 1.666   14.744  0.70 16.25 ?  25  GLU   A C    1 
ATOM   661  O O    A GLU   A 1 25  ? 15.788 2.009   16.033  0.30 15.11 ?  25  GLU   A O    1 
ATOM   662  O O    B GLU   A 1 25  ? 15.819 1.598   15.959  0.70 16.99 ?  25  GLU   A O    1 
ATOM   663  C CB   A GLU   A 1 25  ? 13.893 3.833   14.153  0.30 17.81 ?  25  GLU   A CB   1 
ATOM   664  C CB   B GLU   A 1 25  ? 13.802 3.264   13.959  0.70 18.27 ?  25  GLU   A CB   1 
ATOM   665  C CG   A GLU   A 1 25  ? 13.635 5.275   13.744  0.30 19.64 ?  25  GLU   A CG   1 
ATOM   666  C CG   B GLU   A 1 25  ? 13.467 4.672   13.484  0.70 21.24 ?  25  GLU   A CG   1 
ATOM   667  C CD   A GLU   A 1 25  ? 14.436 6.272   14.565  0.30 21.09 ?  25  GLU   A CD   1 
ATOM   668  C CD   B GLU   A 1 25  ? 14.012 5.744   14.409  0.70 23.84 ?  25  GLU   A CD   1 
ATOM   669  O OE1  A GLU   A 1 25  ? 14.517 6.103   15.800  0.30 21.40 ?  25  GLU   A OE1  1 
ATOM   670  O OE1  B GLU   A 1 25  ? 13.955 5.547   15.644  0.70 24.69 ?  25  GLU   A OE1  1 
ATOM   671  O OE2  A GLU   A 1 25  ? 15.007 7.212   13.970  0.30 21.81 -1 25  GLU   A OE2  1 
ATOM   672  O OE2  B GLU   A 1 25  ? 14.504 6.772   13.901  0.70 25.25 -1 25  GLU   A OE2  1 
ATOM   673  H H    A GLU   A 1 25  ? 15.359 3.598   12.206  0.30 18.15 ?  25  GLU   A H    1 
ATOM   674  H H    B GLU   A 1 25  ? 15.412 3.112   12.117  0.70 18.81 ?  25  GLU   A H    1 
ATOM   675  H HA   A GLU   A 1 25  ? 15.833 4.112   14.738  0.30 19.22 ?  25  GLU   A HA   1 
ATOM   676  H HA   B GLU   A 1 25  ? 15.673 3.691   14.671  0.70 20.18 ?  25  GLU   A HA   1 
ATOM   677  H HB2  A GLU   A 1 25  ? 13.435 3.260   13.517  0.30 21.37 ?  25  GLU   A HB2  1 
ATOM   678  H HB2  B GLU   A 1 25  ? 13.431 2.636   13.319  0.70 21.92 ?  25  GLU   A HB2  1 
ATOM   679  H HB3  A GLU   A 1 25  ? 13.518 3.705   15.039  0.30 21.37 ?  25  GLU   A HB3  1 
ATOM   680  H HB3  B GLU   A 1 25  ? 13.386 3.135   14.826  0.70 21.92 ?  25  GLU   A HB3  1 
ATOM   681  H HG2  A GLU   A 1 25  ? 13.896 5.394   12.820  0.30 23.57 ?  25  GLU   A HG2  1 
ATOM   682  H HG2  B GLU   A 1 25  ? 13.855 4.807   12.604  0.70 25.48 ?  25  GLU   A HG2  1 
ATOM   683  H HG3  A GLU   A 1 25  ? 12.690 5.472   13.853  0.30 23.57 ?  25  GLU   A HG3  1 
ATOM   684  H HG3  B GLU   A 1 25  ? 12.504 4.769   13.440  0.70 25.48 ?  25  GLU   A HG3  1 
ATOM   685  N N    A GLU   A 1 26  ? 15.574 1.032   14.014  0.30 14.94 ?  26  GLU   A N    1 
ATOM   686  N N    B GLU   A 1 26  ? 15.610 0.583   13.959  0.70 15.66 ?  26  GLU   A N    1 
ATOM   687  C CA   A GLU   A 1 26  ? 15.894 -0.291  14.540  0.30 15.30 ?  26  GLU   A CA   1 
ATOM   688  C CA   B GLU   A 1 26  ? 16.004 -0.713  14.505  0.70 15.46 ?  26  GLU   A CA   1 
ATOM   689  C C    A GLU   A 1 26  ? 17.317 -0.326  15.078  0.30 15.14 ?  26  GLU   A C    1 
ATOM   690  C C    B GLU   A 1 26  ? 17.426 -0.662  15.045  0.70 14.53 ?  26  GLU   A C    1 
ATOM   691  O O    A GLU   A 1 26  ? 17.567 -0.826  16.181  0.30 15.07 ?  26  GLU   A O    1 
ATOM   692  O O    B GLU   A 1 26  ? 17.708 -1.191  16.127  0.70 15.39 ?  26  GLU   A O    1 
ATOM   693  C CB   A GLU   A 1 26  ? 15.719 -1.344  13.444  0.30 16.04 ?  26  GLU   A CB   1 
ATOM   694  C CB   B GLU   A 1 26  ? 15.881 -1.806  13.438  0.70 16.46 ?  26  GLU   A CB   1 
ATOM   695  C CG   A GLU   A 1 26  ? 14.295 -1.807  13.240  0.30 17.34 ?  26  GLU   A CG   1 
ATOM   696  C CG   B GLU   A 1 26  ? 14.453 -2.150  13.050  0.70 17.91 ?  26  GLU   A CG   1 
ATOM   697  C CD   A GLU   A 1 26  ? 13.793 -2.660  14.387  0.30 18.46 ?  26  GLU   A CD   1 
ATOM   698  C CD   B GLU   A 1 26  ? 13.680 -2.804  14.179  0.70 19.04 ?  26  GLU   A CD   1 
ATOM   699  O OE1  A GLU   A 1 26  ? 14.308 -3.783  14.572  0.30 18.89 ?  26  GLU   A OE1  1 
ATOM   700  O OE1  B GLU   A 1 26  ? 14.093 -3.891  14.649  0.70 19.73 ?  26  GLU   A OE1  1 
ATOM   701  O OE2  A GLU   A 1 26  ? 12.892 -2.195  15.113  0.30 19.03 -1 26  GLU   A OE2  1 
ATOM   702  O OE2  B GLU   A 1 26  ? 12.654 -2.227  14.592  0.70 19.24 -1 26  GLU   A OE2  1 
ATOM   703  H H    A GLU   A 1 26  ? 15.386 1.052   13.175  0.30 17.93 ?  26  GLU   A H    1 
ATOM   704  H H    B GLU   A 1 26  ? 15.406 0.568   13.123  0.70 18.79 ?  26  GLU   A H    1 
ATOM   705  H HA   A GLU   A 1 26  ? 15.290 -0.502  15.266  0.30 18.37 ?  26  GLU   A HA   1 
ATOM   706  H HA   B GLU   A 1 26  ? 15.419 -0.948  15.238  0.70 18.55 ?  26  GLU   A HA   1 
ATOM   707  H HB2  A GLU   A 1 26  ? 16.027 -0.973  12.603  0.30 19.24 ?  26  GLU   A HB2  1 
ATOM   708  H HB2  B GLU   A 1 26  ? 16.341 -1.519  12.634  0.70 19.75 ?  26  GLU   A HB2  1 
ATOM   709  H HB3  A GLU   A 1 26  ? 16.249 -2.122  13.673  0.30 19.24 ?  26  GLU   A HB3  1 
ATOM   710  H HB3  B GLU   A 1 26  ? 16.294 -2.624  13.771  0.70 19.75 ?  26  GLU   A HB3  1 
ATOM   711  H HG2  A GLU   A 1 26  ? 13.722 -1.030  13.175  0.30 20.81 ?  26  GLU   A HG2  1 
ATOM   712  H HG2  B GLU   A 1 26  ? 13.992 -1.334  12.798  0.70 21.49 ?  26  GLU   A HG2  1 
ATOM   713  H HG3  A GLU   A 1 26  ? 14.247 -2.326  12.420  0.30 20.81 ?  26  GLU   A HG3  1 
ATOM   714  H HG3  B GLU   A 1 26  ? 14.465 -2.767  12.301  0.70 21.49 ?  26  GLU   A HG3  1 
ATOM   715  N N    A ALA   A 1 27  ? 18.266 0.218   14.312  0.30 15.52 ?  27  ALA   A N    1 
ATOM   716  N N    B ALA   A 1 27  ? 18.336 -0.023  14.308  0.70 14.02 ?  27  ALA   A N    1 
ATOM   717  C CA   A ALA   A 1 27  ? 19.664 0.159   14.719  0.30 16.36 ?  27  ALA   A CA   1 
ATOM   718  C CA   B ALA   A 1 27  ? 19.715 0.064   14.771  0.70 14.26 ?  27  ALA   A CA   1 
ATOM   719  C C    A ALA   A 1 27  ? 19.896 0.940   16.006  0.30 17.62 ?  27  ALA   A C    1 
ATOM   720  C C    B ALA   A 1 27  ? 19.814 0.895   16.044  0.70 15.33 ?  27  ALA   A C    1 
ATOM   721  O O    A ALA   A 1 27  ? 20.585 0.463   16.915  0.30 17.74 ?  27  ALA   A O    1 
ATOM   722  O O    B ALA   A 1 27  ? 20.488 0.497   17.001  0.70 15.91 ?  27  ALA   A O    1 
ATOM   723  C CB   A ALA   A 1 27  ? 20.560 0.683   13.595  0.30 16.14 ?  27  ALA   A CB   1 
ATOM   724  C CB   B ALA   A 1 27  ? 20.612 0.632   13.668  0.70 13.85 ?  27  ALA   A CB   1 
ATOM   725  H H    A ALA   A 1 27  ? 18.122 0.631   13.569  0.30 18.62 ?  27  ALA   A H    1 
ATOM   726  H H    B ALA   A 1 27  ? 18.183 0.356   13.552  0.70 16.83 ?  27  ALA   A H    1 
ATOM   727  H HA   A ALA   A 1 27  ? 19.903 -0.764  14.881  0.30 19.63 ?  27  ALA   A HA   1 
ATOM   728  H HA   B ALA   A 1 27  ? 20.036 -0.827  14.976  0.70 17.11 ?  27  ALA   A HA   1 
ATOM   729  H HB1  A ALA   A 1 27  ? 21.486 0.636   13.881  0.30 19.37 ?  27  ALA   A HB1  1 
ATOM   730  H HB1  B ALA   A 1 27  ? 21.526 0.686   13.995  0.70 16.61 ?  27  ALA   A HB1  1 
ATOM   731  H HB2  A ALA   A 1 27  ? 20.431 0.133   12.804  0.30 19.37 ?  27  ALA   A HB2  1 
ATOM   732  H HB2  B ALA   A 1 27  ? 20.576 0.044   12.895  0.70 16.61 ?  27  ALA   A HB2  1 
ATOM   733  H HB3  A ALA   A 1 27  ? 20.321 1.603   13.399  0.30 19.37 ?  27  ALA   A HB3  1 
ATOM   734  H HB3  B ALA   A 1 27  ? 20.298 1.516   13.423  0.70 16.61 ?  27  ALA   A HB3  1 
ATOM   735  N N    A LYS   A 1 28  ? 19.322 2.142   16.106  0.30 19.14 ?  28  LYS   A N    1 
ATOM   736  N N    B LYS   A 1 28  ? 19.133 2.045   16.089  0.70 16.96 ?  28  LYS   A N    1 
ATOM   737  C CA   A LYS   A 1 28  ? 19.506 2.945   17.311  0.30 21.00 ?  28  LYS   A CA   1 
ATOM   738  C CA   B LYS   A 1 28  ? 19.165 2.867   17.295  0.70 19.61 ?  28  LYS   A CA   1 
ATOM   739  C C    A LYS   A 1 28  ? 18.937 2.252   18.541  0.30 21.88 ?  28  LYS   A C    1 
ATOM   740  C C    B LYS   A 1 28  ? 18.632 2.100   18.496  0.70 21.11 ?  28  LYS   A C    1 
ATOM   741  O O    A LYS   A 1 28  ? 19.455 2.434   19.649  0.30 22.05 ?  28  LYS   A O    1 
ATOM   742  O O    B LYS   A 1 28  ? 19.147 2.241   19.612  0.70 22.37 ?  28  LYS   A O    1 
ATOM   743  C CB   A LYS   A 1 28  ? 18.877 4.328   17.130  0.30 22.15 ?  28  LYS   A CB   1 
ATOM   744  C CB   B LYS   A 1 28  ? 18.358 4.149   17.088  0.70 20.75 ?  28  LYS   A CB   1 
ATOM   745  C CG   A LYS   A 1 28  ? 19.678 5.255   16.227  0.30 23.05 ?  28  LYS   A CG   1 
ATOM   746  C CG   B LYS   A 1 28  ? 18.978 5.127   16.110  0.70 22.32 ?  28  LYS   A CG   1 
ATOM   747  C CD   A LYS   A 1 28  ? 19.151 6.682   16.260  0.30 24.13 ?  28  LYS   A CD   1 
ATOM   748  C CD   B LYS   A 1 28  ? 18.283 6.474   16.190  0.70 24.90 ?  28  LYS   A CD   1 
ATOM   749  C CE   A LYS   A 1 28  ? 17.800 6.801   15.574  0.30 24.91 ?  28  LYS   A CE   1 
ATOM   750  C CE   B LYS   A 1 28  ? 18.077 7.075   14.814  0.70 27.16 ?  28  LYS   A CE   1 
ATOM   751  N NZ   A LYS   A 1 28  ? 17.342 8.217   15.506  0.30 25.39 ?  28  LYS   A NZ   1 
ATOM   752  N NZ   B LYS   A 1 28  ? 17.522 8.455   14.869  0.70 28.40 ?  28  LYS   A NZ   1 
ATOM   753  H H    A LYS   A 1 28  ? 18.833 2.506   15.501  0.30 22.97 ?  28  LYS   A H    1 
ATOM   754  H H    B LYS   A 1 28  ? 18.652 2.359   15.451  0.70 20.35 ?  28  LYS   A H    1 
ATOM   755  H HA   A LYS   A 1 28  ? 20.454 3.071   17.461  0.30 25.19 ?  28  LYS   A HA   1 
ATOM   756  H HA   B LYS   A 1 28  ? 20.077 3.116   17.490  0.70 23.53 ?  28  LYS   A HA   1 
ATOM   757  H HB2  A LYS   A 1 28  ? 17.997 4.224   16.738  0.30 26.58 ?  28  LYS   A HB2  1 
ATOM   758  H HB2  B LYS   A 1 28  ? 17.479 3.916   16.751  0.70 24.90 ?  28  LYS   A HB2  1 
ATOM   759  H HB3  A LYS   A 1 28  ? 18.802 4.755   17.997  0.30 26.58 ?  28  LYS   A HB3  1 
ATOM   760  H HB3  B LYS   A 1 28  ? 18.271 4.606   17.939  0.70 24.90 ?  28  LYS   A HB3  1 
ATOM   761  H HG2  A LYS   A 1 28  ? 20.602 5.268   16.523  0.30 27.67 ?  28  LYS   A HG2  1 
ATOM   762  H HG2  B LYS   A 1 28  ? 19.914 5.249   16.328  0.70 26.78 ?  28  LYS   A HG2  1 
ATOM   763  H HG3  A LYS   A 1 28  ? 19.624 4.935   15.313  0.30 27.67 ?  28  LYS   A HG3  1 
ATOM   764  H HG3  B LYS   A 1 28  ? 18.884 4.787   15.206  0.70 26.78 ?  28  LYS   A HG3  1 
ATOM   765  H HD2  A LYS   A 1 28  ? 19.048 6.964   17.183  0.30 28.96 ?  28  LYS   A HD2  1 
ATOM   766  H HD2  B LYS   A 1 28  ? 17.414 6.363   16.608  0.70 29.88 ?  28  LYS   A HD2  1 
ATOM   767  H HD3  A LYS   A 1 28  ? 19.776 7.265   15.800  0.30 28.96 ?  28  LYS   A HD3  1 
ATOM   768  H HD3  B LYS   A 1 28  ? 18.829 7.085   16.710  0.70 29.88 ?  28  LYS   A HD3  1 
ATOM   769  H HE2  A LYS   A 1 28  ? 17.871 6.461   14.668  0.30 29.89 ?  28  LYS   A HE2  1 
ATOM   770  H HE2  B LYS   A 1 28  ? 18.925 7.101   14.344  0.70 32.60 ?  28  LYS   A HE2  1 
ATOM   771  H HE3  A LYS   A 1 28  ? 17.142 6.293   16.073  0.30 29.89 ?  28  LYS   A HE3  1 
ATOM   772  H HE3  B LYS   A 1 28  ? 17.442 6.522   14.333  0.70 32.60 ?  28  LYS   A HE3  1 
ATOM   773  H HZ1  A LYS   A 1 28  ? 16.552 8.263   15.101  0.30 30.46 ?  28  LYS   A HZ1  1 
ATOM   774  H HZ1  B LYS   A 1 28  ? 17.415 8.773   14.045  0.70 34.09 ?  28  LYS   A HZ1  1 
ATOM   775  H HZ2  A LYS   A 1 28  ? 17.267 8.553   16.327  0.30 30.46 ?  28  LYS   A HZ2  1 
ATOM   776  H HZ2  B LYS   A 1 28  ? 16.733 8.450   15.281  0.70 34.09 ?  28  LYS   A HZ2  1 
ATOM   777  H HZ3  A LYS   A 1 28  ? 17.930 8.706   15.048  0.30 30.46 ?  28  LYS   A HZ3  1 
ATOM   778  H HZ3  B LYS   A 1 28  ? 18.078 8.988   15.315  0.70 34.09 ?  28  LYS   A HZ3  1 
ATOM   779  N N    A LYS   A 1 29  ? 17.884 1.452   18.370  0.30 22.95 ?  29  LYS   A N    1 
ATOM   780  N N    B LYS   A 1 29  ? 17.601 1.280   18.286  0.70 21.98 ?  29  LYS   A N    1 
ATOM   781  C CA   A LYS   A 1 29  ? 17.288 0.743   19.498  0.30 24.36 ?  29  LYS   A CA   1 
ATOM   782  C CA   B LYS   A 1 29  ? 16.980 0.544   19.384  0.70 24.02 ?  29  LYS   A CA   1 
ATOM   783  C C    A LYS   A 1 29  ? 18.106 -0.488  19.875  0.30 23.85 ?  29  LYS   A C    1 
ATOM   784  C C    B LYS   A 1 29  ? 17.845 -0.631  19.829  0.70 23.42 ?  29  LYS   A C    1 
ATOM   785  O O    A LYS   A 1 29  ? 18.490 -0.658  21.037  0.30 24.08 ?  29  LYS   A O    1 
ATOM   786  O O    B LYS   A 1 29  ? 18.052 -0.841  21.031  0.70 24.28 ?  29  LYS   A O    1 
ATOM   787  C CB   A LYS   A 1 29  ? 15.852 0.342   19.150  0.30 26.16 ?  29  LYS   A CB   1 
ATOM   788  C CB   B LYS   A 1 29  ? 15.593 0.054   18.952  0.70 26.70 ?  29  LYS   A CB   1 
ATOM   789  C CG   A LYS   A 1 29  ? 15.102 -0.362  20.270  0.30 28.04 ?  29  LYS   A CG   1 
ATOM   790  C CG   B LYS   A 1 29  ? 14.853 -0.781  19.991  0.70 30.05 ?  29  LYS   A CG   1 
ATOM   791  C CD   A LYS   A 1 29  ? 14.712 0.608   21.371  0.30 29.82 ?  29  LYS   A CD   1 
ATOM   792  C CD   B LYS   A 1 29  ? 14.419 0.063   21.177  0.70 33.13 ?  29  LYS   A CD   1 
ATOM   793  C CE   A LYS   A 1 29  ? 13.842 -0.066  22.418  0.30 31.02 ?  29  LYS   A CE   1 
ATOM   794  C CE   B LYS   A 1 29  ? 13.634 -0.760  22.187  0.70 35.31 ?  29  LYS   A CE   1 
ATOM   795  N NZ   A LYS   A 1 29  ? 13.356 0.898   23.442  0.30 31.68 ?  29  LYS   A NZ   1 
ATOM   796  N NZ   B LYS   A 1 29  ? 13.230 0.053   23.367  0.70 36.71 ?  29  LYS   A NZ   1 
ATOM   797  H H    A LYS   A 1 29  ? 17.498 1.305   17.616  0.30 27.54 ?  29  LYS   A H    1 
ATOM   798  H H    B LYS   A 1 29  ? 17.241 1.128   17.517  0.70 26.37 ?  29  LYS   A H    1 
ATOM   799  H HA   A LYS   A 1 29  ? 17.257 1.334   20.266  0.30 29.23 ?  29  LYS   A HA   1 
ATOM   800  H HA   B LYS   A 1 29  ? 16.861 1.135   20.141  0.70 28.83 ?  29  LYS   A HA   1 
ATOM   801  H HB2  A LYS   A 1 29  ? 15.352 1.142   18.921  0.30 31.39 ?  29  LYS   A HB2  1 
ATOM   802  H HB2  B LYS   A 1 29  ? 15.036 0.825   18.752  0.70 32.04 ?  29  LYS   A HB2  1 
ATOM   803  H HB3  A LYS   A 1 29  ? 15.873 -0.258  18.388  0.30 31.39 ?  29  LYS   A HB3  1 
ATOM   804  H HB3  B LYS   A 1 29  ? 15.686 -0.491  18.154  0.70 32.04 ?  29  LYS   A HB3  1 
ATOM   805  H HG2  A LYS   A 1 29  ? 14.291 -0.754  19.912  0.30 33.64 ?  29  LYS   A HG2  1 
ATOM   806  H HG2  B LYS   A 1 29  ? 14.058 -1.161  19.585  0.70 36.06 ?  29  LYS   A HG2  1 
ATOM   807  H HG3  A LYS   A 1 29  ? 15.662 -1.054  20.657  0.30 33.64 ?  29  LYS   A HG3  1 
ATOM   808  H HG3  B LYS   A 1 29  ? 15.430 -1.491  20.314  0.70 36.06 ?  29  LYS   A HG3  1 
ATOM   809  H HD2  A LYS   A 1 29  ? 15.514 0.938   21.806  0.30 35.78 ?  29  LYS   A HD2  1 
ATOM   810  H HD2  B LYS   A 1 29  ? 15.204 0.421   21.620  0.70 39.76 ?  29  LYS   A HD2  1 
ATOM   811  H HD3  A LYS   A 1 29  ? 14.212 1.345   20.985  0.30 35.78 ?  29  LYS   A HD3  1 
ATOM   812  H HD3  B LYS   A 1 29  ? 13.851 0.785   20.864  0.70 39.76 ?  29  LYS   A HD3  1 
ATOM   813  H HE2  A LYS   A 1 29  ? 13.070 -0.462  21.983  0.30 37.23 ?  29  LYS   A HE2  1 
ATOM   814  H HE2  B LYS   A 1 29  ? 12.830 -1.101  21.764  0.70 42.37 ?  29  LYS   A HE2  1 
ATOM   815  H HE3  A LYS   A 1 29  ? 14.359 -0.753  22.868  0.30 37.23 ?  29  LYS   A HE3  1 
ATOM   816  H HE3  B LYS   A 1 29  ? 14.186 -1.494  22.498  0.70 42.37 ?  29  LYS   A HE3  1 
ATOM   817  H HZ1  A LYS   A 1 29  ? 12.850 0.475   24.040  0.30 38.02 ?  29  LYS   A HZ1  1 
ATOM   818  H HZ1  B LYS   A 1 29  ? 12.773 -0.451  23.941  0.70 44.05 ?  29  LYS   A HZ1  1 
ATOM   819  H HZ2  A LYS   A 1 29  ? 14.047 1.271   23.860  0.30 38.02 ?  29  LYS   A HZ2  1 
ATOM   820  H HZ2  B LYS   A 1 29  ? 13.952 0.375   23.776  0.70 44.05 ?  29  LYS   A HZ2  1 
ATOM   821  H HZ3  A LYS   A 1 29  ? 12.873 1.536   23.054  0.30 38.02 ?  29  LYS   A HZ3  1 
ATOM   822  H HZ3  B LYS   A 1 29  ? 12.717 0.733   23.107  0.70 44.05 ?  29  LYS   A HZ3  1 
ATOM   823  N N    A VAL   A 1 30  ? 18.384 -1.355  18.900  0.30 23.19 ?  30  VAL   A N    1 
ATOM   824  N N    B VAL   A 1 30  ? 18.346 -1.412  18.875  0.70 22.22 ?  30  VAL   A N    1 
ATOM   825  C CA   A VAL   A 1 30  ? 19.021 -2.636  19.191  0.30 22.66 ?  30  VAL   A CA   1 
ATOM   826  C CA   B VAL   A 1 30  ? 19.025 -2.663  19.197  0.70 21.79 ?  30  VAL   A CA   1 
ATOM   827  C C    A VAL   A 1 30  ? 20.525 -2.483  19.398  0.30 21.55 ?  30  VAL   A C    1 
ATOM   828  C C    B VAL   A 1 30  ? 20.531 -2.489  19.399  0.70 20.74 ?  30  VAL   A C    1 
ATOM   829  O O    A VAL   A 1 30  ? 21.120 -3.209  20.204  0.30 21.80 ?  30  VAL   A O    1 
ATOM   830  O O    B VAL   A 1 30  ? 21.130 -3.210  20.204  0.70 21.14 ?  30  VAL   A O    1 
ATOM   831  C CB   A VAL   A 1 30  ? 18.704 -3.638  18.066  0.30 23.27 ?  30  VAL   A CB   1 
ATOM   832  C CB   B VAL   A 1 30  ? 18.727 -3.708  18.107  0.70 23.08 ?  30  VAL   A CB   1 
ATOM   833  C CG1  A VAL   A 1 30  ? 19.422 -4.958  18.303  0.30 23.60 ?  30  VAL   A CG1  1 
ATOM   834  C CG1  B VAL   A 1 30  ? 19.606 -4.938  18.282  0.70 23.65 ?  30  VAL   A CG1  1 
ATOM   835  C CG2  A VAL   A 1 30  ? 17.202 -3.855  17.956  0.30 23.48 ?  30  VAL   A CG2  1 
ATOM   836  C CG2  B VAL   A 1 30  ? 17.260 -4.097  18.132  0.70 23.84 ?  30  VAL   A CG2  1 
ATOM   837  H H    A VAL   A 1 30  ? 18.213 -1.224  18.069  0.30 27.83 ?  30  VAL   A H    1 
ATOM   838  H H    B VAL   A 1 30  ? 18.297 -1.244  18.031  0.70 26.66 ?  30  VAL   A H    1 
ATOM   839  H HA   A VAL   A 1 30  ? 18.641 -2.988  20.009  0.30 27.19 ?  30  VAL   A HA   1 
ATOM   840  H HA   B VAL   A 1 30  ? 18.654 -3.003  20.025  0.70 26.15 ?  30  VAL   A HA   1 
ATOM   841  H HB   A VAL   A 1 30  ? 19.017 -3.276  17.222  0.30 27.93 ?  30  VAL   A HB   1 
ATOM   842  H HB   B VAL   A 1 30  ? 18.922 -3.326  17.238  0.70 27.70 ?  30  VAL   A HB   1 
ATOM   843  H HG11 A VAL   A 1 30  ? 19.052 -5.628  17.706  0.30 28.32 ?  30  VAL   A HG11 1 
ATOM   844  H HG11 B VAL   A 1 30  ? 19.219 -5.673  17.779  0.70 28.38 ?  30  VAL   A HG11 1 
ATOM   845  H HG12 A VAL   A 1 30  ? 20.368 -4.843  18.121  0.30 28.32 ?  30  VAL   A HG12 1 
ATOM   846  H HG12 B VAL   A 1 30  ? 20.496 -4.745  17.951  0.70 28.38 ?  30  VAL   A HG12 1 
ATOM   847  H HG13 A VAL   A 1 30  ? 19.290 -5.228  19.224  0.30 28.32 ?  30  VAL   A HG13 1 
ATOM   848  H HG13 B VAL   A 1 30  ? 19.642 -5.169  19.224  0.70 28.38 ?  30  VAL   A HG13 1 
ATOM   849  H HG21 A VAL   A 1 30  ? 17.030 -4.533  17.283  0.30 28.18 ?  30  VAL   A HG21 1 
ATOM   850  H HG21 B VAL   A 1 30  ? 17.097 -4.761  17.443  0.70 28.60 ?  30  VAL   A HG21 1 
ATOM   851  H HG22 A VAL   A 1 30  ? 16.862 -4.150  18.816  0.30 28.18 ?  30  VAL   A HG22 1 
ATOM   852  H HG22 B VAL   A 1 30  ? 17.047 -4.469  19.004  0.70 28.60 ?  30  VAL   A HG22 1 
ATOM   853  H HG23 A VAL   A 1 30  ? 16.779 -3.021  17.701  0.30 28.18 ?  30  VAL   A HG23 1 
ATOM   854  H HG23 B VAL   A 1 30  ? 16.721 -3.309  17.968  0.70 28.60 ?  30  VAL   A HG23 1 
ATOM   855  N N    . LYS   A 1 31  ? 21.156 -1.553  18.691  1.00 20.44 ?  31  LYS   A N    1 
ATOM   856  C CA   . LYS   A 1 31  ? 22.609 -1.416  18.663  1.00 21.19 ?  31  LYS   A CA   1 
ATOM   857  C C    . LYS   A 1 31  ? 23.253 -2.760  18.309  1.00 18.53 ?  31  LYS   A C    1 
ATOM   858  O O    . LYS   A 1 31  ? 24.049 -3.300  19.082  1.00 19.41 ?  31  LYS   A O    1 
ATOM   859  C CB   . LYS   A 1 31  ? 23.171 -0.862  19.964  1.00 26.73 ?  31  LYS   A CB   1 
ATOM   860  C CG   . LYS   A 1 31  ? 22.449 0.373   20.481  1.00 33.10 ?  31  LYS   A CG   1 
ATOM   861  C CD   . LYS   A 1 31  ? 23.402 1.535   20.707  1.00 38.02 ?  31  LYS   A CD   1 
ATOM   862  C CE   . LYS   A 1 31  ? 22.804 2.567   21.654  1.00 41.78 ?  31  LYS   A CE   1 
ATOM   863  N NZ   . LYS   A 1 31  ? 21.499 3.105   21.181  1.00 43.42 ?  31  LYS   A NZ   1 
ATOM   864  H H    A LYS   A 1 31  ? 20.751 -0.974  18.201  0.30 24.52 ?  31  LYS   A H    1 
ATOM   865  H H    B LYS   A 1 31  ? 20.749 -0.972  18.204  0.70 24.52 ?  31  LYS   A H    1 
ATOM   866  H HA   . LYS   A 1 31  ? 22.833 -0.787  17.966  1.00 25.43 ?  31  LYS   A HA   1 
ATOM   867  H HB2  . LYS   A 1 31  ? 23.101 -1.551  20.632  1.00 32.08 ?  31  LYS   A HB2  1 
ATOM   868  H HB3  . LYS   A 1 31  ? 24.108 -0.630  19.827  1.00 32.08 ?  31  LYS   A HB3  1 
ATOM   869  H HG2  . LYS   A 1 31  ? 21.785 0.650   19.830  1.00 39.72 ?  31  LYS   A HG2  1 
ATOM   870  H HG3  . LYS   A 1 31  ? 22.022 0.161   21.325  1.00 39.72 ?  31  LYS   A HG3  1 
ATOM   871  H HD2  . LYS   A 1 31  ? 24.225 1.204   21.099  1.00 45.62 ?  31  LYS   A HD2  1 
ATOM   872  H HD3  . LYS   A 1 31  ? 23.585 1.969   19.858  1.00 45.62 ?  31  LYS   A HD3  1 
ATOM   873  H HE2  . LYS   A 1 31  ? 22.661 2.153   22.520  1.00 50.13 ?  31  LYS   A HE2  1 
ATOM   874  H HE3  . LYS   A 1 31  ? 23.421 3.309   21.740  1.00 50.13 ?  31  LYS   A HE3  1 
ATOM   875  H HZ1  . LYS   A 1 31  ? 21.192 3.709   21.760  1.00 52.10 ?  31  LYS   A HZ1  1 
ATOM   876  H HZ2  . LYS   A 1 31  ? 21.599 3.493   20.387  1.00 52.10 ?  31  LYS   A HZ2  1 
ATOM   877  H HZ3  . LYS   A 1 31  ? 20.904 2.447   21.110  1.00 52.10 ?  31  LYS   A HZ3  1 
ATOM   878  N N    . PRO   A 1 32  ? 22.920 -3.317  17.148  1.00 16.45 ?  32  PRO   A N    1 
ATOM   879  C CA   . PRO   A 1 32  ? 23.418 -4.646  16.789  1.00 16.48 ?  32  PRO   A CA   1 
ATOM   880  C C    . PRO   A 1 32  ? 24.920 -4.640  16.582  1.00 16.32 ?  32  PRO   A C    1 
ATOM   881  O O    . PRO   A 1 32  ? 25.549 -3.602  16.370  1.00 16.47 ?  32  PRO   A O    1 
ATOM   882  C CB   . PRO   A 1 32  ? 22.700 -4.936  15.467  1.00 16.95 ?  32  PRO   A CB   1 
ATOM   883  C CG   . PRO   A 1 32  ? 22.504 -3.579  14.863  1.00 15.94 ?  32  PRO   A CG   1 
ATOM   884  C CD   . PRO   A 1 32  ? 22.165 -2.703  16.043  1.00 15.60 ?  32  PRO   A CD   1 
ATOM   885  H HA   . PRO   A 1 32  ? 23.171 -5.303  17.453  1.00 19.77 ?  32  PRO   A HA   1 
ATOM   886  H HB2  . PRO   A 1 32  ? 23.259 -5.489  14.898  1.00 20.34 ?  32  PRO   A HB2  1 
ATOM   887  H HB3  . PRO   A 1 32  ? 21.847 -5.364  15.638  1.00 20.34 ?  32  PRO   A HB3  1 
ATOM   888  H HG2  . PRO   A 1 32  ? 23.324 -3.289  14.435  1.00 19.13 ?  32  PRO   A HG2  1 
ATOM   889  H HG3  . PRO   A 1 32  ? 21.771 -3.608  14.225  1.00 19.13 ?  32  PRO   A HG3  1 
ATOM   890  H HD2  . PRO   A 1 32  ? 22.469 -1.796  15.874  1.00 18.72 ?  32  PRO   A HD2  1 
ATOM   891  H HD3  . PRO   A 1 32  ? 21.212 -2.732  16.213  1.00 18.72 ?  32  PRO   A HD3  1 
ATOM   892  N N    . THR   A 1 33  ? 25.494 -5.839  16.617  1.00 16.49 ?  33  THR   A N    1 
ATOM   893  C CA   . THR   A 1 33  ? 26.904 -5.977  16.283  1.00 16.33 ?  33  THR   A CA   1 
ATOM   894  C C    . THR   A 1 33  ? 27.177 -5.516  14.857  1.00 14.80 ?  33  THR   A C    1 
ATOM   895  O O    . THR   A 1 33  ? 28.198 -4.868  14.593  1.00 15.28 ?  33  THR   A O    1 
ATOM   896  C CB   . THR   A 1 33  ? 27.337 -7.428  16.480  1.00 18.08 ?  33  THR   A CB   1 
ATOM   897  O OG1  . THR   A 1 33  ? 27.025 -7.835  17.815  1.00 19.86 ?  33  THR   A OG1  1 
ATOM   898  C CG2  . THR   A 1 33  ? 28.829 -7.587  16.241  1.00 18.68 ?  33  THR   A CG2  1 
ATOM   899  H H    . THR   A 1 33  ? 25.096 -6.570  16.826  1.00 19.78 ?  33  THR   A H    1 
ATOM   900  H HA   . THR   A 1 33  ? 27.429 -5.426  16.885  1.00 19.60 ?  33  THR   A HA   1 
ATOM   901  H HB   . THR   A 1 33  ? 26.864 -8.000  15.854  1.00 21.70 ?  33  THR   A HB   1 
ATOM   902  H HG1  . THR   A 1 33  ? 27.437 -7.357  18.372  1.00 23.83 ?  33  THR   A HG1  1 
ATOM   903  H HG21 . THR   A 1 33  ? 29.117 -8.473  16.512  1.00 22.42 ?  33  THR   A HG21 1 
ATOM   904  H HG22 . THR   A 1 33  ? 29.030 -7.465  15.301  1.00 22.42 ?  33  THR   A HG22 1 
ATOM   905  H HG23 . THR   A 1 33  ? 29.318 -6.927  16.758  1.00 22.42 ?  33  THR   A HG23 1 
ATOM   906  N N    . VAL   A 1 34  ? 26.278 -5.840  13.925  1.00 13.56 ?  34  VAL   A N    1 
ATOM   907  C CA   . VAL   A 1 34  ? 26.456 -5.500  12.515  1.00 12.35 ?  34  VAL   A CA   1 
ATOM   908  C C    . VAL   A 1 34  ? 25.151 -4.951  11.952  1.00 12.09 ?  34  VAL   A C    1 
ATOM   909  O O    . VAL   A 1 34  ? 24.117 -5.634  11.985  1.00 12.73 ?  34  VAL   A O    1 
ATOM   910  C CB   . VAL   A 1 34  ? 26.901 -6.706  11.667  1.00 12.97 ?  34  VAL   A CB   1 
ATOM   911  C CG1  . VAL   A 1 34  ? 27.077 -6.284  10.213  1.00 13.48 ?  34  VAL   A CG1  1 
ATOM   912  C CG2  . VAL   A 1 34  ? 28.175 -7.335  12.222  1.00 14.40 ?  34  VAL   A CG2  1 
ATOM   913  H H    . VAL   A 1 34  ? 25.543 -6.267  14.092  1.00 16.28 ?  34  VAL   A H    1 
ATOM   914  H HA   . VAL   A 1 34  ? 27.126 -4.804  12.439  1.00 14.82 ?  34  VAL   A HA   1 
ATOM   915  H HB   . VAL   A 1 34  ? 26.200 -7.375  11.697  1.00 15.56 ?  34  VAL   A HB   1 
ATOM   916  H HG11 . VAL   A 1 34  ? 27.577 -6.968  9.745   1.00 16.18 ?  34  VAL   A HG11 1 
ATOM   917  H HG12 . VAL   A 1 34  ? 26.205 -6.172  9.801   1.00 16.18 ?  34  VAL   A HG12 1 
ATOM   918  H HG13 . VAL   A 1 34  ? 27.565 -5.442  10.182  1.00 16.18 ?  34  VAL   A HG13 1 
ATOM   919  H HG21 . VAL   A 1 34  ? 28.438 -8.066  11.645  1.00 17.28 ?  34  VAL   A HG21 1 
ATOM   920  H HG22 . VAL   A 1 34  ? 28.873 -6.663  12.248  1.00 17.28 ?  34  VAL   A HG22 1 
ATOM   921  H HG23 . VAL   A 1 34  ? 27.999 -7.665  13.118  1.00 17.28 ?  34  VAL   A HG23 1 
ATOM   922  N N    . VAL   A 1 35  ? 25.207 -3.742  11.395  1.00 11.37 ?  35  VAL   A N    1 
ATOM   923  C CA   . VAL   A 1 35  ? 24.169 -3.233  10.507  1.00 11.11 ?  35  VAL   A CA   1 
ATOM   924  C C    . VAL   A 1 35  ? 24.716 -3.233  9.086   1.00 10.17 ?  35  VAL   A C    1 
ATOM   925  O O    . VAL   A 1 35  ? 25.858 -2.821  8.848   1.00 10.96 ?  35  VAL   A O    1 
ATOM   926  C CB   . VAL   A 1 35  ? 23.633 -1.843  10.922  1.00 11.56 ?  35  VAL   A CB   1 
ATOM   927  C CG1  . VAL   A 1 35  ? 24.686 -0.744  10.781  1.00 12.42 ?  35  VAL   A CG1  1 
ATOM   928  C CG2  . VAL   A 1 35  ? 22.387 -1.483  10.113  1.00 12.21 ?  35  VAL   A CG2  1 
ATOM   929  H H    . VAL   A 1 35  ? 25.847 -3.181  11.515  1.00 13.64 ?  35  VAL   A H    1 
ATOM   930  H HA   . VAL   A 1 35  ? 23.412 -3.842  10.530  1.00 13.33 ?  35  VAL   A HA   1 
ATOM   931  H HB   . VAL   A 1 35  ? 23.364 -1.868  11.853  1.00 13.88 ?  35  VAL   A HB   1 
ATOM   932  H HG11 . VAL   A 1 35  ? 24.339 0.085   11.158  1.00 14.90 ?  35  VAL   A HG11 1 
ATOM   933  H HG12 . VAL   A 1 35  ? 25.485 -1.010  11.257  1.00 14.90 ?  35  VAL   A HG12 1 
ATOM   934  H HG13 . VAL   A 1 35  ? 24.888 -0.611  9.840   1.00 14.90 ?  35  VAL   A HG13 1 
ATOM   935  H HG21 . VAL   A 1 35  ? 22.037 -0.632  10.423  1.00 14.65 ?  35  VAL   A HG21 1 
ATOM   936  H HG22 . VAL   A 1 35  ? 22.630 -1.414  9.173   1.00 14.65 ?  35  VAL   A HG22 1 
ATOM   937  H HG23 . VAL   A 1 35  ? 21.723 -2.177  10.231  1.00 14.65 ?  35  VAL   A HG23 1 
ATOM   938  N N    . VAL   A 1 36  ? 23.905 -3.699  8.145   1.00 9.95  ?  36  VAL   A N    1 
ATOM   939  C CA   . VAL   A 1 36  ? 24.271 -3.699  6.735   1.00 9.69  ?  36  VAL   A CA   1 
ATOM   940  C C    . VAL   A 1 36  ? 23.800 -2.408  6.079   1.00 9.77  ?  36  VAL   A C    1 
ATOM   941  O O    . VAL   A 1 36  ? 22.641 -1.995  6.240   1.00 10.53 ?  36  VAL   A O    1 
ATOM   942  C CB   . VAL   A 1 36  ? 23.671 -4.910  6.011   1.00 9.84  ?  36  VAL   A CB   1 
ATOM   943  C CG1  . VAL   A 1 36  ? 23.928 -4.827  4.517   1.00 10.36 ?  36  VAL   A CG1  1 
ATOM   944  C CG2  . VAL   A 1 36  ? 24.208 -6.203  6.590   1.00 10.60 ?  36  VAL   A CG2  1 
ATOM   945  H H    . VAL   A 1 36  ? 23.119 -4.030  8.296   1.00 11.94 ?  36  VAL   A H    1 
ATOM   946  H HA   . VAL   A 1 36  ? 25.241 -3.754  6.656   1.00 11.62 ?  36  VAL   A HA   1 
ATOM   947  H HB   . VAL   A 1 36  ? 22.709 -4.903  6.146   1.00 11.80 ?  36  VAL   A HB   1 
ATOM   948  H HG11 . VAL   A 1 36  ? 23.790 -5.705  4.124   1.00 12.44 ?  36  VAL   A HG11 1 
ATOM   949  H HG12 . VAL   A 1 36  ? 23.313 -4.191  4.119   1.00 12.44 ?  36  VAL   A HG12 1 
ATOM   950  H HG13 . VAL   A 1 36  ? 24.844 -4.543  4.368   1.00 12.44 ?  36  VAL   A HG13 1 
ATOM   951  H HG21 . VAL   A 1 36  ? 23.826 -6.953  6.104   1.00 12.72 ?  36  VAL   A HG21 1 
ATOM   952  H HG22 . VAL   A 1 36  ? 25.174 -6.214  6.504   1.00 12.72 ?  36  VAL   A HG22 1 
ATOM   953  H HG23 . VAL   A 1 36  ? 23.960 -6.262  7.528   1.00 12.72 ?  36  VAL   A HG23 1 
ATOM   954  N N    A ASN   A 1 37  ? 24.691 -1.792  5.304   0.30 9.62  ?  37  ASN   A N    1 
ATOM   955  N N    B ASN   A 1 37  ? 24.712 -1.756  5.358   0.70 9.20  ?  37  ASN   A N    1 
ATOM   956  C CA   A ASN   A 1 37  ? 24.358 -0.639  4.486   0.30 9.61  ?  37  ASN   A CA   1 
ATOM   957  C CA   B ASN   A 1 37  ? 24.369 -0.654  4.479   0.70 8.91  ?  37  ASN   A CA   1 
ATOM   958  C C    A ASN   A 1 37  ? 24.181 -1.059  3.032   0.30 9.87  ?  37  ASN   A C    1 
ATOM   959  C C    B ASN   A 1 37  ? 24.248 -1.147  3.044   0.70 8.88  ?  37  ASN   A C    1 
ATOM   960  O O    A ASN   A 1 37  ? 24.918 -1.910  2.522   0.30 10.32 ?  37  ASN   A O    1 
ATOM   961  O O    B ASN   A 1 37  ? 25.070 -1.945  2.572   0.70 9.62  ?  37  ASN   A O    1 
ATOM   962  C CB   A ASN   A 1 37  ? 25.459 0.417   4.566   0.30 9.57  ?  37  ASN   A CB   1 
ATOM   963  C CB   B ASN   A 1 37  ? 25.422 0.449   4.543   0.70 9.12  ?  37  ASN   A CB   1 
ATOM   964  C CG   A ASN   A 1 37  ? 25.108 1.662   3.794   0.30 9.46  ?  37  ASN   A CG   1 
ATOM   965  C CG   B ASN   A 1 37  ? 25.073 1.622   3.663   0.70 9.32  ?  37  ASN   A CG   1 
ATOM   966  O OD1  A ASN   A 1 37  ? 23.933 2.001   3.660   0.30 9.38  ?  37  ASN   A OD1  1 
ATOM   967  O OD1  B ASN   A 1 37  ? 23.896 1.919   3.450   0.70 10.22 ?  37  ASN   A OD1  1 
ATOM   968  N ND2  A ASN   A 1 37  ? 26.119 2.348   3.273   0.30 9.54  ?  37  ASN   A ND2  1 
ATOM   969  N ND2  B ASN   A 1 37  ? 26.096 2.289   3.134   0.70 9.68  ?  37  ASN   A ND2  1 
ATOM   970  H H    A ASN   A 1 37  ? 25.519 -2.030  5.235   0.30 11.55 ?  37  ASN   A H    1 
ATOM   971  H H    B ASN   A 1 37  ? 25.560 -1.938  5.367   0.70 11.05 ?  37  ASN   A H    1 
ATOM   972  H HA   A ASN   A 1 37  ? 23.533 -0.240  4.801   0.30 11.53 ?  37  ASN   A HA   1 
ATOM   973  H HA   B ASN   A 1 37  ? 23.522 -0.276  4.757   0.70 10.69 ?  37  ASN   A HA   1 
ATOM   974  H HB2  A ASN   A 1 37  ? 25.592 0.672   5.495   0.30 11.49 ?  37  ASN   A HB2  1 
ATOM   975  H HB2  B ASN   A 1 37  ? 25.492 0.776   5.457   0.70 10.94 ?  37  ASN   A HB2  1 
ATOM   976  H HB3  A ASN   A 1 37  ? 26.283 0.055   4.202   0.30 11.49 ?  37  ASN   A HB3  1 
ATOM   977  H HB3  B ASN   A 1 37  ? 26.278 0.097   4.253   0.70 10.94 ?  37  ASN   A HB3  1 
ATOM   978  H HD21 A ASN   A 1 37  ? 25.968 3.062   2.824   0.30 11.45 ?  37  ASN   A HD21 1 
ATOM   979  H HD21 B ASN   A 1 37  ? 25.951 2.960   2.622   0.70 11.62 ?  37  ASN   A HD21 1 
ATOM   980  H HD22 A ASN   A 1 37  ? 26.926 2.081   3.385   0.30 11.45 ?  37  ASN   A HD22 1 
ATOM   981  H HD22 B ASN   A 1 37  ? 26.901 2.050   3.308   0.70 11.62 ?  37  ASN   A HD22 1 
ATOM   982  N N    A ALA   A 1 38  ? 23.194 -0.451  2.371   0.30 9.99  ?  38  ALA   A N    1 
ATOM   983  N N    B ALA   A 1 38  ? 23.210 -0.665  2.360   0.70 9.33  ?  38  ALA   A N    1 
ATOM   984  C CA   A ALA   A 1 38  ? 22.994 -0.601  0.929   0.30 9.31  ?  38  ALA   A CA   1 
ATOM   985  C CA   B ALA   A 1 38  ? 23.020 -0.882  0.929   0.70 9.80  ?  38  ALA   A CA   1 
ATOM   986  C C    A ALA   A 1 38  ? 23.936 0.370   0.219   0.30 9.14  ?  38  ALA   A C    1 
ATOM   987  C C    B ALA   A 1 38  ? 23.824 0.177   0.176   0.70 10.10 ?  38  ALA   A C    1 
ATOM   988  O O    A ALA   A 1 38  ? 23.566 1.479   -0.174  0.30 9.29  ?  38  ALA   A O    1 
ATOM   989  O O    B ALA   A 1 38  ? 23.323 1.235   -0.209  0.70 10.66 ?  38  ALA   A O    1 
ATOM   990  C CB   A ALA   A 1 38  ? 21.536 -0.341  0.568   0.30 9.48  ?  38  ALA   A CB   1 
ATOM   991  C CB   B ALA   A 1 38  ? 21.540 -0.820  0.587   0.70 10.63 ?  38  ALA   A CB   1 
ATOM   992  H H    A ALA   A 1 38  ? 22.616 0.067   2.746   0.30 11.99 ?  38  ALA   A H    1 
ATOM   993  H H    B ALA   A 1 38  ? 22.594 -0.183  2.722   0.70 11.19 ?  38  ALA   A H    1 
ATOM   994  H HA   A ALA   A 1 38  ? 23.224 -1.500  0.663   0.30 11.18 ?  38  ALA   A HA   1 
ATOM   995  H HA   B ALA   A 1 38  ? 23.361 -1.756  0.690   0.70 11.76 ?  38  ALA   A HA   1 
ATOM   996  H HB1  A ALA   A 1 38  ? 21.421 -0.460  -0.388  0.30 11.38 ?  38  ALA   A HB1  1 
ATOM   997  H HB1  B ALA   A 1 38  ? 21.432 -0.952  -0.366  0.70 12.75 ?  38  ALA   A HB1  1 
ATOM   998  H HB2  A ALA   A 1 38  ? 20.976 -0.970  1.050   0.30 11.38 ?  38  ALA   A HB2  1 
ATOM   999  H HB2  B ALA   A 1 38  ? 21.071 -1.518  1.074   0.70 12.75 ?  38  ALA   A HB2  1 
ATOM   1000 H HB3  A ALA   A 1 38  ? 21.303 0.568   0.818   0.30 11.38 ?  38  ALA   A HB3  1 
ATOM   1001 H HB3  B ALA   A 1 38  ? 21.190 0.049   0.843   0.70 12.75 ?  38  ALA   A HB3  1 
ATOM   1002 N N    A ALA   A 1 39  ? 25.187 -0.056  0.061   0.30 8.97  ?  39  ALA   A N    1 
ATOM   1003 N N    B ALA   A 1 39  ? 25.107 -0.118  -0.029  0.70 10.31 ?  39  ALA   A N    1 
ATOM   1004 C CA   A ALA   A 1 39  ? 26.261 0.809   -0.407  0.30 9.07  ?  39  ALA   A CA   1 
ATOM   1005 C CA   B ALA   A 1 39  ? 26.085 0.836   -0.525  0.70 10.09 ?  39  ALA   A CA   1 
ATOM   1006 C C    A ALA   A 1 39  ? 26.401 0.770   -1.926  0.30 9.43  ?  39  ALA   A C    1 
ATOM   1007 C C    B ALA   A 1 39  ? 26.196 0.787   -2.046  0.70 9.65  ?  39  ALA   A C    1 
ATOM   1008 O O    A ALA   A 1 39  ? 25.905 -0.137  -2.601  0.30 9.50  ?  39  ALA   A O    1 
ATOM   1009 O O    B ALA   A 1 39  ? 25.709 -0.135  -2.708  0.70 10.57 ?  39  ALA   A O    1 
ATOM   1010 C CB   A ALA   A 1 39  ? 27.588 0.397   0.241   0.30 9.44  ?  39  ALA   A CB   1 
ATOM   1011 C CB   B ALA   A 1 39  ? 27.448 0.544   0.101   0.70 10.98 ?  39  ALA   A CB   1 
ATOM   1012 H H    A ALA   A 1 39  ? 25.448 -0.861  0.228   0.30 10.77 ?  39  ALA   A H    1 
ATOM   1013 H H    B ALA   A 1 39  ? 25.441 -0.896  0.125   0.70 12.37 ?  39  ALA   A H    1 
ATOM   1014 H HA   A ALA   A 1 39  ? 26.076 1.723   -0.147  0.30 10.88 ?  39  ALA   A HA   1 
ATOM   1015 H HA   B ALA   A 1 39  ? 25.816 1.732   -0.264  0.70 12.11 ?  39  ALA   A HA   1 
ATOM   1016 H HB1  A ALA   A 1 39  ? 28.295 0.983   -0.079  0.30 11.33 ?  39  ALA   A HB1  1 
ATOM   1017 H HB1  B ALA   A 1 39  ? 28.093 1.187   -0.236  0.70 13.18 ?  39  ALA   A HB1  1 
ATOM   1018 H HB2  A ALA   A 1 39  ? 27.508 0.482   1.207   0.30 11.33 ?  39  ALA   A HB2  1 
ATOM   1019 H HB2  B ALA   A 1 39  ? 27.379 0.627   1.068   0.70 13.18 ?  39  ALA   A HB2  1 
ATOM   1020 H HB3  A ALA   A 1 39  ? 27.788 -0.520  0.006   0.30 11.33 ?  39  ALA   A HB3  1 
ATOM   1021 H HB3  B ALA   A 1 39  ? 27.720 -0.355  -0.134  0.70 13.18 ?  39  ALA   A HB3  1 
ATOM   1022 N N    A ASN   A 1 40  ? 27.099 1.777   -2.457  0.30 9.70  ?  40  ASN   A N    1 
ATOM   1023 N N    B ASN   A 1 40  ? 26.866 1.802   -2.596  0.70 9.87  ?  40  ASN   A N    1 
ATOM   1024 C CA   A ASN   A 1 40  ? 27.631 1.744   -3.813  0.30 9.77  ?  40  ASN   A CA   1 
ATOM   1025 C CA   B ASN   A 1 40  ? 27.407 1.755   -3.947  0.70 10.50 ?  40  ASN   A CA   1 
ATOM   1026 C C    A ASN   A 1 40  ? 29.150 1.611   -3.768  0.30 9.52  ?  40  ASN   A C    1 
ATOM   1027 C C    B ASN   A 1 40  ? 28.931 1.625   -3.875  0.70 10.19 ?  40  ASN   A C    1 
ATOM   1028 O O    A ASN   A 1 40  ? 29.775 1.740   -2.711  0.30 9.61  ?  40  ASN   A O    1 
ATOM   1029 O O    B ASN   A 1 40  ? 29.528 1.698   -2.797  0.70 9.99  ?  40  ASN   A O    1 
ATOM   1030 C CB   A ASN   A 1 40  ? 27.174 2.951   -4.651  0.30 10.41 ?  40  ASN   A CB   1 
ATOM   1031 C CB   B ASN   A 1 40  ? 26.948 2.959   -4.787  0.70 11.12 ?  40  ASN   A CB   1 
ATOM   1032 C CG   A ASN   A 1 40  ? 27.582 4.285   -4.058  0.30 10.99 ?  40  ASN   A CG   1 
ATOM   1033 C CG   B ASN   A 1 40  ? 27.293 4.280   -4.151  0.70 11.75 ?  40  ASN   A CG   1 
ATOM   1034 O OD1  A ASN   A 1 40  ? 28.754 4.516   -3.761  0.30 10.85 ?  40  ASN   A OD1  1 
ATOM   1035 O OD1  B ASN   A 1 40  ? 28.456 4.552   -3.862  0.70 13.01 ?  40  ASN   A OD1  1 
ATOM   1036 N ND2  A ASN   A 1 40  ? 26.609 5.184   -3.903  0.30 11.60 ?  40  ASN   A ND2  1 
ATOM   1037 N ND2  B ASN   A 1 40  ? 26.284 5.127   -3.954  0.70 12.15 ?  40  ASN   A ND2  1 
ATOM   1038 H H    A ASN   A 1 40  ? 27.285 2.507   -2.035  0.30 11.64 ?  40  ASN   A H    1 
ATOM   1039 H H    B ASN   A 1 40  ? 27.018 2.543   -2.190  0.70 11.84 ?  40  ASN   A H    1 
ATOM   1040 H HA   A ASN   A 1 40  ? 27.297 0.953   -4.249  0.30 11.73 ?  40  ASN   A HA   1 
ATOM   1041 H HA   B ASN   A 1 40  ? 27.060 0.955   -4.382  0.70 12.60 ?  40  ASN   A HA   1 
ATOM   1042 H HB2  A ASN   A 1 40  ? 27.570 2.885   -5.538  0.30 12.49 ?  40  ASN   A HB2  1 
ATOM   1043 H HB2  B ASN   A 1 40  ? 27.378 2.918   -5.657  0.70 13.35 ?  40  ASN   A HB2  1 
ATOM   1044 H HB3  A ASN   A 1 40  ? 26.211 2.936   -4.718  0.30 12.49 ?  40  ASN   A HB3  1 
ATOM   1045 H HB3  B ASN   A 1 40  ? 25.981 2.922   -4.899  0.70 13.35 ?  40  ASN   A HB3  1 
ATOM   1046 H HD21 A ASN   A 1 40  ? 26.785 5.962   -3.577  0.30 13.91 ?  40  ASN   A HD21 1 
ATOM   1047 H HD21 B ASN   A 1 40  ? 26.432 5.895   -3.598  0.70 14.58 ?  40  ASN   A HD21 1 
ATOM   1048 H HD22 A ASN   A 1 40  ? 25.801 4.985   -4.120  0.30 13.91 ?  40  ASN   A HD22 1 
ATOM   1049 H HD22 B ASN   A 1 40  ? 25.482 4.901   -4.170  0.70 14.58 ?  40  ASN   A HD22 1 
ATOM   1050 N N    A VAL   A 1 41  ? 29.742 1.320   -4.932  0.30 9.86  ?  41  VAL   A N    1 
ATOM   1051 N N    B VAL   A 1 41  ? 29.561 1.414   -5.036  0.70 10.82 ?  41  VAL   A N    1 
ATOM   1052 C CA   A VAL   A 1 41  ? 31.176 1.053   -4.979  0.30 10.70 ?  41  VAL   A CA   1 
ATOM   1053 C CA   B VAL   A 1 41  ? 30.987 1.079   -5.053  0.70 11.53 ?  41  VAL   A CA   1 
ATOM   1054 C C    A VAL   A 1 41  ? 31.975 2.248   -4.509  0.30 10.97 ?  41  VAL   A C    1 
ATOM   1055 C C    B VAL   A 1 41  ? 31.881 2.204   -4.541  0.70 11.13 ?  41  VAL   A C    1 
ATOM   1056 O O    A VAL   A 1 41  ? 33.122 2.090   -4.075  0.30 11.40 ?  41  VAL   A O    1 
ATOM   1057 O O    B VAL   A 1 41  ? 33.021 1.948   -4.137  0.70 11.53 ?  41  VAL   A O    1 
ATOM   1058 C CB   A VAL   A 1 41  ? 31.659 0.592   -6.375  0.30 10.66 ?  41  VAL   A CB   1 
ATOM   1059 C CB   B VAL   A 1 41  ? 31.468 0.597   -6.442  0.70 12.80 ?  41  VAL   A CB   1 
ATOM   1060 C CG1  A VAL   A 1 41  ? 31.014 -0.726  -6.756  0.30 10.39 ?  41  VAL   A CG1  1 
ATOM   1061 C CG1  B VAL   A 1 41  ? 30.736 -0.670  -6.862  0.70 13.51 ?  41  VAL   A CG1  1 
ATOM   1062 C CG2  A VAL   A 1 41  ? 31.397 1.659   -7.429  0.30 11.60 ?  41  VAL   A CG2  1 
ATOM   1063 C CG2  B VAL   A 1 41  ? 31.325 1.687   -7.495  0.70 13.97 ?  41  VAL   A CG2  1 
ATOM   1064 H H    A VAL   A 1 41  ? 29.346 1.280   -5.691  0.30 11.83 ?  41  VAL   A H    1 
ATOM   1065 H H    B VAL   A 1 41  ? 29.179 1.436   -5.810  0.70 12.98 ?  41  VAL   A H    1 
ATOM   1066 H HA   A VAL   A 1 41  ? 31.372 0.329   -4.367  0.30 12.84 ?  41  VAL   A HA   1 
ATOM   1067 H HA   B VAL   A 1 41  ? 31.113 0.333   -4.451  0.70 13.84 ?  41  VAL   A HA   1 
ATOM   1068 H HB   A VAL   A 1 41  ? 32.620 0.445   -6.342  0.30 12.80 ?  41  VAL   A HB   1 
ATOM   1069 H HB   B VAL   A 1 41  ? 32.408 0.376   -6.379  0.70 15.36 ?  41  VAL   A HB   1 
ATOM   1070 H HG11 A VAL   A 1 41  ? 31.400 -1.039  -7.589  0.30 12.46 ?  41  VAL   A HG11 1 
ATOM   1071 H HG11 B VAL   A 1 41  ? 31.054 -0.946  -7.736  0.70 16.22 ?  41  VAL   A HG11 1 
ATOM   1072 H HG12 A VAL   A 1 41  ? 31.177 -1.371  -6.051  0.30 12.46 ?  41  VAL   A HG12 1 
ATOM   1073 H HG12 B VAL   A 1 41  ? 30.913 -1.367  -6.211  0.70 16.22 ?  41  VAL   A HG12 1 
ATOM   1074 H HG13 A VAL   A 1 41  ? 30.060 -0.586  -6.864  0.30 12.46 ?  41  VAL   A HG13 1 
ATOM   1075 H HG13 B VAL   A 1 41  ? 29.783 -0.489  -6.899  0.70 16.22 ?  41  VAL   A HG13 1 
ATOM   1076 H HG21 A VAL   A 1 41  ? 31.641 1.309   -8.302  0.30 13.91 ?  41  VAL   A HG21 1 
ATOM   1077 H HG21 B VAL   A 1 41  ? 31.565 1.323   -8.364  0.70 16.76 ?  41  VAL   A HG21 1 
ATOM   1078 H HG22 A VAL   A 1 41  ? 30.457 1.892   -7.418  0.30 13.91 ?  41  VAL   A HG22 1 
ATOM   1079 H HG22 B VAL   A 1 41  ? 30.410 2.000   -7.509  0.70 16.76 ?  41  VAL   A HG22 1 
ATOM   1080 H HG23 A VAL   A 1 41  ? 31.935 2.443   -7.230  0.30 13.91 ?  41  VAL   A HG23 1 
ATOM   1081 H HG23 B VAL   A 1 41  ? 31.923 2.420   -7.273  0.70 16.76 ?  41  VAL   A HG23 1 
ATOM   1082 N N    . TYR   A 1 42  ? 31.410 3.450   -4.589  1.00 11.20 ?  42  TYR   A N    1 
ATOM   1083 C CA   . TYR   A 1 42  ? 32.148 4.633   -4.164  1.00 11.20 ?  42  TYR   A CA   1 
ATOM   1084 C C    . TYR   A 1 42  ? 31.881 5.000   -2.715  1.00 10.88 ?  42  TYR   A C    1 
ATOM   1085 O O    . TYR   A 1 42  ? 32.448 5.985   -2.217  1.00 11.60 ?  42  TYR   A O    1 
ATOM   1086 C CB   . TYR   A 1 42  ? 31.822 5.828   -5.079  1.00 12.08 ?  42  TYR   A CB   1 
ATOM   1087 C CG   . TYR   A 1 42  ? 32.017 5.525   -6.554  1.00 12.96 ?  42  TYR   A CG   1 
ATOM   1088 C CD1  . TYR   A 1 42  ? 33.281 5.319   -7.082  1.00 13.83 ?  42  TYR   A CD1  1 
ATOM   1089 C CD2  . TYR   A 1 42  ? 30.930 5.412   -7.408  1.00 14.55 ?  42  TYR   A CD2  1 
ATOM   1090 C CE1  . TYR   A 1 42  ? 33.456 5.018   -8.428  1.00 14.07 ?  42  TYR   A CE1  1 
ATOM   1091 C CE2  . TYR   A 1 42  ? 31.095 5.118   -8.751  1.00 15.27 ?  42  TYR   A CE2  1 
ATOM   1092 C CZ   . TYR   A 1 42  ? 32.359 4.917   -9.258  1.00 15.06 ?  42  TYR   A CZ   1 
ATOM   1093 O OH   . TYR   A 1 42  ? 32.527 4.620   -10.589 1.00 16.89 ?  42  TYR   A OH   1 
ATOM   1094 H H    A TYR   A 1 42  ? 30.620 3.606   -4.886  0.30 13.44 ?  42  TYR   A H    1 
ATOM   1095 H H    B TYR   A 1 42  ? 30.629 3.644   -4.888  0.70 13.44 ?  42  TYR   A H    1 
ATOM   1096 H HA   . TYR   A 1 42  ? 33.099 4.460   -4.249  1.00 13.44 ?  42  TYR   A HA   1 
ATOM   1097 H HB2  . TYR   A 1 42  ? 30.897 6.083   -4.942  1.00 14.50 ?  42  TYR   A HB2  1 
ATOM   1098 H HB3  . TYR   A 1 42  ? 32.406 6.569   -4.844  1.00 14.50 ?  42  TYR   A HB3  1 
ATOM   1099 H HD1  . TYR   A 1 42  ? 34.027 5.375   -6.527  1.00 16.60 ?  42  TYR   A HD1  1 
ATOM   1100 H HD2  . TYR   A 1 42  ? 30.073 5.548   -7.069  1.00 17.46 ?  42  TYR   A HD2  1 
ATOM   1101 H HE1  . TYR   A 1 42  ? 34.311 4.884   -8.769  1.00 16.88 ?  42  TYR   A HE1  1 
ATOM   1102 H HE2  . TYR   A 1 42  ? 30.354 5.059   -9.310  1.00 18.33 ?  42  TYR   A HE2  1 
ATOM   1103 H HH   . TYR   A 1 42  ? 33.346 4.534   -10.765 1.00 20.26 ?  42  TYR   A HH   1 
ATOM   1104 N N    A LEU   A 1 43  ? 31.034 4.235   -2.022  0.30 10.59 ?  43  LEU   A N    1 
ATOM   1105 N N    B LEU   A 1 43  ? 31.031 4.233   -2.032  0.70 10.37 ?  43  LEU   A N    1 
ATOM   1106 C CA   A LEU   A 1 43  ? 30.641 4.541   -0.645  0.30 10.48 ?  43  LEU   A CA   1 
ATOM   1107 C CA   B LEU   A 1 43  ? 30.573 4.567   -0.687  0.70 9.97  ?  43  LEU   A CA   1 
ATOM   1108 C C    A LEU   A 1 43  ? 30.139 5.976   -0.507  0.30 10.95 ?  43  LEU   A C    1 
ATOM   1109 C C    B LEU   A 1 43  ? 30.106 6.018   -0.603  0.70 9.79  ?  43  LEU   A C    1 
ATOM   1110 O O    A LEU   A 1 43  ? 30.321 6.618   0.530   0.30 11.30 ?  43  LEU   A O    1 
ATOM   1111 O O    B LEU   A 1 43  ? 30.397 6.730   0.358   0.70 10.68 ?  43  LEU   A O    1 
ATOM   1112 C CB   A LEU   A 1 43  ? 31.753 4.234   0.361   0.30 10.47 ?  43  LEU   A CB   1 
ATOM   1113 C CB   B LEU   A 1 43  ? 31.611 4.248   0.388   0.70 10.19 ?  43  LEU   A CB   1 
ATOM   1114 C CG   A LEU   A 1 43  ? 32.231 2.783   0.463   0.30 10.49 ?  43  LEU   A CG   1 
ATOM   1115 C CG   B LEU   A 1 43  ? 32.108 2.800   0.449   0.70 10.70 ?  43  LEU   A CG   1 
ATOM   1116 C CD1  A LEU   A 1 43  ? 33.316 2.679   1.523   0.30 10.58 ?  43  LEU   A CD1  1 
ATOM   1117 C CD1  B LEU   A 1 43  ? 33.124 2.667   1.572   0.70 11.74 ?  43  LEU   A CD1  1 
ATOM   1118 C CD2  A LEU   A 1 43  ? 31.082 1.835   0.774   0.30 10.65 ?  43  LEU   A CD2  1 
ATOM   1119 C CD2  B LEU   A 1 43  ? 30.964 1.801   0.619   0.70 10.71 ?  43  LEU   A CD2  1 
ATOM   1120 H H    A LEU   A 1 43  ? 30.666 3.518   -2.328  0.30 12.71 ?  43  LEU   A H    1 
ATOM   1121 H H    B LEU   A 1 43  ? 30.697 3.493   -2.331  0.70 12.44 ?  43  LEU   A H    1 
ATOM   1122 H HA   A LEU   A 1 43  ? 29.889 3.975   -0.416  0.30 12.58 ?  43  LEU   A HA   1 
ATOM   1123 H HA   B LEU   A 1 43  ? 29.792 4.012   -0.498  0.70 11.96 ?  43  LEU   A HA   1 
ATOM   1124 H HB2  A LEU   A 1 43  ? 32.524 4.773   0.140   0.30 12.57 ?  43  LEU   A HB2  1 
ATOM   1125 H HB2  B LEU   A 1 43  ? 32.378 4.814   0.241   0.70 12.23 ?  43  LEU   A HB2  1 
ATOM   1126 H HB3  A LEU   A 1 43  ? 31.429 4.477   1.242   0.30 12.57 ?  43  LEU   A HB3  1 
ATOM   1127 H HB3  B LEU   A 1 43  ? 31.218 4.452   1.254   0.70 12.23 ?  43  LEU   A HB3  1 
ATOM   1128 H HG   A LEU   A 1 43  ? 32.620 2.515   -0.385  0.30 12.59 ?  43  LEU   A HG   1 
ATOM   1129 H HG   B LEU   A 1 43  ? 32.561 2.593   -0.381  0.70 12.84 ?  43  LEU   A HG   1 
ATOM   1130 H HD11 A LEU   A 1 43  ? 33.616 1.757   1.581   0.30 12.70 ?  43  LEU   A HD11 1 
ATOM   1131 H HD11 B LEU   A 1 43  ? 33.436 1.748   1.606   0.70 14.09 ?  43  LEU   A HD11 1 
ATOM   1132 H HD12 A LEU   A 1 43  ? 34.057 3.253   1.275   0.30 12.70 ?  43  LEU   A HD12 1 
ATOM   1133 H HD12 B LEU   A 1 43  ? 33.866 3.263   1.400   0.70 14.09 ?  43  LEU   A HD12 1 
ATOM   1134 H HD13 A LEU   A 1 43  ? 32.950 2.961   2.377   0.30 12.70 ?  43  LEU   A HD13 1 
ATOM   1135 H HD13 B LEU   A 1 43  ? 32.697 2.900   2.412   0.70 14.09 ?  43  LEU   A HD13 1 
ATOM   1136 H HD21 A LEU   A 1 43  ? 31.441 0.950   0.946   0.30 12.78 ?  43  LEU   A HD21 1 
ATOM   1137 H HD21 B LEU   A 1 43  ? 31.339 0.914   0.744   0.70 12.85 ?  43  LEU   A HD21 1 
ATOM   1138 H HD22 A LEU   A 1 43  ? 30.612 2.159   1.557   0.30 12.78 ?  43  LEU   A HD22 1 
ATOM   1139 H HD22 B LEU   A 1 43  ? 30.438 2.051   1.391   0.70 12.85 ?  43  LEU   A HD22 1 
ATOM   1140 H HD23 A LEU   A 1 43  ? 30.483 1.808   0.013   0.30 12.78 ?  43  LEU   A HD23 1 
ATOM   1141 H HD23 B LEU   A 1 43  ? 30.414 1.815   -0.180  0.70 12.85 ?  43  LEU   A HD23 1 
ATOM   1142 N N    A LYS   A 1 44  ? 29.484 6.476   -1.553  0.30 11.82 ?  44  LYS   A N    1 
ATOM   1143 N N    B LYS   A 1 44  ? 29.354 6.449   -1.620  0.70 9.92  ?  44  LYS   A N    1 
ATOM   1144 C CA   A LYS   A 1 44  ? 28.860 7.796   -1.532  0.30 12.70 ?  44  LYS   A CA   1 
ATOM   1145 C CA   B LYS   A 1 44  ? 28.692 7.751   -1.611  0.70 10.21 ?  44  LYS   A CA   1 
ATOM   1146 C C    A LYS   A 1 44  ? 27.429 7.605   -1.054  0.30 11.65 ?  44  LYS   A C    1 
ATOM   1147 C C    B LYS   A 1 44  ? 27.275 7.535   -1.094  0.70 9.78  ?  44  LYS   A C    1 
ATOM   1148 O O    A LYS   A 1 44  ? 26.564 7.145   -1.802  0.30 11.83 ?  44  LYS   A O    1 
ATOM   1149 O O    B LYS   A 1 44  ? 26.423 6.978   -1.794  0.70 10.78 ?  44  LYS   A O    1 
ATOM   1150 C CB   A LYS   A 1 44  ? 28.916 8.444   -2.911  0.30 14.92 ?  44  LYS   A CB   1 
ATOM   1151 C CB   B LYS   A 1 44  ? 28.696 8.381   -3.003  0.70 12.14 ?  44  LYS   A CB   1 
ATOM   1152 C CG   A LYS   A 1 44  ? 30.314 8.847   -3.348  0.30 17.40 ?  44  LYS   A CG   1 
ATOM   1153 C CG   B LYS   A 1 44  ? 30.063 8.861   -3.451  0.70 15.17 ?  44  LYS   A CG   1 
ATOM   1154 C CD   A LYS   A 1 44  ? 30.958 9.803   -2.354  0.30 20.05 ?  44  LYS   A CD   1 
ATOM   1155 C CD   B LYS   A 1 44  ? 30.683 9.828   -2.449  0.70 20.64 ?  44  LYS   A CD   1 
ATOM   1156 C CE   A LYS   A 1 44  ? 32.288 10.317  -2.863  0.30 21.93 ?  44  LYS   A CE   1 
ATOM   1157 C CE   B LYS   A 1 44  ? 32.013 10.357  -2.946  0.70 23.75 ?  44  LYS   A CE   1 
ATOM   1158 N NZ   A LYS   A 1 44  ? 32.978 11.150  -1.843  0.30 23.20 ?  44  LYS   A NZ   1 
ATOM   1159 N NZ   B LYS   A 1 44  ? 32.843 10.888  -1.831  0.70 25.76 ?  44  LYS   A NZ   1 
ATOM   1160 H H    A LYS   A 1 44  ? 29.380 6.055   -2.295  0.30 14.18 ?  44  LYS   A H    1 
ATOM   1161 H H    B LYS   A 1 44  ? 29.215 6.002   -2.343  0.70 11.91 ?  44  LYS   A H    1 
ATOM   1162 H HA   A LYS   A 1 44  ? 29.315 8.363   -0.892  0.30 15.24 ?  44  LYS   A HA   1 
ATOM   1163 H HA   B LYS   A 1 44  ? 29.132 8.341   -0.988  0.70 12.26 ?  44  LYS   A HA   1 
ATOM   1164 H HB2  A LYS   A 1 44  ? 28.571 7.814   -3.564  0.30 17.91 ?  44  LYS   A HB2  1 
ATOM   1165 H HB2  B LYS   A 1 44  ? 28.388 7.719   -3.645  0.70 14.57 ?  44  LYS   A HB2  1 
ATOM   1166 H HB3  A LYS   A 1 44  ? 28.366 9.242   -2.902  0.30 17.91 ?  44  LYS   A HB3  1 
ATOM   1167 H HB3  B LYS   A 1 44  ? 28.095 9.142   -3.007  0.70 14.57 ?  44  LYS   A HB3  1 
ATOM   1168 H HG2  A LYS   A 1 44  ? 30.869 8.054   -3.413  0.30 20.88 ?  44  LYS   A HG2  1 
ATOM   1169 H HG2  B LYS   A 1 44  ? 30.655 8.101   -3.550  0.70 18.20 ?  44  LYS   A HG2  1 
ATOM   1170 H HG3  A LYS   A 1 44  ? 30.262 9.292   -4.209  0.30 20.88 ?  44  LYS   A HG3  1 
ATOM   1171 H HG3  B LYS   A 1 44  ? 29.974 9.328   -4.302  0.70 18.20 ?  44  LYS   A HG3  1 
ATOM   1172 H HD2  A LYS   A 1 44  ? 30.363 10.558  -2.211  0.30 24.06 ?  44  LYS   A HD2  1 
ATOM   1173 H HD2  B LYS   A 1 44  ? 30.079 10.574  -2.307  0.70 24.76 ?  44  LYS   A HD2  1 
ATOM   1174 H HD3  A LYS   A 1 44  ? 31.115 9.336   -1.518  0.30 24.06 ?  44  LYS   A HD3  1 
ATOM   1175 H HD3  B LYS   A 1 44  ? 30.846 9.362   -1.612  0.70 24.76 ?  44  LYS   A HD3  1 
ATOM   1176 H HE2  A LYS   A 1 44  ? 32.857 9.561   -3.079  0.30 26.32 ?  44  LYS   A HE2  1 
ATOM   1177 H HE2  B LYS   A 1 44  ? 32.505 9.635   -3.371  0.70 28.50 ?  44  LYS   A HE2  1 
ATOM   1178 H HE3  A LYS   A 1 44  ? 32.137 10.859  -3.652  0.30 26.32 ?  44  LYS   A HE3  1 
ATOM   1179 H HE3  B LYS   A 1 44  ? 31.855 11.073  -3.578  0.70 28.50 ?  44  LYS   A HE3  1 
ATOM   1180 H HZ1  A LYS   A 1 44  ? 33.788 11.369  -2.132  0.30 27.84 ?  44  LYS   A HZ1  1 
ATOM   1181 H HZ1  B LYS   A 1 44  ? 33.616 11.194  -2.147  0.70 30.91 ?  44  LYS   A HZ1  1 
ATOM   1182 H HZ2  A LYS   A 1 44  ? 32.510 11.891  -1.690  0.30 27.84 ?  44  LYS   A HZ2  1 
ATOM   1183 H HZ2  B LYS   A 1 44  ? 32.413 11.556  -1.426  0.70 30.91 ?  44  LYS   A HZ2  1 
ATOM   1184 H HZ3  A LYS   A 1 44  ? 33.055 10.693  -1.082  0.30 27.84 ?  44  LYS   A HZ3  1 
ATOM   1185 H HZ3  B LYS   A 1 44  ? 33.005 10.247  -1.237  0.70 30.91 ?  44  LYS   A HZ3  1 
ATOM   1186 N N    A HIS   A 1 45  ? 27.183 7.953   0.208   0.30 11.14 ?  45  HIS   A N    1 
ATOM   1187 N N    B HIS   A 1 45  ? 27.028 7.952   0.143   0.70 9.54  ?  45  HIS   A N    1 
ATOM   1188 C CA   A HIS   A 1 45  ? 25.918 7.642   0.868   0.30 10.90 ?  45  HIS   A CA   1 
ATOM   1189 C CA   B HIS   A 1 45  ? 25.806 7.586   0.857   0.70 9.62  ?  45  HIS   A CA   1 
ATOM   1190 C C    A HIS   A 1 45  ? 24.986 8.840   0.719   0.30 11.55 ?  45  HIS   A C    1 
ATOM   1191 C C    B HIS   A 1 45  ? 24.737 8.664   0.664   0.70 10.18 ?  45  HIS   A C    1 
ATOM   1192 O O    A HIS   A 1 45  ? 24.767 9.623   1.645   0.30 12.37 ?  45  HIS   A O    1 
ATOM   1193 O O    B HIS   A 1 45  ? 24.387 9.412   1.578   0.70 11.54 ?  45  HIS   A O    1 
ATOM   1194 C CB   A HIS   A 1 45  ? 26.167 7.292   2.326   0.30 10.67 ?  45  HIS   A CB   1 
ATOM   1195 C CB   B HIS   A 1 45  ? 26.115 7.380   2.328   0.70 10.25 ?  45  HIS   A CB   1 
ATOM   1196 C CG   A HIS   A 1 45  ? 27.302 6.338   2.530   0.30 10.07 ?  45  HIS   A CG   1 
ATOM   1197 C CG   B HIS   A 1 45  ? 27.229 6.418   2.572   0.70 9.77  ?  45  HIS   A CG   1 
ATOM   1198 N ND1  A HIS   A 1 45  ? 27.308 5.060   2.010   0.30 10.32 ?  45  HIS   A ND1  1 
ATOM   1199 N ND1  B HIS   A 1 45  ? 27.239 5.140   2.054   0.70 10.03 ?  45  HIS   A ND1  1 
ATOM   1200 C CD2  A HIS   A 1 45  ? 28.473 6.483   3.194   0.30 10.69 ?  45  HIS   A CD2  1 
ATOM   1201 C CD2  B HIS   A 1 45  ? 28.383 6.565   3.264   0.70 10.21 ?  45  HIS   A CD2  1 
ATOM   1202 C CE1  A HIS   A 1 45  ? 28.435 4.459   2.351   0.30 10.50 ?  45  HIS   A CE1  1 
ATOM   1203 C CE1  B HIS   A 1 45  ? 28.352 4.538   2.435   0.70 9.82  ?  45  HIS   A CE1  1 
ATOM   1204 N NE2  A HIS   A 1 45  ? 29.159 5.300   3.069   0.30 10.83 ?  45  HIS   A NE2  1 
ATOM   1205 N NE2  B HIS   A 1 45  ? 29.064 5.380   3.168   0.70 10.23 ?  45  HIS   A NE2  1 
ATOM   1206 H H    A HIS   A 1 45  ? 27.739 8.384   0.705   0.30 13.36 ?  45  HIS   A H    1 
ATOM   1207 H H    B HIS   A 1 45  ? 27.542 8.469   0.593   0.70 11.45 ?  45  HIS   A H    1 
ATOM   1208 H HA   A HIS   A 1 45  ? 25.510 6.880   0.433   0.30 13.07 ?  45  HIS   A HA   1 
ATOM   1209 H HA   B HIS   A 1 45  ? 25.462 6.747   0.501   0.70 11.54 ?  45  HIS   A HA   1 
ATOM   1210 H HB2  A HIS   A 1 45  ? 26.371 8.106   2.813   0.30 12.80 ?  45  HIS   A HB2  1 
ATOM   1211 H HB2  B HIS   A 1 45  ? 26.363 8.235   2.717   0.70 12.30 ?  45  HIS   A HB2  1 
ATOM   1212 H HB3  A HIS   A 1 45  ? 25.367 6.882   2.688   0.30 12.80 ?  45  HIS   A HB3  1 
ATOM   1213 H HB3  B HIS   A 1 45  ? 25.321 7.038   2.774   0.70 12.30 ?  45  HIS   A HB3  1 
ATOM   1214 H HD2  A HIS   A 1 45  ? 28.761 7.242   3.648   0.30 12.82 ?  45  HIS   A HD2  1 
ATOM   1215 H HD2  B HIS   A 1 45  ? 28.662 7.332   3.717   0.70 12.25 ?  45  HIS   A HD2  1 
ATOM   1216 H HE1  A HIS   A 1 45  ? 28.677 3.590   2.128   0.30 12.60 ?  45  HIS   A HE1  1 
ATOM   1217 H HE1  B HIS   A 1 45  ? 28.586 3.667   2.233   0.70 11.78 ?  45  HIS   A HE1  1 
ATOM   1218 H HE2  A HIS   A 1 45  ? 29.934 5.133   3.404   0.30 12.99 ?  45  HIS   A HE2  1 
ATOM   1219 H HE2  B HIS   A 1 45  ? 29.825 5.214   3.524   0.70 12.28 ?  45  HIS   A HE2  1 
ATOM   1220 N N    A GLY   A 1 46  ? 24.429 8.977   -0.481  0.30 11.59 ?  46  GLY   A N    1 
ATOM   1221 N N    B GLY   A 1 46  ? 24.175 8.696   -0.540  0.70 11.19 ?  46  GLY   A N    1 
ATOM   1222 C CA   A GLY   A 1 46  ? 23.637 10.147  -0.813  0.30 11.38 ?  46  GLY   A CA   1 
ATOM   1223 C CA   B GLY   A 1 46  ? 23.321 9.807   -0.929  0.70 12.16 ?  46  GLY   A CA   1 
ATOM   1224 C C    A GLY   A 1 46  ? 22.140 9.999   -0.624  0.30 11.39 ?  46  GLY   A C    1 
ATOM   1225 C C    B GLY   A 1 46  ? 21.854 9.693   -0.552  0.70 12.19 ?  46  GLY   A C    1 
ATOM   1226 O O    A GLY   A 1 46  ? 21.441 10.993  -0.407  0.30 12.56 ?  46  GLY   A O    1 
ATOM   1227 O O    B GLY   A 1 46  ? 21.221 10.687  -0.172  0.70 14.40 ?  46  GLY   A O    1 
ATOM   1228 H H    A GLY   A 1 46  ? 24.504 8.408   -1.124  0.30 13.91 ?  46  GLY   A H    1 
ATOM   1229 H H    B GLY   A 1 46  ? 24.270 8.093   -1.145  0.70 13.42 ?  46  GLY   A H    1 
ATOM   1230 H HA2  A GLY   A 1 46  ? 23.941 10.893  -0.272  0.30 13.65 ?  46  GLY   A HA2  1 
ATOM   1231 H HA2  B GLY   A 1 46  ? 23.659 10.616  -0.521  0.70 14.59 ?  46  GLY   A HA2  1 
ATOM   1232 H HA3  A GLY   A 1 46  ? 23.788 10.373  -1.743  0.30 13.65 ?  46  GLY   A HA3  1 
ATOM   1233 H HA3  B GLY   A 1 46  ? 23.373 9.913   -1.892  0.70 14.59 ?  46  GLY   A HA3  1 
ATOM   1234 N N    A GLY   A 1 47  ? 21.628 8.776   -0.722  0.30 11.17 ?  47  GLY   A N    1 
ATOM   1235 N N    B GLY   A 1 47  ? 21.290 8.493   -0.663  0.70 12.23 ?  47  GLY   A N    1 
ATOM   1236 C CA   A GLY   A 1 47  ? 20.196 8.566   -0.665  0.30 11.33 ?  47  GLY   A CA   1 
ATOM   1237 C CA   B GLY   A 1 47  ? 19.866 8.318   -0.471  0.70 12.14 ?  47  GLY   A CA   1 
ATOM   1238 C C    A GLY   A 1 47  ? 19.887 7.131   -0.301  0.30 11.05 ?  47  GLY   A C    1 
ATOM   1239 C C    B GLY   A 1 47  ? 19.539 6.914   -0.018  0.70 11.30 ?  47  GLY   A C    1 
ATOM   1240 O O    A GLY   A 1 47  ? 20.780 6.324   -0.034  0.30 11.56 ?  47  GLY   A O    1 
ATOM   1241 O O    B GLY   A 1 47  ? 20.426 6.086   0.200   0.70 11.01 ?  47  GLY   A O    1 
ATOM   1242 H H    A GLY   A 1 47  ? 22.089 8.061   -0.820  0.30 13.40 ?  47  GLY   A H    1 
ATOM   1243 H H    B GLY   A 1 47  ? 21.720 7.762   -0.839  0.70 14.68 ?  47  GLY   A H    1 
ATOM   1244 H HA2  A GLY   A 1 47  ? 19.800 9.156   0.001   0.30 13.60 ?  47  GLY   A HA2  1 
ATOM   1245 H HA2  B GLY   A 1 47  ? 19.549 8.940   0.202   0.70 14.57 ?  47  GLY   A HA2  1 
ATOM   1246 H HA3  A GLY   A 1 47  ? 19.804 8.769   -1.531  0.30 13.60 ?  47  GLY   A HA3  1 
ATOM   1247 H HA3  B GLY   A 1 47  ? 19.400 8.494   -1.302  0.70 14.57 ?  47  GLY   A HA3  1 
ATOM   1248 N N    A GLY   A 1 48  ? 18.596 6.817   -0.304  0.30 11.03 ?  48  GLY   A N    1 
ATOM   1249 N N    B GLY   A 1 48  ? 18.242 6.649   0.123   0.70 11.46 ?  48  GLY   A N    1 
ATOM   1250 C CA   A GLY   A 1 48  ? 18.148 5.489   0.058   0.30 10.95 ?  48  GLY   A CA   1 
ATOM   1251 C CA   B GLY   A 1 48  ? 17.819 5.337   0.567   0.70 10.56 ?  48  GLY   A CA   1 
ATOM   1252 C C    A GLY   A 1 48  ? 18.545 5.128   1.476   0.30 10.76 ?  48  GLY   A C    1 
ATOM   1253 C C    B GLY   A 1 48  ? 18.367 4.995   1.940   0.70 10.40 ?  48  GLY   A C    1 
ATOM   1254 O O    A GLY   A 1 48  ? 18.699 5.986   2.354   0.30 10.86 ?  48  GLY   A O    1 
ATOM   1255 O O    B GLY   A 1 48  ? 18.524 5.854   2.820   0.70 10.49 ?  48  GLY   A O    1 
ATOM   1256 H H    A GLY   A 1 48  ? 17.971 7.358   -0.512  0.30 13.24 ?  48  GLY   A H    1 
ATOM   1257 H H    B GLY   A 1 48  ? 17.599 7.204   -0.029  0.70 13.75 ?  48  GLY   A H    1 
ATOM   1258 H HA2  A GLY   A 1 48  ? 17.186 5.444   -0.015  0.30 13.14 ?  48  GLY   A HA2  1 
ATOM   1259 H HA2  B GLY   A 1 48  ? 16.851 5.299   0.601   0.70 12.67 ?  48  GLY   A HA2  1 
ATOM   1260 H HA3  A GLY   A 1 48  ? 18.541 4.836   -0.541  0.30 13.14 ?  48  GLY   A HA3  1 
ATOM   1261 H HA3  B GLY   A 1 48  ? 18.132 4.667   -0.061  0.70 12.67 ?  48  GLY   A HA3  1 
ATOM   1262 N N    A VAL   A 1 49  ? 18.721 3.824   1.701   0.30 10.89 ?  49  VAL   A N    1 
ATOM   1263 N N    B VAL   A 1 49  ? 18.648 3.703   2.129   0.70 10.13 ?  49  VAL   A N    1 
ATOM   1264 C CA   A VAL   A 1 49  ? 19.167 3.339   3.005   0.30 10.60 ?  49  VAL   A CA   1 
ATOM   1265 C CA   B VAL   A 1 49  ? 19.243 3.230   3.376   0.70 9.92  ?  49  VAL   A CA   1 
ATOM   1266 C C    A VAL   A 1 49  ? 20.496 3.976   3.387   0.30 10.18 ?  49  VAL   A C    1 
ATOM   1267 C C    B VAL   A 1 49  ? 20.537 3.976   3.672   0.70 9.89  ?  49  VAL   A C    1 
ATOM   1268 O O    A VAL   A 1 49  ? 20.705 4.360   4.543   0.30 10.25 ?  49  VAL   A O    1 
ATOM   1269 O O    B VAL   A 1 49  ? 20.775 4.406   4.805   0.70 10.26 ?  49  VAL   A O    1 
ATOM   1270 C CB   A VAL   A 1 49  ? 19.257 1.800   3.001   0.30 11.11 ?  49  VAL   A CB   1 
ATOM   1271 C CB   B VAL   A 1 49  ? 19.475 1.709   3.303   0.70 10.79 ?  49  VAL   A CB   1 
ATOM   1272 C CG1  A VAL   A 1 49  ? 19.967 1.295   4.255   0.30 11.37 ?  49  VAL   A CG1  1 
ATOM   1273 C CG1  B VAL   A 1 49  ? 20.345 1.240   4.460   0.70 10.79 ?  49  VAL   A CG1  1 
ATOM   1274 C CG2  A VAL   A 1 49  ? 17.869 1.185   2.885   0.30 11.35 ?  49  VAL   A CG2  1 
ATOM   1275 C CG2  B VAL   A 1 49  ? 18.142 0.964   3.291   0.70 12.41 ?  49  VAL   A CG2  1 
ATOM   1276 H H    A VAL   A 1 49  ? 18.588 3.207   1.123   0.30 13.07 ?  49  VAL   A H    1 
ATOM   1277 H H    B VAL   A 1 49  ? 18.495 3.084   1.553   0.70 12.16 ?  49  VAL   A H    1 
ATOM   1278 H HA   A VAL   A 1 49  ? 18.519 3.592   3.678   0.30 12.72 ?  49  VAL   A HA   1 
ATOM   1279 H HA   B VAL   A 1 49  ? 18.630 3.400   4.106   0.70 11.91 ?  49  VAL   A HA   1 
ATOM   1280 H HB   A VAL   A 1 49  ? 19.776 1.516   2.233   0.30 13.33 ?  49  VAL   A HB   1 
ATOM   1281 H HB   B VAL   A 1 49  ? 19.941 1.501   2.476   0.70 12.95 ?  49  VAL   A HB   1 
ATOM   1282 H HG11 A VAL   A 1 49  ? 19.773 0.349   4.366   0.30 13.64 ?  49  VAL   A HG11 1 
ATOM   1283 H HG11 B VAL   A 1 49  ? 20.236 0.280   4.561   0.70 12.95 ?  49  VAL   A HG11 1 
ATOM   1284 H HG12 A VAL   A 1 49  ? 20.923 1.423   4.157   0.30 13.64 ?  49  VAL   A HG12 1 
ATOM   1285 H HG12 B VAL   A 1 49  ? 21.271 1.448   4.269   0.70 12.95 ?  49  VAL   A HG12 1 
ATOM   1286 H HG13 A VAL   A 1 49  ? 19.641 1.788   5.024   0.30 13.64 ?  49  VAL   A HG13 1 
ATOM   1287 H HG13 B VAL   A 1 49  ? 20.058 1.689   5.270   0.70 12.95 ?  49  VAL   A HG13 1 
ATOM   1288 H HG21 A VAL   A 1 49  ? 17.952 0.218   2.882   0.30 13.62 ?  49  VAL   A HG21 1 
ATOM   1289 H HG21 B VAL   A 1 49  ? 18.315 0.014   3.205   0.70 14.89 ?  49  VAL   A HG21 1 
ATOM   1290 H HG22 A VAL   A 1 49  ? 17.334 1.470   3.642   0.30 13.62 ?  49  VAL   A HG22 1 
ATOM   1291 H HG22 B VAL   A 1 49  ? 17.675 1.145   4.120   0.70 14.89 ?  49  VAL   A HG22 1 
ATOM   1292 H HG23 A VAL   A 1 49  ? 17.462 1.485   2.058   0.30 13.62 ?  49  VAL   A HG23 1 
ATOM   1293 H HG23 B VAL   A 1 49  ? 17.616 1.274   2.538   0.70 14.89 ?  49  VAL   A HG23 1 
ATOM   1294 N N    A ALA   A 1 50  ? 21.422 4.075   2.429   0.30 9.95  ?  50  ALA   A N    1 
ATOM   1295 N N    B ALA   A 1 50  ? 21.415 4.087   2.670   0.70 9.87  ?  50  ALA   A N    1 
ATOM   1296 C CA   A ALA   A 1 50  ? 22.743 4.624   2.718   0.30 9.61  ?  50  ALA   A CA   1 
ATOM   1297 C CA   B ALA   A 1 50  ? 22.737 4.665   2.899   0.70 9.44  ?  50  ALA   A CA   1 
ATOM   1298 C C    A ALA   A 1 50  ? 22.652 6.080   3.154   0.30 9.55  ?  50  ALA   A C    1 
ATOM   1299 C C    B ALA   A 1 50  ? 22.632 6.112   3.357   0.70 9.45  ?  50  ALA   A C    1 
ATOM   1300 O O    A ALA   A 1 50  ? 23.270 6.483   4.145   0.30 9.70  ?  50  ALA   A O    1 
ATOM   1301 O O    B ALA   A 1 50  ? 23.282 6.518   4.327   0.70 10.03 ?  50  ALA   A O    1 
ATOM   1302 C CB   A ALA   A 1 50  ? 23.643 4.481   1.490   0.30 9.91  ?  50  ALA   A CB   1 
ATOM   1303 C CB   B ALA   A 1 50  ? 23.580 4.558   1.629   0.70 9.85  ?  50  ALA   A CB   1 
ATOM   1304 H H    A ALA   A 1 50  ? 21.310 3.828   1.615   0.30 11.94 ?  50  ALA   A H    1 
ATOM   1305 H H    B ALA   A 1 50  ? 21.265 3.842   1.856   0.70 11.85 ?  50  ALA   A H    1 
ATOM   1306 H HA   A ALA   A 1 50  ? 23.147 4.128   3.443   0.30 11.53 ?  50  ALA   A HA   1 
ATOM   1307 H HA   B ALA   A 1 50  ? 23.183 4.167   3.596   0.70 11.32 ?  50  ALA   A HA   1 
ATOM   1308 H HB1  A ALA   A 1 50  ? 24.516 4.852   1.690   0.30 11.90 ?  50  ALA   A HB1  1 
ATOM   1309 H HB1  B ALA   A 1 50  ? 24.452 4.947   1.795   0.70 11.82 ?  50  ALA   A HB1  1 
ATOM   1310 H HB2  A ALA   A 1 50  ? 23.726 3.541   1.265   0.30 11.90 ?  50  ALA   A HB2  1 
ATOM   1311 H HB2  B ALA   A 1 50  ? 23.673 3.624   1.388   0.70 11.82 ?  50  ALA   A HB2  1 
ATOM   1312 H HB3  A ALA   A 1 50  ? 23.243 4.964   0.746   0.30 11.90 ?  50  ALA   A HB3  1 
ATOM   1313 H HB3  B ALA   A 1 50  ? 23.135 5.040   0.912   0.70 11.82 ?  50  ALA   A HB3  1 
ATOM   1314 N N    A GLY   A 1 51  ? 21.889 6.888   2.419   0.30 9.63  ?  51  GLY   A N    1 
ATOM   1315 N N    B GLY   A 1 51  ? 21.822 6.910   2.661   0.70 10.24 ?  51  GLY   A N    1 
ATOM   1316 C CA   A GLY   A 1 51  ? 21.757 8.287   2.786   0.30 9.77  ?  51  GLY   A CA   1 
ATOM   1317 C CA   B GLY   A 1 51  ? 21.642 8.290   3.073   0.70 10.61 ?  51  GLY   A CA   1 
ATOM   1318 C C    A GLY   A 1 51  ? 21.134 8.472   4.157   0.30 9.20  ?  51  GLY   A C    1 
ATOM   1319 C C    B GLY   A 1 51  ? 21.062 8.402   4.469   0.70 10.45 ?  51  GLY   A C    1 
ATOM   1320 O O    A GLY   A 1 51  ? 21.517 9.374   4.907   0.30 9.19  ?  51  GLY   A O    1 
ATOM   1321 O O    B GLY   A 1 51  ? 21.447 9.285   5.244   0.70 10.95 ?  51  GLY   A O    1 
ATOM   1322 H H    A GLY   A 1 51  ? 21.449 6.654   1.720   0.30 11.56 ?  51  GLY   A H    1 
ATOM   1323 H H    B GLY   A 1 51  ? 21.371 6.676   1.961   0.70 12.29 ?  51  GLY   A H    1 
ATOM   1324 H HA2  A GLY   A 1 51  ? 22.633 8.705   2.790   0.30 11.72 ?  51  GLY   A HA2  1 
ATOM   1325 H HA2  B GLY   A 1 51  ? 22.497 8.745   3.054   0.70 12.73 ?  51  GLY   A HA2  1 
ATOM   1326 H HA3  A GLY   A 1 51  ? 21.204 8.741   2.131   0.30 11.72 ?  51  GLY   A HA3  1 
ATOM   1327 H HA3  B GLY   A 1 51  ? 21.044 8.738   2.449   0.70 12.73 ?  51  GLY   A HA3  1 
ATOM   1328 N N    A ALA   A 1 52  ? 20.155 7.629   4.499   0.30 9.63  ?  52  ALA   A N    1 
ATOM   1329 N N    B ALA   A 1 52  ? 20.117 7.516   4.803   0.70 10.37 ?  52  ALA   A N    1 
ATOM   1330 C CA   A ALA   A 1 52  ? 19.498 7.745   5.797   0.30 9.91  ?  52  ALA   A CA   1 
ATOM   1331 C CA   B ALA   A 1 52  ? 19.480 7.555   6.115   0.70 10.68 ?  52  ALA   A CA   1 
ATOM   1332 C C    A ALA   A 1 52  ? 20.424 7.317   6.933   0.30 9.89  ?  52  ALA   A C    1 
ATOM   1333 C C    B ALA   A 1 52  ? 20.447 7.132   7.219   0.70 10.24 ?  52  ALA   A C    1 
ATOM   1334 O O    A ALA   A 1 52  ? 20.487 7.982   7.973   0.30 10.09 ?  52  ALA   A O    1 
ATOM   1335 O O    B ALA   A 1 52  ? 20.515 7.771   8.276   0.70 10.89 ?  52  ALA   A O    1 
ATOM   1336 C CB   A ALA   A 1 52  ? 18.205 6.927   5.805   0.30 10.50 ?  52  ALA   A CB   1 
ATOM   1337 C CB   B ALA   A 1 52  ? 18.221 6.684   6.112   0.70 11.81 ?  52  ALA   A CB   1 
ATOM   1338 H H    A ALA   A 1 52  ? 19.861 6.990   4.003   0.30 11.56 ?  52  ALA   A H    1 
ATOM   1339 H H    B ALA   A 1 52  ? 19.839 6.879   4.286   0.70 12.44 ?  52  ALA   A H    1 
ATOM   1340 H HA   A ALA   A 1 52  ? 19.252 8.674   5.940   0.30 11.89 ?  52  ALA   A HA   1 
ATOM   1341 H HA   B ALA   A 1 52  ? 19.210 8.464   6.293   0.70 12.81 ?  52  ALA   A HA   1 
ATOM   1342 H HB1  A ALA   A 1 52  ? 17.779 7.014   6.674   0.30 12.60 ?  52  ALA   A HB1  1 
ATOM   1343 H HB1  B ALA   A 1 52  ? 17.805 6.729   6.987   0.70 14.17 ?  52  ALA   A HB1  1 
ATOM   1344 H HB2  A ALA   A 1 52  ? 17.611 7.259   5.113   0.30 12.60 ?  52  ALA   A HB2  1 
ATOM   1345 H HB2  B ALA   A 1 52  ? 17.605 7.022   5.438   0.70 14.17 ?  52  ALA   A HB2  1 
ATOM   1346 H HB3  A ALA   A 1 52  ? 18.418 5.995   5.637   0.30 12.60 ?  52  ALA   A HB3  1 
ATOM   1347 H HB3  B ALA   A 1 52  ? 18.464 5.769   5.905   0.70 14.17 ?  52  ALA   A HB3  1 
ATOM   1348 N N    A LEU   A 1 53  ? 21.147 6.209   6.756   0.30 9.91  ?  53  LEU   A N    1 
ATOM   1349 N N    B LEU   A 1 53  ? 21.189 6.039   7.007   0.70 10.02 ?  53  LEU   A N    1 
ATOM   1350 C CA   A LEU   A 1 53  ? 22.069 5.755   7.793   0.30 10.35 ?  53  LEU   A CA   1 
ATOM   1351 C CA   B LEU   A 1 53  ? 22.195 5.648   7.989   0.70 10.19 ?  53  LEU   A CA   1 
ATOM   1352 C C    A LEU   A 1 53  ? 23.172 6.779   8.028   0.30 10.32 ?  53  LEU   A C    1 
ATOM   1353 C C    B LEU   A 1 53  ? 23.212 6.763   8.168   0.70 10.32 ?  53  LEU   A C    1 
ATOM   1354 O O    A LEU   A 1 53  ? 23.542 7.054   9.174   0.30 10.47 ?  53  LEU   A O    1 
ATOM   1355 O O    B LEU   A 1 53  ? 23.529 7.164   9.292   0.70 11.55 ?  53  LEU   A O    1 
ATOM   1356 C CB   A LEU   A 1 53  ? 22.678 4.406   7.404   0.30 11.33 ?  53  LEU   A CB   1 
ATOM   1357 C CB   B LEU   A 1 53  ? 22.904 4.357   7.561   0.70 9.84  ?  53  LEU   A CB   1 
ATOM   1358 C CG   A LEU   A 1 53  ? 21.781 3.166   7.452   0.30 11.71 ?  53  LEU   A CG   1 
ATOM   1359 C CG   B LEU   A 1 53  ? 22.093 3.061   7.636   0.70 10.31 ?  53  LEU   A CG   1 
ATOM   1360 C CD1  A LEU   A 1 53  ? 22.515 1.966   6.877   0.30 11.91 ?  53  LEU   A CD1  1 
ATOM   1361 C CD1  B LEU   A 1 53  ? 22.855 1.945   6.943   0.70 10.84 ?  53  LEU   A CD1  1 
ATOM   1362 C CD2  A LEU   A 1 53  ? 21.334 2.882   8.875   0.30 12.11 ?  53  LEU   A CD2  1 
ATOM   1363 C CD2  B LEU   A 1 53  ? 21.794 2.675   9.072   0.70 11.07 ?  53  LEU   A CD2  1 
ATOM   1364 H H    A LEU   A 1 53  ? 21.121 5.719   6.059   0.30 11.89 ?  53  LEU   A H    1 
ATOM   1365 H H    B LEU   A 1 53  ? 21.134 5.518   6.319   0.70 12.02 ?  53  LEU   A H    1 
ATOM   1366 H HA   A LEU   A 1 53  ? 21.584 5.645   8.626   0.30 12.42 ?  53  LEU   A HA   1 
ATOM   1367 H HA   B LEU   A 1 53  ? 21.769 5.489   8.841   0.70 12.23 ?  53  LEU   A HA   1 
ATOM   1368 H HB2  A LEU   A 1 53  ? 23.004 4.482   6.495   0.30 13.60 ?  53  LEU   A HB2  1 
ATOM   1369 H HB2  B LEU   A 1 53  ? 23.196 4.460   6.638   0.70 11.81 ?  53  LEU   A HB2  1 
ATOM   1370 H HB3  A LEU   A 1 53  ? 23.424 4.235   7.996   0.30 13.60 ?  53  LEU   A HB3  1 
ATOM   1371 H HB3  B LEU   A 1 53  ? 23.686 4.236   8.124   0.70 11.81 ?  53  LEU   A HB3  1 
ATOM   1372 H HG   A LEU   A 1 53  ? 20.989 3.322   6.911   0.30 14.05 ?  53  LEU   A HG   1 
ATOM   1373 H HG   B LEU   A 1 53  ? 21.252 3.185   7.168   0.70 12.37 ?  53  LEU   A HG   1 
ATOM   1374 H HD11 A LEU   A 1 53  ? 21.933 1.190   6.916   0.30 14.29 ?  53  LEU   A HD11 1 
ATOM   1375 H HD11 B LEU   A 1 53  ? 22.333 1.127   6.999   0.70 13.01 ?  53  LEU   A HD11 1 
ATOM   1376 H HD12 A LEU   A 1 53  ? 22.755 2.153   5.956   0.30 14.29 ?  53  LEU   A HD12 1 
ATOM   1377 H HD12 B LEU   A 1 53  ? 22.992 2.184   6.012   0.70 13.01 ?  53  LEU   A HD12 1 
ATOM   1378 H HD13 A LEU   A 1 53  ? 23.315 1.805   7.402   0.30 14.29 ?  53  LEU   A HD13 1 
ATOM   1379 H HD13 B LEU   A 1 53  ? 23.708 1.824   7.384   0.70 13.01 ?  53  LEU   A HD13 1 
ATOM   1380 H HD21 A LEU   A 1 53  ? 20.810 2.068   8.884   0.30 14.54 ?  53  LEU   A HD21 1 
ATOM   1381 H HD21 B LEU   A 1 53  ? 21.275 1.859   9.076   0.70 13.28 ?  53  LEU   A HD21 1 
ATOM   1382 H HD22 A LEU   A 1 53  ? 22.120 2.777   9.434   0.30 14.54 ?  53  LEU   A HD22 1 
ATOM   1383 H HD22 B LEU   A 1 53  ? 22.631 2.543   9.541   0.70 13.28 ?  53  LEU   A HD22 1 
ATOM   1384 H HD23 A LEU   A 1 53  ? 20.799 3.625   9.193   0.30 14.54 ?  53  LEU   A HD23 1 
ATOM   1385 H HD23 B LEU   A 1 53  ? 21.290 3.392   9.490   0.70 13.28 ?  53  LEU   A HD23 1 
ATOM   1386 N N    A ASN   A 1 54  ? 23.709 7.356   6.954   0.30 10.23 ?  54  ASN   A N    1 
ATOM   1387 N N    B ASN   A 1 54  ? 23.729 7.285   7.060   0.70 9.76  ?  54  ASN   A N    1 
ATOM   1388 C CA   A ASN   A 1 54  ? 24.781 8.333   7.106   0.30 10.44 ?  54  ASN   A CA   1 
ATOM   1389 C CA   B ASN   A 1 54  ? 24.769 8.296   7.173   0.70 9.74  ?  54  ASN   A CA   1 
ATOM   1390 C C    A ASN   A 1 54  ? 24.289 9.580   7.831   0.30 10.48 ?  54  ASN   A C    1 
ATOM   1391 C C    B ASN   A 1 54  ? 24.255 9.531   7.909   0.70 10.41 ?  54  ASN   A C    1 
ATOM   1392 O O    A ASN   A 1 54  ? 25.017 10.163  8.643   0.30 10.33 ?  54  ASN   A O    1 
ATOM   1393 O O    B ASN   A 1 54  ? 24.927 10.064  8.801   0.70 10.87 ?  54  ASN   A O    1 
ATOM   1394 C CB   A ASN   A 1 54  ? 25.350 8.691   5.737   0.30 10.96 ?  54  ASN   A CB   1 
ATOM   1395 C CB   B ASN   A 1 54  ? 25.310 8.666   5.802   0.70 9.74  ?  54  ASN   A CB   1 
ATOM   1396 C CG   A ASN   A 1 54  ? 26.381 9.794   5.811   0.30 11.57 ?  54  ASN   A CG   1 
ATOM   1397 C CG   B ASN   A 1 54  ? 26.331 9.761   5.899   0.70 9.69  ?  54  ASN   A CG   1 
ATOM   1398 O OD1  A ASN   A 1 54  ? 27.448 9.618   6.400   0.30 12.32 ?  54  ASN   A OD1  1 
ATOM   1399 O OD1  B ASN   A 1 54  ? 27.314 9.619   6.629   0.70 9.61  ?  54  ASN   A OD1  1 
ATOM   1400 N ND2  A ASN   A 1 54  ? 26.071 10.941  5.219   0.30 11.88 ?  54  ASN   A ND2  1 
ATOM   1401 N ND2  B ASN   A 1 54  ? 26.089 10.877  5.229   0.70 10.79 ?  54  ASN   A ND2  1 
ATOM   1402 H H    A ASN   A 1 54  ? 23.468 7.209   6.148   0.30 12.27 ?  54  ASN   A H    1 
ATOM   1403 H H    B ASN   A 1 54  ? 23.497 7.079   6.256   0.70 11.71 ?  54  ASN   A H    1 
ATOM   1404 H HA   A ASN   A 1 54  ? 25.490 7.946   7.639   0.30 12.53 ?  54  ASN   A HA   1 
ATOM   1405 H HA   B ASN   A 1 54  ? 25.497 7.927   7.692   0.70 11.69 ?  54  ASN   A HA   1 
ATOM   1406 H HB2  A ASN   A 1 54  ? 25.773 7.903   5.361   0.30 13.15 ?  54  ASN   A HB2  1 
ATOM   1407 H HB2  B ASN   A 1 54  ? 25.732 7.880   5.408   0.70 11.69 ?  54  ASN   A HB2  1 
ATOM   1408 H HB3  A ASN   A 1 54  ? 24.627 8.987   5.163   0.30 13.15 ?  54  ASN   A HB3  1 
ATOM   1409 H HB3  B ASN   A 1 54  ? 24.582 8.969   5.241   0.70 11.69 ?  54  ASN   A HB3  1 
ATOM   1410 H HD21 A ASN   A 1 54  ? 26.628 11.595  5.235   0.30 14.26 ?  54  ASN   A HD21 1 
ATOM   1411 H HD21 B ASN   A 1 54  ? 26.652 11.524  5.264   0.70 12.95 ?  54  ASN   A HD21 1 
ATOM   1412 H HD22 A ASN   A 1 54  ? 25.316 11.027  4.816   0.30 14.26 ?  54  ASN   A HD22 1 
ATOM   1413 H HD22 B ASN   A 1 54  ? 25.383 10.941  4.747   0.70 12.95 ?  54  ASN   A HD22 1 
ATOM   1414 N N    . LYS   A 1 55  ? 23.056 10.002  7.547   1.00 10.84 ?  55  LYS   A N    1 
ATOM   1415 C CA   . LYS   A 1 55  ? 22.480 11.158  8.228   1.00 11.81 ?  55  LYS   A CA   1 
ATOM   1416 C C    . LYS   A 1 55  ? 22.394 10.912  9.727   1.00 11.96 ?  55  LYS   A C    1 
ATOM   1417 O O    . LYS   A 1 55  ? 22.682 11.807  10.534  1.00 12.56 ?  55  LYS   A O    1 
ATOM   1418 C CB   . LYS   A 1 55  ? 21.106 11.467  7.619   1.00 13.86 ?  55  LYS   A CB   1 
ATOM   1419 C CG   . LYS   A 1 55  ? 20.345 12.629  8.240   1.00 16.34 ?  55  LYS   A CG   1 
ATOM   1420 C CD   . LYS   A 1 55  ? 19.083 12.954  7.419   1.00 19.97 ?  55  LYS   A CD   1 
ATOM   1421 C CE   . LYS   A 1 55  ? 18.263 14.065  8.050   1.00 23.03 ?  55  LYS   A CE   1 
ATOM   1422 N NZ   . LYS   A 1 55  ? 16.933 14.214  7.392   1.00 24.87 ?  55  LYS   A NZ   1 
ATOM   1423 H H    A LYS   A 1 55  ? 22.531 9.637   6.968   0.30 13.01 ?  55  LYS   A H    1 
ATOM   1424 H H    B LYS   A 1 55  ? 22.559 9.674   6.924   0.70 13.01 ?  55  LYS   A H    1 
ATOM   1425 H HA   . LYS   A 1 55  ? 23.049 11.930  8.085   1.00 14.17 ?  55  LYS   A HA   1 
ATOM   1426 H HB2  . LYS   A 1 55  ? 21.227 11.679  6.680   1.00 16.64 ?  55  LYS   A HB2  1 
ATOM   1427 H HB3  . LYS   A 1 55  ? 20.547 10.682  7.703   1.00 16.64 ?  55  LYS   A HB3  1 
ATOM   1428 H HG2  . LYS   A 1 55  ? 20.064 12.388  9.137   1.00 19.60 ?  55  LYS   A HG2  1 
ATOM   1429 H HG3  . LYS   A 1 55  ? 20.907 13.415  8.258   1.00 19.60 ?  55  LYS   A HG3  1 
ATOM   1430 H HD2  . LYS   A 1 55  ? 19.353 13.238  6.528   1.00 23.96 ?  55  LYS   A HD2  1 
ATOM   1431 H HD3  . LYS   A 1 55  ? 18.530 12.159  7.357   1.00 23.96 ?  55  LYS   A HD3  1 
ATOM   1432 H HE2  . LYS   A 1 55  ? 18.119 13.861  8.986   1.00 27.64 ?  55  LYS   A HE2  1 
ATOM   1433 H HE3  . LYS   A 1 55  ? 18.743 14.905  7.960   1.00 27.64 ?  55  LYS   A HE3  1 
ATOM   1434 H HZ1  . LYS   A 1 55  ? 16.385 14.679  7.917   1.00 29.84 ?  55  LYS   A HZ1  1 
ATOM   1435 H HZ2  . LYS   A 1 55  ? 17.021 14.644  6.617   1.00 29.84 ?  55  LYS   A HZ2  1 
ATOM   1436 H HZ3  . LYS   A 1 55  ? 16.575 13.413  7.241   1.00 29.84 ?  55  LYS   A HZ3  1 
ATOM   1437 N N    . ALA   A 1 56  ? 22.003 9.697   10.121  1.00 12.41 ?  56  ALA   A N    1 
ATOM   1438 C CA   . ALA   A 1 56  ? 21.896 9.367   11.535  1.00 12.95 ?  56  ALA   A CA   1 
ATOM   1439 C C    . ALA   A 1 56  ? 23.244 9.380   12.249  1.00 12.59 ?  56  ALA   A C    1 
ATOM   1440 O O    . ALA   A 1 56  ? 23.273 9.546   13.472  1.00 14.26 ?  56  ALA   A O    1 
ATOM   1441 C CB   . ALA   A 1 56  ? 21.187 8.018   11.714  1.00 13.94 ?  56  ALA   A CB   1 
ATOM   1442 H H    . ALA   A 1 56  ? 21.792 9.056   9.585   1.00 14.89 ?  56  ALA   A H    1 
ATOM   1443 H HA   . ALA   A 1 56  ? 21.345 10.032  11.961  1.00 15.54 ?  56  ALA   A HA   1 
ATOM   1444 H HB1  . ALA   A 1 56  ? 21.134 7.814   12.663  1.00 16.72 ?  56  ALA   A HB1  1 
ATOM   1445 H HB2  . ALA   A 1 56  ? 20.294 8.078   11.341  1.00 16.72 ?  56  ALA   A HB2  1 
ATOM   1446 H HB3  . ALA   A 1 56  ? 21.691 7.327   11.257  1.00 16.72 ?  56  ALA   A HB3  1 
ATOM   1447 N N    . THR   A 1 57  ? 24.354 9.213   11.522  1.00 11.85 ?  57  THR   A N    1 
ATOM   1448 C CA   . THR   A 1 57  ? 25.697 9.334   12.095  1.00 12.06 ?  57  THR   A CA   1 
ATOM   1449 C C    . THR   A 1 57  ? 26.250 10.750  12.017  1.00 12.20 ?  57  THR   A C    1 
ATOM   1450 O O    . THR   A 1 57  ? 27.442 10.961  12.296  1.00 12.60 ?  57  THR   A O    1 
ATOM   1451 C CB   . THR   A 1 57  ? 26.701 8.383   11.416  1.00 11.75 ?  57  THR   A CB   1 
ATOM   1452 O OG1  . THR   A 1 57  ? 27.070 8.877   10.116  1.00 11.04 ?  57  THR   A OG1  1 
ATOM   1453 C CG2  . THR   A 1 57  ? 26.167 6.961   11.316  1.00 11.91 ?  57  THR   A CG2  1 
ATOM   1454 H H    . THR   A 1 57  ? 24.355 9.016   10.679  1.00 14.22 ?  57  THR   A H    1 
ATOM   1455 H HA   . THR   A 1 57  ? 25.650 9.077   13.032  1.00 14.48 ?  57  THR   A HA   1 
ATOM   1456 H HB   . THR   A 1 57  ? 27.500 8.339   11.968  1.00 14.10 ?  57  THR   A HB   1 
ATOM   1457 H HG1  . THR   A 1 57  ? 26.387 8.936   9.634   1.00 13.25 ?  57  THR   A HG1  1 
ATOM   1458 H HG21 . THR   A 1 57  ? 26.840 6.373   10.933  1.00 14.29 ?  57  THR   A HG21 1 
ATOM   1459 H HG22 . THR   A 1 57  ? 25.929 6.626   12.197  1.00 14.29 ?  57  THR   A HG22 1 
ATOM   1460 H HG23 . THR   A 1 57  ? 25.378 6.936   10.753  1.00 14.29 ?  57  THR   A HG23 1 
ATOM   1461 N N    . ASN   A 1 58  ? 25.427 11.721  11.630  1.00 12.69 ?  58  ASN   A N    1 
ATOM   1462 C CA   . ASN   A 1 58  ? 25.887 13.100  11.535  1.00 13.73 ?  58  ASN   A CA   1 
ATOM   1463 C C    . ASN   A 1 58  ? 27.018 13.235  10.512  1.00 12.43 ?  58  ASN   A C    1 
ATOM   1464 O O    . ASN   A 1 58  ? 27.913 14.066  10.671  1.00 13.09 ?  58  ASN   A O    1 
ATOM   1465 C CB   . ASN   A 1 58  ? 26.297 13.626  12.926  1.00 16.08 ?  58  ASN   A CB   1 
ATOM   1466 C CG   . ASN   A 1 58  ? 26.681 15.091  12.929  1.00 19.31 ?  58  ASN   A CG   1 
ATOM   1467 O OD1  . ASN   A 1 58  ? 26.027 15.909  12.289  1.00 20.78 ?  58  ASN   A OD1  1 
ATOM   1468 N ND2  . ASN   A 1 58  ? 27.738 15.435  13.675  1.00 20.26 ?  58  ASN   A ND2  1 
ATOM   1469 H H    . ASN   A 1 58  ? 24.606 11.599  11.403  1.00 15.23 ?  58  ASN   A H    1 
ATOM   1470 H HA   . ASN   A 1 58  ? 25.145 13.642  11.228  1.00 16.48 ?  58  ASN   A HA   1 
ATOM   1471 H HB2  . ASN   A 1 58  ? 25.547 13.509  13.539  1.00 19.29 ?  58  ASN   A HB2  1 
ATOM   1472 H HB3  . ASN   A 1 58  ? 27.058 13.125  13.247  1.00 19.29 ?  58  ASN   A HB3  1 
ATOM   1473 H HD21 . ASN   A 1 58  ? 27.988 16.257  13.712  1.00 24.31 ?  58  ASN   A HD21 1 
ATOM   1474 H HD22 . ASN   A 1 58  ? 28.165 14.832  14.110  1.00 24.31 ?  58  ASN   A HD22 1 
ATOM   1475 N N    . ASN   A 1 59  ? 26.991 12.423  9.452   1.00 11.52 ?  59  ASN   A N    1 
ATOM   1476 C CA   . ASN   A 1 59  ? 27.965 12.408  8.353   1.00 11.12 ?  59  ASN   A CA   1 
ATOM   1477 C C    . ASN   A 1 59  ? 29.284 11.725  8.722   1.00 10.31 ?  59  ASN   A C    1 
ATOM   1478 O O    . ASN   A 1 59  ? 30.197 11.688  7.887   1.00 10.70 ?  59  ASN   A O    1 
ATOM   1479 C CB   . ASN   A 1 59  ? 28.249 13.797  7.754   1.00 11.42 ?  59  ASN   A CB   1 
ATOM   1480 C CG   . ASN   A 1 59  ? 28.597 13.742  6.282   1.00 11.46 ?  59  ASN   A CG   1 
ATOM   1481 O OD1  . ASN   A 1 59  ? 27.890 13.122  5.486   1.00 11.72 ?  59  ASN   A OD1  1 
ATOM   1482 N ND2  . ASN   A 1 59  ? 29.683 14.412  5.903   1.00 12.14 ?  59  ASN   A ND2  1 
ATOM   1483 H H    . ASN   A 1 59  ? 26.376 11.833  9.342   1.00 13.83 ?  59  ASN   A H    1 
ATOM   1484 H HA   . ASN   A 1 59  ? 27.576 11.884  7.638   1.00 13.34 ?  59  ASN   A HA   1 
ATOM   1485 H HB2  . ASN   A 1 59  ? 27.465 14.356  7.845   1.00 13.71 ?  59  ASN   A HB2  1 
ATOM   1486 H HB3  . ASN   A 1 59  ? 29.002 14.198  8.216   1.00 13.71 ?  59  ASN   A HB3  1 
ATOM   1487 H HD21 . ASN   A 1 59  ? 29.927 14.419  5.075   1.00 14.56 ?  59  ASN   A HD21 1 
ATOM   1488 H HD22 . ASN   A 1 59  ? 30.153 14.844  6.485   1.00 14.56 ?  59  ASN   A HD22 1 
ATOM   1489 N N    . ALA   A 1 60  ? 29.416 11.178  9.928   1.00 10.85 ?  60  ALA   A N    1 
ATOM   1490 C CA   . ALA   A 1 60  ? 30.656 10.493  10.277  1.00 10.70 ?  60  ALA   A CA   1 
ATOM   1491 C C    . ALA   A 1 60  ? 30.885 9.266   9.396   1.00 11.05 ?  60  ALA   A C    1 
ATOM   1492 O O    . ALA   A 1 60  ? 32.032 8.952   9.047   1.00 11.20 ?  60  ALA   A O    1 
ATOM   1493 C CB   . ALA   A 1 60  ? 30.654 10.123  11.756  1.00 11.73 ?  60  ALA   A CB   1 
ATOM   1494 H H    . ALA   A 1 60  ? 28.816 11.186  10.544  1.00 13.02 ?  60  ALA   A H    1 
ATOM   1495 H HA   . ALA   A 1 60  ? 31.392 11.103  10.125  1.00 12.84 ?  60  ALA   A HA   1 
ATOM   1496 H HB1  . ALA   A 1 60  ? 31.482 9.673   11.971  1.00 14.08 ?  60  ALA   A HB1  1 
ATOM   1497 H HB2  . ALA   A 1 60  ? 30.572 10.937  12.284  1.00 14.08 ?  60  ALA   A HB2  1 
ATOM   1498 H HB3  . ALA   A 1 60  ? 29.899 9.540   11.937  1.00 14.08 ?  60  ALA   A HB3  1 
ATOM   1499 N N    . MET   A 1 61  ? 29.810 8.561   9.022   1.00 10.49 ?  61  MET   A N    1 
ATOM   1500 C CA   . MET   A 1 61  ? 29.945 7.430   8.108   1.00 10.39 ?  61  MET   A CA   1 
ATOM   1501 C C    . MET   A 1 61  ? 30.567 7.869   6.780   1.00 9.93  ?  61  MET   A C    1 
ATOM   1502 O O    . MET   A 1 61  ? 31.454 7.192   6.240   1.00 10.51 ?  61  MET   A O    1 
ATOM   1503 C CB   . MET   A 1 61  ? 28.576 6.771   7.901   1.00 10.38 ?  61  MET   A CB   1 
ATOM   1504 C CG   . MET   A 1 61  ? 28.583 5.627   6.911   1.00 10.51 ?  61  MET   A CG   1 
ATOM   1505 S SD   . MET   A 1 61  ? 26.961 4.862   6.733   1.00 11.69 ?  61  MET   A SD   1 
ATOM   1506 C CE   . MET   A 1 61  ? 26.870 3.946   8.279   1.00 13.17 ?  61  MET   A CE   1 
ATOM   1507 H H    . MET   A 1 61  ? 29.004 8.718   9.278   1.00 12.59 ?  61  MET   A H    1 
ATOM   1508 H HA   . MET   A 1 61  ? 30.526 6.773   8.516   1.00 12.46 ?  61  MET   A HA   1 
ATOM   1509 H HB2  . MET   A 1 61  ? 28.268 6.419   8.751   1.00 12.46 ?  61  MET   A HB2  1 
ATOM   1510 H HB3  . MET   A 1 61  ? 27.950 7.436   7.577   1.00 12.46 ?  61  MET   A HB3  1 
ATOM   1511 H HG2  . MET   A 1 61  ? 28.842 5.959   6.037   1.00 12.62 ?  61  MET   A HG2  1 
ATOM   1512 H HG3  . MET   A 1 61  ? 29.202 4.947   7.210   1.00 12.62 ?  61  MET   A HG3  1 
ATOM   1513 H HE1  . MET   A 1 61  ? 26.042 3.444   8.304   1.00 15.80 ?  61  MET   A HE1  1 
ATOM   1514 H HE2  . MET   A 1 61  ? 27.627 3.338   8.329   1.00 15.80 ?  61  MET   A HE2  1 
ATOM   1515 H HE3  . MET   A 1 61  ? 26.902 4.570   9.022   1.00 15.80 ?  61  MET   A HE3  1 
ATOM   1516 N N    . GLN   A 1 62  ? 30.110 8.996   6.231   1.00 10.08 ?  62  GLN   A N    1 
ATOM   1517 C CA   . GLN   A 1 62  ? 30.662 9.476   4.967   1.00 10.29 ?  62  GLN   A CA   1 
ATOM   1518 C C    . GLN   A 1 62  ? 32.133 9.856   5.104   1.00 10.37 ?  62  GLN   A C    1 
ATOM   1519 O O    . GLN   A 1 62  ? 32.937 9.554   4.216   1.00 10.87 ?  62  GLN   A O    1 
ATOM   1520 C CB   . GLN   A 1 62  ? 29.853 10.663  4.442   1.00 10.46 ?  62  GLN   A CB   1 
ATOM   1521 C CG   . GLN   A 1 62  ? 30.213 11.039  3.018   1.00 10.60 ?  62  GLN   A CG   1 
ATOM   1522 C CD   . GLN   A 1 62  ? 29.877 9.913   2.066   1.00 10.68 ?  62  GLN   A CD   1 
ATOM   1523 O OE1  . GLN   A 1 62  ? 28.700 9.619   1.846   1.00 11.34 ?  62  GLN   A OE1  1 
ATOM   1524 N NE2  . GLN   A 1 62  ? 30.891 9.238   1.541   1.00 11.30 ?  62  GLN   A NE2  1 
ATOM   1525 H H    . GLN   A 1 62  ? 29.493 9.493   6.567   1.00 12.10 ?  62  GLN   A H    1 
ATOM   1526 H HA   . GLN   A 1 62  ? 30.602 8.755   4.317   1.00 12.35 ?  62  GLN   A HA   1 
ATOM   1527 H HB2  . GLN   A 1 62  ? 28.913 10.440  4.466   1.00 12.56 ?  62  GLN   A HB2  1 
ATOM   1528 H HB3  . GLN   A 1 62  ? 30.030 11.433  5.006   1.00 12.56 ?  62  GLN   A HB3  1 
ATOM   1529 H HG2  . GLN   A 1 62  ? 29.699 11.820  2.755   1.00 12.73 ?  62  GLN   A HG2  1 
ATOM   1530 H HG3  . GLN   A 1 62  ? 31.161 11.222  2.956   1.00 12.73 ?  62  GLN   A HG3  1 
ATOM   1531 H HE21 . GLN   A 1 62  ? 31.698 9.464   1.732   1.00 13.56 ?  62  GLN   A HE21 1 
ATOM   1532 H HE22 . GLN   A 1 62  ? 30.740 8.584   1.006   1.00 13.56 ?  62  GLN   A HE22 1 
ATOM   1533 N N    . VAL   A 1 63  ? 32.500 10.536  6.194   1.00 10.99 ?  63  VAL   A N    1 
ATOM   1534 C CA   . VAL   A 1 63  ? 33.894 10.930  6.399   1.00 11.98 ?  63  VAL   A CA   1 
ATOM   1535 C C    . VAL   A 1 63  ? 34.793 9.698   6.448   1.00 11.22 ?  63  VAL   A C    1 
ATOM   1536 O O    . VAL   A 1 63  ? 35.843 9.641   5.790   1.00 11.70 ?  63  VAL   A O    1 
ATOM   1537 C CB   . VAL   A 1 63  ? 34.009 11.796  7.665   1.00 13.55 ?  63  VAL   A CB   1 
ATOM   1538 C CG1  . VAL   A 1 63  ? 35.462 12.027  8.024   1.00 15.37 ?  63  VAL   A CG1  1 
ATOM   1539 C CG2  . VAL   A 1 63  ? 33.292 13.136  7.460   1.00 13.91 ?  63  VAL   A CG2  1 
ATOM   1540 H H    . VAL   A 1 63  ? 31.960 10.780  6.817   1.00 13.19 ?  63  VAL   A H    1 
ATOM   1541 H HA   . VAL   A 1 63  ? 34.172 11.470  5.646   1.00 14.38 ?  63  VAL   A HA   1 
ATOM   1542 H HB   . VAL   A 1 63  ? 33.587 11.339  8.406   1.00 16.27 ?  63  VAL   A HB   1 
ATOM   1543 H HG11 . VAL   A 1 63  ? 35.515 12.759  8.656   1.00 18.44 ?  63  VAL   A HG11 1 
ATOM   1544 H HG12 . VAL   A 1 63  ? 35.821 11.220  8.420   1.00 18.44 ?  63  VAL   A HG12 1 
ATOM   1545 H HG13 . VAL   A 1 63  ? 35.952 12.251  7.217   1.00 18.44 ?  63  VAL   A HG13 1 
ATOM   1546 H HG21 . VAL   A 1 63  ? 33.386 13.673  8.267   1.00 16.69 ?  63  VAL   A HG21 1 
ATOM   1547 H HG22 . VAL   A 1 63  ? 33.697 13.604  6.710   1.00 16.69 ?  63  VAL   A HG22 1 
ATOM   1548 H HG23 . VAL   A 1 63  ? 32.355 12.973  7.281   1.00 16.69 ?  63  VAL   A HG23 1 
ATOM   1549 N N    . GLU   A 1 64  ? 34.383 8.684   7.217   1.00 11.25 ?  64  GLU   A N    1 
ATOM   1550 C CA   . GLU   A 1 64  ? 35.149 7.448   7.300   1.00 11.04 ?  64  GLU   A CA   1 
ATOM   1551 C C    . GLU   A 1 64  ? 35.227 6.769   5.941   1.00 10.66 ?  64  GLU   A C    1 
ATOM   1552 O O    . GLU   A 1 64  ? 36.274 6.230   5.556   1.00 11.25 ?  64  GLU   A O    1 
ATOM   1553 C CB   . GLU   A 1 64  ? 34.468 6.533   8.313   1.00 11.70 ?  64  GLU   A CB   1 
ATOM   1554 C CG   . GLU   A 1 64  ? 35.126 5.194   8.465   1.00 12.41 ?  64  GLU   A CG   1 
ATOM   1555 C CD   . GLU   A 1 64  ? 34.257 4.197   9.195   1.00 12.72 ?  64  GLU   A CD   1 
ATOM   1556 O OE1  . GLU   A 1 64  ? 33.016 4.290   9.073   1.00 13.44 ?  64  GLU   A OE1  1 
ATOM   1557 O OE2  . GLU   A 1 64  ? 34.819 3.309   9.875   1.00 13.39 -1 64  GLU   A OE2  1 
ATOM   1558 H H    . GLU   A 1 64  ? 33.666 8.688   7.687   1.00 13.50 ?  64  GLU   A H    1 
ATOM   1559 H HA   . GLU   A 1 64  ? 36.051 7.642   7.606   1.00 13.25 ?  64  GLU   A HA   1 
ATOM   1560 H HB2  . GLU   A 1 64  ? 34.484 6.971   9.181   1.00 14.04 ?  64  GLU   A HB2  1 
ATOM   1561 H HB3  . GLU   A 1 64  ? 33.552 6.396   8.032   1.00 14.04 ?  64  GLU   A HB3  1 
ATOM   1562 H HG2  . GLU   A 1 64  ? 35.319 4.826   7.584   1.00 14.89 ?  64  GLU   A HG2  1 
ATOM   1563 H HG3  . GLU   A 1 64  ? 35.946 5.301   8.962   1.00 14.89 ?  64  GLU   A HG3  1 
ATOM   1564 N N    . SER   A 1 65  ? 34.103 6.759   5.220   1.00 10.63 ?  65  SER   A N    1 
ATOM   1565 C CA   . SER   A 1 65  ? 34.039 6.111   3.918   1.00 10.60 ?  65  SER   A CA   1 
ATOM   1566 C C    . SER   A 1 65  ? 34.960 6.783   2.909   1.00 10.77 ?  65  SER   A C    1 
ATOM   1567 O O    . SER   A 1 65  ? 35.594 6.107   2.092   1.00 11.35 ?  65  SER   A O    1 
ATOM   1568 C CB   . SER   A 1 65  ? 32.599 6.135   3.403   1.00 10.61 ?  65  SER   A CB   1 
ATOM   1569 O OG   . SER   A 1 65  ? 31.748 5.300   4.184   1.00 11.00 ?  65  SER   A OG   1 
ATOM   1570 H H    . SER   A 1 65  ? 33.368 7.126   5.466   1.00 12.76 ?  65  SER   A H    1 
ATOM   1571 H HA   . SER   A 1 65  ? 34.316 5.186   4.005   1.00 12.72 ?  65  SER   A HA   1 
ATOM   1572 H HB2  . SER   A 1 65  ? 32.265 7.043   3.447   1.00 12.73 ?  65  SER   A HB2  1 
ATOM   1573 H HB3  . SER   A 1 65  ? 32.590 5.823   2.488   1.00 12.73 ?  65  SER   A HB3  1 
ATOM   1574 H HG   . SER   A 1 65  ? 31.754 5.561   4.987   1.00 13.19 ?  65  SER   A HG   1 
ATOM   1575 N N    . ASP   A 1 66  ? 35.026 8.117   2.927   1.00 10.87 ?  66  ASP   A N    1 
ATOM   1576 C CA   . ASP   A 1 66  ? 35.885 8.819   1.981   1.00 11.54 ?  66  ASP   A CA   1 
ATOM   1577 C C    . ASP   A 1 66  ? 37.351 8.464   2.213   1.00 11.64 ?  66  ASP   A C    1 
ATOM   1578 O O    . ASP   A 1 66  ? 38.119 8.299   1.257   1.00 12.51 ?  66  ASP   A O    1 
ATOM   1579 C CB   . ASP   A 1 66  ? 35.659 10.322  2.100   1.00 12.80 ?  66  ASP   A CB   1 
ATOM   1580 C CG   . ASP   A 1 66  ? 34.316 10.784  1.508   1.00 14.53 ?  66  ASP   A CG   1 
ATOM   1581 O OD1  . ASP   A 1 66  ? 33.599 9.995   0.853   1.00 14.89 ?  66  ASP   A OD1  1 
ATOM   1582 O OD2  . ASP   A 1 66  ? 34.006 11.979  1.683   1.00 17.48 -1 66  ASP   A OD2  1 
ATOM   1583 H H    . ASP   A 1 66  ? 34.589 8.628   3.468   1.00 13.04 ?  66  ASP   A H    1 
ATOM   1584 H HA   . ASP   A 1 66  ? 35.644 8.551   1.081   1.00 13.85 ?  66  ASP   A HA   1 
ATOM   1585 H HB2  . ASP   A 1 66  ? 35.670 10.572  3.038   1.00 15.36 ?  66  ASP   A HB2  1 
ATOM   1586 H HB3  . ASP   A 1 66  ? 36.368 10.786  1.627   1.00 15.36 ?  66  ASP   A HB3  1 
ATOM   1587 N N    . ASP   A 1 67  ? 37.757 8.337   3.476   1.00 12.06 ?  67  ASP   A N    1 
ATOM   1588 C CA   . ASP   A 1 67  ? 39.110 7.884   3.768   1.00 12.88 ?  67  ASP   A CA   1 
ATOM   1589 C C    . ASP   A 1 67  ? 39.330 6.457   3.277   1.00 12.68 ?  67  ASP   A C    1 
ATOM   1590 O O    . ASP   A 1 67  ? 40.391 6.143   2.722   1.00 13.38 ?  67  ASP   A O    1 
ATOM   1591 C CB   . ASP   A 1 67  ? 39.386 8.010   5.267   1.00 14.28 ?  67  ASP   A CB   1 
ATOM   1592 C CG   . ASP   A 1 67  ? 40.687 7.353   5.679   1.00 15.45 ?  67  ASP   A CG   1 
ATOM   1593 O OD1  . ASP   A 1 67  ? 41.759 7.988   5.535   1.00 18.17 ?  67  ASP   A OD1  1 
ATOM   1594 O OD2  . ASP   A 1 67  ? 40.635 6.190   6.138   1.00 15.34 -1 67  ASP   A OD2  1 
ATOM   1595 H H    . ASP   A 1 67  ? 37.276 8.504   4.166   1.00 14.47 ?  67  ASP   A H    1 
ATOM   1596 H HA   . ASP   A 1 67  ? 39.738 8.453   3.300   1.00 15.46 ?  67  ASP   A HA   1 
ATOM   1597 H HB2  . ASP   A 1 67  ? 39.442 8.945   5.494   1.00 17.14 ?  67  ASP   A HB2  1 
ATOM   1598 H HB3  . ASP   A 1 67  ? 38.663 7.585   5.756   1.00 17.14 ?  67  ASP   A HB3  1 
ATOM   1599 N N    A TYR   A 1 68  ? 38.336 5.582   3.454   0.30 12.05 ?  68  TYR   A N    1 
ATOM   1600 N N    B TYR   A 1 68  ? 38.339 5.573   3.475   0.70 12.36 ?  68  TYR   A N    1 
ATOM   1601 C CA   A TYR   A 1 68  ? 38.485 4.208   2.988   0.30 11.72 ?  68  TYR   A CA   1 
ATOM   1602 C CA   B TYR   A 1 68  ? 38.454 4.196   2.987   0.70 12.45 ?  68  TYR   A CA   1 
ATOM   1603 C C    A TYR   A 1 68  ? 38.697 4.153   1.479   0.30 11.61 ?  68  TYR   A C    1 
ATOM   1604 C C    B TYR   A 1 68  ? 38.708 4.166   1.484   0.70 12.26 ?  68  TYR   A C    1 
ATOM   1605 O O    A TYR   A 1 68  ? 39.558 3.410   0.993   0.30 11.64 ?  68  TYR   A O    1 
ATOM   1606 O O    B TYR   A 1 68  ? 39.594 3.448   1.006   0.70 12.74 ?  68  TYR   A O    1 
ATOM   1607 C CB   A TYR   A 1 68  ? 37.267 3.370   3.389   0.30 11.76 ?  68  TYR   A CB   1 
ATOM   1608 C CB   B TYR   A 1 68  ? 37.190 3.374   3.327   0.70 12.81 ?  68  TYR   A CB   1 
ATOM   1609 C CG   A TYR   A 1 68  ? 37.350 1.961   2.854   0.30 12.25 ?  68  TYR   A CG   1 
ATOM   1610 C CG   B TYR   A 1 68  ? 37.207 2.004   2.651   0.70 13.55 ?  68  TYR   A CG   1 
ATOM   1611 C CD1  A TYR   A 1 68  ? 36.834 1.646   1.605   0.30 12.81 ?  68  TYR   A CD1  1 
ATOM   1612 C CD1  B TYR   A 1 68  ? 36.764 1.856   1.337   0.70 14.33 ?  68  TYR   A CD1  1 
ATOM   1613 C CD2  A TYR   A 1 68  ? 37.983 0.960   3.574   0.30 13.41 ?  68  TYR   A CD2  1 
ATOM   1614 C CD2  B TYR   A 1 68  ? 37.714 0.886   3.300   0.70 14.34 ?  68  TYR   A CD2  1 
ATOM   1615 C CE1  A TYR   A 1 68  ? 36.930 0.375   1.091   0.30 13.92 ?  68  TYR   A CE1  1 
ATOM   1616 C CE1  B TYR   A 1 68  ? 36.825 0.643   0.691   0.70 14.32 ?  68  TYR   A CE1  1 
ATOM   1617 C CE2  A TYR   A 1 68  ? 38.080 -0.325  3.069   0.30 14.01 ?  68  TYR   A CE2  1 
ATOM   1618 C CE2  B TYR   A 1 68  ? 37.771 -0.351  2.659   0.70 13.75 ?  68  TYR   A CE2  1 
ATOM   1619 C CZ   A TYR   A 1 68  ? 37.555 -0.607  1.826   0.30 14.63 ?  68  TYR   A CZ   1 
ATOM   1620 C CZ   B TYR   A 1 68  ? 37.337 -0.449  1.355   0.70 13.95 ?  68  TYR   A CZ   1 
ATOM   1621 O OH   A TYR   A 1 68  ? 37.655 -1.872  1.305   0.30 16.20 ?  68  TYR   A OH   1 
ATOM   1622 O OH   B TYR   A 1 68  ? 37.410 -1.658  0.719   0.70 14.86 ?  68  TYR   A OH   1 
ATOM   1623 H H    A TYR   A 1 68  ? 37.582 5.754   3.831   0.30 14.46 ?  68  TYR   A H    1 
ATOM   1624 H H    B TYR   A 1 68  ? 37.599 5.742   3.882   0.70 14.83 ?  68  TYR   A H    1 
ATOM   1625 H HA   A TYR   A 1 68  ? 39.261 3.814   3.409   0.30 14.06 ?  68  TYR   A HA   1 
ATOM   1626 H HA   B TYR   A 1 68  ? 39.205 3.769   3.420   0.70 14.94 ?  68  TYR   A HA   1 
ATOM   1627 H HB2  A TYR   A 1 68  ? 37.218 3.323   4.356   0.30 14.11 ?  68  TYR   A HB2  1 
ATOM   1628 H HB2  B TYR   A 1 68  ? 37.146 3.236   4.284   0.70 15.37 ?  68  TYR   A HB2  1 
ATOM   1629 H HB3  A TYR   A 1 68  ? 36.463 3.782   3.032   0.30 14.11 ?  68  TYR   A HB3  1 
ATOM   1630 H HB3  B TYR   A 1 68  ? 36.402 3.853   3.020   0.70 15.37 ?  68  TYR   A HB3  1 
ATOM   1631 H HD1  A TYR   A 1 68  ? 36.413 2.310   1.104   0.30 15.37 ?  68  TYR   A HD1  1 
ATOM   1632 H HD1  B TYR   A 1 68  ? 36.425 2.594   0.882   0.70 17.19 ?  68  TYR   A HD1  1 
ATOM   1633 H HD2  A TYR   A 1 68  ? 38.344 1.152   4.407   0.30 16.09 ?  68  TYR   A HD2  1 
ATOM   1634 H HD2  B TYR   A 1 68  ? 38.032 0.967   4.166   0.70 17.21 ?  68  TYR   A HD2  1 
ATOM   1635 H HE1  A TYR   A 1 68  ? 36.569 0.182   0.253   0.30 16.70 ?  68  TYR   A HE1  1 
ATOM   1636 H HE1  B TYR   A 1 68  ? 36.513 0.549   -0.183  0.70 17.19 ?  68  TYR   A HE1  1 
ATOM   1637 H HE2  A TYR   A 1 68  ? 38.504 -0.993  3.556   0.30 16.81 ?  68  TYR   A HE2  1 
ATOM   1638 H HE2  B TYR   A 1 68  ? 38.122 -1.095  3.095   0.70 16.50 ?  68  TYR   A HE2  1 
ATOM   1639 H HH   A TYR   A 1 68  ? 38.044 -2.380  1.841   0.30 19.44 ?  68  TYR   A HH   1 
ATOM   1640 H HH   B TYR   A 1 68  ? 37.733 -2.246  1.245   0.70 17.83 ?  68  TYR   A HH   1 
ATOM   1641 N N    . ILE   A 1 69  ? 37.912 4.923   0.720   1.00 11.58 ?  69  ILE   A N    1 
ATOM   1642 C CA   . ILE   A 1 69  ? 38.045 4.921   -0.736  1.00 11.63 ?  69  ILE   A CA   1 
ATOM   1643 C C    . ILE   A 1 69  ? 39.374 5.535   -1.162  1.00 11.58 ?  69  ILE   A C    1 
ATOM   1644 O O    . ILE   A 1 69  ? 40.020 5.057   -2.102  1.00 11.95 ?  69  ILE   A O    1 
ATOM   1645 C CB   . ILE   A 1 69  ? 36.844 5.634   -1.388  1.00 12.78 ?  69  ILE   A CB   1 
ATOM   1646 C CG1  . ILE   A 1 69  ? 35.538 4.889   -1.101  1.00 13.15 ?  69  ILE   A CG1  1 
ATOM   1647 C CG2  . ILE   A 1 69  ? 37.061 5.827   -2.896  1.00 14.51 ?  69  ILE   A CG2  1 
ATOM   1648 C CD1  . ILE   A 1 69  ? 35.367 3.608   -1.870  1.00 13.84 ?  69  ILE   A CD1  1 
ATOM   1649 H H    A ILE   A 1 69  ? 37.302 5.450   1.021   0.30 13.90 ?  69  ILE   A H    1 
ATOM   1650 H H    B ILE   A 1 69  ? 37.298 5.447   1.019   0.70 13.90 ?  69  ILE   A H    1 
ATOM   1651 H HA   . ILE   A 1 69  ? 38.041 4.003   -1.044  1.00 13.95 ?  69  ILE   A HA   1 
ATOM   1652 H HB   . ILE   A 1 69  ? 36.773 6.512   -0.987  1.00 15.34 ?  69  ILE   A HB   1 
ATOM   1653 H HG12 . ILE   A 1 69  ? 35.509 4.669   -0.154  1.00 15.77 ?  69  ILE   A HG12 1 
ATOM   1654 H HG13 . ILE   A 1 69  ? 34.796 5.470   -1.321  1.00 15.77 ?  69  ILE   A HG13 1 
ATOM   1655 H HG21 . ILE   A 1 69  ? 36.210 6.069   -3.306  1.00 17.41 ?  69  ILE   A HG21 1 
ATOM   1656 H HG22 . ILE   A 1 69  ? 37.699 6.548   -3.035  1.00 17.41 ?  69  ILE   A HG22 1 
ATOM   1657 H HG23 . ILE   A 1 69  ? 37.392 5.008   -3.281  1.00 17.41 ?  69  ILE   A HG23 1 
ATOM   1658 H HD11 . ILE   A 1 69  ? 34.577 3.153   -1.542  1.00 16.60 ?  69  ILE   A HD11 1 
ATOM   1659 H HD12 . ILE   A 1 69  ? 35.258 3.820   -2.811  1.00 16.60 ?  69  ILE   A HD12 1 
ATOM   1660 H HD13 . ILE   A 1 69  ? 36.148 3.052   -1.741  1.00 16.60 ?  69  ILE   A HD13 1 
ATOM   1661 N N    . ALA   A 1 70  ? 39.790 6.618   -0.504  1.00 12.01 ?  70  ALA   A N    1 
ATOM   1662 C CA   . ALA   A 1 70  ? 41.068 7.230   -0.855  1.00 12.80 ?  70  ALA   A CA   1 
ATOM   1663 C C    . ALA   A 1 70  ? 42.219 6.244   -0.690  1.00 13.03 ?  70  ALA   A C    1 
ATOM   1664 O O    . ALA   A 1 70  ? 43.187 6.290   -1.452  1.00 15.15 ?  70  ALA   A O    1 
ATOM   1665 C CB   . ALA   A 1 70  ? 41.300 8.481   -0.011  1.00 13.41 ?  70  ALA   A CB   1 
ATOM   1666 H H    . ALA   A 1 70  ? 39.363 7.005   0.131   1.00 14.41 ?  70  ALA   A H    1 
ATOM   1667 H HA   . ALA   A 1 70  ? 41.041 7.505   -1.786  1.00 15.35 ?  70  ALA   A HA   1 
ATOM   1668 H HB1  . ALA   A 1 70  ? 42.160 8.872   -0.259  1.00 16.09 ?  70  ALA   A HB1  1 
ATOM   1669 H HB2  . ALA   A 1 70  ? 40.592 9.116   -0.177  1.00 16.09 ?  70  ALA   A HB2  1 
ATOM   1670 H HB3  . ALA   A 1 70  ? 41.318 8.232   0.926   1.00 16.09 ?  70  ALA   A HB3  1 
ATOM   1671 N N    . THR   A 1 71  ? 42.124 5.335   0.278   1.00 12.66 ?  71  THR   A N    1 
ATOM   1672 C CA   . THR   A 1 71  ? 43.188 4.369   0.522   1.00 14.29 ?  71  THR   A CA   1 
ATOM   1673 C C    . THR   A 1 71  ? 43.073 3.150   -0.382  1.00 14.51 ?  71  THR   A C    1 
ATOM   1674 O O    . THR   A 1 71  ? 44.086 2.661   -0.900  1.00 16.43 ?  71  THR   A O    1 
ATOM   1675 C CB   . THR   A 1 71  ? 43.126 3.922   1.979   1.00 16.33 ?  71  THR   A CB   1 
ATOM   1676 O OG1  . THR   A 1 71  ? 43.368 5.050   2.824   1.00 17.69 ?  71  THR   A OG1  1 
ATOM   1677 C CG2  . THR   A 1 71  ? 44.148 2.830   2.273   1.00 17.49 ?  71  THR   A CG2  1 
ATOM   1678 H H    . THR   A 1 71  ? 41.444 5.244   0.793   1.00 15.19 ?  71  THR   A H    1 
ATOM   1679 H HA   . THR   A 1 71  ? 44.046 4.784   0.362   1.00 17.15 ?  71  THR   A HA   1 
ATOM   1680 H HB   . THR   A 1 71  ? 42.242 3.565   2.166   1.00 19.60 ?  71  THR   A HB   1 
ATOM   1681 H HG1  . THR   A 1 71  ? 43.336 4.815   3.629   1.00 21.23 ?  71  THR   A HG1  1 
ATOM   1682 H HG21 . THR   A 1 71  ? 44.270 2.745   3.233   1.00 20.98 ?  71  THR   A HG21 1 
ATOM   1683 H HG22 . THR   A 1 71  ? 43.846 1.982   1.918   1.00 20.98 ?  71  THR   A HG22 1 
ATOM   1684 H HG23 . THR   A 1 71  ? 45.001 3.060   1.870   1.00 20.98 ?  71  THR   A HG23 1 
ATOM   1685 N N    . ASN   A 1 72  ? 41.849 2.639   -0.572  1.00 13.54 ?  72  ASN   A N    1 
ATOM   1686 C CA   . ASN   A 1 72  ? 41.632 1.315   -1.140  1.00 13.43 ?  72  ASN   A CA   1 
ATOM   1687 C C    . ASN   A 1 72  ? 41.000 1.310   -2.519  1.00 13.58 ?  72  ASN   A C    1 
ATOM   1688 O O    . ASN   A 1 72  ? 41.005 0.257   -3.175  1.00 14.85 ?  72  ASN   A O    1 
ATOM   1689 C CB   . ASN   A 1 72  ? 40.743 0.490   -0.202  1.00 14.06 ?  72  ASN   A CB   1 
ATOM   1690 C CG   . ASN   A 1 72  ? 41.360 0.329   1.160   1.00 15.07 ?  72  ASN   A CG   1 
ATOM   1691 O OD1  . ASN   A 1 72  ? 40.903 0.917   2.138   1.00 16.96 ?  72  ASN   A OD1  1 
ATOM   1692 N ND2  . ASN   A 1 72  ? 42.423 -0.446  1.229   1.00 15.90 ?  72  ASN   A ND2  1 
ATOM   1693 H H    . ASN   A 1 72  ? 41.121 3.054   -0.380  1.00 16.25 ?  72  ASN   A H    1 
ATOM   1694 H HA   . ASN   A 1 72  ? 42.486 0.865   -1.217  1.00 16.11 ?  72  ASN   A HA   1 
ATOM   1695 H HB2  . ASN   A 1 72  ? 39.891 0.934   -0.101  1.00 16.87 ?  72  ASN   A HB2  1 
ATOM   1696 H HB3  . ASN   A 1 72  ? 40.618 -0.395  -0.586  1.00 16.87 ?  72  ASN   A HB3  1 
ATOM   1697 H HD21 . ASN   A 1 72  ? 42.819 -0.568  1.985   1.00 19.08 ?  72  ASN   A HD21 1 
ATOM   1698 H HD22 . ASN   A 1 72  ? 42.723 -0.837  0.523   1.00 19.08 ?  72  ASN   A HD22 1 
ATOM   1699 N N    . GLY   A 1 73  ? 40.448 2.429   -2.970  1.00 13.10 ?  73  GLY   A N    1 
ATOM   1700 C CA   . GLY   A 1 73  ? 39.708 2.449   -4.203  1.00 13.08 ?  73  GLY   A CA   1 
ATOM   1701 C C    . GLY   A 1 73  ? 38.318 1.870   -4.023  1.00 12.24 ?  73  GLY   A C    1 
ATOM   1702 O O    . GLY   A 1 73  ? 37.941 1.401   -2.942  1.00 12.71 ?  73  GLY   A O    1 
ATOM   1703 H H    . GLY   A 1 73  ? 40.488 3.197   -2.573  1.00 15.72 ?  73  GLY   A H    1 
ATOM   1704 H HA2  . GLY   A 1 73  ? 39.634 3.369   -4.518  1.00 15.70 ?  73  GLY   A HA2  1 
ATOM   1705 H HA3  . GLY   A 1 73  ? 40.181 1.934   -4.876  1.00 15.70 ?  73  GLY   A HA3  1 
ATOM   1706 N N    . PRO   A 1 74  ? 37.533 1.892   -5.098  1.00 12.87 ?  74  PRO   A N    1 
ATOM   1707 C CA   . PRO   A 1 74  ? 36.137 1.461   -5.008  1.00 12.98 ?  74  PRO   A CA   1 
ATOM   1708 C C    . PRO   A 1 74  ? 35.994 -0.023  -4.706  1.00 12.29 ?  74  PRO   A C    1 
ATOM   1709 O O    . PRO   A 1 74  ? 36.870 -0.851  -4.991  1.00 13.22 ?  74  PRO   A O    1 
ATOM   1710 C CB   . PRO   A 1 74  ? 35.581 1.773   -6.402  1.00 14.53 ?  74  PRO   A CB   1 
ATOM   1711 C CG   . PRO   A 1 74  ? 36.518 2.771   -6.994  1.00 16.91 ?  74  PRO   A CG   1 
ATOM   1712 C CD   . PRO   A 1 74  ? 37.862 2.437   -6.424  1.00 14.88 ?  74  PRO   A CD   1 
ATOM   1713 H HA   . PRO   A 1 74  ? 35.662 1.978   -4.339  1.00 15.58 ?  74  PRO   A HA   1 
ATOM   1714 H HB2  . PRO   A 1 74  ? 35.558 0.966   -6.934  1.00 17.44 ?  74  PRO   A HB2  1 
ATOM   1715 H HB3  . PRO   A 1 74  ? 34.690 2.154   -6.318  1.00 17.44 ?  74  PRO   A HB3  1 
ATOM   1716 H HG2  . PRO   A 1 74  ? 36.528 2.682   -7.958  1.00 20.29 ?  74  PRO   A HG2  1 
ATOM   1717 H HG3  . PRO   A 1 74  ? 36.253 3.667   -6.734  1.00 20.29 ?  74  PRO   A HG3  1 
ATOM   1718 H HD2  . PRO   A 1 74  ? 38.307 1.768   -6.966  1.00 17.86 ?  74  PRO   A HD2  1 
ATOM   1719 H HD3  . PRO   A 1 74  ? 38.399 3.245   -6.347  1.00 17.86 ?  74  PRO   A HD3  1 
ATOM   1720 N N    A LEU   A 1 75  ? 34.857 -0.361  -4.109  0.30 12.06 ?  75  LEU   A N    1 
ATOM   1721 N N    B LEU   A 1 75  ? 34.839 -0.353  -4.126  0.70 11.58 ?  75  LEU   A N    1 
ATOM   1722 C CA   A LEU   A 1 75  ? 34.505 -1.759  -3.965  0.30 12.05 ?  75  LEU   A CA   1 
ATOM   1723 C CA   B LEU   A 1 75  ? 34.431 -1.739  -3.961  0.70 10.87 ?  75  LEU   A CA   1 
ATOM   1724 C C    A LEU   A 1 75  ? 34.167 -2.348  -5.335  0.30 11.79 ?  75  LEU   A C    1 
ATOM   1725 C C    B LEU   A 1 75  ? 34.016 -2.326  -5.306  0.70 11.46 ?  75  LEU   A C    1 
ATOM   1726 O O    A LEU   A 1 75  ? 34.149 -1.657  -6.359  0.30 11.88 ?  75  LEU   A O    1 
ATOM   1727 O O    B LEU   A 1 75  ? 33.775 -1.611  -6.282  0.70 12.82 ?  75  LEU   A O    1 
ATOM   1728 C CB   A LEU   A 1 75  ? 33.312 -1.915  -3.020  0.30 12.65 ?  75  LEU   A CB   1 
ATOM   1729 C CB   B LEU   A 1 75  ? 33.242 -1.849  -3.000  0.70 10.90 ?  75  LEU   A CB   1 
ATOM   1730 C CG   A LEU   A 1 75  ? 33.486 -1.366  -1.601  0.30 13.71 ?  75  LEU   A CG   1 
ATOM   1731 C CG   B LEU   A 1 75  ? 33.457 -1.467  -1.538  0.70 12.47 ?  75  LEU   A CG   1 
ATOM   1732 C CD1  A LEU   A 1 75  ? 32.188 -1.470  -0.798  0.30 14.42 ?  75  LEU   A CD1  1 
ATOM   1733 C CD1  B LEU   A 1 75  ? 32.164 -1.675  -0.750  0.70 13.78 ?  75  LEU   A CD1  1 
ATOM   1734 C CD2  A LEU   A 1 75  ? 34.619 -2.061  -0.869  0.30 14.61 ?  75  LEU   A CD2  1 
ATOM   1735 C CD2  B LEU   A 1 75  ? 34.581 -2.248  -0.907  0.70 15.28 ?  75  LEU   A CD2  1 
ATOM   1736 H H    A LEU   A 1 75  ? 34.287 0.194   -3.785  0.30 14.47 ?  75  LEU   A H    1 
ATOM   1737 H H    B LEU   A 1 75  ? 34.268 0.214   -3.831  0.70 13.90 ?  75  LEU   A H    1 
ATOM   1738 H HA   A LEU   A 1 75  ? 35.260 -2.244  -3.596  0.30 14.45 ?  75  LEU   A HA   1 
ATOM   1739 H HA   B LEU   A 1 75  ? 35.164 -2.261  -3.613  0.70 13.05 ?  75  LEU   A HA   1 
ATOM   1740 H HB2  A LEU   A 1 75  ? 32.554 -1.461  -3.414  0.30 15.18 ?  75  LEU   A HB2  1 
ATOM   1741 H HB2  B LEU   A 1 75  ? 32.531 -1.284  -3.335  0.70 13.08 ?  75  LEU   A HB2  1 
ATOM   1742 H HB3  A LEU   A 1 75  ? 33.115 -2.862  -2.941  0.30 15.18 ?  75  LEU   A HB3  1 
ATOM   1743 H HB3  B LEU   A 1 75  ? 32.939 -2.773  -3.004  0.70 13.08 ?  75  LEU   A HB3  1 
ATOM   1744 H HG   A LEU   A 1 75  ? 33.714 -0.427  -1.660  0.30 16.45 ?  75  LEU   A HG   1 
ATOM   1745 H HG   B LEU   A 1 75  ? 33.687 -0.526  -1.487  0.70 14.96 ?  75  LEU   A HG   1 
ATOM   1746 H HD11 A LEU   A 1 75  ? 32.339 -1.113  0.093   0.30 17.31 ?  75  LEU   A HD11 1 
ATOM   1747 H HD11 B LEU   A 1 75  ? 32.315 -1.424  0.176   0.70 16.53 ?  75  LEU   A HD11 1 
ATOM   1748 H HD12 A LEU   A 1 75  ? 31.498 -0.956  -1.245  0.30 17.31 ?  75  LEU   A HD12 1 
ATOM   1749 H HD12 B LEU   A 1 75  ? 31.471 -1.113  -1.134  0.70 16.53 ?  75  LEU   A HD12 1 
ATOM   1750 H HD13 A LEU   A 1 75  ? 31.924 -2.401  -0.739  0.30 17.31 ?  75  LEU   A HD13 1 
ATOM   1751 H HD13 B LEU   A 1 75  ? 31.907 -2.605  -0.805  0.70 16.53 ?  75  LEU   A HD13 1 
ATOM   1752 H HD21 A LEU   A 1 75  ? 34.656 -1.732  0.043   0.30 17.53 ?  75  LEU   A HD21 1 
ATOM   1753 H HD21 B LEU   A 1 75  ? 34.641 -2.013  0.032   0.70 18.34 ?  75  LEU   A HD21 1 
ATOM   1754 H HD22 A LEU   A 1 75  ? 34.457 -3.018  -0.868  0.30 17.53 ?  75  LEU   A HD22 1 
ATOM   1755 H HD22 B LEU   A 1 75  ? 34.397 -3.196  -1.000  0.70 18.34 ?  75  LEU   A HD22 1 
ATOM   1756 H HD23 A LEU   A 1 75  ? 35.454 -1.869  -1.323  0.30 17.53 ?  75  LEU   A HD23 1 
ATOM   1757 H HD23 B LEU   A 1 75  ? 35.411 -2.025  -1.357  0.70 18.34 ?  75  LEU   A HD23 1 
ATOM   1758 N N    . LYS   A 1 76  ? 33.932 -3.655  -5.342  1.00 11.88 ?  76  LYS   A N    1 
ATOM   1759 C CA   . LYS   A 1 76  ? 33.348 -4.365  -6.471  1.00 12.59 ?  76  LYS   A CA   1 
ATOM   1760 C C    . LYS   A 1 76  ? 31.835 -4.438  -6.287  1.00 11.42 ?  76  LYS   A C    1 
ATOM   1761 O O    . LYS   A 1 76  ? 31.343 -4.546  -5.164  1.00 11.41 ?  76  LYS   A O    1 
ATOM   1762 C CB   . LYS   A 1 76  ? 33.880 -5.807  -6.525  1.00 13.77 ?  76  LYS   A CB   1 
ATOM   1763 C CG   . LYS   A 1 76  ? 35.387 -5.905  -6.713  1.00 15.27 ?  76  LYS   A CG   1 
ATOM   1764 C CD   . LYS   A 1 76  ? 35.919 -7.298  -6.454  1.00 16.78 ?  76  LYS   A CD   1 
ATOM   1765 C CE   . LYS   A 1 76  ? 37.419 -7.346  -6.632  1.00 19.38 ?  76  LYS   A CE   1 
ATOM   1766 N NZ   . LYS   A 1 76  ? 37.970 -8.689  -6.358  1.00 20.49 ?  76  LYS   A NZ   1 
ATOM   1767 H H    A LYS   A 1 76  ? 34.106 -4.174  -4.675  0.30 14.25 ?  76  LYS   A H    1 
ATOM   1768 H H    B LYS   A 1 76  ? 34.217 -4.176  -4.716  0.70 14.25 ?  76  LYS   A H    1 
ATOM   1769 H HA   . LYS   A 1 76  ? 33.557 -3.911  -7.306  1.00 15.11 ?  76  LYS   A HA   1 
ATOM   1770 H HB2  . LYS   A 1 76  ? 33.654 -6.249  -5.694  1.00 16.53 ?  76  LYS   A HB2  1 
ATOM   1771 H HB3  . LYS   A 1 76  ? 33.458 -6.264  -7.269  1.00 16.53 ?  76  LYS   A HB3  1 
ATOM   1772 H HG2  . LYS   A 1 76  ? 35.610 -5.661  -7.626  1.00 18.33 ?  76  LYS   A HG2  1 
ATOM   1773 H HG3  . LYS   A 1 76  ? 35.825 -5.297  -6.094  1.00 18.33 ?  76  LYS   A HG3  1 
ATOM   1774 H HD2  . LYS   A 1 76  ? 35.708 -7.559  -5.544  1.00 20.13 ?  76  LYS   A HD2  1 
ATOM   1775 H HD3  . LYS   A 1 76  ? 35.514 -7.916  -7.084  1.00 20.13 ?  76  LYS   A HD3  1 
ATOM   1776 H HE2  . LYS   A 1 76  ? 37.640 -7.113  -7.547  1.00 23.26 ?  76  LYS   A HE2  1 
ATOM   1777 H HE3  . LYS   A 1 76  ? 37.833 -6.722  -6.017  1.00 23.26 ?  76  LYS   A HE3  1 
ATOM   1778 H HZ1  . LYS   A 1 76  ? 38.849 -8.693  -6.469  1.00 24.59 ?  76  LYS   A HZ1  1 
ATOM   1779 H HZ2  . LYS   A 1 76  ? 37.781 -8.933  -5.520  1.00 24.59 ?  76  LYS   A HZ2  1 
ATOM   1780 H HZ3  . LYS   A 1 76  ? 37.605 -9.289  -6.913  1.00 24.59 ?  76  LYS   A HZ3  1 
ATOM   1781 N N    . VAL   A 1 77  ? 31.095 -4.415  -7.401  1.00 11.77 ?  77  VAL   A N    1 
ATOM   1782 C CA   . VAL   A 1 77  ? 29.686 -4.792  -7.324  1.00 11.89 ?  77  VAL   A CA   1 
ATOM   1783 C C    . VAL   A 1 77  ? 29.618 -6.245  -6.878  1.00 11.40 ?  77  VAL   A C    1 
ATOM   1784 O O    . VAL   A 1 77  ? 30.287 -7.114  -7.451  1.00 11.93 ?  77  VAL   A O    1 
ATOM   1785 C CB   . VAL   A 1 77  ? 28.974 -4.581  -8.669  1.00 13.03 ?  77  VAL   A CB   1 
ATOM   1786 C CG1  . VAL   A 1 77  ? 27.505 -4.982  -8.556  1.00 14.00 ?  77  VAL   A CG1  1 
ATOM   1787 C CG2  . VAL   A 1 77  ? 29.089 -3.134  -9.117  1.00 14.41 ?  77  VAL   A CG2  1 
ATOM   1788 H H    . VAL   A 1 77  ? 31.378 -4.187  -8.182  1.00 14.12 ?  77  VAL   A H    1 
ATOM   1789 H HA   . VAL   A 1 77  ? 29.245 -4.243  -6.655  1.00 14.27 ?  77  VAL   A HA   1 
ATOM   1790 H HB   . VAL   A 1 77  ? 29.393 -5.140  -9.342  1.00 15.63 ?  77  VAL   A HB   1 
ATOM   1791 H HG11 . VAL   A 1 77  ? 27.042 -4.699  -9.359  1.00 16.80 ?  77  VAL   A HG11 1 
ATOM   1792 H HG12 . VAL   A 1 77  ? 27.443 -5.942  -8.456  1.00 16.80 ?  77  VAL   A HG12 1 
ATOM   1793 H HG13 . VAL   A 1 77  ? 27.119 -4.539  -7.782  1.00 16.80 ?  77  VAL   A HG13 1 
ATOM   1794 H HG21 . VAL   A 1 77  ? 28.580 -3.018  -9.933  1.00 17.29 ?  77  VAL   A HG21 1 
ATOM   1795 H HG22 . VAL   A 1 77  ? 28.733 -2.561  -8.419  1.00 17.29 ?  77  VAL   A HG22 1 
ATOM   1796 H HG23 . VAL   A 1 77  ? 30.022 -2.924  -9.274  1.00 17.29 ?  77  VAL   A HG23 1 
ATOM   1797 N N    . GLY   A 1 78  ? 28.815 -6.516  -5.847  1.00 11.01 ?  78  GLY   A N    1 
ATOM   1798 C CA   . GLY   A 1 78  ? 28.788 -7.806  -5.186  1.00 11.26 ?  78  GLY   A CA   1 
ATOM   1799 C C    . GLY   A 1 78  ? 29.713 -7.905  -3.991  1.00 10.74 ?  78  GLY   A C    1 
ATOM   1800 O O    . GLY   A 1 78  ? 29.666 -8.911  -3.268  1.00 11.51 ?  78  GLY   A O    1 
ATOM   1801 H H    . GLY   A 1 78  ? 28.258 -5.944  -5.509  1.00 13.21 ?  78  GLY   A H    1 
ATOM   1802 H HA2  . GLY   A 1 78  ? 27.885 -7.990  -4.889  1.00 13.51 ?  78  GLY   A HA2  1 
ATOM   1803 H HA3  . GLY   A 1 78  ? 29.043 -8.488  -5.826  1.00 13.51 ?  78  GLY   A HA3  1 
ATOM   1804 N N    . GLY   A 1 79  ? 30.551 -6.892  -3.765  1.00 10.92 ?  79  GLY   A N    1 
ATOM   1805 C CA   . GLY   A 1 79  ? 31.518 -6.897  -2.693  1.00 10.90 ?  79  GLY   A CA   1 
ATOM   1806 C C    . GLY   A 1 79  ? 31.070 -6.115  -1.472  1.00 10.19 ?  79  GLY   A C    1 
ATOM   1807 O O    . GLY   A 1 79  ? 29.945 -5.619  -1.384  1.00 11.14 ?  79  GLY   A O    1 
ATOM   1808 H H    . GLY   A 1 79  ? 30.572 -6.171  -4.238  1.00 13.11 ?  79  GLY   A H    1 
ATOM   1809 H HA2  . GLY   A 1 79  ? 31.685 -7.818  -2.423  1.00 13.08 ?  79  GLY   A HA2  1 
ATOM   1810 H HA3  . GLY   A 1 79  ? 32.350 -6.520  -3.011  1.00 13.08 ?  79  GLY   A HA3  1 
ATOM   1811 N N    . SER   A 1 80  ? 31.985 -6.015  -0.509  1.00 11.01 ?  80  SER   A N    1 
ATOM   1812 C CA   . SER   A 1 80  ? 31.671 -5.397  0.770   1.00 10.36 ?  80  SER   A CA   1 
ATOM   1813 C C    . SER   A 1 80  ? 32.945 -4.947  1.465   1.00 10.34 ?  80  SER   A C    1 
ATOM   1814 O O    . SER   A 1 80  ? 34.054 -5.375  1.127   1.00 11.69 ?  80  SER   A O    1 
ATOM   1815 C CB   . SER   A 1 80  ? 30.924 -6.362  1.693   1.00 11.31 ?  80  SER   A CB   1 
ATOM   1816 O OG   . SER   A 1 80  ? 31.763 -7.421  2.129   1.00 12.81 ?  80  SER   A OG   1 
ATOM   1817 H H    . SER   A 1 80  ? 32.796 -6.292  -0.577  1.00 13.21 ?  80  SER   A H    1 
ATOM   1818 H HA   . SER   A 1 80  ? 31.116 -4.620  0.606   1.00 12.44 ?  80  SER   A HA   1 
ATOM   1819 H HB2  . SER   A 1 80  ? 30.616 -5.875  2.472   1.00 13.57 ?  80  SER   A HB2  1 
ATOM   1820 H HB3  . SER   A 1 80  ? 30.169 -6.733  1.214   1.00 13.57 ?  80  SER   A HB3  1 
ATOM   1821 H HG   . SER   A 1 80  ? 32.033 -7.863  1.462   1.00 15.37 ?  80  SER   A HG   1 
ATOM   1822 N N    . CYS   A 1 81  ? 32.758 -4.104  2.479   1.00 10.13 ?  81  CYS   A N    1 
ATOM   1823 C CA   . CYS   A 1 81  ? 33.809 -3.825  3.445   1.00 10.23 ?  81  CYS   A CA   1 
ATOM   1824 C C    . CYS   A 1 81  ? 33.171 -3.610  4.811   1.00 9.99  ?  81  CYS   A C    1 
ATOM   1825 O O    . CYS   A 1 81  ? 32.004 -3.215  4.913   1.00 11.34 ?  81  CYS   A O    1 
ATOM   1826 C CB   . CYS   A 1 81  ? 34.675 -2.628  3.034   1.00 10.99 ?  81  CYS   A CB   1 
ATOM   1827 S SG   . CYS   A 1 81  ? 33.772 -1.061  3.067   1.00 11.14 ?  81  CYS   A SG   1 
ATOM   1828 H H    . CYS   A 1 81  ? 32.024 -3.676  2.631   1.00 12.15 ?  81  CYS   A H    1 
ATOM   1829 H HA   . CYS   A 1 81  ? 34.392 -4.596  3.503   1.00 12.28 ?  81  CYS   A HA   1 
ATOM   1830 H HB2  . CYS   A 1 81  ? 35.426 -2.559  3.647   1.00 13.18 ?  81  CYS   A HB2  1 
ATOM   1831 H HB3  . CYS   A 1 81  ? 35.004 -2.774  2.131   1.00 13.18 ?  81  CYS   A HB3  1 
ATOM   1832 H HG   . CYS   A 1 81  ? 34.510 -0.172  2.733   1.00 13.37 ?  81  CYS   A HG   1 
ATOM   1833 N N    . VAL   A 1 82  ? 33.950 -3.874  5.858   1.00 10.39 ?  82  VAL   A N    1 
ATOM   1834 C CA   . VAL   A 1 82  ? 33.530 -3.648  7.233   1.00 10.99 ?  82  VAL   A CA   1 
ATOM   1835 C C    . VAL   A 1 82  ? 34.129 -2.335  7.711   1.00 11.08 ?  82  VAL   A C    1 
ATOM   1836 O O    . VAL   A 1 82  ? 35.354 -2.160  7.700   1.00 12.13 ?  82  VAL   A O    1 
ATOM   1837 C CB   . VAL   A 1 82  ? 33.967 -4.793  8.158   1.00 12.53 ?  82  VAL   A CB   1 
ATOM   1838 C CG1  . VAL   A 1 82  ? 33.510 -4.519  9.583   1.00 13.89 ?  82  VAL   A CG1  1 
ATOM   1839 C CG2  . VAL   A 1 82  ? 33.436 -6.127  7.661   1.00 13.20 ?  82  VAL   A CG2  1 
ATOM   1840 H H    . VAL   A 1 82  ? 34.750 -4.211  5.793   1.00 12.47 ?  82  VAL   A H    1 
ATOM   1841 H HA   . VAL   A 1 82  ? 32.565 -3.575  7.265   1.00 13.18 ?  82  VAL   A HA   1 
ATOM   1842 H HB   . VAL   A 1 82  ? 34.937 -4.835  8.163   1.00 15.04 ?  82  VAL   A HB   1 
ATOM   1843 H HG11 . VAL   A 1 82  ? 33.612 -5.328  10.107  1.00 16.67 ?  82  VAL   A HG11 1 
ATOM   1844 H HG12 . VAL   A 1 82  ? 34.052 -3.809  9.966   1.00 16.67 ?  82  VAL   A HG12 1 
ATOM   1845 H HG13 . VAL   A 1 82  ? 32.576 -4.250  9.571   1.00 16.67 ?  82  VAL   A HG13 1 
ATOM   1846 H HG21 . VAL   A 1 82  ? 33.690 -6.818  8.294   1.00 15.84 ?  82  VAL   A HG21 1 
ATOM   1847 H HG22 . VAL   A 1 82  ? 32.474 -6.077  7.591   1.00 15.84 ?  82  VAL   A HG22 1 
ATOM   1848 H HG23 . VAL   A 1 82  ? 33.827 -6.316  6.793   1.00 15.84 ?  82  VAL   A HG23 1 
ATOM   1849 N N    . LEU   A 1 83  ? 33.271 -1.414  8.133   1.00 10.61 ?  83  LEU   A N    1 
ATOM   1850 C CA   . LEU   A 1 83  ? 33.684 -0.148  8.719   1.00 10.85 ?  83  LEU   A CA   1 
ATOM   1851 C C    . LEU   A 1 83  ? 32.973 0.017   10.063  1.00 10.95 ?  83  LEU   A C    1 
ATOM   1852 O O    . LEU   A 1 83  ? 32.264 -0.884  10.532  1.00 11.54 ?  83  LEU   A O    1 
ATOM   1853 C CB   . LEU   A 1 83  ? 33.422 1.011   7.746   1.00 11.13 ?  83  LEU   A CB   1 
ATOM   1854 C CG   . LEU   A 1 83  ? 34.315 1.020   6.501   1.00 12.12 ?  83  LEU   A CG   1 
ATOM   1855 C CD1  . LEU   A 1 83  ? 33.862 2.085   5.516   1.00 12.54 ?  83  LEU   A CD1  1 
ATOM   1856 C CD2  . LEU   A 1 83  ? 35.774 1.254   6.883   1.00 12.81 ?  83  LEU   A CD2  1 
ATOM   1857 H H    . LEU   A 1 83  ? 32.416 -1.503  8.078   1.00 12.73 ?  83  LEU   A H    1 
ATOM   1858 H HA   . LEU   A 1 83  ? 34.637 -0.176  8.891   1.00 13.02 ?  83  LEU   A HA   1 
ATOM   1859 H HB2  . LEU   A 1 83  ? 32.502 0.960   7.439   1.00 13.36 ?  83  LEU   A HB2  1 
ATOM   1860 H HB3  . LEU   A 1 83  ? 33.563 1.849   8.209   1.00 13.36 ?  83  LEU   A HB3  1 
ATOM   1861 H HG   . LEU   A 1 83  ? 34.256 0.159   6.060   1.00 14.54 ?  83  LEU   A HG   1 
ATOM   1862 H HD11 . LEU   A 1 83  ? 34.441 2.061   4.738   1.00 15.04 ?  83  LEU   A HD11 1 
ATOM   1863 H HD12 . LEU   A 1 83  ? 32.946 1.896   5.252   1.00 15.04 ?  83  LEU   A HD12 1 
ATOM   1864 H HD13 . LEU   A 1 83  ? 33.912 2.951   5.944   1.00 15.04 ?  83  LEU   A HD13 1 
ATOM   1865 H HD21 . LEU   A 1 83  ? 36.288 1.429   6.078   1.00 15.37 ?  83  LEU   A HD21 1 
ATOM   1866 H HD22 . LEU   A 1 83  ? 35.824 2.022   7.477   1.00 15.37 ?  83  LEU   A HD22 1 
ATOM   1867 H HD23 . LEU   A 1 83  ? 36.115 0.467   7.331   1.00 15.37 ?  83  LEU   A HD23 1 
ATOM   1868 N N    . SER   A 1 84  ? 33.168 1.168   10.699  1.00 11.70 ?  84  SER   A N    1 
ATOM   1869 C CA   . SER   A 1 84  ? 32.530 1.411   11.981  1.00 11.97 ?  84  SER   A CA   1 
ATOM   1870 C C    . SER   A 1 84  ? 31.011 1.497   11.835  1.00 11.55 ?  84  SER   A C    1 
ATOM   1871 O O    . SER   A 1 84  ? 30.486 1.964   10.826  1.00 11.81 ?  84  SER   A O    1 
ATOM   1872 C CB   . SER   A 1 84  ? 33.038 2.723   12.570  1.00 12.85 ?  84  SER   A CB   1 
ATOM   1873 O OG   . SER   A 1 84  ? 32.422 2.988   13.814  1.00 13.98 ?  84  SER   A OG   1 
ATOM   1874 H H    . SER   A 1 84  ? 33.658 1.818   10.403  1.00 14.04 ?  84  SER   A H    1 
ATOM   1875 H HA   . SER   A 1 84  ? 32.748 0.692   12.587  1.00 14.36 ?  84  SER   A HA   1 
ATOM   1876 H HB2  . SER   A 1 84  ? 34.001 2.661   12.700  1.00 15.42 ?  84  SER   A HB2  1 
ATOM   1877 H HB3  . SER   A 1 84  ? 32.839 3.449   11.956  1.00 15.42 ?  84  SER   A HB3  1 
ATOM   1878 H HG   . SER   A 1 84  ? 32.712 3.713   14.131  1.00 16.77 ?  84  SER   A HG   1 
ATOM   1879 N N    . GLY   A 1 85  ? 30.303 1.078   12.878  1.00 12.49 ?  85  GLY   A N    1 
ATOM   1880 C CA   . GLY   A 1 85  ? 28.884 1.340   12.962  1.00 12.83 ?  85  GLY   A CA   1 
ATOM   1881 C C    . GLY   A 1 85  ? 28.535 2.640   13.651  1.00 12.79 ?  85  GLY   A C    1 
ATOM   1882 O O    . GLY   A 1 85  ? 27.352 2.963   13.804  1.00 13.58 ?  85  GLY   A O    1 
ATOM   1883 H H    . GLY   A 1 85  ? 30.631 0.638   13.544  1.00 14.99 ?  85  GLY   A H    1 
ATOM   1884 H HA2  . GLY   A 1 85  ? 28.518 1.360   12.063  1.00 15.39 ?  85  GLY   A HA2  1 
ATOM   1885 H HA3  . GLY   A 1 85  ? 28.462 0.622   13.446  1.00 15.39 ?  85  GLY   A HA3  1 
ATOM   1886 N N    . HIS   A 1 86  ? 29.537 3.399   14.084  1.00 12.59 ?  86  HIS   A N    1 
ATOM   1887 C CA   . HIS   A 1 86  ? 29.333 4.725   14.677  1.00 13.04 ?  86  HIS   A CA   1 
ATOM   1888 C C    . HIS   A 1 86  ? 28.360 4.599   15.842  1.00 14.20 ?  86  HIS   A C    1 
ATOM   1889 O O    . HIS   A 1 86  ? 28.541 3.712   16.690  1.00 15.55 ?  86  HIS   A O    1 
ATOM   1890 C CB   . HIS   A 1 86  ? 28.953 5.727   13.600  1.00 13.08 ?  86  HIS   A CB   1 
ATOM   1891 C CG   . HIS   A 1 86  ? 29.986 5.826   12.542  1.00 12.89 ?  86  HIS   A CG   1 
ATOM   1892 N ND1  . HIS   A 1 86  ? 31.075 6.663   12.655  1.00 14.39 ?  86  HIS   A ND1  1 
ATOM   1893 C CD2  . HIS   A 1 86  ? 30.156 5.130   11.395  1.00 12.91 ?  86  HIS   A CD2  1 
ATOM   1894 C CE1  . HIS   A 1 86  ? 31.849 6.505   11.597  1.00 14.11 ?  86  HIS   A CE1  1 
ATOM   1895 N NE2  . HIS   A 1 86  ? 31.322 5.573   10.824  1.00 13.31 ?  86  HIS   A NE2  1 
ATOM   1896 H H    . HIS   A 1 86  ? 30.363 3.172   14.047  1.00 15.10 ?  86  HIS   A H    1 
ATOM   1897 H HA   . HIS   A 1 86  ? 30.179 5.024   15.045  1.00 15.64 ?  86  HIS   A HA   1 
ATOM   1898 H HB2  . HIS   A 1 86  ? 28.120 5.460   13.184  1.00 15.70 ?  86  HIS   A HB2  1 
ATOM   1899 H HB3  . HIS   A 1 86  ? 28.854 6.612   13.998  1.00 15.70 ?  86  HIS   A HB3  1 
ATOM   1900 H HD2  . HIS   A 1 86  ? 29.595 4.467   11.057  1.00 15.49 ?  86  HIS   A HD2  1 
ATOM   1901 H HE1  . HIS   A 1 86  ? 32.637 6.971   11.412  1.00 16.93 ?  86  HIS   A HE1  1 
ATOM   1902 H HE2  . HIS   A 1 86  ? 31.648 5.296   10.069  1.00 15.97 ?  86  HIS   A HE2  1 
ATOM   1903 N N    A ASN   A 1 87  ? 27.325 5.434   15.912  0.30 15.05 ?  87  ASN   A N    1 
ATOM   1904 N N    B ASN   A 1 87  ? 27.367 5.465   15.946  0.70 14.96 ?  87  ASN   A N    1 
ATOM   1905 C CA   A ASN   A 1 87  ? 26.322 5.428   16.966  0.30 15.94 ?  87  ASN   A CA   1 
ATOM   1906 C CA   B ASN   A 1 87  ? 26.434 5.443   17.056  0.70 15.88 ?  87  ASN   A CA   1 
ATOM   1907 C C    A ASN   A 1 87  ? 25.162 4.483   16.674  0.30 16.77 ?  87  ASN   A C    1 
ATOM   1908 C C    B ASN   A 1 87  ? 25.322 4.425   16.868  0.70 16.27 ?  87  ASN   A C    1 
ATOM   1909 O O    A ASN   A 1 87  ? 24.175 4.492   17.416  0.30 17.90 ?  87  ASN   A O    1 
ATOM   1910 O O    B ASN   A 1 87  ? 24.487 4.285   17.766  0.70 17.35 ?  87  ASN   A O    1 
ATOM   1911 C CB   A ASN   A 1 87  ? 25.761 6.842   17.142  0.30 16.23 ?  87  ASN   A CB   1 
ATOM   1912 C CB   B ASN   A 1 87  ? 25.833 6.840   17.248  0.70 16.93 ?  87  ASN   A CB   1 
ATOM   1913 C CG   A ASN   A 1 87  ? 25.174 7.400   15.850  0.30 16.32 ?  87  ASN   A CG   1 
ATOM   1914 C CG   B ASN   A 1 87  ? 25.360 7.460   15.939  0.70 17.59 ?  87  ASN   A CG   1 
ATOM   1915 O OD1  A ASN   A 1 87  ? 25.721 7.195   14.766  0.30 15.97 ?  87  ASN   A OD1  1 
ATOM   1916 O OD1  B ASN   A 1 87  ? 26.075 7.452   14.936  0.70 17.87 ?  87  ASN   A OD1  1 
ATOM   1917 N ND2  A ASN   A 1 87  ? 24.054 8.099   15.961  0.30 17.09 ?  87  ASN   A ND2  1 
ATOM   1918 N ND2  B ASN   A 1 87  ? 24.151 7.994   15.945  0.70 18.93 ?  87  ASN   A ND2  1 
ATOM   1919 H H    A ASN   A 1 87  ? 27.176 6.044   15.327  0.30 18.06 ?  87  ASN   A H    1 
ATOM   1920 H H    B ASN   A 1 87  ? 27.206 6.080   15.373  0.70 17.95 ?  87  ASN   A H    1 
ATOM   1921 H HA   A ASN   A 1 87  ? 26.735 5.159   17.804  0.30 19.13 ?  87  ASN   A HA   1 
ATOM   1922 H HA   B ASN   A 1 87  ? 26.904 5.203   17.869  0.70 19.06 ?  87  ASN   A HA   1 
ATOM   1923 H HB2  A ASN   A 1 87  ? 25.053 6.822   17.809  0.30 19.47 ?  87  ASN   A HB2  1 
ATOM   1924 H HB2  B ASN   A 1 87  ? 25.068 6.777   17.848  0.70 20.31 ?  87  ASN   A HB2  1 
ATOM   1925 H HB3  A ASN   A 1 87  ? 26.473 7.431   17.434  0.30 19.47 ?  87  ASN   A HB3  1 
ATOM   1926 H HB3  B ASN   A 1 87  ? 26.508 7.417   17.639  0.70 20.31 ?  87  ASN   A HB3  1 
ATOM   1927 H HD21 A ASN   A 1 87  ? 23.690 8.431   15.257  0.30 20.51 ?  87  ASN   A HD21 1 
ATOM   1928 H HD21 B ASN   A 1 87  ? 23.846 8.358   15.231  0.70 22.72 ?  87  ASN   A HD21 1 
ATOM   1929 H HD22 A ASN   A 1 87  ? 23.697 8.220   16.732  0.30 20.51 ?  87  ASN   A HD22 1 
ATOM   1930 H HD22 B ASN   A 1 87  ? 23.680 7.985   16.664  0.70 22.72 ?  87  ASN   A HD22 1 
ATOM   1931 N N    A LEU   A 1 88  ? 25.245 3.690   15.606  0.30 16.18 ?  88  LEU   A N    1 
ATOM   1932 N N    B LEU   A 1 88  ? 25.306 3.698   15.751  0.70 15.09 ?  88  LEU   A N    1 
ATOM   1933 C CA   A LEU   A 1 88  ? 24.153 2.811   15.205  0.30 15.79 ?  88  LEU   A CA   1 
ATOM   1934 C CA   B LEU   A 1 88  ? 24.176 2.847   15.391  0.70 14.91 ?  88  LEU   A CA   1 
ATOM   1935 C C    A LEU   A 1 88  ? 24.396 1.341   15.507  0.30 15.47 ?  88  LEU   A C    1 
ATOM   1936 C C    B LEU   A 1 88  ? 24.407 1.368   15.661  0.70 14.83 ?  88  LEU   A C    1 
ATOM   1937 O O    A LEU   A 1 88  ? 23.430 0.593   15.671  0.30 15.97 ?  88  LEU   A O    1 
ATOM   1938 O O    B LEU   A 1 88  ? 23.447 0.642   15.938  0.70 16.16 ?  88  LEU   A O    1 
ATOM   1939 C CB   A LEU   A 1 88  ? 23.894 2.946   13.699  0.30 16.10 ?  88  LEU   A CB   1 
ATOM   1940 C CB   B LEU   A 1 88  ? 23.844 3.033   13.907  0.70 15.22 ?  88  LEU   A CB   1 
ATOM   1941 C CG   A LEU   A 1 88  ? 23.613 4.354   13.176  0.30 16.58 ?  88  LEU   A CG   1 
ATOM   1942 C CG   B LEU   A 1 88  ? 23.484 4.457   13.482  0.70 16.28 ?  88  LEU   A CG   1 
ATOM   1943 C CD1  A LEU   A 1 88  ? 23.474 4.329   11.663  0.30 16.56 ?  88  LEU   A CD1  1 
ATOM   1944 C CD1  B LEU   A 1 88  ? 23.206 4.512   11.986  0.70 16.34 ?  88  LEU   A CD1  1 
ATOM   1945 C CD2  A LEU   A 1 88  ? 22.365 4.932   13.825  0.30 17.15 ?  88  LEU   A CD2  1 
ATOM   1946 C CD2  B LEU   A 1 88  ? 22.289 4.970   14.276  0.70 17.44 ?  88  LEU   A CD2  1 
ATOM   1947 H H    A LEU   A 1 88  ? 25.928 3.654   15.088  0.30 19.42 ?  88  LEU   A H    1 
ATOM   1948 H H    B LEU   A 1 88  ? 25.950 3.679   15.181  0.70 18.11 ?  88  LEU   A H    1 
ATOM   1949 H HA   A LEU   A 1 88  ? 23.345 3.079   15.670  0.30 18.95 ?  88  LEU   A HA   1 
ATOM   1950 H HA   B LEU   A 1 88  ? 23.401 3.117   15.903  0.70 17.89 ?  88  LEU   A HA   1 
ATOM   1951 H HB2  A LEU   A 1 88  ? 24.672 2.615   13.227  0.30 19.31 ?  88  LEU   A HB2  1 
ATOM   1952 H HB2  B LEU   A 1 88  ? 24.611 2.761   13.379  0.70 18.27 ?  88  LEU   A HB2  1 
ATOM   1953 H HB3  A LEU   A 1 88  ? 23.125 2.399   13.475  0.30 19.31 ?  88  LEU   A HB3  1 
ATOM   1954 H HB3  B LEU   A 1 88  ? 23.085 2.468   13.686  0.70 18.27 ?  88  LEU   A HB3  1 
ATOM   1955 H HG   A LEU   A 1 88  ? 24.361 4.928   13.398  0.30 19.90 ?  88  LEU   A HG   1 
ATOM   1956 H HG   B LEU   A 1 88  ? 24.238 5.039   13.661  0.70 19.53 ?  88  LEU   A HG   1 
ATOM   1957 H HD11 A LEU   A 1 88  ? 23.313 5.232   11.347  0.30 19.88 ?  88  LEU   A HD11 1 
ATOM   1958 H HD11 B LEU   A 1 88  ? 22.988 5.425   11.736  0.70 19.61 ?  88  LEU   A HD11 1 
ATOM   1959 H HD12 A LEU   A 1 88  ? 24.292 3.983   11.276  0.30 19.88 ?  88  LEU   A HD12 1 
ATOM   1960 H HD12 B LEU   A 1 88  ? 23.994 4.217   11.503  0.70 19.61 ?  88  LEU   A HD12 1 
ATOM   1961 H HD13 A LEU   A 1 88  ? 22.726 3.757   11.425  0.30 19.88 ?  88  LEU   A HD13 1 
ATOM   1962 H HD13 B LEU   A 1 88  ? 22.456 3.928   11.781  0.70 19.61 ?  88  LEU   A HD13 1 
ATOM   1963 H HD21 A LEU   A 1 88  ? 22.165 5.787   13.416  0.30 20.58 ?  88  LEU   A HD21 1 
ATOM   1964 H HD21 B LEU   A 1 88  ? 21.985 5.803   13.884  0.70 20.93 ?  88  LEU   A HD21 1 
ATOM   1965 H HD22 A LEU   A 1 88  ? 21.627 4.318   13.689  0.30 20.58 ?  88  LEU   A HD22 1 
ATOM   1966 H HD22 B LEU   A 1 88  ? 21.582 4.308   14.241  0.70 20.93 ?  88  LEU   A HD22 1 
ATOM   1967 H HD23 A LEU   A 1 88  ? 22.529 5.048   14.774  0.30 20.58 ?  88  LEU   A HD23 1 
ATOM   1968 H HD23 B LEU   A 1 88  ? 22.564 5.115   15.194  0.70 20.93 ?  88  LEU   A HD23 1 
ATOM   1969 N N    . ALA   A 1 89  ? 25.652 0.911   15.570  1.00 14.86 ?  89  ALA   A N    1 
ATOM   1970 C CA   . ALA   A 1 89  ? 25.990 -0.499  15.675  1.00 14.29 ?  89  ALA   A CA   1 
ATOM   1971 C C    . ALA   A 1 89  ? 27.478 -0.566  15.972  1.00 14.65 ?  89  ALA   A C    1 
ATOM   1972 O O    . ALA   A 1 89  ? 28.188 0.430   15.846  1.00 15.57 ?  89  ALA   A O    1 
ATOM   1973 C CB   . ALA   A 1 89  ? 25.692 -1.216  14.359  1.00 14.04 ?  89  ALA   A CB   1 
ATOM   1974 H H    A ALA   A 1 89  ? 26.339 1.429   15.538  0.30 17.83 ?  89  ALA   A H    1 
ATOM   1975 H H    B ALA   A 1 89  ? 26.337 1.416   15.439  0.70 17.83 ?  89  ALA   A H    1 
ATOM   1976 H HA   . ALA   A 1 89  ? 25.491 -0.916  16.397  1.00 17.15 ?  89  ALA   A HA   1 
ATOM   1977 H HB1  . ALA   A 1 89  ? 25.938 -2.152  14.444  1.00 16.85 ?  89  ALA   A HB1  1 
ATOM   1978 H HB2  . ALA   A 1 89  ? 24.744 -1.142  14.162  1.00 16.85 ?  89  ALA   A HB2  1 
ATOM   1979 H HB3  . ALA   A 1 89  ? 26.209 -0.804  13.649  1.00 16.85 ?  89  ALA   A HB3  1 
ATOM   1980 N N    . LYS   A 1 90  ? 27.963 -1.745  16.350  1.00 15.31 ?  90  LYS   A N    1 
ATOM   1981 C CA   . LYS   A 1 90  ? 29.408 -1.883  16.489  1.00 15.83 ?  90  LYS   A CA   1 
ATOM   1982 C C    . LYS   A 1 90  ? 30.096 -1.688  15.140  1.00 14.69 ?  90  LYS   A C    1 
ATOM   1983 O O    . LYS   A 1 90  ? 31.032 -0.881  15.007  1.00 15.82 ?  90  LYS   A O    1 
ATOM   1984 C CB   . LYS   A 1 90  ? 29.758 -3.237  17.106  1.00 18.41 ?  90  LYS   A CB   1 
ATOM   1985 C CG   . LYS   A 1 90  ? 31.230 -3.361  17.463  1.00 22.93 ?  90  LYS   A CG   1 
ATOM   1986 C CD   . LYS   A 1 90  ? 31.481 -4.568  18.351  1.00 27.61 ?  90  LYS   A CD   1 
ATOM   1987 C CE   . LYS   A 1 90  ? 32.903 -4.579  18.893  1.00 31.85 ?  90  LYS   A CE   1 
ATOM   1988 N NZ   . LYS   A 1 90  ? 33.914 -4.834  17.833  1.00 33.75 ?  90  LYS   A NZ   1 
ATOM   1989 H H    . LYS   A 1 90  ? 27.496 -2.445  16.527  1.00 18.37 ?  90  LYS   A H    1 
ATOM   1990 H HA   . LYS   A 1 90  ? 29.729 -1.193  17.085  1.00 18.99 ?  90  LYS   A HA   1 
ATOM   1991 H HB2  . LYS   A 1 90  ? 29.240 -3.354  17.921  1.00 22.09 ?  90  LYS   A HB2  1 
ATOM   1992 H HB3  . LYS   A 1 90  ? 29.540 -3.940  16.475  1.00 22.09 ?  90  LYS   A HB3  1 
ATOM   1993 H HG2  . LYS   A 1 90  ? 31.747 -3.466  16.650  1.00 27.52 ?  90  LYS   A HG2  1 
ATOM   1994 H HG3  . LYS   A 1 90  ? 31.510 -2.565  17.942  1.00 27.52 ?  90  LYS   A HG3  1 
ATOM   1995 H HD2  . LYS   A 1 90  ? 30.868 -4.545  19.103  1.00 33.13 ?  90  LYS   A HD2  1 
ATOM   1996 H HD3  . LYS   A 1 90  ? 31.346 -5.378  17.834  1.00 33.13 ?  90  LYS   A HD3  1 
ATOM   1997 H HE2  . LYS   A 1 90  ? 33.097 -3.715  19.292  1.00 38.22 ?  90  LYS   A HE2  1 
ATOM   1998 H HE3  . LYS   A 1 90  ? 32.983 -5.277  19.561  1.00 38.22 ?  90  LYS   A HE3  1 
ATOM   1999 H HZ1  . LYS   A 1 90  ? 34.732 -4.834  18.186  1.00 40.50 ?  90  LYS   A HZ1  1 
ATOM   2000 H HZ2  . LYS   A 1 90  ? 33.764 -5.626  17.455  1.00 40.50 ?  90  LYS   A HZ2  1 
ATOM   2001 H HZ3  . LYS   A 1 90  ? 33.868 -4.202  17.209  1.00 40.50 ?  90  LYS   A HZ3  1 
ATOM   2002 N N    . HIS   A 1 91  ? 29.618 -2.401  14.122  1.00 13.03 ?  91  HIS   A N    1 
ATOM   2003 C CA   . HIS   A 1 91  ? 30.182 -2.385  12.785  1.00 12.35 ?  91  HIS   A CA   1 
ATOM   2004 C C    . HIS   A 1 91  ? 29.086 -2.118  11.768  1.00 11.56 ?  91  HIS   A C    1 
ATOM   2005 O O    . HIS   A 1 91  ? 27.916 -2.466  11.981  1.00 12.13 ?  91  HIS   A O    1 
ATOM   2006 C CB   . HIS   A 1 91  ? 30.783 -3.750  12.421  1.00 14.35 ?  91  HIS   A CB   1 
ATOM   2007 C CG   . HIS   A 1 91  ? 31.787 -4.255  13.406  1.00 18.61 ?  91  HIS   A CG   1 
ATOM   2008 N ND1  . HIS   A 1 91  ? 33.064 -3.746  13.492  1.00 20.73 ?  91  HIS   A ND1  1 
ATOM   2009 C CD2  . HIS   A 1 91  ? 31.708 -5.232  14.340  1.00 20.49 ?  91  HIS   A CD2  1 
ATOM   2010 C CE1  . HIS   A 1 91  ? 33.728 -4.383  14.440  1.00 21.67 ?  91  HIS   A CE1  1 
ATOM   2011 N NE2  . HIS   A 1 91  ? 32.927 -5.291  14.970  1.00 21.79 ?  91  HIS   A NE2  1 
ATOM   2012 H H    . HIS   A 1 91  ? 28.933 -2.932  14.191  1.00 15.63 ?  91  HIS   A H    1 
ATOM   2013 H HA   . HIS   A 1 91  ? 30.867 -1.711  12.714  1.00 14.82 ?  91  HIS   A HA   1 
ATOM   2014 H HB2  . HIS   A 1 91  ? 30.070 -4.411  12.371  1.00 17.22 ?  91  HIS   A HB2  1 
ATOM   2015 H HB3  . HIS   A 1 91  ? 31.224 -3.684  11.560  1.00 17.22 ?  91  HIS   A HB3  1 
ATOM   2016 H HD1  . HIS   A 1 91  ? 33.381 -3.112  13.002  1.00 24.88 ?  91  HIS   A HD1  1 
ATOM   2017 H HD2  . HIS   A 1 91  ? 30.972 -5.763  14.527  1.00 24.59 ?  91  HIS   A HD2  1 
ATOM   2018 H HE1  . HIS   A 1 91  ? 34.612 -4.216  14.690  1.00 26.00 ?  91  HIS   A HE1  1 
ATOM   2019 N N    . CYS   A 1 92  ? 29.485 -1.530  10.643  1.00 11.04 ?  92  CYS   A N    1 
ATOM   2020 C CA   . CYS   A 1 92  ? 28.639 -1.449  9.463   1.00 11.00 ?  92  CYS   A CA   1 
ATOM   2021 C C    . CYS   A 1 92  ? 29.289 -2.253  8.348   1.00 10.09 ?  92  CYS   A C    1 
ATOM   2022 O O    . CYS   A 1 92  ? 30.444 -1.993  7.981   1.00 10.88 ?  92  CYS   A O    1 
ATOM   2023 C CB   . CYS   A 1 92  ? 28.426 -0.003  9.011   1.00 11.08 ?  92  CYS   A CB   1 
ATOM   2024 S SG   . CYS   A 1 92  ? 27.400 0.107   7.512   1.00 10.72 ?  92  CYS   A SG   1 
ATOM   2025 H H    . CYS   A 1 92  ? 30.257 -1.160  10.541  1.00 13.24 ?  92  CYS   A H    1 
ATOM   2026 H HA   . CYS   A 1 92  ? 27.774 -1.840  9.660   1.00 13.20 ?  92  CYS   A HA   1 
ATOM   2027 H HB2  . CYS   A 1 92  ? 27.972 0.487   9.715   1.00 13.30 ?  92  CYS   A HB2  1 
ATOM   2028 H HB3  . CYS   A 1 92  ? 29.280 0.402   8.815   1.00 13.30 ?  92  CYS   A HB3  1 
ATOM   2029 H HG   . CYS   A 1 92  ? 27.257 1.259   7.218   1.00 12.87 ?  92  CYS   A HG   1 
ATOM   2030 N N    . LEU   A 1 93  ? 28.556 -3.241  7.836   1.00 10.07 ?  93  LEU   A N    1 
ATOM   2031 C CA   . LEU   A 1 93  ? 28.964 -3.992  6.654   1.00 9.59  ?  93  LEU   A CA   1 
ATOM   2032 C C    . LEU   A 1 93  ? 28.356 -3.304  5.438   1.00 9.17  ?  93  LEU   A C    1 
ATOM   2033 O O    . LEU   A 1 93  ? 27.139 -3.361  5.226   1.00 9.69  ?  93  LEU   A O    1 
ATOM   2034 C CB   . LEU   A 1 93  ? 28.489 -5.440  6.759   1.00 10.21 ?  93  LEU   A CB   1 
ATOM   2035 C CG   . LEU   A 1 93  ? 28.876 -6.322  5.573   1.00 10.26 ?  93  LEU   A CG   1 
ATOM   2036 C CD1  . LEU   A 1 93  ? 30.377 -6.562  5.549   1.00 11.41 ?  93  LEU   A CD1  1 
ATOM   2037 C CD2  . LEU   A 1 93  ? 28.107 -7.651  5.586   1.00 11.08 ?  93  LEU   A CD2  1 
ATOM   2038 H H    . LEU   A 1 93  ? 27.802 -3.497  8.168   1.00 12.08 ?  93  LEU   A H    1 
ATOM   2039 H HA   . LEU   A 1 93  ? 29.925 -3.976  6.576   1.00 11.51 ?  93  LEU   A HA   1 
ATOM   2040 H HB2  . LEU   A 1 93  ? 28.874 -5.834  7.557   1.00 12.25 ?  93  LEU   A HB2  1 
ATOM   2041 H HB3  . LEU   A 1 93  ? 27.522 -5.448  6.824   1.00 12.25 ?  93  LEU   A HB3  1 
ATOM   2042 H HG   . LEU   A 1 93  ? 28.647 -5.864  4.754   1.00 12.32 ?  93  LEU   A HG   1 
ATOM   2043 H HD11 . LEU   A 1 93  ? 30.595 -7.174  4.827   1.00 13.69 ?  93  LEU   A HD11 1 
ATOM   2044 H HD12 . LEU   A 1 93  ? 30.838 -5.717  5.411   1.00 13.69 ?  93  LEU   A HD12 1 
ATOM   2045 H HD13 . LEU   A 1 93  ? 30.656 -6.949  6.399   1.00 13.69 ?  93  LEU   A HD13 1 
ATOM   2046 H HD21 . LEU   A 1 93  ? 28.388 -8.184  4.818   1.00 13.30 ?  93  LEU   A HD21 1 
ATOM   2047 H HD22 . LEU   A 1 93  ? 28.312 -8.131  6.404   1.00 13.30 ?  93  LEU   A HD22 1 
ATOM   2048 H HD23 . LEU   A 1 93  ? 27.160 -7.472  5.531   1.00 13.30 ?  93  LEU   A HD23 1 
ATOM   2049 N N    . HIS   A 1 94  ? 29.194 -2.605  4.670   1.00 9.17  ?  94  HIS   A N    1 
ATOM   2050 C CA   . HIS   A 1 94  ? 28.757 -1.929  3.454   1.00 9.11  ?  94  HIS   A CA   1 
ATOM   2051 C C    . HIS   A 1 94  ? 28.766 -2.946  2.331   1.00 9.09  ?  94  HIS   A C    1 
ATOM   2052 O O    . HIS   A 1 94  ? 29.827 -3.469  1.992   1.00 10.70 ?  94  HIS   A O    1 
ATOM   2053 C CB   . HIS   A 1 94  ? 29.698 -0.768  3.118   1.00 9.28  ?  94  HIS   A CB   1 
ATOM   2054 C CG   . HIS   A 1 94  ? 29.689 0.312   4.142   1.00 9.33  ?  94  HIS   A CG   1 
ATOM   2055 N ND1  . HIS   A 1 94  ? 28.812 1.375   4.101   1.00 9.71  ?  94  HIS   A ND1  1 
ATOM   2056 C CD2  . HIS   A 1 94  ? 30.447 0.479   5.251   1.00 9.88  ?  94  HIS   A CD2  1 
ATOM   2057 C CE1  . HIS   A 1 94  ? 29.034 2.149   5.147   1.00 9.72  ?  94  HIS   A CE1  1 
ATOM   2058 N NE2  . HIS   A 1 94  ? 30.020 1.630   5.862   1.00 10.25 ?  94  HIS   A NE2  1 
ATOM   2059 H H    . HIS   A 1 94  ? 30.033 -2.511  4.834   1.00 11.00 ?  94  HIS   A H    1 
ATOM   2060 H HA   . HIS   A 1 94  ? 27.854 -1.590  3.566   1.00 10.93 ?  94  HIS   A HA   1 
ATOM   2061 H HB2  . HIS   A 1 94  ? 30.599 -1.106  3.048   1.00 11.14 ?  94  HIS   A HB2  1 
ATOM   2062 H HB3  . HIS   A 1 94  ? 29.419 -0.378  2.274   1.00 11.14 ?  94  HIS   A HB3  1 
ATOM   2063 H HD2  . HIS   A 1 94  ? 31.126 -0.079  5.547   1.00 11.86 ?  94  HIS   A HD2  1 
ATOM   2064 H HE1  . HIS   A 1 94  ? 28.569 2.932   5.345   1.00 11.66 ?  94  HIS   A HE1  1 
ATOM   2065 H HE2  . HIS   A 1 94  ? 30.340 1.970   6.581   1.00 12.30 ?  94  HIS   A HE2  1 
ATOM   2066 N N    . VAL   A 1 95  ? 27.594 -3.253  1.776   1.00 8.95  ?  95  VAL   A N    1 
ATOM   2067 C CA   . VAL   A 1 95  ? 27.446 -4.294  0.764   1.00 9.05  ?  95  VAL   A CA   1 
ATOM   2068 C C    . VAL   A 1 95  ? 26.891 -3.665  -0.502  1.00 8.94  ?  95  VAL   A C    1 
ATOM   2069 O O    . VAL   A 1 95  ? 25.890 -2.935  -0.447  1.00 9.92  ?  95  VAL   A O    1 
ATOM   2070 C CB   . VAL   A 1 95  ? 26.511 -5.424  1.232   1.00 9.87  ?  95  VAL   A CB   1 
ATOM   2071 C CG1  . VAL   A 1 95  ? 26.373 -6.468  0.134   1.00 10.44 ?  95  VAL   A CG1  1 
ATOM   2072 C CG2  . VAL   A 1 95  ? 27.025 -6.044  2.520   1.00 9.91  ?  95  VAL   A CG2  1 
ATOM   2073 H H    . VAL   A 1 95  ? 26.856 -2.868  1.979   1.00 10.74 ?  95  VAL   A H    1 
ATOM   2074 H HA   . VAL   A 1 95  ? 28.314 -4.675  0.556   1.00 10.86 ?  95  VAL   A HA   1 
ATOM   2075 H HB   . VAL   A 1 95  ? 25.637 -5.059  1.405   1.00 11.84 ?  95  VAL   A HB   1 
ATOM   2076 H HG11 . VAL   A 1 95  ? 25.993 -7.280  0.511   1.00 12.53 ?  95  VAL   A HG11 1 
ATOM   2077 H HG12 . VAL   A 1 95  ? 25.794 -6.131  -0.566  1.00 12.53 ?  95  VAL   A HG12 1 
ATOM   2078 H HG13 . VAL   A 1 95  ? 27.254 -6.669  -0.235  1.00 12.53 ?  95  VAL   A HG13 1 
ATOM   2079 H HG21 . VAL   A 1 95  ? 26.461 -6.794  2.755   1.00 11.89 ?  95  VAL   A HG21 1 
ATOM   2080 H HG22 . VAL   A 1 95  ? 27.939 -6.342  2.386   1.00 11.89 ?  95  VAL   A HG22 1 
ATOM   2081 H HG23 . VAL   A 1 95  ? 26.996 -5.373  3.221   1.00 11.89 ?  95  VAL   A HG23 1 
ATOM   2082 N N    A VAL   A 1 96  ? 27.545 -3.936  -1.630  0.30 9.43  ?  96  VAL   A N    1 
ATOM   2083 N N    B VAL   A 1 96  ? 27.495 -3.976  -1.645  0.70 9.08  ?  96  VAL   A N    1 
ATOM   2084 C CA   A VAL   A 1 96  ? 27.192 -3.347  -2.917  0.30 9.95  ?  96  VAL   A CA   1 
ATOM   2085 C CA   B VAL   A 1 96  ? 27.060 -3.426  -2.924  0.70 9.33  ?  96  VAL   A CA   1 
ATOM   2086 C C    A VAL   A 1 96  ? 26.406 -4.384  -3.709  0.30 10.13 ?  96  VAL   A C    1 
ATOM   2087 C C    B VAL   A 1 96  ? 26.259 -4.480  -3.680  0.70 9.84  ?  96  VAL   A C    1 
ATOM   2088 O O    A VAL   A 1 96  ? 26.982 -5.278  -4.335  0.30 10.71 ?  96  VAL   A O    1 
ATOM   2089 O O    B VAL   A 1 96  ? 26.822 -5.443  -4.209  0.70 10.87 ?  96  VAL   A O    1 
ATOM   2090 C CB   A VAL   A 1 96  ? 28.431 -2.878  -3.685  0.30 10.48 ?  96  VAL   A CB   1 
ATOM   2091 C CB   B VAL   A 1 96  ? 28.241 -2.929  -3.763  0.70 9.63  ?  96  VAL   A CB   1 
ATOM   2092 C CG1  A VAL   A 1 96  ? 28.015 -2.213  -4.993  0.30 11.00 ?  96  VAL   A CG1  1 
ATOM   2093 C CG1  B VAL   A 1 96  ? 27.715 -2.305  -5.041  0.70 9.61  ?  96  VAL   A CG1  1 
ATOM   2094 C CG2  A VAL   A 1 96  ? 29.260 -1.929  -2.837  0.30 10.63 ?  96  VAL   A CG2  1 
ATOM   2095 C CG2  B VAL   A 1 96  ? 29.085 -1.934  -2.975  0.70 10.25 ?  96  VAL   A CG2  1 
ATOM   2096 H H    A VAL   A 1 96  ? 28.222 -4.468  -1.674  0.30 11.31 ?  96  VAL   A H    1 
ATOM   2097 H H    B VAL   A 1 96  ? 28.171 -4.510  -1.710  0.70 10.90 ?  96  VAL   A H    1 
ATOM   2098 H HA   A VAL   A 1 96  ? 26.622 -2.581  -2.772  0.30 11.93 ?  96  VAL   A HA   1 
ATOM   2099 H HA   B VAL   A 1 96  ? 26.479 -2.669  -2.760  0.70 11.20 ?  96  VAL   A HA   1 
ATOM   2100 H HB   A VAL   A 1 96  ? 28.984 -3.644  -3.903  0.30 12.58 ?  96  VAL   A HB   1 
ATOM   2101 H HB   B VAL   A 1 96  ? 28.803 -3.678  -4.005  0.70 11.55 ?  96  VAL   A HB   1 
ATOM   2102 H HG11 A VAL   A 1 96  ? 28.793 -1.799  -5.398  0.30 13.20 ?  96  VAL   A HG11 1 
ATOM   2103 H HG11 B VAL   A 1 96  ? 28.432 -1.803  -5.463  0.70 11.53 ?  96  VAL   A HG11 1 
ATOM   2104 H HG12 A VAL   A 1 96  ? 27.651 -2.884  -5.591  0.30 13.20 ?  96  VAL   A HG12 1 
ATOM   2105 H HG12 B VAL   A 1 96  ? 27.410 -3.005  -5.636  0.70 11.53 ?  96  VAL   A HG12 1 
ATOM   2106 H HG13 A VAL   A 1 96  ? 27.344 -1.538  -4.805  0.30 13.20 ?  96  VAL   A HG13 1 
ATOM   2107 H HG13 B VAL   A 1 96  ? 26.982 -1.708  -4.824  0.70 11.53 ?  96  VAL   A HG13 1 
ATOM   2108 H HG21 A VAL   A 1 96  ? 29.988 -1.580  -3.374  0.30 12.76 ?  96  VAL   A HG21 1 
ATOM   2109 H HG21 B VAL   A 1 96  ? 29.778 -1.579  -3.549  0.70 12.30 ?  96  VAL   A HG21 1 
ATOM   2110 H HG22 A VAL   A 1 96  ? 28.693 -1.202  -2.536  0.30 12.76 ?  96  VAL   A HG22 1 
ATOM   2111 H HG22 B VAL   A 1 96  ? 28.514 -1.215  -2.658  0.70 12.30 ?  96  VAL   A HG22 1 
ATOM   2112 H HG23 A VAL   A 1 96  ? 29.612 -2.413  -2.075  0.30 12.76 ?  96  VAL   A HG23 1 
ATOM   2113 H HG23 B VAL   A 1 96  ? 29.484 -2.392  -2.217  0.70 12.30 ?  96  VAL   A HG23 1 
ATOM   2114 N N    A GLY   A 1 97  ? 25.084 -4.263  -3.697  0.30 10.62 ?  97  GLY   A N    1 
ATOM   2115 N N    B GLY   A 1 97  ? 24.945 -4.300  -3.755  0.70 9.99  ?  97  GLY   A N    1 
ATOM   2116 C CA   A GLY   A 1 97  ? 24.258 -5.002  -4.616  0.30 10.66 ?  97  GLY   A CA   1 
ATOM   2117 C CA   B GLY   A 1 97  ? 24.140 -5.072  -4.669  0.70 10.91 ?  97  GLY   A CA   1 
ATOM   2118 C C    A GLY   A 1 97  ? 24.207 -4.282  -5.949  0.30 10.20 ?  97  GLY   A C    1 
ATOM   2119 C C    B GLY   A 1 97  ? 24.208 -4.486  -6.066  0.70 11.52 ?  97  GLY   A C    1 
ATOM   2120 O O    A GLY   A 1 97  ? 24.443 -3.073  -6.028  0.30 9.88  ?  97  GLY   A O    1 
ATOM   2121 O O    B GLY   A 1 97  ? 24.598 -3.329  -6.259  0.70 12.06 ?  97  GLY   A O    1 
ATOM   2122 H H    A GLY   A 1 97  ? 24.648 -3.750  -3.160  0.30 12.74 ?  97  GLY   A H    1 
ATOM   2123 H H    B GLY   A 1 97  ? 24.498 -3.737  -3.272  0.70 11.99 ?  97  GLY   A H    1 
ATOM   2124 H HA2  A GLY   A 1 97  ? 24.630 -5.888  -4.742  0.30 12.79 ?  97  GLY   A HA2  1 
ATOM   2125 H HA2  B GLY   A 1 97  ? 24.466 -5.982  -4.690  0.70 13.09 ?  97  GLY   A HA2  1 
ATOM   2126 H HA3  A GLY   A 1 97  ? 23.360 -5.084  -4.258  0.30 12.79 ?  97  GLY   A HA3  1 
ATOM   2127 H HA3  B GLY   A 1 97  ? 23.215 -5.075  -4.369  0.70 13.09 ?  97  GLY   A HA3  1 
ATOM   2128 N N    A PRO   A 1 98  ? 23.909 -5.005  -7.026  0.30 10.02 ?  98  PRO   A N    1 
ATOM   2129 N N    B PRO   A 1 98  ? 23.821 -5.269  -7.070  0.70 11.90 ?  98  PRO   A N    1 
ATOM   2130 C CA   A PRO   A 1 98  ? 23.822 -4.356  -8.339  0.30 9.93  ?  98  PRO   A CA   1 
ATOM   2131 C CA   B PRO   A 1 98  ? 23.784 -4.748  -8.438  0.70 13.39 ?  98  PRO   A CA   1 
ATOM   2132 C C    A PRO   A 1 98  ? 22.685 -3.346  -8.402  0.30 10.32 ?  98  PRO   A C    1 
ATOM   2133 C C    B PRO   A 1 98  ? 22.707 -3.691  -8.602  0.70 14.10 ?  98  PRO   A C    1 
ATOM   2134 O O    A PRO   A 1 98  ? 21.593 -3.576  -7.877  0.30 10.37 ?  98  PRO   A O    1 
ATOM   2135 O O    B PRO   A 1 98  ? 21.618 -3.785  -8.031  0.70 14.32 ?  98  PRO   A O    1 
ATOM   2136 C CB   A PRO   A 1 98  ? 23.574 -5.526  -9.294  0.30 10.28 ?  98  PRO   A CB   1 
ATOM   2137 C CB   B PRO   A 1 98  ? 23.452 -5.988  -9.274  0.70 13.56 ?  98  PRO   A CB   1 
ATOM   2138 C CG   A PRO   A 1 98  ? 22.976 -6.596  -8.432  0.30 10.84 ?  98  PRO   A CG   1 
ATOM   2139 C CG   B PRO   A 1 98  ? 22.732 -6.896  -8.332  0.70 13.36 ?  98  PRO   A CG   1 
ATOM   2140 C CD   A PRO   A 1 98  ? 23.671 -6.457  -7.112  0.30 10.61 ?  98  PRO   A CD   1 
ATOM   2141 C CD   B PRO   A 1 98  ? 23.402 -6.678  -7.003  0.70 12.25 ?  98  PRO   A CD   1 
ATOM   2142 H HA   A PRO   A 1 98  ? 24.661 -3.924  -8.557  0.30 11.91 ?  98  PRO   A HA   1 
ATOM   2143 H HA   B PRO   A 1 98  ? 24.648 -4.386  -8.692  0.70 16.07 ?  98  PRO   A HA   1 
ATOM   2144 H HB2  A PRO   A 1 98  ? 22.950 -5.258  -9.984  0.30 12.34 ?  98  PRO   A HB2  1 
ATOM   2145 H HB2  B PRO   A 1 98  ? 22.879 -5.733  -10.013 0.70 16.27 ?  98  PRO   A HB2  1 
ATOM   2146 H HB3  A PRO   A 1 98  ? 24.412 -5.824  -9.675  0.30 12.34 ?  98  PRO   A HB3  1 
ATOM   2147 H HB3  B PRO   A 1 98  ? 24.271 -6.393  -9.591  0.70 16.27 ?  98  PRO   A HB3  1 
ATOM   2148 H HG2  A PRO   A 1 98  ? 22.023 -6.445  -8.332  0.30 13.01 ?  98  PRO   A HG2  1 
ATOM   2149 H HG2  B PRO   A 1 98  ? 21.796 -6.649  -8.286  0.70 16.03 ?  98  PRO   A HG2  1 
ATOM   2150 H HG3  A PRO   A 1 98  ? 23.149 -7.467  -8.820  0.30 13.01 ?  98  PRO   A HG3  1 
ATOM   2151 H HG3  B PRO   A 1 98  ? 22.837 -7.814  -8.619  0.70 16.03 ?  98  PRO   A HG3  1 
ATOM   2152 H HD2  A PRO   A 1 98  ? 23.097 -6.755  -6.385  0.30 12.73 ?  98  PRO   A HD2  1 
ATOM   2153 H HD2  B PRO   A 1 98  ? 22.773 -6.810  -6.274  0.70 14.70 ?  98  PRO   A HD2  1 
ATOM   2154 H HD3  A PRO   A 1 98  ? 24.517 -6.938  -7.113  0.30 12.73 ?  98  PRO   A HD3  1 
ATOM   2155 H HD3  B PRO   A 1 98  ? 24.179 -7.253  -6.908  0.70 14.70 ?  98  PRO   A HD3  1 
ATOM   2156 N N    A ASN   A 1 99  ? 22.954 -2.218  -9.059  0.30 10.36 ?  99  ASN   A N    1 
ATOM   2157 N N    B ASN   A 1 99  ? 23.025 -2.679  -9.395  0.70 15.34 ?  99  ASN   A N    1 
ATOM   2158 C CA   A ASN   A 1 99  ? 21.964 -1.164  -9.282  0.30 10.67 ?  99  ASN   A CA   1 
ATOM   2159 C CA   B ASN   A 1 99  ? 22.061 -1.673  -9.817  0.70 17.66 ?  99  ASN   A CA   1 
ATOM   2160 C C    A ASN   A 1 99  ? 21.393 -1.335  -10.689 0.30 11.53 ?  99  ASN   A C    1 
ATOM   2161 C C    B ASN   A 1 99  ? 21.595 -2.043  -11.220 0.70 18.99 ?  99  ASN   A C    1 
ATOM   2162 O O    A ASN   A 1 99  ? 22.048 -1.000  -11.683 0.30 12.64 ?  99  ASN   A O    1 
ATOM   2163 O O    B ASN   A 1 99  ? 22.328 -1.859  -12.196 0.70 19.16 ?  99  ASN   A O    1 
ATOM   2164 C CB   A ASN   A 1 99  ? 22.610 0.207   -9.114  0.30 10.81 ?  99  ASN   A CB   1 
ATOM   2165 C CB   B ASN   A 1 99  ? 22.700 -0.290  -9.808  0.70 20.06 ?  99  ASN   A CB   1 
ATOM   2166 C CG   A ASN   A 1 99  ? 21.597 1.350   -9.144  0.30 10.51 ?  99  ASN   A CG   1 
ATOM   2167 C CG   B ASN   A 1 99  ? 21.711 0.804   -10.137 0.70 21.46 ?  99  ASN   A CG   1 
ATOM   2168 O OD1  A ASN   A 1 99  ? 20.627 1.322   -9.901  0.30 11.02 ?  99  ASN   A OD1  1 
ATOM   2169 O OD1  B ASN   A 1 99  ? 20.671 0.546   -10.734 0.70 21.24 ?  99  ASN   A OD1  1 
ATOM   2170 N ND2  A ASN   A 1 99  ? 21.825 2.359   -8.315  0.30 11.00 ?  99  ASN   A ND2  1 
ATOM   2171 N ND2  B ASN   A 1 99  ? 22.030 2.033   -9.751  0.70 23.05 ?  99  ASN   A ND2  1 
ATOM   2172 H H    A ASN   A 1 99  ? 23.731 -2.033  -9.373  0.30 12.43 ?  99  ASN   A H    1 
ATOM   2173 H H    B ASN   A 1 99  ? 23.817 -2.542  -9.698  0.70 18.41 ?  99  ASN   A H    1 
ATOM   2174 H HA   A ASN   A 1 99  ? 21.244 -1.257  -8.633  0.30 12.80 ?  99  ASN   A HA   1 
ATOM   2175 H HA   B ASN   A 1 99  ? 21.293 -1.671  -9.224  0.70 21.19 ?  99  ASN   A HA   1 
ATOM   2176 H HB2  A ASN   A 1 99  ? 23.079 0.239   -8.268  0.30 12.97 ?  99  ASN   A HB2  1 
ATOM   2177 H HB2  B ASN   A 1 99  ? 23.058 -0.111  -8.929  0.70 24.07 ?  99  ASN   A HB2  1 
ATOM   2178 H HB3  A ASN   A 1 99  ? 23.236 0.345   -9.845  0.30 12.97 ?  99  ASN   A HB3  1 
ATOM   2179 H HB3  B ASN   A 1 99  ? 23.405 -0.262  -10.473 0.70 24.07 ?  99  ASN   A HB3  1 
ATOM   2180 H HD21 A ASN   A 1 99  ? 21.285 3.027   -8.294  0.30 13.20 ?  99  ASN   A HD21 1 
ATOM   2181 H HD21 B ASN   A 1 99  ? 21.505 2.697   -9.920  0.70 27.66 ?  99  ASN   A HD21 1 
ATOM   2182 H HD22 A ASN   A 1 99  ? 22.516 2.348   -7.802  0.30 13.20 ?  99  ASN   A HD22 1 
ATOM   2183 H HD22 B ASN   A 1 99  ? 22.772 2.172   -9.342  0.70 27.66 ?  99  ASN   A HD22 1 
ATOM   2184 N N    A VAL   A 1 100 ? 20.160 -1.854  -10.763 0.30 12.62 ?  100 VAL   A N    1 
ATOM   2185 N N    B VAL   A 1 100 ? 20.373 -2.571  -11.321 0.70 22.00 ?  100 VAL   A N    1 
ATOM   2186 C CA   A VAL   A 1 100 ? 19.522 -2.104  -12.054 0.30 14.30 ?  100 VAL   A CA   1 
ATOM   2187 C CA   B VAL   A 1 100 ? 19.842 -2.969  -12.620 0.70 25.35 ?  100 VAL   A CA   1 
ATOM   2188 C C    A VAL   A 1 100 ? 19.403 -0.814  -12.859 0.30 14.35 ?  100 VAL   A C    1 
ATOM   2189 C C    B VAL   A 1 100 ? 19.657 -1.775  -13.548 0.70 27.29 ?  100 VAL   A C    1 
ATOM   2190 O O    A VAL   A 1 100 ? 19.481 -0.829  -14.095 0.30 15.57 ?  100 VAL   A O    1 
ATOM   2191 O O    B VAL   A 1 100 ? 19.660 -1.941  -14.772 0.70 27.25 ?  100 VAL   A O    1 
ATOM   2192 C CB   A VAL   A 1 100 ? 18.156 -2.799  -11.849 0.30 15.75 ?  100 VAL   A CB   1 
ATOM   2193 C CB   B VAL   A 1 100 ? 18.535 -3.770  -12.437 0.70 27.16 ?  100 VAL   A CB   1 
ATOM   2194 C CG1  A VAL   A 1 100 ? 17.452 -3.021  -13.181 0.30 16.31 ?  100 VAL   A CG1  1 
ATOM   2195 C CG1  B VAL   A 1 100 ? 17.869 -4.044  -13.780 0.70 27.73 ?  100 VAL   A CG1  1 
ATOM   2196 C CG2  A VAL   A 1 100 ? 18.331 -4.128  -11.120 0.30 16.21 ?  100 VAL   A CG2  1 
ATOM   2197 C CG2  B VAL   A 1 100 ? 18.824 -5.072  -11.716 0.70 27.72 ?  100 VAL   A CG2  1 
ATOM   2198 H H    A VAL   A 1 100 ? 19.673 -2.068  -10.076 0.30 15.14 ?  100 VAL   A H    1 
ATOM   2199 H H    B VAL   A 1 100 ? 19.840 -2.703  -10.662 0.70 26.40 ?  100 VAL   A H    1 
ATOM   2200 H HA   A VAL   A 1 100 ? 20.077 -2.723  -12.553 0.30 17.17 ?  100 VAL   A HA   1 
ATOM   2201 H HA   B VAL   A 1 100 ? 20.482 -3.568  -13.036 0.70 30.42 ?  100 VAL   A HA   1 
ATOM   2202 H HB   A VAL   A 1 100 ? 17.587 -2.237  -11.300 0.30 18.90 ?  100 VAL   A HB   1 
ATOM   2203 H HB   B VAL   A 1 100 ? 17.920 -3.253  -11.898 0.70 32.59 ?  100 VAL   A HB   1 
ATOM   2204 H HG11 A VAL   A 1 100 ? 16.693 -3.614  -13.044 0.30 19.57 ?  100 VAL   A HG11 1 
ATOM   2205 H HG11 B VAL   A 1 100 ? 17.169 -4.706  -13.653 0.70 33.27 ?  100 VAL   A HG11 1 
ATOM   2206 H HG12 A VAL   A 1 100 ? 17.143 -2.168  -13.521 0.30 19.57 ?  100 VAL   A HG12 1 
ATOM   2207 H HG12 B VAL   A 1 100 ? 17.483 -3.222  -14.120 0.70 33.27 ?  100 VAL   A HG12 1 
ATOM   2208 H HG13 A VAL   A 1 100 ? 18.075 -3.425  -13.803 0.30 19.57 ?  100 VAL   A HG13 1 
ATOM   2209 H HG13 B VAL   A 1 100 ? 18.532 -4.383  -14.402 0.70 33.27 ?  100 VAL   A HG13 1 
ATOM   2210 H HG21 A VAL   A 1 100 ? 17.471 -4.576  -11.062 0.30 19.45 ?  100 VAL   A HG21 1 
ATOM   2211 H HG21 B VAL   A 1 100 ? 17.999 -5.572  -11.627 0.70 33.26 ?  100 VAL   A HG21 1 
ATOM   2212 H HG22 A VAL   A 1 100 ? 18.957 -4.679  -11.613 0.30 19.45 ?  100 VAL   A HG22 1 
ATOM   2213 H HG22 B VAL   A 1 100 ? 19.468 -5.584  -12.233 0.70 33.26 ?  100 VAL   A HG22 1 
ATOM   2214 H HG23 A VAL   A 1 100 ? 18.672 -3.957  -10.227 0.30 19.45 ?  100 VAL   A HG23 1 
ATOM   2215 H HG23 B VAL   A 1 100 ? 19.188 -4.873  -10.840 0.70 33.26 ?  100 VAL   A HG23 1 
ATOM   2216 N N    A ASN   A 1 101 ? 19.216 0.318   -12.181 0.30 14.50 ?  101 ASN   A N    1 
ATOM   2217 N N    B ASN   A 1 101 ? 19.483 -0.570  -12.999 0.70 28.75 ?  101 ASN   A N    1 
ATOM   2218 C CA   A ASN   A 1 101 ? 19.145 1.601   -12.869 0.30 15.68 ?  101 ASN   A CA   1 
ATOM   2219 C CA   B ASN   A 1 101 ? 19.404 0.621   -13.839 0.70 30.51 ?  101 ASN   A CA   1 
ATOM   2220 C C    A ASN   A 1 101 ? 20.495 2.048   -13.418 0.30 17.78 ?  101 ASN   A C    1 
ATOM   2221 C C    B ASN   A 1 101 ? 20.753 1.010   -14.435 0.70 31.24 ?  101 ASN   A C    1 
ATOM   2222 O O    A ASN   A 1 101 ? 20.560 3.089   -14.086 0.30 18.46 ?  101 ASN   A O    1 
ATOM   2223 O O    B ASN   A 1 101 ? 20.785 1.743   -15.429 0.70 31.47 ?  101 ASN   A O    1 
ATOM   2224 C CB   A ASN   A 1 101 ? 18.555 2.657   -11.934 0.30 15.12 ?  101 ASN   A CB   1 
ATOM   2225 C CB   B ASN   A 1 101 ? 18.797 1.788   -13.057 0.70 31.62 ?  101 ASN   A CB   1 
ATOM   2226 C CG   A ASN   A 1 101 ? 17.168 2.284   -11.442 0.30 15.10 ?  101 ASN   A CG   1 
ATOM   2227 C CG   B ASN   A 1 101 ? 17.286 1.708   -12.985 0.70 32.97 ?  101 ASN   A CG   1 
ATOM   2228 O OD1  A ASN   A 1 101 ? 16.344 1.768   -12.204 0.30 15.37 ?  101 ASN   A OD1  1 
ATOM   2229 O OD1  B ASN   A 1 101 ? 16.728 0.779   -12.399 0.70 33.07 ?  101 ASN   A OD1  1 
ATOM   2230 N ND2  A ASN   A 1 101 ? 16.903 2.540   -10.162 0.30 15.47 ?  101 ASN   A ND2  1 
ATOM   2231 N ND2  B ASN   A 1 101 ? 16.613 2.682   -13.585 0.70 33.64 ?  101 ASN   A ND2  1 
ATOM   2232 H H    A ASN   A 1 101 ? 19.120 0.358   -11.327 0.30 17.40 ?  101 ASN   A H    1 
ATOM   2233 H H    B ASN   A 1 101 ? 19.387 -0.424  -12.158 0.70 34.50 ?  101 ASN   A H    1 
ATOM   2234 H HA   A ASN   A 1 101 ? 18.537 1.498   -13.617 0.30 18.81 ?  101 ASN   A HA   1 
ATOM   2235 H HA   B ASN   A 1 101 ? 18.813 0.434   -14.580 0.70 36.61 ?  101 ASN   A HA   1 
ATOM   2236 H HB2  A ASN   A 1 101 ? 19.137 2.758   -11.166 0.30 18.15 ?  101 ASN   A HB2  1 
ATOM   2237 H HB2  B ASN   A 1 101 ? 19.139 1.780   -12.152 0.70 37.94 ?  101 ASN   A HB2  1 
ATOM   2238 H HB3  A ASN   A 1 101 ? 18.484 3.490   -12.416 0.30 18.15 ?  101 ASN   A HB3  1 
ATOM   2239 H HB3  B ASN   A 1 101 ? 19.034 2.620   -13.496 0.70 37.94 ?  101 ASN   A HB3  1 
ATOM   2240 H HD21 A ASN   A 1 101 ? 16.137 2.341   -9.828  0.30 18.57 ?  101 ASN   A HD21 1 
ATOM   2241 H HD21 B ASN   A 1 101 ? 15.753 2.679   -13.577 0.70 40.37 ?  101 ASN   A HD21 1 
ATOM   2242 H HD22 A ASN   A 1 101 ? 17.506 2.902   -9.661  0.30 18.57 ?  101 ASN   A HD22 1 
ATOM   2243 H HD22 B ASN   A 1 101 ? 17.036 3.317   -13.982 0.70 40.37 ?  101 ASN   A HD22 1 
ATOM   2244 N N    A LYS   A 1 102 ? 21.563 1.295   -13.147 0.30 19.55 ?  102 LYS   A N    1 
ATOM   2245 N N    B LYS   A 1 102 ? 21.857 0.542   -13.857 0.70 31.76 ?  102 LYS   A N    1 
ATOM   2246 C CA   A LYS   A 1 102 ? 22.850 1.474   -13.804 0.30 21.33 ?  102 LYS   A CA   1 
ATOM   2247 C CA   B LYS   A 1 102 ? 23.181 0.718   -14.442 0.70 31.88 ?  102 LYS   A CA   1 
ATOM   2248 C C    A LYS   A 1 102 ? 23.137 0.390   -14.834 0.30 21.84 ?  102 LYS   A C    1 
ATOM   2249 C C    B LYS   A 1 102 ? 23.570 -0.429  -15.369 0.70 30.64 ?  102 LYS   A C    1 
ATOM   2250 O O    A LYS   A 1 102 ? 24.193 0.430   -15.474 0.30 22.13 ?  102 LYS   A O    1 
ATOM   2251 O O    B LYS   A 1 102 ? 24.700 -0.448  -15.866 0.70 30.96 ?  102 LYS   A O    1 
ATOM   2252 C CB   A LYS   A 1 102 ? 23.981 1.509   -12.768 0.30 22.62 ?  102 LYS   A CB   1 
ATOM   2253 C CB   B LYS   A 1 102 ? 24.245 0.827   -13.341 0.70 33.59 ?  102 LYS   A CB   1 
ATOM   2254 C CG   A LYS   A 1 102 ? 23.885 2.647   -11.765 0.30 23.50 ?  102 LYS   A CG   1 
ATOM   2255 C CG   B LYS   A 1 102 ? 24.185 2.083   -12.485 0.70 35.32 ?  102 LYS   A CG   1 
ATOM   2256 C CD   A LYS   A 1 102 ? 25.035 2.592   -10.770 0.30 24.26 ?  102 LYS   A CD   1 
ATOM   2257 C CD   B LYS   A 1 102 ? 25.292 2.050   -11.437 0.70 37.23 ?  102 LYS   A CD   1 
ATOM   2258 C CE   A LYS   A 1 102 ? 24.965 3.728   -9.762  0.30 24.91 ?  102 LYS   A CE   1 
ATOM   2259 C CE   B LYS   A 1 102 ? 25.082 3.082   -10.342 0.70 38.71 ?  102 LYS   A CE   1 
ATOM   2260 N NZ   A LYS   A 1 102 ? 26.057 3.637   -8.752  0.30 25.27 ?  102 LYS   A NZ   1 
ATOM   2261 N NZ   B LYS   A 1 102 ? 25.702 2.646   -9.054  0.70 39.60 ?  102 LYS   A NZ   1 
ATOM   2262 H H    A LYS   A 1 102 ? 21.568 0.659   -12.564 0.30 23.46 ?  102 LYS   A H    1 
ATOM   2263 H H    B LYS   A 1 102 ? 21.865 0.114   -13.112 0.70 38.11 ?  102 LYS   A H    1 
ATOM   2264 H HA   A LYS   A 1 102 ? 22.850 2.317   -14.272 0.30 25.60 ?  102 LYS   A HA   1 
ATOM   2265 H HA   B LYS   A 1 102 ? 23.194 1.549   -14.946 0.70 38.26 ?  102 LYS   A HA   1 
ATOM   2266 H HB2  A LYS   A 1 102 ? 23.974 0.677   -12.269 0.30 27.15 ?  102 LYS   A HB2  1 
ATOM   2267 H HB2  B LYS   A 1 102 ? 24.150 0.068   -12.746 0.70 40.31 ?  102 LYS   A HB2  1 
ATOM   2268 H HB3  A LYS   A 1 102 ? 24.826 1.601   -13.235 0.30 27.15 ?  102 LYS   A HB3  1 
ATOM   2269 H HB3  B LYS   A 1 102 ? 25.121 0.804   -13.757 0.70 40.31 ?  102 LYS   A HB3  1 
ATOM   2270 H HG2  A LYS   A 1 102 ? 23.926 3.495   -12.234 0.30 28.20 ?  102 LYS   A HG2  1 
ATOM   2271 H HG2  B LYS   A 1 102 ? 24.314 2.867   -13.044 0.70 42.38 ?  102 LYS   A HG2  1 
ATOM   2272 H HG3  A LYS   A 1 102 ? 23.051 2.574   -11.274 0.30 28.20 ?  102 LYS   A HG3  1 
ATOM   2273 H HG3  B LYS   A 1 102 ? 23.330 2.128   -12.030 0.70 42.38 ?  102 LYS   A HG3  1 
ATOM   2274 H HD2  A LYS   A 1 102 ? 24.998 1.753   -10.284 0.30 29.11 ?  102 LYS   A HD2  1 
ATOM   2275 H HD2  B LYS   A 1 102 ? 25.316 1.173   -11.026 0.70 44.68 ?  102 LYS   A HD2  1 
ATOM   2276 H HD3  A LYS   A 1 102 ? 25.875 2.663   -11.250 0.30 29.11 ?  102 LYS   A HD3  1 
ATOM   2277 H HD3  B LYS   A 1 102 ? 26.143 2.240   -11.866 0.70 44.68 ?  102 LYS   A HD3  1 
ATOM   2278 H HE2  A LYS   A 1 102 ? 25.052 4.574   -10.229 0.30 29.89 ?  102 LYS   A HE2  1 
ATOM   2279 H HE2  B LYS   A 1 102 ? 25.504 3.910   -10.608 0.70 46.45 ?  102 LYS   A HE2  1 
ATOM   2280 H HE3  A LYS   A 1 102 ? 24.115 3.689   -9.296  0.30 29.89 ?  102 LYS   A HE3  1 
ATOM   2281 H HE3  B LYS   A 1 102 ? 24.135 3.228   -10.203 0.70 46.45 ?  102 LYS   A HE3  1 
ATOM   2282 H HZ1  A LYS   A 1 102 ? 25.995 4.311   -8.175  0.30 30.32 ?  102 LYS   A HZ1  1 
ATOM   2283 H HZ1  B LYS   A 1 102 ? 25.565 3.261   -8.426  0.70 47.52 ?  102 LYS   A HZ1  1 
ATOM   2284 H HZ2  A LYS   A 1 102 ? 25.995 2.868   -8.307  0.30 30.32 ?  102 LYS   A HZ2  1 
ATOM   2285 H HZ2  B LYS   A 1 102 ? 25.343 1.875   -8.787  0.70 47.52 ?  102 LYS   A HZ2  1 
ATOM   2286 H HZ3  A LYS   A 1 102 ? 26.849 3.673   -9.156  0.30 30.32 ?  102 LYS   A HZ3  1 
ATOM   2287 H HZ3  B LYS   A 1 102 ? 26.578 2.533   -9.163  0.70 47.52 ?  102 LYS   A HZ3  1 
ATOM   2288 N N    A GLY   A 1 103 ? 22.230 -0.569  -15.014 0.30 22.41 ?  103 GLY   A N    1 
ATOM   2289 N N    B GLY   A 1 103 ? 22.676 -1.389  -15.600 0.70 29.19 ?  103 GLY   A N    1 
ATOM   2290 C CA   A GLY   A 1 103 ? 22.454 -1.663  -15.938 0.30 22.83 ?  103 GLY   A CA   1 
ATOM   2291 C CA   B GLY   A 1 103 ? 23.003 -2.535  -16.428 0.70 28.09 ?  103 GLY   A CA   1 
ATOM   2292 C C    A GLY   A 1 103 ? 23.317 -2.778  -15.399 0.30 23.42 ?  103 GLY   A C    1 
ATOM   2293 C C    B GLY   A 1 103 ? 23.757 -3.645  -15.726 0.70 26.60 ?  103 GLY   A C    1 
ATOM   2294 O O    A GLY   A 1 103 ? 23.822 -3.587  -16.183 0.30 24.13 ?  103 GLY   A O    1 
ATOM   2295 O O    B GLY   A 1 103 ? 24.308 -4.526  -16.392 0.70 27.18 ?  103 GLY   A O    1 
ATOM   2296 H H    A GLY   A 1 103 ? 21.472 -0.607  -14.611 0.30 26.89 ?  103 GLY   A H    1 
ATOM   2297 H H    B GLY   A 1 103 ? 21.873 -1.382  -15.294 0.70 35.03 ?  103 GLY   A H    1 
ATOM   2298 H HA2  A GLY   A 1 103 ? 21.598 -2.041  -16.198 0.30 27.40 ?  103 GLY   A HA2  1 
ATOM   2299 H HA2  B GLY   A 1 103 ? 22.184 -2.915  -16.779 0.70 33.71 ?  103 GLY   A HA2  1 
ATOM   2300 H HA3  A GLY   A 1 103 ? 22.886 -1.322  -16.735 0.30 27.40 ?  103 GLY   A HA3  1 
ATOM   2301 H HA3  B GLY   A 1 103 ? 23.533 -2.215  -17.179 0.70 33.71 ?  103 GLY   A HA3  1 
ATOM   2302 N N    A GLU   A 1 104 ? 23.500 -2.853  -14.085 0.30 23.04 ?  104 GLU   A N    1 
ATOM   2303 N N    B GLU   A 1 104 ? 23.775 -3.649  -14.399 0.70 24.30 ?  104 GLU   A N    1 
ATOM   2304 C CA   A GLU   A 1 104 ? 24.388 -3.844  -13.498 0.30 22.67 ?  104 GLU   A CA   1 
ATOM   2305 C CA   B GLU   A 1 104 ? 24.619 -4.571  -13.655 0.70 22.00 ?  104 GLU   A CA   1 
ATOM   2306 C C    A GLU   A 1 104 ? 23.707 -5.205  -13.405 0.30 23.11 ?  104 GLU   A C    1 
ATOM   2307 C C    B GLU   A 1 104 ? 23.924 -5.921  -13.489 0.70 21.73 ?  104 GLU   A C    1 
ATOM   2308 O O    A GLU   A 1 104 ? 22.492 -5.310  -13.211 0.30 22.99 ?  104 GLU   A O    1 
ATOM   2309 O O    B GLU   A 1 104 ? 22.698 -6.009  -13.370 0.70 22.37 ?  104 GLU   A O    1 
ATOM   2310 C CB   A GLU   A 1 104 ? 24.873 -3.374  -12.125 0.30 22.00 ?  104 GLU   A CB   1 
ATOM   2311 C CB   B GLU   A 1 104 ? 25.006 -3.955  -12.306 0.70 21.57 ?  104 GLU   A CB   1 
ATOM   2312 C CG   A GLU   A 1 104 ? 25.852 -2.205  -12.228 0.30 21.41 ?  104 GLU   A CG   1 
ATOM   2313 C CG   B GLU   A 1 104 ? 25.798 -2.649  -12.474 0.70 22.15 ?  104 GLU   A CG   1 
ATOM   2314 C CD   A GLU   A 1 104 ? 26.134 -1.514  -10.904 0.30 20.71 ?  104 GLU   A CD   1 
ATOM   2315 C CD   B GLU   A 1 104 ? 26.136 -1.921  -11.190 0.70 22.13 ?  104 GLU   A CD   1 
ATOM   2316 O OE1  A GLU   A 1 104 ? 25.494 -1.858  -9.891  0.30 19.55 ?  104 GLU   A OE1  1 
ATOM   2317 O OE1  B GLU   A 1 104 ? 25.598 -2.260  -10.121 0.70 21.54 ?  104 GLU   A OE1  1 
ATOM   2318 O OE2  A GLU   A 1 104 ? 26.999 -0.610  -10.883 0.30 21.22 -1 104 GLU   A OE2  1 
ATOM   2319 O OE2  B GLU   A 1 104 ? 26.947 -0.971  -11.274 0.70 22.78 -1 104 GLU   A OE2  1 
ATOM   2320 H H    A GLU   A 1 104 ? 23.122 -2.337  -13.512 0.30 27.65 ?  104 GLU   A H    1 
ATOM   2321 H H    B GLU   A 1 104 ? 23.290 -3.135  -13.921 0.70 29.16 ?  104 GLU   A H    1 
ATOM   2322 H HA   A GLU   A 1 104 ? 25.163 -3.945  -14.068 0.30 27.21 ?  104 GLU   A HA   1 
ATOM   2323 H HA   B GLU   A 1 104 ? 25.438 -4.714  -14.159 0.70 26.40 ?  104 GLU   A HA   1 
ATOM   2324 H HB2  A GLU   A 1 104 ? 24.109 -3.086  -11.601 0.30 26.40 ?  104 GLU   A HB2  1 
ATOM   2325 H HB2  B GLU   A 1 104 ? 24.200 -3.759  -11.806 0.70 25.88 ?  104 GLU   A HB2  1 
ATOM   2326 H HB3  A GLU   A 1 104 ? 25.322 -4.110  -11.679 0.30 26.40 ?  104 GLU   A HB3  1 
ATOM   2327 H HB3  B GLU   A 1 104 ? 25.560 -4.584  -11.824 0.70 25.88 ?  104 GLU   A HB3  1 
ATOM   2328 H HG2  A GLU   A 1 104 ? 26.692 -2.538  -12.580 0.30 25.69 ?  104 GLU   A HG2  1 
ATOM   2329 H HG2  B GLU   A 1 104 ? 26.635 -2.844  -12.915 0.70 26.58 ?  104 GLU   A HG2  1 
ATOM   2330 H HG3  A GLU   A 1 104 ? 25.480 -1.544  -12.830 0.30 25.69 ?  104 GLU   A HG3  1 
ATOM   2331 H HG3  B GLU   A 1 104 ? 25.275 -2.031  -13.005 0.70 26.58 ?  104 GLU   A HG3  1 
ATOM   2332 N N    A ASP   A 1 105 ? 24.514 -6.254  -13.553 0.30 23.81 ?  105 ASP   A N    1 
ATOM   2333 N N    B ASP   A 1 105 ? 24.734 -6.977  -13.485 0.70 21.56 ?  105 ASP   A N    1 
ATOM   2334 C CA   A ASP   A 1 105 ? 24.005 -7.615  -13.637 0.30 24.67 ?  105 ASP   A CA   1 
ATOM   2335 C CA   B ASP   A 1 105 ? 24.246 -8.352  -13.555 0.70 21.91 ?  105 ASP   A CA   1 
ATOM   2336 C C    A ASP   A 1 105 ? 23.303 -8.002  -12.343 0.30 24.31 ?  105 ASP   A C    1 
ATOM   2337 C C    B ASP   A 1 105 ? 23.498 -8.721  -12.278 0.70 19.52 ?  105 ASP   A C    1 
ATOM   2338 O O    A ASP   A 1 105 ? 23.897 -7.943  -11.262 0.30 24.21 ?  105 ASP   A O    1 
ATOM   2339 O O    B ASP   A 1 105 ? 24.076 -8.704  -11.191 0.70 17.39 ?  105 ASP   A O    1 
ATOM   2340 C CB   A ASP   A 1 105 ? 25.169 -8.567  -13.912 0.30 25.83 ?  105 ASP   A CB   1 
ATOM   2341 C CB   B ASP   A 1 105 ? 25.452 -9.271  -13.753 0.70 24.43 ?  105 ASP   A CB   1 
ATOM   2342 C CG   A ASP   A 1 105 ? 24.705 -9.968  -14.239 0.30 26.77 ?  105 ASP   A CG   1 
ATOM   2343 C CG   B ASP   A 1 105 ? 25.074 -10.735 -13.904 0.70 26.57 ?  105 ASP   A CG   1 
ATOM   2344 O OD1  A ASP   A 1 105 ? 23.480 -10.170 -14.374 0.30 26.96 ?  105 ASP   A OD1  1 
ATOM   2345 O OD1  B ASP   A 1 105 ? 23.868 -11.052 -13.979 0.70 26.73 ?  105 ASP   A OD1  1 
ATOM   2346 O OD2  A ASP   A 1 105 ? 25.563 -10.866 -14.369 0.30 27.42 -1 105 ASP   A OD2  1 
ATOM   2347 O OD2  B ASP   A 1 105 ? 26.005 -11.573 -13.947 0.70 27.92 -1 105 ASP   A OD2  1 
ATOM   2348 H H    A ASP   A 1 105 ? 25.369 -6.204  -13.601 0.30 28.57 ?  105 ASP   A H    1 
ATOM   2349 H H    B ASP   A 1 105 ? 25.588 -6.917  -13.434 0.70 25.87 ?  105 ASP   A H    1 
ATOM   2350 H HA   A ASP   A 1 105 ? 23.371 -7.692  -14.367 0.30 29.60 ?  105 ASP   A HA   1 
ATOM   2351 H HA   B ASP   A 1 105 ? 23.642 -8.448  -14.304 0.70 26.29 ?  105 ASP   A HA   1 
ATOM   2352 H HB2  A ASP   A 1 105 ? 25.674 -8.242  -14.675 0.30 31.00 ?  105 ASP   A HB2  1 
ATOM   2353 H HB2  B ASP   A 1 105 ? 25.927 -8.989  -14.551 0.70 29.32 ?  105 ASP   A HB2  1 
ATOM   2354 H HB3  A ASP   A 1 105 ? 25.746 -8.602  -13.129 0.30 31.00 ?  105 ASP   A HB3  1 
ATOM   2355 H HB3  B ASP   A 1 105 ? 26.033 -9.196  -12.979 0.70 29.32 ?  105 ASP   A HB3  1 
ATOM   2356 N N    A ILE   A 1 106 ? 22.033 -8.401  -12.456 0.30 24.15 ?  106 ILE   A N    1 
ATOM   2357 N N    B ILE   A 1 106 ? 22.215 -9.069  -12.407 0.70 19.93 ?  106 ILE   A N    1 
ATOM   2358 C CA   A ILE   A 1 106 ? 21.276 -8.829  -11.286 0.30 23.77 ?  106 ILE   A CA   1 
ATOM   2359 C CA   B ILE   A 1 106 ? 21.430 -9.459  -11.242 0.70 19.91 ?  106 ILE   A CA   1 
ATOM   2360 C C    A ILE   A 1 106 ? 21.822 -10.124 -10.696 0.30 23.33 ?  106 ILE   A C    1 
ATOM   2361 C C    B ILE   A 1 106 ? 22.021 -10.681 -10.555 0.70 18.89 ?  106 ILE   A C    1 
ATOM   2362 O O    A ILE   A 1 106 ? 21.575 -10.416 -9.521  0.30 22.81 ?  106 ILE   A O    1 
ATOM   2363 O O    B ILE   A 1 106 ? 21.800 -10.873 -9.355  0.70 18.42 ?  106 ILE   A O    1 
ATOM   2364 C CB   A ILE   A 1 106 ? 19.772 -8.929  -11.620 0.30 23.91 ?  106 ILE   A CB   1 
ATOM   2365 C CB   B ILE   A 1 106 ? 19.946 -9.665  -11.627 0.70 21.59 ?  106 ILE   A CB   1 
ATOM   2366 C CG1  A ILE   A 1 106 ? 18.933 -8.989  -10.340 0.30 24.01 ?  106 ILE   A CG1  1 
ATOM   2367 C CG1  B ILE   A 1 106 ? 19.057 -9.782  -10.385 0.70 22.66 ?  106 ILE   A CG1  1 
ATOM   2368 C CG2  A ILE   A 1 106 ? 19.495 -10.149 -12.483 0.30 23.92 ?  106 ILE   A CG2  1 
ATOM   2369 C CG2  B ILE   A 1 106 ? 19.780 -10.912 -12.461 0.70 22.02 ?  106 ILE   A CG2  1 
ATOM   2370 C CD1  A ILE   A 1 106 ? 19.119 -7.789  -9.433  0.30 24.11 ?  106 ILE   A CD1  1 
ATOM   2371 C CD1  B ILE   A 1 106 ? 19.008 -8.535  -9.534  0.70 23.33 ?  106 ILE   A CD1  1 
ATOM   2372 H H    A ILE   A 1 106 ? 21.590 -8.419  -13.191 0.30 28.97 ?  106 ILE   A H    1 
ATOM   2373 H H    B ILE   A 1 106 ? 21.785 -9.078  -13.145 0.70 23.91 ?  106 ILE   A H    1 
ATOM   2374 H HA   A ILE   A 1 106 ? 21.380 -8.152  -10.608 0.30 28.52 ?  106 ILE   A HA   1 
ATOM   2375 H HA   B ILE   A 1 106 ? 21.465 -8.744  -10.596 0.70 23.90 ?  106 ILE   A HA   1 
ATOM   2376 H HB   A ILE   A 1 106 ? 19.512 -8.138  -12.118 0.30 28.69 ?  106 ILE   A HB   1 
ATOM   2377 H HB   B ILE   A 1 106 ? 19.653 -8.900  -12.147 0.70 25.91 ?  106 ILE   A HB   1 
ATOM   2378 H HG12 A ILE   A 1 106 ? 17.993 -9.032  -10.582 0.30 28.81 ?  106 ILE   A HG12 1 
ATOM   2379 H HG12 B ILE   A 1 106 ? 18.151 -9.976  -10.668 0.70 27.19 ?  106 ILE   A HG12 1 
ATOM   2380 H HG13 A ILE   A 1 106 ? 19.177 -9.782  -9.839  0.30 28.81 ?  106 ILE   A HG13 1 
ATOM   2381 H HG13 B ILE   A 1 106 ? 19.387 -10.503 -9.828  0.70 27.19 ?  106 ILE   A HG13 1 
ATOM   2382 H HG21 A ILE   A 1 106 ? 18.609 -10.066 -12.871 0.30 28.71 ?  106 ILE   A HG21 1 
ATOM   2383 H HG21 B ILE   A 1 106 ? 18.902 -10.899 -12.867 0.70 26.42 ?  106 ILE   A HG21 1 
ATOM   2384 H HG22 A ILE   A 1 106 ? 20.161 -10.193 -13.185 0.30 28.71 ?  106 ILE   A HG22 1 
ATOM   2385 H HG22 B ILE   A 1 106 ? 20.466 -10.923 -13.142 0.70 26.42 ?  106 ILE   A HG22 1 
ATOM   2386 H HG23 A ILE   A 1 106 ? 19.540 -10.945 -11.931 0.30 28.71 ?  106 ILE   A HG23 1 
ATOM   2387 H HG23 B ILE   A 1 106 ? 19.869 -11.687 -11.884 0.70 26.42 ?  106 ILE   A HG23 1 
ATOM   2388 H HD11 A ILE   A 1 106 ? 18.365 -7.733  -8.828  0.30 28.93 ?  106 ILE   A HD11 1 
ATOM   2389 H HD11 B ILE   A 1 106 ? 18.289 -8.623  -8.889  0.70 28.00 ?  106 ILE   A HD11 1 
ATOM   2390 H HD12 A ILE   A 1 106 ? 19.941 -7.899  -8.930  0.30 28.93 ?  106 ILE   A HD12 1 
ATOM   2391 H HD12 B ILE   A 1 106 ? 19.855 -8.433  -9.070  0.70 28.00 ?  106 ILE   A HD12 1 
ATOM   2392 H HD13 A ILE   A 1 106 ? 19.166 -6.988  -9.979  0.30 28.93 ?  106 ILE   A HD13 1 
ATOM   2393 H HD13 B ILE   A 1 106 ? 18.848 -7.768  -10.105 0.70 28.00 ?  106 ILE   A HD13 1 
ATOM   2394 N N    A GLN   A 1 107 ? 22.568 -10.909 -11.478 0.30 23.66 ?  107 GLN   A N    1 
ATOM   2395 N N    B GLN   A 1 107 ? 22.779 -11.509 -11.285 0.70 19.60 ?  107 GLN   A N    1 
ATOM   2396 C CA   A GLN   A 1 107 ? 23.141 -12.148 -10.962 0.30 23.96 ?  107 GLN   A CA   1 
ATOM   2397 C CA   B GLN   A 1 107 ? 23.454 -12.640 -10.653 0.70 21.67 ?  107 GLN   A CA   1 
ATOM   2398 C C    A GLN   A 1 107 ? 24.131 -11.894 -9.832  0.30 21.77 ?  107 GLN   A C    1 
ATOM   2399 C C    B GLN   A 1 107 ? 24.369 -12.172 -9.530  0.70 18.84 ?  107 GLN   A C    1 
ATOM   2400 O O    A GLN   A 1 107 ? 24.364 -12.790 -9.013  0.30 22.54 ?  107 GLN   A O    1 
ATOM   2401 O O    B GLN   A 1 107 ? 24.599 -12.904 -8.558  0.70 18.85 ?  107 GLN   A O    1 
ATOM   2402 C CB   A GLN   A 1 107 ? 23.826 -12.924 -12.091 0.30 26.46 ?  107 GLN   A CB   1 
ATOM   2403 C CB   B GLN   A 1 107 ? 24.248 -13.427 -11.702 0.70 26.63 ?  107 GLN   A CB   1 
ATOM   2404 C CG   A GLN   A 1 107 ? 22.939 -13.175 -13.302 0.30 28.78 ?  107 GLN   A CG   1 
ATOM   2405 C CG   B GLN   A 1 107 ? 23.384 -14.051 -12.788 0.70 31.51 ?  107 GLN   A CG   1 
ATOM   2406 C CD   A GLN   A 1 107 ? 21.681 -13.947 -12.957 0.30 30.72 ?  107 GLN   A CD   1 
ATOM   2407 C CD   B GLN   A 1 107 ? 22.425 -15.088 -12.237 0.70 35.71 ?  107 GLN   A CD   1 
ATOM   2408 O OE1  A GLN   A 1 107 ? 21.736 -14.981 -12.291 0.30 31.50 ?  107 GLN   A OE1  1 
ATOM   2409 O OE1  B GLN   A 1 107 ? 22.758 -15.829 -11.312 0.70 37.01 ?  107 GLN   A OE1  1 
ATOM   2410 N NE2  A GLN   A 1 107 ? 20.537 -13.444 -13.405 0.30 31.38 ?  107 GLN   A NE2  1 
ATOM   2411 N NE2  B GLN   A 1 107 ? 21.223 -15.139 -12.798 0.70 37.00 ?  107 GLN   A NE2  1 
ATOM   2412 H H    A GLN   A 1 107 ? 22.756 -10.745 -12.299 0.30 28.39 ?  107 GLN   A H    1 
ATOM   2413 H H    B GLN   A 1 107 ? 22.921 -11.436 -12.134 0.70 23.52 ?  107 GLN   A H    1 
ATOM   2414 H HA   A GLN   A 1 107 ? 22.429 -12.704 -10.612 0.30 28.75 ?  107 GLN   A HA   1 
ATOM   2415 H HA   B GLN   A 1 107 ? 22.791 -13.240 -10.279 0.70 26.00 ?  107 GLN   A HA   1 
ATOM   2416 H HB2  A GLN   A 1 107 ? 24.599 -12.423 -12.393 0.30 31.76 ?  107 GLN   A HB2  1 
ATOM   2417 H HB2  B GLN   A 1 107 ? 24.879 -12.833 -12.138 0.70 31.95 ?  107 GLN   A HB2  1 
ATOM   2418 H HB3  A GLN   A 1 107 ? 24.109 -13.789 -11.751 0.30 31.76 ?  107 GLN   A HB3  1 
ATOM   2419 H HB3  B GLN   A 1 107 ? 24.727 -14.149 -11.265 0.70 31.95 ?  107 GLN   A HB3  1 
ATOM   2420 H HG2  A GLN   A 1 107 ? 22.671 -12.326 -13.684 0.30 34.54 ?  107 GLN   A HG2  1 
ATOM   2421 H HG2  B GLN   A 1 107 ? 22.862 -13.355 -13.217 0.70 37.81 ?  107 GLN   A HG2  1 
ATOM   2422 H HG3  A GLN   A 1 107 ? 23.437 -13.690 -13.958 0.30 34.54 ?  107 GLN   A HG3  1 
ATOM   2423 H HG3  B GLN   A 1 107 ? 23.956 -14.486 -13.442 0.70 37.81 ?  107 GLN   A HG3  1 
ATOM   2424 H HE21 A GLN   A 1 107 ? 20.538 -12.717 -13.865 0.30 37.66 ?  107 GLN   A HE21 1 
ATOM   2425 H HE21 B GLN   A 1 107 ? 21.025 -14.603 -13.440 0.70 44.40 ?  107 GLN   A HE21 1 
ATOM   2426 H HE22 A GLN   A 1 107 ? 19.795 -13.845 -13.236 0.30 37.66 ?  107 GLN   A HE22 1 
ATOM   2427 H HE22 B GLN   A 1 107 ? 20.645 -15.709 -12.518 0.70 44.40 ?  107 GLN   A HE22 1 
ATOM   2428 N N    A LEU   A 1 108 ? 24.708 -10.691 -9.761  0.30 18.81 ?  108 LEU   A N    1 
ATOM   2429 N N    B LEU   A 1 108 ? 24.878 -10.944 -9.630  0.70 15.99 ?  108 LEU   A N    1 
ATOM   2430 C CA   A LEU   A 1 108 ? 25.644 -10.348 -8.696  0.30 16.47 ?  108 LEU   A CA   1 
ATOM   2431 C CA   B LEU   A 1 108 ? 25.724 -10.392 -8.585  0.70 14.90 ?  108 LEU   A CA   1 
ATOM   2432 C C    A LEU   A 1 108 ? 24.963 -10.173 -7.344  0.30 14.33 ?  108 LEU   A C    1 
ATOM   2433 C C    B LEU   A 1 108 ? 24.967 -10.170 -7.285  0.70 13.23 ?  108 LEU   A C    1 
ATOM   2434 O O    A LEU   A 1 108 ? 25.657 -10.002 -6.337  0.30 14.37 ?  108 LEU   A O    1 
ATOM   2435 O O    B LEU   A 1 108 ? 25.607 -9.977  -6.248  0.70 13.55 ?  108 LEU   A O    1 
ATOM   2436 C CB   A LEU   A 1 108 ? 26.407 -9.075  -9.073  0.30 16.31 ?  108 LEU   A CB   1 
ATOM   2437 C CB   B LEU   A 1 108 ? 26.386 -9.096  -9.061  0.70 15.31 ?  108 LEU   A CB   1 
ATOM   2438 C CG   A LEU   A 1 108 ? 27.350 -9.221  -10.270 0.30 16.70 ?  108 LEU   A CG   1 
ATOM   2439 C CG   B LEU   A 1 108 ? 27.439 -9.296  -10.154 0.70 16.65 ?  108 LEU   A CG   1 
ATOM   2440 C CD1  A LEU   A 1 108 ? 27.795 -7.862  -10.786 0.30 17.06 ?  108 LEU   A CD1  1 
ATOM   2441 C CD1  B LEU   A 1 108 ? 27.889 -7.969  -10.747 0.70 17.30 ?  108 LEU   A CD1  1 
ATOM   2442 C CD2  A LEU   A 1 108 ? 28.555 -10.068 -9.893  0.30 17.23 ?  108 LEU   A CD2  1 
ATOM   2443 C CD2  B LEU   A 1 108 ? 28.635 -10.061 -9.605  0.70 18.05 ?  108 LEU   A CD2  1 
ATOM   2444 H H    A LEU   A 1 108 ? 24.572 -10.060 -10.325 0.30 22.57 ?  108 LEU   A H    1 
ATOM   2445 H H    B LEU   A 1 108 ? 24.745 -10.423 -10.295 0.70 19.19 ?  108 LEU   A H    1 
ATOM   2446 H HA   A LEU   A 1 108 ? 26.289 -11.064 -8.607  0.30 19.76 ?  108 LEU   A HA   1 
ATOM   2447 H HA   B LEU   A 1 108 ? 26.428 -11.031 -8.396  0.70 17.88 ?  108 LEU   A HA   1 
ATOM   2448 H HB2  A LEU   A 1 108 ? 25.765 -8.382  -9.291  0.30 19.57 ?  108 LEU   A HB2  1 
ATOM   2449 H HB2  B LEU   A 1 108 ? 25.701 -8.509  -9.415  0.70 18.37 ?  108 LEU   A HB2  1 
ATOM   2450 H HB3  A LEU   A 1 108 ? 26.941 -8.799  -8.314  0.30 19.57 ?  108 LEU   A HB3  1 
ATOM   2451 H HB3  B LEU   A 1 108 ? 26.821 -8.678  -8.306  0.70 18.37 ?  108 LEU   A HB3  1 
ATOM   2452 H HG   A LEU   A 1 108 ? 26.882 -9.673  -10.989 0.30 20.04 ?  108 LEU   A HG   1 
ATOM   2453 H HG   B LEU   A 1 108 ? 27.055 -9.824  -10.871 0.70 19.99 ?  108 LEU   A HG   1 
ATOM   2454 H HD11 A LEU   A 1 108 ? 28.373 -7.989  -11.556 0.30 20.47 ?  108 LEU   A HD11 1 
ATOM   2455 H HD11 B LEU   A 1 108 ? 28.536 -8.138  -11.452 0.70 20.76 ?  108 LEU   A HD11 1 
ATOM   2456 H HD12 A LEU   A 1 108 ? 27.013 -7.349  -11.042 0.30 20.47 ?  108 LEU   A HD12 1 
ATOM   2457 H HD12 B LEU   A 1 108 ? 27.118 -7.508  -11.114 0.70 20.76 ?  108 LEU   A HD12 1 
ATOM   2458 H HD13 A LEU   A 1 108 ? 28.279 -7.400  -10.084 0.30 20.47 ?  108 LEU   A HD13 1 
ATOM   2459 H HD13 B LEU   A 1 108 ? 28.295 -7.430  -10.050 0.70 20.76 ?  108 LEU   A HD13 1 
ATOM   2460 H HD21 A LEU   A 1 108 ? 29.185 -10.066 -10.629 0.30 20.67 ?  108 LEU   A HD21 1 
ATOM   2461 H HD21 B LEU   A 1 108 ? 29.365 -10.002 -10.239 0.70 21.66 ?  108 LEU   A HD21 1 
ATOM   2462 H HD22 A LEU   A 1 108 ? 28.969 -9.689  -9.101  0.30 20.67 ?  108 LEU   A HD22 1 
ATOM   2463 H HD22 B LEU   A 1 108 ? 28.898 -9.668  -8.759  0.70 21.66 ?  108 LEU   A HD22 1 
ATOM   2464 H HD23 A LEU   A 1 108 ? 28.259 -10.973 -9.711  0.30 20.67 ?  108 LEU   A HD23 1 
ATOM   2465 H HD23 B LEU   A 1 108 ? 28.383 -10.989 -9.475  0.70 21.66 ?  108 LEU   A HD23 1 
ATOM   2466 N N    . LEU   A 1 109 ? 23.631 -10.222 -7.301  1.00 12.94 ?  109 LEU   A N    1 
ATOM   2467 C CA   . LEU   A 1 109 ? 22.906 -10.101 -6.045  1.00 12.61 ?  109 LEU   A CA   1 
ATOM   2468 C C    . LEU   A 1 109 ? 23.226 -11.263 -5.110  1.00 11.81 ?  109 LEU   A C    1 
ATOM   2469 O O    . LEU   A 1 109 ? 23.323 -11.084 -3.892  1.00 12.34 ?  109 LEU   A O    1 
ATOM   2470 C CB   . LEU   A 1 109 ? 21.409 -10.013 -6.334  1.00 12.87 ?  109 LEU   A CB   1 
ATOM   2471 C CG   . LEU   A 1 109 ? 20.484 -9.738  -5.155  1.00 13.22 ?  109 LEU   A CG   1 
ATOM   2472 C CD1  . LEU   A 1 109 ? 20.901 -8.475  -4.434  1.00 12.92 ?  109 LEU   A CD1  1 
ATOM   2473 C CD2  . LEU   A 1 109 ? 19.052 -9.607  -5.651  1.00 14.43 ?  109 LEU   A CD2  1 
ATOM   2474 H H    A LEU   A 1 109 ? 23.125 -10.320 -7.988  0.30 15.53 ?  109 LEU   A H    1 
ATOM   2475 H H    B LEU   A 1 109 ? 23.141 -10.318 -8.000  0.70 15.53 ?  109 LEU   A H    1 
ATOM   2476 H HA   . LEU   A 1 109 ? 23.179 -9.284  -5.604  1.00 15.14 ?  109 LEU   A HA   1 
ATOM   2477 H HB2  . LEU   A 1 109 ? 21.269 -9.303  -6.975  1.00 15.44 ?  109 LEU   A HB2  1 
ATOM   2478 H HB3  . LEU   A 1 109 ? 21.127 -10.856 -6.720  1.00 15.44 ?  109 LEU   A HB3  1 
ATOM   2479 H HG   . LEU   A 1 109 ? 20.523 -10.474 -4.525  1.00 15.86 ?  109 LEU   A HG   1 
ATOM   2480 H HD11 . LEU   A 1 109 ? 20.207 -8.217  -3.813  1.00 15.51 ?  109 LEU   A HD11 1 
ATOM   2481 H HD12 . LEU   A 1 109 ? 21.731 -8.638  -3.959  1.00 15.51 ?  109 LEU   A HD12 1 
ATOM   2482 H HD13 . LEU   A 1 109 ? 21.033 -7.767  -5.091  1.00 15.51 ?  109 LEU   A HD13 1 
ATOM   2483 H HD21 . LEU   A 1 109 ? 18.489 -9.312  -4.918  1.00 17.31 ?  109 LEU   A HD21 1 
ATOM   2484 H HD22 . LEU   A 1 109 ? 19.026 -8.957  -6.369  1.00 17.31 ?  109 LEU   A HD22 1 
ATOM   2485 H HD23 . LEU   A 1 109 ? 18.751 -10.470 -5.974  1.00 17.31 ?  109 LEU   A HD23 1 
ATOM   2486 N N    . LYS   A 1 110 ? 23.379 -12.474 -5.655  1.00 11.90 ?  110 LYS   A N    1 
ATOM   2487 C CA   . LYS   A 1 110 ? 23.758 -13.606 -4.809  1.00 11.89 ?  110 LYS   A CA   1 
ATOM   2488 C C    . LYS   A 1 110 ? 25.135 -13.384 -4.188  1.00 11.32 ?  110 LYS   A C    1 
ATOM   2489 O O    . LYS   A 1 110 ? 25.331 -13.598 -2.987  1.00 11.43 ?  110 LYS   A O    1 
ATOM   2490 C CB   . LYS   A 1 110 ? 23.701 -14.916 -5.598  1.00 12.65 ?  110 LYS   A CB   1 
ATOM   2491 C CG   . LYS   A 1 110 ? 23.897 -16.146 -4.720  1.00 12.69 ?  110 LYS   A CG   1 
ATOM   2492 C CD   . LYS   A 1 110 ? 23.652 -17.450 -5.456  1.00 13.33 ?  110 LYS   A CD   1 
ATOM   2493 C CE   . LYS   A 1 110 ? 23.757 -18.644 -4.519  1.00 14.49 ?  110 LYS   A CE   1 
ATOM   2494 N NZ   . LYS   A 1 110 ? 22.569 -18.783 -3.644  1.00 15.08 ?  110 LYS   A NZ   1 
ATOM   2495 H H    . LYS   A 1 110 ? 23.263 -12.666 -6.486  1.00 14.28 ?  110 LYS   A H    1 
ATOM   2496 H HA   . LYS   A 1 110 ? 23.116 -13.677 -4.084  1.00 14.27 ?  110 LYS   A HA   1 
ATOM   2497 H HB2  . LYS   A 1 110 ? 22.836 -14.988 -6.029  1.00 15.18 ?  110 LYS   A HB2  1 
ATOM   2498 H HB3  . LYS   A 1 110 ? 24.406 -14.911 -6.266  1.00 15.18 ?  110 LYS   A HB3  1 
ATOM   2499 H HG2  . LYS   A 1 110 ? 24.806 -16.156 -4.386  1.00 15.23 ?  110 LYS   A HG2  1 
ATOM   2500 H HG3  . LYS   A 1 110 ? 23.273 -16.102 -3.975  1.00 15.23 ?  110 LYS   A HG3  1 
ATOM   2501 H HD2  . LYS   A 1 110 ? 22.761 -17.438 -5.835  1.00 16.00 ?  110 LYS   A HD2  1 
ATOM   2502 H HD3  . LYS   A 1 110 ? 24.317 -17.548 -6.153  1.00 16.00 ?  110 LYS   A HD3  1 
ATOM   2503 H HE2  . LYS   A 1 110 ? 23.842 -19.455 -5.045  1.00 17.39 ?  110 LYS   A HE2  1 
ATOM   2504 H HE3  . LYS   A 1 110 ? 24.538 -18.536 -3.948  1.00 17.39 ?  110 LYS   A HE3  1 
ATOM   2505 H HZ1  . LYS   A 1 110 ? 22.655 -19.486 -3.111  1.00 18.10 ?  110 LYS   A HZ1  1 
ATOM   2506 H HZ2  . LYS   A 1 110 ? 22.468 -18.050 -3.145  1.00 18.10 ?  110 LYS   A HZ2  1 
ATOM   2507 H HZ3  . LYS   A 1 110 ? 21.835 -18.887 -4.144  1.00 18.10 ?  110 LYS   A HZ3  1 
ATOM   2508 N N    . SER   A 1 111 ? 26.098 -12.928 -4.993  1.00 11.35 ?  111 SER   A N    1 
ATOM   2509 C CA   . SER   A 1 111 ? 27.420 -12.610 -4.462  1.00 11.59 ?  111 SER   A CA   1 
ATOM   2510 C C    . SER   A 1 111 ? 27.328 -11.578 -3.344  1.00 10.94 ?  111 SER   A C    1 
ATOM   2511 O O    . SER   A 1 111 ? 28.012 -11.691 -2.322  1.00 11.51 ?  111 SER   A O    1 
ATOM   2512 C CB   . SER   A 1 111 ? 28.310 -12.096 -5.591  1.00 12.83 ?  111 SER   A CB   1 
ATOM   2513 O OG   . SER   A 1 111 ? 28.392 -13.067 -6.620  1.00 14.78 ?  111 SER   A OG   1 
ATOM   2514 H H    . SER   A 1 111 ? 26.008 -12.782 -5.835  1.00 13.62 ?  111 SER   A H    1 
ATOM   2515 H HA   . SER   A 1 111 ? 27.821 -13.417 -4.102  1.00 13.91 ?  111 SER   A HA   1 
ATOM   2516 H HB2  . SER   A 1 111 ? 27.920 -11.288 -5.960  1.00 15.39 ?  111 SER   A HB2  1 
ATOM   2517 H HB3  . SER   A 1 111 ? 29.195 -11.913 -5.243  1.00 15.39 ?  111 SER   A HB3  1 
ATOM   2518 H HG   . SER   A 1 111 ? 28.898 -12.785 -7.240  1.00 17.73 ?  111 SER   A HG   1 
ATOM   2519 N N    . ALA   A 1 112 ? 26.483 -10.561 -3.525  1.00 11.06 ?  112 ALA   A N    1 
ATOM   2520 C CA   . ALA   A 1 112 ? 26.314 -9.537  -2.498  1.00 10.70 ?  112 ALA   A CA   1 
ATOM   2521 C C    . ALA   A 1 112 ? 25.840 -10.155 -1.185  1.00 10.60 ?  112 ALA   A C    1 
ATOM   2522 O O    . ALA   A 1 112 ? 26.385 -9.874  -0.113  1.00 10.92 ?  112 ALA   A O    1 
ATOM   2523 C CB   . ALA   A 1 112 ? 25.343 -8.460  -2.992  1.00 11.36 ?  112 ALA   A CB   1 
ATOM   2524 H H    . ALA   A 1 112 ? 26.004 -10.444 -4.225  1.00 13.28 ?  112 ALA   A H    1 
ATOM   2525 H HA   . ALA   A 1 112 ? 27.167 -9.107  -2.333  1.00 12.84 ?  112 ALA   A HA   1 
ATOM   2526 H HB1  . ALA   A 1 112 ? 25.264 -7.766  -2.314  1.00 13.63 ?  112 ALA   A HB1  1 
ATOM   2527 H HB2  . ALA   A 1 112 ? 25.684 -8.075  -3.814  1.00 13.63 ?  112 ALA   A HB2  1 
ATOM   2528 H HB3  . ALA   A 1 112 ? 24.474 -8.862  -3.152  1.00 13.63 ?  112 ALA   A HB3  1 
ATOM   2529 N N    . TYR   A 1 113 ? 24.807 -11.000 -1.245  1.00 10.92 ?  113 TYR   A N    1 
ATOM   2530 C CA   . TYR   A 1 113 ? 24.295 -11.610 -0.019  1.00 10.74 ?  113 TYR   A CA   1 
ATOM   2531 C C    . TYR   A 1 113 ? 25.303 -12.567 0.621   1.00 10.15 ?  113 TYR   A C    1 
ATOM   2532 O O    . TYR   A 1 113 ? 25.264 -12.767 1.839   1.00 11.09 ?  113 TYR   A O    1 
ATOM   2533 C CB   . TYR   A 1 113 ? 22.983 -12.344 -0.296  1.00 11.01 ?  113 TYR   A CB   1 
ATOM   2534 C CG   . TYR   A 1 113 ? 21.761 -11.448 -0.266  1.00 10.94 ?  113 TYR   A CG   1 
ATOM   2535 C CD1  . TYR   A 1 113 ? 21.360 -10.835 0.911   1.00 11.00 ?  113 TYR   A CD1  1 
ATOM   2536 C CD2  . TYR   A 1 113 ? 20.989 -11.249 -1.403  1.00 11.47 ?  113 TYR   A CD2  1 
ATOM   2537 C CE1  . TYR   A 1 113 ? 20.231 -10.029 0.952   1.00 11.33 ?  113 TYR   A CE1  1 
ATOM   2538 C CE2  . TYR   A 1 113 ? 19.846 -10.441 -1.370  1.00 11.18 ?  113 TYR   A CE2  1 
ATOM   2539 C CZ   . TYR   A 1 113 ? 19.482 -9.843  -0.189  1.00 11.15 ?  113 TYR   A CZ   1 
ATOM   2540 O OH   . TYR   A 1 113 ? 18.348 -9.047  -0.135  1.00 12.20 ?  113 TYR   A OH   1 
ATOM   2541 H H    . TYR   A 1 113 ? 24.398 -11.229 -1.967  1.00 13.10 ?  113 TYR   A H    1 
ATOM   2542 H HA   . TYR   A 1 113 ? 24.113 -10.909 0.620   1.00 12.89 ?  113 TYR   A HA   1 
ATOM   2543 H HB2  . TYR   A 1 113 ? 23.026 -12.746 -1.179  1.00 13.21 ?  113 TYR   A HB2  1 
ATOM   2544 H HB3  . TYR   A 1 113 ? 22.861 -13.032 0.374   1.00 13.21 ?  113 TYR   A HB3  1 
ATOM   2545 H HD1  . TYR   A 1 113 ? 21.863 -10.966 1.685   1.00 13.20 ?  113 TYR   A HD1  1 
ATOM   2546 H HD2  . TYR   A 1 113 ? 21.234 -11.655 -2.200  1.00 13.76 ?  113 TYR   A HD2  1 
ATOM   2547 H HE1  . TYR   A 1 113 ? 19.983 -9.630  1.753   1.00 13.60 ?  113 TYR   A HE1  1 
ATOM   2548 H HE2  . TYR   A 1 113 ? 19.333 -10.306 -2.135  1.00 13.42 ?  113 TYR   A HE2  1 
ATOM   2549 H HH   . TYR   A 1 113 ? 17.988 -9.013  -0.897  1.00 14.65 ?  113 TYR   A HH   1 
ATOM   2550 N N    . GLU   A 1 114 ? 26.205 -13.170 -0.170  1.00 10.68 ?  114 GLU   A N    1 
ATOM   2551 C CA   . GLU   A 1 114 ? 27.201 -14.071 0.416   1.00 11.07 ?  114 GLU   A CA   1 
ATOM   2552 C C    . GLU   A 1 114 ? 28.048 -13.369 1.468   1.00 10.70 ?  114 GLU   A C    1 
ATOM   2553 O O    . GLU   A 1 114 ? 28.529 -14.009 2.412   1.00 10.96 ?  114 GLU   A O    1 
ATOM   2554 C CB   . GLU   A 1 114 ? 28.082 -14.703 -0.673  1.00 11.11 ?  114 GLU   A CB   1 
ATOM   2555 C CG   . GLU   A 1 114 ? 27.326 -15.748 -1.479  1.00 11.59 ?  114 GLU   A CG   1 
ATOM   2556 C CD   . GLU   A 1 114 ? 28.051 -16.267 -2.722  1.00 12.00 ?  114 GLU   A CD   1 
ATOM   2557 O OE1  . GLU   A 1 114 ? 28.996 -15.623 -3.219  1.00 12.03 ?  114 GLU   A OE1  1 
ATOM   2558 O OE2  . GLU   A 1 114 ? 27.627 -17.339 -3.219  1.00 13.09 -1 114 GLU   A OE2  1 
ATOM   2559 H H    . GLU   A 1 114 ? 26.258 -13.077 -1.029  1.00 12.82 ?  114 GLU   A H    1 
ATOM   2560 H HA   . GLU   A 1 114 ? 26.732 -14.789 0.860   1.00 13.29 ?  114 GLU   A HA   1 
ATOM   2561 H HB2  . GLU   A 1 114 ? 28.381 -14.015 -1.286  1.00 13.33 ?  114 GLU   A HB2  1 
ATOM   2562 H HB3  . GLU   A 1 114 ? 28.837 -15.140 -0.258  1.00 13.33 ?  114 GLU   A HB3  1 
ATOM   2563 H HG2  . GLU   A 1 114 ? 27.149 -16.513 -0.908  1.00 13.90 ?  114 GLU   A HG2  1 
ATOM   2564 H HG3  . GLU   A 1 114 ? 26.478 -15.365 -1.768  1.00 13.90 ?  114 GLU   A HG3  1 
ATOM   2565 N N    . ASN   A 1 115 ? 28.231 -12.055 1.337   1.00 10.49 ?  115 ASN   A N    1 
ATOM   2566 C CA   . ASN   A 1 115 ? 29.007 -11.329 2.334   1.00 10.72 ?  115 ASN   A CA   1 
ATOM   2567 C C    . ASN   A 1 115 ? 28.392 -11.450 3.723   1.00 10.70 ?  115 ASN   A C    1 
ATOM   2568 O O    . ASN   A 1 115 ? 29.109 -11.383 4.732   1.00 10.89 ?  115 ASN   A O    1 
ATOM   2569 C CB   . ASN   A 1 115 ? 29.117 -9.852  1.949   1.00 10.85 ?  115 ASN   A CB   1 
ATOM   2570 C CG   . ASN   A 1 115 ? 29.907 -9.642  0.678   1.00 11.65 ?  115 ASN   A CG   1 
ATOM   2571 O OD1  . ASN   A 1 115 ? 31.125 -9.777  0.673   1.00 15.16 ?  115 ASN   A OD1  1 
ATOM   2572 N ND2  . ASN   A 1 115 ? 29.223 -9.311  -0.405  1.00 11.22 ?  115 ASN   A ND2  1 
ATOM   2573 H H    . ASN   A 1 115 ? 27.917 -11.563 0.698   1.00 12.58 ?  115 ASN   A H    1 
ATOM   2574 H HA   . ASN   A 1 115 ? 29.904 -11.696 2.367   1.00 12.87 ?  115 ASN   A HA   1 
ATOM   2575 H HB2  . ASN   A 1 115 ? 28.224 -9.494  1.822   1.00 13.02 ?  115 ASN   A HB2  1 
ATOM   2576 H HB3  . ASN   A 1 115 ? 29.564 -9.373  2.668   1.00 13.02 ?  115 ASN   A HB3  1 
ATOM   2577 H HD21 . ASN   A 1 115 ? 29.629 -9.174  -1.150  1.00 13.46 ?  115 ASN   A HD21 1 
ATOM   2578 H HD22 . ASN   A 1 115 ? 28.362 -9.250  -0.371  1.00 13.46 ?  115 ASN   A HD22 1 
ATOM   2579 N N    . PHE   A 1 116 ? 27.067 -11.622 3.801   1.00 10.66 ?  116 PHE   A N    1 
ATOM   2580 C CA   . PHE   A 1 116 ? 26.424 -11.717 5.106   1.00 10.61 ?  116 PHE   A CA   1 
ATOM   2581 C C    . PHE   A 1 116 ? 26.903 -12.948 5.875   1.00 10.74 ?  116 PHE   A C    1 
ATOM   2582 O O    . PHE   A 1 116 ? 26.827 -12.972 7.104   1.00 11.48 ?  116 PHE   A O    1 
ATOM   2583 C CB   . PHE   A 1 116 ? 24.897 -11.851 4.979   1.00 10.76 ?  116 PHE   A CB   1 
ATOM   2584 C CG   . PHE   A 1 116 ? 24.134 -10.612 4.497   1.00 10.28 ?  116 PHE   A CG   1 
ATOM   2585 C CD1  . PHE   A 1 116 ? 24.695 -9.594  3.733   1.00 10.41 ?  116 PHE   A CD1  1 
ATOM   2586 C CD2  . PHE   A 1 116 ? 22.777 -10.519 4.804   1.00 11.23 ?  116 PHE   A CD2  1 
ATOM   2587 C CE1  . PHE   A 1 116 ? 23.915 -8.532  3.296   1.00 10.79 ?  116 PHE   A CE1  1 
ATOM   2588 C CE2  . PHE   A 1 116 ? 22.002 -9.455  4.379   1.00 11.32 ?  116 PHE   A CE2  1 
ATOM   2589 C CZ   . PHE   A 1 116 ? 22.566 -8.463  3.626   1.00 10.88 ?  116 PHE   A CZ   1 
ATOM   2590 H H    . PHE   A 1 116 ? 26.533 -11.680 3.127   1.00 12.79 ?  116 PHE   A H    1 
ATOM   2591 H HA   . PHE   A 1 116 ? 26.623 -10.927 5.630   1.00 12.74 ?  116 PHE   A HA   1 
ATOM   2592 H HB2  . PHE   A 1 116 ? 24.705 -12.567 4.354   1.00 12.91 ?  116 PHE   A HB2  1 
ATOM   2593 H HB3  . PHE   A 1 116 ? 24.541 -12.087 5.852   1.00 12.91 ?  116 PHE   A HB3  1 
ATOM   2594 H HD1  . PHE   A 1 116 ? 25.592 -9.643  3.505   1.00 12.49 ?  116 PHE   A HD1  1 
ATOM   2595 H HD2  . PHE   A 1 116 ? 22.384 -11.195 5.306   1.00 13.47 ?  116 PHE   A HD2  1 
ATOM   2596 H HE1  . PHE   A 1 116 ? 24.309 -7.854  2.797   1.00 12.95 ?  116 PHE   A HE1  1 
ATOM   2597 H HE2  . PHE   A 1 116 ? 21.104 -9.415  4.603   1.00 13.58 ?  116 PHE   A HE2  1 
ATOM   2598 H HZ   . PHE   A 1 116 ? 22.057 -7.740  3.349   1.00 13.05 ?  116 PHE   A HZ   1 
ATOM   2599 N N    . ASN   A 1 117 ? 27.343 -13.997 5.171   1.00 11.11 ?  117 ASN   A N    1 
ATOM   2600 C CA   . ASN   A 1 117 ? 27.711 -15.245 5.837   1.00 11.21 ?  117 ASN   A CA   1 
ATOM   2601 C C    . ASN   A 1 117 ? 28.973 -15.127 6.669   1.00 11.75 ?  117 ASN   A C    1 
ATOM   2602 O O    . ASN   A 1 117 ? 29.277 -16.050 7.436   1.00 12.77 ?  117 ASN   A O    1 
ATOM   2603 C CB   . ASN   A 1 117 ? 27.834 -16.370 4.817   1.00 11.65 ?  117 ASN   A CB   1 
ATOM   2604 C CG   . ASN   A 1 117 ? 26.492 -16.754 4.276   1.00 11.70 ?  117 ASN   A CG   1 
ATOM   2605 O OD1  . ASN   A 1 117 ? 25.518 -16.799 5.027   1.00 12.89 ?  117 ASN   A OD1  1 
ATOM   2606 N ND2  . ASN   A 1 117 ? 26.406 -17.005 2.986   1.00 11.48 ?  117 ASN   A ND2  1 
ATOM   2607 H H    . ASN   A 1 117 ? 27.413 -14.017 4.314   1.00 13.33 ?  117 ASN   A H    1 
ATOM   2608 H HA   . ASN   A 1 117 ? 26.989 -15.484 6.441   1.00 13.45 ?  117 ASN   A HA   1 
ATOM   2609 H HB2  . ASN   A 1 117 ? 28.385 -16.071 4.075   1.00 13.98 ?  117 ASN   A HB2  1 
ATOM   2610 H HB3  . ASN   A 1 117 ? 28.229 -17.144 5.241   1.00 13.98 ?  117 ASN   A HB3  1 
ATOM   2611 H HD21 . ASN   A 1 117 ? 25.645 -17.223 2.644   1.00 13.77 ?  117 ASN   A HD21 1 
ATOM   2612 H HD22 . ASN   A 1 117 ? 27.102 -16.953 2.492   1.00 13.77 ?  117 ASN   A HD22 1 
ATOM   2613 N N    . GLN   A 1 118 ? 29.697 -14.016 6.555   1.00 11.44 ?  118 GLN   A N    1 
ATOM   2614 C CA   . GLN   A 1 118 ? 30.875 -13.793 7.380   1.00 11.84 ?  118 GLN   A CA   1 
ATOM   2615 C C    . GLN   A 1 118 ? 30.533 -13.230 8.756   1.00 12.04 ?  118 GLN   A C    1 
ATOM   2616 O O    . GLN   A 1 118 ? 31.447 -12.944 9.541   1.00 13.46 ?  118 GLN   A O    1 
ATOM   2617 C CB   . GLN   A 1 118 ? 31.865 -12.879 6.652   1.00 12.03 ?  118 GLN   A CB   1 
ATOM   2618 C CG   . GLN   A 1 118 ? 32.351 -13.445 5.329   1.00 12.32 ?  118 GLN   A CG   1 
ATOM   2619 C CD   . GLN   A 1 118 ? 33.178 -14.705 5.497   1.00 12.61 ?  118 GLN   A CD   1 
ATOM   2620 O OE1  . GLN   A 1 118 ? 34.039 -14.776 6.383   1.00 13.65 ?  118 GLN   A OE1  1 
ATOM   2621 N NE2  . GLN   A 1 118 ? 32.928 -15.705 4.648   1.00 12.82 ?  118 GLN   A NE2  1 
ATOM   2622 H H    . GLN   A 1 118 ? 29.523 -13.371 6.004   1.00 13.73 ?  118 GLN   A H    1 
ATOM   2623 H HA   . GLN   A 1 118 ? 31.305 -14.652 7.517   1.00 14.20 ?  118 GLN   A HA   1 
ATOM   2624 H HB2  . GLN   A 1 118 ? 31.433 -12.035 6.478   1.00 14.44 ?  118 GLN   A HB2  1 
ATOM   2625 H HB3  . GLN   A 1 118 ? 32.635 -12.753 7.226   1.00 14.44 ?  118 GLN   A HB3  1 
ATOM   2626 H HG2  . GLN   A 1 118 ? 31.589 -13.661 4.770   1.00 14.79 ?  118 GLN   A HG2  1 
ATOM   2627 H HG3  . GLN   A 1 118 ? 32.907 -12.782 4.889   1.00 14.79 ?  118 GLN   A HG3  1 
ATOM   2628 H HE21 . GLN   A 1 118 ? 32.311 -15.616 4.046   1.00 15.39 ?  118 GLN   A HE21 1 
ATOM   2629 H HE22 . GLN   A 1 118 ? 33.364 -16.443 4.699   1.00 15.39 ?  118 GLN   A HE22 1 
ATOM   2630 N N    . HIS   A 1 119 ? 29.246 -13.074 9.070   1.00 11.82 ?  119 HIS   A N    1 
ATOM   2631 C CA   . HIS   A 1 119 ? 28.798 -12.473 10.322  1.00 12.47 ?  119 HIS   A CA   1 
ATOM   2632 C C    . HIS   A 1 119 ? 27.669 -13.309 10.893  1.00 12.80 ?  119 HIS   A C    1 
ATOM   2633 O O    . HIS   A 1 119 ? 26.714 -13.621 10.180  1.00 13.47 ?  119 HIS   A O    1 
ATOM   2634 C CB   . HIS   A 1 119 ? 28.332 -11.039 10.056  1.00 12.84 ?  119 HIS   A CB   1 
ATOM   2635 C CG   . HIS   A 1 119 ? 29.401 -10.227 9.426   1.00 13.68 ?  119 HIS   A CG   1 
ATOM   2636 N ND1  . HIS   A 1 119 ? 30.387 -9.623  10.168  1.00 15.87 ?  119 HIS   A ND1  1 
ATOM   2637 C CD2  . HIS   A 1 119 ? 29.725 -10.035 8.127   1.00 14.73 ?  119 HIS   A CD2  1 
ATOM   2638 C CE1  . HIS   A 1 119 ? 31.247 -9.043  9.350   1.00 16.22 ?  119 HIS   A CE1  1 
ATOM   2639 N NE2  . HIS   A 1 119 ? 30.880 -9.292  8.107   1.00 16.07 ?  119 HIS   A NE2  1 
ATOM   2640 H H    . HIS   A 1 119 ? 28.590 -13.318 8.562   1.00 14.19 ?  119 HIS   A H    1 
ATOM   2641 H HA   . HIS   A 1 119 ? 29.527 -12.460 10.961  1.00 14.97 ?  119 HIS   A HA   1 
ATOM   2642 H HB2  . HIS   A 1 119 ? 27.568 -11.063 9.459   1.00 15.41 ?  119 HIS   A HB2  1 
ATOM   2643 H HB3  . HIS   A 1 119 ? 28.091 -10.626 10.898  1.00 15.41 ?  119 HIS   A HB3  1 
ATOM   2644 H HD2  . HIS   A 1 119 ? 29.258 -10.352 7.382   1.00 17.68 ?  119 HIS   A HD2  1 
ATOM   2645 H HE1  . HIS   A 1 119 ? 31.992 -8.549  9.603   1.00 19.46 ?  119 HIS   A HE1  1 
ATOM   2646 H HE2  . HIS   A 1 119 ? 31.278 -9.001  7.397   1.00 19.29 ?  119 HIS   A HE2  1 
ATOM   2647 N N    . GLU   A 1 120 ? 27.765 -13.639 12.182  1.00 13.64 ?  120 GLU   A N    1 
ATOM   2648 C CA   . GLU   A 1 120 ? 26.809 -14.570 12.779  1.00 16.06 ?  120 GLU   A CA   1 
ATOM   2649 C C    . GLU   A 1 120 ? 25.392 -14.005 12.852  1.00 14.74 ?  120 GLU   A C    1 
ATOM   2650 O O    . GLU   A 1 120 ? 24.421 -14.769 12.738  1.00 14.69 ?  120 GLU   A O    1 
ATOM   2651 C CB   . GLU   A 1 120 ? 27.283 -14.995 14.169  1.00 21.06 ?  120 GLU   A CB   1 
ATOM   2652 C CG   . GLU   A 1 120 ? 28.444 -15.975 14.151  1.00 29.12 ?  120 GLU   A CG   1 
ATOM   2653 C CD   . GLU   A 1 120 ? 28.596 -16.713 15.464  1.00 36.37 ?  120 GLU   A CD   1 
ATOM   2654 O OE1  . GLU   A 1 120 ? 28.137 -16.186 16.500  1.00 38.11 ?  120 GLU   A OE1  1 
ATOM   2655 O OE2  . GLU   A 1 120 ? 29.166 -17.824 15.458  1.00 39.51 -1 120 GLU   A OE2  1 
ATOM   2656 H H    . GLU   A 1 120 ? 28.374 -13.358 12.721  1.00 16.36 ?  120 GLU   A H    1 
ATOM   2657 H HA   . GLU   A 1 120 ? 26.776 -15.372 12.236  1.00 19.27 ?  120 GLU   A HA   1 
ATOM   2658 H HB2  . GLU   A 1 120 ? 27.571 -14.214 14.663  1.00 25.27 ?  120 GLU   A HB2  1 
ATOM   2659 H HB3  . GLU   A 1 120 ? 26.548 -15.427 14.638  1.00 25.27 ?  120 GLU   A HB3  1 
ATOM   2660 H HG2  . GLU   A 1 120 ? 28.299 -16.633 13.453  1.00 34.94 ?  120 GLU   A HG2  1 
ATOM   2661 H HG3  . GLU   A 1 120 ? 29.268 -15.493 13.990  1.00 34.94 ?  120 GLU   A HG3  1 
ATOM   2662 N N    . VAL   A 1 121 ? 25.254 -12.695 13.074  1.00 13.88 ?  121 VAL   A N    1 
ATOM   2663 C CA   . VAL   A 1 121 ? 23.960 -12.027 13.195  1.00 14.31 ?  121 VAL   A CA   1 
ATOM   2664 C C    . VAL   A 1 121 ? 24.073 -10.647 12.556  1.00 12.99 ?  121 VAL   A C    1 
ATOM   2665 O O    . VAL   A 1 121 ? 25.045 -9.923  12.799  1.00 13.57 ?  121 VAL   A O    1 
ATOM   2666 C CB   . VAL   A 1 121 ? 23.523 -11.877 14.671  1.00 17.28 ?  121 VAL   A CB   1 
ATOM   2667 C CG1  . VAL   A 1 121 ? 22.134 -11.237 14.762  1.00 17.86 ?  121 VAL   A CG1  1 
ATOM   2668 C CG2  . VAL   A 1 121 ? 23.536 -13.206 15.396  1.00 19.50 ?  121 VAL   A CG2  1 
ATOM   2669 H H    . VAL   A 1 121 ? 25.923 -12.157 13.160  1.00 16.66 ?  121 VAL   A H    1 
ATOM   2670 H HA   . VAL   A 1 121 ? 23.289 -12.538 12.721  1.00 17.17 ?  121 VAL   A HA   1 
ATOM   2671 H HB   . VAL   A 1 121 ? 24.145 -11.292 15.124  1.00 20.74 ?  121 VAL   A HB   1 
ATOM   2672 H HG11 . VAL   A 1 121 ? 21.822 -11.286 15.682  1.00 21.43 ?  121 VAL   A HG11 1 
ATOM   2673 H HG12 . VAL   A 1 121 ? 22.190 -10.310 14.486  1.00 21.43 ?  121 VAL   A HG12 1 
ATOM   2674 H HG13 . VAL   A 1 121 ? 21.521 -11.720 14.184  1.00 21.43 ?  121 VAL   A HG13 1 
ATOM   2675 H HG21 . VAL   A 1 121 ? 23.186 -13.081 16.297  1.00 23.40 ?  121 VAL   A HG21 1 
ATOM   2676 H HG22 . VAL   A 1 121 ? 22.976 -13.839 14.916  1.00 23.40 ?  121 VAL   A HG22 1 
ATOM   2677 H HG23 . VAL   A 1 121 ? 24.445 -13.537 15.442  1.00 23.40 ?  121 VAL   A HG23 1 
ATOM   2678 N N    . LEU   A 1 122 ? 23.067 -10.267 11.761  1.00 12.20 ?  122 LEU   A N    1 
ATOM   2679 C CA   . LEU   A 1 122 ? 23.056 -8.962  11.104  1.00 11.98 ?  122 LEU   A CA   1 
ATOM   2680 C C    . LEU   A 1 122 ? 21.656 -8.376  11.069  1.00 11.80 ?  122 LEU   A C    1 
ATOM   2681 O O    . LEU   A 1 122 ? 20.667 -9.101  10.949  1.00 12.76 ?  122 LEU   A O    1 
ATOM   2682 C CB   . LEU   A 1 122 ? 23.477 -9.041  9.629   1.00 13.25 ?  122 LEU   A CB   1 
ATOM   2683 C CG   . LEU   A 1 122 ? 24.690 -9.893  9.262   1.00 13.21 ?  122 LEU   A CG   1 
ATOM   2684 C CD1  . LEU   A 1 122 ? 24.301 -11.346 9.026   1.00 14.08 ?  122 LEU   A CD1  1 
ATOM   2685 C CD2  . LEU   A 1 122 ? 25.393 -9.322  8.035   1.00 12.64 ?  122 LEU   A CD2  1 
ATOM   2686 H H    . LEU   A 1 122 ? 22.379 -10.750 11.590  1.00 14.64 ?  122 LEU   A H    1 
ATOM   2687 H HA   . LEU   A 1 122 ? 23.648 -8.349  11.567  1.00 14.38 ?  122 LEU   A HA   1 
ATOM   2688 H HB2  . LEU   A 1 122 ? 22.737 -9.395  9.121   1.00 15.90 ?  122 LEU   A HB2  1 
ATOM   2689 H HB3  . LEU   A 1 122 ? 23.676 -8.144  9.323   1.00 15.90 ?  122 LEU   A HB3  1 
ATOM   2690 H HG   . LEU   A 1 122 ? 25.333 -9.876  9.989   1.00 15.85 ?  122 LEU   A HG   1 
ATOM   2691 H HD11 . LEU   A 1 122 ? 25.081 -11.847 8.739   1.00 16.89 ?  122 LEU   A HD11 1 
ATOM   2692 H HD12 . LEU   A 1 122 ? 23.958 -11.716 9.854   1.00 16.89 ?  122 LEU   A HD12 1 
ATOM   2693 H HD13 . LEU   A 1 122 ? 23.617 -11.382 8.339   1.00 16.89 ?  122 LEU   A HD13 1 
ATOM   2694 H HD21 . LEU   A 1 122 ? 26.149 -9.890  7.798   1.00 15.17 ?  122 LEU   A HD21 1 
ATOM   2695 H HD22 . LEU   A 1 122 ? 24.770 -9.281  7.296   1.00 15.17 ?  122 LEU   A HD22 1 
ATOM   2696 H HD23 . LEU   A 1 122 ? 25.718 -8.427  8.242   1.00 15.17 ?  122 LEU   A HD23 1 
ATOM   2697 N N    A LEU   A 1 123 ? 21.588 -7.048  11.144  0.30 11.52 ?  123 LEU   A N    1 
ATOM   2698 N N    B LEU   A 1 123 ? 21.595 -7.049  11.197  0.70 11.40 ?  123 LEU   A N    1 
ATOM   2699 C CA   A LEU   A 1 123 ? 20.417 -6.282  10.735  0.30 11.28 ?  123 LEU   A CA   1 
ATOM   2700 C CA   B LEU   A 1 123 ? 20.422 -6.248  10.864  0.70 11.20 ?  123 LEU   A CA   1 
ATOM   2701 C C    A LEU   A 1 123 ? 20.677 -5.765  9.324   0.30 10.69 ?  123 LEU   A C    1 
ATOM   2702 C C    B LEU   A 1 123 ? 20.655 -5.693  9.469   0.70 10.82 ?  123 LEU   A C    1 
ATOM   2703 O O    A LEU   A 1 123 ? 21.781 -5.298  9.032   0.30 10.71 ?  123 LEU   A O    1 
ATOM   2704 O O    B LEU   A 1 123 ? 21.673 -5.035  9.239   0.70 11.04 ?  123 LEU   A O    1 
ATOM   2705 C CB   A LEU   A 1 123 ? 20.220 -5.102  11.689  0.30 11.95 ?  123 LEU   A CB   1 
ATOM   2706 C CB   B LEU   A 1 123 ? 20.288 -5.089  11.851  0.70 11.77 ?  123 LEU   A CB   1 
ATOM   2707 C CG   A LEU   A 1 123 ? 19.161 -4.050  11.358  0.30 12.46 ?  123 LEU   A CG   1 
ATOM   2708 C CG   B LEU   A 1 123 ? 19.260 -4.013  11.503  0.70 12.36 ?  123 LEU   A CG   1 
ATOM   2709 C CD1  A LEU   A 1 123 ? 17.763 -4.650  11.369  0.30 12.68 ?  123 LEU   A CD1  1 
ATOM   2710 C CD1  B LEU   A 1 123 ? 17.846 -4.586  11.521  0.70 13.07 ?  123 LEU   A CD1  1 
ATOM   2711 C CD2  A LEU   A 1 123 ? 19.256 -2.894  12.344  0.30 12.74 ?  123 LEU   A CD2  1 
ATOM   2712 C CD2  B LEU   A 1 123 ? 19.378 -2.852  12.467  0.70 13.01 ?  123 LEU   A CD2  1 
ATOM   2713 H H    A LEU   A 1 123 ? 22.232 -6.552  11.440  0.30 13.83 ?  123 LEU   A H    1 
ATOM   2714 H H    B LEU   A 1 123 ? 22.257 -6.567  11.472  0.70 13.68 ?  123 LEU   A H    1 
ATOM   2715 H HA   A LEU   A 1 123 ? 19.626 -6.849  10.746  0.30 13.54 ?  123 LEU   A HA   1 
ATOM   2716 H HA   B LEU   A 1 123 ? 19.621 -6.792  10.869  0.70 13.43 ?  123 LEU   A HA   1 
ATOM   2717 H HB2  A LEU   A 1 123 ? 19.989 -5.461  12.561  0.30 14.34 ?  123 LEU   A HB2  1 
ATOM   2718 H HB2  B LEU   A 1 123 ? 20.035 -5.454  12.712  0.70 14.13 ?  123 LEU   A HB2  1 
ATOM   2719 H HB3  A LEU   A 1 123 ? 21.064 -4.635  11.755  0.30 14.34 ?  123 LEU   A HB3  1 
ATOM   2720 H HB3  B LEU   A 1 123 ? 21.145 -4.648  11.924  0.70 14.13 ?  123 LEU   A HB3  1 
ATOM   2721 H HG   A LEU   A 1 123 ? 19.328 -3.697  10.471  0.30 14.95 ?  123 LEU   A HG   1 
ATOM   2722 H HG   B LEU   A 1 123 ? 19.428 -3.674  10.608  0.70 14.83 ?  123 LEU   A HG   1 
ATOM   2723 H HD11 A LEU   A 1 123 ? 17.116 -3.947  11.200  0.30 15.21 ?  123 LEU   A HD11 1 
ATOM   2724 H HD11 B LEU   A 1 123 ? 17.212 -3.880  11.319  0.70 15.69 ?  123 LEU   A HD11 1 
ATOM   2725 H HD12 A LEU   A 1 123 ? 17.704 -5.327  10.678  0.30 15.21 ?  123 LEU   A HD12 1 
ATOM   2726 H HD12 B LEU   A 1 123 ? 17.777 -5.290  10.855  0.70 15.69 ?  123 LEU   A HD12 1 
ATOM   2727 H HD13 A LEU   A 1 123 ? 17.597 -5.049  12.239  0.30 15.21 ?  123 LEU   A HD13 1 
ATOM   2728 H HD13 B LEU   A 1 123 ? 17.663 -4.950  12.403  0.70 15.69 ?  123 LEU   A HD13 1 
ATOM   2729 H HD21 A LEU   A 1 123 ? 18.580 -2.236  12.126  0.30 15.28 ?  123 LEU   A HD21 1 
ATOM   2730 H HD21 B LEU   A 1 123 ? 18.719 -2.182  12.237  0.70 15.61 ?  123 LEU   A HD21 1 
ATOM   2731 H HD22 A LEU   A 1 123 ? 19.112 -3.235  13.242  0.30 15.28 ?  123 LEU   A HD22 1 
ATOM   2732 H HD22 B LEU   A 1 123 ? 19.221 -3.180  13.367  0.70 15.61 ?  123 LEU   A HD22 1 
ATOM   2733 H HD23 A LEU   A 1 123 ? 20.140 -2.499  12.280  0.30 15.28 ?  123 LEU   A HD23 1 
ATOM   2734 H HD23 B LEU   A 1 123 ? 20.271 -2.482  12.399  0.70 15.61 ?  123 LEU   A HD23 1 
ATOM   2735 N N    A ALA   A 1 124 ? 19.679 -5.853  8.441   0.30 10.13 ?  124 ALA   A N    1 
ATOM   2736 N N    B ALA   A 1 124 ? 19.727 -5.933  8.544   0.70 10.60 ?  124 ALA   A N    1 
ATOM   2737 C CA   A ALA   A 1 124 ? 19.962 -5.589  7.034   0.30 10.11 ?  124 ALA   A CA   1 
ATOM   2738 C CA   B ALA   A 1 124 ? 20.003 -5.635  7.147   0.70 10.77 ?  124 ALA   A CA   1 
ATOM   2739 C C    A ALA   A 1 124 ? 18.712 -5.152  6.288   0.30 10.27 ?  124 ALA   A C    1 
ATOM   2740 C C    B ALA   A 1 124 ? 18.776 -5.125  6.407   0.70 10.55 ?  124 ALA   A C    1 
ATOM   2741 O O    A ALA   A 1 124 ? 17.596 -5.501  6.688   0.30 10.61 ?  124 ALA   A O    1 
ATOM   2742 O O    B ALA   A 1 124 ? 17.636 -5.440  6.776   0.70 11.68 ?  124 ALA   A O    1 
ATOM   2743 C CB   A ALA   A 1 124 ? 20.565 -6.825  6.352   0.30 10.48 ?  124 ALA   A CB   1 
ATOM   2744 C CB   B ALA   A 1 124 ? 20.532 -6.878  6.413   0.70 11.70 ?  124 ALA   A CB   1 
ATOM   2745 H H    A ALA   A 1 124 ? 18.866 -6.051  8.632   0.30 12.15 ?  124 ALA   A H    1 
ATOM   2746 H H    B ALA   A 1 124 ? 18.946 -6.255  8.691   0.70 12.72 ?  124 ALA   A H    1 
ATOM   2747 H HA   A ALA   A 1 124 ? 20.603 -4.874  6.986   0.30 12.13 ?  124 ALA   A HA   1 
ATOM   2748 H HA   B ALA   A 1 124 ? 20.704 -4.959  7.108   0.70 12.92 ?  124 ALA   A HA   1 
ATOM   2749 H HB1  A ALA   A 1 124 ? 20.736 -6.615  5.419   0.30 12.58 ?  124 ALA   A HB1  1 
ATOM   2750 H HB1  B ALA   A 1 124 ? 20.716 -6.653  5.485   0.70 14.04 ?  124 ALA   A HB1  1 
ATOM   2751 H HB2  A ALA   A 1 124 ? 21.399 -7.051  6.795   0.30 12.58 ?  124 ALA   A HB2  1 
ATOM   2752 H HB2  B ALA   A 1 124 ? 21.360 -7.176  6.840   0.70 14.04 ?  124 ALA   A HB2  1 
ATOM   2753 H HB3  A ALA   A 1 124 ? 19.943 -7.564  6.417   0.30 12.58 ?  124 ALA   A HB3  1 
ATOM   2754 H HB3  B ALA   A 1 124 ? 19.871 -7.581  6.459   0.70 14.04 ?  124 ALA   A HB3  1 
ATOM   2755 N N    A PRO   A 1 125 ? 18.872 -4.403  5.198   0.30 10.78 ?  125 PRO   A N    1 
ATOM   2756 N N    B PRO   A 1 125 ? 18.991 -4.361  5.339   0.70 10.17 ?  125 PRO   A N    1 
ATOM   2757 C CA   A PRO   A 1 125 ? 17.783 -4.187  4.246   0.30 11.00 ?  125 PRO   A CA   1 
ATOM   2758 C CA   B PRO   A 1 125 ? 17.912 -4.004  4.422   0.70 10.57 ?  125 PRO   A CA   1 
ATOM   2759 C C    A PRO   A 1 125 ? 17.869 -5.202  3.111   0.30 10.44 ?  125 PRO   A C    1 
ATOM   2760 C C    B PRO   A 1 125 ? 17.820 -5.055  3.320   0.70 10.82 ?  125 PRO   A C    1 
ATOM   2761 O O    A PRO   A 1 125 ? 18.841 -5.949  2.978   0.30 10.47 ?  125 PRO   A O    1 
ATOM   2762 O O    B PRO   A 1 125 ? 18.669 -5.944  3.196   0.70 11.18 ?  125 PRO   A O    1 
ATOM   2763 C CB   A PRO   A 1 125 ? 18.106 -2.789  3.708   0.30 11.37 ?  125 PRO   A CB   1 
ATOM   2764 C CB   B PRO   A 1 125 ? 18.431 -2.687  3.841   0.70 10.44 ?  125 PRO   A CB   1 
ATOM   2765 C CG   A PRO   A 1 125 ? 19.601 -2.791  3.651   0.30 11.38 ?  125 PRO   A CG   1 
ATOM   2766 C CG   B PRO   A 1 125 ? 19.913 -2.964  3.668   0.70 10.33 ?  125 PRO   A CG   1 
ATOM   2767 C CD   A PRO   A 1 125 ? 20.062 -3.605  4.844   0.30 11.15 ?  125 PRO   A CD   1 
ATOM   2768 C CD   B PRO   A 1 125 ? 20.291 -3.844  4.857   0.70 10.15 ?  125 PRO   A CD   1 
ATOM   2769 H HA   A PRO   A 1 125 ? 16.914 -4.208  4.671   0.30 13.20 ?  125 PRO   A HA   1 
ATOM   2770 H HA   B PRO   A 1 125 ? 17.061 -3.888  4.881   0.70 12.68 ?  125 PRO   A HA   1 
ATOM   2771 H HB2  A PRO   A 1 125 ? 17.724 -2.672  2.822   0.30 13.65 ?  125 PRO   A HB2  1 
ATOM   2772 H HB2  B PRO   A 1 125 ? 17.996 -2.506  2.993   0.70 12.52 ?  125 PRO   A HB2  1 
ATOM   2773 H HB3  A PRO   A 1 125 ? 17.781 -2.112  4.321   0.30 13.65 ?  125 PRO   A HB3  1 
ATOM   2774 H HB3  B PRO   A 1 125 ? 18.274 -1.962  4.474   0.70 12.52 ?  125 PRO   A HB3  1 
ATOM   2775 H HG2  A PRO   A 1 125 ? 19.892 -3.204  2.823   0.30 13.66 ?  125 PRO   A HG2  1 
ATOM   2776 H HG2  B PRO   A 1 125 ? 20.066 -3.433  2.832   0.70 12.40 ?  125 PRO   A HG2  1 
ATOM   2777 H HG3  A PRO   A 1 125 ? 19.928 -1.881  3.711   0.30 13.66 ?  125 PRO   A HG3  1 
ATOM   2778 H HG3  B PRO   A 1 125 ? 20.410 -2.128  3.685   0.70 12.40 ?  125 PRO   A HG3  1 
ATOM   2779 H HD2  A PRO   A 1 125 ? 20.801 -4.184  4.598   0.30 13.37 ?  125 PRO   A HD2  1 
ATOM   2780 H HD2  B PRO   A 1 125 ? 20.867 -4.568  4.567   0.70 12.18 ?  125 PRO   A HD2  1 
ATOM   2781 H HD3  A PRO   A 1 125 ? 20.299 -3.022  5.583   0.30 13.37 ?  125 PRO   A HD3  1 
ATOM   2782 H HD3  B PRO   A 1 125 ? 20.721 -3.305  5.544   0.70 12.18 ?  125 PRO   A HD3  1 
ATOM   2783 N N    A LEU   A 1 126 ? 16.833 -5.201  2.276   0.30 10.83 ?  126 LEU   A N    1 
ATOM   2784 N N    B LEU   A 1 126 ? 16.790 -4.907  2.493   0.70 11.82 ?  126 LEU   A N    1 
ATOM   2785 C CA   A LEU   A 1 126 ? 16.856 -5.995  1.055   0.30 11.48 ?  126 LEU   A CA   1 
ATOM   2786 C CA   B LEU   A 1 126 ? 16.629 -5.753  1.320   0.70 11.94 ?  126 LEU   A CA   1 
ATOM   2787 C C    A LEU   A 1 126 ? 17.800 -5.355  0.045   0.30 11.62 ?  126 LEU   A C    1 
ATOM   2788 C C    B LEU   A 1 126 ? 17.513 -5.236  0.189   0.70 12.36 ?  126 LEU   A C    1 
ATOM   2789 O O    A LEU   A 1 126 ? 17.613 -4.199  -0.351  0.30 12.31 ?  126 LEU   A O    1 
ATOM   2790 O O    B LEU   A 1 126 ? 17.287 -4.138  -0.333  0.70 13.75 ?  126 LEU   A O    1 
ATOM   2791 C CB   A LEU   A 1 126 ? 15.448 -6.095  0.479   0.30 12.18 ?  126 LEU   A CB   1 
ATOM   2792 C CB   B LEU   A 1 126 ? 15.161 -5.777  0.903   0.70 13.10 ?  126 LEU   A CB   1 
ATOM   2793 C CG   A LEU   A 1 126 ? 14.539 -7.072  1.221   0.30 12.45 ?  126 LEU   A CG   1 
ATOM   2794 C CG   B LEU   A 1 126 ? 14.753 -6.850  -0.107  0.70 13.60 ?  126 LEU   A CG   1 
ATOM   2795 C CD1  A LEU   A 1 126 ? 13.141 -7.007  0.643   0.30 12.78 ?  126 LEU   A CD1  1 
ATOM   2796 C CD1  B LEU   A 1 126 ? 14.900 -8.254  0.461   0.70 13.42 ?  126 LEU   A CD1  1 
ATOM   2797 C CD2  A LEU   A 1 126 ? 15.091 -8.492  1.142   0.30 12.41 ?  126 LEU   A CD2  1 
ATOM   2798 C CD2  B LEU   A 1 126 ? 13.322 -6.607  -0.547  0.70 14.52 ?  126 LEU   A CD2  1 
ATOM   2799 H H    A LEU   A 1 126 ? 16.111 -4.748  2.389   0.30 12.99 ?  126 LEU   A H    1 
ATOM   2800 H H    B LEU   A 1 126 ? 16.174 -4.306  2.584   0.70 14.18 ?  126 LEU   A H    1 
ATOM   2801 H HA   A LEU   A 1 126 ? 17.179 -6.888  1.251   0.30 13.78 ?  126 LEU   A HA   1 
ATOM   2802 H HA   B LEU   A 1 126 ? 16.904 -6.648  1.533   0.70 14.33 ?  126 LEU   A HA   1 
ATOM   2803 H HB2  A LEU   A 1 126 ? 15.028 -5.222  0.518   0.30 14.62 ?  126 LEU   A HB2  1 
ATOM   2804 H HB2  B LEU   A 1 126 ? 14.625 -5.917  1.698   0.70 15.72 ?  126 LEU   A HB2  1 
ATOM   2805 H HB3  A LEU   A 1 126 ? 15.502 -6.393  -0.442  0.30 14.62 ?  126 LEU   A HB3  1 
ATOM   2806 H HB3  B LEU   A 1 126 ? 14.937 -4.916  0.514   0.70 15.72 ?  126 LEU   A HB3  1 
ATOM   2807 H HG   A LEU   A 1 126 ? 14.489 -6.819  2.159   0.30 14.94 ?  126 LEU   A HG   1 
ATOM   2808 H HG   B LEU   A 1 126 ? 15.318 -6.777  -0.893  0.70 16.32 ?  126 LEU   A HG   1 
ATOM   2809 H HD11 A LEU   A 1 126 ? 12.570 -7.625  1.126   0.30 15.33 ?  126 LEU   A HD11 1 
ATOM   2810 H HD11 B LEU   A 1 126 ? 14.540 -8.890  -0.176  0.70 16.11 ?  126 LEU   A HD11 1 
ATOM   2811 H HD12 A LEU   A 1 126 ? 12.805 -6.102  0.737   0.30 15.33 ?  126 LEU   A HD12 1 
ATOM   2812 H HD12 B LEU   A 1 126 ? 15.841 -8.433  0.613   0.70 16.11 ?  126 LEU   A HD12 1 
ATOM   2813 H HD13 A LEU   A 1 126 ? 13.179 -7.252  -0.294  0.30 15.33 ?  126 LEU   A HD13 1 
ATOM   2814 H HD13 B LEU   A 1 126 ? 14.411 -8.308  1.296   0.70 16.11 ?  126 LEU   A HD13 1 
ATOM   2815 H HD21 A LEU   A 1 126 ? 14.388 -9.119  1.374   0.30 14.89 ?  126 LEU   A HD21 1 
ATOM   2816 H HD21 B LEU   A 1 126 ? 13.066 -7.291  -1.186  0.70 17.43 ?  126 LEU   A HD21 1 
ATOM   2817 H HD22 A LEU   A 1 126 ? 15.399 -8.658  0.238   0.30 14.89 ?  126 LEU   A HD22 1 
ATOM   2818 H HD22 B LEU   A 1 126 ? 12.741 -6.648  0.230   0.70 17.43 ?  126 LEU   A HD22 1 
ATOM   2819 H HD23 A LEU   A 1 126 ? 15.830 -8.580  1.765   0.30 14.89 ?  126 LEU   A HD23 1 
ATOM   2820 H HD23 B LEU   A 1 126 ? 13.259 -5.730  -0.959  0.70 17.43 ?  126 LEU   A HD23 1 
ATOM   2821 N N    A LEU   A 1 127 ? 18.812 -6.109  -0.375  0.30 11.60 ?  127 LEU   A N    1 
ATOM   2822 N N    B LEU   A 1 127 ? 18.506 -6.028  -0.207  0.70 12.23 ?  127 LEU   A N    1 
ATOM   2823 C CA   A LEU   A 1 127 ? 19.804 -5.584  -1.301  0.30 11.17 ?  127 LEU   A CA   1 
ATOM   2824 C CA   B LEU   A 1 127 ? 19.505 -5.548  -1.152  0.70 12.20 ?  127 LEU   A CA   1 
ATOM   2825 C C    A LEU   A 1 127 ? 19.204 -5.397  -2.687  0.30 11.05 ?  127 LEU   A C    1 
ATOM   2826 C C    B LEU   A 1 127 ? 18.920 -5.355  -2.548  0.70 11.84 ?  127 LEU   A C    1 
ATOM   2827 O O    A LEU   A 1 127 ? 18.393 -6.204  -3.154  0.30 11.00 ?  127 LEU   A O    1 
ATOM   2828 O O    B LEU   A 1 127 ? 18.039 -6.100  -3.002  0.70 12.39 ?  127 LEU   A O    1 
ATOM   2829 C CB   A LEU   A 1 127 ? 20.990 -6.538  -1.398  0.30 11.32 ?  127 LEU   A CB   1 
ATOM   2830 C CB   B LEU   A 1 127 ? 20.696 -6.508  -1.222  0.70 12.76 ?  127 LEU   A CB   1 
ATOM   2831 C CG   A LEU   A 1 127 ? 21.723 -6.881  -0.102  0.30 11.75 ?  127 LEU   A CG   1 
ATOM   2832 C CG   B LEU   A 1 127 ? 21.546 -6.666  0.045   0.70 13.76 ?  127 LEU   A CG   1 
ATOM   2833 C CD1  A LEU   A 1 127 ? 22.789 -7.923  -0.377  0.30 11.91 ?  127 LEU   A CD1  1 
ATOM   2834 C CD1  B LEU   A 1 127 ? 22.725 -7.590  -0.221  0.70 14.07 ?  127 LEU   A CD1  1 
ATOM   2835 C CD2  A LEU   A 1 127 ? 22.340 -5.642  0.513   0.30 12.04 ?  127 LEU   A CD2  1 
ATOM   2836 C CD2  B LEU   A 1 127 ? 22.025 -5.331  0.586   0.70 14.77 ?  127 LEU   A CD2  1 
ATOM   2837 H H    A LEU   A 1 127 ? 18.947 -6.922  -0.131  0.30 13.92 ?  127 LEU   A H    1 
ATOM   2838 H H    B LEU   A 1 127 ? 18.629 -6.836  0.061   0.70 14.68 ?  127 LEU   A H    1 
ATOM   2839 H HA   A LEU   A 1 127 ? 20.123 -4.726  -0.978  0.30 13.40 ?  127 LEU   A HA   1 
ATOM   2840 H HA   B LEU   A 1 127 ? 19.842 -4.691  -0.845  0.70 14.64 ?  127 LEU   A HA   1 
ATOM   2841 H HB2  A LEU   A 1 127 ? 20.673 -7.372  -1.773  0.30 13.58 ?  127 LEU   A HB2  1 
ATOM   2842 H HB2  B LEU   A 1 127 ? 20.364 -7.389  -1.450  0.70 15.32 ?  127 LEU   A HB2  1 
ATOM   2843 H HB3  A LEU   A 1 127 ? 21.643 -6.144  -1.996  0.30 13.58 ?  127 LEU   A HB3  1 
ATOM   2844 H HB3  B LEU   A 1 127 ? 21.294 -6.201  -1.922  0.70 15.32 ?  127 LEU   A HB3  1 
ATOM   2845 H HG   A LEU   A 1 127 ? 21.092 -7.256  0.534   0.30 14.10 ?  127 LEU   A HG   1 
ATOM   2846 H HG   B LEU   A 1 127 ? 21.005 -7.087  0.731   0.70 16.52 ?  127 LEU   A HG   1 
ATOM   2847 H HD11 A LEU   A 1 127 ? 23.217 -8.165  0.459   0.30 14.29 ?  127 LEU   A HD11 1 
ATOM   2848 H HD11 B LEU   A 1 127 ? 23.246 -7.682  0.594   0.70 16.88 ?  127 LEU   A HD11 1 
ATOM   2849 H HD12 A LEU   A 1 127 ? 22.371 -8.705  -0.773  0.30 14.29 ?  127 LEU   A HD12 1 
ATOM   2850 H HD12 B LEU   A 1 127 ? 22.391 -8.460  -0.496  0.70 16.88 ?  127 LEU   A HD12 1 
ATOM   2851 H HD13 A LEU   A 1 127 ? 23.441 -7.551  -0.989  0.30 14.29 ?  127 LEU   A HD13 1 
ATOM   2852 H HD13 B LEU   A 1 127 ? 23.274 -7.211  -0.923  0.70 16.88 ?  127 LEU   A HD13 1 
ATOM   2853 H HD21 A LEU   A 1 127 ? 22.848 -5.898  1.298   0.30 14.45 ?  127 LEU   A HD21 1 
ATOM   2854 H HD21 B LEU   A 1 127 ? 22.666 -5.489  1.298   0.70 17.73 ?  127 LEU   A HD21 1 
ATOM   2855 H HD22 A LEU   A 1 127 ? 22.925 -5.226  -0.140  0.30 14.45 ?  127 LEU   A HD22 1 
ATOM   2856 H HD22 B LEU   A 1 127 ? 22.443 -4.832  -0.131  0.70 17.73 ?  127 LEU   A HD22 1 
ATOM   2857 H HD23 A LEU   A 1 127 ? 21.632 -5.028  0.761   0.30 14.45 ?  127 LEU   A HD23 1 
ATOM   2858 H HD23 B LEU   A 1 127 ? 21.262 -4.842  0.931   0.70 17.73 ?  127 LEU   A HD23 1 
ATOM   2859 N N    A SER   A 1 128 ? 19.631 -4.325  -3.350  0.30 11.52 ?  128 SER   A N    1 
ATOM   2860 N N    B SER   A 1 128 ? 19.428 -4.328  -3.225  0.70 11.71 ?  128 SER   A N    1 
ATOM   2861 C CA   A SER   A 1 128 ? 19.230 -3.947  -4.698  0.30 11.63 ?  128 SER   A CA   1 
ATOM   2862 C CA   B SER   A 1 128 ? 19.067 -3.963  -4.591  0.70 11.86 ?  128 SER   A CA   1 
ATOM   2863 C C    A SER   A 1 128 ? 17.774 -3.495  -4.793  0.30 11.82 ?  128 SER   A C    1 
ATOM   2864 C C    B SER   A 1 128 ? 17.603 -3.564  -4.744  0.70 12.47 ?  128 SER   A C    1 
ATOM   2865 O O    A SER   A 1 128 ? 17.316 -3.173  -5.897  0.30 11.90 ?  128 SER   A O    1 
ATOM   2866 O O    B SER   A 1 128 ? 17.113 -3.443  -5.876  0.70 14.50 ?  128 SER   A O    1 
ATOM   2867 C CB   A SER   A 1 128 ? 19.551 -5.022  -5.749  0.30 11.72 ?  128 SER   A CB   1 
ATOM   2868 C CB   B SER   A 1 128 ? 19.495 -5.023  -5.614  0.70 12.20 ?  128 SER   A CB   1 
ATOM   2869 O OG   A SER   A 1 128 ? 20.950 -5.269  -5.812  0.30 12.04 ?  128 SER   A OG   1 
ATOM   2870 O OG   B SER   A 1 128 ? 20.918 -5.106  -5.678  0.70 12.83 ?  128 SER   A OG   1 
ATOM   2871 H H    A SER   A 1 128 ? 20.202 -3.770  -3.013  0.30 13.83 ?  128 SER   A H    1 
ATOM   2872 H H    B SER   A 1 128 ? 20.026 -3.798  -2.892  0.70 14.05 ?  128 SER   A H    1 
ATOM   2873 H HA   A SER   A 1 128 ? 19.762 -3.183  -4.936  0.30 13.95 ?  128 SER   A HA   1 
ATOM   2874 H HA   B SER   A 1 128 ? 19.572 -3.174  -4.807  0.70 14.23 ?  128 SER   A HA   1 
ATOM   2875 H HB2  A SER   A 1 128 ? 19.097 -5.846  -5.515  0.30 14.06 ?  128 SER   A HB2  1 
ATOM   2876 H HB2  B SER   A 1 128 ? 19.137 -5.889  -5.352  0.70 14.64 ?  128 SER   A HB2  1 
ATOM   2877 H HB3  A SER   A 1 128 ? 19.253 -4.712  -6.617  0.30 14.06 ?  128 SER   A HB3  1 
ATOM   2878 H HB3  B SER   A 1 128 ? 19.158 -4.776  -6.489  0.70 14.64 ?  128 SER   A HB3  1 
ATOM   2879 H HG   A SER   A 1 128 ? 21.361 -4.563  -6.005  0.30 14.45 ?  128 SER   A HG   1 
ATOM   2880 H HG   B SER   A 1 128 ? 21.238 -4.364  -5.892  0.70 15.40 ?  128 SER   A HG   1 
ATOM   2881 N N    A ALA   A 1 129 ? 17.049 -3.418  -3.674  0.30 12.71 ?  129 ALA   A N    1 
ATOM   2882 N N    B ALA   A 1 129 ? 16.911 -3.315  -3.633  0.70 13.58 ?  129 ALA   A N    1 
ATOM   2883 C CA   A ALA   A 1 129 ? 15.696 -2.883  -3.646  0.30 13.38 ?  129 ALA   A CA   1 
ATOM   2884 C CA   B ALA   A 1 129 ? 15.586 -2.721  -3.647  0.70 14.89 ?  129 ALA   A CA   1 
ATOM   2885 C C    A ALA   A 1 129 ? 15.732 -1.354  -3.549  0.30 12.98 ?  129 ALA   A C    1 
ATOM   2886 C C    B ALA   A 1 129 ? 15.697 -1.200  -3.816  0.70 14.26 ?  129 ALA   A C    1 
ATOM   2887 O O    A ALA   A 1 129 ? 16.798 -0.730  -3.522  0.30 13.52 ?  129 ALA   A O    1 
ATOM   2888 O O    B ALA   A 1 129 ? 16.786 -0.634  -3.954  0.70 14.42 ?  129 ALA   A O    1 
ATOM   2889 C CB   A ALA   A 1 129 ? 14.907 -3.510  -2.495  0.30 14.06 ?  129 ALA   A CB   1 
ATOM   2890 C CB   B ALA   A 1 129 ? 14.822 -3.102  -2.378  0.70 15.97 ?  129 ALA   A CB   1 
ATOM   2891 H H    A ALA   A 1 129 ? 17.331 -3.672  -2.900  0.30 15.25 ?  129 ALA   A H    1 
ATOM   2892 H H    B ALA   A 1 129 ? 17.203 -3.484  -2.837  0.70 16.29 ?  129 ALA   A H    1 
ATOM   2893 H HA   A ALA   A 1 129 ? 15.252 -3.114  -4.471  0.30 16.06 ?  129 ALA   A HA   1 
ATOM   2894 H HA   B ALA   A 1 129 ? 15.096 -3.071  -4.405  0.70 17.86 ?  129 ALA   A HA   1 
ATOM   2895 H HB1  A ALA   A 1 129 ? 14.010 -3.144  -2.492  0.30 16.88 ?  129 ALA   A HB1  1 
ATOM   2896 H HB1  B ALA   A 1 129 ? 13.940 -2.704  -2.411  0.70 19.17 ?  129 ALA   A HB1  1 
ATOM   2897 H HB2  A ALA   A 1 129 ? 14.876 -4.470  -2.624  0.30 16.88 ?  129 ALA   A HB2  1 
ATOM   2898 H HB2  B ALA   A 1 129 ? 14.747 -4.070  -2.330  0.70 19.17 ?  129 ALA   A HB2  1 
ATOM   2899 H HB3  A ALA   A 1 129 ? 15.353 -3.303  -1.656  0.30 16.88 ?  129 ALA   A HB3  1 
ATOM   2900 H HB3  B ALA   A 1 129 ? 15.308 -2.772  -1.605  0.70 19.17 ?  129 ALA   A HB3  1 
ATOM   2901 N N    A GLY   A 1 130 ? 14.552 -0.738  -3.515  0.30 12.62 ?  130 GLY   A N    1 
ATOM   2902 N N    B GLY   A 1 130 ? 14.555 -0.528  -3.814  0.70 16.07 ?  130 GLY   A N    1 
ATOM   2903 C CA   A GLY   A 1 130 ? 14.499 0.711   -3.415  0.30 12.61 ?  130 GLY   A CA   1 
ATOM   2904 C CA   B GLY   A 1 130 ? 14.605 0.907   -4.005  0.70 16.69 ?  130 GLY   A CA   1 
ATOM   2905 C C    A GLY   A 1 130 ? 15.023 1.340   -4.694  0.30 11.87 ?  130 GLY   A C    1 
ATOM   2906 C C    B GLY   A 1 130 ? 15.223 1.262   -5.343  0.70 15.88 ?  130 GLY   A C    1 
ATOM   2907 O O    A GLY   A 1 130 ? 14.735 0.877   -5.804  0.30 11.79 ?  130 GLY   A O    1 
ATOM   2908 O O    B GLY   A 1 130 ? 14.920 0.653   -6.374  0.70 15.22 ?  130 GLY   A O    1 
ATOM   2909 H H    A GLY   A 1 130 ? 13.789 -1.119  -3.582  0.30 15.14 ?  130 GLY   A H    1 
ATOM   2910 H H    B GLY   A 1 130 ? 13.772 -0.868  -3.715  0.70 19.28 ?  130 GLY   A H    1 
ATOM   2911 H HA2  A GLY   A 1 130 ? 13.583 1.005   -3.256  0.30 15.13 ?  130 GLY   A HA2  1 
ATOM   2912 H HA2  B GLY   A 1 130 ? 13.709 1.269   -3.970  0.70 20.03 ?  130 GLY   A HA2  1 
ATOM   2913 H HA3  A GLY   A 1 130 ? 15.049 1.017   -2.675  0.30 15.13 ?  130 GLY   A HA3  1 
ATOM   2914 H HA3  B GLY   A 1 130 ? 15.136 1.311   -3.303  0.70 20.03 ?  130 GLY   A HA3  1 
ATOM   2915 N N    A ILE   A 1 131 ? 15.818 2.399   -4.542  0.30 11.65 ?  131 ILE   A N    1 
ATOM   2916 N N    B ILE   A 1 131 ? 16.116 2.257   -5.330  0.70 16.30 ?  131 ILE   A N    1 
ATOM   2917 C CA   A ILE   A 1 131 ? 16.362 3.126   -5.687  0.30 10.89 ?  131 ILE   A CA   1 
ATOM   2918 C CA   B ILE   A 1 131 ? 16.635 2.818   -6.575  0.70 17.03 ?  131 ILE   A CA   1 
ATOM   2919 C C    A ILE   A 1 131 ? 17.408 2.340   -6.483  0.30 9.79  ?  131 ILE   A C    1 
ATOM   2920 C C    B ILE   A 1 131 ? 17.534 1.867   -7.346  0.70 17.04 ?  131 ILE   A C    1 
ATOM   2921 O O    A ILE   A 1 131 ? 17.888 2.830   -7.512  0.30 9.60  ?  131 ILE   A O    1 
ATOM   2922 O O    B ILE   A 1 131 ? 17.860 2.153   -8.503  0.70 17.59 ?  131 ILE   A O    1 
ATOM   2923 C CB   A ILE   A 1 131 ? 16.905 4.496   -5.239  0.30 12.28 ?  131 ILE   A CB   1 
ATOM   2924 C CB   B ILE   A 1 131 ? 17.334 4.181   -6.378  0.70 18.76 ?  131 ILE   A CB   1 
ATOM   2925 C CG1  A ILE   A 1 131 ? 18.154 4.319   -4.374  0.30 13.60 ?  131 ILE   A CG1  1 
ATOM   2926 C CG1  B ILE   A 1 131 ? 18.689 4.016   -5.684  0.70 20.77 ?  131 ILE   A CG1  1 
ATOM   2927 C CG2  A ILE   A 1 131 ? 15.836 5.250   -4.465  0.30 12.55 ?  131 ILE   A CG2  1 
ATOM   2928 C CG2  B ILE   A 1 131 ? 16.428 5.125   -5.598  0.70 19.16 ?  131 ILE   A CG2  1 
ATOM   2929 C CD1  A ILE   A 1 131 ? 18.801 5.613   -3.933  0.30 14.50 ?  131 ILE   A CD1  1 
ATOM   2930 C CD1  B ILE   A 1 131 ? 19.683 5.098   -6.039  0.70 22.38 ?  131 ILE   A CD1  1 
ATOM   2931 H H    A ILE   A 1 131 ? 16.034 2.758   -3.778  0.30 13.98 ?  131 ILE   A H    1 
ATOM   2932 H H    B ILE   A 1 131 ? 16.427 2.624   -4.618  0.70 19.55 ?  131 ILE   A H    1 
ATOM   2933 H HA   A ILE   A 1 131 ? 15.635 3.315   -6.301  0.30 13.06 ?  131 ILE   A HA   1 
ATOM   2934 H HA   B ILE   A 1 131 ? 15.888 2.979   -7.156  0.70 20.44 ?  131 ILE   A HA   1 
ATOM   2935 H HB   A ILE   A 1 131 ? 17.144 5.019   -6.023  0.30 14.73 ?  131 ILE   A HB   1 
ATOM   2936 H HB   B ILE   A 1 131 ? 17.488 4.572   -7.252  0.70 22.52 ?  131 ILE   A HB   1 
ATOM   2937 H HG12 A ILE   A 1 131 ? 17.910 3.825   -3.577  0.30 16.32 ?  131 ILE   A HG12 1 
ATOM   2938 H HG12 B ILE   A 1 131 ? 18.547 4.048   -4.728  0.70 24.92 ?  131 ILE   A HG12 1 
ATOM   2939 H HG13 A ILE   A 1 131 ? 18.818 3.823   -4.877  0.30 16.32 ?  131 ILE   A HG13 1 
ATOM   2940 H HG13 B ILE   A 1 131 ? 19.091 3.165   -5.921  0.70 24.92 ?  131 ILE   A HG13 1 
ATOM   2941 H HG21 A ILE   A 1 131 ? 16.105 6.178   -4.375  0.30 15.06 ?  131 ILE   A HG21 1 
ATOM   2942 H HG21 B ILE   A 1 131 ? 16.839 6.002   -5.565  0.70 23.00 ?  131 ILE   A HG21 1 
ATOM   2943 H HG22 A ILE   A 1 131 ? 15.001 5.190   -4.950  0.30 15.06 ?  131 ILE   A HG22 1 
ATOM   2944 H HG22 B ILE   A 1 131 ? 15.569 5.177   -6.044  0.70 23.00 ?  131 ILE   A HG22 1 
ATOM   2945 H HG23 A ILE   A 1 131 ? 15.741 4.847   -3.587  0.30 15.06 ?  131 ILE   A HG23 1 
ATOM   2946 H HG23 B ILE   A 1 131 ? 16.313 4.780   -4.698  0.70 23.00 ?  131 ILE   A HG23 1 
ATOM   2947 H HD11 A ILE   A 1 131 ? 19.636 5.406   -3.480  0.30 17.40 ?  131 ILE   A HD11 1 
ATOM   2948 H HD11 B ILE   A 1 131 ? 20.485 4.972   -5.508  0.70 26.85 ?  131 ILE   A HD11 1 
ATOM   2949 H HD12 A ILE   A 1 131 ? 18.977 6.159   -4.714  0.30 17.40 ?  131 ILE   A HD12 1 
ATOM   2950 H HD12 B ILE   A 1 131 ? 19.898 5.031   -6.984  0.70 26.85 ?  131 ILE   A HD12 1 
ATOM   2951 H HD13 A ILE   A 1 131 ? 18.204 6.076   -3.329  0.30 17.40 ?  131 ILE   A HD13 1 
ATOM   2952 H HD13 B ILE   A 1 131 ? 19.289 5.961   -5.849  0.70 26.85 ?  131 ILE   A HD13 1 
ATOM   2953 N N    A PHE   A 1 132 ? 17.771 1.124   -6.038  0.30 9.54  ?  132 PHE   A N    1 
ATOM   2954 N N    B PHE   A 1 132 ? 17.947 0.747   -6.757  0.70 17.74 ?  132 PHE   A N    1 
ATOM   2955 C CA   A PHE   A 1 132 ? 18.647 0.272   -6.844  0.30 9.46  ?  132 PHE   A CA   1 
ATOM   2956 C CA   B PHE   A 1 132 ? 18.738 -0.201  -7.533  0.70 19.36 ?  132 PHE   A CA   1 
ATOM   2957 C C    A PHE   A 1 132 ? 17.905 -0.437  -7.969  0.30 10.28 ?  132 PHE   A C    1 
ATOM   2958 C C    B PHE   A 1 132 ? 17.896 -1.056  -8.471  0.70 19.13 ?  132 PHE   A C    1 
ATOM   2959 O O    A PHE   A 1 132 ? 18.552 -0.984  -8.869  0.30 11.17 ?  132 PHE   A O    1 
ATOM   2960 O O    B PHE   A 1 132 ? 18.452 -1.693  -9.370  0.70 20.43 ?  132 PHE   A O    1 
ATOM   2961 C CB   A PHE   A 1 132 ? 19.374 -0.764  -5.979  0.30 8.68  ?  132 PHE   A CB   1 
ATOM   2962 C CB   B PHE   A 1 132 ? 19.656 -1.028  -6.620  0.70 21.43 ?  132 PHE   A CB   1 
ATOM   2963 C CG   A PHE   A 1 132 ? 20.575 -0.223  -5.258  0.30 7.73  ?  132 PHE   A CG   1 
ATOM   2964 C CG   B PHE   A 1 132 ? 21.008 -0.387  -6.379  0.70 23.91 ?  132 PHE   A CG   1 
ATOM   2965 C CD1  A PHE   A 1 132 ? 20.429 0.780   -4.318  0.30 8.69  ?  132 PHE   A CD1  1 
ATOM   2966 C CD1  B PHE   A 1 132 ? 21.293 0.891   -6.846  0.70 25.25 ?  132 PHE   A CD1  1 
ATOM   2967 C CD2  A PHE   A 1 132 ? 21.846 -0.718  -5.508  0.30 7.68  ?  132 PHE   A CD2  1 
ATOM   2968 C CD2  B PHE   A 1 132 ? 21.998 -1.070  -5.702  0.70 24.25 ?  132 PHE   A CD2  1 
ATOM   2969 C CE1  A PHE   A 1 132 ? 21.524 1.286   -3.646  0.30 8.95  ?  132 PHE   A CE1  1 
ATOM   2970 C CE1  B PHE   A 1 132 ? 22.529 1.467   -6.634  0.70 25.70 ?  132 PHE   A CE1  1 
ATOM   2971 C CE2  A PHE   A 1 132 ? 22.944 -0.223  -4.830  0.30 8.21  ?  132 PHE   A CE2  1 
ATOM   2972 C CE2  B PHE   A 1 132 ? 23.238 -0.499  -5.485  0.70 25.03 ?  132 PHE   A CE2  1 
ATOM   2973 C CZ   A PHE   A 1 132 ? 22.784 0.779   -3.900  0.30 8.50  ?  132 PHE   A CZ   1 
ATOM   2974 C CZ   B PHE   A 1 132 ? 23.504 0.771   -5.951  0.70 25.75 ?  132 PHE   A CZ   1 
ATOM   2975 H H    A PHE   A 1 132 ? 17.526 0.762   -5.292  0.30 11.45 ?  132 PHE   A H    1 
ATOM   2976 H H    B PHE   A 1 132 ? 17.784 0.509   -5.939  0.70 21.29 ?  132 PHE   A H    1 
ATOM   2977 H HA   A PHE   A 1 132 ? 19.319 0.833   -7.255  0.30 11.35 ?  132 PHE   A HA   1 
ATOM   2978 H HA   B PHE   A 1 132 ? 19.298 0.299   -8.134  0.70 23.23 ?  132 PHE   A HA   1 
ATOM   2979 H HB2  A PHE   A 1 132 ? 18.757 -1.090  -5.308  0.30 10.42 ?  132 PHE   A HB2  1 
ATOM   2980 H HB2  B PHE   A 1 132 ? 19.229 -1.143  -5.754  0.70 25.71 ?  132 PHE   A HB2  1 
ATOM   2981 H HB3  A PHE   A 1 132 ? 19.671 -1.494  -6.542  0.30 10.42 ?  132 PHE   A HB3  1 
ATOM   2982 H HB3  B PHE   A 1 132 ? 19.813 -1.897  -7.025  0.70 25.71 ?  132 PHE   A HB3  1 
ATOM   2983 H HD1  A PHE   A 1 132 ? 19.584 1.132   -4.141  0.30 10.43 ?  132 PHE   A HD1  1 
ATOM   2984 H HD1  B PHE   A 1 132 ? 20.638 1.369   -7.309  0.70 30.29 ?  132 PHE   A HD1  1 
ATOM   2985 H HD2  A PHE   A 1 132 ? 21.958 -1.394  -6.126  0.30 9.21  ?  132 PHE   A HD2  1 
ATOM   2986 H HD2  B PHE   A 1 132 ? 21.828 -1.927  -5.384  0.70 29.10 ?  132 PHE   A HD2  1 
ATOM   2987 H HE1  A PHE   A 1 132 ? 21.409 1.968   -3.016  0.30 10.74 ?  132 PHE   A HE1  1 
ATOM   2988 H HE1  B PHE   A 1 132 ? 22.700 2.324   -6.953  0.70 30.84 ?  132 PHE   A HE1  1 
ATOM   2989 H HE2  A PHE   A 1 132 ? 23.789 -0.562  -5.003  0.30 9.85  ?  132 PHE   A HE2  1 
ATOM   2990 H HE2  B PHE   A 1 132 ? 23.893 -0.972  -5.025  0.70 30.03 ?  132 PHE   A HE2  1 
ATOM   2991 H HZ   A PHE   A 1 132 ? 23.517 1.124   -3.445  0.30 10.20 ?  132 PHE   A HZ   1 
ATOM   2992 H HZ   B PHE   A 1 132 ? 24.337 1.157   -5.807  0.70 30.90 ?  132 PHE   A HZ   1 
ATOM   2993 N N    A GLY   A 1 133 ? 16.575 -0.462  -7.931  0.30 11.06 ?  133 GLY   A N    1 
ATOM   2994 N N    B GLY   A 1 133 ? 16.577 -1.051  -8.318  0.70 18.93 ?  133 GLY   A N    1 
ATOM   2995 C CA   A GLY   A 1 133 ? 15.781 -0.809  -9.089  0.30 11.66 ?  133 GLY   A CA   1 
ATOM   2996 C CA   B GLY   A 1 133 ? 15.696 -1.505  -9.374  0.70 19.09 ?  133 GLY   A CA   1 
ATOM   2997 C C    A GLY   A 1 133 ? 15.451 -2.270  -9.278  0.30 12.38 ?  133 GLY   A C    1 
ATOM   2998 C C    B GLY   A 1 133 ? 15.485 -2.998  -9.491  0.70 18.72 ?  133 GLY   A C    1 
ATOM   2999 O O    A GLY   A 1 133 ? 14.789 -2.600  -10.270 0.30 12.88 ?  133 GLY   A O    1 
ATOM   3000 O O    B GLY   A 1 133 ? 14.838 -3.438  -10.449 0.70 20.02 ?  133 GLY   A O    1 
ATOM   3001 H H    A GLY   A 1 133 ? 16.107 -0.281  -7.235  0.30 13.27 ?  133 GLY   A H    1 
ATOM   3002 H H    B GLY   A 1 133 ? 16.179 -0.779  -7.610  0.70 22.72 ?  133 GLY   A H    1 
ATOM   3003 H HA2  A GLY   A 1 133 ? 14.939 -0.338  -9.037  0.30 13.99 ?  133 GLY   A HA2  1 
ATOM   3004 H HA2  B GLY   A 1 133 ? 14.834 -1.083  -9.245  0.70 22.91 ?  133 GLY   A HA2  1 
ATOM   3005 H HA3  A GLY   A 1 133 ? 16.241 -0.528  -9.889  0.30 13.99 ?  133 GLY   A HA3  1 
ATOM   3006 H HA3  B GLY   A 1 133 ? 16.052 -1.194  -10.222 0.70 22.91 ?  133 GLY   A HA3  1 
ATOM   3007 N N    A ALA   A 1 134 ? 15.876 -3.155  -8.380  0.30 12.58 ?  134 ALA   A N    1 
ATOM   3008 N N    B ALA   A 1 134 ? 16.002 -3.797  -8.568  0.70 17.71 ?  134 ALA   A N    1 
ATOM   3009 C CA   A ALA   A 1 134 ? 15.552 -4.566  -8.520  0.30 13.20 ?  134 ALA   A CA   1 
ATOM   3010 C CA   B ALA   A 1 134 ? 15.758 -5.225  -8.649  0.70 17.25 ?  134 ALA   A CA   1 
ATOM   3011 C C    A ALA   A 1 134 ? 14.189 -4.868  -7.894  0.30 13.89 ?  134 ALA   A C    1 
ATOM   3012 C C    B ALA   A 1 134 ? 14.359 -5.553  -8.139  0.70 17.35 ?  134 ALA   A C    1 
ATOM   3013 O O    A ALA   A 1 134 ? 13.622 -4.057  -7.161  0.30 13.87 ?  134 ALA   A O    1 
ATOM   3014 O O    B ALA   A 1 134 ? 13.759 -4.811  -7.356  0.70 18.93 ?  134 ALA   A O    1 
ATOM   3015 C CB   A ALA   A 1 134 ? 16.649 -5.439  -7.906  0.30 13.62 ?  134 ALA   A CB   1 
ATOM   3016 C CB   B ALA   A 1 134 ? 16.795 -6.000  -7.841  0.70 17.07 ?  134 ALA   A CB   1 
ATOM   3017 H H    A ALA   A 1 134 ? 16.360 -2.968  -7.684  0.30 15.09 ?  134 ALA   A H    1 
ATOM   3018 H H    B ALA   A 1 134 ? 16.489 -3.547  -7.910  0.70 21.25 ?  134 ALA   A H    1 
ATOM   3019 H HA   A ALA   A 1 134 ? 15.497 -4.782  -9.456  0.30 15.83 ?  134 ALA   A HA   1 
ATOM   3020 H HA   B ALA   A 1 134 ? 15.818 -5.510  -9.575  0.70 20.70 ?  134 ALA   A HA   1 
ATOM   3021 H HB1  A ALA   A 1 134 ? 16.432 -6.372  -8.053  0.30 16.35 ?  134 ALA   A HB1  1 
ATOM   3022 H HB1  B ALA   A 1 134 ? 16.609 -6.951  -7.919  0.70 20.48 ?  134 ALA   A HB1  1 
ATOM   3023 H HB2  A ALA   A 1 134 ? 17.495 -5.226  -8.336  0.30 16.35 ?  134 ALA   A HB2  1 
ATOM   3024 H HB2  B ALA   A 1 134 ? 17.677 -5.807  -8.194  0.70 20.48 ?  134 ALA   A HB2  1 
ATOM   3025 H HB3  A ALA   A 1 134 ? 16.711 -5.259  -6.955  0.30 16.35 ?  134 ALA   A HB3  1 
ATOM   3026 H HB3  B ALA   A 1 134 ? 16.740 -5.728  -6.913  0.70 20.48 ?  134 ALA   A HB3  1 
ATOM   3027 N N    A ASP   A 1 135 ? 13.655 -6.046  -8.215  0.30 14.50 ?  135 ASP   A N    1 
ATOM   3028 N N    B ASP   A 1 135 ? 13.840 -6.677  -8.607  0.70 17.02 ?  135 ASP   A N    1 
ATOM   3029 C CA   A ASP   A 1 135 ? 12.399 -6.514  -7.623  0.30 15.21 ?  135 ASP   A CA   1 
ATOM   3030 C CA   B ASP   A 1 135 ? 12.560 -7.173  -8.137  0.70 17.77 ?  135 ASP   A CA   1 
ATOM   3031 C C    A ASP   A 1 135 ? 12.652 -6.951  -6.186  0.30 14.46 ?  135 ASP   A C    1 
ATOM   3032 C C    B ASP   A 1 135 ? 12.694 -7.528  -6.661  0.70 16.07 ?  135 ASP   A C    1 
ATOM   3033 O O    A ASP   A 1 135 ? 13.416 -7.900  -5.965  0.30 14.32 ?  135 ASP   A O    1 
ATOM   3034 O O    B ASP   A 1 135 ? 13.519 -8.380  -6.316  0.70 15.55 ?  135 ASP   A O    1 
ATOM   3035 C CB   A ASP   A 1 135 ? 11.859 -7.699  -8.426  0.30 17.03 ?  135 ASP   A CB   1 
ATOM   3036 C CB   B ASP   A 1 135 ? 12.194 -8.409  -8.954  0.70 20.87 ?  135 ASP   A CB   1 
ATOM   3037 C CG   A ASP   A 1 135 ? 10.546 -8.254  -7.873  0.30 18.41 ?  135 ASP   A CG   1 
ATOM   3038 C CG   B ASP   A 1 135 ? 10.838 -8.978  -8.577  0.70 23.94 ?  135 ASP   A CG   1 
ATOM   3039 O OD1  A ASP   A 1 135 ? 10.009 -7.691  -6.899  0.30 19.10 ?  135 ASP   A OD1  1 
ATOM   3040 O OD1  B ASP   A 1 135 ? 10.691 -9.472  -7.442  0.70 24.98 ?  135 ASP   A OD1  1 
ATOM   3041 O OD2  A ASP   A 1 135 ? 10.054 -9.266  -8.420  0.30 19.61 -1 135 ASP   A OD2  1 
ATOM   3042 O OD2  B ASP   A 1 135 ? 9.911  -8.922  -9.414  0.70 25.33 -1 135 ASP   A OD2  1 
ATOM   3043 H H    A ASP   A 1 135 ? 13.996 -6.594  -8.778  0.30 17.40 ?  135 ASP   A H    1 
ATOM   3044 H H    B ASP   A 1 135 ? 14.218 -7.187  -9.190  0.70 20.43 ?  135 ASP   A H    1 
ATOM   3045 H HA   A ASP   A 1 135 ? 11.742 -5.800  -7.644  0.30 18.25 ?  135 ASP   A HA   1 
ATOM   3046 H HA   B ASP   A 1 135 ? 11.876 -6.502  -8.262  0.70 21.33 ?  135 ASP   A HA   1 
ATOM   3047 H HB2  A ASP   A 1 135 ? 11.698 -7.417  -9.334  0.30 20.43 ?  135 ASP   A HB2  1 
ATOM   3048 H HB2  B ASP   A 1 135 ? 12.168 -8.167  -9.894  0.70 25.05 ?  135 ASP   A HB2  1 
ATOM   3049 H HB3  A ASP   A 1 135 ? 12.511 -8.415  -8.404  0.30 20.43 ?  135 ASP   A HB3  1 
ATOM   3050 H HB3  B ASP   A 1 135 ? 12.872 -9.093  -8.812  0.70 25.05 ?  135 ASP   A HB3  1 
ATOM   3051 N N    A PRO   A 1 136 ? 12.046 -6.304  -5.186  0.30 13.57 ?  136 PRO   A N    1 
ATOM   3052 N N    B PRO   A 1 136 ? 11.933 -6.901  -5.760  0.70 15.69 ?  136 PRO   A N    1 
ATOM   3053 C CA   A PRO   A 1 136 ? 12.286 -6.729  -3.795  0.30 13.48 ?  136 PRO   A CA   1 
ATOM   3054 C CA   B PRO   A 1 136 ? 12.123 -7.194  -4.328  0.70 15.18 ?  136 PRO   A CA   1 
ATOM   3055 C C    A PRO   A 1 136 ? 11.852 -8.156  -3.502  0.30 13.11 ?  136 PRO   A C    1 
ATOM   3056 C C    B PRO   A 1 136 ? 11.769 -8.619  -3.933  0.70 14.53 ?  136 PRO   A C    1 
ATOM   3057 O O    A PRO   A 1 136 ? 12.452 -8.809  -2.637  0.30 12.83 ?  136 PRO   A O    1 
ATOM   3058 O O    B PRO   A 1 136 ? 12.406 -9.174  -3.030  0.70 13.95 ?  136 PRO   A O    1 
ATOM   3059 C CB   A PRO   A 1 136 ? 11.505 -5.695  -2.967  0.30 13.90 ?  136 PRO   A CB   1 
ATOM   3060 C CB   B PRO   A 1 136 ? 11.239 -6.148  -3.631  0.70 16.02 ?  136 PRO   A CB   1 
ATOM   3061 C CG   A PRO   A 1 136 ? 10.512 -5.107  -3.912  0.30 14.27 ?  136 PRO   A CG   1 
ATOM   3062 C CG   B PRO   A 1 136 ? 10.240 -5.740  -4.674  0.70 17.58 ?  136 PRO   A CG   1 
ATOM   3063 C CD   A PRO   A 1 136 ? 11.155 -5.132  -5.259  0.30 13.66 ?  136 PRO   A CD   1 
ATOM   3064 C CD   B PRO   A 1 136 ? 10.972 -5.807  -5.979  0.70 16.97 ?  136 PRO   A CD   1 
ATOM   3065 H HA   A PRO   A 1 136 ? 13.228 -6.639  -3.580  0.30 16.18 ?  136 PRO   A HA   1 
ATOM   3066 H HA   B PRO   A 1 136 ? 13.046 -7.037  -4.084  0.70 18.22 ?  136 PRO   A HA   1 
ATOM   3067 H HB2  A PRO   A 1 136 ? 11.056 -6.131  -2.227  0.30 16.68 ?  136 PRO   A HB2  1 
ATOM   3068 H HB2  B PRO   A 1 136 ? 10.799 -6.546  -2.863  0.70 19.22 ?  136 PRO   A HB2  1 
ATOM   3069 H HB3  A PRO   A 1 136 ? 12.110 -5.005  -2.639  0.30 16.68 ?  136 PRO   A HB3  1 
ATOM   3070 H HB3  B PRO   A 1 136 ? 11.788 -5.393  -3.358  0.70 19.22 ?  136 PRO   A HB3  1 
ATOM   3071 H HG2  A PRO   A 1 136 ? 9.708  -5.650  -3.910  0.30 17.13 ?  136 PRO   A HG2  1 
ATOM   3072 H HG2  B PRO   A 1 136 ? 9.495  -6.359  -4.671  0.70 21.09 ?  136 PRO   A HG2  1 
ATOM   3073 H HG3  A PRO   A 1 136 ? 10.310 -4.197  -3.647  0.30 17.13 ?  136 PRO   A HG3  1 
ATOM   3074 H HG3  B PRO   A 1 136 ? 9.939  -4.836  -4.502  0.70 21.09 ?  136 PRO   A HG3  1 
ATOM   3075 H HD2  A PRO   A 1 136 ? 10.483 -5.260  -5.948  0.30 16.40 ?  136 PRO   A HD2  1 
ATOM   3076 H HD2  B PRO   A 1 136 ? 10.362 -6.032  -6.700  0.70 20.37 ?  136 PRO   A HD2  1 
ATOM   3077 H HD3  A PRO   A 1 136 ? 11.668 -4.320  -5.408  0.30 16.40 ?  136 PRO   A HD3  1 
ATOM   3078 H HD3  B PRO   A 1 136 ? 11.444 -4.978  -6.154  0.70 20.37 ?  136 PRO   A HD3  1 
ATOM   3079 N N    A ILE   A 1 137 ? 10.825 -8.664  -4.188  0.30 13.59 ?  137 ILE   A N    1 
ATOM   3080 N N    B ILE   A 1 137 ? 10.763 -9.229  -4.566  0.70 15.27 ?  137 ILE   A N    1 
ATOM   3081 C CA   A ILE   A 1 137 ? 10.440 -10.060 -4.000  0.30 14.63 ?  137 ILE   A CA   1 
ATOM   3082 C CA   B ILE   A 1 137 ? 10.457 -10.636 -4.300  0.70 16.30 ?  137 ILE   A CA   1 
ATOM   3083 C C    A ILE   A 1 137 ? 11.577 -10.982 -4.420  0.30 14.49 ?  137 ILE   A C    1 
ATOM   3084 C C    B ILE   A 1 137 ? 11.664 -11.509 -4.619  0.70 15.64 ?  137 ILE   A C    1 
ATOM   3085 O O    A ILE   A 1 137 ? 11.855 -11.992 -3.761  0.30 15.11 ?  137 ILE   A O    1 
ATOM   3086 O O    B ILE   A 1 137 ? 12.025 -12.407 -3.848  0.70 15.88 ?  137 ILE   A O    1 
ATOM   3087 C CB   A ILE   A 1 137 ? 9.133  -10.370 -4.755  0.30 15.53 ?  137 ILE   A CB   1 
ATOM   3088 C CB   B ILE   A 1 137 ? 9.202  -11.084 -5.078  0.70 17.74 ?  137 ILE   A CB   1 
ATOM   3089 C CG1  A ILE   A 1 137 ? 7.986  -9.515  -4.210  0.30 16.09 ?  137 ILE   A CG1  1 
ATOM   3090 C CG1  B ILE   A 1 137 ? 7.980  -10.272 -4.646  0.70 18.83 ?  137 ILE   A CG1  1 
ATOM   3091 C CG2  A ILE   A 1 137 ? 8.788  -11.850 -4.644  0.30 15.82 ?  137 ILE   A CG2  1 
ATOM   3092 C CG2  B ILE   A 1 137 ? 8.939  -12.577 -4.871  0.70 18.23 ?  137 ILE   A CG2  1 
ATOM   3093 C CD1  A ILE   A 1 137 ? 6.664  -9.784  -4.882  0.30 16.66 ?  137 ILE   A CD1  1 
ATOM   3094 C CD1  B ILE   A 1 137 ? 6.734  -10.543 -5.468  0.70 20.01 ?  137 ILE   A CD1  1 
ATOM   3095 H H    A ILE   A 1 137 ? 10.346 -8.225  -4.755  0.30 16.31 ?  137 ILE   A H    1 
ATOM   3096 H H    B ILE   A 1 137 ? 10.242 -8.860  -5.139  0.70 18.33 ?  137 ILE   A H    1 
ATOM   3097 H HA   A ILE   A 1 137 ? 10.275 -10.205 -3.057  0.30 17.56 ?  137 ILE   A HA   1 
ATOM   3098 H HA   B ILE   A 1 137 ? 10.265 -10.747 -3.357  0.70 19.57 ?  137 ILE   A HA   1 
ATOM   3099 H HB   A ILE   A 1 137 ? 9.256  -10.150 -5.688  0.30 18.64 ?  137 ILE   A HB   1 
ATOM   3100 H HB   B ILE   A 1 137 ? 9.352  -10.937 -6.022  0.70 21.29 ?  137 ILE   A HB   1 
ATOM   3101 H HG12 A ILE   A 1 137 ? 7.877  -9.693  -3.262  0.30 19.31 ?  137 ILE   A HG12 1 
ATOM   3102 H HG12 B ILE   A 1 137 ? 7.777  -10.484 -3.722  0.70 22.59 ?  137 ILE   A HG12 1 
ATOM   3103 H HG13 A ILE   A 1 137 ? 8.197  -8.576  -4.344  0.30 19.31 ?  137 ILE   A HG13 1 
ATOM   3104 H HG13 B ILE   A 1 137 ? 8.191  -9.331  -4.730  0.70 22.59 ?  137 ILE   A HG13 1 
ATOM   3105 H HG21 A ILE   A 1 137 ? 8.023  -12.041 -5.205  0.30 18.99 ?  137 ILE   A HG21 1 
ATOM   3106 H HG21 B ILE   A 1 137 ? 8.093  -12.815 -5.284  0.70 21.87 ?  137 ILE   A HG21 1 
ATOM   3107 H HG22 A ILE   A 1 137 ? 9.539  -12.381 -4.940  0.30 18.99 ?  137 ILE   A HG22 1 
ATOM   3108 H HG22 B ILE   A 1 137 ? 9.653  -13.088 -5.283  0.70 21.87 ?  137 ILE   A HG22 1 
ATOM   3109 H HG23 A ILE   A 1 137 ? 8.581  -12.054 -3.719  0.30 18.99 ?  137 ILE   A HG23 1 
ATOM   3110 H HG23 B ILE   A 1 137 ? 8.904  -12.763 -3.920  0.70 21.87 ?  137 ILE   A HG23 1 
ATOM   3111 H HD11 A ILE   A 1 137 ? 6.007  -9.214  -4.468  0.30 19.99 ?  137 ILE   A HD11 1 
ATOM   3112 H HD11 B ILE   A 1 137 ? 6.090  -9.840  -5.297  0.70 24.02 ?  137 ILE   A HD11 1 
ATOM   3113 H HD12 A ILE   A 1 137 ? 6.737  -9.584  -5.830  0.30 19.99 ?  137 ILE   A HD12 1 
ATOM   3114 H HD12 B ILE   A 1 137 ? 6.976  -10.550 -6.408  0.70 24.02 ?  137 ILE   A HD12 1 
ATOM   3115 H HD13 A ILE   A 1 137 ? 6.410  -10.712 -4.754  0.30 19.99 ?  137 ILE   A HD13 1 
ATOM   3116 H HD13 B ILE   A 1 137 ? 6.367  -11.402 -5.213  0.70 24.02 ?  137 ILE   A HD13 1 
ATOM   3117 N N    A HIS   A 1 138 ? 12.251 -10.652 -5.525  0.30 14.02 ?  138 HIS   A N    1 
ATOM   3118 N N    B HIS   A 1 138 ? 12.313 -11.254 -5.757  0.70 15.36 ?  138 HIS   A N    1 
ATOM   3119 C CA   A HIS   A 1 138 ? 13.411 -11.433 -5.939  0.30 13.75 ?  138 HIS   A CA   1 
ATOM   3120 C CA   B HIS   A 1 138 ? 13.509 -12.012 -6.109  0.70 15.39 ?  138 HIS   A CA   1 
ATOM   3121 C C    A HIS   A 1 138 ? 14.554 -11.294 -4.940  0.30 13.01 ?  138 HIS   A C    1 
ATOM   3122 C C    B HIS   A 1 138 ? 14.624 -11.783 -5.097  0.70 13.88 ?  138 HIS   A C    1 
ATOM   3123 O O    A HIS   A 1 138 ? 15.241 -12.277 -4.634  0.30 13.22 ?  138 HIS   A O    1 
ATOM   3124 O O    B HIS   A 1 138 ? 15.303 -12.732 -4.689  0.70 14.31 ?  138 HIS   A O    1 
ATOM   3125 C CB   A HIS   A 1 138 ? 13.852 -11.012 -7.341  0.30 14.01 ?  138 HIS   A CB   1 
ATOM   3126 C CB   B HIS   A 1 138 ? 13.975 -11.626 -7.512  0.70 16.91 ?  138 HIS   A CB   1 
ATOM   3127 C CG   A HIS   A 1 138 ? 15.128 -11.657 -7.790  0.30 14.43 ?  138 HIS   A CG   1 
ATOM   3128 C CG   B HIS   A 1 138 ? 15.250 -12.290 -7.931  0.70 18.38 ?  138 HIS   A CG   1 
ATOM   3129 N ND1  A HIS   A 1 138 ? 15.237 -13.013 -8.017  0.30 14.93 ?  138 HIS   A ND1  1 
ATOM   3130 N ND1  B HIS   A 1 138 ? 15.352 -13.650 -8.128  0.70 18.99 ?  138 HIS   A ND1  1 
ATOM   3131 C CD2  A HIS   A 1 138 ? 16.351 -11.134 -8.043  0.30 14.48 ?  138 HIS   A CD2  1 
ATOM   3132 C CD2  B HIS   A 1 138 ? 16.477 -11.780 -8.191  0.70 19.25 ?  138 HIS   A CD2  1 
ATOM   3133 C CE1  A HIS   A 1 138 ? 16.471 -13.295 -8.395  0.30 14.97 ?  138 HIS   A CE1  1 
ATOM   3134 C CE1  B HIS   A 1 138 ? 16.585 -13.950 -8.494  0.70 19.69 ?  138 HIS   A CE1  1 
ATOM   3135 N NE2  A HIS   A 1 138 ? 17.168 -12.173 -8.419  0.30 14.69 ?  138 HIS   A NE2  1 
ATOM   3136 N NE2  B HIS   A 1 138 ? 17.289 -12.833 -8.538  0.70 19.69 ?  138 HIS   A NE2  1 
ATOM   3137 H H    A HIS   A 1 138 ? 12.051 -9.996  -6.046  0.30 16.82 ?  138 HIS   A H    1 
ATOM   3138 H H    B HIS   A 1 138 ? 12.090 -10.653 -6.328  0.70 18.43 ?  138 HIS   A H    1 
ATOM   3139 H HA   A HIS   A 1 138 ? 13.162 -12.366 -5.972  0.30 16.49 ?  138 HIS   A HA   1 
ATOM   3140 H HA   B HIS   A 1 138 ? 13.294 -12.959 -6.115  0.70 18.46 ?  138 HIS   A HA   1 
ATOM   3141 H HB2  A HIS   A 1 138 ? 13.154 -11.256 -7.971  0.30 16.81 ?  138 HIS   A HB2  1 
ATOM   3142 H HB2  B HIS   A 1 138 ? 13.286 -11.875 -8.149  0.70 20.30 ?  138 HIS   A HB2  1 
ATOM   3143 H HB3  A HIS   A 1 138 ? 13.982 -10.051 -7.353  0.30 16.81 ?  138 HIS   A HB3  1 
ATOM   3144 H HB3  B HIS   A 1 138 ? 14.119 -10.668 -7.540  0.70 20.30 ?  138 HIS   A HB3  1 
ATOM   3145 H HD1  A HIS   A 1 138 ? 14.595 -13.585 -7.926  0.30 17.92 ?  138 HIS   A HD1  1 
ATOM   3146 H HD1  B HIS   A 1 138 ? 14.707 -14.217 -8.032  0.70 22.79 ?  138 HIS   A HD1  1 
ATOM   3147 H HD2  A HIS   A 1 138 ? 16.587 -10.239 -7.976  0.30 17.38 ?  138 HIS   A HD2  1 
ATOM   3148 H HD2  B HIS   A 1 138 ? 16.723 -10.889 -8.146  0.70 23.10 ?  138 HIS   A HD2  1 
ATOM   3149 H HE1  A HIS   A 1 138 ? 16.788 -14.143 -8.606  0.30 17.96 ?  138 HIS   A HE1  1 
ATOM   3150 H HE1  B HIS   A 1 138 ? 16.899 -14.805 -8.685  0.70 23.63 ?  138 HIS   A HE1  1 
ATOM   3151 N N    A SER   A 1 139 ? 14.767 -10.082 -4.416  0.30 12.10 ?  139 SER   A N    1 
ATOM   3152 N N    B SER   A 1 139 ? 14.831 -10.533 -4.676  0.70 12.79 ?  139 SER   A N    1 
ATOM   3153 C CA   A SER   A 1 139 ? 15.829 -9.869  -3.436  0.30 11.69 ?  139 SER   A CA   1 
ATOM   3154 C CA   B SER   A 1 139 ? 15.893 -10.266 -3.714  0.70 12.08 ?  139 SER   A CA   1 
ATOM   3155 C C    A SER   A 1 139 ? 15.620 -10.731 -2.194  0.30 11.64 ?  139 SER   A C    1 
ATOM   3156 C C    B SER   A 1 139 ? 15.663 -11.028 -2.419  0.70 12.00 ?  139 SER   A C    1 
ATOM   3157 O O    A SER   A 1 139 ? 16.577 -11.309 -1.666  0.30 11.74 ?  139 SER   A O    1 
ATOM   3158 O O    B SER   A 1 139 ? 16.608 -11.575 -1.840  0.70 12.18 ?  139 SER   A O    1 
ATOM   3159 C CB   A SER   A 1 139 ? 15.920 -8.380  -3.077  0.30 11.37 ?  139 SER   A CB   1 
ATOM   3160 C CB   B SER   A 1 139 ? 16.005 -8.770  -3.433  0.70 11.35 ?  139 SER   A CB   1 
ATOM   3161 O OG   A SER   A 1 139 ? 16.933 -8.143  -2.107  0.30 11.66 ?  139 SER   A OG   1 
ATOM   3162 O OG   B SER   A 1 139 ? 17.077 -8.532  -2.535  0.70 10.76 ?  139 SER   A OG   1 
ATOM   3163 H H    A SER   A 1 139 ? 14.317 -9.372  -4.608  0.30 14.52 ?  139 SER   A H    1 
ATOM   3164 H H    B SER   A 1 139 ? 14.385 -9.851  -4.926  0.70 15.34 ?  139 SER   A H    1 
ATOM   3165 H HA   A SER   A 1 139 ? 16.678 -10.121 -3.827  0.30 14.03 ?  139 SER   A HA   1 
ATOM   3166 H HA   B SER   A 1 139 ? 16.737 -10.566 -4.085  0.70 14.49 ?  139 SER   A HA   1 
ATOM   3167 H HB2  A SER   A 1 139 ? 16.128 -7.869  -3.882  0.30 13.65 ?  139 SER   A HB2  1 
ATOM   3168 H HB2  B SER   A 1 139 ? 16.186 -8.307  -4.263  0.70 13.62 ?  139 SER   A HB2  1 
ATOM   3169 H HB3  A SER   A 1 139 ? 15.074 -8.082  -2.713  0.30 13.65 ?  139 SER   A HB3  1 
ATOM   3170 H HB3  B SER   A 1 139 ? 15.175 -8.458  -3.043  0.70 13.62 ?  139 SER   A HB3  1 
ATOM   3171 H HG   A SER   A 1 139 ? 16.981 -7.314  -1.935  0.30 13.99 ?  139 SER   A HG   1 
ATOM   3172 H HG   B SER   A 1 139 ? 17.134 -7.712  -2.365  0.70 12.92 ?  139 SER   A HG   1 
ATOM   3173 N N    A LEU   A 1 140 ? 14.378 -10.840 -1.715  0.30 11.72 ?  140 LEU   A N    1 
ATOM   3174 N N    B LEU   A 1 140 ? 14.416 -11.079 -1.950  0.70 12.48 ?  140 LEU   A N    1 
ATOM   3175 C CA   A LEU   A 1 140 ? 14.130 -11.657 -0.529  0.30 11.81 ?  140 LEU   A CA   1 
ATOM   3176 C CA   B LEU   A 1 140 ? 14.128 -11.829 -0.736  0.70 12.62 ?  140 LEU   A CA   1 
ATOM   3177 C C    A LEU   A 1 140 ? 14.394 -13.135 -0.810  0.30 12.13 ?  140 LEU   A C    1 
ATOM   3178 C C    B LEU   A 1 140 ? 14.395 -13.313 -0.948  0.70 12.92 ?  140 LEU   A C    1 
ATOM   3179 O O    A LEU   A 1 140 ? 14.910 -13.855 0.055   0.30 12.50 ?  140 LEU   A O    1 
ATOM   3180 O O    B LEU   A 1 140 ? 14.957 -13.985 -0.074  0.70 13.54 ?  140 LEU   A O    1 
ATOM   3181 C CB   A LEU   A 1 140 ? 12.704 -11.435 -0.020  0.30 12.11 ?  140 LEU   A CB   1 
ATOM   3182 C CB   B LEU   A 1 140 ? 12.679 -11.589 -0.313  0.70 12.93 ?  140 LEU   A CB   1 
ATOM   3183 C CG   A LEU   A 1 140 ? 12.273 -12.331 1.145   0.30 12.73 ?  140 LEU   A CG   1 
ATOM   3184 C CG   B LEU   A 1 140 ? 12.235 -12.274 0.981   0.70 13.85 ?  140 LEU   A CG   1 
ATOM   3185 C CD1  A LEU   A 1 140 ? 13.204 -12.181 2.337   0.30 12.98 ?  140 LEU   A CD1  1 
ATOM   3186 C CD1  B LEU   A 1 140 ? 13.130 -11.914 2.157   0.70 14.04 ?  140 LEU   A CD1  1 
ATOM   3187 C CD2  A LEU   A 1 140 ? 10.835 -12.040 1.552   0.30 13.01 ?  140 LEU   A CD2  1 
ATOM   3188 C CD2  B LEU   A 1 140 ? 10.783 -11.919 1.284   0.70 14.48 ?  140 LEU   A CD2  1 
ATOM   3189 H H    A LEU   A 1 140 ? 13.681 -10.459 -2.051  0.30 14.07 ?  140 LEU   A H    1 
ATOM   3190 H H    B LEU   A 1 140 ? 13.737 -10.700 -2.308  0.70 14.97 ?  140 LEU   A H    1 
ATOM   3191 H HA   A LEU   A 1 140 ? 14.738 -11.374 0.170   0.30 14.18 ?  140 LEU   A HA   1 
ATOM   3192 H HA   B LEU   A 1 140 ? 14.707 -11.524 -0.027  0.70 15.14 ?  140 LEU   A HA   1 
ATOM   3193 H HB2  A LEU   A 1 140 ? 12.624 -10.514 0.281   0.30 14.54 ?  140 LEU   A HB2  1 
ATOM   3194 H HB2  B LEU   A 1 140 ? 12.552 -10.640 -0.192  0.70 15.51 ?  140 LEU   A HB2  1 
ATOM   3195 H HB3  A LEU   A 1 140 ? 12.087 -11.591 -0.749  0.30 14.54 ?  140 LEU   A HB3  1 
ATOM   3196 H HB3  B LEU   A 1 140 ? 12.096 -11.908 -1.020  0.70 15.51 ?  140 LEU   A HB3  1 
ATOM   3197 H HG   A LEU   A 1 140 ? 12.309 -13.256 0.858   0.30 15.27 ?  140 LEU   A HG   1 
ATOM   3198 H HG   B LEU   A 1 140 ? 12.276 -13.237 0.858   0.70 16.62 ?  140 LEU   A HG   1 
ATOM   3199 H HD11 A LEU   A 1 140 ? 12.849 -12.695 3.079   0.30 15.58 ?  140 LEU   A HD11 1 
ATOM   3200 H HD11 B LEU   A 1 140 ? 12.737 -12.269 2.971   0.70 16.85 ?  140 LEU   A HD11 1 
ATOM   3201 H HD12 A LEU   A 1 140 ? 14.081 -12.515 2.094   0.30 15.58 ?  140 LEU   A HD12 1 
ATOM   3202 H HD12 B LEU   A 1 140 ? 14.005 -12.302 2.014   0.70 16.85 ?  140 LEU   A HD12 1 
ATOM   3203 H HD13 A LEU   A 1 140 ? 13.258 -11.244 2.578   0.30 15.58 ?  140 LEU   A HD13 1 
ATOM   3204 H HD13 B LEU   A 1 140 ? 13.196 -10.949 2.216   0.70 16.85 ?  140 LEU   A HD13 1 
ATOM   3205 H HD21 A LEU   A 1 140 ? 10.590 -12.625 2.287   0.30 15.61 ?  140 LEU   A HD21 1 
ATOM   3206 H HD21 B LEU   A 1 140 ? 10.512 -12.365 2.105   0.70 17.38 ?  140 LEU   A HD21 1 
ATOM   3207 H HD22 A LEU   A 1 140 ? 10.765 -11.114 1.828   0.30 15.61 ?  140 LEU   A HD22 1 
ATOM   3208 H HD22 B LEU   A 1 140 ? 10.705 -10.960 1.387   0.70 17.38 ?  140 LEU   A HD22 1 
ATOM   3209 H HD23 A LEU   A 1 140 ? 10.253 -12.204 0.793   0.30 15.61 ?  140 LEU   A HD23 1 
ATOM   3210 H HD23 B LEU   A 1 140 ? 10.222 -12.221 0.549   0.70 17.38 ?  140 LEU   A HD23 1 
ATOM   3211 N N    A ARG   A 1 141 ? 14.056 -13.599 -2.016  0.30 13.01 ?  141 ARG   A N    1 
ATOM   3212 N N    B ARG   A 1 141 ? 14.004 -13.840 -2.111  0.70 13.87 ?  141 ARG   A N    1 
ATOM   3213 C CA   A ARG   A 1 141 ? 14.262 -15.002 -2.370  0.30 14.22 ?  141 ARG   A CA   1 
ATOM   3214 C CA   B ARG   A 1 141 ? 14.290 -15.235 -2.426  0.70 15.20 ?  141 ARG   A CA   1 
ATOM   3215 C C    A ARG   A 1 141 ? 15.745 -15.362 -2.338  0.30 14.04 ?  141 ARG   A C    1 
ATOM   3216 C C    B ARG   A 1 141 ? 15.789 -15.490 -2.438  0.70 14.57 ?  141 ARG   A C    1 
ATOM   3217 O O    A ARG   A 1 141 ? 16.154 -16.329 -1.683  0.30 14.17 ?  141 ARG   A O    1 
ATOM   3218 O O    B ARG   A 1 141 ? 16.260 -16.495 -1.891  0.70 14.84 ?  141 ARG   A O    1 
ATOM   3219 C CB   A ARG   A 1 141 ? 13.674 -15.248 -3.763  0.30 15.33 ?  141 ARG   A CB   1 
ATOM   3220 C CB   B ARG   A 1 141 ? 13.687 -15.585 -3.785  0.70 17.02 ?  141 ARG   A CB   1 
ATOM   3221 C CG   A ARG   A 1 141 ? 13.624 -16.702 -4.206  0.30 16.83 ?  141 ARG   A CG   1 
ATOM   3222 C CG   B ARG   A 1 141 ? 13.804 -17.054 -4.167  0.70 19.47 ?  141 ARG   A CG   1 
ATOM   3223 C CD   A ARG   A 1 141 ? 12.580 -17.472 -3.432  0.30 18.15 ?  141 ARG   A CD   1 
ATOM   3224 C CD   B ARG   A 1 141 ? 12.784 -17.889 -3.429  0.70 22.04 ?  141 ARG   A CD   1 
ATOM   3225 N NE   A ARG   A 1 141 ? 13.176 -18.292 -2.386  0.30 18.60 ?  141 ARG   A NE   1 
ATOM   3226 N NE   B ARG   A 1 141 ? 13.381 -18.677 -2.360  0.70 23.89 ?  141 ARG   A NE   1 
ATOM   3227 C CZ   A ARG   A 1 141 ? 12.488 -18.874 -1.413  0.30 19.19 ?  141 ARG   A CZ   1 
ATOM   3228 C CZ   B ARG   A 1 141 ? 12.701 -19.190 -1.344  0.70 24.67 ?  141 ARG   A CZ   1 
ATOM   3229 N NH1  A ARG   A 1 141 ? 11.182 -18.700 -1.291  0.30 19.41 ?  141 ARG   A NH1  1 
ATOM   3230 N NH1  B ARG   A 1 141 ? 11.411 -18.946 -1.181  0.70 25.29 ?  141 ARG   A NH1  1 
ATOM   3231 N NH2  A ARG   A 1 141 ? 13.127 -19.645 -0.537  0.30 19.58 ?  141 ARG   A NH2  1 
ATOM   3232 N NH2  B ARG   A 1 141 ? 13.334 -19.956 -0.461  0.70 25.33 ?  141 ARG   A NH2  1 
ATOM   3233 H H    A ARG   A 1 141 ? 13.708 -13.122 -2.644  0.30 15.61 ?  141 ARG   A H    1 
ATOM   3234 H H    B ARG   A 1 141 ? 13.577 -13.420 -2.726  0.70 16.65 ?  141 ARG   A H    1 
ATOM   3235 H HA   A ARG   A 1 141 ? 13.797 -15.565 -1.737  0.30 17.07 ?  141 ARG   A HA   1 
ATOM   3236 H HA   B ARG   A 1 141 ? 13.891 -15.812 -1.758  0.70 18.24 ?  141 ARG   A HA   1 
ATOM   3237 H HB2  A ARG   A 1 141 ? 12.764 -14.908 -3.778  0.30 18.40 ?  141 ARG   A HB2  1 
ATOM   3238 H HB2  B ARG   A 1 141 ? 12.746 -15.356 -3.780  0.70 20.43 ?  141 ARG   A HB2  1 
ATOM   3239 H HB3  A ARG   A 1 141 ? 14.207 -14.766 -4.413  0.30 18.40 ?  141 ARG   A HB3  1 
ATOM   3240 H HB3  B ARG   A 1 141 ? 14.143 -15.074 -4.470  0.70 20.43 ?  141 ARG   A HB3  1 
ATOM   3241 H HG2  A ARG   A 1 141 ? 13.398 -16.743 -5.149  0.30 20.19 ?  141 ARG   A HG2  1 
ATOM   3242 H HG2  B ARG   A 1 141 ? 13.649 -17.154 -5.119  0.70 23.37 ?  141 ARG   A HG2  1 
ATOM   3243 H HG3  A ARG   A 1 141 ? 14.488 -17.116 -4.051  0.30 20.19 ?  141 ARG   A HG3  1 
ATOM   3244 H HG3  B ARG   A 1 141 ? 14.690 -17.385 -3.938  0.70 23.37 ?  141 ARG   A HG3  1 
ATOM   3245 H HD2  A ARG   A 1 141 ? 11.969 -16.848 -3.009  0.30 21.79 ?  141 ARG   A HD2  1 
ATOM   3246 H HD2  B ARG   A 1 141 ? 12.120 -17.302 -3.030  0.70 26.44 ?  141 ARG   A HD2  1 
ATOM   3247 H HD3  A ARG   A 1 141 ? 12.093 -18.052 -4.041  0.30 21.79 ?  141 ARG   A HD3  1 
ATOM   3248 H HD3  B ARG   A 1 141 ? 12.354 -18.494 -4.055  0.70 26.44 ?  141 ARG   A HD3  1 
ATOM   3249 H HE   A ARG   A 1 141 ? 14.014 -18.474 -2.447  0.30 22.32 ?  141 ARG   A HE   1 
ATOM   3250 H HE   B ARG   A 1 141 ? 14.209 -18.894 -2.438  0.70 28.67 ?  141 ARG   A HE   1 
ATOM   3251 H HH11 A ARG   A 1 141 ? 10.756 -18.210 -1.854  0.30 23.30 ?  141 ARG   A HH11 1 
ATOM   3252 H HH11 B ARG   A 1 141 ? 10.985 -18.460 -1.748  0.70 30.35 ?  141 ARG   A HH11 1 
ATOM   3253 H HH12 A ARG   A 1 141 ? 10.757 -19.085 -0.650  0.30 23.30 ?  141 ARG   A HH12 1 
ATOM   3254 H HH12 B ARG   A 1 141 ? 10.991 -19.286 -0.511  0.70 30.35 ?  141 ARG   A HH12 1 
ATOM   3255 H HH21 A ARG   A 1 141 ? 13.977 -19.763 -0.608  0.30 23.50 ?  141 ARG   A HH21 1 
ATOM   3256 H HH21 B ARG   A 1 141 ? 14.174 -20.115 -0.555  0.70 30.40 ?  141 ARG   A HH21 1 
ATOM   3257 H HH22 A ARG   A 1 141 ? 12.694 -20.022 0.103   0.30 23.50 ?  141 ARG   A HH22 1 
ATOM   3258 H HH22 B ARG   A 1 141 ? 12.907 -20.284 0.209   0.70 30.40 ?  141 ARG   A HH22 1 
ATOM   3259 N N    . VAL   A 1 142 ? 16.563 -14.590 -3.056  1.00 13.91 ?  142 VAL   A N    1 
ATOM   3260 C CA   . VAL   A 1 142 ? 18.013 -14.781 -3.060  1.00 13.77 ?  142 VAL   A CA   1 
ATOM   3261 C C    . VAL   A 1 142 ? 18.563 -14.734 -1.641  1.00 12.88 ?  142 VAL   A C    1 
ATOM   3262 O O    . VAL   A 1 142 ? 19.426 -15.536 -1.270  1.00 13.42 ?  142 VAL   A O    1 
ATOM   3263 C CB   . VAL   A 1 142 ? 18.707 -13.758 -3.985  1.00 14.38 ?  142 VAL   A CB   1 
ATOM   3264 C CG1  . VAL   A 1 142 ? 20.223 -13.898 -3.900  1.00 14.11 ?  142 VAL   A CG1  1 
ATOM   3265 C CG2  . VAL   A 1 142 ? 18.244 -13.919 -5.428  1.00 15.61 ?  142 VAL   A CG2  1 
ATOM   3266 H H    A VAL   A 1 142 ? 16.299 -13.940 -3.554  0.30 16.70 ?  142 VAL   A H    1 
ATOM   3267 H H    B VAL   A 1 142 ? 16.284 -13.887 -3.466  0.70 16.70 ?  142 VAL   A H    1 
ATOM   3268 H HA   . VAL   A 1 142 ? 18.205 -15.657 -3.419  1.00 16.53 ?  142 VAL   A HA   1 
ATOM   3269 H HB   . VAL   A 1 142 ? 18.475 -12.857 -3.698  1.00 17.25 ?  142 VAL   A HB   1 
ATOM   3270 H HG11 . VAL   A 1 142 ? 20.624 -13.405 -4.631  1.00 16.93 ?  142 VAL   A HG11 1 
ATOM   3271 H HG12 . VAL   A 1 142 ? 20.525 -13.531 -3.052  1.00 16.93 ?  142 VAL   A HG12 1 
ATOM   3272 H HG13 . VAL   A 1 142 ? 20.453 -14.833 -3.961  1.00 16.93 ?  142 VAL   A HG13 1 
ATOM   3273 H HG21 . VAL   A 1 142 ? 18.652 -13.222 -5.970  1.00 18.74 ?  142 VAL   A HG21 1 
ATOM   3274 H HG22 . VAL   A 1 142 ? 18.521 -14.790 -5.749  1.00 18.74 ?  142 VAL   A HG22 1 
ATOM   3275 H HG23 . VAL   A 1 142 ? 17.280 -13.841 -5.463  1.00 18.74 ?  142 VAL   A HG23 1 
ATOM   3276 N N    . CYS   A 1 143 ? 18.088 -13.791 -0.827  1.00 12.38 ?  143 CYS   A N    1 
ATOM   3277 C CA   . CYS   A 1 143 ? 18.536 -13.713 0.558   1.00 12.42 ?  143 CYS   A CA   1 
ATOM   3278 C C    . CYS   A 1 143 ? 18.316 -15.037 1.275   1.00 12.81 ?  143 CYS   A C    1 
ATOM   3279 O O    . CYS   A 1 143 ? 19.239 -15.609 1.862   1.00 12.93 ?  143 CYS   A O    1 
ATOM   3280 C CB   . CYS   A 1 143 ? 17.782 -12.598 1.276   1.00 12.81 ?  143 CYS   A CB   1 
ATOM   3281 S SG   . CYS   A 1 143 ? 18.245 -12.395 2.998   1.00 13.23 ?  143 CYS   A SG   1 
ATOM   3282 H H    . CYS   A 1 143 ? 17.518 -13.194 -1.050  1.00 14.85 ?  143 CYS   A H    1 
ATOM   3283 H HA   . CYS   A 1 143 ? 19.485 -13.513 0.583   1.00 14.90 ?  143 CYS   A HA   1 
ATOM   3284 H HB2  . CYS   A 1 143 ? 17.957 -11.761 0.817   1.00 15.37 ?  143 CYS   A HB2  1 
ATOM   3285 H HB3  . CYS   A 1 143 ? 16.836 -12.794 1.244   1.00 15.37 ?  143 CYS   A HB3  1 
ATOM   3286 H HG   . CYS   A 1 143 ? 17.663 -11.447 3.443   1.00 15.87 ?  143 CYS   A HG   1 
ATOM   3287 N N    . VAL   A 1 144 ? 17.089 -15.546 1.230   1.00 13.70 ?  144 VAL   A N    1 
ATOM   3288 C CA   . VAL   A 1 144 ? 16.759 -16.773 1.947   1.00 15.48 ?  144 VAL   A CA   1 
ATOM   3289 C C    . VAL   A 1 144 ? 17.580 -17.950 1.436   1.00 15.32 ?  144 VAL   A C    1 
ATOM   3290 O O    . VAL   A 1 144 ? 17.946 -18.847 2.206   1.00 16.13 ?  144 VAL   A O    1 
ATOM   3291 C CB   . VAL   A 1 144 ? 15.244 -17.027 1.833   1.00 18.67 ?  144 VAL   A CB   1 
ATOM   3292 C CG1  . VAL   A 1 144 ? 14.890 -18.473 2.161   1.00 20.12 ?  144 VAL   A CG1  1 
ATOM   3293 C CG2  . VAL   A 1 144 ? 14.487 -16.035 2.717   1.00 18.86 ?  144 VAL   A CG2  1 
ATOM   3294 H H    . VAL   A 1 144 ? 16.428 -15.201 0.798   1.00 16.44 ?  144 VAL   A H    1 
ATOM   3295 H HA   . VAL   A 1 144 ? 16.961 -16.658 2.884   1.00 18.57 ?  144 VAL   A HA   1 
ATOM   3296 H HB   . VAL   A 1 144 ? 14.966 -16.863 0.917   1.00 22.40 ?  144 VAL   A HB   1 
ATOM   3297 H HG11 . VAL   A 1 144 ? 13.938 -18.530 2.354   1.00 24.14 ?  144 VAL   A HG11 1 
ATOM   3298 H HG12 . VAL   A 1 144 ? 15.100 -19.033 1.397   1.00 24.14 ?  144 VAL   A HG12 1 
ATOM   3299 H HG13 . VAL   A 1 144 ? 15.399 -18.755 2.934   1.00 24.14 ?  144 VAL   A HG13 1 
ATOM   3300 H HG21 . VAL   A 1 144 ? 13.540 -16.264 2.724   1.00 22.63 ?  144 VAL   A HG21 1 
ATOM   3301 H HG22 . VAL   A 1 144 ? 14.837 -16.077 3.620   1.00 22.63 ?  144 VAL   A HG22 1 
ATOM   3302 H HG23 . VAL   A 1 144 ? 14.601 -15.137 2.361   1.00 22.63 ?  144 VAL   A HG23 1 
ATOM   3303 N N    . ASP   A 1 145 ? 17.837 -17.993 0.133   1.00 15.47 ?  145 ASP   A N    1 
ATOM   3304 C CA   . ASP   A 1 145 ? 18.560 -19.100 -0.488  1.00 16.25 ?  145 ASP   A CA   1 
ATOM   3305 C C    . ASP   A 1 145 ? 20.081 -18.948 -0.433  1.00 15.98 ?  145 ASP   A C    1 
ATOM   3306 O O    . ASP   A 1 145 ? 20.794 -19.852 -0.886  1.00 18.50 ?  145 ASP   A O    1 
ATOM   3307 C CB   . ASP   A 1 145 ? 18.129 -19.244 -1.952  1.00 18.11 ?  145 ASP   A CB   1 
ATOM   3308 C CG   . ASP   A 1 145 ? 16.690 -19.712 -2.103  1.00 20.52 ?  145 ASP   A CG   1 
ATOM   3309 O OD1  . ASP   A 1 145 ? 16.108 -20.228 -1.125  1.00 21.13 ?  145 ASP   A OD1  1 
ATOM   3310 O OD2  . ASP   A 1 145 ? 16.140 -19.556 -3.212  1.00 22.03 -1 145 ASP   A OD2  1 
ATOM   3311 H H    . ASP   A 1 145 ? 17.590 -17.384 -0.422  1.00 18.56 ?  145 ASP   A H    1 
ATOM   3312 H HA   . ASP   A 1 145 ? 18.324 -19.920 -0.029  1.00 19.50 ?  145 ASP   A HA   1 
ATOM   3313 H HB2  . ASP   A 1 145 ? 18.213 -18.381 -2.389  1.00 21.73 ?  145 ASP   A HB2  1 
ATOM   3314 H HB3  . ASP   A 1 145 ? 18.701 -19.894 -2.383  1.00 21.73 ?  145 ASP   A HB3  1 
ATOM   3315 N N    . THR   A 1 146 ? 20.595 -17.845 0.102   1.00 13.55 ?  146 THR   A N    1 
ATOM   3316 C CA   . THR   A 1 146 ? 22.033 -17.579 0.126   1.00 12.97 ?  146 THR   A CA   1 
ATOM   3317 C C    . THR   A 1 146 ? 22.584 -17.383 1.526   1.00 12.95 ?  146 THR   A C    1 
ATOM   3318 O O    . THR   A 1 146 ? 23.663 -17.903 1.841   1.00 13.89 ?  146 THR   A O    1 
ATOM   3319 C CB   . THR   A 1 146 ? 22.341 -16.327 -0.715  1.00 12.71 ?  146 THR   A CB   1 
ATOM   3320 O OG1  . THR   A 1 146 ? 21.824 -16.505 -2.036  1.00 13.60 ?  146 THR   A OG1  1 
ATOM   3321 C CG2  . THR   A 1 146 ? 23.840 -16.077 -0.802  1.00 13.02 ?  146 THR   A CG2  1 
ATOM   3322 H H    . THR   A 1 146 ? 20.119 -17.220 0.466   1.00 16.26 ?  146 THR   A H    1 
ATOM   3323 H HA   . THR   A 1 146 ? 22.496 -18.328 -0.269  1.00 15.56 ?  146 THR   A HA   1 
ATOM   3324 H HB   . THR   A 1 146 ? 21.927 -15.549 -0.304  1.00 15.25 ?  146 THR   A HB   1 
ATOM   3325 H HG1  . THR   A 1 146 ? 20.991 -16.597 -2.008  1.00 16.32 ?  146 THR   A HG1  1 
ATOM   3326 H HG21 . THR   A 1 146 ? 24.020 -15.401 -1.472  1.00 15.63 ?  146 THR   A HG21 1 
ATOM   3327 H HG22 . THR   A 1 146 ? 24.180 -15.776 0.053   1.00 15.63 ?  146 THR   A HG22 1 
ATOM   3328 H HG23 . THR   A 1 146 ? 24.294 -16.898 -1.054  1.00 15.63 ?  146 THR   A HG23 1 
ATOM   3329 N N    . VAL   A 1 147 ? 21.892 -16.617 2.362   1.00 12.60 ?  147 VAL   A N    1 
ATOM   3330 C CA   . VAL   A 1 147 ? 22.371 -16.322 3.702   1.00 12.70 ?  147 VAL   A CA   1 
ATOM   3331 C C    . VAL   A 1 147 ? 22.055 -17.494 4.617   1.00 13.13 ?  147 VAL   A C    1 
ATOM   3332 O O    . VAL   A 1 147 ? 20.917 -17.981 4.660   1.00 13.98 ?  147 VAL   A O    1 
ATOM   3333 C CB   . VAL   A 1 147 ? 21.746 -15.019 4.222   1.00 12.84 ?  147 VAL   A CB   1 
ATOM   3334 C CG1  . VAL   A 1 147 ? 22.274 -14.698 5.593   1.00 13.62 ?  147 VAL   A CG1  1 
ATOM   3335 C CG2  . VAL   A 1 147 ? 22.009 -13.871 3.249   1.00 12.94 ?  147 VAL   A CG2  1 
ATOM   3336 H H    . VAL   A 1 147 ? 21.129 -16.258 2.179   1.00 15.12 ?  147 VAL   A H    1 
ATOM   3337 H HA   . VAL   A 1 147 ? 23.333 -16.204 3.676   1.00 15.24 ?  147 VAL   A HA   1 
ATOM   3338 H HB   . VAL   A 1 147 ? 20.786 -15.133 4.292   1.00 15.41 ?  147 VAL   A HB   1 
ATOM   3339 H HG11 . VAL   A 1 147 ? 22.019 -13.794 5.826   1.00 16.34 ?  147 VAL   A HG11 1 
ATOM   3340 H HG12 . VAL   A 1 147 ? 21.891 -15.323 6.232   1.00 16.34 ?  147 VAL   A HG12 1 
ATOM   3341 H HG13 . VAL   A 1 147 ? 23.239 -14.782 5.586   1.00 16.34 ?  147 VAL   A HG13 1 
ATOM   3342 H HG21 . VAL   A 1 147 ? 21.682 -13.045 3.638   1.00 15.53 ?  147 VAL   A HG21 1 
ATOM   3343 H HG22 . VAL   A 1 147 ? 22.964 -13.807 3.089   1.00 15.53 ?  147 VAL   A HG22 1 
ATOM   3344 H HG23 . VAL   A 1 147 ? 21.545 -14.050 2.416   1.00 15.53 ?  147 VAL   A HG23 1 
ATOM   3345 N N    . ARG   A 1 148 ? 23.074 -17.947 5.347   1.00 13.15 ?  148 ARG   A N    1 
ATOM   3346 C CA   . ARG   A 1 148 ? 22.950 -19.027 6.313   1.00 13.15 ?  148 ARG   A CA   1 
ATOM   3347 C C    . ARG   A 1 148 ? 23.079 -18.560 7.751   1.00 13.52 ?  148 ARG   A C    1 
ATOM   3348 O O    . ARG   A 1 148 ? 22.674 -19.297 8.663   1.00 15.50 ?  148 ARG   A O    1 
ATOM   3349 C CB   . ARG   A 1 148 ? 23.997 -20.118 6.031   1.00 14.22 ?  148 ARG   A CB   1 
ATOM   3350 C CG   . ARG   A 1 148 ? 23.842 -20.759 4.656   1.00 15.30 ?  148 ARG   A CG   1 
ATOM   3351 C CD   . ARG   A 1 148 ? 24.928 -21.791 4.367   1.00 16.02 ?  148 ARG   A CD   1 
ATOM   3352 N NE   . ARG   A 1 148 ? 26.264 -21.205 4.388   1.00 15.96 ?  148 ARG   A NE   1 
ATOM   3353 C CZ   . ARG   A 1 148 ? 26.763 -20.455 3.415   1.00 15.25 ?  148 ARG   A CZ   1 
ATOM   3354 N NH1  . ARG   A 1 148 ? 26.080 -20.219 2.307   1.00 15.49 ?  148 ARG   A NH1  1 
ATOM   3355 N NH2  . ARG   A 1 148 ? 27.981 -19.929 3.555   1.00 15.82 ?  148 ARG   A NH2  1 
ATOM   3356 H H    . ARG   A 1 148 ? 23.882 -17.636 5.283   1.00 15.77 ?  148 ARG   A H    1 
ATOM   3357 H HA   . ARG   A 1 148 ? 22.077 -19.423 6.219   1.00 15.78 ?  148 ARG   A HA   1 
ATOM   3358 H HB2  . ARG   A 1 148 ? 24.881 -19.737 6.083   1.00 17.06 ?  148 ARG   A HB2  1 
ATOM   3359 H HB3  . ARG   A 1 148 ? 23.897 -20.824 6.692   1.00 17.06 ?  148 ARG   A HB3  1 
ATOM   3360 H HG2  . ARG   A 1 148 ? 22.979 -21.198 4.606   1.00 18.36 ?  148 ARG   A HG2  1 
ATOM   3361 H HG3  . ARG   A 1 148 ? 23.898 -20.063 3.980   1.00 18.36 ?  148 ARG   A HG3  1 
ATOM   3362 H HD2  . ARG   A 1 148 ? 24.892 -22.487 5.044   1.00 19.23 ?  148 ARG   A HD2  1 
ATOM   3363 H HD3  . ARG   A 1 148 ? 24.775 -22.177 3.489   1.00 19.23 ?  148 ARG   A HD3  1 
ATOM   3364 H HE   . ARG   A 1 148 ? 26.757 -21.360 5.072   1.00 19.15 ?  148 ARG   A HE   1 
ATOM   3365 H HH11 . ARG   A 1 148 ? 25.292 -20.546 2.206   1.00 18.59 ?  148 ARG   A HH11 1 
ATOM   3366 H HH12 . ARG   A 1 148 ? 26.423 -19.728 1.690   1.00 18.59 ?  148 ARG   A HH12 1 
ATOM   3367 H HH21 . ARG   A 1 148 ? 28.432 -20.080 4.269   1.00 18.98 ?  148 ARG   A HH21 1 
ATOM   3368 H HH22 . ARG   A 1 148 ? 28.313 -19.445 2.927   1.00 18.98 ?  148 ARG   A HH22 1 
ATOM   3369 N N    . THR   A 1 149 ? 23.619 -17.364 7.970   1.00 13.55 ?  149 THR   A N    1 
ATOM   3370 C CA   . THR   A 1 149 ? 23.694 -16.769 9.288   1.00 13.73 ?  149 THR   A CA   1 
ATOM   3371 C C    . THR   A 1 149 ? 22.369 -16.070 9.586   1.00 13.11 ?  149 THR   A C    1 
ATOM   3372 O O    . THR   A 1 149 ? 21.446 -16.057 8.764   1.00 13.83 ?  149 THR   A O    1 
ATOM   3373 C CB   . THR   A 1 149 ? 24.891 -15.828 9.340   1.00 13.67 ?  149 THR   A CB   1 
ATOM   3374 O OG1  . THR   A 1 149 ? 24.768 -14.901 8.257   1.00 13.46 ?  149 THR   A OG1  1 
ATOM   3375 C CG2  . THR   A 1 149 ? 26.201 -16.619 9.210   1.00 14.06 ?  149 THR   A CG2  1 
ATOM   3376 H H    . THR   A 1 149 ? 23.967 -16.866 7.355   1.00 16.26 ?  149 THR   A H    1 
ATOM   3377 H HA   . THR   A 1 149 ? 23.827 -17.470 9.948   1.00 16.48 ?  149 THR   A HA   1 
ATOM   3378 H HB   . THR   A 1 149 ? 24.892 -15.354 10.186  1.00 16.41 ?  149 THR   A HB   1 
ATOM   3379 H HG1  . THR   A 1 149 ? 25.412 -14.369 8.262   1.00 16.15 ?  149 THR   A HG1  1 
ATOM   3380 H HG21 . THR   A 1 149 ? 26.961 -16.015 9.267   1.00 16.87 ?  149 THR   A HG21 1 
ATOM   3381 H HG22 . THR   A 1 149 ? 26.273 -17.277 9.920   1.00 16.87 ?  149 THR   A HG22 1 
ATOM   3382 H HG23 . THR   A 1 149 ? 26.234 -17.079 8.354   1.00 16.87 ?  149 THR   A HG23 1 
ATOM   3383 N N    . ASN   A 1 150 ? 22.234 -15.537 10.795  1.00 13.43 ?  150 ASN   A N    1 
ATOM   3384 C CA   . ASN   A 1 150 ? 20.948 -15.027 11.259  1.00 14.15 ?  150 ASN   A CA   1 
ATOM   3385 C C    . ASN   A 1 150 ? 20.778 -13.586 10.803  1.00 13.62 ?  150 ASN   A C    1 
ATOM   3386 O O    . ASN   A 1 150 ? 21.542 -12.702 11.213  1.00 14.86 ?  150 ASN   A O    1 
ATOM   3387 C CB   . ASN   A 1 150 ? 20.860 -15.130 12.777  1.00 16.56 ?  150 ASN   A CB   1 
ATOM   3388 C CG   . ASN   A 1 150 ? 20.743 -16.556 13.248  1.00 20.10 ?  150 ASN   A CG   1 
ATOM   3389 O OD1  . ASN   A 1 150 ? 20.165 -17.398 12.558  1.00 21.77 ?  150 ASN   A OD1  1 
ATOM   3390 N ND2  . ASN   A 1 150 ? 21.301 -16.846 14.419  1.00 22.24 ?  150 ASN   A ND2  1 
ATOM   3391 H H    . ASN   A 1 150 ? 22.868 -15.468 11.372  1.00 16.12 ?  150 ASN   A H    1 
ATOM   3392 H HA   . ASN   A 1 150 ? 20.230 -15.564 10.878  1.00 16.98 ?  150 ASN   A HA   1 
ATOM   3393 H HB2  . ASN   A 1 150 ? 21.660 -14.750 13.170  1.00 19.87 ?  150 ASN   A HB2  1 
ATOM   3394 H HB3  . ASN   A 1 150 ? 20.075 -14.647 13.085  1.00 19.87 ?  150 ASN   A HB3  1 
ATOM   3395 H HD21 . ASN   A 1 150 ? 21.260 -17.648 14.735  1.00 26.68 ?  150 ASN   A HD21 1 
ATOM   3396 H HD22 . ASN   A 1 150 ? 21.698 -16.230 14.873  1.00 26.68 ?  150 ASN   A HD22 1 
ATOM   3397 N N    . VAL   A 1 151 ? 19.786 -13.352 9.949   1.00 13.33 ?  151 VAL   A N    1 
ATOM   3398 C CA   . VAL   A 1 151 ? 19.575 -12.039 9.360   1.00 13.30 ?  151 VAL   A CA   1 
ATOM   3399 C C    . VAL   A 1 151 ? 18.187 -11.529 9.712   1.00 13.18 ?  151 VAL   A C    1 
ATOM   3400 O O    . VAL   A 1 151 ? 17.185 -12.238 9.542   1.00 14.46 ?  151 VAL   A O    1 
ATOM   3401 C CB   . VAL   A 1 151 ? 19.880 -12.008 7.846   1.00 14.71 ?  151 VAL   A CB   1 
ATOM   3402 C CG1  . VAL   A 1 151 ? 19.078 -13.027 7.076   1.00 15.70 ?  151 VAL   A CG1  1 
ATOM   3403 C CG2  . VAL   A 1 151 ? 19.669 -10.599 7.283   1.00 14.97 ?  151 VAL   A CG2  1 
ATOM   3404 H H    . VAL   A 1 151 ? 19.221 -13.944 9.685   1.00 15.99 ?  151 VAL   A H    1 
ATOM   3405 H HA   . VAL   A 1 151 ? 20.212 -11.428 9.769   1.00 15.96 ?  151 VAL   A HA   1 
ATOM   3406 H HB   . VAL   A 1 151 ? 20.817 -12.220 7.714   1.00 17.65 ?  151 VAL   A HB   1 
ATOM   3407 H HG11 . VAL   A 1 151 ? 19.284 -12.956 6.130   1.00 18.84 ?  151 VAL   A HG11 1 
ATOM   3408 H HG12 . VAL   A 1 151 ? 19.312 -13.919 7.393   1.00 18.84 ?  151 VAL   A HG12 1 
ATOM   3409 H HG13 . VAL   A 1 151 ? 18.131 -12.870 7.220   1.00 18.84 ?  151 VAL   A HG13 1 
ATOM   3410 H HG21 . VAL   A 1 151 ? 20.002 -10.566 6.373   1.00 17.96 ?  151 VAL   A HG21 1 
ATOM   3411 H HG22 . VAL   A 1 151 ? 18.717 -10.393 7.290   1.00 17.96 ?  151 VAL   A HG22 1 
ATOM   3412 H HG23 . VAL   A 1 151 ? 20.146 -9.961  7.834   1.00 17.96 ?  151 VAL   A HG23 1 
ATOM   3413 N N    . TYR   A 1 152 ? 18.160 -10.296 10.223  1.00 12.93 ?  152 TYR   A N    1 
ATOM   3414 C CA   . TYR   A 1 152 ? 16.954 -9.567  10.587  1.00 12.72 ?  152 TYR   A CA   1 
ATOM   3415 C C    . TYR   A 1 152 ? 16.780 -8.469  9.555   1.00 12.11 ?  152 TYR   A C    1 
ATOM   3416 O O    . TYR   A 1 152 ? 17.539 -7.495  9.540   1.00 12.40 ?  152 TYR   A O    1 
ATOM   3417 C CB   . TYR   A 1 152 ? 17.102 -9.015  12.002  1.00 13.58 ?  152 TYR   A CB   1 
ATOM   3418 C CG   . TYR   A 1 152 ? 17.061 -10.130 13.007  1.00 14.41 ?  152 TYR   A CG   1 
ATOM   3419 C CD1  . TYR   A 1 152 ? 18.196 -10.871 13.305  1.00 15.72 ?  152 TYR   A CD1  1 
ATOM   3420 C CD2  . TYR   A 1 152 ? 15.873 -10.484 13.624  1.00 15.09 ?  152 TYR   A CD2  1 
ATOM   3421 C CE1  . TYR   A 1 152 ? 18.159 -11.917 14.203  1.00 17.46 ?  152 TYR   A CE1  1 
ATOM   3422 C CE2  . TYR   A 1 152 ? 15.820 -11.537 14.528  1.00 16.72 ?  152 TYR   A CE2  1 
ATOM   3423 C CZ   . TYR   A 1 152 ? 16.969 -12.250 14.815  1.00 17.50 ?  152 TYR   A CZ   1 
ATOM   3424 O OH   . TYR   A 1 152 ? 16.932 -13.301 15.709  1.00 19.44 ?  152 TYR   A OH   1 
ATOM   3425 H H    . TYR   A 1 152 ? 18.879 -9.826  10.359  1.00 15.52 ?  152 TYR   A H    1 
ATOM   3426 H HA   . TYR   A 1 152 ? 16.193 -10.162 10.556  1.00 15.26 ?  152 TYR   A HA   1 
ATOM   3427 H HB2  . TYR   A 1 152 ? 17.954 -8.567  12.087  1.00 16.29 ?  152 TYR   A HB2  1 
ATOM   3428 H HB3  . TYR   A 1 152 ? 16.377 -8.404  12.192  1.00 16.29 ?  152 TYR   A HB3  1 
ATOM   3429 H HD1  . TYR   A 1 152 ? 18.999 -10.648 12.891  1.00 18.86 ?  152 TYR   A HD1  1 
ATOM   3430 H HD2  . TYR   A 1 152 ? 15.094 -10.008 13.428  1.00 18.11 ?  152 TYR   A HD2  1 
ATOM   3431 H HE1  . TYR   A 1 152 ? 18.933 -12.392 14.393  1.00 20.95 ?  152 TYR   A HE1  1 
ATOM   3432 H HE2  . TYR   A 1 152 ? 15.016 -11.757 14.939  1.00 20.07 ?  152 TYR   A HE2  1 
ATOM   3433 H HH   . TYR   A 1 152 ? 16.151 -13.384 16.007  1.00 23.33 ?  152 TYR   A HH   1 
ATOM   3434 N N    . LEU   A 1 153 ? 15.806 -8.656  8.671   1.00 12.23 ?  153 LEU   A N    1 
ATOM   3435 C CA   . LEU   A 1 153 ? 15.537 -7.727  7.585   1.00 12.40 ?  153 LEU   A CA   1 
ATOM   3436 C C    . LEU   A 1 153 ? 14.529 -6.675  8.017   1.00 12.60 ?  153 LEU   A C    1 
ATOM   3437 O O    . LEU   A 1 153 ? 13.431 -7.004  8.481   1.00 13.67 ?  153 LEU   A O    1 
ATOM   3438 C CB   . LEU   A 1 153 ? 14.975 -8.472  6.374   1.00 12.57 ?  153 LEU   A CB   1 
ATOM   3439 C CG   . LEU   A 1 153 ? 15.910 -9.468  5.687   1.00 12.82 ?  153 LEU   A CG   1 
ATOM   3440 C CD1  . LEU   A 1 153 ? 15.127 -10.317 4.702   1.00 13.27 ?  153 LEU   A CD1  1 
ATOM   3441 C CD2  . LEU   A 1 153 ? 17.055 -8.758  4.981   1.00 13.58 ?  153 LEU   A CD2  1 
ATOM   3442 H H    . LEU   A 1 153 ? 15.274 -9.338  8.685   1.00 14.68 ?  153 LEU   A H    1 
ATOM   3443 H HA   . LEU   A 1 153 ? 16.360 -7.295  7.336   1.00 14.88 ?  153 LEU   A HA   1 
ATOM   3444 H HB2  . LEU   A 1 153 ? 14.189 -8.957  6.662   1.00 15.08 ?  153 LEU   A HB2  1 
ATOM   3445 H HB3  . LEU   A 1 153 ? 14.721 -7.807  5.715   1.00 15.08 ?  153 LEU   A HB3  1 
ATOM   3446 H HG   . LEU   A 1 153 ? 16.292 -10.057 6.359   1.00 15.39 ?  153 LEU   A HG   1 
ATOM   3447 H HD11 . LEU   A 1 153 ? 15.698 -11.026 4.377   1.00 15.92 ?  153 LEU   A HD11 1 
ATOM   3448 H HD12 . LEU   A 1 153 ? 14.357 -10.689 5.157   1.00 15.92 ?  153 LEU   A HD12 1 
ATOM   3449 H HD13 . LEU   A 1 153 ? 14.840 -9.753  3.968   1.00 15.92 ?  153 LEU   A HD13 1 
ATOM   3450 H HD21 . LEU   A 1 153 ? 17.607 -9.425  4.546   1.00 16.29 ?  153 LEU   A HD21 1 
ATOM   3451 H HD22 . LEU   A 1 153 ? 16.683 -8.152  4.326   1.00 16.29 ?  153 LEU   A HD22 1 
ATOM   3452 H HD23 . LEU   A 1 153 ? 17.572 -8.272  5.638   1.00 16.29 ?  153 LEU   A HD23 1 
ATOM   3453 N N    A ALA   A 1 154 ? 14.900 -5.413  7.827   0.30 12.39 ?  154 ALA   A N    1 
ATOM   3454 N N    B ALA   A 1 154 ? 14.905 -5.411  7.871   0.70 12.30 ?  154 ALA   A N    1 
ATOM   3455 C CA   A ALA   A 1 154 ? 14.004 -4.282  8.024   0.30 12.59 ?  154 ALA   A CA   1 
ATOM   3456 C CA   B ALA   A 1 154 ? 14.026 -4.282  8.142   0.70 12.47 ?  154 ALA   A CA   1 
ATOM   3457 C C    A ALA   A 1 154 ? 13.537 -3.794  6.659   0.30 12.70 ?  154 ALA   A C    1 
ATOM   3458 C C    B ALA   A 1 154 ? 13.635 -3.679  6.802   0.70 12.13 ?  154 ALA   A C    1 
ATOM   3459 O O    A ALA   A 1 154 ? 14.361 -3.457  5.799   0.30 13.32 ?  154 ALA   A O    1 
ATOM   3460 O O    B ALA   A 1 154 ? 14.505 -3.225  6.048   0.70 12.45 ?  154 ALA   A O    1 
ATOM   3461 C CB   A ALA   A 1 154 ? 14.709 -3.151  8.772   0.30 13.14 ?  154 ALA   A CB   1 
ATOM   3462 C CB   B ALA   A 1 154 ? 14.732 -3.235  9.006   0.70 13.30 ?  154 ALA   A CB   1 
ATOM   3463 H H    A ALA   A 1 154 ? 15.690 -5.182  7.577   0.30 14.87 ?  154 ALA   A H    1 
ATOM   3464 H H    B ALA   A 1 154 ? 15.688 -5.171  7.606   0.70 14.76 ?  154 ALA   A H    1 
ATOM   3465 H HA   A ALA   A 1 154 ? 13.232 -4.561  8.537   0.30 15.11 ?  154 ALA   A HA   1 
ATOM   3466 H HA   B ALA   A 1 154 ? 13.228 -4.581  8.610   0.70 14.96 ?  154 ALA   A HA   1 
ATOM   3467 H HB1  A ALA   A 1 154 ? 14.088 -2.412  8.883   0.30 15.76 ?  154 ALA   A HB1  1 
ATOM   3468 H HB1  B ALA   A 1 154 ? 14.126 -2.494  9.172   0.70 15.96 ?  154 ALA   A HB1  1 
ATOM   3469 H HB2  A ALA   A 1 154 ? 14.995 -3.474  9.640   0.30 15.76 ?  154 ALA   A HB2  1 
ATOM   3470 H HB2  B ALA   A 1 154 ? 15.000 -3.635  9.849   0.70 15.96 ?  154 ALA   A HB2  1 
ATOM   3471 H HB3  A ALA   A 1 154 ? 15.478 -2.859  8.257   0.30 15.76 ?  154 ALA   A HB3  1 
ATOM   3472 H HB3  B ALA   A 1 154 ? 15.520 -2.912  8.533   0.70 15.96 ?  154 ALA   A HB3  1 
ATOM   3473 N N    A VAL   A 1 155 ? 12.222 -3.770  6.466   0.30 13.06 ?  155 VAL   A N    1 
ATOM   3474 N N    B VAL   A 1 155 ? 12.336 -3.673  6.514   0.70 12.35 ?  155 VAL   A N    1 
ATOM   3475 C CA   A VAL   A 1 155 ? 11.592 -3.223  5.272   0.30 13.45 ?  155 VAL   A CA   1 
ATOM   3476 C CA   B VAL   A 1 155 ? 11.786 -3.118  5.284   0.70 12.64 ?  155 VAL   A CA   1 
ATOM   3477 C C    A VAL   A 1 155 ? 10.859 -1.955  5.688   0.30 13.45 ?  155 VAL   A C    1 
ATOM   3478 C C    B VAL   A 1 155 ? 10.864 -1.978  5.684   0.70 13.23 ?  155 VAL   A C    1 
ATOM   3479 O O    A VAL   A 1 155 ? 10.018 -1.987  6.594   0.30 12.89 ?  155 VAL   A O    1 
ATOM   3480 O O    B VAL   A 1 155 ? 9.780  -2.215  6.222   0.70 13.69 ?  155 VAL   A O    1 
ATOM   3481 C CB   A VAL   A 1 155 ? 10.635 -4.237  4.629   0.30 14.06 ?  155 VAL   A CB   1 
ATOM   3482 C CB   B VAL   A 1 155 ? 11.029 -4.171  4.466   0.70 12.61 ?  155 VAL   A CB   1 
ATOM   3483 C CG1  A VAL   A 1 155 ? 9.982  -3.642  3.392   0.30 14.03 ?  155 VAL   A CG1  1 
ATOM   3484 C CG1  B VAL   A 1 155 ? 10.372 -3.521  3.257   0.70 13.14 ?  155 VAL   A CG1  1 
ATOM   3485 C CG2  A VAL   A 1 155 ? 11.380 -5.517  4.285   0.30 14.10 ?  155 VAL   A CG2  1 
ATOM   3486 C CG2  B VAL   A 1 155 ? 11.964 -5.295  4.057   0.70 12.69 ?  155 VAL   A CG2  1 
ATOM   3487 H H    A VAL   A 1 155 ? 11.659 -4.080  7.038   0.30 15.67 ?  155 VAL   A H    1 
ATOM   3488 H H    B VAL   A 1 155 ? 11.735 -3.999  7.045   0.70 14.82 ?  155 VAL   A H    1 
ATOM   3489 H HA   A VAL   A 1 155 ? 12.272 -2.984  4.626   0.30 16.14 ?  155 VAL   A HA   1 
ATOM   3490 H HA   B VAL   A 1 155 ? 12.499 -2.757  4.746   0.70 15.17 ?  155 VAL   A HA   1 
ATOM   3491 H HB   A VAL   A 1 155 ? 9.934  -4.457  5.264   0.30 16.87 ?  155 VAL   A HB   1 
ATOM   3492 H HB   B VAL   A 1 155 ? 10.321 -4.548  5.019   0.70 15.14 ?  155 VAL   A HB   1 
ATOM   3493 H HG11 A VAL   A 1 155 ? 9.505  -4.341  2.921   0.30 16.84 ?  155 VAL   A HG11 1 
ATOM   3494 H HG11 B VAL   A 1 155 ? 10.107 -4.210  2.633   0.70 15.76 ?  155 VAL   A HG11 1 
ATOM   3495 H HG12 A VAL   A 1 155 ? 9.363  -2.944  3.663   0.30 16.84 ?  155 VAL   A HG12 1 
ATOM   3496 H HG12 B VAL   A 1 155 ? 9.589  -3.018  3.544   0.70 15.76 ?  155 VAL   A HG12 1 
ATOM   3497 H HG13 A VAL   A 1 155 ? 10.671 -3.268  2.821   0.30 16.84 ?  155 VAL   A HG13 1 
ATOM   3498 H HG13 B VAL   A 1 155 ? 11.009 -2.920  2.836   0.70 15.76 ?  155 VAL   A HG13 1 
ATOM   3499 H HG21 A VAL   A 1 155 ? 10.782 -6.107  3.803   0.30 16.92 ?  155 VAL   A HG21 1 
ATOM   3500 H HG21 B VAL   A 1 155 ? 11.468 -5.932  3.521   0.70 15.23 ?  155 VAL   A HG21 1 
ATOM   3501 H HG22 A VAL   A 1 155 ? 12.145 -5.295  3.731   0.30 16.92 ?  155 VAL   A HG22 1 
ATOM   3502 H HG22 B VAL   A 1 155 ? 12.694 -4.921  3.546   0.70 15.23 ?  155 VAL   A HG22 1 
ATOM   3503 H HG23 A VAL   A 1 155 ? 11.677 -5.941  5.105   0.30 16.92 ?  155 VAL   A HG23 1 
ATOM   3504 H HG23 B VAL   A 1 155 ? 12.301 -5.727  4.858   0.70 15.23 ?  155 VAL   A HG23 1 
ATOM   3505 N N    A PHE   A 1 156 ? 11.177 -0.841  5.028   0.30 14.28 ?  156 PHE   A N    1 
ATOM   3506 N N    B PHE   A 1 156 ? 11.286 -0.742  5.414   0.70 13.64 ?  156 PHE   A N    1 
ATOM   3507 C CA   A PHE   A 1 156 ? 10.663 0.464   5.440   0.30 15.72 ?  156 PHE   A CA   1 
ATOM   3508 C CA   B PHE   A 1 156 ? 10.570 0.432   5.916   0.70 14.98 ?  156 PHE   A CA   1 
ATOM   3509 C C    A PHE   A 1 156 ? 9.224  0.685   4.983   0.30 15.85 ?  156 PHE   A C    1 
ATOM   3510 C C    B PHE   A 1 156 ? 9.259  0.660   5.164   0.70 15.10 ?  156 PHE   A C    1 
ATOM   3511 O O    A PHE   A 1 156 ? 8.425  1.285   5.711   0.30 15.80 ?  156 PHE   A O    1 
ATOM   3512 O O    B PHE   A 1 156 ? 8.249  1.046   5.767   0.70 16.47 ?  156 PHE   A O    1 
ATOM   3513 C CB   A PHE   A 1 156 ? 11.576 1.568   4.896   0.30 16.87 ?  156 PHE   A CB   1 
ATOM   3514 C CB   B PHE   A 1 156 ? 11.509 1.636   5.798   0.70 16.55 ?  156 PHE   A CB   1 
ATOM   3515 C CG   A PHE   A 1 156 ? 11.102 2.962   5.210   0.30 17.58 ?  156 PHE   A CG   1 
ATOM   3516 C CG   B PHE   A 1 156 ? 11.065 2.866   6.553   0.70 18.28 ?  156 PHE   A CG   1 
ATOM   3517 C CD1  A PHE   A 1 156 ? 11.028 3.402   6.522   0.30 18.00 ?  156 PHE   A CD1  1 
ATOM   3518 C CD1  B PHE   A 1 156 ? 9.997  2.852   7.443   0.70 19.30 ?  156 PHE   A CD1  1 
ATOM   3519 C CD2  A PHE   A 1 156 ? 10.744 3.837   4.193   0.30 18.09 ?  156 PHE   A CD2  1 
ATOM   3520 C CD2  B PHE   A 1 156 ? 11.747 4.055   6.365   0.70 19.30 ?  156 PHE   A CD2  1 
ATOM   3521 C CE1  A PHE   A 1 156 ? 10.594 4.681   6.818   0.30 18.25 ?  156 PHE   A CE1  1 
ATOM   3522 C CE1  B PHE   A 1 156 ? 9.624  4.011   8.119   0.70 19.97 ?  156 PHE   A CE1  1 
ATOM   3523 C CE2  A PHE   A 1 156 ? 10.311 5.120   4.484   0.30 18.52 ?  156 PHE   A CE2  1 
ATOM   3524 C CE2  B PHE   A 1 156 ? 11.378 5.207   7.032   0.70 20.30 ?  156 PHE   A CE2  1 
ATOM   3525 C CZ   A PHE   A 1 156 ? 10.240 5.542   5.799   0.30 18.59 ?  156 PHE   A CZ   1 
ATOM   3526 C CZ   B PHE   A 1 156 ? 10.322 5.182   7.912   0.70 20.28 ?  156 PHE   A CZ   1 
ATOM   3527 H H    A PHE   A 1 156 ? 11.690 -0.818  4.345   0.30 17.13 ?  156 PHE   A H    1 
ATOM   3528 H H    B PHE   A 1 156 ? 11.990 -0.557  4.961   0.70 16.37 ?  156 PHE   A H    1 
ATOM   3529 H HA   A PHE   A 1 156 ? 10.682 0.518   6.410   0.30 18.86 ?  156 PHE   A HA   1 
ATOM   3530 H HA   B PHE   A 1 156 ? 10.367 0.297   6.854   0.70 17.98 ?  156 PHE   A HA   1 
ATOM   3531 H HB2  A PHE   A 1 156 ? 12.460 1.462   5.282   0.30 20.24 ?  156 PHE   A HB2  1 
ATOM   3532 H HB2  B PHE   A 1 156 ? 12.375 1.391   6.149   0.70 19.86 ?  156 PHE   A HB2  1 
ATOM   3533 H HB3  A PHE   A 1 156 ? 11.626 1.483   3.932   0.30 20.24 ?  156 PHE   A HB3  1 
ATOM   3534 H HB3  B PHE   A 1 156 ? 11.597 1.874   4.863   0.70 19.86 ?  156 PHE   A HB3  1 
ATOM   3535 H HD1  A PHE   A 1 156 ? 11.266 2.825   7.213   0.30 21.60 ?  156 PHE   A HD1  1 
ATOM   3536 H HD1  B PHE   A 1 156 ? 9.527  2.062   7.586   0.70 23.16 ?  156 PHE   A HD1  1 
ATOM   3537 H HD2  A PHE   A 1 156 ? 10.789 3.558   3.309   0.30 21.71 ?  156 PHE   A HD2  1 
ATOM   3538 H HD2  B PHE   A 1 156 ? 12.460 4.082   5.771   0.70 23.16 ?  156 PHE   A HD2  1 
ATOM   3539 H HE1  A PHE   A 1 156 ? 10.548 4.962   7.703   0.30 21.90 ?  156 PHE   A HE1  1 
ATOM   3540 H HE1  B PHE   A 1 156 ? 8.910  3.990   8.713   0.70 23.96 ?  156 PHE   A HE1  1 
ATOM   3541 H HE2  A PHE   A 1 156 ? 10.070 5.696   3.797   0.30 22.22 ?  156 PHE   A HE2  1 
ATOM   3542 H HE2  B PHE   A 1 156 ? 11.847 5.998   6.891   0.70 24.36 ?  156 PHE   A HE2  1 
ATOM   3543 H HZ   A PHE   A 1 156 ? 9.948  6.402   5.998   0.30 22.31 ?  156 PHE   A HZ   1 
ATOM   3544 H HZ   B PHE   A 1 156 ? 10.073 5.958   8.363   0.70 24.34 ?  156 PHE   A HZ   1 
ATOM   3545 N N    A ASP   A 1 157 ? 8.875  0.220   3.789   0.30 16.64 ?  157 ASP   A N    1 
ATOM   3546 N N    B ASP   A 1 157 ? 9.252  0.440   3.854   0.70 13.85 ?  157 ASP   A N    1 
ATOM   3547 C CA   A ASP   A 1 157 ? 7.543  0.437   3.238   0.30 18.21 ?  157 ASP   A CA   1 
ATOM   3548 C CA   B ASP   A 1 157 ? 8.049  0.644   3.057   0.70 13.84 ?  157 ASP   A CA   1 
ATOM   3549 C C    A ASP   A 1 157 ? 6.592  -0.633  3.760   0.30 18.79 ?  157 ASP   A C    1 
ATOM   3550 C C    B ASP   A 1 157 ? 6.978  -0.371  3.452   0.70 14.02 ?  157 ASP   A C    1 
ATOM   3551 O O    A ASP   A 1 157 ? 6.779  -1.824  3.487   0.30 18.79 ?  157 ASP   A O    1 
ATOM   3552 O O    B ASP   A 1 157 ? 7.139  -1.582  3.245   0.70 14.17 ?  157 ASP   A O    1 
ATOM   3553 C CB   A ASP   A 1 157 ? 7.614  0.373   1.716   0.30 19.45 ?  157 ASP   A CB   1 
ATOM   3554 C CB   B ASP   A 1 157 ? 8.388  0.530   1.573   0.70 14.47 ?  157 ASP   A CB   1 
ATOM   3555 C CG   A ASP   A 1 157 ? 6.377  0.933   1.049   0.30 20.66 ?  157 ASP   A CG   1 
ATOM   3556 C CG   B ASP   A 1 157 ? 7.256  0.999   0.686   0.70 15.69 ?  157 ASP   A CG   1 
ATOM   3557 O OD1  A ASP   A 1 157 ? 6.241  2.173   0.996   0.30 21.51 ?  157 ASP   A OD1  1 
ATOM   3558 O OD1  B ASP   A 1 157 ? 6.235  0.290   0.594   0.70 15.78 ?  157 ASP   A OD1  1 
ATOM   3559 O OD2  A ASP   A 1 157 ? 5.539  0.135   0.576   0.30 20.96 -1 157 ASP   A OD2  1 
ATOM   3560 O OD2  B ASP   A 1 157 ? 7.376  2.092   0.096   0.70 17.10 -1 157 ASP   A OD2  1 
ATOM   3561 H H    A ASP   A 1 157 ? 9.402  -0.223  3.278   0.30 19.97 ?  157 ASP   A H    1 
ATOM   3562 H H    B ASP   A 1 157 ? 9.941  0.191   3.403   0.70 16.62 ?  157 ASP   A H    1 
ATOM   3563 H HA   A ASP   A 1 157 ? 7.215  1.309   3.508   0.30 21.86 ?  157 ASP   A HA   1 
ATOM   3564 H HA   B ASP   A 1 157 ? 7.694  1.536   3.225   0.70 16.60 ?  157 ASP   A HA   1 
ATOM   3565 H HB2  A ASP   A 1 157 ? 8.384  0.878   1.421   0.30 23.34 ?  157 ASP   A HB2  1 
ATOM   3566 H HB2  B ASP   A 1 157 ? 9.173  1.067   1.380   0.70 17.37 ?  157 ASP   A HB2  1 
ATOM   3567 H HB3  A ASP   A 1 157 ? 7.704  -0.551  1.451   0.30 23.34 ?  157 ASP   A HB3  1 
ATOM   3568 H HB3  B ASP   A 1 157 ? 8.572  -0.405  1.371   0.70 17.37 ?  157 ASP   A HB3  1 
ATOM   3569 N N    A LYS   A 1 158 ? 5.562  -0.209  4.499   0.30 19.74 ?  158 LYS   A N    1 
ATOM   3570 N N    B LYS   A 1 158 ? 5.875  0.140   4.008   0.70 14.57 ?  158 LYS   A N    1 
ATOM   3571 C CA   A LYS   A 1 158 ? 4.604  -1.164  5.050   0.30 20.66 ?  158 LYS   A CA   1 
ATOM   3572 C CA   B LYS   A 1 158 ? 4.821  -0.728  4.521   0.70 15.81 ?  158 LYS   A CA   1 
ATOM   3573 C C    A LYS   A 1 158 ? 3.877  -1.914  3.941   0.30 20.59 ?  158 LYS   A C    1 
ATOM   3574 C C    B LYS   A 1 158 ? 4.187  -1.539  3.401   0.70 15.08 ?  158 LYS   A C    1 
ATOM   3575 O O    A LYS   A 1 158 ? 3.662  -3.128  4.037   0.30 20.87 ?  158 LYS   A O    1 
ATOM   3576 O O    B LYS   A 1 158 ? 3.945  -2.742  3.549   0.70 15.58 ?  158 LYS   A O    1 
ATOM   3577 C CB   A LYS   A 1 158 ? 3.613  -0.440  5.968   0.30 21.60 ?  158 LYS   A CB   1 
ATOM   3578 C CB   B LYS   A 1 158 ? 3.753  0.108   5.225   0.70 17.56 ?  158 LYS   A CB   1 
ATOM   3579 C CG   A LYS   A 1 158 ? 2.384  -1.257  6.369   0.30 22.61 ?  158 LYS   A CG   1 
ATOM   3580 C CG   B LYS   A 1 158 ? 2.519  -0.699  5.614   0.70 19.39 ?  158 LYS   A CG   1 
ATOM   3581 C CD   A LYS   A 1 158 ? 2.745  -2.483  7.196   0.30 23.34 ?  158 LYS   A CD   1 
ATOM   3582 C CD   B LYS   A 1 158 ? 1.370  0.170   6.071   0.70 21.64 ?  158 LYS   A CD   1 
ATOM   3583 C CE   A LYS   A 1 158 ? 1.493  -3.204  7.679   0.30 23.76 ?  158 LYS   A CE   1 
ATOM   3584 C CE   B LYS   A 1 158 ? 0.226  -0.676  6.613   0.70 22.96 ?  158 LYS   A CE   1 
ATOM   3585 N NZ   A LYS   A 1 158 ? 1.796  -4.512  8.324   0.30 24.03 ?  158 LYS   A NZ   1 
ATOM   3586 N NZ   B LYS   A 1 158 ? -0.307 -1.645  5.612   0.70 23.99 ?  158 LYS   A NZ   1 
ATOM   3587 H H    A LYS   A 1 158 ? 5.395  0.615   4.688   0.30 23.69 ?  158 LYS   A H    1 
ATOM   3588 H H    B LYS   A 1 158 ? 5.714  0.986   4.088   0.70 17.48 ?  158 LYS   A H    1 
ATOM   3589 H HA   A LYS   A 1 158 ? 5.079  -1.813  5.591   0.30 24.79 ?  158 LYS   A HA   1 
ATOM   3590 H HA   B LYS   A 1 158 ? 5.206  -1.338  5.167   0.70 18.97 ?  158 LYS   A HA   1 
ATOM   3591 H HB2  A LYS   A 1 158 ? 4.071  -0.190  6.789   0.30 25.91 ?  158 LYS   A HB2  1 
ATOM   3592 H HB2  B LYS   A 1 158 ? 4.134  0.486   6.036   0.70 21.08 ?  158 LYS   A HB2  1 
ATOM   3593 H HB3  A LYS   A 1 158 ? 3.296  0.359   5.520   0.30 25.91 ?  158 LYS   A HB3  1 
ATOM   3594 H HB3  B LYS   A 1 158 ? 3.472  0.824   4.632   0.70 21.08 ?  158 LYS   A HB3  1 
ATOM   3595 H HG2  A LYS   A 1 158 ? 1.801  -0.700  6.907   0.30 27.14 ?  158 LYS   A HG2  1 
ATOM   3596 H HG2  B LYS   A 1 158 ? 2.207  -1.209  4.851   0.70 23.26 ?  158 LYS   A HG2  1 
ATOM   3597 H HG3  A LYS   A 1 158 ? 1.910  -1.552  5.576   0.30 27.14 ?  158 LYS   A HG3  1 
ATOM   3598 H HG3  B LYS   A 1 158 ? 2.760  -1.297  6.337   0.70 23.26 ?  158 LYS   A HG3  1 
ATOM   3599 H HD2  A LYS   A 1 158 ? 3.263  -3.097  6.654   0.30 28.00 ?  158 LYS   A HD2  1 
ATOM   3600 H HD2  B LYS   A 1 158 ? 1.677  0.761   6.774   0.70 25.96 ?  158 LYS   A HD2  1 
ATOM   3601 H HD3  A LYS   A 1 158 ? 3.256  -2.206  7.974   0.30 28.00 ?  158 LYS   A HD3  1 
ATOM   3602 H HD3  B LYS   A 1 158 ? 1.041  0.686   5.317   0.70 25.96 ?  158 LYS   A HD3  1 
ATOM   3603 H HE2  A LYS   A 1 158 ? 1.039  -2.647  8.331   0.30 28.51 ?  158 LYS   A HE2  1 
ATOM   3604 H HE2  B LYS   A 1 158 ? 0.545  -1.183  7.374   0.70 27.56 ?  158 LYS   A HE2  1 
ATOM   3605 H HE3  A LYS   A 1 158 ? 0.909  -3.368  6.922   0.30 28.51 ?  158 LYS   A HE3  1 
ATOM   3606 H HE3  B LYS   A 1 158 ? -0.498 -0.092  6.881   0.70 27.56 ?  158 LYS   A HE3  1 
ATOM   3607 H HZ1  A LYS   A 1 158 ? 1.042  -4.902  8.591   0.30 28.84 ?  158 LYS   A HZ1  1 
ATOM   3608 H HZ1  B LYS   A 1 158 ? -0.980 -2.107  5.965   0.70 28.79 ?  158 LYS   A HZ1  1 
ATOM   3609 H HZ2  A LYS   A 1 158 ? 2.209  -5.047  7.745   0.30 28.84 ?  158 LYS   A HZ2  1 
ATOM   3610 H HZ2  B LYS   A 1 158 ? -0.599 -1.211  4.893   0.70 28.79 ?  158 LYS   A HZ2  1 
ATOM   3611 H HZ3  A LYS   A 1 158 ? 2.323  -4.387  9.030   0.30 28.84 ?  158 LYS   A HZ3  1 
ATOM   3612 H HZ3  B LYS   A 1 158 ? 0.334  -2.213  5.366   0.70 28.79 ?  158 LYS   A HZ3  1 
ATOM   3613 N N    A ASN   A 1 159 ? 3.482  -1.207  2.880   0.30 20.35 ?  159 ASN   A N    1 
ATOM   3614 N N    B ASN   A 1 159 ? 3.871  -0.890  2.282   0.70 15.42 ?  159 ASN   A N    1 
ATOM   3615 C CA   A ASN   A 1 159 ? 2.814  -1.871  1.765   0.30 19.87 ?  159 ASN   A CA   1 
ATOM   3616 C CA   B ASN   A 1 159 ? 3.238  -1.609  1.184   0.70 15.96 ?  159 ASN   A CA   1 
ATOM   3617 C C    A ASN   A 1 159 ? 3.726  -2.902  1.111   0.30 19.37 ?  159 ASN   A C    1 
ATOM   3618 C C    B ASN   A 1 159 ? 4.132  -2.727  0.664   0.70 15.91 ?  159 ASN   A C    1 
ATOM   3619 O O    A ASN   A 1 159 ? 3.270  -3.982  0.715   0.30 19.53 ?  159 ASN   A O    1 
ATOM   3620 O O    B ASN   A 1 159 ? 3.647  -3.819  0.353   0.70 16.04 ?  159 ASN   A O    1 
ATOM   3621 C CB   A ASN   A 1 159 ? 2.337  -0.837  0.744   0.30 20.05 ?  159 ASN   A CB   1 
ATOM   3622 C CB   B ASN   A 1 159 ? 2.868  -0.641  0.062   0.70 17.60 ?  159 ASN   A CB   1 
ATOM   3623 C CG   A ASN   A 1 159 ? 1.113  -0.075  1.214   0.30 20.32 ?  159 ASN   A CG   1 
ATOM   3624 C CG   B ASN   A 1 159 ? 1.650  0.202   0.398   0.70 19.25 ?  159 ASN   A CG   1 
ATOM   3625 O OD1  A ASN   A 1 159 ? 0.260  -0.624  1.907   0.30 20.28 ?  159 ASN   A OD1  1 
ATOM   3626 O OD1  B ASN   A 1 159 ? 0.790  -0.205  1.183   0.70 20.83 ?  159 ASN   A OD1  1 
ATOM   3627 N ND2  A ASN   A 1 159 ? 1.019  1.194   0.835   0.30 20.22 ?  159 ASN   A ND2  1 
ATOM   3628 N ND2  B ASN   A 1 159 ? 1.567  1.384   -0.201  0.70 19.49 ?  159 ASN   A ND2  1 
ATOM   3629 H H    A ASN   A 1 159 ? 3.583  -0.361  2.792   0.30 24.42 ?  159 ASN   A H    1 
ATOM   3630 H H    B ASN   A 1 159 ? 4.012  -0.059  2.138   0.70 18.51 ?  159 ASN   A H    1 
ATOM   3631 H HA   A ASN   A 1 159 ? 2.032  -2.338  2.105   0.30 23.85 ?  159 ASN   A HA   1 
ATOM   3632 H HA   B ASN   A 1 159 ? 2.421  -2.018  1.505   0.70 19.15 ?  159 ASN   A HA   1 
ATOM   3633 H HB2  A ASN   A 1 159 ? 3.044  -0.198  0.588   0.30 24.06 ?  159 ASN   A HB2  1 
ATOM   3634 H HB2  B ASN   A 1 159 ? 3.618  -0.041  -0.096  0.70 21.12 ?  159 ASN   A HB2  1 
ATOM   3635 H HB3  A ASN   A 1 159 ? 2.107  -1.295  -0.079  0.30 24.06 ?  159 ASN   A HB3  1 
ATOM   3636 H HB3  B ASN   A 1 159 ? 2.676  -1.146  -0.744  0.70 21.12 ?  159 ASN   A HB3  1 
ATOM   3637 H HD21 A ASN   A 1 159 ? 0.342  1.666   1.077   0.30 24.26 ?  159 ASN   A HD21 1 
ATOM   3638 H HD21 B ASN   A 1 159 ? 0.896  1.894   -0.046  0.70 23.38 ?  159 ASN   A HD21 1 
ATOM   3639 H HD22 A ASN   A 1 159 ? 1.637  1.540   0.352   0.30 24.26 ?  159 ASN   A HD22 1 
ATOM   3640 H HD22 B ASN   A 1 159 ? 2.184  1.636   -0.748  0.70 23.38 ?  159 ASN   A HD22 1 
ATOM   3641 N N    A LEU   A 1 160 ? 5.019  -2.595  0.993   0.30 18.89 ?  160 LEU   A N    1 
ATOM   3642 N N    B LEU   A 1 160 ? 5.439  -2.477  0.553   0.70 15.54 ?  160 LEU   A N    1 
ATOM   3643 C CA   A LEU   A 1 160 ? 5.951  -3.582  0.459   0.30 18.48 ?  160 LEU   A CA   1 
ATOM   3644 C CA   B LEU   A 1 160 ? 6.346  -3.526  0.096   0.70 15.81 ?  160 LEU   A CA   1 
ATOM   3645 C C    A LEU   A 1 160 ? 6.156  -4.728  1.441   0.30 18.31 ?  160 LEU   A C    1 
ATOM   3646 C C    B LEU   A 1 160 ? 6.395  -4.677  1.092   0.70 15.71 ?  160 LEU   A C    1 
ATOM   3647 O O    A LEU   A 1 160 ? 6.277  -5.889  1.033   0.30 18.45 ?  160 LEU   A O    1 
ATOM   3648 O O    B LEU   A 1 160 ? 6.330  -5.851  0.704   0.70 16.18 ?  160 LEU   A O    1 
ATOM   3649 C CB   A LEU   A 1 160 ? 7.286  -2.926  0.112   0.30 18.22 ?  160 LEU   A CB   1 
ATOM   3650 C CB   B LEU   A 1 160 ? 7.747  -2.959  -0.144  0.70 16.24 ?  160 LEU   A CB   1 
ATOM   3651 C CG   A LEU   A 1 160 ? 8.374  -3.908  -0.328  0.30 18.26 ?  160 LEU   A CG   1 
ATOM   3652 C CG   B LEU   A 1 160 ? 8.741  -4.037  -0.591  0.70 17.39 ?  160 LEU   A CG   1 
ATOM   3653 C CD1  A LEU   A 1 160 ? 7.913  -4.699  -1.540  0.30 18.35 ?  160 LEU   A CD1  1 
ATOM   3654 C CD1  B LEU   A 1 160 ? 8.252  -4.702  -1.868  0.70 18.34 ?  160 LEU   A CD1  1 
ATOM   3655 C CD2  A LEU   A 1 160 ? 9.678  -3.185  -0.612  0.30 18.14 ?  160 LEU   A CD2  1 
ATOM   3656 C CD2  B LEU   A 1 160 ? 10.137 -3.478  -0.778  0.70 17.88 ?  160 LEU   A CD2  1 
ATOM   3657 H H    A LEU   A 1 160 ? 5.370  -1.840  1.211   0.30 22.67 ?  160 LEU   A H    1 
ATOM   3658 H H    B LEU   A 1 160 ? 5.816  -1.724  0.727   0.70 18.65 ?  160 LEU   A H    1 
ATOM   3659 H HA   A LEU   A 1 160 ? 5.578  -3.951  -0.352  0.30 22.18 ?  160 LEU   A HA   1 
ATOM   3660 H HA   B LEU   A 1 160 ? 6.019  -3.870  -0.749  0.70 18.97 ?  160 LEU   A HA   1 
ATOM   3661 H HB2  A LEU   A 1 160 ? 7.150  -2.277  -0.601  0.30 21.87 ?  160 LEU   A HB2  1 
ATOM   3662 H HB2  B LEU   A 1 160 ? 7.710  -2.281  -0.842  0.70 19.49 ?  160 LEU   A HB2  1 
ATOM   3663 H HB3  A LEU   A 1 160 ? 7.617  -2.483  0.904   0.30 21.87 ?  160 LEU   A HB3  1 
ATOM   3664 H HB3  B LEU   A 1 160 ? 8.083  -2.567  0.679   0.70 19.49 ?  160 LEU   A HB3  1 
ATOM   3665 H HG   A LEU   A 1 160 ? 8.542  -4.536  0.392   0.30 21.92 ?  160 LEU   A HG   1 
ATOM   3666 H HG   B LEU   A 1 160 ? 8.795  -4.724  0.094   0.70 20.87 ?  160 LEU   A HG   1 
ATOM   3667 H HD11 A LEU   A 1 160 ? 8.656  -5.224  -1.871  0.30 22.02 ?  160 LEU   A HD11 1 
ATOM   3668 H HD11 B LEU   A 1 160 ? 8.981  -5.203  -2.259  0.70 22.01 ?  160 LEU   A HD11 1 
ATOM   3669 H HD12 A LEU   A 1 160 ? 7.185  -5.285  -1.280  0.30 22.02 ?  160 LEU   A HD12 1 
ATOM   3670 H HD12 B LEU   A 1 160 ? 7.517  -5.299  -1.654  0.70 22.01 ?  160 LEU   A HD12 1 
ATOM   3671 H HD13 A LEU   A 1 160 ? 7.613  -4.080  -2.224  0.30 22.02 ?  160 LEU   A HD13 1 
ATOM   3672 H HD13 B LEU   A 1 160 ? 7.952  -4.015  -2.483  0.70 22.01 ?  160 LEU   A HD13 1 
ATOM   3673 H HD21 A LEU   A 1 160 ? 10.344 -3.836  -0.883  0.30 21.77 ?  160 LEU   A HD21 1 
ATOM   3674 H HD21 B LEU   A 1 160 ? 10.729 -4.199  -1.049  0.70 21.45 ?  160 LEU   A HD21 1 
ATOM   3675 H HD22 A LEU   A 1 160 ? 9.534  -2.542  -1.322  0.30 21.77 ?  160 LEU   A HD22 1 
ATOM   3676 H HD22 B LEU   A 1 160 ? 10.111 -2.795  -1.463  0.70 21.45 ?  160 LEU   A HD22 1 
ATOM   3677 H HD23 A LEU   A 1 160 ? 9.969  -2.731  0.195   0.30 21.77 ?  160 LEU   A HD23 1 
ATOM   3678 H HD23 B LEU   A 1 160 ? 10.437 -3.101  0.062   0.70 21.45 ?  160 LEU   A HD23 1 
ATOM   3679 N N    A TYR   A 1 161 ? 6.207  -4.422  2.739   0.30 18.14 ?  161 TYR   A N    1 
ATOM   3680 N N    B TYR   A 1 161 ? 6.529  -4.359  2.381   0.70 14.91 ?  161 TYR   A N    1 
ATOM   3681 C CA   A TYR   A 1 161 ? 6.378  -5.470  3.739   0.30 18.13 ?  161 TYR   A CA   1 
ATOM   3682 C CA   B TYR   A 1 161 ? 6.554  -5.402  3.399   0.70 15.37 ?  161 TYR   A CA   1 
ATOM   3683 C C    A TYR   A 1 161 ? 5.245  -6.487  3.665   0.30 18.86 ?  161 TYR   A C    1 
ATOM   3684 C C    B TYR   A 1 161 ? 5.340  -6.309  3.273   0.70 16.01 ?  161 TYR   A C    1 
ATOM   3685 O O    A TYR   A 1 161 ? 5.483  -7.700  3.666   0.30 18.66 ?  161 TYR   A O    1 
ATOM   3686 O O    B TYR   A 1 161 ? 5.461  -7.540  3.265   0.70 15.59 ?  161 TYR   A O    1 
ATOM   3687 C CB   A TYR   A 1 161 ? 6.470  -4.852  5.135   0.30 17.92 ?  161 TYR   A CB   1 
ATOM   3688 C CB   B TYR   A 1 161 ? 6.604  -4.784  4.795   0.70 15.79 ?  161 TYR   A CB   1 
ATOM   3689 C CG   A TYR   A 1 161 ? 6.387  -5.862  6.256   0.30 17.87 ?  161 TYR   A CG   1 
ATOM   3690 C CG   B TYR   A 1 161 ? 6.426  -5.820  5.871   0.70 15.95 ?  161 TYR   A CG   1 
ATOM   3691 C CD1  A TYR   A 1 161 ? 7.518  -6.531  6.700   0.30 17.82 ?  161 TYR   A CD1  1 
ATOM   3692 C CD1  B TYR   A 1 161 ? 7.511  -6.530  6.348   0.70 16.01 ?  161 TYR   A CD1  1 
ATOM   3693 C CD2  A TYR   A 1 161 ? 5.176  -6.142  6.875   0.30 17.83 ?  161 TYR   A CD2  1 
ATOM   3694 C CD2  B TYR   A 1 161 ? 5.171  -6.106  6.400   0.70 16.13 ?  161 TYR   A CD2  1 
ATOM   3695 C CE1  A TYR   A 1 161 ? 7.444  -7.454  7.725   0.30 18.02 ?  161 TYR   A CE1  1 
ATOM   3696 C CE1  B TYR   A 1 161 ? 7.360  -7.492  7.319   0.70 16.05 ?  161 TYR   A CE1  1 
ATOM   3697 C CE2  A TYR   A 1 161 ? 5.093  -7.062  7.900   0.30 18.08 ?  161 TYR   A CE2  1 
ATOM   3698 C CE2  B TYR   A 1 161 ? 5.011  -7.070  7.376   0.70 16.52 ?  161 TYR   A CE2  1 
ATOM   3699 C CZ   A TYR   A 1 161 ? 6.230  -7.717  8.322   0.30 18.37 ?  161 TYR   A CZ   1 
ATOM   3700 C CZ   B TYR   A 1 161 ? 6.112  -7.762  7.834   0.70 16.86 ?  161 TYR   A CZ   1 
ATOM   3701 O OH   A TYR   A 1 161 ? 6.153  -8.635  9.344   0.30 19.10 ?  161 TYR   A OH   1 
ATOM   3702 O OH   B TYR   A 1 161 ? 5.980  -8.728  8.803   0.70 17.59 ?  161 TYR   A OH   1 
ATOM   3703 H H    A TYR   A 1 161 ? 6.139  -3.627  3.062   0.30 21.76 ?  161 TYR   A H    1 
ATOM   3704 H H    B TYR   A 1 161 ? 6.609  -3.556  2.680   0.70 17.89 ?  161 TYR   A H    1 
ATOM   3705 H HA   A TYR   A 1 161 ? 7.207  -5.938  3.566   0.30 21.76 ?  161 TYR   A HA   1 
ATOM   3706 H HA   B TYR   A 1 161 ? 7.352  -5.942  3.279   0.70 18.44 ?  161 TYR   A HA   1 
ATOM   3707 H HB2  A TYR   A 1 161 ? 7.320  -4.389  5.216   0.30 21.50 ?  161 TYR   A HB2  1 
ATOM   3708 H HB2  B TYR   A 1 161 ? 7.470  -4.356  4.925   0.70 18.95 ?  161 TYR   A HB2  1 
ATOM   3709 H HB3  A TYR   A 1 161 ? 5.742  -4.222  5.249   0.30 21.50 ?  161 TYR   A HB3  1 
ATOM   3710 H HB3  B TYR   A 1 161 ? 5.896  -4.129  4.881   0.70 18.95 ?  161 TYR   A HB3  1 
ATOM   3711 H HD1  A TYR   A 1 161 ? 8.340  -6.357  6.299   0.30 21.38 ?  161 TYR   A HD1  1 
ATOM   3712 H HD1  B TYR   A 1 161 ? 8.359  -6.358  6.005   0.70 19.21 ?  161 TYR   A HD1  1 
ATOM   3713 H HD2  A TYR   A 1 161 ? 4.407  -5.702  6.593   0.30 21.40 ?  161 TYR   A HD2  1 
ATOM   3714 H HD2  B TYR   A 1 161 ? 4.428  -5.639  6.095   0.70 19.35 ?  161 TYR   A HD2  1 
ATOM   3715 H HE1  A TYR   A 1 161 ? 8.210  -7.896  8.010   0.30 21.63 ?  161 TYR   A HE1  1 
ATOM   3716 H HE1  B TYR   A 1 161 ? 8.104  -7.960  7.632   0.70 19.26 ?  161 TYR   A HE1  1 
ATOM   3717 H HE2  A TYR   A 1 161 ? 4.272  -7.239  8.302   0.30 21.69 ?  161 TYR   A HE2  1 
ATOM   3718 H HE2  B TYR   A 1 161 ? 4.166  -7.245  7.726   0.70 19.83 ?  161 TYR   A HE2  1 
ATOM   3719 H HH   A TYR   A 1 161 ? 5.358  -8.695  9.608   0.30 22.92 ?  161 TYR   A HH   1 
ATOM   3720 H HH   B TYR   A 1 161 ? 6.727  -9.062  8.983   0.70 21.11 ?  161 TYR   A HH   1 
ATOM   3721 N N    A ASP   A 1 162 ? 4.000  -6.009  3.594   0.30 19.56 ?  162 ASP   A N    1 
ATOM   3722 N N    B ASP   A 1 162 ? 4.152  -5.705  3.191   0.70 17.06 ?  162 ASP   A N    1 
ATOM   3723 C CA   A ASP   A 1 162 ? 2.864  -6.924  3.534   0.30 20.06 ?  162 ASP   A CA   1 
ATOM   3724 C CA   B ASP   A 1 162 ? 2.928  -6.489  3.065   0.70 18.41 ?  162 ASP   A CA   1 
ATOM   3725 C C    A ASP   A 1 162 ? 2.910  -7.781  2.277   0.30 20.26 ?  162 ASP   A C    1 
ATOM   3726 C C    B ASP   A 1 162 ? 2.981  -7.394  1.838   0.70 18.16 ?  162 ASP   A C    1 
ATOM   3727 O O    A ASP   A 1 162 ? 2.552  -8.964  2.310   0.30 20.36 ?  162 ASP   A O    1 
ATOM   3728 O O    B ASP   A 1 162 ? 2.575  -8.562  1.895   0.70 18.35 ?  162 ASP   A O    1 
ATOM   3729 C CB   A ASP   A 1 162 ? 1.550  -6.144  3.604   0.30 20.38 ?  162 ASP   A CB   1 
ATOM   3730 C CB   B ASP   A 1 162 ? 1.717  -5.553  2.987   0.70 20.11 ?  162 ASP   A CB   1 
ATOM   3731 C CG   A ASP   A 1 162 ? 1.268  -5.602  4.985   0.30 20.60 ?  162 ASP   A CG   1 
ATOM   3732 C CG   B ASP   A 1 162 ? 1.418  -4.849  4.305   0.70 21.70 ?  162 ASP   A CG   1 
ATOM   3733 O OD1  A ASP   A 1 162 ? 1.813  -6.154  5.963   0.30 20.93 ?  162 ASP   A OD1  1 
ATOM   3734 O OD1  B ASP   A 1 162 ? 1.924  -5.295  5.355   0.70 22.39 ?  162 ASP   A OD1  1 
ATOM   3735 O OD2  A ASP   A 1 162 ? 0.490  -4.631  5.092   0.30 20.58 -1 162 ASP   A OD2  1 
ATOM   3736 O OD2  B ASP   A 1 162 ? 0.657  -3.852  4.291   0.70 22.79 -1 162 ASP   A OD2  1 
ATOM   3737 H H    A ASP   A 1 162 ? 3.791  -5.176  3.579   0.30 23.47 ?  162 ASP   A H    1 
ATOM   3738 H H    B ASP   A 1 162 ? 4.036  -4.846  3.206   0.70 20.47 ?  162 ASP   A H    1 
ATOM   3739 H HA   A ASP   A 1 162 ? 2.895  -7.519  4.299   0.30 24.07 ?  162 ASP   A HA   1 
ATOM   3740 H HA   B ASP   A 1 162 ? 2.829  -7.044  3.847   0.70 22.09 ?  162 ASP   A HA   1 
ATOM   3741 H HB2  A ASP   A 1 162 ? 1.588  -5.396  2.990   0.30 24.46 ?  162 ASP   A HB2  1 
ATOM   3742 H HB2  B ASP   A 1 162 ? 1.883  -4.870  2.315   0.70 24.13 ?  162 ASP   A HB2  1 
ATOM   3743 H HB3  A ASP   A 1 162 ? 0.815  -6.732  3.369   0.30 24.46 ?  162 ASP   A HB3  1 
ATOM   3744 H HB3  B ASP   A 1 162 ? 0.935  -6.068  2.751   0.70 24.13 ?  162 ASP   A HB3  1 
ATOM   3745 N N    A LYS   A 1 163 ? 3.348  -7.207  1.156   0.30 20.46 ?  163 LYS   A N    1 
ATOM   3746 N N    B LYS   A 1 163 ? 3.496  -6.870  0.720   0.70 18.59 ?  163 LYS   A N    1 
ATOM   3747 C CA   A LYS   A 1 163 ? 3.437  -7.988  -0.073  0.30 20.76 ?  163 LYS   A CA   1 
ATOM   3748 C CA   B LYS   A 1 163 ? 3.569  -7.649  -0.516  0.70 19.88 ?  163 LYS   A CA   1 
ATOM   3749 C C    A LYS   A 1 163 ? 4.563  -9.014  0.011   0.30 19.27 ?  163 LYS   A C    1 
ATOM   3750 C C    B LYS   A 1 163 ? 4.568  -8.799  -0.407  0.70 18.79 ?  163 LYS   A C    1 
ATOM   3751 O O    A LYS   A 1 163 ? 4.408  -10.153 -0.443  0.30 19.26 ?  163 LYS   A O    1 
ATOM   3752 O O    B LYS   A 1 163 ? 4.322  -9.896  -0.922  0.70 18.99 ?  163 LYS   A O    1 
ATOM   3753 C CB   A LYS   A 1 163 ? 3.633  -7.059  -1.270  0.30 22.84 ?  163 LYS   A CB   1 
ATOM   3754 C CB   B LYS   A 1 163 ? 3.947  -6.731  -1.682  0.70 22.85 ?  163 LYS   A CB   1 
ATOM   3755 C CG   A LYS   A 1 163 ? 3.604  -7.768  -2.612  0.30 24.94 ?  163 LYS   A CG   1 
ATOM   3756 C CG   B LYS   A 1 163 ? 4.216  -7.465  -2.989  0.70 26.41 ?  163 LYS   A CG   1 
ATOM   3757 C CD   A LYS   A 1 163 ? 4.041  -6.840  -3.728  0.30 26.85 ?  163 LYS   A CD   1 
ATOM   3758 C CD   B LYS   A 1 163 ? 4.295  -6.504  -4.168  0.70 29.91 ?  163 LYS   A CD   1 
ATOM   3759 C CE   A LYS   A 1 163 ? 3.915  -7.508  -5.086  0.30 28.25 ?  163 LYS   A CE   1 
ATOM   3760 C CE   B LYS   A 1 163 ? 4.460  -7.255  -5.482  0.70 32.49 ?  163 LYS   A CE   1 
ATOM   3761 N NZ   A LYS   A 1 163 ? 4.614  -6.738  -6.149  0.30 29.02 ?  163 LYS   A NZ   1 
ATOM   3762 N NZ   B LYS   A 1 163 ? 4.208  -6.382  -6.662  0.70 33.96 ?  163 LYS   A NZ   1 
ATOM   3763 H H    A LYS   A 1 163 ? 3.598  -6.389  1.086   0.30 24.55 ?  163 LYS   A H    1 
ATOM   3764 H H    B LYS   A 1 163 ? 3.807  -6.061  0.649   0.70 22.30 ?  163 LYS   A H    1 
ATOM   3765 H HA   A LYS   A 1 163 ? 2.602  -8.466  -0.203  0.30 24.91 ?  163 LYS   A HA   1 
ATOM   3766 H HA   B LYS   A 1 163 ? 2.692  -8.014  -0.701  0.70 23.86 ?  163 LYS   A HA   1 
ATOM   3767 H HB2  A LYS   A 1 163 ? 2.922  -6.396  -1.271  0.30 27.41 ?  163 LYS   A HB2  1 
ATOM   3768 H HB2  B LYS   A 1 163 ? 3.220  -6.106  -1.843  0.70 27.43 ?  163 LYS   A HB2  1 
ATOM   3769 H HB3  A LYS   A 1 163 ? 4.491  -6.617  -1.186  0.30 27.41 ?  163 LYS   A HB3  1 
ATOM   3770 H HB3  B LYS   A 1 163 ? 4.751  -6.241  -1.450  0.70 27.43 ?  163 LYS   A HB3  1 
ATOM   3771 H HG2  A LYS   A 1 163 ? 4.211  -8.525  -2.593  0.30 29.93 ?  163 LYS   A HG2  1 
ATOM   3772 H HG2  B LYS   A 1 163 ? 5.064  -7.932  -2.926  0.70 31.70 ?  163 LYS   A HG2  1 
ATOM   3773 H HG3  A LYS   A 1 163 ? 2.700  -8.067  -2.799  0.30 29.93 ?  163 LYS   A HG3  1 
ATOM   3774 H HG3  B LYS   A 1 163 ? 3.498  -8.094  -3.157  0.70 31.70 ?  163 LYS   A HG3  1 
ATOM   3775 H HD2  A LYS   A 1 163 ? 3.477  -6.050  -3.727  0.30 32.22 ?  163 LYS   A HD2  1 
ATOM   3776 H HD2  B LYS   A 1 163 ? 3.477  -5.985  -4.215  0.70 35.89 ?  163 LYS   A HD2  1 
ATOM   3777 H HD3  A LYS   A 1 163 ? 4.969  -6.590  -3.592  0.30 32.22 ?  163 LYS   A HD3  1 
ATOM   3778 H HD3  B LYS   A 1 163 ? 5.059  -5.918  -4.055  0.70 35.89 ?  163 LYS   A HD3  1 
ATOM   3779 H HE2  A LYS   A 1 163 ? 4.282  -8.405  -5.052  0.30 33.90 ?  163 LYS   A HE2  1 
ATOM   3780 H HE2  B LYS   A 1 163 ? 5.367  -7.593  -5.544  0.70 38.99 ?  163 LYS   A HE2  1 
ATOM   3781 H HE3  A LYS   A 1 163 ? 2.980  -7.552  -5.321  0.30 33.90 ?  163 LYS   A HE3  1 
ATOM   3782 H HE3  B LYS   A 1 163 ? 3.828  -7.991  -5.510  0.70 38.99 ?  163 LYS   A HE3  1 
ATOM   3783 H HZ1  A LYS   A 1 163 ? 4.527  -7.154  -6.931  0.30 34.82 ?  163 LYS   A HZ1  1 
ATOM   3784 H HZ1  B LYS   A 1 163 ? 4.312  -6.848  -7.413  0.70 40.75 ?  163 LYS   A HZ1  1 
ATOM   3785 H HZ2  A LYS   A 1 163 ? 4.260  -5.924  -6.213  0.30 34.82 ?  163 LYS   A HZ2  1 
ATOM   3786 H HZ2  B LYS   A 1 163 ? 3.378  -6.063  -6.632  0.70 40.75 ?  163 LYS   A HZ2  1 
ATOM   3787 H HZ3  A LYS   A 1 163 ? 5.479  -6.663  -5.956  0.30 34.82 ?  163 LYS   A HZ3  1 
ATOM   3788 H HZ3  B LYS   A 1 163 ? 4.780  -5.700  -6.663  0.70 40.75 ?  163 LYS   A HZ3  1 
ATOM   3789 N N    A LEU   A 1 164 ? 5.700  -8.631  0.594   0.30 17.66 ?  164 LEU   A N    1 
ATOM   3790 N N    B LEU   A 1 164 ? 5.713  -8.567  0.232   0.70 17.48 ?  164 LEU   A N    1 
ATOM   3791 C CA   A LEU   A 1 164 ? 6.795  -9.578  0.775   0.30 16.54 ?  164 LEU   A CA   1 
ATOM   3792 C CA   B LEU   A 1 164 ? 6.713  -9.625  0.342   0.70 17.53 ?  164 LEU   A CA   1 
ATOM   3793 C C    A LEU   A 1 164 ? 6.359  -10.759 1.626   0.30 16.33 ?  164 LEU   A C    1 
ATOM   3794 C C    B LEU   A 1 164 ? 6.212  -10.768 1.207   0.70 18.36 ?  164 LEU   A C    1 
ATOM   3795 O O    A LEU   A 1 164 ? 6.672  -11.913 1.310   0.30 16.06 ?  164 LEU   A O    1 
ATOM   3796 O O    B LEU   A 1 164 ? 6.465  -11.940 0.906   0.70 18.46 ?  164 LEU   A O    1 
ATOM   3797 C CB   A LEU   A 1 164 ? 7.982  -8.880  1.431   0.30 15.68 ?  164 LEU   A CB   1 
ATOM   3798 C CB   B LEU   A 1 164 ? 7.994  -9.071  0.946   0.70 16.65 ?  164 LEU   A CB   1 
ATOM   3799 C CG   A LEU   A 1 164 ? 8.773  -7.902  0.563   0.30 15.43 ?  164 LEU   A CG   1 
ATOM   3800 C CG   B LEU   A 1 164 ? 8.798  -8.095  0.092   0.70 16.03 ?  164 LEU   A CG   1 
ATOM   3801 C CD1  A LEU   A 1 164 ? 9.660  -7.038  1.441   0.30 15.25 ?  164 LEU   A CD1  1 
ATOM   3802 C CD1  B LEU   A 1 164 ? 9.800  -7.356  0.965   0.70 15.74 ?  164 LEU   A CD1  1 
ATOM   3803 C CD2  A LEU   A 1 164 ? 9.603  -8.636  -0.484  0.30 15.31 ?  164 LEU   A CD2  1 
ATOM   3804 C CD2  B LEU   A 1 164 ? 9.508  -8.815  -1.044  0.70 16.42 ?  164 LEU   A CD2  1 
ATOM   3805 H H    A LEU   A 1 164 ? 5.855  -7.842  0.891   0.30 21.19 ?  164 LEU   A H    1 
ATOM   3806 H H    B LEU   A 1 164 ? 5.934  -7.819  0.595   0.70 20.98 ?  164 LEU   A H    1 
ATOM   3807 H HA   A LEU   A 1 164 ? 7.072  -9.917  -0.088  0.30 19.84 ?  164 LEU   A HA   1 
ATOM   3808 H HA   B LEU   A 1 164 ? 6.908  -9.976  -0.539  0.70 21.03 ?  164 LEU   A HA   1 
ATOM   3809 H HB2  A LEU   A 1 164 ? 7.653  -8.384  2.196   0.30 18.82 ?  164 LEU   A HB2  1 
ATOM   3810 H HB2  B LEU   A 1 164 ? 7.768  -8.615  1.767   0.70 19.98 ?  164 LEU   A HB2  1 
ATOM   3811 H HB3  A LEU   A 1 164 ? 8.601  -9.562  1.733   0.30 18.82 ?  164 LEU   A HB3  1 
ATOM   3812 H HB3  B LEU   A 1 164 ? 8.578  -9.821  1.143   0.70 19.98 ?  164 LEU   A HB3  1 
ATOM   3813 H HG   A LEU   A 1 164 ? 8.153  -7.319  0.100   0.30 18.52 ?  164 LEU   A HG   1 
ATOM   3814 H HG   B LEU   A 1 164 ? 8.195  -7.440  -0.294  0.70 19.24 ?  164 LEU   A HG   1 
ATOM   3815 H HD11 A LEU   A 1 164 ? 10.164 -6.430  0.879   0.30 18.30 ?  164 LEU   A HD11 1 
ATOM   3816 H HD11 B LEU   A 1 164 ? 10.314 -6.747  0.411   0.70 18.88 ?  164 LEU   A HD11 1 
ATOM   3817 H HD12 A LEU   A 1 164 ? 9.101  -6.535  2.056   0.30 18.30 ?  164 LEU   A HD12 1 
ATOM   3818 H HD12 B LEU   A 1 164 ? 9.321  -6.857  1.646   0.70 18.88 ?  164 LEU   A HD12 1 
ATOM   3819 H HD13 A LEU   A 1 164 ? 10.265 -7.610  1.938   0.30 18.30 ?  164 LEU   A HD13 1 
ATOM   3820 H HD13 B LEU   A 1 164 ? 10.392 -8.001  1.383   0.70 18.88 ?  164 LEU   A HD13 1 
ATOM   3821 H HD21 A LEU   A 1 164 ? 10.114 -7.985  -0.993  0.30 18.37 ?  164 LEU   A HD21 1 
ATOM   3822 H HD21 B LEU   A 1 164 ? 10.064 -8.179  -1.521  0.70 19.70 ?  164 LEU   A HD21 1 
ATOM   3823 H HD22 A LEU   A 1 164 ? 10.203 -9.252  -0.037  0.30 18.37 ?  164 LEU   A HD22 1 
ATOM   3824 H HD22 B LEU   A 1 164 ? 10.058 -9.522  -0.674  0.70 19.70 ?  164 LEU   A HD22 1 
ATOM   3825 H HD23 A LEU   A 1 164 ? 9.007  -9.123  -1.075  0.30 18.37 ?  164 LEU   A HD23 1 
ATOM   3826 H HD23 B LEU   A 1 164 ? 8.844  -9.189  -1.643  0.70 19.70 ?  164 LEU   A HD23 1 
ATOM   3827 N N    A VAL   A 1 165 ? 5.643  -10.491 2.718   0.30 16.14 ?  165 VAL   A N    1 
ATOM   3828 N N    B VAL   A 1 165 ? 5.521  -10.442 2.302   0.70 19.01 ?  165 VAL   A N    1 
ATOM   3829 C CA   A VAL   A 1 165 ? 5.138  -11.572 3.557   0.30 16.32 ?  165 VAL   A CA   1 
ATOM   3830 C CA   B VAL   A 1 165 ? 5.036  -11.472 3.214   0.70 20.98 ?  165 VAL   A CA   1 
ATOM   3831 C C    A VAL   A 1 165 ? 4.109  -12.393 2.793   0.30 15.93 ?  165 VAL   A C    1 
ATOM   3832 C C    B VAL   A 1 165 ? 3.988  -12.355 2.539   0.70 22.91 ?  165 VAL   A C    1 
ATOM   3833 O O    A VAL   A 1 165 ? 4.259  -13.607 2.622   0.30 15.77 ?  165 VAL   A O    1 
ATOM   3834 O O    B VAL   A 1 165 ? 3.984  -13.576 2.727   0.70 23.79 ?  165 VAL   A O    1 
ATOM   3835 C CB   A VAL   A 1 165 ? 4.560  -11.017 4.871   0.30 16.94 ?  165 VAL   A CB   1 
ATOM   3836 C CB   B VAL   A 1 165 ? 4.553  -10.835 4.536   0.70 21.64 ?  165 VAL   A CB   1 
ATOM   3837 C CG1  A VAL   A 1 165 ? 3.833  -12.117 5.638   0.30 17.13 ?  165 VAL   A CG1  1 
ATOM   3838 C CG1  B VAL   A 1 165 ? 3.825  -11.844 5.419   0.70 21.89 ?  165 VAL   A CG1  1 
ATOM   3839 C CG2  A VAL   A 1 165 ? 5.662  -10.402 5.716   0.30 17.35 ?  165 VAL   A CG2  1 
ATOM   3840 C CG2  B VAL   A 1 165 ? 5.743  -10.225 5.287   0.70 21.93 ?  165 VAL   A CG2  1 
ATOM   3841 H H    A VAL   A 1 165 ? 5.430  -9.705  2.989   0.30 19.37 ?  165 VAL   A H    1 
ATOM   3842 H H    B VAL   A 1 165 ? 5.334  -9.638  2.546   0.70 22.81 ?  165 VAL   A H    1 
ATOM   3843 H HA   A VAL   A 1 165 ? 5.872  -12.162 3.791   0.30 19.58 ?  165 VAL   A HA   1 
ATOM   3844 H HA   B VAL   A 1 165 ? 5.773  -12.049 3.443   0.70 25.17 ?  165 VAL   A HA   1 
ATOM   3845 H HB   A VAL   A 1 165 ? 3.916  -10.321 4.667   0.30 20.33 ?  165 VAL   A HB   1 
ATOM   3846 H HB   B VAL   A 1 165 ? 3.939  -10.112 4.345   0.70 25.96 ?  165 VAL   A HB   1 
ATOM   3847 H HG11 A VAL   A 1 165 ? 3.729  -11.842 6.562   0.30 20.56 ?  165 VAL   A HG11 1 
ATOM   3848 H HG11 B VAL   A 1 165 ? 3.740  -11.479 6.320   0.70 26.26 ?  165 VAL   A HG11 1 
ATOM   3849 H HG12 A VAL   A 1 165 ? 2.960  -12.260 5.239   0.30 20.56 ?  165 VAL   A HG12 1 
ATOM   3850 H HG12 B VAL   A 1 165 ? 2.944  -12.006 5.051   0.70 26.26 ?  165 VAL   A HG12 1 
ATOM   3851 H HG13 A VAL   A 1 165 ? 4.357  -12.931 5.594   0.30 20.56 ?  165 VAL   A HG13 1 
ATOM   3852 H HG13 B VAL   A 1 165 ? 4.334  -12.666 5.449   0.70 26.26 ?  165 VAL   A HG13 1 
ATOM   3853 H HG21 A VAL   A 1 165 ? 5.279  -10.063 6.540   0.30 20.83 ?  165 VAL   A HG21 1 
ATOM   3854 H HG21 B VAL   A 1 165 ? 5.443  -9.874  6.142   0.70 26.31 ?  165 VAL   A HG21 1 
ATOM   3855 H HG22 A VAL   A 1 165 ? 6.325  -11.081 5.913   0.30 20.83 ?  165 VAL   A HG22 1 
ATOM   3856 H HG22 B VAL   A 1 165 ? 6.415  -10.911 5.434   0.70 26.31 ?  165 VAL   A HG22 1 
ATOM   3857 H HG23 A VAL   A 1 165 ? 6.070  -9.675  5.219   0.30 20.83 ?  165 VAL   A HG23 1 
ATOM   3858 H HG23 B VAL   A 1 165 ? 6.122  -9.506  4.754   0.70 26.31 ?  165 VAL   A HG23 1 
ATOM   3859 N N    A SER   A 1 166 ? 3.060  -11.736 2.299   0.30 15.18 ?  166 SER   A N    1 
ATOM   3860 N N    B SER   A 1 166 ? 3.118  -11.775 1.708   0.70 23.35 ?  166 SER   A N    1 
ATOM   3861 C CA   A SER   A 1 166 ? 1.950  -12.465 1.695   0.30 15.09 ?  166 SER   A CA   1 
ATOM   3862 C CA   B SER   A 1 166 ? 2.045  -12.562 1.099   0.70 24.78 ?  166 SER   A CA   1 
ATOM   3863 C C    A SER   A 1 166 ? 2.383  -13.310 0.505   0.30 15.13 ?  166 SER   A C    1 
ATOM   3864 C C    B SER   A 1 166 ? 2.473  -13.335 -0.140  0.70 25.20 ?  166 SER   A C    1 
ATOM   3865 O O    A SER   A 1 166 ? 1.704  -14.290 0.183   0.30 15.87 ?  166 SER   A O    1 
ATOM   3866 O O    B SER   A 1 166 ? 1.713  -14.198 -0.592  0.70 25.26 ?  166 SER   A O    1 
ATOM   3867 C CB   A SER   A 1 166 ? 0.851  -11.498 1.249   0.30 16.08 ?  166 SER   A CB   1 
ATOM   3868 C CB   B SER   A 1 166 ? 0.858  -11.683 0.696   0.70 26.02 ?  166 SER   A CB   1 
ATOM   3869 O OG   A SER   A 1 166 ? 0.232  -10.871 2.358   0.30 16.86 ?  166 SER   A OG   1 
ATOM   3870 O OG   B SER   A 1 166 ? 1.273  -10.502 0.044   0.70 26.78 ?  166 SER   A OG   1 
ATOM   3871 H H    A SER   A 1 166 ? 2.965  -10.888 2.302   0.30 18.22 ?  166 SER   A H    1 
ATOM   3872 H H    B SER   A 1 166 ? 3.127  -10.950 1.481   0.70 28.03 ?  166 SER   A H    1 
ATOM   3873 H HA   A SER   A 1 166 ? 1.562  -13.062 2.359   0.30 18.11 ?  166 SER   A HA   1 
ATOM   3874 H HA   B SER   A 1 166 ? 1.725  -13.209 1.748   0.70 29.73 ?  166 SER   A HA   1 
ATOM   3875 H HB2  A SER   A 1 166 ? 1.243  -10.820 0.683   0.30 19.29 ?  166 SER   A HB2  1 
ATOM   3876 H HB2  B SER   A 1 166 ? 0.308  -12.190 0.076   0.70 31.22 ?  166 SER   A HB2  1 
ATOM   3877 H HB3  A SER   A 1 166 ? 0.177  -11.996 0.751   0.30 19.29 ?  166 SER   A HB3  1 
ATOM   3878 H HB3  B SER   A 1 166 ? 0.335  -11.462 1.472   0.70 31.22 ?  166 SER   A HB3  1 
ATOM   3879 H HG   A SER   A 1 166 ? 0.809  -10.454 2.802   0.30 20.23 ?  166 SER   A HG   1 
ATOM   3880 H HG   B SER   A 1 166 ? 1.707  -10.014 0.575   0.70 32.14 ?  166 SER   A HG   1 
ATOM   3881 N N    A SER   A 1 167 ? 3.481  -12.961 -0.159  0.30 14.80 ?  167 SER   A N    1 
ATOM   3882 N N    B SER   A 1 167 ? 3.640  -13.044 -0.712  0.70 25.66 ?  167 SER   A N    1 
ATOM   3883 C CA   A SER   A 1 167 ? 3.939  -13.691 -1.335  0.30 15.01 ?  167 SER   A CA   1 
ATOM   3884 C CA   B SER   A 1 167 ? 4.051  -13.645 -1.975  0.70 26.59 ?  167 SER   A CA   1 
ATOM   3885 C C    A SER   A 1 167 ? 5.124  -14.605 -1.058  0.30 14.10 ?  167 SER   A C    1 
ATOM   3886 C C    B SER   A 1 167 ? 5.176  -14.658 -1.823  0.70 27.84 ?  167 SER   A C    1 
ATOM   3887 O O    A SER   A 1 167 ? 5.626  -15.239 -1.991  0.30 14.27 ?  167 SER   A O    1 
ATOM   3888 O O    B SER   A 1 167 ? 5.603  -15.245 -2.824  0.70 28.10 ?  167 SER   A O    1 
ATOM   3889 C CB   A SER   A 1 167 ? 4.321  -12.712 -2.448  0.30 16.16 ?  167 SER   A CB   1 
ATOM   3890 C CB   B SER   A 1 167 ? 4.477  -12.550 -2.961  0.70 26.21 ?  167 SER   A CB   1 
ATOM   3891 O OG   A SER   A 1 167 ? 5.313  -11.802 -1.998  0.30 17.05 ?  167 SER   A OG   1 
ATOM   3892 O OG   B SER   A 1 167 ? 5.640  -11.883 -2.503  0.70 25.98 ?  167 SER   A OG   1 
ATOM   3893 H H    A SER   A 1 167 ? 3.966  -12.285 0.046   0.30 17.76 ?  167 SER   A H    1 
ATOM   3894 H H    B SER   A 1 167 ? 4.214  -12.489 -0.385  0.70 30.79 ?  167 SER   A H    1 
ATOM   3895 H HA   A SER   A 1 167 ? 3.204  -14.238 -1.660  0.30 18.01 ?  167 SER   A HA   1 
ATOM   3896 H HA   B SER   A 1 167 ? 3.295  -14.107 -2.361  0.70 31.90 ?  167 SER   A HA   1 
ATOM   3897 H HB2  A SER   A 1 167 ? 4.669  -13.221 -3.199  0.30 19.39 ?  167 SER   A HB2  1 
ATOM   3898 H HB2  B SER   A 1 167 ? 4.660  -12.956 -3.823  0.70 31.45 ?  167 SER   A HB2  1 
ATOM   3899 H HB3  A SER   A 1 167 ? 3.522  -12.229 -2.722  0.30 19.39 ?  167 SER   A HB3  1 
ATOM   3900 H HB3  B SER   A 1 167 ? 3.753  -11.904 -3.050  0.70 31.45 ?  167 SER   A HB3  1 
ATOM   3901 H HG   A SER   A 1 167 ? 5.017  -11.386 -1.329  0.30 20.45 ?  167 SER   A HG   1 
ATOM   3902 H HG   B SER   A 1 167 ? 5.488  -11.525 -1.757  0.70 31.18 ?  167 SER   A HG   1 
ATOM   3903 N N    A PHE   A 1 168 ? 5.583  -14.699 0.186   0.30 13.34 ?  168 PHE   A N    1 
ATOM   3904 N N    B PHE   A 1 168 ? 5.654  -14.896 -0.608  0.70 28.73 ?  168 PHE   A N    1 
ATOM   3905 C CA   A PHE   A 1 168 ? 6.751  -15.517 0.478   0.30 13.14 ?  168 PHE   A CA   1 
ATOM   3906 C CA   B PHE   A 1 168 ? 6.866  -15.682 -0.428  0.70 29.96 ?  168 PHE   A CA   1 
ATOM   3907 C C    A PHE   A 1 168 ? 6.399  -16.992 0.379   0.30 14.12 ?  168 PHE   A C    1 
ATOM   3908 C C    B PHE   A 1 168 ? 6.634  -17.132 -0.839  0.70 32.77 ?  168 PHE   A C    1 
ATOM   3909 O O    A PHE   A 1 168 ? 5.385  -17.429 0.922   0.30 14.27 ?  168 PHE   A O    1 
ATOM   3910 O O    B PHE   A 1 168 ? 5.654  -17.759 -0.423  0.70 33.13 ?  168 PHE   A O    1 
ATOM   3911 C CB   A PHE   A 1 168 ? 7.284  -15.209 1.873   0.30 12.59 ?  168 PHE   A CB   1 
ATOM   3912 C CB   B PHE   A 1 168 ? 7.313  -15.601 1.027   0.70 28.55 ?  168 PHE   A CB   1 
ATOM   3913 C CG   A PHE   A 1 168 ? 8.545  -15.956 2.210   0.30 12.09 ?  168 PHE   A CG   1 
ATOM   3914 C CG   B PHE   A 1 168 ? 8.626  -16.271 1.297   0.70 27.23 ?  168 PHE   A CG   1 
ATOM   3915 C CD1  A PHE   A 1 168 ? 9.752  -15.591 1.643   0.30 12.07 ?  168 PHE   A CD1  1 
ATOM   3916 C CD1  B PHE   A 1 168 ? 9.796  -15.810 0.712   0.70 26.69 ?  168 PHE   A CD1  1 
ATOM   3917 C CD2  A PHE   A 1 168 ? 8.522  -17.029 3.086   0.30 11.43 ?  168 PHE   A CD2  1 
ATOM   3918 C CD2  B PHE   A 1 168 ? 8.690  -17.355 2.152   0.70 26.73 ?  168 PHE   A CD2  1 
ATOM   3919 C CE1  A PHE   A 1 168 ? 10.909 -16.277 1.942   0.30 11.82 ?  168 PHE   A CE1  1 
ATOM   3920 C CE1  B PHE   A 1 168 ? 11.002 -16.433 0.971   0.70 26.58 ?  168 PHE   A CE1  1 
ATOM   3921 C CE2  A PHE   A 1 168 ? 9.680  -17.720 3.393   0.30 11.43 ?  168 PHE   A CE2  1 
ATOM   3922 C CE2  B PHE   A 1 168 ? 9.890  -17.978 2.414   0.70 26.52 ?  168 PHE   A CE2  1 
ATOM   3923 C CZ   A PHE   A 1 168 ? 10.876 -17.343 2.820   0.30 11.95 ?  168 PHE   A CZ   1 
ATOM   3924 C CZ   B PHE   A 1 168 ? 11.048 -17.517 1.825   0.70 26.46 ?  168 PHE   A CZ   1 
ATOM   3925 H H    A PHE   A 1 168 ? 5.232  -14.317 0.874   0.30 16.01 ?  168 PHE   A H    1 
ATOM   3926 H H    B PHE   A 1 168 ? 5.293  -14.619 0.122   0.70 34.47 ?  168 PHE   A H    1 
ATOM   3927 H HA   A PHE   A 1 168 ? 7.434  -15.345 -0.166  0.30 15.76 ?  168 PHE   A HA   1 
ATOM   3928 H HA   B PHE   A 1 168 ? 7.566  -15.314 -0.988  0.70 35.95 ?  168 PHE   A HA   1 
ATOM   3929 H HB2  A PHE   A 1 168 ? 7.473  -14.265 1.925   0.30 15.11 ?  168 PHE   A HB2  1 
ATOM   3930 H HB2  B PHE   A 1 168 ? 7.398  -14.670 1.274   0.70 34.26 ?  168 PHE   A HB2  1 
ATOM   3931 H HB3  A PHE   A 1 168 ? 6.609  -15.449 2.534   0.30 15.11 ?  168 PHE   A HB3  1 
ATOM   3932 H HB3  B PHE   A 1 168 ? 6.641  -16.031 1.581   0.70 34.26 ?  168 PHE   A HB3  1 
ATOM   3933 H HD1  A PHE   A 1 168 ? 9.780  -14.877 1.054   0.30 14.48 ?  168 PHE   A HD1  1 
ATOM   3934 H HD1  B PHE   A 1 168 ? 9.770  -15.081 0.133   0.70 32.03 ?  168 PHE   A HD1  1 
ATOM   3935 H HD2  A PHE   A 1 168 ? 7.717  -17.293 3.478   0.30 13.71 ?  168 PHE   A HD2  1 
ATOM   3936 H HD2  B PHE   A 1 168 ? 7.912  -17.672 2.549   0.70 32.08 ?  168 PHE   A HD2  1 
ATOM   3937 H HE1  A PHE   A 1 168 ? 11.716 -16.021 1.559   0.30 14.18 ?  168 PHE   A HE1  1 
ATOM   3938 H HE1  B PHE   A 1 168 ? 11.784 -16.120 0.573   0.70 31.89 ?  168 PHE   A HE1  1 
ATOM   3939 H HE2  A PHE   A 1 168 ? 9.650  -18.440 3.987   0.30 13.71 ?  168 PHE   A HE2  1 
ATOM   3940 H HE2  B PHE   A 1 168 ? 9.919  -18.709 2.988   0.70 31.83 ?  168 PHE   A HE2  1 
ATOM   3941 H HZ   A PHE   A 1 168 ? 11.657 -17.806 3.028   0.30 14.34 ?  168 PHE   A HZ   1 
ATOM   3942 H HZ   B PHE   A 1 168 ? 11.859 -17.936 2.001   0.70 31.75 ?  168 PHE   A HZ   1 
ATOM   3943 N N    A LEU   A 1 169 ? 7.235  -17.764 -0.307  0.30 15.25 ?  169 LEU   A N    1 
ATOM   3944 N N    B LEU   A 1 169 ? 7.547  -17.660 -1.653  0.70 35.05 ?  169 LEU   A N    1 
ATOM   3945 C CA   A LEU   A 1 169 ? 6.998  -19.198 -0.454  0.30 17.17 ?  169 LEU   A CA   1 
ATOM   3946 C CA   B LEU   A 1 169 ? 7.433  -19.013 -2.193  0.70 37.06 ?  169 LEU   A CA   1 
ATOM   3947 C C    A LEU   A 1 169 ? 7.857  -19.970 0.540   0.30 17.64 ?  169 LEU   A C    1 
ATOM   3948 C C    B LEU   A 1 169 ? 8.436  -19.956 -1.532  0.70 38.27 ?  169 LEU   A C    1 
ATOM   3949 O O    A LEU   A 1 169 ? 7.338  -20.463 1.542   0.30 17.50 ?  169 LEU   A O    1 
ATOM   3950 O O    B LEU   A 1 169 ? 9.016  -19.653 -0.490  0.70 38.69 ?  169 LEU   A O    1 
ATOM   3951 C CB   A LEU   A 1 169 ? 7.282  -19.650 -1.892  0.30 18.78 ?  169 LEU   A CB   1 
ATOM   3952 C CB   B LEU   A 1 169 ? 7.664  -19.013 -3.709  0.70 37.73 ?  169 LEU   A CB   1 
ATOM   3953 C CG   A LEU   A 1 169 ? 6.930  -21.093 -2.273  0.30 20.34 ?  169 LEU   A CG   1 
ATOM   3954 C CG   B LEU   A 1 169 ? 6.658  -18.273 -4.595  0.70 38.18 ?  169 LEU   A CG   1 
ATOM   3955 C CD1  A LEU   A 1 169 ? 5.484  -21.414 -1.930  0.30 20.88 ?  169 LEU   A CD1  1 
ATOM   3956 C CD1  B LEU   A 1 169 ? 7.066  -18.379 -6.059  0.70 38.26 ?  169 LEU   A CD1  1 
ATOM   3957 C CD2  A LEU   A 1 169 ? 7.186  -21.333 -3.757  0.30 20.94 ?  169 LEU   A CD2  1 
ATOM   3958 C CD2  B LEU   A 1 169 ? 5.256  -18.818 -4.394  0.70 38.41 ?  169 LEU   A CD2  1 
ATOM   3959 O OXT  A LEU   A 1 169 ? 9.073  -20.104 0.382   0.30 18.23 -1 169 LEU   A OXT  1 
ATOM   3960 O OXT  B LEU   A 1 169 ? 8.688  -21.052 -2.031  0.70 38.84 -1 169 LEU   A OXT  1 
ATOM   3961 H H    A LEU   A 1 169 ? 7.940  -17.493 -0.689  0.30 18.30 ?  169 LEU   A H    1 
ATOM   3962 H H    B LEU   A 1 169 ? 8.259  -17.248 -1.904  0.70 42.06 ?  169 LEU   A H    1 
ATOM   3963 H HA   A LEU   A 1 169 ? 6.071  -19.406 -0.256  0.30 20.61 ?  169 LEU   A HA   1 
ATOM   3964 H HA   B LEU   A 1 169 ? 6.544  -19.354 -2.023  0.70 44.47 ?  169 LEU   A HA   1 
ATOM   3965 H HB2  A LEU   A 1 169 ? 6.777  -19.077 -2.487  0.30 22.54 ?  169 LEU   A HB2  1 
ATOM   3966 H HB2  B LEU   A 1 169 ? 8.531  -18.616 -3.879  0.70 45.28 ?  169 LEU   A HB2  1 
ATOM   3967 H HB3  A LEU   A 1 169 ? 8.227  -19.541 -2.065  0.30 22.54 ?  169 LEU   A HB3  1 
ATOM   3968 H HB3  B LEU   A 1 169 ? 7.674  -19.935 -4.009  0.70 45.28 ?  169 LEU   A HB3  1 
ATOM   3969 H HG   A LEU   A 1 169 ? 7.496  -21.704 -1.775  0.30 24.41 ?  169 LEU   A HG   1 
ATOM   3970 H HG   B LEU   A 1 169 ? 6.654  -17.334 -4.355  0.70 45.81 ?  169 LEU   A HG   1 
ATOM   3971 H HD11 A LEU   A 1 169 ? 5.247  -22.271 -2.321  0.30 25.06 ?  169 LEU   A HD11 1 
ATOM   3972 H HD11 B LEU   A 1 169 ? 6.418  -17.903 -6.603  0.70 45.92 ?  169 LEU   A HD11 1 
ATOM   3973 H HD12 A LEU   A 1 169 ? 5.389  -21.455 -0.966  0.30 25.06 ?  169 LEU   A HD12 1 
ATOM   3974 H HD12 B LEU   A 1 169 ? 7.945  -17.985 -6.172  0.70 45.92 ?  169 LEU   A HD12 1 
ATOM   3975 H HD13 A LEU   A 1 169 ? 4.912  -20.719 -2.292  0.30 25.06 ?  169 LEU   A HD13 1 
ATOM   3976 H HD13 B LEU   A 1 169 ? 7.088  -19.315 -6.314  0.70 45.92 ?  169 LEU   A HD13 1 
ATOM   3977 H HD21 A LEU   A 1 169 ? 6.960  -22.252 -3.976  0.30 25.13 ?  169 LEU   A HD21 1 
ATOM   3978 H HD21 B LEU   A 1 169 ? 4.664  -18.418 -5.050  0.70 46.09 ?  169 LEU   A HD21 1 
ATOM   3979 H HD22 A LEU   A 1 169 ? 6.634  -20.726 -4.275  0.30 25.13 ?  169 LEU   A HD22 1 
ATOM   3980 H HD22 B LEU   A 1 169 ? 5.273  -19.781 -4.507  0.70 46.09 ?  169 LEU   A HD22 1 
ATOM   3981 H HD23 A LEU   A 1 169 ? 8.123  -21.170 -3.946  0.30 25.13 ?  169 LEU   A HD23 1 
ATOM   3982 H HD23 B LEU   A 1 169 ? 4.957  -18.595 -3.499  0.70 46.09 ?  169 LEU   A HD23 1 
ATOM   3983 N N    A SER   B 1 1   ? 50.678 -9.057  -23.648 0.30 29.97 ?  1   SER   B N    1 
ATOM   3984 N N    B SER   B 1 1   ? 50.724 -9.248  -23.835 0.70 29.26 ?  1   SER   B N    1 
ATOM   3985 C CA   A SER   B 1 1   ? 51.230 -10.152 -22.825 0.30 29.65 ?  1   SER   B CA   1 
ATOM   3986 C CA   B SER   B 1 1   ? 51.180 -10.257 -22.855 0.70 29.21 ?  1   SER   B CA   1 
ATOM   3987 C C    A SER   B 1 1   ? 50.185 -11.234 -22.610 0.30 28.91 ?  1   SER   B C    1 
ATOM   3988 C C    B SER   B 1 1   ? 50.079 -11.265 -22.556 0.70 28.97 ?  1   SER   B C    1 
ATOM   3989 O O    A SER   B 1 1   ? 49.007 -11.058 -22.933 0.30 28.89 ?  1   SER   B O    1 
ATOM   3990 O O    B SER   B 1 1   ? 48.906 -11.063 -22.894 0.70 28.50 ?  1   SER   B O    1 
ATOM   3991 C CB   A SER   B 1 1   ? 51.708 -9.617  -21.479 0.30 29.80 ?  1   SER   B CB   1 
ATOM   3992 C CB   B SER   B 1 1   ? 51.637 -9.593  -21.559 0.70 29.09 ?  1   SER   B CB   1 
ATOM   3993 O OG   A SER   B 1 1   ? 50.613 -9.183  -20.693 0.30 30.28 ?  1   SER   B OG   1 
ATOM   3994 O OG   B SER   B 1 1   ? 50.642 -9.707  -20.558 0.70 29.88 ?  1   SER   B OG   1 
ATOM   3995 H H1   A SER   B 1 1   ? 50.315 -9.401  -24.381 0.30 35.96 ?  1   SER   B H1   1 
ATOM   3996 H H1   B SER   B 1 1   ? 51.436 -8.857  -24.197 0.70 35.12 ?  1   SER   B H1   1 
ATOM   3997 H H2   A SER   B 1 1   ? 50.063 -8.624  -23.179 0.30 35.96 ?  1   SER   B H2   1 
ATOM   3998 H H2   B SER   B 1 1   ? 50.249 -9.652  -24.467 0.70 35.12 ?  1   SER   B H2   1 
ATOM   3999 H H3   A SER   B 1 1   ? 51.337 -8.504  -23.868 0.30 35.96 ?  1   SER   B H3   1 
ATOM   4000 H H3   B SER   B 1 1   ? 50.227 -8.645  -23.419 0.70 35.12 ?  1   SER   B H3   1 
ATOM   4001 H HA   A SER   B 1 1   ? 51.983 -10.537 -23.290 0.30 35.58 ?  1   SER   B HA   1 
ATOM   4002 H HA   B SER   B 1 1   ? 51.933 -10.726 -23.237 0.70 35.06 ?  1   SER   B HA   1 
ATOM   4003 H HB2  A SER   B 1 1   ? 52.183 -10.325 -21.017 0.30 35.76 ?  1   SER   B HB2  1 
ATOM   4004 H HB2  B SER   B 1 1   ? 52.440 -10.037 -21.251 0.70 34.90 ?  1   SER   B HB2  1 
ATOM   4005 H HB3  A SER   B 1 1   ? 52.298 -8.863  -21.629 0.30 35.76 ?  1   SER   B HB3  1 
ATOM   4006 H HB3  B SER   B 1 1   ? 51.819 -8.656  -21.729 0.70 34.90 ?  1   SER   B HB3  1 
ATOM   4007 H HG   A SER   B 1 1   ? 50.880 -8.648  -20.106 0.30 36.34 ?  1   SER   B HG   1 
ATOM   4008 H HG   B SER   B 1 1   ? 50.959 -9.468  -19.818 0.70 35.85 ?  1   SER   B HG   1 
ATOM   4009 N N    A MET   B 1 2   ? 50.628 -12.352 -22.048 0.30 27.99 ?  2   MET   B N    1 
ATOM   4010 N N    B MET   B 1 2   ? 50.476 -12.344 -21.893 0.70 28.86 ?  2   MET   B N    1 
ATOM   4011 C CA   A MET   B 1 2   ? 49.802 -13.536 -21.872 0.30 27.16 ?  2   MET   B CA   1 
ATOM   4012 C CA   B MET   B 1 2   ? 49.660 -13.545 -21.741 0.70 28.84 ?  2   MET   B CA   1 
ATOM   4013 C C    A MET   B 1 2   ? 49.584 -13.755 -20.383 0.30 23.81 ?  2   MET   B C    1 
ATOM   4014 C C    B MET   B 1 2   ? 49.430 -13.795 -20.257 0.70 25.90 ?  2   MET   B C    1 
ATOM   4015 O O    A MET   B 1 2   ? 50.542 -13.991 -19.639 0.30 22.87 ?  2   MET   B O    1 
ATOM   4016 O O    B MET   B 1 2   ? 50.310 -14.321 -19.567 0.70 26.43 ?  2   MET   B O    1 
ATOM   4017 C CB   A MET   B 1 2   ? 50.490 -14.745 -22.501 0.30 29.70 ?  2   MET   B CB   1 
ATOM   4018 C CB   B MET   B 1 2   ? 50.394 -14.711 -22.377 0.70 31.96 ?  2   MET   B CB   1 
ATOM   4019 C CG   A MET   B 1 2   ? 49.611 -15.976 -22.626 0.30 31.92 ?  2   MET   B CG   1 
ATOM   4020 C CG   B MET   B 1 2   ? 49.528 -15.886 -22.801 0.70 34.60 ?  2   MET   B CG   1 
ATOM   4021 S SD   A MET   B 1 2   ? 50.412 -17.279 -23.580 0.30 33.95 ?  2   MET   B SD   1 
ATOM   4022 S SD   B MET   B 1 2   ? 50.445 -17.017 -23.861 0.70 37.10 ?  2   MET   B SD   1 
ATOM   4023 C CE   A MET   B 1 2   ? 50.954 -16.331 -25.001 0.30 34.30 ?  2   MET   B CE   1 
ATOM   4024 C CE   B MET   B 1 2   ? 51.444 -15.848 -24.774 0.70 37.50 ?  2   MET   B CE   1 
ATOM   4025 H H    A MET   B 1 2   ? 51.428 -12.448 -21.746 0.30 33.59 ?  2   MET   B H    1 
ATOM   4026 H H    B MET   B 1 2   ? 51.245 -12.411 -21.517 0.70 34.63 ?  2   MET   B H    1 
ATOM   4027 H HA   A MET   B 1 2   ? 48.948 -13.414 -22.311 0.30 32.59 ?  2   MET   B HA   1 
ATOM   4028 H HA   B MET   B 1 2   ? 48.814 -13.434 -22.202 0.70 34.61 ?  2   MET   B HA   1 
ATOM   4029 H HB2  A MET   B 1 2   ? 50.780 -14.478 -23.385 0.30 35.64 ?  2   MET   B HB2  1 
ATOM   4030 H HB2  B MET   B 1 2   ? 50.821 -14.325 -23.148 0.70 38.36 ?  2   MET   B HB2  1 
ATOM   4031 H HB3  A MET   B 1 2   ? 51.258 -14.991 -21.965 0.30 35.64 ?  2   MET   B HB3  1 
ATOM   4032 H HB3  B MET   B 1 2   ? 51.066 -15.061 -21.772 0.70 38.36 ?  2   MET   B HB3  1 
ATOM   4033 H HG2  A MET   B 1 2   ? 49.422 -16.319 -21.738 0.30 38.30 ?  2   MET   B HG2  1 
ATOM   4034 H HG2  B MET   B 1 2   ? 49.240 -16.373 -22.010 0.70 41.52 ?  2   MET   B HG2  1 
ATOM   4035 H HG3  A MET   B 1 2   ? 48.787 -15.740 -23.079 0.30 38.30 ?  2   MET   B HG3  1 
ATOM   4036 H HG3  B MET   B 1 2   ? 48.761 -15.573 -23.297 0.70 41.52 ?  2   MET   B HG3  1 
ATOM   4037 H HE1  A MET   B 1 2   ? 51.105 -16.934 -25.737 0.30 41.17 ?  2   MET   B HE1  1 
ATOM   4038 H HE1  B MET   B 1 2   ? 51.806 -16.301 -25.528 0.70 45.01 ?  2   MET   B HE1  1 
ATOM   4039 H HE2  A MET   B 1 2   ? 50.260 -15.690 -25.228 0.30 41.17 ?  2   MET   B HE2  1 
ATOM   4040 H HE2  B MET   B 1 2   ? 50.881 -15.108 -25.067 0.70 45.01 ?  2   MET   B HE2  1 
ATOM   4041 H HE3  A MET   B 1 2   ? 51.776 -15.857 -24.781 0.30 41.17 ?  2   MET   B HE3  1 
ATOM   4042 H HE3  B MET   B 1 2   ? 52.167 -15.516 -24.206 0.70 45.01 ?  2   MET   B HE3  1 
ATOM   4043 N N    A VAL   B 1 3   ? 48.328 -13.653 -19.952 0.30 21.40 ?  3   VAL   B N    1 
ATOM   4044 N N    B VAL   B 1 3   ? 48.253 -13.414 -19.769 0.70 22.70 ?  3   VAL   B N    1 
ATOM   4045 C CA   A VAL   B 1 3   ? 47.934 -13.899 -18.573 0.30 19.54 ?  3   VAL   B CA   1 
ATOM   4046 C CA   B VAL   B 1 3   ? 47.831 -13.715 -18.408 0.70 20.80 ?  3   VAL   B CA   1 
ATOM   4047 C C    A VAL   B 1 3   ? 46.710 -14.805 -18.595 0.30 17.83 ?  3   VAL   B C    1 
ATOM   4048 C C    B VAL   B 1 3   ? 46.589 -14.592 -18.470 0.70 18.91 ?  3   VAL   B C    1 
ATOM   4049 O O    A VAL   B 1 3   ? 46.043 -14.962 -19.620 0.30 17.13 ?  3   VAL   B O    1 
ATOM   4050 O O    B VAL   B 1 3   ? 45.804 -14.538 -19.421 0.70 19.41 ?  3   VAL   B O    1 
ATOM   4051 C CB   A VAL   B 1 3   ? 47.643 -12.586 -17.808 0.30 20.08 ?  3   VAL   B CB   1 
ATOM   4052 C CB   B VAL   B 1 3   ? 47.582 -12.445 -17.557 0.70 21.80 ?  3   VAL   B CB   1 
ATOM   4053 C CG1  A VAL   B 1 3   ? 48.897 -11.718 -17.739 0.30 20.33 ?  3   VAL   B CG1  1 
ATOM   4054 C CG1  B VAL   B 1 3   ? 48.865 -11.634 -17.411 0.70 22.12 ?  3   VAL   B CG1  1 
ATOM   4055 C CG2  A VAL   B 1 3   ? 46.502 -11.827 -18.468 0.30 20.23 ?  3   VAL   B CG2  1 
ATOM   4056 C CG2  B VAL   B 1 3   ? 46.465 -11.600 -18.155 0.70 22.04 ?  3   VAL   B CG2  1 
ATOM   4057 H H    A VAL   B 1 3   ? 47.669 -13.427 -20.456 0.30 25.68 ?  3   VAL   B H    1 
ATOM   4058 H H    B VAL   B 1 3   ? 47.673 -12.967 -20.220 0.70 27.25 ?  3   VAL   B H    1 
ATOM   4059 H HA   A VAL   B 1 3   ? 48.647 -14.364 -18.110 0.30 23.45 ?  3   VAL   B HA   1 
ATOM   4060 H HA   B VAL   B 1 3   ? 48.526 -14.221 -17.966 0.70 24.96 ?  3   VAL   B HA   1 
ATOM   4061 H HB   A VAL   B 1 3   ? 47.380 -12.797 -16.897 0.30 24.10 ?  3   VAL   B HB   1 
ATOM   4062 H HB   B VAL   B 1 3   ? 47.308 -12.712 -16.665 0.70 26.16 ?  3   VAL   B HB   1 
ATOM   4063 H HG11 A VAL   B 1 3   ? 48.697 -10.911 -17.238 0.30 24.39 ?  3   VAL   B HG11 1 
ATOM   4064 H HG11 B VAL   B 1 3   ? 48.685 -10.853 -16.864 0.70 26.54 ?  3   VAL   B HG11 1 
ATOM   4065 H HG12 A VAL   B 1 3   ? 49.602 -12.215 -17.294 0.30 24.39 ?  3   VAL   B HG12 1 
ATOM   4066 H HG12 B VAL   B 1 3   ? 49.540 -12.186 -16.988 0.70 26.54 ?  3   VAL   B HG12 1 
ATOM   4067 H HG13 A VAL   B 1 3   ? 49.172 -11.488 -18.640 0.30 24.39 ?  3   VAL   B HG13 1 
ATOM   4068 H HG13 B VAL   B 1 3   ? 49.164 -11.360 -18.292 0.70 26.54 ?  3   VAL   B HG13 1 
ATOM   4069 H HG21 A VAL   B 1 3   ? 46.436 -10.946 -18.067 0.30 24.27 ?  3   VAL   B HG21 1 
ATOM   4070 H HG21 B VAL   B 1 3   ? 46.423 -10.751 -17.686 0.70 26.45 ?  3   VAL   B HG21 1 
ATOM   4071 H HG22 A VAL   B 1 3   ? 46.687 -11.744 -19.417 0.30 24.27 ?  3   VAL   B HG22 1 
ATOM   4072 H HG22 B VAL   B 1 3   ? 46.651 -11.450 -19.094 0.70 26.45 ?  3   VAL   B HG22 1 
ATOM   4073 H HG23 A VAL   B 1 3   ? 45.677 -12.316 -18.332 0.30 24.27 ?  3   VAL   B HG23 1 
ATOM   4074 H HG23 B VAL   B 1 3   ? 45.624 -12.073 -18.055 0.70 26.45 ?  3   VAL   B HG23 1 
ATOM   4075 N N    . ASN   B 1 4   ? 46.430 -15.425 -17.448 1.00 17.15 ?  4   ASN   B N    1 
ATOM   4076 C CA   . ASN   B 1 4   ? 45.286 -16.331 -17.337 1.00 16.05 ?  4   ASN   B CA   1 
ATOM   4077 C C    . ASN   B 1 4   ? 45.233 -17.303 -18.515 1.00 16.58 ?  4   ASN   B C    1 
ATOM   4078 O O    . ASN   B 1 4   ? 44.168 -17.589 -19.062 1.00 17.44 ?  4   ASN   B O    1 
ATOM   4079 C CB   . ASN   B 1 4   ? 43.965 -15.568 -17.188 1.00 15.55 ?  4   ASN   B CB   1 
ATOM   4080 C CG   . ASN   B 1 4   ? 43.911 -14.758 -15.914 1.00 14.73 ?  4   ASN   B CG   1 
ATOM   4081 O OD1  . ASN   B 1 4   ? 44.199 -15.269 -14.837 1.00 14.40 ?  4   ASN   B OD1  1 
ATOM   4082 N ND2  . ASN   B 1 4   ? 43.573 -13.477 -16.034 1.00 15.19 ?  4   ASN   B ND2  1 
ATOM   4083 H H    A ASN   B 1 4   ? 46.888 -15.342 -16.727 0.30 20.58 ?  4   ASN   B H    1 
ATOM   4084 H H    B ASN   B 1 4   ? 46.990 -15.497 -16.802 0.70 20.58 ?  4   ASN   B H    1 
ATOM   4085 H HA   . ASN   B 1 4   ? 45.403 -16.858 -16.530 1.00 19.26 ?  4   ASN   B HA   1 
ATOM   4086 H HB2  . ASN   B 1 4   ? 43.859 -14.960 -17.934 1.00 18.66 ?  4   ASN   B HB2  1 
ATOM   4087 H HB3  . ASN   B 1 4   ? 43.232 -16.204 -17.170 1.00 18.66 ?  4   ASN   B HB3  1 
ATOM   4088 H HD21 . ASN   B 1 4   ? 43.536 -12.970 -15.333 1.00 18.23 ?  4   ASN   B HD21 1 
ATOM   4089 H HD22 . ASN   B 1 4   ? 43.393 -13.146 -16.805 1.00 18.23 ?  4   ASN   B HD22 1 
ATOM   4090 N N    . SER   B 1 5   ? 46.395 -17.818 -18.910 1.00 18.34 ?  5   SER   B N    1 
ATOM   4091 C CA   . SER   B 1 5   ? 46.487 -18.734 -20.046 1.00 21.13 ?  5   SER   B CA   1 
ATOM   4092 C C    . SER   B 1 5   ? 46.488 -20.173 -19.536 1.00 21.94 ?  5   SER   B C    1 
ATOM   4093 O O    . SER   B 1 5   ? 47.499 -20.869 -19.519 1.00 24.19 ?  5   SER   B O    1 
ATOM   4094 C CB   . SER   B 1 5   ? 47.725 -18.425 -20.881 1.00 23.42 ?  5   SER   B CB   1 
ATOM   4095 O OG   . SER   B 1 5   ? 48.915 -18.600 -20.130 1.00 25.55 ?  5   SER   B OG   1 
ATOM   4096 H H    . SER   B 1 5   ? 47.151 -17.646 -18.536 1.00 22.00 ?  5   SER   B H    1 
ATOM   4097 H HA   . SER   B 1 5   ? 45.706 -18.619 -20.608 1.00 25.35 ?  5   SER   B HA   1 
ATOM   4098 H HB2  . SER   B 1 5   ? 47.733 -19.019 -21.648 1.00 28.11 ?  5   SER   B HB2  1 
ATOM   4099 H HB3  . SER   B 1 5   ? 47.656 -17.507 -21.174 1.00 28.11 ?  5   SER   B HB3  1 
ATOM   4100 H HG   . SER   B 1 5   ? 48.982 -19.401 -19.890 1.00 30.66 ?  5   SER   B HG   1 
ATOM   4101 N N    . PHE   B 1 6   ? 45.309 -20.599 -19.103 1.00 21.47 ?  6   PHE   B N    1 
ATOM   4102 C CA   . PHE   B 1 6   ? 45.116 -21.945 -18.586 1.00 20.69 ?  6   PHE   B CA   1 
ATOM   4103 C C    . PHE   B 1 6   ? 45.055 -22.930 -19.743 1.00 24.04 ?  6   PHE   B C    1 
ATOM   4104 O O    . PHE   B 1 6   ? 44.380 -22.679 -20.746 1.00 25.77 ?  6   PHE   B O    1 
ATOM   4105 C CB   . PHE   B 1 6   ? 43.821 -21.998 -17.778 1.00 18.24 ?  6   PHE   B CB   1 
ATOM   4106 C CG   . PHE   B 1 6   ? 43.840 -21.137 -16.541 1.00 16.78 ?  6   PHE   B CG   1 
ATOM   4107 C CD1  . PHE   B 1 6   ? 44.347 -21.632 -15.355 1.00 15.63 ?  6   PHE   B CD1  1 
ATOM   4108 C CD2  . PHE   B 1 6   ? 43.353 -19.836 -16.570 1.00 16.34 ?  6   PHE   B CD2  1 
ATOM   4109 C CE1  . PHE   B 1 6   ? 44.360 -20.851 -14.210 1.00 15.23 ?  6   PHE   B CE1  1 
ATOM   4110 C CE2  . PHE   B 1 6   ? 43.375 -19.043 -15.432 1.00 16.40 ?  6   PHE   B CE2  1 
ATOM   4111 C CZ   . PHE   B 1 6   ? 43.883 -19.550 -14.250 1.00 15.50 ?  6   PHE   B CZ   1 
ATOM   4112 H H    . PHE   B 1 6   ? 44.598 -20.122 -19.099 1.00 25.76 ?  6   PHE   B H    1 
ATOM   4113 H HA   . PHE   B 1 6   ? 45.856 -22.188 -18.014 1.00 24.82 ?  6   PHE   B HA   1 
ATOM   4114 H HB2  . PHE   B 1 6   ? 43.088 -21.698 -18.341 1.00 21.89 ?  6   PHE   B HB2  1 
ATOM   4115 H HB3  . PHE   B 1 6   ? 43.664 -22.916 -17.502 1.00 21.89 ?  6   PHE   B HB3  1 
ATOM   4116 H HD1  . PHE   B 1 6   ? 44.677 -22.501 -15.320 1.00 18.76 ?  6   PHE   B HD1  1 
ATOM   4117 H HD2  . PHE   B 1 6   ? 43.010 -19.493 -17.364 1.00 19.61 ?  6   PHE   B HD2  1 
ATOM   4118 H HE1  . PHE   B 1 6   ? 44.710 -21.189 -13.415 1.00 18.28 ?  6   PHE   B HE1  1 
ATOM   4119 H HE2  . PHE   B 1 6   ? 43.040 -18.174 -15.461 1.00 19.68 ?  6   PHE   B HE2  1 
ATOM   4120 H HZ   . PHE   B 1 6   ? 43.892 -19.024 -13.483 1.00 18.60 ?  6   PHE   B HZ   1 
ATOM   4121 N N    A SER   B 1 7   ? 45.758 -24.054 -19.608 0.30 25.01 ?  7   SER   B N    1 
ATOM   4122 N N    B SER   B 1 7   ? 45.769 -24.048 -19.601 0.70 24.53 ?  7   SER   B N    1 
ATOM   4123 C CA   A SER   B 1 7   ? 45.824 -25.043 -20.673 0.30 26.20 ?  7   SER   B CA   1 
ATOM   4124 C CA   B SER   B 1 7   ? 45.908 -25.038 -20.659 0.70 26.08 ?  7   SER   B CA   1 
ATOM   4125 C C    A SER   B 1 7   ? 45.785 -26.448 -20.089 0.30 25.69 ?  7   SER   B C    1 
ATOM   4126 C C    B SER   B 1 7   ? 45.836 -26.439 -20.069 0.70 25.20 ?  7   SER   B C    1 
ATOM   4127 O O    A SER   B 1 7   ? 46.366 -26.712 -19.032 0.30 26.06 ?  7   SER   B O    1 
ATOM   4128 O O    B SER   B 1 7   ? 46.432 -26.717 -19.025 0.70 26.09 ?  7   SER   B O    1 
ATOM   4129 C CB   A SER   B 1 7   ? 47.091 -24.863 -21.521 0.30 27.49 ?  7   SER   B CB   1 
ATOM   4130 C CB   B SER   B 1 7   ? 47.247 -24.864 -21.392 0.70 27.98 ?  7   SER   B CB   1 
ATOM   4131 O OG   A SER   B 1 7   ? 47.077 -25.726 -22.645 0.30 28.47 ?  7   SER   B OG   1 
ATOM   4132 O OG   B SER   B 1 7   ? 47.454 -25.898 -22.339 0.70 29.68 ?  7   SER   B OG   1 
ATOM   4133 H H    A SER   B 1 7   ? 46.209 -24.262 -18.905 0.30 30.01 ?  7   SER   B H    1 
ATOM   4134 H H    B SER   B 1 7   ? 46.195 -24.254 -18.883 0.70 29.44 ?  7   SER   B H    1 
ATOM   4135 H HA   A SER   B 1 7   ? 45.059 -24.940 -21.257 0.30 31.45 ?  7   SER   B HA   1 
ATOM   4136 H HA   B SER   B 1 7   ? 45.190 -24.938 -21.302 0.70 31.30 ?  7   SER   B HA   1 
ATOM   4137 H HB2  A SER   B 1 7   ? 47.136 -23.943 -21.834 0.30 32.99 ?  7   SER   B HB2  1 
ATOM   4138 H HB2  B SER   B 1 7   ? 47.245 -24.009 -21.853 0.70 33.58 ?  7   SER   B HB2  1 
ATOM   4139 H HB3  A SER   B 1 7   ? 47.869 -25.064 -20.978 0.30 32.99 ?  7   SER   B HB3  1 
ATOM   4140 H HB3  B SER   B 1 7   ? 47.968 -24.885 -20.743 0.70 33.58 ?  7   SER   B HB3  1 
ATOM   4141 H HG   A SER   B 1 7   ? 47.775 -25.619 -23.100 0.30 34.17 ?  7   SER   B HG   1 
ATOM   4142 H HG   B SER   B 1 7   ? 48.188 -25.784 -22.732 0.70 35.61 ?  7   SER   B HG   1 
ATOM   4143 N N    A GLY   B 1 8   ? 45.094 -27.344 -20.790 0.30 25.18 ?  8   GLY   B N    1 
ATOM   4144 N N    B GLY   B 1 8   ? 45.099 -27.318 -20.742 0.70 24.99 ?  8   GLY   B N    1 
ATOM   4145 C CA   A GLY   B 1 8   ? 45.037 -28.739 -20.408 0.30 24.44 ?  8   GLY   B CA   1 
ATOM   4146 C CA   B GLY   B 1 8   ? 45.072 -28.712 -20.358 0.70 24.38 ?  8   GLY   B CA   1 
ATOM   4147 C C    A GLY   B 1 8   ? 44.070 -29.076 -19.298 0.30 23.39 ?  8   GLY   B C    1 
ATOM   4148 C C    B GLY   B 1 8   ? 44.106 -29.051 -19.253 0.70 23.30 ?  8   GLY   B C    1 
ATOM   4149 O O    A GLY   B 1 8   ? 44.171 -30.163 -18.719 0.30 23.98 ?  8   GLY   B O    1 
ATOM   4150 O O    B GLY   B 1 8   ? 44.242 -30.115 -18.637 0.70 24.33 ?  8   GLY   B O    1 
ATOM   4151 H H    A GLY   B 1 8   ? 44.655 -27.159 -21.502 0.30 30.22 ?  8   GLY   B H    1 
ATOM   4152 H H    B GLY   B 1 8   ? 44.599 -27.124 -21.412 0.70 29.99 ?  8   GLY   B H    1 
ATOM   4153 H HA2  A GLY   B 1 8   ? 44.792 -29.262 -21.189 0.30 29.33 ?  8   GLY   B HA2  1 
ATOM   4154 H HA2  B GLY   B 1 8   ? 44.840 -29.249 -21.130 0.70 29.25 ?  8   GLY   B HA2  1 
ATOM   4155 H HA3  A GLY   B 1 8   ? 45.915 -29.024 -20.122 0.30 29.33 ?  8   GLY   B HA3  1 
ATOM   4156 H HA3  B GLY   B 1 8   ? 45.954 -28.977 -20.058 0.70 29.25 ?  8   GLY   B HA3  1 
ATOM   4157 N N    . TYR   B 1 9   ? 43.128 -28.190 -18.982 1.00 21.96 ?  9   TYR   B N    1 
ATOM   4158 C CA   . TYR   B 1 9   ? 42.152 -28.458 -17.939 1.00 19.43 ?  9   TYR   B CA   1 
ATOM   4159 C C    . TYR   B 1 9   ? 40.971 -29.242 -18.480 1.00 18.93 ?  9   TYR   B C    1 
ATOM   4160 O O    . TYR   B 1 9   ? 40.578 -29.103 -19.643 1.00 20.84 ?  9   TYR   B O    1 
ATOM   4161 C CB   . TYR   B 1 9   ? 41.648 -27.167 -17.299 1.00 18.92 ?  9   TYR   B CB   1 
ATOM   4162 C CG   . TYR   B 1 9   ? 42.668 -26.554 -16.372 1.00 18.33 ?  9   TYR   B CG   1 
ATOM   4163 C CD1  . TYR   B 1 9   ? 43.774 -25.889 -16.877 1.00 18.85 ?  9   TYR   B CD1  1 
ATOM   4164 C CD2  . TYR   B 1 9   ? 42.540 -26.655 -14.997 1.00 17.59 ?  9   TYR   B CD2  1 
ATOM   4165 C CE1  . TYR   B 1 9   ? 44.725 -25.342 -16.037 1.00 19.12 ?  9   TYR   B CE1  1 
ATOM   4166 C CE2  . TYR   B 1 9   ? 43.485 -26.107 -14.147 1.00 18.24 ?  9   TYR   B CE2  1 
ATOM   4167 C CZ   . TYR   B 1 9   ? 44.577 -25.448 -14.674 1.00 18.96 ?  9   TYR   B CZ   1 
ATOM   4168 O OH   . TYR   B 1 9   ? 45.521 -24.909 -13.834 1.00 19.81 ?  9   TYR   B OH   1 
ATOM   4169 H H    A TYR   B 1 9   ? 43.026 -27.427 -19.365 0.30 26.35 ?  9   TYR   B H    1 
ATOM   4170 H H    B TYR   B 1 9   ? 43.001 -27.448 -19.398 0.70 26.35 ?  9   TYR   B H    1 
ATOM   4171 H HA   . TYR   B 1 9   ? 42.563 -28.989 -17.245 1.00 23.31 ?  9   TYR   B HA   1 
ATOM   4172 H HB2  . TYR   B 1 9   ? 41.436 -26.518 -17.990 1.00 22.70 ?  9   TYR   B HB2  1 
ATOM   4173 H HB3  . TYR   B 1 9   ? 40.858 -27.369 -16.777 1.00 22.70 ?  9   TYR   B HB3  1 
ATOM   4174 H HD1  . TYR   B 1 9   ? 43.878 -25.816 -17.799 1.00 22.62 ?  9   TYR   B HD1  1 
ATOM   4175 H HD2  . TYR   B 1 9   ? 41.799 -27.107 -14.639 1.00 21.11 ?  9   TYR   B HD2  1 
ATOM   4176 H HE1  . TYR   B 1 9   ? 45.456 -24.899 -16.390 1.00 22.94 ?  9   TYR   B HE1  1 
ATOM   4177 H HE2  . TYR   B 1 9   ? 43.374 -26.191 -13.226 1.00 21.89 ?  9   TYR   B HE2  1 
ATOM   4178 H HH   . TYR   B 1 9   ? 46.113 -24.538 -14.284 1.00 23.77 ?  9   TYR   B HH   1 
ATOM   4179 N N    . LEU   B 1 10  ? 40.413 -30.079 -17.614 1.00 17.25 ?  10  LEU   B N    1 
ATOM   4180 C CA   . LEU   B 1 10  ? 39.210 -30.840 -17.899 1.00 16.99 ?  10  LEU   B CA   1 
ATOM   4181 C C    . LEU   B 1 10  ? 38.017 -30.076 -17.340 1.00 16.42 ?  10  LEU   B C    1 
ATOM   4182 O O    . LEU   B 1 10  ? 38.025 -29.663 -16.178 1.00 16.13 ?  10  LEU   B O    1 
ATOM   4183 C CB   . LEU   B 1 10  ? 39.308 -32.218 -17.242 1.00 17.74 ?  10  LEU   B CB   1 
ATOM   4184 C CG   . LEU   B 1 10  ? 38.174 -33.180 -17.570 1.00 19.34 ?  10  LEU   B CG   1 
ATOM   4185 C CD1  . LEU   B 1 10  ? 38.303 -33.697 -19.000 1.00 20.79 ?  10  LEU   B CD1  1 
ATOM   4186 C CD2  . LEU   B 1 10  ? 38.143 -34.327 -16.577 1.00 20.32 ?  10  LEU   B CD2  1 
ATOM   4187 H H    . LEU   B 1 10  ? 40.721 -30.225 -16.819 1.00 20.69 ?  10  LEU   B H    1 
ATOM   4188 H HA   . LEU   B 1 10  ? 39.096 -30.951 -18.852 1.00 20.39 ?  10  LEU   B HA   1 
ATOM   4189 H HB2  . LEU   B 1 10  ? 40.137 -32.638 -17.528 1.00 21.29 ?  10  LEU   B HB2  1 
ATOM   4190 H HB3  . LEU   B 1 10  ? 39.322 -32.105 -16.277 1.00 21.29 ?  10  LEU   B HB3  1 
ATOM   4191 H HG   . LEU   B 1 10  ? 37.330 -32.710 -17.501 1.00 23.21 ?  10  LEU   B HG   1 
ATOM   4192 H HD11 . LEU   B 1 10  ? 37.591 -34.332 -19.171 1.00 24.95 ?  10  LEU   B HD11 1 
ATOM   4193 H HD12 . LEU   B 1 10  ? 38.233 -32.947 -19.611 1.00 24.95 ?  10  LEU   B HD12 1 
ATOM   4194 H HD13 . LEU   B 1 10  ? 39.165 -34.129 -19.102 1.00 24.95 ?  10  LEU   B HD13 1 
ATOM   4195 H HD21 . LEU   B 1 10  ? 37.419 -34.927 -16.814 1.00 24.39 ?  10  LEU   B HD21 1 
ATOM   4196 H HD22 . LEU   B 1 10  ? 38.990 -34.796 -16.612 1.00 24.39 ?  10  LEU   B HD22 1 
ATOM   4197 H HD23 . LEU   B 1 10  ? 37.997 -33.966 -15.688 1.00 24.39 ?  10  LEU   B HD23 1 
ATOM   4198 N N    . LYS   B 1 11  ? 36.997 -29.895 -18.166 1.00 17.54 ?  11  LYS   B N    1 
ATOM   4199 C CA   . LYS   B 1 11  ? 35.794 -29.188 -17.751 1.00 19.75 ?  11  LYS   B CA   1 
ATOM   4200 C C    . LYS   B 1 11  ? 34.925 -30.115 -16.904 1.00 18.91 ?  11  LYS   B C    1 
ATOM   4201 O O    . LYS   B 1 11  ? 34.568 -31.214 -17.343 1.00 20.93 ?  11  LYS   B O    1 
ATOM   4202 C CB   . LYS   B 1 11  ? 35.044 -28.723 -18.998 1.00 24.37 ?  11  LYS   B CB   1 
ATOM   4203 C CG   . LYS   B 1 11  ? 33.921 -27.733 -18.746 1.00 28.67 ?  11  LYS   B CG   1 
ATOM   4204 C CD   . LYS   B 1 11  ? 33.149 -27.455 -20.033 1.00 32.23 ?  11  LYS   B CD   1 
ATOM   4205 C CE   . LYS   B 1 11  ? 32.138 -26.334 -19.852 1.00 34.76 ?  11  LYS   B CE   1 
ATOM   4206 N NZ   . LYS   B 1 11  ? 32.798 -25.011 -19.666 1.00 36.00 ?  11  LYS   B NZ   1 
ATOM   4207 H H    . LYS   B 1 11  ? 36.967 -30.190 -18.972 1.00 21.05 ?  11  LYS   B H    1 
ATOM   4208 H HA   . LYS   B 1 11  ? 36.034 -28.414 -17.220 1.00 23.70 ?  11  LYS   B HA   1 
ATOM   4209 H HB2  . LYS   B 1 11  ? 35.679 -28.294 -19.596 1.00 29.25 ?  11  LYS   B HB2  1 
ATOM   4210 H HB3  . LYS   B 1 11  ? 34.658 -29.496 -19.436 1.00 29.25 ?  11  LYS   B HB3  1 
ATOM   4211 H HG2  . LYS   B 1 11  ? 33.306 -28.103 -18.095 1.00 34.41 ?  11  LYS   B HG2  1 
ATOM   4212 H HG3  . LYS   B 1 11  ? 34.293 -26.897 -18.427 1.00 34.41 ?  11  LYS   B HG3  1 
ATOM   4213 H HD2  . LYS   B 1 11  ? 33.772 -27.192 -20.730 1.00 38.68 ?  11  LYS   B HD2  1 
ATOM   4214 H HD3  . LYS   B 1 11  ? 32.669 -28.256 -20.298 1.00 38.68 ?  11  LYS   B HD3  1 
ATOM   4215 H HE2  . LYS   B 1 11  ? 31.573 -26.280 -20.638 1.00 41.71 ?  11  LYS   B HE2  1 
ATOM   4216 H HE3  . LYS   B 1 11  ? 31.600 -26.521 -19.067 1.00 41.71 ?  11  LYS   B HE3  1 
ATOM   4217 H HZ1  . LYS   B 1 11  ? 32.183 -24.373 -19.582 1.00 43.21 ?  11  LYS   B HZ1  1 
ATOM   4218 H HZ2  . LYS   B 1 11  ? 33.303 -25.024 -18.934 1.00 43.21 ?  11  LYS   B HZ2  1 
ATOM   4219 H HZ3  . LYS   B 1 11  ? 33.312 -24.827 -20.369 1.00 43.21 ?  11  LYS   B HZ3  1 
ATOM   4220 N N    . LEU   B 1 12  ? 34.589 -29.678 -15.690 1.00 17.14 ?  12  LEU   B N    1 
ATOM   4221 C CA   . LEU   B 1 12  ? 33.630 -30.384 -14.846 1.00 16.63 ?  12  LEU   B CA   1 
ATOM   4222 C C    . LEU   B 1 12  ? 32.241 -29.775 -14.940 1.00 16.74 ?  12  LEU   B C    1 
ATOM   4223 O O    . LEU   B 1 12  ? 31.257 -30.491 -15.118 1.00 17.66 ?  12  LEU   B O    1 
ATOM   4224 C CB   . LEU   B 1 12  ? 34.090 -30.389 -13.384 1.00 15.88 ?  12  LEU   B CB   1 
ATOM   4225 C CG   . LEU   B 1 12  ? 35.421 -31.086 -13.109 1.00 15.78 ?  12  LEU   B CG   1 
ATOM   4226 C CD1  . LEU   B 1 12  ? 35.755 -31.038 -11.627 1.00 15.81 ?  12  LEU   B CD1  1 
ATOM   4227 C CD2  . LEU   B 1 12  ? 35.395 -32.510 -13.611 1.00 16.50 ?  12  LEU   B CD2  1 
ATOM   4228 H H    . LEU   B 1 12  ? 34.900 -28.964 -15.332 1.00 20.57 ?  12  LEU   B H    1 
ATOM   4229 H HA   . LEU   B 1 12  ? 33.561 -31.303 -15.147 1.00 19.95 ?  12  LEU   B HA   1 
ATOM   4230 H HB2  . LEU   B 1 12  ? 34.173 -29.473 -13.088 1.00 19.06 ?  12  LEU   B HB2  1 
ATOM   4231 H HB3  . LEU   B 1 12  ? 33.411 -30.841 -12.854 1.00 19.06 ?  12  LEU   B HB3  1 
ATOM   4232 H HG   . LEU   B 1 12  ? 36.121 -30.617 -13.587 1.00 18.94 ?  12  LEU   B HG   1 
ATOM   4233 H HD11 . LEU   B 1 12  ? 36.604 -31.485 -11.478 1.00 18.97 ?  12  LEU   B HD11 1 
ATOM   4234 H HD12 . LEU   B 1 12  ? 35.812 -30.115 -11.342 1.00 18.97 ?  12  LEU   B HD12 1 
ATOM   4235 H HD13 . LEU   B 1 12  ? 35.054 -31.495 -11.129 1.00 18.97 ?  12  LEU   B HD13 1 
ATOM   4236 H HD21 . LEU   B 1 12  ? 36.171 -32.982 -13.276 1.00 19.80 ?  12  LEU   B HD21 1 
ATOM   4237 H HD22 . LEU   B 1 12  ? 34.583 -32.945 -13.297 1.00 19.80 ?  12  LEU   B HD22 1 
ATOM   4238 H HD23 . LEU   B 1 12  ? 35.405 -32.508 -14.584 1.00 19.80 ?  12  LEU   B HD23 1 
ATOM   4239 N N    . THR   B 1 13  ? 32.153 -28.460 -14.812 1.00 16.47 ?  13  THR   B N    1 
ATOM   4240 C CA   . THR   B 1 13  ? 30.934 -27.702 -15.025 1.00 16.35 ?  13  THR   B CA   1 
ATOM   4241 C C    . THR   B 1 13  ? 31.283 -26.507 -15.904 1.00 18.51 ?  13  THR   B C    1 
ATOM   4242 O O    . THR   B 1 13  ? 32.438 -26.310 -16.297 1.00 19.48 ?  13  THR   B O    1 
ATOM   4243 C CB   . THR   B 1 13  ? 30.329 -27.227 -13.700 1.00 16.02 ?  13  THR   B CB   1 
ATOM   4244 O OG1  . THR   B 1 13  ? 31.172 -26.206 -13.147 1.00 15.90 ?  13  THR   B OG1  1 
ATOM   4245 C CG2  . THR   B 1 13  ? 30.192 -28.377 -12.709 1.00 16.86 ?  13  THR   B CG2  1 
ATOM   4246 H H    . THR   B 1 13  ? 32.817 -27.965 -14.595 1.00 19.76 ?  13  THR   B H    1 
ATOM   4247 H HA   . THR   B 1 13  ? 30.278 -28.250 -15.485 1.00 19.62 ?  13  THR   B HA   1 
ATOM   4248 H HB   . THR   B 1 13  ? 29.446 -26.858 -13.864 1.00 19.23 ?  13  THR   B HB   1 
ATOM   4249 H HG1  . THR   B 1 13  ? 30.864 -25.443 -13.344 1.00 19.08 ?  13  THR   B HG1  1 
ATOM   4250 H HG21 . THR   B 1 13  ? 29.671 -28.094 -11.942 1.00 20.23 ?  13  THR   B HG21 1 
ATOM   4251 H HG22 . THR   B 1 13  ? 29.743 -29.126 -13.134 1.00 20.23 ?  13  THR   B HG22 1 
ATOM   4252 H HG23 . THR   B 1 13  ? 31.068 -28.665 -12.409 1.00 20.23 ?  13  THR   B HG23 1 
ATOM   4253 N N    A ASP   B 1 14  ? 30.273 -25.684 -16.192 0.30 19.48 ?  14  ASP   B N    1 
ATOM   4254 N N    B ASP   B 1 14  ? 30.275 -25.685 -16.200 0.70 19.62 ?  14  ASP   B N    1 
ATOM   4255 C CA   A ASP   B 1 14  ? 30.484 -24.518 -17.043 0.30 20.54 ?  14  ASP   B CA   1 
ATOM   4256 C CA   B ASP   B 1 14  ? 30.496 -24.525 -17.056 0.70 21.02 ?  14  ASP   B CA   1 
ATOM   4257 C C    A ASP   B 1 14  ? 31.575 -23.603 -16.499 0.30 19.04 ?  14  ASP   B C    1 
ATOM   4258 C C    B ASP   B 1 14  ? 31.525 -23.557 -16.489 0.70 19.60 ?  14  ASP   B C    1 
ATOM   4259 O O    A ASP   B 1 14  ? 32.225 -22.894 -17.276 0.30 19.79 ?  14  ASP   B O    1 
ATOM   4260 O O    B ASP   B 1 14  ? 32.064 -22.745 -17.248 0.70 21.04 ?  14  ASP   B O    1 
ATOM   4261 C CB   A ASP   B 1 14  ? 29.174 -23.747 -17.211 0.30 23.23 ?  14  ASP   B CB   1 
ATOM   4262 C CB   B ASP   B 1 14  ? 29.181 -23.784 -17.299 0.70 24.55 ?  14  ASP   B CB   1 
ATOM   4263 C CG   A ASP   B 1 14  ? 28.176 -24.467 -18.098 0.30 25.48 ?  14  ASP   B CG   1 
ATOM   4264 C CG   B ASP   B 1 14  ? 28.291 -24.492 -18.295 0.70 27.99 ?  14  ASP   B CG   1 
ATOM   4265 O OD1  A ASP   B 1 14  ? 28.508 -25.542 -18.646 0.30 26.13 ?  14  ASP   B OD1  1 
ATOM   4266 O OD1  B ASP   B 1 14  ? 28.825 -25.194 -19.180 0.70 29.07 ?  14  ASP   B OD1  1 
ATOM   4267 O OD2  A ASP   B 1 14  ? 27.049 -23.950 -18.241 0.30 26.37 -1 14  ASP   B OD2  1 
ATOM   4268 O OD2  B ASP   B 1 14  ? 27.055 -24.348 -18.195 0.70 29.54 -1 14  ASP   B OD2  1 
ATOM   4269 H H    A ASP   B 1 14  ? 29.471 -25.773 -15.907 0.30 23.37 ?  14  ASP   B H    1 
ATOM   4270 H H    B ASP   B 1 14  ? 29.472 -25.767 -15.914 0.70 23.55 ?  14  ASP   B H    1 
ATOM   4271 H HA   A ASP   B 1 14  ? 30.773 -24.806 -17.917 0.30 24.65 ?  14  ASP   B HA   1 
ATOM   4272 H HA   B ASP   B 1 14  ? 30.830 -24.822 -17.913 0.70 25.23 ?  14  ASP   B HA   1 
ATOM   4273 H HB2  A ASP   B 1 14  ? 28.751 -23.635 -16.347 0.30 27.88 ?  14  ASP   B HB2  1 
ATOM   4274 H HB2  B ASP   B 1 14  ? 28.696 -23.713 -16.463 0.70 29.46 ?  14  ASP   B HB2  1 
ATOM   4275 H HB3  A ASP   B 1 14  ? 29.359 -22.880 -17.606 0.30 27.88 ?  14  ASP   B HB3  1 
ATOM   4276 H HB3  B ASP   B 1 14  ? 29.372 -22.898 -17.649 0.70 29.46 ?  14  ASP   B HB3  1 
ATOM   4277 N N    . ASN   B 1 15  ? 31.804 -23.611 -15.184 1.00 16.98 ?  15  ASN   B N    1 
ATOM   4278 C CA   . ASN   B 1 15  ? 32.754 -22.687 -14.570 1.00 14.61 ?  15  ASN   B CA   1 
ATOM   4279 C C    . ASN   B 1 15  ? 33.836 -23.344 -13.725 1.00 13.57 ?  15  ASN   B C    1 
ATOM   4280 O O    . ASN   B 1 15  ? 34.682 -22.620 -13.191 1.00 14.09 ?  15  ASN   B O    1 
ATOM   4281 C CB   . ASN   B 1 15  ? 32.035 -21.633 -13.710 1.00 14.62 ?  15  ASN   B CB   1 
ATOM   4282 C CG   . ASN   B 1 15  ? 31.400 -22.233 -12.470 1.00 14.73 ?  15  ASN   B CG   1 
ATOM   4283 O OD1  . ASN   B 1 15  ? 30.457 -23.025 -12.566 1.00 16.65 ?  15  ASN   B OD1  1 
ATOM   4284 N ND2  . ASN   B 1 15  ? 31.922 -21.893 -11.306 1.00 14.04 ?  15  ASN   B ND2  1 
ATOM   4285 H H    A ASN   B 1 15  ? 31.433 -24.150 -14.626 0.30 20.38 ?  15  ASN   B H    1 
ATOM   4286 H H    B ASN   B 1 15  ? 31.451 -24.167 -14.631 0.70 20.38 ?  15  ASN   B H    1 
ATOM   4287 H HA   . ASN   B 1 15  ? 33.214 -22.207 -15.271 1.00 17.54 ?  15  ASN   B HA   1 
ATOM   4288 H HB2  . ASN   B 1 15  ? 32.679 -20.964 -13.426 1.00 17.54 ?  15  ASN   B HB2  1 
ATOM   4289 H HB3  . ASN   B 1 15  ? 31.335 -21.219 -14.236 1.00 17.54 ?  15  ASN   B HB3  1 
ATOM   4290 H HD21 . ASN   B 1 15  ? 31.596 -22.210 -10.575 1.00 16.85 ?  15  ASN   B HD21 1 
ATOM   4291 H HD22 . ASN   B 1 15  ? 32.585 -21.340 -11.271 1.00 16.85 ?  15  ASN   B HD22 1 
ATOM   4292 N N    . VAL   B 1 16  ? 33.844 -24.668 -13.580 1.00 13.54 ?  16  VAL   B N    1 
ATOM   4293 C CA   . VAL   B 1 16  ? 34.837 -25.360 -12.764 1.00 13.07 ?  16  VAL   B CA   1 
ATOM   4294 C C    . VAL   B 1 16  ? 35.626 -26.306 -13.655 1.00 13.21 ?  16  VAL   B C    1 
ATOM   4295 O O    . VAL   B 1 16  ? 35.046 -27.183 -14.315 1.00 14.36 ?  16  VAL   B O    1 
ATOM   4296 C CB   . VAL   B 1 16  ? 34.205 -26.121 -11.588 1.00 13.71 ?  16  VAL   B CB   1 
ATOM   4297 C CG1  . VAL   B 1 16  ? 35.285 -26.858 -10.792 1.00 13.82 ?  16  VAL   B CG1  1 
ATOM   4298 C CG2  . VAL   B 1 16  ? 33.406 -25.169 -10.696 1.00 14.08 ?  16  VAL   B CG2  1 
ATOM   4299 H H    . VAL   B 1 16  ? 33.276 -25.203 -13.950 1.00 16.25 ?  16  VAL   B H    1 
ATOM   4300 H HA   . VAL   B 1 16  ? 35.455 -24.710 -12.393 1.00 15.68 ?  16  VAL   B HA   1 
ATOM   4301 H HB   . VAL   B 1 16  ? 33.589 -26.785 -11.936 1.00 16.45 ?  16  VAL   B HB   1 
ATOM   4302 H HG11 . VAL   B 1 16  ? 34.905 -27.146 -9.942  1.00 16.58 ?  16  VAL   B HG11 1 
ATOM   4303 H HG12 . VAL   B 1 16  ? 35.580 -27.629 -11.296 1.00 16.58 ?  16  VAL   B HG12 1 
ATOM   4304 H HG13 . VAL   B 1 16  ? 36.024 -26.254 -10.631 1.00 16.58 ?  16  VAL   B HG13 1 
ATOM   4305 H HG21 . VAL   B 1 16  ? 33.057 -25.664 -9.937  1.00 16.90 ?  16  VAL   B HG21 1 
ATOM   4306 H HG22 . VAL   B 1 16  ? 33.988 -24.459 -10.390 1.00 16.90 ?  16  VAL   B HG22 1 
ATOM   4307 H HG23 . VAL   B 1 16  ? 32.671 -24.798 -11.211 1.00 16.90 ?  16  VAL   B HG23 1 
ATOM   4308 N N    . TYR   B 1 17  ? 36.952 -26.141 -13.636 1.00 13.54 ?  17  TYR   B N    1 
ATOM   4309 C CA   . TYR   B 1 17  ? 37.899 -26.895 -14.442 1.00 13.88 ?  17  TYR   B CA   1 
ATOM   4310 C C    . TYR   B 1 17  ? 38.945 -27.510 -13.522 1.00 13.17 ?  17  TYR   B C    1 
ATOM   4311 O O    . TYR   B 1 17  ? 39.220 -26.981 -12.443 1.00 13.09 ?  17  TYR   B O    1 
ATOM   4312 C CB   . TYR   B 1 17  ? 38.612 -25.970 -15.441 1.00 17.16 ?  17  TYR   B CB   1 
ATOM   4313 C CG   . TYR   B 1 17  ? 37.685 -25.184 -16.337 1.00 20.78 ?  17  TYR   B CG   1 
ATOM   4314 C CD1  . TYR   B 1 17  ? 37.107 -23.991 -15.911 1.00 22.48 ?  17  TYR   B CD1  1 
ATOM   4315 C CD2  . TYR   B 1 17  ? 37.391 -25.632 -17.616 1.00 22.99 ?  17  TYR   B CD2  1 
ATOM   4316 C CE1  . TYR   B 1 17  ? 36.260 -23.271 -16.737 1.00 24.34 ?  17  TYR   B CE1  1 
ATOM   4317 C CE2  . TYR   B 1 17  ? 36.547 -24.920 -18.449 1.00 24.83 ?  17  TYR   B CE2  1 
ATOM   4318 C CZ   . TYR   B 1 17  ? 35.983 -23.744 -18.003 1.00 25.73 ?  17  TYR   B CZ   1 
ATOM   4319 O OH   . TYR   B 1 17  ? 35.146 -23.033 -18.830 1.00 27.22 ?  17  TYR   B OH   1 
ATOM   4320 H H    . TYR   B 1 17  ? 37.346 -25.549 -13.141 1.00 16.25 ?  17  TYR   B H    1 
ATOM   4321 H HA   . TYR   B 1 17  ? 37.439 -27.600 -14.927 1.00 16.65 ?  17  TYR   B HA   1 
ATOM   4322 H HB2  . TYR   B 1 17  ? 39.162 -25.341 -14.950 1.00 20.59 ?  17  TYR   B HB2  1 
ATOM   4323 H HB3  . TYR   B 1 17  ? 39.168 -26.516 -16.015 1.00 20.59 ?  17  TYR   B HB3  1 
ATOM   4324 H HD1  . TYR   B 1 17  ? 37.293 -23.671 -15.058 1.00 26.98 ?  17  TYR   B HD1  1 
ATOM   4325 H HD2  . TYR   B 1 17  ? 37.765 -26.425 -17.922 1.00 27.59 ?  17  TYR   B HD2  1 
ATOM   4326 H HE1  . TYR   B 1 17  ? 35.878 -22.475 -16.441 1.00 29.20 ?  17  TYR   B HE1  1 
ATOM   4327 H HE2  . TYR   B 1 17  ? 36.353 -25.234 -19.305 1.00 29.80 ?  17  TYR   B HE2  1 
ATOM   4328 H HH   . TYR   B 1 17  ? 35.058 -23.426 -19.568 1.00 32.66 ?  17  TYR   B HH   1 
ATOM   4329 N N    . ILE   B 1 18  ? 39.555 -28.616 -13.951 1.00 13.33 ?  18  ILE   B N    1 
ATOM   4330 C CA   . ILE   B 1 18  ? 40.489 -29.338 -13.094 1.00 13.21 ?  18  ILE   B CA   1 
ATOM   4331 C C    . ILE   B 1 18  ? 41.652 -29.889 -13.914 1.00 13.33 ?  18  ILE   B C    1 
ATOM   4332 O O    . ILE   B 1 18  ? 41.492 -30.288 -15.071 1.00 14.65 ?  18  ILE   B O    1 
ATOM   4333 C CB   . ILE   B 1 18  ? 39.742 -30.438 -12.302 1.00 13.60 ?  18  ILE   B CB   1 
ATOM   4334 C CG1  . ILE   B 1 18  ? 40.598 -30.988 -11.160 1.00 13.97 ?  18  ILE   B CG1  1 
ATOM   4335 C CG2  . ILE   B 1 18  ? 39.242 -31.547 -13.237 1.00 14.23 ?  18  ILE   B CG2  1 
ATOM   4336 C CD1  . ILE   B 1 18  ? 39.780 -31.808 -10.168 1.00 15.97 ?  18  ILE   B CD1  1 
ATOM   4337 H H    . ILE   B 1 18  ? 39.442 -28.971 -14.724 1.00 15.99 ?  18  ILE   B H    1 
ATOM   4338 H HA   . ILE   B 1 18  ? 40.852 -28.722 -12.439 1.00 15.86 ?  18  ILE   B HA   1 
ATOM   4339 H HB   . ILE   B 1 18  ? 38.959 -30.038 -11.899 1.00 16.33 ?  18  ILE   B HB   1 
ATOM   4340 H HG12 . ILE   B 1 18  ? 41.289 -31.561 -11.521 1.00 16.76 ?  18  ILE   B HG12 1 
ATOM   4341 H HG13 . ILE   B 1 18  ? 40.992 -30.247 -10.676 1.00 16.76 ?  18  ILE   B HG13 1 
ATOM   4342 H HG21 . ILE   B 1 18  ? 38.646 -32.134 -12.743 1.00 17.07 ?  18  ILE   B HG21 1 
ATOM   4343 H HG22 . ILE   B 1 18  ? 38.762 -31.137 -13.973 1.00 17.07 ?  18  ILE   B HG22 1 
ATOM   4344 H HG23 . ILE   B 1 18  ? 39.999 -32.048 -13.570 1.00 17.07 ?  18  ILE   B HG23 1 
ATOM   4345 H HD11 . ILE   B 1 18  ? 40.353 -32.082 -9.434  1.00 19.16 ?  18  ILE   B HD11 1 
ATOM   4346 H HD12 . ILE   B 1 18  ? 39.050 -31.265 -9.832  1.00 19.16 ?  18  ILE   B HD12 1 
ATOM   4347 H HD13 . ILE   B 1 18  ? 39.427 -32.592 -10.620 1.00 19.16 ?  18  ILE   B HD13 1 
ATOM   4348 N N    . LYS   B 1 19  ? 42.835 -29.919 -13.296 1.00 13.99 ?  19  LYS   B N    1 
ATOM   4349 C CA   . LYS   B 1 19  ? 44.044 -30.408 -13.947 1.00 14.68 ?  19  LYS   B CA   1 
ATOM   4350 C C    . LYS   B 1 19  ? 44.933 -31.095 -12.920 1.00 14.38 ?  19  LYS   B C    1 
ATOM   4351 O O    . LYS   B 1 19  ? 45.020 -30.660 -11.771 1.00 14.02 ?  19  LYS   B O    1 
ATOM   4352 C CB   . LYS   B 1 19  ? 44.833 -29.256 -14.580 1.00 16.32 ?  19  LYS   B CB   1 
ATOM   4353 C CG   . LYS   B 1 19  ? 46.049 -29.678 -15.397 1.00 17.77 ?  19  LYS   B CG   1 
ATOM   4354 C CD   . LYS   B 1 19  ? 46.799 -28.451 -15.906 1.00 19.49 ?  19  LYS   B CD   1 
ATOM   4355 C CE   . LYS   B 1 19  ? 47.984 -28.821 -16.781 1.00 21.65 ?  19  LYS   B CE   1 
ATOM   4356 N NZ   . LYS   B 1 19  ? 48.684 -27.613 -17.295 1.00 22.87 ?  19  LYS   B NZ   1 
ATOM   4357 H H    . LYS   B 1 19  ? 42.954 -29.667 -12.482 1.00 16.79 ?  19  LYS   B H    1 
ATOM   4358 H HA   . LYS   B 1 19  ? 43.805 -31.049 -14.640 1.00 17.62 ?  19  LYS   B HA   1 
ATOM   4359 H HB2  . LYS   B 1 19  ? 44.238 -28.767 -15.166 1.00 19.59 ?  19  LYS   B HB2  1 
ATOM   4360 H HB3  . LYS   B 1 19  ? 45.140 -28.673 -13.865 1.00 19.59 ?  19  LYS   B HB3  1 
ATOM   4361 H HG2  . LYS   B 1 19  ? 46.645 -30.200 -14.839 1.00 21.33 ?  19  LYS   B HG2  1 
ATOM   4362 H HG3  . LYS   B 1 19  ? 45.752 -30.200 -16.159 1.00 21.33 ?  19  LYS   B HG3  1 
ATOM   4363 H HD2  . LYS   B 1 19  ? 46.193 -27.903 -16.429 1.00 23.39 ?  19  LYS   B HD2  1 
ATOM   4364 H HD3  . LYS   B 1 19  ? 47.130 -27.946 -15.145 1.00 23.39 ?  19  LYS   B HD3  1 
ATOM   4365 H HE2  . LYS   B 1 19  ? 48.615 -29.343 -16.259 1.00 25.98 ?  19  LYS   B HE2  1 
ATOM   4366 H HE3  . LYS   B 1 19  ? 47.668 -29.340 -17.539 1.00 25.98 ?  19  LYS   B HE3  1 
ATOM   4367 H HZ1  . LYS   B 1 19  ? 49.342 -27.853 -17.845 1.00 27.44 ?  19  LYS   B HZ1  1 
ATOM   4368 H HZ2  . LYS   B 1 19  ? 48.111 -27.095 -17.740 1.00 27.44 ?  19  LYS   B HZ2  1 
ATOM   4369 H HZ3  . LYS   B 1 19  ? 49.027 -27.148 -16.619 1.00 27.44 ?  19  LYS   B HZ3  1 
ATOM   4370 N N    . ASN   B 1 20  ? 45.607 -32.158 -13.349 1.00 15.49 ?  20  ASN   B N    1 
ATOM   4371 C CA   . ASN   B 1 20  ? 46.646 -32.784 -12.538 1.00 16.36 ?  20  ASN   B CA   1 
ATOM   4372 C C    . ASN   B 1 20  ? 47.911 -31.955 -12.729 1.00 16.71 ?  20  ASN   B C    1 
ATOM   4373 O O    . ASN   B 1 20  ? 48.563 -32.028 -13.776 1.00 18.74 ?  20  ASN   B O    1 
ATOM   4374 C CB   . ASN   B 1 20  ? 46.836 -34.234 -12.972 1.00 17.86 ?  20  ASN   B CB   1 
ATOM   4375 C CG   . ASN   B 1 20  ? 47.990 -34.929 -12.271 1.00 19.47 ?  20  ASN   B CG   1 
ATOM   4376 O OD1  . ASN   B 1 20  ? 48.669 -35.771 -12.869 1.00 21.68 ?  20  ASN   B OD1  1 
ATOM   4377 N ND2  . ASN   B 1 20  ? 48.207 -34.607 -11.003 1.00 19.30 ?  20  ASN   B ND2  1 
ATOM   4378 H H    . ASN   B 1 20  ? 45.476 -32.540 -14.107 1.00 18.59 ?  20  ASN   B H    1 
ATOM   4379 H HA   . ASN   B 1 20  ? 46.382 -32.765 -11.604 1.00 19.64 ?  20  ASN   B HA   1 
ATOM   4380 H HB2  . ASN   B 1 20  ? 46.032 -34.729 -12.770 1.00 21.44 ?  20  ASN   B HB2  1 
ATOM   4381 H HB3  . ASN   B 1 20  ? 47.011 -34.249 -13.925 1.00 21.44 ?  20  ASN   B HB3  1 
ATOM   4382 H HD21 . ASN   B 1 20  ? 48.859 -34.958 -10.569 1.00 23.16 ?  20  ASN   B HD21 1 
ATOM   4383 H HD22 . ASN   B 1 20  ? 47.707 -34.017 -10.611 1.00 23.16 ?  20  ASN   B HD22 1 
ATOM   4384 N N    . ALA   B 1 21  ? 48.254 -31.145 -11.725 1.00 16.04 ?  21  ALA   B N    1 
ATOM   4385 C CA   . ALA   B 1 21  ? 49.357 -30.207 -11.875 1.00 16.98 ?  21  ALA   B CA   1 
ATOM   4386 C C    . ALA   B 1 21  ? 49.821 -29.725 -10.509 1.00 16.08 ?  21  ALA   B C    1 
ATOM   4387 O O    . ALA   B 1 21  ? 49.074 -29.748 -9.527  1.00 16.10 ?  21  ALA   B O    1 
ATOM   4388 C CB   . ALA   B 1 21  ? 48.945 -29.021 -12.749 1.00 18.70 ?  21  ALA   B CB   1 
ATOM   4389 H H    . ALA   B 1 21  ? 47.871 -31.123 -10.952 1.00 19.24 ?  21  ALA   B H    1 
ATOM   4390 H HA   . ALA   B 1 21  ? 50.101 -30.656 -12.303 1.00 20.38 ?  21  ALA   B HA   1 
ATOM   4391 H HB1  . ALA   B 1 21  ? 49.723 -28.471 -12.909 1.00 22.44 ?  21  ALA   B HB1  1 
ATOM   4392 H HB2  . ALA   B 1 21  ? 48.599 -29.362 -13.589 1.00 22.44 ?  21  ALA   B HB2  1 
ATOM   4393 H HB3  . ALA   B 1 21  ? 48.257 -28.514 -12.291 1.00 22.44 ?  21  ALA   B HB3  1 
ATOM   4394 N N    . ASP   B 1 22  ? 51.082 -29.285 -10.483 1.00 15.44 ?  22  ASP   B N    1 
ATOM   4395 C CA   . ASP   B 1 22  ? 51.698 -28.595 -9.355  1.00 14.99 ?  22  ASP   B CA   1 
ATOM   4396 C C    . ASP   B 1 22  ? 51.290 -27.123 -9.426  1.00 13.91 ?  22  ASP   B C    1 
ATOM   4397 O O    . ASP   B 1 22  ? 51.605 -26.439 -10.403 1.00 14.35 ?  22  ASP   B O    1 
ATOM   4398 C CB   . ASP   B 1 22  ? 53.215 -28.773 -9.518  1.00 16.62 ?  22  ASP   B CB   1 
ATOM   4399 C CG   . ASP   B 1 22  ? 54.049 -28.035 -8.475  1.00 18.29 ?  22  ASP   B CG   1 
ATOM   4400 O OD1  . ASP   B 1 22  ? 53.684 -26.924 -8.059  1.00 18.42 ?  22  ASP   B OD1  1 
ATOM   4401 O OD2  . ASP   B 1 22  ? 55.117 -28.567 -8.096  1.00 20.79 -1 22  ASP   B OD2  1 
ATOM   4402 H H    . ASP   B 1 22  ? 51.627 -29.380 -11.147 1.00 18.53 ?  22  ASP   B H    1 
ATOM   4403 H HA   . ASP   B 1 22  ? 51.413 -28.983 -8.513  1.00 17.99 ?  22  ASP   B HA   1 
ATOM   4404 H HB2  . ASP   B 1 22  ? 53.436 -29.711 -9.456  1.00 19.95 ?  22  ASP   B HB2  1 
ATOM   4405 H HB3  . ASP   B 1 22  ? 53.481 -28.427 -10.386 1.00 19.95 ?  22  ASP   B HB3  1 
ATOM   4406 N N    . ILE   B 1 23  ? 50.573 -26.637 -8.404  1.00 13.26 ?  23  ILE   B N    1 
ATOM   4407 C CA   . ILE   B 1 23  ? 49.985 -25.292 -8.459  1.00 12.31 ?  23  ILE   B CA   1 
ATOM   4408 C C    . ILE   B 1 23  ? 51.045 -24.204 -8.593  1.00 12.22 ?  23  ILE   B C    1 
ATOM   4409 O O    . ILE   B 1 23  ? 50.786 -23.159 -9.198  1.00 12.19 ?  23  ILE   B O    1 
ATOM   4410 C CB   . ILE   B 1 23  ? 49.048 -25.053 -7.257  1.00 12.89 ?  23  ILE   B CB   1 
ATOM   4411 C CG1  . ILE   B 1 23  ? 48.222 -23.774 -7.446  1.00 13.29 ?  23  ILE   B CG1  1 
ATOM   4412 C CG2  . ILE   B 1 23  ? 49.822 -25.049 -5.946  1.00 14.00 ?  23  ILE   B CG2  1 
ATOM   4413 C CD1  . ILE   B 1 23  ? 47.100 -23.612 -6.440  1.00 14.64 ?  23  ILE   B CD1  1 
ATOM   4414 H H    . ILE   B 1 23  ? 50.411 -27.067 -7.677  1.00 15.92 ?  23  ILE   B H    1 
ATOM   4415 H HA   . ILE   B 1 23  ? 49.434 -25.247 -9.253  1.00 14.77 ?  23  ILE   B HA   1 
ATOM   4416 H HB   . ILE   B 1 23  ? 48.424 -25.796 -7.222  1.00 15.47 ?  23  ILE   B HB   1 
ATOM   4417 H HG12 . ILE   B 1 23  ? 48.819 -23.007 -7.353  1.00 15.95 ?  23  ILE   B HG12 1 
ATOM   4418 H HG13 . ILE   B 1 23  ? 47.837 -23.779 -8.332  1.00 15.95 ?  23  ILE   B HG13 1 
ATOM   4419 H HG21 . ILE   B 1 23  ? 49.196 -25.026 -5.207  1.00 16.80 ?  23  ILE   B HG21 1 
ATOM   4420 H HG22 . ILE   B 1 23  ? 50.361 -25.858 -5.895  1.00 16.80 ?  23  ILE   B HG22 1 
ATOM   4421 H HG23 . ILE   B 1 23  ? 50.398 -24.271 -5.920  1.00 16.80 ?  23  ILE   B HG23 1 
ATOM   4422 H HD11 . ILE   B 1 23  ? 46.594 -22.816 -6.664  1.00 17.56 ?  23  ILE   B HD11 1 
ATOM   4423 H HD12 . ILE   B 1 23  ? 46.530 -24.394 -6.484  1.00 17.56 ?  23  ILE   B HD12 1 
ATOM   4424 H HD13 . ILE   B 1 23  ? 47.481 -23.526 -5.553  1.00 17.56 ?  23  ILE   B HD13 1 
ATOM   4425 N N    . VAL   B 1 24  ? 52.241 -24.418 -8.034  1.00 12.43 ?  24  VAL   B N    1 
ATOM   4426 C CA   . VAL   B 1 24  ? 53.323 -23.441 -8.197  1.00 13.23 ?  24  VAL   B CA   1 
ATOM   4427 C C    . VAL   B 1 24  ? 53.777 -23.384 -9.650  1.00 13.42 ?  24  VAL   B C    1 
ATOM   4428 O O    . VAL   B 1 24  ? 53.922 -22.305 -10.239 1.00 13.92 ?  24  VAL   B O    1 
ATOM   4429 C CB   . VAL   B 1 24  ? 54.498 -23.765 -7.255  1.00 13.80 ?  24  VAL   B CB   1 
ATOM   4430 C CG1  . VAL   B 1 24  ? 55.708 -22.871 -7.564  1.00 14.78 ?  24  VAL   B CG1  1 
ATOM   4431 C CG2  . VAL   B 1 24  ? 54.069 -23.621 -5.808  1.00 15.26 ?  24  VAL   B CG2  1 
ATOM   4432 H H    . VAL   B 1 24  ? 52.447 -25.102 -7.561  1.00 14.92 ?  24  VAL   B H    1 
ATOM   4433 H HA   . VAL   B 1 24  ? 52.991 -22.563 -7.956  1.00 15.88 ?  24  VAL   B HA   1 
ATOM   4434 H HB   . VAL   B 1 24  ? 54.768 -24.688 -7.392  1.00 16.56 ?  24  VAL   B HB   1 
ATOM   4435 H HG11 . VAL   B 1 24  ? 56.281 -22.837 -6.781  1.00 17.74 ?  24  VAL   B HG11 1 
ATOM   4436 H HG12 . VAL   B 1 24  ? 56.196 -23.252 -8.310  1.00 17.74 ?  24  VAL   B HG12 1 
ATOM   4437 H HG13 . VAL   B 1 24  ? 55.396 -21.981 -7.784  1.00 17.74 ?  24  VAL   B HG13 1 
ATOM   4438 H HG21 . VAL   B 1 24  ? 54.802 -23.888 -5.231  1.00 18.32 ?  24  VAL   B HG21 1 
ATOM   4439 H HG22 . VAL   B 1 24  ? 53.837 -22.694 -5.640  1.00 18.32 ?  24  VAL   B HG22 1 
ATOM   4440 H HG23 . VAL   B 1 24  ? 53.299 -24.190 -5.647  1.00 18.32 ?  24  VAL   B HG23 1 
ATOM   4441 N N    . GLU   B 1 25  ? 54.041 -24.553 -10.240 1.00 14.54 ?  25  GLU   B N    1 
ATOM   4442 C CA   . GLU   B 1 25  ? 54.433 -24.593 -11.643 1.00 16.51 ?  25  GLU   B CA   1 
ATOM   4443 C C    . GLU   B 1 25  ? 53.334 -24.036 -12.531 1.00 14.97 ?  25  GLU   B C    1 
ATOM   4444 O O    . GLU   B 1 25  ? 53.610 -23.310 -13.493 1.00 15.59 ?  25  GLU   B O    1 
ATOM   4445 C CB   . GLU   B 1 25  ? 54.802 -26.020 -12.046 1.00 21.73 ?  25  GLU   B CB   1 
ATOM   4446 C CG   . GLU   B 1 25  ? 56.084 -26.503 -11.391 1.00 28.33 ?  25  GLU   B CG   1 
ATOM   4447 C CD   . GLU   B 1 25  ? 57.223 -25.502 -11.494 1.00 34.28 ?  25  GLU   B CD   1 
ATOM   4448 O OE1  . GLU   B 1 25  ? 57.521 -25.043 -12.617 1.00 36.60 ?  25  GLU   B OE1  1 
ATOM   4449 O OE2  . GLU   B 1 25  ? 57.809 -25.159 -10.443 1.00 36.68 -1 25  GLU   B OE2  1 
ATOM   4450 H H    . GLU   B 1 25  ? 53.995 -25.321 -9.854  1.00 17.44 ?  25  GLU   B H    1 
ATOM   4451 H HA   . GLU   B 1 25  ? 55.198 -24.021 -11.769 1.00 19.82 ?  25  GLU   B HA   1 
ATOM   4452 H HB2  . GLU   B 1 25  ? 54.086 -26.622 -11.778 1.00 26.07 ?  25  GLU   B HB2  1 
ATOM   4453 H HB3  . GLU   B 1 25  ? 54.920 -26.057 -13.008 1.00 26.07 ?  25  GLU   B HB3  1 
ATOM   4454 H HG2  . GLU   B 1 25  ? 55.923 -26.645 -10.451 1.00 33.99 ?  25  GLU   B HG2  1 
ATOM   4455 H HG3  . GLU   B 1 25  ? 56.363 -27.325 -11.820 1.00 33.99 ?  25  GLU   B HG3  1 
ATOM   4456 N N    . GLU   B 1 26  ? 52.078 -24.348 -12.207 1.00 14.08 ?  26  GLU   B N    1 
ATOM   4457 C CA   . GLU   B 1 26  ? 50.955 -23.811 -12.967 1.00 14.49 ?  26  GLU   B CA   1 
ATOM   4458 C C    . GLU   B 1 26  ? 50.910 -22.292 -12.878 1.00 13.75 ?  26  GLU   B C    1 
ATOM   4459 O O    . GLU   B 1 26  ? 50.723 -21.605 -13.888 1.00 14.89 ?  26  GLU   B O    1 
ATOM   4460 C CB   . GLU   B 1 26  ? 49.640 -24.397 -12.452 1.00 16.15 ?  26  GLU   B CB   1 
ATOM   4461 C CG   . GLU   B 1 26  ? 49.218 -25.689 -13.117 1.00 19.85 ?  26  GLU   B CG   1 
ATOM   4462 C CD   . GLU   B 1 26  ? 48.973 -25.555 -14.614 1.00 21.48 ?  26  GLU   B CD   1 
ATOM   4463 O OE1  . GLU   B 1 26  ? 48.005 -24.886 -15.038 1.00 21.57 ?  26  GLU   B OE1  1 
ATOM   4464 O OE2  . GLU   B 1 26  ? 49.753 -26.151 -15.369 1.00 23.76 -1 26  GLU   B OE2  1 
ATOM   4465 H H    . GLU   B 1 26  ? 51.845 -24.864 -11.550 1.00 16.90 ?  26  GLU   B H    1 
ATOM   4466 H HA   . GLU   B 1 26  ? 51.054 -24.055 -13.897 1.00 17.39 ?  26  GLU   B HA   1 
ATOM   4467 H HB2  . GLU   B 1 26  ? 49.727 -24.575 -11.501 1.00 19.38 ?  26  GLU   B HB2  1 
ATOM   4468 H HB3  . GLU   B 1 26  ? 48.931 -23.747 -12.594 1.00 19.38 ?  26  GLU   B HB3  1 
ATOM   4469 H HG2  . GLU   B 1 26  ? 49.923 -26.334 -12.999 1.00 23.83 ?  26  GLU   B HG2  1 
ATOM   4470 H HG3  . GLU   B 1 26  ? 48.397 -26.000 -12.707 1.00 23.83 ?  26  GLU   B HG3  1 
ATOM   4471 N N    . ALA   B 1 27  ? 51.062 -21.747 -11.669 1.00 13.03 ?  27  ALA   B N    1 
ATOM   4472 C CA   . ALA   B 1 27  ? 51.024 -20.296 -11.517 1.00 13.50 ?  27  ALA   B CA   1 
ATOM   4473 C C    . ALA   B 1 27  ? 52.103 -19.632 -12.362 1.00 14.27 ?  27  ALA   B C    1 
ATOM   4474 O O    . ALA   B 1 27  ? 51.851 -18.623 -13.038 1.00 15.30 ?  27  ALA   B O    1 
ATOM   4475 C CB   . ALA   B 1 27  ? 51.158 -19.917 -10.041 1.00 13.85 ?  27  ALA   B CB   1 
ATOM   4476 H H    . ALA   B 1 27  ? 51.187 -22.186 -10.938 1.00 15.64 ?  27  ALA   B H    1 
ATOM   4477 H HA   . ALA   B 1 27  ? 50.171 -19.972 -11.829 1.00 16.20 ?  27  ALA   B HA   1 
ATOM   4478 H HB1  . ALA   B 1 27  ? 51.119 -18.952 -9.958  1.00 16.62 ?  27  ALA   B HB1  1 
ATOM   4479 H HB2  . ALA   B 1 27  ? 50.420 -20.318 -9.548  1.00 16.62 ?  27  ALA   B HB2  1 
ATOM   4480 H HB3  . ALA   B 1 27  ? 52.000 -20.248 -9.700  1.00 16.62 ?  27  ALA   B HB3  1 
ATOM   4481 N N    . LYS   B 1 28  ? 53.312 -20.190 -12.350 1.00 15.41 ?  28  LYS   B N    1 
ATOM   4482 C CA   . LYS   B 1 28  ? 54.395 -19.582 -13.109 1.00 17.67 ?  28  LYS   B CA   1 
ATOM   4483 C C    . LYS   B 1 28  ? 54.142 -19.649 -14.608 1.00 18.13 ?  28  LYS   B C    1 
ATOM   4484 O O    . LYS   B 1 28  ? 54.571 -18.752 -15.345 1.00 19.17 ?  28  LYS   B O    1 
ATOM   4485 C CB   . LYS   B 1 28  ? 55.742 -20.205 -12.722 1.00 20.63 ?  28  LYS   B CB   1 
ATOM   4486 C CG   . LYS   B 1 28  ? 56.156 -19.866 -11.290 1.00 23.91 ?  28  LYS   B CG   1 
ATOM   4487 C CD   . LYS   B 1 28  ? 57.554 -20.352 -10.937 1.00 28.45 ?  28  LYS   B CD   1 
ATOM   4488 C CE   . LYS   B 1 28  ? 57.584 -21.838 -10.659 1.00 32.78 ?  28  LYS   B CE   1 
ATOM   4489 N NZ   . LYS   B 1 28  ? 58.918 -22.271 -10.147 1.00 34.26 ?  28  LYS   B NZ   1 
ATOM   4490 H H    . LYS   B 1 28  ? 53.532 -20.902 -11.919 1.00 18.50 ?  28  LYS   B H    1 
ATOM   4491 H HA   . LYS   B 1 28  ? 54.445 -18.645 -12.881 1.00 21.20 ?  28  LYS   B HA   1 
ATOM   4492 H HB2  . LYS   B 1 28  ? 55.683 -21.169 -12.793 1.00 24.76 ?  28  LYS   B HB2  1 
ATOM   4493 H HB3  . LYS   B 1 28  ? 56.434 -19.870 -13.318 1.00 24.76 ?  28  LYS   B HB3  1 
ATOM   4494 H HG2  . LYS   B 1 28  ? 56.136 -18.900 -11.182 1.00 28.69 ?  28  LYS   B HG2  1 
ATOM   4495 H HG3  . LYS   B 1 28  ? 55.528 -20.278 -10.679 1.00 28.69 ?  28  LYS   B HG3  1 
ATOM   4496 H HD2  . LYS   B 1 28  ? 58.151 -20.168 -11.679 1.00 34.14 ?  28  LYS   B HD2  1 
ATOM   4497 H HD3  . LYS   B 1 28  ? 57.858 -19.886 -10.141 1.00 34.14 ?  28  LYS   B HD3  1 
ATOM   4498 H HE2  . LYS   B 1 28  ? 56.916 -22.051 -9.989  1.00 39.34 ?  28  LYS   B HE2  1 
ATOM   4499 H HE3  . LYS   B 1 28  ? 57.402 -22.322 -11.479 1.00 39.34 ?  28  LYS   B HE3  1 
ATOM   4500 H HZ1  . LYS   B 1 28  ? 58.914 -23.147 -9.989  1.00 41.12 ?  28  LYS   B HZ1  1 
ATOM   4501 H HZ2  . LYS   B 1 28  ? 59.548 -22.087 -10.747 1.00 41.12 ?  28  LYS   B HZ2  1 
ATOM   4502 H HZ3  . LYS   B 1 28  ? 59.106 -21.842 -9.389  1.00 41.12 ?  28  LYS   B HZ3  1 
ATOM   4503 N N    . LYS   B 1 29  ? 53.435 -20.676 -15.077 1.00 19.23 ?  29  LYS   B N    1 
ATOM   4504 C CA   . LYS   B 1 29  ? 53.161 -20.803 -16.503 1.00 21.95 ?  29  LYS   B CA   1 
ATOM   4505 C C    . LYS   B 1 29  ? 51.917 -20.033 -16.934 1.00 20.82 ?  29  LYS   B C    1 
ATOM   4506 O O    . LYS   B 1 29  ? 51.925 -19.389 -17.990 1.00 22.07 ?  29  LYS   B O    1 
ATOM   4507 C CB   . LYS   B 1 29  ? 53.028 -22.279 -16.886 1.00 26.77 ?  29  LYS   B CB   1 
ATOM   4508 C CG   . LYS   B 1 29  ? 52.743 -22.510 -18.359 1.00 31.00 ?  29  LYS   B CG   1 
ATOM   4509 C CD   . LYS   B 1 29  ? 52.981 -23.962 -18.752 1.00 34.44 ?  29  LYS   B CD   1 
ATOM   4510 C CE   . LYS   B 1 29  ? 51.912 -24.888 -18.195 1.00 37.05 ?  29  LYS   B CE   1 
ATOM   4511 N NZ   . LYS   B 1 29  ? 52.144 -26.305 -18.606 1.00 38.52 ?  29  LYS   B NZ   1 
ATOM   4512 H H    . LYS   B 1 29  ? 53.098 -21.310 -14.589 1.00 23.08 ?  29  LYS   B H    1 
ATOM   4513 H HA   . LYS   B 1 29  ? 53.911 -20.441 -16.992 1.00 26.34 ?  29  LYS   B HA   1 
ATOM   4514 H HB2  . LYS   B 1 29  ? 53.862 -22.731 -16.676 1.00 32.13 ?  29  LYS   B HB2  1 
ATOM   4515 H HB3  . LYS   B 1 29  ? 52.304 -22.674 -16.381 1.00 32.13 ?  29  LYS   B HB3  1 
ATOM   4516 H HG2  . LYS   B 1 29  ? 51.815 -22.292 -18.541 1.00 37.20 ?  29  LYS   B HG2  1 
ATOM   4517 H HG3  . LYS   B 1 29  ? 53.330 -21.949 -18.890 1.00 37.20 ?  29  LYS   B HG3  1 
ATOM   4518 H HD2  . LYS   B 1 29  ? 52.970 -24.035 -19.718 1.00 41.33 ?  29  LYS   B HD2  1 
ATOM   4519 H HD3  . LYS   B 1 29  ? 53.840 -24.250 -18.404 1.00 41.33 ?  29  LYS   B HD3  1 
ATOM   4520 H HE2  . LYS   B 1 29  ? 51.924 -24.848 -17.226 1.00 44.47 ?  29  LYS   B HE2  1 
ATOM   4521 H HE3  . LYS   B 1 29  ? 51.044 -24.614 -18.531 1.00 44.47 ?  29  LYS   B HE3  1 
ATOM   4522 H HZ1  . LYS   B 1 29  ? 51.507 -26.828 -18.270 1.00 46.22 ?  29  LYS   B HZ1  1 
ATOM   4523 H HZ2  . LYS   B 1 29  ? 52.133 -26.370 -19.494 1.00 46.22 ?  29  LYS   B HZ2  1 
ATOM   4524 H HZ3  . LYS   B 1 29  ? 52.935 -26.583 -18.306 1.00 46.22 ?  29  LYS   B HZ3  1 
ATOM   4525 N N    . VAL   B 1 30  ? 50.850 -20.093 -16.132 1.00 19.76 ?  30  VAL   B N    1 
ATOM   4526 C CA   . VAL   B 1 30  ? 49.563 -19.498 -16.500 1.00 20.08 ?  30  VAL   B CA   1 
ATOM   4527 C C    . VAL   B 1 30  ? 49.570 -17.984 -16.340 1.00 19.49 ?  30  VAL   B C    1 
ATOM   4528 O O    . VAL   B 1 30  ? 48.826 -17.272 -17.032 1.00 20.43 ?  30  VAL   B O    1 
ATOM   4529 C CB   . VAL   B 1 30  ? 48.453 -20.124 -15.631 1.00 21.36 ?  30  VAL   B CB   1 
ATOM   4530 C CG1  . VAL   B 1 30  ? 47.160 -19.321 -15.718 1.00 21.83 ?  30  VAL   B CG1  1 
ATOM   4531 C CG2  . VAL   B 1 30  ? 48.215 -21.577 -16.025 1.00 22.27 ?  30  VAL   B CG2  1 
ATOM   4532 H H    . VAL   B 1 30  ? 50.837 -20.501 -15.361 1.00 23.71 ?  30  VAL   B H    1 
ATOM   4533 H HA   . VAL   B 1 30  ? 49.367 -19.721 -17.422 1.00 24.10 ?  30  VAL   B HA   1 
ATOM   4534 H HB   . VAL   B 1 30  ? 48.734 -20.121 -14.701 1.00 25.63 ?  30  VAL   B HB   1 
ATOM   4535 H HG11 . VAL   B 1 30  ? 46.418 -19.904 -15.488 1.00 26.20 ?  30  VAL   B HG11 1 
ATOM   4536 H HG12 . VAL   B 1 30  ? 47.200 -18.583 -15.092 1.00 26.20 ?  30  VAL   B HG12 1 
ATOM   4537 H HG13 . VAL   B 1 30  ? 47.047 -18.998 -16.620 1.00 26.20 ?  30  VAL   B HG13 1 
ATOM   4538 H HG21 . VAL   B 1 30  ? 47.520 -21.955 -15.457 1.00 26.73 ?  30  VAL   B HG21 1 
ATOM   4539 H HG22 . VAL   B 1 30  ? 47.930 -21.610 -16.953 1.00 26.73 ?  30  VAL   B HG22 1 
ATOM   4540 H HG23 . VAL   B 1 30  ? 49.038 -22.074 -15.913 1.00 26.73 ?  30  VAL   B HG23 1 
ATOM   4541 N N    . LYS   B 1 31  ? 50.361 -17.486 -15.400 1.00 19.21 ?  31  LYS   B N    1 
ATOM   4542 C CA   . LYS   B 1 31  ? 50.363 -16.079 -15.021 1.00 19.98 ?  31  LYS   B CA   1 
ATOM   4543 C C    . LYS   B 1 31  ? 48.954 -15.607 -14.644 1.00 17.22 ?  31  LYS   B C    1 
ATOM   4544 O O    . LYS   B 1 31  ? 48.408 -14.695 -15.271 1.00 18.04 ?  31  LYS   B O    1 
ATOM   4545 C CB   . LYS   B 1 31  ? 50.971 -15.221 -16.123 1.00 23.41 ?  31  LYS   B CB   1 
ATOM   4546 C CG   . LYS   B 1 31  ? 52.388 -15.664 -16.491 1.00 27.30 ?  31  LYS   B CG   1 
ATOM   4547 C CD   . LYS   B 1 31  ? 52.928 -14.915 -17.692 1.00 31.07 ?  31  LYS   B CD   1 
ATOM   4548 C CE   . LYS   B 1 31  ? 54.407 -15.180 -17.877 1.00 34.23 ?  31  LYS   B CE   1 
ATOM   4549 N NZ   . LYS   B 1 31  ? 55.198 -14.720 -16.700 1.00 35.55 ?  31  LYS   B NZ   1 
ATOM   4550 H H    . LYS   B 1 31  ? 50.927 -17.969 -14.966 1.00 23.05 ?  31  LYS   B H    1 
ATOM   4551 H HA   . LYS   B 1 31  ? 50.913 -15.992 -14.240 1.00 23.98 ?  31  LYS   B HA   1 
ATOM   4552 H HB2  . LYS   B 1 31  ? 50.418 -15.286 -16.919 1.00 28.09 ?  31  LYS   B HB2  1 
ATOM   4553 H HB3  . LYS   B 1 31  ? 51.008 -14.307 -15.813 1.00 28.09 ?  31  LYS   B HB3  1 
ATOM   4554 H HG2  . LYS   B 1 31  ? 52.971 -15.498 -15.736 1.00 32.77 ?  31  LYS   B HG2  1 
ATOM   4555 H HG3  . LYS   B 1 31  ? 52.381 -16.612 -16.704 1.00 32.77 ?  31  LYS   B HG3  1 
ATOM   4556 H HD2  . LYS   B 1 31  ? 52.458 -15.214 -18.488 1.00 37.28 ?  31  LYS   B HD2  1 
ATOM   4557 H HD3  . LYS   B 1 31  ? 52.796 -13.965 -17.559 1.00 37.28 ?  31  LYS   B HD3  1 
ATOM   4558 H HE2  . LYS   B 1 31  ? 54.551 -16.134 -17.986 1.00 41.07 ?  31  LYS   B HE2  1 
ATOM   4559 H HE3  . LYS   B 1 31  ? 54.720 -14.702 -18.660 1.00 41.07 ?  31  LYS   B HE3  1 
ATOM   4560 H HZ1  . LYS   B 1 31  ? 56.067 -14.769 -16.880 1.00 42.67 ?  31  LYS   B HZ1  1 
ATOM   4561 H HZ2  . LYS   B 1 31  ? 54.989 -13.877 -16.505 1.00 42.67 ?  31  LYS   B HZ2  1 
ATOM   4562 H HZ3  . LYS   B 1 31  ? 55.019 -15.231 -15.993 1.00 42.67 ?  31  LYS   B HZ3  1 
ATOM   4563 N N    . PRO   B 1 32  ? 48.343 -16.213 -13.618 1.00 14.48 ?  32  PRO   B N    1 
ATOM   4564 C CA   . PRO   B 1 32  ? 46.960 -15.864 -13.273 1.00 13.59 ?  32  PRO   B CA   1 
ATOM   4565 C C    . PRO   B 1 32  ? 46.871 -14.518 -12.574 1.00 13.60 ?  32  PRO   B C    1 
ATOM   4566 O O    . PRO   B 1 32  ? 47.790 -14.090 -11.869 1.00 14.88 ?  32  PRO   B O    1 
ATOM   4567 C CB   . PRO   B 1 32  ? 46.556 -16.982 -12.307 1.00 13.73 ?  32  PRO   B CB   1 
ATOM   4568 C CG   . PRO   B 1 32  ? 47.844 -17.331 -11.623 1.00 14.15 ?  32  PRO   B CG   1 
ATOM   4569 C CD   . PRO   B 1 32  ? 48.900 -17.218 -12.686 1.00 14.16 ?  32  PRO   B CD   1 
ATOM   4570 H HA   . PRO   B 1 32  ? 46.382 -15.882 -14.057 1.00 16.31 ?  32  PRO   B HA   1 
ATOM   4571 H HB2  . PRO   B 1 32  ? 45.907 -16.647 -11.669 1.00 16.47 ?  32  PRO   B HB2  1 
ATOM   4572 H HB3  . PRO   B 1 32  ? 46.209 -17.740 -12.797 1.00 16.47 ?  32  PRO   B HB3  1 
ATOM   4573 H HG2  . PRO   B 1 32  ? 48.018 -16.702 -10.900 1.00 16.98 ?  32  PRO   B HG2  1 
ATOM   4574 H HG3  . PRO   B 1 32  ? 47.801 -18.238 -11.279 1.00 16.98 ?  32  PRO   B HG3  1 
ATOM   4575 H HD2  . PRO   B 1 32  ? 49.729 -16.889 -12.306 1.00 16.99 ?  32  PRO   B HD2  1 
ATOM   4576 H HD3  . PRO   B 1 32  ? 49.022 -18.069 -13.130 1.00 16.99 ?  32  PRO   B HD3  1 
ATOM   4577 N N    . THR   B 1 33  ? 45.720 -13.867 -12.748 1.00 13.04 ?  33  THR   B N    1 
ATOM   4578 C CA   . THR   B 1 33  ? 45.421 -12.691 -11.941 1.00 13.26 ?  33  THR   B CA   1 
ATOM   4579 C C    . THR   B 1 33  ? 45.367 -13.041 -10.459 1.00 12.99 ?  33  THR   B C    1 
ATOM   4580 O O    . THR   B 1 33  ? 45.834 -12.260 -9.613  1.00 13.78 ?  33  THR   B O    1 
ATOM   4581 C CB   . THR   B 1 33  ? 44.104 -12.065 -12.401 1.00 13.99 ?  33  THR   B CB   1 
ATOM   4582 O OG1  . THR   B 1 33  ? 44.159 -11.812 -13.806 1.00 14.12 ?  33  THR   B OG1  1 
ATOM   4583 C CG2  . THR   B 1 33  ? 43.838 -10.767 -11.661 1.00 15.27 ?  33  THR   B CG2  1 
ATOM   4584 H H    . THR   B 1 33  ? 45.108 -14.086 -13.315 1.00 15.65 ?  33  THR   B H    1 
ATOM   4585 H HA   . THR   B 1 33  ? 46.120 -12.039 -12.066 1.00 15.92 ?  33  THR   B HA   1 
ATOM   4586 H HB   . THR   B 1 33  ? 43.371 -12.679 -12.212 1.00 16.78 ?  33  THR   B HB   1 
ATOM   4587 H HG1  . THR   B 1 33  ? 43.443 -11.444 -14.062 1.00 16.94 ?  33  THR   B HG1  1 
ATOM   4588 H HG21 . THR   B 1 33  ? 43.086 -10.308 -12.058 1.00 18.32 ?  33  THR   B HG21 1 
ATOM   4589 H HG22 . THR   B 1 33  ? 43.643 -10.949 -10.728 1.00 18.32 ?  33  THR   B HG22 1 
ATOM   4590 H HG23 . THR   B 1 33  ? 44.622 -10.196 -11.713 1.00 18.32 ?  33  THR   B HG23 1 
ATOM   4591 N N    . VAL   B 1 34  ? 44.818 -14.216 -10.124 1.00 12.32 ?  34  VAL   B N    1 
ATOM   4592 C CA   . VAL   B 1 34  ? 44.623 -14.613 -8.733  1.00 11.72 ?  34  VAL   B CA   1 
ATOM   4593 C C    . VAL   B 1 34  ? 45.052 -16.062 -8.568  1.00 10.65 ?  34  VAL   B C    1 
ATOM   4594 O O    . VAL   B 1 34  ? 44.536 -16.948 -9.260  1.00 11.33 ?  34  VAL   B O    1 
ATOM   4595 C CB   . VAL   B 1 34  ? 43.152 -14.474 -8.285  1.00 12.48 ?  34  VAL   B CB   1 
ATOM   4596 C CG1  . VAL   B 1 34  ? 42.997 -14.931 -6.842  1.00 13.10 ?  34  VAL   B CG1  1 
ATOM   4597 C CG2  . VAL   B 1 34  ? 42.648 -13.049 -8.466  1.00 14.03 ?  34  VAL   B CG2  1 
ATOM   4598 H H    . VAL   B 1 34  ? 44.558 -14.811 -10.688 1.00 14.78 ?  34  VAL   B H    1 
ATOM   4599 H HA   . VAL   B 1 34  ? 45.171 -14.052 -8.153  1.00 14.06 ?  34  VAL   B HA   1 
ATOM   4600 H HB   . VAL   B 1 34  ? 42.601 -15.046 -8.841  1.00 14.97 ?  34  VAL   B HB   1 
ATOM   4601 H HG11 . VAL   B 1 34  ? 42.145 -14.605 -6.499  1.00 15.72 ?  34  VAL   B HG11 1 
ATOM   4602 H HG12 . VAL   B 1 34  ? 43.010 -15.898 -6.813  1.00 15.72 ?  34  VAL   B HG12 1 
ATOM   4603 H HG13 . VAL   B 1 34  ? 43.721 -14.566 -6.315  1.00 15.72 ?  34  VAL   B HG13 1 
ATOM   4604 H HG21 . VAL   B 1 34  ? 41.725 -12.996 -8.162  1.00 16.84 ?  34  VAL   B HG21 1 
ATOM   4605 H HG22 . VAL   B 1 34  ? 43.201 -12.446 -7.949  1.00 16.84 ?  34  VAL   B HG22 1 
ATOM   4606 H HG23 . VAL   B 1 34  ? 42.692 -12.813 -9.409  1.00 16.84 ?  34  VAL   B HG23 1 
ATOM   4607 N N    . VAL   B 1 35  ? 45.961 -16.309 -7.628  1.00 10.17 ?  35  VAL   B N    1 
ATOM   4608 C CA   . VAL   B 1 35  ? 46.205 -17.653 -7.112  1.00 9.94  ?  35  VAL   B CA   1 
ATOM   4609 C C    . VAL   B 1 35  ? 45.660 -17.714 -5.693  1.00 9.59  ?  35  VAL   B C    1 
ATOM   4610 O O    . VAL   B 1 35  ? 45.872 -16.791 -4.897  1.00 10.36 ?  35  VAL   B O    1 
ATOM   4611 C CB   . VAL   B 1 35  ? 47.686 -18.074 -7.198  1.00 10.60 ?  35  VAL   B CB   1 
ATOM   4612 C CG1  . VAL   B 1 35  ? 48.582 -17.254 -6.272  1.00 11.13 ?  35  VAL   B CG1  1 
ATOM   4613 C CG2  . VAL   B 1 35  ? 47.825 -19.577 -6.894  1.00 11.41 ?  35  VAL   B CG2  1 
ATOM   4614 H H    . VAL   B 1 35  ? 46.447 -15.701 -7.252  1.00 12.21 ?  35  VAL   B H    1 
ATOM   4615 H HA   . VAL   B 1 35  ? 45.690 -18.280 -7.645  1.00 11.93 ?  35  VAL   B HA   1 
ATOM   4616 H HB   . VAL   B 1 35  ? 47.996 -17.945 -8.108  1.00 12.72 ?  35  VAL   B HB   1 
ATOM   4617 H HG11 . VAL   B 1 35  ? 49.506 -17.483 -6.453  1.00 13.36 ?  35  VAL   B HG11 1 
ATOM   4618 H HG12 . VAL   B 1 35  ? 48.422 -16.321 -6.440  1.00 13.36 ?  35  VAL   B HG12 1 
ATOM   4619 H HG13 . VAL   B 1 35  ? 48.361 -17.477 -5.352  1.00 13.36 ?  35  VAL   B HG13 1 
ATOM   4620 H HG21 . VAL   B 1 35  ? 48.751 -19.845 -6.995  1.00 13.69 ?  35  VAL   B HG21 1 
ATOM   4621 H HG22 . VAL   B 1 35  ? 47.533 -19.749 -5.980  1.00 13.69 ?  35  VAL   B HG22 1 
ATOM   4622 H HG23 . VAL   B 1 35  ? 47.268 -20.087 -7.509  1.00 13.69 ?  35  VAL   B HG23 1 
ATOM   4623 N N    . VAL   B 1 36  ? 44.945 -18.796 -5.383  1.00 9.79  ?  36  VAL   B N    1 
ATOM   4624 C CA   . VAL   B 1 36  ? 44.389 -19.000 -4.056  1.00 9.49  ?  36  VAL   B CA   1 
ATOM   4625 C C    . VAL   B 1 36  ? 45.389 -19.766 -3.201  1.00 9.32  ?  36  VAL   B C    1 
ATOM   4626 O O    . VAL   B 1 36  ? 45.940 -20.793 -3.627  1.00 10.41 ?  36  VAL   B O    1 
ATOM   4627 C CB   . VAL   B 1 36  ? 43.053 -19.757 -4.133  1.00 9.87  ?  36  VAL   B CB   1 
ATOM   4628 C CG1  . VAL   B 1 36  ? 42.557 -20.120 -2.739  1.00 10.48 ?  36  VAL   B CG1  1 
ATOM   4629 C CG2  . VAL   B 1 36  ? 42.022 -18.937 -4.890  1.00 10.78 ?  36  VAL   B CG2  1 
ATOM   4630 H H    . VAL   B 1 36  ? 44.769 -19.434 -5.936  1.00 11.75 ?  36  VAL   B H    1 
ATOM   4631 H HA   . VAL   B 1 36  ? 44.224 -18.141 -3.640  1.00 11.39 ?  36  VAL   B HA   1 
ATOM   4632 H HB   . VAL   B 1 36  ? 43.189 -20.585 -4.620  1.00 11.85 ?  36  VAL   B HB   1 
ATOM   4633 H HG11 . VAL   B 1 36  ? 41.613 -20.330 -2.787  1.00 12.57 ?  36  VAL   B HG11 1 
ATOM   4634 H HG12 . VAL   B 1 36  ? 43.054 -20.878 -2.410  1.00 12.57 ?  36  VAL   B HG12 1 
ATOM   4635 H HG13 . VAL   B 1 36  ? 42.690 -19.351 -2.153  1.00 12.57 ?  36  VAL   B HG13 1 
ATOM   4636 H HG21 . VAL   B 1 36  ? 41.185 -19.429 -4.910  1.00 12.94 ?  36  VAL   B HG21 1 
ATOM   4637 H HG22 . VAL   B 1 36  ? 41.903 -18.091 -4.442  1.00 12.94 ?  36  VAL   B HG22 1 
ATOM   4638 H HG23 . VAL   B 1 36  ? 42.341 -18.796 -5.797  1.00 12.94 ?  36  VAL   B HG23 1 
ATOM   4639 N N    . ASN   B 1 37  ? 45.613 -19.270 -1.987  1.00 9.42  ?  37  ASN   B N    1 
ATOM   4640 C CA   . ASN   B 1 37  ? 46.364 -19.990 -0.976  1.00 9.71  ?  37  ASN   B CA   1 
ATOM   4641 C C    . ASN   B 1 37  ? 45.406 -20.657 0.002   1.00 9.71  ?  37  ASN   B C    1 
ATOM   4642 O O    . ASN   B 1 37  ? 44.396 -20.077 0.409   1.00 10.56 ?  37  ASN   B O    1 
ATOM   4643 C CB   . ASN   B 1 37  ? 47.293 -19.042 -0.216  1.00 10.14 ?  37  ASN   B CB   1 
ATOM   4644 C CG   . ASN   B 1 37  ? 48.149 -19.761 0.799   1.00 10.31 ?  37  ASN   B CG   1 
ATOM   4645 O OD1  . ASN   B 1 37  ? 48.480 -20.937 0.629   1.00 11.08 ?  37  ASN   B OD1  1 
ATOM   4646 N ND2  . ASN   B 1 37  ? 48.493 -19.073 1.872   1.00 10.50 ?  37  ASN   B ND2  1 
ATOM   4647 H H    . ASN   B 1 37  ? 45.331 -18.500 -1.720  1.00 11.31 ?  37  ASN   B H    1 
ATOM   4648 H HA   . ASN   B 1 37  ? 46.901 -20.680 -1.392  1.00 11.65 ?  37  ASN   B HA   1 
ATOM   4649 H HB2  . ASN   B 1 37  ? 47.884 -18.609 -0.846  1.00 12.17 ?  37  ASN   B HB2  1 
ATOM   4650 H HB3  . ASN   B 1 37  ? 46.761 -18.382 0.257   1.00 12.17 ?  37  ASN   B HB3  1 
ATOM   4651 H HD21 . ASN   B 1 37  ? 48.989 -19.437 2.472   1.00 12.60 ?  37  ASN   B HD21 1 
ATOM   4652 H HD22 . ASN   B 1 37  ? 48.256 -18.255 1.954   1.00 12.60 ?  37  ASN   B HD22 1 
ATOM   4653 N N    . ALA   B 1 38  ? 45.760 -21.889 0.385   1.00 10.10 ?  38  ALA   B N    1 
ATOM   4654 C CA   . ALA   B 1 38  ? 45.098 -22.643 1.455   1.00 10.34 ?  38  ALA   B CA   1 
ATOM   4655 C C    . ALA   B 1 38  ? 45.679 -22.161 2.783   1.00 10.28 ?  38  ALA   B C    1 
ATOM   4656 O O    . ALA   B 1 38  ? 46.583 -22.770 3.368   1.00 11.25 ?  38  ALA   B O    1 
ATOM   4657 C CB   . ALA   B 1 38  ? 45.326 -24.138 1.262   1.00 11.42 ?  38  ALA   B CB   1 
ATOM   4658 H H    . ALA   B 1 38  ? 46.409 -22.328 0.028   1.00 12.11 ?  38  ALA   B H    1 
ATOM   4659 H HA   . ALA   B 1 38  ? 44.146 -22.465 1.446   1.00 12.40 ?  38  ALA   B HA   1 
ATOM   4660 H HB1  . ALA   B 1 38  ? 44.878 -24.622 1.981   1.00 13.70 ?  38  ALA   B HB1  1 
ATOM   4661 H HB2  . ALA   B 1 38  ? 44.954 -24.409 0.409   1.00 13.70 ?  38  ALA   B HB2  1 
ATOM   4662 H HB3  . ALA   B 1 38  ? 46.276 -24.324 1.286   1.00 13.70 ?  38  ALA   B HB3  1 
ATOM   4663 N N    . ALA   B 1 39  ? 45.169 -21.018 3.239   1.00 10.04 ?  39  ALA   B N    1 
ATOM   4664 C CA   . ALA   B 1 39  ? 45.709 -20.285 4.370   1.00 10.73 ?  39  ALA   B CA   1 
ATOM   4665 C C    . ALA   B 1 39  ? 45.087 -20.732 5.692   1.00 10.89 ?  39  ALA   B C    1 
ATOM   4666 O O    . ALA   B 1 39  ? 44.050 -21.398 5.734   1.00 11.68 ?  39  ALA   B O    1 
ATOM   4667 C CB   . ALA   B 1 39  ? 45.473 -18.783 4.180   1.00 11.16 ?  39  ALA   B CB   1 
ATOM   4668 H H    . ALA   B 1 39  ? 44.486 -20.633 2.882   1.00 12.05 ?  39  ALA   B H    1 
ATOM   4669 H HA   . ALA   B 1 39  ? 46.664 -20.434 4.419   1.00 12.88 ?  39  ALA   B HA   1 
ATOM   4670 H HB1  . ALA   B 1 39  ? 45.837 -18.305 4.941   1.00 13.39 ?  39  ALA   B HB1  1 
ATOM   4671 H HB2  . ALA   B 1 39  ? 45.920 -18.492 3.365   1.00 13.39 ?  39  ALA   B HB2  1 
ATOM   4672 H HB3  . ALA   B 1 39  ? 44.521 -18.615 4.107   1.00 13.39 ?  39  ALA   B HB3  1 
ATOM   4673 N N    . ASN   B 1 40  ? 45.734 -20.327 6.783   1.00 11.77 ?  40  ASN   B N    1 
ATOM   4674 C CA   . ASN   B 1 40  ? 45.169 -20.362 8.123   1.00 12.44 ?  40  ASN   B CA   1 
ATOM   4675 C C    . ASN   B 1 40  ? 44.990 -18.934 8.646   1.00 11.87 ?  40  ASN   B C    1 
ATOM   4676 O O    . ASN   B 1 40  ? 45.405 -17.956 8.014   1.00 11.90 ?  40  ASN   B O    1 
ATOM   4677 C CB   . ASN   B 1 40  ? 46.006 -21.244 9.060   1.00 12.86 ?  40  ASN   B CB   1 
ATOM   4678 C CG   . ASN   B 1 40  ? 47.460 -20.839 9.100   1.00 14.02 ?  40  ASN   B CG   1 
ATOM   4679 O OD1  . ASN   B 1 40  ? 47.777 -19.657 9.168   1.00 16.22 ?  40  ASN   B OD1  1 
ATOM   4680 N ND2  . ASN   B 1 40  ? 48.356 -21.816 9.048   1.00 14.46 ?  40  ASN   B ND2  1 
ATOM   4681 H H    . ASN   B 1 40  ? 46.538 -20.020 6.760   1.00 14.13 ?  40  ASN   B H    1 
ATOM   4682 H HA   . ASN   B 1 40  ? 44.288 -20.759 8.071   1.00 14.93 ?  40  ASN   B HA   1 
ATOM   4683 H HB2  . ASN   B 1 40  ? 45.652 -21.173 9.962   1.00 15.43 ?  40  ASN   B HB2  1 
ATOM   4684 H HB3  . ASN   B 1 40  ? 45.959 -22.165 8.759   1.00 15.43 ?  40  ASN   B HB3  1 
ATOM   4685 H HD21 . ASN   B 1 40  ? 49.197 -21.640 9.074   1.00 17.35 ?  40  ASN   B HD21 1 
ATOM   4686 H HD22 . ASN   B 1 40  ? 48.095 -22.639 9.002   1.00 17.35 ?  40  ASN   B HD22 1 
ATOM   4687 N N    . VAL   B 1 41  ? 44.340 -18.809 9.805   1.00 12.64 ?  41  VAL   B N    1 
ATOM   4688 C CA   . VAL   B 1 41  ? 43.881 -17.490 10.247  1.00 13.03 ?  41  VAL   B CA   1 
ATOM   4689 C C    . VAL   B 1 41  ? 45.033 -16.539 10.551  1.00 12.81 ?  41  VAL   B C    1 
ATOM   4690 O O    . VAL   B 1 41  ? 44.854 -15.317 10.481  1.00 13.11 ?  41  VAL   B O    1 
ATOM   4691 C CB   . VAL   B 1 41  ? 42.894 -17.563 11.428  1.00 14.53 ?  41  VAL   B CB   1 
ATOM   4692 C CG1  . VAL   B 1 41  ? 41.599 -18.245 11.015  1.00 15.28 ?  41  VAL   B CG1  1 
ATOM   4693 C CG2  . VAL   B 1 41  ? 43.530 -18.240 12.631  1.00 15.44 ?  41  VAL   B CG2  1 
ATOM   4694 H H    . VAL   B 1 41  ? 44.163 -19.455 10.336  1.00 15.17 ?  41  VAL   B H    1 
ATOM   4695 H HA   . VAL   B 1 41  ? 43.393 -17.098 9.508   1.00 15.64 ?  41  VAL   B HA   1 
ATOM   4696 H HB   . VAL   B 1 41  ? 42.672 -16.657 11.691  1.00 17.44 ?  41  VAL   B HB   1 
ATOM   4697 H HG11 . VAL   B 1 41  ? 40.990 -18.248 11.770  1.00 18.34 ?  41  VAL   B HG11 1 
ATOM   4698 H HG12 . VAL   B 1 41  ? 41.208 -17.758 10.274  1.00 18.34 ?  41  VAL   B HG12 1 
ATOM   4699 H HG13 . VAL   B 1 41  ? 41.796 -19.157 10.746  1.00 18.34 ?  41  VAL   B HG13 1 
ATOM   4700 H HG21 . VAL   B 1 41  ? 42.882 -18.275 13.351  1.00 18.52 ?  41  VAL   B HG21 1 
ATOM   4701 H HG22 . VAL   B 1 41  ? 43.798 -19.140 12.384  1.00 18.52 ?  41  VAL   B HG22 1 
ATOM   4702 H HG23 . VAL   B 1 41  ? 44.307 -17.730 12.910  1.00 18.52 ?  41  VAL   B HG23 1 
ATOM   4703 N N    . TYR   B 1 42  ? 46.204 -17.056 10.930  1.00 12.95 ?  42  TYR   B N    1 
ATOM   4704 C CA   . TYR   B 1 42  ? 47.358 -16.205 11.200  1.00 13.69 ?  42  TYR   B CA   1 
ATOM   4705 C C    . TYR   B 1 42  ? 48.326 -16.132 10.022  1.00 12.87 ?  42  TYR   B C    1 
ATOM   4706 O O    . TYR   B 1 42  ? 49.419 -15.565 10.159  1.00 14.09 ?  42  TYR   B O    1 
ATOM   4707 C CB   . TYR   B 1 42  ? 48.057 -16.607 12.505  1.00 15.54 ?  42  TYR   B CB   1 
ATOM   4708 C CG   . TYR   B 1 42  ? 47.448 -15.941 13.734  1.00 16.41 ?  42  TYR   B CG   1 
ATOM   4709 C CD1  . TYR   B 1 42  ? 47.670 -14.589 14.002  1.00 15.67 ?  42  TYR   B CD1  1 
ATOM   4710 C CD2  . TYR   B 1 42  ? 46.644 -16.650 14.611  1.00 18.27 ?  42  TYR   B CD2  1 
ATOM   4711 C CE1  . TYR   B 1 42  ? 47.114 -13.974 15.106  1.00 16.75 ?  42  TYR   B CE1  1 
ATOM   4712 C CE2  . TYR   B 1 42  ? 46.084 -16.043 15.721  1.00 18.55 ?  42  TYR   B CE2  1 
ATOM   4713 C CZ   . TYR   B 1 42  ? 46.320 -14.703 15.963  1.00 18.83 ?  42  TYR   B CZ   1 
ATOM   4714 O OH   . TYR   B 1 42  ? 45.767 -14.097 17.069  1.00 21.70 ?  42  TYR   B OH   1 
ATOM   4715 H H    . TYR   B 1 42  ? 46.354 -17.899 11.024  1.00 15.54 ?  42  TYR   B H    1 
ATOM   4716 H HA   . TYR   B 1 42  ? 47.023 -15.304 11.335  1.00 16.42 ?  42  TYR   B HA   1 
ATOM   4717 H HB2  . TYR   B 1 42  ? 47.981 -17.563 12.619  1.00 18.65 ?  42  TYR   B HB2  1 
ATOM   4718 H HB3  . TYR   B 1 42  ? 48.985 -16.344 12.454  1.00 18.65 ?  42  TYR   B HB3  1 
ATOM   4719 H HD1  . TYR   B 1 42  ? 48.205 -14.094 13.417  1.00 18.81 ?  42  TYR   B HD1  1 
ATOM   4720 H HD2  . TYR   B 1 42  ? 46.475 -17.552 14.447  1.00 21.92 ?  42  TYR   B HD2  1 
ATOM   4721 H HE1  . TYR   B 1 42  ? 47.279 -13.074 15.268  1.00 20.10 ?  42  TYR   B HE1  1 
ATOM   4722 H HE2  . TYR   B 1 42  ? 45.547 -16.536 16.300  1.00 22.26 ?  42  TYR   B HE2  1 
ATOM   4723 H HH   . TYR   B 1 42  ? 45.997 -13.293 17.092  1.00 26.04 ?  42  TYR   B HH   1 
ATOM   4724 N N    . LEU   B 1 43  ? 47.928 -16.645 8.859   1.00 12.04 ?  43  LEU   B N    1 
ATOM   4725 C CA   . LEU   B 1 43  ? 48.742 -16.577 7.651   1.00 11.65 ?  43  LEU   B CA   1 
ATOM   4726 C C    . LEU   B 1 43  ? 50.153 -17.091 7.911   1.00 11.90 ?  43  LEU   B C    1 
ATOM   4727 O O    . LEU   B 1 43  ? 51.138 -16.503 7.461   1.00 12.97 ?  43  LEU   B O    1 
ATOM   4728 C CB   . LEU   B 1 43  ? 48.761 -15.176 7.036   1.00 11.69 ?  43  LEU   B CB   1 
ATOM   4729 C CG   . LEU   B 1 43  ? 47.407 -14.563 6.676   1.00 12.06 ?  43  LEU   B CG   1 
ATOM   4730 C CD1  . LEU   B 1 43  ? 47.615 -13.171 6.091   1.00 13.27 ?  43  LEU   B CD1  1 
ATOM   4731 C CD2  . LEU   B 1 43  ? 46.625 -15.449 5.717   1.00 12.09 ?  43  LEU   B CD2  1 
ATOM   4732 H H    . LEU   B 1 43  ? 47.181 -17.050 8.744   1.00 14.45 ?  43  LEU   B H    1 
ATOM   4733 H HA   . LEU   B 1 43  ? 48.343 -17.166 6.991   1.00 13.99 ?  43  LEU   B HA   1 
ATOM   4734 H HB2  . LEU   B 1 43  ? 49.193 -14.576 7.662   1.00 14.03 ?  43  LEU   B HB2  1 
ATOM   4735 H HB3  . LEU   B 1 43  ? 49.286 -15.216 6.218   1.00 14.03 ?  43  LEU   B HB3  1 
ATOM   4736 H HG   . LEU   B 1 43  ? 46.882 -14.473 7.482   1.00 14.47 ?  43  LEU   B HG   1 
ATOM   4737 H HD11 . LEU   B 1 43  ? 46.752 -12.790 5.865   1.00 15.93 ?  43  LEU   B HD11 1 
ATOM   4738 H HD12 . LEU   B 1 43  ? 48.058 -12.617 6.753   1.00 15.93 ?  43  LEU   B HD12 1 
ATOM   4739 H HD13 . LEU   B 1 43  ? 48.165 -13.238 5.295   1.00 15.93 ?  43  LEU   B HD13 1 
ATOM   4740 H HD21 . LEU   B 1 43  ? 45.822 -14.982 5.440   1.00 14.50 ?  43  LEU   B HD21 1 
ATOM   4741 H HD22 . LEU   B 1 43  ? 47.177 -15.648 4.946   1.00 14.50 ?  43  LEU   B HD22 1 
ATOM   4742 H HD23 . LEU   B 1 43  ? 46.386 -16.274 6.173   1.00 14.50 ?  43  LEU   B HD23 1 
ATOM   4743 N N    . LYS   B 1 44  ? 50.246 -18.217 8.625   1.00 11.83 ?  44  LYS   B N    1 
ATOM   4744 C CA   . LYS   B 1 44  ? 51.509 -18.900 8.874   1.00 12.59 ?  44  LYS   B CA   1 
ATOM   4745 C C    . LYS   B 1 44  ? 51.631 -20.017 7.845   1.00 12.13 ?  44  LYS   B C    1 
ATOM   4746 O O    . LYS   B 1 44  ? 50.928 -21.029 7.925   1.00 13.44 ?  44  LYS   B O    1 
ATOM   4747 C CB   . LYS   B 1 44  ? 51.550 -19.410 10.313  1.00 14.50 ?  44  LYS   B CB   1 
ATOM   4748 C CG   . LYS   B 1 44  ? 51.743 -18.291 11.333  1.00 17.29 ?  44  LYS   B CG   1 
ATOM   4749 C CD   . LYS   B 1 44  ? 52.978 -17.460 10.979  1.00 20.07 ?  44  LYS   B CD   1 
ATOM   4750 C CE   . LYS   B 1 44  ? 53.366 -16.491 12.063  1.00 22.55 ?  44  LYS   B CE   1 
ATOM   4751 N NZ   . LYS   B 1 44  ? 54.589 -15.717 11.723  1.00 23.85 ?  44  LYS   B NZ   1 
ATOM   4752 H H    . LYS   B 1 44  ? 49.569 -18.610 8.981   1.00 14.20 ?  44  LYS   B H    1 
ATOM   4753 H HA   . LYS   B 1 44  ? 52.244 -18.287 8.719   1.00 15.11 ?  44  LYS   B HA   1 
ATOM   4754 H HB2  . LYS   B 1 44  ? 50.705 -19.847 10.516  1.00 17.39 ?  44  LYS   B HB2  1 
ATOM   4755 H HB3  . LYS   B 1 44  ? 52.280 -20.030 10.413  1.00 17.39 ?  44  LYS   B HB3  1 
ATOM   4756 H HG2  . LYS   B 1 44  ? 50.967 -17.708 11.331  1.00 20.75 ?  44  LYS   B HG2  1 
ATOM   4757 H HG3  . LYS   B 1 44  ? 51.874 -18.678 12.216  1.00 20.75 ?  44  LYS   B HG3  1 
ATOM   4758 H HD2  . LYS   B 1 44  ? 53.724 -18.066 10.813  1.00 24.08 ?  44  LYS   B HD2  1 
ATOM   4759 H HD3  . LYS   B 1 44  ? 52.791 -16.941 10.182  1.00 24.08 ?  44  LYS   B HD3  1 
ATOM   4760 H HE2  . LYS   B 1 44  ? 52.642 -15.861 12.184  1.00 27.07 ?  44  LYS   B HE2  1 
ATOM   4761 H HE3  . LYS   B 1 44  ? 53.536 -16.981 12.880  1.00 27.07 ?  44  LYS   B HE3  1 
ATOM   4762 H HZ1  . LYS   B 1 44  ? 54.783 -15.151 12.382  1.00 28.62 ?  44  LYS   B HZ1  1 
ATOM   4763 H HZ2  . LYS   B 1 44  ? 55.277 -16.267 11.600  1.00 28.62 ?  44  LYS   B HZ2  1 
ATOM   4764 H HZ3  . LYS   B 1 44  ? 54.457 -15.250 10.974  1.00 28.62 ?  44  LYS   B HZ3  1 
ATOM   4765 N N    . HIS   B 1 45  ? 52.484 -19.796 6.843   1.00 11.82 ?  45  HIS   B N    1 
ATOM   4766 C CA   . HIS   B 1 45  ? 52.506 -20.627 5.638   1.00 12.01 ?  45  HIS   B CA   1 
ATOM   4767 C C    . HIS   B 1 45  ? 53.527 -21.751 5.790   1.00 14.07 ?  45  HIS   B C    1 
ATOM   4768 O O    . HIS   B 1 45  ? 54.587 -21.760 5.174   1.00 16.52 ?  45  HIS   B O    1 
ATOM   4769 C CB   . HIS   B 1 45  ? 52.819 -19.769 4.423   1.00 11.89 ?  45  HIS   B CB   1 
ATOM   4770 C CG   . HIS   B 1 45  ? 51.952 -18.561 4.313   1.00 11.67 ?  45  HIS   B CG   1 
ATOM   4771 N ND1  . HIS   B 1 45  ? 50.575 -18.639 4.267   1.00 11.86 ?  45  HIS   B ND1  1 
ATOM   4772 C CD2  . HIS   B 1 45  ? 52.268 -17.248 4.249   1.00 12.37 ?  45  HIS   B CD2  1 
ATOM   4773 C CE1  . HIS   B 1 45  ? 50.088 -17.414 4.164   1.00 11.94 ?  45  HIS   B CE1  1 
ATOM   4774 N NE2  . HIS   B 1 45  ? 51.091 -16.553 4.152   1.00 12.44 ?  45  HIS   B NE2  1 
ATOM   4775 H H    . HIS   B 1 45  ? 53.063 -19.158 6.837   1.00 14.18 ?  45  HIS   B H    1 
ATOM   4776 H HA   . HIS   B 1 45  ? 51.629 -21.026 5.513   1.00 14.41 ?  45  HIS   B HA   1 
ATOM   4777 H HB2  . HIS   B 1 45  ? 53.738 -19.478 4.474   1.00 14.26 ?  45  HIS   B HB2  1 
ATOM   4778 H HB3  . HIS   B 1 45  ? 52.690 -20.312 3.622   1.00 14.26 ?  45  HIS   B HB3  1 
ATOM   4779 H HD2  . HIS   B 1 45  ? 53.123 -16.888 4.267   1.00 14.84 ?  45  HIS   B HD2  1 
ATOM   4780 H HE1  . HIS   B 1 45  ? 49.184 -17.195 4.101   1.00 14.33 ?  45  HIS   B HE1  1 
ATOM   4781 H HE2  . HIS   B 1 45  ? 51.015 -15.701 4.102   1.00 14.93 ?  45  HIS   B HE2  1 
ATOM   4782 N N    A GLY   B 1 46  ? 53.167 -22.726 6.619   0.30 15.23 ?  46  GLY   B N    1 
ATOM   4783 N N    B GLY   B 1 46  ? 53.175 -22.720 6.625   0.70 15.24 ?  46  GLY   B N    1 
ATOM   4784 C CA   A GLY   B 1 46  ? 54.091 -23.785 6.978   0.30 16.47 ?  46  GLY   B CA   1 
ATOM   4785 C CA   B GLY   B 1 46  ? 54.106 -23.784 6.948   0.70 16.58 ?  46  GLY   B CA   1 
ATOM   4786 C C    A GLY   B 1 46  ? 54.118 -24.988 6.052   0.30 17.71 ?  46  GLY   B C    1 
ATOM   4787 C C    B GLY   B 1 46  ? 54.114 -24.963 5.994   0.70 18.08 ?  46  GLY   B C    1 
ATOM   4788 O O    A GLY   B 1 46  ? 55.182 -25.378 5.560   0.30 19.35 ?  46  GLY   B O    1 
ATOM   4789 O O    B GLY   B 1 46  ? 55.152 -25.317 5.425   0.70 20.84 ?  46  GLY   B O    1 
ATOM   4790 H H    A GLY   B 1 46  ? 52.395 -22.786 6.996   0.30 18.27 ?  46  GLY   B H    1 
ATOM   4791 H H    B GLY   B 1 46  ? 52.418 -22.769 7.031   0.70 18.28 ?  46  GLY   B H    1 
ATOM   4792 H HA2  A GLY   B 1 46  ? 54.987 -23.416 7.011   0.30 19.76 ?  46  GLY   B HA2  1 
ATOM   4793 H HA2  B GLY   B 1 46  ? 55.004 -23.417 6.979   0.70 19.89 ?  46  GLY   B HA2  1 
ATOM   4794 H HA3  A GLY   B 1 46  ? 53.869 -24.099 7.870   0.30 19.76 ?  46  GLY   B HA3  1 
ATOM   4795 H HA3  B GLY   B 1 46  ? 53.895 -24.125 7.831   0.70 19.89 ?  46  GLY   B HA3  1 
ATOM   4796 N N    . GLY   B 1 47  ? 52.955 -25.589 5.804   1.00 17.78 ?  47  GLY   B N    1 
ATOM   4797 C CA   . GLY   B 1 47  ? 52.877 -26.859 5.115   1.00 15.85 ?  47  GLY   B CA   1 
ATOM   4798 C C    . GLY   B 1 47  ? 51.975 -26.827 3.897   1.00 13.40 ?  47  GLY   B C    1 
ATOM   4799 O O    . GLY   B 1 47  ? 51.336 -25.817 3.595   1.00 13.60 ?  47  GLY   B O    1 
ATOM   4800 H H    A GLY   B 1 47  ? 52.189 -25.273 6.039   0.30 21.34 ?  47  GLY   B H    1 
ATOM   4801 H H    B GLY   B 1 47  ? 52.195 -25.300 6.089   0.70 21.34 ?  47  GLY   B H    1 
ATOM   4802 H HA2  . GLY   B 1 47  ? 53.762 -27.128 4.821   1.00 19.02 ?  47  GLY   B HA2  1 
ATOM   4803 H HA3  . GLY   B 1 47  ? 52.542 -27.533 5.724   1.00 19.02 ?  47  GLY   B HA3  1 
ATOM   4804 N N    . GLY   B 1 48  ? 51.927 -27.966 3.209   1.00 12.29 ?  48  GLY   B N    1 
ATOM   4805 C CA   . GLY   B 1 48  ? 51.007 -28.104 2.097   1.00 12.16 ?  48  GLY   B CA   1 
ATOM   4806 C C    . GLY   B 1 48  ? 51.151 -26.988 1.087   1.00 11.48 ?  48  GLY   B C    1 
ATOM   4807 O O    . GLY   B 1 48  ? 52.261 -26.521 0.785   1.00 12.37 ?  48  GLY   B O    1 
ATOM   4808 H H    . GLY   B 1 48  ? 52.415 -28.652 3.357   1.00 14.75 ?  48  GLY   B H    1 
ATOM   4809 H HA2  . GLY   B 1 48  ? 51.167 -28.952 1.645   1.00 14.60 ?  48  GLY   B HA2  1 
ATOM   4810 H HA3  . GLY   B 1 48  ? 50.094 -28.102 2.422   1.00 14.60 ?  48  GLY   B HA3  1 
ATOM   4811 N N    . VAL   B 1 49  ? 50.009 -26.556 0.547   1.00 11.45 ?  49  VAL   B N    1 
ATOM   4812 C CA   . VAL   B 1 49  ? 50.004 -25.528 -0.491  1.00 11.72 ?  49  VAL   B CA   1 
ATOM   4813 C C    . VAL   B 1 49  ? 50.666 -24.243 -0.000  1.00 10.90 ?  49  VAL   B C    1 
ATOM   4814 O O    . VAL   B 1 49  ? 51.453 -23.619 -0.722  1.00 11.56 ?  49  VAL   B O    1 
ATOM   4815 C CB   . VAL   B 1 49  ? 48.565 -25.275 -0.983  1.00 12.80 ?  49  VAL   B CB   1 
ATOM   4816 C CG1  . VAL   B 1 49  ? 48.507 -24.022 -1.849  1.00 13.12 ?  49  VAL   B CG1  1 
ATOM   4817 C CG2  . VAL   B 1 49  ? 48.037 -26.480 -1.752  1.00 14.34 ?  49  VAL   B CG2  1 
ATOM   4818 H H    . VAL   B 1 49  ? 49.222 -26.838 0.764   1.00 13.74 ?  49  VAL   B H    1 
ATOM   4819 H HA   . VAL   B 1 49  ? 50.512 -25.847 -1.250  1.00 14.06 ?  49  VAL   B HA   1 
ATOM   4820 H HB   . VAL   B 1 49  ? 47.986 -25.132 -0.220  1.00 15.37 ?  49  VAL   B HB   1 
ATOM   4821 H HG11 . VAL   B 1 49  ? 47.687 -24.034 -2.370  1.00 15.74 ?  49  VAL   B HG11 1 
ATOM   4822 H HG12 . VAL   B 1 49  ? 48.520 -23.237 -1.279  1.00 15.74 ?  49  VAL   B HG12 1 
ATOM   4823 H HG13 . VAL   B 1 49  ? 49.272 -24.013 -2.446  1.00 15.74 ?  49  VAL   B HG13 1 
ATOM   4824 H HG21 . VAL   B 1 49  ? 47.130 -26.295 -2.048  1.00 17.21 ?  49  VAL   B HG21 1 
ATOM   4825 H HG22 . VAL   B 1 49  ? 48.607 -26.636 -2.523  1.00 17.21 ?  49  VAL   B HG22 1 
ATOM   4826 H HG23 . VAL   B 1 49  ? 48.045 -27.252 -1.171  1.00 17.21 ?  49  VAL   B HG23 1 
ATOM   4827 N N    . ALA   B 1 50  ? 50.328 -23.802 1.212   1.00 10.89 ?  50  ALA   B N    1 
ATOM   4828 C CA   . ALA   B 1 50  ? 50.847 -22.526 1.692   1.00 10.94 ?  50  ALA   B CA   1 
ATOM   4829 C C    . ALA   B 1 50  ? 52.366 -22.558 1.797   1.00 11.08 ?  50  ALA   B C    1 
ATOM   4830 O O    . ALA   B 1 50  ? 53.049 -21.587 1.440   1.00 10.95 ?  50  ALA   B O    1 
ATOM   4831 C CB   . ALA   B 1 50  ? 50.224 -22.175 3.040   1.00 11.08 ?  50  ALA   B CB   1 
ATOM   4832 H H    . ALA   B 1 50  ? 49.812 -24.215 1.764   1.00 13.07 ?  50  ALA   B H    1 
ATOM   4833 H HA   . ALA   B 1 50  ? 50.615 -21.831 1.064   1.00 13.13 ?  50  ALA   B HA   1 
ATOM   4834 H HB1  . ALA   B 1 50  ? 50.581 -21.322 3.343   1.00 13.30 ?  50  ALA   B HB1  1 
ATOM   4835 H HB2  . ALA   B 1 50  ? 49.261 -22.107 2.936   1.00 13.30 ?  50  ALA   B HB2  1 
ATOM   4836 H HB3  . ALA   B 1 50  ? 50.439 -22.867 3.684   1.00 13.30 ?  50  ALA   B HB3  1 
ATOM   4837 N N    . GLY   B 1 51  ? 52.914 -23.658 2.308   1.00 11.35 ?  51  GLY   B N    1 
ATOM   4838 C CA   . GLY   B 1 51  ? 54.358 -23.759 2.387   1.00 12.31 ?  51  GLY   B CA   1 
ATOM   4839 C C    . GLY   B 1 51  ? 55.009 -23.711 1.022   1.00 12.12 ?  51  GLY   B C    1 
ATOM   4840 O O    . GLY   B 1 51  ? 56.053 -23.078 0.846   1.00 12.98 ?  51  GLY   B O    1 
ATOM   4841 H H    . GLY   B 1 51  ? 52.488 -24.346 2.604   1.00 13.63 ?  51  GLY   B H    1 
ATOM   4842 H HA2  . GLY   B 1 51  ? 54.709 -23.025 2.916   1.00 14.77 ?  51  GLY   B HA2  1 
ATOM   4843 H HA3  . GLY   B 1 51  ? 54.608 -24.594 2.818   1.00 14.77 ?  51  GLY   B HA3  1 
ATOM   4844 N N    . ALA   B 1 52  ? 54.406 -24.376 0.037   1.00 11.77 ?  52  ALA   B N    1 
ATOM   4845 C CA   . ALA   B 1 52  ? 54.968 -24.378 -1.309  1.00 12.05 ?  52  ALA   B CA   1 
ATOM   4846 C C    . ALA   B 1 52  ? 54.891 -22.999 -1.954  1.00 11.65 ?  52  ALA   B C    1 
ATOM   4847 O O    . ALA   B 1 52  ? 55.860 -22.547 -2.583  1.00 12.01 ?  52  ALA   B O    1 
ATOM   4848 C CB   . ALA   B 1 52  ? 54.264 -25.418 -2.176  1.00 12.69 ?  52  ALA   B CB   1 
ATOM   4849 H H    . ALA   B 1 52  ? 53.672 -24.822 0.119   1.00 14.12 ?  52  ALA   B H    1 
ATOM   4850 H HA   . ALA   B 1 52  ? 55.903 -24.621 -1.253  1.00 14.46 ?  52  ALA   B HA   1 
ATOM   4851 H HB1  . ALA   B 1 52  ? 54.658 -25.403 -3.065  1.00 15.22 ?  52  ALA   B HB1  1 
ATOM   4852 H HB2  . ALA   B 1 52  ? 54.392 -26.294 -1.777  1.00 15.22 ?  52  ALA   B HB2  1 
ATOM   4853 H HB3  . ALA   B 1 52  ? 53.324 -25.207 -2.226  1.00 15.22 ?  52  ALA   B HB3  1 
ATOM   4854 N N    . LEU   B 1 53  ? 53.749 -22.317 -1.827  1.00 10.98 ?  53  LEU   B N    1 
ATOM   4855 C CA   . LEU   B 1 53  ? 53.639 -20.982 -2.402  1.00 11.31 ?  53  LEU   B CA   1 
ATOM   4856 C C    . LEU   B 1 53  ? 54.642 -20.041 -1.753  1.00 11.12 ?  53  LEU   B C    1 
ATOM   4857 O O    . LEU   B 1 53  ? 55.348 -19.291 -2.438  1.00 11.84 ?  53  LEU   B O    1 
ATOM   4858 C CB   . LEU   B 1 53  ? 52.216 -20.443 -2.239  1.00 11.65 ?  53  LEU   B CB   1 
ATOM   4859 C CG   . LEU   B 1 53  ? 51.087 -21.169 -2.985  1.00 11.96 ?  53  LEU   B CG   1 
ATOM   4860 C CD1  . LEU   B 1 53  ? 49.745 -20.551 -2.626  1.00 13.15 ?  53  LEU   B CD1  1 
ATOM   4861 C CD2  . LEU   B 1 53  ? 51.287 -21.152 -4.494  1.00 13.66 ?  53  LEU   B CD2  1 
ATOM   4862 H H    . LEU   B 1 53  ? 53.050 -22.594 -1.414  1.00 13.18 ?  53  LEU   B H    1 
ATOM   4863 H HA   . LEU   B 1 53  ? 53.839 -21.030 -3.352  1.00 13.57 ?  53  LEU   B HA   1 
ATOM   4864 H HB2  . LEU   B 1 53  ? 51.994 -20.470 -1.298  1.00 13.98 ?  53  LEU   B HB2  1 
ATOM   4865 H HB3  . LEU   B 1 53  ? 52.207 -19.526 -2.545  1.00 13.98 ?  53  LEU   B HB3  1 
ATOM   4866 H HG   . LEU   B 1 53  ? 51.061 -22.095 -2.697  1.00 14.36 ?  53  LEU   B HG   1 
ATOM   4867 H HD11 . LEU   B 1 53  ? 49.038 -21.023 -3.101  1.00 15.78 ?  53  LEU   B HD11 1 
ATOM   4868 H HD12 . LEU   B 1 53  ? 49.600 -20.632 -1.667  1.00 15.78 ?  53  LEU   B HD12 1 
ATOM   4869 H HD13 . LEU   B 1 53  ? 49.744 -19.617 -2.881  1.00 15.78 ?  53  LEU   B HD13 1 
ATOM   4870 H HD21 . LEU   B 1 53  ? 50.594 -21.684 -4.912  1.00 16.39 ?  53  LEU   B HD21 1 
ATOM   4871 H HD22 . LEU   B 1 53  ? 51.231 -20.235 -4.808  1.00 16.39 ?  53  LEU   B HD22 1 
ATOM   4872 H HD23 . LEU   B 1 53  ? 52.158 -21.521 -4.701  1.00 16.39 ?  53  LEU   B HD23 1 
ATOM   4873 N N    . ASN   B 1 54  ? 54.731 -20.072 -0.428  1.00 10.94 ?  54  ASN   B N    1 
ATOM   4874 C CA   . ASN   B 1 54  ? 55.645 -19.161 0.245   1.00 11.57 ?  54  ASN   B CA   1 
ATOM   4875 C C    . ASN   B 1 54  ? 57.093 -19.442 -0.152  1.00 12.17 ?  54  ASN   B C    1 
ATOM   4876 O O    . ASN   B 1 54  ? 57.872 -18.509 -0.389  1.00 12.33 ?  54  ASN   B O    1 
ATOM   4877 C CB   . ASN   B 1 54  ? 55.476 -19.246 1.752   1.00 12.22 ?  54  ASN   B CB   1 
ATOM   4878 C CG   . ASN   B 1 54  ? 56.451 -18.349 2.470   1.00 12.43 ?  54  ASN   B CG   1 
ATOM   4879 O OD1  . ASN   B 1 54  ? 56.474 -17.137 2.225   1.00 12.51 ?  54  ASN   B OD1  1 
ATOM   4880 N ND2  . ASN   B 1 54  ? 57.287 -18.929 3.325   1.00 13.98 ?  54  ASN   B ND2  1 
ATOM   4881 H H    . ASN   B 1 54  ? 54.293 -20.599 0.087   1.00 13.13 ?  54  ASN   B H    1 
ATOM   4882 H HA   . ASN   B 1 54  ? 55.436 -18.254 -0.031  1.00 13.88 ?  54  ASN   B HA   1 
ATOM   4883 H HB2  . ASN   B 1 54  ? 54.579 -18.962 1.987   1.00 14.67 ?  54  ASN   B HB2  1 
ATOM   4884 H HB3  . ASN   B 1 54  ? 55.631 -20.156 2.040   1.00 14.67 ?  54  ASN   B HB3  1 
ATOM   4885 H HD21 . ASN   B 1 54  ? 57.865 -18.461 3.752   1.00 16.77 ?  54  ASN   B HD21 1 
ATOM   4886 H HD22 . ASN   B 1 54  ? 57.244 -19.782 3.458   1.00 16.77 ?  54  ASN   B HD22 1 
ATOM   4887 N N    . LYS   B 1 55  ? 57.477 -20.719 -0.215  1.00 12.76 ?  55  LYS   B N    1 
ATOM   4888 C CA   . LYS   B 1 55  ? 58.833 -21.062 -0.632  1.00 13.51 ?  55  LYS   B CA   1 
ATOM   4889 C C    . LYS   B 1 55  ? 59.134 -20.513 -2.020  1.00 13.24 ?  55  LYS   B C    1 
ATOM   4890 O O    . LYS   B 1 55  ? 60.234 -20.008 -2.268  1.00 13.86 ?  55  LYS   B O    1 
ATOM   4891 C CB   . LYS   B 1 55  ? 59.012 -22.581 -0.597  1.00 15.22 ?  55  LYS   B CB   1 
ATOM   4892 C CG   . LYS   B 1 55  ? 60.387 -23.048 -1.019  1.00 19.12 ?  55  LYS   B CG   1 
ATOM   4893 C CD   . LYS   B 1 55  ? 60.538 -24.545 -0.839  1.00 22.34 ?  55  LYS   B CD   1 
ATOM   4894 C CE   . LYS   B 1 55  ? 60.582 -24.938 0.637   1.00 25.09 ?  55  LYS   B CE   1 
ATOM   4895 N NZ   . LYS   B 1 55  ? 60.891 -26.377 0.818   1.00 26.51 ?  55  LYS   B NZ   1 
ATOM   4896 H H    . LYS   B 1 55  ? 56.977 -21.390 -0.028  1.00 15.31 ?  55  LYS   B H    1 
ATOM   4897 H HA   . LYS   B 1 55  ? 59.464 -20.669 -0.010  1.00 16.21 ?  55  LYS   B HA   1 
ATOM   4898 H HB2  . LYS   B 1 55  ? 58.853 -22.882 0.312   1.00 18.26 ?  55  LYS   B HB2  1 
ATOM   4899 H HB3  . LYS   B 1 55  ? 58.361 -22.983 -1.193  1.00 18.26 ?  55  LYS   B HB3  1 
ATOM   4900 H HG2  . LYS   B 1 55  ? 60.522 -22.839 -1.958  1.00 22.95 ?  55  LYS   B HG2  1 
ATOM   4901 H HG3  . LYS   B 1 55  ? 61.057 -22.603 -0.477  1.00 22.95 ?  55  LYS   B HG3  1 
ATOM   4902 H HD2  . LYS   B 1 55  ? 59.781 -24.995 -1.247  1.00 26.81 ?  55  LYS   B HD2  1 
ATOM   4903 H HD3  . LYS   B 1 55  ? 61.364 -24.837 -1.253  1.00 26.81 ?  55  LYS   B HD3  1 
ATOM   4904 H HE2  . LYS   B 1 55  ? 61.271 -24.414 1.081   1.00 30.11 ?  55  LYS   B HE2  1 
ATOM   4905 H HE3  . LYS   B 1 55  ? 59.718 -24.755 1.041   1.00 30.11 ?  55  LYS   B HE3  1 
ATOM   4906 H HZ1  . LYS   B 1 55  ? 60.863 -26.582 1.684   1.00 31.81 ?  55  LYS   B HZ1  1 
ATOM   4907 H HZ2  . LYS   B 1 55  ? 60.290 -26.867 0.383   1.00 31.81 ?  55  LYS   B HZ2  1 
ATOM   4908 H HZ3  . LYS   B 1 55  ? 61.699 -26.554 0.501   1.00 31.81 ?  55  LYS   B HZ3  1 
ATOM   4909 N N    . ALA   B 1 56  ? 58.169 -20.600 -2.942  1.00 12.81 ?  56  ALA   B N    1 
ATOM   4910 C CA   . ALA   B 1 56  ? 58.389 -20.092 -4.291  1.00 13.41 ?  56  ALA   B CA   1 
ATOM   4911 C C    . ALA   B 1 56  ? 58.657 -18.594 -4.284  1.00 13.08 ?  56  ALA   B C    1 
ATOM   4912 O O    . ALA   B 1 56  ? 59.382 -18.088 -5.152  1.00 14.33 ?  56  ALA   B O    1 
ATOM   4913 C CB   . ALA   B 1 56  ? 57.190 -20.424 -5.179  1.00 14.41 ?  56  ALA   B CB   1 
ATOM   4914 H H    . ALA   B 1 56  ? 57.389 -20.938 -2.807  1.00 15.37 ?  56  ALA   B H    1 
ATOM   4915 H HA   . ALA   B 1 56  ? 59.169 -20.526 -4.665  1.00 16.09 ?  56  ALA   B HA   1 
ATOM   4916 H HB1  . ALA   B 1 56  ? 57.359 -20.086 -6.075  1.00 17.29 ?  56  ALA   B HB1  1 
ATOM   4917 H HB2  . ALA   B 1 56  ? 57.075 -21.385 -5.204  1.00 17.29 ?  56  ALA   B HB2  1 
ATOM   4918 H HB3  . ALA   B 1 56  ? 56.398 -20.002 -4.813  1.00 17.29 ?  56  ALA   B HB3  1 
ATOM   4919 N N    . THR   B 1 57  ? 58.079 -17.868 -3.329  1.00 12.94 ?  57  THR   B N    1 
ATOM   4920 C CA   . THR   B 1 57  ? 58.320 -16.435 -3.198  1.00 12.92 ?  57  THR   B CA   1 
ATOM   4921 C C    . THR   B 1 57  ? 59.575 -16.114 -2.395  1.00 13.90 ?  57  THR   B C    1 
ATOM   4922 O O    . THR   B 1 57  ? 59.812 -14.939 -2.096  1.00 14.51 ?  57  THR   B O    1 
ATOM   4923 C CB   . THR   B 1 57  ? 57.124 -15.712 -2.553  1.00 12.39 ?  57  THR   B CB   1 
ATOM   4924 O OG1  . THR   B 1 57  ? 57.101 -15.931 -1.136  1.00 12.58 ?  57  THR   B OG1  1 
ATOM   4925 C CG2  . THR   B 1 57  ? 55.800 -16.134 -3.186  1.00 12.55 ?  57  THR   B CG2  1 
ATOM   4926 H H    . THR   B 1 57  ? 57.525 -18.180 -2.748  1.00 15.53 ?  57  THR   B H    1 
ATOM   4927 H HA   . THR   B 1 57  ? 58.434 -16.059 -4.085  1.00 15.50 ?  57  THR   B HA   1 
ATOM   4928 H HB   . THR   B 1 57  ? 57.223 -14.760 -2.709  1.00 14.87 ?  57  THR   B HB   1 
ATOM   4929 H HG1  . THR   B 1 57  ? 57.033 -16.757 -0.975  1.00 15.10 ?  57  THR   B HG1  1 
ATOM   4930 H HG21 . THR   B 1 57  ? 55.076 -15.587 -2.845  1.00 15.06 ?  57  THR   B HG21 1 
ATOM   4931 H HG22 . THR   B 1 57  ? 55.844 -16.037 -4.150  1.00 15.06 ?  57  THR   B HG22 1 
ATOM   4932 H HG23 . THR   B 1 57  ? 55.612 -17.064 -2.976  1.00 15.06 ?  57  THR   B HG23 1 
ATOM   4933 N N    . ASN   B 1 58  ? 60.369 -17.117 -2.029  1.00 14.49 ?  58  ASN   B N    1 
ATOM   4934 C CA   . ASN   B 1 58  ? 61.570 -16.897 -1.229  1.00 16.40 ?  58  ASN   B CA   1 
ATOM   4935 C C    . ASN   B 1 58  ? 61.234 -16.198 0.088   1.00 14.88 ?  58  ASN   B C    1 
ATOM   4936 O O    . ASN   B 1 58  ? 61.972 -15.326 0.559   1.00 15.70 ?  58  ASN   B O    1 
ATOM   4937 C CB   . ASN   B 1 58  ? 62.639 -16.130 -2.012  1.00 21.32 ?  58  ASN   B CB   1 
ATOM   4938 C CG   . ASN   B 1 58  ? 64.003 -16.226 -1.372  1.00 28.35 ?  58  ASN   B CG   1 
ATOM   4939 O OD1  . ASN   B 1 58  ? 64.307 -17.200 -0.685  1.00 30.34 ?  58  ASN   B OD1  1 
ATOM   4940 N ND2  . ASN   B 1 58  ? 64.835 -15.212 -1.587  1.00 30.42 ?  58  ASN   B ND2  1 
ATOM   4941 H H    . ASN   B 1 58  ? 60.233 -17.942 -2.236  1.00 17.38 ?  58  ASN   B H    1 
ATOM   4942 H HA   . ASN   B 1 58  ? 61.945 -17.764 -1.011  1.00 19.68 ?  58  ASN   B HA   1 
ATOM   4943 H HB2  . ASN   B 1 58  ? 62.702 -16.499 -2.911  1.00 25.58 ?  58  ASN   B HB2  1 
ATOM   4944 H HB3  . ASN   B 1 58  ? 62.397 -15.195 -2.055  1.00 25.58 ?  58  ASN   B HB3  1 
ATOM   4945 H HD21 . ASN   B 1 58  ? 65.627 -15.220 -1.247  1.00 36.50 ?  58  ASN   B HD21 1 
ATOM   4946 H HD22 . ASN   B 1 58  ? 64.584 -14.546 -2.069  1.00 36.50 ?  58  ASN   B HD22 1 
ATOM   4947 N N    . ASN   B 1 59  ? 60.105 -16.579 0.686   1.00 13.78 ?  59  ASN   B N    1 
ATOM   4948 C CA   . ASN   B 1 59  ? 59.627 -16.116 1.987   1.00 14.00 ?  59  ASN   B CA   1 
ATOM   4949 C C    . ASN   B 1 59  ? 59.033 -14.709 1.939   1.00 13.23 ?  59  ASN   B C    1 
ATOM   4950 O O    . ASN   B 1 59  ? 58.601 -14.208 2.985   1.00 13.60 ?  59  ASN   B O    1 
ATOM   4951 C CB   . ASN   B 1 59  ? 60.696 -16.192 3.093   1.00 15.11 ?  59  ASN   B CB   1 
ATOM   4952 C CG   . ASN   B 1 59  ? 60.102 -16.357 4.472   1.00 15.81 ?  59  ASN   B CG   1 
ATOM   4953 O OD1  . ASN   B 1 59  ? 59.277 -17.243 4.695   1.00 16.16 ?  59  ASN   B OD1  1 
ATOM   4954 N ND2  . ASN   B 1 59  ? 60.512 -15.507 5.406   1.00 16.52 ?  59  ASN   B ND2  1 
ATOM   4955 H H    . ASN   B 1 59  ? 59.564 -17.149 0.332   1.00 16.53 ?  59  ASN   B H    1 
ATOM   4956 H HA   . ASN   B 1 59  ? 58.912 -16.708 2.261   1.00 16.80 ?  59  ASN   B HA   1 
ATOM   4957 H HB2  . ASN   B 1 59  ? 61.270 -16.958 2.934   1.00 18.14 ?  59  ASN   B HB2  1 
ATOM   4958 H HB3  . ASN   B 1 59  ? 61.216 -15.378 3.099   1.00 18.14 ?  59  ASN   B HB3  1 
ATOM   4959 H HD21 . ASN   B 1 59  ? 60.198 -15.560 6.209   1.00 19.82 ?  59  ASN   B HD21 1 
ATOM   4960 H HD22 . ASN   B 1 59  ? 61.087 -14.901 5.211   1.00 19.82 ?  59  ASN   B HD22 1 
ATOM   4961 N N    . ALA   B 1 60  ? 58.966 -14.065 0.771   1.00 13.23 ?  60  ALA   B N    1 
ATOM   4962 C CA   . ALA   B 1 60  ? 58.375 -12.730 0.704   1.00 13.35 ?  60  ALA   B CA   1 
ATOM   4963 C C    . ALA   B 1 60  ? 56.905 -12.754 1.102   1.00 12.61 ?  60  ALA   B C    1 
ATOM   4964 O O    . ALA   B 1 60  ? 56.406 -11.804 1.720   1.00 13.06 ?  60  ALA   B O    1 
ATOM   4965 C CB   . ALA   B 1 60  ? 58.538 -12.151 -0.702  1.00 14.25 ?  60  ALA   B CB   1 
ATOM   4966 H H    . ALA   B 1 60  ? 59.263 -14.371 0.026   1.00 15.88 ?  60  ALA   B H    1 
ATOM   4967 H HA   . ALA   B 1 60  ? 58.844 -12.148 1.324   1.00 16.02 ?  60  ALA   B HA   1 
ATOM   4968 H HB1  . ALA   B 1 60  ? 58.140 -11.268 -0.724  1.00 17.10 ?  60  ALA   B HB1  1 
ATOM   4969 H HB2  . ALA   B 1 60  ? 59.485 -12.092 -0.912  1.00 17.10 ?  60  ALA   B HB2  1 
ATOM   4970 H HB3  . ALA   B 1 60  ? 58.094 -12.734 -1.336  1.00 17.10 ?  60  ALA   B HB3  1 
ATOM   4971 N N    . MET   B 1 61  ? 56.196 -13.829 0.753   1.00 12.32 ?  61  MET   B N    1 
ATOM   4972 C CA   . MET   B 1 61  ? 54.800 -13.956 1.147   1.00 11.90 ?  61  MET   B CA   1 
ATOM   4973 C C    . MET   B 1 61  ? 54.660 -13.962 2.669   1.00 11.91 ?  61  MET   B C    1 
ATOM   4974 O O    . MET   B 1 61  ? 53.768 -13.310 3.223   1.00 11.74 ?  61  MET   B O    1 
ATOM   4975 C CB   . MET   B 1 61  ? 54.223 -15.226 0.518   1.00 11.57 ?  61  MET   B CB   1 
ATOM   4976 C CG   . MET   B 1 61  ? 52.781 -15.506 0.912   1.00 11.68 ?  61  MET   B CG   1 
ATOM   4977 S SD   . MET   B 1 61  ? 52.138 -17.011 0.164   1.00 12.30 ?  61  MET   B SD   1 
ATOM   4978 C CE   . MET   B 1 61  ? 51.899 -16.453 -1.524  1.00 13.53 ?  61  MET   B CE   1 
ATOM   4979 H H    . MET   B 1 61  ? 56.506 -14.494 0.299   1.00 14.79 ?  61  MET   B H    1 
ATOM   4980 H HA   . MET   B 1 61  ? 54.306 -13.202 0.784   1.00 14.28 ?  61  MET   B HA   1 
ATOM   4981 H HB2  . MET   B 1 61  ? 54.254 -15.141 -0.452  1.00 13.89 ?  61  MET   B HB2  1 
ATOM   4982 H HB3  . MET   B 1 61  ? 54.762 -15.985 0.793   1.00 13.89 ?  61  MET   B HB3  1 
ATOM   4983 H HG2  . MET   B 1 61  ? 52.726 -15.615 1.874   1.00 14.02 ?  61  MET   B HG2  1 
ATOM   4984 H HG3  . MET   B 1 61  ? 52.222 -14.768 0.627   1.00 14.02 ?  61  MET   B HG3  1 
ATOM   4985 H HE1  . MET   B 1 61  ? 51.527 -17.183 -2.049  1.00 16.24 ?  61  MET   B HE1  1 
ATOM   4986 H HE2  . MET   B 1 61  ? 51.290 -15.701 -1.527  1.00 16.24 ?  61  MET   B HE2  1 
ATOM   4987 H HE3  . MET   B 1 61  ? 52.757 -16.188 -1.896  1.00 16.24 ?  61  MET   B HE3  1 
ATOM   4988 N N    . GLN   B 1 62  ? 55.538 -14.683 3.367   1.00 11.70 ?  62  GLN   B N    1 
ATOM   4989 C CA   . GLN   B 1 62  ? 55.436 -14.744 4.821   1.00 12.14 ?  62  GLN   B CA   1 
ATOM   4990 C C    . GLN   B 1 62  ? 55.723 -13.390 5.454   1.00 12.27 ?  62  GLN   B C    1 
ATOM   4991 O O    . GLN   B 1 62  ? 55.040 -12.990 6.402   1.00 12.85 ?  62  GLN   B O    1 
ATOM   4992 C CB   . GLN   B 1 62  ? 56.383 -15.802 5.380   1.00 12.47 ?  62  GLN   B CB   1 
ATOM   4993 C CG   . GLN   B 1 62  ? 56.163 -16.071 6.858   1.00 12.67 ?  62  GLN   B CG   1 
ATOM   4994 C CD   . GLN   B 1 62  ? 54.790 -16.653 7.104   1.00 12.38 ?  62  GLN   B CD   1 
ATOM   4995 O OE1  . GLN   B 1 62  ? 54.529 -17.796 6.745   1.00 12.79 ?  62  GLN   B OE1  1 
ATOM   4996 N NE2  . GLN   B 1 62  ? 53.885 -15.854 7.669   1.00 12.96 ?  62  GLN   B NE2  1 
ATOM   4997 H H    . GLN   B 1 62  ? 56.181 -15.144 3.024   1.00 14.03 ?  62  GLN   B H    1 
ATOM   4998 H HA   . GLN   B 1 62  ? 54.530 -14.997 5.054   1.00 14.57 ?  62  GLN   B HA   1 
ATOM   4999 H HB2  . GLN   B 1 62  ? 56.248 -16.636 4.897   1.00 14.96 ?  62  GLN   B HB2  1 
ATOM   5000 H HB3  . GLN   B 1 62  ? 57.299 -15.501 5.259   1.00 14.96 ?  62  GLN   B HB3  1 
ATOM   5001 H HG2  . GLN   B 1 62  ? 56.824 -16.714 7.164   1.00 15.20 ?  62  GLN   B HG2  1 
ATOM   5002 H HG3  . GLN   B 1 62  ? 56.244 -15.243 7.351   1.00 15.20 ?  62  GLN   B HG3  1 
ATOM   5003 H HE21 . GLN   B 1 62  ? 54.100 -15.050 7.892   1.00 15.56 ?  62  GLN   B HE21 1 
ATOM   5004 H HE22 . GLN   B 1 62  ? 53.089 -16.141 7.817   1.00 15.56 ?  62  GLN   B HE22 1 
ATOM   5005 N N    . VAL   B 1 63  ? 56.738 -12.678 4.960   1.00 13.12 ?  63  VAL   B N    1 
ATOM   5006 C CA   . VAL   B 1 63  ? 57.052 -11.361 5.512   1.00 13.93 ?  63  VAL   B CA   1 
ATOM   5007 C C    . VAL   B 1 63  ? 55.861 -10.424 5.337   1.00 13.13 ?  63  VAL   B C    1 
ATOM   5008 O O    . VAL   B 1 63  ? 55.454 -9.716  6.269   1.00 13.58 ?  63  VAL   B O    1 
ATOM   5009 C CB   . VAL   B 1 63  ? 58.333 -10.805 4.870   1.00 15.01 ?  63  VAL   B CB   1 
ATOM   5010 C CG1  . VAL   B 1 63  ? 58.560 -9.362  5.304   1.00 15.88 ?  63  VAL   B CG1  1 
ATOM   5011 C CG2  . VAL   B 1 63  ? 59.525 -11.672 5.252   1.00 15.69 ?  63  VAL   B CG2  1 
ATOM   5012 H H    . VAL   B 1 63  ? 57.251 -12.934 4.311   1.00 15.74 ?  63  VAL   B H    1 
ATOM   5013 H HA   . VAL   B 1 63  ? 57.218 -11.461 6.460   1.00 16.72 ?  63  VAL   B HA   1 
ATOM   5014 H HB   . VAL   B 1 63  ? 58.248 -10.828 3.903   1.00 18.01 ?  63  VAL   B HB   1 
ATOM   5015 H HG11 . VAL   B 1 63  ? 59.476 -9.117  5.112   1.00 19.06 ?  63  VAL   B HG11 1 
ATOM   5016 H HG12 . VAL   B 1 63  ? 57.952 -8.788  4.813   1.00 19.06 ?  63  VAL   B HG12 1 
ATOM   5017 H HG13 . VAL   B 1 63  ? 58.389 -9.293  6.257   1.00 19.06 ?  63  VAL   B HG13 1 
ATOM   5018 H HG21 . VAL   B 1 63  ? 60.330 -11.299 4.857   1.00 18.83 ?  63  VAL   B HG21 1 
ATOM   5019 H HG22 . VAL   B 1 63  ? 59.611 -11.683 6.220   1.00 18.83 ?  63  VAL   B HG22 1 
ATOM   5020 H HG23 . VAL   B 1 63  ? 59.385 -12.574 4.925   1.00 18.83 ?  63  VAL   B HG23 1 
ATOM   5021 N N    . GLU   B 1 64  ? 55.282 -10.410 4.136   1.00 12.50 ?  64  GLU   B N    1 
ATOM   5022 C CA   . GLU   B 1 64  ? 54.116 -9.571  3.870   1.00 12.33 ?  64  GLU   B CA   1 
ATOM   5023 C C    . GLU   B 1 64  ? 52.938 -9.971  4.750   1.00 12.37 ?  64  GLU   B C    1 
ATOM   5024 O O    . GLU   B 1 64  ? 52.197 -9.109  5.254   1.00 12.89 ?  64  GLU   B O    1 
ATOM   5025 C CB   . GLU   B 1 64  ? 53.747 -9.716  2.395   1.00 12.51 ?  64  GLU   B CB   1 
ATOM   5026 C CG   . GLU   B 1 64  ? 52.495 -8.969  1.965   1.00 12.96 ?  64  GLU   B CG   1 
ATOM   5027 C CD   . GLU   B 1 64  ? 51.953 -9.461  0.631   1.00 13.73 ?  64  GLU   B CD   1 
ATOM   5028 O OE1  . GLU   B 1 64  ? 52.130 -10.669 0.313   1.00 14.44 ?  64  GLU   B OE1  1 
ATOM   5029 O OE2  . GLU   B 1 64  ? 51.331 -8.638  -0.086  1.00 14.39 -1 64  GLU   B OE2  1 
ATOM   5030 H H    . GLU   B 1 64  ? 55.548 -10.874 3.457   1.00 15.01 ?  64  GLU   B H    1 
ATOM   5031 H HA   . GLU   B 1 64  ? 54.334 -8.644  4.044   1.00 14.80 ?  64  GLU   B HA   1 
ATOM   5032 H HB2  . GLU   B 1 64  ? 54.478 -9.377  1.854   1.00 15.01 ?  64  GLU   B HB2  1 
ATOM   5033 H HB3  . GLU   B 1 64  ? 53.604 -10.653 2.201   1.00 15.01 ?  64  GLU   B HB3  1 
ATOM   5034 H HG2  . GLU   B 1 64  ? 51.796 -9.084  2.632   1.00 15.55 ?  64  GLU   B HG2  1 
ATOM   5035 H HG3  . GLU   B 1 64  ? 52.705 -8.024  1.875   1.00 15.55 ?  64  GLU   B HG3  1 
ATOM   5036 N N    . SER   B 1 65  ? 52.750 -11.280 4.931   1.00 12.07 ?  65  SER   B N    1 
ATOM   5037 C CA   . SER   B 1 65  ? 51.645 -11.785 5.732   1.00 11.93 ?  65  SER   B CA   1 
ATOM   5038 C C    . SER   B 1 65  ? 51.780 -11.388 7.195   1.00 11.84 ?  65  SER   B C    1 
ATOM   5039 O O    . SER   B 1 65  ? 50.785 -11.014 7.831   1.00 12.70 ?  65  SER   B O    1 
ATOM   5040 C CB   . SER   B 1 65  ? 51.557 -13.304 5.596   1.00 12.17 ?  65  SER   B CB   1 
ATOM   5041 O OG   . SER   B 1 65  ? 51.216 -13.699 4.272   1.00 12.42 ?  65  SER   B OG   1 
ATOM   5042 H H    . SER   B 1 65  ? 53.260 -11.900 4.604   1.00 14.49 ?  65  SER   B H    1 
ATOM   5043 H HA   . SER   B 1 65  ? 50.819 -11.408 5.394   1.00 14.32 ?  65  SER   B HA   1 
ATOM   5044 H HB2  . SER   B 1 65  ? 52.408 -13.693 5.829   1.00 14.61 ?  65  SER   B HB2  1 
ATOM   5045 H HB3  . SER   B 1 65  ? 50.866 -13.629 6.199   1.00 14.61 ?  65  SER   B HB3  1 
ATOM   5046 H HG   . SER   B 1 65  ? 51.806 -13.415 3.733   1.00 14.90 ?  65  SER   B HG   1 
ATOM   5047 N N    . ASP   B 1 66  ? 52.987 -11.496 7.760   1.00 12.71 ?  66  ASP   B N    1 
ATOM   5048 C CA   . ASP   B 1 66  ? 53.176 -11.112 9.155   1.00 13.08 ?  66  ASP   B CA   1 
ATOM   5049 C C    . ASP   B 1 66  ? 52.865 -9.636  9.356   1.00 13.10 ?  66  ASP   B C    1 
ATOM   5050 O O    . ASP   B 1 66  ? 52.291 -9.247  10.378  1.00 13.74 ?  66  ASP   B O    1 
ATOM   5051 C CB   . ASP   B 1 66  ? 54.605 -11.418 9.606   1.00 14.37 ?  66  ASP   B CB   1 
ATOM   5052 C CG   . ASP   B 1 66  ? 54.881 -12.906 9.751   1.00 15.87 ?  66  ASP   B CG   1 
ATOM   5053 O OD1  . ASP   B 1 66  ? 53.934 -13.720 9.685   1.00 16.63 ?  66  ASP   B OD1  1 
ATOM   5054 O OD2  . ASP   B 1 66  ? 56.066 -13.264 9.937   1.00 18.64 -1 66  ASP   B OD2  1 
ATOM   5055 H H    . ASP   B 1 66  ? 53.690 -11.796 7.369   1.00 15.25 ?  66  ASP   B H    1 
ATOM   5056 H HA   . ASP   B 1 66  ? 52.569 -11.618 9.717   1.00 15.70 ?  66  ASP   B HA   1 
ATOM   5057 H HB2  . ASP   B 1 66  ? 55.225 -11.058 8.955   1.00 17.25 ?  66  ASP   B HB2  1 
ATOM   5058 H HB3  . ASP   B 1 66  ? 54.758 -11.001 10.472  1.00 17.25 ?  66  ASP   B HB3  1 
ATOM   5059 N N    . ASP   B 1 67  ? 53.245 -8.793  8.395   1.00 12.99 ?  67  ASP   B N    1 
ATOM   5060 C CA   . ASP   B 1 67  ? 52.903 -7.380  8.488   1.00 13.55 ?  67  ASP   B CA   1 
ATOM   5061 C C    . ASP   B 1 67  ? 51.393 -7.170  8.404   1.00 13.55 ?  67  ASP   B C    1 
ATOM   5062 O O    . ASP   B 1 67  ? 50.831 -6.368  9.158   1.00 14.43 ?  67  ASP   B O    1 
ATOM   5063 C CB   . ASP   B 1 67  ? 53.621 -6.597  7.396   1.00 14.82 ?  67  ASP   B CB   1 
ATOM   5064 C CG   . ASP   B 1 67  ? 53.199 -5.156  7.368   1.00 16.19 ?  67  ASP   B CG   1 
ATOM   5065 O OD1  . ASP   B 1 67  ? 53.697 -4.350  8.190   1.00 17.28 ?  67  ASP   B OD1  1 
ATOM   5066 O OD2  . ASP   B 1 67  ? 52.329 -4.848  6.536   1.00 17.25 -1 67  ASP   B OD2  1 
ATOM   5067 H H    . ASP   B 1 67  ? 53.703 -9.009  7.697   1.00 15.58 ?  67  ASP   B H    1 
ATOM   5068 H HA   . ASP   B 1 67  ? 53.211 -7.035  9.342   1.00 16.26 ?  67  ASP   B HA   1 
ATOM   5069 H HB2  . ASP   B 1 67  ? 54.579 -6.628  7.548   1.00 17.78 ?  67  ASP   B HB2  1 
ATOM   5070 H HB3  . ASP   B 1 67  ? 53.415 -6.995  6.529   1.00 17.78 ?  67  ASP   B HB3  1 
ATOM   5071 N N    . TYR   B 1 68  ? 50.715 -7.892  7.505   1.00 13.19 ?  68  TYR   B N    1 
ATOM   5072 C CA   . TYR   B 1 68  ? 49.256 -7.810  7.431   1.00 13.89 ?  68  TYR   B CA   1 
ATOM   5073 C C    . TYR   B 1 68  ? 48.617 -8.158  8.772   1.00 13.56 ?  68  TYR   B C    1 
ATOM   5074 O O    . TYR   B 1 68  ? 47.683 -7.481  9.222   1.00 14.14 ?  68  TYR   B O    1 
ATOM   5075 C CB   . TYR   B 1 68  ? 48.716 -8.730  6.326   1.00 14.93 ?  68  TYR   B CB   1 
ATOM   5076 C CG   . TYR   B 1 68  ? 47.206 -8.883  6.388   1.00 16.47 ?  68  TYR   B CG   1 
ATOM   5077 C CD1  . TYR   B 1 68  ? 46.614 -9.839  7.215   1.00 17.28 ?  68  TYR   B CD1  1 
ATOM   5078 C CD2  . TYR   B 1 68  ? 46.371 -8.047  5.662   1.00 17.64 ?  68  TYR   B CD2  1 
ATOM   5079 C CE1  . TYR   B 1 68  ? 45.249 -9.959  7.312   1.00 18.33 ?  68  TYR   B CE1  1 
ATOM   5080 C CE2  . TYR   B 1 68  ? 44.986 -8.175  5.744   1.00 18.07 ?  68  TYR   B CE2  1 
ATOM   5081 C CZ   . TYR   B 1 68  ? 44.450 -9.130  6.574   1.00 18.18 ?  68  TYR   B CZ   1 
ATOM   5082 O OH   . TYR   B 1 68  ? 43.086 -9.255  6.679   1.00 19.64 ?  68  TYR   B OH   1 
ATOM   5083 H H    . TYR   B 1 68  ? 51.075 -8.436  6.939   1.00 15.83 ?  68  TYR   B H    1 
ATOM   5084 H HA   . TYR   B 1 68  ? 49.010 -6.902  7.216   1.00 16.67 ?  68  TYR   B HA   1 
ATOM   5085 H HB2  . TYR   B 1 68  ? 48.937 -8.349  5.463   1.00 17.92 ?  68  TYR   B HB2  1 
ATOM   5086 H HB3  . TYR   B 1 68  ? 49.109 -9.608  6.418   1.00 17.92 ?  68  TYR   B HB3  1 
ATOM   5087 H HD1  . TYR   B 1 68  ? 47.152 -10.406 7.721   1.00 20.73 ?  68  TYR   B HD1  1 
ATOM   5088 H HD2  . TYR   B 1 68  ? 46.733 -7.393  5.117   1.00 21.17 ?  68  TYR   B HD2  1 
ATOM   5089 H HE1  . TYR   B 1 68  ? 44.864 -10.613 7.860   1.00 22.00 ?  68  TYR   B HE1  1 
ATOM   5090 H HE2  . TYR   B 1 68  ? 44.422 -7.609  5.262   1.00 21.68 ?  68  TYR   B HE2  1 
ATOM   5091 H HH   . TYR   B 1 68  ? 42.687 -8.701  6.180   1.00 23.57 ?  68  TYR   B HH   1 
ATOM   5092 N N    . ILE   B 1 69  ? 49.089 -9.235  9.410   1.00 13.29 ?  69  ILE   B N    1 
ATOM   5093 C CA   . ILE   B 1 69  ? 48.531 -9.666  10.689  1.00 14.02 ?  69  ILE   B CA   1 
ATOM   5094 C C    . ILE   B 1 69  ? 48.789 -8.627  11.775  1.00 13.84 ?  69  ILE   B C    1 
ATOM   5095 O O    . ILE   B 1 69  ? 47.919 -8.350  12.608  1.00 14.41 ?  69  ILE   B O    1 
ATOM   5096 C CB   . ILE   B 1 69  ? 49.097 -11.048 11.069  1.00 15.07 ?  69  ILE   B CB   1 
ATOM   5097 C CG1  . ILE   B 1 69  ? 48.569 -12.135 10.121  1.00 15.72 ?  69  ILE   B CG1  1 
ATOM   5098 C CG2  . ILE   B 1 69  ? 48.793 -11.390 12.522  1.00 16.45 ?  69  ILE   B CG2  1 
ATOM   5099 C CD1  . ILE   B 1 69  ? 47.101 -12.467 10.302  1.00 16.04 ?  69  ILE   B CD1  1 
ATOM   5100 H H    . ILE   B 1 69  ? 49.738 -9.728  9.129   1.00 15.95 ?  69  ILE   B H    1 
ATOM   5101 H HA   . ILE   B 1 69  ? 47.575 -9.759  10.592  1.00 16.82 ?  69  ILE   B HA   1 
ATOM   5102 H HB   . ILE   B 1 69  ? 50.063 -11.017 10.969  1.00 18.08 ?  69  ILE   B HB   1 
ATOM   5103 H HG12 . ILE   B 1 69  ? 48.692 -11.834 9.206   1.00 18.86 ?  69  ILE   B HG12 1 
ATOM   5104 H HG13 . ILE   B 1 69  ? 49.077 -12.949 10.265  1.00 18.86 ?  69  ILE   B HG13 1 
ATOM   5105 H HG21 . ILE   B 1 69  ? 48.946 -12.341 12.657  1.00 19.74 ?  69  ILE   B HG21 1 
ATOM   5106 H HG22 . ILE   B 1 69  ? 49.380 -10.881 13.099  1.00 19.74 ?  69  ILE   B HG22 1 
ATOM   5107 H HG23 . ILE   B 1 69  ? 47.867 -11.177 12.709  1.00 19.74 ?  69  ILE   B HG23 1 
ATOM   5108 H HD11 . ILE   B 1 69  ? 46.846 -13.123 9.635   1.00 19.25 ?  69  ILE   B HD11 1 
ATOM   5109 H HD12 . ILE   B 1 69  ? 46.967 -12.834 11.191  1.00 19.25 ?  69  ILE   B HD12 1 
ATOM   5110 H HD13 . ILE   B 1 69  ? 46.575 -11.663 10.191  1.00 19.25 ?  69  ILE   B HD13 1 
ATOM   5111 N N    . ALA   B 1 70  ? 49.986 -8.046  11.801  1.00 13.78 ?  70  ALA   B N    1 
ATOM   5112 C CA   . ALA   B 1 70  ? 50.262 -7.017  12.796  1.00 13.63 ?  70  ALA   B CA   1 
ATOM   5113 C C    . ALA   B 1 70  ? 49.274 -5.865  12.679  1.00 14.08 ?  70  ALA   B C    1 
ATOM   5114 O O    . ALA   B 1 70  ? 48.833 -5.311  13.690  1.00 14.50 ?  70  ALA   B O    1 
ATOM   5115 C CB   . ALA   B 1 70  ? 51.698 -6.519  12.640  1.00 14.02 ?  70  ALA   B CB   1 
ATOM   5116 H H    . ALA   B 1 70  ? 50.631 -8.219  11.267  1.00 16.54 ?  70  ALA   B H    1 
ATOM   5117 H HA   . ALA   B 1 70  ? 50.175 -7.399  13.684  1.00 16.36 ?  70  ALA   B HA   1 
ATOM   5118 H HB1  . ALA   B 1 70  ? 51.887 -5.863  13.333  1.00 16.82 ?  70  ALA   B HB1  1 
ATOM   5119 H HB2  . ALA   B 1 70  ? 52.308 -7.270  12.728  1.00 16.82 ?  70  ALA   B HB2  1 
ATOM   5120 H HB3  . ALA   B 1 70  ? 51.803 -6.112  11.765  1.00 16.82 ?  70  ALA   B HB3  1 
ATOM   5121 N N    . THR   B 1 71  ? 48.910 -5.497  11.452  1.00 14.34 ?  71  THR   B N    1 
ATOM   5122 C CA   . THR   B 1 71  ? 48.034 -4.351  11.238  1.00 15.06 ?  71  THR   B CA   1 
ATOM   5123 C C    . THR   B 1 71  ? 46.565 -4.703  11.443  1.00 15.50 ?  71  THR   B C    1 
ATOM   5124 O O    . THR   B 1 71  ? 45.797 -3.880  11.960  1.00 16.80 ?  71  THR   B O    1 
ATOM   5125 C CB   . THR   B 1 71  ? 48.266 -3.792  9.833   1.00 16.96 ?  71  THR   B CB   1 
ATOM   5126 O OG1  . THR   B 1 71  ? 49.599 -3.271  9.740   1.00 18.23 ?  71  THR   B OG1  1 
ATOM   5127 C CG2  . THR   B 1 71  ? 47.263 -2.694  9.501   1.00 17.88 ?  71  THR   B CG2  1 
ATOM   5128 H H    . THR   B 1 71  ? 49.162 -5.891  10.735  1.00 17.20 ?  71  THR   B H    1 
ATOM   5129 H HA   . THR   B 1 71  ? 48.261 -3.656  11.874  1.00 18.07 ?  71  THR   B HA   1 
ATOM   5130 H HB   . THR   B 1 71  ? 48.161 -4.506  9.182   1.00 20.35 ?  71  THR   B HB   1 
ATOM   5131 H HG1  . THR   B 1 71  ? 49.732 -2.959  8.968   1.00 21.87 ?  71  THR   B HG1  1 
ATOM   5132 H HG21 . THR   B 1 71  ? 47.573 -2.187  8.733   1.00 21.46 ?  71  THR   B HG21 1 
ATOM   5133 H HG22 . THR   B 1 71  ? 46.400 -3.081  9.293   1.00 21.46 ?  71  THR   B HG22 1 
ATOM   5134 H HG23 . THR   B 1 71  ? 47.171 -2.093  10.255  1.00 21.46 ?  71  THR   B HG23 1 
ATOM   5135 N N    . ASN   B 1 72  ? 46.157 -5.915  11.048  1.00 15.21 ?  72  ASN   B N    1 
ATOM   5136 C CA   . ASN   B 1 72  ? 44.750 -6.268  10.929  1.00 15.98 ?  72  ASN   B CA   1 
ATOM   5137 C C    . ASN   B 1 72  ? 44.279 -7.365  11.873  1.00 16.56 ?  72  ASN   B C    1 
ATOM   5138 O O    . ASN   B 1 72  ? 43.064 -7.515  12.048  1.00 17.67 ?  72  ASN   B O    1 
ATOM   5139 C CB   . ASN   B 1 72  ? 44.425 -6.683  9.483   1.00 16.83 ?  72  ASN   B CB   1 
ATOM   5140 C CG   . ASN   B 1 72  ? 44.707 -5.576  8.491   1.00 17.94 ?  72  ASN   B CG   1 
ATOM   5141 O OD1  . ASN   B 1 72  ? 45.716 -5.589  7.786   1.00 19.04 ?  72  ASN   B OD1  1 
ATOM   5142 N ND2  . ASN   B 1 72  ? 43.829 -4.591  8.452   1.00 19.54 ?  72  ASN   B ND2  1 
ATOM   5143 H H    . ASN   B 1 72  ? 46.696 -6.562  10.836  1.00 18.25 ?  72  ASN   B H    1 
ATOM   5144 H HA   . ASN   B 1 72  ? 44.226 -5.483  11.127  1.00 19.18 ?  72  ASN   B HA   1 
ATOM   5145 H HB2  . ASN   B 1 72  ? 44.971 -7.449  9.241   1.00 20.20 ?  72  ASN   B HB2  1 
ATOM   5146 H HB3  . ASN   B 1 72  ? 43.487 -6.909  9.422   1.00 20.20 ?  72  ASN   B HB3  1 
ATOM   5147 H HD21 . ASN   B 1 72  ? 43.938 -3.935  7.906   1.00 23.45 ?  72  ASN   B HD21 1 
ATOM   5148 H HD22 . ASN   B 1 72  ? 43.133 -4.613  8.960   1.00 23.45 ?  72  ASN   B HD22 1 
ATOM   5149 N N    . GLY   B 1 73  ? 45.181 -8.128  12.484  1.00 16.07 ?  73  GLY   B N    1 
ATOM   5150 C CA   . GLY   B 1 73  ? 44.791 -9.264  13.284  1.00 15.79 ?  73  GLY   B CA   1 
ATOM   5151 C C    . GLY   B 1 73  ? 44.412 -10.445 12.418  1.00 14.40 ?  73  GLY   B C    1 
ATOM   5152 O O    . GLY   B 1 73  ? 44.393 -10.359 11.189  1.00 14.24 ?  73  GLY   B O    1 
ATOM   5153 H H    . GLY   B 1 73  ? 46.036 -8.005  12.442  1.00 19.28 ?  73  GLY   B H    1 
ATOM   5154 H HA2  . GLY   B 1 73  ? 45.530 -9.522  13.864  1.00 18.95 ?  73  GLY   B HA2  1 
ATOM   5155 H HA3  . GLY   B 1 73  ? 44.034 -9.026  13.839  1.00 18.95 ?  73  GLY   B HA3  1 
ATOM   5156 N N    . PRO   B 1 74  ? 44.103 -11.572 13.056  1.00 14.62 ?  74  PRO   B N    1 
ATOM   5157 C CA   . PRO   B 1 74  ? 43.845 -12.805 12.309  1.00 13.77 ?  74  PRO   B CA   1 
ATOM   5158 C C    . PRO   B 1 74  ? 42.547 -12.736 11.519  1.00 13.25 ?  74  PRO   B C    1 
ATOM   5159 O O    . PRO   B 1 74  ? 41.609 -11.999 11.846  1.00 14.59 ?  74  PRO   B O    1 
ATOM   5160 C CB   . PRO   B 1 74  ? 43.758 -13.872 13.408  1.00 15.10 ?  74  PRO   B CB   1 
ATOM   5161 C CG   . PRO   B 1 74  ? 43.324 -13.113 14.624  1.00 16.70 ?  74  PRO   B CG   1 
ATOM   5162 C CD   . PRO   B 1 74  ? 44.015 -11.782 14.512  1.00 16.02 ?  74  PRO   B CD   1 
ATOM   5163 H HA   . PRO   B 1 74  ? 44.588 -13.008 11.716  1.00 16.53 ?  74  PRO   B HA   1 
ATOM   5164 H HB2  . PRO   B 1 74  ? 43.095 -14.541 13.163  1.00 18.12 ?  74  PRO   B HB2  1 
ATOM   5165 H HB3  . PRO   B 1 74  ? 44.625 -14.281 13.544  1.00 18.12 ?  74  PRO   B HB3  1 
ATOM   5166 H HG2  . PRO   B 1 74  ? 42.359 -13.005 14.616  1.00 20.03 ?  74  PRO   B HG2  1 
ATOM   5167 H HG3  . PRO   B 1 74  ? 43.609 -13.587 15.422  1.00 20.03 ?  74  PRO   B HG3  1 
ATOM   5168 H HD2  . PRO   B 1 74  ? 43.476 -11.091 14.929  1.00 19.23 ?  74  PRO   B HD2  1 
ATOM   5169 H HD3  . PRO   B 1 74  ? 44.900 -11.830 14.906  1.00 19.23 ?  74  PRO   B HD3  1 
ATOM   5170 N N    . LEU   B 1 75  ? 42.510 -13.556 10.471  1.00 12.38 ?  75  LEU   B N    1 
ATOM   5171 C CA   . LEU   B 1 75  ? 41.298 -13.758 9.701   1.00 12.23 ?  75  LEU   B CA   1 
ATOM   5172 C C    . LEU   B 1 75  ? 40.318 -14.618 10.496  1.00 12.76 ?  75  LEU   B C    1 
ATOM   5173 O O    . LEU   B 1 75  ? 40.654 -15.183 11.539  1.00 14.36 ?  75  LEU   B O    1 
ATOM   5174 C CB   . LEU   B 1 75  ? 41.619 -14.464 8.381   1.00 12.40 ?  75  LEU   B CB   1 
ATOM   5175 C CG   . LEU   B 1 75  ? 42.464 -13.713 7.349   1.00 14.26 ?  75  LEU   B CG   1 
ATOM   5176 C CD1  . LEU   B 1 75  ? 42.626 -14.534 6.075   1.00 15.74 ?  75  LEU   B CD1  1 
ATOM   5177 C CD2  . LEU   B 1 75  ? 41.896 -12.356 7.034   1.00 17.92 ?  75  LEU   B CD2  1 
ATOM   5178 H H    . LEU   B 1 75  ? 43.178 -14.026 10.189  1.00 14.85 ?  75  LEU   B H    1 
ATOM   5179 H HA   . LEU   B 1 75  ? 40.880 -12.907 9.512   1.00 14.68 ?  75  LEU   B HA   1 
ATOM   5180 H HB2  . LEU   B 1 75  ? 42.094 -15.286 8.588   1.00 14.87 ?  75  LEU   B HB2  1 
ATOM   5181 H HB3  . LEU   B 1 75  ? 40.780 -14.688 7.948   1.00 14.87 ?  75  LEU   B HB3  1 
ATOM   5182 H HG   . LEU   B 1 75  ? 43.350 -13.578 7.719   1.00 17.11 ?  75  LEU   B HG   1 
ATOM   5183 H HD11 . LEU   B 1 75  ? 43.169 -14.033 5.443   1.00 18.89 ?  75  LEU   B HD11 1 
ATOM   5184 H HD12 . LEU   B 1 75  ? 43.065 -15.372 6.291   1.00 18.89 ?  75  LEU   B HD12 1 
ATOM   5185 H HD13 . LEU   B 1 75  ? 41.752 -14.707 5.694   1.00 18.89 ?  75  LEU   B HD13 1 
ATOM   5186 H HD21 . LEU   B 1 75  ? 42.413 -11.952 6.321   1.00 21.50 ?  75  LEU   B HD21 1 
ATOM   5187 H HD22 . LEU   B 1 75  ? 40.972 -12.458 6.759   1.00 21.50 ?  75  LEU   B HD22 1 
ATOM   5188 H HD23 . LEU   B 1 75  ? 41.943 -11.801 7.831   1.00 21.50 ?  75  LEU   B HD23 1 
ATOM   5189 N N    . LYS   B 1 76  ? 39.090 -14.709 9.982   1.00 13.57 ?  76  LYS   B N    1 
ATOM   5190 C CA   . LYS   B 1 76  ? 38.101 -15.676 10.445  1.00 14.91 ?  76  LYS   B CA   1 
ATOM   5191 C C    . LYS   B 1 76  ? 38.195 -16.950 9.606   1.00 13.39 ?  76  LYS   B C    1 
ATOM   5192 O O    . LYS   B 1 76  ? 38.472 -16.895 8.410   1.00 13.14 ?  76  LYS   B O    1 
ATOM   5193 C CB   . LYS   B 1 76  ? 36.682 -15.111 10.256  1.00 17.56 ?  76  LYS   B CB   1 
ATOM   5194 C CG   . LYS   B 1 76  ? 36.387 -13.745 10.886  1.00 19.39 ?  76  LYS   B CG   1 
ATOM   5195 C CD   . LYS   B 1 76  ? 35.001 -13.199 10.483  1.00 20.58 ?  76  LYS   B CD   1 
ATOM   5196 C CE   . LYS   B 1 76  ? 34.737 -11.832 11.091  1.00 22.71 ?  76  LYS   B CE   1 
ATOM   5197 N NZ   . LYS   B 1 76  ? 33.459 -11.226 10.624  1.00 23.37 ?  76  LYS   B NZ   1 
ATOM   5198 H H    . LYS   B 1 76  ? 38.802 -14.213 9.343   1.00 16.28 ?  76  LYS   B H    1 
ATOM   5199 H HA   . LYS   B 1 76  ? 38.245 -15.895 11.381  1.00 17.89 ?  76  LYS   B HA   1 
ATOM   5200 H HB2  . LYS   B 1 76  ? 36.519 -15.030 9.303   1.00 21.07 ?  76  LYS   B HB2  1 
ATOM   5201 H HB3  . LYS   B 1 76  ? 36.054 -15.745 10.635  1.00 21.07 ?  76  LYS   B HB3  1 
ATOM   5202 H HG2  . LYS   B 1 76  ? 36.412 -13.831 11.852  1.00 23.27 ?  76  LYS   B HG2  1 
ATOM   5203 H HG3  . LYS   B 1 76  ? 37.061 -13.109 10.593  1.00 23.27 ?  76  LYS   B HG3  1 
ATOM   5204 H HD2  . LYS   B 1 76  ? 34.959 -13.117 9.516   1.00 24.69 ?  76  LYS   B HD2  1 
ATOM   5205 H HD3  . LYS   B 1 76  ? 34.315 -13.810 10.795  1.00 24.69 ?  76  LYS   B HD3  1 
ATOM   5206 H HE2  . LYS   B 1 76  ? 34.693 -11.919 12.055  1.00 27.25 ?  76  LYS   B HE2  1 
ATOM   5207 H HE3  . LYS   B 1 76  ? 35.459 -11.233 10.844  1.00 27.25 ?  76  LYS   B HE3  1 
ATOM   5208 H HZ1  . LYS   B 1 76  ? 33.341 -10.427 11.002  1.00 28.04 ?  76  LYS   B HZ1  1 
ATOM   5209 H HZ2  . LYS   B 1 76  ? 33.470 -11.124 9.739   1.00 28.04 ?  76  LYS   B HZ2  1 
ATOM   5210 H HZ3  . LYS   B 1 76  ? 32.771 -11.750 10.843  1.00 28.04 ?  76  LYS   B HZ3  1 
ATOM   5211 N N    . VAL   B 1 77  ? 37.936 -18.105 10.232  1.00 13.85 ?  77  VAL   B N    1 
ATOM   5212 C CA   . VAL   B 1 77  ? 37.735 -19.317 9.442   1.00 13.95 ?  77  VAL   B CA   1 
ATOM   5213 C C    . VAL   B 1 77  ? 36.542 -19.081 8.524   1.00 12.82 ?  77  VAL   B C    1 
ATOM   5214 O O    . VAL   B 1 77  ? 35.477 -18.630 8.967   1.00 13.23 ?  77  VAL   B O    1 
ATOM   5215 C CB   . VAL   B 1 77  ? 37.547 -20.553 10.338  1.00 15.31 ?  77  VAL   B CB   1 
ATOM   5216 C CG1  . VAL   B 1 77  ? 37.240 -21.771 9.483   1.00 15.72 ?  77  VAL   B CG1  1 
ATOM   5217 C CG2  . VAL   B 1 77  ? 38.795 -20.801 11.179  1.00 16.52 ?  77  VAL   B CG2  1 
ATOM   5218 H H    . VAL   B 1 77  ? 37.874 -18.208 11.079  1.00 16.62 ?  77  VAL   B H    1 
ATOM   5219 H HA   . VAL   B 1 77  ? 38.515 -19.465 8.884   1.00 16.74 ?  77  VAL   B HA   1 
ATOM   5220 H HB   . VAL   B 1 77  ? 36.798 -20.399 10.935  1.00 18.38 ?  77  VAL   B HB   1 
ATOM   5221 H HG11 . VAL   B 1 77  ? 37.305 -22.564 10.038  1.00 18.86 ?  77  VAL   B HG11 1 
ATOM   5222 H HG12 . VAL   B 1 77  ? 36.340 -21.693 9.127   1.00 18.86 ?  77  VAL   B HG12 1 
ATOM   5223 H HG13 . VAL   B 1 77  ? 37.881 -21.819 8.759   1.00 18.86 ?  77  VAL   B HG13 1 
ATOM   5224 H HG21 . VAL   B 1 77  ? 38.652 -21.592 11.719  1.00 19.82 ?  77  VAL   B HG21 1 
ATOM   5225 H HG22 . VAL   B 1 77  ? 39.549 -20.930 10.586  1.00 19.82 ?  77  VAL   B HG22 1 
ATOM   5226 H HG23 . VAL   B 1 77  ? 38.946 -20.031 11.748  1.00 19.82 ?  77  VAL   B HG23 1 
ATOM   5227 N N    . GLY   B 1 78  ? 36.725 -19.363 7.233   1.00 12.71 ?  78  GLY   B N    1 
ATOM   5228 C CA   . GLY   B 1 78  ? 35.758 -19.042 6.211   1.00 12.16 ?  78  GLY   B CA   1 
ATOM   5229 C C    . GLY   B 1 78  ? 36.004 -17.724 5.511   1.00 11.68 ?  78  GLY   B C    1 
ATOM   5230 O O    . GLY   B 1 78  ? 35.327 -17.438 4.517   1.00 12.56 ?  78  GLY   B O    1 
ATOM   5231 H H    . GLY   B 1 78  ? 37.430 -19.754 6.922   1.00 15.25 ?  78  GLY   B H    1 
ATOM   5232 H HA2  . GLY   B 1 78  ? 35.758 -19.740 5.543   1.00 14.59 ?  78  GLY   B HA2  1 
ATOM   5233 H HA3  . GLY   B 1 78  ? 34.876 -19.008 6.616   1.00 14.59 ?  78  GLY   B HA3  1 
ATOM   5234 N N    . GLY   B 1 79  ? 36.947 -16.915 6.005   1.00 11.88 ?  79  GLY   B N    1 
ATOM   5235 C CA   . GLY   B 1 79  ? 37.250 -15.620 5.432   1.00 11.98 ?  79  GLY   B CA   1 
ATOM   5236 C C    . GLY   B 1 79  ? 38.487 -15.642 4.546   1.00 11.36 ?  79  GLY   B C    1 
ATOM   5237 O O    . GLY   B 1 79  ? 39.097 -16.682 4.298   1.00 11.91 ?  79  GLY   B O    1 
ATOM   5238 H H    . GLY   B 1 79  ? 37.435 -17.104 6.684   1.00 14.26 ?  79  GLY   B H    1 
ATOM   5239 H HA2  . GLY   B 1 79  ? 36.498 -15.316 4.897   1.00 14.37 ?  79  GLY   B HA2  1 
ATOM   5240 H HA3  . GLY   B 1 79  ? 37.400 -14.978 6.141   1.00 14.37 ?  79  GLY   B HA3  1 
ATOM   5241 N N    . SER   B 1 80  ? 38.857 -14.446 4.075   1.00 11.41 ?  80  SER   B N    1 
ATOM   5242 C CA   . SER   B 1 80  ? 39.968 -14.316 3.143   1.00 11.30 ?  80  SER   B CA   1 
ATOM   5243 C C    . SER   B 1 80  ? 40.551 -12.912 3.209   1.00 11.16 ?  80  SER   B C    1 
ATOM   5244 O O    . SER   B 1 80  ? 39.932 -11.979 3.727   1.00 12.31 ?  80  SER   B O    1 
ATOM   5245 C CB   . SER   B 1 80  ? 39.527 -14.601 1.704   1.00 11.61 ?  80  SER   B CB   1 
ATOM   5246 O OG   . SER   B 1 80  ? 38.689 -13.577 1.199   1.00 12.72 ?  80  SER   B OG   1 
ATOM   5247 H H    . SER   B 1 80  ? 38.480 -13.703 4.283   1.00 13.69 ?  80  SER   B H    1 
ATOM   5248 H HA   . SER   B 1 80  ? 40.658 -14.946 3.393   1.00 13.56 ?  80  SER   B HA   1 
ATOM   5249 H HB2  . SER   B 1 80  ? 40.312 -14.664 1.137   1.00 13.93 ?  80  SER   B HB2  1 
ATOM   5250 H HB3  . SER   B 1 80  ? 39.041 -15.442 1.684   1.00 13.93 ?  80  SER   B HB3  1 
ATOM   5251 H HG   . SER   B 1 80  ? 37.995 -13.514 1.677   1.00 15.26 ?  80  SER   B HG   1 
ATOM   5252 N N    . CYS   B 1 81  ? 41.739 -12.764 2.626   1.00 11.11 ?  81  CYS   B N    1 
ATOM   5253 C CA   . CYS   B 1 81  ? 42.283 -11.450 2.325   1.00 11.34 ?  81  CYS   B CA   1 
ATOM   5254 C C    . CYS   B 1 81  ? 43.062 -11.526 1.021   1.00 10.73 ?  81  CYS   B C    1 
ATOM   5255 O O    . CYS   B 1 81  ? 43.569 -12.586 0.640   1.00 11.56 ?  81  CYS   B O    1 
ATOM   5256 C CB   . CYS   B 1 81  ? 43.165 -10.909 3.457   1.00 11.87 ?  81  CYS   B CB   1 
ATOM   5257 S SG   . CYS   B 1 81  ? 44.694 -11.851 3.694   1.00 12.38 ?  81  CYS   B SG   1 
ATOM   5258 H H    . CYS   B 1 81  ? 42.247 -13.414 2.384   1.00 13.33 ?  81  CYS   B H    1 
ATOM   5259 H HA   . CYS   B 1 81  ? 41.552 -10.826 2.195   1.00 13.61 ?  81  CYS   B HA   1 
ATOM   5260 H HB2  . CYS   B 1 81  ? 43.406 -9.992  3.262   1.00 14.24 ?  81  CYS   B HB2  1 
ATOM   5261 H HB3  . CYS   B 1 81  ? 42.658 -10.944 4.289   1.00 14.24 ?  81  CYS   B HB3  1 
ATOM   5262 H HG   . CYS   B 1 81  ? 45.317 -11.373 4.598   1.00 14.86 ?  81  CYS   B HG   1 
ATOM   5263 N N    . VAL   B 1 82  ? 43.162 -10.385 0.346   1.00 11.34 ?  82  VAL   B N    1 
ATOM   5264 C CA   . VAL   B 1 82  ? 43.916 -10.261 -0.897  1.00 11.27 ?  82  VAL   B CA   1 
ATOM   5265 C C    . VAL   B 1 82  ? 45.256 -9.616  -0.583  1.00 11.31 ?  82  VAL   B C    1 
ATOM   5266 O O    . VAL   B 1 82  ? 45.307 -8.499  -0.048  1.00 12.43 ?  82  VAL   B O    1 
ATOM   5267 C CB   . VAL   B 1 82  ? 43.167 -9.419  -1.941  1.00 12.53 ?  82  VAL   B CB   1 
ATOM   5268 C CG1  . VAL   B 1 82  ? 44.011 -9.271  -3.199  1.00 14.04 ?  82  VAL   B CG1  1 
ATOM   5269 C CG2  . VAL   B 1 82  ? 41.813 -10.022 -2.262  1.00 12.71 ?  82  VAL   B CG2  1 
ATOM   5270 H H    . VAL   B 1 82  ? 42.787 -9.648  0.595   1.00 13.61 ?  82  VAL   B H    1 
ATOM   5271 H HA   . VAL   B 1 82  ? 44.073 -11.140 -1.268  1.00 13.53 ?  82  VAL   B HA   1 
ATOM   5272 H HB   . VAL   B 1 82  ? 43.016 -8.533  -1.580  1.00 15.03 ?  82  VAL   B HB   1 
ATOM   5273 H HG11 . VAL   B 1 82  ? 43.448 -8.959  -3.925  1.00 16.85 ?  82  VAL   B HG11 1 
ATOM   5274 H HG12 . VAL   B 1 82  ? 44.718 -8.622  -3.034  1.00 16.85 ?  82  VAL   B HG12 1 
ATOM   5275 H HG13 . VAL   B 1 82  ? 44.399 -10.129 -3.426  1.00 16.85 ?  82  VAL   B HG13 1 
ATOM   5276 H HG21 . VAL   B 1 82  ? 41.379 -9.482  -2.945  1.00 15.26 ?  82  VAL   B HG21 1 
ATOM   5277 H HG22 . VAL   B 1 82  ? 41.936 -10.927 -2.592  1.00 15.26 ?  82  VAL   B HG22 1 
ATOM   5278 H HG23 . VAL   B 1 82  ? 41.270 -10.033 -1.459  1.00 15.26 ?  82  VAL   B HG23 1 
ATOM   5279 N N    . LEU   B 1 83  ? 46.337 -10.303 -0.944  1.00 11.24 ?  83  LEU   B N    1 
ATOM   5280 C CA   . LEU   B 1 83  ? 47.693 -9.786  -0.815  1.00 11.26 ?  83  LEU   B CA   1 
ATOM   5281 C C    . LEU   B 1 83  ? 48.400 -9.920  -2.163  1.00 10.88 ?  83  LEU   B C    1 
ATOM   5282 O O    . LEU   B 1 83  ? 47.800 -10.335 -3.161  1.00 11.24 ?  83  LEU   B O    1 
ATOM   5283 C CB   . LEU   B 1 83  ? 48.437 -10.470 0.340   1.00 11.36 ?  83  LEU   B CB   1 
ATOM   5284 C CG   . LEU   B 1 83  ? 47.928 -10.122 1.743   1.00 12.95 ?  83  LEU   B CG   1 
ATOM   5285 C CD1  . LEU   B 1 83  ? 48.584 -10.979 2.804   1.00 13.27 ?  83  LEU   B CD1  1 
ATOM   5286 C CD2  . LEU   B 1 83  ? 48.130 -8.638  2.062   1.00 14.00 ?  83  LEU   B CD2  1 
ATOM   5287 H H    . LEU   B 1 83  ? 46.303 -11.101 -1.272  1.00 13.49 ?  83  LEU   B H    1 
ATOM   5288 H HA   . LEU   B 1 83  ? 47.643 -8.845  -0.614  1.00 13.51 ?  83  LEU   B HA   1 
ATOM   5289 H HB2  . LEU   B 1 83  ? 48.363 -11.427 0.239   1.00 13.63 ?  83  LEU   B HB2  1 
ATOM   5290 H HB3  . LEU   B 1 83  ? 49.372 -10.209 0.299   1.00 13.63 ?  83  LEU   B HB3  1 
ATOM   5291 H HG   . LEU   B 1 83  ? 46.978 -10.290 1.775   1.00 15.55 ?  83  LEU   B HG   1 
ATOM   5292 H HD11 . LEU   B 1 83  ? 48.233 -10.733 3.675   1.00 15.92 ?  83  LEU   B HD11 1 
ATOM   5293 H HD12 . LEU   B 1 83  ? 48.383 -11.912 2.621   1.00 15.92 ?  83  LEU   B HD12 1 
ATOM   5294 H HD13 . LEU   B 1 83  ? 49.543 -10.838 2.783   1.00 15.92 ?  83  LEU   B HD13 1 
ATOM   5295 H HD21 . LEU   B 1 83  ? 47.934 -8.485  3.000   1.00 16.80 ?  83  LEU   B HD21 1 
ATOM   5296 H HD22 . LEU   B 1 83  ? 49.050 -8.393  1.873   1.00 16.80 ?  83  LEU   B HD22 1 
ATOM   5297 H HD23 . LEU   B 1 83  ? 47.530 -8.109  1.511   1.00 16.80 ?  83  LEU   B HD23 1 
ATOM   5298 N N    . SER   B 1 84  ? 49.677 -9.550  -2.208  1.00 11.93 ?  84  SER   B N    1 
ATOM   5299 C CA   . SER   B 1 84  ? 50.413 -9.652  -3.458  1.00 12.31 ?  84  SER   B CA   1 
ATOM   5300 C C    . SER   B 1 84  ? 50.572 -11.108 -3.882  1.00 11.40 ?  84  SER   B C    1 
ATOM   5301 O O    . SER   B 1 84  ? 50.680 -12.014 -3.055  1.00 11.27 ?  84  SER   B O    1 
ATOM   5302 C CB   . SER   B 1 84  ? 51.812 -9.048  -3.304  1.00 13.89 ?  84  SER   B CB   1 
ATOM   5303 O OG   . SER   B 1 84  ? 52.562 -9.267  -4.483  1.00 15.53 ?  84  SER   B OG   1 
ATOM   5304 H H    . SER   B 1 84  ? 50.126 -9.227  -1.542  1.00 14.32 ?  84  SER   B H    1 
ATOM   5305 H HA   . SER   B 1 84  ? 49.946 -9.172  -4.154  1.00 14.77 ?  84  SER   B HA   1 
ATOM   5306 H HB2  . SER   B 1 84  ? 51.734 -8.090  -3.142  1.00 16.67 ?  84  SER   B HB2  1 
ATOM   5307 H HB3  . SER   B 1 84  ? 52.271 -9.472  -2.564  1.00 16.67 ?  84  SER   B HB3  1 
ATOM   5308 H HG   . SER   B 1 84  ? 53.326 -8.919  -4.412  1.00 18.63 ?  84  SER   B HG   1 
ATOM   5309 N N    . GLY   B 1 85  ? 50.643 -11.322 -5.190  1.00 12.59 ?  85  GLY   B N    1 
ATOM   5310 C CA   . GLY   B 1 85  ? 50.986 -12.614 -5.733  1.00 13.34 ?  85  GLY   B CA   1 
ATOM   5311 C C    . GLY   B 1 85  ? 52.457 -12.813 -6.026  1.00 12.20 ?  85  GLY   B C    1 
ATOM   5312 O O    . GLY   B 1 85  ? 52.831 -13.899 -6.478  1.00 12.70 ?  85  GLY   B O    1 
ATOM   5313 H H    . GLY   B 1 85  ? 50.509 -10.723 -5.784  1.00 15.10 ?  85  GLY   B H    1 
ATOM   5314 H HA2  . GLY   B 1 85  ? 50.711 -13.305 -5.106  1.00 16.00 ?  85  GLY   B HA2  1 
ATOM   5315 H HA3  . GLY   B 1 85  ? 50.501 -12.748 -6.557  1.00 16.00 ?  85  GLY   B HA3  1 
ATOM   5316 N N    . HIS   B 1 86  ? 53.304 -11.813 -5.796  1.00 12.05 ?  86  HIS   B N    1 
ATOM   5317 C CA   . HIS   B 1 86  ? 54.766 -11.985 -5.883  1.00 12.15 ?  86  HIS   B CA   1 
ATOM   5318 C C    . HIS   B 1 86  ? 55.135 -12.495 -7.275  1.00 12.28 ?  86  HIS   B C    1 
ATOM   5319 O O    . HIS   B 1 86  ? 54.747 -11.879 -8.280  1.00 13.27 ?  86  HIS   B O    1 
ATOM   5320 C CB   . HIS   B 1 86  ? 55.261 -12.832 -4.709  1.00 12.66 ?  86  HIS   B CB   1 
ATOM   5321 C CG   . HIS   B 1 86  ? 54.948 -12.231 -3.381  1.00 12.64 ?  86  HIS   B CG   1 
ATOM   5322 N ND1  . HIS   B 1 86  ? 55.774 -11.323 -2.759  1.00 14.19 ?  86  HIS   B ND1  1 
ATOM   5323 C CD2  . HIS   B 1 86  ? 53.872 -12.378 -2.573  1.00 13.11 ?  86  HIS   B CD2  1 
ATOM   5324 C CE1  . HIS   B 1 86  ? 55.223 -10.942 -1.621  1.00 14.25 ?  86  HIS   B CE1  1 
ATOM   5325 N NE2  . HIS   B 1 86  ? 54.061 -11.557 -1.491  1.00 13.46 ?  86  HIS   B NE2  1 
ATOM   5326 H H    . HIS   B 1 86  ? 53.067 -11.017 -5.583  1.00 14.46 ?  86  HIS   B H    1 
ATOM   5327 H HA   . HIS   B 1 86  ? 55.177 -11.118 -5.785  1.00 14.58 ?  86  HIS   B HA   1 
ATOM   5328 H HB2  . HIS   B 1 86  ? 54.848 -13.709 -4.747  1.00 15.19 ?  86  HIS   B HB2  1 
ATOM   5329 H HB3  . HIS   B 1 86  ? 56.230 -12.927 -4.773  1.00 15.19 ?  86  HIS   B HB3  1 
ATOM   5330 H HD2  . HIS   B 1 86  ? 53.133 -12.915 -2.736  1.00 15.73 ?  86  HIS   B HD2  1 
ATOM   5331 H HE1  . HIS   B 1 86  ? 55.599 -10.347 -1.011  1.00 17.10 ?  86  HIS   B HE1  1 
ATOM   5332 H HE2  . HIS   B 1 86  ? 53.530 -11.480 -0.822  1.00 16.16 ?  86  HIS   B HE2  1 
ATOM   5333 N N    . ASN   B 1 87  ? 55.910 -13.574 -7.387  1.00 12.67 ?  87  ASN   B N    1 
ATOM   5334 C CA   . ASN   B 1 87  ? 56.304 -14.150 -8.666  1.00 13.33 ?  87  ASN   B CA   1 
ATOM   5335 C C    . ASN   B 1 87  ? 55.316 -15.189 -9.174  1.00 13.18 ?  87  ASN   B C    1 
ATOM   5336 O O    . ASN   B 1 87  ? 55.616 -15.885 -10.147 1.00 15.27 ?  87  ASN   B O    1 
ATOM   5337 C CB   . ASN   B 1 87  ? 57.695 -14.788 -8.552  1.00 15.42 ?  87  ASN   B CB   1 
ATOM   5338 C CG   . ASN   B 1 87  ? 57.752 -15.890 -7.500  1.00 16.11 ?  87  ASN   B CG   1 
ATOM   5339 O OD1  . ASN   B 1 87  ? 57.114 -15.800 -6.447  1.00 15.48 ?  87  ASN   B OD1  1 
ATOM   5340 N ND2  . ASN   B 1 87  ? 58.497 -16.956 -7.798  1.00 18.22 ?  87  ASN   B ND2  1 
ATOM   5341 H H    . ASN   B 1 87  ? 56.229 -14.005 -6.714  1.00 15.21 ?  87  ASN   B H    1 
ATOM   5342 H HA   . ASN   B 1 87  ? 56.358 -13.444 -9.325  1.00 15.99 ?  87  ASN   B HA   1 
ATOM   5343 H HB2  . ASN   B 1 87  ? 57.934 -15.179 -9.410  1.00 18.50 ?  87  ASN   B HB2  1 
ATOM   5344 H HB3  . ASN   B 1 87  ? 58.336 -14.107 -8.308  1.00 18.50 ?  87  ASN   B HB3  1 
ATOM   5345 H HD21 . ASN   B 1 87  ? 58.562 -17.604 -7.237  1.00 21.86 ?  87  ASN   B HD21 1 
ATOM   5346 H HD22 . ASN   B 1 87  ? 58.919 -16.991 -8.547  1.00 21.86 ?  87  ASN   B HD22 1 
ATOM   5347 N N    . LEU   B 1 88  ? 54.147 -15.300 -8.547  1.00 12.16 ?  88  LEU   B N    1 
ATOM   5348 C CA   . LEU   B 1 88  ? 53.167 -16.329 -8.870  1.00 12.67 ?  88  LEU   B CA   1 
ATOM   5349 C C    . LEU   B 1 88  ? 51.933 -15.817 -9.596  1.00 12.07 ?  88  LEU   B C    1 
ATOM   5350 O O    . LEU   B 1 88  ? 51.332 -16.570 -10.373 1.00 14.04 ?  88  LEU   B O    1 
ATOM   5351 C CB   . LEU   B 1 88  ? 52.698 -17.013 -7.580  1.00 13.73 ?  88  LEU   B CB   1 
ATOM   5352 C CG   . LEU   B 1 88  ? 53.823 -17.662 -6.779  1.00 15.73 ?  88  LEU   B CG   1 
ATOM   5353 C CD1  . LEU   B 1 88  ? 53.332 -18.063 -5.400  1.00 17.33 ?  88  LEU   B CD1  1 
ATOM   5354 C CD2  . LEU   B 1 88  ? 54.380 -18.857 -7.530  1.00 19.29 ?  88  LEU   B CD2  1 
ATOM   5355 H H    . LEU   B 1 88  ? 53.893 -14.779 -7.906  1.00 14.59 ?  88  LEU   B H    1 
ATOM   5356 H HA   . LEU   B 1 88  ? 53.579 -17.000 -9.423  1.00 15.20 ?  88  LEU   B HA   1 
ATOM   5357 H HB2  . LEU   B 1 88  ? 52.271 -16.353 -7.004  1.00 16.47 ?  88  LEU   B HB2  1 
ATOM   5358 H HB3  . LEU   B 1 88  ? 52.055 -17.707 -7.803  1.00 16.47 ?  88  LEU   B HB3  1 
ATOM   5359 H HG   . LEU   B 1 88  ? 54.538 -17.020 -6.664  1.00 18.88 ?  88  LEU   B HG   1 
ATOM   5360 H HD11 . LEU   B 1 88  ? 54.024 -18.578 -4.954  1.00 20.79 ?  88  LEU   B HD11 1 
ATOM   5361 H HD12 . LEU   B 1 88  ? 53.133 -17.264 -4.888  1.00 20.79 ?  88  LEU   B HD12 1 
ATOM   5362 H HD13 . LEU   B 1 88  ? 52.531 -18.603 -5.495  1.00 20.79 ?  88  LEU   B HD13 1 
ATOM   5363 H HD21 . LEU   B 1 88  ? 55.017 -19.319 -6.958  1.00 23.14 ?  88  LEU   B HD21 1 
ATOM   5364 H HD22 . LEU   B 1 88  ? 53.653 -19.454 -7.762  1.00 23.14 ?  88  LEU   B HD22 1 
ATOM   5365 H HD23 . LEU   B 1 88  ? 54.826 -18.547 -8.333  1.00 23.14 ?  88  LEU   B HD23 1 
ATOM   5366 N N    . ALA   B 1 89  ? 51.530 -14.577 -9.343  1.00 11.51 ?  89  ALA   B N    1 
ATOM   5367 C CA   . ALA   B 1 89  ? 50.234 -14.085 -9.785  1.00 11.37 ?  89  ALA   B CA   1 
ATOM   5368 C C    . ALA   B 1 89  ? 50.214 -12.593 -9.515  1.00 11.61 ?  89  ALA   B C    1 
ATOM   5369 O O    . ALA   B 1 89  ? 51.047 -12.080 -8.768  1.00 12.26 ?  89  ALA   B O    1 
ATOM   5370 C CB   . ALA   B 1 89  ? 49.103 -14.750 -9.003  1.00 11.44 ?  89  ALA   B CB   1 
ATOM   5371 H H    . ALA   B 1 89  ? 51.994 -13.991 -8.913  1.00 13.82 ?  89  ALA   B H    1 
ATOM   5372 H HA   . ALA   B 1 89  ? 50.109 -14.245 -10.734 1.00 13.64 ?  89  ALA   B HA   1 
ATOM   5373 H HB1  . ALA   B 1 89  ? 48.252 -14.413 -9.327  1.00 13.72 ?  89  ALA   B HB1  1 
ATOM   5374 H HB2  . ALA   B 1 89  ? 49.150 -15.711 -9.137  1.00 13.72 ?  89  ALA   B HB2  1 
ATOM   5375 H HB3  . ALA   B 1 89  ? 49.205 -14.542 -8.062  1.00 13.72 ?  89  ALA   B HB3  1 
ATOM   5376 N N    . LYS   B 1 90  ? 49.217 -11.904 -10.067 1.00 12.66 ?  90  LYS   B N    1 
ATOM   5377 C CA   . LYS   B 1 90  ? 49.030 -10.516 -9.664  1.00 12.87 ?  90  LYS   B CA   1 
ATOM   5378 C C    . LYS   B 1 90  ? 48.713 -10.438 -8.174  1.00 12.08 ?  90  LYS   B C    1 
ATOM   5379 O O    . LYS   B 1 90  ? 49.345 -9.677  -7.424  1.00 13.63 ?  90  LYS   B O    1 
ATOM   5380 C CB   . LYS   B 1 90  ? 47.950 -9.854  -10.520 1.00 14.12 ?  90  LYS   B CB   1 
ATOM   5381 C CG   . LYS   B 1 90  ? 47.663 -8.414  -10.147 1.00 14.61 ?  90  LYS   B CG   1 
ATOM   5382 C CD   . LYS   B 1 90  ? 48.865 -7.517  -10.271 1.00 17.61 ?  90  LYS   B CD   1 
ATOM   5383 C CE   . LYS   B 1 90  ? 48.416 -6.103  -9.998  1.00 20.04 ?  90  LYS   B CE   1 
ATOM   5384 N NZ   . LYS   B 1 90  ? 49.538 -5.152  -9.907  1.00 20.38 ?  90  LYS   B NZ   1 
ATOM   5385 H H    . LYS   B 1 90  ? 48.654 -12.208 -10.646 1.00 15.19 ?  90  LYS   B H    1 
ATOM   5386 H HA   . LYS   B 1 90  ? 49.855 -10.041 -9.811  1.00 15.44 ?  90  LYS   B HA   1 
ATOM   5387 H HB2  . LYS   B 1 90  ? 48.241 -9.863  -11.448 1.00 16.94 ?  90  LYS   B HB2  1 
ATOM   5388 H HB3  . LYS   B 1 90  ? 47.125 -10.355 -10.434 1.00 16.94 ?  90  LYS   B HB3  1 
ATOM   5389 H HG2  . LYS   B 1 90  ? 46.971 -8.071  -10.735 1.00 17.53 ?  90  LYS   B HG2  1 
ATOM   5390 H HG3  . LYS   B 1 90  ? 47.352 -8.381  -9.226  1.00 17.53 ?  90  LYS   B HG3  1 
ATOM   5391 H HD2  . LYS   B 1 90  ? 49.535 -7.769  -9.615  1.00 21.13 ?  90  LYS   B HD2  1 
ATOM   5392 H HD3  . LYS   B 1 90  ? 49.225 -7.571  -11.171 1.00 21.13 ?  90  LYS   B HD3  1 
ATOM   5393 H HE2  . LYS   B 1 90  ? 47.836 -5.810  -10.720 1.00 24.04 ?  90  LYS   B HE2  1 
ATOM   5394 H HE3  . LYS   B 1 90  ? 47.937 -6.078  -9.157  1.00 24.04 ?  90  LYS   B HE3  1 
ATOM   5395 H HZ1  . LYS   B 1 90  ? 49.233 -4.330  -9.748  1.00 24.46 ?  90  LYS   B HZ1  1 
ATOM   5396 H HZ2  . LYS   B 1 90  ? 50.088 -5.388  -9.247  1.00 24.46 ?  90  LYS   B HZ2  1 
ATOM   5397 H HZ3  . LYS   B 1 90  ? 49.997 -5.144  -10.673 1.00 24.46 ?  90  LYS   B HZ3  1 
ATOM   5398 N N    . HIS   B 1 91  ? 47.758 -11.260 -7.728  1.00 10.99 ?  91  HIS   B N    1 
ATOM   5399 C CA   . HIS   B 1 91  ? 47.285 -11.284 -6.358  1.00 11.04 ?  91  HIS   B CA   1 
ATOM   5400 C C    . HIS   B 1 91  ? 47.280 -12.712 -5.840  1.00 10.32 ?  91  HIS   B C    1 
ATOM   5401 O O    . HIS   B 1 91  ? 47.048 -13.662 -6.595  1.00 11.09 ?  91  HIS   B O    1 
ATOM   5402 C CB   . HIS   B 1 91  ? 45.829 -10.794 -6.250  1.00 13.07 ?  91  HIS   B CB   1 
ATOM   5403 C CG   . HIS   B 1 91  ? 45.624 -9.384  -6.686  1.00 16.17 ?  91  HIS   B CG   1 
ATOM   5404 N ND1  . HIS   B 1 91  ? 46.239 -8.313  -6.071  1.00 18.46 ?  91  HIS   B ND1  1 
ATOM   5405 C CD2  . HIS   B 1 91  ? 44.841 -8.860  -7.656  1.00 18.70 ?  91  HIS   B CD2  1 
ATOM   5406 C CE1  . HIS   B 1 91  ? 45.863 -7.190  -6.660  1.00 19.64 ?  91  HIS   B CE1  1 
ATOM   5407 N NE2  . HIS   B 1 91  ? 45.005 -7.495  -7.619  1.00 19.82 ?  91  HIS   B NE2  1 
ATOM   5408 H H    . HIS   B 1 91  ? 47.356 -11.842 -8.225  1.00 13.19 ?  91  HIS   B H    1 
ATOM   5409 H HA   . HIS   B 1 91  ? 47.851 -10.729 -5.792  1.00 13.25 ?  91  HIS   B HA   1 
ATOM   5410 H HB2  . HIS   B 1 91  ? 45.266 -11.352 -6.806  1.00 15.68 ?  91  HIS   B HB2  1 
ATOM   5411 H HB3  . HIS   B 1 91  ? 45.540 -10.855 -5.324  1.00 15.68 ?  91  HIS   B HB3  1 
ATOM   5412 H HD1  . HIS   B 1 91  ? 46.793 -8.366  -5.412  1.00 22.16 ?  91  HIS   B HD1  1 
ATOM   5413 H HD2  . HIS   B 1 91  ? 44.298 -9.324  -8.244  1.00 22.44 ?  91  HIS   B HD2  1 
ATOM   5414 H HE1  . HIS   B 1 91  ? 46.148 -6.330  -6.426  1.00 23.57 ?  91  HIS   B HE1  1 
ATOM   5415 N N    . CYS   B 1 92  ? 47.470 -12.844 -4.535  1.00 10.31 ?  92  CYS   B N    1 
ATOM   5416 C CA   . CYS   B 1 92  ? 47.174 -14.078 -3.824  1.00 10.03 ?  92  CYS   B CA   1 
ATOM   5417 C C    . CYS   B 1 92  ? 45.950 -13.844 -2.945  1.00 9.79  ?  92  CYS   B C    1 
ATOM   5418 O O    . CYS   B 1 92  ? 45.949 -12.949 -2.088  1.00 10.69 ?  92  CYS   B O    1 
ATOM   5419 C CB   . CYS   B 1 92  ? 48.351 -14.540 -2.970  1.00 10.53 ?  92  CYS   B CB   1 
ATOM   5420 S SG   . CYS   B 1 92  ? 47.987 -16.079 -2.081  1.00 10.79 ?  92  CYS   B SG   1 
ATOM   5421 H H    . CYS   B 1 92  ? 47.793 -12.222 -4.027  1.00 12.37 ?  92  CYS   B H    1 
ATOM   5422 H HA   . CYS   B 1 92  ? 46.973 -14.775 -4.466  1.00 12.04 ?  92  CYS   B HA   1 
ATOM   5423 H HB2  . CYS   B 1 92  ? 49.117 -14.689 -3.537  1.00 12.63 ?  92  CYS   B HB2  1 
ATOM   5424 H HB3  . CYS   B 1 92  ? 48.547 -13.850 -2.312  1.00 12.63 ?  92  CYS   B HB3  1 
ATOM   5425 H HG   . CYS   B 1 92  ? 48.954 -16.398 -1.450  1.00 12.95 ?  92  CYS   B HG   1 
ATOM   5426 N N    . LEU   B 1 93  ? 44.909 -14.647 -3.167  1.00 9.83  ?  93  LEU   B N    1 
ATOM   5427 C CA   . LEU   B 1 93  ? 43.736 -14.671 -2.302  1.00 9.73  ?  93  LEU   B CA   1 
ATOM   5428 C C    . LEU   B 1 93  ? 43.966 -15.739 -1.237  1.00 9.35  ?  93  LEU   B C    1 
ATOM   5429 O O    . LEU   B 1 93  ? 43.922 -16.941 -1.535  1.00 10.15 ?  93  LEU   B O    1 
ATOM   5430 C CB   . LEU   B 1 93  ? 42.478 -14.971 -3.111  1.00 10.53 ?  93  LEU   B CB   1 
ATOM   5431 C CG   . LEU   B 1 93  ? 41.180 -14.990 -2.303  1.00 10.89 ?  93  LEU   B CG   1 
ATOM   5432 C CD1  . LEU   B 1 93  ? 40.812 -13.602 -1.801  1.00 11.59 ?  93  LEU   B CD1  1 
ATOM   5433 C CD2  . LEU   B 1 93  ? 40.045 -15.568 -3.137  1.00 11.44 ?  93  LEU   B CD2  1 
ATOM   5434 H H    . LEU   B 1 93  ? 44.864 -15.199 -3.832  1.00 11.79 ?  93  LEU   B H    1 
ATOM   5435 H HA   . LEU   B 1 93  ? 43.638 -13.813 -1.870  1.00 11.68 ?  93  LEU   B HA   1 
ATOM   5436 H HB2  . LEU   B 1 93  ? 42.382 -14.284 -3.793  1.00 12.63 ?  93  LEU   B HB2  1 
ATOM   5437 H HB3  . LEU   B 1 93  ? 42.572 -15.835 -3.530  1.00 12.63 ?  93  LEU   B HB3  1 
ATOM   5438 H HG   . LEU   B 1 93  ? 41.295 -15.561 -1.532  1.00 13.07 ?  93  LEU   B HG   1 
ATOM   5439 H HD11 . LEU   B 1 93  ? 39.959 -13.646 -1.340  1.00 13.91 ?  93  LEU   B HD11 1 
ATOM   5440 H HD12 . LEU   B 1 93  ? 41.500 -13.292 -1.192  1.00 13.91 ?  93  LEU   B HD12 1 
ATOM   5441 H HD13 . LEU   B 1 93  ? 40.745 -12.996 -2.558  1.00 13.91 ?  93  LEU   B HD13 1 
ATOM   5442 H HD21 . LEU   B 1 93  ? 39.230 -15.562 -2.611  1.00 13.73 ?  93  LEU   B HD21 1 
ATOM   5443 H HD22 . LEU   B 1 93  ? 39.927 -15.022 -3.933  1.00 13.73 ?  93  LEU   B HD22 1 
ATOM   5444 H HD23 . LEU   B 1 93  ? 40.270 -16.476 -3.391  1.00 13.73 ?  93  LEU   B HD23 1 
ATOM   5445 N N    . HIS   B 1 94  ? 44.238 -15.304 -0.010  1.00 9.42  ?  94  HIS   B N    1 
ATOM   5446 C CA   . HIS   B 1 94  ? 44.454 -16.214 1.109   1.00 9.42  ?  94  HIS   B CA   1 
ATOM   5447 C C    . HIS   B 1 94  ? 43.089 -16.573 1.676   1.00 9.99  ?  94  HIS   B C    1 
ATOM   5448 O O    . HIS   B 1 94  ? 42.410 -15.705 2.227   1.00 11.52 ?  94  HIS   B O    1 
ATOM   5449 C CB   . HIS   B 1 94  ? 45.324 -15.540 2.169   1.00 9.87  ?  94  HIS   B CB   1 
ATOM   5450 C CG   . HIS   B 1 94  ? 46.705 -15.238 1.698   1.00 9.96  ?  94  HIS   B CG   1 
ATOM   5451 N ND1  . HIS   B 1 94  ? 47.731 -16.157 1.770   1.00 10.26 ?  94  HIS   B ND1  1 
ATOM   5452 C CD2  . HIS   B 1 94  ? 47.210 -14.127 1.108   1.00 10.27 ?  94  HIS   B CD2  1 
ATOM   5453 C CE1  . HIS   B 1 94  ? 48.820 -15.601 1.264   1.00 10.42 ?  94  HIS   B CE1  1 
ATOM   5454 N NE2  . HIS   B 1 94  ? 48.532 -14.375 0.850   1.00 10.65 ?  94  HIS   B NE2  1 
ATOM   5455 H H    . HIS   B 1 94  ? 44.304 -14.468 0.204   1.00 11.30 ?  94  HIS   B H    1 
ATOM   5456 H HA   . HIS   B 1 94  ? 44.897 -17.020 0.798   1.00 11.31 ?  94  HIS   B HA   1 
ATOM   5457 H HB2  . HIS   B 1 94  ? 44.909 -14.704 2.429   1.00 11.84 ?  94  HIS   B HB2  1 
ATOM   5458 H HB3  . HIS   B 1 94  ? 45.396 -16.129 2.935   1.00 11.84 ?  94  HIS   B HB3  1 
ATOM   5459 H HD2  . HIS   B 1 94  ? 46.750 -13.341 0.917   1.00 12.32 ?  94  HIS   B HD2  1 
ATOM   5460 H HE1  . HIS   B 1 94  ? 49.655 -16.010 1.199   1.00 12.50 ?  94  HIS   B HE1  1 
ATOM   5461 H HE2  . HIS   B 1 94  ? 49.086 -13.825 0.485   1.00 12.78 ?  94  HIS   B HE2  1 
ATOM   5462 N N    . VAL   B 1 95  ? 42.664 -17.828 1.517   1.00 9.84  ?  95  VAL   B N    1 
ATOM   5463 C CA   . VAL   B 1 95  ? 41.334 -18.263 1.945   1.00 10.28 ?  95  VAL   B CA   1 
ATOM   5464 C C    . VAL   B 1 95  ? 41.496 -19.301 3.041   1.00 10.22 ?  95  VAL   B C    1 
ATOM   5465 O O    . VAL   B 1 95  ? 42.267 -20.255 2.884   1.00 10.78 ?  95  VAL   B O    1 
ATOM   5466 C CB   . VAL   B 1 95  ? 40.517 -18.863 0.785   1.00 10.36 ?  95  VAL   B CB   1 
ATOM   5467 C CG1  . VAL   B 1 95  ? 39.133 -19.313 1.273   1.00 11.51 ?  95  VAL   B CG1  1 
ATOM   5468 C CG2  . VAL   B 1 95  ? 40.386 -17.883 -0.349  1.00 10.68 ?  95  VAL   B CG2  1 
ATOM   5469 H H    . VAL   B 1 95  ? 43.128 -18.454 1.146   1.00 11.80 ?  95  VAL   B H    1 
ATOM   5470 H HA   . VAL   B 1 95  ? 40.842 -17.513 2.306   1.00 12.34 ?  95  VAL   B HA   1 
ATOM   5471 H HB   . VAL   B 1 95  ? 40.966 -19.645 0.444   1.00 12.44 ?  95  VAL   B HB   1 
ATOM   5472 H HG11 . VAL   B 1 95  ? 38.566 -19.499 0.502   1.00 13.82 ?  95  VAL   B HG11 1 
ATOM   5473 H HG12 . VAL   B 1 95  ? 39.224 -20.113 1.810   1.00 13.82 ?  95  VAL   B HG12 1 
ATOM   5474 H HG13 . VAL   B 1 95  ? 38.732 -18.601 1.802   1.00 13.82 ?  95  VAL   B HG13 1 
ATOM   5475 H HG21 . VAL   B 1 95  ? 39.802 -18.255 -1.030  1.00 12.81 ?  95  VAL   B HG21 1 
ATOM   5476 H HG22 . VAL   B 1 95  ? 39.999 -17.054 -0.009  1.00 12.81 ?  95  VAL   B HG22 1 
ATOM   5477 H HG23 . VAL   B 1 95  ? 41.261 -17.710 -0.717  1.00 12.81 ?  95  VAL   B HG23 1 
ATOM   5478 N N    . VAL   B 1 96  ? 40.758 -19.132 4.135   1.00 10.72 ?  96  VAL   B N    1 
ATOM   5479 C CA   . VAL   B 1 96  ? 40.836 -20.043 5.276   1.00 10.91 ?  96  VAL   B CA   1 
ATOM   5480 C C    . VAL   B 1 96  ? 39.646 -20.999 5.232   1.00 11.25 ?  96  VAL   B C    1 
ATOM   5481 O O    . VAL   B 1 96  ? 38.528 -20.643 5.614   1.00 12.24 ?  96  VAL   B O    1 
ATOM   5482 C CB   . VAL   B 1 96  ? 40.895 -19.292 6.608   1.00 11.86 ?  96  VAL   B CB   1 
ATOM   5483 C CG1  . VAL   B 1 96  ? 41.068 -20.288 7.753   1.00 12.46 ?  96  VAL   B CG1  1 
ATOM   5484 C CG2  . VAL   B 1 96  ? 42.016 -18.257 6.596   1.00 12.43 ?  96  VAL   B CG2  1 
ATOM   5485 H H    . VAL   B 1 96  ? 40.190 -18.493 4.242   1.00 12.86 ?  96  VAL   B H    1 
ATOM   5486 H HA   . VAL   B 1 96  ? 41.645 -20.573 5.197   1.00 13.10 ?  96  VAL   B HA   1 
ATOM   5487 H HB   . VAL   B 1 96  ? 40.055 -18.826 6.740   1.00 14.23 ?  96  VAL   B HB   1 
ATOM   5488 H HG11 . VAL   B 1 96  ? 41.262 -19.797 8.570   1.00 14.95 ?  96  VAL   B HG11 1 
ATOM   5489 H HG12 . VAL   B 1 96  ? 40.248 -20.795 7.864   1.00 14.95 ?  96  VAL   B HG12 1 
ATOM   5490 H HG13 . VAL   B 1 96  ? 41.804 -20.885 7.548   1.00 14.95 ?  96  VAL   B HG13 1 
ATOM   5491 H HG21 . VAL   B 1 96  ? 42.080 -17.850 7.474   1.00 14.91 ?  96  VAL   B HG21 1 
ATOM   5492 H HG22 . VAL   B 1 96  ? 42.849 -18.690 6.367   1.00 14.91 ?  96  VAL   B HG22 1 
ATOM   5493 H HG23 . VAL   B 1 96  ? 41.807 -17.572 5.934   1.00 14.91 ?  96  VAL   B HG23 1 
ATOM   5494 N N    . GLY   B 1 97  ? 39.881 -22.232 4.793   1.00 11.48 ?  97  GLY   B N    1 
ATOM   5495 C CA   . GLY   B 1 97  ? 38.905 -23.286 4.949   1.00 11.87 ?  97  GLY   B CA   1 
ATOM   5496 C C    . GLY   B 1 97  ? 39.012 -23.893 6.330   1.00 12.56 ?  97  GLY   B C    1 
ATOM   5497 O O    . GLY   B 1 97  ? 40.047 -23.769 6.998   1.00 12.94 ?  97  GLY   B O    1 
ATOM   5498 H H    . GLY   B 1 97  ? 40.615 -22.480 4.405   1.00 13.78 ?  97  GLY   B H    1 
ATOM   5499 H HA2  . GLY   B 1 97  ? 38.015 -22.918 4.820   1.00 14.24 ?  97  GLY   B HA2  1 
ATOM   5500 H HA3  . GLY   B 1 97  ? 39.057 -23.974 4.278   1.00 14.24 ?  97  GLY   B HA3  1 
ATOM   5501 N N    . PRO   B 1 98  ? 37.956 -24.562 6.793   1.00 13.23 ?  98  PRO   B N    1 
ATOM   5502 C CA   . PRO   B 1 98  ? 38.045 -25.258 8.079   1.00 14.04 ?  98  PRO   B CA   1 
ATOM   5503 C C    . PRO   B 1 98  ? 39.069 -26.382 8.038   1.00 13.61 ?  98  PRO   B C    1 
ATOM   5504 O O    . PRO   B 1 98  ? 39.179 -27.115 7.057   1.00 13.66 ?  98  PRO   B O    1 
ATOM   5505 C CB   . PRO   B 1 98  ? 36.627 -25.803 8.278   1.00 14.25 ?  98  PRO   B CB   1 
ATOM   5506 C CG   . PRO   B 1 98  ? 36.082 -25.951 6.903   1.00 14.06 ?  98  PRO   B CG   1 
ATOM   5507 C CD   . PRO   B 1 98  ? 36.643 -24.764 6.153   1.00 13.23 ?  98  PRO   B CD   1 
ATOM   5508 H HA   . PRO   B 1 98  ? 38.267 -24.637 8.784   1.00 16.85 ?  98  PRO   B HA   1 
ATOM   5509 H HB2  . PRO   B 1 98  ? 36.669 -26.664 8.725   1.00 17.10 ?  98  PRO   B HB2  1 
ATOM   5510 H HB3  . PRO   B 1 98  ? 36.103 -25.171 8.788   1.00 17.10 ?  98  PRO   B HB3  1 
ATOM   5511 H HG2  . PRO   B 1 98  ? 36.397 -26.785 6.514   1.00 16.87 ?  98  PRO   B HG2  1 
ATOM   5512 H HG3  . PRO   B 1 98  ? 35.117 -25.923 6.927   1.00 16.87 ?  98  PRO   B HG3  1 
ATOM   5513 H HD2  . PRO   B 1 98  ? 36.743 -24.975 5.209   1.00 15.87 ?  98  PRO   B HD2  1 
ATOM   5514 H HD3  . PRO   B 1 98  ? 36.083 -23.984 6.284   1.00 15.87 ?  98  PRO   B HD3  1 
ATOM   5515 N N    . ASN   B 1 99  ? 39.818 -26.513 9.125   1.00 14.34 ?  99  ASN   B N    1 
ATOM   5516 C CA   . ASN   B 1 99  ? 40.793 -27.588 9.289   1.00 15.28 ?  99  ASN   B CA   1 
ATOM   5517 C C    . ASN   B 1 99  ? 40.154 -28.668 10.159  1.00 17.22 ?  99  ASN   B C    1 
ATOM   5518 O O    . ASN   B 1 99  ? 40.059 -28.520 11.380  1.00 17.84 ?  99  ASN   B O    1 
ATOM   5519 C CB   . ASN   B 1 99  ? 42.071 -27.036 9.911   1.00 15.76 ?  99  ASN   B CB   1 
ATOM   5520 C CG   . ASN   B 1 99  ? 43.197 -28.042 9.920   1.00 16.79 ?  99  ASN   B CG   1 
ATOM   5521 O OD1  . ASN   B 1 99  ? 42.970 -29.234 10.080  1.00 17.61 ?  99  ASN   B OD1  1 
ATOM   5522 N ND2  . ASN   B 1 99  ? 44.420 -27.569 9.751   1.00 17.65 ?  99  ASN   B ND2  1 
ATOM   5523 H H    . ASN   B 1 99  ? 39.779 -25.978 9.793   1.00 17.21 ?  99  ASN   B H    1 
ATOM   5524 H HA   . ASN   B 1 99  ? 41.006 -27.974 8.426   1.00 18.34 ?  99  ASN   B HA   1 
ATOM   5525 H HB2  . ASN   B 1 99  ? 42.361 -26.267 9.408   1.00 18.92 ?  99  ASN   B HB2  1 
ATOM   5526 H HB3  . ASN   B 1 99  ? 41.885 -26.787 10.832  1.00 18.92 ?  99  ASN   B HB3  1 
ATOM   5527 H HD21 . ASN   B 1 99  ? 45.093 -28.106 9.746   1.00 21.18 ?  99  ASN   B HD21 1 
ATOM   5528 H HD22 . ASN   B 1 99  ? 44.537 -26.728 9.645   1.00 21.18 ?  99  ASN   B HD22 1 
ATOM   5529 N N    A VAL   B 1 100 ? 39.693 -29.747 9.519   0.30 19.32 ?  100 VAL   B N    1 
ATOM   5530 N N    B VAL   B 1 100 ? 39.698 -29.750 9.520   0.70 19.04 ?  100 VAL   B N    1 
ATOM   5531 C CA   A VAL   B 1 100 ? 39.071 -30.845 10.256  0.30 21.64 ?  100 VAL   B CA   1 
ATOM   5532 C CA   B VAL   B 1 100 ? 39.069 -30.851 10.249  0.70 21.61 ?  100 VAL   B CA   1 
ATOM   5533 C C    A VAL   B 1 100 ? 40.067 -31.489 11.208  0.30 22.44 ?  100 VAL   B C    1 
ATOM   5534 C C    B VAL   B 1 100 ? 40.059 -31.527 11.187  0.70 22.10 ?  100 VAL   B C    1 
ATOM   5535 O O    A VAL   B 1 100 ? 39.693 -31.945 12.296  0.30 22.85 ?  100 VAL   B O    1 
ATOM   5536 O O    B VAL   B 1 100 ? 39.671 -32.054 12.237  0.70 22.60 ?  100 VAL   B O    1 
ATOM   5537 C CB   A VAL   B 1 100 ? 38.459 -31.870 9.279   0.30 23.32 ?  100 VAL   B CB   1 
ATOM   5538 C CB   B VAL   B 1 100 ? 38.435 -31.851 9.261   0.70 24.19 ?  100 VAL   B CB   1 
ATOM   5539 C CG1  A VAL   B 1 100 ? 37.986 -33.110 10.026  0.30 23.98 ?  100 VAL   B CG1  1 
ATOM   5540 C CG1  B VAL   B 1 100 ? 37.920 -33.086 9.995   0.70 25.32 ?  100 VAL   B CG1  1 
ATOM   5541 C CG2  A VAL   B 1 100 ? 37.309 -31.244 8.507   0.30 23.93 ?  100 VAL   B CG2  1 
ATOM   5542 C CG2  B VAL   B 1 100 ? 37.311 -31.186 8.491   0.70 25.11 ?  100 VAL   B CG2  1 
ATOM   5543 H H    A VAL   B 1 100 ? 39.729 -29.866 8.669   0.30 23.18 ?  100 VAL   B H    1 
ATOM   5544 H H    B VAL   B 1 100 ? 39.734 -29.866 8.668   0.70 22.85 ?  100 VAL   B H    1 
ATOM   5545 H HA   A VAL   B 1 100 ? 38.344 -30.488 10.790  0.30 25.97 ?  100 VAL   B HA   1 
ATOM   5546 H HA   B VAL   B 1 100 ? 38.351 -30.491 10.793  0.70 25.93 ?  100 VAL   B HA   1 
ATOM   5547 H HB   A VAL   B 1 100 ? 39.137 -32.145 8.643   0.30 27.98 ?  100 VAL   B HB   1 
ATOM   5548 H HB   B VAL   B 1 100 ? 39.108 -32.142 8.626   0.70 29.03 ?  100 VAL   B HB   1 
ATOM   5549 H HG11 A VAL   B 1 100 ? 37.401 -33.622 9.445   0.30 28.77 ?  100 VAL   B HG11 1 
ATOM   5550 H HG11 B VAL   B 1 100 ? 37.341 -33.588 9.398   0.70 30.38 ?  100 VAL   B HG11 1 
ATOM   5551 H HG12 A VAL   B 1 100 ? 38.754 -33.647 10.274  0.30 28.77 ?  100 VAL   B HG12 1 
ATOM   5552 H HG12 B VAL   B 1 100 ? 38.672 -33.638 10.262  0.70 30.38 ?  100 VAL   B HG12 1 
ATOM   5553 H HG13 A VAL   B 1 100 ? 37.501 -32.836 10.820  0.30 28.77 ?  100 VAL   B HG13 1 
ATOM   5554 H HG13 B VAL   B 1 100 ? 37.420 -32.805 10.777  0.70 30.38 ?  100 VAL   B HG13 1 
ATOM   5555 H HG21 A VAL   B 1 100 ? 36.933 -31.907 7.906   0.30 28.71 ?  100 VAL   B HG21 1 
ATOM   5556 H HG21 B VAL   B 1 100 ? 36.907 -31.838 7.897   0.70 30.13 ?  100 VAL   B HG21 1 
ATOM   5557 H HG22 A VAL   B 1 100 ? 36.631 -30.946 9.135   0.30 28.71 ?  100 VAL   B HG22 1 
ATOM   5558 H HG22 B VAL   B 1 100 ? 36.650 -30.858 9.121   0.70 30.13 ?  100 VAL   B HG22 1 
ATOM   5559 H HG23 A VAL   B 1 100 ? 37.644 -30.489 7.999   0.30 28.71 ?  100 VAL   B HG23 1 
ATOM   5560 H HG23 B VAL   B 1 100 ? 37.675 -30.449 7.978   0.70 30.13 ?  100 VAL   B HG23 1 
ATOM   5561 N N    . ASN   B 1 101 ? 41.345 -31.544 10.822  1.00 22.98 ?  101 ASN   B N    1 
ATOM   5562 C CA   . ASN   B 1 101 ? 42.363 -32.097 11.711  1.00 25.37 ?  101 ASN   B CA   1 
ATOM   5563 C C    . ASN   B 1 101 ? 42.511 -31.276 12.986  1.00 28.23 ?  101 ASN   B C    1 
ATOM   5564 O O    . ASN   B 1 101 ? 43.037 -31.788 13.983  1.00 29.04 ?  101 ASN   B O    1 
ATOM   5565 C CB   . ASN   B 1 101 ? 43.700 -32.226 10.975  1.00 25.50 ?  101 ASN   B CB   1 
ATOM   5566 C CG   . ASN   B 1 101 ? 43.695 -33.356 9.959   1.00 25.25 ?  101 ASN   B CG   1 
ATOM   5567 O OD1  . ASN   B 1 101 ? 43.017 -34.362 10.143  1.00 26.10 ?  101 ASN   B OD1  1 
ATOM   5568 N ND2  . ASN   B 1 101 ? 44.450 -33.191 8.881   1.00 25.10 ?  101 ASN   B ND2  1 
ATOM   5569 H H    A ASN   B 1 101 ? 41.637 -31.277 10.058  0.30 27.58 ?  101 ASN   B H    1 
ATOM   5570 H H    B ASN   B 1 101 ? 41.643 -31.254 10.069  0.70 27.58 ?  101 ASN   B H    1 
ATOM   5571 H HA   . ASN   B 1 101 ? 42.091 -32.984 11.975  1.00 30.45 ?  101 ASN   B HA   1 
ATOM   5572 H HB2  . ASN   B 1 101 ? 43.892 -31.403 10.500  1.00 30.61 ?  101 ASN   B HB2  1 
ATOM   5573 H HB3  . ASN   B 1 101 ? 44.402 -32.408 11.620  1.00 30.61 ?  101 ASN   B HB3  1 
ATOM   5574 H HD21 . ASN   B 1 101 ? 44.480 -33.807 8.280   1.00 30.12 ?  101 ASN   B HD21 1 
ATOM   5575 H HD22 . ASN   B 1 101 ? 44.911 -32.473 8.785   1.00 30.12 ?  101 ASN   B HD22 1 
ATOM   5576 N N    A LYS   B 1 102 ? 42.095 -30.010 12.967  0.30 29.85 ?  102 LYS   B N    1 
ATOM   5577 N N    B LYS   B 1 102 ? 42.028 -30.033 12.986  0.70 29.65 ?  102 LYS   B N    1 
ATOM   5578 C CA   A LYS   B 1 102 ? 42.074 -29.166 14.154  0.30 31.41 ?  102 LYS   B CA   1 
ATOM   5579 C CA   B LYS   B 1 102 ? 41.954 -29.203 14.181  0.70 31.44 ?  102 LYS   B CA   1 
ATOM   5580 C C    A LYS   B 1 102 ? 40.707 -29.154 14.824  0.30 30.89 ?  102 LYS   B C    1 
ATOM   5581 C C    B LYS   B 1 102 ? 40.554 -29.177 14.785  0.70 30.73 ?  102 LYS   B C    1 
ATOM   5582 O O    A LYS   B 1 102 ? 40.487 -28.365 15.749  0.30 31.06 ?  102 LYS   B O    1 
ATOM   5583 O O    B LYS   B 1 102 ? 40.308 -28.409 15.721  0.70 31.20 ?  102 LYS   B O    1 
ATOM   5584 C CB   A LYS   B 1 102 ? 42.482 -27.733 13.801  0.30 33.47 ?  102 LYS   B CB   1 
ATOM   5585 C CB   B LYS   B 1 102 ? 42.378 -27.768 13.862  0.70 34.06 ?  102 LYS   B CB   1 
ATOM   5586 C CG   A LYS   B 1 102 ? 43.943 -27.554 13.419  0.30 35.39 ?  102 LYS   B CG   1 
ATOM   5587 C CG   B LYS   B 1 102 ? 43.824 -27.597 13.436  0.70 36.65 ?  102 LYS   B CG   1 
ATOM   5588 C CD   A LYS   B 1 102 ? 44.232 -26.097 13.082  0.30 37.13 ?  102 LYS   B CD   1 
ATOM   5589 C CD   B LYS   B 1 102 ? 44.063 -26.166 12.976  0.70 39.05 ?  102 LYS   B CD   1 
ATOM   5590 C CE   A LYS   B 1 102 ? 45.698 -25.867 12.755  0.30 38.39 ?  102 LYS   B CE   1 
ATOM   5591 C CE   B LYS   B 1 102 ? 45.530 -25.881 12.715  0.70 40.84 ?  102 LYS   B CE   1 
ATOM   5592 N NZ   A LYS   B 1 102 ? 45.964 -24.445 12.394  0.30 39.15 ?  102 LYS   B NZ   1 
ATOM   5593 N NZ   B LYS   B 1 102 ? 45.732 -24.476 12.259  0.70 41.91 ?  102 LYS   B NZ   1 
ATOM   5594 H H    A LYS   B 1 102 ? 41.808 -29.610 12.262  0.30 35.82 ?  102 LYS   B H    1 
ATOM   5595 H H    B LYS   B 1 102 ? 41.724 -29.640 12.284  0.70 35.58 ?  102 LYS   B H    1 
ATOM   5596 H HA   A LYS   B 1 102 ? 42.722 -29.506 14.791  0.30 37.69 ?  102 LYS   B HA   1 
ATOM   5597 H HA   B LYS   B 1 102 ? 42.570 -29.552 14.844  0.70 37.72 ?  102 LYS   B HA   1 
ATOM   5598 H HB2  A LYS   B 1 102 ? 41.947 -27.434 13.050  0.30 40.16 ?  102 LYS   B HB2  1 
ATOM   5599 H HB2  B LYS   B 1 102 ? 41.821 -27.436 13.142  0.70 40.87 ?  102 LYS   B HB2  1 
ATOM   5600 H HB3  A LYS   B 1 102 ? 42.312 -27.165 14.569  0.30 40.16 ?  102 LYS   B HB3  1 
ATOM   5601 H HB3  B LYS   B 1 102 ? 42.241 -27.225 14.655  0.70 40.87 ?  102 LYS   B HB3  1 
ATOM   5602 H HG2  A LYS   B 1 102 ? 44.508 -27.813 14.165  0.30 42.47 ?  102 LYS   B HG2  1 
ATOM   5603 H HG2  B LYS   B 1 102 ? 44.409 -27.780 14.189  0.70 43.97 ?  102 LYS   B HG2  1 
ATOM   5604 H HG3  A LYS   B 1 102 ? 44.144 -28.094 12.639  0.30 42.47 ?  102 LYS   B HG3  1 
ATOM   5605 H HG3  B LYS   B 1 102 ? 44.020 -28.196 12.699  0.70 43.97 ?  102 LYS   B HG3  1 
ATOM   5606 H HD2  A LYS   B 1 102 ? 43.706 -25.838 12.309  0.30 44.55 ?  102 LYS   B HD2  1 
ATOM   5607 H HD2  B LYS   B 1 102 ? 43.575 -26.012 12.152  0.70 46.86 ?  102 LYS   B HD2  1 
ATOM   5608 H HD3  A LYS   B 1 102 ? 44.002 -25.541 13.844  0.30 44.55 ?  102 LYS   B HD3  1 
ATOM   5609 H HD3  B LYS   B 1 102 ? 43.754 -25.556 13.664  0.70 46.86 ?  102 LYS   B HD3  1 
ATOM   5610 H HE2  A LYS   B 1 102 ? 46.238 -26.089 13.530  0.30 46.07 ?  102 LYS   B HE2  1 
ATOM   5611 H HE2  B LYS   B 1 102 ? 46.033 -26.010 13.535  0.70 49.00 ?  102 LYS   B HE2  1 
ATOM   5612 H HE3  A LYS   B 1 102 ? 45.949 -26.424 12.001  0.30 46.07 ?  102 LYS   B HE3  1 
ATOM   5613 H HE3  B LYS   B 1 102 ? 45.855 -26.477 12.023  0.70 49.00 ?  102 LYS   B HE3  1 
ATOM   5614 H HZ1  A LYS   B 1 102 ? 46.827 -24.335 12.207  0.30 46.98 ?  102 LYS   B HZ1  1 
ATOM   5615 H HZ1  B LYS   B 1 102 ? 46.596 -24.325 12.111  0.70 50.30 ?  102 LYS   B HZ1  1 
ATOM   5616 H HZ2  A LYS   B 1 102 ? 45.482 -24.218 11.681  0.30 46.98 ?  102 LYS   B HZ2  1 
ATOM   5617 H HZ2  B LYS   B 1 102 ? 45.280 -24.334 11.505  0.70 50.30 ?  102 LYS   B HZ2  1 
ATOM   5618 H HZ3  A LYS   B 1 102 ? 45.745 -23.913 13.073  0.30 46.98 ?  102 LYS   B HZ3  1 
ATOM   5619 H HZ3  B LYS   B 1 102 ? 45.441 -23.910 12.881  0.70 50.30 ?  102 LYS   B HZ3  1 
ATOM   5620 N N    A GLY   B 1 103 ? 39.784 -30.000 14.371  0.30 30.27 ?  103 GLY   B N    1 
ATOM   5621 N N    B GLY   B 1 103 ? 39.625 -29.970 14.256  0.70 29.85 ?  103 GLY   B N    1 
ATOM   5622 C CA   A GLY   B 1 103 ? 38.449 -30.047 14.929  0.30 29.73 ?  103 GLY   B CA   1 
ATOM   5623 C CA   B GLY   B 1 103 ? 38.283 -30.033 14.800  0.70 29.27 ?  103 GLY   B CA   1 
ATOM   5624 C C    A GLY   B 1 103 ? 37.520 -28.952 14.457  0.30 29.03 ?  103 GLY   B C    1 
ATOM   5625 C C    B GLY   B 1 103 ? 37.364 -28.906 14.385  0.70 28.19 ?  103 GLY   B C    1 
ATOM   5626 O O    A GLY   B 1 103 ? 36.408 -28.836 14.985  0.30 29.30 ?  103 GLY   B O    1 
ATOM   5627 O O    B GLY   B 1 103 ? 36.306 -28.731 15.001  0.70 28.79 ?  103 GLY   B O    1 
ATOM   5628 H H    A GLY   B 1 103 ? 39.915 -30.560 13.733  0.30 36.33 ?  103 GLY   B H    1 
ATOM   5629 H H    B GLY   B 1 103 ? 39.749 -30.473 13.570  0.70 35.82 ?  103 GLY   B H    1 
ATOM   5630 H HA2  A GLY   B 1 103 ? 38.050 -30.904 14.706  0.30 35.68 ?  103 GLY   B HA2  1 
ATOM   5631 H HA2  B GLY   B 1 103 ? 37.876 -30.873 14.529  0.70 35.12 ?  103 GLY   B HA2  1 
ATOM   5632 H HA3  A GLY   B 1 103 ? 38.510 -29.987 15.894  0.30 35.68 ?  103 GLY   B HA3  1 
ATOM   5633 H HA3  B GLY   B 1 103 ? 38.338 -30.031 15.769  0.70 35.12 ?  103 GLY   B HA3  1 
ATOM   5634 N N    A GLU   B 1 104 ? 37.935 -28.144 13.486  0.30 27.99 ?  104 GLU   B N    1 
ATOM   5635 N N    B GLU   B 1 104 ? 37.730 -28.133 13.368  0.70 26.30 ?  104 GLU   B N    1 
ATOM   5636 C CA   A GLU   B 1 104 ? 37.096 -27.054 13.010  0.30 27.04 ?  104 GLU   B CA   1 
ATOM   5637 C CA   B GLU   B 1 104 ? 36.897 -27.027 12.923  0.70 24.71 ?  104 GLU   B CA   1 
ATOM   5638 C C    A GLU   B 1 104 ? 35.921 -27.594 12.200  0.30 27.27 ?  104 GLU   B C    1 
ATOM   5639 C C    B GLU   B 1 104 ? 35.731 -27.541 12.082  0.70 25.36 ?  104 GLU   B C    1 
ATOM   5640 O O    A GLU   B 1 104 ? 35.977 -28.686 11.627  0.30 27.34 ?  104 GLU   B O    1 
ATOM   5641 O O    B GLU   B 1 104 ? 35.800 -28.612 11.470  0.70 26.06 ?  104 GLU   B O    1 
ATOM   5642 C CB   A GLU   B 1 104 ? 37.931 -26.071 12.188  0.30 26.12 ?  104 GLU   B CB   1 
ATOM   5643 C CB   B GLU   B 1 104 ? 37.747 -26.017 12.151  0.70 23.12 ?  104 GLU   B CB   1 
ATOM   5644 C CG   A GLU   B 1 104 ? 39.032 -25.408 13.010  0.30 25.48 ?  104 GLU   B CG   1 
ATOM   5645 C CG   B GLU   B 1 104 ? 38.856 -25.432 13.023  0.70 21.89 ?  104 GLU   B CG   1 
ATOM   5646 C CD   A GLU   B 1 104 ? 39.943 -24.517 12.186  0.30 24.96 ?  104 GLU   B CD   1 
ATOM   5647 C CD   B GLU   B 1 104 ? 39.839 -24.544 12.281  0.70 20.63 ?  104 GLU   B CD   1 
ATOM   5648 O OE1  A GLU   B 1 104 ? 39.867 -24.562 10.941  0.30 24.36 ?  104 GLU   B OE1  1 
ATOM   5649 O OE1  B GLU   B 1 104 ? 39.883 -24.557 11.032  0.70 19.02 ?  104 GLU   B OE1  1 
ATOM   5650 O OE2  A GLU   B 1 104 ? 40.740 -23.770 12.792  0.30 25.19 -1 104 GLU   B OE2  1 
ATOM   5651 O OE2  B GLU   B 1 104 ? 40.588 -23.828 12.978  0.70 20.94 -1 104 GLU   B OE2  1 
ATOM   5652 H H    A GLU   B 1 104 ? 38.699 -28.202 13.092  0.30 33.59 ?  104 GLU   B H    1 
ATOM   5653 H H    B GLU   B 1 104 ? 38.462 -28.225 12.928  0.70 31.56 ?  104 GLU   B H    1 
ATOM   5654 H HA   A GLU   B 1 104 ? 36.737 -26.578 13.773  0.30 32.45 ?  104 GLU   B HA   1 
ATOM   5655 H HA   B GLU   B 1 104 ? 36.529 -26.579 13.702  0.70 29.66 ?  104 GLU   B HA   1 
ATOM   5656 H HB2  A GLU   B 1 104 ? 38.350 -26.545 11.453  0.30 31.34 ?  104 GLU   B HB2  1 
ATOM   5657 H HB2  B GLU   B 1 104 ? 38.156 -26.460 11.394  0.70 27.74 ?  104 GLU   B HB2  1 
ATOM   5658 H HB3  A GLU   B 1 104 ? 37.352 -25.372 11.845  0.30 31.34 ?  104 GLU   B HB3  1 
ATOM   5659 H HB3  B GLU   B 1 104 ? 37.179 -25.291 11.851  0.70 27.74 ?  104 GLU   B HB3  1 
ATOM   5660 H HG2  A GLU   B 1 104 ? 38.625 -24.863 13.702  0.30 30.57 ?  104 GLU   B HG2  1 
ATOM   5661 H HG2  B GLU   B 1 104 ? 38.452 -24.901 13.729  0.70 26.27 ?  104 GLU   B HG2  1 
ATOM   5662 H HG3  A GLU   B 1 104 ? 39.582 -26.097 13.416  0.30 30.57 ?  104 GLU   B HG3  1 
ATOM   5663 H HG3  B GLU   B 1 104 ? 39.368 -26.156 13.412  0.70 26.27 ?  104 GLU   B HG3  1 
ATOM   5664 N N    A ASP   B 1 105 ? 34.844 -26.812 12.163  0.30 27.41 ?  105 ASP   B N    1 
ATOM   5665 N N    B ASP   B 1 105 ? 34.646 -26.767 12.068  0.70 25.33 ?  105 ASP   B N    1 
ATOM   5666 C CA   A ASP   B 1 105 ? 33.573 -27.271 11.614  0.30 27.83 ?  105 ASP   B CA   1 
ATOM   5667 C CA   B ASP   B 1 105 ? 33.383 -27.237 11.508  0.70 25.96 ?  105 ASP   B CA   1 
ATOM   5668 C C    A ASP   B 1 105 ? 33.638 -27.302 10.090  0.30 26.71 ?  105 ASP   B C    1 
ATOM   5669 C C    B ASP   B 1 105 ? 33.452 -27.271 9.986   0.70 23.44 ?  105 ASP   B C    1 
ATOM   5670 O O    A ASP   B 1 105 ? 33.868 -26.272 9.449   0.30 26.50 ?  105 ASP   B O    1 
ATOM   5671 O O    B ASP   B 1 105 ? 33.597 -26.229 9.337   0.70 21.96 ?  105 ASP   B O    1 
ATOM   5672 C CB   A ASP   B 1 105 ? 32.449 -26.350 12.083  0.30 29.33 ?  105 ASP   B CB   1 
ATOM   5673 C CB   B ASP   B 1 105 ? 32.242 -26.332 11.969  0.70 29.20 ?  105 ASP   B CB   1 
ATOM   5674 C CG   A ASP   B 1 105 ? 31.082 -26.816 11.622  0.30 30.61 ?  105 ASP   B CG   1 
ATOM   5675 C CG   B ASP   B 1 105 ? 30.870 -26.893 11.621  0.70 31.71 ?  105 ASP   B CG   1 
ATOM   5676 O OD1  A ASP   B 1 105 ? 30.982 -27.940 11.085  0.30 30.83 ?  105 ASP   B OD1  1 
ATOM   5677 O OD1  B ASP   B 1 105 ? 30.790 -27.832 10.803  0.70 32.28 ?  105 ASP   B OD1  1 
ATOM   5678 O OD2  A ASP   B 1 105 ? 30.108 -26.053 11.790  0.30 31.32 -1 105 ASP   B OD2  1 
ATOM   5679 O OD2  B ASP   B 1 105 ? 29.867 -26.397 12.177  0.70 32.76 -1 105 ASP   B OD2  1 
ATOM   5680 H H    A ASP   B 1 105 ? 34.825 -26.002 12.453  0.30 32.89 ?  105 ASP   B H    1 
ATOM   5681 H H    B ASP   B 1 105 ? 34.619 -25.964 12.375  0.70 30.39 ?  105 ASP   B H    1 
ATOM   5682 H HA   A ASP   B 1 105 ? 33.388 -28.168 11.932  0.30 33.40 ?  105 ASP   B HA   1 
ATOM   5683 H HA   B ASP   B 1 105 ? 33.206 -28.134 11.822  0.70 31.15 ?  105 ASP   B HA   1 
ATOM   5684 H HB2  A ASP   B 1 105 ? 32.456 -26.312 13.055  0.30 35.19 ?  105 ASP   B HB2  1 
ATOM   5685 H HB2  B ASP   B 1 105 ? 32.295 -26.222 12.932  0.70 35.04 ?  105 ASP   B HB2  1 
ATOM   5686 H HB3  A ASP   B 1 105 ? 32.591 -25.463 11.719  0.30 35.19 ?  105 ASP   B HB3  1 
ATOM   5687 H HB3  B ASP   B 1 105 ? 32.323 -25.469 11.533  0.70 35.04 ?  105 ASP   B HB3  1 
ATOM   5688 N N    A ILE   B 1 106 ? 33.419 -28.488 9.515   0.30 26.00 ?  106 ILE   B N    1 
ATOM   5689 N N    B ILE   B 1 106 ? 33.317 -28.473 9.418   0.70 23.24 ?  106 ILE   B N    1 
ATOM   5690 C CA   A ILE   B 1 106 ? 33.431 -28.654 8.065   0.30 25.41 ?  106 ILE   B CA   1 
ATOM   5691 C CA   B ILE   B 1 106 ? 33.321 -28.639 7.970   0.70 22.74 ?  106 ILE   B CA   1 
ATOM   5692 C C    A ILE   B 1 106 ? 32.343 -27.829 7.385   0.30 24.89 ?  106 ILE   B C    1 
ATOM   5693 C C    B ILE   B 1 106 ? 32.237 -27.799 7.305   0.70 21.76 ?  106 ILE   B C    1 
ATOM   5694 O O    A ILE   B 1 106 ? 32.442 -27.544 6.187   0.30 24.59 ?  106 ILE   B O    1 
ATOM   5695 O O    B ILE   B 1 106 ? 32.358 -27.447 6.128   0.70 20.60 ?  106 ILE   B O    1 
ATOM   5696 C CB   A ILE   B 1 106 ? 33.314 -30.158 7.721   0.30 25.47 ?  106 ILE   B CB   1 
ATOM   5697 C CB   B ILE   B 1 106 ? 33.202 -30.140 7.621   0.70 23.77 ?  106 ILE   B CB   1 
ATOM   5698 C CG1  A ILE   B 1 106 ? 33.533 -30.402 6.226   0.30 25.26 ?  106 ILE   B CG1  1 
ATOM   5699 C CG1  B ILE   B 1 106 ? 33.524 -30.387 6.148   0.70 23.88 ?  106 ILE   B CG1  1 
ATOM   5700 C CG2  A ILE   B 1 106 ? 31.960 -30.706 8.154   0.30 25.82 ?  106 ILE   B CG2  1 
ATOM   5701 C CG2  B ILE   B 1 106 ? 31.807 -30.662 7.946   0.70 24.78 ?  106 ILE   B CG2  1 
ATOM   5702 C CD1  A ILE   B 1 106 ? 34.884 -29.946 5.728   0.30 25.10 ?  106 ILE   B CD1  1 
ATOM   5703 C CD1  B ILE   B 1 106 ? 34.904 -29.936 5.752   0.70 23.84 ?  106 ILE   B CD1  1 
ATOM   5704 H H    A ILE   B 1 106 ? 33.275 -29.215 9.949   0.30 31.20 ?  106 ILE   B H    1 
ATOM   5705 H H    B ILE   B 1 106 ? 33.230 -29.204 9.855   0.70 27.89 ?  106 ILE   B H    1 
ATOM   5706 H HA   A ILE   B 1 106 ? 34.285 -28.343 7.734   0.30 30.49 ?  106 ILE   B HA   1 
ATOM   5707 H HA   B ILE   B 1 106 ? 34.172 -28.324 7.636   0.70 27.29 ?  106 ILE   B HA   1 
ATOM   5708 H HB   A ILE   B 1 106 ? 34.003 -30.637 8.208   0.30 30.56 ?  106 ILE   B HB   1 
ATOM   5709 H HB   B ILE   B 1 106 ? 33.842 -30.635 8.159   0.70 28.53 ?  106 ILE   B HB   1 
ATOM   5710 H HG12 A ILE   B 1 106 ? 33.464 -31.356 6.051   0.30 30.31 ?  106 ILE   B HG12 1 
ATOM   5711 H HG12 B ILE   B 1 106 ? 33.465 -31.341 5.968   0.70 28.65 ?  106 ILE   B HG12 1 
ATOM   5712 H HG13 A ILE   B 1 106 ? 32.855 -29.928 5.723   0.30 30.31 ?  106 ILE   B HG13 1 
ATOM   5713 H HG13 B ILE   B 1 106 ? 32.886 -29.910 5.600   0.70 28.65 ?  106 ILE   B HG13 1 
ATOM   5714 H HG21 A ILE   B 1 106 ? 31.954 -31.668 8.028   0.30 30.98 ?  106 ILE   B HG21 1 
ATOM   5715 H HG21 B ILE   B 1 106 ? 31.815 -31.632 7.906   0.70 29.73 ?  106 ILE   B HG21 1 
ATOM   5716 H HG22 A ILE   B 1 106 ? 31.818 -30.495 9.090   0.30 30.98 ?  106 ILE   B HG22 1 
ATOM   5717 H HG22 B ILE   B 1 106 ? 31.564 -30.371 8.838   0.70 29.73 ?  106 ILE   B HG22 1 
ATOM   5718 H HG23 A ILE   B 1 106 ? 31.265 -30.299 7.614   0.30 30.98 ?  106 ILE   B HG23 1 
ATOM   5719 H HG23 B ILE   B 1 106 ? 31.178 -30.310 7.298   0.70 29.73 ?  106 ILE   B HG23 1 
ATOM   5720 H HD11 A ILE   B 1 106 ? 35.044 -30.331 4.853   0.30 30.12 ?  106 ILE   B HD11 1 
ATOM   5721 H HD11 B ILE   B 1 106 ? 35.155 -30.370 4.923   0.70 28.60 ?  106 ILE   B HD11 1 
ATOM   5722 H HD12 A ILE   B 1 106 ? 34.889 -28.978 5.669   0.30 30.12 ?  106 ILE   B HD12 1 
ATOM   5723 H HD12 B ILE   B 1 106 ? 34.900 -28.972 5.630   0.70 28.60 ?  106 ILE   B HD12 1 
ATOM   5724 H HD13 A ILE   B 1 106 ? 35.567 -30.245 6.350   0.30 30.12 ?  106 ILE   B HD13 1 
ATOM   5725 H HD13 B ILE   B 1 106 ? 35.531 -30.177 6.453   0.70 28.60 ?  106 ILE   B HD13 1 
ATOM   5726 N N    A GLN   B 1 107 ? 31.302 -27.433 8.123   0.30 24.92 ?  107 GLN   B N    1 
ATOM   5727 N N    B GLN   B 1 107 ? 31.186 -27.440 8.042   0.70 22.62 ?  107 GLN   B N    1 
ATOM   5728 C CA   A GLN   B 1 107 ? 30.208 -26.672 7.523   0.30 24.86 ?  107 GLN   B CA   1 
ATOM   5729 C CA   B GLN   B 1 107 ? 30.125 -26.618 7.475   0.70 23.61 ?  107 GLN   B CA   1 
ATOM   5730 C C    A GLN   B 1 107 ? 30.679 -25.325 6.984   0.30 22.52 ?  107 GLN   B C    1 
ATOM   5731 C C    B GLN   B 1 107 ? 30.629 -25.255 7.013   0.70 21.97 ?  107 GLN   B C    1 
ATOM   5732 O O    A GLN   B 1 107 ? 30.058 -24.774 6.067   0.30 22.81 ?  107 GLN   B O    1 
ATOM   5733 O O    B GLN   B 1 107 ? 29.986 -24.631 6.164   0.70 22.95 ?  107 GLN   B O    1 
ATOM   5734 C CB   A GLN   B 1 107 ? 29.092 -26.481 8.552   0.30 27.55 ?  107 GLN   B CB   1 
ATOM   5735 C CB   B GLN   B 1 107 ? 28.994 -26.453 8.493   0.70 27.65 ?  107 GLN   B CB   1 
ATOM   5736 C CG   A GLN   B 1 107 ? 27.773 -25.976 7.980   0.30 30.03 ?  107 GLN   B CG   1 
ATOM   5737 C CG   B GLN   B 1 107 ? 27.671 -25.979 7.904   0.70 31.62 ?  107 GLN   B CG   1 
ATOM   5738 C CD   A GLN   B 1 107 ? 27.713 -24.463 7.878   0.30 32.02 ?  107 GLN   B CD   1 
ATOM   5739 C CD   B GLN   B 1 107 ? 27.555 -24.467 7.850   0.70 34.82 ?  107 GLN   B CD   1 
ATOM   5740 O OE1  A GLN   B 1 107 ? 28.542 -23.755 8.453   0.30 32.74 ?  107 GLN   B OE1  1 
ATOM   5741 O OE1  B GLN   B 1 107 ? 28.340 -23.748 8.471   0.70 36.02 ?  107 GLN   B OE1  1 
ATOM   5742 N NE2  A GLN   B 1 107 ? 26.725 -23.958 7.145   0.30 32.73 ?  107 GLN   B NE2  1 
ATOM   5743 N NE2  B GLN   B 1 107 ? 26.567 -23.976 7.108   0.70 35.93 ?  107 GLN   B NE2  1 
ATOM   5744 H H    A GLN   B 1 107 ? 31.206 -27.598 8.959   0.30 29.91 ?  107 GLN   B H    1 
ATOM   5745 H H    B GLN   B 1 107 ? 31.071 -27.652 8.862   0.70 27.15 ?  107 GLN   B H    1 
ATOM   5746 H HA   A GLN   B 1 107 ? 29.845 -27.180 6.782   0.30 29.84 ?  107 GLN   B HA   1 
ATOM   5747 H HA   B GLN   B 1 107 ? 29.759 -27.073 6.700   0.70 28.34 ?  107 GLN   B HA   1 
ATOM   5748 H HB2  A GLN   B 1 107 ? 28.917 -27.333 8.977   0.30 33.06 ?  107 GLN   B HB2  1 
ATOM   5749 H HB2  B GLN   B 1 107 ? 28.836 -27.308 8.914   0.70 33.18 ?  107 GLN   B HB2  1 
ATOM   5750 H HB3  A GLN   B 1 107 ? 29.391 -25.842 9.218   0.30 33.06 ?  107 GLN   B HB3  1 
ATOM   5751 H HB3  B GLN   B 1 107 ? 29.271 -25.806 9.161   0.70 33.18 ?  107 GLN   B HB3  1 
ATOM   5752 H HG2  A GLN   B 1 107 ? 27.654 -26.338 7.089   0.30 36.03 ?  107 GLN   B HG2  1 
ATOM   5753 H HG2  B GLN   B 1 107 ? 27.587 -26.316 6.998   0.70 37.95 ?  107 GLN   B HG2  1 
ATOM   5754 H HG3  A GLN   B 1 107 ? 27.047 -26.269 8.556   0.30 36.03 ?  107 GLN   B HG3  1 
ATOM   5755 H HG3  B GLN   B 1 107 ? 26.943 -26.320 8.451   0.70 37.95 ?  107 GLN   B HG3  1 
ATOM   5756 H HE21 A GLN   B 1 107 ? 26.165 -24.484 6.756   0.30 39.27 ?  107 GLN   B HE21 1 
ATOM   5757 H HE21 B GLN   B 1 107 ? 26.039 -24.508 6.685   0.70 43.12 ?  107 GLN   B HE21 1 
ATOM   5758 H HE22 A GLN   B 1 107 ? 26.644 -23.106 7.059   0.30 39.27 ?  107 GLN   B HE22 1 
ATOM   5759 H HE22 B GLN   B 1 107 ? 26.456 -23.125 7.048   0.70 43.12 ?  107 GLN   B HE22 1 
ATOM   5760 N N    . LEU   B 1 108 ? 31.770 -24.785 7.530   1.00 20.10 ?  108 LEU   B N    1 
ATOM   5761 C CA   . LEU   B 1 108 ? 32.323 -23.494 7.117   1.00 17.55 ?  108 LEU   B CA   1 
ATOM   5762 C C    . LEU   B 1 108 ? 32.981 -23.529 5.745   1.00 15.49 ?  108 LEU   B C    1 
ATOM   5763 O O    . LEU   B 1 108 ? 33.420 -22.479 5.256   1.00 15.04 ?  108 LEU   B O    1 
ATOM   5764 C CB   . LEU   B 1 108 ? 33.331 -23.008 8.156   1.00 17.61 ?  108 LEU   B CB   1 
ATOM   5765 C CG   . LEU   B 1 108 ? 32.707 -22.556 9.474   1.00 19.09 ?  108 LEU   B CG   1 
ATOM   5766 C CD1  . LEU   B 1 108 ? 33.745 -22.510 10.580  1.00 19.60 ?  108 LEU   B CD1  1 
ATOM   5767 C CD2  . LEU   B 1 108 ? 32.069 -21.189 9.294   1.00 20.24 ?  108 LEU   B CD2  1 
ATOM   5768 H H    A LEU   B 1 108 ? 32.217 -25.157 8.161   0.30 24.12 ?  108 LEU   B H    1 
ATOM   5769 H H    B LEU   B 1 108 ? 32.236 -25.193 8.124   0.70 24.12 ?  108 LEU   B H    1 
ATOM   5770 H HA   . LEU   B 1 108 ? 31.601 -22.850 7.075   1.00 21.05 ?  108 LEU   B HA   1 
ATOM   5771 H HB2  . LEU   B 1 108 ? 33.942 -23.728 8.358   1.00 21.14 ?  108 LEU   B HB2  1 
ATOM   5772 H HB3  . LEU   B 1 108 ? 33.815 -22.253 7.791   1.00 21.14 ?  108 LEU   B HB3  1 
ATOM   5773 H HG   . LEU   B 1 108 ? 32.007 -23.179 9.738   1.00 22.90 ?  108 LEU   B HG   1 
ATOM   5774 H HD11 . LEU   B 1 108 ? 33.311 -22.270 11.415  1.00 23.52 ?  108 LEU   B HD11 1 
ATOM   5775 H HD12 . LEU   B 1 108 ? 34.156 -23.383 10.661  1.00 23.52 ?  108 LEU   B HD12 1 
ATOM   5776 H HD13 . LEU   B 1 108 ? 34.414 -21.846 10.355  1.00 23.52 ?  108 LEU   B HD13 1 
ATOM   5777 H HD21 . LEU   B 1 108 ? 31.725 -20.882 10.148  1.00 24.29 ?  108 LEU   B HD21 1 
ATOM   5778 H HD22 . LEU   B 1 108 ? 32.740 -20.570 8.967   1.00 24.29 ?  108 LEU   B HD22 1 
ATOM   5779 H HD23 . LEU   B 1 108 ? 31.343 -21.258 8.653   1.00 24.29 ?  108 LEU   B HD23 1 
ATOM   5780 N N    . LEU   B 1 109 ? 33.049 -24.699 5.117   1.00 14.25 ?  109 LEU   B N    1 
ATOM   5781 C CA   . LEU   B 1 109 ? 33.685 -24.812 3.813   1.00 13.46 ?  109 LEU   B CA   1 
ATOM   5782 C C    . LEU   B 1 109 ? 32.926 -24.026 2.749   1.00 12.71 ?  109 LEU   B C    1 
ATOM   5783 O O    . LEU   B 1 109 ? 33.543 -23.441 1.851   1.00 12.53 ?  109 LEU   B O    1 
ATOM   5784 C CB   . LEU   B 1 109 ? 33.789 -26.291 3.436   1.00 13.52 ?  109 LEU   B CB   1 
ATOM   5785 C CG   . LEU   B 1 109 ? 34.586 -26.619 2.179   1.00 13.18 ?  109 LEU   B CG   1 
ATOM   5786 C CD1  . LEU   B 1 109 ? 35.972 -25.986 2.215   1.00 13.40 ?  109 LEU   B CD1  1 
ATOM   5787 C CD2  . LEU   B 1 109 ? 34.705 -28.129 2.030   1.00 14.10 ?  109 LEU   B CD2  1 
ATOM   5788 H H    . LEU   B 1 109 ? 32.736 -25.436 5.416   1.00 17.10 ?  109 LEU   B H    1 
ATOM   5789 H HA   . LEU   B 1 109 ? 34.581 -24.448 3.864   1.00 16.15 ?  109 LEU   B HA   1 
ATOM   5790 H HB2  . LEU   B 1 109 ? 34.204 -26.760 4.171   1.00 16.22 ?  109 LEU   B HB2  1 
ATOM   5791 H HB3  . LEU   B 1 109 ? 32.890 -26.632 3.299   1.00 16.22 ?  109 LEU   B HB3  1 
ATOM   5792 H HG   . LEU   B 1 109 ? 34.118 -26.284 1.400   1.00 15.82 ?  109 LEU   B HG   1 
ATOM   5793 H HD11 . LEU   B 1 109 ? 36.510 -26.360 1.497   1.00 16.08 ?  109 LEU   B HD11 1 
ATOM   5794 H HD12 . LEU   B 1 109 ? 35.884 -25.030 2.099   1.00 16.08 ?  109 LEU   B HD12 1 
ATOM   5795 H HD13 . LEU   B 1 109 ? 36.387 -26.183 3.071   1.00 16.08 ?  109 LEU   B HD13 1 
ATOM   5796 H HD21 . LEU   B 1 109 ? 35.268 -28.329 1.266   1.00 16.92 ?  109 LEU   B HD21 1 
ATOM   5797 H HD22 . LEU   B 1 109 ? 35.096 -28.497 2.836   1.00 16.92 ?  109 LEU   B HD22 1 
ATOM   5798 H HD23 . LEU   B 1 109 ? 33.818 -28.503 1.893   1.00 16.92 ?  109 LEU   B HD23 1 
ATOM   5799 N N    . LYS   B 1 110 ? 31.592 -23.997 2.823   1.00 12.73 ?  110 LYS   B N    1 
ATOM   5800 C CA   . LYS   B 1 110 ? 30.834 -23.234 1.836   1.00 12.72 ?  110 LYS   B CA   1 
ATOM   5801 C C    . LYS   B 1 110 ? 31.172 -21.748 1.931   1.00 12.40 ?  110 LYS   B C    1 
ATOM   5802 O O    . LYS   B 1 110 ? 31.433 -21.094 0.917   1.00 12.28 ?  110 LYS   B O    1 
ATOM   5803 C CB   . LYS   B 1 110 ? 29.328 -23.475 1.989   1.00 13.43 ?  110 LYS   B CB   1 
ATOM   5804 C CG   . LYS   B 1 110 ? 28.530 -22.865 0.845   1.00 13.81 ?  110 LYS   B CG   1 
ATOM   5805 C CD   . LYS   B 1 110 ? 27.066 -23.298 0.865   1.00 14.46 ?  110 LYS   B CD   1 
ATOM   5806 C CE   . LYS   B 1 110 ? 26.305 -22.764 -0.351  1.00 15.23 ?  110 LYS   B CE   1 
ATOM   5807 N NZ   . LYS   B 1 110 ? 26.646 -23.487 -1.608  1.00 15.42 ?  110 LYS   B NZ   1 
ATOM   5808 H H    . LYS   B 1 110 ? 31.120 -24.402 3.408   1.00 15.28 ?  110 LYS   B H    1 
ATOM   5809 H HA   . LYS   B 1 110 ? 31.089 -23.533 0.945   1.00 15.26 ?  110 LYS   B HA   1 
ATOM   5810 H HB2  . LYS   B 1 110 ? 29.162 -24.430 2.000   1.00 16.11 ?  110 LYS   B HB2  1 
ATOM   5811 H HB3  . LYS   B 1 110 ? 29.027 -23.073 2.817   1.00 16.11 ?  110 LYS   B HB3  1 
ATOM   5812 H HG2  . LYS   B 1 110 ? 28.545 -21.900 0.914   1.00 16.57 ?  110 LYS   B HG2  1 
ATOM   5813 H HG3  . LYS   B 1 110 ? 28.902 -23.149 -0.002  1.00 16.57 ?  110 LYS   B HG3  1 
ATOM   5814 H HD2  . LYS   B 1 110 ? 27.007 -24.270 0.849   1.00 17.36 ?  110 LYS   B HD2  1 
ATOM   5815 H HD3  . LYS   B 1 110 ? 26.629 -22.955 1.665   1.00 17.36 ?  110 LYS   B HD3  1 
ATOM   5816 H HE2  . LYS   B 1 110 ? 25.349 -22.857 -0.202  1.00 18.27 ?  110 LYS   B HE2  1 
ATOM   5817 H HE3  . LYS   B 1 110 ? 26.529 -21.827 -0.475  1.00 18.27 ?  110 LYS   B HE3  1 
ATOM   5818 H HZ1  . LYS   B 1 110 ? 26.192 -23.148 -2.292  1.00 18.51 ?  110 LYS   B HZ1  1 
ATOM   5819 H HZ2  . LYS   B 1 110 ? 27.519 -23.412 -1.774  1.00 18.51 ?  110 LYS   B HZ2  1 
ATOM   5820 H HZ3  . LYS   B 1 110 ? 26.444 -24.351 -1.526  1.00 18.51 ?  110 LYS   B HZ3  1 
ATOM   5821 N N    . SER   B 1 111 ? 31.195 -21.204 3.152   1.00 12.53 ?  111 SER   B N    1 
ATOM   5822 C CA   . SER   B 1 111 ? 31.589 -19.809 3.336   1.00 12.81 ?  111 SER   B CA   1 
ATOM   5823 C C    . SER   B 1 111 ? 32.972 -19.543 2.751   1.00 12.09 ?  111 SER   B C    1 
ATOM   5824 O O    . SER   B 1 111 ? 33.203 -18.506 2.113   1.00 12.55 ?  111 SER   B O    1 
ATOM   5825 C CB   . SER   B 1 111 ? 31.589 -19.461 4.824   1.00 13.94 ?  111 SER   B CB   1 
ATOM   5826 O OG   . SER   B 1 111 ? 30.282 -19.475 5.365   1.00 15.91 ?  111 SER   B OG   1 
ATOM   5827 H H    . SER   B 1 111 ? 30.999 -21.623 3.876   1.00 15.04 ?  111 SER   B H    1 
ATOM   5828 H HA   . SER   B 1 111 ? 30.953 -19.237 2.887   1.00 15.38 ?  111 SER   B HA   1 
ATOM   5829 H HB2  . SER   B 1 111 ? 32.129 -20.114 5.301   1.00 16.73 ?  111 SER   B HB2  1 
ATOM   5830 H HB3  . SER   B 1 111 ? 31.963 -18.577 4.941   1.00 16.73 ?  111 SER   B HB3  1 
ATOM   5831 H HG   . SER   B 1 111 ? 30.307 -19.284 6.188   1.00 19.09 ?  111 SER   B HG   1 
ATOM   5832 N N    . ALA   B 1 112 ? 33.909 -20.467 2.965   1.00 12.30 ?  112 ALA   B N    1 
ATOM   5833 C CA   . ALA   B 1 112 ? 35.252 -20.291 2.422   1.00 12.07 ?  112 ALA   B CA   1 
ATOM   5834 C C    . ALA   B 1 112 ? 35.225 -20.193 0.898   1.00 11.16 ?  112 ALA   B C    1 
ATOM   5835 O O    . ALA   B 1 112 ? 35.851 -19.300 0.307   1.00 11.52 ?  112 ALA   B O    1 
ATOM   5836 C CB   . ALA   B 1 112 ? 36.159 -21.428 2.898   1.00 12.36 ?  112 ALA   B CB   1 
ATOM   5837 H H    . ALA   B 1 112 ? 33.794 -21.194 3.415   1.00 14.75 ?  112 ALA   B H    1 
ATOM   5838 H HA   . ALA   B 1 112 ? 35.613 -19.462 2.766   1.00 14.48 ?  112 ALA   B HA   1 
ATOM   5839 H HB1  . ALA   B 1 112 ? 37.048 -21.288 2.535   1.00 14.83 ?  112 ALA   B HB1  1 
ATOM   5840 H HB2  . ALA   B 1 112 ? 36.195 -21.413 3.869   1.00 14.83 ?  112 ALA   B HB2  1 
ATOM   5841 H HB3  . ALA   B 1 112 ? 35.800 -22.270 2.591   1.00 14.83 ?  112 ALA   B HB3  1 
ATOM   5842 N N    . TYR   B 1 113 ? 34.500 -21.097 0.236   1.00 11.35 ?  113 TYR   B N    1 
ATOM   5843 C CA   . TYR   B 1 113 ? 34.423 -21.044 -1.218  1.00 11.02 ?  113 TYR   B CA   1 
ATOM   5844 C C    . TYR   B 1 113 ? 33.718 -19.791 -1.725  1.00 10.74 ?  113 TYR   B C    1 
ATOM   5845 O O    . TYR   B 1 113 ? 33.989 -19.361 -2.848  1.00 11.00 ?  113 TYR   B O    1 
ATOM   5846 C CB   . TYR   B 1 113 ? 33.749 -22.298 -1.779  1.00 11.09 ?  113 TYR   B CB   1 
ATOM   5847 C CG   . TYR   B 1 113 ? 34.701 -23.449 -2.027  1.00 11.31 ?  113 TYR   B CG   1 
ATOM   5848 C CD1  . TYR   B 1 113 ? 35.698 -23.352 -2.989  1.00 11.88 ?  113 TYR   B CD1  1 
ATOM   5849 C CD2  . TYR   B 1 113 ? 34.597 -24.635 -1.315  1.00 11.71 ?  113 TYR   B CD2  1 
ATOM   5850 C CE1  . TYR   B 1 113 ? 36.577 -24.387 -3.231  1.00 11.98 ?  113 TYR   B CE1  1 
ATOM   5851 C CE2  . TYR   B 1 113 ? 35.467 -25.687 -1.553  1.00 12.00 ?  113 TYR   B CE2  1 
ATOM   5852 C CZ   . TYR   B 1 113 ? 36.451 -25.560 -2.517  1.00 11.93 ?  113 TYR   B CZ   1 
ATOM   5853 O OH   . TYR   B 1 113 ? 37.340 -26.574 -2.794  1.00 12.88 ?  113 TYR   B OH   1 
ATOM   5854 H H    . TYR   B 1 113 ? 34.055 -21.737 0.602   1.00 13.62 ?  113 TYR   B H    1 
ATOM   5855 H HA   . TYR   B 1 113 ? 35.323 -21.024 -1.565  1.00 13.22 ?  113 TYR   B HA   1 
ATOM   5856 H HB2  . TYR   B 1 113 ? 33.075 -22.605 -1.148  1.00 13.31 ?  113 TYR   B HB2  1 
ATOM   5857 H HB3  . TYR   B 1 113 ? 33.324 -22.075 -2.623  1.00 13.31 ?  113 TYR   B HB3  1 
ATOM   5858 H HD1  . TYR   B 1 113 ? 35.783 -22.563 -3.480  1.00 14.26 ?  113 TYR   B HD1  1 
ATOM   5859 H HD2  . TYR   B 1 113 ? 33.931 -24.723 -0.675  1.00 14.05 ?  113 TYR   B HD2  1 
ATOM   5860 H HE1  . TYR   B 1 113 ? 37.239 -24.303 -3.886  1.00 14.37 ?  113 TYR   B HE1  1 
ATOM   5861 H HE2  . TYR   B 1 113 ? 35.383 -26.476 -1.072  1.00 14.40 ?  113 TYR   B HE2  1 
ATOM   5862 H HH   . TYR   B 1 113 ? 37.170 -27.241 -2.307  1.00 15.45 ?  113 TYR   B HH   1 
ATOM   5863 N N    . GLU   B 1 114 ? 32.790 -19.223 -0.947  1.00 11.22 ?  114 GLU   B N    1 
ATOM   5864 C CA   . GLU   B 1 114 ? 32.111 -18.010 -1.397  1.00 10.93 ?  114 GLU   B CA   1 
ATOM   5865 C C    . GLU   B 1 114 ? 33.097 -16.887 -1.687  1.00 10.84 ?  114 GLU   B C    1 
ATOM   5866 O O    . GLU   B 1 114 ? 32.814 -16.018 -2.516  1.00 11.40 ?  114 GLU   B O    1 
ATOM   5867 C CB   . GLU   B 1 114 ? 31.050 -17.584 -0.376  1.00 11.27 ?  114 GLU   B CB   1 
ATOM   5868 C CG   . GLU   B 1 114 ? 29.827 -18.504 -0.445  1.00 11.89 ?  114 GLU   B CG   1 
ATOM   5869 C CD   . GLU   B 1 114 ? 28.803 -18.325 0.665   1.00 12.13 ?  114 GLU   B CD   1 
ATOM   5870 O OE1  . GLU   B 1 114 ? 29.094 -17.713 1.713   1.00 12.27 ?  114 GLU   B OE1  1 
ATOM   5871 O OE2  . GLU   B 1 114 ? 27.678 -18.859 0.488   1.00 13.22 -1 114 GLU   B OE2  1 
ATOM   5872 H H    . GLU   B 1 114 ? 32.540 -19.517 -0.174  1.00 13.46 ?  114 GLU   B H    1 
ATOM   5873 H HA   . GLU   B 1 114 ? 31.650 -18.209 -2.221  1.00 13.12 ?  114 GLU   B HA   1 
ATOM   5874 H HB2  . GLU   B 1 114 ? 31.424 -17.638 0.520   1.00 13.53 ?  114 GLU   B HB2  1 
ATOM   5875 H HB3  . GLU   B 1 114 ? 30.764 -16.680 -0.568  1.00 13.53 ?  114 GLU   B HB3  1 
ATOM   5876 H HG2  . GLU   B 1 114 ? 29.374 -18.346 -1.283  1.00 14.26 ?  114 GLU   B HG2  1 
ATOM   5877 H HG3  . GLU   B 1 114 ? 30.135 -19.424 -0.408  1.00 14.26 ?  114 GLU   B HG3  1 
ATOM   5878 N N    . ASN   B 1 115 ? 34.265 -16.888 -1.037  1.00 10.63 ?  115 ASN   B N    1 
ATOM   5879 C CA   . ASN   B 1 115 ? 35.253 -15.852 -1.329  1.00 10.48 ?  115 ASN   B CA   1 
ATOM   5880 C C    . ASN   B 1 115 ? 35.670 -15.873 -2.790  1.00 10.71 ?  115 ASN   B C    1 
ATOM   5881 O O    . ASN   B 1 115 ? 36.056 -14.831 -3.344  1.00 11.15 ?  115 ASN   B O    1 
ATOM   5882 C CB   . ASN   B 1 115 ? 36.496 -16.022 -0.450  1.00 11.47 ?  115 ASN   B CB   1 
ATOM   5883 C CG   . ASN   B 1 115 ? 36.222 -15.762 1.014   1.00 11.79 ?  115 ASN   B CG   1 
ATOM   5884 O OD1  . ASN   B 1 115 ? 36.221 -14.614 1.460   1.00 13.61 ?  115 ASN   B OD1  1 
ATOM   5885 N ND2  . ASN   B 1 115 ? 36.045 -16.828 1.784   1.00 11.76 ?  115 ASN   B ND2  1 
ATOM   5886 H H    . ASN   B 1 115 ? 34.499 -17.449 -0.428  1.00 12.75 ?  115 ASN   B H    1 
ATOM   5887 H HA   . ASN   B 1 115 ? 34.872 -14.978 -1.142  1.00 12.57 ?  115 ASN   B HA   1 
ATOM   5888 H HB2  . ASN   B 1 115 ? 36.823 -16.931 -0.538  1.00 13.76 ?  115 ASN   B HB2  1 
ATOM   5889 H HB3  . ASN   B 1 115 ? 37.177 -15.395 -0.738  1.00 13.76 ?  115 ASN   B HB3  1 
ATOM   5890 H HD21 . ASN   B 1 115 ? 35.891 -16.737 2.628   1.00 14.11 ?  115 ASN   B HD21 1 
ATOM   5891 H HD22 . ASN   B 1 115 ? 36.065 -17.620 1.441   1.00 14.11 ?  115 ASN   B HD22 1 
ATOM   5892 N N    . PHE   B 1 116 ? 35.643 -17.052 -3.425  1.00 10.50 ?  116 PHE   B N    1 
ATOM   5893 C CA   . PHE   B 1 116 ? 36.072 -17.143 -4.815  1.00 10.64 ?  116 PHE   B CA   1 
ATOM   5894 C C    . PHE   B 1 116 ? 35.170 -16.320 -5.726  1.00 10.63 ?  116 PHE   B C    1 
ATOM   5895 O O    . PHE   B 1 116 ? 35.609 -15.883 -6.798  1.00 11.21 ?  116 PHE   B O    1 
ATOM   5896 C CB   . PHE   B 1 116 ? 36.047 -18.587 -5.347  1.00 10.81 ?  116 PHE   B CB   1 
ATOM   5897 C CG   . PHE   B 1 116 ? 37.111 -19.540 -4.800  1.00 10.64 ?  116 PHE   B CG   1 
ATOM   5898 C CD1  . PHE   B 1 116 ? 37.762 -19.353 -3.593  1.00 10.97 ?  116 PHE   B CD1  1 
ATOM   5899 C CD2  . PHE   B 1 116 ? 37.408 -20.678 -5.535  1.00 10.90 ?  116 PHE   B CD2  1 
ATOM   5900 C CE1  . PHE   B 1 116 ? 38.696 -20.292 -3.141  1.00 11.40 ?  116 PHE   B CE1  1 
ATOM   5901 C CE2  . PHE   B 1 116 ? 38.333 -21.615 -5.089  1.00 11.08 ?  116 PHE   B CE2  1 
ATOM   5902 C CZ   . PHE   B 1 116 ? 38.971 -21.423 -3.897  1.00 10.94 ?  116 PHE   B CZ   1 
ATOM   5903 H H    . PHE   B 1 116 ? 35.384 -17.799 -3.077  1.00 12.60 ?  116 PHE   B H    1 
ATOM   5904 H HA   . PHE   B 1 116 ? 36.973 -16.808 -4.898  1.00 12.76 ?  116 PHE   B HA   1 
ATOM   5905 H HB2  . PHE   B 1 116 ? 35.176 -18.972 -5.140  1.00 12.97 ?  116 PHE   B HB2  1 
ATOM   5906 H HB3  . PHE   B 1 116 ? 36.152 -18.556 -6.313  1.00 12.97 ?  116 PHE   B HB3  1 
ATOM   5907 H HD1  . PHE   B 1 116 ? 37.570 -18.598 -3.077  1.00 13.16 ?  116 PHE   B HD1  1 
ATOM   5908 H HD2  . PHE   B 1 116 ? 36.969 -20.826 -6.343  1.00 13.08 ?  116 PHE   B HD2  1 
ATOM   5909 H HE1  . PHE   B 1 116 ? 39.135 -20.151 -2.335  1.00 13.69 ?  116 PHE   B HE1  1 
ATOM   5910 H HE2  . PHE   B 1 116 ? 38.523 -22.367 -5.605  1.00 13.30 ?  116 PHE   B HE2  1 
ATOM   5911 H HZ   . PHE   B 1 116 ? 39.607 -22.031 -3.601  1.00 13.13 ?  116 PHE   B HZ   1 
ATOM   5912 N N    . ASN   B 1 117 ? 33.900 -16.124 -5.345  1.00 10.91 ?  117 ASN   B N    1 
ATOM   5913 C CA   . ASN   B 1 117 ? 32.961 -15.413 -6.212  1.00 11.04 ?  117 ASN   B CA   1 
ATOM   5914 C C    . ASN   B 1 117 ? 33.275 -13.933 -6.357  1.00 11.73 ?  117 ASN   B C    1 
ATOM   5915 O O    . ASN   B 1 117 ? 32.681 -13.275 -7.216  1.00 12.90 ?  117 ASN   B O    1 
ATOM   5916 C CB   . ASN   B 1 117 ? 31.535 -15.626 -5.730  1.00 11.36 ?  117 ASN   B CB   1 
ATOM   5917 C CG   . ASN   B 1 117 ? 31.080 -17.036 -5.987  1.00 11.56 ?  117 ASN   B CG   1 
ATOM   5918 O OD1  . ASN   B 1 117 ? 31.438 -17.622 -7.009  1.00 12.65 ?  117 ASN   B OD1  1 
ATOM   5919 N ND2  . ASN   B 1 117 ? 30.354 -17.615 -5.049  1.00 11.83 ?  117 ASN   B ND2  1 
ATOM   5920 H H    . ASN   B 1 117 ? 33.565 -16.384 -4.593  1.00 13.09 ?  117 ASN   B H    1 
ATOM   5921 H HA   . ASN   B 1 117 ? 33.025 -15.803 -7.093  1.00 13.25 ?  117 ASN   B HA   1 
ATOM   5922 H HB2  . ASN   B 1 117 ? 31.486 -15.461 -4.774  1.00 13.63 ?  117 ASN   B HB2  1 
ATOM   5923 H HB3  . ASN   B 1 117 ? 30.943 -15.016 -6.203  1.00 13.63 ?  117 ASN   B HB3  1 
ATOM   5924 H HD21 . ASN   B 1 117 ? 30.072 -18.415 -5.159  1.00 14.19 ?  117 ASN   B HD21 1 
ATOM   5925 H HD22 . ASN   B 1 117 ? 30.131 -17.168 -4.347  1.00 14.19 ?  117 ASN   B HD22 1 
ATOM   5926 N N    . GLN   B 1 118 ? 34.203 -13.408 -5.568  1.00 11.50 ?  118 GLN   B N    1 
ATOM   5927 C CA   . GLN   B 1 118 ? 34.629 -12.020 -5.700  1.00 11.86 ?  118 GLN   B CA   1 
ATOM   5928 C C    . GLN   B 1 118 ? 35.703 -11.824 -6.764  1.00 12.22 ?  118 GLN   B C    1 
ATOM   5929 O O    . GLN   B 1 118 ? 36.180 -10.696 -6.940  1.00 13.57 ?  118 GLN   B O    1 
ATOM   5930 C CB   . GLN   B 1 118 ? 35.092 -11.490 -4.344  1.00 12.46 ?  118 GLN   B CB   1 
ATOM   5931 C CG   . GLN   B 1 118 ? 34.000 -11.531 -3.283  1.00 12.60 ?  118 GLN   B CG   1 
ATOM   5932 C CD   . GLN   B 1 118 ? 32.831 -10.630 -3.618  1.00 12.56 ?  118 GLN   B CD   1 
ATOM   5933 O OE1  . GLN   B 1 118 ? 33.017 -9.492  -4.062  1.00 13.38 ?  118 GLN   B OE1  1 
ATOM   5934 N NE2  . GLN   B 1 118 ? 31.617 -11.124 -3.403  1.00 12.85 ?  118 GLN   B NE2  1 
ATOM   5935 H H    . GLN   B 1 118 ? 34.611 -13.833 -4.936  1.00 13.80 ?  118 GLN   B H    1 
ATOM   5936 H HA   . GLN   B 1 118 ? 33.860 -11.495 -5.975  1.00 14.23 ?  118 GLN   B HA   1 
ATOM   5937 H HB2  . GLN   B 1 118 ? 35.832 -12.020 -4.028  1.00 14.95 ?  118 GLN   B HB2  1 
ATOM   5938 H HB3  . GLN   B 1 118 ? 35.365 -10.560 -4.446  1.00 14.95 ?  118 GLN   B HB3  1 
ATOM   5939 H HG2  . GLN   B 1 118 ? 33.667 -12.437 -3.203  1.00 15.12 ?  118 GLN   B HG2  1 
ATOM   5940 H HG3  . GLN   B 1 118 ? 34.371 -11.237 -2.434  1.00 15.12 ?  118 GLN   B HG3  1 
ATOM   5941 H HE21 . GLN   B 1 118 ? 31.529 -11.922 -3.091  1.00 15.42 ?  118 GLN   B HE21 1 
ATOM   5942 H HE22 . GLN   B 1 118 ? 30.928 -10.648 -3.576  1.00 15.42 ?  118 GLN   B HE22 1 
ATOM   5943 N N    . HIS   B 1 119 ? 36.060 -12.881 -7.498  1.00 11.45 ?  119 HIS   B N    1 
ATOM   5944 C CA   . HIS   B 1 119 ? 37.110 -12.829 -8.508  1.00 11.71 ?  119 HIS   B CA   1 
ATOM   5945 C C    . HIS   B 1 119 ? 36.635 -13.551 -9.752  1.00 11.82 ?  119 HIS   B C    1 
ATOM   5946 O O    . HIS   B 1 119 ? 36.137 -14.671 -9.660  1.00 12.65 ?  119 HIS   B O    1 
ATOM   5947 C CB   . HIS   B 1 119 ? 38.384 -13.470 -7.957  1.00 12.13 ?  119 HIS   B CB   1 
ATOM   5948 C CG   . HIS   B 1 119 ? 38.858 -12.781 -6.727  1.00 13.65 ?  119 HIS   B CG   1 
ATOM   5949 N ND1  . HIS   B 1 119 ? 39.649 -11.654 -6.774  1.00 15.26 ?  119 HIS   B ND1  1 
ATOM   5950 C CD2  . HIS   B 1 119 ? 38.551 -12.975 -5.425  1.00 14.92 ?  119 HIS   B CD2  1 
ATOM   5951 C CE1  . HIS   B 1 119 ? 39.847 -11.213 -5.547  1.00 16.13 ?  119 HIS   B CE1  1 
ATOM   5952 N NE2  . HIS   B 1 119 ? 39.186 -11.990 -4.710  1.00 16.20 ?  119 HIS   B NE2  1 
ATOM   5953 H H    . HIS   B 1 119 ? 35.686 -13.659 -7.431  1.00 13.74 ?  119 HIS   B H    1 
ATOM   5954 H HA   . HIS   B 1 119 ? 37.290 -11.902 -8.736  1.00 14.05 ?  119 HIS   B HA   1 
ATOM   5955 H HB2  . HIS   B 1 119 ? 38.201 -14.396 -7.743  1.00 14.56 ?  119 HIS   B HB2  1 
ATOM   5956 H HB3  . HIS   B 1 119 ? 39.077 -13.410 -8.633  1.00 14.56 ?  119 HIS   B HB3  1 
ATOM   5957 H HD2  . HIS   B 1 119 ? 38.014 -13.653 -5.081  1.00 17.90 ?  119 HIS   B HD2  1 
ATOM   5958 H HE1  . HIS   B 1 119 ? 40.379 -10.489 -5.310  1.00 19.36 ?  119 HIS   B HE1  1 
ATOM   5959 H HE2  . HIS   B 1 119 ? 39.185 -11.918 -3.854  1.00 19.44 ?  119 HIS   B HE2  1 
ATOM   5960 N N    . GLU   B 1 120 ? 36.790 -12.922 -10.916 1.00 12.35 ?  120 GLU   B N    1 
ATOM   5961 C CA   . GLU   B 1 120 ? 36.214 -13.499 -12.126 1.00 13.87 ?  120 GLU   B CA   1 
ATOM   5962 C C    . GLU   B 1 120 ? 36.891 -14.802 -12.534 1.00 12.52 ?  120 GLU   B C    1 
ATOM   5963 O O    . GLU   B 1 120 ? 36.230 -15.677 -13.111 1.00 13.10 ?  120 GLU   B O    1 
ATOM   5964 C CB   . GLU   B 1 120 ? 36.258 -12.490 -13.269 1.00 18.13 ?  120 GLU   B CB   1 
ATOM   5965 C CG   . GLU   B 1 120 ? 35.321 -11.309 -13.069 1.00 24.11 ?  120 GLU   B CG   1 
ATOM   5966 C CD   . GLU   B 1 120 ? 35.137 -10.482 -14.322 1.00 29.84 ?  120 GLU   B CD   1 
ATOM   5967 O OE1  . GLU   B 1 120 ? 36.148 -10.205 -15.003 1.00 31.75 ?  120 GLU   B OE1  1 
ATOM   5968 O OE2  . GLU   B 1 120 ? 33.982 -10.112 -14.625 1.00 32.10 -1 120 GLU   B OE2  1 
ATOM   5969 H H    . GLU   B 1 120 ? 37.209 -12.176 -11.031 1.00 14.82 ?  120 GLU   B H    1 
ATOM   5970 H HA   . GLU   B 1 120 ? 35.283 -13.702 -11.953 1.00 16.65 ?  120 GLU   B HA   1 
ATOM   5971 H HB2  . GLU   B 1 120 ? 37.156 -12.144 -13.353 1.00 21.76 ?  120 GLU   B HB2  1 
ATOM   5972 H HB3  . GLU   B 1 120 ? 35.995 -12.936 -14.091 1.00 21.76 ?  120 GLU   B HB3  1 
ATOM   5973 H HG2  . GLU   B 1 120 ? 34.447 -11.636 -12.804 1.00 28.94 ?  120 GLU   B HG2  1 
ATOM   5974 H HG3  . GLU   B 1 120 ? 35.683 -10.731 -12.381 1.00 28.94 ?  120 GLU   B HG3  1 
ATOM   5975 N N    . VAL   B 1 121 ? 38.190 -14.944 -12.270 1.00 12.25 ?  121 VAL   B N    1 
ATOM   5976 C CA   . VAL   B 1 121 ? 38.928 -16.152 -12.627 1.00 12.21 ?  121 VAL   B CA   1 
ATOM   5977 C C    . VAL   B 1 121 ? 40.035 -16.372 -11.605 1.00 11.93 ?  121 VAL   B C    1 
ATOM   5978 O O    . VAL   B 1 121 ? 40.717 -15.421 -11.201 1.00 12.24 ?  121 VAL   B O    1 
ATOM   5979 C CB   . VAL   B 1 121 ? 39.446 -16.102 -14.082 1.00 13.90 ?  121 VAL   B CB   1 
ATOM   5980 C CG1  . VAL   B 1 121 ? 40.326 -14.886 -14.318 1.00 15.01 ?  121 VAL   B CG1  1 
ATOM   5981 C CG2  . VAL   B 1 121 ? 40.168 -17.391 -14.439 1.00 15.45 ?  121 VAL   B CG2  1 
ATOM   5982 H H    . VAL   B 1 121 ? 38.676 -14.338 -11.888 1.00 14.71 ?  121 VAL   B H    1 
ATOM   5983 H HA   . VAL   B 1 121 ? 38.314 -16.898 -12.565 1.00 14.65 ?  121 VAL   B HA   1 
ATOM   5984 H HB   . VAL   B 1 121 ? 38.680 -16.022 -14.676 1.00 16.67 ?  121 VAL   B HB   1 
ATOM   5985 H HG11 . VAL   B 1 121 ? 40.631 -14.893 -15.238 1.00 18.02 ?  121 VAL   B HG11 1 
ATOM   5986 H HG12 . VAL   B 1 121 ? 39.809 -14.082 -14.148 1.00 18.02 ?  121 VAL   B HG12 1 
ATOM   5987 H HG13 . VAL   B 1 121 ? 41.085 -14.926 -13.716 1.00 18.02 ?  121 VAL   B HG13 1 
ATOM   5988 H HG21 . VAL   B 1 121 ? 40.366 -17.387 -15.389 1.00 18.53 ?  121 VAL   B HG21 1 
ATOM   5989 H HG22 . VAL   B 1 121 ? 40.990 -17.445 -13.930 1.00 18.53 ?  121 VAL   B HG22 1 
ATOM   5990 H HG23 . VAL   B 1 121 ? 39.594 -18.144 -14.226 1.00 18.53 ?  121 VAL   B HG23 1 
ATOM   5991 N N    . LEU   B 1 122 ? 40.212 -17.633 -11.188 1.00 11.28 ?  122 LEU   B N    1 
ATOM   5992 C CA   . LEU   B 1 122 ? 41.184 -17.994 -10.157 1.00 11.01 ?  122 LEU   B CA   1 
ATOM   5993 C C    . LEU   B 1 122 ? 41.853 -19.316 -10.488 1.00 10.67 ?  122 LEU   B C    1 
ATOM   5994 O O    . LEU   B 1 122 ? 41.198 -20.233 -10.990 1.00 11.92 ?  122 LEU   B O    1 
ATOM   5995 C CB   . LEU   B 1 122 ? 40.519 -18.234 -8.792  1.00 12.46 ?  122 LEU   B CB   1 
ATOM   5996 C CG   . LEU   B 1 122 ? 39.498 -17.208 -8.295  1.00 12.58 ?  122 LEU   B CG   1 
ATOM   5997 C CD1  . LEU   B 1 122 ? 38.090 -17.548 -8.760  1.00 13.20 ?  122 LEU   B CD1  1 
ATOM   5998 C CD2  . LEU   B 1 122 ? 39.555 -17.098 -6.787  1.00 12.04 ?  122 LEU   B CD2  1 
ATOM   5999 H H    . LEU   B 1 122 ? 39.777 -18.308 -11.499 1.00 13.54 ?  122 LEU   B H    1 
ATOM   6000 H HA   . LEU   B 1 122 ? 41.856 -17.300 -10.070 1.00 13.21 ?  122 LEU   B HA   1 
ATOM   6001 H HB2  . LEU   B 1 122 ? 40.062 -19.085 -8.828  1.00 14.96 ?  122 LEU   B HB2  1 
ATOM   6002 H HB3  . LEU   B 1 122 ? 41.219 -18.274 -8.124  1.00 14.96 ?  122 LEU   B HB3  1 
ATOM   6003 H HG   . LEU   B 1 122 ? 39.724 -16.337 -8.661  1.00 15.10 ?  122 LEU   B HG   1 
ATOM   6004 H HD11 . LEU   B 1 122 ? 37.472 -16.886 -8.409  1.00 15.84 ?  122 LEU   B HD11 1 
ATOM   6005 H HD12 . LEU   B 1 122 ? 38.066 -17.536 -9.730  1.00 15.84 ?  122 LEU   B HD12 1 
ATOM   6006 H HD13 . LEU   B 1 122 ? 37.853 -18.428 -8.433  1.00 15.84 ?  122 LEU   B HD13 1 
ATOM   6007 H HD21 . LEU   B 1 122 ? 38.881 -16.469 -6.488  1.00 14.45 ?  122 LEU   B HD21 1 
ATOM   6008 H HD22 . LEU   B 1 122 ? 39.396 -17.969 -6.400  1.00 14.45 ?  122 LEU   B HD22 1 
ATOM   6009 H HD23 . LEU   B 1 122 ? 40.439 -16.778 -6.530  1.00 14.45 ?  122 LEU   B HD23 1 
ATOM   6010 N N    . LEU   B 1 123 ? 43.139 -19.421 -10.139 1.00 10.68 ?  123 LEU   B N    1 
ATOM   6011 C CA   . LEU   B 1 123 ? 43.852 -20.690 -10.009 1.00 10.44 ?  123 LEU   B CA   1 
ATOM   6012 C C    . LEU   B 1 123 ? 43.814 -21.090 -8.537  1.00 9.96  ?  123 LEU   B C    1 
ATOM   6013 O O    . LEU   B 1 123 ? 44.166 -20.270 -7.683  1.00 10.79 ?  123 LEU   B O    1 
ATOM   6014 C CB   . LEU   B 1 123 ? 45.306 -20.509 -10.448 1.00 11.09 ?  123 LEU   B CB   1 
ATOM   6015 C CG   . LEU   B 1 123 ? 46.239 -21.696 -10.203 1.00 11.62 ?  123 LEU   B CG   1 
ATOM   6016 C CD1  . LEU   B 1 123 ? 45.798 -22.933 -10.985 1.00 11.99 ?  123 LEU   B CD1  1 
ATOM   6017 C CD2  . LEU   B 1 123 ? 47.671 -21.313 -10.571 1.00 12.31 ?  123 LEU   B CD2  1 
ATOM   6018 H H    . LEU   B 1 123 ? 43.634 -18.738 -9.952  1.00 12.82 ?  123 LEU   B H    1 
ATOM   6019 H HA   . LEU   B 1 123 ? 43.419 -21.377 -10.545 1.00 12.53 ?  123 LEU   B HA   1 
ATOM   6020 H HB2  . LEU   B 1 123 ? 45.311 -20.334 -11.401 1.00 13.30 ?  123 LEU   B HB2  1 
ATOM   6021 H HB3  . LEU   B 1 123 ? 45.673 -19.753 -9.974  1.00 13.30 ?  123 LEU   B HB3  1 
ATOM   6022 H HG   . LEU   B 1 123 ? 46.228 -21.925 -9.259  1.00 13.94 ?  123 LEU   B HG   1 
ATOM   6023 H HD11 . LEU   B 1 123 ? 46.432 -23.645 -10.830 1.00 14.38 ?  123 LEU   B HD11 1 
ATOM   6024 H HD12 . LEU   B 1 123 ? 44.915 -23.198 -10.679 1.00 14.38 ?  123 LEU   B HD12 1 
ATOM   6025 H HD13 . LEU   B 1 123 ? 45.767 -22.709 -11.928 1.00 14.38 ?  123 LEU   B HD13 1 
ATOM   6026 H HD21 . LEU   B 1 123 ? 48.249 -22.074 -10.411 1.00 14.77 ?  123 LEU   B HD21 1 
ATOM   6027 H HD22 . LEU   B 1 123 ? 47.695 -21.068 -11.509 1.00 14.77 ?  123 LEU   B HD22 1 
ATOM   6028 H HD23 . LEU   B 1 123 ? 47.943 -20.564 -10.022 1.00 14.77 ?  123 LEU   B HD23 1 
ATOM   6029 N N    . ALA   B 1 124 ? 43.372 -22.315 -8.227  1.00 10.04 ?  124 ALA   B N    1 
ATOM   6030 C CA   . ALA   B 1 124 ? 43.110 -22.639 -6.832  1.00 10.27 ?  124 ALA   B CA   1 
ATOM   6031 C C    . ALA   B 1 124 ? 43.388 -24.103 -6.520  1.00 10.04 ?  124 ALA   B C    1 
ATOM   6032 O O    . ALA   B 1 124 ? 43.258 -24.976 -7.392  1.00 10.78 ?  124 ALA   B O    1 
ATOM   6033 C CB   . ALA   B 1 124 ? 41.654 -22.343 -6.464  1.00 10.78 ?  124 ALA   B CB   1 
ATOM   6034 H H    . ALA   B 1 124 ? 43.203 -22.950 -8.791  1.00 12.05 ?  124 ALA   B H    1 
ATOM   6035 H HA   . ALA   B 1 124 ? 43.685 -22.088 -6.280  1.00 12.32 ?  124 ALA   B HA   1 
ATOM   6036 H HB1  . ALA   B 1 124 ? 41.509 -22.569 -5.531  1.00 12.94 ?  124 ALA   B HB1  1 
ATOM   6037 H HB2  . ALA   B 1 124 ? 41.478 -21.402 -6.609  1.00 12.94 ?  124 ALA   B HB2  1 
ATOM   6038 H HB3  . ALA   B 1 124 ? 41.071 -22.880 -7.027  1.00 12.94 ?  124 ALA   B HB3  1 
ATOM   6039 N N    . PRO   B 1 125 ? 43.677 -24.404 -5.257  1.00 10.32 ?  125 PRO   B N    1 
ATOM   6040 C CA   . PRO   B 1 125 ? 43.615 -25.770 -4.740  1.00 10.82 ?  125 PRO   B CA   1 
ATOM   6041 C C    . PRO   B 1 125 ? 42.212 -26.042 -4.199  1.00 11.08 ?  125 PRO   B C    1 
ATOM   6042 O O    . PRO   B 1 125 ? 41.411 -25.127 -3.993  1.00 11.50 ?  125 PRO   B O    1 
ATOM   6043 C CB   . PRO   B 1 125 ? 44.602 -25.702 -3.565  1.00 12.16 ?  125 PRO   B CB   1 
ATOM   6044 C CG   . PRO   B 1 125 ? 44.355 -24.311 -2.992  1.00 12.05 ?  125 PRO   B CG   1 
ATOM   6045 C CD   . PRO   B 1 125 ? 44.005 -23.441 -4.189  1.00 11.29 ?  125 PRO   B CD   1 
ATOM   6046 H HA   . PRO   B 1 125 ? 43.892 -26.435 -5.386  1.00 12.98 ?  125 PRO   B HA   1 
ATOM   6047 H HB2  . PRO   B 1 125 ? 44.392 -26.388 -2.906  1.00 14.59 ?  125 PRO   B HB2  1 
ATOM   6048 H HB3  . PRO   B 1 125 ? 45.512 -25.790 -3.880  1.00 14.59 ?  125 PRO   B HB3  1 
ATOM   6049 H HG2  . PRO   B 1 125 ? 43.612 -24.336 -2.362  1.00 14.46 ?  125 PRO   B HG2  1 
ATOM   6050 H HG3  . PRO   B 1 125 ? 45.158 -23.985 -2.548  1.00 14.46 ?  125 PRO   B HG3  1 
ATOM   6051 H HD2  . PRO   B 1 125 ? 43.244 -22.877 -3.987  1.00 13.54 ?  125 PRO   B HD2  1 
ATOM   6052 H HD3  . PRO   B 1 125 ? 44.781 -22.904 -4.443  1.00 13.54 ?  125 PRO   B HD3  1 
ATOM   6053 N N    . LEU   B 1 126 ? 41.945 -27.320 -3.916  1.00 11.77 ?  126 LEU   B N    1 
ATOM   6054 C CA   . LEU   B 1 126 ? 40.718 -27.684 -3.211  1.00 11.91 ?  126 LEU   B CA   1 
ATOM   6055 C C    . LEU   B 1 126 ? 40.828 -27.282 -1.747  1.00 12.03 ?  126 LEU   B C    1 
ATOM   6056 O O    . LEU   B 1 126 ? 41.719 -27.740 -1.026  1.00 13.84 ?  126 LEU   B O    1 
ATOM   6057 C CB   . LEU   B 1 126 ? 40.460 -29.179 -3.321  1.00 13.12 ?  126 LEU   B CB   1 
ATOM   6058 C CG   . LEU   B 1 126 ? 39.937 -29.659 -4.673  1.00 14.17 ?  126 LEU   B CG   1 
ATOM   6059 C CD1  . LEU   B 1 126 ? 39.987 -31.169 -4.740  1.00 15.82 ?  126 LEU   B CD1  1 
ATOM   6060 C CD2  . LEU   B 1 126 ? 38.520 -29.166 -4.923  1.00 14.26 ?  126 LEU   B CD2  1 
ATOM   6061 H H    . LEU   B 1 126 ? 42.455 -27.986 -4.111  1.00 14.13 ?  126 LEU   B H    1 
ATOM   6062 H HA   . LEU   B 1 126 ? 39.969 -27.206 -3.607  1.00 14.29 ?  126 LEU   B HA   1 
ATOM   6063 H HB2  . LEU   B 1 126 ? 41.288 -29.643 -3.147  1.00 15.74 ?  126 LEU   B HB2  1 
ATOM   6064 H HB3  . LEU   B 1 126 ? 39.799 -29.421 -2.653  1.00 15.74 ?  126 LEU   B HB3  1 
ATOM   6065 H HG   . LEU   B 1 126 ? 40.507 -29.305 -5.377  1.00 17.00 ?  126 LEU   B HG   1 
ATOM   6066 H HD11 . LEU   B 1 126 ? 39.647 -31.456 -5.602  1.00 18.99 ?  126 LEU   B HD11 1 
ATOM   6067 H HD12 . LEU   B 1 126 ? 40.901 -31.460 -4.626  1.00 18.99 ?  126 LEU   B HD12 1 
ATOM   6068 H HD13 . LEU   B 1 126 ? 39.430 -31.530 -4.030  1.00 18.99 ?  126 LEU   B HD13 1 
ATOM   6069 H HD21 . LEU   B 1 126 ? 38.177 -29.580 -5.728  1.00 17.11 ?  126 LEU   B HD21 1 
ATOM   6070 H HD22 . LEU   B 1 126 ? 37.965 -29.400 -4.164  1.00 17.11 ?  126 LEU   B HD22 1 
ATOM   6071 H HD23 . LEU   B 1 126 ? 38.535 -28.197 -5.032  1.00 17.11 ?  126 LEU   B HD23 1 
ATOM   6072 N N    . LEU   B 1 127 ? 39.896 -26.452 -1.295  1.00 11.99 ?  127 LEU   B N    1 
ATOM   6073 C CA   . LEU   B 1 127 ? 39.946 -25.957 0.069   1.00 12.39 ?  127 LEU   B CA   1 
ATOM   6074 C C    . LEU   B 1 127 ? 39.667 -27.077 1.063   1.00 12.20 ?  127 LEU   B C    1 
ATOM   6075 O O    . LEU   B 1 127 ? 38.848 -27.976 0.829   1.00 12.41 ?  127 LEU   B O    1 
ATOM   6076 C CB   . LEU   B 1 127 ? 38.925 -24.837 0.272   1.00 12.89 ?  127 LEU   B CB   1 
ATOM   6077 C CG   . LEU   B 1 127 ? 39.110 -23.571 -0.565  1.00 13.31 ?  127 LEU   B CG   1 
ATOM   6078 C CD1  . LEU   B 1 127 ? 37.993 -22.595 -0.244  1.00 13.54 ?  127 LEU   B CD1  1 
ATOM   6079 C CD2  . LEU   B 1 127 ? 40.477 -22.932 -0.324  1.00 13.83 ?  127 LEU   B CD2  1 
ATOM   6080 H H    . LEU   B 1 127 ? 39.231 -26.151 -1.759  1.00 14.39 ?  127 LEU   B H    1 
ATOM   6081 H HA   . LEU   B 1 127 ? 40.830 -25.599 0.249   1.00 14.87 ?  127 LEU   B HA   1 
ATOM   6082 H HB2  . LEU   B 1 127 ? 38.043 -25.190 0.069   1.00 15.46 ?  127 LEU   B HB2  1 
ATOM   6083 H HB3  . LEU   B 1 127 ? 38.951 -24.569 1.205   1.00 15.46 ?  127 LEU   B HB3  1 
ATOM   6084 H HG   . LEU   B 1 127 ? 39.036 -23.797 -1.502  1.00 15.98 ?  127 LEU   B HG   1 
ATOM   6085 H HD11 . LEU   B 1 127 ? 38.115 -21.787 -0.770  1.00 16.25 ?  127 LEU   B HD11 1 
ATOM   6086 H HD12 . LEU   B 1 127 ? 37.138 -23.001 -0.459  1.00 16.25 ?  127 LEU   B HD12 1 
ATOM   6087 H HD13 . LEU   B 1 127 ? 38.023 -22.375 0.703   1.00 16.25 ?  127 LEU   B HD13 1 
ATOM   6088 H HD21 . LEU   B 1 127 ? 40.520 -22.079 -0.787  1.00 16.59 ?  127 LEU   B HD21 1 
ATOM   6089 H HD22 . LEU   B 1 127 ? 40.604 -22.793 0.629   1.00 16.59 ?  127 LEU   B HD22 1 
ATOM   6090 H HD23 . LEU   B 1 127 ? 41.167 -23.525 -0.663  1.00 16.59 ?  127 LEU   B HD23 1 
ATOM   6091 N N    . SER   B 1 128 ? 40.345 -26.993 2.198   1.00 12.09 ?  128 SER   B N    1 
ATOM   6092 C CA   . SER   B 1 128 ? 40.224 -27.906 3.323   1.00 12.60 ?  128 SER   B CA   1 
ATOM   6093 C C    . SER   B 1 128 ? 40.722 -29.314 3.010   1.00 13.51 ?  128 SER   B C    1 
ATOM   6094 O O    . SER   B 1 128 ? 40.618 -30.192 3.865   1.00 14.75 ?  128 SER   B O    1 
ATOM   6095 C CB   . SER   B 1 128 ? 38.815 -27.906 3.932   1.00 13.05 ?  128 SER   B CB   1 
ATOM   6096 O OG   . SER   B 1 128 ? 38.506 -26.631 4.489   1.00 13.66 ?  128 SER   B OG   1 
ATOM   6097 H H    . SER   B 1 128 ? 40.926 -26.374 2.342   1.00 14.51 ?  128 SER   B H    1 
ATOM   6098 H HA   . SER   B 1 128 ? 40.803 -27.569 4.012   1.00 15.12 ?  128 SER   B HA   1 
ATOM   6099 H HB2  . SER   B 1 128 ? 38.159 -28.121 3.243   1.00 15.66 ?  128 SER   B HB2  1 
ATOM   6100 H HB3  . SER   B 1 128 ? 38.771 -28.574 4.640   1.00 15.66 ?  128 SER   B HB3  1 
ATOM   6101 H HG   . SER   B 1 128 ? 39.072 -26.437 5.074   1.00 16.40 ?  128 SER   B HG   1 
ATOM   6102 N N    . ALA   B 1 129 ? 41.290 -29.542 1.824   1.00 14.15 ?  129 ALA   B N    1 
ATOM   6103 C CA   . ALA   B 1 129 ? 41.836 -30.838 1.456   1.00 14.93 ?  129 ALA   B CA   1 
ATOM   6104 C C    . ALA   B 1 129 ? 43.221 -31.020 2.060   1.00 14.37 ?  129 ALA   B C    1 
ATOM   6105 O O    . ALA   B 1 129 ? 43.780 -30.125 2.707   1.00 14.38 ?  129 ALA   B O    1 
ATOM   6106 C CB   . ALA   B 1 129 ? 41.895 -30.983 -0.062  1.00 17.23 ?  129 ALA   B CB   1 
ATOM   6107 H H    . ALA   B 1 129 ? 41.373 -28.948 1.207   1.00 16.98 ?  129 ALA   B H    1 
ATOM   6108 H HA   . ALA   B 1 129 ? 41.259 -31.531 1.802   1.00 17.91 ?  129 ALA   B HA   1 
ATOM   6109 H HB1  . ALA   B 1 129 ? 42.254 -31.856 -0.280  1.00 20.68 ?  129 ALA   B HB1  1 
ATOM   6110 H HB2  . ALA   B 1 129 ? 40.999 -30.893 -0.422  1.00 20.68 ?  129 ALA   B HB2  1 
ATOM   6111 H HB3  . ALA   B 1 129 ? 42.468 -30.288 -0.425  1.00 20.68 ?  129 ALA   B HB3  1 
ATOM   6112 N N    . GLY   B 1 130 ? 43.780 -32.205 1.839   1.00 14.57 ?  130 GLY   B N    1 
ATOM   6113 C CA   . GLY   B 1 130 ? 45.165 -32.438 2.195   1.00 14.65 ?  130 GLY   B CA   1 
ATOM   6114 C C    . GLY   B 1 130 ? 45.378 -32.333 3.685   1.00 14.66 ?  130 GLY   B C    1 
ATOM   6115 O O    . GLY   B 1 130 ? 44.678 -32.969 4.484   1.00 15.70 ?  130 GLY   B O    1 
ATOM   6116 H H    . GLY   B 1 130 ? 43.384 -32.877 1.479   1.00 17.48 ?  130 GLY   B H    1 
ATOM   6117 H HA2  . GLY   B 1 130 ? 45.429 -33.329 1.908   1.00 17.58 ?  130 GLY   B HA2  1 
ATOM   6118 H HA3  . GLY   B 1 130 ? 45.733 -31.791 1.753   1.00 17.58 ?  130 GLY   B HA3  1 
ATOM   6119 N N    . ILE   B 1 131 ? 46.353 -31.504 4.071   1.00 15.21 ?  131 ILE   B N    1 
ATOM   6120 C CA   . ILE   B 1 131 ? 46.713 -31.364 5.472   1.00 16.16 ?  131 ILE   B CA   1 
ATOM   6121 C C    . ILE   B 1 131 ? 45.593 -30.768 6.308   1.00 15.54 ?  131 ILE   B C    1 
ATOM   6122 O O    . ILE   B 1 131 ? 45.660 -30.833 7.536   1.00 17.06 ?  131 ILE   B O    1 
ATOM   6123 C CB   . ILE   B 1 131 ? 48.043 -30.592 5.669   1.00 17.96 ?  131 ILE   B CB   1 
ATOM   6124 C CG1  . ILE   B 1 131 ? 47.889 -29.105 5.318   1.00 18.83 ?  131 ILE   B CG1  1 
ATOM   6125 C CG2  . ILE   B 1 131 ? 49.164 -31.245 4.863   1.00 19.19 ?  131 ILE   B CG2  1 
ATOM   6126 C CD1  . ILE   B 1 131 ? 49.122 -28.276 5.639   1.00 20.16 ?  131 ILE   B CD1  1 
ATOM   6127 H H    . ILE   B 1 131 ? 46.818 -31.014 3.535   1.00 18.25 ?  131 ILE   B H    1 
ATOM   6128 H HA   . ILE   B 1 131 ? 46.864 -32.254 5.817   1.00 19.40 ?  131 ILE   B HA   1 
ATOM   6129 H HB   . ILE   B 1 131 ? 48.281 -30.651 6.606   1.00 21.55 ?  131 ILE   B HB   1 
ATOM   6130 H HG12 . ILE   B 1 131 ? 47.710 -29.023 4.370   1.00 22.60 ?  131 ILE   B HG12 1 
ATOM   6131 H HG13 . ILE   B 1 131 ? 47.147 -28.733 5.825   1.00 22.60 ?  131 ILE   B HG13 1 
ATOM   6132 H HG21 . ILE   B 1 131 ? 50.008 -30.848 5.123   1.00 23.03 ?  131 ILE   B HG21 1 
ATOM   6133 H HG22 . ILE   B 1 131 ? 49.169 -32.194 5.049   1.00 23.03 ?  131 ILE   B HG22 1 
ATOM   6134 H HG23 . ILE   B 1 131 ? 49.000 -31.091 3.920   1.00 23.03 ?  131 ILE   B HG23 1 
ATOM   6135 H HD11 . ILE   B 1 131 ? 48.916 -27.340 5.494   1.00 24.20 ?  131 ILE   B HD11 1 
ATOM   6136 H HD12 . ILE   B 1 131 ? 49.365 -28.422 6.567   1.00 24.20 ?  131 ILE   B HD12 1 
ATOM   6137 H HD13 . ILE   B 1 131 ? 49.846 -28.552 5.059   1.00 24.20 ?  131 ILE   B HD13 1 
ATOM   6138 N N    . PHE   B 1 132 ? 44.563 -30.193 5.676   1.00 13.96 ?  132 PHE   B N    1 
ATOM   6139 C CA   . PHE   B 1 132 ? 43.402 -29.692 6.403   1.00 14.57 ?  132 PHE   B CA   1 
ATOM   6140 C C    . PHE   B 1 132 ? 42.379 -30.786 6.723   1.00 15.59 ?  132 PHE   B C    1 
ATOM   6141 O O    . PHE   B 1 132 ? 41.460 -30.540 7.512   1.00 17.41 ?  132 PHE   B O    1 
ATOM   6142 C CB   . PHE   B 1 132 ? 42.727 -28.556 5.623   1.00 13.74 ?  132 PHE   B CB   1 
ATOM   6143 C CG   . PHE   B 1 132 ? 43.428 -27.213 5.733   1.00 13.67 ?  132 PHE   B CG   1 
ATOM   6144 C CD1  . PHE   B 1 132 ? 44.715 -27.026 5.239   1.00 14.85 ?  132 PHE   B CD1  1 
ATOM   6145 C CD2  . PHE   B 1 132 ? 42.763 -26.121 6.281   1.00 13.36 ?  132 PHE   B CD2  1 
ATOM   6146 C CE1  . PHE   B 1 132 ? 45.332 -25.787 5.329   1.00 15.49 ?  132 PHE   B CE1  1 
ATOM   6147 C CE2  . PHE   B 1 132 ? 43.375 -24.885 6.368   1.00 13.87 ?  132 PHE   B CE2  1 
ATOM   6148 C CZ   . PHE   B 1 132 ? 44.659 -24.724 5.896   1.00 15.00 ?  132 PHE   B CZ   1 
ATOM   6149 H H    . PHE   B 1 132 ? 44.516 -30.080 4.823   1.00 16.76 ?  132 PHE   B H    1 
ATOM   6150 H HA   . PHE   B 1 132 ? 43.708 -29.325 7.244   1.00 17.49 ?  132 PHE   B HA   1 
ATOM   6151 H HB2  . PHE   B 1 132 ? 42.708 -28.800 4.686   1.00 16.48 ?  132 PHE   B HB2  1 
ATOM   6152 H HB3  . PHE   B 1 132 ? 41.822 -28.447 5.954   1.00 16.48 ?  132 PHE   B HB3  1 
ATOM   6153 H HD1  . PHE   B 1 132 ? 45.173 -27.748 4.863   1.00 17.82 ?  132 PHE   B HD1  1 
ATOM   6154 H HD2  . PHE   B 1 132 ? 41.899 -26.239 6.606   1.00 16.03 ?  132 PHE   B HD2  1 
ATOM   6155 H HE1  . PHE   B 1 132 ? 46.196 -25.676 5.011   1.00 18.59 ?  132 PHE   B HE1  1 
ATOM   6156 H HE2  . PHE   B 1 132 ? 42.919 -24.172 6.753   1.00 16.65 ?  132 PHE   B HE2  1 
ATOM   6157 H HZ   . PHE   B 1 132 ? 45.069 -23.890 5.958   1.00 18.00 ?  132 PHE   B HZ   1 
ATOM   6158 N N    . GLY   B 1 133 ? 42.495 -31.978 6.127   1.00 15.18 ?  133 GLY   B N    1 
ATOM   6159 C CA   . GLY   B 1 133 ? 41.793 -33.151 6.610   1.00 16.19 ?  133 GLY   B CA   1 
ATOM   6160 C C    . GLY   B 1 133 ? 40.398 -33.412 6.073   1.00 16.66 ?  133 GLY   B C    1 
ATOM   6161 O O    . GLY   B 1 133 ? 39.817 -34.439 6.430   1.00 18.78 ?  133 GLY   B O    1 
ATOM   6162 H H    . GLY   B 1 133 ? 42.983 -32.124 5.433   1.00 18.22 ?  133 GLY   B H    1 
ATOM   6163 H HA2  . GLY   B 1 133 ? 42.332 -33.934 6.408   1.00 19.43 ?  133 GLY   B HA2  1 
ATOM   6164 H HA3  . GLY   B 1 133 ? 41.721 -33.090 7.574   1.00 19.43 ?  133 GLY   B HA3  1 
ATOM   6165 N N    . ALA   B 1 134 ? 39.835 -32.540 5.246   1.00 15.80 ?  134 ALA   B N    1 
ATOM   6166 C CA   . ALA   B 1 134 ? 38.513 -32.815 4.705   1.00 16.16 ?  134 ALA   B CA   1 
ATOM   6167 C C    . ALA   B 1 134 ? 38.607 -33.803 3.545   1.00 16.00 ?  134 ALA   B C    1 
ATOM   6168 O O    . ALA   B 1 134 ? 39.664 -33.985 2.932   1.00 17.01 ?  134 ALA   B O    1 
ATOM   6169 C CB   . ALA   B 1 134 ? 37.832 -31.525 4.246   1.00 16.70 ?  134 ALA   B CB   1 
ATOM   6170 H H    . ALA   B 1 134 ? 40.188 -31.797 4.991   1.00 18.96 ?  134 ALA   B H    1 
ATOM   6171 H HA   . ALA   B 1 134 ? 37.964 -33.214 5.398   1.00 19.39 ?  134 ALA   B HA   1 
ATOM   6172 H HB1  . ALA   B 1 134 ? 36.945 -31.737 3.914   1.00 20.04 ?  134 ALA   B HB1  1 
ATOM   6173 H HB2  . ALA   B 1 134 ? 37.764 -30.918 5.002   1.00 20.04 ?  134 ALA   B HB2  1 
ATOM   6174 H HB3  . ALA   B 1 134 ? 38.361 -31.119 3.544   1.00 20.04 ?  134 ALA   B HB3  1 
ATOM   6175 N N    . ASP   B 1 135 ? 37.479 -34.438 3.248   1.00 16.27 ?  135 ASP   B N    1 
ATOM   6176 C CA   . ASP   B 1 135 ? 37.389 -35.330 2.099   1.00 16.77 ?  135 ASP   B CA   1 
ATOM   6177 C C    . ASP   B 1 135 ? 37.487 -34.493 0.830   1.00 15.43 ?  135 ASP   B C    1 
ATOM   6178 O O    . ASP   B 1 135 ? 36.630 -33.623 0.607   1.00 15.41 ?  135 ASP   B O    1 
ATOM   6179 C CB   . ASP   B 1 135 ? 36.047 -36.057 2.145   1.00 18.47 ?  135 ASP   B CB   1 
ATOM   6180 C CG   . ASP   B 1 135 ? 35.866 -37.046 1.007   1.00 20.46 ?  135 ASP   B CG   1 
ATOM   6181 O OD1  . ASP   B 1 135 ? 36.732 -37.113 0.111   1.00 20.33 ?  135 ASP   B OD1  1 
ATOM   6182 O OD2  . ASP   B 1 135 ? 34.855 -37.785 1.024   1.00 23.60 -1 135 ASP   B OD2  1 
ATOM   6183 H H    . ASP   B 1 135 ? 36.743 -34.357 3.689   1.00 19.53 ?  135 ASP   B H    1 
ATOM   6184 H HA   . ASP   B 1 135 ? 38.109 -35.978 2.133   1.00 20.13 ?  135 ASP   B HA   1 
ATOM   6185 H HB2  . ASP   B 1 135 ? 35.990 -36.548 2.976   1.00 22.17 ?  135 ASP   B HB2  1 
ATOM   6186 H HB3  . ASP   B 1 135 ? 35.337 -35.403 2.088   1.00 22.17 ?  135 ASP   B HB3  1 
ATOM   6187 N N    . PRO   B 1 136 ? 38.501 -34.696 -0.016  1.00 15.75 ?  136 PRO   B N    1 
ATOM   6188 C CA   . PRO   B 1 136 ? 38.599 -33.874 -1.233  1.00 14.98 ?  136 PRO   B CA   1 
ATOM   6189 C C    . PRO   B 1 136 ? 37.408 -34.023 -2.156  1.00 14.34 ?  136 PRO   B C    1 
ATOM   6190 O O    . PRO   B 1 136 ? 37.083 -33.075 -2.877  1.00 13.60 ?  136 PRO   B O    1 
ATOM   6191 C CB   . PRO   B 1 136 ? 39.914 -34.340 -1.880  1.00 16.05 ?  136 PRO   B CB   1 
ATOM   6192 C CG   . PRO   B 1 136 ? 40.136 -35.714 -1.333  1.00 17.51 ?  136 PRO   B CG   1 
ATOM   6193 C CD   . PRO   B 1 136 ? 39.588 -35.685 0.066   1.00 16.91 ?  136 PRO   B CD   1 
ATOM   6194 H HA   . PRO   B 1 136 ? 38.690 -32.941 -0.995  1.00 17.98 ?  136 PRO   B HA   1 
ATOM   6195 H HB2  . PRO   B 1 136 ? 39.823 -34.368 -2.848  1.00 19.26 ?  136 PRO   B HB2  1 
ATOM   6196 H HB3  . PRO   B 1 136 ? 40.639 -33.748 -1.623  1.00 19.26 ?  136 PRO   B HB3  1 
ATOM   6197 H HG2  . PRO   B 1 136 ? 39.658 -36.361 -1.874  1.00 21.02 ?  136 PRO   B HG2  1 
ATOM   6198 H HG3  . PRO   B 1 136 ? 41.086 -35.913 -1.323  1.00 21.02 ?  136 PRO   B HG3  1 
ATOM   6199 H HD2  . PRO   B 1 136 ? 39.238 -36.557 0.309   1.00 20.30 ?  136 PRO   B HD2  1 
ATOM   6200 H HD3  . PRO   B 1 136 ? 40.267 -35.387 0.693   1.00 20.30 ?  136 PRO   B HD3  1 
ATOM   6201 N N    . ILE   B 1 137 ? 36.754 -35.189 -2.166  1.00 14.79 ?  137 ILE   B N    1 
ATOM   6202 C CA   . ILE   B 1 137 ? 35.540 -35.358 -2.961  1.00 15.40 ?  137 ILE   B CA   1 
ATOM   6203 C C    . ILE   B 1 137 ? 34.461 -34.390 -2.489  1.00 14.62 ?  137 ILE   B C    1 
ATOM   6204 O O    . ILE   B 1 137 ? 33.738 -33.789 -3.295  1.00 14.57 ?  137 ILE   B O    1 
ATOM   6205 C CB   . ILE   B 1 137 ? 35.069 -36.827 -2.894  1.00 17.58 ?  137 ILE   B CB   1 
ATOM   6206 C CG1  . ILE   B 1 137 ? 36.046 -37.737 -3.647  1.00 19.96 ?  137 ILE   B CG1  1 
ATOM   6207 C CG2  . ILE   B 1 137 ? 33.661 -36.973 -3.460  1.00 18.02 ?  137 ILE   B CG2  1 
ATOM   6208 C CD1  . ILE   B 1 137 ? 35.716 -39.216 -3.545  1.00 22.42 ?  137 ILE   B CD1  1 
ATOM   6209 H H    . ILE   B 1 137 ? 36.997 -35.889 -1.739  1.00 17.74 ?  137 ILE   B H    1 
ATOM   6210 H HA   . ILE   B 1 137 ? 35.733 -35.156 -3.892  1.00 18.48 ?  137 ILE   B HA   1 
ATOM   6211 H HB   . ILE   B 1 137 ? 35.051 -37.100 -1.968  1.00 21.09 ?  137 ILE   B HB   1 
ATOM   6212 H HG12 . ILE   B 1 137 ? 36.034 -37.502 -4.589  1.00 23.96 ?  137 ILE   B HG12 1 
ATOM   6213 H HG13 . ILE   B 1 137 ? 36.933 -37.611 -3.286  1.00 23.96 ?  137 ILE   B HG13 1 
ATOM   6214 H HG21 . ILE   B 1 137 ? 33.431 -37.915 -3.522  1.00 21.62 ?  137 ILE   B HG21 1 
ATOM   6215 H HG22 . ILE   B 1 137 ? 33.030 -36.532 -2.871  1.00 21.62 ?  137 ILE   B HG22 1 
ATOM   6216 H HG23 . ILE   B 1 137 ? 33.628 -36.572 -4.342  1.00 21.62 ?  137 ILE   B HG23 1 
ATOM   6217 H HD11 . ILE   B 1 137 ? 36.458 -39.724 -3.906  1.00 26.91 ?  137 ILE   B HD11 1 
ATOM   6218 H HD12 . ILE   B 1 137 ? 35.576 -39.449 -2.614  1.00 26.91 ?  137 ILE   B HD12 1 
ATOM   6219 H HD13 . ILE   B 1 137 ? 34.913 -39.406 -4.058  1.00 26.91 ?  137 ILE   B HD13 1 
ATOM   6220 N N    . HIS   B 1 138 ? 34.325 -34.242 -1.174  1.00 14.84 ?  138 HIS   B N    1 
ATOM   6221 C CA   . HIS   B 1 138 ? 33.377 -33.277 -0.634  1.00 15.01 ?  138 HIS   B CA   1 
ATOM   6222 C C    . HIS   B 1 138 ? 33.792 -31.851 -0.955  1.00 14.62 ?  138 HIS   B C    1 
ATOM   6223 O O    . HIS   B 1 138 ? 32.945 -31.008 -1.267  1.00 15.06 ?  138 HIS   B O    1 
ATOM   6224 C CB   . HIS   B 1 138 ? 33.262 -33.451 0.874   1.00 16.32 ?  138 HIS   B CB   1 
ATOM   6225 C CG   . HIS   B 1 138 ? 32.327 -32.475 1.509   1.00 17.56 ?  138 HIS   B CG   1 
ATOM   6226 N ND1  . HIS   B 1 138 ? 30.986 -32.422 1.198   1.00 18.75 ?  138 HIS   B ND1  1 
ATOM   6227 C CD2  . HIS   B 1 138 ? 32.544 -31.482 2.404   1.00 17.84 ?  138 HIS   B CD2  1 
ATOM   6228 C CE1  . HIS   B 1 138 ? 30.411 -31.460 1.896   1.00 18.95 ?  138 HIS   B CE1  1 
ATOM   6229 N NE2  . HIS   B 1 138 ? 31.335 -30.872 2.635   1.00 18.27 ?  138 HIS   B NE2  1 
ATOM   6230 H H    . HIS   B 1 138 ? 34.763 -34.684 -0.586  1.00 17.81 ?  138 HIS   B H    1 
ATOM   6231 H HA   . HIS   B 1 138 ? 32.502 -33.438 -1.026  1.00 18.01 ?  138 HIS   B HA   1 
ATOM   6232 H HB2  . HIS   B 1 138 ? 32.935 -34.341 1.065   1.00 19.58 ?  138 HIS   B HB2  1 
ATOM   6233 H HB3  . HIS   B 1 138 ? 34.138 -33.324 1.270   1.00 19.58 ?  138 HIS   B HB3  1 
ATOM   6234 H HD1  . HIS   B 1 138 ? 30.583 -32.948 0.649   1.00 22.50 ?  138 HIS   B HD1  1 
ATOM   6235 H HD2  . HIS   B 1 138 ? 33.351 -31.261 2.804   1.00 21.41 ?  138 HIS   B HD2  1 
ATOM   6236 H HE1  . HIS   B 1 138 ? 29.505 -31.237 1.871   1.00 22.75 ?  138 HIS   B HE1  1 
ATOM   6237 N N    . SER   B 1 139 ? 35.082 -31.550 -0.861  1.00 14.08 ?  139 SER   B N    1 
ATOM   6238 C CA   . SER   B 1 139 ? 35.525 -30.203 -1.185  1.00 13.30 ?  139 SER   B CA   1 
ATOM   6239 C C    . SER   B 1 139 ? 35.190 -29.848 -2.626  1.00 12.41 ?  139 SER   B C    1 
ATOM   6240 O O    . SER   B 1 139 ? 34.746 -28.728 -2.906  1.00 12.63 ?  139 SER   B O    1 
ATOM   6241 C CB   . SER   B 1 139 ? 37.018 -30.063 -0.912  1.00 13.53 ?  139 SER   B CB   1 
ATOM   6242 O OG   . SER   B 1 139 ? 37.436 -28.738 -1.179  1.00 13.86 ?  139 SER   B OG   1 
ATOM   6243 H H    . SER   B 1 139 ? 35.701 -32.088 -0.630  1.00 16.89 ?  139 SER   B H    1 
ATOM   6244 H HA   . SER   B 1 139 ? 35.053 -29.573 -0.621  1.00 15.95 ?  139 SER   B HA   1 
ATOM   6245 H HB2  . SER   B 1 139 ? 37.188 -30.259 0.019   1.00 16.23 ?  139 SER   B HB2  1 
ATOM   6246 H HB3  . SER   B 1 139 ? 37.507 -30.672 -1.483  1.00 16.23 ?  139 SER   B HB3  1 
ATOM   6247 H HG   . SER   B 1 139 ? 38.265 -28.660 -1.033  1.00 16.63 ?  139 SER   B HG   1 
ATOM   6248 N N    . LEU   B 1 140 ? 35.390 -30.788 -3.554  1.00 12.16 ?  140 LEU   B N    1 
ATOM   6249 C CA   . LEU   B 1 140 ? 35.024 -30.543 -4.942  1.00 12.36 ?  140 LEU   B CA   1 
ATOM   6250 C C    . LEU   B 1 140 ? 33.524 -30.318 -5.077  1.00 12.63 ?  140 LEU   B C    1 
ATOM   6251 O O    . LEU   B 1 140 ? 33.094 -29.431 -5.818  1.00 12.86 ?  140 LEU   B O    1 
ATOM   6252 C CB   . LEU   B 1 140 ? 35.485 -31.703 -5.824  1.00 12.64 ?  140 LEU   B CB   1 
ATOM   6253 C CG   . LEU   B 1 140 ? 35.138 -31.591 -7.303  1.00 12.82 ?  140 LEU   B CG   1 
ATOM   6254 C CD1  . LEU   B 1 140 ? 35.701 -30.314 -7.912  1.00 13.98 ?  140 LEU   B CD1  1 
ATOM   6255 C CD2  . LEU   B 1 140 ? 35.635 -32.817 -8.049  1.00 13.60 ?  140 LEU   B CD2  1 
ATOM   6256 H H    . LEU   B 1 140 ? 35.733 -31.563 -3.412  1.00 14.59 ?  140 LEU   B H    1 
ATOM   6257 H HA   . LEU   B 1 140 ? 35.477 -29.739 -5.254  1.00 14.83 ?  140 LEU   B HA   1 
ATOM   6258 H HB2  . LEU   B 1 140 ? 36.450 -31.777 -5.760  1.00 15.16 ?  140 LEU   B HB2  1 
ATOM   6259 H HB3  . LEU   B 1 140 ? 35.074 -32.518 -5.498  1.00 15.16 ?  140 LEU   B HB3  1 
ATOM   6260 H HG   . LEU   B 1 140 ? 34.175 -31.557 -7.401  1.00 15.39 ?  140 LEU   B HG   1 
ATOM   6261 H HD11 . LEU   B 1 140 ? 35.564 -30.339 -8.873  1.00 16.78 ?  140 LEU   B HD11 1 
ATOM   6262 H HD12 . LEU   B 1 140 ? 35.231 -29.552 -7.535  1.00 16.78 ?  140 LEU   B HD12 1 
ATOM   6263 H HD13 . LEU   B 1 140 ? 36.644 -30.258 -7.712  1.00 16.78 ?  140 LEU   B HD13 1 
ATOM   6264 H HD21 . LEU   B 1 140 ? 35.406 -32.727 -8.989  1.00 16.32 ?  140 LEU   B HD21 1 
ATOM   6265 H HD22 . LEU   B 1 140 ? 36.595 -32.880 -7.947  1.00 16.32 ?  140 LEU   B HD22 1 
ATOM   6266 H HD23 . LEU   B 1 140 ? 35.205 -33.601 -7.678  1.00 16.32 ?  140 LEU   B HD23 1 
ATOM   6267 N N    . ARG   B 1 141 ? 32.718 -31.108 -4.363  1.00 13.15 ?  141 ARG   B N    1 
ATOM   6268 C CA   . ARG   B 1 141 ? 31.268 -30.929 -4.354  1.00 14.27 ?  141 ARG   B CA   1 
ATOM   6269 C C    . ARG   B 1 141 ? 30.891 -29.515 -3.928  1.00 13.68 ?  141 ARG   B C    1 
ATOM   6270 O O    . ARG   B 1 141 ? 30.091 -28.839 -4.590  1.00 13.70 ?  141 ARG   B O    1 
ATOM   6271 C CB   . ARG   B 1 141 ? 30.666 -31.958 -3.387  1.00 15.99 ?  141 ARG   B CB   1 
ATOM   6272 C CG   . ARG   B 1 141 ? 29.204 -31.816 -3.038  1.00 18.45 ?  141 ARG   B CG   1 
ATOM   6273 C CD   . ARG   B 1 141 ? 28.380 -32.449 -4.082  1.00 20.37 ?  141 ARG   B CD   1 
ATOM   6274 N NE   . ARG   B 1 141 ? 28.120 -31.543 -5.188  1.00 21.28 ?  141 ARG   B NE   1 
ATOM   6275 C CZ   . ARG   B 1 141 ? 28.134 -31.888 -6.467  1.00 20.75 ?  141 ARG   B CZ   1 
ATOM   6276 N NH1  . ARG   B 1 141 ? 28.584 -33.067 -6.861  1.00 20.94 ?  141 ARG   B NH1  1 
ATOM   6277 N NH2  . ARG   B 1 141 ? 27.695 -31.019 -7.376  1.00 22.04 ?  141 ARG   B NH2  1 
ATOM   6278 H H    . ARG   B 1 141 ? 32.993 -31.750 -3.868  1.00 15.78 ?  141 ARG   B H    1 
ATOM   6279 H HA   . ARG   B 1 141 ? 30.912 -31.084 -5.237  1.00 17.12 ?  141 ARG   B HA   1 
ATOM   6280 H HB2  . ARG   B 1 141 ? 30.793 -32.839 -3.772  1.00 19.19 ?  141 ARG   B HB2  1 
ATOM   6281 H HB3  . ARG   B 1 141 ? 31.158 -31.911 -2.553  1.00 19.19 ?  141 ARG   B HB3  1 
ATOM   6282 H HG2  . ARG   B 1 141 ? 29.032 -32.253 -2.193  1.00 22.14 ?  141 ARG   B HG2  1 
ATOM   6283 H HG3  . ARG   B 1 141 ? 28.961 -30.872 -2.979  1.00 22.14 ?  141 ARG   B HG3  1 
ATOM   6284 H HD2  . ARG   B 1 141 ? 28.840 -33.237 -4.420  1.00 24.45 ?  141 ARG   B HD2  1 
ATOM   6285 H HD3  . ARG   B 1 141 ? 27.535 -32.710 -3.695  1.00 24.45 ?  141 ARG   B HD3  1 
ATOM   6286 H HE   . ARG   B 1 141 ? 27.926 -30.724 -4.995  1.00 25.53 ?  141 ARG   B HE   1 
ATOM   6287 H HH11 . ARG   B 1 141 ? 28.858 -33.642 -6.288  1.00 25.13 ?  141 ARG   B HH11 1 
ATOM   6288 H HH12 . ARG   B 1 141 ? 28.588 -33.260 -7.698  1.00 25.13 ?  141 ARG   B HH12 1 
ATOM   6289 H HH21 . ARG   B 1 141 ? 27.405 -30.246 -7.133  1.00 26.45 ?  141 ARG   B HH21 1 
ATOM   6290 H HH22 . ARG   B 1 141 ? 27.716 -31.224 -8.213  1.00 26.45 ?  141 ARG   B HH22 1 
ATOM   6291 N N    . VAL   B 1 142 ? 31.430 -29.071 -2.795  1.00 13.14 ?  142 VAL   B N    1 
ATOM   6292 C CA   . VAL   B 1 142 ? 31.099 -27.737 -2.310  1.00 13.26 ?  142 VAL   B CA   1 
ATOM   6293 C C    . VAL   B 1 142 ? 31.578 -26.681 -3.298  1.00 13.12 ?  142 VAL   B C    1 
ATOM   6294 O O    . VAL   B 1 142 ? 30.880 -25.693 -3.557  1.00 13.76 ?  142 VAL   B O    1 
ATOM   6295 C CB   . VAL   B 1 142 ? 31.641 -27.510 -0.886  1.00 13.49 ?  142 VAL   B CB   1 
ATOM   6296 C CG1  . VAL   B 1 142 ? 31.319 -26.091 -0.405  1.00 14.03 ?  142 VAL   B CG1  1 
ATOM   6297 C CG2  . VAL   B 1 142 ? 31.063 -28.535 0.075   1.00 14.38 ?  142 VAL   B CG2  1 
ATOM   6298 H H    . VAL   B 1 142 ? 31.980 -29.501 -2.299  1.00 15.77 ?  142 VAL   B H    1 
ATOM   6299 H HA   . VAL   B 1 142 ? 30.136 -27.654 -2.258  1.00 15.91 ?  142 VAL   B HA   1 
ATOM   6300 H HB   . VAL   B 1 142 ? 32.606 -27.611 -0.888  1.00 16.18 ?  142 VAL   B HB   1 
ATOM   6301 H HG11 . VAL   B 1 142 ? 31.503 -26.031 0.546   1.00 16.84 ?  142 VAL   B HG11 1 
ATOM   6302 H HG12 . VAL   B 1 142 ? 31.870 -25.458 -0.888  1.00 16.84 ?  142 VAL   B HG12 1 
ATOM   6303 H HG13 . VAL   B 1 142 ? 30.380 -25.910 -0.569  1.00 16.84 ?  142 VAL   B HG13 1 
ATOM   6304 H HG21 . VAL   B 1 142 ? 31.381 -28.346 0.970   1.00 17.25 ?  142 VAL   B HG21 1 
ATOM   6305 H HG22 . VAL   B 1 142 ? 30.095 -28.479 0.047   1.00 17.25 ?  142 VAL   B HG22 1 
ATOM   6306 H HG23 . VAL   B 1 142 ? 31.351 -29.420 -0.201  1.00 17.25 ?  142 VAL   B HG23 1 
ATOM   6307 N N    . CYS   B 1 143 ? 32.757 -26.882 -3.882  1.00 12.66 ?  143 CYS   B N    1 
ATOM   6308 C CA   . CYS   B 1 143 ? 33.258 -25.942 -4.881  1.00 12.73 ?  143 CYS   B CA   1 
ATOM   6309 C C    . CYS   B 1 143 ? 32.259 -25.794 -6.023  1.00 12.73 ?  143 CYS   B C    1 
ATOM   6310 O O    . CYS   B 1 143 ? 31.853 -24.681 -6.374  1.00 12.83 ?  143 CYS   B O    1 
ATOM   6311 C CB   . CYS   B 1 143 ? 34.615 -26.424 -5.401  1.00 12.76 ?  143 CYS   B CB   1 
ATOM   6312 S SG   . CYS   B 1 143 ? 35.371 -25.326 -6.614  1.00 13.03 ?  143 CYS   B SG   1 
ATOM   6313 H H    . CYS   B 1 143 ? 33.287 -27.537 -3.715  1.00 15.19 ?  143 CYS   B H    1 
ATOM   6314 H HA   . CYS   B 1 143 ? 33.383 -25.068 -4.476  1.00 15.28 ?  143 CYS   B HA   1 
ATOM   6315 H HB2  . CYS   B 1 143 ? 35.229 -26.497 -4.655  1.00 15.31 ?  143 CYS   B HB2  1 
ATOM   6316 H HB3  . CYS   B 1 143 ? 34.499 -27.285 -5.817  1.00 15.31 ?  143 CYS   B HB3  1 
ATOM   6317 H HG   . CYS   B 1 143 ? 36.442 -25.762 -6.934  1.00 15.64 ?  143 CYS   B HG   1 
ATOM   6318 N N    . VAL   B 1 144 ? 31.851 -26.913 -6.616  1.00 13.04 ?  144 VAL   B N    1 
ATOM   6319 C CA   . VAL   B 1 144 ? 30.954 -26.846 -7.764  1.00 14.06 ?  144 VAL   B CA   1 
ATOM   6320 C C    . VAL   B 1 144 ? 29.611 -26.236 -7.392  1.00 14.15 ?  144 VAL   B C    1 
ATOM   6321 O O    . VAL   B 1 144 ? 28.988 -25.537 -8.206  1.00 15.54 ?  144 VAL   B O    1 
ATOM   6322 C CB   . VAL   B 1 144 ? 30.796 -28.250 -8.355  1.00 16.76 ?  144 VAL   B CB   1 
ATOM   6323 C CG1  . VAL   B 1 144 ? 29.524 -28.372 -9.202  1.00 19.43 ?  144 VAL   B CG1  1 
ATOM   6324 C CG2  . VAL   B 1 144 ? 32.049 -28.644 -9.137  1.00 16.97 ?  144 VAL   B CG2  1 
ATOM   6325 H H    . VAL   B 1 144 ? 32.073 -27.712 -6.377  1.00 15.65 ?  144 VAL   B H    1 
ATOM   6326 H HA   . VAL   B 1 144 ? 31.349 -26.291 -8.447  1.00 16.88 ?  144 VAL   B HA   1 
ATOM   6327 H HB   . VAL   B 1 144 ? 30.707 -28.888 -7.626  1.00 20.12 ?  144 VAL   B HB   1 
ATOM   6328 H HG11 . VAL   B 1 144 ? 29.606 -29.150 -9.785  1.00 23.32 ?  144 VAL   B HG11 1 
ATOM   6329 H HG12 . VAL   B 1 144 ? 28.761 -28.491 -8.615  1.00 23.32 ?  144 VAL   B HG12 1 
ATOM   6330 H HG13 . VAL   B 1 144 ? 29.419 -27.575 -9.738  1.00 23.32 ?  144 VAL   B HG13 1 
ATOM   6331 H HG21 . VAL   B 1 144 ? 31.927 -29.539 -9.499  1.00 20.36 ?  144 VAL   B HG21 1 
ATOM   6332 H HG22 . VAL   B 1 144 ? 32.173 -28.012 -9.862  1.00 20.36 ?  144 VAL   B HG22 1 
ATOM   6333 H HG23 . VAL   B 1 144 ? 32.806 -28.627 -8.541  1.00 20.36 ?  144 VAL   B HG23 1 
ATOM   6334 N N    . ASP   B 1 145 ? 29.145 -26.477 -6.170  1.00 14.13 ?  145 ASP   B N    1 
ATOM   6335 C CA   . ASP   B 1 145 ? 27.836 -26.009 -5.738  1.00 15.01 ?  145 ASP   B CA   1 
ATOM   6336 C C    . ASP   B 1 145 ? 27.860 -24.587 -5.190  1.00 14.69 ?  145 ASP   B C    1 
ATOM   6337 O O    . ASP   B 1 145 ? 26.795 -24.053 -4.855  1.00 16.47 ?  145 ASP   B O    1 
ATOM   6338 C CB   . ASP   B 1 145 ? 27.264 -26.940 -4.660  1.00 16.70 ?  145 ASP   B CB   1 
ATOM   6339 C CG   . ASP   B 1 145 ? 26.881 -28.310 -5.190  1.00 18.35 ?  145 ASP   B CG   1 
ATOM   6340 O OD1  . ASP   B 1 145 ? 26.794 -28.488 -6.420  1.00 18.78 ?  145 ASP   B OD1  1 
ATOM   6341 O OD2  . ASP   B 1 145 ? 26.680 -29.211 -4.353  1.00 20.36 -1 145 ASP   B OD2  1 
ATOM   6342 H H    . ASP   B 1 145 ? 29.584 -26.899 -5.569  1.00 16.96 ?  145 ASP   B H    1 
ATOM   6343 H HA   . ASP   B 1 145 ? 27.238 -26.006 -6.494  1.00 18.01 ?  145 ASP   B HA   1 
ATOM   6344 H HB2  . ASP   B 1 145 ? 27.928 -27.078 -3.977  1.00 20.04 ?  145 ASP   B HB2  1 
ATOM   6345 H HB3  . ASP   B 1 145 ? 26.471 -26.527 -4.285  1.00 20.04 ?  145 ASP   B HB3  1 
ATOM   6346 N N    . THR   B 1 146 ? 29.036 -23.973 -5.073  1.00 13.03 ?  146 THR   B N    1 
ATOM   6347 C CA   . THR   B 1 146 ? 29.164 -22.656 -4.463  1.00 12.80 ?  146 THR   B CA   1 
ATOM   6348 C C    . THR   B 1 146 ? 29.798 -21.627 -5.380  1.00 12.37 ?  146 THR   B C    1 
ATOM   6349 O O    . THR   B 1 146 ? 29.347 -20.468 -5.421  1.00 13.05 ?  146 THR   B O    1 
ATOM   6350 C CB   . THR   B 1 146 ? 30.002 -22.763 -3.181  1.00 12.88 ?  146 THR   B CB   1 
ATOM   6351 O OG1  . THR   B 1 146 ? 29.432 -23.756 -2.322  1.00 13.25 ?  146 THR   B OG1  1 
ATOM   6352 C CG2  . THR   B 1 146 ? 30.054 -21.440 -2.458  1.00 13.31 ?  146 THR   B CG2  1 
ATOM   6353 H H    . THR   B 1 146 ? 29.788 -24.303 -5.339  1.00 15.64 ?  146 THR   B H    1 
ATOM   6354 H HA   . THR   B 1 146 ? 28.290 -22.330 -4.218  1.00 15.36 ?  146 THR   B HA   1 
ATOM   6355 H HB   . THR   B 1 146 ? 30.912 -23.010 -3.405  1.00 15.46 ?  146 THR   B HB   1 
ATOM   6356 H HG1  . THR   B 1 146 ? 29.467 -24.512 -2.701  1.00 15.90 ?  146 THR   B HG1  1 
ATOM   6357 H HG21 . THR   B 1 146 ? 30.399 -21.561 -1.562  1.00 15.98 ?  146 THR   B HG21 1 
ATOM   6358 H HG22 . THR   B 1 146 ? 30.630 -20.818 -2.934  1.00 15.98 ?  146 THR   B HG22 1 
ATOM   6359 H HG23 . THR   B 1 146 ? 29.162 -21.057 -2.401  1.00 15.98 ?  146 THR   B HG23 1 
ATOM   6360 N N    . VAL   B 1 147 ? 30.868 -22.001 -6.081  1.00 12.15 ?  147 VAL   B N    1 
ATOM   6361 C CA   . VAL   B 1 147 ? 31.596 -21.053 -6.913  1.00 12.24 ?  147 VAL   B CA   1 
ATOM   6362 C C    . VAL   B 1 147 ? 30.874 -20.917 -8.242  1.00 12.20 ?  147 VAL   B C    1 
ATOM   6363 O O    . VAL   B 1 147 ? 30.510 -21.919 -8.875  1.00 12.98 ?  147 VAL   B O    1 
ATOM   6364 C CB   . VAL   B 1 147 ? 33.052 -21.508 -7.106  1.00 12.01 ?  147 VAL   B CB   1 
ATOM   6365 C CG1  . VAL   B 1 147 ? 33.822 -20.486 -7.926  1.00 12.16 ?  147 VAL   B CG1  1 
ATOM   6366 C CG2  . VAL   B 1 147 ? 33.718 -21.718 -5.758  1.00 12.43 ?  147 VAL   B CG2  1 
ATOM   6367 H H    . VAL   B 1 147 ? 31.192 -22.801 -6.092  1.00 14.58 ?  147 VAL   B H    1 
ATOM   6368 H HA   . VAL   B 1 147 ? 31.606 -20.188 -6.476  1.00 14.69 ?  147 VAL   B HA   1 
ATOM   6369 H HB   . VAL   B 1 147 ? 33.065 -22.352 -7.586  1.00 14.41 ?  147 VAL   B HB   1 
ATOM   6370 H HG11 . VAL   B 1 147 ? 34.765 -20.718 -7.916  1.00 14.59 ?  147 VAL   B HG11 1 
ATOM   6371 H HG12 . VAL   B 1 147 ? 33.492 -20.492 -8.837  1.00 14.59 ?  147 VAL   B HG12 1 
ATOM   6372 H HG13 . VAL   B 1 147 ? 33.698 -19.607 -7.533  1.00 14.59 ?  147 VAL   B HG13 1 
ATOM   6373 H HG21 . VAL   B 1 147 ? 34.660 -21.904 -5.896  1.00 14.92 ?  147 VAL   B HG21 1 
ATOM   6374 H HG22 . VAL   B 1 147 ? 33.610 -20.918 -5.225  1.00 14.92 ?  147 VAL   B HG22 1 
ATOM   6375 H HG23 . VAL   B 1 147 ? 33.296 -22.473 -5.312  1.00 14.92 ?  147 VAL   B HG23 1 
ATOM   6376 N N    . ARG   B 1 148 ? 30.670 -19.665 -8.663  1.00 12.03 ?  148 ARG   B N    1 
ATOM   6377 C CA   . ARG   B 1 148 ? 30.049 -19.337 -9.935  1.00 12.65 ?  148 ARG   B CA   1 
ATOM   6378 C C    . ARG   B 1 148 ? 31.010 -18.660 -10.897 1.00 12.91 ?  148 ARG   B C    1 
ATOM   6379 O O    . ARG   B 1 148 ? 30.741 -18.642 -12.100 1.00 14.21 ?  148 ARG   B O    1 
ATOM   6380 C CB   . ARG   B 1 148 ? 28.816 -18.447 -9.714  1.00 13.37 ?  148 ARG   B CB   1 
ATOM   6381 C CG   . ARG   B 1 148 ? 27.738 -19.153 -8.909  1.00 13.71 ?  148 ARG   B CG   1 
ATOM   6382 C CD   . ARG   B 1 148 ? 26.539 -18.275 -8.600  1.00 14.77 ?  148 ARG   B CD   1 
ATOM   6383 N NE   . ARG   B 1 148 ? 26.919 -17.072 -7.868  1.00 14.72 ?  148 ARG   B NE   1 
ATOM   6384 C CZ   . ARG   B 1 148 ? 27.215 -17.039 -6.574  1.00 13.78 ?  148 ARG   B CZ   1 
ATOM   6385 N NH1  . ARG   B 1 148 ? 27.159 -18.127 -5.820  1.00 13.86 ?  148 ARG   B NH1  1 
ATOM   6386 N NH2  . ARG   B 1 148 ? 27.592 -15.887 -6.025  1.00 14.03 ?  148 ARG   B NH2  1 
ATOM   6387 H H    . ARG   B 1 148 ? 30.903 -18.969 -8.206  1.00 14.44 ?  148 ARG   B H    1 
ATOM   6388 H HA   . ARG   B 1 148 ? 29.750 -20.159 -10.350 1.00 15.18 ?  148 ARG   B HA   1 
ATOM   6389 H HB2  . ARG   B 1 148 ? 29.084 -17.651 -9.230  1.00 16.05 ?  148 ARG   B HB2  1 
ATOM   6390 H HB3  . ARG   B 1 148 ? 28.445 -18.206 -10.577 1.00 16.05 ?  148 ARG   B HB3  1 
ATOM   6391 H HG2  . ARG   B 1 148 ? 27.424 -19.922 -9.417  1.00 16.45 ?  148 ARG   B HG2  1 
ATOM   6392 H HG3  . ARG   B 1 148 ? 28.118 -19.452 -8.068  1.00 16.45 ?  148 ARG   B HG3  1 
ATOM   6393 H HD2  . ARG   B 1 148 ? 26.124 -18.006 -9.431  1.00 17.72 ?  148 ARG   B HD2  1 
ATOM   6394 H HD3  . ARG   B 1 148 ? 25.912 -18.780 -8.059  1.00 17.72 ?  148 ARG   B HD3  1 
ATOM   6395 H HE   . ARG   B 1 148 ? 26.963 -16.339 -8.303  1.00 17.67 ?  148 ARG   B HE   1 
ATOM   6396 H HH11 . ARG   B 1 148 ? 26.916 -18.882 -6.157  1.00 16.64 ?  148 ARG   B HH11 1 
ATOM   6397 H HH12 . ARG   B 1 148 ? 27.349 -18.082 -4.979  1.00 16.64 ?  148 ARG   B HH12 1 
ATOM   6398 H HH21 . ARG   B 1 148 ? 27.632 -15.179 -6.507  1.00 16.84 ?  148 ARG   B HH21 1 
ATOM   6399 H HH22 . ARG   B 1 148 ? 27.781 -15.851 -5.187  1.00 16.84 ?  148 ARG   B HH22 1 
ATOM   6400 N N    . THR   B 1 149 ? 32.114 -18.114 -10.398 1.00 12.38 ?  149 THR   B N    1 
ATOM   6401 C CA   . THR   B 1 149 ? 33.161 -17.563 -11.242 1.00 12.38 ?  149 THR   B CA   1 
ATOM   6402 C C    . THR   B 1 149 ? 34.053 -18.697 -11.749 1.00 12.17 ?  149 THR   B C    1 
ATOM   6403 O O    . THR   B 1 149 ? 33.860 -19.867 -11.411 1.00 12.75 ?  149 THR   B O    1 
ATOM   6404 C CB   . THR   B 1 149 ? 33.935 -16.515 -10.458 1.00 12.52 ?  149 THR   B CB   1 
ATOM   6405 O OG1  . THR   B 1 149 ? 34.381 -17.121 -9.241  1.00 12.67 ?  149 THR   B OG1  1 
ATOM   6406 C CG2  . THR   B 1 149 ? 33.054 -15.305 -10.163 1.00 13.53 ?  149 THR   B CG2  1 
ATOM   6407 H H    . THR   B 1 149 ? 32.276 -18.046 -9.557  1.00 14.86 ?  149 THR   B H    1 
ATOM   6408 H HA   . THR   B 1 149 ? 32.756 -17.128 -12.009 1.00 14.86 ?  149 THR   B HA   1 
ATOM   6409 H HB   . THR   B 1 149 ? 34.701 -16.231 -10.976 1.00 15.03 ?  149 THR   B HB   1 
ATOM   6410 H HG1  . THR   B 1 149 ? 34.814 -16.556 -8.782  1.00 15.20 ?  149 THR   B HG1  1 
ATOM   6411 H HG21 . THR   B 1 149 ? 33.564 -14.637 -9.678  1.00 16.24 ?  149 THR   B HG21 1 
ATOM   6412 H HG22 . THR   B 1 149 ? 32.740 -14.914 -10.996 1.00 16.24 ?  149 THR   B HG22 1 
ATOM   6413 H HG23 . THR   B 1 149 ? 32.290 -15.567 -9.631  1.00 16.24 ?  149 THR   B HG23 1 
ATOM   6414 N N    . ASN   B 1 150 ? 35.012 -18.375 -12.605 1.00 12.21 ?  150 ASN   B N    1 
ATOM   6415 C CA   . ASN   B 1 150 ? 35.782 -19.400 -13.300 1.00 12.81 ?  150 ASN   B CA   1 
ATOM   6416 C C    . ASN   B 1 150 ? 36.942 -19.851 -12.424 1.00 12.43 ?  150 ASN   B C    1 
ATOM   6417 O O    . ASN   B 1 150 ? 37.872 -19.083 -12.166 1.00 13.34 ?  150 ASN   B O    1 
ATOM   6418 C CB   . ASN   B 1 150 ? 36.270 -18.862 -14.637 1.00 14.38 ?  150 ASN   B CB   1 
ATOM   6419 C CG   . ASN   B 1 150 ? 35.141 -18.639 -15.595 1.00 17.21 ?  150 ASN   B CG   1 
ATOM   6420 O OD1  . ASN   B 1 150 ? 34.229 -19.455 -15.677 1.00 18.42 ?  150 ASN   B OD1  1 
ATOM   6421 N ND2  . ASN   B 1 150 ? 35.165 -17.515 -16.298 1.00 19.14 ?  150 ASN   B ND2  1 
ATOM   6422 H H    . ASN   B 1 150 ? 35.241 -17.566 -12.798 1.00 14.65 ?  150 ASN   B H    1 
ATOM   6423 H HA   . ASN   B 1 150 ? 35.204 -20.165 -13.472 1.00 15.38 ?  150 ASN   B HA   1 
ATOM   6424 H HB2  . ASN   B 1 150 ? 36.718 -18.015 -14.494 1.00 17.26 ?  150 ASN   B HB2  1 
ATOM   6425 H HB3  . ASN   B 1 150 ? 36.880 -19.503 -15.033 1.00 17.26 ?  150 ASN   B HB3  1 
ATOM   6426 H HD21 . ASN   B 1 150 ? 34.540 -17.340 -16.866 1.00 22.97 ?  150 ASN   B HD21 1 
ATOM   6427 H HD22 . ASN   B 1 150 ? 35.822 -16.962 -16.208 1.00 22.97 ?  150 ASN   B HD22 1 
ATOM   6428 N N    . VAL   B 1 151 ? 36.896 -21.103 -11.978 1.00 11.96 ?  151 VAL   B N    1 
ATOM   6429 C CA   . VAL   B 1 151 ? 37.909 -21.637 -11.083 1.00 11.75 ?  151 VAL   B CA   1 
ATOM   6430 C C    . VAL   B 1 151 ? 38.617 -22.805 -11.760 1.00 11.82 ?  151 VAL   B C    1 
ATOM   6431 O O    . VAL   B 1 151 ? 37.976 -23.731 -12.277 1.00 12.79 ?  151 VAL   B O    1 
ATOM   6432 C CB   . VAL   B 1 151 ? 37.349 -21.968 -9.685  1.00 13.27 ?  151 VAL   B CB   1 
ATOM   6433 C CG1  . VAL   B 1 151 ? 36.196 -22.965 -9.764  1.00 14.26 ?  151 VAL   B CG1  1 
ATOM   6434 C CG2  . VAL   B 1 151 ? 38.461 -22.460 -8.763  1.00 13.57 ?  151 VAL   B CG2  1 
ATOM   6435 H H    . VAL   B 1 151 ? 36.275 -21.669 -12.178 1.00 14.35 ?  151 VAL   B H    1 
ATOM   6436 H HA   . VAL   B 1 151 ? 38.579 -20.944 -10.951 1.00 14.10 ?  151 VAL   B HA   1 
ATOM   6437 H HB   . VAL   B 1 151 ? 37.000 -21.150 -9.296  1.00 15.93 ?  151 VAL   B HB   1 
ATOM   6438 H HG11 . VAL   B 1 151 ? 35.877 -23.153 -8.866  1.00 17.11 ?  151 VAL   B HG11 1 
ATOM   6439 H HG12 . VAL   B 1 151 ? 35.482 -22.584 -10.296 1.00 17.11 ?  151 VAL   B HG12 1 
ATOM   6440 H HG13 . VAL   B 1 151 ? 36.514 -23.786 -10.176 1.00 17.11 ?  151 VAL   B HG13 1 
ATOM   6441 H HG21 . VAL   B 1 151 ? 38.110 -22.540 -7.860  1.00 16.28 ?  151 VAL   B HG21 1 
ATOM   6442 H HG22 . VAL   B 1 151 ? 38.778 -23.320 -9.071  1.00 16.28 ?  151 VAL   B HG22 1 
ATOM   6443 H HG23 . VAL   B 1 151 ? 39.191 -21.815 -8.770  1.00 16.28 ?  151 VAL   B HG23 1 
ATOM   6444 N N    . TYR   B 1 152 ? 39.947 -22.720 -11.775 1.00 11.35 ?  152 TYR   B N    1 
ATOM   6445 C CA   . TYR   B 1 152 ? 40.849 -23.707 -12.352 1.00 11.37 ?  152 TYR   B CA   1 
ATOM   6446 C C    . TYR   B 1 152 ? 41.567 -24.384 -11.194 1.00 10.81 ?  152 TYR   B C    1 
ATOM   6447 O O    . TYR   B 1 152 ? 42.416 -23.770 -10.540 1.00 11.62 ?  152 TYR   B O    1 
ATOM   6448 C CB   . TYR   B 1 152 ? 41.826 -23.008 -13.298 1.00 12.18 ?  152 TYR   B CB   1 
ATOM   6449 C CG   . TYR   B 1 152 ? 41.153 -22.533 -14.560 1.00 12.77 ?  152 TYR   B CG   1 
ATOM   6450 C CD1  . TYR   B 1 152 ? 40.491 -21.306 -14.620 1.00 13.48 ?  152 TYR   B CD1  1 
ATOM   6451 C CD2  . TYR   B 1 152 ? 41.156 -23.326 -15.695 1.00 13.83 ?  152 TYR   B CD2  1 
ATOM   6452 C CE1  . TYR   B 1 152 ? 39.854 -20.892 -15.783 1.00 14.83 ?  152 TYR   B CE1  1 
ATOM   6453 C CE2  . TYR   B 1 152 ? 40.531 -22.922 -16.857 1.00 15.02 ?  152 TYR   B CE2  1 
ATOM   6454 C CZ   . TYR   B 1 152 ? 39.881 -21.704 -16.900 1.00 15.31 ?  152 TYR   B CZ   1 
ATOM   6455 O OH   . TYR   B 1 152 ? 39.262 -21.312 -18.061 1.00 17.71 ?  152 TYR   B OH   1 
ATOM   6456 H H    . TYR   B 1 152 ? 40.379 -22.053 -11.433 1.00 13.62 ?  152 TYR   B H    1 
ATOM   6457 H HA   . TYR   B 1 152 ? 40.338 -24.372 -12.849 1.00 13.64 ?  152 TYR   B HA   1 
ATOM   6458 H HB2  . TYR   B 1 152 ? 42.203 -22.241 -12.849 1.00 14.61 ?  152 TYR   B HB2  1 
ATOM   6459 H HB3  . TYR   B 1 152 ? 42.528 -23.632 -13.545 1.00 14.61 ?  152 TYR   B HB3  1 
ATOM   6460 H HD1  . TYR   B 1 152 ? 40.463 -20.763 -13.867 1.00 16.18 ?  152 TYR   B HD1  1 
ATOM   6461 H HD2  . TYR   B 1 152 ? 41.591 -24.151 -15.677 1.00 16.59 ?  152 TYR   B HD2  1 
ATOM   6462 H HE1  . TYR   B 1 152 ? 39.418 -20.073 -15.813 1.00 17.80 ?  152 TYR   B HE1  1 
ATOM   6463 H HE2  . TYR   B 1 152 ? 40.554 -23.468 -17.610 1.00 18.02 ?  152 TYR   B HE2  1 
ATOM   6464 H HH   . TYR   B 1 152 ? 39.370 -21.903 -18.651 1.00 21.25 ?  152 TYR   B HH   1 
ATOM   6465 N N    . LEU   B 1 153 ? 41.199 -25.638 -10.930 1.00 11.12 ?  153 LEU   B N    1 
ATOM   6466 C CA   . LEU   B 1 153 ? 41.699 -26.390 -9.790  1.00 10.68 ?  153 LEU   B CA   1 
ATOM   6467 C C    . LEU   B 1 153 ? 42.933 -27.191 -10.184 1.00 10.98 ?  153 LEU   B C    1 
ATOM   6468 O O    . LEU   B 1 153 ? 42.913 -27.929 -11.173 1.00 12.15 ?  153 LEU   B O    1 
ATOM   6469 C CB   . LEU   B 1 153 ? 40.612 -27.342 -9.291  1.00 11.03 ?  153 LEU   B CB   1 
ATOM   6470 C CG   . LEU   B 1 153 ? 39.358 -26.685 -8.714  1.00 11.96 ?  153 LEU   B CG   1 
ATOM   6471 C CD1  . LEU   B 1 153 ? 38.269 -27.735 -8.559  1.00 12.51 ?  153 LEU   B CD1  1 
ATOM   6472 C CD2  . LEU   B 1 153 ? 39.648 -26.033 -7.376  1.00 12.74 ?  153 LEU   B CD2  1 
ATOM   6473 H H    . LEU   B 1 153 ? 40.637 -26.086 -11.416 1.00 13.35 ?  153 LEU   B H    1 
ATOM   6474 H HA   . LEU   B 1 153 ? 41.925 -25.777 -9.079  1.00 12.82 ?  153 LEU   B HA   1 
ATOM   6475 H HB2  . LEU   B 1 153 ? 40.327 -27.903 -10.031 1.00 13.23 ?  153 LEU   B HB2  1 
ATOM   6476 H HB3  . LEU   B 1 153 ? 40.987 -27.899 -8.592  1.00 13.23 ?  153 LEU   B HB3  1 
ATOM   6477 H HG   . LEU   B 1 153 ? 39.032 -26.000 -9.325  1.00 14.35 ?  153 LEU   B HG   1 
ATOM   6478 H HD11 . LEU   B 1 153 ? 37.464 -27.308 -8.221  1.00 15.01 ?  153 LEU   B HD11 1 
ATOM   6479 H HD12 . LEU   B 1 153 ? 38.093 -28.134 -9.423  1.00 15.01 ?  153 LEU   B HD12 1 
ATOM   6480 H HD13 . LEU   B 1 153 ? 38.574 -28.408 -7.933  1.00 15.01 ?  153 LEU   B HD13 1 
ATOM   6481 H HD21 . LEU   B 1 153 ? 38.829 -25.662 -7.016  1.00 15.29 ?  153 LEU   B HD21 1 
ATOM   6482 H HD22 . LEU   B 1 153 ? 40.001 -26.706 -6.771  1.00 15.29 ?  153 LEU   B HD22 1 
ATOM   6483 H HD23 . LEU   B 1 153 ? 40.303 -25.330 -7.505  1.00 15.29 ?  153 LEU   B HD23 1 
ATOM   6484 N N    . ALA   B 1 154 ? 43.985 -27.080 -9.378  1.00 11.20 ?  154 ALA   B N    1 
ATOM   6485 C CA   . ALA   B 1 154 ? 45.217 -27.833 -9.563  1.00 12.12 ?  154 ALA   B CA   1 
ATOM   6486 C C    . ALA   B 1 154 ? 45.277 -28.916 -8.494  1.00 12.57 ?  154 ALA   B C    1 
ATOM   6487 O O    . ALA   B 1 154 ? 45.202 -28.621 -7.294  1.00 14.15 ?  154 ALA   B O    1 
ATOM   6488 C CB   . ALA   B 1 154 ? 46.441 -26.925 -9.498  1.00 13.67 ?  154 ALA   B CB   1 
ATOM   6489 H H    . ALA   B 1 154 ? 44.007 -26.548 -8.696  1.00 13.44 ?  154 ALA   B H    1 
ATOM   6490 H HA   . ALA   B 1 154 ? 45.203 -28.261 -10.431 1.00 14.54 ?  154 ALA   B HA   1 
ATOM   6491 H HB1  . ALA   B 1 154 ? 47.242 -27.458 -9.625  1.00 16.40 ?  154 ALA   B HB1  1 
ATOM   6492 H HB2  . ALA   B 1 154 ? 46.379 -26.254 -10.199 1.00 16.40 ?  154 ALA   B HB2  1 
ATOM   6493 H HB3  . ALA   B 1 154 ? 46.471 -26.489 -8.630  1.00 16.40 ?  154 ALA   B HB3  1 
ATOM   6494 N N    . VAL   B 1 155 ? 45.379 -30.165 -8.931  1.00 12.14 ?  155 VAL   B N    1 
ATOM   6495 C CA   . VAL   B 1 155 ? 45.477 -31.316 -8.042  1.00 12.46 ?  155 VAL   B CA   1 
ATOM   6496 C C    . VAL   B 1 155 ? 46.815 -31.996 -8.311  1.00 12.23 ?  155 VAL   B C    1 
ATOM   6497 O O    . VAL   B 1 155 ? 47.054 -32.485 -9.422  1.00 14.04 ?  155 VAL   B O    1 
ATOM   6498 C CB   . VAL   B 1 155 ? 44.312 -32.298 -8.248  1.00 14.02 ?  155 VAL   B CB   1 
ATOM   6499 C CG1  . VAL   B 1 155 ? 44.484 -33.505 -7.344  1.00 14.04 ?  155 VAL   B CG1  1 
ATOM   6500 C CG2  . VAL   B 1 155 ? 42.985 -31.604 -7.982  1.00 15.21 ?  155 VAL   B CG2  1 
ATOM   6501 H H    . VAL   B 1 155 ? 45.395 -30.379 -9.765  1.00 14.57 ?  155 VAL   B H    1 
ATOM   6502 H HA   . VAL   B 1 155 ? 45.462 -31.022 -7.122  1.00 14.95 ?  155 VAL   B HA   1 
ATOM   6503 H HB   . VAL   B 1 155 ? 44.307 -32.607 -9.169  1.00 16.83 ?  155 VAL   B HB   1 
ATOM   6504 H HG11 . VAL   B 1 155 ? 43.652 -34.004 -7.312  1.00 16.84 ?  155 VAL   B HG11 1 
ATOM   6505 H HG12 . VAL   B 1 155 ? 45.189 -34.074 -7.701  1.00 16.84 ?  155 VAL   B HG12 1 
ATOM   6506 H HG13 . VAL   B 1 155 ? 44.723 -33.206 -6.454  1.00 16.84 ?  155 VAL   B HG13 1 
ATOM   6507 H HG21 . VAL   B 1 155 ? 42.266 -32.251 -8.068  1.00 18.25 ?  155 VAL   B HG21 1 
ATOM   6508 H HG22 . VAL   B 1 155 ? 42.995 -31.241 -7.083  1.00 18.25 ?  155 VAL   B HG22 1 
ATOM   6509 H HG23 . VAL   B 1 155 ? 42.866 -30.891 -8.627  1.00 18.25 ?  155 VAL   B HG23 1 
ATOM   6510 N N    . PHE   B 1 156 ? 47.678 -32.041 -7.294  1.00 12.66 ?  156 PHE   B N    1 
ATOM   6511 C CA   . PHE   B 1 156 ? 49.056 -32.494 -7.496  1.00 13.97 ?  156 PHE   B CA   1 
ATOM   6512 C C    . PHE   B 1 156 ? 49.151 -33.992 -7.776  1.00 14.77 ?  156 PHE   B C    1 
ATOM   6513 O O    . PHE   B 1 156 ? 49.884 -34.419 -8.678  1.00 16.59 ?  156 PHE   B O    1 
ATOM   6514 C CB   . PHE   B 1 156 ? 49.890 -32.128 -6.269  1.00 13.64 ?  156 PHE   B CB   1 
ATOM   6515 C CG   . PHE   B 1 156 ? 51.304 -32.598 -6.333  1.00 14.29 ?  156 PHE   B CG   1 
ATOM   6516 C CD1  . PHE   B 1 156 ? 52.182 -32.064 -7.256  1.00 16.26 ?  156 PHE   B CD1  1 
ATOM   6517 C CD2  . PHE   B 1 156 ? 51.764 -33.556 -5.452  1.00 14.56 ?  156 PHE   B CD2  1 
ATOM   6518 C CE1  . PHE   B 1 156 ? 53.497 -32.485 -7.311  1.00 17.34 ?  156 PHE   B CE1  1 
ATOM   6519 C CE2  . PHE   B 1 156 ? 53.079 -33.980 -5.502  1.00 16.19 ?  156 PHE   B CE2  1 
ATOM   6520 C CZ   . PHE   B 1 156 ? 53.939 -33.442 -6.435  1.00 16.75 ?  156 PHE   B CZ   1 
ATOM   6521 H H    . PHE   B 1 156 ? 47.487 -31.816 -6.486  1.00 15.19 ?  156 PHE   B H    1 
ATOM   6522 H HA   . PHE   B 1 156 ? 49.424 -32.024 -8.256  1.00 16.77 ?  156 PHE   B HA   1 
ATOM   6523 H HB2  . PHE   B 1 156 ? 49.905 -31.161 -6.183  1.00 16.37 ?  156 PHE   B HB2  1 
ATOM   6524 H HB3  . PHE   B 1 156 ? 49.482 -32.521 -5.483  1.00 16.37 ?  156 PHE   B HB3  1 
ATOM   6525 H HD1  . PHE   B 1 156 ? 51.886 -31.413 -7.853  1.00 19.51 ?  156 PHE   B HD1  1 
ATOM   6526 H HD2  . PHE   B 1 156 ? 51.182 -33.924 -4.823  1.00 17.48 ?  156 PHE   B HD2  1 
ATOM   6527 H HE1  . PHE   B 1 156 ? 54.080 -32.124 -7.940  1.00 20.81 ?  156 PHE   B HE1  1 
ATOM   6528 H HE2  . PHE   B 1 156 ? 53.376 -34.635 -4.911  1.00 19.42 ?  156 PHE   B HE2  1 
ATOM   6529 H HZ   . PHE   B 1 156 ? 54.820 -33.734 -6.470  1.00 20.10 ?  156 PHE   B HZ   1 
ATOM   6530 N N    . ASP   B 1 157 ? 48.482 -34.810 -6.976  1.00 15.23 ?  157 ASP   B N    1 
ATOM   6531 C CA   . ASP   B 1 157 ? 48.627 -36.259 -7.071  1.00 16.50 ?  157 ASP   B CA   1 
ATOM   6532 C C    . ASP   B 1 157 ? 47.714 -36.800 -8.167  1.00 16.45 ?  157 ASP   B C    1 
ATOM   6533 O O    . ASP   B 1 157 ? 46.488 -36.674 -8.071  1.00 15.88 ?  157 ASP   B O    1 
ATOM   6534 C CB   . ASP   B 1 157 ? 48.253 -36.871 -5.728  1.00 17.94 ?  157 ASP   B CB   1 
ATOM   6535 C CG   . ASP   B 1 157 ? 48.402 -38.379 -5.702  1.00 20.16 ?  157 ASP   B CG   1 
ATOM   6536 O OD1  . ASP   B 1 157 ? 48.740 -38.994 -6.742  1.00 20.92 ?  157 ASP   B OD1  1 
ATOM   6537 O OD2  . ASP   B 1 157 ? 48.184 -38.949 -4.619  1.00 22.21 -1 157 ASP   B OD2  1 
ATOM   6538 H H    . ASP   B 1 157 ? 47.937 -34.553 -6.369  1.00 18.28 ?  157 ASP   B H    1 
ATOM   6539 H HA   . ASP   B 1 157 ? 49.548 -36.491 -7.280  1.00 19.80 ?  157 ASP   B HA   1 
ATOM   6540 H HB2  . ASP   B 1 157 ? 48.818 -36.490 -5.043  1.00 21.53 ?  157 ASP   B HB2  1 
ATOM   6541 H HB3  . ASP   B 1 157 ? 47.321 -36.659 -5.541  1.00 21.53 ?  157 ASP   B HB3  1 
ATOM   6542 N N    . LYS   B 1 158 ? 48.311 -37.432 -9.188  1.00 17.27 ?  158 LYS   B N    1 
ATOM   6543 C CA   . LYS   B 1 158 ? 47.534 -38.024 -10.280 1.00 18.35 ?  158 LYS   B CA   1 
ATOM   6544 C C    . LYS   B 1 158 ? 46.473 -38.993 -9.760  1.00 17.79 ?  158 LYS   B C    1 
ATOM   6545 O O    . LYS   B 1 158 ? 45.364 -39.067 -10.304 1.00 17.93 ?  158 LYS   B O    1 
ATOM   6546 C CB   . LYS   B 1 158 ? 48.483 -38.729 -11.262 1.00 20.19 ?  158 LYS   B CB   1 
ATOM   6547 C CG   . LYS   B 1 158 ? 47.808 -39.623 -12.294 1.00 22.68 ?  158 LYS   B CG   1 
ATOM   6548 C CD   . LYS   B 1 158 ? 46.929 -38.838 -13.245 1.00 25.38 ?  158 LYS   B CD   1 
ATOM   6549 C CE   . LYS   B 1 158 ? 46.360 -39.740 -14.328 1.00 27.19 ?  158 LYS   B CE   1 
ATOM   6550 N NZ   . LYS   B 1 158 ? 45.308 -39.049 -15.124 1.00 27.67 ?  158 LYS   B NZ   1 
ATOM   6551 H H    . LYS   B 1 158 ? 49.170 -37.530 -9.270  1.00 20.73 ?  158 LYS   B H    1 
ATOM   6552 H HA   . LYS   B 1 158 ? 47.090 -37.313 -10.766 1.00 22.02 ?  158 LYS   B HA   1 
ATOM   6553 H HB2  . LYS   B 1 158 ? 48.986 -38.052 -11.753 1.00 24.23 ?  158 LYS   B HB2  1 
ATOM   6554 H HB3  . LYS   B 1 158 ? 49.103 -39.279 -10.758 1.00 24.23 ?  158 LYS   B HB3  1 
ATOM   6555 H HG2  . LYS   B 1 158 ? 48.492 -40.066 -12.822 1.00 27.21 ?  158 LYS   B HG2  1 
ATOM   6556 H HG3  . LYS   B 1 158 ? 47.261 -40.290 -11.848 1.00 27.21 ?  158 LYS   B HG3  1 
ATOM   6557 H HD2  . LYS   B 1 158 ? 46.190 -38.447 -12.753 1.00 30.46 ?  158 LYS   B HD2  1 
ATOM   6558 H HD3  . LYS   B 1 158 ? 47.455 -38.144 -13.673 1.00 30.46 ?  158 LYS   B HD3  1 
ATOM   6559 H HE2  . LYS   B 1 158 ? 47.069 -40.006 -14.931 1.00 32.63 ?  158 LYS   B HE2  1 
ATOM   6560 H HE3  . LYS   B 1 158 ? 45.959 -40.523 -13.915 1.00 32.63 ?  158 LYS   B HE3  1 
ATOM   6561 H HZ1  . LYS   B 1 158 ? 44.989 -39.595 -15.749 1.00 33.20 ?  158 LYS   B HZ1  1 
ATOM   6562 H HZ2  . LYS   B 1 158 ? 44.639 -38.797 -14.592 1.00 33.20 ?  158 LYS   B HZ2  1 
ATOM   6563 H HZ3  . LYS   B 1 158 ? 45.650 -38.327 -15.518 1.00 33.20 ?  158 LYS   B HZ3  1 
ATOM   6564 N N    . ASN   B 1 159 ? 46.790 -39.748 -8.707  1.00 18.37 ?  159 ASN   B N    1 
ATOM   6565 C CA   . ASN   B 1 159 ? 45.834 -40.729 -8.203  1.00 18.79 ?  159 ASN   B CA   1 
ATOM   6566 C C    . ASN   B 1 159 ? 44.635 -40.054 -7.536  1.00 17.55 ?  159 ASN   B C    1 
ATOM   6567 O O    . ASN   B 1 159 ? 43.496 -40.529 -7.664  1.00 17.80 ?  159 ASN   B O    1 
ATOM   6568 C CB   . ASN   B 1 159 ? 46.537 -41.696 -7.258  1.00 20.30 ?  159 ASN   B CB   1 
ATOM   6569 C CG   . ASN   B 1 159 ? 47.565 -42.544 -7.967  1.00 22.17 ?  159 ASN   B CG   1 
ATOM   6570 O OD1  . ASN   B 1 159 ? 47.322 -43.046 -9.073  1.00 23.22 ?  159 ASN   B OD1  1 
ATOM   6571 N ND2  . ASN   B 1 159 ? 48.720 -42.722 -7.334  1.00 22.75 ?  159 ASN   B ND2  1 
ATOM   6572 H H    . ASN   B 1 159 ? 47.533 -39.697 -8.277  1.00 22.04 ?  159 ASN   B H    1 
ATOM   6573 H HA   . ASN   B 1 159 ? 45.503 -41.235 -8.956  1.00 22.55 ?  159 ASN   B HA   1 
ATOM   6574 H HB2  . ASN   B 1 159 ? 46.989 -41.193 -6.563  1.00 24.36 ?  159 ASN   B HB2  1 
ATOM   6575 H HB3  . ASN   B 1 159 ? 45.878 -42.288 -6.870  1.00 24.36 ?  159 ASN   B HB3  1 
ATOM   6576 H HD21 . ASN   B 1 159 ? 49.342 -43.199 -7.694  1.00 27.30 ?  159 ASN   B HD21 1 
ATOM   6577 H HD22 . ASN   B 1 159 ? 48.850 -42.368 -6.560  1.00 27.30 ?  159 ASN   B HD22 1 
ATOM   6578 N N    . LEU   B 1 160 ? 44.858 -38.939 -6.833  1.00 16.98 ?  160 LEU   B N    1 
ATOM   6579 C CA   . LEU   B 1 160 ? 43.726 -38.193 -6.296  1.00 15.75 ?  160 LEU   B CA   1 
ATOM   6580 C C    . LEU   B 1 160 ? 42.939 -37.528 -7.413  1.00 15.15 ?  160 LEU   B C    1 
ATOM   6581 O O    . LEU   B 1 160 ? 41.700 -37.522 -7.388  1.00 14.71 ?  160 LEU   B O    1 
ATOM   6582 C CB   . LEU   B 1 160 ? 44.186 -37.149 -5.280  1.00 15.84 ?  160 LEU   B CB   1 
ATOM   6583 C CG   . LEU   B 1 160 ? 43.058 -36.253 -4.747  1.00 15.80 ?  160 LEU   B CG   1 
ATOM   6584 C CD1  . LEU   B 1 160 ? 41.918 -37.071 -4.146  1.00 16.83 ?  160 LEU   B CD1  1 
ATOM   6585 C CD2  . LEU   B 1 160 ? 43.592 -35.250 -3.734  1.00 16.07 ?  160 LEU   B CD2  1 
ATOM   6586 H H    . LEU   B 1 160 ? 45.634 -38.604 -6.660  1.00 20.37 ?  160 LEU   B H    1 
ATOM   6587 H HA   . LEU   B 1 160 ? 43.136 -38.811 -5.846  1.00 18.90 ?  160 LEU   B HA   1 
ATOM   6588 H HB2  . LEU   B 1 160 ? 44.586 -37.610 -4.526  1.00 19.01 ?  160 LEU   B HB2  1 
ATOM   6589 H HB3  . LEU   B 1 160 ? 44.848 -36.577 -5.701  1.00 19.01 ?  160 LEU   B HB3  1 
ATOM   6590 H HG   . LEU   B 1 160 ? 42.695 -35.745 -5.484  1.00 18.97 ?  160 LEU   B HG   1 
ATOM   6591 H HD11 . LEU   B 1 160 ? 41.287 -36.467 -3.727  1.00 20.19 ?  160 LEU   B HD11 1 
ATOM   6592 H HD12 . LEU   B 1 160 ? 41.477 -37.569 -4.854  1.00 20.19 ?  160 LEU   B HD12 1 
ATOM   6593 H HD13 . LEU   B 1 160 ? 42.279 -37.684 -3.486  1.00 20.19 ?  160 LEU   B HD13 1 
ATOM   6594 H HD21 . LEU   B 1 160 ? 42.867 -34.677 -3.445  1.00 19.28 ?  160 LEU   B HD21 1 
ATOM   6595 H HD22 . LEU   B 1 160 ? 43.960 -35.729 -2.973  1.00 19.28 ?  160 LEU   B HD22 1 
ATOM   6596 H HD23 . LEU   B 1 160 ? 44.288 -34.716 -4.153  1.00 19.28 ?  160 LEU   B HD23 1 
ATOM   6597 N N    . TYR   B 1 161 ? 43.639 -36.963 -8.401  1.00 15.15 ?  161 TYR   B N    1 
ATOM   6598 C CA   . TYR   B 1 161 ? 42.967 -36.389 -9.562  1.00 14.99 ?  161 TYR   B CA   1 
ATOM   6599 C C    . TYR   B 1 161 ? 42.022 -37.406 -10.192 1.00 15.19 ?  161 TYR   B C    1 
ATOM   6600 O O    . TYR   B 1 161 ? 40.855 -37.107 -10.462 1.00 14.88 ?  161 TYR   B O    1 
ATOM   6601 C CB   . TYR   B 1 161 ? 44.012 -35.902 -10.575 1.00 15.88 ?  161 TYR   B CB   1 
ATOM   6602 C CG   . TYR   B 1 161 ? 43.444 -35.430 -11.894 1.00 16.52 ?  161 TYR   B CG   1 
ATOM   6603 C CD1  . TYR   B 1 161 ? 43.066 -34.106 -12.074 1.00 16.44 ?  161 TYR   B CD1  1 
ATOM   6604 C CD2  . TYR   B 1 161 ? 43.263 -36.311 -12.954 1.00 17.46 ?  161 TYR   B CD2  1 
ATOM   6605 C CE1  . TYR   B 1 161 ? 42.539 -33.674 -13.266 1.00 17.42 ?  161 TYR   B CE1  1 
ATOM   6606 C CE2  . TYR   B 1 161 ? 42.732 -35.885 -14.151 1.00 18.35 ?  161 TYR   B CE2  1 
ATOM   6607 C CZ   . TYR   B 1 161 ? 42.379 -34.561 -14.305 1.00 18.23 ?  161 TYR   B CZ   1 
ATOM   6608 O OH   . TYR   B 1 161 ? 41.845 -34.131 -15.494 1.00 20.31 ?  161 TYR   B OH   1 
ATOM   6609 H H    . TYR   B 1 161 ? 44.495 -36.906 -8.428  1.00 18.19 ?  161 TYR   B H    1 
ATOM   6610 H HA   . TYR   B 1 161 ? 42.440 -35.625 -9.284  1.00 17.99 ?  161 TYR   B HA   1 
ATOM   6611 H HB2  . TYR   B 1 161 ? 44.496 -35.153 -10.188 1.00 19.06 ?  161 TYR   B HB2  1 
ATOM   6612 H HB3  . TYR   B 1 161 ? 44.627 -36.623 -10.767 1.00 19.06 ?  161 TYR   B HB3  1 
ATOM   6613 H HD1  . TYR   B 1 161 ? 43.185 -33.495 -11.383 1.00 19.72 ?  161 TYR   B HD1  1 
ATOM   6614 H HD2  . TYR   B 1 161 ? 43.497 -37.207 -12.855 1.00 20.95 ?  161 TYR   B HD2  1 
ATOM   6615 H HE1  . TYR   B 1 161 ? 42.304 -32.778 -13.376 1.00 20.90 ?  161 TYR   B HE1  1 
ATOM   6616 H HE2  . TYR   B 1 161 ? 42.614 -36.488 -14.854 1.00 22.02 ?  161 TYR   B HE2  1 
ATOM   6617 H HH   . TYR   B 1 161 ? 41.801 -34.775 -16.038 1.00 24.37 ?  161 TYR   B HH   1 
ATOM   6618 N N    . ASP   B 1 162 ? 42.513 -38.626 -10.416 1.00 16.06 ?  162 ASP   B N    1 
ATOM   6619 C CA   . ASP   B 1 162 ? 41.682 -39.657 -11.030 1.00 16.54 ?  162 ASP   B CA   1 
ATOM   6620 C C    . ASP   B 1 162 ? 40.471 -39.985 -10.163 1.00 15.91 ?  162 ASP   B C    1 
ATOM   6621 O O    . ASP   B 1 162 ? 39.368 -40.189 -10.679 1.00 16.12 ?  162 ASP   B O    1 
ATOM   6622 C CB   . ASP   B 1 162 ? 42.512 -40.922 -11.279 1.00 17.90 ?  162 ASP   B CB   1 
ATOM   6623 C CG   . ASP   B 1 162 ? 43.527 -40.761 -12.402 1.00 19.02 ?  162 ASP   B CG   1 
ATOM   6624 O OD1  . ASP   B 1 162 ? 43.404 -39.815 -13.205 1.00 19.37 ?  162 ASP   B OD1  1 
ATOM   6625 O OD2  . ASP   B 1 162 ? 44.434 -41.621 -12.500 1.00 20.72 -1 162 ASP   B OD2  1 
ATOM   6626 H H    . ASP   B 1 162 ? 43.312 -38.873 -10.231 1.00 19.27 ?  162 ASP   B H    1 
ATOM   6627 H HA   . ASP   B 1 162 ? 41.359 -39.339 -11.886 1.00 19.85 ?  162 ASP   B HA   1 
ATOM   6628 H HB2  . ASP   B 1 162 ? 42.993 -41.150 -10.471 1.00 21.48 ?  162 ASP   B HB2  1 
ATOM   6629 H HB3  . ASP   B 1 162 ? 41.916 -41.645 -11.530 1.00 21.48 ?  162 ASP   B HB3  1 
ATOM   6630 N N    . LYS   B 1 163 ? 40.662 -40.071 -8.844  1.00 15.33 ?  163 LYS   B N    1 
ATOM   6631 C CA   . LYS   B 1 163 ? 39.540 -40.344 -7.951  1.00 15.63 ?  163 LYS   B CA   1 
ATOM   6632 C C    . LYS   B 1 163 ? 38.498 -39.230 -8.009  1.00 14.38 ?  163 LYS   B C    1 
ATOM   6633 O O    . LYS   B 1 163 ? 37.287 -39.496 -8.013  1.00 15.26 ?  163 LYS   B O    1 
ATOM   6634 C CB   . LYS   B 1 163 ? 40.040 -40.521 -6.519  1.00 18.85 ?  163 LYS   B CB   1 
ATOM   6635 C CG   . LYS   B 1 163 ? 38.953 -40.976 -5.573  1.00 24.91 ?  163 LYS   B CG   1 
ATOM   6636 C CD   . LYS   B 1 163 ? 39.468 -41.252 -4.176  1.00 30.96 ?  163 LYS   B CD   1 
ATOM   6637 C CE   . LYS   B 1 163 ? 38.376 -41.894 -3.333  1.00 35.59 ?  163 LYS   B CE   1 
ATOM   6638 N NZ   . LYS   B 1 163 ? 38.531 -41.605 -1.882  1.00 38.44 ?  163 LYS   B NZ   1 
ATOM   6639 H H    . LYS   B 1 163 ? 41.423 -39.978 -8.453  1.00 18.39 ?  163 LYS   B H    1 
ATOM   6640 H HA   . LYS   B 1 163 ? 39.114 -41.167 -8.224  1.00 18.75 ?  163 LYS   B HA   1 
ATOM   6641 H HB2  . LYS   B 1 163 ? 40.744 -41.191 -6.511  1.00 22.62 ?  163 LYS   B HB2  1 
ATOM   6642 H HB3  . LYS   B 1 163 ? 40.385 -39.675 -6.195  1.00 22.62 ?  163 LYS   B HB3  1 
ATOM   6643 H HG2  . LYS   B 1 163 ? 38.276 -40.284 -5.510  1.00 29.89 ?  163 LYS   B HG2  1 
ATOM   6644 H HG3  . LYS   B 1 163 ? 38.558 -41.795 -5.916  1.00 29.89 ?  163 LYS   B HG3  1 
ATOM   6645 H HD2  . LYS   B 1 163 ? 40.220 -41.866 -4.223  1.00 37.16 ?  163 LYS   B HD2  1 
ATOM   6646 H HD3  . LYS   B 1 163 ? 39.734 -40.420 -3.756  1.00 37.16 ?  163 LYS   B HD3  1 
ATOM   6647 H HE2  . LYS   B 1 163 ? 37.512 -41.561 -3.621  1.00 42.71 ?  163 LYS   B HE2  1 
ATOM   6648 H HE3  . LYS   B 1 163 ? 38.412 -42.856 -3.451  1.00 42.71 ?  163 LYS   B HE3  1 
ATOM   6649 H HZ1  . LYS   B 1 163 ? 37.874 -41.994 -1.424  1.00 46.13 ?  163 LYS   B HZ1  1 
ATOM   6650 H HZ2  . LYS   B 1 163 ? 39.311 -41.917 -1.593  1.00 46.13 ?  163 LYS   B HZ2  1 
ATOM   6651 H HZ3  . LYS   B 1 163 ? 38.499 -40.727 -1.743  1.00 46.13 ?  163 LYS   B HZ3  1 
ATOM   6652 N N    . LEU   B 1 164 ? 38.954 -37.978 -8.053  1.00 13.40 ?  164 LEU   B N    1 
ATOM   6653 C CA   . LEU   B 1 164 ? 38.049 -36.834 -8.117  1.00 13.40 ?  164 LEU   B CA   1 
ATOM   6654 C C    . LEU   B 1 164 ? 37.265 -36.813 -9.425  1.00 13.49 ?  164 LEU   B C    1 
ATOM   6655 O O    . LEU   B 1 164 ? 36.043 -36.612 -9.423  1.00 14.31 ?  164 LEU   B O    1 
ATOM   6656 C CB   . LEU   B 1 164 ? 38.858 -35.547 -7.964  1.00 12.94 ?  164 LEU   B CB   1 
ATOM   6657 C CG   . LEU   B 1 164 ? 39.389 -35.284 -6.559  1.00 13.69 ?  164 LEU   B CG   1 
ATOM   6658 C CD1  . LEU   B 1 164 ? 40.483 -34.219 -6.589  1.00 14.29 ?  164 LEU   B CD1  1 
ATOM   6659 C CD2  . LEU   B 1 164 ? 38.268 -34.875 -5.618  1.00 15.95 ?  164 LEU   B CD2  1 
ATOM   6660 H H    . LEU   B 1 164 ? 39.791 -37.764 -8.042  1.00 16.08 ?  164 LEU   B H    1 
ATOM   6661 H HA   . LEU   B 1 164 ? 37.420 -36.886 -7.389  1.00 16.08 ?  164 LEU   B HA   1 
ATOM   6662 H HB2  . LEU   B 1 164 ? 39.626 -35.588 -8.562  1.00 15.52 ?  164 LEU   B HB2  1 
ATOM   6663 H HB3  . LEU   B 1 164 ? 38.299 -34.798 -8.210  1.00 15.52 ?  164 LEU   B HB3  1 
ATOM   6664 H HG   . LEU   B 1 164 ? 39.787 -36.095 -6.215  1.00 16.43 ?  164 LEU   B HG   1 
ATOM   6665 H HD11 . LEU   B 1 164 ? 40.804 -34.065 -5.685  1.00 17.14 ?  164 LEU   B HD11 1 
ATOM   6666 H HD12 . LEU   B 1 164 ? 41.219 -34.533 -7.145  1.00 17.14 ?  164 LEU   B HD12 1 
ATOM   6667 H HD13 . LEU   B 1 164 ? 40.123 -33.398 -6.956  1.00 17.14 ?  164 LEU   B HD13 1 
ATOM   6668 H HD21 . LEU   B 1 164 ? 38.645 -34.628 -4.760  1.00 19.14 ?  164 LEU   B HD21 1 
ATOM   6669 H HD22 . LEU   B 1 164 ? 37.792 -34.122 -6.000  1.00 19.14 ?  164 LEU   B HD22 1 
ATOM   6670 H HD23 . LEU   B 1 164 ? 37.663 -35.627 -5.509  1.00 19.14 ?  164 LEU   B HD23 1 
ATOM   6671 N N    . VAL   B 1 165 ? 37.954 -36.989 -10.554 1.00 14.71 ?  165 VAL   B N    1 
ATOM   6672 C CA   . VAL   B 1 165 ? 37.301 -36.913 -11.857 1.00 16.27 ?  165 VAL   B CA   1 
ATOM   6673 C C    . VAL   B 1 165 ? 36.385 -38.111 -12.056 1.00 17.91 ?  165 VAL   B C    1 
ATOM   6674 O O    . VAL   B 1 165 ? 35.230 -37.973 -12.479 1.00 18.84 ?  165 VAL   B O    1 
ATOM   6675 C CB   . VAL   B 1 165 ? 38.353 -36.825 -12.978 1.00 17.24 ?  165 VAL   B CB   1 
ATOM   6676 C CG1  . VAL   B 1 165 ? 37.690 -36.917 -14.340 1.00 18.86 ?  165 VAL   B CG1  1 
ATOM   6677 C CG2  . VAL   B 1 165 ? 39.157 -35.550 -12.853 1.00 17.14 ?  165 VAL   B CG2  1 
ATOM   6678 H H    . VAL   B 1 165 ? 38.802 -37.148 -10.592 1.00 17.65 ?  165 VAL   B H    1 
ATOM   6679 H HA   . VAL   B 1 165 ? 36.760 -36.115 -11.896 1.00 19.53 ?  165 VAL   B HA   1 
ATOM   6680 H HB   . VAL   B 1 165 ? 38.972 -37.570 -12.893 1.00 20.69 ?  165 VAL   B HB   1 
ATOM   6681 H HG11 . VAL   B 1 165 ? 38.316 -36.619 -15.015 1.00 22.64 ?  165 VAL   B HG11 1 
ATOM   6682 H HG12 . VAL   B 1 165 ? 37.444 -37.842 -14.507 1.00 22.64 ?  165 VAL   B HG12 1 
ATOM   6683 H HG13 . VAL   B 1 165 ? 36.901 -36.358 -14.343 1.00 22.64 ?  165 VAL   B HG13 1 
ATOM   6684 H HG21 . VAL   B 1 165 ? 39.797 -35.502 -13.581 1.00 20.57 ?  165 VAL   B HG21 1 
ATOM   6685 H HG22 . VAL   B 1 165 ? 38.554 -34.790 -12.895 1.00 20.57 ?  165 VAL   B HG22 1 
ATOM   6686 H HG23 . VAL   B 1 165 ? 39.626 -35.549 -12.002 1.00 20.57 ?  165 VAL   B HG23 1 
ATOM   6687 N N    . SER   B 1 166 ? 36.901 -39.312 -11.764 1.00 19.09 ?  166 SER   B N    1 
ATOM   6688 C CA   . SER   B 1 166 ? 36.147 -40.525 -12.042 1.00 20.41 ?  166 SER   B CA   1 
ATOM   6689 C C    . SER   B 1 166 ? 34.887 -40.609 -11.193 1.00 20.70 ?  166 SER   B C    1 
ATOM   6690 O O    . SER   B 1 166 ? 33.914 -41.235 -11.614 1.00 21.92 ?  166 SER   B O    1 
ATOM   6691 C CB   . SER   B 1 166 ? 37.021 -41.776 -11.863 1.00 21.24 ?  166 SER   B CB   1 
ATOM   6692 O OG   . SER   B 1 166 ? 37.375 -41.981 -10.507 1.00 20.96 ?  166 SER   B OG   1 
ATOM   6693 H H    . SER   B 1 166 ? 37.686 -39.446 -11.427 1.00 22.90 ?  166 SER   B H    1 
ATOM   6694 H HA   . SER   B 1 166 ? 35.874 -40.511 -12.971 1.00 24.50 ?  166 SER   B HA   1 
ATOM   6695 H HB2  . SER   B 1 166 ? 36.528 -42.554 -12.173 1.00 25.48 ?  166 SER   B HB2  1 
ATOM   6696 H HB3  . SER   B 1 166 ? 37.832 -41.678 -12.395 1.00 25.48 ?  166 SER   B HB3  1 
ATOM   6697 H HG   . SER   B 1 166 ? 37.829 -41.326 -10.231 1.00 25.16 ?  166 SER   B HG   1 
ATOM   6698 N N    . SER   B 1 167 ? 34.868 -39.987 -10.015 1.00 19.34 ?  167 SER   B N    1 
ATOM   6699 C CA   . SER   B 1 167 ? 33.711 -40.049 -9.128  1.00 18.77 ?  167 SER   B CA   1 
ATOM   6700 C C    . SER   B 1 167 ? 32.792 -38.827 -9.218  1.00 18.11 ?  167 SER   B C    1 
ATOM   6701 O O    . SER   B 1 167 ? 31.716 -38.824 -8.607  1.00 18.34 ?  167 SER   B O    1 
ATOM   6702 C CB   . SER   B 1 167 ? 34.160 -40.238 -7.675  1.00 18.64 ?  167 SER   B CB   1 
ATOM   6703 O OG   . SER   B 1 167 ? 34.831 -39.083 -7.198  1.00 18.49 ?  167 SER   B OG   1 
ATOM   6704 H H    . SER   B 1 167 ? 35.518 -39.517 -9.711  1.00 23.20 ?  167 SER   B H    1 
ATOM   6705 H HA   . SER   B 1 167 ? 33.188 -40.832 -9.376  1.00 22.53 ?  167 SER   B HA   1 
ATOM   6706 H HB2  . SER   B 1 167 ? 33.375 -40.399 -7.127  1.00 22.37 ?  167 SER   B HB2  1 
ATOM   6707 H HB3  . SER   B 1 167 ? 34.755 -41.006 -7.628  1.00 22.37 ?  167 SER   B HB3  1 
ATOM   6708 H HG   . SER   B 1 167 ? 35.518 -38.947 -7.668  1.00 22.19 ?  167 SER   B HG   1 
ATOM   6709 N N    . PHE   B 1 168 ? 33.175 -37.791 -9.963  1.00 18.08 ?  168 PHE   B N    1 
ATOM   6710 C CA   . PHE   B 1 168 ? 32.344 -36.587 -10.025 1.00 17.70 ?  168 PHE   B CA   1 
ATOM   6711 C C    . PHE   B 1 168 ? 31.024 -36.844 -10.748 1.00 15.15 ?  168 PHE   B C    1 
ATOM   6712 O O    . PHE   B 1 168 ? 29.986 -36.248 -10.401 1.00 15.75 ?  168 PHE   B O    1 
ATOM   6713 C CB   . PHE   B 1 168 ? 33.110 -35.461 -10.710 1.00 18.59 ?  168 PHE   B CB   1 
ATOM   6714 C CG   . PHE   B 1 168 ? 32.313 -34.207 -10.853 1.00 18.71 ?  168 PHE   B CG   1 
ATOM   6715 C CD1  . PHE   B 1 168 ? 31.975 -33.463 -9.731  1.00 19.94 ?  168 PHE   B CD1  1 
ATOM   6716 C CD2  . PHE   B 1 168 ? 31.884 -33.778 -12.093 1.00 18.40 ?  168 PHE   B CD2  1 
ATOM   6717 C CE1  . PHE   B 1 168 ? 31.223 -32.311 -9.844  1.00 20.78 ?  168 PHE   B CE1  1 
ATOM   6718 C CE2  . PHE   B 1 168 ? 31.146 -32.615 -12.216 1.00 19.23 ?  168 PHE   B CE2  1 
ATOM   6719 C CZ   . PHE   B 1 168 ? 30.808 -31.882 -11.087 1.00 19.96 ?  168 PHE   B CZ   1 
ATOM   6720 H H    . PHE   B 1 168 ? 33.897 -37.756 -10.426 1.00 21.69 ?  168 PHE   B H    1 
ATOM   6721 H HA   . PHE   B 1 168 ? 32.132 -36.308 -9.125  1.00 21.24 ?  168 PHE   B HA   1 
ATOM   6722 H HB2  . PHE   B 1 168 ? 33.895 -35.253 -10.184 1.00 22.30 ?  168 PHE   B HB2  1 
ATOM   6723 H HB3  . PHE   B 1 168 ? 33.368 -35.747 -11.598 1.00 22.30 ?  168 PHE   B HB3  1 
ATOM   6724 H HD1  . PHE   B 1 168 ? 32.244 -33.756 -8.892  1.00 23.93 ?  168 PHE   B HD1  1 
ATOM   6725 H HD2  . PHE   B 1 168 ? 32.104 -34.259 -12.853 1.00 22.08 ?  168 PHE   B HD2  1 
ATOM   6726 H HE1  . PHE   B 1 168 ? 30.999 -31.822 -9.085  1.00 24.93 ?  168 PHE   B HE1  1 
ATOM   6727 H HE2  . PHE   B 1 168 ? 30.860 -32.327 -13.058 1.00 23.07 ?  168 PHE   B HE2  1 
ATOM   6728 H HZ   . PHE   B 1 168 ? 30.304 -31.101 -11.174 1.00 23.96 ?  168 PHE   B HZ   1 
ATOM   6729 N N    . LEU   B 1 169 ? 31.051 -37.717 -11.752 1.00 15.53 ?  169 LEU   B N    1 
ATOM   6730 C CA   . LEU   B 1 169 ? 29.871 -38.027 -12.554 1.00 18.36 ?  169 LEU   B CA   1 
ATOM   6731 C C    . LEU   B 1 169 ? 29.869 -39.459 -13.067 1.00 21.20 ?  169 LEU   B C    1 
ATOM   6732 O O    . LEU   B 1 169 ? 28.947 -39.862 -13.781 1.00 23.95 ?  169 LEU   B O    1 
ATOM   6733 C CB   . LEU   B 1 169 ? 29.797 -37.087 -13.754 1.00 20.99 ?  169 LEU   B CB   1 
ATOM   6734 C CG   . LEU   B 1 169 ? 28.578 -36.173 -13.827 1.00 24.10 ?  169 LEU   B CG   1 
ATOM   6735 C CD1  . LEU   B 1 169 ? 28.543 -35.474 -15.169 1.00 24.79 ?  169 LEU   B CD1  1 
ATOM   6736 C CD2  . LEU   B 1 169 ? 27.296 -36.951 -13.592 1.00 23.92 ?  169 LEU   B CD2  1 
ATOM   6737 O OXT  . LEU   B 1 169 ? 30.795 -40.220 -12.801 1.00 22.16 -1 169 LEU   B OXT  1 
ATOM   6738 H H    . LEU   B 1 169 ? 31.750 -38.151 -12.002 1.00 18.64 ?  169 LEU   B H    1 
ATOM   6739 H HA   . LEU   B 1 169 ? 29.079 -37.896 -12.008 1.00 22.03 ?  169 LEU   B HA   1 
ATOM   6740 H HB2  . LEU   B 1 169 ? 30.581 -36.519 -13.748 1.00 25.19 ?  169 LEU   B HB2  1 
ATOM   6741 H HB3  . LEU   B 1 169 ? 29.796 -37.624 -14.565 1.00 25.19 ?  169 LEU   B HB3  1 
ATOM   6742 H HG   . LEU   B 1 169 ? 28.648 -35.493 -13.137 1.00 28.92 ?  169 LEU   B HG   1 
ATOM   6743 H HD11 . LEU   B 1 169 ? 27.780 -34.878 -15.194 1.00 29.75 ?  169 LEU   B HD11 1 
ATOM   6744 H HD12 . LEU   B 1 169 ? 29.364 -34.971 -15.280 1.00 29.75 ?  169 LEU   B HD12 1 
ATOM   6745 H HD13 . LEU   B 1 169 ? 28.465 -36.143 -15.867 1.00 29.75 ?  169 LEU   B HD13 1 
ATOM   6746 H HD21 . LEU   B 1 169 ? 26.559 -36.487 -14.015 1.00 28.70 ?  169 LEU   B HD21 1 
ATOM   6747 H HD22 . LEU   B 1 169 ? 27.394 -37.839 -13.974 1.00 28.70 ?  169 LEU   B HD22 1 
ATOM   6748 H HD23 . LEU   B 1 169 ? 27.141 -37.020 -12.637 1.00 28.70 ?  169 LEU   B HD23 1 
HETATM 6749 S S    B DMS   C 2 .   ? 10.807 3.767   3.170   0.70 28.96 ?  301 DMS   A S    1 
HETATM 6750 O O    B DMS   C 2 .   ? 11.224 3.053   1.899   0.70 28.17 ?  301 DMS   A O    1 
HETATM 6751 C C1   B DMS   C 2 .   ? 9.031  4.114   2.950   0.70 30.62 ?  301 DMS   A C1   1 
HETATM 6752 C C2   B DMS   C 2 .   ? 11.468 5.474   3.132   0.70 30.07 ?  301 DMS   A C2   1 
HETATM 6753 H H11  B DMS   C 2 .   ? 8.689  4.377   3.891   0.70 36.74 ?  301 DMS   A H11  1 
HETATM 6754 H H12  B DMS   C 2 .   ? 8.587  3.260   2.570   0.70 36.74 ?  301 DMS   A H12  1 
HETATM 6755 H H13  B DMS   C 2 .   ? 8.992  4.893   2.270   0.70 36.74 ?  301 DMS   A H13  1 
HETATM 6756 H H21  B DMS   C 2 .   ? 10.941 5.974   2.391   0.70 36.08 ?  301 DMS   A H21  1 
HETATM 6757 H H22  B DMS   C 2 .   ? 12.491 5.418   2.915   0.70 36.08 ?  301 DMS   A H22  1 
HETATM 6758 H H23  B DMS   C 2 .   ? 11.288 5.847   4.080   0.70 36.08 ?  301 DMS   A H23  1 
HETATM 6759 N N2   B A1BBS D 3 .   ? 14.574 0.019   4.191   0.70 11.48 ?  302 A1BBS A N2   1 
HETATM 6760 C C3   B A1BBS D 3 .   ? 12.710 0.391   -0.714  0.70 18.08 ?  302 A1BBS A C3   1 
HETATM 6761 C C6   B A1BBS D 3 .   ? 14.731 2.334   1.178   0.70 14.62 ?  302 A1BBS A C6   1 
HETATM 6762 C C9   B A1BBS D 3 .   ? 15.094 2.199   5.665   0.70 11.42 ?  302 A1BBS A C9   1 
HETATM 6763 C C12  B A1BBS D 3 .   ? 15.398 4.383   5.283   0.70 11.99 ?  302 A1BBS A C12  1 
HETATM 6764 C C1   B A1BBS D 3 .   ? 12.662 -0.519  1.636   0.70 15.93 ?  302 A1BBS A C1   1 
HETATM 6765 C C10  B A1BBS D 3 .   ? 14.959 2.381   4.263   0.70 11.95 ?  302 A1BBS A C10  1 
HETATM 6766 C C11  B A1BBS D 3 .   ? 15.165 3.796   4.059   0.70 12.62 ?  302 A1BBS A C11  1 
HETATM 6767 C C13  B A1BBS D 3 .   ? 14.040 0.095   1.384   0.70 15.14 ?  302 A1BBS A C13  1 
HETATM 6768 C C2   B A1BBS D 3 .   ? 12.127 -0.706  0.170   0.70 17.58 ?  302 A1BBS A C2   1 
HETATM 6769 C C4   B A1BBS D 3 .   ? 14.108 0.464   -0.167  0.70 16.47 ?  302 A1BBS A C4   1 
HETATM 6770 C C5   B A1BBS D 3 .   ? 14.832 1.779   -0.272  0.70 15.84 ?  302 A1BBS A C5   1 
HETATM 6771 C C7   B A1BBS D 3 .   ? 14.680 1.195   3.534   0.70 12.07 ?  302 A1BBS A C7   1 
HETATM 6772 C C8   B A1BBS D 3 .   ? 14.732 -0.007  5.543   0.70 11.03 ?  302 A1BBS A C8   1 
HETATM 6773 N N1   B A1BBS D 3 .   ? 14.532 1.217   2.168   0.70 13.54 ?  302 A1BBS A N1   1 
HETATM 6774 N N3   B A1BBS D 3 .   ? 14.982 1.020   6.329   0.70 11.16 ?  302 A1BBS A N3   1 
HETATM 6775 N N4   B A1BBS D 3 .   ? 15.345 3.400   6.275   0.70 11.80 ?  302 A1BBS A N4   1 
HETATM 6776 O O1   B A1BBS D 3 .   ? 11.886 0.341   2.442   0.70 15.39 ?  302 A1BBS A O1   1 
HETATM 6777 H H8   B A1BBS D 3 .   ? 12.706 0.212   -1.810  0.70 21.69 ?  302 A1BBS A H8   1 
HETATM 6778 H H7   B A1BBS D 3 .   ? 12.204 1.384   -0.708  0.70 21.69 ?  302 A1BBS A H7   1 
HETATM 6779 H H11  B A1BBS D 3 .   ? 14.012 3.175   1.232   0.70 17.55 ?  302 A1BBS A H11  1 
HETATM 6780 H H12  B A1BBS D 3 .   ? 15.723 2.782   1.435   0.70 17.55 ?  302 A1BBS A H12  1 
HETATM 6781 H H15  B A1BBS D 3 .   ? 15.603 5.404   5.610   0.70 14.39 ?  302 A1BBS A H15  1 
HETATM 6782 H H1   B A1BBS D 3 .   ? 12.844 -1.468  2.168   0.70 19.12 ?  302 A1BBS A H1   1 
HETATM 6783 H H14  B A1BBS D 3 .   ? 15.153 4.379   3.148   0.70 15.14 ?  302 A1BBS A H14  1 
HETATM 6784 H H3   B A1BBS D 3 .   ? 14.796 -0.675  1.648   0.70 18.17 ?  302 A1BBS A H3   1 
HETATM 6785 H H6   B A1BBS D 3 .   ? 12.348 -1.728  -0.216  0.70 21.09 ?  302 A1BBS A H6   1 
HETATM 6786 H H5   B A1BBS D 3 .   ? 11.015 -0.679  0.168   0.70 21.09 ?  302 A1BBS A H5   1 
HETATM 6787 H H2   B A1BBS D 3 .   ? 14.708 -0.262  -0.759  0.70 19.76 ?  302 A1BBS A H2   1 
HETATM 6788 H H10  B A1BBS D 3 .   ? 14.429 2.390   -1.113  0.70 19.01 ?  302 A1BBS A H10  1 
HETATM 6789 H H9   B A1BBS D 3 .   ? 15.862 1.600   -0.680  0.70 19.01 ?  302 A1BBS A H9   1 
HETATM 6790 H H13  B A1BBS D 3 .   ? 14.628 -0.960  6.110   0.70 13.23 ?  302 A1BBS A H13  1 
HETATM 6791 H H16  B A1BBS D 3 .   ? 15.498 3.570   7.274   0.70 14.16 ?  302 A1BBS A H16  1 
HETATM 6792 H H4   B A1BBS D 3 .   ? 12.279 0.378   3.302   0.70 18.47 ?  302 A1BBS A H4   1 
HETATM 6793 O O    . HOH   E 4 .   ? 6.818  -8.273  11.516  1.00 22.05 ?  401 HOH   A O    1 
HETATM 6794 O O    . HOH   E 4 .   ? 28.823 0.377   -9.768  1.00 20.83 ?  402 HOH   A O    1 
HETATM 6795 O O    A HOH   E 4 .   ? 4.585  3.888   0.635   0.30 23.24 ?  403 HOH   A O    1 
HETATM 6796 O O    . HOH   E 4 .   ? 10.543 -22.371 -1.210  1.00 48.29 ?  404 HOH   A O    1 
HETATM 6797 O O    . HOH   E 4 .   ? 23.922 -15.742 -9.188  1.00 37.35 ?  405 HOH   A O    1 
HETATM 6798 O O    . HOH   E 4 .   ? 1.043  -4.171  -0.249  1.00 30.20 ?  406 HOH   A O    1 
HETATM 6799 O O    A HOH   E 4 .   ? 14.678 -4.680  20.419  0.30 26.48 ?  407 HOH   A O    1 
HETATM 6800 O O    . HOH   E 4 .   ? 34.298 -1.908  12.471  1.00 34.51 ?  408 HOH   A O    1 
HETATM 6801 O O    . HOH   E 4 .   ? 14.864 -12.117 18.669  1.00 41.42 ?  409 HOH   A O    1 
HETATM 6802 O O    . HOH   E 4 .   ? 13.659 -15.475 -7.751  1.00 31.59 ?  410 HOH   A O    1 
HETATM 6803 O O    A HOH   E 4 .   ? -0.722 -8.540  2.375   0.30 23.69 ?  411 HOH   A O    1 
HETATM 6804 O O    . HOH   E 4 .   ? 20.042 -12.591 -8.805  1.00 31.75 ?  412 HOH   A O    1 
HETATM 6805 O O    . HOH   E 4 .   ? 17.048 -17.954 14.844  1.00 30.61 ?  413 HOH   A O    1 
HETATM 6806 O O    . HOH   E 4 .   ? 9.611  -16.414 -2.487  1.00 34.43 ?  414 HOH   A O    1 
HETATM 6807 O O    . HOH   E 4 .   ? 7.960  -21.404 3.831   1.00 48.56 ?  415 HOH   A O    1 
HETATM 6808 O O    . HOH   E 4 .   ? 14.725 3.639   17.699  1.00 34.35 ?  416 HOH   A O    1 
HETATM 6809 O O    . HOH   E 4 .   ? 28.192 -0.187  -13.374 1.00 35.79 ?  417 HOH   A O    1 
HETATM 6810 O O    B HOH   E 4 .   ? 5.159  3.393   0.043   0.70 19.09 ?  418 HOH   A O    1 
HETATM 6811 O O    A HOH   E 4 .   ? 13.988 -4.558  -11.735 0.30 20.31 ?  419 HOH   A O    1 
HETATM 6812 O O    . HOH   E 4 .   ? 26.637 11.393  1.739   1.00 16.66 ?  420 HOH   A O    1 
HETATM 6813 O O    . HOH   E 4 .   ? 18.632 -19.438 13.442  1.00 31.82 ?  421 HOH   A O    1 
HETATM 6814 O O    . HOH   E 4 .   ? 30.181 -13.244 -8.469  1.00 30.22 ?  422 HOH   A O    1 
HETATM 6815 O O    . HOH   E 4 .   ? 42.258 10.500  5.219   1.00 20.82 ?  423 HOH   A O    1 
HETATM 6816 O O    . HOH   E 4 .   ? 14.675 -13.864 16.835  1.00 28.73 ?  424 HOH   A O    1 
HETATM 6817 O O    . HOH   E 4 .   ? 8.877  -10.242 19.173  1.00 41.99 ?  425 HOH   A O    1 
HETATM 6818 O O    . HOH   E 4 .   ? 22.472 -11.976 21.935  1.00 54.79 ?  426 HOH   A O    1 
HETATM 6819 O O    . HOH   E 4 .   ? 28.075 -6.304  19.640  1.00 41.99 ?  427 HOH   A O    1 
HETATM 6820 O O    . HOH   E 4 .   ? 36.128 -5.107  -0.463  1.00 29.82 ?  428 HOH   A O    1 
HETATM 6821 O O    . HOH   E 4 .   ? 14.414 -0.475  -12.386 1.00 38.26 ?  429 HOH   A O    1 
HETATM 6822 O O    . HOH   E 4 .   ? 18.799 -0.679  -1.804  1.00 29.56 ?  430 HOH   A O    1 
HETATM 6823 O O    . HOH   E 4 .   ? 17.305 -1.580  0.314   1.00 38.53 ?  431 HOH   A O    1 
HETATM 6824 O O    . HOH   E 4 .   ? 22.127 -19.357 11.244  1.00 33.27 ?  432 HOH   A O    1 
HETATM 6825 O O    B HOH   E 4 .   ? 12.390 -0.097  -6.339  0.70 42.71 ?  433 HOH   A O    1 
HETATM 6826 O O    . HOH   E 4 .   ? 33.825 -0.994  -8.898  1.00 26.79 ?  434 HOH   A O    1 
HETATM 6827 O O    . HOH   E 4 .   ? 19.411 -11.267 24.194  1.00 74.29 ?  435 HOH   A O    1 
HETATM 6828 O O    B HOH   E 4 .   ? 14.557 7.094   7.718   0.70 22.85 ?  436 HOH   A O    1 
HETATM 6829 O O    . HOH   E 4 .   ? 19.010 -21.958 6.996   1.00 38.18 ?  437 HOH   A O    1 
HETATM 6830 O O    . HOH   E 4 .   ? 9.944  -21.355 5.720   1.00 25.10 ?  438 HOH   A O    1 
HETATM 6831 O O    . HOH   E 4 .   ? 25.590 -0.821  -7.447  1.00 19.01 ?  439 HOH   A O    1 
HETATM 6832 O O    . HOH   E 4 .   ? 30.922 -18.114 7.777   1.00 18.75 ?  440 HOH   A O    1 
HETATM 6833 O O    . HOH   E 4 .   ? 28.495 -10.625 -14.036 1.00 44.95 ?  441 HOH   A O    1 
HETATM 6834 O O    . HOH   E 4 .   ? 26.435 -19.300 -1.855  1.00 14.80 ?  442 HOH   A O    1 
HETATM 6835 O O    . HOH   E 4 .   ? 27.275 13.756  2.961   1.00 29.94 ?  443 HOH   A O    1 
HETATM 6836 O O    . HOH   E 4 .   ? 11.825 0.314   14.736  1.00 32.86 ?  444 HOH   A O    1 
HETATM 6837 O O    . HOH   E 4 .   ? 20.613 -19.696 -5.236  1.00 32.52 ?  445 HOH   A O    1 
HETATM 6838 O O    . HOH   E 4 .   ? 22.097 5.266   18.927  1.00 36.29 ?  446 HOH   A O    1 
HETATM 6839 O O    . HOH   E 4 .   ? 21.131 -2.310  -2.399  1.00 16.12 ?  447 HOH   A O    1 
HETATM 6840 O O    . HOH   E 4 .   ? 37.441 2.803   10.198  1.00 28.54 ?  448 HOH   A O    1 
HETATM 6841 O O    . HOH   E 4 .   ? 37.088 11.905  5.021   1.00 30.55 ?  449 HOH   A O    1 
HETATM 6842 O O    B HOH   E 4 .   ? 20.985 2.520   0.180   0.70 14.33 ?  450 HOH   A O    1 
HETATM 6843 O O    B HOH   E 4 .   ? 14.911 -2.693  3.428   0.70 12.54 ?  451 HOH   A O    1 
HETATM 6844 O O    . HOH   E 4 .   ? 38.139 10.046  7.164   1.00 37.41 ?  452 HOH   A O    1 
HETATM 6845 O O    . HOH   E 4 .   ? 38.399 4.896   6.957   1.00 15.33 ?  453 HOH   A O    1 
HETATM 6846 O O    . HOH   E 4 .   ? 10.750 1.687   12.501  1.00 24.32 ?  454 HOH   A O    1 
HETATM 6847 O O    . HOH   E 4 .   ? 44.152 7.087   6.440   1.00 28.12 ?  455 HOH   A O    1 
HETATM 6848 O O    . HOH   E 4 .   ? 14.405 -21.303 -4.350  1.00 32.10 ?  456 HOH   A O    1 
HETATM 6849 O O    A HOH   E 4 .   ? 14.167 0.539   6.816   0.30 24.75 ?  457 HOH   A O    1 
HETATM 6850 O O    . HOH   E 4 .   ? 31.705 -9.308  -6.717  1.00 22.14 ?  458 HOH   A O    1 
HETATM 6851 O O    A HOH   E 4 .   ? 14.537 -3.675  3.099   0.30 19.83 ?  459 HOH   A O    1 
HETATM 6852 O O    A HOH   E 4 .   ? -0.576 -3.138  3.090   0.30 25.08 ?  460 HOH   A O    1 
HETATM 6853 O O    . HOH   E 4 .   ? 8.038  -12.526 -1.230  1.00 23.14 ?  461 HOH   A O    1 
HETATM 6854 O O    . HOH   E 4 .   ? 11.450 -10.728 16.844  1.00 26.16 ?  462 HOH   A O    1 
HETATM 6855 O O    . HOH   E 4 .   ? 24.218 3.576   -1.785  1.00 18.84 ?  463 HOH   A O    1 
HETATM 6856 O O    . HOH   E 4 .   ? 14.302 -24.573 11.644  1.00 42.59 ?  464 HOH   A O    1 
HETATM 6857 O O    . HOH   E 4 .   ? 31.553 8.152   14.894  1.00 25.14 ?  465 HOH   A O    1 
HETATM 6858 O O    A HOH   E 4 .   ? 19.995 4.568   -7.511  0.30 13.29 ?  466 HOH   A O    1 
HETATM 6859 O O    . HOH   E 4 .   ? 22.660 12.417  1.590   1.00 16.92 ?  467 HOH   A O    1 
HETATM 6860 O O    . HOH   E 4 .   ? 17.186 -17.884 -5.114  1.00 31.27 ?  468 HOH   A O    1 
HETATM 6861 O O    A HOH   E 4 .   ? 13.215 -1.425  -6.516  0.30 17.24 ?  469 HOH   A O    1 
HETATM 6862 O O    . HOH   E 4 .   ? 23.311 11.320  4.194   1.00 12.93 ?  470 HOH   A O    1 
HETATM 6863 O O    . HOH   E 4 .   ? 43.169 7.782   2.718   1.00 28.74 ?  471 HOH   A O    1 
HETATM 6864 O O    . HOH   E 4 .   ? 37.093 -2.825  9.718   1.00 42.35 ?  472 HOH   A O    1 
HETATM 6865 O O    . HOH   E 4 .   ? 31.011 -13.897 -2.506  1.00 13.59 ?  473 HOH   A O    1 
HETATM 6866 O O    . HOH   E 4 .   ? 35.708 -12.635 6.813   1.00 15.15 ?  474 HOH   A O    1 
HETATM 6867 O O    . HOH   E 4 .   ? 23.893 -2.129  -2.158  1.00 10.82 ?  475 HOH   A O    1 
HETATM 6868 O O    . HOH   E 4 .   ? 39.606 -1.007  -5.228  1.00 19.50 ?  476 HOH   A O    1 
HETATM 6869 O O    B HOH   E 4 .   ? 19.575 3.935   -9.707  0.70 37.55 ?  477 HOH   A O    1 
HETATM 6870 O O    . HOH   E 4 .   ? 18.425 9.337   9.189   1.00 25.91 ?  478 HOH   A O    1 
HETATM 6871 O O    B HOH   E 4 .   ? 9.700  3.341   -0.698  0.70 26.93 ?  479 HOH   A O    1 
HETATM 6872 O O    B HOH   E 4 .   ? 11.561 6.467   10.584  0.70 24.75 ?  480 HOH   A O    1 
HETATM 6873 O O    . HOH   E 4 .   ? 37.951 -1.357  -1.975  1.00 17.81 ?  481 HOH   A O    1 
HETATM 6874 O O    . HOH   E 4 .   ? 30.664 3.026   8.276   1.00 11.98 ?  482 HOH   A O    1 
HETATM 6875 O O    . HOH   E 4 .   ? 42.406 4.210   5.280   1.00 31.75 ?  483 HOH   A O    1 
HETATM 6876 O O    . HOH   E 4 .   ? 21.835 -21.922 8.383   1.00 29.63 ?  484 HOH   A O    1 
HETATM 6877 O O    . HOH   E 4 .   ? 43.790 8.473   -3.053  1.00 25.55 ?  485 HOH   A O    1 
HETATM 6878 O O    . HOH   E 4 .   ? 33.551 -7.159  4.246   1.00 15.77 ?  486 HOH   A O    1 
HETATM 6879 O O    . HOH   E 4 .   ? 27.415 -10.652 14.066  1.00 17.39 ?  487 HOH   A O    1 
HETATM 6880 O O    . HOH   E 4 .   ? 24.235 -7.838  14.459  1.00 16.63 ?  488 HOH   A O    1 
HETATM 6881 O O    . HOH   E 4 .   ? 21.140 10.169  15.168  1.00 33.56 ?  489 HOH   A O    1 
HETATM 6882 O O    . HOH   E 4 .   ? 31.770 -7.221  -9.827  1.00 20.69 ?  490 HOH   A O    1 
HETATM 6883 O O    . HOH   E 4 .   ? 13.613 -4.939  17.214  1.00 27.37 ?  491 HOH   A O    1 
HETATM 6884 O O    . HOH   E 4 .   ? 17.037 -19.305 4.828   1.00 16.61 ?  492 HOH   A O    1 
HETATM 6885 O O    A HOH   E 4 .   ? 3.506  -9.526  9.702   0.30 18.89 ?  493 HOH   A O    1 
HETATM 6886 O O    A HOH   E 4 .   ? 15.129 -7.969  -9.662  0.30 19.69 ?  494 HOH   A O    1 
HETATM 6887 O O    . HOH   E 4 .   ? 16.260 -14.275 20.244  1.00 60.38 ?  495 HOH   A O    1 
HETATM 6888 O O    . HOH   E 4 .   ? 8.871  -11.986 17.200  1.00 37.18 ?  496 HOH   A O    1 
HETATM 6889 O O    . HOH   E 4 .   ? 32.691 -9.272  5.924   1.00 18.67 ?  497 HOH   A O    1 
HETATM 6890 O O    . HOH   E 4 .   ? 24.650 -17.598 12.631  1.00 23.36 ?  498 HOH   A O    1 
HETATM 6891 O O    . HOH   E 4 .   ? 6.486  -3.373  12.757  1.00 33.12 ?  499 HOH   A O    1 
HETATM 6892 O O    . HOH   E 4 .   ? 37.413 -2.041  5.742   1.00 27.18 ?  500 HOH   A O    1 
HETATM 6893 O O    . HOH   E 4 .   ? 14.036 -23.037 7.422   1.00 20.12 ?  501 HOH   A O    1 
HETATM 6894 O O    A HOH   E 4 .   ? 24.483 2.072   -6.957  0.30 11.71 ?  502 HOH   A O    1 
HETATM 6895 O O    A HOH   E 4 .   ? 10.964 -0.403  1.943   0.30 23.43 ?  503 HOH   A O    1 
HETATM 6896 O O    . HOH   E 4 .   ? 15.122 -21.460 14.229  1.00 21.61 ?  504 HOH   A O    1 
HETATM 6897 O O    . HOH   E 4 .   ? 26.780 4.139   -0.646  1.00 12.07 ?  505 HOH   A O    1 
HETATM 6898 O O    . HOH   E 4 .   ? 27.756 0.839   -7.181  1.00 14.49 ?  506 HOH   A O    1 
HETATM 6899 O O    . HOH   E 4 .   ? 16.161 16.711  8.565   1.00 48.18 ?  507 HOH   A O    1 
HETATM 6900 O O    . HOH   E 4 .   ? 30.824 6.196   -12.273 1.00 30.27 ?  508 HOH   A O    1 
HETATM 6901 O O    A HOH   E 4 .   ? 15.696 -0.971  5.282   0.30 30.00 ?  509 HOH   A O    1 
HETATM 6902 O O    A HOH   E 4 .   ? 21.241 3.158   -0.318  0.30 10.69 ?  510 HOH   A O    1 
HETATM 6903 O O    . HOH   E 4 .   ? 23.788 3.933   -4.731  1.00 25.87 ?  511 HOH   A O    1 
HETATM 6904 O O    B HOH   E 4 .   ? 3.380  2.924   -1.829  0.70 26.53 ?  512 HOH   A O    1 
HETATM 6905 O O    . HOH   E 4 .   ? 16.468 -22.087 1.049   1.00 34.62 ?  513 HOH   A O    1 
HETATM 6906 O O    . HOH   E 4 .   ? 27.284 2.216   18.810  1.00 29.15 ?  514 HOH   A O    1 
HETATM 6907 O O    . HOH   E 4 .   ? 27.471 -6.208  -13.993 1.00 35.74 ?  515 HOH   A O    1 
HETATM 6908 O O    . HOH   E 4 .   ? 30.664 1.753   16.687  1.00 20.34 ?  516 HOH   A O    1 
HETATM 6909 O O    . HOH   E 4 .   ? 20.529 -20.060 2.678   1.00 20.06 ?  517 HOH   A O    1 
HETATM 6910 O O    . HOH   E 4 .   ? 22.604 7.891   18.456  1.00 41.89 ?  518 HOH   A O    1 
HETATM 6911 O O    . HOH   E 4 .   ? 30.250 -12.940 13.512  1.00 19.79 ?  519 HOH   A O    1 
HETATM 6912 O O    A HOH   E 4 .   ? 18.489 -2.409  -16.329 0.30 23.21 ?  520 HOH   A O    1 
HETATM 6913 O O    . HOH   E 4 .   ? 26.937 -3.244  19.454  1.00 35.90 ?  521 HOH   A O    1 
HETATM 6914 O O    A HOH   E 4 .   ? 6.366  -5.667  11.166  0.30 12.87 ?  522 HOH   A O    1 
HETATM 6915 O O    . HOH   E 4 .   ? 29.997 -10.196 13.000  1.00 22.00 ?  523 HOH   A O    1 
HETATM 6916 O O    . HOH   E 4 .   ? 34.886 -5.196  -3.057  1.00 18.17 ?  524 HOH   A O    1 
HETATM 6917 O O    . HOH   E 4 .   ? 15.822 6.954   2.865   1.00 12.88 ?  525 HOH   A O    1 
HETATM 6918 O O    . HOH   E 4 .   ? 10.434 -13.867 -1.879  1.00 20.11 ?  526 HOH   A O    1 
HETATM 6919 O O    . HOH   E 4 .   ? 32.589 -4.385  -9.925  1.00 26.14 ?  527 HOH   A O    1 
HETATM 6920 O O    . HOH   E 4 .   ? 7.484  -6.217  -6.659  1.00 49.15 ?  528 HOH   A O    1 
HETATM 6921 O O    A HOH   E 4 .   ? 5.192  2.593   5.287   0.30 23.78 ?  529 HOH   A O    1 
HETATM 6922 O O    . HOH   E 4 .   ? 41.502 1.542   4.946   1.00 37.19 ?  530 HOH   A O    1 
HETATM 6923 O O    . HOH   E 4 .   ? 36.640 -4.959  5.325   1.00 23.59 ?  531 HOH   A O    1 
HETATM 6924 O O    . HOH   E 4 .   ? 21.721 -13.889 -8.228  1.00 48.49 ?  532 HOH   A O    1 
HETATM 6925 O O    . HOH   E 4 .   ? 32.425 -10.638 3.204   1.00 29.95 ?  533 HOH   A O    1 
HETATM 6926 O O    . HOH   E 4 .   ? 18.310 -15.900 16.162  1.00 41.27 ?  534 HOH   A O    1 
HETATM 6927 O O    . HOH   E 4 .   ? 40.867 -8.174  -6.817  1.00 34.45 ?  535 HOH   A O    1 
HETATM 6928 O O    . HOH   E 4 .   ? 23.893 -20.248 -1.411  1.00 17.97 ?  536 HOH   A O    1 
HETATM 6929 O O    . HOH   E 4 .   ? 15.371 11.723  7.988   1.00 53.81 ?  537 HOH   A O    1 
HETATM 6930 O O    A HOH   E 4 .   ? 15.737 2.112   24.809  0.30 33.88 ?  538 HOH   A O    1 
HETATM 6931 O O    A HOH   E 4 .   ? 18.337 4.891   -14.994 0.30 32.79 ?  539 HOH   A O    1 
HETATM 6932 O O    B HOH   E 4 .   ? 5.530  3.114   4.266   0.70 23.84 ?  540 HOH   A O    1 
HETATM 6933 O O    . HOH   E 4 .   ? 23.614 -8.144  17.047  1.00 22.42 ?  541 HOH   A O    1 
HETATM 6934 O O    B HOH   E 4 .   ? 6.067  -0.139  -2.384  0.70 36.47 ?  542 HOH   A O    1 
HETATM 6935 O O    A HOH   E 4 .   ? 18.759 2.033   -0.726  0.30 9.64  ?  543 HOH   A O    1 
HETATM 6936 O O    . HOH   E 4 .   ? 44.795 -0.577  3.098   1.00 37.60 ?  544 HOH   A O    1 
HETATM 6937 O O    B HOH   E 4 .   ? 15.227 -5.776  -4.270  0.70 44.64 ?  545 HOH   A O    1 
HETATM 6938 O O    B HOH   E 4 .   ? 11.514 -0.434  -3.587  0.70 40.87 ?  546 HOH   A O    1 
HETATM 6939 O O    . HOH   E 4 .   ? 23.339 -20.994 1.209   1.00 19.06 ?  547 HOH   A O    1 
HETATM 6940 O O    . HOH   E 4 .   ? 37.615 -8.755  -3.317  1.00 24.25 ?  548 HOH   A O    1 
HETATM 6941 O O    . HOH   E 4 .   ? 20.567 -17.800 24.736  1.00 61.15 ?  549 HOH   A O    1 
HETATM 6942 O O    B HOH   E 4 .   ? 16.902 6.424   -2.663  0.70 28.35 ?  550 HOH   A O    1 
HETATM 6943 O O    . HOH   E 4 .   ? 31.251 -12.810 0.001   1.00 19.44 ?  551 HOH   A O    1 
HETATM 6944 O O    . HOH   E 4 .   ? 34.206 -8.192  -0.524  1.00 30.30 ?  552 HOH   A O    1 
HETATM 6945 O O    . HOH   E 4 .   ? 21.414 -14.788 17.945  1.00 64.03 ?  553 HOH   A O    1 
HETATM 6946 O O    B HOH   E 4 .   ? 20.201 4.153   -2.232  0.70 25.88 ?  554 HOH   A O    1 
HETATM 6947 O O    B HOH   E 4 .   ? 17.085 3.429   -2.593  0.70 28.31 ?  555 HOH   A O    1 
HETATM 6948 O O    B HOH   E 4 .   ? 18.214 1.420   -0.005  0.70 23.90 ?  556 HOH   A O    1 
HETATM 6949 O O    . HOH   E 4 .   ? 30.404 14.705  2.814   1.00 19.57 ?  557 HOH   A O    1 
HETATM 6950 O O    A HOH   E 4 .   ? 16.153 2.946   -1.415  0.30 20.16 ?  558 HOH   A O    1 
HETATM 6951 O O    A HOH   E 4 .   ? 13.924 -0.361  3.474   0.30 26.20 ?  559 HOH   A O    1 
HETATM 6952 O O    . HOH   E 4 .   ? 23.113 7.443   -3.295  1.00 37.11 ?  560 HOH   A O    1 
HETATM 6953 O O    B HOH   E 4 .   ? 4.033  2.357   2.231   0.70 18.45 ?  561 HOH   A O    1 
HETATM 6954 O O    . HOH   E 4 .   ? 29.775 -16.094 10.650  1.00 30.64 ?  562 HOH   A O    1 
HETATM 6955 O O    . HOH   E 4 .   ? 24.734 5.538   20.769  1.00 53.40 ?  563 HOH   A O    1 
HETATM 6956 O O    A HOH   E 4 .   ? -1.529 -5.007  7.628   0.30 29.42 ?  564 HOH   A O    1 
HETATM 6957 O O    . HOH   E 4 .   ? 21.383 -9.238  21.419  1.00 57.10 ?  565 HOH   A O    1 
HETATM 6958 O O    . HOH   E 4 .   ? 29.654 -1.983  -12.880 1.00 48.22 ?  566 HOH   A O    1 
HETATM 6959 O O    . HOH   E 4 .   ? 19.949 -17.417 -5.228  1.00 31.37 ?  567 HOH   A O    1 
HETATM 6960 O O    . HOH   E 4 .   ? 11.836 -11.451 -10.525 1.00 55.19 ?  568 HOH   A O    1 
HETATM 6961 O O    . HOH   E 4 .   ? 25.344 8.265   -4.826  1.00 38.71 ?  569 HOH   A O    1 
HETATM 6962 O O    . HOH   E 4 .   ? 27.679 7.143   -6.536  1.00 33.56 ?  570 HOH   A O    1 
HETATM 6963 O O    . HOH   E 4 .   ? 32.293 -16.040 10.850  1.00 36.84 ?  571 HOH   A O    1 
HETATM 6964 O O    . HOH   E 4 .   ? 26.771 11.499  -1.250  1.00 34.23 ?  572 HOH   A O    1 
HETATM 6965 O O    . HOH   E 4 .   ? 23.173 -22.288 -3.407  1.00 34.14 ?  573 HOH   A O    1 
HETATM 6966 O O    . HOH   E 4 .   ? 39.569 -6.983  -3.519  1.00 43.57 ?  574 HOH   A O    1 
HETATM 6967 O O    . HOH   E 4 .   ? 18.782 10.853  11.484  1.00 32.64 ?  575 HOH   A O    1 
HETATM 6968 O O    . HOH   E 4 .   ? 24.398 14.539  7.899   1.00 37.48 ?  576 HOH   A O    1 
HETATM 6969 O O    . HOH   E 4 .   ? 11.286 -15.091 -6.298  1.00 33.69 ?  577 HOH   A O    1 
HETATM 6970 O O    . HOH   E 4 .   ? 11.863 -13.375 16.216  1.00 53.19 ?  578 HOH   A O    1 
HETATM 6971 O O    . HOH   E 4 .   ? 27.346 -11.384 16.586  1.00 37.47 ?  579 HOH   A O    1 
HETATM 6972 O O    B HOH   E 4 .   ? 1.920  3.746   2.728   0.70 33.83 ?  580 HOH   A O    1 
HETATM 6973 O O    . HOH   E 4 .   ? 15.819 -21.595 3.729   1.00 25.57 ?  581 HOH   A O    1 
HETATM 6974 O O    . HOH   E 4 .   ? 12.178 1.541   17.328  1.00 43.98 ?  582 HOH   A O    1 
HETATM 6975 O O    A HOH   E 4 .   ? 21.859 5.290   -5.797  0.30 20.02 ?  583 HOH   A O    1 
HETATM 6976 O O    . HOH   E 4 .   ? 25.773 10.774  -3.628  1.00 28.94 ?  584 HOH   A O    1 
HETATM 6977 O O    . HOH   E 4 .   ? 18.172 -16.592 -8.909  1.00 49.73 ?  585 HOH   A O    1 
HETATM 6978 O O    . HOH   E 4 .   ? 23.269 13.621  5.595   1.00 21.20 ?  586 HOH   A O    1 
HETATM 6979 O O    . HOH   E 4 .   ? 15.971 -7.014  -11.937 1.00 55.49 ?  587 HOH   A O    1 
HETATM 6980 O O    . HOH   E 4 .   ? 15.962 -17.443 -7.121  1.00 40.03 ?  588 HOH   A O    1 
HETATM 6981 O O    . HOH   E 4 .   ? 35.011 7.369   12.309  1.00 47.51 ?  589 HOH   A O    1 
HETATM 6982 O O    . HOH   E 4 .   ? 28.758 8.882   17.563  1.00 35.28 ?  590 HOH   A O    1 
HETATM 6983 O O    . HOH   E 4 .   ? 17.287 -18.640 19.700  1.00 56.58 ?  591 HOH   A O    1 
HETATM 6984 O O    . HOH   E 4 .   ? 40.865 -3.876  -0.452  1.00 42.32 ?  592 HOH   A O    1 
HETATM 6985 O O    . HOH   E 4 .   ? 28.552 -4.668  -12.281 1.00 36.10 ?  593 HOH   A O    1 
HETATM 6986 O O    . HOH   E 4 .   ? 23.147 11.830  -4.108  1.00 23.64 ?  594 HOH   A O    1 
HETATM 6987 O O    . HOH   E 4 .   ? 16.861 -20.427 16.118  1.00 38.02 ?  595 HOH   A O    1 
HETATM 6988 O O    B HOH   E 4 .   ? 16.622 10.286  5.959   0.70 22.92 ?  596 HOH   A O    1 
HETATM 6989 O O    B HOH   E 4 .   ? 5.723  5.888   0.933   0.70 22.49 ?  597 HOH   A O    1 
HETATM 6990 O O    . HOH   E 4 .   ? 30.743 0.604   19.226  1.00 40.23 ?  598 HOH   A O    1 
HETATM 6991 O O    . HOH   E 4 .   ? 14.115 -10.427 -11.196 1.00 39.11 ?  599 HOH   A O    1 
HETATM 6992 O O    . HOH   E 4 .   ? 44.303 10.430  -1.576  1.00 36.40 ?  600 HOH   A O    1 
HETATM 6993 O O    . HOH   E 4 .   ? 20.590 -15.998 -7.597  1.00 30.79 ?  601 HOH   A O    1 
HETATM 6994 O O    B HOH   E 4 .   ? 18.988 7.784   -4.238  0.70 44.78 ?  602 HOH   A O    1 
HETATM 6995 O O    . HOH   E 4 .   ? 41.552 9.275   -4.114  1.00 30.96 ?  603 HOH   A O    1 
HETATM 6996 O O    . HOH   E 4 .   ? 39.067 2.334   7.453   1.00 32.35 ?  604 HOH   A O    1 
HETATM 6997 O O    . HOH   E 4 .   ? 31.357 -0.572  -10.560 1.00 26.78 ?  605 HOH   A O    1 
HETATM 6998 O O    . HOH   E 4 .   ? 25.790 -18.895 -12.080 1.00 42.38 ?  606 HOH   A O    1 
HETATM 6999 O O    . HOH   E 4 .   ? 13.825 -25.165 8.910   1.00 35.96 ?  607 HOH   A O    1 
HETATM 7000 O O    . HOH   E 4 .   ? 18.402 -23.230 1.871   1.00 41.30 ?  608 HOH   A O    1 
HETATM 7001 O O    . HOH   E 4 .   ? 23.215 -12.925 19.255  1.00 48.29 ?  609 HOH   A O    1 
HETATM 7002 O O    . HOH   E 4 .   ? 28.796 -7.930  -15.243 1.00 50.45 ?  610 HOH   A O    1 
HETATM 7003 O O    . HOH   E 4 .   ? 40.339 -0.246  -7.833  1.00 32.31 ?  611 HOH   A O    1 
HETATM 7004 O O    . HOH   E 4 .   ? 20.089 -22.357 4.233   1.00 28.71 ?  612 HOH   A O    1 
HETATM 7005 O O    . HOH   E 4 .   ? 16.149 -23.442 5.823   1.00 31.77 ?  613 HOH   A O    1 
HETATM 7006 O O    . HOH   E 4 .   ? 37.314 -6.602  7.515   1.00 24.74 ?  614 HOH   A O    1 
HETATM 7007 O O    . HOH   E 4 .   ? 30.692 -5.741  -11.878 1.00 47.43 ?  615 HOH   A O    1 
HETATM 7008 O O    . HOH   E 4 .   ? 23.184 -23.804 1.627   1.00 32.39 ?  616 HOH   A O    1 
HETATM 7009 O O    B HOH   E 4 .   ? 14.485 7.837   5.014   0.70 16.44 ?  617 HOH   A O    1 
HETATM 7010 O O    . HOH   E 4 .   ? 30.620 5.770   -14.734 1.00 39.59 ?  618 HOH   A O    1 
HETATM 7011 O O    . HOH   E 4 .   ? 39.424 -0.059  6.607   1.00 29.88 ?  619 HOH   A O    1 
HETATM 7012 O O    . HOH   E 4 .   ? 37.890 13.793  6.774   1.00 48.72 ?  620 HOH   A O    1 
HETATM 7013 O O    . HOH   E 4 .   ? 28.855 14.307  0.850   1.00 49.68 ?  621 HOH   A O    1 
HETATM 7014 O O    B HOH   E 4 .   ? 9.949  0.635   -6.917  0.70 40.77 ?  622 HOH   A O    1 
HETATM 7015 O O    . HOH   E 4 .   ? 8.038  -3.033  -5.864  1.00 53.99 ?  623 HOH   A O    1 
HETATM 7016 O O    . HOH   E 4 .   ? 22.039 -24.053 4.362   1.00 30.26 ?  624 HOH   A O    1 
HETATM 7017 O O    . HOH   E 4 .   ? 36.330 -6.562  10.131  1.00 46.12 ?  625 HOH   A O    1 
HETATM 7018 O O    . HOH   E 4 .   ? 17.189 -7.215  -14.239 1.00 50.83 ?  626 HOH   A O    1 
HETATM 7019 O O    A HOH   E 4 .   ? 14.730 8.624   4.933   0.30 23.29 ?  627 HOH   A O    1 
HETATM 7020 O O    . HOH   E 4 .   ? 24.016 9.107   -7.179  1.00 42.41 ?  628 HOH   A O    1 
HETATM 7021 O O    . HOH   E 4 .   ? 15.773 -12.421 27.379  1.00 44.60 ?  629 HOH   A O    1 
HETATM 7022 O O    . HOH   E 4 .   ? 16.174 -21.137 18.717  1.00 45.02 ?  630 HOH   A O    1 
HETATM 7023 O O    . HOH   E 4 .   ? 14.634 -22.686 19.898  1.00 39.94 ?  631 HOH   A O    1 
HETATM 7024 O O    . HOH   F 4 .   ? 29.759 -22.348 5.380   1.00 21.48 ?  201 HOH   B O    1 
HETATM 7025 O O    . HOH   F 4 .   ? 27.799 -41.525 -15.260 1.00 32.70 ?  202 HOH   B O    1 
HETATM 7026 O O    . HOH   F 4 .   ? 27.604 -29.079 -2.023  1.00 35.77 ?  203 HOH   B O    1 
HETATM 7027 O O    . HOH   F 4 .   ? 48.093 -6.863  15.552  1.00 36.61 ?  204 HOH   B O    1 
HETATM 7028 O O    . HOH   F 4 .   ? 52.912 -13.350 -20.369 1.00 38.09 ?  205 HOH   B O    1 
HETATM 7029 O O    . HOH   F 4 .   ? 54.412 -9.362  -8.776  1.00 21.12 ?  206 HOH   B O    1 
HETATM 7030 O O    . HOH   F 4 .   ? 47.326 -7.410  -3.903  1.00 41.58 ?  207 HOH   B O    1 
HETATM 7031 O O    . HOH   F 4 .   ? 41.787 -35.880 -17.416 1.00 30.43 ?  208 HOH   B O    1 
HETATM 7032 O O    . HOH   F 4 .   ? 37.917 -39.408 -0.282  1.00 36.52 ?  209 HOH   B O    1 
HETATM 7033 O O    . HOH   F 4 .   ? 59.039 -18.730 6.839   1.00 34.76 ?  210 HOH   B O    1 
HETATM 7034 O O    . HOH   F 4 .   ? 41.297 -7.752  5.488   1.00 41.99 ?  211 HOH   B O    1 
HETATM 7035 O O    . HOH   F 4 .   ? 29.828 -26.265 3.912   1.00 28.86 ?  212 HOH   B O    1 
HETATM 7036 O O    . HOH   F 4 .   ? 49.397 -22.683 -19.737 1.00 48.94 ?  213 HOH   B O    1 
HETATM 7037 O O    . HOH   F 4 .   ? 44.408 -7.088  2.001   1.00 34.95 ?  214 HOH   B O    1 
HETATM 7038 O O    . HOH   F 4 .   ? 58.158 -12.983 8.342   1.00 33.03 ?  215 HOH   B O    1 
HETATM 7039 O O    . HOH   F 4 .   ? 30.152 -40.916 -8.173  1.00 15.65 ?  216 HOH   B O    1 
HETATM 7040 O O    . HOH   F 4 .   ? 50.181 -3.268  7.142   1.00 34.58 ?  217 HOH   B O    1 
HETATM 7041 O O    . HOH   F 4 .   ? 56.292 -19.711 7.322   1.00 32.72 ?  218 HOH   B O    1 
HETATM 7042 O O    . HOH   F 4 .   ? 56.632 -30.759 -7.868  1.00 28.52 ?  219 HOH   B O    1 
HETATM 7043 O O    . HOH   F 4 .   ? 57.604 -24.351 4.964   1.00 35.95 ?  220 HOH   B O    1 
HETATM 7044 O O    . HOH   F 4 .   ? 44.903 -43.486 -10.629 1.00 26.77 ?  221 HOH   B O    1 
HETATM 7045 O O    . HOH   F 4 .   ? 57.401 -16.216 -12.126 1.00 17.95 ?  222 HOH   B O    1 
HETATM 7046 O O    . HOH   F 4 .   ? 55.437 -16.420 -14.326 1.00 35.73 ?  223 HOH   B O    1 
HETATM 7047 O O    . HOH   F 4 .   ? 29.727 -34.155 -0.438  1.00 32.41 ?  224 HOH   B O    1 
HETATM 7048 O O    . HOH   F 4 .   ? 35.879 -43.136 -8.584  1.00 31.80 ?  225 HOH   B O    1 
HETATM 7049 O O    . HOH   F 4 .   ? 41.470 -39.102 -14.948 1.00 20.71 ?  226 HOH   B O    1 
HETATM 7050 O O    . HOH   F 4 .   ? 37.201 -19.569 -18.141 1.00 43.78 ?  227 HOH   B O    1 
HETATM 7051 O O    . HOH   F 4 .   ? 50.702 -6.031  0.271   1.00 26.93 ?  228 HOH   B O    1 
HETATM 7052 O O    . HOH   F 4 .   ? 48.056 -24.473 -17.713 1.00 28.99 ?  229 HOH   B O    1 
HETATM 7053 O O    . HOH   F 4 .   ? 34.954 -7.982  -2.912  1.00 18.92 ?  230 HOH   B O    1 
HETATM 7054 O O    . HOH   F 4 .   ? 41.306 -9.589  13.060  1.00 23.23 ?  231 HOH   B O    1 
HETATM 7055 O O    . HOH   F 4 .   ? 28.438 -19.580 -13.197 1.00 24.83 ?  232 HOH   B O    1 
HETATM 7056 O O    . HOH   F 4 .   ? 39.277 -10.870 6.125   1.00 22.05 ?  233 HOH   B O    1 
HETATM 7057 O O    . HOH   F 4 .   ? 34.478 -36.270 -7.218  1.00 17.06 ?  234 HOH   B O    1 
HETATM 7058 O O    . HOH   F 4 .   ? 40.579 -16.046 14.131  1.00 27.75 ?  235 HOH   B O    1 
HETATM 7059 O O    . HOH   F 4 .   ? 30.795 -28.701 4.269   1.00 25.98 ?  236 HOH   B O    1 
HETATM 7060 O O    . HOH   F 4 .   ? 25.402 -25.913 -1.376  1.00 32.92 ?  237 HOH   B O    1 
HETATM 7061 O O    . HOH   F 4 .   ? 51.652 -6.481  4.446   1.00 21.47 ?  238 HOH   B O    1 
HETATM 7062 O O    . HOH   F 4 .   ? 46.404 -1.540  13.246  1.00 29.61 ?  239 HOH   B O    1 
HETATM 7063 O O    . HOH   F 4 .   ? 50.678 -12.923 -0.468  1.00 11.85 ?  240 HOH   B O    1 
HETATM 7064 O O    . HOH   F 4 .   ? 58.090 -10.548 -4.007  1.00 21.80 ?  241 HOH   B O    1 
HETATM 7065 O O    . HOH   F 4 .   ? 43.606 -15.315 18.243  1.00 30.71 ?  242 HOH   B O    1 
HETATM 7066 O O    . HOH   F 4 .   ? 43.003 -43.161 -8.267  1.00 27.76 ?  243 HOH   B O    1 
HETATM 7067 O O    . HOH   F 4 .   ? 41.784 -23.451 9.313   1.00 16.35 ?  244 HOH   B O    1 
HETATM 7068 O O    . HOH   F 4 .   ? 33.460 -17.011 8.032   1.00 18.47 ?  245 HOH   B O    1 
HETATM 7069 O O    . HOH   F 4 .   ? 38.398 -11.012 -2.262  1.00 19.46 ?  246 HOH   B O    1 
HETATM 7070 O O    . HOH   F 4 .   ? 32.740 -43.717 -11.416 1.00 18.98 ?  247 HOH   B O    1 
HETATM 7071 O O    . HOH   F 4 .   ? 50.865 -39.939 -8.222  1.00 30.50 ?  248 HOH   B O    1 
HETATM 7072 O O    . HOH   F 4 .   ? 42.564 -22.826 3.839   1.00 11.26 ?  249 HOH   B O    1 
HETATM 7073 O O    . HOH   F 4 .   ? 44.464 -27.732 -0.724  1.00 21.25 ?  250 HOH   B O    1 
HETATM 7074 O O    . HOH   F 4 .   ? 42.491 -25.299 2.601   1.00 14.89 ?  251 HOH   B O    1 
HETATM 7075 O O    . HOH   F 4 .   ? 31.791 -17.786 -14.510 1.00 28.75 ?  252 HOH   B O    1 
HETATM 7076 O O    . HOH   F 4 .   ? 39.454 -11.067 0.319   1.00 16.91 ?  253 HOH   B O    1 
HETATM 7077 O O    . HOH   F 4 .   ? 27.090 -31.731 -9.989  1.00 23.35 ?  254 HOH   B O    1 
HETATM 7078 O O    . HOH   F 4 .   ? 34.194 -18.393 11.418  1.00 23.54 ?  255 HOH   B O    1 
HETATM 7079 O O    . HOH   F 4 .   ? 45.071 -34.894 6.772   1.00 38.77 ?  256 HOH   B O    1 
HETATM 7080 O O    . HOH   F 4 .   ? 29.697 -25.136 -10.865 1.00 15.92 ?  257 HOH   B O    1 
HETATM 7081 O O    . HOH   F 4 .   ? 42.338 -9.899  9.367   1.00 20.76 ?  258 HOH   B O    1 
HETATM 7082 O O    . HOH   F 4 .   ? 30.794 -15.703 2.624   1.00 13.43 ?  259 HOH   B O    1 
HETATM 7083 O O    . HOH   F 4 .   ? 49.265 -28.668 -6.963  1.00 14.88 ?  260 HOH   B O    1 
HETATM 7084 O O    . HOH   F 4 .   ? 40.326 -12.677 -11.511 1.00 15.20 ?  261 HOH   B O    1 
HETATM 7085 O O    . HOH   F 4 .   ? 57.608 -24.335 -3.822  1.00 21.39 ?  262 HOH   B O    1 
HETATM 7086 O O    . HOH   F 4 .   ? 43.176 -32.321 -17.154 1.00 22.41 ?  263 HOH   B O    1 
HETATM 7087 O O    . HOH   F 4 .   ? 56.915 -8.645  8.396   1.00 20.22 ?  264 HOH   B O    1 
HETATM 7088 O O    . HOH   F 4 .   ? 57.250 -26.804 -7.710  1.00 43.09 ?  265 HOH   B O    1 
HETATM 7089 O O    . HOH   F 4 .   ? 56.998 -12.211 12.353  1.00 41.58 ?  266 HOH   B O    1 
HETATM 7090 O O    . HOH   F 4 .   ? 56.153 -23.423 -14.655 1.00 26.34 ?  267 HOH   B O    1 
HETATM 7091 O O    . HOH   F 4 .   ? 42.287 -34.624 3.722   1.00 25.78 ?  268 HOH   B O    1 
HETATM 7092 O O    . HOH   F 4 .   ? 34.426 -12.774 2.618   1.00 23.23 ?  269 HOH   B O    1 
HETATM 7093 O O    . HOH   F 4 .   ? 38.854 -11.895 12.442  1.00 34.36 ?  270 HOH   B O    1 
HETATM 7094 O O    . HOH   F 4 .   ? 34.825 -24.541 13.841  1.00 28.81 ?  271 HOH   B O    1 
HETATM 7095 O O    . HOH   F 4 .   ? 46.534 -31.210 -4.847  1.00 17.96 ?  272 HOH   B O    1 
HETATM 7096 O O    . HOH   F 4 .   ? 42.849 -20.303 -20.804 1.00 41.28 ?  273 HOH   B O    1 
HETATM 7097 O O    . HOH   F 4 .   ? 34.867 -33.249 -19.283 1.00 25.76 ?  274 HOH   B O    1 
HETATM 7098 O O    . HOH   F 4 .   ? 47.929 -22.730 5.855   1.00 16.59 ?  275 HOH   B O    1 
HETATM 7099 O O    . HOH   F 4 .   ? 43.355 -15.763 -12.182 1.00 14.08 ?  276 HOH   B O    1 
HETATM 7100 O O    . HOH   F 4 .   ? 51.420 -13.767 11.053  1.00 25.47 ?  277 HOH   B O    1 
HETATM 7101 O O    . HOH   F 4 .   ? 48.515 -36.385 -15.633 1.00 42.84 ?  278 HOH   B O    1 
HETATM 7102 O O    . HOH   F 4 .   ? 28.235 -34.237 -9.435  1.00 20.57 ?  279 HOH   B O    1 
HETATM 7103 O O    . HOH   F 4 .   ? 57.418 -9.174  1.378   1.00 20.21 ?  280 HOH   B O    1 
HETATM 7104 O O    . HOH   F 4 .   ? 37.318 -35.650 7.046   1.00 31.66 ?  281 HOH   B O    1 
HETATM 7105 O O    . HOH   F 4 .   ? 49.906 -24.623 5.749   1.00 33.34 ?  282 HOH   B O    1 
HETATM 7106 O O    . HOH   F 4 .   ? 52.551 -10.360 12.988  1.00 22.89 ?  283 HOH   B O    1 
HETATM 7107 O O    . HOH   F 4 .   ? 41.038 -5.568  11.566  1.00 43.50 ?  284 HOH   B O    1 
HETATM 7108 O O    . HOH   F 4 .   ? 46.833 -29.408 9.710   1.00 30.65 ?  285 HOH   B O    1 
HETATM 7109 O O    . HOH   F 4 .   ? 27.922 -22.798 -8.060  1.00 17.20 ?  286 HOH   B O    1 
HETATM 7110 O O    . HOH   F 4 .   ? 36.747 -12.742 -1.523  1.00 24.28 ?  287 HOH   B O    1 
HETATM 7111 O O    . HOH   F 4 .   ? 48.355 -25.008 3.088   1.00 12.68 ?  288 HOH   B O    1 
HETATM 7112 O O    . HOH   F 4 .   ? 42.322 -9.890  -14.883 1.00 36.30 ?  289 HOH   B O    1 
HETATM 7113 O O    . HOH   F 4 .   ? 33.523 -15.232 -13.980 1.00 21.47 ?  290 HOH   B O    1 
HETATM 7114 O O    . HOH   F 4 .   ? 28.418 -30.859 -14.810 1.00 31.42 ?  291 HOH   B O    1 
HETATM 7115 O O    . HOH   F 4 .   ? 37.474 -18.093 13.078  1.00 28.69 ?  292 HOH   B O    1 
HETATM 7116 O O    . HOH   F 4 .   ? 27.590 -26.639 -15.740 1.00 33.02 ?  293 HOH   B O    1 
HETATM 7117 O O    . HOH   F 4 .   ? 47.000 -33.912 -4.663  1.00 16.94 ?  294 HOH   B O    1 
HETATM 7118 O O    . HOH   F 4 .   ? 48.641 -20.002 5.927   1.00 13.79 ?  295 HOH   B O    1 
HETATM 7119 O O    . HOH   F 4 .   ? 51.168 -37.607 -9.598  1.00 24.98 ?  296 HOH   B O    1 
HETATM 7120 O O    . HOH   F 4 .   ? 49.764 -0.433  10.288  1.00 30.37 ?  297 HOH   B O    1 
HETATM 7121 O O    . HOH   F 4 .   ? 62.603 -13.581 4.841   1.00 26.34 ?  298 HOH   B O    1 
HETATM 7122 O O    . HOH   F 4 .   ? 53.282 -16.119 -12.698 1.00 28.83 ?  299 HOH   B O    1 
HETATM 7123 O O    . HOH   F 4 .   ? 52.543 -35.589 -8.785  1.00 28.17 ?  300 HOH   B O    1 
HETATM 7124 O O    . HOH   F 4 .   ? 34.984 -33.541 4.449   1.00 29.26 ?  301 HOH   B O    1 
HETATM 7125 O O    . HOH   F 4 .   ? 42.638 -12.136 -18.445 1.00 28.64 ?  302 HOH   B O    1 
HETATM 7126 O O    . HOH   F 4 .   ? 45.350 -33.310 -16.014 1.00 22.10 ?  303 HOH   B O    1 
HETATM 7127 O O    . HOH   F 4 .   ? 45.796 -40.317 -3.648  1.00 28.98 ?  304 HOH   B O    1 
HETATM 7128 O O    . HOH   F 4 .   ? 43.145 -21.324 10.679  1.00 15.61 ?  305 HOH   B O    1 
HETATM 7129 O O    . HOH   F 4 .   ? 43.940 -29.297 -4.716  1.00 24.08 ?  306 HOH   B O    1 
HETATM 7130 O O    . HOH   F 4 .   ? 59.732 -15.311 8.214   1.00 30.15 ?  307 HOH   B O    1 
HETATM 7131 O O    . HOH   F 4 .   ? 30.462 -42.185 -10.663 1.00 29.54 ?  308 HOH   B O    1 
HETATM 7132 O O    . HOH   F 4 .   ? 53.339 -30.164 4.526   1.00 17.87 ?  309 HOH   B O    1 
HETATM 7133 O O    . HOH   F 4 .   ? 41.168 -24.404 15.791  1.00 39.96 ?  310 HOH   B O    1 
HETATM 7134 O O    . HOH   F 4 .   ? 32.768 -34.543 -5.956  1.00 16.24 ?  311 HOH   B O    1 
HETATM 7135 O O    . HOH   F 4 .   ? 40.216 -10.764 -9.510  1.00 17.41 ?  312 HOH   B O    1 
HETATM 7136 O O    . HOH   F 4 .   ? 44.548 -27.393 1.964   1.00 14.73 ?  313 HOH   B O    1 
HETATM 7137 O O    . HOH   F 4 .   ? 41.742 -8.054  1.433   1.00 25.83 ?  314 HOH   B O    1 
HETATM 7138 O O    . HOH   F 4 .   ? 48.101 -32.510 -16.647 1.00 40.39 ?  315 HOH   B O    1 
HETATM 7139 O O    . HOH   F 4 .   ? 37.850 -10.177 -10.742 1.00 17.25 ?  316 HOH   B O    1 
HETATM 7140 O O    . HOH   F 4 .   ? 57.545 -22.058 3.181   1.00 28.01 ?  317 HOH   B O    1 
HETATM 7141 O O    . HOH   F 4 .   ? 52.494 -29.188 -13.076 1.00 25.68 ?  318 HOH   B O    1 
HETATM 7142 O O    . HOH   F 4 .   ? 25.899 -21.419 -3.602  1.00 17.12 ?  319 HOH   B O    1 
HETATM 7143 O O    . HOH   F 4 .   ? 44.489 -24.574 9.561   1.00 18.86 ?  320 HOH   B O    1 
HETATM 7144 O O    . HOH   F 4 .   ? 38.262 -12.695 7.951   1.00 17.34 ?  321 HOH   B O    1 
HETATM 7145 O O    . HOH   F 4 .   ? 37.218 -30.415 -21.104 1.00 30.60 ?  322 HOH   B O    1 
HETATM 7146 O O    . HOH   F 4 .   ? 44.025 -1.707  7.676   1.00 40.45 ?  323 HOH   B O    1 
HETATM 7147 O O    . HOH   F 4 .   ? 27.697 -14.677 -9.486  1.00 33.88 ?  324 HOH   B O    1 
HETATM 7148 O O    . HOH   F 4 .   ? 53.607 -12.458 -22.334 1.00 38.90 ?  325 HOH   B O    1 
HETATM 7149 O O    . HOH   F 4 .   ? 38.397 -9.243  -13.265 1.00 29.03 ?  326 HOH   B O    1 
HETATM 7150 O O    . HOH   F 4 .   ? 51.687 -5.965  -7.974  1.00 47.25 ?  327 HOH   B O    1 
HETATM 7151 O O    . HOH   F 4 .   ? 59.840 -17.201 -10.474 1.00 34.04 ?  328 HOH   B O    1 
HETATM 7152 O O    . HOH   F 4 .   ? 26.307 -20.968 -6.306  1.00 17.06 ?  329 HOH   B O    1 
HETATM 7153 O O    . HOH   F 4 .   ? 36.668 -12.378 4.276   1.00 17.05 ?  330 HOH   B O    1 
HETATM 7154 O O    . HOH   F 4 .   ? 43.045 -34.525 0.033   1.00 20.13 ?  331 HOH   B O    1 
HETATM 7155 O O    . HOH   F 4 .   ? 33.507 -31.130 11.044  1.00 34.81 ?  332 HOH   B O    1 
HETATM 7156 O O    . HOH   F 4 .   ? 47.092 -24.445 8.131   1.00 23.44 ?  333 HOH   B O    1 
HETATM 7157 O O    . HOH   F 4 .   ? 48.560 -11.830 -13.795 1.00 26.19 ?  334 HOH   B O    1 
HETATM 7158 O O    . HOH   F 4 .   ? 45.666 -36.211 -16.232 1.00 34.42 ?  335 HOH   B O    1 
HETATM 7159 O O    . HOH   F 4 .   ? 62.910 -20.122 -0.764  1.00 39.49 ?  336 HOH   B O    1 
HETATM 7160 O O    . HOH   F 4 .   ? 51.396 -32.926 -10.912 1.00 39.44 ?  337 HOH   B O    1 
HETATM 7161 O O    . HOH   F 4 .   ? 47.394 -27.380 1.997   1.00 14.13 ?  338 HOH   B O    1 
HETATM 7162 O O    . HOH   F 4 .   ? 42.909 -43.451 -14.487 1.00 38.36 ?  339 HOH   B O    1 
HETATM 7163 O O    . HOH   F 4 .   ? 36.983 -15.010 -16.600 1.00 38.88 ?  340 HOH   B O    1 
HETATM 7164 O O    . HOH   F 4 .   ? 38.398 -12.073 -16.217 1.00 43.58 ?  341 HOH   B O    1 
HETATM 7165 O O    . HOH   F 4 .   ? 39.569 -23.481 -20.352 1.00 38.40 ?  342 HOH   B O    1 
HETATM 7166 O O    . HOH   F 4 .   ? 46.625 -19.929 12.271  1.00 31.90 ?  343 HOH   B O    1 
HETATM 7167 O O    . HOH   F 4 .   ? 28.868 -42.786 -12.481 1.00 35.90 ?  344 HOH   B O    1 
HETATM 7168 O O    . HOH   F 4 .   ? 34.407 -10.369 7.679   1.00 21.91 ?  345 HOH   B O    1 
HETATM 7169 O O    . HOH   F 4 .   ? 38.444 -22.420 14.980  1.00 40.04 ?  346 HOH   B O    1 
HETATM 7170 O O    . HOH   F 4 .   ? 32.965 -14.652 1.051   1.00 18.55 ?  347 HOH   B O    1 
HETATM 7171 O O    . HOH   F 4 .   ? 23.302 -23.741 6.839   1.00 36.54 ?  348 HOH   B O    1 
HETATM 7172 O O    . HOH   F 4 .   ? 40.322 -43.418 -9.219  1.00 25.24 ?  349 HOH   B O    1 
HETATM 7173 O O    . HOH   F 4 .   ? 36.994 -45.255 -9.734  1.00 35.99 ?  350 HOH   B O    1 
HETATM 7174 O O    . HOH   F 4 .   ? 39.781 -44.201 -11.377 1.00 43.34 ?  351 HOH   B O    1 
HETATM 7175 O O    . HOH   F 4 .   ? 62.431 -20.017 -4.852  1.00 51.06 ?  352 HOH   B O    1 
HETATM 7176 O O    . HOH   F 4 .   ? 44.182 -37.326 -17.874 1.00 32.18 ?  353 HOH   B O    1 
HETATM 7177 O O    . HOH   F 4 .   ? 27.708 -26.635 -0.663  1.00 29.85 ?  354 HOH   B O    1 
HETATM 7178 O O    . HOH   F 4 .   ? 33.754 -9.124  -8.849  1.00 28.96 ?  355 HOH   B O    1 
HETATM 7179 O O    . HOH   F 4 .   ? 55.641 -8.240  10.852  1.00 26.09 ?  356 HOH   B O    1 
HETATM 7180 O O    . HOH   F 4 .   ? 33.896 -7.868  11.556  1.00 38.67 ?  357 HOH   B O    1 
HETATM 7181 O O    . HOH   F 4 .   ? 36.134 -8.403  -9.652  1.00 33.19 ?  358 HOH   B O    1 
HETATM 7182 O O    . HOH   F 4 .   ? 56.485 -7.172  3.056   1.00 30.08 ?  359 HOH   B O    1 
HETATM 7183 O O    . HOH   F 4 .   ? 61.381 -19.831 1.758   1.00 40.43 ?  360 HOH   B O    1 
HETATM 7184 O O    . HOH   F 4 .   ? 56.900 -21.465 -16.404 1.00 42.24 ?  361 HOH   B O    1 
HETATM 7185 O O    . HOH   F 4 .   ? 40.173 -8.826  9.921   1.00 38.25 ?  362 HOH   B O    1 
HETATM 7186 O O    . HOH   F 4 .   ? 43.081 -12.672 -21.352 1.00 46.38 ?  363 HOH   B O    1 
HETATM 7187 O O    . HOH   F 4 .   ? 27.113 -25.835 -11.529 1.00 30.58 ?  364 HOH   B O    1 
HETATM 7188 O O    . HOH   F 4 .   ? 40.241 -11.278 -13.908 1.00 30.97 ?  365 HOH   B O    1 
HETATM 7189 O O    . HOH   F 4 .   ? 36.116 -8.682  8.984   1.00 33.02 ?  366 HOH   B O    1 
HETATM 7190 O O    . HOH   F 4 .   ? 58.975 -10.517 9.225   1.00 43.59 ?  367 HOH   B O    1 
HETATM 7191 O O    . HOH   F 4 .   ? 32.432 -23.565 14.027  1.00 41.61 ?  368 HOH   B O    1 
HETATM 7192 O O    . HOH   F 4 .   ? 48.224 -26.434 8.812   1.00 44.42 ?  369 HOH   B O    1 
HETATM 7193 O O    . HOH   F 4 .   ? 52.059 -12.912 13.320  1.00 33.39 ?  370 HOH   B O    1 
HETATM 7194 O O    . HOH   F 4 .   ? 39.788 -7.025  7.764   1.00 39.91 ?  371 HOH   B O    1 
HETATM 7195 O O    . HOH   F 4 .   ? 41.722 -10.042 -17.451 1.00 58.22 ?  372 HOH   B O    1 
HETATM 7196 O O    . HOH   F 4 .   ? 54.243 -5.760  2.951   1.00 36.02 ?  373 HOH   B O    1 
HETATM 7197 O O    . HOH   F 4 .   ? 55.889 -7.672  -0.619  1.00 36.67 ?  374 HOH   B O    1 
HETATM 7198 O O    . HOH   F 4 .   ? 38.055 -10.490 9.983   1.00 27.25 ?  375 HOH   B O    1 
HETATM 7199 O O    . HOH   F 4 .   ? 62.863 -12.243 6.970   1.00 35.52 ?  376 HOH   B O    1 
HETATM 7200 O O    . HOH   F 4 .   ? 36.433 -22.703 13.314  1.00 27.70 ?  377 HOH   B O    1 
HETATM 7201 O O    . HOH   F 4 .   ? 40.119 -7.710  3.082   1.00 42.78 ?  378 HOH   B O    1 
HETATM 7202 O O    . HOH   F 4 .   ? 41.709 -6.692  -4.795  1.00 48.27 ?  379 HOH   B O    1 
HETATM 7203 O O    . HOH   F 4 .   ? 39.569 -14.068 15.691  1.00 52.98 ?  380 HOH   B O    1 
HETATM 7204 O O    . HOH   F 4 .   ? 44.038 -5.554  -3.381  1.00 44.43 ?  381 HOH   B O    1 
HETATM 7205 O O    . HOH   F 4 .   ? 60.302 -22.304 2.828   1.00 40.42 ?  382 HOH   B O    1 
HETATM 7206 O O    . HOH   F 4 .   ? 52.791 -29.913 7.145   1.00 22.06 ?  383 HOH   B O    1 
HETATM 7207 O O    . HOH   F 4 .   ? 42.586 -17.042 -23.232 1.00 42.05 ?  384 HOH   B O    1 
HETATM 7208 O O    . HOH   F 4 .   ? 35.280 -33.703 7.132   1.00 39.11 ?  385 HOH   B O    1 
HETATM 7209 O O    . HOH   F 4 .   ? 46.680 -5.383  2.971   1.00 42.02 ?  386 HOH   B O    1 
HETATM 7210 O O    . HOH   F 4 .   ? 40.876 -9.790  15.823  1.00 44.42 ?  387 HOH   B O    1 
HETATM 7211 O O    . HOH   F 4 .   ? 35.132 -20.259 13.266  1.00 34.58 ?  388 HOH   B O    1 
HETATM 7212 O O    . HOH   F 4 .   ? 23.871 -20.814 -7.788  1.00 27.06 ?  389 HOH   B O    1 
HETATM 7213 O O    . HOH   F 4 .   ? 40.660 -6.585  -0.852  1.00 26.44 ?  390 HOH   B O    1 
HETATM 7214 O O    . HOH   F 4 .   ? 27.888 -27.045 2.178   1.00 33.21 ?  391 HOH   B O    1 
HETATM 7215 O O    . HOH   F 4 .   ? 26.630 -27.879 -13.503 1.00 36.01 ?  392 HOH   B O    1 
HETATM 7216 O O    . HOH   F 4 .   ? 44.023 -31.753 -3.759  1.00 35.10 ?  393 HOH   B O    1 
HETATM 7217 O O    . HOH   F 4 .   ? 45.661 -20.369 15.095  1.00 59.75 ?  394 HOH   B O    1 
HETATM 7218 O O    . HOH   F 4 .   ? 34.287 -33.325 9.624   1.00 32.90 ?  395 HOH   B O    1 
HETATM 7219 O O    . HOH   F 4 .   ? 26.832 -30.510 -12.745 1.00 28.49 ?  396 HOH   B O    1 
HETATM 7220 O O    . HOH   F 4 .   ? 50.531 -30.799 8.775   1.00 28.35 ?  397 HOH   B O    1 
HETATM 7221 O O    . HOH   F 4 .   ? 24.585 -20.625 -10.573 1.00 40.21 ?  398 HOH   B O    1 
HETATM 7222 O O    . HOH   F 4 .   ? 57.464 -6.422  -2.326  1.00 32.50 ?  399 HOH   B O    1 
HETATM 7223 O O    . HOH   F 4 .   ? 40.926 -11.766 -22.362 1.00 39.82 ?  400 HOH   B O    1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N   A VAL   A 3   ? 0.6596 0.6574 0.7609 -0.0013 0.0042  0.0260  3   VAL   A N   
2    N N   B VAL   A 3   ? 0.6920 0.6815 0.8102 -0.0057 0.0092  0.0652  3   VAL   A N   
3    C CA  A VAL   A 3   ? 0.6563 0.6540 0.7510 -0.0025 0.0041  0.0260  3   VAL   A CA  
4    C CA  B VAL   A 3   ? 0.6886 0.6780 0.7947 -0.0081 0.0091  0.0658  3   VAL   A CA  
5    C C   A VAL   A 3   ? 0.6375 0.6360 0.7090 -0.0066 0.0009  0.0283  3   VAL   A C   
6    C C   B VAL   A 3   ? 0.6688 0.6599 0.7451 -0.0164 0.0031  0.0699  3   VAL   A C   
7    O O   A VAL   A 3   ? 0.6405 0.6388 0.7201 -0.0060 0.0008  0.0281  3   VAL   A O   
8    O O   B VAL   A 3   ? 0.6722 0.6628 0.7642 -0.0151 0.0030  0.0703  3   VAL   A O   
9    C CB  A VAL   A 3   ? 0.6681 0.6654 0.7745 -0.0002 0.0068  0.0238  3   VAL   A CB  
10   C CB  B VAL   A 3   ? 0.7010 0.6891 0.8159 -0.0032 0.0142  0.0619  3   VAL   A CB  
11   C CG1 A VAL   A 3   ? 0.6721 0.6692 0.7809 0.0008  0.0076  0.0232  3   VAL   A CG1 
12   C CG1 B VAL   A 3   ? 0.7049 0.6923 0.8209 -0.0009 0.0157  0.0608  3   VAL   A CG1 
13   C CG2 A VAL   A 3   ? 0.6721 0.6693 0.7809 0.0005  0.0077  0.0233  3   VAL   A CG2 
14   C CG2 B VAL   A 3   ? 0.7051 0.6928 0.8209 -0.0016 0.0161  0.0613  3   VAL   A CG2 
31   N N   A ASN   A 4   ? 0.6125 0.6120 0.6495 -0.0115 -0.0022 0.0305  4   ASN   A N   
32   N N   B ASN   A 4   ? 0.6420 0.6356 0.6644 -0.0261 -0.0025 0.0740  4   ASN   A N   
33   C CA  A ASN   A 4   ? 0.5850 0.5857 0.5850 -0.0168 -0.0051 0.0318  4   ASN   A CA  
34   C CA  B ASN   A 4   ? 0.6120 0.6087 0.5753 -0.0361 -0.0073 0.0761  4   ASN   A CA  
35   C C   A ASN   A 4   ? 0.5490 0.5531 0.5416 -0.0235 -0.0028 0.0268  4   ASN   A C   
36   C C   B ASN   A 4   ? 0.5706 0.5761 0.5172 -0.0489 0.0029  0.0672  4   ASN   A C   
37   O O   A ASN   A 4   ? 0.5496 0.5541 0.5402 -0.0240 -0.0034 0.0278  4   ASN   A O   
38   O O   B ASN   A 4   ? 0.5710 0.5782 0.5074 -0.0499 0.0022  0.0690  4   ASN   A O   
39   C CB  A ASN   A 4   ? 0.5911 0.5900 0.5621 -0.0156 -0.0091 0.0376  4   ASN   A CB  
40   C CB  B ASN   A 4   ? 0.6204 0.6119 0.5432 -0.0346 -0.0197 0.0875  4   ASN   A CB  
41   C CG  A ASN   A 4   ? 0.5953 0.5928 0.5416 -0.0146 -0.0128 0.0426  4   ASN   A CG  
42   C CG  B ASN   A 4   ? 0.6258 0.6132 0.5134 -0.0329 -0.0317 0.0979  4   ASN   A CG  
43   O OD1 A ASN   A 4   ? 0.5970 0.5942 0.5349 -0.0144 -0.0139 0.0442  4   ASN   A OD1 
44   O OD1 B ASN   A 4   ? 0.6281 0.6140 0.5031 -0.0325 -0.0356 0.1016  4   ASN   A OD1 
45   N ND2 A ASN   A 4   ? 0.5966 0.5935 0.5354 -0.0141 -0.0144 0.0447  4   ASN   A ND2 
46   N ND2 B ASN   A 4   ? 0.6271 0.6131 0.5054 -0.0316 -0.0364 0.1024  4   ASN   A ND2 
59   N N   A SER   A 5   ? 0.5108 0.5173 0.4982 -0.0298 0.0001  0.0206  5   SER   A N   
60   N N   B SER   A 5   ? 0.5265 0.5388 0.4706 -0.0616 0.0140  0.0573  5   SER   A N   
61   C CA  A SER   A 5   ? 0.4716 0.4802 0.4547 -0.0360 0.0050  0.0142  5   SER   A CA  
62   C CA  B SER   A 5   ? 0.4808 0.4991 0.4286 -0.0741 0.0288  0.0482  5   SER   A CA  
63   C C   A SER   A 5   ? 0.4317 0.4402 0.4070 -0.0403 0.0121  0.0108  5   SER   A C   
64   C C   B SER   A 5   ? 0.4335 0.4528 0.3724 -0.0849 0.0504  0.0489  5   SER   A C   
65   O O   A SER   A 5   ? 0.4320 0.4413 0.4059 -0.0405 0.0113  0.0097  5   SER   A O   
66   O O   B SER   A 5   ? 0.4356 0.4573 0.3629 -0.0836 0.0472  0.0406  5   SER   A O   
67   C CB  A SER   A 5   ? 0.4727 0.4825 0.4616 -0.0373 0.0033  0.0118  5   SER   A CB  
68   C CB  B SER   A 5   ? 0.4830 0.5048 0.4498 -0.0741 0.0233  0.0408  5   SER   A CB  
69   O OG  A SER   A 5   ? 0.4738 0.4840 0.4646 -0.0375 0.0021  0.0096  5   SER   A OG  
70   O OG  B SER   A 5   ? 0.4859 0.5081 0.4630 -0.0730 0.0196  0.0344  5   SER   A OG  
81   N N   A PHE   A 6   ? 0.3908 0.3984 0.3564 -0.0432 0.0212  0.0095  6   PHE   A N   
82   N N   B PHE   A 6   ? 0.3839 0.4018 0.3202 -0.0950 0.0758  0.0614  6   PHE   A N   
83   C CA  A PHE   A 6   ? 0.3504 0.3572 0.3074 -0.0448 0.0286  0.0108  6   PHE   A CA  
84   C CA  B PHE   A 6   ? 0.3363 0.3521 0.2704 -0.0982 0.0918  0.0779  6   PHE   A CA  
85   C C   A PHE   A 6   ? 0.3348 0.3437 0.2987 -0.0500 0.0330  0.0067  6   PHE   A C   
86   C C   B PHE   A 6   ? 0.3217 0.3432 0.2747 -0.0957 0.1053  0.0758  6   PHE   A C   
87   O O   A PHE   A 6   ? 0.3358 0.3440 0.2983 -0.0538 0.0345  0.0094  6   PHE   A O   
88   O O   B PHE   A 6   ? 0.3241 0.3403 0.2916 -0.0908 0.1023  0.0872  6   PHE   A O   
89   C CB  A PHE   A 6   ? 0.3284 0.3304 0.2715 -0.0396 0.0283  0.0137  6   PHE   A CB  
90   C CB  B PHE   A 6   ? 0.3115 0.3173 0.2409 -0.0936 0.0740  0.0829  6   PHE   A CB  
91   C CG  A PHE   A 6   ? 0.3083 0.3062 0.2419 -0.0349 0.0287  0.0161  6   PHE   A CG  
92   C CG  B PHE   A 6   ? 0.2914 0.2907 0.2241 -0.0818 0.0551  0.0719  6   PHE   A CG  
93   C CD1 A PHE   A 6   ? 0.2991 0.2957 0.2280 -0.0321 0.0270  0.0154  6   PHE   A CD1 
94   C CD1 B PHE   A 6   ? 0.2825 0.2774 0.2091 -0.0762 0.0456  0.0632  6   PHE   A CD1 
95   C CD2 A PHE   A 6   ? 0.3012 0.2966 0.2350 -0.0314 0.0322  0.0165  6   PHE   A CD2 
96   C CD2 B PHE   A 6   ? 0.2878 0.2844 0.2306 -0.0712 0.0460  0.0626  6   PHE   A CD2 
97   C CE1 A PHE   A 6   ? 0.2934 0.2897 0.2223 -0.0298 0.0275  0.0163  6   PHE   A CE1 
98   C CE1 B PHE   A 6   ? 0.2767 0.2723 0.2065 -0.0706 0.0423  0.0600  6   PHE   A CE1 
99   C CE2 A PHE   A 6   ? 0.2962 0.2910 0.2321 -0.0291 0.0324  0.0155  6   PHE   A CE2 
100  C CE2 B PHE   A 6   ? 0.2837 0.2814 0.2420 -0.0644 0.0393  0.0483  6   PHE   A CE2 
101  C CZ  A PHE   A 6   ? 0.2936 0.2880 0.2260 -0.0286 0.0299  0.0155  6   PHE   A CZ  
102  C CZ  B PHE   A 6   ? 0.2794 0.2748 0.2270 -0.0666 0.0411  0.0514  6   PHE   A CZ  
121  N N   A SER   A 7   ? 0.3192 0.3305 0.2927 -0.0490 0.0356  0.0003  7   SER   A N   
122  N N   B SER   A 7   ? 0.3109 0.3370 0.2752 -0.0904 0.1167  0.0649  7   SER   A N   
123  C CA  A SER   A 7   ? 0.3039 0.3176 0.2933 -0.0445 0.0370  -0.0087 7   SER   A CA  
124  C CA  B SER   A 7   ? 0.2991 0.3336 0.2917 -0.0740 0.1130  0.0438  7   SER   A CA  
125  C C   A SER   A 7   ? 0.2817 0.2962 0.2678 -0.0442 0.0461  -0.0131 7   SER   A C   
126  C C   B SER   A 7   ? 0.2701 0.3027 0.2730 -0.0671 0.1218  0.0522  7   SER   A C   
127  O O   A SER   A 7   ? 0.2837 0.2947 0.2693 -0.0429 0.0466  -0.0157 7   SER   A O   
128  O O   B SER   A 7   ? 0.2674 0.2968 0.2777 -0.0706 0.1215  0.0559  7   SER   A O   
129  C CB  A SER   A 7   ? 0.3088 0.3239 0.3133 -0.0429 0.0303  -0.0107 7   SER   A CB  
130  C CB  B SER   A 7   ? 0.3147 0.3618 0.3200 -0.0663 0.0981  0.0267  7   SER   A CB  
131  O OG  A SER   A 7   ? 0.3136 0.3281 0.3314 -0.0422 0.0247  -0.0118 7   SER   A OG  
132  O OG  B SER   A 7   ? 0.3312 0.3732 0.3485 -0.0619 0.0845  0.0170  7   SER   A OG  
143  N N   A GLY   A 8   ? 0.2587 0.2775 0.2435 -0.0454 0.0527  -0.0150 8   GLY   A N   
144  N N   B GLY   A 8   ? 0.2466 0.2808 0.2612 -0.0542 0.1073  0.0477  8   GLY   A N   
145  C CA  A GLY   A 8   ? 0.2335 0.2587 0.2272 -0.0437 0.0567  -0.0154 8   GLY   A CA  
146  C CA  B GLY   A 8   ? 0.2289 0.2576 0.2643 -0.0347 0.0849  0.0454  8   GLY   A CA  
147  C C   A GLY   A 8   ? 0.2073 0.2386 0.2063 -0.0423 0.0548  -0.0178 8   GLY   A C   
148  C C   B GLY   A 8   ? 0.1975 0.2297 0.2503 -0.0181 0.0681  0.0466  8   GLY   A C   
149  O O   A GLY   A 8   ? 0.2021 0.2419 0.2152 -0.0433 0.0556  -0.0317 8   GLY   A O   
150  O O   B GLY   A 8   ? 0.1963 0.2408 0.2647 0.0028  0.0673  0.0196  8   GLY   A O   
157  N N   A TYR   A 9   ? 0.1864 0.2162 0.1825 -0.0406 0.0444  -0.0041 9   TYR   A N   
158  N N   B TYR   A 9   ? 0.1766 0.1916 0.2462 -0.0216 0.0458  0.0569  9   TYR   A N   
159  C CA  A TYR   A 9   ? 0.1679 0.1955 0.1591 -0.0380 0.0320  0.0064  9   TYR   A CA  
160  C CA  B TYR   A 9   ? 0.1555 0.1709 0.2404 -0.0163 0.0378  0.0644  9   TYR   A CA  
161  C C   A TYR   A 9   ? 0.1625 0.1822 0.1426 -0.0381 0.0281  0.0171  9   TYR   A C   
162  C C   B TYR   A 9   ? 0.1527 0.1632 0.2409 -0.0070 0.0336  0.0716  9   TYR   A C   
163  O O   A TYR   A 9   ? 0.1621 0.1839 0.1449 -0.0444 0.0214  0.0238  9   TYR   A O   
164  O O   B TYR   A 9   ? 0.1624 0.1806 0.2426 -0.0109 0.0171  0.0534  9   TYR   A O   
165  C CB  A TYR   A 9   ? 0.1591 0.1983 0.1578 -0.0280 0.0263  0.0054  9   TYR   A CB  
166  C CB  B TYR   A 9   ? 0.1536 0.1767 0.2319 -0.0144 0.0337  0.0554  9   TYR   A CB  
167  C CG  A TYR   A 9   ? 0.1494 0.1971 0.1486 -0.0209 0.0199  0.0061  9   TYR   A CG  
168  C CG  B TYR   A 9   ? 0.1621 0.1822 0.2353 -0.0095 0.0363  0.0428  9   TYR   A CG  
169  C CD1 A TYR   A 9   ? 0.1482 0.1994 0.1599 -0.0179 0.0156  -0.0030 9   TYR   A CD1 
170  C CD1 B TYR   A 9   ? 0.1657 0.1912 0.2315 -0.0207 0.0372  0.0402  9   TYR   A CD1 
171  C CD2 A TYR   A 9   ? 0.1469 0.1915 0.1449 -0.0197 0.0130  0.0051  9   TYR   A CD2 
172  C CD2 B TYR   A 9   ? 0.1590 0.1681 0.2348 0.0006  0.0325  0.0439  9   TYR   A CD2 
173  C CE1 A TYR   A 9   ? 0.1483 0.1997 0.1666 -0.0211 0.0090  -0.0124 9   TYR   A CE1 
174  C CE1 B TYR   A 9   ? 0.1647 0.1911 0.2366 -0.0185 0.0424  0.0397  9   TYR   A CE1 
175  C CE2 A TYR   A 9   ? 0.1470 0.1937 0.1532 -0.0232 0.0095  -0.0031 9   TYR   A CE2 
176  C CE2 B TYR   A 9   ? 0.1564 0.1666 0.2298 -0.0017 0.0412  0.0388  9   TYR   A CE2 
177  C CZ  A TYR   A 9   ? 0.1500 0.1996 0.1674 -0.0268 0.0121  -0.0106 9   TYR   A CZ  
178  C CZ  B TYR   A 9   ? 0.1535 0.1779 0.2311 -0.0164 0.0448  0.0423  9   TYR   A CZ  
179  O OH  A TYR   A 9   ? 0.1596 0.2097 0.1825 -0.0337 0.0112  -0.0146 9   TYR   A OH  
180  O OH  B TYR   A 9   ? 0.1585 0.1900 0.2444 -0.0198 0.0422  0.0353  9   TYR   A OH  
199  N N   A LEU   A 10  ? 0.1578 0.1698 0.1314 -0.0331 0.0174  0.0137  10  LEU   A N   
200  N N   B LEU   A 10  ? 0.1546 0.1537 0.2554 -0.0044 0.0351  0.0714  10  LEU   A N   
201  C CA  A LEU   A 10  ? 0.1532 0.1666 0.1453 -0.0339 0.0025  0.0182  10  LEU   A CA  
202  C CA  B LEU   A 10  ? 0.1417 0.1568 0.2403 -0.0118 0.0315  0.0796  10  LEU   A CA  
203  C C   A LEU   A 10  ? 0.1487 0.1580 0.1428 -0.0335 -0.0048 0.0180  10  LEU   A C   
204  C C   B LEU   A 10  ? 0.1340 0.1540 0.2578 -0.0137 0.0306  0.0746  10  LEU   A C   
205  O O   A LEU   A 10  ? 0.1472 0.1453 0.1273 -0.0344 0.0025  0.0178  10  LEU   A O   
206  O O   B LEU   A 10  ? 0.1390 0.1492 0.2575 -0.0123 0.0417  0.0698  10  LEU   A O   
207  C CB  A LEU   A 10  ? 0.1564 0.1695 0.1642 -0.0336 0.0026  0.0264  10  LEU   A CB  
208  C CB  B LEU   A 10  ? 0.1495 0.1689 0.2354 -0.0068 0.0259  0.0825  10  LEU   A CB  
209  C CG  A LEU   A 10  ? 0.1637 0.1760 0.1810 -0.0298 0.0001  0.0234  10  LEU   A CG  
210  C CG  B LEU   A 10  ? 0.1545 0.1843 0.2168 -0.0025 0.0158  0.0786  10  LEU   A CG  
211  C CD1 A LEU   A 10  ? 0.1679 0.1812 0.1928 -0.0321 0.0099  0.0245  10  LEU   A CD1 
212  C CD1 B LEU   A 10  ? 0.1583 0.1847 0.2042 -0.0107 0.0168  0.0630  10  LEU   A CD1 
213  C CD2 A LEU   A 10  ? 0.1745 0.1857 0.1802 -0.0272 0.0004  0.0147  10  LEU   A CD2 
214  C CD2 B LEU   A 10  ? 0.1670 0.2068 0.2223 -0.0008 0.0185  0.0750  10  LEU   A CD2 
237  N N   A LYS   A 11  ? 0.1496 0.1599 0.1558 -0.0324 -0.0072 0.0273  11  LYS   A N   
238  N N   B LYS   A 11  ? 0.1325 0.1552 0.2623 -0.0128 0.0251  0.0788  11  LYS   A N   
239  C CA  A LYS   A 11  ? 0.1466 0.1546 0.1752 -0.0366 -0.0040 0.0271  11  LYS   A CA  
240  C CA  B LYS   A 11  ? 0.1342 0.1517 0.2721 -0.0154 0.0171  0.0781  11  LYS   A CA  
241  C C   A LYS   A 11  ? 0.1387 0.1613 0.1881 -0.0321 0.0052  0.0181  11  LYS   A C   
242  C C   B LYS   A 11  ? 0.1293 0.1577 0.2528 -0.0134 0.0263  0.0733  11  LYS   A C   
243  O O   A LYS   A 11  ? 0.1377 0.1623 0.2033 -0.0405 0.0144  0.0145  11  LYS   A O   
244  O O   B LYS   A 11  ? 0.1238 0.1753 0.2592 -0.0207 0.0159  0.0722  11  LYS   A O   
245  C CB  A LYS   A 11  ? 0.1528 0.1452 0.1799 -0.0426 0.0006  0.0276  11  LYS   A CB  
246  C CB  B LYS   A 11  ? 0.1471 0.1532 0.2859 -0.0230 0.0169  0.0770  11  LYS   A CB  
247  C CG  A LYS   A 11  ? 0.1605 0.1471 0.1882 -0.0369 -0.0012 0.0365  11  LYS   A CG  
248  C CG  B LYS   A 11  ? 0.1631 0.1576 0.2848 -0.0195 0.0190  0.0794  11  LYS   A CG  
249  C CD  A LYS   A 11  ? 0.1676 0.1531 0.2022 -0.0296 -0.0052 0.0412  11  LYS   A CD  
250  C CD  B LYS   A 11  ? 0.1841 0.1749 0.2828 -0.0162 0.0159  0.0819  11  LYS   A CD  
251  C CE  A LYS   A 11  ? 0.1707 0.1562 0.2155 -0.0244 -0.0117 0.0449  11  LYS   A CE  
252  C CE  B LYS   A 11  ? 0.1980 0.1842 0.2788 -0.0140 0.0141  0.0793  11  LYS   A CE  
253  N NZ  A LYS   A 11  ? 0.1683 0.1557 0.2241 -0.0182 -0.0158 0.0414  11  LYS   A NZ  
254  N NZ  B LYS   A 11  ? 0.2013 0.1855 0.2776 -0.0088 0.0139  0.0744  11  LYS   A NZ  
281  N N   A LEU   A 12  ? 0.1357 0.1633 0.1853 -0.0289 0.0059  0.0202  12  LEU   A N   
282  N N   B LEU   A 12  ? 0.1316 0.1554 0.2473 -0.0133 0.0308  0.0574  12  LEU   A N   
283  C CA  A LEU   A 12  ? 0.1378 0.1725 0.1972 -0.0206 0.0097  0.0301  12  LEU   A CA  
284  C CA  B LEU   A 12  ? 0.1467 0.1725 0.2532 -0.0093 0.0281  0.0648  12  LEU   A CA  
285  C C   A LEU   A 12  ? 0.1380 0.1682 0.2066 -0.0187 0.0117  0.0362  12  LEU   A C   
286  C C   B LEU   A 12  ? 0.1475 0.1690 0.2364 -0.0188 0.0233  0.0596  12  LEU   A C   
287  O O   A LEU   A 12  ? 0.1392 0.1729 0.1939 -0.0129 0.0058  0.0231  12  LEU   A O   
288  O O   B LEU   A 12  ? 0.1545 0.1803 0.2275 -0.0160 0.0247  0.0550  12  LEU   A O   
289  C CB  A LEU   A 12  ? 0.1391 0.1808 0.2088 -0.0162 0.0160  0.0337  12  LEU   A CB  
290  C CB  B LEU   A 12  ? 0.1570 0.1751 0.2666 -0.0041 0.0414  0.0737  12  LEU   A CB  
291  C CG  A LEU   A 12  ? 0.1402 0.1869 0.2183 -0.0129 0.0274  0.0399  12  LEU   A CG  
292  C CG  B LEU   A 12  ? 0.1785 0.1870 0.2823 0.0056  0.0516  0.0891  12  LEU   A CG  
293  C CD1 A LEU   A 12  ? 0.1437 0.1908 0.2241 -0.0111 0.0353  0.0418  12  LEU   A CD1 
294  C CD1 B LEU   A 12  ? 0.1929 0.1931 0.2887 0.0110  0.0576  0.0891  12  LEU   A CD1 
295  C CD2 A LEU   A 12  ? 0.1390 0.1935 0.2298 -0.0079 0.0242  0.0369  12  LEU   A CD2 
296  C CD2 B LEU   A 12  ? 0.1848 0.1976 0.3025 0.0139  0.0425  0.0891  12  LEU   A CD2 
319  N N   . THR   A 13  ? 0.1389 0.1595 0.2406 -0.0180 0.0142  0.0469  13  THR   A N   
320  C CA  . THR   A 13  ? 0.1455 0.1550 0.2481 -0.0208 0.0180  0.0445  13  THR   A CA  
321  C C   . THR   A 13  ? 0.1476 0.1533 0.2582 -0.0250 0.0130  0.0466  13  THR   A C   
322  O O   . THR   A 13  ? 0.1470 0.1599 0.2562 -0.0129 0.0100  0.0403  13  THR   A O   
323  C CB  . THR   A 13  ? 0.1524 0.1666 0.2651 -0.0175 0.0267  0.0441  13  THR   A CB  
324  O OG1 . THR   A 13  ? 0.1504 0.1663 0.2893 -0.0216 0.0270  0.0530  13  THR   A OG1 
325  C CG2 . THR   A 13  ? 0.1658 0.1916 0.2725 -0.0162 0.0329  0.0228  13  THR   A CG2 
334  N N   A ASP   A 14  ? 0.1553 0.1595 0.2610 -0.0225 0.0035  0.0431  14  ASP   A N   
335  N N   B ASP   A 14  ? 0.1558 0.1508 0.2737 -0.0271 0.0026  0.0565  14  ASP   A N   
336  C CA  A ASP   A 14  ? 0.1617 0.1661 0.2661 -0.0204 -0.0019 0.0476  14  ASP   A CA  
337  C CA  B ASP   A 14  ? 0.1667 0.1525 0.2945 -0.0246 -0.0119 0.0659  14  ASP   A CA  
338  C C   A ASP   A 14  ? 0.1532 0.1552 0.2477 -0.0157 -0.0004 0.0523  14  ASP   A C   
339  C C   B ASP   A 14  ? 0.1581 0.1513 0.2695 -0.0223 -0.0040 0.0598  14  ASP   A C   
340  O O   A ASP   A 14  ? 0.1512 0.1606 0.2339 -0.0085 -0.0049 0.0586  14  ASP   A O   
341  O O   B ASP   A 14  ? 0.1645 0.1682 0.2841 -0.0303 -0.0101 0.0584  14  ASP   A O   
342  C CB  A ASP   A 14  ? 0.1794 0.1873 0.3015 -0.0216 -0.0035 0.0514  14  ASP   A CB  
343  C CB  B ASP   A 14  ? 0.1992 0.1726 0.3526 -0.0206 -0.0237 0.0864  14  ASP   A CB  
344  C CG  A ASP   A 14  ? 0.1918 0.2127 0.3352 -0.0297 -0.0016 0.0510  14  ASP   A CG  
345  C CG  B ASP   A 14  ? 0.2387 0.2311 0.4244 -0.0215 -0.0313 0.0743  14  ASP   A CG  
346  O OD1 A ASP   A 14  ? 0.1920 0.2055 0.3447 -0.0439 -0.0008 0.0552  14  ASP   A OD1 
347  O OD1 B ASP   A 14  ? 0.2508 0.2445 0.4502 -0.0132 -0.0473 0.0728  14  ASP   A OD1 
348  O OD2 A ASP   A 14  ? 0.2022 0.2356 0.3599 -0.0251 -0.0058 0.0416  14  ASP   A OD2 
349  O OD2 B ASP   A 14  ? 0.2486 0.2575 0.4635 -0.0213 -0.0325 0.0587  14  ASP   A OD2 
358  N N   . ASN   A 15  ? 0.1450 0.1413 0.2573 -0.0202 0.0062  0.0527  15  ASN   A N   
359  C CA  . ASN   A 15  ? 0.1405 0.1431 0.2746 -0.0142 0.0063  0.0419  15  ASN   A CA  
360  C C   . ASN   A 15  ? 0.1393 0.1345 0.2927 -0.0149 0.0132  0.0366  15  ASN   A C   
361  O O   . ASN   A 15  ? 0.1480 0.1452 0.3209 -0.0167 -0.0045 0.0343  15  ASN   A O   
362  C CB  . ASN   A 15  ? 0.1385 0.1422 0.2790 -0.0044 0.0098  0.0410  15  ASN   A CB  
363  C CG  . ASN   A 15  ? 0.1387 0.1453 0.2823 -0.0048 0.0191  0.0295  15  ASN   A CG  
364  O OD1 . ASN   A 15  ? 0.1567 0.1552 0.3039 -0.0198 0.0177  0.0239  15  ASN   A OD1 
365  N ND2 . ASN   A 15  ? 0.1448 0.1681 0.2768 -0.0089 0.0297  0.0302  15  ASN   A ND2 
373  N N   . VAL   A 16  ? 0.1358 0.1325 0.2877 -0.0116 0.0191  0.0431  16  VAL   A N   
374  C CA  . VAL   A 16  ? 0.1347 0.1394 0.2748 -0.0132 0.0264  0.0492  16  VAL   A CA  
375  C C   . VAL   A 16  ? 0.1271 0.1404 0.2552 -0.0111 0.0183  0.0450  16  VAL   A C   
376  O O   . VAL   A 16  ? 0.1256 0.1435 0.2634 -0.0150 0.0248  0.0392  16  VAL   A O   
377  C CB  . VAL   A 16  ? 0.1528 0.1516 0.2795 0.0049  0.0417  0.0559  16  VAL   A CB  
378  C CG1 . VAL   A 16  ? 0.1652 0.1627 0.2853 0.0164  0.0485  0.0566  16  VAL   A CG1 
379  C CG2 . VAL   A 16  ? 0.1615 0.1628 0.2846 0.0091  0.0494  0.0483  16  VAL   A CG2 
389  N N   A TYR   A 17  ? 0.1268 0.1435 0.2265 -0.0150 0.0152  0.0419  17  TYR   A N   
390  N N   B TYR   A 17  ? 0.1251 0.1324 0.2563 -0.0114 0.0294  0.0494  17  TYR   A N   
391  C CA  A TYR   A 17  ? 0.1281 0.1487 0.1918 -0.0187 0.0090  0.0385  17  TYR   A CA  
392  C CA  B TYR   A 17  ? 0.1284 0.1344 0.2415 -0.0140 0.0319  0.0501  17  TYR   A CA  
393  C C   A TYR   A 17  ? 0.1304 0.1495 0.1792 -0.0213 0.0005  0.0388  17  TYR   A C   
394  C C   B TYR   A 17  ? 0.1306 0.1280 0.2405 -0.0078 0.0310  0.0451  17  TYR   A C   
395  O O   A TYR   A 17  ? 0.1253 0.1470 0.1718 -0.0231 -0.0106 0.0447  17  TYR   A O   
396  O O   B TYR   A 17  ? 0.1324 0.1285 0.2453 -0.0077 0.0426  0.0371  17  TYR   A O   
397  C CB  A TYR   A 17  ? 0.1389 0.1545 0.1908 -0.0175 0.0061  0.0319  17  TYR   A CB  
398  C CB  B TYR   A 17  ? 0.1581 0.1402 0.2496 -0.0200 0.0119  0.0616  17  TYR   A CB  
399  C CG  A TYR   A 17  ? 0.1546 0.1615 0.2029 -0.0177 0.0072  0.0250  17  TYR   A CG  
400  C CG  B TYR   A 17  ? 0.1869 0.1564 0.2662 -0.0225 -0.0099 0.0598  17  TYR   A CG  
401  C CD1 A TYR   A 17  ? 0.1659 0.1659 0.2131 -0.0121 0.0051  0.0261  17  TYR   A CD1 
402  C CD1 B TYR   A 17  ? 0.2044 0.1695 0.2844 -0.0131 -0.0249 0.0613  17  TYR   A CD1 
403  C CD2 A TYR   A 17  ? 0.1615 0.1644 0.2093 -0.0186 0.0127  0.0250  17  TYR   A CD2 
404  C CD2 B TYR   A 17  ? 0.2002 0.1679 0.2711 -0.0314 -0.0099 0.0698  17  TYR   A CD2 
405  C CE1 A TYR   A 17  ? 0.1773 0.1657 0.2268 -0.0130 0.0001  0.0282  17  TYR   A CE1 
406  C CE1 B TYR   A 17  ? 0.2184 0.1759 0.3013 -0.0166 -0.0376 0.0678  17  TYR   A CE1 
407  C CE2 A TYR   A 17  ? 0.1750 0.1640 0.2219 -0.0185 0.0104  0.0266  17  TYR   A CE2 
408  C CE2 B TYR   A 17  ? 0.2212 0.1773 0.2899 -0.0328 -0.0226 0.0691  17  TYR   A CE2 
409  C CZ  A TYR   A 17  ? 0.1845 0.1635 0.2271 -0.0138 0.0043  0.0340  17  TYR   A CZ  
410  C CZ  B TYR   A 17  ? 0.2361 0.1800 0.2946 -0.0243 -0.0386 0.0751  17  TYR   A CZ  
411  O OH  A TYR   A 17  ? 0.1928 0.1656 0.2329 -0.0107 0.0118  0.0359  17  TYR   A OH  
412  O OH  B TYR   A 17  ? 0.2602 0.1884 0.3034 -0.0241 -0.0392 0.0743  17  TYR   A OH  
431  N N   A ILE   A 18  ? 0.1323 0.1514 0.1708 -0.0263 0.0103  0.0377  18  ILE   A N   
432  N N   B ILE   A 18  ? 0.1374 0.1305 0.2511 -0.0081 0.0382  0.0561  18  ILE   A N   
433  C CA  A ILE   A 18  ? 0.1325 0.1551 0.1553 -0.0216 0.0108  0.0300  18  ILE   A CA  
434  C CA  B ILE   A 18  ? 0.1430 0.1339 0.2411 0.0026  0.0463  0.0624  18  ILE   A CA  
435  C C   A ILE   A 18  ? 0.1367 0.1594 0.1458 -0.0238 0.0124  0.0231  18  ILE   A C   
436  C C   B ILE   A 18  ? 0.1431 0.1407 0.2575 0.0011  0.0449  0.0621  18  ILE   A C   
437  O O   A ILE   A 18  ? 0.1374 0.1612 0.1508 -0.0312 0.0160  0.0207  18  ILE   A O   
438  O O   B ILE   A 18  ? 0.1325 0.1405 0.2577 -0.0095 0.0393  0.0576  18  ILE   A O   
439  C CB  A ILE   A 18  ? 0.1329 0.1536 0.1486 -0.0188 0.0120  0.0312  18  ILE   A CB  
440  C CB  B ILE   A 18  ? 0.1567 0.1424 0.2415 0.0047  0.0416  0.0637  18  ILE   A CB  
441  C CG1 A ILE   A 18  ? 0.1405 0.1612 0.1627 -0.0189 0.0034  0.0352  18  ILE   A CG1 
442  C CG1 B ILE   A 18  ? 0.1699 0.1614 0.2337 -0.0036 0.0405  0.0610  18  ILE   A CG1 
443  C CG2 A ILE   A 18  ? 0.1373 0.1573 0.1532 -0.0202 0.0168  0.0322  18  ILE   A CG2 
444  C CG2 B ILE   A 18  ? 0.1600 0.1417 0.2468 0.0072  0.0346  0.0523  18  ILE   A CG2 
445  C CD1 A ILE   A 18  ? 0.1552 0.1681 0.1743 -0.0167 -0.0065 0.0344  18  ILE   A CD1 
446  C CD1 B ILE   A 18  ? 0.1948 0.1801 0.2533 -0.0035 0.0291  0.0497  18  ILE   A CD1 
469  N N   A LYS   A 19  ? 0.1459 0.1614 0.1462 -0.0192 0.0296  0.0180  19  LYS   A N   
470  N N   B LYS   A 19  ? 0.1450 0.1424 0.2650 0.0026  0.0636  0.0627  19  LYS   A N   
471  C CA  A LYS   A 19  ? 0.1574 0.1666 0.1556 -0.0093 0.0419  0.0143  19  LYS   A CA  
472  C CA  B LYS   A 19  ? 0.1535 0.1525 0.2636 0.0092  0.0622  0.0633  19  LYS   A CA  
473  C C   A LYS   A 19  ? 0.1610 0.1682 0.1527 -0.0036 0.0450  0.0169  19  LYS   A C   
474  C C   B LYS   A 19  ? 0.1473 0.1438 0.2564 0.0077  0.0629  0.0617  19  LYS   A C   
475  O O   A LYS   A 19  ? 0.1598 0.1672 0.1398 -0.0037 0.0363  0.0226  19  LYS   A O   
476  O O   B LYS   A 19  ? 0.1357 0.1395 0.2426 0.0090  0.0490  0.0632  19  LYS   A O   
477  C CB  A LYS   A 19  ? 0.1650 0.1742 0.1659 -0.0035 0.0471  0.0135  19  LYS   A CB  
478  C CB  B LYS   A 19  ? 0.1637 0.1763 0.2577 0.0094  0.0657  0.0706  19  LYS   A CB  
479  C CG  A LYS   A 19  ? 0.1800 0.1762 0.1683 0.0021  0.0449  0.0134  19  LYS   A CG  
480  C CG  B LYS   A 19  ? 0.1804 0.1942 0.2558 0.0053  0.0594  0.0644  19  LYS   A CG  
481  C CD  A LYS   A 19  ? 0.1906 0.1814 0.1721 0.0079  0.0460  0.0103  19  LYS   A CD  
482  C CD  B LYS   A 19  ? 0.1948 0.2118 0.2521 0.0005  0.0524  0.0527  19  LYS   A CD  
483  C CE  A LYS   A 19  ? 0.1953 0.1851 0.1766 0.0072  0.0491  0.0127  19  LYS   A CE  
484  C CE  B LYS   A 19  ? 0.2125 0.2250 0.2543 -0.0087 0.0547  0.0436  19  LYS   A CE  
485  N NZ  A LYS   A 19  ? 0.1989 0.1908 0.1777 0.0093  0.0526  0.0095  19  LYS   A NZ  
486  N NZ  B LYS   A 19  ? 0.2255 0.2373 0.2513 -0.0076 0.0580  0.0347  19  LYS   A NZ  
513  N N   A ASN   A 20  ? 0.1645 0.1710 0.1690 -0.0021 0.0514  0.0109  20  ASN   A N   
514  N N   B ASN   A 20  ? 0.1498 0.1535 0.2723 0.0042  0.0692  0.0617  20  ASN   A N   
515  C CA  A ASN   A 20  ? 0.1682 0.1761 0.1667 0.0082  0.0539  0.0087  20  ASN   A CA  
516  C CA  B ASN   A 20  ? 0.1535 0.1686 0.2549 0.0225  0.0600  0.0546  20  ASN   A CA  
517  C C   A ASN   A 20  ? 0.1709 0.1717 0.1601 0.0118  0.0604  0.0171  20  ASN   A C   
518  C C   B ASN   A 20  ? 0.1684 0.1739 0.2457 0.0253  0.0618  0.0565  20  ASN   A C   
519  O O   A ASN   A 20  ? 0.1766 0.1783 0.1558 0.0045  0.0645  0.0241  20  ASN   A O   
520  O O   B ASN   A 20  ? 0.1891 0.2038 0.2454 0.0128  0.0606  0.0504  20  ASN   A O   
521  C CB  A ASN   A 20  ? 0.1763 0.1829 0.1814 0.0106  0.0541  0.0007  20  ASN   A CB  
522  C CB  B ASN   A 20  ? 0.1453 0.1766 0.2516 0.0191  0.0573  0.0435  20  ASN   A CB  
523  C CG  A ASN   A 20  ? 0.1878 0.1882 0.1952 0.0162  0.0531  0.0028  20  ASN   A CG  
524  C CG  B ASN   A 20  ? 0.1441 0.1753 0.2494 0.0232  0.0385  0.0449  20  ASN   A CG  
525  O OD1 A ASN   A 20  ? 0.1999 0.2007 0.2169 0.0184  0.0501  0.0068  20  ASN   A OD1 
526  O OD1 B ASN   A 20  ? 0.1416 0.1846 0.2651 0.0299  0.0340  0.0311  20  ASN   A OD1 
527  N ND2 A ASN   A 20  ? 0.1858 0.1787 0.1895 0.0170  0.0528  -0.0054 20  ASN   A ND2 
528  N ND2 B ASN   A 20  ? 0.1521 0.1763 0.2591 0.0218  0.0284  0.0527  20  ASN   A ND2 
541  N N   A ALA   A 21  ? 0.1682 0.1702 0.1590 0.0143  0.0484  0.0119  21  ALA   A N   
542  N N   B ALA   A 21  ? 0.1768 0.1727 0.2452 0.0160  0.0643  0.0466  21  ALA   A N   
543  C CA  A ALA   A 21  ? 0.1684 0.1681 0.1663 0.0128  0.0371  0.0165  21  ALA   A CA  
544  C CA  B ALA   A 21  ? 0.1868 0.1702 0.2416 0.0058  0.0583  0.0479  21  ALA   A CA  
545  C C   A ALA   A 21  ? 0.1731 0.1703 0.1798 0.0152  0.0255  0.0126  21  ALA   A C   
546  C C   B ALA   A 21  ? 0.1781 0.1572 0.2245 0.0044  0.0649  0.0304  21  ALA   A C   
547  O O   A ALA   A 21  ? 0.1773 0.1781 0.1875 0.0109  0.0241  0.0096  21  ALA   A O   
548  O O   B ALA   A 21  ? 0.1789 0.1536 0.2277 -0.0093 0.0694  0.0159  21  ALA   A O   
549  C CB  A ALA   A 21  ? 0.1658 0.1696 0.1731 0.0103  0.0370  0.0201  21  ALA   A CB  
550  C CB  B ALA   A 21  ? 0.2071 0.1914 0.2660 0.0026  0.0461  0.0534  21  ALA   A CB  
561  N N   A ASP   A 22  ? 0.1773 0.1664 0.1872 0.0177  0.0206  0.0126  22  ASP   A N   
562  N N   B ASP   A 22  ? 0.1747 0.1543 0.2198 0.0054  0.0677  0.0258  22  ASP   A N   
563  C CA  A ASP   A 22  ? 0.1829 0.1618 0.1777 0.0177  0.0146  0.0183  22  ASP   A CA  
564  C CA  B ASP   A 22  ? 0.1761 0.1539 0.2062 0.0016  0.0636  0.0171  22  ASP   A CA  
565  C C   A ASP   A 22  ? 0.1806 0.1665 0.1604 0.0151  0.0162  0.0281  22  ASP   A C   
566  C C   B ASP   A 22  ? 0.1601 0.1485 0.1765 -0.0097 0.0662  0.0166  22  ASP   A C   
567  O O   A ASP   A 22  ? 0.1834 0.1699 0.1486 0.0110  0.0211  0.0362  22  ASP   A O   
568  O O   B ASP   A 22  ? 0.1685 0.1611 0.1816 -0.0135 0.0589  0.0057  22  ASP   A O   
569  C CB  A ASP   A 22  ? 0.1942 0.1497 0.1856 0.0205  0.0169  0.0054  22  ASP   A CB  
570  C CB  B ASP   A 22  ? 0.1994 0.1606 0.2266 0.0138  0.0682  0.0065  22  ASP   A CB  
571  C CG  A ASP   A 22  ? 0.1993 0.1345 0.1811 0.0220  0.0109  -0.0022 22  ASP   A CG  
572  C CG  B ASP   A 22  ? 0.2137 0.1576 0.2515 0.0239  0.0546  0.0112  22  ASP   A CG  
573  O OD1 A ASP   A 22  ? 0.2010 0.1241 0.1754 0.0019  0.0008  -0.0012 22  ASP   A OD1 
574  O OD1 B ASP   A 22  ? 0.2130 0.1596 0.2367 0.0138  0.0582  0.0231  22  ASP   A OD1 
575  O OD2 A ASP   A 22  ? 0.1976 0.1407 0.1952 0.0373  0.0182  -0.0060 22  ASP   A OD2 
576  O OD2 B ASP   A 22  ? 0.2297 0.1757 0.3039 0.0252  0.0378  0.0109  22  ASP   A OD2 
585  N N   A ILE   A 23  ? 0.1790 0.1669 0.1594 0.0122  0.0218  0.0246  23  ILE   A N   
586  N N   B ILE   A 23  ? 0.1547 0.1470 0.1675 -0.0059 0.0488  0.0187  23  ILE   A N   
587  C CA  A ILE   A 23  ? 0.1780 0.1595 0.1595 0.0107  0.0316  0.0176  23  ILE   A CA  
588  C CA  B ILE   A 23  ? 0.1576 0.1531 0.1628 -0.0094 0.0360  0.0251  23  ILE   A CA  
589  C C   A ILE   A 23  ? 0.1761 0.1611 0.1575 0.0109  0.0359  0.0155  23  ILE   A C   
590  C C   B ILE   A 23  ? 0.1627 0.1613 0.1569 -0.0187 0.0482  0.0139  23  ILE   A C   
591  O O   A ILE   A 23  ? 0.1803 0.1637 0.1604 0.0102  0.0326  0.0134  23  ILE   A O   
592  O O   B ILE   A 23  ? 0.1697 0.1619 0.1667 -0.0181 0.0451  0.0111  23  ILE   A O   
593  C CB  A ILE   A 23  ? 0.1811 0.1543 0.1589 0.0090  0.0368  0.0081  23  ILE   A CB  
594  C CB  B ILE   A 23  ? 0.1567 0.1486 0.1520 -0.0012 0.0271  0.0216  23  ILE   A CB  
595  C CG1 A ILE   A 23  ? 0.1843 0.1543 0.1599 0.0129  0.0378  -0.0008 23  ILE   A CG1 
596  C CG1 B ILE   A 23  ? 0.1632 0.1485 0.1541 0.0008  0.0220  0.0110  23  ILE   A CG1 
597  C CG2 A ILE   A 23  ? 0.1795 0.1520 0.1630 0.0062  0.0407  0.0100  23  ILE   A CG2 
598  C CG2 B ILE   A 23  ? 0.1519 0.1503 0.1472 0.0014  0.0220  0.0256  23  ILE   A CG2 
599  C CD1 A ILE   A 23  ? 0.1823 0.1533 0.1645 0.0156  0.0379  -0.0069 23  ILE   A CD1 
600  C CD1 B ILE   A 23  ? 0.1592 0.1539 0.1706 -0.0012 0.0127  0.0028  23  ILE   A CD1 
623  N N   A VAL   A 24  ? 0.1793 0.1623 0.1641 0.0102  0.0339  0.0132  24  VAL   A N   
624  N N   B VAL   A 24  ? 0.1812 0.1673 0.1770 -0.0235 0.0467  0.0023  24  VAL   A N   
625  C CA  A VAL   A 24  ? 0.1822 0.1689 0.1752 0.0053  0.0341  0.0090  24  VAL   A CA  
626  C CA  B VAL   A 24  ? 0.1992 0.1697 0.1962 -0.0249 0.0444  -0.0061 24  VAL   A CA  
627  C C   A VAL   A 24  ? 0.1889 0.1840 0.1798 -0.0002 0.0249  0.0111  24  VAL   A C   
628  C C   B VAL   A 24  ? 0.2091 0.1806 0.1940 -0.0221 0.0527  -0.0191 24  VAL   A C   
629  O O   A VAL   A 24  ? 0.1960 0.1892 0.1797 -0.0026 0.0196  0.0151  24  VAL   A O   
630  O O   B VAL   A 24  ? 0.2218 0.1950 0.1992 -0.0206 0.0497  -0.0205 24  VAL   A O   
631  C CB  A VAL   A 24  ? 0.1794 0.1638 0.1875 0.0036  0.0463  0.0073  24  VAL   A CB  
632  C CB  B VAL   A 24  ? 0.2072 0.1730 0.2356 -0.0309 0.0402  0.0047  24  VAL   A CB  
633  C CG1 A VAL   A 24  ? 0.1782 0.1665 0.1900 0.0053  0.0499  -0.0068 24  VAL   A CG1 
634  C CG1 B VAL   A 24  ? 0.2213 0.1770 0.2642 -0.0315 0.0212  -0.0013 24  VAL   A CG1 
635  C CG2 A VAL   A 24  ? 0.1824 0.1607 0.1849 0.0018  0.0547  0.0166  24  VAL   A CG2 
636  C CG2 B VAL   A 24  ? 0.2162 0.1809 0.2403 -0.0268 0.0442  0.0150  24  VAL   A CG2 
655  N N   A GLU   A 25  ? 0.1936 0.1969 0.1843 -0.0049 0.0248  0.0050  25  GLU   A N   
656  N N   B GLU   A 25  ? 0.2135 0.1924 0.1897 -0.0180 0.0774  -0.0236 25  GLU   A N   
657  C CA  A GLU   A 25  ? 0.2060 0.2103 0.1923 -0.0084 0.0252  0.0096  25  GLU   A CA  
658  C CA  B GLU   A 25  ? 0.2309 0.2118 0.1961 -0.0250 0.0883  -0.0305 25  GLU   A CA  
659  C C   A GLU   A 25  ? 0.1968 0.2114 0.1686 -0.0164 0.0299  0.0136  25  GLU   A C   
660  C C   B GLU   A 25  ? 0.2272 0.2165 0.1737 -0.0229 0.0833  -0.0263 25  GLU   A C   
661  O O   A GLU   A 25  ? 0.1967 0.2138 0.1635 -0.0138 0.0302  0.0124  25  GLU   A O   
662  O O   B GLU   A 25  ? 0.2407 0.2252 0.1796 -0.0167 0.0773  -0.0281 25  GLU   A O   
663  C CB  A GLU   A 25  ? 0.2245 0.2248 0.2275 -0.0060 0.0213  0.0111  25  GLU   A CB  
664  C CB  B GLU   A 25  ? 0.2491 0.2216 0.2235 -0.0295 0.1089  -0.0245 25  GLU   A CB  
665  C CG  A GLU   A 25  ? 0.2429 0.2371 0.2662 -0.0118 0.0110  0.0066  25  GLU   A CG  
666  C CG  B GLU   A 25  ? 0.2843 0.2406 0.2820 -0.0335 0.1036  -0.0168 25  GLU   A CG  
667  C CD  A GLU   A 25  ? 0.2549 0.2471 0.2991 -0.0218 0.0074  0.0081  25  GLU   A CD  
668  C CD  B GLU   A 25  ? 0.3135 0.2613 0.3311 -0.0310 0.0981  -0.0141 25  GLU   A CD  
669  O OE1 A GLU   A 25  ? 0.2567 0.2502 0.3061 -0.0246 0.0021  0.0046  25  GLU   A OE1 
670  O OE1 B GLU   A 25  ? 0.3235 0.2687 0.3459 -0.0216 0.0962  -0.0163 25  GLU   A OE1 
671  O OE2 A GLU   A 25  ? 0.2599 0.2522 0.3165 -0.0277 0.0076  0.0036  25  GLU   A OE2 
672  O OE2 B GLU   A 25  ? 0.3285 0.2700 0.3608 -0.0300 0.0936  -0.0121 25  GLU   A OE2 
685  N N   A GLU   A 26  ? 0.1916 0.2107 0.1653 -0.0255 0.0346  0.0098  26  GLU   A N   
686  N N   B GLU   A 26  ? 0.2139 0.2070 0.1741 -0.0297 0.0817  -0.0191 26  GLU   A N   
687  C CA  A GLU   A 26  ? 0.1964 0.2144 0.1707 -0.0334 0.0366  0.0117  26  GLU   A CA  
688  C CA  B GLU   A 26  ? 0.2140 0.2007 0.1726 -0.0382 0.0836  -0.0036 26  GLU   A CA  
689  C C   A GLU   A 26  ? 0.1966 0.2159 0.1628 -0.0302 0.0334  0.0143  26  GLU   A C   
690  C C   B GLU   A 26  ? 0.2095 0.1984 0.1443 -0.0389 0.0692  -0.0095 26  GLU   A C   
691  O O   A GLU   A 26  ? 0.1949 0.2145 0.1632 -0.0336 0.0372  0.0175  26  GLU   A O   
692  O O   B GLU   A 26  ? 0.2196 0.2074 0.1578 -0.0419 0.0629  -0.0108 26  GLU   A O   
693  C CB  A GLU   A 26  ? 0.2022 0.2175 0.1896 -0.0398 0.0393  0.0133  26  GLU   A CB  
694  C CB  B GLU   A 26  ? 0.2228 0.2006 0.2018 -0.0411 0.0796  0.0073  26  GLU   A CB  
695  C CG  A GLU   A 26  ? 0.2132 0.2251 0.2204 -0.0408 0.0438  0.0125  26  GLU   A CG  
696  C CG  B GLU   A 26  ? 0.2364 0.2063 0.2377 -0.0459 0.0875  -0.0027 26  GLU   A CG  
697  C CD  A GLU   A 26  ? 0.2252 0.2332 0.2430 -0.0434 0.0495  0.0135  26  GLU   A CD  
698  C CD  B GLU   A 26  ? 0.2528 0.2111 0.2597 -0.0527 0.0963  -0.0095 26  GLU   A CD  
699  O OE1 A GLU   A 26  ? 0.2263 0.2438 0.2475 -0.0365 0.0603  0.0171  26  GLU   A OE1 
700  O OE1 B GLU   A 26  ? 0.2573 0.2255 0.2668 -0.0520 0.1135  -0.0090 26  GLU   A OE1 
701  O OE2 A GLU   A 26  ? 0.2364 0.2374 0.2491 -0.0470 0.0511  0.0162  26  GLU   A OE2 
702  O OE2 B GLU   A 26  ? 0.2644 0.2190 0.2477 -0.0470 0.0961  -0.0054 26  GLU   A OE2 
715  N N   A ALA   A 27  ? 0.2009 0.2218 0.1668 -0.0252 0.0256  0.0142  27  ALA   A N   
716  N N   B ALA   A 27  ? 0.1986 0.1880 0.1461 -0.0343 0.0560  -0.0074 27  ALA   A N   
717  C CA  A ALA   A 27  ? 0.2144 0.2343 0.1730 -0.0231 0.0232  0.0123  27  ALA   A CA  
718  C CA  B ALA   A 27  ? 0.1976 0.1959 0.1481 -0.0327 0.0542  -0.0076 27  ALA   A CA  
719  C C   A ALA   A 27  ? 0.2366 0.2522 0.1805 -0.0253 0.0227  0.0054  27  ALA   A C   
720  C C   B ALA   A 27  ? 0.2214 0.2142 0.1469 -0.0345 0.0594  -0.0167 27  ALA   A C   
721  O O   A ALA   A 27  ? 0.2415 0.2535 0.1792 -0.0265 0.0194  0.0083  27  ALA   A O   
722  O O   B ALA   A 27  ? 0.2320 0.2169 0.1556 -0.0342 0.0427  -0.0066 27  ALA   A O   
723  C CB  A ALA   A 27  ? 0.2092 0.2313 0.1729 -0.0225 0.0223  0.0117  27  ALA   A CB  
724  C CB  B ALA   A 27  ? 0.1818 0.1895 0.1548 -0.0330 0.0479  -0.0041 27  ALA   A CB  
735  N N   A LYS   A 28  ? 0.2585 0.2694 0.1995 -0.0263 0.0179  -0.0044 28  LYS   A N   
736  N N   B LYS   A 28  ? 0.2509 0.2325 0.1608 -0.0350 0.0530  -0.0418 28  LYS   A N   
737  C CA  A LYS   A 28  ? 0.2824 0.2905 0.2248 -0.0232 0.0181  -0.0153 28  LYS   A CA  
738  C CA  B LYS   A 28  ? 0.2882 0.2670 0.1899 -0.0233 0.0519  -0.0529 28  LYS   A CA  
739  C C   A LYS   A 28  ? 0.2970 0.3068 0.2275 -0.0316 0.0213  -0.0158 28  LYS   A C   
740  C C   B LYS   A 28  ? 0.3192 0.3011 0.1819 -0.0307 0.0568  -0.0471 28  LYS   A C   
741  O O   A LYS   A 28  ? 0.2979 0.3096 0.2303 -0.0339 0.0103  -0.0196 28  LYS   A O   
742  O O   B LYS   A 28  ? 0.3310 0.3096 0.2093 -0.0318 0.0303  -0.0475 28  LYS   A O   
743  C CB  A LYS   A 28  ? 0.2922 0.2978 0.2515 -0.0115 0.0126  -0.0223 28  LYS   A CB  
744  C CB  B LYS   A 28  ? 0.2982 0.2739 0.2163 -0.0085 0.0565  -0.0606 28  LYS   A CB  
745  C CG  A LYS   A 28  ? 0.2990 0.3030 0.2740 -0.0029 0.0112  -0.0229 28  LYS   A CG  
746  C CG  B LYS   A 28  ? 0.3121 0.2867 0.2493 0.0059  0.0527  -0.0567 28  LYS   A CG  
747  C CD  A LYS   A 28  ? 0.3051 0.3107 0.3011 0.0025  0.0085  -0.0207 28  LYS   A CD  
748  C CD  B LYS   A 28  ? 0.3302 0.3090 0.3069 0.0166  0.0418  -0.0457 28  LYS   A CD  
749  C CE  A LYS   A 28  ? 0.3109 0.3168 0.3187 0.0047  0.0055  -0.0167 28  LYS   A CE  
750  C CE  B LYS   A 28  ? 0.3475 0.3292 0.3554 0.0229  0.0358  -0.0428 28  LYS   A CE  
751  N NZ  A LYS   A 28  ? 0.3146 0.3192 0.3308 0.0056  0.0055  -0.0149 28  LYS   A NZ  
752  N NZ  B LYS   A 28  ? 0.3593 0.3389 0.3810 0.0256  0.0314  -0.0421 28  LYS   A NZ  
779  N N   A LYS   A 29  ? 0.3113 0.3201 0.2406 -0.0380 0.0334  -0.0104 29  LYS   A N   
780  N N   B LYS   A 29  ? 0.3320 0.3267 0.1763 -0.0417 0.1040  -0.0281 29  LYS   A N   
781  C CA  A LYS   A 29  ? 0.3281 0.3344 0.2631 -0.0424 0.0404  -0.0059 29  LYS   A CA  
782  C CA  B LYS   A 29  ? 0.3526 0.3523 0.2080 -0.0520 0.1249  -0.0088 29  LYS   A CA  
783  C C   A LYS   A 29  ? 0.3323 0.3308 0.2433 -0.0489 0.0400  -0.0002 29  LYS   A C   
784  C C   B LYS   A 29  ? 0.3520 0.3465 0.1913 -0.0653 0.1111  0.0064  29  LYS   A C   
785  O O   A LYS   A 29  ? 0.3354 0.3350 0.2446 -0.0485 0.0370  -0.0042 29  LYS   A O   
786  O O   B LYS   A 29  ? 0.3579 0.3554 0.2091 -0.0649 0.1044  0.0004  29  LYS   A O   
787  C CB  A LYS   A 29  ? 0.3389 0.3501 0.3049 -0.0385 0.0454  -0.0048 29  LYS   A CB  
788  C CB  B LYS   A 29  ? 0.3723 0.3816 0.2607 -0.0443 0.1520  -0.0015 29  LYS   A CB  
789  C CG  A LYS   A 29  ? 0.3506 0.3638 0.3508 -0.0347 0.0472  -0.0041 29  LYS   A CG  
790  C CG  B LYS   A 29  ? 0.3966 0.4092 0.3359 -0.0341 0.1567  0.0038  29  LYS   A CG  
791  C CD  A LYS   A 29  ? 0.3612 0.3765 0.3952 -0.0311 0.0470  -0.0038 29  LYS   A CD  
792  C CD  B LYS   A 29  ? 0.4167 0.4314 0.4107 -0.0251 0.1560  0.0036  29  LYS   A CD  
793  C CE  A LYS   A 29  ? 0.3682 0.3849 0.4257 -0.0287 0.0481  -0.0039 29  LYS   A CE  
794  C CE  B LYS   A 29  ? 0.4308 0.4475 0.4633 -0.0178 0.1564  0.0005  29  LYS   A CE  
795  N NZ  A LYS   A 29  ? 0.3707 0.3882 0.4450 -0.0274 0.0483  -0.0039 29  LYS   A NZ  
796  N NZ  B LYS   A 29  ? 0.4396 0.4564 0.4988 -0.0131 0.1559  -0.0043 29  LYS   A NZ  
823  N N   A VAL   A 30  ? 0.3321 0.3215 0.2275 -0.0550 0.0419  0.0087  30  VAL   A N   
824  N N   B VAL   A 30  ? 0.3412 0.3282 0.1748 -0.0784 0.1066  0.0235  30  VAL   A N   
825  C CA  A VAL   A 30  ? 0.3337 0.3146 0.2128 -0.0609 0.0381  0.0208  30  VAL   A CA  
826  C CA  B VAL   A 30  ? 0.3388 0.3187 0.1703 -0.0846 0.0783  0.0412  30  VAL   A CA  
827  C C   A VAL   A 30  ? 0.3359 0.3095 0.1733 -0.0691 0.0398  0.0282  30  VAL   A C   
828  C C   B VAL   A 30  ? 0.3387 0.3088 0.1405 -0.0843 0.0568  0.0452  30  VAL   A C   
829  O O   A VAL   A 30  ? 0.3389 0.3097 0.1798 -0.0713 0.0378  0.0265  30  VAL   A O   
830  O O   B VAL   A 30  ? 0.3455 0.3064 0.1513 -0.0921 0.0483  0.0522  30  VAL   A O   
831  C CB  A VAL   A 30  ? 0.3347 0.3122 0.2374 -0.0570 0.0315  0.0239  30  VAL   A CB  
832  C CB  B VAL   A 30  ? 0.3421 0.3205 0.2145 -0.0862 0.0630  0.0463  30  VAL   A CB  
833  C CG1 A VAL   A 30  ? 0.3360 0.3113 0.2496 -0.0549 0.0268  0.0240  30  VAL   A CG1 
834  C CG1 B VAL   A 30  ? 0.3458 0.3194 0.2334 -0.0848 0.0526  0.0532  30  VAL   A CG1 
835  C CG2 A VAL   A 30  ? 0.3350 0.3110 0.2462 -0.0569 0.0312  0.0275  30  VAL   A CG2 
836  C CG2 B VAL   A 30  ? 0.3420 0.3239 0.2398 -0.0897 0.0602  0.0413  30  VAL   A CG2 
855  N N   . LYS   A 31  ? 0.3334 0.3040 0.1391 -0.0751 0.0425  0.0359  31  LYS   A N   
856  C CA  . LYS   A 31  ? 0.3393 0.3089 0.1569 -0.0653 0.0159  0.0260  31  LYS   A CA  
857  C C   . LYS   A 31  ? 0.3102 0.2806 0.1132 -0.0530 0.0040  0.0509  31  LYS   A C   
858  O O   . LYS   A 31  ? 0.3120 0.2901 0.1353 -0.0506 -0.0098 0.0547  31  LYS   A O   
859  C CB  . LYS   A 31  ? 0.3808 0.3498 0.2851 -0.0546 0.0033  0.0036  31  LYS   A CB  
860  C CG  . LYS   A 31  ? 0.4266 0.3933 0.4376 -0.0398 -0.0100 -0.0112 31  LYS   A CG  
861  C CD  . LYS   A 31  ? 0.4629 0.4282 0.5535 -0.0268 -0.0223 -0.0237 31  LYS   A CD  
862  C CE  . LYS   A 31  ? 0.4902 0.4649 0.6322 -0.0165 -0.0323 -0.0345 31  LYS   A CE  
863  N NZ  . LYS   A 31  ? 0.5032 0.4700 0.6765 -0.0113 -0.0384 -0.0408 31  LYS   A NZ  
878  N N   . PRO   A 32  ? 0.2773 0.2431 0.1045 -0.0488 0.0098  0.0310  32  PRO   A N   
879  C CA  . PRO   A 32  ? 0.2664 0.2273 0.1324 -0.0429 0.0003  0.0452  32  PRO   A CA  
880  C C   . PRO   A 32  ? 0.2589 0.2241 0.1369 -0.0341 -0.0060 0.0555  32  PRO   A C   
881  O O   . PRO   A 32  ? 0.2554 0.2127 0.1577 -0.0321 -0.0168 0.0536  32  PRO   A O   
882  C CB  . PRO   A 32  ? 0.2607 0.2293 0.1540 -0.0458 0.0034  0.0281  32  PRO   A CB  
883  C CG  . PRO   A 32  ? 0.2581 0.2330 0.1146 -0.0385 -0.0024 0.0200  32  PRO   A CG  
884  C CD  . PRO   A 32  ? 0.2623 0.2311 0.0994 -0.0429 0.0063  0.0247  32  PRO   A CD  
892  N N   . THR   A 33  ? 0.2584 0.2275 0.1405 -0.0275 -0.0046 0.0516  33  THR   A N   
893  C CA  . THR   A 33  ? 0.2512 0.2277 0.1416 -0.0180 -0.0185 0.0509  33  THR   A CA  
894  C C   . THR   A 33  ? 0.2216 0.2100 0.1308 -0.0242 -0.0199 0.0418  33  THR   A C   
895  O O   . THR   A 33  ? 0.2210 0.2192 0.1403 -0.0282 -0.0279 0.0348  33  THR   A O   
896  C CB  . THR   A 33  ? 0.2782 0.2493 0.1596 -0.0031 -0.0170 0.0665  33  THR   A CB  
897  O OG1 . THR   A 33  ? 0.3014 0.2628 0.1904 0.0100  -0.0061 0.0708  33  THR   A OG1 
898  C CG2 . THR   A 33  ? 0.2818 0.2588 0.1694 0.0023  -0.0194 0.0568  33  THR   A CG2 
906  N N   . VAL   A 34  ? 0.1921 0.1958 0.1275 -0.0241 -0.0100 0.0347  34  VAL   A N   
907  C CA  . VAL   A 34  ? 0.1801 0.1723 0.1168 -0.0193 -0.0047 0.0345  34  VAL   A CA  
908  C C   . VAL   A 34  ? 0.1710 0.1683 0.1200 -0.0238 0.0036  0.0277  34  VAL   A C   
909  O O   . VAL   A 34  ? 0.1738 0.1643 0.1455 -0.0311 0.0038  0.0312  34  VAL   A O   
910  C CB  . VAL   A 34  ? 0.1888 0.1672 0.1367 -0.0198 0.0054  0.0289  34  VAL   A CB  
911  C CG1 . VAL   A 34  ? 0.2037 0.1712 0.1374 -0.0157 0.0152  0.0057  34  VAL   A CG1 
912  C CG2 . VAL   A 34  ? 0.2007 0.1811 0.1654 -0.0080 -0.0096 0.0256  34  VAL   A CG2 
922  N N   . VAL   A 35  ? 0.1563 0.1572 0.1185 -0.0256 0.0058  0.0212  35  VAL   A N   
923  C CA  . VAL   A 35  ? 0.1483 0.1556 0.1182 -0.0186 0.0089  0.0118  35  VAL   A CA  
924  C C   . VAL   A 35  ? 0.1428 0.1395 0.1042 -0.0139 0.0093  0.0065  35  VAL   A C   
925  O O   . VAL   A 35  ? 0.1341 0.1511 0.1310 -0.0195 0.0167  0.0082  35  VAL   A O   
926  C CB  . VAL   A 35  ? 0.1560 0.1562 0.1271 -0.0132 0.0258  0.0105  35  VAL   A CB  
927  C CG1 . VAL   A 35  ? 0.1696 0.1572 0.1451 -0.0098 0.0112  0.0042  35  VAL   A CG1 
928  C CG2 . VAL   A 35  ? 0.1560 0.1607 0.1472 -0.0073 0.0275  -0.0019 35  VAL   A CG2 
938  N N   . VAL   A 36  ? 0.1330 0.1380 0.1072 -0.0203 0.0190  0.0196  36  VAL   A N   
939  C CA  . VAL   A 36  ? 0.1253 0.1232 0.1195 -0.0127 0.0094  0.0109  36  VAL   A CA  
940  C C   . VAL   A 36  ? 0.1263 0.1263 0.1184 -0.0154 0.0110  0.0075  36  VAL   A C   
941  O O   . VAL   A 36  ? 0.1246 0.1266 0.1490 -0.0079 0.0221  0.0071  36  VAL   A O   
942  C CB  . VAL   A 36  ? 0.1236 0.1215 0.1286 -0.0093 0.0108  0.0123  36  VAL   A CB  
943  C CG1 . VAL   A 36  ? 0.1322 0.1270 0.1346 -0.0135 0.0124  0.0033  36  VAL   A CG1 
944  C CG2 . VAL   A 36  ? 0.1306 0.1249 0.1474 -0.0110 0.0065  0.0166  36  VAL   A CG2 
954  N N   A ASN   A 37  ? 0.1288 0.1237 0.1131 -0.0105 0.0095  0.0094  37  ASN   A N   
955  N N   B ASN   A 37  ? 0.1181 0.1193 0.1123 -0.0066 0.0097  0.0068  37  ASN   A N   
956  C CA  A ASN   A 37  ? 0.1313 0.1193 0.1146 -0.0036 0.0079  0.0127  37  ASN   A CA  
957  C CA  B ASN   A 37  ? 0.1129 0.1138 0.1120 0.0027  0.0110  0.0144  37  ASN   A CA  
958  C C   A ASN   A 37  ? 0.1307 0.1215 0.1228 -0.0026 0.0110  0.0142  37  ASN   A C   
959  C C   B ASN   A 37  ? 0.1054 0.1179 0.1142 -0.0006 0.0134  0.0145  37  ASN   A C   
960  O O   A ASN   A 37  ? 0.1384 0.1268 0.1269 -0.0001 0.0082  0.0145  37  ASN   A O   
961  O O   B ASN   A 37  ? 0.1147 0.1285 0.1223 0.0054  0.0080  0.0058  37  ASN   A O   
962  C CB  A ASN   A 37  ? 0.1332 0.1163 0.1143 -0.0038 0.0037  0.0073  37  ASN   A CB  
963  C CB  B ASN   A 37  ? 0.1114 0.1113 0.1238 0.0001  0.0057  0.0048  37  ASN   A CB  
964  C CG  A ASN   A 37  ? 0.1361 0.1158 0.1074 -0.0011 -0.0025 0.0099  37  ASN   A CG  
965  C CG  B ASN   A 37  ? 0.1123 0.1145 0.1273 0.0090  0.0024  0.0085  37  ASN   A CG  
966  O OD1 A ASN   A 37  ? 0.1364 0.1132 0.1068 -0.0054 -0.0053 0.0052  37  ASN   A OD1 
967  O OD1 B ASN   A 37  ? 0.1146 0.1201 0.1535 -0.0007 0.0084  0.0136  37  ASN   A OD1 
968  N ND2 A ASN   A 37  ? 0.1376 0.1161 0.1088 -0.0061 -0.0091 0.0231  37  ASN   A ND2 
969  N ND2 B ASN   A 37  ? 0.1176 0.1179 0.1325 0.0017  -0.0010 0.0202  37  ASN   A ND2 
982  N N   A ALA   A 38  ? 0.1272 0.1218 0.1308 -0.0008 0.0087  0.0086  38  ALA   A N   
983  N N   B ALA   A 38  ? 0.1164 0.1217 0.1162 -0.0008 0.0091  0.0054  38  ALA   A N   
984  C CA  A ALA   A 38  ? 0.1252 0.1108 0.1179 0.0037  0.0032  -0.0121 38  ALA   A CA  
985  C CA  B ALA   A 38  ? 0.1257 0.1253 0.1214 -0.0025 0.0013  0.0075  38  ALA   A CA  
986  C C   A ALA   A 38  ? 0.1245 0.1140 0.1090 -0.0025 0.0005  -0.0181 38  ALA   A C   
987  C C   B ALA   A 38  ? 0.1290 0.1210 0.1336 0.0010  -0.0089 0.0022  38  ALA   A C   
988  O O   A ALA   A 38  ? 0.1263 0.1155 0.1110 -0.0032 -0.0096 -0.0183 38  ALA   A O   
989  O O   B ALA   A 38  ? 0.1243 0.1185 0.1621 0.0044  -0.0119 0.0087  38  ALA   A O   
990  C CB  A ALA   A 38  ? 0.1244 0.1148 0.1210 -0.0012 -0.0046 -0.0216 38  ALA   A CB  
991  C CB  B ALA   A 38  ? 0.1290 0.1393 0.1355 -0.0135 -0.0065 0.0085  38  ALA   A CB  
1002 N N   A ALA   A 39  ? 0.1193 0.1107 0.1109 0.0018  0.0128  -0.0203 39  ALA   A N   
1003 N N   B ALA   A 39  ? 0.1313 0.1248 0.1357 0.0068  -0.0002 0.0131  39  ALA   A N   
1004 C CA  A ALA   A 39  ? 0.1143 0.1119 0.1184 0.0030  0.0091  -0.0117 39  ALA   A CA  
1005 C CA  B ALA   A 39  ? 0.1331 0.1202 0.1300 -0.0042 0.0008  0.0067  39  ALA   A CA  
1006 C C   A ALA   A 39  ? 0.1214 0.1217 0.1152 0.0041  -0.0029 -0.0029 39  ALA   A C   
1007 C C   B ALA   A 39  ? 0.1277 0.1154 0.1235 0.0022  -0.0021 0.0103  39  ALA   A C   
1008 O O   A ALA   A 39  ? 0.1226 0.1273 0.1112 0.0048  -0.0077 0.0031  39  ALA   A O   
1009 O O   B ALA   A 39  ? 0.1456 0.1214 0.1347 -0.0067 0.0075  0.0050  39  ALA   A O   
1010 C CB  A ALA   A 39  ? 0.1099 0.1192 0.1297 0.0072  0.0023  -0.0081 39  ALA   A CB  
1011 C CB  B ALA   A 39  ? 0.1444 0.1399 0.1330 -0.0080 -0.0035 0.0057  39  ALA   A CB  
1022 N N   A ASN   A 40  ? 0.1238 0.1289 0.1158 -0.0017 0.0042  -0.0011 40  ASN   A N   
1023 N N   B ASN   A 40  ? 0.1393 0.1255 0.1101 -0.0046 0.0083  0.0086  40  ASN   A N   
1024 C CA  A ASN   A 40  ? 0.1344 0.1244 0.1126 -0.0068 0.0036  0.0024  40  ASN   A CA  
1025 C CA  B ASN   A 40  ? 0.1500 0.1243 0.1246 -0.0016 -0.0037 0.0078  40  ASN   A CA  
1026 C C   A ASN   A 40  ? 0.1416 0.1145 0.1055 -0.0034 0.0114  0.0163  40  ASN   A C   
1027 C C   B ASN   A 40  ? 0.1543 0.1157 0.1172 -0.0008 0.0110  0.0141  40  ASN   A C   
1028 O O   A ASN   A 40  ? 0.1432 0.1119 0.1098 -0.0111 0.0066  0.0166  40  ASN   A O   
1029 O O   B ASN   A 40  ? 0.1426 0.1163 0.1209 -0.0049 0.0144  0.0119  40  ASN   A O   
1030 C CB  A ASN   A 40  ? 0.1399 0.1341 0.1216 -0.0069 0.0056  0.0044  40  ASN   A CB  
1031 C CB  B ASN   A 40  ? 0.1525 0.1305 0.1396 0.0015  -0.0163 0.0120  40  ASN   A CB  
1032 C CG  A ASN   A 40  ? 0.1406 0.1340 0.1431 -0.0022 0.0001  0.0068  40  ASN   A CG  
1033 C CG  B ASN   A 40  ? 0.1545 0.1289 0.1631 0.0019  -0.0326 0.0167  40  ASN   A CG  
1034 O OD1 A ASN   A 40  ? 0.1427 0.1298 0.1398 -0.0023 0.0030  0.0188  40  ASN   A OD1 
1035 O OD1 B ASN   A 40  ? 0.1588 0.1337 0.2019 0.0019  -0.0294 0.0016  40  ASN   A OD1 
1036 N ND2 A ASN   A 40  ? 0.1406 0.1430 0.1569 0.0017  -0.0046 -0.0057 40  ASN   A ND2 
1037 N ND2 B ASN   A 40  ? 0.1506 0.1333 0.1777 -0.0002 -0.0178 0.0020  40  ASN   A ND2 
1050 N N   A VAL   A 41  ? 0.1485 0.1145 0.1117 0.0013  0.0239  0.0204  41  VAL   A N   
1051 N N   B VAL   A 41  ? 0.1650 0.1228 0.1234 0.0050  0.0146  0.0138  41  VAL   A N   
1052 C CA  A VAL   A 41  ? 0.1544 0.1241 0.1282 0.0021  0.0246  0.0193  41  VAL   A CA  
1053 C CA  B VAL   A 41  ? 0.1696 0.1318 0.1367 0.0017  0.0303  0.0134  41  VAL   A CA  
1054 C C   A VAL   A 41  ? 0.1539 0.1261 0.1369 0.0041  0.0243  0.0190  41  VAL   A C   
1055 C C   B VAL   A 41  ? 0.1651 0.1237 0.1339 -0.0018 0.0326  0.0190  41  VAL   A C   
1056 O O   A VAL   A 41  ? 0.1504 0.1298 0.1530 0.0084  0.0252  0.0152  41  VAL   A O   
1057 O O   B VAL   A 41  ? 0.1650 0.1134 0.1598 -0.0001 0.0326  0.0075  41  VAL   A O   
1058 C CB  A VAL   A 41  ? 0.1595 0.1258 0.1199 -0.0010 0.0259  0.0215  41  VAL   A CB  
1059 C CB  B VAL   A 41  ? 0.1922 0.1510 0.1432 -0.0065 0.0454  0.0066  41  VAL   A CB  
1060 C CG1 A VAL   A 41  ? 0.1582 0.1218 0.1147 0.0091  0.0222  0.0182  41  VAL   A CG1 
1061 C CG1 B VAL   A 41  ? 0.2034 0.1572 0.1529 -0.0030 0.0497  -0.0119 41  VAL   A CG1 
1062 C CG2 A VAL   A 41  ? 0.1769 0.1385 0.1251 -0.0049 0.0306  0.0170  41  VAL   A CG2 
1063 C CG2 B VAL   A 41  ? 0.2173 0.1685 0.1450 -0.0122 0.0517  0.0034  41  VAL   A CG2 
1082 N N   . TYR   A 42  ? 0.1543 0.1216 0.1498 0.0005  0.0282  0.0232  42  TYR   A N   
1083 C CA  . TYR   A 42  ? 0.1551 0.1206 0.1499 0.0007  0.0274  0.0243  42  TYR   A CA  
1084 C C   . TYR   A 42  ? 0.1405 0.1202 0.1529 0.0005  0.0174  0.0193  42  TYR   A C   
1085 O O   . TYR   A 42  ? 0.1440 0.1234 0.1733 -0.0092 0.0210  0.0080  42  TYR   A O   
1086 C CB  . TYR   A 42  ? 0.1813 0.1246 0.1532 -0.0044 0.0230  0.0312  42  TYR   A CB  
1087 C CG  . TYR   A 42  ? 0.2000 0.1412 0.1512 -0.0004 0.0219  0.0362  42  TYR   A CG  
1088 C CD1 . TYR   A 42  ? 0.2090 0.1544 0.1621 -0.0040 0.0312  0.0337  42  TYR   A CD1 
1089 C CD2 . TYR   A 42  ? 0.2175 0.1680 0.1674 0.0034  0.0241  0.0277  42  TYR   A CD2 
1090 C CE1 . TYR   A 42  ? 0.2201 0.1692 0.1453 -0.0119 0.0320  0.0310  42  TYR   A CE1 
1091 C CE2 . TYR   A 42  ? 0.2296 0.1826 0.1681 -0.0104 0.0202  0.0292  42  TYR   A CE2 
1092 C CZ  . TYR   A 42  ? 0.2384 0.1824 0.1513 -0.0168 0.0312  0.0261  42  TYR   A CZ  
1093 O OH  . TYR   A 42  ? 0.2508 0.2140 0.1768 -0.0310 0.0351  0.0180  42  TYR   A OH  
1104 N N   A LEU   A 43  ? 0.1379 0.1265 0.1381 0.0009  0.0132  0.0146  43  LEU   A N   
1105 N N   B LEU   A 43  ? 0.1361 0.1170 0.1409 -0.0009 0.0134  0.0112  43  LEU   A N   
1106 C CA  A LEU   A 43  ? 0.1310 0.1317 0.1356 -0.0014 0.0077  0.0120  43  LEU   A CA  
1107 C CA  B LEU   A 43  ? 0.1230 0.1110 0.1447 -0.0067 0.0055  0.0100  43  LEU   A CA  
1108 C C   A LEU   A 43  ? 0.1379 0.1430 0.1353 -0.0044 0.0132  0.0057  43  LEU   A C   
1109 C C   B LEU   A 43  ? 0.1248 0.1149 0.1321 -0.0006 0.0075  0.0041  43  LEU   A C   
1110 O O   A LEU   A 43  ? 0.1418 0.1423 0.1451 -0.0051 0.0138  0.0085  43  LEU   A O   
1111 O O   B LEU   A 43  ? 0.1470 0.1189 0.1400 0.0066  -0.0075 0.0049  43  LEU   A O   
1112 C CB  A LEU   A 43  ? 0.1292 0.1304 0.1384 0.0018  0.0012  0.0107  43  LEU   A CB  
1113 C CB  B LEU   A 43  ? 0.1247 0.1069 0.1555 -0.0083 0.0109  0.0098  43  LEU   A CB  
1114 C CG  A LEU   A 43  ? 0.1328 0.1293 0.1366 0.0016  -0.0004 0.0083  43  LEU   A CG  
1115 C CG  B LEU   A 43  ? 0.1316 0.1169 0.1581 -0.0050 0.0081  0.0145  43  LEU   A CG  
1116 C CD1 A LEU   A 43  ? 0.1321 0.1298 0.1401 -0.0003 -0.0066 0.0108  43  LEU   A CD1 
1117 C CD1 B LEU   A 43  ? 0.1384 0.1252 0.1825 -0.0039 -0.0028 0.0246  43  LEU   A CD1 
1118 C CD2 A LEU   A 43  ? 0.1390 0.1293 0.1362 -0.0012 -0.0043 0.0063  43  LEU   A CD2 
1119 C CD2 B LEU   A 43  ? 0.1414 0.1181 0.1474 -0.0049 -0.0004 0.0209  43  LEU   A CD2 
1142 N N   A LYS   A 44  ? 0.1530 0.1542 0.1419 -0.0067 0.0120  0.0021  44  LYS   A N   
1143 N N   B LYS   A 44  ? 0.1318 0.1118 0.1335 -0.0003 0.0022  0.0090  44  LYS   A N   
1144 C CA  A LYS   A 44  ? 0.1636 0.1624 0.1566 -0.0123 0.0081  -0.0046 44  LYS   A CA  
1145 C CA  B LYS   A 44  ? 0.1383 0.1106 0.1392 -0.0011 0.0083  0.0207  44  LYS   A CA  
1146 C C   A LYS   A 44  ? 0.1562 0.1521 0.1344 -0.0032 -0.0020 -0.0104 44  LYS   A C   
1147 C C   B LYS   A 44  ? 0.1318 0.1113 0.1286 0.0068  -0.0042 0.0143  44  LYS   A C   
1148 O O   A LYS   A 44  ? 0.1616 0.1546 0.1332 -0.0004 -0.0099 -0.0241 44  LYS   A O   
1149 O O   B LYS   A 44  ? 0.1376 0.1281 0.1440 0.0000  -0.0035 0.0046  44  LYS   A O   
1150 C CB  A LYS   A 44  ? 0.1865 0.1815 0.1990 -0.0250 0.0081  -0.0059 44  LYS   A CB  
1151 C CB  B LYS   A 44  ? 0.1667 0.1300 0.1645 0.0103  0.0239  0.0468  44  LYS   A CB  
1152 C CG  A LYS   A 44  ? 0.2089 0.2040 0.2482 -0.0349 0.0169  -0.0029 44  LYS   A CG  
1153 C CG  B LYS   A 44  ? 0.1939 0.1682 0.2142 0.0053  0.0579  0.0605  44  LYS   A CG  
1154 C CD  A LYS   A 44  ? 0.2309 0.2284 0.3025 -0.0436 0.0209  -0.0009 44  LYS   A CD  
1155 C CD  B LYS   A 44  ? 0.2279 0.2341 0.3221 -0.0026 0.0476  0.0414  44  LYS   A CD  
1156 C CE  A LYS   A 44  ? 0.2453 0.2460 0.3420 -0.0475 0.0249  -0.0001 44  LYS   A CE  
1157 C CE  B LYS   A 44  ? 0.2427 0.2666 0.3932 -0.0046 0.0474  0.0283  44  LYS   A CE  
1158 N NZ  A LYS   A 44  ? 0.2553 0.2591 0.3672 -0.0483 0.0259  0.0007  44  LYS   A NZ  
1159 N NZ  B LYS   A 44  ? 0.2562 0.2875 0.4351 -0.0071 0.0442  0.0175  44  LYS   A NZ  
1186 N N   A HIS   A 45  ? 0.1448 0.1456 0.1327 0.0028  0.0005  -0.0013 45  HIS   A N   
1187 N N   B HIS   A 45  ? 0.1237 0.1091 0.1298 0.0013  -0.0052 0.0063  45  HIS   A N   
1188 C CA  A HIS   A 45  ? 0.1404 0.1397 0.1339 0.0041  -0.0062 -0.0014 45  HIS   A CA  
1189 C CA  B HIS   A 45  ? 0.1234 0.1161 0.1260 -0.0020 -0.0132 0.0068  45  HIS   A CA  
1190 C C   A HIS   A 45  ? 0.1369 0.1481 0.1540 0.0047  -0.0144 0.0029  45  HIS   A C   
1191 C C   B HIS   A 45  ? 0.1285 0.1210 0.1372 -0.0035 -0.0027 0.0039  45  HIS   A C   
1192 O O   A HIS   A 45  ? 0.1357 0.1554 0.1787 0.0082  -0.0249 -0.0051 45  HIS   A O   
1193 O O   B HIS   A 45  ? 0.1406 0.1254 0.1726 0.0034  -0.0053 -0.0038 45  HIS   A O   
1194 C CB  A HIS   A 45  ? 0.1461 0.1297 0.1295 0.0046  0.0068  -0.0037 45  HIS   A CB  
1195 C CB  B HIS   A 45  ? 0.1277 0.1195 0.1422 -0.0035 -0.0032 0.0026  45  HIS   A CB  
1196 C CG  A HIS   A 45  ? 0.1494 0.1179 0.1152 0.0010  0.0124  -0.0030 45  HIS   A CG  
1197 C CG  B HIS   A 45  ? 0.1219 0.1215 0.1279 -0.0086 -0.0018 0.0127  45  HIS   A CG  
1198 N ND1 A HIS   A 45  ? 0.1500 0.1188 0.1233 -0.0036 0.0180  -0.0047 45  HIS   A ND1 
1199 N ND1 B HIS   A 45  ? 0.1087 0.1259 0.1464 -0.0099 -0.0089 0.0178  45  HIS   A ND1 
1200 C CD2 A HIS   A 45  ? 0.1539 0.1237 0.1284 -0.0045 0.0063  0.0043  45  HIS   A CD2 
1201 C CD2 B HIS   A 45  ? 0.1177 0.1291 0.1410 -0.0073 -0.0098 0.0114  45  HIS   A CD2 
1202 C CE1 A HIS   A 45  ? 0.1525 0.1224 0.1242 -0.0057 0.0153  0.0060  45  HIS   A CE1 
1203 C CE1 B HIS   A 45  ? 0.1125 0.1262 0.1342 -0.0100 -0.0065 0.0221  45  HIS   A CE1 
1204 N NE2 A HIS   A 45  ? 0.1545 0.1258 0.1310 -0.0038 0.0107  0.0112  45  HIS   A NE2 
1205 N NE2 B HIS   A 45  ? 0.1143 0.1340 0.1405 -0.0026 -0.0027 0.0138  45  HIS   A NE2 
1220 N N   A GLY   A 46  ? 0.1389 0.1492 0.1524 0.0105  -0.0171 0.0176  46  GLY   A N   
1221 N N   B GLY   A 46  ? 0.1431 0.1270 0.1550 0.0014  -0.0105 0.0154  46  GLY   A N   
1222 C CA  A GLY   A 46  ? 0.1385 0.1420 0.1518 0.0097  -0.0222 0.0329  46  GLY   A CA  
1223 C CA  B GLY   A 46  ? 0.1470 0.1410 0.1741 0.0039  -0.0182 0.0182  46  GLY   A CA  
1224 C C   A GLY   A 46  ? 0.1436 0.1350 0.1542 0.0138  -0.0197 0.0423  46  GLY   A C   
1225 C C   B GLY   A 46  ? 0.1511 0.1351 0.1772 0.0078  -0.0141 0.0243  46  GLY   A C   
1226 O O   A GLY   A 46  ? 0.1601 0.1294 0.1876 0.0157  -0.0216 0.0548  46  GLY   A O   
1227 O O   B GLY   A 46  ? 0.1645 0.1444 0.2383 0.0031  -0.0122 0.0034  46  GLY   A O   
1234 N N   A GLY   A 47  ? 0.1349 0.1341 0.1552 0.0141  -0.0132 0.0327  47  GLY   A N   
1235 N N   B GLY   A 47  ? 0.1513 0.1395 0.1740 0.0078  -0.0074 0.0187  47  GLY   A N   
1236 C CA  A GLY   A 47  ? 0.1346 0.1385 0.1574 0.0175  -0.0107 0.0209  47  GLY   A CA  
1237 C CA  B GLY   A 47  ? 0.1442 0.1456 0.1714 0.0035  -0.0230 0.0233  47  GLY   A CA  
1238 C C   A GLY   A 47  ? 0.1288 0.1377 0.1534 0.0166  -0.0067 0.0126  47  GLY   A C   
1239 C C   B GLY   A 47  ? 0.1346 0.1394 0.1551 0.0122  -0.0163 0.0172  47  GLY   A C   
1240 O O   A GLY   A 47  ? 0.1301 0.1349 0.1741 0.0222  -0.0054 0.0199  47  GLY   A O   
1241 O O   B GLY   A 47  ? 0.1325 0.1343 0.1517 0.0113  -0.0167 0.0154  47  GLY   A O   
1248 N N   A GLY   A 48  ? 0.1266 0.1395 0.1531 0.0177  -0.0022 0.0057  48  GLY   A N   
1249 N N   B GLY   A 48  ? 0.1320 0.1368 0.1666 0.0199  -0.0069 0.0202  48  GLY   A N   
1250 C CA  A GLY   A 48  ? 0.1208 0.1394 0.1557 0.0103  0.0002  -0.0023 48  GLY   A CA  
1251 C CA  B GLY   A 48  ? 0.1269 0.1245 0.1499 0.0162  -0.0048 0.0129  48  GLY   A CA  
1252 C C   A GLY   A 48  ? 0.1214 0.1367 0.1508 0.0057  0.0029  -0.0076 48  GLY   A C   
1253 C C   B GLY   A 48  ? 0.1244 0.1259 0.1447 0.0033  -0.0021 0.0044  48  GLY   A C   
1254 O O   A GLY   A 48  ? 0.1243 0.1376 0.1505 0.0098  -0.0049 -0.0158 48  GLY   A O   
1255 O O   B GLY   A 48  ? 0.1346 0.1235 0.1405 0.0016  0.0021  -0.0078 48  GLY   A O   
1262 N N   A VAL   A 49  ? 0.1254 0.1287 0.1596 0.0035  0.0040  -0.0078 49  VAL   A N   
1263 N N   B VAL   A 49  ? 0.1202 0.1243 0.1405 -0.0013 -0.0017 -0.0032 49  VAL   A N   
1264 C CA  A VAL   A 49  ? 0.1348 0.1139 0.1541 0.0002  0.0075  -0.0041 49  VAL   A CA  
1265 C CA  B VAL   A 49  ? 0.1239 0.1200 0.1331 -0.0023 -0.0032 0.0054  49  VAL   A CA  
1266 C C   A VAL   A 49  ? 0.1322 0.1077 0.1467 0.0004  0.0086  0.0070  49  VAL   A C   
1267 C C   B VAL   A 49  ? 0.1227 0.1230 0.1300 -0.0014 -0.0019 -0.0037 49  VAL   A C   
1268 O O   A VAL   A 49  ? 0.1320 0.1045 0.1529 -0.0059 0.0132  -0.0060 49  VAL   A O   
1269 O O   B VAL   A 49  ? 0.1307 0.1259 0.1334 -0.0052 0.0036  -0.0077 49  VAL   A O   
1270 C CB  A VAL   A 49  ? 0.1481 0.1099 0.1641 -0.0078 0.0005  -0.0038 49  VAL   A CB  
1271 C CB  B VAL   A 49  ? 0.1279 0.1310 0.1510 -0.0004 -0.0097 0.0075  49  VAL   A CB  
1272 C CG1 A VAL   A 49  ? 0.1501 0.1091 0.1728 -0.0091 -0.0031 -0.0028 49  VAL   A CG1 
1273 C CG1 B VAL   A 49  ? 0.1238 0.1281 0.1581 0.0019  -0.0072 0.0144  49  VAL   A CG1 
1274 C CG2 A VAL   A 49  ? 0.1551 0.1080 0.1682 -0.0157 -0.0095 0.0002  49  VAL   A CG2 
1275 C CG2 B VAL   A 49  ? 0.1420 0.1427 0.1868 -0.0124 -0.0329 0.0093  49  VAL   A CG2 
1294 N N   A ALA   A 50  ? 0.1292 0.1094 0.1394 0.0047  0.0011  0.0149  50  ALA   A N   
1295 N N   B ALA   A 50  ? 0.1222 0.1206 0.1323 0.0009  -0.0011 -0.0031 50  ALA   A N   
1296 C CA  A ALA   A 50  ? 0.1283 0.1112 0.1257 0.0040  -0.0085 0.0201  50  ALA   A CA  
1297 C CA  B ALA   A 50  ? 0.1119 0.1190 0.1277 0.0019  0.0001  -0.0003 50  ALA   A CA  
1298 C C   A ALA   A 50  ? 0.1273 0.1145 0.1211 0.0017  -0.0089 0.0153  50  ALA   A C   
1299 C C   B ALA   A 50  ? 0.1114 0.1206 0.1270 -0.0029 0.0009  -0.0037 50  ALA   A C   
1300 O O   A ALA   A 50  ? 0.1336 0.1142 0.1206 0.0026  -0.0138 0.0214  50  ALA   A O   
1301 O O   B ALA   A 50  ? 0.1177 0.1264 0.1372 -0.0013 0.0003  -0.0068 50  ALA   A O   
1302 C CB  A ALA   A 50  ? 0.1300 0.1141 0.1326 0.0035  -0.0084 0.0227  50  ALA   A CB  
1303 C CB  B ALA   A 50  ? 0.1146 0.1239 0.1357 0.0008  0.0050  -0.0048 50  ALA   A CB  
1314 N N   A GLY   A 51  ? 0.1264 0.1193 0.1204 0.0057  -0.0098 0.0026  51  GLY   A N   
1315 N N   B GLY   A 51  ? 0.1237 0.1168 0.1485 0.0002  -0.0046 -0.0042 51  GLY   A N   
1316 C CA  A GLY   A 51  ? 0.1263 0.1225 0.1225 0.0087  -0.0051 0.0052  51  GLY   A CA  
1317 C CA  B GLY   A 51  ? 0.1362 0.1145 0.1523 -0.0016 -0.0058 -0.0001 51  GLY   A CA  
1318 C C   A GLY   A 51  ? 0.1148 0.1248 0.1100 0.0098  0.0008  0.0088  51  GLY   A C   
1319 C C   B GLY   A 51  ? 0.1239 0.1204 0.1526 0.0009  -0.0116 0.0009  51  GLY   A C   
1320 O O   A GLY   A 51  ? 0.1123 0.1273 0.1096 0.0087  0.0004  0.0036  51  GLY   A O   
1321 O O   B GLY   A 51  ? 0.1255 0.1271 0.1635 -0.0033 -0.0064 -0.0038 51  GLY   A O   
1328 N N   A ALA   A 52  ? 0.1144 0.1315 0.1200 0.0085  -0.0013 0.0129  52  ALA   A N   
1329 N N   B ALA   A 52  ? 0.1206 0.1256 0.1476 -0.0041 -0.0025 -0.0078 52  ALA   A N   
1330 C CA  A ALA   A 52  ? 0.1215 0.1350 0.1199 0.0057  -0.0020 0.0222  52  ALA   A CA  
1331 C CA  B ALA   A 52  ? 0.1218 0.1326 0.1513 -0.0018 0.0020  -0.0076 52  ALA   A CA  
1332 C C   A ALA   A 52  ? 0.1261 0.1322 0.1174 -0.0019 -0.0035 0.0242  52  ALA   A C   
1333 C C   B ALA   A 52  ? 0.1220 0.1294 0.1375 -0.0074 0.0022  -0.0174 52  ALA   A C   
1334 O O   A ALA   A 52  ? 0.1286 0.1365 0.1183 -0.0029 -0.0079 0.0186  52  ALA   A O   
1335 O O   B ALA   A 52  ? 0.1309 0.1320 0.1511 -0.0045 0.0055  -0.0121 52  ALA   A O   
1336 C CB  A ALA   A 52  ? 0.1267 0.1478 0.1245 0.0043  -0.0025 0.0207  52  ALA   A CB  
1337 C CB  B ALA   A 52  ? 0.1300 0.1581 0.1606 -0.0038 -0.0012 -0.0104 52  ALA   A CB  
1348 N N   A LEU   A 53  ? 0.1275 0.1321 0.1170 -0.0084 -0.0024 0.0291  53  LEU   A N   
1349 N N   B LEU   A 53  ? 0.1168 0.1330 0.1309 -0.0056 0.0022  -0.0117 53  LEU   A N   
1350 C CA  A LEU   A 53  ? 0.1340 0.1368 0.1225 -0.0085 0.0039  0.0233  53  LEU   A CA  
1351 C CA  B LEU   A 53  ? 0.1243 0.1352 0.1276 -0.0014 0.0043  -0.0066 53  LEU   A CA  
1352 C C   A LEU   A 53  ? 0.1367 0.1450 0.1103 -0.0054 0.0075  0.0228  53  LEU   A C   
1353 C C   B LEU   A 53  ? 0.1304 0.1411 0.1208 0.0083  -0.0048 -0.0107 53  LEU   A C   
1354 O O   A LEU   A 53  ? 0.1424 0.1524 0.1031 -0.0142 0.0151  0.0162  53  LEU   A O   
1355 O O   B LEU   A 53  ? 0.1447 0.1526 0.1418 -0.0016 0.0004  -0.0164 53  LEU   A O   
1356 C CB  A LEU   A 53  ? 0.1406 0.1371 0.1529 -0.0077 0.0068  0.0233  53  LEU   A CB  
1357 C CB  B LEU   A 53  ? 0.1236 0.1338 0.1166 0.0008  -0.0034 0.0039  53  LEU   A CB  
1358 C CG  A LEU   A 53  ? 0.1437 0.1357 0.1655 -0.0052 0.0079  0.0190  53  LEU   A CG  
1359 C CG  B LEU   A 53  ? 0.1333 0.1385 0.1199 -0.0004 -0.0002 0.0024  53  LEU   A CG  
1360 C CD1 A LEU   A 53  ? 0.1495 0.1385 0.1647 -0.0061 0.0163  0.0241  53  LEU   A CD1 
1361 C CD1 B LEU   A 53  ? 0.1414 0.1478 0.1227 0.0006  -0.0061 0.0010  53  LEU   A CD1 
1362 C CD2 A LEU   A 53  ? 0.1429 0.1415 0.1758 -0.0055 0.0012  0.0180  53  LEU   A CD2 
1363 C CD2 B LEU   A 53  ? 0.1502 0.1483 0.1221 -0.0057 0.0046  0.0032  53  LEU   A CD2 
1386 N N   A ASN   A 54  ? 0.1314 0.1446 0.1125 -0.0045 0.0047  0.0215  54  ASN   A N   
1387 N N   B ASN   A 54  ? 0.1194 0.1291 0.1223 0.0029  -0.0005 -0.0084 54  ASN   A N   
1388 C CA  A ASN   A 54  ? 0.1304 0.1435 0.1228 -0.0046 0.0005  0.0117  54  ASN   A CA  
1389 C CA  B ASN   A 54  ? 0.1165 0.1222 0.1314 -0.0030 -0.0067 -0.0106 54  ASN   A CA  
1390 C C   A ASN   A 54  ? 0.1296 0.1438 0.1249 -0.0070 0.0018  0.0031  54  ASN   A C   
1391 C C   B ASN   A 54  ? 0.1244 0.1309 0.1401 -0.0077 0.0010  -0.0047 54  ASN   A C   
1392 O O   A ASN   A 54  ? 0.1319 0.1485 0.1119 -0.0134 -0.0031 -0.0012 54  ASN   A O   
1393 O O   B ASN   A 54  ? 0.1281 0.1391 0.1460 -0.0052 -0.0009 -0.0167 54  ASN   A O   
1394 C CB  A ASN   A 54  ? 0.1326 0.1473 0.1365 -0.0037 0.0015  0.0162  54  ASN   A CB  
1395 C CB  B ASN   A 54  ? 0.1066 0.1237 0.1397 -0.0055 -0.0089 -0.0030 54  ASN   A CB  
1396 C CG  A ASN   A 54  ? 0.1387 0.1520 0.1489 -0.0013 0.0000  0.0169  54  ASN   A CG  
1397 C CG  B ASN   A 54  ? 0.1084 0.1222 0.1374 0.0001  -0.0064 -0.0034 54  ASN   A CG  
1398 O OD1 A ASN   A 54  ? 0.1456 0.1595 0.1629 0.0017  -0.0007 0.0196  54  ASN   A OD1 
1399 O OD1 B ASN   A 54  ? 0.1093 0.1209 0.1349 -0.0037 -0.0070 -0.0028 54  ASN   A OD1 
1400 N ND2 A ASN   A 54  ? 0.1431 0.1538 0.1546 -0.0043 -0.0069 0.0179  54  ASN   A ND2 
1401 N ND2 B ASN   A 54  ? 0.1230 0.1325 0.1546 -0.0123 -0.0171 0.0044  54  ASN   A ND2 
1414 N N   . LYS   A 55  ? 0.1235 0.1399 0.1484 0.0009  -0.0032 -0.0082 55  LYS   A N   
1415 C CA  . LYS   A 55  ? 0.1365 0.1435 0.1686 0.0066  -0.0002 -0.0172 55  LYS   A CA  
1416 C C   . LYS   A 55  ? 0.1335 0.1532 0.1680 0.0018  0.0085  -0.0214 55  LYS   A C   
1417 O O   . LYS   A 55  ? 0.1472 0.1619 0.1681 0.0021  0.0036  -0.0378 55  LYS   A O   
1418 C CB  . LYS   A 55  ? 0.1517 0.1624 0.2127 0.0246  -0.0125 -0.0335 55  LYS   A CB  
1419 C CG  . LYS   A 55  ? 0.1791 0.2018 0.2398 0.0494  -0.0108 -0.0453 55  LYS   A CG  
1420 C CD  . LYS   A 55  ? 0.2092 0.2537 0.2959 0.0767  0.0027  -0.0456 55  LYS   A CD  
1421 C CE  . LYS   A 55  ? 0.2331 0.2974 0.3447 0.0905  -0.0094 -0.0380 55  LYS   A CE  
1422 N NZ  . LYS   A 55  ? 0.2578 0.3153 0.3717 0.1009  -0.0155 -0.0264 55  LYS   A NZ  
1437 N N   . ALA   A 56  ? 0.1377 0.1624 0.1713 -0.0038 0.0133  -0.0270 56  ALA   A N   
1438 C CA  . ALA   A 56  ? 0.1495 0.1724 0.1701 -0.0122 0.0185  -0.0306 56  ALA   A CA  
1439 C C   . ALA   A 56  ? 0.1589 0.1843 0.1351 -0.0106 0.0205  -0.0335 56  ALA   A C   
1440 O O   . ALA   A 56  ? 0.1684 0.2213 0.1521 0.0030  0.0277  -0.0182 56  ALA   A O   
1441 C CB  . ALA   A 56  ? 0.1555 0.1888 0.1853 -0.0184 0.0138  -0.0056 56  ALA   A CB  
1447 N N   . THR   A 57  ? 0.1483 0.1658 0.1361 -0.0075 0.0092  -0.0221 57  THR   A N   
1448 C CA  . THR   A 57  ? 0.1521 0.1653 0.1409 -0.0093 0.0020  -0.0169 57  THR   A CA  
1449 C C   . THR   A 57  ? 0.1571 0.1686 0.1378 -0.0022 0.0017  -0.0248 57  THR   A C   
1450 O O   . THR   A 57  ? 0.1535 0.1685 0.1570 -0.0111 -0.0074 -0.0316 57  THR   A O   
1451 C CB  . THR   A 57  ? 0.1458 0.1658 0.1348 -0.0061 0.0012  -0.0172 57  THR   A CB  
1452 O OG1 . THR   A 57  ? 0.1304 0.1574 0.1318 -0.0081 0.0021  -0.0150 57  THR   A OG1 
1453 C CG2 . THR   A 57  ? 0.1462 0.1640 0.1422 -0.0048 0.0020  -0.0093 57  THR   A CG2 
1461 N N   . ASN   A 58  ? 0.1543 0.1622 0.1657 -0.0072 0.0014  -0.0337 58  ASN   A N   
1462 C CA  . ASN   A 58  ? 0.1729 0.1586 0.1903 -0.0104 0.0146  -0.0483 58  ASN   A CA  
1463 C C   . ASN   A 58  ? 0.1534 0.1424 0.1764 -0.0012 0.0014  -0.0296 58  ASN   A C   
1464 O O   . ASN   A 58  ? 0.1583 0.1571 0.1819 -0.0141 -0.0063 -0.0337 58  ASN   A O   
1465 C CB  . ASN   A 58  ? 0.2161 0.1784 0.2164 -0.0204 0.0284  -0.0613 58  ASN   A CB  
1466 C CG  . ASN   A 58  ? 0.2596 0.2003 0.2737 -0.0166 0.0221  -0.0587 58  ASN   A CG  
1467 O OD1 . ASN   A 58  ? 0.2851 0.1977 0.3067 0.0202  0.0546  -0.0464 58  ASN   A OD1 
1468 N ND2 . ASN   A 58  ? 0.2666 0.2135 0.2895 -0.0204 0.0084  -0.0598 58  ASN   A ND2 
1475 N N   . ASN   A 59  ? 0.1351 0.1337 0.1689 -0.0077 -0.0088 -0.0235 59  ASN   A N   
1476 C CA  . ASN   A 59  ? 0.1340 0.1308 0.1574 -0.0020 -0.0105 -0.0179 59  ASN   A CA  
1477 C C   . ASN   A 59  ? 0.1303 0.1304 0.1311 -0.0068 -0.0072 -0.0108 59  ASN   A C   
1478 O O   . ASN   A 59  ? 0.1292 0.1376 0.1398 -0.0079 0.0020  -0.0042 59  ASN   A O   
1479 C CB  . ASN   A 59  ? 0.1384 0.1271 0.1685 -0.0001 -0.0224 -0.0165 59  ASN   A CB  
1480 C CG  . ASN   A 59  ? 0.1407 0.1290 0.1658 -0.0042 -0.0244 0.0003  59  ASN   A CG  
1481 O OD1 . ASN   A 59  ? 0.1506 0.1379 0.1568 -0.0154 -0.0201 0.0017  59  ASN   A OD1 
1482 N ND2 . ASN   A 59  ? 0.1524 0.1383 0.1705 -0.0126 -0.0234 0.0019  59  ASN   A ND2 
1489 N N   . ALA   A 60  ? 0.1299 0.1368 0.1456 0.0005  -0.0115 -0.0126 60  ALA   A N   
1490 C CA  . ALA   A 60  ? 0.1290 0.1368 0.1407 -0.0036 -0.0177 -0.0101 60  ALA   A CA  
1491 C C   . ALA   A 60  ? 0.1308 0.1379 0.1512 -0.0024 -0.0064 -0.0028 60  ALA   A C   
1492 O O   . ALA   A 60  ? 0.1242 0.1356 0.1656 -0.0029 -0.0119 -0.0117 60  ALA   A O   
1493 C CB  . ALA   A 60  ? 0.1406 0.1503 0.1548 -0.0061 -0.0180 -0.0208 60  ALA   A CB  
1499 N N   . MET   A 61  ? 0.1263 0.1333 0.1390 -0.0056 -0.0038 -0.0116 61  MET   A N   
1500 C CA  . MET   A 61  ? 0.1268 0.1252 0.1426 -0.0071 -0.0066 -0.0041 61  MET   A CA  
1501 C C   . MET   A 61  ? 0.1218 0.1198 0.1358 -0.0078 -0.0043 -0.0037 61  MET   A C   
1502 O O   . MET   A 61  ? 0.1208 0.1258 0.1528 -0.0062 0.0074  0.0048  61  MET   A O   
1503 C CB  . MET   A 61  ? 0.1287 0.1297 0.1360 -0.0061 -0.0011 -0.0054 61  MET   A CB  
1504 C CG  . MET   A 61  ? 0.1259 0.1287 0.1449 -0.0044 -0.0023 -0.0086 61  MET   A CG  
1505 S SD  . MET   A 61  ? 0.1328 0.1368 0.1746 -0.0134 -0.0003 -0.0208 61  MET   A SD  
1506 C CE  . MET   A 61  ? 0.1512 0.1490 0.2002 -0.0168 0.0116  -0.0100 61  MET   A CE  
1516 N N   . GLN   A 62  ? 0.1227 0.1188 0.1416 -0.0067 -0.0042 -0.0031 62  GLN   A N   
1517 C CA  . GLN   A 62  ? 0.1300 0.1141 0.1468 -0.0043 -0.0029 0.0011  62  GLN   A CA  
1518 C C   . GLN   A 62  ? 0.1288 0.1133 0.1521 -0.0041 0.0059  -0.0038 62  GLN   A C   
1519 O O   . GLN   A 62  ? 0.1333 0.1279 0.1516 -0.0036 0.0064  -0.0057 62  GLN   A O   
1520 C CB  . GLN   A 62  ? 0.1278 0.1178 0.1519 -0.0024 0.0036  -0.0079 62  GLN   A CB  
1521 C CG  . GLN   A 62  ? 0.1339 0.1207 0.1483 -0.0019 -0.0040 0.0074  62  GLN   A CG  
1522 C CD  . GLN   A 62  ? 0.1399 0.1217 0.1442 -0.0026 0.0028  0.0056  62  GLN   A CD  
1523 O OE1 . GLN   A 62  ? 0.1407 0.1309 0.1594 -0.0023 -0.0034 0.0000  62  GLN   A OE1 
1524 N NE2 . GLN   A 62  ? 0.1451 0.1266 0.1578 0.0009  0.0005  -0.0088 62  GLN   A NE2 
1533 N N   . VAL   A 63  ? 0.1225 0.1277 0.1674 -0.0088 -0.0006 -0.0179 63  VAL   A N   
1534 C CA  . VAL   A 63  ? 0.1284 0.1331 0.1936 -0.0157 -0.0064 -0.0185 63  VAL   A CA  
1535 C C   . VAL   A 63  ? 0.1164 0.1348 0.1752 -0.0101 -0.0063 -0.0214 63  VAL   A C   
1536 O O   . VAL   A 63  ? 0.1206 0.1326 0.1913 -0.0103 -0.0054 -0.0157 63  VAL   A O   
1537 C CB  . VAL   A 63  ? 0.1384 0.1539 0.2227 -0.0157 -0.0125 -0.0438 63  VAL   A CB  
1538 C CG1 . VAL   A 63  ? 0.1535 0.1751 0.2553 -0.0176 -0.0118 -0.0676 63  VAL   A CG1 
1539 C CG2 . VAL   A 63  ? 0.1470 0.1440 0.2377 -0.0132 0.0056  -0.0429 63  VAL   A CG2 
1549 N N   . GLU   A 64  ? 0.1206 0.1390 0.1678 -0.0031 -0.0086 -0.0190 64  GLU   A N   
1550 C CA  . GLU   A 64  ? 0.1206 0.1342 0.1648 -0.0056 -0.0056 -0.0014 64  GLU   A CA  
1551 C C   . GLU   A 64  ? 0.1175 0.1291 0.1583 -0.0098 0.0003  0.0028  64  GLU   A C   
1552 O O   . GLU   A 64  ? 0.1244 0.1367 0.1663 -0.0027 0.0021  -0.0001 64  GLU   A O   
1553 C CB  . GLU   A 64  ? 0.1342 0.1508 0.1595 -0.0048 -0.0059 -0.0041 64  GLU   A CB  
1554 C CG  . GLU   A 64  ? 0.1441 0.1510 0.1764 -0.0102 -0.0007 -0.0041 64  GLU   A CG  
1555 C CD  . GLU   A 64  ? 0.1537 0.1574 0.1722 -0.0158 0.0034  -0.0070 64  GLU   A CD  
1556 O OE1 . GLU   A 64  ? 0.1570 0.1682 0.1856 -0.0211 0.0083  -0.0077 64  GLU   A OE1 
1557 O OE2 . GLU   A 64  ? 0.1713 0.1579 0.1794 -0.0224 -0.0011 0.0026  64  GLU   A OE2 
1564 N N   . SER   A 65  ? 0.1167 0.1279 0.1593 -0.0010 0.0005  0.0031  65  SER   A N   
1565 C CA  . SER   A 65  ? 0.1253 0.1231 0.1545 -0.0001 -0.0023 -0.0024 65  SER   A CA  
1566 C C   . SER   A 65  ? 0.1216 0.1311 0.1564 -0.0084 0.0041  -0.0017 65  SER   A C   
1567 O O   . SER   A 65  ? 0.1277 0.1331 0.1706 0.0012  0.0167  -0.0024 65  SER   A O   
1568 C CB  . SER   A 65  ? 0.1271 0.1238 0.1521 -0.0037 -0.0036 0.0040  65  SER   A CB  
1569 O OG  . SER   A 65  ? 0.1257 0.1380 0.1541 -0.0070 -0.0148 0.0087  65  SER   A OG  
1575 N N   . ASP   A 66  ? 0.1285 0.1291 0.1553 -0.0090 0.0099  0.0033  66  ASP   A N   
1576 C CA  . ASP   A 66  ? 0.1351 0.1352 0.1681 -0.0032 0.0097  0.0121  66  ASP   A CA  
1577 C C   . ASP   A 66  ? 0.1393 0.1373 0.1656 -0.0016 0.0162  0.0117  66  ASP   A C   
1578 O O   . ASP   A 66  ? 0.1385 0.1493 0.1876 -0.0037 0.0242  0.0241  66  ASP   A O   
1579 C CB  . ASP   A 66  ? 0.1483 0.1449 0.1931 0.0007  0.0130  0.0270  66  ASP   A CB  
1580 C CG  . ASP   A 66  ? 0.1758 0.1607 0.2154 0.0007  -0.0034 0.0440  66  ASP   A CG  
1581 O OD1 . ASP   A 66  ? 0.1707 0.1943 0.2009 -0.0061 -0.0087 0.0419  66  ASP   A OD1 
1582 O OD2 . ASP   A 66  ? 0.1934 0.1698 0.3010 0.0199  -0.0236 0.0237  66  ASP   A OD2 
1587 N N   . ASP   A 67  ? 0.1297 0.1368 0.1916 -0.0047 0.0087  0.0160  67  ASP   A N   
1588 C CA  . ASP   A 67  ? 0.1256 0.1533 0.2105 -0.0056 0.0062  0.0209  67  ASP   A CA  
1589 C C   . ASP   A 67  ? 0.1304 0.1536 0.1976 -0.0001 0.0155  0.0235  67  ASP   A C   
1590 O O   . ASP   A 67  ? 0.1260 0.1659 0.2165 0.0045  0.0280  0.0348  67  ASP   A O   
1591 C CB  . ASP   A 67  ? 0.1396 0.1628 0.2404 -0.0081 -0.0113 0.0253  67  ASP   A CB  
1592 C CG  . ASP   A 67  ? 0.1364 0.1849 0.2655 -0.0110 -0.0358 0.0361  67  ASP   A CG  
1593 O OD1 . ASP   A 67  ? 0.1446 0.2024 0.3432 -0.0176 -0.0423 0.0540  67  ASP   A OD1 
1594 O OD2 . ASP   A 67  ? 0.1435 0.1863 0.2531 -0.0054 -0.0245 0.0285  67  ASP   A OD2 
1599 N N   A TYR   A 68  ? 0.1322 0.1414 0.1841 -0.0012 0.0215  0.0255  68  TYR   A N   
1600 N N   B TYR   A 68  ? 0.1335 0.1417 0.1944 -0.0008 0.0217  0.0288  68  TYR   A N   
1601 C CA  A TYR   A 68  ? 0.1361 0.1341 0.1751 0.0010  0.0267  0.0223  68  TYR   A CA  
1602 C CA  B TYR   A 68  ? 0.1403 0.1400 0.1926 0.0044  0.0254  0.0274  68  TYR   A CA  
1603 C C   A TYR   A 68  ? 0.1337 0.1347 0.1727 -0.0006 0.0274  0.0261  68  TYR   A C   
1604 C C   B TYR   A 68  ? 0.1368 0.1385 0.1903 0.0015  0.0276  0.0259  68  TYR   A C   
1605 O O   A TYR   A 68  ? 0.1333 0.1392 0.1698 0.0040  0.0329  0.0300  68  TYR   A O   
1606 O O   B TYR   A 68  ? 0.1390 0.1461 0.1989 0.0146  0.0360  0.0216  68  TYR   A O   
1607 C CB  A TYR   A 68  ? 0.1428 0.1260 0.1781 0.0044  0.0373  0.0174  68  TYR   A CB  
1608 C CB  B TYR   A 68  ? 0.1491 0.1398 0.1977 0.0107  0.0410  0.0337  68  TYR   A CB  
1609 C CG  A TYR   A 68  ? 0.1472 0.1269 0.1913 -0.0028 0.0467  0.0060  68  TYR   A CG  
1610 C CG  B TYR   A 68  ? 0.1506 0.1562 0.2082 0.0045  0.0519  0.0270  68  TYR   A CG  
1611 C CD1 A TYR   A 68  ? 0.1458 0.1301 0.2109 -0.0233 0.0462  -0.0197 68  TYR   A CD1 
1612 C CD1 B TYR   A 68  ? 0.1599 0.1641 0.2204 -0.0049 0.0319  0.0136  68  TYR   A CD1 
1613 C CD2 A TYR   A 68  ? 0.1630 0.1307 0.2158 0.0046  0.0423  0.0082  68  TYR   A CD2 
1614 C CD2 B TYR   A 68  ? 0.1650 0.1591 0.2209 0.0045  0.0435  0.0353  68  TYR   A CD2 
1615 C CE1 A TYR   A 68  ? 0.1486 0.1358 0.2444 -0.0256 0.0417  -0.0357 68  TYR   A CE1 
1616 C CE1 B TYR   A 68  ? 0.1670 0.1636 0.2136 -0.0016 0.0229  0.0369  68  TYR   A CE1 
1617 C CE2 A TYR   A 68  ? 0.1595 0.1350 0.2378 0.0082  0.0481  -0.0059 68  TYR   A CE2 
1618 C CE2 B TYR   A 68  ? 0.1592 0.1608 0.2024 -0.0031 0.0411  0.0253  68  TYR   A CE2 
1619 C CZ  A TYR   A 68  ? 0.1503 0.1389 0.2665 -0.0120 0.0385  -0.0382 68  TYR   A CZ  
1620 C CZ  B TYR   A 68  ? 0.1688 0.1636 0.1978 -0.0001 0.0289  0.0347  68  TYR   A CZ  
1621 O OH  A TYR   A 68  ? 0.1572 0.1454 0.3129 -0.0054 0.0229  -0.0687 68  TYR   A OH  
1622 O OH  B TYR   A 68  ? 0.2054 0.1585 0.2008 0.0064  0.0057  0.0299  68  TYR   A OH  
1641 N N   . ILE   A 69  ? 0.1314 0.1306 0.1781 -0.0014 0.0212  0.0234  69  ILE   A N   
1642 C CA  . ILE   A 69  ? 0.1425 0.1366 0.1627 0.0065  0.0165  0.0077  69  ILE   A CA  
1643 C C   . ILE   A 69  ? 0.1415 0.1371 0.1614 0.0039  0.0190  0.0214  69  ILE   A C   
1644 O O   . ILE   A 69  ? 0.1518 0.1447 0.1575 -0.0001 0.0282  0.0216  69  ILE   A O   
1645 C CB  . ILE   A 69  ? 0.1511 0.1670 0.1675 0.0088  0.0165  -0.0061 69  ILE   A CB  
1646 C CG1 . ILE   A 69  ? 0.1450 0.1766 0.1778 0.0036  0.0102  -0.0195 69  ILE   A CG1 
1647 C CG2 . ILE   A 69  ? 0.1688 0.1877 0.1946 0.0168  0.0061  -0.0073 69  ILE   A CG2 
1648 C CD1 . ILE   A 69  ? 0.1488 0.1880 0.1889 0.0004  0.0114  -0.0263 69  ILE   A CD1 
1661 N N   . ALA   A 70  ? 0.1436 0.1407 0.1719 -0.0075 0.0211  0.0212  70  ALA   A N   
1662 C CA  . ALA   A 70  ? 0.1449 0.1563 0.1850 -0.0173 0.0242  0.0192  70  ALA   A CA  
1663 C C   . ALA   A 70  ? 0.1448 0.1648 0.1854 -0.0110 0.0266  0.0197  70  ALA   A C   
1664 O O   . ALA   A 70  ? 0.1630 0.1970 0.2156 0.0046  0.0445  0.0359  70  ALA   A O   
1665 C CB  . ALA   A 70  ? 0.1429 0.1550 0.2115 -0.0275 0.0187  0.0147  70  ALA   A CB  
1671 N N   . THR   A 71  ? 0.1389 0.1628 0.1791 -0.0029 0.0157  0.0212  71  THR   A N   
1672 C CA  . THR   A 71  ? 0.1531 0.1807 0.2091 0.0066  0.0212  0.0250  71  THR   A CA  
1673 C C   . THR   A 71  ? 0.1426 0.1811 0.2275 0.0132  0.0338  0.0243  71  THR   A C   
1674 O O   . THR   A 71  ? 0.1463 0.2089 0.2692 0.0106  0.0434  0.0007  71  THR   A O   
1675 C CB  . THR   A 71  ? 0.1816 0.2080 0.2309 0.0130  -0.0167 0.0270  71  THR   A CB  
1676 O OG1 . THR   A 71  ? 0.2067 0.2250 0.2406 0.0063  -0.0357 0.0224  71  THR   A OG1 
1677 C CG2 . THR   A 71  ? 0.1915 0.2204 0.2524 0.0128  -0.0268 0.0404  71  THR   A CG2 
1685 N N   . ASN   A 72  ? 0.1449 0.1629 0.2067 0.0110  0.0306  0.0308  72  ASN   A N   
1686 C CA  . ASN   A 72  ? 0.1535 0.1547 0.2021 0.0190  0.0361  0.0260  72  ASN   A CA  
1687 C C   . ASN   A 72  ? 0.1663 0.1540 0.1955 0.0153  0.0509  0.0173  72  ASN   A C   
1688 O O   . ASN   A 72  ? 0.1821 0.1612 0.2210 0.0131  0.0456  0.0027  72  ASN   A O   
1689 C CB  . ASN   A 72  ? 0.1706 0.1614 0.2020 0.0143  0.0356  0.0269  72  ASN   A CB  
1690 C CG  . ASN   A 72  ? 0.1880 0.1760 0.2087 0.0232  0.0370  0.0360  72  ASN   A CG  
1691 O OD1 . ASN   A 72  ? 0.1998 0.2082 0.2365 0.0157  0.0438  0.0231  72  ASN   A OD1 
1692 N ND2 . ASN   A 72  ? 0.2038 0.1813 0.2188 0.0504  0.0165  0.0281  72  ASN   A ND2 
1699 N N   . GLY   A 73  ? 0.1703 0.1493 0.1783 0.0089  0.0452  0.0180  73  GLY   A N   
1700 C CA  . GLY   A 73  ? 0.1822 0.1522 0.1627 0.0018  0.0453  0.0202  73  GLY   A CA  
1701 C C   . GLY   A 73  ? 0.1750 0.1413 0.1487 0.0084  0.0498  0.0247  73  GLY   A C   
1702 O O   . GLY   A 73  ? 0.1723 0.1563 0.1543 0.0122  0.0346  0.0283  73  GLY   A O   
1706 N N   . PRO   A 74  ? 0.1855 0.1464 0.1571 -0.0028 0.0472  0.0189  74  PRO   A N   
1707 C CA  . PRO   A 74  ? 0.1804 0.1434 0.1695 -0.0020 0.0475  0.0214  74  PRO   A CA  
1708 C C   . PRO   A 74  ? 0.1737 0.1359 0.1574 0.0054  0.0347  0.0111  74  PRO   A C   
1709 O O   . PRO   A 74  ? 0.1777 0.1424 0.1822 0.0113  0.0391  0.0034  74  PRO   A O   
1710 C CB  . PRO   A 74  ? 0.1939 0.1715 0.1866 0.0037  0.0426  0.0331  74  PRO   A CB  
1711 C CG  . PRO   A 74  ? 0.2185 0.2019 0.2221 -0.0114 0.0294  0.0188  74  PRO   A CG  
1712 C CD  . PRO   A 74  ? 0.2054 0.1827 0.1773 -0.0156 0.0362  0.0140  74  PRO   A CD  
1720 N N   A LEU   A 75  ? 0.1737 0.1353 0.1494 0.0106  0.0276  0.0107  75  LEU   A N   
1721 N N   B LEU   A 75  ? 0.1721 0.1209 0.1471 0.0045  0.0288  0.0057  75  LEU   A N   
1722 C CA  A LEU   A 75  ? 0.1758 0.1393 0.1426 0.0160  0.0150  0.0125  75  LEU   A CA  
1723 C CA  B LEU   A 75  ? 0.1747 0.1146 0.1238 0.0070  0.0076  0.0145  75  LEU   A CA  
1724 C C   A LEU   A 75  ? 0.1734 0.1399 0.1345 0.0154  0.0180  0.0076  75  LEU   A C   
1725 C C   B LEU   A 75  ? 0.1817 0.1298 0.1240 0.0146  0.0111  0.0173  75  LEU   A C   
1726 O O   A LEU   A 75  ? 0.1722 0.1491 0.1299 0.0240  0.0209  -0.0038 75  LEU   A O   
1727 O O   B LEU   A 75  ? 0.2039 0.1452 0.1380 0.0194  0.0097  0.0208  75  LEU   A O   
1728 C CB  A LEU   A 75  ? 0.1816 0.1528 0.1461 0.0194  0.0081  0.0158  75  LEU   A CB  
1729 C CB  B LEU   A 75  ? 0.1755 0.1264 0.1122 -0.0073 0.0114  0.0136  75  LEU   A CB  
1730 C CG  A LEU   A 75  ? 0.1924 0.1751 0.1534 0.0136  0.0037  0.0157  75  LEU   A CG  
1731 C CG  B LEU   A 75  ? 0.1923 0.1559 0.1255 -0.0392 0.0085  0.0154  75  LEU   A CG  
1732 C CD1 A LEU   A 75  ? 0.1949 0.1899 0.1633 0.0166  -0.0000 0.0108  75  LEU   A CD1 
1733 C CD1 B LEU   A 75  ? 0.1990 0.1907 0.1339 -0.0452 0.0072  0.0008  75  LEU   A CD1 
1734 C CD2 A LEU   A 75  ? 0.2015 0.1867 0.1669 0.0177  0.0051  0.0152  75  LEU   A CD2 
1735 C CD2 B LEU   A 75  ? 0.2139 0.1951 0.1716 -0.0216 0.0090  0.0140  75  LEU   A CD2 
1758 N N   . LYS   A 76  ? 0.1743 0.1357 0.1413 0.0063  0.0099  0.0064  76  LYS   A N   
1759 C CA  . LYS   A 76  ? 0.1749 0.1511 0.1525 -0.0018 0.0050  -0.0095 76  LYS   A CA  
1760 C C   . LYS   A 76  ? 0.1703 0.1381 0.1254 0.0069  0.0065  0.0003  76  LYS   A C   
1761 O O   . LYS   A 76  ? 0.1719 0.1370 0.1245 0.0037  0.0156  0.0070  76  LYS   A O   
1762 C CB  . LYS   A 76  ? 0.1732 0.1630 0.1871 0.0089  0.0111  -0.0249 76  LYS   A CB  
1763 C CG  . LYS   A 76  ? 0.1813 0.1611 0.2379 0.0151  0.0039  -0.0259 76  LYS   A CG  
1764 C CD  . LYS   A 76  ? 0.1803 0.1680 0.2892 0.0162  -0.0114 -0.0377 76  LYS   A CD  
1765 C CE  . LYS   A 76  ? 0.1968 0.1841 0.3556 0.0121  -0.0146 -0.0421 76  LYS   A CE  
1766 N NZ  . LYS   A 76  ? 0.1979 0.1759 0.4050 -0.0022 -0.0198 -0.0472 76  LYS   A NZ  
1781 N N   . VAL   A 77  ? 0.1765 0.1472 0.1234 0.0059  0.0128  0.0113  77  VAL   A N   
1782 C CA  . VAL   A 77  ? 0.1754 0.1523 0.1240 0.0106  0.0157  0.0106  77  VAL   A CA  
1783 C C   . VAL   A 77  ? 0.1741 0.1486 0.1105 0.0137  0.0074  -0.0042 77  VAL   A C   
1784 O O   . VAL   A 77  ? 0.1755 0.1508 0.1269 0.0209  0.0227  -0.0069 77  VAL   A O   
1785 C CB  . VAL   A 77  ? 0.1859 0.1666 0.1425 0.0121  0.0089  0.0187  77  VAL   A CB  
1786 C CG1 . VAL   A 77  ? 0.1870 0.1763 0.1685 0.0195  0.0061  0.0104  77  VAL   A CG1 
1787 C CG2 . VAL   A 77  ? 0.2028 0.1805 0.1642 0.0036  -0.0060 0.0320  77  VAL   A CG2 
1797 N N   . GLY   A 78  ? 0.1633 0.1428 0.1121 0.0129  0.0164  0.0013  78  GLY   A N   
1798 C CA  . GLY   A 78  ? 0.1646 0.1316 0.1316 0.0072  0.0108  0.0051  78  GLY   A CA  
1799 C C   . GLY   A 78  ? 0.1488 0.1237 0.1356 0.0105  0.0164  0.0099  78  GLY   A C   
1800 O O   . GLY   A 78  ? 0.1481 0.1305 0.1587 0.0074  0.0110  0.0124  78  GLY   A O   
1804 N N   . GLY   A 79  ? 0.1550 0.1266 0.1334 0.0091  0.0115  0.0072  79  GLY   A N   
1805 C CA  . GLY   A 79  ? 0.1488 0.1237 0.1416 0.0024  0.0144  0.0082  79  GLY   A CA  
1806 C C   . GLY   A 79  ? 0.1342 0.1209 0.1323 0.0027  0.0125  0.0061  79  GLY   A C   
1807 O O   . GLY   A 79  ? 0.1383 0.1381 0.1471 0.0203  0.0135  0.0026  79  GLY   A O   
1811 N N   . SER   A 80  ? 0.1283 0.1378 0.1521 0.0035  0.0119  -0.0016 80  SER   A N   
1812 C CA  . SER   A 80  ? 0.1243 0.1341 0.1354 0.0032  0.0043  0.0009  80  SER   A CA  
1813 C C   . SER   A 80  ? 0.1267 0.1304 0.1358 0.0000  0.0064  0.0086  80  SER   A C   
1814 O O   . SER   A 80  ? 0.1279 0.1521 0.1643 0.0073  0.0112  -0.0071 80  SER   A O   
1815 C CB  . SER   A 80  ? 0.1395 0.1326 0.1575 -0.0101 -0.0000 0.0095  80  SER   A CB  
1816 O OG  . SER   A 80  ? 0.1611 0.1343 0.1913 0.0063  -0.0023 0.0150  80  SER   A OG  
1822 N N   . CYS   A 81  ? 0.1245 0.1279 0.1325 0.0000  -0.0037 0.0111  81  CYS   A N   
1823 C CA  . CYS   A 81  ? 0.1196 0.1378 0.1314 -0.0028 -0.0051 0.0197  81  CYS   A CA  
1824 C C   . CYS   A 81  ? 0.1197 0.1334 0.1263 -0.0048 -0.0034 0.0205  81  CYS   A C   
1825 O O   . CYS   A 81  ? 0.1167 0.1619 0.1524 0.0040  0.0029  0.0268  81  CYS   A O   
1826 C CB  . CYS   A 81  ? 0.1305 0.1399 0.1471 -0.0111 -0.0032 0.0181  81  CYS   A CB  
1827 S SG  . CYS   A 81  ? 0.1418 0.1320 0.1496 -0.0150 0.0002  0.0138  81  CYS   A SG  
1833 N N   . VAL   A 82  ? 0.1267 0.1387 0.1294 0.0032  -0.0100 0.0147  82  VAL   A N   
1834 C CA  . VAL   A 82  ? 0.1386 0.1433 0.1355 0.0030  -0.0155 0.0187  82  VAL   A CA  
1835 C C   . VAL   A 82  ? 0.1341 0.1526 0.1342 -0.0015 -0.0120 0.0205  82  VAL   A C   
1836 O O   . VAL   A 82  ? 0.1279 0.1630 0.1699 0.0030  -0.0021 -0.0007 82  VAL   A O   
1837 C CB  . VAL   A 82  ? 0.1677 0.1604 0.1482 -0.0011 -0.0014 0.0297  82  VAL   A CB  
1838 C CG1 . VAL   A 82  ? 0.1884 0.1744 0.1651 0.0007  0.0012  0.0291  82  VAL   A CG1 
1839 C CG2 . VAL   A 82  ? 0.1718 0.1567 0.1732 -0.0053 -0.0034 0.0345  82  VAL   A CG2 
1849 N N   . LEU   A 83  ? 0.1240 0.1453 0.1338 -0.0095 -0.0150 0.0075  83  LEU   A N   
1850 C CA  . LEU   A 83  ? 0.1317 0.1494 0.1313 -0.0117 -0.0125 0.0071  83  LEU   A CA  
1851 C C   . LEU   A 83  ? 0.1459 0.1526 0.1176 -0.0094 -0.0157 0.0114  83  LEU   A C   
1852 O O   . LEU   A 83  ? 0.1490 0.1512 0.1384 -0.0154 -0.0063 0.0137  83  LEU   A O   
1853 C CB  . LEU   A 83  ? 0.1394 0.1494 0.1341 -0.0097 -0.0149 0.0087  83  LEU   A CB  
1854 C CG  . LEU   A 83  ? 0.1562 0.1585 0.1457 -0.0110 -0.0013 0.0046  83  LEU   A CG  
1855 C CD1 . LEU   A 83  ? 0.1695 0.1615 0.1453 -0.0206 -0.0074 0.0123  83  LEU   A CD1 
1856 C CD2 . LEU   A 83  ? 0.1545 0.1746 0.1577 -0.0111 0.0148  0.0154  83  LEU   A CD2 
1868 N N   . SER   A 84  ? 0.1589 0.1560 0.1295 -0.0106 -0.0133 0.0086  84  SER   A N   
1869 C CA  . SER   A 84  ? 0.1692 0.1620 0.1234 -0.0107 -0.0115 0.0052  84  SER   A CA  
1870 C C   . SER   A 84  ? 0.1710 0.1542 0.1136 -0.0165 -0.0012 0.0030  84  SER   A C   
1871 O O   . SER   A 84  ? 0.1629 0.1661 0.1196 -0.0142 -0.0034 0.0051  84  SER   A O   
1872 C CB  . SER   A 84  ? 0.1750 0.1861 0.1270 -0.0080 -0.0134 -0.0009 84  SER   A CB  
1873 O OG  . SER   A 84  ? 0.1795 0.2091 0.1425 -0.0067 -0.0136 -0.0129 84  SER   A OG  
1879 N N   . GLY   A 85  ? 0.1790 0.1718 0.1238 -0.0170 0.0105  0.0077  85  GLY   A N   
1880 C CA  . GLY   A 85  ? 0.1766 0.1805 0.1303 -0.0210 0.0106  -0.0019 85  GLY   A CA  
1881 C C   . GLY   A 85  ? 0.1799 0.1861 0.1199 -0.0116 0.0007  -0.0066 85  GLY   A C   
1882 O O   . GLY   A 85  ? 0.1800 0.1961 0.1399 -0.0262 0.0109  -0.0086 85  GLY   A O   
1886 N N   . HIS   A 86  ? 0.1861 0.1764 0.1157 -0.0100 -0.0027 -0.0006 86  HIS   A N   
1887 C CA  . HIS   A 86  ? 0.2005 0.1815 0.1133 -0.0158 0.0010  0.0038  86  HIS   A CA  
1888 C C   . HIS   A 86  ? 0.2281 0.1997 0.1119 -0.0132 0.0055  -0.0027 86  HIS   A C   
1889 O O   . HIS   A 86  ? 0.2431 0.2280 0.1198 -0.0083 0.0110  0.0025  86  HIS   A O   
1890 C CB  . HIS   A 86  ? 0.1969 0.1741 0.1261 -0.0078 0.0049  -0.0002 86  HIS   A CB  
1891 C CG  . HIS   A 86  ? 0.1903 0.1701 0.1294 -0.0018 -0.0007 0.0019  86  HIS   A CG  
1892 N ND1 . HIS   A 86  ? 0.2023 0.1756 0.1689 -0.0150 -0.0001 0.0001  86  HIS   A ND1 
1893 C CD2 . HIS   A 86  ? 0.1882 0.1641 0.1381 0.0064  0.0039  0.0066  86  HIS   A CD2 
1894 C CE1 . HIS   A 86  ? 0.1927 0.1770 0.1664 -0.0109 0.0226  0.0120  86  HIS   A CE1 
1895 N NE2 . HIS   A 86  ? 0.1908 0.1634 0.1515 0.0061  0.0181  0.0284  86  HIS   A NE2 
1903 N N   A ASN   A 87  ? 0.2337 0.2047 0.1336 -0.0100 0.0148  -0.0032 87  ASN   A N   
1904 N N   B ASN   A 87  ? 0.2355 0.2069 0.1258 -0.0124 0.0279  -0.0234 87  ASN   A N   
1905 C CA  A ASN   A 87  ? 0.2413 0.2133 0.1511 -0.0088 0.0233  0.0012  87  ASN   A CA  
1906 C CA  B ASN   A 87  ? 0.2484 0.2223 0.1328 -0.0132 0.0461  -0.0364 87  ASN   A CA  
1907 C C   A ASN   A 87  ? 0.2405 0.2225 0.1741 -0.0130 0.0389  0.0108  87  ASN   A C   
1908 C C   B ASN   A 87  ? 0.2401 0.2382 0.1398 -0.0170 0.0520  -0.0257 87  ASN   A C   
1909 O O   A ASN   A 87  ? 0.2475 0.2336 0.1991 -0.0162 0.0533  0.0136  87  ASN   A O   
1910 O O   B ASN   A 87  ? 0.2475 0.2571 0.1548 -0.0224 0.0649  -0.0150 87  ASN   A O   
1911 C CB  A ASN   A 87  ? 0.2479 0.2151 0.1536 -0.0049 0.0155  0.0018  87  ASN   A CB  
1912 C CB  B ASN   A 87  ? 0.2693 0.2287 0.1452 -0.0067 0.0567  -0.0458 87  ASN   A CB  
1913 C CG  A ASN   A 87  ? 0.2498 0.2144 0.1559 -0.0026 0.0084  0.0092  87  ASN   A CG  
1914 C CG  B ASN   A 87  ? 0.2824 0.2340 0.1520 -0.0027 0.0685  -0.0388 87  ASN   A CG  
1915 O OD1 A ASN   A 87  ? 0.2490 0.2096 0.1483 -0.0005 -0.0012 0.0171  87  ASN   A OD1 
1916 O OD1 B ASN   A 87  ? 0.2894 0.2302 0.1595 0.0039  0.0665  -0.0276 87  ASN   A OD1 
1917 N ND2 A ASN   A 87  ? 0.2530 0.2257 0.1705 -0.0018 0.0080  0.0117  87  ASN   A ND2 
1918 N ND2 B ASN   A 87  ? 0.2902 0.2554 0.1738 -0.0022 0.0732  -0.0228 87  ASN   A ND2 
1931 N N   A LEU   A 88  ? 0.2273 0.2162 0.1714 -0.0161 0.0328  0.0200  88  LEU   A N   
1932 N N   B LEU   A 88  ? 0.2182 0.2270 0.1283 -0.0248 0.0344  -0.0169 88  LEU   A N   
1933 C CA  A LEU   A 88  ? 0.2162 0.2120 0.1718 -0.0168 0.0332  0.0268  88  LEU   A CA  
1934 C CA  B LEU   A 88  ? 0.2034 0.2220 0.1410 -0.0232 0.0395  0.0041  88  LEU   A CA  
1935 C C   A LEU   A 88  ? 0.2103 0.2146 0.1630 -0.0183 0.0343  0.0282  88  LEU   A C   
1936 C C   B LEU   A 88  ? 0.2012 0.2228 0.1395 -0.0242 0.0395  0.0239  88  LEU   A C   
1937 O O   A LEU   A 88  ? 0.2124 0.2180 0.1763 -0.0165 0.0412  0.0355  88  LEU   A O   
1938 O O   B LEU   A 88  ? 0.2046 0.2330 0.1764 -0.0267 0.0460  0.0318  88  LEU   A O   
1939 C CB  A LEU   A 88  ? 0.2136 0.2108 0.1872 -0.0168 0.0224  0.0326  88  LEU   A CB  
1940 C CB  B LEU   A 88  ? 0.1966 0.2253 0.1566 -0.0195 0.0283  0.0013  88  LEU   A CB  
1941 C CG  A LEU   A 88  ? 0.2178 0.2120 0.2004 -0.0138 0.0140  0.0341  88  LEU   A CG  
1942 C CG  B LEU   A 88  ? 0.2094 0.2337 0.1755 -0.0067 0.0265  -0.0029 88  LEU   A CG  
1943 C CD1 A LEU   A 88  ? 0.2183 0.2125 0.1986 -0.0153 0.0110  0.0299  88  LEU   A CD1 
1944 C CD1 B LEU   A 88  ? 0.2135 0.2384 0.1690 -0.0072 0.0233  -0.0136 88  LEU   A CD1 
1945 C CD2 A LEU   A 88  ? 0.2218 0.2172 0.2126 -0.0098 0.0118  0.0300  88  LEU   A CD2 
1946 C CD2 B LEU   A 88  ? 0.2155 0.2435 0.2036 0.0042  0.0300  -0.0073 88  LEU   A CD2 
1969 N N   . ALA   A 89  ? 0.2034 0.2132 0.1478 -0.0210 0.0282  0.0129  89  ALA   A N   
1970 C CA  . ALA   A 89  ? 0.2082 0.2130 0.1219 -0.0155 0.0164  0.0185  89  ALA   A CA  
1971 C C   . ALA   A 89  ? 0.2139 0.2182 0.1246 -0.0108 -0.0017 0.0143  89  ALA   A C   
1972 O O   . ALA   A 89  ? 0.2106 0.2138 0.1672 -0.0156 -0.0056 -0.0093 89  ALA   A O   
1973 C CB  . ALA   A 89  ? 0.2012 0.2155 0.1167 -0.0176 0.0187  0.0182  89  ALA   A CB  
1980 N N   . LYS   A 90  ? 0.2250 0.2318 0.1250 -0.0146 -0.0190 0.0203  90  LYS   A N   
1981 C CA  . LYS   A 90  ? 0.2282 0.2413 0.1319 -0.0140 -0.0294 0.0247  90  LYS   A CA  
1982 C C   . LYS   A 90  ? 0.2085 0.2211 0.1286 -0.0136 -0.0271 0.0085  90  LYS   A C   
1983 O O   . LYS   A 90  ? 0.2106 0.2292 0.1613 -0.0215 -0.0275 0.0023  90  LYS   A O   
1984 C CB  . LYS   A 90  ? 0.2557 0.2734 0.1705 -0.0122 -0.0280 0.0403  90  LYS   A CB  
1985 C CG  . LYS   A 90  ? 0.2911 0.3071 0.2732 -0.0079 -0.0313 0.0386  90  LYS   A CG  
1986 C CD  . LYS   A 90  ? 0.3291 0.3405 0.3796 -0.0081 -0.0219 0.0318  90  LYS   A CD  
1987 C CE  . LYS   A 90  ? 0.3722 0.3785 0.4595 -0.0108 -0.0125 0.0251  90  LYS   A CE  
1988 N NZ  . LYS   A 90  ? 0.3822 0.3878 0.5124 -0.0123 -0.0075 0.0204  90  LYS   A NZ  
2002 N N   . HIS   A 91  ? 0.1938 0.1938 0.1073 -0.0155 -0.0248 0.0102  91  HIS   A N   
2003 C CA  . HIS   A 91  ? 0.1808 0.1765 0.1120 -0.0078 -0.0214 0.0159  91  HIS   A CA  
2004 C C   . HIS   A 91  ? 0.1650 0.1669 0.1074 -0.0139 -0.0035 0.0143  91  HIS   A C   
2005 O O   . HIS   A 91  ? 0.1629 0.1759 0.1220 -0.0206 0.0036  0.0198  91  HIS   A O   
2006 C CB  . HIS   A 91  ? 0.1968 0.1995 0.1490 0.0086  -0.0302 0.0179  91  HIS   A CB  
2007 C CG  . HIS   A 91  ? 0.2355 0.2499 0.2218 0.0219  -0.0612 0.0041  91  HIS   A CG  
2008 N ND1 . HIS   A 91  ? 0.2436 0.2800 0.2641 0.0245  -0.0707 -0.0158 91  HIS   A ND1 
2009 C CD2 . HIS   A 91  ? 0.2590 0.2733 0.2463 0.0307  -0.0732 0.0134  91  HIS   A CD2 
2010 C CE1 . HIS   A 91  ? 0.2559 0.2897 0.2775 0.0316  -0.0722 -0.0061 91  HIS   A CE1 
2011 N NE2 . HIS   A 91  ? 0.2688 0.2903 0.2688 0.0365  -0.0755 0.0072  91  HIS   A NE2 
2019 N N   . CYS   A 92  ? 0.1524 0.1554 0.1115 -0.0173 -0.0049 0.0106  92  CYS   A N   
2020 C CA  . CYS   A 92  ? 0.1441 0.1511 0.1228 -0.0144 0.0036  0.0110  92  CYS   A CA  
2021 C C   . CYS   A 92  ? 0.1344 0.1442 0.1046 -0.0107 0.0008  0.0119  92  CYS   A C   
2022 O O   . CYS   A 92  ? 0.1302 0.1492 0.1338 -0.0124 0.0025  0.0074  92  CYS   A O   
2023 C CB  . CYS   A 92  ? 0.1404 0.1444 0.1362 -0.0097 -0.0035 0.0043  92  CYS   A CB  
2024 S SG  . CYS   A 92  ? 0.1405 0.1366 0.1304 -0.0105 -0.0027 0.0086  92  CYS   A SG  
2030 N N   . LEU   A 93  ? 0.1334 0.1354 0.1138 -0.0102 0.0105  0.0143  93  LEU   A N   
2031 C CA  . LEU   A 93  ? 0.1244 0.1307 0.1093 -0.0026 0.0033  0.0131  93  LEU   A CA  
2032 C C   . LEU   A 93  ? 0.1212 0.1146 0.1126 -0.0001 0.0023  0.0062  93  LEU   A C   
2033 O O   . LEU   A 93  ? 0.1156 0.1278 0.1247 -0.0012 0.0027  0.0141  93  LEU   A O   
2034 C CB  . LEU   A 93  ? 0.1351 0.1298 0.1229 -0.0014 0.0020  0.0198  93  LEU   A CB  
2035 C CG  . LEU   A 93  ? 0.1363 0.1293 0.1244 0.0012  0.0045  0.0133  93  LEU   A CG  
2036 C CD1 . LEU   A 93  ? 0.1472 0.1312 0.1551 0.0038  0.0145  0.0127  93  LEU   A CD1 
2037 C CD2 . LEU   A 93  ? 0.1454 0.1314 0.1443 -0.0102 -0.0013 0.0114  93  LEU   A CD2 
2049 N N   . HIS   A 94  ? 0.1136 0.1181 0.1165 -0.0065 0.0072  0.0180  94  HIS   A N   
2050 C CA  . HIS   A 94  ? 0.1157 0.1155 0.1150 -0.0034 0.0004  0.0098  94  HIS   A CA  
2051 C C   . HIS   A 94  ? 0.1125 0.1157 0.1170 -0.0030 0.0020  0.0094  94  HIS   A C   
2052 O O   . HIS   A 94  ? 0.1152 0.1398 0.1517 0.0039  0.0046  -0.0134 94  HIS   A O   
2053 C CB  . HIS   A 94  ? 0.1215 0.1129 0.1181 -0.0070 -0.0020 0.0182  94  HIS   A CB  
2054 C CG  . HIS   A 94  ? 0.1196 0.1166 0.1180 -0.0058 -0.0017 0.0171  94  HIS   A CG  
2055 N ND1 . HIS   A 94  ? 0.1184 0.1137 0.1368 -0.0099 0.0053  0.0142  94  HIS   A ND1 
2056 C CD2 . HIS   A 94  ? 0.1256 0.1262 0.1237 -0.0088 -0.0056 0.0067  94  HIS   A CD2 
2057 C CE1 . HIS   A 94  ? 0.1251 0.1154 0.1288 -0.0082 -0.0104 0.0038  94  HIS   A CE1 
2058 N NE2 . HIS   A 94  ? 0.1357 0.1230 0.1307 -0.0079 -0.0049 -0.0034 94  HIS   A NE2 
2066 N N   . VAL   A 95  ? 0.1146 0.1124 0.1131 -0.0032 0.0044  0.0052  95  VAL   A N   
2067 C CA  . VAL   A 95  ? 0.1226 0.1129 0.1082 -0.0037 0.0056  0.0046  95  VAL   A CA  
2068 C C   . VAL   A 95  ? 0.1248 0.1154 0.0995 -0.0083 0.0064  0.0023  95  VAL   A C   
2069 O O   . VAL   A 95  ? 0.1267 0.1231 0.1272 0.0089  0.0076  0.0043  95  VAL   A O   
2070 C CB  . VAL   A 95  ? 0.1282 0.1188 0.1279 -0.0070 0.0004  0.0028  95  VAL   A CB  
2071 C CG1 . VAL   A 95  ? 0.1473 0.1170 0.1323 -0.0064 0.0017  -0.0020 95  VAL   A CG1 
2072 C CG2 . VAL   A 95  ? 0.1214 0.1249 0.1303 -0.0113 0.0056  0.0176  95  VAL   A CG2 
2082 N N   A VAL   A 96  ? 0.1279 0.1222 0.1082 -0.0015 0.0049  0.0054  96  VAL   A N   
2083 N N   B VAL   A 96  ? 0.1329 0.1143 0.0980 0.0008  -0.0003 0.0020  96  VAL   A N   
2084 C CA  A VAL   A 96  ? 0.1309 0.1277 0.1193 0.0020  0.0066  0.0104  96  VAL   A CA  
2085 C CA  B VAL   A 96  ? 0.1349 0.1123 0.1072 0.0033  0.0073  0.0084  96  VAL   A CA  
2086 C C   A VAL   A 96  ? 0.1335 0.1315 0.1197 0.0075  0.0122  0.0171  96  VAL   A C   
2087 C C   B VAL   A 96  ? 0.1422 0.1210 0.1106 0.0068  0.0055  0.0097  96  VAL   A C   
2088 O O   A VAL   A 96  ? 0.1402 0.1350 0.1318 0.0051  0.0147  0.0102  96  VAL   A O   
2089 O O   B VAL   A 96  ? 0.1489 0.1295 0.1348 -0.0037 0.0064  -0.0085 96  VAL   A O   
2090 C CB  A VAL   A 96  ? 0.1340 0.1344 0.1298 0.0003  0.0024  0.0116  96  VAL   A CB  
2091 C CB  B VAL   A 96  ? 0.1381 0.1190 0.1088 0.0048  0.0130  0.0073  96  VAL   A CB  
2092 C CG1 A VAL   A 96  ? 0.1380 0.1431 0.1370 -0.0007 -0.0003 0.0123  96  VAL   A CG1 
2093 C CG1 B VAL   A 96  ? 0.1373 0.1277 0.1001 0.0080  0.0152  0.0036  96  VAL   A CG1 
2094 C CG2 A VAL   A 96  ? 0.1328 0.1363 0.1348 -0.0062 0.0001  0.0095  96  VAL   A CG2 
2095 C CG2 B VAL   A 96  ? 0.1425 0.1291 0.1180 -0.0128 0.0163  0.0078  96  VAL   A CG2 
2114 N N   A GLY   A 97  ? 0.1315 0.1342 0.1376 0.0086  0.0070  0.0146  97  GLY   A N   
2115 N N   B GLY   A 97  ? 0.1414 0.1233 0.1150 -0.0012 -0.0060 0.0083  97  GLY   A N   
2116 C CA  A GLY   A 97  ? 0.1322 0.1397 0.1330 0.0141  0.0037  0.0125  97  GLY   A CA  
2117 C CA  B GLY   A 97  ? 0.1535 0.1372 0.1237 -0.0065 -0.0125 0.0144  97  GLY   A CA  
2118 C C   A GLY   A 97  ? 0.1335 0.1444 0.1099 0.0143  0.0052  0.0043  97  GLY   A C   
2119 C C   B GLY   A 97  ? 0.1654 0.1525 0.1199 -0.0045 -0.0106 0.0155  97  GLY   A C   
2120 O O   A GLY   A 97  ? 0.1426 0.1382 0.0947 0.0135  0.0053  -0.0005 97  GLY   A O   
2121 O O   B GLY   A 97  ? 0.1706 0.1495 0.1380 -0.0040 -0.0026 0.0190  97  GLY   A O   
2128 N N   A PRO   A 98  ? 0.1345 0.1488 0.0975 0.0173  -0.0018 0.0001  98  PRO   A N   
2129 N N   B PRO   A 98  ? 0.1825 0.1534 0.1164 -0.0002 -0.0201 0.0156  98  PRO   A N   
2130 C CA  A PRO   A 98  ? 0.1378 0.1610 0.0783 0.0156  -0.0032 -0.0068 98  PRO   A CA  
2131 C CA  B PRO   A 98  ? 0.2038 0.1701 0.1348 -0.0003 -0.0149 0.0126  98  PRO   A CA  
2132 C C   A PRO   A 98  ? 0.1370 0.1751 0.0799 0.0124  -0.0097 0.0032  98  PRO   A C   
2133 C C   B PRO   A 98  ? 0.2224 0.1745 0.1388 -0.0001 -0.0155 0.0314  98  PRO   A C   
2134 O O   A PRO   A 98  ? 0.1288 0.1716 0.0937 0.0144  -0.0164 0.0050  98  PRO   A O   
2135 O O   B PRO   A 98  ? 0.2110 0.1645 0.1686 0.0080  -0.0087 0.0258  98  PRO   A O   
2136 C CB  A PRO   A 98  ? 0.1462 0.1633 0.0812 0.0166  -0.0022 -0.0167 98  PRO   A CB  
2137 C CB  B PRO   A 98  ? 0.2107 0.1729 0.1315 0.0023  -0.0248 0.0083  98  PRO   A CB  
2138 C CG  A PRO   A 98  ? 0.1442 0.1584 0.1092 0.0196  0.0027  -0.0116 98  PRO   A CG  
2139 C CG  B PRO   A 98  ? 0.1993 0.1694 0.1389 -0.0048 -0.0210 0.0099  98  PRO   A CG  
2140 C CD  A PRO   A 98  ? 0.1411 0.1499 0.1120 0.0190  0.0003  -0.0095 98  PRO   A CD  
2141 C CD  B PRO   A 98  ? 0.1908 0.1533 0.1212 -0.0027 -0.0167 0.0140  98  PRO   A CD  
2156 N N   A ASN   A 99  ? 0.1377 0.1887 0.0672 0.0174  -0.0014 0.0130  99  ASN   A N   
2157 N N   B ASN   A 99  ? 0.2495 0.1891 0.1444 0.0078  -0.0189 0.0507  99  ASN   A N   
2158 C CA  A ASN   A 99  ? 0.1491 0.1969 0.0594 0.0183  -0.0020 0.0161  99  ASN   A CA  
2159 C CA  B ASN   A 99  ? 0.2824 0.2112 0.1774 0.0134  -0.0279 0.0785  99  ASN   A CA  
2160 C C   A ASN   A 99  ? 0.1690 0.2116 0.0573 0.0126  -0.0023 0.0211  99  ASN   A C   
2161 C C   B ASN   A 99  ? 0.3059 0.2441 0.1716 0.0186  -0.0197 0.0879  99  ASN   A C   
2162 O O   A ASN   A 99  ? 0.1789 0.2216 0.0797 0.0187  -0.0070 0.0134  99  ASN   A O   
2163 O O   B ASN   A 99  ? 0.3021 0.2384 0.1873 0.0241  -0.0064 0.0871  99  ASN   A O   
2164 C CB  A ASN   A 99  ? 0.1451 0.1884 0.0771 0.0150  -0.0039 0.0158  99  ASN   A CB  
2165 C CB  B ASN   A 99  ? 0.2955 0.2137 0.2530 0.0070  -0.0413 0.0810  99  ASN   A CB  
2166 C CG  A ASN   A 99  ? 0.1451 0.1737 0.0807 0.0123  -0.0107 0.0293  99  ASN   A CG  
2167 C CG  B ASN   A 99  ? 0.3063 0.2165 0.2926 -0.0001 -0.0516 0.0923  99  ASN   A CG  
2168 O OD1 A ASN   A 99  ? 0.1557 0.1736 0.0893 0.0095  -0.0275 0.0057  99  ASN   A OD1 
2169 O OD1 B ASN   A 99  ? 0.3066 0.2240 0.2766 0.0059  -0.0681 0.0900  99  ASN   A OD1 
2170 N ND2 A ASN   A 99  ? 0.1441 0.1643 0.1095 0.0132  -0.0068 0.0423  99  ASN   A ND2 
2171 N ND2 B ASN   A 99  ? 0.3133 0.2199 0.3427 0.0029  -0.0597 0.0833  99  ASN   A ND2 
2184 N N   A VAL   A 100 ? 0.1796 0.2203 0.0796 0.0034  -0.0163 0.0098  100 VAL   A N   
2185 N N   B VAL   A 100 ? 0.3317 0.2933 0.2108 0.0208  -0.0129 0.0771  100 VAL   A N   
2186 C CA  A VAL   A 100 ? 0.1865 0.2330 0.1240 0.0008  -0.0194 0.0101  100 VAL   A CA  
2187 C CA  B VAL   A 100 ? 0.3593 0.3348 0.2690 0.0263  -0.0130 0.0665  100 VAL   A CA  
2188 C C   A VAL   A 100 ? 0.1841 0.2446 0.1167 -0.0010 -0.0290 0.0236  100 VAL   A C   
2189 C C   B VAL   A 100 ? 0.3767 0.3580 0.3021 0.0385  -0.0100 0.0760  100 VAL   A C   
2190 O O   A VAL   A 100 ? 0.1882 0.2563 0.1469 -0.0053 -0.0183 0.0219  100 VAL   A O   
2191 O O   B VAL   A 100 ? 0.3766 0.3610 0.2978 0.0379  -0.0086 0.0724  100 VAL   A O   
2192 C CB  A VAL   A 100 ? 0.1946 0.2360 0.1679 -0.0038 -0.0076 -0.0078 100 VAL   A CB  
2193 C CB  B VAL   A 100 ? 0.3701 0.3527 0.3091 0.0215  -0.0107 0.0457  100 VAL   A CB  
2194 C CG1 A VAL   A 100 ? 0.1955 0.2413 0.1830 -0.0055 0.0012  -0.0138 100 VAL   A CG1 
2195 C CG1 B VAL   A 100 ? 0.3733 0.3578 0.3225 0.0203  -0.0114 0.0397  100 VAL   A CG1 
2196 C CG2 A VAL   A 100 ? 0.1977 0.2357 0.1824 -0.0077 -0.0016 -0.0109 100 VAL   A CG2 
2197 C CG2 B VAL   A 100 ? 0.3737 0.3592 0.3203 0.0214  -0.0096 0.0398  100 VAL   A CG2 
2216 N N   A ASN   A 101 ? 0.1859 0.2444 0.1208 -0.0040 -0.0305 0.0374  101 ASN   A N   
2217 N N   B ASN   A 101 ? 0.3950 0.3796 0.3178 0.0470  -0.0073 0.0866  101 ASN   A N   
2218 C CA  A ASN   A 101 ? 0.2013 0.2486 0.1458 -0.0027 -0.0278 0.0345  101 ASN   A CA  
2219 C CA  B ASN   A 101 ? 0.4152 0.4002 0.3437 0.0535  -0.0080 0.1042  101 ASN   A CA  
2220 C C   A ASN   A 101 ? 0.2295 0.2680 0.1780 -0.0026 -0.0160 0.0376  101 ASN   A C   
2221 C C   B ASN   A 101 ? 0.4283 0.4139 0.3448 0.0494  -0.0063 0.1108  101 ASN   A C   
2222 O O   A ASN   A 101 ? 0.2390 0.2704 0.1919 -0.0026 -0.0161 0.0298  101 ASN   A O   
2223 O O   B ASN   A 101 ? 0.4348 0.4164 0.3446 0.0501  -0.0082 0.1194  101 ASN   A O   
2224 C CB  A ASN   A 101 ? 0.1943 0.2339 0.1464 -0.0009 -0.0322 0.0252  101 ASN   A CB  
2225 C CB  B ASN   A 101 ? 0.4237 0.4057 0.3719 0.0604  -0.0025 0.1118  101 ASN   A CB  
2226 C CG  A ASN   A 101 ? 0.1919 0.2228 0.1590 0.0009  -0.0272 0.0061  101 ASN   A CG  
2227 C CG  B ASN   A 101 ? 0.4329 0.4136 0.4061 0.0616  0.0080  0.1119  101 ASN   A CG  
2228 O OD1 A ASN   A 101 ? 0.1901 0.2215 0.1726 0.0100  -0.0145 -0.0106 101 ASN   A OD1 
2229 O OD1 B ASN   A 101 ? 0.4347 0.4134 0.4084 0.0669  0.0081  0.1222  101 ASN   A OD1 
2230 N ND2 A ASN   A 101 ? 0.1958 0.2198 0.1722 0.0021  -0.0229 0.0103  101 ASN   A ND2 
2231 N ND2 B ASN   A 101 ? 0.4364 0.4186 0.4232 0.0605  0.0101  0.1036  101 ASN   A ND2 
2244 N N   A LYS   A 102 ? 0.2454 0.2855 0.2121 -0.0012 -0.0085 0.0369  102 LYS   A N   
2245 N N   B LYS   A 102 ? 0.4342 0.4266 0.3460 0.0427  -0.0035 0.1020  102 LYS   A N   
2246 C CA  A LYS   A 102 ? 0.2640 0.3024 0.2440 0.0048  -0.0118 0.0264  102 LYS   A CA  
2247 C CA  B LYS   A 102 ? 0.4391 0.4398 0.3325 0.0326  0.0012  0.0935  102 LYS   A CA  
2248 C C   A LYS   A 102 ? 0.2749 0.3134 0.2416 0.0137  -0.0078 0.0259  102 LYS   A C   
2249 C C   B LYS   A 102 ? 0.4307 0.4355 0.2981 0.0342  -0.0015 0.1012  102 LYS   A C   
2250 O O   A LYS   A 102 ? 0.2783 0.3168 0.2458 0.0168  -0.0053 0.0264  102 LYS   A O   
2251 O O   B LYS   A 102 ? 0.4348 0.4406 0.3010 0.0369  0.0045  0.1017  102 LYS   A O   
2252 C CB  A LYS   A 102 ? 0.2730 0.3084 0.2782 0.0017  -0.0133 0.0095  102 LYS   A CB  
2253 C CB  B LYS   A 102 ? 0.4513 0.4564 0.3685 0.0220  -0.0015 0.0712  102 LYS   A CB  
2254 C CG  A LYS   A 102 ? 0.2804 0.3118 0.3007 0.0002  -0.0168 -0.0062 102 LYS   A CG  
2255 C CG  B LYS   A 102 ? 0.4627 0.4711 0.4082 0.0124  -0.0057 0.0532  102 LYS   A CG  
2256 C CD  A LYS   A 102 ? 0.2880 0.3137 0.3200 -0.0007 -0.0196 -0.0227 102 LYS   A CD  
2257 C CD  B LYS   A 102 ? 0.4737 0.4860 0.4550 0.0057  -0.0102 0.0383  102 LYS   A CD  
2258 C CE  A LYS   A 102 ? 0.2946 0.3151 0.3367 -0.0014 -0.0205 -0.0348 102 LYS   A CE  
2259 C CE  B LYS   A 102 ? 0.4814 0.4967 0.4928 0.0020  -0.0146 0.0298  102 LYS   A CE  
2260 N NZ  A LYS   A 102 ? 0.2977 0.3165 0.3459 -0.0027 -0.0191 -0.0431 102 LYS   A NZ  
2261 N NZ  B LYS   A 102 ? 0.4863 0.5022 0.5160 0.0007  -0.0156 0.0254  102 LYS   A NZ  
2288 N N   A GLY   A 103 ? 0.2814 0.3229 0.2470 0.0200  -0.0055 0.0175  103 GLY   A N   
2289 N N   B GLY   A 103 ? 0.4149 0.4250 0.2693 0.0361  -0.0129 0.1016  103 GLY   A N   
2290 C CA  A GLY   A 103 ? 0.2881 0.3286 0.2508 0.0242  0.0004  0.0113  103 GLY   A CA  
2291 C CA  B GLY   A 103 ? 0.3964 0.4114 0.2595 0.0378  -0.0225 0.1018  103 GLY   A CA  
2292 C C   A GLY   A 103 ? 0.2934 0.3355 0.2609 0.0265  0.0060  0.0055  103 GLY   A C   
2293 C C   B GLY   A 103 ? 0.3753 0.3965 0.2389 0.0361  -0.0264 0.0936  103 GLY   A C   
2294 O O   A GLY   A 103 ? 0.2985 0.3391 0.2790 0.0304  0.0040  -0.0024 103 GLY   A O   
2295 O O   B GLY   A 103 ? 0.3800 0.3994 0.2533 0.0395  -0.0321 0.0908  103 GLY   A O   
2302 N N   A GLU   A 104 ? 0.2920 0.3382 0.2453 0.0222  0.0136  0.0045  104 GLU   A N   
2303 N N   B GLU   A 104 ? 0.3467 0.3755 0.2012 0.0273  -0.0261 0.0907  104 GLU   A N   
2304 C CA  A GLU   A 104 ? 0.2890 0.3389 0.2336 0.0165  0.0195  0.0042  104 GLU   A CA  
2305 C CA  B GLU   A 104 ? 0.3208 0.3567 0.1583 0.0159  -0.0236 0.0887  104 GLU   A CA  
2306 C C   A GLU   A 104 ? 0.3006 0.3461 0.2315 0.0166  0.0149  -0.0100 104 GLU   A C   
2307 C C   B GLU   A 104 ? 0.3103 0.3495 0.1659 0.0138  -0.0114 0.0539  104 GLU   A C   
2308 O O   A GLU   A 104 ? 0.3020 0.3485 0.2230 0.0168  0.0126  -0.0164 104 GLU   A O   
2309 O O   B GLU   A 104 ? 0.3114 0.3526 0.1859 0.0180  -0.0078 0.0524  104 GLU   A O   
2310 C CB  A GLU   A 104 ? 0.2731 0.3327 0.2303 0.0103  0.0250  0.0176  104 GLU   A CB  
2311 C CB  B GLU   A 104 ? 0.3103 0.3471 0.1621 0.0067  -0.0258 0.1109  104 GLU   A CB  
2312 C CG  A GLU   A 104 ? 0.2580 0.3259 0.2296 0.0069  0.0277  0.0281  104 GLU   A CG  
2313 C CG  B GLU   A 104 ? 0.3074 0.3445 0.1896 -0.0017 -0.0282 0.1187  104 GLU   A CG  
2314 C CD  A GLU   A 104 ? 0.2436 0.3193 0.2240 0.0045  0.0314  0.0376  104 GLU   A CD  
2315 C CD  B GLU   A 104 ? 0.3035 0.3434 0.1939 -0.0076 -0.0316 0.1289  104 GLU   A CD  
2316 O OE1 A GLU   A 104 ? 0.2327 0.3131 0.1970 0.0030  0.0358  0.0459  104 GLU   A OE1 
2317 O OE1 B GLU   A 104 ? 0.2960 0.3419 0.1806 -0.0057 -0.0400 0.1281  104 GLU   A OE1 
2318 O OE2 A GLU   A 104 ? 0.2450 0.3196 0.2416 0.0038  0.0302  0.0348  104 GLU   A OE2 
2319 O OE2 B GLU   A 104 ? 0.3115 0.3452 0.2088 -0.0165 -0.0309 0.1306  104 GLU   A OE2 
2332 N N   A ASP   A 105 ? 0.3086 0.3507 0.2453 0.0185  0.0152  -0.0199 105 ASP   A N   
2333 N N   B ASP   A 105 ? 0.3036 0.3380 0.1776 0.0073  -0.0008 0.0201  105 ASP   A N   
2334 C CA  A ASP   A 105 ? 0.3144 0.3547 0.2681 0.0202  0.0103  -0.0310 105 ASP   A CA  
2335 C CA  B ASP   A 105 ? 0.2964 0.3280 0.2080 0.0077  0.0077  -0.0228 105 ASP   A CA  
2336 C C   A ASP   A 105 ? 0.3081 0.3516 0.2639 0.0125  0.0025  -0.0428 105 ASP   A C   
2337 C C   B ASP   A 105 ? 0.2743 0.3045 0.1630 -0.0053 0.0026  -0.0370 105 ASP   A C   
2338 O O   A ASP   A 105 ? 0.3068 0.3534 0.2596 0.0147  -0.0016 -0.0483 105 ASP   A O   
2339 O O   B ASP   A 105 ? 0.2605 0.2911 0.1094 -0.0012 -0.0021 -0.0372 105 ASP   A O   
2340 C CB  A ASP   A 105 ? 0.3240 0.3604 0.2971 0.0282  0.0126  -0.0306 105 ASP   A CB  
2341 C CB  B ASP   A 105 ? 0.3102 0.3404 0.2777 0.0194  0.0225  -0.0478 105 ASP   A CB  
2342 C CG  A ASP   A 105 ? 0.3311 0.3646 0.3214 0.0350  0.0112  -0.0315 105 ASP   A CG  
2343 C CG  B ASP   A 105 ? 0.3235 0.3523 0.3336 0.0284  0.0304  -0.0657 105 ASP   A CG  
2344 O OD1 A ASP   A 105 ? 0.3328 0.3666 0.3251 0.0390  0.0126  -0.0367 105 ASP   A OD1 
2345 O OD1 B ASP   A 105 ? 0.3303 0.3550 0.3304 0.0265  0.0262  -0.0803 105 ASP   A OD1 
2346 O OD2 A ASP   A 105 ? 0.3353 0.3660 0.3405 0.0367  0.0088  -0.0277 105 ASP   A OD2 
2347 O OD2 B ASP   A 105 ? 0.3291 0.3588 0.3730 0.0328  0.0342  -0.0619 105 ASP   A OD2 
2356 N N   A ILE   A 106 ? 0.3014 0.3438 0.2722 0.0008  -0.0057 -0.0472 106 ILE   A N   
2357 N N   B ILE   A 106 ? 0.2668 0.3013 0.1890 -0.0162 -0.0158 -0.0392 106 ILE   A N   
2358 C CA  A ILE   A 106 ? 0.2922 0.3330 0.2779 -0.0106 -0.0142 -0.0514 106 ILE   A CA  
2359 C CA  B ILE   A 106 ? 0.2578 0.2921 0.2067 -0.0318 -0.0301 -0.0552 106 ILE   A CA  
2360 C C   A ILE   A 106 ? 0.2851 0.3246 0.2767 -0.0192 -0.0152 -0.0619 106 ILE   A C   
2361 C C   B ILE   A 106 ? 0.2474 0.2767 0.1934 -0.0436 -0.0373 -0.0536 106 ILE   A C   
2362 O O   A ILE   A 106 ? 0.2793 0.3227 0.2648 -0.0234 -0.0224 -0.0700 106 ILE   A O   
2363 O O   B ILE   A 106 ? 0.2356 0.2761 0.1884 -0.0482 -0.0318 -0.0481 106 ILE   A O   
2364 C CB  A ILE   A 106 ? 0.2893 0.3282 0.2910 -0.0098 -0.0193 -0.0429 106 ILE   A CB  
2365 C CB  B ILE   A 106 ? 0.2632 0.3094 0.2477 -0.0343 -0.0413 -0.0611 106 ILE   A CB  
2366 C CG1 A ILE   A 106 ? 0.2834 0.3214 0.3075 -0.0080 -0.0224 -0.0385 106 ILE   A CG1 
2367 C CG1 B ILE   A 106 ? 0.2575 0.3193 0.2843 -0.0327 -0.0473 -0.0642 106 ILE   A CG1 
2368 C CG2 A ILE   A 106 ? 0.2907 0.3286 0.2896 -0.0098 -0.0203 -0.0391 106 ILE   A CG2 
2369 C CG2 B ILE   A 106 ? 0.2703 0.3139 0.2523 -0.0364 -0.0392 -0.0652 106 ILE   A CG2 
2370 C CD1 A ILE   A 106 ? 0.2814 0.3171 0.3176 -0.0074 -0.0213 -0.0359 106 ILE   A CD1 
2371 C CD1 B ILE   A 106 ? 0.2578 0.3239 0.3049 -0.0302 -0.0456 -0.0688 106 ILE   A CD1 
2394 N N   A GLN   A 107 ? 0.2869 0.3163 0.2958 -0.0190 -0.0087 -0.0653 107 GLN   A N   
2395 N N   B GLN   A 107 ? 0.2613 0.2641 0.2193 -0.0420 -0.0317 -0.0619 107 GLN   A N   
2396 C CA  A GLN   A 107 ? 0.2865 0.3059 0.3180 -0.0126 0.0011  -0.0629 107 GLN   A CA  
2397 C CA  B GLN   A 107 ? 0.2858 0.2583 0.2792 -0.0338 -0.0073 -0.0563 107 GLN   A CA  
2398 C C   A GLN   A 107 ? 0.2584 0.2746 0.2942 -0.0079 0.0128  -0.0605 107 GLN   A C   
2399 C C   B GLN   A 107 ? 0.2505 0.2146 0.2506 -0.0242 0.0091  -0.0325 107 GLN   A C   
2400 O O   A GLN   A 107 ? 0.2607 0.2780 0.3176 -0.0056 0.0219  -0.0659 107 GLN   A O   
2401 O O   B GLN   A 107 ? 0.2520 0.2104 0.2536 -0.0200 0.0112  -0.0314 107 GLN   A O   
2402 C CB  A GLN   A 107 ? 0.3119 0.3235 0.3701 -0.0107 -0.0034 -0.0562 107 GLN   A CB  
2403 C CB  B GLN   A 107 ? 0.3375 0.3044 0.3697 -0.0430 -0.0141 -0.0607 107 GLN   A CB  
2404 C CG  A GLN   A 107 ? 0.3330 0.3389 0.4217 -0.0070 -0.0070 -0.0473 107 GLN   A CG  
2405 C CG  B GLN   A 107 ? 0.3860 0.3496 0.4615 -0.0492 -0.0239 -0.0462 107 GLN   A CG  
2406 C CD  A GLN   A 107 ? 0.3501 0.3514 0.4656 -0.0037 -0.0093 -0.0387 107 GLN   A CD  
2407 C CD  B GLN   A 107 ? 0.4270 0.3874 0.5424 -0.0511 -0.0316 -0.0276 107 GLN   A CD  
2408 O OE1 A GLN   A 107 ? 0.3559 0.3572 0.4839 -0.0018 -0.0103 -0.0361 107 GLN   A OE1 
2409 O OE1 B GLN   A 107 ? 0.4391 0.3993 0.5677 -0.0502 -0.0341 -0.0190 107 GLN   A OE1 
2410 N NE2 A GLN   A 107 ? 0.3565 0.3557 0.4801 -0.0030 -0.0103 -0.0361 107 GLN   A NE2 
2411 N NE2 B GLN   A 107 ? 0.4371 0.3987 0.5699 -0.0533 -0.0358 -0.0256 107 GLN   A NE2 
2428 N N   A LEU   A 108 ? 0.2286 0.2380 0.2480 -0.0032 0.0184  -0.0558 108 LEU   A N   
2429 N N   B LEU   A 108 ? 0.2183 0.1903 0.1990 -0.0253 0.0130  -0.0327 108 LEU   A N   
2430 C CA  A LEU   A 108 ? 0.2039 0.2057 0.2160 0.0036  0.0167  -0.0304 108 LEU   A CA  
2431 C CA  B LEU   A 108 ? 0.1994 0.1733 0.1933 -0.0114 0.0221  -0.0160 108 LEU   A CA  
2432 C C   A LEU   A 108 ? 0.1796 0.1698 0.1950 0.0081  0.0127  -0.0107 108 LEU   A C   
2433 C C   B LEU   A 108 ? 0.1714 0.1448 0.1865 0.0040  0.0148  0.0028  108 LEU   A C   
2434 O O   A LEU   A 108 ? 0.1783 0.1694 0.1984 0.0095  0.0121  -0.0096 108 LEU   A O   
2435 O O   B LEU   A 108 ? 0.1653 0.1502 0.1992 0.0045  0.0157  0.0161  108 LEU   A O   
2436 C CB  A LEU   A 108 ? 0.2042 0.2131 0.2024 0.0029  0.0173  -0.0259 108 LEU   A CB  
2437 C CB  B LEU   A 108 ? 0.2085 0.1938 0.1793 -0.0125 0.0296  -0.0182 108 LEU   A CB  
2438 C CG  A LEU   A 108 ? 0.2082 0.2230 0.2035 0.0029  0.0198  -0.0229 108 LEU   A CG  
2439 C CG  B LEU   A 108 ? 0.2245 0.2167 0.1916 -0.0102 0.0367  -0.0193 108 LEU   A CG  
2440 C CD1 A LEU   A 108 ? 0.2141 0.2279 0.2061 -0.0006 0.0217  -0.0190 108 LEU   A CD1 
2441 C CD1 B LEU   A 108 ? 0.2385 0.2268 0.1920 -0.0142 0.0439  -0.0126 108 LEU   A CD1 
2442 C CD2 A LEU   A 108 ? 0.2095 0.2310 0.2141 0.0049  0.0232  -0.0163 108 LEU   A CD2 
2443 C CD2 B LEU   A 108 ? 0.2307 0.2353 0.2198 -0.0065 0.0392  -0.0081 108 LEU   A CD2 
2466 N N   . LEU   A 109 ? 0.1610 0.1470 0.1837 0.0066  0.0095  0.0058  109 LEU   A N   
2467 C CA  . LEU   A 109 ? 0.1527 0.1407 0.1858 0.0047  -0.0046 0.0021  109 LEU   A CA  
2468 C C   . LEU   A 109 ? 0.1430 0.1362 0.1693 0.0056  -0.0012 -0.0065 109 LEU   A C   
2469 O O   . LEU   A 109 ? 0.1500 0.1318 0.1870 0.0006  -0.0149 -0.0075 109 LEU   A O   
2470 C CB  . LEU   A 109 ? 0.1566 0.1481 0.1842 0.0049  -0.0086 0.0050  109 LEU   A CB  
2471 C CG  . LEU   A 109 ? 0.1509 0.1580 0.1933 0.0029  -0.0003 0.0159  109 LEU   A CG  
2472 C CD1 . LEU   A 109 ? 0.1580 0.1477 0.1853 0.0037  0.0023  0.0066  109 LEU   A CD1 
2473 C CD2 . LEU   A 109 ? 0.1518 0.1805 0.2159 0.0020  0.0073  0.0200  109 LEU   A CD2 
2486 N N   . LYS   A 110 ? 0.1463 0.1329 0.1729 -0.0019 -0.0045 -0.0011 110 LYS   A N   
2487 C CA  . LYS   A 110 ? 0.1393 0.1306 0.1821 -0.0081 -0.0108 -0.0022 110 LYS   A CA  
2488 C C   . LYS   A 110 ? 0.1399 0.1255 0.1645 -0.0063 -0.0031 -0.0090 110 LYS   A C   
2489 O O   . LYS   A 110 ? 0.1342 0.1242 0.1758 -0.0002 -0.0026 -0.0123 110 LYS   A O   
2490 C CB  . LYS   A 110 ? 0.1483 0.1346 0.1979 -0.0039 -0.0070 -0.0099 110 LYS   A CB  
2491 C CG  . LYS   A 110 ? 0.1527 0.1326 0.1969 0.0028  -0.0056 -0.0072 110 LYS   A CG  
2492 C CD  . LYS   A 110 ? 0.1569 0.1338 0.2158 -0.0104 -0.0082 -0.0144 110 LYS   A CD  
2493 C CE  . LYS   A 110 ? 0.1694 0.1357 0.2454 -0.0031 0.0080  -0.0162 110 LYS   A CE  
2494 N NZ  . LYS   A 110 ? 0.1757 0.1343 0.2631 -0.0094 0.0143  -0.0156 110 LYS   A NZ  
2508 N N   . SER   A 111 ? 0.1368 0.1264 0.1681 -0.0013 0.0005  -0.0022 111 SER   A N   
2509 C CA  . SER   A 111 ? 0.1372 0.1344 0.1687 -0.0026 0.0058  -0.0026 111 SER   A CA  
2510 C C   . SER   A 111 ? 0.1323 0.1250 0.1582 -0.0026 -0.0019 -0.0008 111 SER   A C   
2511 O O   . SER   A 111 ? 0.1433 0.1204 0.1738 -0.0036 0.0004  0.0030  111 SER   A O   
2512 C CB  . SER   A 111 ? 0.1557 0.1554 0.1763 -0.0057 0.0071  -0.0160 111 SER   A CB  
2513 O OG  . SER   A 111 ? 0.2015 0.1794 0.1807 0.0017  0.0108  -0.0264 111 SER   A OG  
2519 N N   . ALA   A 112 ? 0.1353 0.1160 0.1690 0.0038  0.0001  0.0013  112 ALA   A N   
2520 C CA  . ALA   A 112 ? 0.1348 0.1169 0.1548 -0.0013 -0.0003 -0.0072 112 ALA   A CA  
2521 C C   . ALA   A 112 ? 0.1329 0.1119 0.1579 -0.0013 0.0017  -0.0023 112 ALA   A C   
2522 O O   . ALA   A 112 ? 0.1372 0.1149 0.1627 -0.0064 0.0090  0.0024  112 ALA   A O   
2523 C CB  . ALA   A 112 ? 0.1457 0.1231 0.1628 -0.0021 -0.0010 -0.0061 112 ALA   A CB  
2529 N N   . TYR   A 113 ? 0.1237 0.1160 0.1752 -0.0005 0.0008  -0.0020 113 TYR   A N   
2530 C CA  . TYR   A 113 ? 0.1212 0.1151 0.1718 -0.0018 0.0095  0.0058  113 TYR   A CA  
2531 C C   . TYR   A 113 ? 0.1151 0.1176 0.1531 -0.0095 0.0040  0.0036  113 TYR   A C   
2532 O O   . TYR   A 113 ? 0.1242 0.1248 0.1726 -0.0026 0.0100  0.0047  113 TYR   A O   
2533 C CB  . TYR   A 113 ? 0.1255 0.1265 0.1665 -0.0034 -0.0031 0.0026  113 TYR   A CB  
2534 C CG  . TYR   A 113 ? 0.1275 0.1298 0.1585 -0.0093 0.0035  0.0119  113 TYR   A CG  
2535 C CD1 . TYR   A 113 ? 0.1340 0.1392 0.1446 -0.0006 -0.0010 0.0142  113 TYR   A CD1 
2536 C CD2 . TYR   A 113 ? 0.1392 0.1362 0.1603 -0.0092 0.0001  0.0017  113 TYR   A CD2 
2537 C CE1 . TYR   A 113 ? 0.1329 0.1435 0.1542 0.0020  0.0107  0.0145  113 TYR   A CE1 
2538 C CE2 . TYR   A 113 ? 0.1299 0.1448 0.1501 -0.0029 -0.0010 0.0153  113 TYR   A CE2 
2539 C CZ  . TYR   A 113 ? 0.1315 0.1394 0.1530 0.0051  0.0055  0.0219  113 TYR   A CZ  
2540 O OH  . TYR   A 113 ? 0.1335 0.1549 0.1753 0.0132  0.0018  0.0142  113 TYR   A OH  
2550 N N   . GLU   A 114 ? 0.1223 0.1190 0.1645 -0.0047 0.0074  0.0063  114 GLU   A N   
2551 C CA  . GLU   A 114 ? 0.1262 0.1184 0.1762 0.0005  0.0055  0.0050  114 GLU   A CA  
2552 C C   . GLU   A 114 ? 0.1246 0.1193 0.1628 -0.0003 0.0145  0.0054  114 GLU   A C   
2553 O O   . GLU   A 114 ? 0.1305 0.1201 0.1659 0.0015  0.0056  0.0073  114 GLU   A O   
2554 C CB  . GLU   A 114 ? 0.1239 0.1126 0.1857 0.0008  0.0059  0.0057  114 GLU   A CB  
2555 C CG  . GLU   A 114 ? 0.1325 0.1187 0.1890 0.0067  0.0073  -0.0047 114 GLU   A CG  
2556 C CD  . GLU   A 114 ? 0.1404 0.1279 0.1877 -0.0005 0.0013  -0.0038 114 GLU   A CD  
2557 O OE1 . GLU   A 114 ? 0.1435 0.1290 0.1845 -0.0045 0.0092  -0.0135 114 GLU   A OE1 
2558 O OE2 . GLU   A 114 ? 0.1589 0.1328 0.2058 -0.0088 0.0075  -0.0191 114 GLU   A OE2 
2565 N N   . ASN   A 115 ? 0.1225 0.1208 0.1551 -0.0021 0.0105  0.0024  115 ASN   A N   
2566 C CA  . ASN   A 115 ? 0.1247 0.1214 0.1613 -0.0059 0.0159  0.0050  115 ASN   A CA  
2567 C C   . ASN   A 115 ? 0.1264 0.1201 0.1600 -0.0070 0.0080  0.0046  115 ASN   A C   
2568 O O   . ASN   A 115 ? 0.1300 0.1284 0.1553 -0.0054 0.0148  0.0117  115 ASN   A O   
2569 C CB  . ASN   A 115 ? 0.1353 0.1287 0.1484 -0.0082 0.0113  0.0046  115 ASN   A CB  
2570 C CG  . ASN   A 115 ? 0.1317 0.1507 0.1601 -0.0160 0.0132  0.0007  115 ASN   A CG  
2571 O OD1 . ASN   A 115 ? 0.1360 0.2530 0.1872 -0.0100 0.0184  0.0143  115 ASN   A OD1 
2572 N ND2 . ASN   A 115 ? 0.1395 0.1316 0.1552 -0.0098 0.0179  0.0093  115 ASN   A ND2 
2579 N N   . PHE   A 116 ? 0.1214 0.1217 0.1619 -0.0011 0.0168  0.0146  116 PHE   A N   
2580 C CA  . PHE   A 116 ? 0.1215 0.1259 0.1558 -0.0022 0.0174  0.0124  116 PHE   A CA  
2581 C C   . PHE   A 116 ? 0.1246 0.1323 0.1513 -0.0055 0.0160  0.0145  116 PHE   A C   
2582 O O   . PHE   A 116 ? 0.1322 0.1429 0.1609 0.0025  0.0166  0.0237  116 PHE   A O   
2583 C CB  . PHE   A 116 ? 0.1266 0.1206 0.1615 -0.0049 0.0241  0.0107  116 PHE   A CB  
2584 C CG  . PHE   A 116 ? 0.1217 0.1166 0.1522 -0.0044 0.0106  0.0079  116 PHE   A CG  
2585 C CD1 . PHE   A 116 ? 0.1228 0.1221 0.1507 -0.0046 0.0116  0.0082  116 PHE   A CD1 
2586 C CD2 . PHE   A 116 ? 0.1308 0.1265 0.1693 -0.0071 0.0166  0.0131  116 PHE   A CD2 
2587 C CE1 . PHE   A 116 ? 0.1315 0.1238 0.1549 -0.0102 0.0100  0.0061  116 PHE   A CE1 
2588 C CE2 . PHE   A 116 ? 0.1289 0.1214 0.1797 -0.0023 0.0173  0.0079  116 PHE   A CE2 
2589 C CZ  . PHE   A 116 ? 0.1325 0.1176 0.1632 -0.0015 0.0047  0.0079  116 PHE   A CZ  
2599 N N   . ASN   A 117 ? 0.1262 0.1272 0.1688 -0.0019 0.0125  0.0192  117 ASN   A N   
2600 C CA  . ASN   A 117 ? 0.1261 0.1251 0.1746 -0.0013 0.0163  0.0241  117 ASN   A CA  
2601 C C   . ASN   A 117 ? 0.1341 0.1324 0.1802 0.0002  0.0219  0.0272  117 ASN   A C   
2602 O O   . ASN   A 117 ? 0.1454 0.1342 0.2057 -0.0018 0.0048  0.0376  117 ASN   A O   
2603 C CB  . ASN   A 117 ? 0.1275 0.1248 0.1905 -0.0003 0.0180  0.0258  117 ASN   A CB  
2604 C CG  . ASN   A 117 ? 0.1304 0.1307 0.1834 -0.0022 0.0226  0.0224  117 ASN   A CG  
2605 O OD1 . ASN   A 117 ? 0.1331 0.1498 0.2067 -0.0113 0.0271  0.0115  117 ASN   A OD1 
2606 N ND2 . ASN   A 117 ? 0.1243 0.1309 0.1809 -0.0016 0.0131  0.0248  117 ASN   A ND2 
2613 N N   . GLN   A 118 ? 0.1308 0.1293 0.1748 -0.0017 0.0102  0.0267  118 GLN   A N   
2614 C CA  . GLN   A 118 ? 0.1334 0.1430 0.1733 -0.0042 0.0021  0.0201  118 GLN   A CA  
2615 C C   . GLN   A 118 ? 0.1371 0.1529 0.1673 0.0002  0.0040  0.0277  118 GLN   A C   
2616 O O   . GLN   A 118 ? 0.1424 0.1831 0.1861 0.0079  -0.0050 0.0131  118 GLN   A O   
2617 C CB  . GLN   A 118 ? 0.1312 0.1389 0.1870 -0.0017 0.0109  0.0215  118 GLN   A CB  
2618 C CG  . GLN   A 118 ? 0.1350 0.1439 0.1893 0.0030  0.0146  0.0209  118 GLN   A CG  
2619 C CD  . GLN   A 118 ? 0.1322 0.1490 0.1978 0.0054  0.0122  0.0165  118 GLN   A CD  
2620 O OE1 . GLN   A 118 ? 0.1349 0.1663 0.2174 0.0112  -0.0010 0.0065  118 GLN   A OE1 
2621 N NE2 . GLN   A 118 ? 0.1379 0.1484 0.2008 0.0006  0.0053  0.0201  118 GLN   A NE2 
2630 N N   . HIS   A 119 ? 0.1390 0.1482 0.1621 0.0000  0.0116  0.0248  119 HIS   A N   
2631 C CA  . HIS   A 119 ? 0.1453 0.1575 0.1710 0.0016  0.0079  0.0295  119 HIS   A CA  
2632 C C   . HIS   A 119 ? 0.1539 0.1688 0.1636 0.0013  0.0157  0.0397  119 HIS   A C   
2633 O O   . HIS   A 119 ? 0.1605 0.1745 0.1766 -0.0173 0.0111  0.0384  119 HIS   A O   
2634 C CB  . HIS   A 119 ? 0.1505 0.1514 0.1861 -0.0003 0.0236  0.0326  119 HIS   A CB  
2635 C CG  . HIS   A 119 ? 0.1580 0.1532 0.2087 0.0037  0.0280  0.0396  119 HIS   A CG  
2636 N ND1 . HIS   A 119 ? 0.1701 0.1714 0.2614 -0.0077 0.0179  0.0205  119 HIS   A ND1 
2637 C CD2 . HIS   A 119 ? 0.1688 0.1628 0.2282 0.0171  0.0470  0.0582  119 HIS   A CD2 
2638 C CE1 . HIS   A 119 ? 0.1692 0.1673 0.2797 -0.0155 0.0355  0.0315  119 HIS   A CE1 
2639 N NE2 . HIS   A 119 ? 0.1785 0.1671 0.2652 0.0066  0.0596  0.0570  119 HIS   A NE2 
2647 N N   . GLU   A 120 ? 0.1614 0.1909 0.1657 0.0039  0.0151  0.0552  120 GLU   A N   
2648 C CA  . GLU   A 120 ? 0.1889 0.2199 0.2015 0.0121  0.0197  0.0878  120 GLU   A CA  
2649 C C   . GLU   A 120 ? 0.1703 0.1993 0.1904 0.0026  0.0221  0.0814  120 GLU   A C   
2650 O O   . GLU   A 120 ? 0.1647 0.1906 0.2028 0.0031  0.0266  0.0797  120 GLU   A O   
2651 C CB  . GLU   A 120 ? 0.2541 0.2878 0.2582 0.0209  0.0185  0.1387  120 GLU   A CB  
2652 C CG  . GLU   A 120 ? 0.3480 0.3658 0.3924 0.0363  0.0076  0.1353  120 GLU   A CG  
2653 C CD  . GLU   A 120 ? 0.4316 0.4351 0.5153 0.0481  0.0047  0.1163  120 GLU   A CD  
2654 O OE1 . GLU   A 120 ? 0.4524 0.4487 0.5469 0.0510  0.0051  0.1094  120 GLU   A OE1 
2655 O OE2 . GLU   A 120 ? 0.4660 0.4660 0.5692 0.0525  0.0026  0.1060  120 GLU   A OE2 
2662 N N   . VAL   A 121 ? 0.1640 0.1914 0.1721 -0.0016 0.0219  0.0617  121 VAL   A N   
2663 C CA  . VAL   A 121 ? 0.1755 0.1999 0.1682 -0.0043 0.0376  0.0691  121 VAL   A CA  
2664 C C   . VAL   A 121 ? 0.1612 0.1824 0.1500 -0.0119 0.0213  0.0376  121 VAL   A C   
2665 O O   . VAL   A 121 ? 0.1662 0.1817 0.1677 -0.0203 0.0084  0.0320  121 VAL   A O   
2666 C CB  . VAL   A 121 ? 0.2190 0.2397 0.1980 0.0090  0.0524  0.0766  121 VAL   A CB  
2667 C CG1 . VAL   A 121 ? 0.2207 0.2583 0.1995 0.0174  0.0653  0.0692  121 VAL   A CG1 
2668 C CG2 . VAL   A 121 ? 0.2454 0.2597 0.2360 -0.0015 0.0400  0.0620  121 VAL   A CG2 
2678 N N   . LEU   A 122 ? 0.1526 0.1582 0.1527 -0.0153 0.0203  0.0321  122 LEU   A N   
2679 C CA  . LEU   A 122 ? 0.1539 0.1463 0.1550 -0.0128 0.0363  0.0326  122 LEU   A CA  
2680 C C   . LEU   A 122 ? 0.1496 0.1448 0.1541 -0.0150 0.0191  0.0258  122 LEU   A C   
2681 O O   . LEU   A 122 ? 0.1531 0.1474 0.1845 -0.0198 0.0146  0.0292  122 LEU   A O   
2682 C CB  . LEU   A 122 ? 0.1698 0.1497 0.1840 -0.0023 0.0212  0.0334  122 LEU   A CB  
2683 C CG  . LEU   A 122 ? 0.1737 0.1512 0.1770 -0.0064 0.0271  0.0281  122 LEU   A CG  
2684 C CD1 . LEU   A 122 ? 0.1840 0.1517 0.1992 -0.0091 0.0365  0.0313  122 LEU   A CD1 
2685 C CD2 . LEU   A 122 ? 0.1701 0.1464 0.1638 -0.0055 0.0273  0.0239  122 LEU   A CD2 
2697 N N   A LEU   A 123 ? 0.1483 0.1410 0.1485 -0.0183 0.0200  0.0243  123 LEU   A N   
2698 N N   B LEU   A 123 ? 0.1436 0.1434 0.1461 -0.0180 0.0112  0.0215  123 LEU   A N   
2699 C CA  A LEU   A 123 ? 0.1483 0.1383 0.1421 -0.0183 0.0225  0.0292  123 LEU   A CA  
2700 C CA  B LEU   A 123 ? 0.1461 0.1458 0.1335 -0.0103 0.0096  0.0250  123 LEU   A CA  
2701 C C   A LEU   A 123 ? 0.1378 0.1250 0.1433 -0.0244 0.0269  0.0305  123 LEU   A C   
2702 C C   B LEU   A 123 ? 0.1373 0.1415 0.1321 -0.0084 0.0069  0.0234  123 LEU   A C   
2703 O O   A LEU   A 123 ? 0.1357 0.1302 0.1413 -0.0309 0.0338  0.0187  123 LEU   A O   
2704 O O   B LEU   A 123 ? 0.1373 0.1494 0.1327 -0.0159 0.0123  0.0158  123 LEU   A O   
2705 C CB  A LEU   A 123 ? 0.1571 0.1506 0.1462 -0.0174 0.0303  0.0242  123 LEU   A CB  
2706 C CB  B LEU   A 123 ? 0.1554 0.1562 0.1358 -0.0168 0.0226  0.0171  123 LEU   A CB  
2707 C CG  A LEU   A 123 ? 0.1611 0.1593 0.1530 -0.0117 0.0293  0.0151  123 LEU   A CG  
2708 C CG  B LEU   A 123 ? 0.1562 0.1658 0.1475 -0.0155 0.0230  0.0089  123 LEU   A CG  
2709 C CD1 A LEU   A 123 ? 0.1625 0.1637 0.1554 -0.0067 0.0255  0.0084  123 LEU   A CD1 
2710 C CD1 B LEU   A 123 ? 0.1592 0.1699 0.1675 -0.0061 0.0206  -0.0008 123 LEU   A CD1 
2711 C CD2 A LEU   A 123 ? 0.1645 0.1633 0.1560 -0.0105 0.0225  0.0118  123 LEU   A CD2 
2712 C CD2 B LEU   A 123 ? 0.1656 0.1744 0.1544 -0.0124 0.0131  0.0039  123 LEU   A CD2 
2735 N N   A ALA   A 124 ? 0.1324 0.1151 0.1374 -0.0279 0.0322  0.0363  124 ALA   A N   
2736 N N   B ALA   A 124 ? 0.1387 0.1327 0.1316 -0.0079 0.0115  0.0181  124 ALA   A N   
2737 C CA  A ALA   A 124 ? 0.1257 0.1158 0.1426 -0.0204 0.0258  0.0271  124 ALA   A CA  
2738 C CA  B ALA   A 124 ? 0.1344 0.1313 0.1434 -0.0068 0.0109  0.0128  124 ALA   A CA  
2739 C C   A ALA   A 124 ? 0.1199 0.1189 0.1514 -0.0164 0.0269  0.0150  124 ALA   A C   
2740 C C   B ALA   A 124 ? 0.1310 0.1277 0.1422 -0.0074 0.0169  0.0163  124 ALA   A C   
2741 O O   A ALA   A 124 ? 0.1148 0.1223 0.1659 -0.0198 0.0317  0.0159  124 ALA   A O   
2742 O O   B ALA   A 124 ? 0.1332 0.1377 0.1730 -0.0069 0.0217  0.0278  124 ALA   A O   
2743 C CB  A ALA   A 124 ? 0.1302 0.1163 0.1517 -0.0188 0.0215  0.0252  124 ALA   A CB  
2744 C CB  B ALA   A 124 ? 0.1377 0.1341 0.1729 -0.0040 0.0110  0.0108  124 ALA   A CB  
2755 N N   A PRO   A 125 ? 0.1231 0.1242 0.1622 -0.0104 0.0241  0.0078  125 PRO   A N   
2756 N N   B PRO   A 125 ? 0.1264 0.1225 0.1376 -0.0060 0.0187  0.0227  125 PRO   A N   
2757 C CA  A PRO   A 125 ? 0.1287 0.1237 0.1656 -0.0073 0.0160  0.0037  125 PRO   A CA  
2758 C CA  B PRO   A 125 ? 0.1311 0.1260 0.1444 -0.0092 0.0094  0.0182  125 PRO   A CA  
2759 C C   A PRO   A 125 ? 0.1212 0.1159 0.1595 -0.0096 0.0169  0.0193  125 PRO   A C   
2760 C C   B PRO   A 125 ? 0.1251 0.1323 0.1537 -0.0066 -0.0038 0.0128  125 PRO   A C   
2761 O O   A PRO   A 125 ? 0.1200 0.1129 0.1648 -0.0063 0.0220  0.0140  125 PRO   A O   
2762 O O   B PRO   A 125 ? 0.1303 0.1285 0.1661 -0.0031 0.0019  0.0098  125 PRO   A O   
2763 C CB  A PRO   A 125 ? 0.1346 0.1266 0.1709 -0.0126 0.0100  -0.0057 125 PRO   A CB  
2764 C CB  B PRO   A 125 ? 0.1304 0.1220 0.1442 -0.0152 0.0140  0.0225  125 PRO   A CB  
2765 C CG  A PRO   A 125 ? 0.1363 0.1287 0.1675 -0.0120 0.0105  0.0019  125 PRO   A CG  
2766 C CG  B PRO   A 125 ? 0.1255 0.1194 0.1477 -0.0087 0.0212  0.0166  125 PRO   A CG  
2767 C CD  A PRO   A 125 ? 0.1285 0.1305 0.1645 -0.0102 0.0206  0.0063  125 PRO   A CD  
2768 C CD  B PRO   A 125 ? 0.1195 0.1235 0.1426 -0.0105 0.0282  0.0230  125 PRO   A CD  
2783 N N   A LEU   A 126 ? 0.1216 0.1243 0.1655 -0.0059 0.0146  0.0285  126 LEU   A N   
2784 N N   B LEU   A 126 ? 0.1300 0.1496 0.1695 0.0034  -0.0109 0.0016  126 LEU   A N   
2785 C CA  A LEU   A 126 ? 0.1268 0.1413 0.1681 -0.0126 0.0101  0.0305  126 LEU   A CA  
2786 C CA  B LEU   A 126 ? 0.1334 0.1548 0.1655 0.0010  -0.0097 0.0064  126 LEU   A CA  
2787 C C   A LEU   A 126 ? 0.1322 0.1389 0.1703 -0.0058 0.0100  0.0301  126 LEU   A C   
2788 C C   B LEU   A 126 ? 0.1488 0.1524 0.1683 0.0059  -0.0128 -0.0084 126 LEU   A C   
2789 O O   A LEU   A 126 ? 0.1320 0.1388 0.1971 0.0024  0.0278  0.0376  126 LEU   A O   
2790 O O   B LEU   A 126 ? 0.1636 0.1564 0.2026 0.0057  -0.0086 0.0006  126 LEU   A O   
2791 C CB  A LEU   A 126 ? 0.1363 0.1566 0.1700 -0.0158 0.0105  0.0258  126 LEU   A CB  
2792 C CB  B LEU   A 126 ? 0.1445 0.1686 0.1845 -0.0001 -0.0112 -0.0005 126 LEU   A CB  
2793 C CG  A LEU   A 126 ? 0.1398 0.1721 0.1612 -0.0178 0.0187  0.0243  126 LEU   A CG  
2794 C CG  B LEU   A 126 ? 0.1510 0.1816 0.1841 -0.0170 -0.0173 0.0066  126 LEU   A CG  
2795 C CD1 A LEU   A 126 ? 0.1460 0.1776 0.1619 -0.0118 0.0255  0.0262  126 LEU   A CD1 
2796 C CD1 B LEU   A 126 ? 0.1519 0.1894 0.1687 -0.0275 -0.0094 0.0084  126 LEU   A CD1 
2797 C CD2 A LEU   A 126 ? 0.1456 0.1713 0.1546 -0.0211 0.0160  0.0304  126 LEU   A CD2 
2798 C CD2 B LEU   A 126 ? 0.1595 0.1915 0.2007 -0.0249 -0.0313 0.0125  126 LEU   A CD2 
2821 N N   A LEU   A 127 ? 0.1404 0.1441 0.1562 -0.0021 0.0084  0.0238  127 LEU   A N   
2822 N N   B LEU   A 127 ? 0.1512 0.1610 0.1526 0.0138  -0.0202 -0.0065 127 LEU   A N   
2823 C CA  A LEU   A 127 ? 0.1383 0.1418 0.1442 -0.0055 0.0020  0.0107  127 LEU   A CA  
2824 C CA  B LEU   A 127 ? 0.1572 0.1614 0.1448 0.0155  -0.0253 -0.0016 127 LEU   A CA  
2825 C C   A LEU   A 127 ? 0.1381 0.1350 0.1468 -0.0109 0.0007  -0.0022 127 LEU   A C   
2826 C C   B LEU   A 127 ? 0.1597 0.1468 0.1433 0.0093  -0.0313 0.0023  127 LEU   A C   
2827 O O   A LEU   A 127 ? 0.1408 0.1319 0.1451 -0.0149 0.0031  -0.0094 127 LEU   A O   
2828 O O   B LEU   A 127 ? 0.1682 0.1464 0.1560 0.0002  -0.0311 0.0118  127 LEU   A O   
2829 C CB  A LEU   A 127 ? 0.1425 0.1459 0.1415 0.0028  0.0003  0.0080  127 LEU   A CB  
2830 C CB  B LEU   A 127 ? 0.1582 0.1821 0.1447 0.0242  -0.0225 0.0051  127 LEU   A CB  
2831 C CG  A LEU   A 127 ? 0.1467 0.1462 0.1533 0.0051  -0.0023 0.0077  127 LEU   A CG  
2832 C CG  B LEU   A 127 ? 0.1623 0.2038 0.1569 0.0284  -0.0150 0.0141  127 LEU   A CG  
2833 C CD1 A LEU   A 127 ? 0.1500 0.1411 0.1614 0.0027  -0.0020 0.0071  127 LEU   A CD1 
2834 C CD1 B LEU   A 127 ? 0.1646 0.2028 0.1672 0.0236  -0.0072 0.0256  127 LEU   A CD1 
2835 C CD2 A LEU   A 127 ? 0.1497 0.1450 0.1628 0.0189  -0.0032 0.0046  127 LEU   A CD2 
2836 C CD2 B LEU   A 127 ? 0.1743 0.2236 0.1634 0.0356  -0.0237 0.0095  127 LEU   A CD2 
2859 N N   A SER   A 128 ? 0.1441 0.1410 0.1527 -0.0127 -0.0086 0.0001  128 SER   A N   
2860 N N   B SER   A 128 ? 0.1555 0.1485 0.1409 0.0008  -0.0245 0.0028  128 SER   A N   
2861 C CA  A SER   A 128 ? 0.1489 0.1453 0.1477 -0.0098 -0.0103 -0.0008 128 SER   A CA  
2862 C CA  B SER   A 128 ? 0.1654 0.1482 0.1369 0.0032  -0.0284 0.0030  128 SER   A CA  
2863 C C   A SER   A 128 ? 0.1499 0.1421 0.1572 -0.0054 -0.0157 -0.0030 128 SER   A C   
2864 C C   B SER   A 128 ? 0.1736 0.1508 0.1493 0.0104  -0.0339 0.0142  128 SER   A C   
2865 O O   A SER   A 128 ? 0.1543 0.1391 0.1588 -0.0083 -0.0243 -0.0104 128 SER   A O   
2866 O O   B SER   A 128 ? 0.1898 0.1651 0.1962 0.0143  -0.0374 -0.0027 128 SER   A O   
2867 C CB  A SER   A 128 ? 0.1511 0.1542 0.1399 -0.0102 -0.0076 0.0139  128 SER   A CB  
2868 C CB  B SER   A 128 ? 0.1680 0.1543 0.1412 0.0019  -0.0347 0.0063  128 SER   A CB  
2869 O OG  A SER   A 128 ? 0.1511 0.1640 0.1424 -0.0084 0.0013  0.0230  128 SER   A OG  
2870 O OG  B SER   A 128 ? 0.1668 0.1602 0.1606 0.0004  -0.0285 0.0063  128 SER   A OG  
2881 N N   A ALA   A 129 ? 0.1507 0.1513 0.1809 -0.0022 -0.0021 0.0107  129 ALA   A N   
2882 N N   B ALA   A 129 ? 0.1691 0.1688 0.1779 0.0153  -0.0111 0.0438  129 ALA   A N   
2883 C CA  A ALA   A 129 ? 0.1504 0.1649 0.1933 0.0037  0.0047  0.0164  129 ALA   A CA  
2884 C CA  B ALA   A 129 ? 0.1721 0.1931 0.2004 0.0153  -0.0062 0.0554  129 ALA   A CA  
2885 C C   A ALA   A 129 ? 0.1563 0.1635 0.1734 -0.0029 0.0066  -0.0048 129 ALA   A C   
2886 C C   B ALA   A 129 ? 0.1747 0.1869 0.1802 0.0057  -0.0082 0.0508  129 ALA   A C   
2887 O O   A ALA   A 129 ? 0.1653 0.1693 0.1791 -0.0106 0.0011  -0.0133 129 ALA   A O   
2888 O O   B ALA   A 129 ? 0.1809 0.1855 0.1814 -0.0013 -0.0139 0.0465  129 ALA   A O   
2889 C CB  A ALA   A 129 ? 0.1514 0.1748 0.2082 0.0099  0.0118  0.0268  129 ALA   A CB  
2890 C CB  B ALA   A 129 ? 0.1821 0.2072 0.2176 0.0168  0.0081  0.0508  129 ALA   A CB  
2901 N N   A GLY   A 130 ? 0.1587 0.1539 0.1670 0.0077  0.0172  0.0042  130 GLY   A N   
2902 N N   B GLY   A 130 ? 0.1973 0.2053 0.2078 0.0066  -0.0093 0.0567  130 GLY   A N   
2903 C CA  A GLY   A 130 ? 0.1661 0.1486 0.1645 0.0088  0.0155  0.0078  130 GLY   A CA  
2904 C CA  B GLY   A 130 ? 0.2181 0.2080 0.2081 -0.0079 -0.0141 0.0603  130 GLY   A CA  
2905 C C   A GLY   A 130 ? 0.1652 0.1334 0.1524 0.0072  0.0136  0.0042  130 GLY   A C   
2906 C C   B GLY   A 130 ? 0.2192 0.1933 0.1910 -0.0244 -0.0353 0.0583  130 GLY   A C   
2907 O O   A GLY   A 130 ? 0.1650 0.1283 0.1545 -0.0007 0.0088  -0.0011 130 GLY   A O   
2908 O O   B GLY   A 130 ? 0.2107 0.1893 0.1784 -0.0315 -0.0431 0.0384  130 GLY   A O   
2915 N N   A ILE   A 131 ? 0.1678 0.1274 0.1474 0.0055  0.0081  -0.0116 131 ILE   A N   
2916 N N   B ILE   A 131 ? 0.2251 0.1868 0.2072 -0.0340 -0.0430 0.0558  131 ILE   A N   
2917 C CA  A ILE   A 131 ? 0.1646 0.1229 0.1261 -0.0033 -0.0054 -0.0095 131 ILE   A CA  
2918 C CA  B ILE   A 131 ? 0.2275 0.1805 0.2391 -0.0231 -0.0451 0.0640  131 ILE   A CA  
2919 C C   A ILE   A 131 ? 0.1461 0.1231 0.1027 -0.0117 -0.0168 0.0024  131 ILE   A C   
2920 C C   B ILE   A 131 ? 0.2138 0.1761 0.2576 -0.0070 -0.0418 0.0714  131 ILE   A C   
2921 O O   A ILE   A 131 ? 0.1462 0.1133 0.1051 -0.0110 -0.0263 0.0028  131 ILE   A O   
2922 O O   B ILE   A 131 ? 0.2117 0.1857 0.2708 0.0078  -0.0242 0.0696  131 ILE   A O   
2923 C CB  A ILE   A 131 ? 0.1839 0.1324 0.1502 -0.0090 -0.0064 -0.0213 131 ILE   A CB  
2924 C CB  B ILE   A 131 ? 0.2467 0.1910 0.2752 -0.0330 -0.0411 0.0490  131 ILE   A CB  
2925 C CG1 A ILE   A 131 ? 0.1978 0.1521 0.1671 -0.0171 -0.0172 -0.0310 131 ILE   A CG1 
2926 C CG1 B ILE   A 131 ? 0.2614 0.2110 0.3168 -0.0298 -0.0411 0.0426  131 ILE   A CG1 
2927 C CG2 A ILE   A 131 ? 0.1898 0.1276 0.1595 -0.0095 0.0109  -0.0253 131 ILE   A CG2 
2928 C CG2 B ILE   A 131 ? 0.2528 0.1902 0.2851 -0.0354 -0.0424 0.0415  131 ILE   A CG2 
2929 C CD1 A ILE   A 131 ? 0.2064 0.1640 0.1806 -0.0195 -0.0216 -0.0340 131 ILE   A CD1 
2930 C CD1 B ILE   A 131 ? 0.2714 0.2235 0.3554 -0.0296 -0.0358 0.0350  131 ILE   A CD1 
2953 N N   A PHE   A 132 ? 0.1444 0.1323 0.0857 -0.0093 -0.0074 0.0062  132 PHE   A N   
2954 N N   B PHE   A 132 ? 0.2191 0.1767 0.2785 -0.0079 -0.0522 0.0750  132 PHE   A N   
2955 C CA  A PHE   A 132 ? 0.1475 0.1420 0.0697 -0.0023 -0.0081 0.0027  132 PHE   A CA  
2956 C CA  B PHE   A 132 ? 0.2306 0.1927 0.3122 0.0017  -0.0642 0.0710  132 PHE   A CA  
2957 C C   A PHE   A 132 ? 0.1597 0.1530 0.0778 0.0021  -0.0185 -0.0149 132 PHE   A C   
2958 C C   B PHE   A 132 ? 0.2318 0.2125 0.2825 0.0069  -0.0559 0.0720  132 PHE   A C   
2959 O O   A PHE   A 132 ? 0.1675 0.1648 0.0919 0.0039  -0.0147 -0.0279 132 PHE   A O   
2960 O O   B PHE   A 132 ? 0.2478 0.2176 0.3106 0.0082  -0.0430 0.0605  132 PHE   A O   
2961 C CB  A PHE   A 132 ? 0.1367 0.1300 0.0632 0.0084  -0.0022 0.0126  132 PHE   A CB  
2962 C CB  B PHE   A 132 ? 0.2436 0.1996 0.3708 -0.0065 -0.0763 0.0670  132 PHE   A CB  
2963 C CG  A PHE   A 132 ? 0.1301 0.1187 0.0450 0.0181  -0.0063 0.0247  132 PHE   A CG  
2964 C CG  B PHE   A 132 ? 0.2601 0.2144 0.4339 -0.0165 -0.0820 0.0633  132 PHE   A CG  
2965 C CD1 A PHE   A 132 ? 0.1375 0.1269 0.0659 0.0324  -0.0122 -0.0032 132 PHE   A CD1 
2966 C CD1 B PHE   A 132 ? 0.2727 0.2247 0.4618 -0.0215 -0.0834 0.0580  132 PHE   A CD1 
2967 C CD2 A PHE   A 132 ? 0.1208 0.1127 0.0581 0.0168  -0.0126 0.0369  132 PHE   A CD2 
2968 C CD2 B PHE   A 132 ? 0.2596 0.2159 0.4458 -0.0176 -0.0878 0.0658  132 PHE   A CD2 
2969 C CE1 A PHE   A 132 ? 0.1366 0.1320 0.0714 0.0326  -0.0200 -0.0053 132 PHE   A CE1 
2970 C CE1 B PHE   A 132 ? 0.2761 0.2281 0.4722 -0.0198 -0.0885 0.0566  132 PHE   A CE1 
2971 C CE2 A PHE   A 132 ? 0.1215 0.1175 0.0729 0.0222  -0.0206 0.0159  132 PHE   A CE2 
2972 C CE2 B PHE   A 132 ? 0.2656 0.2220 0.4633 -0.0186 -0.0939 0.0630  132 PHE   A CE2 
2973 C CZ  A PHE   A 132 ? 0.1295 0.1243 0.0691 0.0271  -0.0263 0.0019  132 PHE   A CZ  
2974 C CZ  B PHE   A 132 ? 0.2757 0.2283 0.4743 -0.0185 -0.0904 0.0573  132 PHE   A CZ  
2993 N N   A GLY   A 133 ? 0.1631 0.1573 0.0997 0.0032  -0.0268 -0.0081 133 GLY   A N   
2994 N N   B GLY   A 133 ? 0.2293 0.2304 0.2596 0.0114  -0.0577 0.0572  133 GLY   A N   
2995 C CA  A GLY   A 133 ? 0.1675 0.1648 0.1107 0.0032  -0.0362 -0.0173 133 GLY   A CA  
2996 C CA  B GLY   A 133 ? 0.2343 0.2449 0.2462 0.0133  -0.0611 0.0375  133 GLY   A CA  
2997 C C   A GLY   A 133 ? 0.1715 0.1750 0.1239 0.0046  -0.0420 -0.0242 133 GLY   A C   
2998 C C   B GLY   A 133 ? 0.2336 0.2493 0.2285 0.0133  -0.0565 0.0246  133 GLY   A C   
2999 O O   A GLY   A 133 ? 0.1779 0.1798 0.1318 0.0072  -0.0526 -0.0310 133 GLY   A O   
3000 O O   B GLY   A 133 ? 0.2531 0.2589 0.2486 0.0161  -0.0624 0.0222  133 GLY   A O   
3007 N N   A ALA   A 134 ? 0.1698 0.1758 0.1323 0.0036  -0.0322 -0.0304 134 ALA   A N   
3008 N N   B ALA   A 134 ? 0.2189 0.2493 0.2046 0.0076  -0.0393 0.0105  134 ALA   A N   
3009 C CA  A ALA   A 134 ? 0.1650 0.1819 0.1545 0.0047  -0.0329 -0.0229 134 ALA   A CA  
3010 C CA  B ALA   A 134 ? 0.2084 0.2496 0.1974 -0.0019 -0.0305 -0.0161 134 ALA   A CA  
3011 C C   A ALA   A 134 ? 0.1696 0.1890 0.1692 -0.0007 -0.0256 -0.0156 134 ALA   A C   
3012 C C   B ALA   A 134 ? 0.2031 0.2656 0.1906 -0.0086 -0.0310 -0.0202 134 ALA   A C   
3013 O O   A ALA   A 134 ? 0.1729 0.1801 0.1741 0.0027  -0.0155 -0.0138 134 ALA   A O   
3014 O O   B ALA   A 134 ? 0.2136 0.2769 0.2287 -0.0039 -0.0209 -0.0369 134 ALA   A O   
3015 C CB  A ALA   A 134 ? 0.1641 0.1821 0.1714 0.0087  -0.0313 -0.0175 134 ALA   A CB  
3016 C CB  B ALA   A 134 ? 0.2058 0.2393 0.2033 -0.0013 -0.0271 -0.0294 134 ALA   A CB  
3027 N N   A ASP   A 135 ? 0.1732 0.1999 0.1779 -0.0061 -0.0289 -0.0059 135 ASP   A N   
3028 N N   B ASP   A 135 ? 0.1937 0.2749 0.1783 -0.0191 -0.0451 -0.0049 135 ASP   A N   
3029 C CA  A ASP   A 135 ? 0.1773 0.2073 0.1934 -0.0123 -0.0376 -0.0005 135 ASP   A CA  
3030 C CA  B ASP   A 135 ? 0.1973 0.2879 0.1901 -0.0253 -0.0509 0.0145  135 ASP   A CA  
3031 C C   A ASP   A 135 ? 0.1695 0.1978 0.1822 -0.0089 -0.0327 0.0058  135 ASP   A C   
3032 C C   B ASP   A 135 ? 0.1839 0.2676 0.1591 -0.0153 -0.0353 0.0037  135 ASP   A C   
3033 O O   A ASP   A 135 ? 0.1688 0.1934 0.1818 -0.0162 -0.0225 0.0094  135 ASP   A O   
3034 O O   B ASP   A 135 ? 0.1762 0.2598 0.1547 -0.0131 -0.0271 -0.0120 135 ASP   A O   
3035 C CB  A ASP   A 135 ? 0.1942 0.2268 0.2260 -0.0206 -0.0489 0.0043  135 ASP   A CB  
3036 C CB  B ASP   A 135 ? 0.2206 0.3192 0.2533 -0.0403 -0.0675 0.0372  135 ASP   A CB  
3037 C CG  A ASP   A 135 ? 0.2080 0.2422 0.2493 -0.0252 -0.0562 0.0110  135 ASP   A CG  
3038 C CG  B ASP   A 135 ? 0.2454 0.3507 0.3136 -0.0540 -0.0814 0.0578  135 ASP   A CG  
3039 O OD1 A ASP   A 135 ? 0.2083 0.2516 0.2660 -0.0259 -0.0523 0.0166  135 ASP   A OD1 
3040 O OD1 B ASP   A 135 ? 0.2533 0.3623 0.3335 -0.0600 -0.0892 0.0671  135 ASP   A OD1 
3041 O OD2 A ASP   A 135 ? 0.2221 0.2532 0.2696 -0.0221 -0.0540 0.0193  135 ASP   A OD2 
3042 O OD2 B ASP   A 135 ? 0.2643 0.3651 0.3329 -0.0567 -0.0874 0.0609  135 ASP   A OD2 
3051 N N   A PRO   A 136 ? 0.1583 0.1877 0.1695 0.0018  -0.0365 0.0069  136 PRO   A N   
3052 N N   B PRO   A 136 ? 0.1726 0.2612 0.1625 0.0021  -0.0266 0.0089  136 PRO   A N   
3053 C CA  A PRO   A 136 ? 0.1547 0.1884 0.1693 0.0025  -0.0297 0.0044  136 PRO   A CA  
3054 C CA  B PRO   A 136 ? 0.1639 0.2460 0.1669 0.0037  -0.0213 0.0023  136 PRO   A CA  
3055 C C   A PRO   A 136 ? 0.1385 0.1863 0.1733 0.0025  -0.0219 -0.0019 136 PRO   A C   
3056 C C   B PRO   A 136 ? 0.1468 0.2324 0.1727 0.0024  -0.0192 -0.0150 136 PRO   A C   
3057 O O   A PRO   A 136 ? 0.1351 0.1836 0.1687 0.0064  -0.0069 0.0037  136 PRO   A O   
3058 O O   B PRO   A 136 ? 0.1415 0.2247 0.1637 0.0041  -0.0144 -0.0058 136 PRO   A O   
3059 C CB  A PRO   A 136 ? 0.1640 0.1878 0.1762 0.0052  -0.0323 0.0078  136 PRO   A CB  
3060 C CB  B PRO   A 136 ? 0.1789 0.2528 0.1767 0.0090  -0.0211 0.0121  136 PRO   A CB  
3061 C CG  A PRO   A 136 ? 0.1701 0.1867 0.1856 0.0057  -0.0408 0.0052  136 PRO   A CG  
3062 C CG  B PRO   A 136 ? 0.1940 0.2700 0.2038 0.0111  -0.0238 0.0071  136 PRO   A CG  
3063 C CD  A PRO   A 136 ? 0.1583 0.1816 0.1793 0.0030  -0.0419 0.0125  136 PRO   A CD  
3064 C CD  B PRO   A 136 ? 0.1871 0.2697 0.1881 0.0151  -0.0254 0.0130  136 PRO   A CD  
3079 N N   A ILE   A 137 ? 0.1408 0.1868 0.1889 0.0019  -0.0226 -0.0206 137 ILE   A N   
3080 N N   B ILE   A 137 ? 0.1466 0.2349 0.1987 -0.0070 -0.0286 -0.0213 137 ILE   A N   
3081 C CA  A ILE   A 137 ? 0.1545 0.1906 0.2108 -0.0020 -0.0148 -0.0312 137 ILE   A CA  
3082 C CA  B ILE   A 137 ? 0.1470 0.2384 0.2341 -0.0088 -0.0226 -0.0266 137 ILE   A CA  
3083 C C   A ILE   A 137 ? 0.1549 0.1888 0.2068 -0.0050 -0.0022 -0.0345 137 ILE   A C   
3084 C C   B ILE   A 137 ? 0.1460 0.2286 0.2198 -0.0112 -0.0261 -0.0258 137 ILE   A C   
3085 O O   A ILE   A 137 ? 0.1553 0.1936 0.2253 -0.0130 0.0074  -0.0280 137 ILE   A O   
3086 O O   B ILE   A 137 ? 0.1500 0.2174 0.2360 -0.0148 -0.0126 -0.0267 137 ILE   A O   
3087 C CB  A ILE   A 137 ? 0.1607 0.1959 0.2335 0.0017  -0.0280 -0.0330 137 ILE   A CB  
3088 C CB  B ILE   A 137 ? 0.1471 0.2546 0.2723 -0.0045 -0.0260 -0.0334 137 ILE   A CB  
3089 C CG1 A ILE   A 137 ? 0.1676 0.2035 0.2403 0.0067  -0.0291 -0.0321 137 ILE   A CG1 
3090 C CG1 B ILE   A 137 ? 0.1558 0.2651 0.2944 0.0020  -0.0271 -0.0326 137 ILE   A CG1 
3091 C CG2 A ILE   A 137 ? 0.1608 0.1946 0.2457 0.0020  -0.0400 -0.0356 137 ILE   A CG2 
3092 C CG2 B ILE   A 137 ? 0.1479 0.2544 0.2903 -0.0061 -0.0280 -0.0482 137 ILE   A CG2 
3093 C CD1 A ILE   A 137 ? 0.1750 0.2092 0.2488 0.0112  -0.0272 -0.0321 137 ILE   A CD1 
3094 C CD1 B ILE   A 137 ? 0.1686 0.2759 0.3160 0.0099  -0.0251 -0.0274 137 ILE   A CD1 
3117 N N   A HIS   A 138 ? 0.1581 0.1830 0.1916 -0.0009 -0.0037 -0.0423 138 HIS   A N   
3118 N N   B HIS   A 138 ? 0.1476 0.2307 0.2053 -0.0028 -0.0258 -0.0288 138 HIS   A N   
3119 C CA  A HIS   A 138 ? 0.1572 0.1791 0.1860 0.0034  -0.0089 -0.0410 138 HIS   A CA  
3120 C CA  B HIS   A 138 ? 0.1563 0.2250 0.2033 -0.0023 -0.0182 -0.0354 138 HIS   A CA  
3121 C C   A HIS   A 138 ? 0.1521 0.1649 0.1774 0.0058  -0.0119 -0.0298 138 HIS   A C   
3122 C C   B HIS   A 138 ? 0.1456 0.1974 0.1843 -0.0051 -0.0082 -0.0267 138 HIS   A C   
3123 O O   A HIS   A 138 ? 0.1574 0.1652 0.1797 0.0017  -0.0182 -0.0255 138 HIS   A O   
3124 O O   B HIS   A 138 ? 0.1545 0.1904 0.1987 -0.0077 -0.0028 -0.0193 138 HIS   A O   
3125 C CB  A HIS   A 138 ? 0.1574 0.1897 0.1853 0.0029  -0.0180 -0.0518 138 HIS   A CB  
3126 C CB  B HIS   A 138 ? 0.1824 0.2417 0.2185 -0.0058 -0.0183 -0.0407 138 HIS   A CB  
3127 C CG  A HIS   A 138 ? 0.1612 0.1971 0.1900 0.0016  -0.0222 -0.0601 138 HIS   A CG  
3128 C CG  B HIS   A 138 ? 0.2062 0.2557 0.2365 0.0023  -0.0132 -0.0475 138 HIS   A CG  
3129 N ND1 A HIS   A 138 ? 0.1639 0.2008 0.2028 0.0023  -0.0202 -0.0608 138 HIS   A ND1 
3130 N ND1 B HIS   A 138 ? 0.2165 0.2606 0.2445 0.0023  -0.0054 -0.0562 138 HIS   A ND1 
3131 C CD2 A HIS   A 138 ? 0.1619 0.1995 0.1890 0.0024  -0.0231 -0.0667 138 HIS   A CD2 
3132 C CD2 B HIS   A 138 ? 0.2180 0.2633 0.2501 0.0094  -0.0028 -0.0466 138 HIS   A CD2 
3133 C CE1 A HIS   A 138 ? 0.1661 0.2016 0.2009 0.0070  -0.0221 -0.0643 138 HIS   A CE1 
3134 C CE1 B HIS   A 138 ? 0.2286 0.2658 0.2538 0.0090  -0.0010 -0.0557 138 HIS   A CE1 
3135 N NE2 A HIS   A 138 ? 0.1652 0.2013 0.1917 0.0079  -0.0230 -0.0687 138 HIS   A NE2 
3136 N NE2 B HIS   A 138 ? 0.2283 0.2680 0.2520 0.0124  0.0059  -0.0500 138 HIS   A NE2 
3151 N N   A SER   A 139 ? 0.1452 0.1546 0.1597 0.0144  -0.0053 -0.0200 139 SER   A N   
3152 N N   B SER   A 139 ? 0.1363 0.1841 0.1654 0.0067  -0.0092 -0.0153 139 SER   A N   
3153 C CA  A SER   A 139 ? 0.1399 0.1524 0.1518 0.0132  0.0006  -0.0083 139 SER   A CA  
3154 C CA  B SER   A 139 ? 0.1281 0.1719 0.1589 0.0008  -0.0045 -0.0047 139 SER   A CA  
3155 C C   A SER   A 139 ? 0.1374 0.1501 0.1547 0.0075  0.0048  0.0068  139 SER   A C   
3156 C C   B SER   A 139 ? 0.1234 0.1615 0.1710 -0.0085 0.0024  -0.0051 139 SER   A C   
3157 O O   A SER   A 139 ? 0.1385 0.1449 0.1626 0.0065  -0.0011 0.0163  139 SER   A O   
3158 O O   B SER   A 139 ? 0.1228 0.1568 0.1831 -0.0129 0.0038  -0.0045 139 SER   A O   
3159 C CB  A SER   A 139 ? 0.1392 0.1525 0.1405 0.0106  -0.0011 -0.0071 139 SER   A CB  
3160 C CB  B SER   A 139 ? 0.1237 0.1622 0.1453 0.0016  0.0004  -0.0021 139 SER   A CB  
3161 O OG  A SER   A 139 ? 0.1436 0.1516 0.1478 0.0045  0.0002  -0.0015 139 SER   A OG  
3162 O OG  B SER   A 139 ? 0.1205 0.1422 0.1462 -0.0011 0.0029  0.0066  139 SER   A OG  
3173 N N   A LEU   A 140 ? 0.1370 0.1563 0.1521 0.0056  0.0051  0.0178  140 LEU   A N   
3174 N N   B LEU   A 140 ? 0.1191 0.1676 0.1873 -0.0096 0.0018  0.0026  140 LEU   A N   
3175 C CA  A LEU   A 140 ? 0.1373 0.1564 0.1552 -0.0027 0.0036  0.0170  140 LEU   A CA  
3176 C CA  B LEU   A 140 ? 0.1196 0.1656 0.1941 -0.0183 0.0004  0.0043  140 LEU   A CA  
3177 C C   A LEU   A 140 ? 0.1328 0.1631 0.1649 -0.0057 0.0056  0.0139  140 LEU   A C   
3178 C C   B LEU   A 140 ? 0.1119 0.1719 0.2074 -0.0171 0.0018  0.0001  140 LEU   A C   
3179 O O   A LEU   A 140 ? 0.1363 0.1632 0.1753 -0.0009 0.0067  0.0201  140 LEU   A O   
3180 O O   B LEU   A 140 ? 0.1194 0.1692 0.2259 -0.0058 0.0032  0.0022  140 LEU   A O   
3181 C CB  A LEU   A 140 ? 0.1361 0.1624 0.1617 -0.0044 -0.0011 0.0157  140 LEU   A CB  
3182 C CB  B LEU   A 140 ? 0.1201 0.1697 0.2014 -0.0138 0.0054  0.0071  140 LEU   A CB  
3183 C CG  A LEU   A 140 ? 0.1403 0.1698 0.1736 -0.0095 0.0016  0.0216  140 LEU   A CG  
3184 C CG  B LEU   A 140 ? 0.1279 0.1799 0.2184 -0.0272 0.0225  0.0324  140 LEU   A CG  
3185 C CD1 A LEU   A 140 ? 0.1435 0.1696 0.1801 -0.0049 -0.0037 0.0293  140 LEU   A CD1 
3186 C CD1 B LEU   A 140 ? 0.1391 0.1839 0.2106 -0.0186 0.0210  0.0505  140 LEU   A CD1 
3187 C CD2 A LEU   A 140 ? 0.1435 0.1740 0.1767 -0.0057 0.0037  0.0242  140 LEU   A CD2 
3188 C CD2 B LEU   A 140 ? 0.1340 0.1840 0.2322 -0.0168 0.0263  0.0429  140 LEU   A CD2 
3211 N N   A ARG   A 141 ? 0.1391 0.1719 0.1832 -0.0086 0.0018  0.0029  141 ARG   A N   
3212 N N   B ARG   A 141 ? 0.1224 0.1781 0.2265 -0.0172 -0.0096 -0.0174 141 ARG   A N   
3213 C CA  A ARG   A 141 ? 0.1484 0.1834 0.2086 -0.0109 -0.0043 -0.0138 141 ARG   A CA  
3214 C CA  B ARG   A 141 ? 0.1424 0.1908 0.2442 -0.0222 -0.0121 -0.0358 141 ARG   A CA  
3215 C C   A ARG   A 141 ? 0.1429 0.1812 0.2095 -0.0124 0.0004  -0.0186 141 ARG   A C   
3216 C C   B ARG   A 141 ? 0.1388 0.1806 0.2343 -0.0132 -0.0055 -0.0267 141 ARG   A C   
3217 O O   A ARG   A 141 ? 0.1454 0.1791 0.2138 -0.0161 0.0100  -0.0248 141 ARG   A O   
3218 O O   B ARG   A 141 ? 0.1395 0.1694 0.2549 -0.0110 0.0102  -0.0298 141 ARG   A O   
3219 C CB  A ARG   A 141 ? 0.1608 0.1921 0.2295 -0.0107 -0.0100 -0.0201 141 ARG   A CB  
3220 C CB  B ARG   A 141 ? 0.1644 0.2131 0.2692 -0.0297 -0.0202 -0.0536 141 ARG   A CB  
3221 C CG  A ARG   A 141 ? 0.1783 0.2022 0.2590 -0.0149 -0.0125 -0.0185 141 ARG   A CG  
3222 C CG  B ARG   A 141 ? 0.1949 0.2449 0.3001 -0.0283 -0.0216 -0.0631 141 ARG   A CG  
3223 C CD  A ARG   A 141 ? 0.1921 0.2107 0.2870 -0.0158 -0.0199 -0.0052 141 ARG   A CD  
3224 C CD  B ARG   A 141 ? 0.2215 0.2775 0.3382 -0.0309 -0.0195 -0.0566 141 ARG   A CD  
3225 N NE  A ARG   A 141 ? 0.1969 0.2107 0.2991 -0.0145 -0.0275 0.0008  141 ARG   A NE  
3226 N NE  B ARG   A 141 ? 0.2354 0.3105 0.3621 -0.0346 -0.0172 -0.0558 141 ARG   A NE  
3227 C CZ  A ARG   A 141 ? 0.1983 0.2185 0.3124 -0.0156 -0.0357 0.0059  141 ARG   A CZ  
3228 C CZ  B ARG   A 141 ? 0.2362 0.3264 0.3749 -0.0518 -0.0236 -0.0530 141 ARG   A CZ  
3229 N NH1 A ARG   A 141 ? 0.2001 0.2219 0.3157 -0.0103 -0.0382 0.0072  141 ARG   A NH1 
3230 N NH1 B ARG   A 141 ? 0.2380 0.3364 0.3865 -0.0523 -0.0146 -0.0559 141 ARG   A NH1 
3231 N NH2 A ARG   A 141 ? 0.1994 0.2237 0.3210 -0.0131 -0.0390 0.0084  141 ARG   A NH2 
3232 N NH2 B ARG   A 141 ? 0.2428 0.3324 0.3872 -0.0512 -0.0246 -0.0512 141 ARG   A NH2 
3259 N N   . VAL   A 142 ? 0.1352 0.1785 0.2149 -0.0128 -0.0005 -0.0226 142 VAL   A N   
3260 C CA  . VAL   A 142 ? 0.1377 0.1717 0.2139 -0.0086 0.0130  -0.0221 142 VAL   A CA  
3261 C C   . VAL   A 142 ? 0.1263 0.1613 0.2021 -0.0155 0.0122  -0.0071 142 VAL   A C   
3262 O O   . VAL   A 142 ? 0.1325 0.1600 0.2174 -0.0041 0.0057  -0.0082 142 VAL   A O   
3263 C CB  . VAL   A 142 ? 0.1449 0.1886 0.2128 -0.0056 0.0092  -0.0143 142 VAL   A CB  
3264 C CG1 . VAL   A 142 ? 0.1416 0.1805 0.2140 -0.0096 0.0038  -0.0081 142 VAL   A CG1 
3265 C CG2 . VAL   A 142 ? 0.1539 0.2094 0.2300 -0.0035 0.0103  -0.0150 142 VAL   A CG2 
3276 N N   . CYS   A 143 ? 0.1286 0.1521 0.1895 -0.0136 0.0081  -0.0002 143 CYS   A N   
3277 C CA  . CYS   A 143 ? 0.1270 0.1446 0.2002 -0.0118 0.0110  0.0086  143 CYS   A CA  
3278 C C   . CYS   A 143 ? 0.1304 0.1408 0.2155 -0.0143 0.0075  0.0152  143 CYS   A C   
3279 O O   . CYS   A 143 ? 0.1298 0.1420 0.2194 -0.0067 0.0072  0.0188  143 CYS   A O   
3280 C CB  . CYS   A 143 ? 0.1383 0.1446 0.2036 -0.0069 0.0203  0.0215  143 CYS   A CB  
3281 S SG  . CYS   A 143 ? 0.1542 0.1527 0.1957 0.0043  0.0121  0.0152  143 CYS   A SG  
3287 N N   . VAL   A 144 ? 0.1351 0.1412 0.2442 -0.0137 0.0097  0.0180  144 VAL   A N   
3288 C CA  . VAL   A 144 ? 0.1383 0.1549 0.2949 -0.0140 0.0262  0.0276  144 VAL   A CA  
3289 C C   . VAL   A 144 ? 0.1359 0.1471 0.2989 -0.0167 -0.0030 0.0177  144 VAL   A C   
3290 O O   . VAL   A 144 ? 0.1568 0.1527 0.3032 -0.0095 0.0018  0.0229  144 VAL   A O   
3291 C CB  . VAL   A 144 ? 0.1647 0.1841 0.3605 -0.0001 0.0452  0.0350  144 VAL   A CB  
3292 C CG1 . VAL   A 144 ? 0.1832 0.2011 0.3801 -0.0166 0.0218  0.0390  144 VAL   A CG1 
3293 C CG2 . VAL   A 144 ? 0.1544 0.1863 0.3759 0.0005  0.0554  0.0478  144 VAL   A CG2 
3303 N N   . ASP   A 145 ? 0.1412 0.1424 0.3041 -0.0159 -0.0065 -0.0048 145 ASP   A N   
3304 C CA  . ASP   A 145 ? 0.1540 0.1474 0.3160 -0.0190 -0.0082 -0.0175 145 ASP   A CA  
3305 C C   . ASP   A 145 ? 0.1523 0.1488 0.3059 -0.0118 -0.0036 -0.0233 145 ASP   A C   
3306 O O   . ASP   A 145 ? 0.1683 0.1681 0.3663 -0.0122 -0.0027 -0.0607 145 ASP   A O   
3307 C CB  . ASP   A 145 ? 0.1691 0.1772 0.3418 -0.0204 -0.0174 -0.0253 145 ASP   A CB  
3308 C CG  . ASP   A 145 ? 0.1946 0.2110 0.3742 -0.0306 -0.0250 -0.0255 145 ASP   A CG  
3309 O OD1 . ASP   A 145 ? 0.1974 0.2133 0.3922 -0.0430 -0.0194 -0.0256 145 ASP   A OD1 
3310 O OD2 . ASP   A 145 ? 0.2159 0.2337 0.3874 -0.0311 -0.0352 -0.0301 145 ASP   A OD2 
3315 N N   . THR   A 146 ? 0.1390 0.1367 0.2393 -0.0126 0.0072  -0.0098 146 THR   A N   
3316 C CA  . THR   A 146 ? 0.1358 0.1364 0.2205 -0.0082 0.0048  -0.0040 146 THR   A CA  
3317 C C   . THR   A 146 ? 0.1317 0.1383 0.2219 -0.0045 0.0144  0.0065  146 THR   A C   
3318 O O   . THR   A 146 ? 0.1400 0.1539 0.2340 0.0007  0.0052  0.0028  146 THR   A O   
3319 C CB  . THR   A 146 ? 0.1321 0.1439 0.2068 -0.0042 0.0115  -0.0036 146 THR   A CB  
3320 O OG1 . THR   A 146 ? 0.1324 0.1649 0.2194 0.0043  0.0005  -0.0128 146 THR   A OG1 
3321 C CG2 . THR   A 146 ? 0.1349 0.1433 0.2166 -0.0045 0.0123  -0.0048 146 THR   A CG2 
3329 N N   . VAL   A 147 ? 0.1272 0.1410 0.2107 -0.0058 0.0193  0.0079  147 VAL   A N   
3330 C CA  . VAL   A 147 ? 0.1320 0.1379 0.2128 -0.0139 0.0294  0.0106  147 VAL   A CA  
3331 C C   . VAL   A 147 ? 0.1361 0.1338 0.2290 -0.0129 0.0220  0.0131  147 VAL   A C   
3332 O O   . VAL   A 147 ? 0.1361 0.1422 0.2529 -0.0164 0.0224  0.0179  147 VAL   A O   
3333 C CB  . VAL   A 147 ? 0.1431 0.1364 0.2084 -0.0148 0.0256  0.0170  147 VAL   A CB  
3334 C CG1 . VAL   A 147 ? 0.1737 0.1403 0.2034 -0.0110 0.0260  0.0175  147 VAL   A CG1 
3335 C CG2 . VAL   A 147 ? 0.1501 0.1400 0.2016 -0.0135 0.0151  0.0179  147 VAL   A CG2 
3345 N N   . ARG   A 148 ? 0.1341 0.1357 0.2296 -0.0190 0.0230  0.0282  148 ARG   A N   
3346 C CA  . ARG   A 148 ? 0.1415 0.1390 0.2193 -0.0131 0.0235  0.0339  148 ARG   A CA  
3347 C C   . ARG   A 148 ? 0.1505 0.1368 0.2266 -0.0111 0.0304  0.0501  148 ARG   A C   
3348 O O   . ARG   A 148 ? 0.1857 0.1487 0.2546 -0.0159 0.0414  0.0451  148 ARG   A O   
3349 C CB  . ARG   A 148 ? 0.1537 0.1410 0.2455 -0.0084 0.0343  0.0227  148 ARG   A CB  
3350 C CG  . ARG   A 148 ? 0.1678 0.1380 0.2753 -0.0088 0.0416  0.0194  148 ARG   A CG  
3351 C CD  . ARG   A 148 ? 0.1828 0.1418 0.2841 -0.0053 0.0513  0.0381  148 ARG   A CD  
3352 N NE  . ARG   A 148 ? 0.1780 0.1448 0.2837 0.0049  0.0547  0.0438  148 ARG   A NE  
3353 C CZ  . ARG   A 148 ? 0.1726 0.1367 0.2704 0.0057  0.0566  0.0307  148 ARG   A CZ  
3354 N NH1 . ARG   A 148 ? 0.1829 0.1410 0.2648 -0.0115 0.0564  0.0009  148 ARG   A NH1 
3355 N NH2 . ARG   A 148 ? 0.1654 0.1558 0.2799 0.0159  0.0598  0.0449  148 ARG   A NH2 
3369 N N   . THR   A 149 ? 0.1485 0.1458 0.2204 -0.0140 0.0135  0.0411  149 THR   A N   
3370 C CA  . THR   A 149 ? 0.1504 0.1560 0.2155 -0.0083 0.0172  0.0455  149 THR   A CA  
3371 C C   . THR   A 149 ? 0.1452 0.1515 0.2013 -0.0191 0.0192  0.0505  149 THR   A C   
3372 O O   . THR   A 149 ? 0.1448 0.1645 0.2163 -0.0170 0.0123  0.0371  149 THR   A O   
3373 C CB  . THR   A 149 ? 0.1513 0.1642 0.2040 -0.0119 0.0165  0.0363  149 THR   A CB  
3374 O OG1 . THR   A 149 ? 0.1559 0.1535 0.2021 -0.0187 0.0128  0.0277  149 THR   A OG1 
3375 C CG2 . THR   A 149 ? 0.1515 0.1751 0.2075 -0.0027 0.0176  0.0328  149 THR   A CG2 
3383 N N   . ASN   A 150 ? 0.1536 0.1570 0.1999 -0.0057 0.0224  0.0521  150 ASN   A N   
3384 C CA  . ASN   A 150 ? 0.1586 0.1632 0.2158 -0.0062 0.0329  0.0459  150 ASN   A CA  
3385 C C   . ASN   A 150 ? 0.1411 0.1542 0.2222 -0.0137 0.0228  0.0396  150 ASN   A C   
3386 O O   . ASN   A 150 ? 0.1580 0.1646 0.2422 -0.0110 0.0010  0.0477  150 ASN   A O   
3387 C CB  . ASN   A 150 ? 0.1956 0.1867 0.2470 -0.0057 0.0541  0.0692  150 ASN   A CB  
3388 C CG  . ASN   A 150 ? 0.2489 0.2173 0.2976 -0.0154 0.0413  0.0758  150 ASN   A CG  
3389 O OD1 . ASN   A 150 ? 0.2794 0.2239 0.3237 -0.0222 0.0363  0.0804  150 ASN   A OD1 
3390 N ND2 . ASN   A 150 ? 0.2741 0.2376 0.3332 -0.0115 0.0163  0.0771  150 ASN   A ND2 
3397 N N   . VAL   A 151 ? 0.1416 0.1395 0.2252 -0.0192 0.0209  0.0418  151 VAL   A N   
3398 C CA  . VAL   A 151 ? 0.1461 0.1380 0.2211 -0.0162 0.0280  0.0404  151 VAL   A CA  
3399 C C   . VAL   A 151 ? 0.1376 0.1348 0.2285 -0.0207 0.0220  0.0460  151 VAL   A C   
3400 O O   . VAL   A 151 ? 0.1443 0.1405 0.2648 -0.0189 0.0251  0.0322  151 VAL   A O   
3401 C CB  . VAL   A 151 ? 0.1749 0.1588 0.2251 0.0052  0.0260  0.0379  151 VAL   A CB  
3402 C CG1 . VAL   A 151 ? 0.1698 0.1781 0.2487 -0.0057 0.0267  0.0343  151 VAL   A CG1 
3403 C CG2 . VAL   A 151 ? 0.1857 0.1581 0.2248 0.0069  0.0445  0.0364  151 VAL   A CG2 
3413 N N   . TYR   A 152 ? 0.1319 0.1397 0.2198 -0.0197 0.0243  0.0411  152 TYR   A N   
3414 C CA  . TYR   A 152 ? 0.1390 0.1476 0.1966 -0.0151 0.0321  0.0428  152 TYR   A CA  
3415 C C   . TYR   A 152 ? 0.1363 0.1386 0.1850 -0.0147 0.0343  0.0410  152 TYR   A C   
3416 O O   . TYR   A 152 ? 0.1478 0.1374 0.1858 -0.0177 0.0306  0.0283  152 TYR   A O   
3417 C CB  . TYR   A 152 ? 0.1551 0.1605 0.2002 -0.0063 0.0374  0.0442  152 TYR   A CB  
3418 C CG  . TYR   A 152 ? 0.1688 0.1837 0.1949 -0.0130 0.0425  0.0542  152 TYR   A CG  
3419 C CD1 . TYR   A 152 ? 0.1836 0.2066 0.2070 -0.0043 0.0393  0.0623  152 TYR   A CD1 
3420 C CD2 . TYR   A 152 ? 0.1799 0.1970 0.1965 -0.0241 0.0413  0.0548  152 TYR   A CD2 
3421 C CE1 . TYR   A 152 ? 0.2151 0.2295 0.2187 -0.0039 0.0251  0.0721  152 TYR   A CE1 
3422 C CE2 . TYR   A 152 ? 0.2048 0.2209 0.2097 -0.0256 0.0367  0.0636  152 TYR   A CE2 
3423 C CZ  . TYR   A 152 ? 0.2276 0.2282 0.2092 -0.0163 0.0245  0.0888  152 TYR   A CZ  
3424 O OH  . TYR   A 152 ? 0.2525 0.2473 0.2388 -0.0132 0.0260  0.0856  152 TYR   A OH  
3434 N N   . LEU   A 153 ? 0.1373 0.1295 0.1980 -0.0173 0.0412  0.0421  153 LEU   A N   
3435 C CA  . LEU   A 153 ? 0.1307 0.1301 0.2103 -0.0081 0.0350  0.0350  153 LEU   A CA  
3436 C C   . LEU   A 153 ? 0.1356 0.1354 0.2078 -0.0042 0.0452  0.0382  153 LEU   A C   
3437 O O   . LEU   A 153 ? 0.1411 0.1412 0.2372 -0.0028 0.0518  0.0368  153 LEU   A O   
3438 C CB  . LEU   A 153 ? 0.1245 0.1356 0.2173 -0.0040 0.0266  0.0288  153 LEU   A CB  
3439 C CG  . LEU   A 153 ? 0.1321 0.1421 0.2129 -0.0063 0.0251  0.0269  153 LEU   A CG  
3440 C CD1 . LEU   A 153 ? 0.1438 0.1423 0.2182 -0.0054 0.0107  0.0229  153 LEU   A CD1 
3441 C CD2 . LEU   A 153 ? 0.1448 0.1478 0.2233 -0.0095 0.0420  0.0188  153 LEU   A CD2 
3453 N N   A ALA   A 154 ? 0.1410 0.1317 0.1981 -0.0007 0.0530  0.0333  154 ALA   A N   
3454 N N   B ALA   A 154 ? 0.1344 0.1331 0.1997 -0.0021 0.0388  0.0413  154 ALA   A N   
3455 C CA  A ALA   A 154 ? 0.1509 0.1324 0.1952 0.0015  0.0608  0.0258  154 ALA   A CA  
3456 C CA  B ALA   A 154 ? 0.1442 0.1382 0.1914 -0.0004 0.0369  0.0412  154 ALA   A CA  
3457 C C   A ALA   A 154 ? 0.1532 0.1330 0.1962 0.0061  0.0652  0.0205  154 ALA   A C   
3458 C C   B ALA   A 154 ? 0.1401 0.1388 0.1822 0.0020  0.0320  0.0377  154 ALA   A C   
3459 O O   A ALA   A 154 ? 0.1544 0.1357 0.2158 0.0012  0.0701  0.0291  154 ALA   A O   
3460 O O   B ALA   A 154 ? 0.1431 0.1465 0.1835 -0.0046 0.0276  0.0409  154 ALA   A O   
3461 C CB  A ALA   A 154 ? 0.1598 0.1375 0.2018 0.0053  0.0524  0.0155  154 ALA   A CB  
3462 C CB  B ALA   A 154 ? 0.1588 0.1510 0.1956 0.0054  0.0175  0.0269  154 ALA   A CB  
3473 N N   A VAL   A 155 ? 0.1613 0.1431 0.1919 0.0127  0.0587  0.0221  155 VAL   A N   
3474 N N   B VAL   A 155 ? 0.1426 0.1405 0.1861 -0.0026 0.0398  0.0518  155 VAL   A N   
3475 C CA  A VAL   A 155 ? 0.1682 0.1528 0.1901 0.0188  0.0492  0.0321  155 VAL   A CA  
3476 C CA  B VAL   A 155 ? 0.1447 0.1462 0.1896 0.0005  0.0330  0.0488  155 VAL   A CA  
3477 C C   A VAL   A 155 ? 0.1724 0.1559 0.1828 0.0268  0.0429  0.0402  155 VAL   A C   
3478 C C   B VAL   A 155 ? 0.1479 0.1459 0.2089 0.0091  0.0331  0.0487  155 VAL   A C   
3479 O O   A VAL   A 155 ? 0.1599 0.1585 0.1713 0.0273  0.0323  0.0304  155 VAL   A O   
3480 O O   B VAL   A 155 ? 0.1423 0.1475 0.2304 0.0122  0.0418  0.0314  155 VAL   A O   
3481 C CB  A VAL   A 155 ? 0.1714 0.1608 0.2020 0.0225  0.0377  0.0323  155 VAL   A CB  
3482 C CB  B VAL   A 155 ? 0.1452 0.1560 0.1781 -0.0015 0.0182  0.0317  155 VAL   A CB  
3483 C CG1 A VAL   A 155 ? 0.1695 0.1652 0.1984 0.0221  0.0454  0.0387  155 VAL   A CG1 
3484 C CG1 B VAL   A 155 ? 0.1537 0.1651 0.1804 -0.0060 0.0113  0.0251  155 VAL   A CG1 
3485 C CG2 A VAL   A 155 ? 0.1719 0.1625 0.2014 0.0266  0.0297  0.0378  155 VAL   A CG2 
3486 C CG2 B VAL   A 155 ? 0.1445 0.1504 0.1872 -0.0058 0.0151  0.0234  155 VAL   A CG2 
3505 N N   A PHE   A 156 ? 0.1879 0.1585 0.1961 0.0324  0.0474  0.0515  156 PHE   A N   
3506 N N   B PHE   A 156 ? 0.1530 0.1513 0.2138 0.0119  0.0149  0.0377  156 PHE   A N   
3507 C CA  A PHE   A 156 ? 0.2070 0.1682 0.2221 0.0375  0.0420  0.0488  156 PHE   A CA  
3508 C CA  B PHE   A 156 ? 0.1646 0.1540 0.2506 0.0168  0.0025  0.0153  156 PHE   A CA  
3509 C C   A PHE   A 156 ? 0.2110 0.1730 0.2181 0.0387  0.0479  0.0575  156 PHE   A C   
3510 C C   B PHE   A 156 ? 0.1660 0.1499 0.2578 0.0194  0.0004  0.0252  156 PHE   A C   
3511 O O   A PHE   A 156 ? 0.2141 0.1748 0.2114 0.0407  0.0546  0.0510  156 PHE   A O   
3512 O O   B PHE   A 156 ? 0.1730 0.1539 0.2989 0.0182  0.0141  0.0271  156 PHE   A O   
3513 C CB  A PHE   A 156 ? 0.2222 0.1717 0.2471 0.0402  0.0329  0.0427  156 PHE   A CB  
3514 C CB  B PHE   A 156 ? 0.1813 0.1656 0.2819 0.0167  -0.0110 -0.0064 156 PHE   A CB  
3515 C CG  A PHE   A 156 ? 0.2361 0.1713 0.2605 0.0422  0.0186  0.0446  156 PHE   A CG  
3516 C CG  B PHE   A 156 ? 0.2000 0.1772 0.3171 0.0221  -0.0288 -0.0116 156 PHE   A CG  
3517 C CD1 A PHE   A 156 ? 0.2432 0.1774 0.2634 0.0402  0.0082  0.0410  156 PHE   A CD1 
3518 C CD1 B PHE   A 156 ? 0.2168 0.1895 0.3271 0.0308  -0.0199 -0.0225 156 PHE   A CD1 
3519 C CD2 A PHE   A 156 ? 0.2464 0.1705 0.2706 0.0464  0.0054  0.0547  156 PHE   A CD2 
3520 C CD2 B PHE   A 156 ? 0.2147 0.1803 0.3384 0.0159  -0.0226 -0.0147 156 PHE   A CD2 
3521 C CE1 A PHE   A 156 ? 0.2490 0.1806 0.2638 0.0413  0.0099  0.0362  156 PHE   A CE1 
3522 C CE1 B PHE   A 156 ? 0.2217 0.2010 0.3359 0.0364  -0.0243 -0.0238 156 PHE   A CE1 
3523 C CE2 A PHE   A 156 ? 0.2543 0.1783 0.2711 0.0450  0.0047  0.0440  156 PHE   A CE2 
3524 C CE2 B PHE   A 156 ? 0.2274 0.1914 0.3523 0.0179  -0.0298 -0.0195 156 PHE   A CE2 
3525 C CZ  A PHE   A 156 ? 0.2556 0.1814 0.2692 0.0446  0.0129  0.0335  156 PHE   A CZ  
3526 C CZ  B PHE   A 156 ? 0.2238 0.1999 0.3469 0.0356  -0.0319 -0.0207 156 PHE   A CZ  
3545 N N   A ASP   A 157 ? 0.2135 0.1805 0.2384 0.0361  0.0456  0.0721  157 ASP   A N   
3546 N N   B ASP   A 157 ? 0.1645 0.1444 0.2174 0.0130  -0.0061 0.0356  157 ASP   A N   
3547 C CA  A ASP   A 157 ? 0.2224 0.2015 0.2682 0.0271  0.0390  0.0720  157 ASP   A CA  
3548 C CA  B ASP   A 157 ? 0.1688 0.1544 0.2025 0.0011  -0.0055 0.0467  157 ASP   A CA  
3549 C C   A ASP   A 157 ? 0.2252 0.2114 0.2772 0.0252  0.0493  0.0718  157 ASP   A C   
3550 C C   B ASP   A 157 ? 0.1657 0.1608 0.2064 0.0119  0.0089  0.0553  157 ASP   A C   
3551 O O   A ASP   A 157 ? 0.2238 0.2093 0.2808 0.0279  0.0535  0.0754  157 ASP   A O   
3552 O O   B ASP   A 157 ? 0.1649 0.1605 0.2130 0.0162  0.0205  0.0545  157 ASP   A O   
3553 C CB  A ASP   A 157 ? 0.2282 0.2142 0.2965 0.0228  0.0268  0.0655  157 ASP   A CB  
3554 C CB  B ASP   A 157 ? 0.1761 0.1531 0.2208 0.0015  -0.0193 0.0524  157 ASP   A CB  
3555 C CG  A ASP   A 157 ? 0.2359 0.2281 0.3211 0.0159  0.0230  0.0632  157 ASP   A CG  
3556 C CG  B ASP   A 157 ? 0.1884 0.1555 0.2522 -0.0049 -0.0295 0.0499  157 ASP   A CG  
3557 O OD1 A ASP   A 157 ? 0.2442 0.2374 0.3356 0.0097  0.0231  0.0591  157 ASP   A OD1 
3558 O OD1 B ASP   A 157 ? 0.1946 0.1411 0.2639 -0.0156 -0.0359 0.0291  157 ASP   A OD1 
3559 O OD2 A ASP   A 157 ? 0.2345 0.2297 0.3322 0.0149  0.0205  0.0631  157 ASP   A OD2 
3560 O OD2 B ASP   A 157 ? 0.2010 0.1718 0.2769 0.0002  -0.0372 0.0698  157 ASP   A OD2 
3569 N N   A LYS   A 158 ? 0.2320 0.2272 0.2909 0.0211  0.0513  0.0673  158 LYS   A N   
3570 N N   B LYS   A 158 ? 0.1662 0.1717 0.2156 0.0145  0.0165  0.0551  158 LYS   A N   
3571 C CA  A LYS   A 158 ? 0.2386 0.2445 0.3018 0.0165  0.0519  0.0643  158 LYS   A CA  
3572 C CA  B LYS   A 158 ? 0.1690 0.1931 0.2386 0.0128  0.0213  0.0471  158 LYS   A CA  
3573 C C   A LYS   A 158 ? 0.2326 0.2482 0.3016 0.0111  0.0541  0.0712  158 LYS   A C   
3574 C C   B LYS   A 158 ? 0.1570 0.1802 0.2357 0.0094  0.0069  0.0560  158 LYS   A C   
3575 O O   A LYS   A 158 ? 0.2330 0.2507 0.3093 0.0067  0.0567  0.0802  158 LYS   A O   
3576 O O   B LYS   A 158 ? 0.1589 0.1902 0.2427 0.0103  0.0234  0.0472  158 LYS   A O   
3577 C CB  A LYS   A 158 ? 0.2524 0.2575 0.3107 0.0158  0.0541  0.0571  158 LYS   A CB  
3578 C CB  B LYS   A 158 ? 0.1859 0.2154 0.2661 0.0111  0.0412  0.0439  158 LYS   A CB  
3579 C CG  A LYS   A 158 ? 0.2669 0.2713 0.3210 0.0141  0.0554  0.0496  158 LYS   A CG  
3580 C CG  B LYS   A 158 ? 0.1983 0.2416 0.2967 0.0072  0.0452  0.0415  158 LYS   A CG  
3581 C CD  A LYS   A 158 ? 0.2778 0.2821 0.3267 0.0136  0.0584  0.0433  158 LYS   A CD  
3582 C CD  B LYS   A 158 ? 0.2163 0.2702 0.3355 0.0006  0.0459  0.0295  158 LYS   A CD  
3583 C CE  A LYS   A 158 ? 0.2851 0.2904 0.3272 0.0115  0.0623  0.0415  158 LYS   A CE  
3584 C CE  B LYS   A 158 ? 0.2286 0.2894 0.3545 -0.0027 0.0433  0.0256  158 LYS   A CE  
3585 N NZ  A LYS   A 158 ? 0.2891 0.2956 0.3285 0.0100  0.0652  0.0413  158 LYS   A NZ  
3586 N NZ  B LYS   A 158 ? 0.2412 0.2982 0.3722 -0.0053 0.0412  0.0266  158 LYS   A NZ  
3613 N N   A ASN   A 159 ? 0.2255 0.2480 0.2997 0.0052  0.0513  0.0701  159 ASN   A N   
3614 N N   B ASN   A 159 ? 0.1670 0.1774 0.2416 -0.0002 -0.0174 0.0523  159 ASN   A N   
3615 C CA  A ASN   A 159 ? 0.2197 0.2451 0.2903 0.0036  0.0443  0.0682  159 ASN   A CA  
3616 C CA  B ASN   A 159 ? 0.1791 0.1714 0.2557 -0.0025 -0.0332 0.0501  159 ASN   A CA  
3617 C C   A ASN   A 159 ? 0.2138 0.2419 0.2803 0.0029  0.0524  0.0640  159 ASN   A C   
3618 C C   B ASN   A 159 ? 0.1826 0.1724 0.2496 -0.0101 -0.0239 0.0463  159 ASN   A C   
3619 O O   A ASN   A 159 ? 0.2121 0.2432 0.2869 0.0070  0.0518  0.0639  159 ASN   A O   
3620 O O   B ASN   A 159 ? 0.1756 0.1782 0.2557 -0.0199 -0.0189 0.0317  159 ASN   A O   
3621 C CB  A ASN   A 159 ? 0.2201 0.2459 0.2959 -0.0023 0.0288  0.0720  159 ASN   A CB  
3622 C CB  B ASN   A 159 ? 0.1952 0.1894 0.2839 0.0038  -0.0476 0.0479  159 ASN   A CB  
3623 C CG  A ASN   A 159 ? 0.2234 0.2465 0.3021 -0.0067 0.0170  0.0737  159 ASN   A CG  
3624 C CG  B ASN   A 159 ? 0.2043 0.2071 0.3199 0.0164  -0.0450 0.0373  159 ASN   A CG  
3625 O OD1 A ASN   A 159 ? 0.2262 0.2455 0.2989 -0.0118 0.0180  0.0813  159 ASN   A OD1 
3626 O OD1 B ASN   A 159 ? 0.2124 0.2265 0.3527 0.0224  -0.0333 0.0346  159 ASN   A OD1 
3627 N ND2 A ASN   A 159 ? 0.2203 0.2457 0.3021 -0.0074 0.0143  0.0715  159 ASN   A ND2 
3628 N ND2 B ASN   A 159 ? 0.2086 0.2105 0.3213 0.0285  -0.0566 0.0403  159 ASN   A ND2 
3641 N N   A LEU   A 160 ? 0.2119 0.2372 0.2686 0.0012  0.0506  0.0598  160 LEU   A N   
3642 N N   B LEU   A 160 ? 0.1877 0.1714 0.2313 0.0058  -0.0081 0.0574  160 LEU   A N   
3643 C CA  A LEU   A 160 ? 0.2128 0.2328 0.2567 -0.0035 0.0481  0.0596  160 LEU   A CA  
3644 C CA  B LEU   A 160 ? 0.1987 0.1781 0.2239 0.0104  0.0180  0.0604  160 LEU   A CA  
3645 C C   A LEU   A 160 ? 0.2110 0.2340 0.2509 -0.0042 0.0420  0.0570  160 LEU   A C   
3646 C C   B LEU   A 160 ? 0.1895 0.1773 0.2301 0.0131  0.0273  0.0735  160 LEU   A C   
3647 O O   A LEU   A 160 ? 0.2112 0.2355 0.2542 -0.0079 0.0383  0.0547  160 LEU   A O   
3648 O O   B LEU   A 160 ? 0.1932 0.1859 0.2358 0.0051  0.0338  0.0741  160 LEU   A O   
3649 C CB  A LEU   A 160 ? 0.2141 0.2290 0.2492 -0.0025 0.0531  0.0573  160 LEU   A CB  
3650 C CB  B LEU   A 160 ? 0.2139 0.1852 0.2179 0.0072  0.0358  0.0538  160 LEU   A CB  
3651 C CG  A LEU   A 160 ? 0.2173 0.2253 0.2513 -0.0018 0.0522  0.0467  160 LEU   A CG  
3652 C CG  B LEU   A 160 ? 0.2283 0.2005 0.2319 0.0017  0.0469  0.0339  160 LEU   A CG  
3653 C CD1 A LEU   A 160 ? 0.2192 0.2281 0.2500 -0.0019 0.0496  0.0421  160 LEU   A CD1 
3654 C CD1 B LEU   A 160 ? 0.2366 0.2164 0.2439 -0.0054 0.0491  0.0337  160 LEU   A CD1 
3655 C CD2 A LEU   A 160 ? 0.2178 0.2212 0.2502 -0.0021 0.0579  0.0455  160 LEU   A CD2 
3656 C CD2 B LEU   A 160 ? 0.2345 0.2043 0.2403 0.0004  0.0508  0.0330  160 LEU   A CD2 
3679 N N   A TYR   A 161 ? 0.2095 0.2352 0.2443 -0.0044 0.0448  0.0615  161 TYR   A N   
3680 N N   B TYR   A 161 ? 0.1730 0.1771 0.2166 0.0176  0.0407  0.0783  161 TYR   A N   
3681 C CA  A TYR   A 161 ? 0.2088 0.2370 0.2430 -0.0039 0.0403  0.0607  161 TYR   A CA  
3682 C CA  B TYR   A 161 ? 0.1689 0.1894 0.2255 0.0271  0.0427  0.0756  161 TYR   A CA  
3683 C C   A TYR   A 161 ? 0.2141 0.2439 0.2585 0.0016  0.0295  0.0615  161 TYR   A C   
3684 C C   B TYR   A 161 ? 0.1678 0.1921 0.2483 0.0181  0.0318  0.0825  161 TYR   A C   
3685 O O   A TYR   A 161 ? 0.2139 0.2410 0.2540 0.0018  0.0261  0.0693  161 TYR   A O   
3686 O O   B TYR   A 161 ? 0.1659 0.1878 0.2387 0.0142  0.0378  0.0832  161 TYR   A O   
3687 C CB  A TYR   A 161 ? 0.2073 0.2372 0.2363 -0.0068 0.0437  0.0554  161 TYR   A CB  
3688 C CB  B TYR   A 161 ? 0.1747 0.2067 0.2186 0.0361  0.0479  0.0773  161 TYR   A CB  
3689 C CG  A TYR   A 161 ? 0.2078 0.2387 0.2325 -0.0058 0.0391  0.0488  161 TYR   A CG  
3690 C CG  B TYR   A 161 ? 0.1711 0.2184 0.2163 0.0505  0.0521  0.0769  161 TYR   A CG  
3691 C CD1 A TYR   A 161 ? 0.2073 0.2378 0.2317 -0.0070 0.0358  0.0435  161 TYR   A CD1 
3692 C CD1 B TYR   A 161 ? 0.1714 0.2196 0.2173 0.0547  0.0567  0.0748  161 TYR   A CD1 
3693 C CD2 A TYR   A 161 ? 0.2081 0.2400 0.2294 -0.0038 0.0351  0.0517  161 TYR   A CD2 
3694 C CD2 B TYR   A 161 ? 0.1680 0.2267 0.2180 0.0571  0.0508  0.0762  161 TYR   A CD2 
3695 C CE1 A TYR   A 161 ? 0.2107 0.2391 0.2351 -0.0071 0.0307  0.0467  161 TYR   A CE1 
3696 C CE1 B TYR   A 161 ? 0.1745 0.2237 0.2117 0.0592  0.0437  0.0903  161 TYR   A CE1 
3697 C CE2 A TYR   A 161 ? 0.2119 0.2409 0.2340 -0.0055 0.0303  0.0539  161 TYR   A CE2 
3698 C CE2 B TYR   A 161 ? 0.1777 0.2343 0.2158 0.0477  0.0499  0.0813  161 TYR   A CE2 
3699 C CZ  A TYR   A 161 ? 0.2161 0.2420 0.2400 -0.0060 0.0244  0.0529  161 TYR   A CZ  
3700 C CZ  B TYR   A 161 ? 0.1922 0.2378 0.2107 0.0451  0.0473  0.0870  161 TYR   A CZ  
3701 O OH  A TYR   A 161 ? 0.2247 0.2455 0.2554 -0.0038 0.0119  0.0560  161 TYR   A OH  
3702 O OH  B TYR   A 161 ? 0.2150 0.2488 0.2045 0.0374  0.0474  0.0948  161 TYR   A OH  
3721 N N   A ASP   A 162 ? 0.2184 0.2531 0.2715 0.0064  0.0302  0.0582  162 ASP   A N   
3722 N N   B ASP   A 162 ? 0.1669 0.2043 0.2769 0.0100  0.0343  0.0836  162 ASP   A N   
3723 C CA  A ASP   A 162 ? 0.2216 0.2617 0.2789 0.0078  0.0301  0.0552  162 ASP   A CA  
3724 C CA  B ASP   A 162 ? 0.1744 0.2211 0.3039 0.0089  0.0143  0.0825  162 ASP   A CA  
3725 C C   A ASP   A 162 ? 0.2271 0.2641 0.2786 0.0048  0.0275  0.0558  162 ASP   A C   
3726 C C   B ASP   A 162 ? 0.1819 0.2104 0.2978 -0.0042 -0.0143 0.0736  162 ASP   A C   
3727 O O   A ASP   A 162 ? 0.2294 0.2609 0.2830 0.0027  0.0326  0.0660  162 ASP   A O   
3728 O O   B ASP   A 162 ? 0.1830 0.2022 0.3119 -0.0096 -0.0278 0.0452  162 ASP   A O   
3729 C CB  A ASP   A 162 ? 0.2189 0.2680 0.2876 0.0132  0.0291  0.0498  162 ASP   A CB  
3730 C CB  B ASP   A 162 ? 0.1720 0.2439 0.3480 0.0173  0.0220  0.0850  162 ASP   A CB  
3731 C CG  A ASP   A 162 ? 0.2159 0.2732 0.2935 0.0161  0.0305  0.0479  162 ASP   A CG  
3732 C CG  B ASP   A 162 ? 0.1743 0.2639 0.3863 0.0252  0.0237  0.0904  162 ASP   A CG  
3733 O OD1 A ASP   A 162 ? 0.2177 0.2776 0.2998 0.0171  0.0277  0.0470  162 ASP   A OD1 
3734 O OD1 B ASP   A 162 ? 0.1806 0.2732 0.3968 0.0313  0.0246  0.0958  162 ASP   A OD1 
3735 O OD2 A ASP   A 162 ? 0.2133 0.2725 0.2962 0.0181  0.0352  0.0491  162 ASP   A OD2 
3736 O OD2 B ASP   A 162 ? 0.1859 0.2739 0.4059 0.0306  0.0214  0.0879  162 ASP   A OD2 
3745 N N   A LYS   A 163 ? 0.2316 0.2674 0.2785 0.0083  0.0171  0.0456  163 LYS   A N   
3746 N N   B LYS   A 163 ? 0.1980 0.2259 0.2823 -0.0059 -0.0128 0.0879  163 LYS   A N   
3747 C CA  A LYS   A 163 ? 0.2371 0.2710 0.2806 0.0117  0.0041  0.0376  163 LYS   A CA  
3748 C CA  B LYS   A 163 ? 0.2237 0.2445 0.2872 -0.0022 -0.0212 0.0882  163 LYS   A CA  
3749 C C   A LYS   A 163 ? 0.2210 0.2521 0.2590 0.0132  0.0013  0.0369  163 LYS   A C   
3750 C C   B LYS   A 163 ? 0.2081 0.2303 0.2756 -0.0074 -0.0100 0.0814  163 LYS   A C   
3751 O O   A LYS   A 163 ? 0.2190 0.2509 0.2619 0.0125  -0.0115 0.0384  163 LYS   A O   
3752 O O   B LYS   A 163 ? 0.2057 0.2379 0.2781 -0.0099 -0.0222 0.0673  163 LYS   A O   
3753 C CB  A LYS   A 163 ? 0.2615 0.2921 0.3141 0.0160  -0.0011 0.0292  163 LYS   A CB  
3754 C CB  B LYS   A 163 ? 0.2731 0.2785 0.3168 0.0083  -0.0230 0.0929  163 LYS   A CB  
3755 C CG  A LYS   A 163 ? 0.2836 0.3112 0.3527 0.0182  -0.0026 0.0229  163 LYS   A CG  
3756 C CG  B LYS   A 163 ? 0.3193 0.3126 0.3717 0.0152  -0.0205 0.0866  163 LYS   A CG  
3757 C CD  A LYS   A 163 ? 0.3034 0.3277 0.3891 0.0196  -0.0053 0.0187  163 LYS   A CD  
3758 C CD  B LYS   A 163 ? 0.3642 0.3414 0.4309 0.0176  -0.0189 0.0773  163 LYS   A CD  
3759 C CE  A LYS   A 163 ? 0.3172 0.3391 0.4170 0.0197  -0.0081 0.0167  163 LYS   A CE  
3760 C CE  B LYS   A 163 ? 0.3948 0.3645 0.4753 0.0198  -0.0206 0.0743  163 LYS   A CE  
3761 N NZ  A LYS   A 163 ? 0.3250 0.3455 0.4320 0.0196  -0.0097 0.0188  163 LYS   A NZ  
3762 N NZ  B LYS   A 163 ? 0.4095 0.3756 0.5053 0.0221  -0.0232 0.0724  163 LYS   A NZ  
3789 N N   A LEU   A 164 ? 0.2045 0.2330 0.2334 0.0124  0.0106  0.0381  164 LEU   A N   
3790 N N   B LEU   A 164 ? 0.1905 0.2136 0.2602 -0.0146 -0.0004 0.0817  164 LEU   A N   
3791 C CA  A LEU   A 164 ? 0.1911 0.2173 0.2199 0.0118  0.0219  0.0390  164 LEU   A CA  
3792 C CA  B LEU   A 164 ? 0.1868 0.2083 0.2709 -0.0191 0.0164  0.0716  164 LEU   A CA  
3793 C C   A LEU   A 164 ? 0.1823 0.2066 0.2316 0.0108  0.0256  0.0487  164 LEU   A C   
3794 C C   B LEU   A 164 ? 0.1842 0.2173 0.2960 -0.0201 0.0143  0.0876  164 LEU   A C   
3795 O O   A LEU   A 164 ? 0.1796 0.2050 0.2255 0.0097  0.0305  0.0451  164 LEU   A O   
3796 O O   B LEU   A 164 ? 0.1787 0.2185 0.3041 -0.0238 0.0270  0.0728  164 LEU   A O   
3797 C CB  A LEU   A 164 ? 0.1850 0.2144 0.1965 0.0109  0.0312  0.0348  164 LEU   A CB  
3798 C CB  B LEU   A 164 ? 0.1806 0.1979 0.2542 -0.0223 0.0282  0.0524  164 LEU   A CB  
3799 C CG  A LEU   A 164 ? 0.1872 0.2129 0.1862 0.0103  0.0336  0.0334  164 LEU   A CG  
3800 C CG  B LEU   A 164 ? 0.1818 0.1915 0.2358 -0.0135 0.0385  0.0402  164 LEU   A CG  
3801 C CD1 A LEU   A 164 ? 0.1860 0.2131 0.1803 0.0078  0.0372  0.0316  164 LEU   A CD1 
3802 C CD1 B LEU   A 164 ? 0.1751 0.1921 0.2307 -0.0178 0.0436  0.0286  164 LEU   A CD1 
3803 C CD2 A LEU   A 164 ? 0.1905 0.2133 0.1778 0.0100  0.0344  0.0337  164 LEU   A CD2 
3804 C CD2 B LEU   A 164 ? 0.1943 0.1941 0.2354 -0.0084 0.0325  0.0369  164 LEU   A CD2 
3827 N N   A VAL   A 165 ? 0.1711 0.2006 0.2417 0.0091  0.0359  0.0608  165 VAL   A N   
3828 N N   B VAL   A 165 ? 0.1771 0.2341 0.3110 -0.0153 0.0203  0.1118  165 VAL   A N   
3829 C CA  A VAL   A 165 ? 0.1676 0.2029 0.2496 0.0016  0.0529  0.0655  165 VAL   A CA  
3830 C CA  B VAL   A 165 ? 0.1992 0.2610 0.3369 -0.0140 0.0181  0.1270  165 VAL   A CA  
3831 C C   A VAL   A 165 ? 0.1507 0.2075 0.2473 -0.0075 0.0530  0.0507  165 VAL   A C   
3832 C C   B VAL   A 165 ? 0.2041 0.2815 0.3847 -0.0247 0.0022  0.1227  165 VAL   A C   
3833 O O   A VAL   A 165 ? 0.1348 0.2078 0.2565 -0.0083 0.0834  0.0492  165 VAL   A O   
3834 O O   B VAL   A 165 ? 0.1989 0.2849 0.4202 -0.0256 0.0008  0.1146  165 VAL   A O   
3835 C CB  A VAL   A 165 ? 0.1815 0.2008 0.2614 0.0024  0.0656  0.0800  165 VAL   A CB  
3836 C CB  B VAL   A 165 ? 0.2224 0.2719 0.3279 -0.0112 0.0369  0.1356  165 VAL   A CB  
3837 C CG1 A VAL   A 165 ? 0.1801 0.2042 0.2667 -0.0020 0.0691  0.0810  165 VAL   A CG1 
3838 C CG1 B VAL   A 165 ? 0.2232 0.2797 0.3287 -0.0107 0.0317  0.1318  165 VAL   A CG1 
3839 C CG2 A VAL   A 165 ? 0.1913 0.2029 0.2652 0.0075  0.0686  0.0877  165 VAL   A CG2 
3840 C CG2 B VAL   A 165 ? 0.2358 0.2790 0.3183 0.0021  0.0352  0.1427  165 VAL   A CG2 
3859 N N   A SER   A 166 ? 0.1424 0.2084 0.2260 -0.0131 0.0334  0.0331  166 SER   A N   
3860 N N   B SER   A 166 ? 0.2074 0.2962 0.3838 -0.0331 -0.0040 0.1210  166 SER   A N   
3861 C CA  A SER   A 166 ? 0.1453 0.2150 0.2130 -0.0232 0.0177  0.0257  166 SER   A CA  
3862 C CA  B SER   A 166 ? 0.2329 0.3171 0.3915 -0.0375 -0.0259 0.1147  166 SER   A CA  
3863 C C   A SER   A 166 ? 0.1531 0.2201 0.2018 -0.0275 -0.0030 0.0205  166 SER   A C   
3864 C C   B SER   A 166 ? 0.2594 0.3307 0.3674 -0.0469 -0.0310 0.1069  166 SER   A C   
3865 O O   A SER   A 166 ? 0.1662 0.2297 0.2073 -0.0324 -0.0003 0.0203  166 SER   A O   
3866 O O   B SER   A 166 ? 0.2685 0.3379 0.3532 -0.0524 -0.0361 0.1141  166 SER   A O   
3867 C CB  A SER   A 166 ? 0.1570 0.2229 0.2310 -0.0186 0.0069  0.0162  166 SER   A CB  
3868 C CB  B SER   A 166 ? 0.2372 0.3297 0.4216 -0.0229 -0.0466 0.1020  166 SER   A CB  
3869 O OG  A SER   A 166 ? 0.1686 0.2251 0.2470 -0.0205 0.0058  0.0175  166 SER   A OG  
3870 O OG  B SER   A 166 ? 0.2401 0.3335 0.4440 -0.0173 -0.0602 0.0950  166 SER   A OG  
3881 N N   A SER   A 167 ? 0.1502 0.2162 0.1960 -0.0285 -0.0154 0.0149  167 SER   A N   
3882 N N   B SER   A 167 ? 0.2794 0.3370 0.3586 -0.0484 -0.0244 0.0874  167 SER   A N   
3883 C CA  A SER   A 167 ? 0.1616 0.2114 0.1973 -0.0334 -0.0204 0.0255  167 SER   A CA  
3884 C CA  B SER   A 167 ? 0.3073 0.3419 0.3609 -0.0475 -0.0177 0.0692  167 SER   A CA  
3885 C C   A SER   A 167 ? 0.1590 0.1999 0.1767 -0.0353 -0.0104 0.0359  167 SER   A C   
3886 C C   B SER   A 167 ? 0.3320 0.3503 0.3753 -0.0414 -0.0062 0.0443  167 SER   A C   
3887 O O   A SER   A 167 ? 0.1626 0.2016 0.1780 -0.0276 -0.0179 0.0456  167 SER   A O   
3888 O O   B SER   A 167 ? 0.3403 0.3509 0.3767 -0.0367 -0.0128 0.0297  167 SER   A O   
3889 C CB  A SER   A 167 ? 0.1803 0.2159 0.2177 -0.0289 -0.0152 0.0346  167 SER   A CB  
3890 C CB  B SER   A 167 ? 0.3065 0.3376 0.3518 -0.0532 -0.0132 0.0752  167 SER   A CB  
3891 O OG  A SER   A 167 ? 0.1973 0.2174 0.2329 -0.0275 -0.0133 0.0352  167 SER   A OG  
3892 O OG  B SER   A 167 ? 0.3026 0.3343 0.3502 -0.0574 -0.0031 0.0731  167 SER   A OG  
3903 N N   A PHE   A 168 ? 0.1500 0.1898 0.1671 -0.0329 -0.0163 0.0318  168 PHE   A N   
3904 N N   B PHE   A 168 ? 0.3432 0.3568 0.3915 -0.0385 0.0106  0.0367  168 PHE   A N   
3905 C CA  A PHE   A 168 ? 0.1533 0.1807 0.1651 -0.0320 -0.0116 0.0322  168 PHE   A CA  
3906 C CA  B PHE   A 168 ? 0.3578 0.3671 0.4133 -0.0334 0.0267  0.0259  168 PHE   A CA  
3907 C C   A PHE   A 168 ? 0.1708 0.1862 0.1793 -0.0338 -0.0010 0.0214  168 PHE   A C   
3908 C C   B PHE   A 168 ? 0.3866 0.4001 0.4585 -0.0227 0.0365  0.0024  168 PHE   A C   
3909 O O   A PHE   A 168 ? 0.1697 0.1779 0.1946 -0.0472 0.0140  0.0254  168 PHE   A O   
3910 O O   B PHE   A 168 ? 0.3887 0.4005 0.4697 -0.0255 0.0477  0.0007  168 PHE   A O   
3911 C CB  A PHE   A 168 ? 0.1451 0.1753 0.1581 -0.0291 -0.0225 0.0238  168 PHE   A CB  
3912 C CB  B PHE   A 168 ? 0.3436 0.3470 0.3942 -0.0413 0.0335  0.0431  168 PHE   A CB  
3913 C CG  A PHE   A 168 ? 0.1405 0.1722 0.1466 -0.0270 -0.0244 0.0217  168 PHE   A CG  
3914 C CG  B PHE   A 168 ? 0.3304 0.3270 0.3772 -0.0479 0.0378  0.0602  168 PHE   A CG  
3915 C CD1 A PHE   A 168 ? 0.1402 0.1729 0.1454 -0.0278 -0.0236 0.0300  168 PHE   A CD1 
3916 C CD1 B PHE   A 168 ? 0.3248 0.3198 0.3696 -0.0498 0.0367  0.0653  168 PHE   A CD1 
3917 C CD2 A PHE   A 168 ? 0.1308 0.1678 0.1356 -0.0252 -0.0123 0.0183  168 PHE   A CD2 
3918 C CD2 B PHE   A 168 ? 0.3261 0.3185 0.3711 -0.0525 0.0400  0.0714  168 PHE   A CD2 
3919 C CE1 A PHE   A 168 ? 0.1345 0.1763 0.1381 -0.0281 -0.0140 0.0364  168 PHE   A CE1 
3920 C CE1 B PHE   A 168 ? 0.3222 0.3175 0.3702 -0.0515 0.0328  0.0656  168 PHE   A CE1 
3921 C CE2 A PHE   A 168 ? 0.1312 0.1674 0.1356 -0.0220 -0.0052 0.0313  168 PHE   A CE2 
3922 C CE2 B PHE   A 168 ? 0.3228 0.3137 0.3712 -0.0537 0.0395  0.0718  168 PHE   A CE2 
3923 C CZ  A PHE   A 168 ? 0.1334 0.1738 0.1466 -0.0271 -0.0085 0.0315  168 PHE   A CZ  
3924 C CZ  B PHE   A 168 ? 0.3203 0.3152 0.3699 -0.0536 0.0369  0.0677  168 PHE   A CZ  
3943 N N   A LEU   A 169 ? 0.1901 0.1978 0.1916 -0.0328 -0.0044 0.0076  169 LEU   A N   
3944 N N   B LEU   A 169 ? 0.4110 0.4318 0.4891 -0.0043 0.0346  -0.0195 169 LEU   A N   
3945 C CA  A LEU   A 169 ? 0.2167 0.2187 0.2170 -0.0185 -0.0130 0.0052  169 LEU   A CA  
3946 C CA  B LEU   A 169 ? 0.4334 0.4629 0.5116 0.0127  0.0334  -0.0329 169 LEU   A CA  
3947 C C   A LEU   A 169 ? 0.2199 0.2269 0.2234 -0.0109 -0.0104 0.0124  169 LEU   A C   
3948 C C   B LEU   A 169 ? 0.4435 0.4738 0.5366 0.0205  0.0363  -0.0480 169 LEU   A C   
3949 O O   A LEU   A 169 ? 0.2207 0.2300 0.2141 -0.0100 -0.0083 0.0169  169 LEU   A O   
3950 O O   B LEU   A 169 ? 0.4451 0.4772 0.5478 0.0232  0.0382  -0.0496 169 LEU   A O   
3951 C CB  A LEU   A 169 ? 0.2370 0.2344 0.2422 -0.0120 -0.0202 -0.0029 169 LEU   A CB  
3952 C CB  B LEU   A 169 ? 0.4431 0.4810 0.5096 0.0195  0.0315  -0.0273 169 LEU   A CB  
3953 C CG  A LEU   A 169 ? 0.2534 0.2471 0.2724 -0.0087 -0.0261 -0.0163 169 LEU   A CG  
3954 C CG  B LEU   A 169 ? 0.4506 0.4949 0.5050 0.0244  0.0273  -0.0226 169 LEU   A CG  
3955 C CD1 A LEU   A 169 ? 0.2590 0.2519 0.2826 -0.0092 -0.0326 -0.0201 169 LEU   A CD1 
3956 C CD1 B LEU   A 169 ? 0.4531 0.4996 0.5012 0.0263  0.0262  -0.0210 169 LEU   A CD1 
3957 C CD2 A LEU   A 169 ? 0.2584 0.2522 0.2851 -0.0084 -0.0255 -0.0195 169 LEU   A CD2 
3958 C CD2 B LEU   A 169 ? 0.4533 0.4999 0.5062 0.0265  0.0269  -0.0221 169 LEU   A CD2 
3959 O OXT A LEU   A 169 ? 0.2239 0.2336 0.2350 -0.0057 -0.0069 0.0150  169 LEU   A OXT 
3960 O OXT B LEU   A 169 ? 0.4483 0.4796 0.5478 0.0235  0.0369  -0.0530 169 LEU   A OXT 
3983 N N   A SER   B 1   ? 0.3794 0.3715 0.3877 -0.0683 -0.0507 0.0411  1   SER   B N   
3984 N N   B SER   B 1   ? 0.4102 0.3423 0.3594 -0.1075 -0.0921 0.0207  1   SER   B N   
3985 C CA  A SER   B 1   ? 0.3736 0.3671 0.3859 -0.0701 -0.0476 0.0434  1   SER   B CA  
3986 C CA  B SER   B 1   ? 0.4028 0.3438 0.3633 -0.1081 -0.0905 0.0222  1   SER   B CA  
3987 C C   A SER   B 1   ? 0.3594 0.3589 0.3801 -0.0709 -0.0457 0.0526  1   SER   B C   
3988 C C   B SER   B 1   ? 0.3824 0.3521 0.3661 -0.1006 -0.0838 0.0500  1   SER   B C   
3989 O O   A SER   B 1   ? 0.3641 0.3603 0.3734 -0.0668 -0.0478 0.0499  1   SER   B O   
3990 O O   B SER   B 1   ? 0.3861 0.3519 0.3450 -0.0963 -0.0888 0.0515  1   SER   B O   
3991 C CB  A SER   B 1   ? 0.3794 0.3687 0.3841 -0.0697 -0.0450 0.0382  1   SER   B CB  
3992 C CB  B SER   B 1   ? 0.4139 0.3340 0.3573 -0.1103 -0.0942 -0.0044 1   SER   B CB  
3993 O OG  A SER   B 1   ? 0.3842 0.3722 0.3941 -0.0699 -0.0421 0.0376  1   SER   B OG  
3994 O OG  B SER   B 1   ? 0.4238 0.3348 0.3766 -0.1086 -0.0960 -0.0193 1   SER   B OG  
4009 N N   A MET   B 2   ? 0.3404 0.3474 0.3758 -0.0747 -0.0387 0.0717  2   MET   B N   
4010 N N   B MET   B 2   ? 0.3607 0.3593 0.3767 -0.0917 -0.0693 0.0868  2   MET   B N   
4011 C CA  A MET   B 2   ? 0.3219 0.3353 0.3746 -0.0725 -0.0347 0.0838  2   MET   B CA  
4012 C CA  B MET   B 2   ? 0.3422 0.3663 0.3875 -0.0707 -0.0619 0.1068  2   MET   B CA  
4013 C C   A MET   B 2   ? 0.2820 0.3024 0.3204 -0.0811 -0.0435 0.1086  2   MET   B C   
4014 C C   B MET   B 2   ? 0.3031 0.3437 0.3372 -0.0563 -0.0750 0.1366  2   MET   B C   
4015 O O   A MET   B 2   ? 0.2694 0.2967 0.3028 -0.0903 -0.0501 0.1228  2   MET   B O   
4016 O O   B MET   B 2   ? 0.3017 0.3560 0.3465 -0.0450 -0.0915 0.1300  2   MET   B O   
4017 C CB  A MET   B 2   ? 0.3437 0.3566 0.4280 -0.0569 -0.0234 0.0672  2   MET   B CB  
4018 C CB  B MET   B 2   ? 0.3671 0.3960 0.4514 -0.0544 -0.0458 0.0908  2   MET   B CB  
4019 C CG  A MET   B 2   ? 0.3640 0.3751 0.4737 -0.0417 -0.0134 0.0564  2   MET   B CG  
4020 C CG  B MET   B 2   ? 0.3907 0.4211 0.5030 -0.0382 -0.0325 0.0840  2   MET   B CG  
4021 S SD  A MET   B 2   ? 0.3805 0.3899 0.5195 -0.0297 -0.0070 0.0493  2   MET   B SD  
4022 S SD  B MET   B 2   ? 0.4107 0.4461 0.5529 -0.0245 -0.0296 0.0799  2   MET   B SD  
4023 C CE  A MET   B 2   ? 0.3837 0.3946 0.5251 -0.0276 -0.0036 0.0457  2   MET   B CE  
4024 C CE  B MET   B 2   ? 0.4132 0.4515 0.5603 -0.0232 -0.0262 0.0732  2   MET   B CE  
4043 N N   A VAL   B 3   ? 0.2532 0.2726 0.2872 -0.0868 -0.0471 0.1097  3   VAL   B N   
4044 N N   B VAL   B 3   ? 0.2638 0.3050 0.2938 -0.0653 -0.0716 0.1503  3   VAL   B N   
4045 C CA  A VAL   B 3   ? 0.2344 0.2455 0.2626 -0.0826 -0.0480 0.1048  3   VAL   B CA  
4046 C CA  B VAL   B 3   ? 0.2411 0.2719 0.2774 -0.0625 -0.0657 0.1293  3   VAL   B CA  
4047 C C   A VAL   B 3   ? 0.2143 0.2321 0.2309 -0.0748 -0.0507 0.1072  3   VAL   B C   
4048 C C   B VAL   B 3   ? 0.2172 0.2597 0.2415 -0.0597 -0.0616 0.1089  3   VAL   B C   
4049 O O   A VAL   B 3   ? 0.2094 0.2215 0.2200 -0.0770 -0.0442 0.1188  3   VAL   B O   
4050 O O   B VAL   B 3   ? 0.2171 0.2783 0.2423 -0.0435 -0.0637 0.1012  3   VAL   B O   
4051 C CB  A VAL   B 3   ? 0.2410 0.2409 0.2810 -0.0803 -0.0405 0.0921  3   VAL   B CB  
4052 C CB  B VAL   B 3   ? 0.2538 0.2606 0.3140 -0.0598 -0.0521 0.1209  3   VAL   B CB  
4053 C CG1 A VAL   B 3   ? 0.2433 0.2400 0.2891 -0.0791 -0.0419 0.0827  3   VAL   B CG1 
4054 C CG1 B VAL   B 3   ? 0.2582 0.2579 0.3243 -0.0597 -0.0535 0.1128  3   VAL   B CG1 
4055 C CG2 A VAL   B 3   ? 0.2420 0.2403 0.2862 -0.0788 -0.0342 0.0923  3   VAL   B CG2 
4056 C CG2 B VAL   B 3   ? 0.2556 0.2604 0.3213 -0.0568 -0.0456 0.1259  3   VAL   B CG2 
4075 N N   . ASN   B 4   ? 0.2039 0.2281 0.2195 -0.0649 -0.0565 0.0925  4   ASN   B N   
4076 C CA  . ASN   B 4   ? 0.2021 0.2259 0.1818 -0.0654 -0.0470 0.0563  4   ASN   B CA  
4077 C C   . ASN   B 4   ? 0.2144 0.2404 0.1751 -0.0694 -0.0328 0.0407  4   ASN   B C   
4078 O O   . ASN   B 4   ? 0.2180 0.2477 0.1971 -0.0639 -0.0356 0.0189  4   ASN   B O   
4079 C CB  . ASN   B 4   ? 0.1975 0.2171 0.1760 -0.0585 -0.0534 0.0478  4   ASN   B CB  
4080 C CG  . ASN   B 4   ? 0.1967 0.1993 0.1635 -0.0527 -0.0473 0.0353  4   ASN   B CG  
4081 O OD1 . ASN   B 4   ? 0.1988 0.1834 0.1650 -0.0492 -0.0478 0.0339  4   ASN   B OD1 
4082 N ND2 . ASN   B 4   ? 0.2081 0.1981 0.1710 -0.0324 -0.0327 0.0303  4   ASN   B ND2 
4090 N N   . SER   B 5   ? 0.2299 0.2587 0.2081 -0.0691 -0.0073 0.0403  5   SER   B N   
4091 C CA  . SER   B 5   ? 0.2486 0.2946 0.2595 -0.0513 0.0256  0.0457  5   SER   B CA  
4092 C C   . SER   B 5   ? 0.2669 0.2951 0.2716 -0.0673 0.0543  0.0393  5   SER   B C   
4093 O O   . SER   B 5   ? 0.2863 0.2990 0.3339 -0.0604 0.0719  0.0316  5   SER   B O   
4094 C CB  . SER   B 5   ? 0.2546 0.3253 0.3101 -0.0385 0.0337  0.0549  5   SER   B CB  
4095 O OG  . SER   B 5   ? 0.2732 0.3396 0.3579 -0.0271 0.0420  0.0585  5   SER   B OG  
4101 N N   . PHE   B 6   ? 0.2801 0.3038 0.2317 -0.0700 0.0593  0.0332  6   PHE   B N   
4102 C CA  . PHE   B 6   ? 0.2862 0.3005 0.1993 -0.0835 0.0535  0.0201  6   PHE   B CA  
4103 C C   . PHE   B 6   ? 0.3394 0.3279 0.2463 -0.0857 0.0742  -0.0098 6   PHE   B C   
4104 O O   . PHE   B 6   ? 0.3506 0.3553 0.2734 -0.0807 0.0538  -0.0252 6   PHE   B O   
4105 C CB  . PHE   B 6   ? 0.2484 0.2773 0.1674 -0.0777 0.0207  0.0151  6   PHE   B CB  
4106 C CG  . PHE   B 6   ? 0.2236 0.2494 0.1645 -0.0726 0.0080  0.0109  6   PHE   B CG  
4107 C CD1 . PHE   B 6   ? 0.2200 0.2215 0.1524 -0.0642 -0.0039 0.0089  6   PHE   B CD1 
4108 C CD2 . PHE   B 6   ? 0.2071 0.2515 0.1624 -0.0563 0.0105  0.0352  6   PHE   B CD2 
4109 C CE1 . PHE   B 6   ? 0.2180 0.1988 0.1618 -0.0559 -0.0105 0.0139  6   PHE   B CE1 
4110 C CE2 . PHE   B 6   ? 0.2039 0.2296 0.1897 -0.0503 0.0104  0.0378  6   PHE   B CE2 
4111 C CZ  . PHE   B 6   ? 0.2039 0.2049 0.1803 -0.0577 -0.0064 0.0171  6   PHE   B CZ  
4121 N N   A SER   B 7   ? 0.3534 0.3222 0.2748 -0.0881 0.0800  -0.0198 7   SER   B N   
4122 N N   B SER   B 7   ? 0.3638 0.3161 0.2522 -0.1010 0.1008  -0.0250 7   SER   B N   
4123 C CA  A SER   B 7   ? 0.3658 0.3196 0.3102 -0.0846 0.0822  -0.0278 7   SER   B CA  
4124 C CA  B SER   B 7   ? 0.3856 0.3156 0.2897 -0.0999 0.1182  -0.0355 7   SER   B CA  
4125 C C   A SER   B 7   ? 0.3652 0.3082 0.3029 -0.0880 0.0858  -0.0322 7   SER   B C   
4126 C C   B SER   B 7   ? 0.3823 0.3043 0.2710 -0.1096 0.1299  -0.0416 7   SER   B C   
4127 O O   A SER   B 7   ? 0.3678 0.3100 0.3124 -0.0870 0.0839  -0.0301 7   SER   B O   
4128 O O   B SER   B 7   ? 0.3889 0.3074 0.2948 -0.1075 0.1257  -0.0394 7   SER   B O   
4129 C CB  A SER   B 7   ? 0.3742 0.3264 0.3441 -0.0794 0.0827  -0.0302 7   SER   B CB  
4130 C CB  B SER   B 7   ? 0.4007 0.3250 0.3374 -0.0908 0.1258  -0.0388 7   SER   B CB  
4131 O OG  A SER   B 7   ? 0.3798 0.3322 0.3699 -0.0775 0.0802  -0.0306 7   SER   B OG  
4132 O OG  B SER   B 7   ? 0.4124 0.3377 0.3774 -0.0860 0.1202  -0.0370 7   SER   B OG  
4143 N N   A GLY   B 8   ? 0.3643 0.2952 0.2974 -0.0876 0.0897  -0.0386 8   GLY   B N   
4144 N N   B GLY   B 8   ? 0.3805 0.2945 0.2745 -0.1048 0.1305  -0.0501 8   GLY   B N   
4145 C CA  A GLY   B 8   ? 0.3595 0.2798 0.2894 -0.0879 0.0972  -0.0439 8   GLY   B CA  
4146 C CA  B GLY   B 8   ? 0.3698 0.2793 0.2771 -0.1016 0.1351  -0.0520 8   GLY   B CA  
4147 C C   A GLY   B 8   ? 0.3520 0.2613 0.2755 -0.0879 0.1067  -0.0498 8   GLY   B C   
4148 C C   B GLY   B 8   ? 0.3550 0.2605 0.2696 -0.0958 0.1357  -0.0542 8   GLY   B C   
4149 O O   A GLY   B 8   ? 0.3567 0.2651 0.2893 -0.0841 0.1070  -0.0524 8   GLY   B O   
4150 O O   B GLY   B 8   ? 0.3636 0.2694 0.2915 -0.0843 0.1387  -0.0669 8   GLY   B O   
4157 N N   . TYR   B 9   ? 0.3431 0.2416 0.2496 -0.0883 0.1086  -0.0623 9   TYR   B N   
4158 C CA  . TYR   B 9   ? 0.3224 0.2056 0.2102 -0.0722 0.0840  -0.0493 9   TYR   B CA  
4159 C C   . TYR   B 9   ? 0.3170 0.2098 0.1924 -0.0642 0.0507  -0.0337 9   TYR   B C   
4160 O O   . TYR   B 9   ? 0.3344 0.2335 0.2237 -0.0657 0.0491  -0.0173 9   TYR   B O   
4161 C CB  . TYR   B 9   ? 0.3166 0.1854 0.2168 -0.0577 0.0842  -0.0361 9   TYR   B CB  
4162 C CG  . TYR   B 9   ? 0.3044 0.1692 0.2228 -0.0629 0.0776  -0.0395 9   TYR   B CG  
4163 C CD1 . TYR   B 9   ? 0.3074 0.1685 0.2403 -0.0760 0.0791  -0.0340 9   TYR   B CD1 
4164 C CD2 . TYR   B 9   ? 0.2858 0.1635 0.2190 -0.0663 0.0699  -0.0428 9   TYR   B CD2 
4165 C CE1 . TYR   B 9   ? 0.3020 0.1806 0.2438 -0.0848 0.0736  -0.0492 9   TYR   B CE1 
4166 C CE2 . TYR   B 9   ? 0.2877 0.1672 0.2382 -0.0641 0.0680  -0.0440 9   TYR   B CE2 
4167 C CZ  . TYR   B 9   ? 0.2921 0.1843 0.2442 -0.0779 0.0714  -0.0578 9   TYR   B CZ  
4168 O OH  . TYR   B 9   ? 0.2916 0.1970 0.2641 -0.0843 0.0659  -0.0682 9   TYR   B OH  
4179 N N   . LEU   B 10  ? 0.2921 0.1867 0.1765 -0.0630 0.0213  -0.0315 10  LEU   B N   
4180 C CA  . LEU   B 10  ? 0.2895 0.1870 0.1690 -0.0661 -0.0107 -0.0300 10  LEU   B CA  
4181 C C   . LEU   B 10  ? 0.2731 0.1876 0.1631 -0.0619 -0.0343 -0.0282 10  LEU   B C   
4182 O O   . LEU   B 10  ? 0.2571 0.1871 0.1685 -0.0546 -0.0286 -0.0167 10  LEU   B O   
4183 C CB  . LEU   B 10  ? 0.3025 0.1845 0.1872 -0.0718 -0.0315 -0.0126 10  LEU   B CB  
4184 C CG  . LEU   B 10  ? 0.3151 0.1939 0.2258 -0.0661 -0.0612 0.0010  10  LEU   B CG  
4185 C CD1 . LEU   B 10  ? 0.3265 0.2100 0.2536 -0.0632 -0.0609 -0.0010 10  LEU   B CD1 
4186 C CD2 . LEU   B 10  ? 0.3201 0.1968 0.2554 -0.0671 -0.0603 0.0189  10  LEU   B CD2 
4198 N N   . LYS   B 11  ? 0.2854 0.2131 0.1681 -0.0557 -0.0368 -0.0265 11  LYS   B N   
4199 C CA  . LYS   B 11  ? 0.3026 0.2437 0.2041 -0.0479 -0.0444 -0.0305 11  LYS   B CA  
4200 C C   . LYS   B 11  ? 0.2827 0.2236 0.2121 -0.0765 -0.0375 -0.0406 11  LYS   B C   
4201 O O   . LYS   B 11  ? 0.3025 0.2441 0.2487 -0.0935 -0.0314 -0.0687 11  LYS   B O   
4202 C CB  . LYS   B 11  ? 0.3396 0.2974 0.2891 -0.0243 -0.0529 -0.0280 11  LYS   B CB  
4203 C CG  . LYS   B 11  ? 0.3755 0.3347 0.3793 -0.0119 -0.0516 -0.0342 11  LYS   B CG  
4204 C CD  . LYS   B 11  ? 0.4051 0.3626 0.4570 -0.0043 -0.0478 -0.0378 11  LYS   B CD  
4205 C CE  . LYS   B 11  ? 0.4273 0.3800 0.5133 -0.0030 -0.0444 -0.0415 11  LYS   B CE  
4206 N NZ  . LYS   B 11  ? 0.4356 0.3876 0.5448 -0.0028 -0.0441 -0.0425 11  LYS   B NZ  
4220 N N   . LEU   B 12  ? 0.2448 0.1961 0.2106 -0.0684 -0.0389 -0.0343 12  LEU   B N   
4221 C CA  . LEU   B 12  ? 0.2259 0.1800 0.2259 -0.0566 -0.0364 -0.0240 12  LEU   B CA  
4222 C C   . LEU   B 12  ? 0.2146 0.1791 0.2423 -0.0529 -0.0520 -0.0191 12  LEU   B C   
4223 O O   . LEU   B 12  ? 0.2180 0.1800 0.2731 -0.0644 -0.0644 -0.0111 12  LEU   B O   
4224 C CB  . LEU   B 12  ? 0.2260 0.1657 0.2119 -0.0452 -0.0253 -0.0241 12  LEU   B CB  
4225 C CG  . LEU   B 12  ? 0.2237 0.1584 0.2175 -0.0436 -0.0126 -0.0185 12  LEU   B CG  
4226 C CD1 . LEU   B 12  ? 0.2327 0.1597 0.2083 -0.0306 -0.0101 -0.0111 12  LEU   B CD1 
4227 C CD2 . LEU   B 12  ? 0.2254 0.1610 0.2406 -0.0434 -0.0149 -0.0253 12  LEU   B CD2 
4239 N N   . THR   B 13  ? 0.2055 0.1810 0.2391 -0.0493 -0.0508 -0.0334 13  THR   B N   
4240 C CA  . THR   B 13  ? 0.2125 0.1890 0.2198 -0.0538 -0.0602 -0.0205 13  THR   B CA  
4241 C C   . THR   B 13  ? 0.2503 0.2106 0.2425 -0.0637 -0.0763 -0.0114 13  THR   B C   
4242 O O   . THR   B 13  ? 0.2634 0.2097 0.2671 -0.0623 -0.0397 -0.0154 13  THR   B O   
4243 C CB  . THR   B 13  ? 0.1971 0.1884 0.2233 -0.0436 -0.0507 -0.0161 13  THR   B CB  
4244 O OG1 . THR   B 13  ? 0.1879 0.1818 0.2345 -0.0422 -0.0375 -0.0138 13  THR   B OG1 
4245 C CG2 . THR   B 13  ? 0.2061 0.1951 0.2393 -0.0408 -0.0371 -0.0191 13  THR   B CG2 
4253 N N   A ASP   B 14  ? 0.2603 0.2180 0.2618 -0.0652 -0.0849 -0.0022 14  ASP   B N   
4254 N N   B ASP   B 14  ? 0.2671 0.2248 0.2537 -0.0666 -0.0999 0.0038  14  ASP   B N   
4255 C CA  A ASP   B 14  ? 0.2675 0.2273 0.2856 -0.0652 -0.0863 0.0062  14  ASP   B CA  
4256 C CA  B ASP   B 14  ? 0.2783 0.2417 0.2788 -0.0653 -0.1095 0.0207  14  ASP   B CA  
4257 C C   A ASP   B 14  ? 0.2566 0.2144 0.2522 -0.0660 -0.0791 0.0138  14  ASP   B C   
4258 C C   B ASP   B 14  ? 0.2678 0.2258 0.2510 -0.0702 -0.0891 0.0219  14  ASP   B C   
4259 O O   A ASP   B 14  ? 0.2713 0.2232 0.2572 -0.0683 -0.0719 0.0183  14  ASP   B O   
4260 O O   B ASP   B 14  ? 0.2949 0.2424 0.2623 -0.0712 -0.0817 0.0300  14  ASP   B O   
4261 C CB  A ASP   B 14  ? 0.2848 0.2503 0.3476 -0.0623 -0.0870 0.0051  14  ASP   B CB  
4262 C CB  B ASP   B 14  ? 0.3000 0.2764 0.3564 -0.0531 -0.1189 0.0274  14  ASP   B CB  
4263 C CG  A ASP   B 14  ? 0.2998 0.2672 0.4010 -0.0617 -0.0820 -0.0006 14  ASP   B CG  
4264 C CG  B ASP   B 14  ? 0.3224 0.3090 0.4322 -0.0469 -0.1082 0.0192  14  ASP   B CG  
4265 O OD1 A ASP   B 14  ? 0.3059 0.2712 0.4158 -0.0662 -0.0808 -0.0045 14  ASP   B OD1 
4266 O OD1 B ASP   B 14  ? 0.3331 0.3212 0.4503 -0.0449 -0.1008 0.0170  14  ASP   B OD1 
4267 O OD2 A ASP   B 14  ? 0.3044 0.2739 0.4236 -0.0609 -0.0784 0.0005  14  ASP   B OD2 
4268 O OD2 B ASP   B 14  ? 0.3310 0.3227 0.4688 -0.0477 -0.0994 0.0159  14  ASP   B OD2 
4277 N N   . ASN   B 15  ? 0.2316 0.1937 0.2199 -0.0579 -0.0830 0.0155  15  ASN   B N   
4278 C CA  . ASN   B 15  ? 0.1921 0.1656 0.1976 -0.0356 -0.0513 0.0062  15  ASN   B CA  
4279 C C   . ASN   B 15  ? 0.1698 0.1498 0.1960 -0.0277 -0.0370 0.0002  15  ASN   B C   
4280 O O   . ASN   B 15  ? 0.1702 0.1467 0.2183 -0.0269 -0.0481 -0.0075 15  ASN   B O   
4281 C CB  . ASN   B 15  ? 0.1824 0.1567 0.2164 -0.0152 -0.0489 0.0020  15  ASN   B CB  
4282 C CG  . ASN   B 15  ? 0.1690 0.1563 0.2342 -0.0178 -0.0274 0.0077  15  ASN   B CG  
4283 O OD1 . ASN   B 15  ? 0.1733 0.1917 0.2675 -0.0362 -0.0326 0.0139  15  ASN   B OD1 
4284 N ND2 . ASN   B 15  ? 0.1702 0.1398 0.2236 -0.0102 -0.0061 -0.0066 15  ASN   B ND2 
4292 N N   . VAL   B 16  ? 0.1755 0.1440 0.1950 -0.0326 -0.0493 -0.0008 16  VAL   B N   
4293 C CA  . VAL   B 16  ? 0.1695 0.1464 0.1806 -0.0252 -0.0354 -0.0144 16  VAL   B CA  
4294 C C   . VAL   B 16  ? 0.1674 0.1527 0.1817 -0.0327 -0.0354 -0.0077 16  VAL   B C   
4295 O O   . VAL   B 16  ? 0.1756 0.1665 0.2036 -0.0281 -0.0327 -0.0261 16  VAL   B O   
4296 C CB  . VAL   B 16  ? 0.1785 0.1442 0.1981 -0.0104 -0.0235 -0.0168 16  VAL   B CB  
4297 C CG1 . VAL   B 16  ? 0.1853 0.1407 0.1992 0.0013  -0.0250 -0.0067 16  VAL   B CG1 
4298 C CG2 . VAL   B 16  ? 0.1771 0.1458 0.2120 -0.0020 -0.0194 -0.0214 16  VAL   B CG2 
4308 N N   . TYR   B 17  ? 0.1769 0.1553 0.1823 -0.0291 -0.0326 -0.0137 17  TYR   B N   
4309 C CA  . TYR   B 17  ? 0.1831 0.1706 0.1736 -0.0354 -0.0345 0.0033  17  TYR   B CA  
4310 C C   . TYR   B 17  ? 0.1767 0.1519 0.1720 -0.0384 -0.0208 -0.0065 17  TYR   B C   
4311 O O   . TYR   B 17  ? 0.1725 0.1536 0.1711 -0.0286 -0.0246 -0.0292 17  TYR   B O   
4312 C CB  . TYR   B 17  ? 0.2174 0.2226 0.2120 -0.0162 -0.0340 0.0397  17  TYR   B CB  
4313 C CG  . TYR   B 17  ? 0.2488 0.2789 0.2617 -0.0085 -0.0495 0.0558  17  TYR   B CG  
4314 C CD1 . TYR   B 17  ? 0.2707 0.2974 0.2862 -0.0073 -0.0637 0.0684  17  TYR   B CD1 
4315 C CD2 . TYR   B 17  ? 0.2731 0.3100 0.2905 -0.0023 -0.0646 0.0560  17  TYR   B CD2 
4316 C CE1 . TYR   B 17  ? 0.2916 0.3273 0.3057 0.0027  -0.0725 0.0691  17  TYR   B CE1 
4317 C CE2 . TYR   B 17  ? 0.2930 0.3351 0.3154 0.0111  -0.0778 0.0653  17  TYR   B CE2 
4318 C CZ  . TYR   B 17  ? 0.3032 0.3541 0.3201 0.0174  -0.0848 0.0768  17  TYR   B CZ  
4319 O OH  . TYR   B 17  ? 0.3235 0.3676 0.3430 0.0297  -0.0849 0.0790  17  TYR   B OH  
4329 N N   . ILE   B 18  ? 0.1898 0.1490 0.1675 -0.0329 -0.0137 -0.0157 18  ILE   B N   
4330 C CA  . ILE   B 18  ? 0.1916 0.1451 0.1654 -0.0353 -0.0113 -0.0139 18  ILE   B CA  
4331 C C   . ILE   B 18  ? 0.2055 0.1466 0.1543 -0.0429 -0.0053 -0.0292 18  ILE   B C   
4332 O O   . ILE   B 18  ? 0.2256 0.1638 0.1672 -0.0422 0.0022  -0.0288 18  ILE   B O   
4333 C CB  . ILE   B 18  ? 0.1944 0.1432 0.1793 -0.0442 -0.0148 -0.0185 18  ILE   B CB  
4334 C CG1 . ILE   B 18  ? 0.1999 0.1465 0.1844 -0.0366 -0.0130 -0.0078 18  ILE   B CG1 
4335 C CG2 . ILE   B 18  ? 0.2026 0.1544 0.1835 -0.0451 -0.0150 -0.0103 18  ILE   B CG2 
4336 C CD1 . ILE   B 18  ? 0.2153 0.1795 0.2118 -0.0367 -0.0302 0.0256  18  ILE   B CD1 
4348 N N   . LYS   B 19  ? 0.2018 0.1520 0.1778 -0.0274 0.0197  -0.0420 19  LYS   B N   
4349 C CA  . LYS   B 19  ? 0.2061 0.1638 0.1878 -0.0314 0.0261  -0.0439 19  LYS   B CA  
4350 C C   . LYS   B 19  ? 0.1912 0.1554 0.1999 -0.0253 0.0254  -0.0482 19  LYS   B C   
4351 O O   . LYS   B 19  ? 0.1847 0.1561 0.1918 -0.0161 0.0169  -0.0378 19  LYS   B O   
4352 C CB  . LYS   B 19  ? 0.2303 0.1843 0.2056 -0.0358 0.0399  -0.0341 19  LYS   B CB  
4353 C CG  . LYS   B 19  ? 0.2539 0.2069 0.2145 -0.0422 0.0590  -0.0296 19  LYS   B CG  
4354 C CD  . LYS   B 19  ? 0.2784 0.2387 0.2236 -0.0497 0.0646  -0.0184 19  LYS   B CD  
4355 C CE  . LYS   B 19  ? 0.2989 0.2666 0.2571 -0.0561 0.0559  -0.0210 19  LYS   B CE  
4356 N NZ  . LYS   B 19  ? 0.3175 0.2849 0.2664 -0.0601 0.0500  -0.0205 19  LYS   B NZ  
4370 N N   . ASN   B 20  ? 0.1869 0.1692 0.2326 -0.0215 0.0315  -0.0598 20  ASN   B N   
4371 C CA  . ASN   B 20  ? 0.1877 0.1814 0.2527 -0.0142 0.0322  -0.0723 20  ASN   B CA  
4372 C C   . ASN   B 20  ? 0.1903 0.1996 0.2451 -0.0205 0.0493  -0.0822 20  ASN   B C   
4373 O O   . ASN   B 20  ? 0.2071 0.2357 0.2693 -0.0290 0.0544  -0.0820 20  ASN   B O   
4374 C CB  . ASN   B 20  ? 0.2110 0.1833 0.2845 0.0081  0.0173  -0.0695 20  ASN   B CB  
4375 C CG  . ASN   B 20  ? 0.2401 0.1863 0.3135 0.0361  0.0205  -0.0809 20  ASN   B CG  
4376 O OD1 . ASN   B 20  ? 0.2656 0.2215 0.3367 0.0493  0.0197  -0.0776 20  ASN   B OD1 
4377 N ND2 . ASN   B 20  ? 0.2370 0.1863 0.3100 0.0338  0.0050  -0.0898 20  ASN   B ND2 
4384 N N   . ALA   B 21  ? 0.1910 0.1849 0.2334 -0.0286 0.0518  -0.0647 21  ALA   B N   
4385 C CA  . ALA   B 21  ? 0.1974 0.1963 0.2516 -0.0306 0.0446  -0.0574 21  ALA   B CA  
4386 C C   . ALA   B 21  ? 0.1929 0.1704 0.2477 -0.0235 0.0399  -0.0493 21  ALA   B C   
4387 O O   . ALA   B 21  ? 0.2042 0.1619 0.2458 -0.0292 0.0265  -0.0419 21  ALA   B O   
4388 C CB  . ALA   B 21  ? 0.2162 0.2266 0.2678 -0.0422 0.0361  -0.0261 21  ALA   B CB  
4394 N N   . ASP   B 22  ? 0.1821 0.1580 0.2466 -0.0198 0.0350  -0.0375 22  ASP   B N   
4395 C CA  . ASP   B 22  ? 0.1777 0.1493 0.2427 -0.0142 0.0264  -0.0285 22  ASP   B CA  
4396 C C   . ASP   B 22  ? 0.1763 0.1470 0.2051 -0.0186 0.0159  -0.0132 22  ASP   B C   
4397 O O   . ASP   B 22  ? 0.1846 0.1487 0.2118 -0.0153 0.0198  -0.0082 22  ASP   B O   
4398 C CB  . ASP   B 22  ? 0.1887 0.1603 0.2826 -0.0106 0.0288  -0.0185 22  ASP   B CB  
4399 C CG  . ASP   B 22  ? 0.1924 0.1777 0.3250 0.0016  0.0087  -0.0180 22  ASP   B CG  
4400 O OD1 . ASP   B 22  ? 0.2068 0.1711 0.3220 0.0112  -0.0120 -0.0143 22  ASP   B OD1 
4401 O OD2 . ASP   B 22  ? 0.2022 0.2083 0.3795 0.0129  -0.0215 -0.0265 22  ASP   B OD2 
4406 N N   . ILE   B 23  ? 0.1818 0.1425 0.1796 -0.0134 0.0048  0.0148  23  ILE   B N   
4407 C CA  . ILE   B 23  ? 0.1708 0.1408 0.1562 -0.0088 0.0019  0.0044  23  ILE   B CA  
4408 C C   . ILE   B 23  ? 0.1652 0.1404 0.1586 -0.0063 -0.0121 0.0058  23  ILE   B C   
4409 O O   . ILE   B 23  ? 0.1595 0.1420 0.1615 -0.0090 -0.0019 0.0047  23  ILE   B O   
4410 C CB  . ILE   B 23  ? 0.1682 0.1457 0.1758 -0.0152 -0.0024 0.0136  23  ILE   B CB  
4411 C CG1 . ILE   B 23  ? 0.1639 0.1562 0.1848 -0.0107 0.0090  0.0214  23  ILE   B CG1 
4412 C CG2 . ILE   B 23  ? 0.1811 0.1670 0.1837 -0.0133 -0.0020 0.0046  23  ILE   B CG2 
4413 C CD1 . ILE   B 23  ? 0.1790 0.1760 0.2011 -0.0065 0.0085  0.0212  23  ILE   B CD1 
4425 N N   . VAL   B 24  ? 0.1657 0.1444 0.1623 -0.0094 -0.0078 0.0035  24  VAL   B N   
4426 C CA  . VAL   B 24  ? 0.1598 0.1526 0.1902 -0.0085 -0.0131 0.0006  24  VAL   B CA  
4427 C C   . VAL   B 24  ? 0.1603 0.1527 0.1968 -0.0185 -0.0053 -0.0005 24  VAL   B C   
4428 O O   . VAL   B 24  ? 0.1635 0.1544 0.2111 -0.0204 -0.0009 0.0118  24  VAL   B O   
4429 C CB  . VAL   B 24  ? 0.1699 0.1629 0.1915 -0.0046 -0.0273 -0.0047 24  VAL   B CB  
4430 C CG1 . VAL   B 24  ? 0.1685 0.1735 0.2198 -0.0116 -0.0256 -0.0017 24  VAL   B CG1 
4431 C CG2 . VAL   B 24  ? 0.1850 0.1909 0.2040 0.0093  -0.0273 -0.0074 24  VAL   B CG2 
4441 N N   . GLU   B 25  ? 0.1846 0.1588 0.2089 -0.0118 0.0019  0.0056  25  GLU   B N   
4442 C CA  . GLU   B 25  ? 0.2001 0.1922 0.2351 -0.0039 0.0130  0.0025  25  GLU   B CA  
4443 C C   . GLU   B 25  ? 0.1897 0.1831 0.1958 -0.0146 0.0152  -0.0019 25  GLU   B C   
4444 O O   . GLU   B 25  ? 0.1960 0.2001 0.1963 -0.0131 0.0235  0.0080  25  GLU   B O   
4445 C CB  . GLU   B 25  ? 0.2542 0.2523 0.3190 0.0210  0.0297  0.0019  25  GLU   B CB  
4446 C CG  . GLU   B 25  ? 0.3016 0.3341 0.4407 0.0311  0.0245  0.0073  25  GLU   B CG  
4447 C CD  . GLU   B 25  ? 0.3494 0.4098 0.5435 0.0328  0.0222  0.0140  25  GLU   B CD  
4448 O OE1 . GLU   B 25  ? 0.3840 0.4321 0.5746 0.0363  0.0229  0.0154  25  GLU   B OE1 
4449 O OE2 . GLU   B 25  ? 0.3820 0.4331 0.5786 0.0322  0.0201  0.0151  25  GLU   B OE2 
4456 N N   . GLU   B 26  ? 0.1919 0.1710 0.1722 -0.0256 0.0144  0.0046  26  GLU   B N   
4457 C CA  . GLU   B 26  ? 0.1905 0.1803 0.1798 -0.0361 -0.0054 0.0091  26  GLU   B CA  
4458 C C   . GLU   B 26  ? 0.1732 0.1803 0.1690 -0.0291 0.0083  0.0143  26  GLU   B C   
4459 O O   . GLU   B 26  ? 0.1894 0.2015 0.1748 -0.0264 0.0020  0.0168  26  GLU   B O   
4460 C CB  . GLU   B 26  ? 0.2226 0.2010 0.1901 -0.0505 0.0013  0.0198  26  GLU   B CB  
4461 C CG  . GLU   B 26  ? 0.2593 0.2387 0.2564 -0.0549 0.0104  0.0027  26  GLU   B CG  
4462 C CD  . GLU   B 26  ? 0.2820 0.2618 0.2726 -0.0707 0.0257  -0.0364 26  GLU   B CD  
4463 O OE1 . GLU   B 26  ? 0.3008 0.2419 0.2769 -0.0801 0.0635  -0.0353 26  GLU   B OE1 
4464 O OE2 . GLU   B 26  ? 0.2859 0.2971 0.3200 -0.0619 0.0305  -0.0246 26  GLU   B OE2 
4471 N N   . ALA   B 27  ? 0.1596 0.1604 0.1751 -0.0288 0.0092  0.0156  27  ALA   B N   
4472 C CA  . ALA   B 27  ? 0.1621 0.1599 0.1908 -0.0215 0.0120  0.0250  27  ALA   B CA  
4473 C C   . ALA   B 27  ? 0.1616 0.1729 0.2075 -0.0152 0.0180  0.0359  27  ALA   B C   
4474 O O   . ALA   B 27  ? 0.1727 0.1813 0.2275 -0.0090 0.0199  0.0493  27  ALA   B O   
4475 C CB  . ALA   B 27  ? 0.1744 0.1499 0.2020 -0.0262 0.0061  0.0102  27  ALA   B CB  
4481 N N   . LYS   B 28  ? 0.1572 0.1883 0.2401 -0.0169 0.0209  0.0513  28  LYS   B N   
4482 C CA  . LYS   B 28  ? 0.1764 0.2278 0.2670 -0.0100 0.0514  0.0713  28  LYS   B CA  
4483 C C   . LYS   B 28  ? 0.1938 0.2415 0.2536 -0.0027 0.0573  0.0665  28  LYS   B C   
4484 O O   . LYS   B 28  ? 0.2145 0.2477 0.2661 -0.0092 0.0604  0.0669  28  LYS   B O   
4485 C CB  . LYS   B 28  ? 0.1985 0.2700 0.3154 -0.0021 0.0703  0.0949  28  LYS   B CB  
4486 C CG  . LYS   B 28  ? 0.2259 0.3174 0.3651 0.0126  0.0775  0.1099  28  LYS   B CG  
4487 C CD  . LYS   B 28  ? 0.2750 0.3750 0.4310 0.0254  0.0911  0.1144  28  LYS   B CD  
4488 C CE  . LYS   B 28  ? 0.3321 0.4281 0.4853 0.0330  0.0910  0.1189  28  LYS   B CE  
4489 N NZ  . LYS   B 28  ? 0.3545 0.4386 0.5087 0.0378  0.0855  0.1231  28  LYS   B NZ  
4503 N N   . LYS   B 29  ? 0.2080 0.2655 0.2572 0.0115  0.0595  0.0533  29  LYS   B N   
4504 C CA  . LYS   B 29  ? 0.2510 0.3034 0.2795 0.0061  0.0581  0.0559  29  LYS   B CA  
4505 C C   . LYS   B 29  ? 0.2432 0.3101 0.2377 0.0041  0.0419  0.0710  29  LYS   B C   
4506 O O   . LYS   B 29  ? 0.2599 0.3323 0.2464 0.0112  0.0441  0.0689  29  LYS   B O   
4507 C CB  . LYS   B 29  ? 0.3078 0.3421 0.3673 0.0036  0.0557  0.0407  29  LYS   B CB  
4508 C CG  . LYS   B 29  ? 0.3556 0.3739 0.4484 -0.0007 0.0625  0.0371  29  LYS   B CG  
4509 C CD  . LYS   B 29  ? 0.3925 0.3970 0.5191 -0.0078 0.0716  0.0316  29  LYS   B CD  
4510 C CE  . LYS   B 29  ? 0.4245 0.4139 0.5695 -0.0135 0.0786  0.0290  29  LYS   B CE  
4511 N NZ  . LYS   B 29  ? 0.4387 0.4208 0.6040 -0.0151 0.0800  0.0276  29  LYS   B NZ  
4525 N N   . VAL   B 30  ? 0.2191 0.2958 0.2357 -0.0089 0.0273  0.0752  30  VAL   B N   
4526 C CA  . VAL   B 30  ? 0.2057 0.2819 0.2755 -0.0205 -0.0003 0.0883  30  VAL   B CA  
4527 C C   . VAL   B 30  ? 0.1889 0.2775 0.2742 -0.0159 0.0104  0.1131  30  VAL   B C   
4528 O O   . VAL   B 30  ? 0.2077 0.2973 0.2714 -0.0089 0.0144  0.1282  30  VAL   B O   
4529 C CB  . VAL   B 30  ? 0.2146 0.2761 0.3208 -0.0324 -0.0268 0.0784  30  VAL   B CB  
4530 C CG1 . VAL   B 30  ? 0.2175 0.2820 0.3300 -0.0324 -0.0189 0.0739  30  VAL   B CG1 
4531 C CG2 . VAL   B 30  ? 0.2293 0.2777 0.3393 -0.0354 -0.0296 0.0680  30  VAL   B CG2 
4541 N N   . LYS   B 31  ? 0.1827 0.2412 0.3060 -0.0281 0.0104  0.1178  31  LYS   B N   
4542 C CA  . LYS   B 31  ? 0.1742 0.2362 0.3488 -0.0361 0.0045  0.1162  31  LYS   B CA  
4543 C C   . LYS   B 31  ? 0.1631 0.2002 0.2908 -0.0338 -0.0221 0.0948  31  LYS   B C   
4544 O O   . LYS   B 31  ? 0.1605 0.2159 0.3091 -0.0247 -0.0181 0.1135  31  LYS   B O   
4545 C CB  . LYS   B 31  ? 0.1937 0.2795 0.4163 -0.0365 0.0431  0.1355  31  LYS   B CB  
4546 C CG  . LYS   B 31  ? 0.2325 0.3279 0.4770 -0.0305 0.0573  0.1378  31  LYS   B CG  
4547 C CD  . LYS   B 31  ? 0.2749 0.3838 0.5216 -0.0248 0.0632  0.1296  31  LYS   B CD  
4548 C CE  . LYS   B 31  ? 0.3223 0.4191 0.5591 -0.0229 0.0602  0.1204  31  LYS   B CE  
4549 N NZ  . LYS   B 31  ? 0.3330 0.4418 0.5761 -0.0157 0.0512  0.1138  31  LYS   B NZ  
4563 N N   . PRO   B 32  ? 0.1734 0.1605 0.2162 -0.0295 -0.0372 0.0531  32  PRO   B N   
4564 C CA  . PRO   B 32  ? 0.1848 0.1534 0.1784 -0.0326 -0.0382 0.0323  32  PRO   B CA  
4565 C C   . PRO   B 32  ? 0.1932 0.1457 0.1779 -0.0385 -0.0537 0.0380  32  PRO   B C   
4566 O O   . PRO   B 32  ? 0.2059 0.1463 0.2129 -0.0375 -0.0775 0.0323  32  PRO   B O   
4567 C CB  . PRO   B 32  ? 0.2047 0.1476 0.1693 -0.0371 -0.0324 0.0168  32  PRO   B CB  
4568 C CG  . PRO   B 32  ? 0.2203 0.1408 0.1764 -0.0277 -0.0477 0.0229  32  PRO   B CG  
4569 C CD  . PRO   B 32  ? 0.2015 0.1413 0.1950 -0.0166 -0.0559 0.0268  32  PRO   B CD  
4577 N N   . THR   B 33  ? 0.1963 0.1395 0.1598 -0.0368 -0.0503 0.0295  33  THR   B N   
4578 C CA  . THR   B 33  ? 0.2055 0.1464 0.1521 -0.0387 -0.0535 0.0261  33  THR   B CA  
4579 C C   . THR   B 33  ? 0.2075 0.1329 0.1532 -0.0350 -0.0536 0.0197  33  THR   B C   
4580 O O   . THR   B 33  ? 0.2278 0.1337 0.1620 -0.0428 -0.0628 0.0170  33  THR   B O   
4581 C CB  . THR   B 33  ? 0.2103 0.1562 0.1649 -0.0230 -0.0518 0.0269  33  THR   B CB  
4582 O OG1 . THR   B 33  ? 0.1996 0.1621 0.1748 -0.0235 -0.0497 0.0355  33  THR   B OG1 
4583 C CG2 . THR   B 33  ? 0.2318 0.1590 0.1894 -0.0134 -0.0453 0.0236  33  THR   B CG2 
4591 N N   . VAL   B 34  ? 0.1922 0.1288 0.1471 -0.0332 -0.0377 0.0143  34  VAL   B N   
4592 C CA  . VAL   B 34  ? 0.1728 0.1294 0.1431 -0.0244 -0.0376 0.0057  34  VAL   B CA  
4593 C C   . VAL   B 34  ? 0.1553 0.1215 0.1278 -0.0239 -0.0212 0.0052  34  VAL   B C   
4594 O O   . VAL   B 34  ? 0.1730 0.1278 0.1296 -0.0289 -0.0317 0.0045  34  VAL   B O   
4595 C CB  . VAL   B 34  ? 0.1699 0.1407 0.1635 -0.0077 -0.0354 0.0013  34  VAL   B CB  
4596 C CG1 . VAL   B 34  ? 0.1702 0.1531 0.1745 -0.0081 -0.0244 -0.0004 34  VAL   B CG1 
4597 C CG2 . VAL   B 34  ? 0.1808 0.1542 0.1981 -0.0086 -0.0377 0.0059  34  VAL   B CG2 
4607 N N   . VAL   B 35  ? 0.1487 0.1211 0.1167 -0.0218 -0.0109 0.0091  35  VAL   B N   
4608 C CA  . VAL   B 35  ? 0.1432 0.1209 0.1137 -0.0182 -0.0067 0.0028  35  VAL   B CA  
4609 C C   . VAL   B 35  ? 0.1318 0.1158 0.1167 -0.0164 -0.0085 0.0066  35  VAL   B C   
4610 O O   . VAL   B 35  ? 0.1394 0.1206 0.1337 -0.0192 -0.0027 -0.0019 35  VAL   B O   
4611 C CB  . VAL   B 35  ? 0.1402 0.1349 0.1276 -0.0167 0.0043  0.0085  35  VAL   B CB  
4612 C CG1 . VAL   B 35  ? 0.1361 0.1434 0.1434 -0.0169 0.0064  0.0097  35  VAL   B CG1 
4613 C CG2 . VAL   B 35  ? 0.1447 0.1377 0.1512 -0.0076 0.0007  0.0063  35  VAL   B CG2 
4623 N N   . VAL   B 36  ? 0.1367 0.1162 0.1192 -0.0163 -0.0113 0.0074  36  VAL   B N   
4624 C CA  . VAL   B 36  ? 0.1298 0.1145 0.1162 -0.0128 -0.0083 0.0047  36  VAL   B CA  
4625 C C   . VAL   B 36  ? 0.1266 0.1162 0.1115 -0.0118 -0.0033 0.0002  36  VAL   B C   
4626 O O   . VAL   B 36  ? 0.1360 0.1248 0.1347 -0.0048 -0.0031 -0.0104 36  VAL   B O   
4627 C CB  . VAL   B 36  ? 0.1321 0.1193 0.1237 -0.0114 -0.0049 0.0043  36  VAL   B CB  
4628 C CG1 . VAL   B 36  ? 0.1298 0.1314 0.1368 -0.0124 -0.0018 0.0031  36  VAL   B CG1 
4629 C CG2 . VAL   B 36  ? 0.1354 0.1285 0.1457 -0.0120 -0.0083 0.0049  36  VAL   B CG2 
4639 N N   . ASN   B 37  ? 0.1272 0.1154 0.1153 0.0008  -0.0044 -0.0026 37  ASN   B N   
4640 C CA  . ASN   B 37  ? 0.1265 0.1161 0.1263 0.0055  -0.0036 0.0040  37  ASN   B CA  
4641 C C   . ASN   B 37  ? 0.1315 0.1231 0.1143 0.0030  -0.0069 0.0000  37  ASN   B C   
4642 O O   . ASN   B 37  ? 0.1366 0.1278 0.1370 0.0023  0.0113  0.0072  37  ASN   B O   
4643 C CB  . ASN   B 37  ? 0.1296 0.1250 0.1309 0.0015  -0.0055 0.0011  37  ASN   B CB  
4644 C CG  . ASN   B 37  ? 0.1325 0.1211 0.1380 -0.0001 -0.0047 0.0047  37  ASN   B CG  
4645 O OD1 . ASN   B 37  ? 0.1405 0.1305 0.1499 0.0078  -0.0104 -0.0012 37  ASN   B OD1 
4646 N ND2 . ASN   B 37  ? 0.1399 0.1203 0.1386 0.0035  -0.0169 0.0037  37  ASN   B ND2 
4653 N N   . ALA   B 38  ? 0.1377 0.1239 0.1220 0.0042  0.0064  0.0047  38  ALA   B N   
4654 C CA  . ALA   B 38  ? 0.1412 0.1228 0.1287 0.0000  0.0052  0.0029  38  ALA   B CA  
4655 C C   . ALA   B 38  ? 0.1414 0.1236 0.1256 0.0001  0.0053  0.0061  38  ALA   B C   
4656 O O   . ALA   B 38  ? 0.1544 0.1359 0.1374 0.0106  0.0004  0.0078  38  ALA   B O   
4657 C CB  . ALA   B 38  ? 0.1661 0.1279 0.1398 -0.0093 0.0137  -0.0010 38  ALA   B CB  
4663 N N   . ALA   B 39  ? 0.1408 0.1233 0.1175 0.0061  0.0023  -0.0017 39  ALA   B N   
4664 C CA  . ALA   B 39  ? 0.1419 0.1342 0.1317 0.0059  0.0016  0.0014  39  ALA   B CA  
4665 C C   . ALA   B 39  ? 0.1489 0.1438 0.1211 0.0104  0.0006  -0.0048 39  ALA   B C   
4666 O O   . ALA   B 39  ? 0.1536 0.1467 0.1435 0.0042  0.0097  0.0058  39  ALA   B O   
4667 C CB  . ALA   B 39  ? 0.1509 0.1276 0.1456 -0.0051 0.0018  0.0002  39  ALA   B CB  
4673 N N   . ASN   B 40  ? 0.1590 0.1665 0.1219 -0.0023 0.0050  -0.0145 40  ASN   B N   
4674 C CA  . ASN   B 40  ? 0.1672 0.1712 0.1343 0.0024  -0.0020 -0.0082 40  ASN   B CA  
4675 C C   . ASN   B 40  ? 0.1698 0.1688 0.1124 0.0074  -0.0063 -0.0029 40  ASN   B C   
4676 O O   . ASN   B 40  ? 0.1657 0.1619 0.1245 0.0094  -0.0041 -0.0011 40  ASN   B O   
4677 C CB  . ASN   B 40  ? 0.1756 0.1643 0.1488 0.0072  -0.0063 0.0074  40  ASN   B CB  
4678 C CG  . ASN   B 40  ? 0.1823 0.1683 0.1822 0.0054  -0.0181 0.0129  40  ASN   B CG  
4679 O OD1 . ASN   B 40  ? 0.1811 0.1645 0.2706 -0.0007 -0.0356 0.0162  40  ASN   B OD1 
4680 N ND2 . ASN   B 40  ? 0.1883 0.1740 0.1870 0.0117  -0.0125 0.0149  40  ASN   B ND2 
4687 N N   . VAL   B 41  ? 0.1827 0.1758 0.1218 0.0135  -0.0007 -0.0016 41  VAL   B N   
4688 C CA  . VAL   B 41  ? 0.1876 0.1826 0.1249 0.0111  0.0010  -0.0196 41  VAL   B CA  
4689 C C   . VAL   B 41  ? 0.1814 0.1854 0.1199 0.0164  -0.0086 -0.0145 41  VAL   B C   
4690 O O   . VAL   B 41  ? 0.1796 0.1787 0.1399 0.0181  -0.0128 -0.0225 41  VAL   B O   
4691 C CB  . VAL   B 41  ? 0.1973 0.1992 0.1556 0.0006  0.0212  -0.0353 41  VAL   B CB  
4692 C CG1 . VAL   B 41  ? 0.1962 0.2057 0.1786 -0.0048 0.0341  -0.0341 41  VAL   B CG1 
4693 C CG2 . VAL   B 41  ? 0.2093 0.2179 0.1593 -0.0101 0.0213  -0.0278 41  VAL   B CG2 
4703 N N   . TYR   B 42  ? 0.1864 0.1890 0.1166 0.0198  -0.0153 -0.0124 42  TYR   B N   
4704 C CA  . TYR   B 42  ? 0.1897 0.1960 0.1344 0.0211  -0.0293 -0.0209 42  TYR   B CA  
4705 C C   . TYR   B 42  ? 0.1747 0.1768 0.1373 0.0209  -0.0203 -0.0214 42  TYR   B C   
4706 O O   . TYR   B 42  ? 0.1787 0.1834 0.1734 0.0175  -0.0288 -0.0275 42  TYR   B O   
4707 C CB  . TYR   B 42  ? 0.2132 0.2259 0.1515 0.0105  -0.0283 -0.0043 42  TYR   B CB  
4708 C CG  . TYR   B 42  ? 0.2217 0.2509 0.1508 -0.0050 -0.0182 0.0009  42  TYR   B CG  
4709 C CD1 . TYR   B 42  ? 0.2222 0.2550 0.1182 -0.0082 -0.0083 0.0042  42  TYR   B CD1 
4710 C CD2 . TYR   B 42  ? 0.2417 0.2631 0.1893 -0.0095 0.0021  0.0055  42  TYR   B CD2 
4711 C CE1 . TYR   B 42  ? 0.2396 0.2694 0.1274 -0.0055 -0.0027 0.0068  42  TYR   B CE1 
4712 C CE2 . TYR   B 42  ? 0.2518 0.2728 0.1804 -0.0078 0.0253  0.0217  42  TYR   B CE2 
4713 C CZ  . TYR   B 42  ? 0.2630 0.2892 0.1633 0.0019  0.0213  0.0112  42  TYR   B CZ  
4714 O OH  . TYR   B 42  ? 0.2986 0.3197 0.2061 0.0183  0.0367  0.0113  42  TYR   B OH  
4724 N N   . LEU   B 43  ? 0.1687 0.1578 0.1310 0.0104  -0.0089 -0.0193 43  LEU   B N   
4725 C CA  . LEU   B 43  ? 0.1609 0.1552 0.1266 0.0081  -0.0089 -0.0130 43  LEU   B CA  
4726 C C   . LEU   B 43  ? 0.1634 0.1613 0.1274 0.0108  -0.0142 -0.0016 43  LEU   B C   
4727 O O   . LEU   B 43  ? 0.1605 0.1650 0.1674 0.0093  -0.0144 0.0088  43  LEU   B O   
4728 C CB  . LEU   B 43  ? 0.1551 0.1434 0.1458 0.0019  -0.0251 -0.0114 43  LEU   B CB  
4729 C CG  . LEU   B 43  ? 0.1629 0.1424 0.1529 0.0021  -0.0248 -0.0095 43  LEU   B CG  
4730 C CD1 . LEU   B 43  ? 0.1759 0.1426 0.1857 -0.0017 -0.0410 -0.0082 43  LEU   B CD1 
4731 C CD2 . LEU   B 43  ? 0.1631 0.1420 0.1541 -0.0018 -0.0198 -0.0035 43  LEU   B CD2 
4743 N N   . LYS   B 44  ? 0.1599 0.1591 0.1306 0.0111  -0.0091 -0.0035 44  LYS   B N   
4744 C CA  . LYS   B 44  ? 0.1769 0.1663 0.1351 0.0085  -0.0103 0.0064  44  LYS   B CA  
4745 C C   . LYS   B 44  ? 0.1705 0.1581 0.1321 0.0096  -0.0103 -0.0012 44  LYS   B C   
4746 O O   . LYS   B 44  ? 0.1859 0.1567 0.1682 0.0019  -0.0006 0.0006  44  LYS   B O   
4747 C CB  . LYS   B 44  ? 0.2121 0.1894 0.1492 0.0094  -0.0199 0.0022  44  LYS   B CB  
4748 C CG  . LYS   B 44  ? 0.2519 0.2159 0.1892 0.0027  -0.0449 0.0081  44  LYS   B CG  
4749 C CD  . LYS   B 44  ? 0.2802 0.2369 0.2454 -0.0088 -0.0636 0.0076  44  LYS   B CD  
4750 C CE  . LYS   B 44  ? 0.3060 0.2601 0.2908 -0.0156 -0.0750 0.0142  44  LYS   B CE  
4751 N NZ  . LYS   B 44  ? 0.3181 0.2701 0.3181 -0.0124 -0.0878 0.0248  44  LYS   B NZ  
4765 N N   . HIS   B 45  ? 0.1566 0.1584 0.1340 0.0064  -0.0114 0.0037  45  HIS   B N   
4766 C CA  . HIS   B 45  ? 0.1611 0.1614 0.1339 0.0059  -0.0114 0.0051  45  HIS   B CA  
4767 C C   . HIS   B 45  ? 0.1878 0.1777 0.1693 0.0192  -0.0215 0.0040  45  HIS   B C   
4768 O O   . HIS   B 45  ? 0.1980 0.2063 0.2235 0.0466  0.0053  0.0059  45  HIS   B O   
4769 C CB  . HIS   B 45  ? 0.1563 0.1628 0.1325 -0.0023 0.0001  -0.0036 45  HIS   B CB  
4770 C CG  . HIS   B 45  ? 0.1563 0.1511 0.1360 -0.0043 -0.0062 0.0019  45  HIS   B CG  
4771 N ND1 . HIS   B 45  ? 0.1556 0.1474 0.1476 -0.0004 -0.0076 -0.0047 45  HIS   B ND1 
4772 C CD2 . HIS   B 45  ? 0.1697 0.1516 0.1486 -0.0084 -0.0160 0.0042  45  HIS   B CD2 
4773 C CE1 . HIS   B 45  ? 0.1717 0.1422 0.1399 -0.0014 -0.0194 -0.0067 45  HIS   B CE1 
4774 N NE2 . HIS   B 45  ? 0.1794 0.1446 0.1487 -0.0013 -0.0163 -0.0033 45  HIS   B NE2 
4782 N N   A GLY   B 46  ? 0.1985 0.1835 0.1964 0.0157  -0.0291 0.0070  46  GLY   B N   
4783 N N   B GLY   B 46  ? 0.2040 0.1796 0.1954 0.0188  -0.0378 0.0224  46  GLY   B N   
4784 C CA  A GLY   B 46  ? 0.2060 0.1927 0.2270 0.0094  -0.0328 0.0034  46  GLY   B CA  
4785 C CA  B GLY   B 46  ? 0.2111 0.1903 0.2284 0.0108  -0.0476 0.0169  46  GLY   B CA  
4786 C C   A GLY   B 46  ? 0.2087 0.2031 0.2611 0.0119  -0.0311 -0.0006 46  GLY   B C   
4787 C C   B GLY   B 46  ? 0.2096 0.2060 0.2715 0.0203  -0.0451 0.0111  46  GLY   B C   
4788 O O   A GLY   B 46  ? 0.2169 0.2114 0.3071 0.0144  -0.0174 -0.0118 46  GLY   B O   
4789 O O   B GLY   B 46  ? 0.2262 0.2238 0.3418 0.0208  -0.0240 -0.0021 46  GLY   B O   
4796 N N   . GLY   B 47  ? 0.2108 0.2092 0.2556 0.0043  -0.0289 -0.0042 47  GLY   B N   
4797 C CA  . GLY   B 47  ? 0.2032 0.1804 0.2187 -0.0014 -0.0228 -0.0054 47  GLY   B CA  
4798 C C   . GLY   B 47  ? 0.1799 0.1502 0.1789 0.0002  -0.0109 0.0060  47  GLY   B C   
4799 O O   . GLY   B 47  ? 0.1907 0.1399 0.1862 0.0034  -0.0081 0.0074  47  GLY   B O   
4804 N N   . GLY   B 48  ? 0.1530 0.1411 0.1728 0.0063  -0.0125 0.0117  48  GLY   B N   
4805 C CA  . GLY   B 48  ? 0.1524 0.1426 0.1671 0.0001  -0.0076 0.0132  48  GLY   B CA  
4806 C C   . GLY   B 48  ? 0.1472 0.1362 0.1527 0.0057  -0.0001 0.0064  48  GLY   B C   
4807 O O   . GLY   B 48  ? 0.1452 0.1410 0.1838 0.0064  -0.0049 0.0056  48  GLY   B O   
4811 N N   . VAL   B 49  ? 0.1508 0.1385 0.1458 0.0073  0.0006  0.0075  49  VAL   B N   
4812 C CA  . VAL   B 49  ? 0.1575 0.1471 0.1407 0.0108  -0.0090 -0.0092 49  VAL   B CA  
4813 C C   . VAL   B 49  ? 0.1484 0.1382 0.1277 0.0123  0.0008  0.0074  49  VAL   B C   
4814 O O   . VAL   B 49  ? 0.1510 0.1426 0.1456 0.0042  -0.0006 0.0105  49  VAL   B O   
4815 C CB  . VAL   B 49  ? 0.1592 0.1644 0.1629 0.0052  -0.0220 -0.0043 49  VAL   B CB  
4816 C CG1 . VAL   B 49  ? 0.1590 0.1756 0.1637 0.0097  -0.0276 0.0111  49  VAL   B CG1 
4817 C CG2 . VAL   B 49  ? 0.1774 0.1769 0.1906 -0.0046 -0.0398 -0.0013 49  VAL   B CG2 
4827 N N   . ALA   B 50  ? 0.1429 0.1355 0.1353 0.0050  0.0005  0.0097  50  ALA   B N   
4828 C CA  . ALA   B 50  ? 0.1400 0.1320 0.1436 0.0102  0.0009  0.0092  50  ALA   B CA  
4829 C C   . ALA   B 50  ? 0.1475 0.1371 0.1365 0.0105  0.0055  0.0056  50  ALA   B C   
4830 O O   . ALA   B 50  ? 0.1436 0.1339 0.1387 0.0024  0.0021  0.0065  50  ALA   B O   
4831 C CB  . ALA   B 50  ? 0.1431 0.1320 0.1460 0.0022  0.0040  0.0098  50  ALA   B CB  
4837 N N   . GLY   B 51  ? 0.1469 0.1407 0.1438 0.0123  -0.0028 0.0115  51  GLY   B N   
4838 C CA  . GLY   B 51  ? 0.1481 0.1493 0.1702 0.0195  -0.0094 0.0061  51  GLY   B CA  
4839 C C   . GLY   B 51  ? 0.1445 0.1449 0.1712 0.0247  -0.0062 0.0103  51  GLY   B C   
4840 O O   . GLY   B 51  ? 0.1497 0.1554 0.1879 0.0109  -0.0085 0.0029  51  GLY   B O   
4844 N N   . ALA   B 52  ? 0.1400 0.1471 0.1599 0.0172  -0.0025 0.0117  52  ALA   B N   
4845 C CA  . ALA   B 52  ? 0.1493 0.1477 0.1608 0.0133  0.0072  0.0074  52  ALA   B CA  
4846 C C   . ALA   B 52  ? 0.1431 0.1461 0.1533 0.0079  0.0038  0.0049  52  ALA   B C   
4847 O O   . ALA   B 52  ? 0.1421 0.1494 0.1650 0.0097  0.0064  0.0065  52  ALA   B O   
4848 C CB  . ALA   B 52  ? 0.1607 0.1534 0.1679 0.0073  0.0064  0.0004  52  ALA   B CB  
4854 N N   . LEU   B 53  ? 0.1346 0.1410 0.1417 0.0135  0.0062  0.0094  53  LEU   B N   
4855 C CA  . LEU   B 53  ? 0.1392 0.1509 0.1395 0.0130  -0.0006 0.0068  53  LEU   B CA  
4856 C C   . LEU   B 53  ? 0.1398 0.1473 0.1355 0.0099  0.0109  0.0043  53  LEU   B C   
4857 O O   . LEU   B 53  ? 0.1507 0.1559 0.1433 0.0025  0.0099  0.0136  53  LEU   B O   
4858 C CB  . LEU   B 53  ? 0.1409 0.1573 0.1446 0.0133  -0.0072 0.0133  53  LEU   B CB  
4859 C CG  . LEU   B 53  ? 0.1395 0.1677 0.1474 -0.0006 -0.0021 0.0220  53  LEU   B CG  
4860 C CD1 . LEU   B 53  ? 0.1509 0.1884 0.1603 0.0098  -0.0053 0.0092  53  LEU   B CD1 
4861 C CD2 . LEU   B 53  ? 0.1509 0.1941 0.1739 -0.0079 0.0002  -0.0096 53  LEU   B CD2 
4873 N N   . ASN   B 54  ? 0.1391 0.1375 0.1391 0.0047  0.0005  0.0073  54  ASN   B N   
4874 C CA  . ASN   B 54  ? 0.1390 0.1502 0.1504 0.0065  -0.0044 0.0064  54  ASN   B CA  
4875 C C   . ASN   B 54  ? 0.1458 0.1532 0.1636 0.0065  0.0015  0.0038  54  ASN   B C   
4876 O O   . ASN   B 54  ? 0.1402 0.1585 0.1700 -0.0024 0.0030  0.0028  54  ASN   B O   
4877 C CB  . ASN   B 54  ? 0.1461 0.1613 0.1571 0.0061  -0.0042 0.0001  54  ASN   B CB  
4878 C CG  . ASN   B 54  ? 0.1465 0.1721 0.1539 0.0039  -0.0120 0.0031  54  ASN   B CG  
4879 O OD1 . ASN   B 54  ? 0.1420 0.1695 0.1637 -0.0014 -0.0042 -0.0139 54  ASN   B OD1 
4880 N ND2 . ASN   B 54  ? 0.1590 0.1916 0.1805 -0.0027 -0.0231 0.0166  54  ASN   B ND2 
4887 N N   . LYS   B 55  ? 0.1445 0.1521 0.1882 0.0121  -0.0017 0.0087  55  LYS   B N   
4888 C CA  . LYS   B 55  ? 0.1464 0.1650 0.2019 0.0202  -0.0035 0.0065  55  LYS   B CA  
4889 C C   . LYS   B 55  ? 0.1414 0.1624 0.1994 0.0140  0.0065  -0.0028 55  LYS   B C   
4890 O O   . LYS   B 55  ? 0.1352 0.1812 0.2101 0.0147  0.0044  -0.0008 55  LYS   B O   
4891 C CB  . LYS   B 55  ? 0.1637 0.1846 0.2298 0.0338  0.0081  0.0178  55  LYS   B CB  
4892 C CG  . LYS   B 55  ? 0.2063 0.2134 0.3069 0.0463  0.0281  0.0349  55  LYS   B CG  
4893 C CD  . LYS   B 55  ? 0.2350 0.2376 0.3762 0.0547  0.0448  0.0474  55  LYS   B CD  
4894 C CE  . LYS   B 55  ? 0.2559 0.2594 0.4379 0.0600  0.0544  0.0512  55  LYS   B CE  
4895 N NZ  . LYS   B 55  ? 0.2547 0.2775 0.4751 0.0647  0.0355  0.0588  55  LYS   B NZ  
4909 N N   . ALA   B 56  ? 0.1413 0.1679 0.1774 0.0120  0.0093  -0.0023 56  ALA   B N   
4910 C CA  . ALA   B 56  ? 0.1532 0.1866 0.1699 0.0049  0.0109  0.0015  56  ALA   B CA  
4911 C C   . ALA   B 56  ? 0.1571 0.1801 0.1596 0.0052  0.0170  0.0129  56  ALA   B C   
4912 O O   . ALA   B 56  ? 0.1693 0.1901 0.1851 0.0049  0.0299  0.0094  56  ALA   B O   
4913 C CB  . ALA   B 56  ? 0.1690 0.2072 0.1712 -0.0072 0.0083  0.0022  56  ALA   B CB  
4919 N N   . THR   B 57  ? 0.1528 0.1695 0.1693 0.0018  0.0184  0.0073  57  THR   B N   
4920 C CA  . THR   B 57  ? 0.1573 0.1709 0.1626 0.0027  0.0196  0.0110  57  THR   B CA  
4921 C C   . THR   B 57  ? 0.1581 0.1816 0.1885 -0.0030 0.0204  0.0125  57  THR   B C   
4922 O O   . THR   B 57  ? 0.1606 0.1813 0.2095 -0.0190 0.0137  0.0066  57  THR   B O   
4923 C CB  . THR   B 57  ? 0.1593 0.1543 0.1573 0.0022  0.0140  0.0117  57  THR   B CB  
4924 O OG1 . THR   B 57  ? 0.1533 0.1523 0.1724 0.0001  0.0108  0.0076  57  THR   B OG1 
4925 C CG2 . THR   B 57  ? 0.1580 0.1636 0.1554 0.0033  0.0105  0.0160  57  THR   B CG2 
4933 N N   . ASN   B 58  ? 0.1453 0.1959 0.2092 -0.0062 0.0078  -0.0098 58  ASN   B N   
4934 C CA  . ASN   B 58  ? 0.1516 0.2251 0.2464 -0.0127 0.0232  -0.0108 58  ASN   B CA  
4935 C C   . ASN   B 58  ? 0.1407 0.2113 0.2132 -0.0063 -0.0049 -0.0023 58  ASN   B C   
4936 O O   . ASN   B 58  ? 0.1522 0.2209 0.2234 -0.0070 -0.0026 -0.0081 58  ASN   B O   
4937 C CB  . ASN   B 58  ? 0.2035 0.2653 0.3412 -0.0335 0.0571  -0.0071 58  ASN   B CB  
4938 C CG  . ASN   B 58  ? 0.2875 0.3177 0.4719 -0.0373 0.0705  0.0177  58  ASN   B CG  
4939 O OD1 . ASN   B 58  ? 0.3028 0.3292 0.5209 -0.0340 0.0697  0.0266  58  ASN   B OD1 
4940 N ND2 . ASN   B 58  ? 0.3114 0.3268 0.5174 -0.0408 0.0793  0.0242  58  ASN   B ND2 
4947 N N   . ASN   B 59  ? 0.1388 0.1947 0.1900 -0.0056 -0.0032 0.0054  59  ASN   B N   
4948 C CA  . ASN   B 59  ? 0.1441 0.1983 0.1894 -0.0077 -0.0125 0.0083  59  ASN   B CA  
4949 C C   . ASN   B 59  ? 0.1364 0.1883 0.1779 -0.0098 -0.0097 0.0017  59  ASN   B C   
4950 O O   . ASN   B 59  ? 0.1456 0.1909 0.1804 -0.0124 -0.0102 -0.0025 59  ASN   B O   
4951 C CB  . ASN   B 59  ? 0.1541 0.2197 0.2005 -0.0004 -0.0202 0.0100  59  ASN   B CB  
4952 C CG  . ASN   B 59  ? 0.1591 0.2345 0.2072 0.0057  -0.0340 -0.0005 59  ASN   B CG  
4953 O OD1 . ASN   B 59  ? 0.1605 0.2380 0.2155 0.0012  -0.0281 0.0156  59  ASN   B OD1 
4954 N ND2 . ASN   B 59  ? 0.1709 0.2478 0.2090 0.0058  -0.0350 -0.0007 59  ASN   B ND2 
4961 N N   . ALA   B 60  ? 0.1417 0.1806 0.1805 -0.0103 -0.0002 0.0025  60  ALA   B N   
4962 C CA  . ALA   B 60  ? 0.1521 0.1720 0.1832 -0.0163 -0.0064 0.0085  60  ALA   B CA  
4963 C C   . ALA   B 60  ? 0.1543 0.1610 0.1636 -0.0097 -0.0067 0.0036  60  ALA   B C   
4964 O O   . ALA   B 60  ? 0.1547 0.1612 0.1803 -0.0107 -0.0052 -0.0054 60  ALA   B O   
4965 C CB  . ALA   B 60  ? 0.1639 0.1756 0.2021 -0.0180 0.0041  0.0130  60  ALA   B CB  
4971 N N   . MET   B 61  ? 0.1492 0.1509 0.1680 -0.0081 -0.0065 0.0058  61  MET   B N   
4972 C CA  . MET   B 61  ? 0.1432 0.1496 0.1594 -0.0020 -0.0122 0.0079  61  MET   B CA  
4973 C C   . MET   B 61  ? 0.1459 0.1500 0.1567 -0.0050 -0.0115 0.0037  61  MET   B C   
4974 O O   . MET   B 61  ? 0.1491 0.1491 0.1479 0.0017  -0.0100 -0.0158 61  MET   B O   
4975 C CB  . MET   B 61  ? 0.1405 0.1472 0.1520 0.0011  -0.0035 0.0020  61  MET   B CB  
4976 C CG  . MET   B 61  ? 0.1381 0.1464 0.1595 0.0027  -0.0091 0.0043  61  MET   B CG  
4977 S SD  . MET   B 61  ? 0.1427 0.1509 0.1737 -0.0031 -0.0066 -0.0092 61  MET   B SD  
4978 C CE  . MET   B 61  ? 0.1501 0.1670 0.1969 0.0048  -0.0137 -0.0099 61  MET   B CE  
4988 N N   . GLN   B 62  ? 0.1444 0.1528 0.1472 -0.0024 -0.0195 -0.0002 62  GLN   B N   
4989 C CA  . GLN   B 62  ? 0.1469 0.1573 0.1571 -0.0010 -0.0180 -0.0015 62  GLN   B CA  
4990 C C   . GLN   B 62  ? 0.1474 0.1626 0.1561 -0.0015 -0.0225 -0.0021 62  GLN   B C   
4991 O O   . GLN   B 62  ? 0.1595 0.1660 0.1627 -0.0008 -0.0231 -0.0069 62  GLN   B O   
4992 C CB  . GLN   B 62  ? 0.1516 0.1618 0.1603 0.0025  -0.0154 0.0019  62  GLN   B CB  
4993 C CG  . GLN   B 62  ? 0.1554 0.1670 0.1590 0.0043  -0.0254 -0.0012 62  GLN   B CG  
4994 C CD  . GLN   B 62  ? 0.1559 0.1638 0.1507 0.0019  -0.0246 0.0079  62  GLN   B CD  
4995 O OE1 . GLN   B 62  ? 0.1530 0.1669 0.1660 0.0012  -0.0242 -0.0068 62  GLN   B OE1 
4996 N NE2 . GLN   B 62  ? 0.1569 0.1719 0.1638 0.0026  -0.0199 -0.0045 62  GLN   B NE2 
5005 N N   . VAL   B 63  ? 0.1493 0.1652 0.1840 -0.0078 -0.0206 -0.0081 63  VAL   B N   
5006 C CA  . VAL   B 63  ? 0.1624 0.1673 0.1997 -0.0070 -0.0321 -0.0061 63  VAL   B CA  
5007 C C   . VAL   B 63  ? 0.1597 0.1601 0.1790 -0.0154 -0.0266 -0.0174 63  VAL   B C   
5008 O O   . VAL   B 63  ? 0.1649 0.1617 0.1894 -0.0080 -0.0341 -0.0186 63  VAL   B O   
5009 C CB  . VAL   B 63  ? 0.1593 0.1827 0.2282 -0.0156 -0.0289 -0.0092 63  VAL   B CB  
5010 C CG1 . VAL   B 63  ? 0.1672 0.1867 0.2497 -0.0286 -0.0258 -0.0073 63  VAL   B CG1 
5011 C CG2 . VAL   B 63  ? 0.1526 0.1961 0.2475 -0.0126 -0.0297 -0.0175 63  VAL   B CG2 
5021 N N   . GLU   B 64  ? 0.1549 0.1520 0.1682 -0.0104 -0.0223 -0.0086 64  GLU   B N   
5022 C CA  . GLU   B 64  ? 0.1551 0.1482 0.1653 -0.0114 -0.0292 -0.0103 64  GLU   B CA  
5023 C C   . GLU   B 64  ? 0.1599 0.1506 0.1596 -0.0057 -0.0199 -0.0130 64  GLU   B C   
5024 O O   . GLU   B 64  ? 0.1688 0.1558 0.1650 -0.0073 -0.0182 -0.0170 64  GLU   B O   
5025 C CB  . GLU   B 64  ? 0.1542 0.1545 0.1665 -0.0129 -0.0200 -0.0012 64  GLU   B CB  
5026 C CG  . GLU   B 64  ? 0.1664 0.1537 0.1723 -0.0162 -0.0268 -0.0151 64  GLU   B CG  
5027 C CD  . GLU   B 64  ? 0.1676 0.1681 0.1859 -0.0234 -0.0267 -0.0038 64  GLU   B CD  
5028 O OE1 . GLU   B 64  ? 0.1729 0.1816 0.1940 -0.0271 -0.0225 -0.0233 64  GLU   B OE1 
5029 O OE2 . GLU   B 64  ? 0.1788 0.1831 0.1848 -0.0286 -0.0430 -0.0068 64  GLU   B OE2 
5036 N N   . SER   B 65  ? 0.1574 0.1435 0.1578 -0.0084 -0.0156 -0.0177 65  SER   B N   
5037 C CA  . SER   B 65  ? 0.1526 0.1432 0.1576 -0.0004 -0.0105 -0.0081 65  SER   B CA  
5038 C C   . SER   B 65  ? 0.1530 0.1430 0.1538 0.0003  -0.0190 -0.0186 65  SER   B C   
5039 O O   . SER   B 65  ? 0.1594 0.1580 0.1652 0.0019  -0.0176 -0.0301 65  SER   B O   
5040 C CB  . SER   B 65  ? 0.1553 0.1478 0.1595 -0.0099 -0.0113 -0.0109 65  SER   B CB  
5041 O OG  . SER   B 65  ? 0.1627 0.1453 0.1639 -0.0065 -0.0093 -0.0233 65  SER   B OG  
5047 N N   . ASP   B 66  ? 0.1666 0.1586 0.1577 0.0049  -0.0276 -0.0216 66  ASP   B N   
5048 C CA  . ASP   B 66  ? 0.1767 0.1691 0.1513 0.0064  -0.0254 -0.0157 66  ASP   B CA  
5049 C C   . ASP   B 66  ? 0.1794 0.1711 0.1475 0.0035  -0.0252 -0.0187 66  ASP   B C   
5050 O O   . ASP   B 66  ? 0.1871 0.1769 0.1580 0.0014  -0.0250 -0.0277 66  ASP   B O   
5051 C CB  . ASP   B 66  ? 0.1916 0.1787 0.1758 0.0085  -0.0415 -0.0178 66  ASP   B CB  
5052 C CG  . ASP   B 66  ? 0.2154 0.1960 0.1915 0.0205  -0.0541 -0.0063 66  ASP   B CG  
5053 O OD1 . ASP   B 66  ? 0.2417 0.1930 0.1972 0.0135  -0.0493 -0.0062 66  ASP   B OD1 
5054 O OD2 . ASP   B 66  ? 0.2268 0.2222 0.2593 0.0397  -0.0557 -0.0019 66  ASP   B OD2 
5059 N N   . ASP   B 67  ? 0.1758 0.1632 0.1545 -0.0056 -0.0195 -0.0208 67  ASP   B N   
5060 C CA  . ASP   B 67  ? 0.1889 0.1582 0.1677 -0.0101 -0.0301 -0.0174 67  ASP   B CA  
5061 C C   . ASP   B 67  ? 0.1878 0.1586 0.1685 0.0034  -0.0297 -0.0294 67  ASP   B C   
5062 O O   . ASP   B 67  ? 0.1993 0.1646 0.1845 0.0038  -0.0176 -0.0317 67  ASP   B O   
5063 C CB  . ASP   B 67  ? 0.2170 0.1648 0.1811 -0.0142 -0.0379 -0.0147 67  ASP   B CB  
5064 C CG  . ASP   B 67  ? 0.2525 0.1751 0.1873 -0.0101 -0.0610 -0.0138 67  ASP   B CG  
5065 O OD1 . ASP   B 67  ? 0.2760 0.1842 0.1963 -0.0138 -0.0539 -0.0138 67  ASP   B OD1 
5066 O OD2 . ASP   B 67  ? 0.2675 0.1909 0.1968 0.0055  -0.0650 -0.0091 67  ASP   B OD2 
5071 N N   . TYR   B 68  ? 0.1775 0.1609 0.1628 0.0048  -0.0335 -0.0359 68  TYR   B N   
5072 C CA  . TYR   B 68  ? 0.1764 0.1772 0.1743 0.0143  -0.0375 -0.0415 68  TYR   B CA  
5073 C C   . TYR   B 68  ? 0.1705 0.1731 0.1717 0.0074  -0.0334 -0.0481 68  TYR   B C   
5074 O O   . TYR   B 68  ? 0.1733 0.1842 0.1798 0.0100  -0.0254 -0.0620 68  TYR   B O   
5075 C CB  . TYR   B 68  ? 0.1784 0.2008 0.1882 0.0225  -0.0407 -0.0515 68  TYR   B CB  
5076 C CG  . TYR   B 68  ? 0.1941 0.2249 0.2069 0.0278  -0.0377 -0.0724 68  TYR   B CG  
5077 C CD1 . TYR   B 68  ? 0.2015 0.2286 0.2263 0.0087  -0.0413 -0.0885 68  TYR   B CD1 
5078 C CD2 . TYR   B 68  ? 0.1993 0.2448 0.2261 0.0362  -0.0480 -0.0796 68  TYR   B CD2 
5079 C CE1 . TYR   B 68  ? 0.2072 0.2404 0.2490 0.0115  -0.0460 -0.0925 68  TYR   B CE1 
5080 C CE2 . TYR   B 68  ? 0.2027 0.2507 0.2332 0.0322  -0.0457 -0.0927 68  TYR   B CE2 
5081 C CZ  . TYR   B 68  ? 0.2011 0.2471 0.2426 0.0173  -0.0535 -0.0965 68  TYR   B CZ  
5082 O OH  . TYR   B 68  ? 0.2003 0.2651 0.2809 0.0110  -0.0479 -0.0663 68  TYR   B OH  
5092 N N   . ILE   B 69  ? 0.1719 0.1653 0.1677 0.0083  -0.0293 -0.0433 69  ILE   B N   
5093 C CA  . ILE   B 69  ? 0.1754 0.1722 0.1852 0.0071  -0.0253 -0.0444 69  ILE   B CA  
5094 C C   . ILE   B 69  ? 0.1776 0.1722 0.1759 0.0146  -0.0371 -0.0350 69  ILE   B C   
5095 O O   . ILE   B 69  ? 0.1842 0.1876 0.1758 0.0144  -0.0214 -0.0371 69  ILE   B O   
5096 C CB  . ILE   B 69  ? 0.1819 0.1793 0.2114 0.0013  0.0002  -0.0378 69  ILE   B CB  
5097 C CG1 . ILE   B 69  ? 0.1850 0.1861 0.2260 -0.0060 0.0109  -0.0391 69  ILE   B CG1 
5098 C CG2 . ILE   B 69  ? 0.1988 0.1889 0.2374 0.0052  0.0015  -0.0352 69  ILE   B CG2 
5099 C CD1 . ILE   B 69  ? 0.1884 0.1884 0.2326 -0.0098 0.0094  -0.0526 69  ILE   B CD1 
5111 N N   . ALA   B 70  ? 0.1780 0.1700 0.1756 0.0157  -0.0407 -0.0321 70  ALA   B N   
5112 C CA  . ALA   B 70  ? 0.1795 0.1735 0.1650 0.0055  -0.0448 -0.0332 70  ALA   B CA  
5113 C C   . ALA   B 70  ? 0.1893 0.1756 0.1699 0.0041  -0.0473 -0.0460 70  ALA   B C   
5114 O O   . ALA   B 70  ? 0.1994 0.1778 0.1736 0.0102  -0.0439 -0.0457 70  ALA   B O   
5115 C CB  . ALA   B 70  ? 0.1831 0.1898 0.1596 0.0038  -0.0368 -0.0319 70  ALA   B CB  
5121 N N   . THR   B 71  ? 0.1931 0.1753 0.1762 0.0103  -0.0542 -0.0453 71  THR   B N   
5122 C CA  . THR   B 71  ? 0.2059 0.1799 0.1863 0.0145  -0.0611 -0.0451 71  THR   B CA  
5123 C C   . THR   B 71  ? 0.2033 0.1796 0.2061 0.0294  -0.0596 -0.0543 71  THR   B C   
5124 O O   . THR   B 71  ? 0.2098 0.1874 0.2412 0.0291  -0.0544 -0.0704 71  THR   B O   
5125 C CB  . THR   B 71  ? 0.2346 0.2026 0.2070 0.0104  -0.0689 -0.0241 71  THR   B CB  
5126 O OG1 . THR   B 71  ? 0.2470 0.2276 0.2179 -0.0076 -0.0574 -0.0046 71  THR   B OG1 
5127 C CG2 . THR   B 71  ? 0.2536 0.1992 0.2266 0.0194  -0.0632 -0.0061 71  THR   B CG2 
5135 N N   . ASN   B 72  ? 0.1850 0.1889 0.2040 0.0201  -0.0541 -0.0690 72  ASN   B N   
5136 C CA  . ASN   B 72  ? 0.1830 0.2045 0.2198 0.0244  -0.0469 -0.0781 72  ASN   B CA  
5137 C C   . ASN   B 72  ? 0.1829 0.2168 0.2293 0.0085  -0.0216 -0.0818 72  ASN   B C   
5138 O O   . ASN   B 72  ? 0.1863 0.2326 0.2526 0.0135  -0.0101 -0.0800 72  ASN   B O   
5139 C CB  . ASN   B 72  ? 0.1917 0.2188 0.2290 0.0184  -0.0603 -0.0717 72  ASN   B CB  
5140 C CG  . ASN   B 72  ? 0.2108 0.2344 0.2363 0.0349  -0.0614 -0.0477 72  ASN   B CG  
5141 O OD1 . ASN   B 72  ? 0.2355 0.2498 0.2382 0.0232  -0.0417 -0.0542 72  ASN   B OD1 
5142 N ND2 . ASN   B 72  ? 0.2188 0.2446 0.2789 0.0507  -0.0546 -0.0140 72  ASN   B ND2 
5149 N N   . GLY   B 73  ? 0.1848 0.2186 0.2071 -0.0010 -0.0255 -0.0763 73  GLY   B N   
5150 C CA  . GLY   B 73  ? 0.1845 0.2282 0.1872 0.0007  -0.0212 -0.0627 73  GLY   B CA  
5151 C C   . GLY   B 73  ? 0.1818 0.2252 0.1403 0.0066  -0.0189 -0.0657 73  GLY   B C   
5152 O O   . GLY   B 73  ? 0.1726 0.2131 0.1551 0.0084  -0.0162 -0.0530 73  GLY   B O   
5156 N N   . PRO   B 74  ? 0.1833 0.2284 0.1437 0.0044  -0.0216 -0.0533 74  PRO   B N   
5157 C CA  . PRO   B 74  ? 0.1770 0.2232 0.1232 0.0101  -0.0196 -0.0390 74  PRO   B CA  
5158 C C   . PRO   B 74  ? 0.1629 0.2084 0.1322 0.0098  -0.0147 -0.0331 74  PRO   B C   
5159 O O   . PRO   B 74  ? 0.1693 0.2150 0.1703 0.0127  -0.0087 -0.0472 74  PRO   B O   
5160 C CB  . PRO   B 74  ? 0.1958 0.2359 0.1421 0.0070  -0.0054 -0.0315 74  PRO   B CB  
5161 C CG  . PRO   B 74  ? 0.2135 0.2498 0.1711 0.0055  0.0000  -0.0297 74  PRO   B CG  
5162 C CD  . PRO   B 74  ? 0.2092 0.2433 0.1564 0.0067  -0.0035 -0.0447 74  PRO   B CD  
5170 N N   . LEU   B 75  ? 0.1556 0.1892 0.1254 0.0113  -0.0159 -0.0258 75  LEU   B N   
5171 C CA  . LEU   B 75  ? 0.1538 0.1831 0.1279 0.0051  -0.0174 -0.0179 75  LEU   B CA  
5172 C C   . LEU   B 75  ? 0.1588 0.1954 0.1309 0.0097  -0.0012 -0.0126 75  LEU   B C   
5173 O O   . LEU   B 75  ? 0.1810 0.2146 0.1499 0.0035  0.0013  -0.0059 75  LEU   B O   
5174 C CB  . LEU   B 75  ? 0.1654 0.1857 0.1199 -0.0052 -0.0215 -0.0029 75  LEU   B CB  
5175 C CG  . LEU   B 75  ? 0.1988 0.1995 0.1436 -0.0317 -0.0129 -0.0061 75  LEU   B CG  
5176 C CD1 . LEU   B 75  ? 0.2297 0.2187 0.1496 -0.0392 0.0076  -0.0122 75  LEU   B CD1 
5177 C CD2 . LEU   B 75  ? 0.2360 0.2249 0.2199 -0.0179 -0.0071 0.0075  75  LEU   B CD2 
5189 N N   . LYS   B 76  ? 0.1620 0.2083 0.1452 0.0046  0.0028  -0.0064 76  LYS   B N   
5190 C CA  . LYS   B 76  ? 0.1751 0.2119 0.1795 0.0007  0.0256  -0.0077 76  LYS   B CA  
5191 C C   . LYS   B 76  ? 0.1703 0.1957 0.1428 0.0054  0.0137  0.0080  76  LYS   B C   
5192 O O   . LYS   B 76  ? 0.1690 0.1821 0.1481 -0.0016 0.0090  0.0114  76  LYS   B O   
5193 C CB  . LYS   B 76  ? 0.1959 0.2249 0.2464 -0.0037 0.0441  -0.0399 76  LYS   B CB  
5194 C CG  . LYS   B 76  ? 0.2024 0.2410 0.2933 0.0020  0.0309  -0.0491 76  LYS   B CG  
5195 C CD  . LYS   B 76  ? 0.2048 0.2469 0.3301 0.0056  0.0143  -0.0627 76  LYS   B CD  
5196 C CE  . LYS   B 76  ? 0.2188 0.2640 0.3799 0.0096  0.0003  -0.0708 76  LYS   B CE  
5197 N NZ  . LYS   B 76  ? 0.2174 0.2740 0.3966 0.0059  -0.0111 -0.0832 76  LYS   B NZ  
5211 N N   . VAL   B 77  ? 0.1778 0.2051 0.1435 0.0107  0.0122  0.0158  77  VAL   B N   
5212 C CA  . VAL   B 77  ? 0.1781 0.1951 0.1567 0.0162  0.0197  0.0340  77  VAL   B CA  
5213 C C   . VAL   B 77  ? 0.1610 0.1722 0.1540 0.0152  0.0228  0.0264  77  VAL   B C   
5214 O O   . VAL   B 77  ? 0.1657 0.1725 0.1644 0.0219  0.0277  0.0133  77  VAL   B O   
5215 C CB  . VAL   B 77  ? 0.1932 0.2078 0.1808 0.0124  0.0261  0.0416  77  VAL   B CB  
5216 C CG1 . VAL   B 77  ? 0.1970 0.1976 0.2027 0.0011  0.0323  0.0506  77  VAL   B CG1 
5217 C CG2 . VAL   B 77  ? 0.2019 0.2240 0.2018 0.0139  0.0157  0.0478  77  VAL   B CG2 
5227 N N   . GLY   B 78  ? 0.1556 0.1679 0.1594 0.0092  0.0252  0.0162  78  GLY   B N   
5228 C CA  . GLY   B 78  ? 0.1528 0.1636 0.1456 0.0107  0.0186  0.0070  78  GLY   B CA  
5229 C C   . GLY   B 78  ? 0.1536 0.1515 0.1386 0.0141  0.0199  0.0039  78  GLY   B C   
5230 O O   . GLY   B 78  ? 0.1594 0.1565 0.1613 0.0172  0.0176  0.0136  78  GLY   B O   
5234 N N   . GLY   B 79  ? 0.1487 0.1593 0.1435 0.0091  0.0178  0.0050  79  GLY   B N   
5235 C CA  . GLY   B 79  ? 0.1551 0.1493 0.1506 0.0129  0.0137  0.0032  79  GLY   B CA  
5236 C C   . GLY   B 79  ? 0.1437 0.1423 0.1456 0.0156  0.0106  -0.0032 79  GLY   B C   
5237 O O   . GLY   B 79  ? 0.1448 0.1461 0.1616 0.0100  0.0201  0.0032  79  GLY   B O   
5241 N N   . SER   B 80  ? 0.1398 0.1383 0.1553 0.0067  0.0130  0.0003  80  SER   B N   
5242 C CA  . SER   B 80  ? 0.1380 0.1386 0.1526 0.0040  0.0096  0.0034  80  SER   B CA  
5243 C C   . SER   B 80  ? 0.1415 0.1349 0.1476 0.0063  -0.0047 -0.0015 80  SER   B C   
5244 O O   . SER   B 80  ? 0.1539 0.1364 0.1773 0.0112  0.0062  -0.0099 80  SER   B O   
5245 C CB  . SER   B 80  ? 0.1425 0.1427 0.1558 -0.0056 0.0007  0.0029  80  SER   B CB  
5246 O OG  . SER   B 80  ? 0.1499 0.1595 0.1738 0.0021  -0.0060 0.0080  80  SER   B OG  
5252 N N   . CYS   B 81  ? 0.1390 0.1246 0.1586 0.0024  0.0010  -0.0069 81  CYS   B N   
5253 C CA  . CYS   B 81  ? 0.1464 0.1217 0.1629 0.0037  -0.0042 -0.0051 81  CYS   B CA  
5254 C C   . CYS   B 81  ? 0.1464 0.1207 0.1407 0.0005  -0.0102 -0.0078 81  CYS   B C   
5255 O O   . CYS   B 81  ? 0.1657 0.1235 0.1500 0.0083  0.0053  -0.0055 81  CYS   B O   
5256 C CB  . CYS   B 81  ? 0.1591 0.1343 0.1576 -0.0004 -0.0084 -0.0102 81  CYS   B CB  
5257 S SG  . CYS   B 81  ? 0.1603 0.1571 0.1531 -0.0034 -0.0230 -0.0143 81  CYS   B SG  
5263 N N   . VAL   B 82  ? 0.1513 0.1207 0.1589 0.0004  -0.0172 -0.0080 82  VAL   B N   
5264 C CA  . VAL   B 82  ? 0.1502 0.1260 0.1521 0.0009  -0.0102 -0.0010 82  VAL   B CA  
5265 C C   . VAL   B 82  ? 0.1502 0.1213 0.1581 -0.0048 -0.0115 0.0027  82  VAL   B C   
5266 O O   . VAL   B 82  ? 0.1591 0.1261 0.1870 -0.0055 -0.0126 -0.0188 82  VAL   B O   
5267 C CB  . VAL   B 82  ? 0.1562 0.1506 0.1690 0.0009  -0.0116 0.0077  82  VAL   B CB  
5268 C CG1 . VAL   B 82  ? 0.1773 0.1802 0.1761 0.0065  -0.0144 0.0183  82  VAL   B CG1 
5269 C CG2 . VAL   B 82  ? 0.1608 0.1506 0.1717 -0.0044 -0.0220 0.0084  82  VAL   B CG2 
5279 N N   . LEU   B 83  ? 0.1435 0.1230 0.1606 -0.0105 -0.0174 -0.0073 83  LEU   B N   
5280 C CA  . LEU   B 83  ? 0.1466 0.1252 0.1560 -0.0108 -0.0136 -0.0050 83  LEU   B CA  
5281 C C   . LEU   B 83  ? 0.1483 0.1163 0.1486 -0.0193 -0.0177 0.0052  83  LEU   B C   
5282 O O   . LEU   B 83  ? 0.1525 0.1339 0.1408 -0.0213 -0.0176 0.0022  83  LEU   B O   
5283 C CB  . LEU   B 83  ? 0.1482 0.1379 0.1454 -0.0105 -0.0242 -0.0033 83  LEU   B CB  
5284 C CG  . LEU   B 83  ? 0.1750 0.1656 0.1516 -0.0154 -0.0137 -0.0070 83  LEU   B CG  
5285 C CD1 . LEU   B 83  ? 0.1887 0.1721 0.1434 -0.0205 -0.0277 -0.0028 83  LEU   B CD1 
5286 C CD2 . LEU   B 83  ? 0.1950 0.1733 0.1637 -0.0067 -0.0108 -0.0293 83  LEU   B CD2 
5298 N N   . SER   B 84  ? 0.1495 0.1364 0.1675 -0.0182 -0.0132 0.0074  84  SER   B N   
5299 C CA  . SER   B 84  ? 0.1515 0.1562 0.1600 -0.0219 -0.0150 0.0183  84  SER   B CA  
5300 C C   . SER   B 84  ? 0.1453 0.1712 0.1167 -0.0187 -0.0243 0.0176  84  SER   B C   
5301 O O   . SER   B 84  ? 0.1555 0.1551 0.1177 -0.0153 -0.0164 0.0060  84  SER   B O   
5302 C CB  . SER   B 84  ? 0.1758 0.1601 0.1919 -0.0259 0.0101  0.0187  84  SER   B CB  
5303 O OG  . SER   B 84  ? 0.1741 0.1732 0.2427 -0.0375 0.0040  0.0251  84  SER   B OG  
5309 N N   . GLY   B 85  ? 0.1555 0.1925 0.1303 -0.0229 -0.0147 0.0143  85  GLY   B N   
5310 C CA  . GLY   B 85  ? 0.1568 0.2001 0.1499 -0.0319 -0.0089 -0.0086 85  GLY   B CA  
5311 C C   . GLY   B 85  ? 0.1486 0.1787 0.1364 -0.0375 -0.0060 0.0042  85  GLY   B C   
5312 O O   . GLY   B 85  ? 0.1588 0.1789 0.1446 -0.0470 0.0164  -0.0068 85  GLY   B O   
5316 N N   . HIS   B 86  ? 0.1443 0.1638 0.1498 -0.0272 -0.0141 0.0190  86  HIS   B N   
5317 C CA  . HIS   B 86  ? 0.1477 0.1643 0.1495 -0.0315 -0.0168 0.0230  86  HIS   B CA  
5318 C C   . HIS   B 86  ? 0.1512 0.1775 0.1380 -0.0420 -0.0053 0.0362  86  HIS   B C   
5319 O O   . HIS   B 86  ? 0.1690 0.1936 0.1414 -0.0348 0.0017  0.0341  86  HIS   B O   
5320 C CB  . HIS   B 86  ? 0.1567 0.1713 0.1529 -0.0186 -0.0220 0.0121  86  HIS   B CB  
5321 C CG  . HIS   B 86  ? 0.1560 0.1752 0.1492 -0.0063 -0.0182 0.0129  86  HIS   B CG  
5322 N ND1 . HIS   B 86  ? 0.1693 0.1980 0.1719 -0.0206 -0.0222 -0.0047 86  HIS   B ND1 
5323 C CD2 . HIS   B 86  ? 0.1577 0.1800 0.1602 -0.0011 -0.0156 0.0092  86  HIS   B CD2 
5324 C CE1 . HIS   B 86  ? 0.1740 0.1998 0.1677 -0.0104 -0.0172 -0.0137 86  HIS   B CE1 
5325 N NE2 . HIS   B 86  ? 0.1666 0.1894 0.1557 0.0049  -0.0106 -0.0011 86  HIS   B NE2 
5333 N N   . ASN   B 87  ? 0.1469 0.1804 0.1542 -0.0339 -0.0069 0.0319  87  ASN   B N   
5334 C CA  . ASN   B 87  ? 0.1620 0.1958 0.1485 -0.0349 0.0201  0.0229  87  ASN   B CA  
5335 C C   . ASN   B 87  ? 0.1808 0.1815 0.1385 -0.0258 0.0302  0.0149  87  ASN   B C   
5336 O O   . ASN   B 87  ? 0.2099 0.1951 0.1751 -0.0281 0.0460  0.0085  87  ASN   B O   
5337 C CB  . ASN   B 87  ? 0.1633 0.2375 0.1850 -0.0230 0.0219  0.0159  87  ASN   B CB  
5338 C CG  . ASN   B 87  ? 0.1637 0.2525 0.1960 0.0057  0.0352  0.0336  87  ASN   B CG  
5339 O OD1 . ASN   B 87  ? 0.1663 0.2343 0.1877 0.0124  0.0421  0.0434  87  ASN   B OD1 
5340 N ND2 . ASN   B 87  ? 0.2002 0.2649 0.2272 0.0034  0.0420  0.0309  87  ASN   B ND2 
5347 N N   . LEU   B 88  ? 0.1624 0.1691 0.1304 -0.0292 0.0128  0.0089  88  LEU   B N   
5348 C CA  . LEU   B 88  ? 0.1779 0.1627 0.1407 -0.0333 0.0026  0.0058  88  LEU   B CA  
5349 C C   . LEU   B 88  ? 0.1728 0.1511 0.1346 -0.0366 -0.0009 -0.0016 88  LEU   B C   
5350 O O   . LEU   B 88  ? 0.2005 0.1600 0.1730 -0.0170 -0.0220 -0.0075 88  LEU   B O   
5351 C CB  . LEU   B 88  ? 0.1875 0.1685 0.1656 -0.0440 -0.0127 0.0133  88  LEU   B CB  
5352 C CG  . LEU   B 88  ? 0.2221 0.1963 0.1792 -0.0364 -0.0233 0.0330  88  LEU   B CG  
5353 C CD1 . LEU   B 88  ? 0.2303 0.2268 0.2012 -0.0472 -0.0199 0.0532  88  LEU   B CD1 
5354 C CD2 . LEU   B 88  ? 0.2622 0.2257 0.2450 0.0049  -0.0418 0.0065  88  LEU   B CD2 
5366 N N   . ALA   B 89  ? 0.1604 0.1509 0.1261 -0.0381 0.0119  0.0003  89  ALA   B N   
5367 C CA  . ALA   B 89  ? 0.1598 0.1480 0.1241 -0.0376 -0.0006 0.0072  89  ALA   B CA  
5368 C C   . ALA   B 89  ? 0.1712 0.1510 0.1188 -0.0407 0.0081  0.0074  89  ALA   B C   
5369 O O   . ALA   B 89  ? 0.1585 0.1600 0.1473 -0.0409 0.0084  -0.0221 89  ALA   B O   
5370 C CB  . ALA   B 89  ? 0.1517 0.1519 0.1309 -0.0390 0.0030  0.0141  89  ALA   B CB  
5376 N N   . LYS   B 90  ? 0.2051 0.1368 0.1392 -0.0455 -0.0157 0.0128  90  LYS   B N   
5377 C CA  . LYS   B 90  ? 0.2179 0.1366 0.1344 -0.0392 -0.0100 0.0159  90  LYS   B CA  
5378 C C   . LYS   B 90  ? 0.1990 0.1306 0.1293 -0.0396 -0.0094 0.0045  90  LYS   B C   
5379 O O   . LYS   B 90  ? 0.2139 0.1473 0.1567 -0.0556 -0.0049 -0.0024 90  LYS   B O   
5380 C CB  . LYS   B 90  ? 0.2337 0.1444 0.1584 -0.0333 -0.0083 0.0216  90  LYS   B CB  
5381 C CG  . LYS   B 90  ? 0.2348 0.1553 0.1649 -0.0183 0.0234  0.0210  90  LYS   B CG  
5382 C CD  . LYS   B 90  ? 0.2623 0.1870 0.2197 -0.0100 0.0404  -0.0016 90  LYS   B CD  
5383 C CE  . LYS   B 90  ? 0.2692 0.2076 0.2845 -0.0136 0.0469  -0.0104 90  LYS   B CE  
5384 N NZ  . LYS   B 90  ? 0.2768 0.2056 0.2920 -0.0226 0.0683  -0.0056 90  LYS   B NZ  
5398 N N   . HIS   B 91  ? 0.1752 0.1189 0.1236 -0.0284 -0.0150 0.0054  91  HIS   B N   
5399 C CA  . HIS   B 91  ? 0.1599 0.1262 0.1334 -0.0241 -0.0215 0.0035  91  HIS   B CA  
5400 C C   . HIS   B 91  ? 0.1475 0.1307 0.1139 -0.0267 -0.0013 0.0020  91  HIS   B C   
5401 O O   . HIS   B 91  ? 0.1668 0.1293 0.1253 -0.0260 -0.0161 0.0010  91  HIS   B O   
5402 C CB  . HIS   B 91  ? 0.1774 0.1315 0.1876 -0.0086 -0.0115 0.0138  91  HIS   B CB  
5403 C CG  . HIS   B 91  ? 0.2170 0.1471 0.2502 0.0021  0.0212  0.0285  91  HIS   B CG  
5404 N ND1 . HIS   B 91  ? 0.2481 0.1569 0.2966 -0.0003 0.0286  0.0132  91  HIS   B ND1 
5405 C CD2 . HIS   B 91  ? 0.2342 0.1794 0.2968 0.0190  0.0098  0.0636  91  HIS   B CD2 
5406 C CE1 . HIS   B 91  ? 0.2513 0.1745 0.3204 0.0137  0.0221  0.0291  91  HIS   B CE1 
5407 N NE2 . HIS   B 91  ? 0.2441 0.1852 0.3237 0.0313  0.0183  0.0629  91  HIS   B NE2 
5415 N N   . CYS   B 92  ? 0.1456 0.1270 0.1190 -0.0244 -0.0072 -0.0029 92  CYS   B N   
5416 C CA  . CYS   B 92  ? 0.1417 0.1288 0.1107 -0.0186 -0.0052 -0.0026 92  CYS   B CA  
5417 C C   . CYS   B 92  ? 0.1363 0.1207 0.1151 -0.0106 -0.0078 0.0005  92  CYS   B C   
5418 O O   . CYS   B 92  ? 0.1448 0.1234 0.1380 -0.0169 -0.0030 -0.0103 92  CYS   B O   
5419 C CB  . CYS   B 92  ? 0.1406 0.1331 0.1263 -0.0095 -0.0041 -0.0027 92  CYS   B CB  
5420 S SG  . CYS   B 92  ? 0.1429 0.1357 0.1314 -0.0098 -0.0096 0.0050  92  CYS   B SG  
5426 N N   . LEU   B 93  ? 0.1315 0.1226 0.1191 -0.0097 -0.0087 -0.0035 93  LEU   B N   
5427 C CA  . LEU   B 93  ? 0.1310 0.1187 0.1202 -0.0037 -0.0119 -0.0012 93  LEU   B CA  
5428 C C   . LEU   B 93  ? 0.1277 0.1189 0.1085 -0.0007 -0.0060 0.0040  93  LEU   B C   
5429 O O   . LEU   B 93  ? 0.1320 0.1180 0.1357 -0.0028 -0.0005 -0.0032 93  LEU   B O   
5430 C CB  . LEU   B 93  ? 0.1357 0.1248 0.1395 -0.0013 -0.0083 0.0004  93  LEU   B CB  
5431 C CG  . LEU   B 93  ? 0.1286 0.1341 0.1512 -0.0039 -0.0053 0.0089  93  LEU   B CG  
5432 C CD1 . LEU   B 93  ? 0.1340 0.1491 0.1572 0.0050  -0.0069 -0.0066 93  LEU   B CD1 
5433 C CD2 . LEU   B 93  ? 0.1373 0.1364 0.1612 -0.0077 -0.0101 -0.0038 93  LEU   B CD2 
5445 N N   . HIS   B 94  ? 0.1310 0.1147 0.1121 -0.0048 -0.0084 -0.0004 94  HIS   B N   
5446 C CA  . HIS   B 94  ? 0.1334 0.1110 0.1137 0.0001  -0.0004 0.0010  94  HIS   B CA  
5447 C C   . HIS   B 94  ? 0.1329 0.1146 0.1320 0.0034  0.0038  0.0025  94  HIS   B C   
5448 O O   . HIS   B 94  ? 0.1322 0.1288 0.1767 -0.0049 0.0173  -0.0118 94  HIS   B O   
5449 C CB  . HIS   B 94  ? 0.1337 0.1217 0.1193 -0.0017 -0.0077 0.0043  94  HIS   B CB  
5450 C CG  . HIS   B 94  ? 0.1322 0.1221 0.1239 -0.0048 -0.0202 -0.0017 94  HIS   B CG  
5451 N ND1 . HIS   B 94  ? 0.1394 0.1256 0.1246 -0.0042 -0.0164 -0.0047 94  HIS   B ND1 
5452 C CD2 . HIS   B 94  ? 0.1328 0.1251 0.1322 -0.0042 -0.0176 -0.0006 94  HIS   B CD2 
5453 C CE1 . HIS   B 94  ? 0.1391 0.1314 0.1254 -0.0074 -0.0131 -0.0002 94  HIS   B CE1 
5454 N NE2 . HIS   B 94  ? 0.1330 0.1328 0.1387 -0.0154 -0.0137 0.0007  94  HIS   B NE2 
5462 N N   . VAL   B 95  ? 0.1270 0.1159 0.1308 0.0006  0.0007  0.0059  95  VAL   B N   
5463 C CA  . VAL   B 95  ? 0.1249 0.1312 0.1344 -0.0007 0.0083  0.0091  95  VAL   B CA  
5464 C C   . VAL   B 95  ? 0.1314 0.1269 0.1299 -0.0009 0.0098  -0.0032 95  VAL   B C   
5465 O O   . VAL   B 95  ? 0.1375 0.1234 0.1487 0.0068  0.0119  0.0077  95  VAL   B O   
5466 C CB  . VAL   B 95  ? 0.1356 0.1275 0.1307 -0.0030 -0.0047 -0.0018 95  VAL   B CB  
5467 C CG1 . VAL   B 95  ? 0.1376 0.1497 0.1502 -0.0106 -0.0008 0.0068  95  VAL   B CG1 
5468 C CG2 . VAL   B 95  ? 0.1475 0.1221 0.1361 -0.0019 -0.0044 0.0040  95  VAL   B CG2 
5478 N N   . VAL   B 96  ? 0.1386 0.1297 0.1389 0.0081  0.0082  0.0027  96  VAL   B N   
5479 C CA  . VAL   B 96  ? 0.1486 0.1386 0.1275 0.0039  0.0037  0.0120  96  VAL   B CA  
5480 C C   . VAL   B 96  ? 0.1486 0.1449 0.1338 0.0071  0.0093  0.0112  96  VAL   B C   
5481 O O   . VAL   B 96  ? 0.1517 0.1527 0.1607 0.0059  0.0214  -0.0022 96  VAL   B O   
5482 C CB  . VAL   B 96  ? 0.1576 0.1620 0.1311 0.0082  0.0079  0.0076  96  VAL   B CB  
5483 C CG1 . VAL   B 96  ? 0.1636 0.1751 0.1346 0.0091  0.0152  0.0068  96  VAL   B CG1 
5484 C CG2 . VAL   B 96  ? 0.1672 0.1614 0.1435 0.0006  0.0124  -0.0032 96  VAL   B CG2 
5494 N N   . GLY   B 97  ? 0.1548 0.1406 0.1409 0.0062  0.0078  0.0131  97  GLY   B N   
5495 C CA  . GLY   B 97  ? 0.1681 0.1435 0.1395 -0.0015 0.0089  0.0157  97  GLY   B CA  
5496 C C   . GLY   B 97  ? 0.1805 0.1566 0.1400 0.0073  0.0098  0.0128  97  GLY   B C   
5497 O O   . GLY   B 97  ? 0.1872 0.1607 0.1438 -0.0023 0.0095  0.0063  97  GLY   B O   
5501 N N   . PRO   B 98  ? 0.1918 0.1579 0.1532 0.0038  0.0267  0.0228  98  PRO   B N   
5502 C CA  . PRO   B 98  ? 0.1996 0.1694 0.1644 0.0086  0.0317  0.0199  98  PRO   B CA  
5503 C C   . PRO   B 98  ? 0.2110 0.1741 0.1322 0.0168  0.0262  0.0352  98  PRO   B C   
5504 O O   . PRO   B 98  ? 0.1982 0.1697 0.1509 0.0174  0.0225  0.0287  98  PRO   B O   
5505 C CB  . PRO   B 98  ? 0.1870 0.1723 0.1823 0.0069  0.0466  0.0192  98  PRO   B CB  
5506 C CG  . PRO   B 98  ? 0.1842 0.1715 0.1786 0.0053  0.0319  0.0345  98  PRO   B CG  
5507 C CD  . PRO   B 98  ? 0.1724 0.1651 0.1650 0.0051  0.0225  0.0310  98  PRO   B CD  
5515 N N   . ASN   B 99  ? 0.2195 0.1845 0.1410 0.0285  0.0325  0.0118  99  ASN   B N   
5516 C CA  . ASN   B 99  ? 0.2389 0.1934 0.1485 0.0354  0.0249  0.0277  99  ASN   B CA  
5517 C C   . ASN   B 99  ? 0.2643 0.2232 0.1670 0.0229  0.0441  0.0486  99  ASN   B C   
5518 O O   . ASN   B 99  ? 0.2772 0.2260 0.1748 0.0221  0.0351  0.0468  99  ASN   B O   
5519 C CB  . ASN   B 99  ? 0.2499 0.1917 0.1573 0.0334  0.0172  0.0291  99  ASN   B CB  
5520 C CG  . ASN   B 99  ? 0.2581 0.2014 0.1785 0.0320  0.0104  0.0209  99  ASN   B CG  
5521 O OD1 . ASN   B 99  ? 0.2630 0.2037 0.2024 0.0383  0.0029  0.0259  99  ASN   B OD1 
5522 N ND2 . ASN   B 99  ? 0.2610 0.2019 0.2076 0.0325  -0.0076 0.0219  99  ASN   B ND2 
5529 N N   A VAL   B 100 ? 0.2850 0.2403 0.2087 0.0163  0.0397  0.0620  100 VAL   B N   
5530 N N   B VAL   B 100 ? 0.2807 0.2360 0.2067 0.0102  0.0512  0.0677  100 VAL   B N   
5531 C CA  A VAL   B 100 ? 0.3091 0.2593 0.2540 0.0110  0.0333  0.0770  100 VAL   B CA  
5532 C CA  B VAL   B 100 ? 0.3056 0.2559 0.2595 -0.0002 0.0520  0.0913  100 VAL   B CA  
5533 C C   A VAL   B 100 ? 0.3296 0.2680 0.2551 0.0148  0.0315  0.0969  100 VAL   B C   
5534 C C   B VAL   B 100 ? 0.3291 0.2633 0.2475 0.0084  0.0479  0.1078  100 VAL   B C   
5535 O O   A VAL   B 100 ? 0.3347 0.2738 0.2598 0.0152  0.0315  0.0907  100 VAL   B O   
5536 O O   B VAL   B 100 ? 0.3382 0.2705 0.2501 0.0096  0.0527  0.0971  100 VAL   B O   
5537 C CB  A VAL   B 100 ? 0.3155 0.2702 0.3002 0.0020  0.0261  0.0749  100 VAL   B CB  
5538 C CB  B VAL   B 100 ? 0.3144 0.2709 0.3340 -0.0186 0.0465  0.1001  100 VAL   B CB  
5539 C CG1 A VAL   B 100 ? 0.3180 0.2739 0.3191 -0.0002 0.0245  0.0718  100 VAL   B CG1 
5540 C CG1 B VAL   B 100 ? 0.3192 0.2765 0.3664 -0.0216 0.0447  0.0965  100 VAL   B CG1 
5541 C CG2 A VAL   B 100 ? 0.3175 0.2756 0.3160 -0.0013 0.0236  0.0749  100 VAL   B CG2 
5542 C CG2 B VAL   B 100 ? 0.3165 0.2794 0.3580 -0.0257 0.0464  0.1052  100 VAL   B CG2 
5561 N N   . ASN   B 101 ? 0.3453 0.2737 0.2541 0.0204  0.0263  0.1133  101 ASN   B N   
5562 C CA  . ASN   B 101 ? 0.3862 0.2996 0.2782 0.0219  0.0040  0.1263  101 ASN   B CA  
5563 C C   . ASN   B 101 ? 0.4306 0.3498 0.2922 0.0177  -0.0140 0.1133  101 ASN   B C   
5564 O O   . ASN   B 101 ? 0.4389 0.3620 0.3025 0.0263  -0.0237 0.0991  101 ASN   B O   
5565 C CB  . ASN   B 101 ? 0.3847 0.2855 0.2989 0.0206  0.0083  0.1235  101 ASN   B CB  
5566 C CG  . ASN   B 101 ? 0.3837 0.2712 0.3044 0.0168  0.0219  0.1258  101 ASN   B CG  
5567 O OD1 . ASN   B 101 ? 0.3886 0.2705 0.3327 0.0147  0.0373  0.1178  101 ASN   B OD1 
5568 N ND2 . ASN   B 101 ? 0.3797 0.2722 0.3017 0.0130  0.0197  0.1110  101 ASN   B ND2 
5576 N N   A LYS   B 102 ? 0.4417 0.3712 0.3211 0.0129  -0.0134 0.0888  102 LYS   B N   
5577 N N   B LYS   B 102 ? 0.4521 0.3725 0.3020 0.0072  -0.0087 0.1085  102 LYS   B N   
5578 C CA  A LYS   B 102 ? 0.4518 0.3928 0.3488 0.0077  -0.0087 0.0614  102 LYS   B CA  
5579 C CA  B LYS   B 102 ? 0.4736 0.4013 0.3195 -0.0044 0.0017  0.0924  102 LYS   B CA  
5580 C C   A LYS   B 102 ? 0.4457 0.3918 0.3360 0.0090  -0.0023 0.0569  102 LYS   B C   
5581 C C   B LYS   B 102 ? 0.4731 0.4022 0.2922 -0.0027 0.0130  0.1063  102 LYS   B C   
5582 O O   A LYS   B 102 ? 0.4502 0.3947 0.3350 0.0096  -0.0063 0.0551  102 LYS   B O   
5583 O O   B LYS   B 102 ? 0.4815 0.4074 0.2965 -0.0009 0.0019  0.1041  102 LYS   B O   
5584 C CB  A LYS   B 102 ? 0.4667 0.4124 0.3924 0.0018  -0.0055 0.0377  102 LYS   B CB  
5585 C CB  B LYS   B 102 ? 0.4940 0.4263 0.3739 -0.0156 0.0088  0.0557  102 LYS   B CB  
5586 C CG  A LYS   B 102 ? 0.4798 0.4291 0.4359 -0.0029 -0.0007 0.0163  102 LYS   B CG  
5587 C CG  B LYS   B 102 ? 0.5120 0.4479 0.4325 -0.0241 0.0184  0.0205  102 LYS   B CG  
5588 C CD  A LYS   B 102 ? 0.4907 0.4427 0.4772 -0.0063 0.0048  -0.0006 102 LYS   B CD  
5589 C CD  B LYS   B 102 ? 0.5272 0.4663 0.4902 -0.0309 0.0286  -0.0074 102 LYS   B CD  
5590 C CE  A LYS   B 102 ? 0.4988 0.4524 0.5076 -0.0089 0.0090  -0.0134 102 LYS   B CE  
5591 C CE  B LYS   B 102 ? 0.5382 0.4793 0.5341 -0.0365 0.0357  -0.0290 102 LYS   B CE  
5592 N NZ  A LYS   B 102 ? 0.5037 0.4580 0.5258 -0.0099 0.0111  -0.0206 102 LYS   B NZ  
5593 N NZ  B LYS   B 102 ? 0.5449 0.4868 0.5608 -0.0383 0.0387  -0.0418 102 LYS   B NZ  
5620 N N   A GLY   B 103 ? 0.4336 0.3859 0.3308 0.0097  0.0081  0.0533  103 GLY   B N   
5621 N N   B GLY   B 103 ? 0.4612 0.3949 0.2780 -0.0027 0.0362  0.1158  103 GLY   B N   
5622 C CA  A GLY   B 103 ? 0.4202 0.3788 0.3306 0.0103  0.0192  0.0458  103 GLY   B CA  
5623 C CA  B GLY   B 103 ? 0.4460 0.3859 0.2801 -0.0028 0.0607  0.1084  103 GLY   B CA  
5624 C C   A GLY   B 103 ? 0.4053 0.3700 0.3278 0.0097  0.0301  0.0368  103 GLY   B C   
5625 C C   B GLY   B 103 ? 0.4263 0.3721 0.2725 -0.0059 0.0886  0.0945  103 GLY   B C   
5626 O O   A GLY   B 103 ? 0.4069 0.3730 0.3331 0.0091  0.0305  0.0384  103 GLY   B O   
5627 O O   B GLY   B 103 ? 0.4300 0.3789 0.2851 -0.0057 0.0926  0.0953  103 GLY   B O   
5634 N N   A GLU   B 104 ? 0.3885 0.3565 0.3186 0.0096  0.0375  0.0247  104 GLU   B N   
5635 N N   B GLU   B 104 ? 0.4015 0.3476 0.2502 -0.0066 0.1035  0.0722  104 GLU   B N   
5636 C CA  A GLU   B 104 ? 0.3725 0.3449 0.3100 0.0096  0.0412  0.0128  104 GLU   B CA  
5637 C CA  B GLU   B 104 ? 0.3788 0.3255 0.2346 -0.0029 0.1026  0.0457  104 GLU   B CA  
5638 C C   A GLU   B 104 ? 0.3718 0.3442 0.3202 0.0032  0.0527  0.0106  104 GLU   B C   
5639 C C   B GLU   B 104 ? 0.3780 0.3264 0.2589 -0.0170 0.1220  0.0397  104 GLU   B C   
5640 O O   A GLU   B 104 ? 0.3723 0.3440 0.3226 0.0028  0.0513  0.0083  104 GLU   B O   
5641 O O   B GLU   B 104 ? 0.3821 0.3299 0.2781 -0.0175 0.1163  0.0378  104 GLU   B O   
5642 C CB  A GLU   B 104 ? 0.3604 0.3346 0.2974 0.0152  0.0317  -0.0000 104 GLU   B CB  
5643 C CB  B GLU   B 104 ? 0.3621 0.3016 0.2146 0.0147  0.0707  0.0151  104 GLU   B CB  
5644 C CG  A GLU   B 104 ? 0.3508 0.3270 0.2902 0.0204  0.0200  -0.0131 104 GLU   B CG  
5645 C CG  B GLU   B 104 ? 0.3482 0.2820 0.2015 0.0332  0.0331  -0.0165 104 GLU   B CG  
5646 C CD  A GLU   B 104 ? 0.3430 0.3211 0.2843 0.0231  0.0080  -0.0216 104 GLU   B CD  
5647 C CD  B GLU   B 104 ? 0.3388 0.2639 0.1811 0.0414  -0.0060 -0.0274 104 GLU   B CD  
5648 O OE1 A GLU   B 104 ? 0.3362 0.3161 0.2732 0.0238  0.0102  -0.0210 104 GLU   B OE1 
5649 O OE1 B GLU   B 104 ? 0.3214 0.2459 0.1553 0.0511  -0.0035 -0.0215 104 GLU   B OE1 
5650 O OE2 A GLU   B 104 ? 0.3439 0.3237 0.2893 0.0245  -0.0028 -0.0271 104 GLU   B OE2 
5651 O OE2 B GLU   B 104 ? 0.3439 0.2719 0.1799 0.0365  -0.0357 -0.0284 104 GLU   B OE2 
5664 N N   A ASP   B 105 ? 0.3705 0.3444 0.3265 -0.0034 0.0634  0.0101  105 ASP   B N   
5665 N N   B ASP   B 105 ? 0.3712 0.3245 0.2667 -0.0306 0.1417  0.0279  105 ASP   B N   
5666 C CA  A ASP   B 105 ? 0.3708 0.3447 0.3419 -0.0094 0.0711  0.0057  105 ASP   B CA  
5667 C CA  B ASP   B 105 ? 0.3701 0.3226 0.2936 -0.0424 0.1567  0.0062  105 ASP   B CA  
5668 C C   A ASP   B 105 ? 0.3641 0.3327 0.3180 -0.0142 0.0734  0.0017  105 ASP   B C   
5669 C C   B ASP   B 105 ? 0.3496 0.2878 0.2530 -0.0541 0.1590  -0.0058 105 ASP   B C   
5670 O O   A ASP   B 105 ? 0.3632 0.3305 0.3133 -0.0141 0.0768  0.0018  105 ASP   B O   
5671 O O   B ASP   B 105 ? 0.3217 0.2715 0.2413 -0.0561 0.1579  -0.0141 105 ASP   B O   
5672 C CB  A ASP   B 105 ? 0.3759 0.3550 0.3835 -0.0092 0.0733  0.0044  105 ASP   B CB  
5673 C CB  B ASP   B 105 ? 0.3843 0.3491 0.3759 -0.0400 0.1503  -0.0085 105 ASP   B CB  
5674 C CG  A ASP   B 105 ? 0.3798 0.3624 0.4208 -0.0106 0.0764  0.0052  105 ASP   B CG  
5675 C CG  B ASP   B 105 ? 0.3954 0.3669 0.4426 -0.0424 0.1514  -0.0129 105 ASP   B CG  
5676 O OD1 A ASP   B 105 ? 0.3798 0.3640 0.4277 -0.0143 0.0804  0.0094  105 ASP   B OD1 
5677 O OD1 B ASP   B 105 ? 0.3965 0.3727 0.4574 -0.0512 0.1555  -0.0089 105 ASP   B OD1 
5678 O OD2 A ASP   B 105 ? 0.3821 0.3664 0.4416 -0.0087 0.0730  0.0025  105 ASP   B OD2 
5679 O OD2 B ASP   B 105 ? 0.4013 0.3741 0.4696 -0.0388 0.1508  -0.0172 105 ASP   B OD2 
5688 N N   A ILE   B 106 ? 0.3576 0.3220 0.3083 -0.0158 0.0683  -0.0017 106 ILE   B N   
5689 N N   B ILE   B 106 ? 0.3506 0.2690 0.2634 -0.0614 0.1431  -0.0093 106 ILE   B N   
5690 C CA  A ILE   B 106 ? 0.3481 0.3115 0.3056 -0.0169 0.0674  -0.0048 106 ILE   B CA  
5691 C CA  B ILE   B 106 ? 0.3399 0.2491 0.2750 -0.0687 0.1430  -0.0083 106 ILE   B CA  
5692 C C   A ILE   B 106 ? 0.3332 0.3108 0.3015 -0.0130 0.0672  -0.0126 106 ILE   B C   
5693 C C   B ILE   B 106 ? 0.3090 0.2552 0.2628 -0.0654 0.1477  -0.0259 106 ILE   B C   
5694 O O   A ILE   B 106 ? 0.3305 0.3077 0.2959 -0.0125 0.0641  -0.0139 106 ILE   B O   
5695 O O   B ILE   B 106 ? 0.2952 0.2402 0.2474 -0.0756 0.1461  -0.0327 106 ILE   B O   
5696 C CB  A ILE   B 106 ? 0.3540 0.3040 0.3097 -0.0216 0.0662  -0.0009 106 ILE   B CB  
5697 C CB  B ILE   B 106 ? 0.3639 0.2338 0.3055 -0.0703 0.1339  0.0024  106 ILE   B CB  
5698 C CG1 A ILE   B 106 ? 0.3555 0.2982 0.3061 -0.0213 0.0645  -0.0014 106 ILE   B CG1 
5699 C CG1 B ILE   B 106 ? 0.3741 0.2245 0.3087 -0.0556 0.1265  -0.0029 106 ILE   B CG1 
5700 C CG2 A ILE   B 106 ? 0.3572 0.3054 0.3184 -0.0236 0.0663  0.0013  106 ILE   B CG2 
5701 C CG2 B ILE   B 106 ? 0.3725 0.2404 0.3284 -0.0776 0.1330  0.0084  106 ILE   B CG2 
5702 C CD1 A ILE   B 106 ? 0.3561 0.2963 0.3013 -0.0195 0.0645  -0.0001 106 ILE   B CD1 
5703 C CD1 B ILE   B 106 ? 0.3787 0.2256 0.3014 -0.0423 0.1262  -0.0008 106 ILE   B CD1 
5726 N N   A GLN   B 107 ? 0.3218 0.3139 0.3113 -0.0126 0.0670  -0.0163 107 GLN   B N   
5727 N N   B GLN   B 107 ? 0.2983 0.2791 0.2823 -0.0597 0.1414  -0.0270 107 GLN   B N   
5728 C CA  A GLN   B 107 ? 0.3081 0.3142 0.3224 -0.0119 0.0635  -0.0168 107 GLN   B CA  
5729 C CA  B GLN   B 107 ? 0.2851 0.3022 0.3099 -0.0462 0.1278  -0.0215 107 GLN   B CA  
5730 C C   A GLN   B 107 ? 0.2751 0.2911 0.2896 -0.0103 0.0683  -0.0267 107 GLN   B C   
5731 C C   B GLN   B 107 ? 0.2600 0.2869 0.2878 -0.0279 0.1007  -0.0322 107 GLN   B C   
5732 O O   A GLN   B 107 ? 0.2757 0.2943 0.2966 -0.0050 0.0579  -0.0341 107 GLN   B O   
5733 O O   B GLN   B 107 ? 0.2575 0.2970 0.3176 -0.0160 0.0785  -0.0488 107 GLN   B O   
5734 C CB  A GLN   B 107 ? 0.3296 0.3374 0.3798 -0.0090 0.0506  -0.0095 107 GLN   B CB  
5735 C CB  B GLN   B 107 ? 0.3151 0.3429 0.3925 -0.0373 0.1070  -0.0107 107 GLN   B CB  
5736 C CG  A GLN   B 107 ? 0.3489 0.3578 0.4342 -0.0058 0.0354  -0.0030 107 GLN   B CG  
5737 C CG  B GLN   B 107 ? 0.3480 0.3783 0.4752 -0.0264 0.0719  -0.0029 107 GLN   B CG  
5738 C CD  A GLN   B 107 ? 0.3636 0.3736 0.4794 -0.0048 0.0247  0.0017  107 GLN   B CD  
5739 C CD  B GLN   B 107 ? 0.3740 0.4075 0.5415 -0.0213 0.0473  0.0030  107 GLN   B CD  
5740 O OE1 A GLN   B 107 ? 0.3691 0.3798 0.4952 -0.0039 0.0230  0.0019  107 GLN   B OE1 
5741 O OE1 B GLN   B 107 ? 0.3856 0.4184 0.5647 -0.0197 0.0418  0.0037  107 GLN   B OE1 
5742 N NE2 A GLN   B 107 ? 0.3693 0.3787 0.4955 -0.0030 0.0206  0.0044  107 GLN   B NE2 
5743 N NE2 B GLN   B 107 ? 0.3840 0.4166 0.5647 -0.0164 0.0391  0.0065  107 GLN   B NE2 
5760 N N   . LEU   B 108 ? 0.2393 0.2657 0.2586 -0.0116 0.0834  -0.0327 108 LEU   B N   
5761 C CA  . LEU   B 108 ? 0.2181 0.2332 0.2153 0.0114  0.0603  -0.0111 108 LEU   B CA  
5762 C C   . LEU   B 108 ? 0.1952 0.1882 0.2053 0.0234  0.0372  0.0108  108 LEU   B C   
5763 O O   . LEU   B 108 ? 0.1939 0.1736 0.2041 0.0222  0.0283  0.0082  108 LEU   B O   
5764 C CB  . LEU   B 108 ? 0.2312 0.2471 0.1910 0.0148  0.0593  -0.0058 108 LEU   B CB  
5765 C CG  . LEU   B 108 ? 0.2453 0.2770 0.2029 0.0225  0.0479  -0.0184 108 LEU   B CG  
5766 C CD1 . LEU   B 108 ? 0.2584 0.2941 0.1923 0.0116  0.0428  -0.0104 108 LEU   B CD1 
5767 C CD2 . LEU   B 108 ? 0.2600 0.2848 0.2242 0.0349  0.0339  -0.0286 108 LEU   B CD2 
5780 N N   . LEU   B 109 ? 0.1810 0.1648 0.1958 0.0176  0.0406  0.0136  109 LEU   B N   
5781 C CA  . LEU   B 109 ? 0.1624 0.1426 0.2062 0.0133  0.0336  0.0172  109 LEU   B CA  
5782 C C   . LEU   B 109 ? 0.1506 0.1320 0.2003 0.0062  0.0286  0.0200  109 LEU   B C   
5783 O O   . LEU   B 109 ? 0.1483 0.1313 0.1965 0.0071  0.0218  0.0220  109 LEU   B O   
5784 C CB  . LEU   B 109 ? 0.1703 0.1392 0.2040 0.0083  0.0254  0.0223  109 LEU   B CB  
5785 C CG  . LEU   B 109 ? 0.1648 0.1376 0.1984 0.0097  0.0160  0.0127  109 LEU   B CG  
5786 C CD1 . LEU   B 109 ? 0.1659 0.1467 0.1966 0.0078  0.0122  0.0137  109 LEU   B CD1 
5787 C CD2 . LEU   B 109 ? 0.1763 0.1540 0.2056 0.0079  0.0150  0.0114  109 LEU   B CD2 
5799 N N   . LYS   B 110 ? 0.1465 0.1386 0.1986 -0.0028 0.0300  0.0134  110 LYS   B N   
5800 C CA  . LYS   B 110 ? 0.1445 0.1303 0.2084 0.0010  0.0278  0.0119  110 LYS   B CA  
5801 C C   . LYS   B 110 ? 0.1394 0.1354 0.1965 0.0022  0.0261  0.0040  110 LYS   B C   
5802 O O   . LYS   B 110 ? 0.1392 0.1327 0.1946 -0.0017 0.0246  -0.0014 110 LYS   B O   
5803 C CB  . LYS   B 110 ? 0.1455 0.1296 0.2350 -0.0028 0.0312  0.0114  110 LYS   B CB  
5804 C CG  . LYS   B 110 ? 0.1403 0.1367 0.2476 -0.0025 0.0223  0.0071  110 LYS   B CG  
5805 C CD  . LYS   B 110 ? 0.1516 0.1378 0.2601 -0.0051 0.0222  -0.0003 110 LYS   B CD  
5806 C CE  . LYS   B 110 ? 0.1486 0.1551 0.2748 0.0028  0.0179  -0.0003 110 LYS   B CE  
5807 N NZ  . LYS   B 110 ? 0.1463 0.1693 0.2704 0.0052  0.0121  -0.0077 110 LYS   B NZ  
5821 N N   . SER   B 111 ? 0.1483 0.1329 0.1949 -0.0015 0.0245  0.0115  111 SER   B N   
5822 C CA  . SER   B 111 ? 0.1587 0.1386 0.1896 0.0025  0.0219  0.0114  111 SER   B CA  
5823 C C   . SER   B 111 ? 0.1453 0.1290 0.1849 0.0020  0.0171  0.0001  111 SER   B C   
5824 O O   . SER   B 111 ? 0.1463 0.1333 0.1973 -0.0016 0.0032  0.0010  111 SER   B O   
5825 C CB  . SER   B 111 ? 0.1788 0.1544 0.1963 0.0043  0.0384  0.0144  111 SER   B CB  
5826 O OG  . SER   B 111 ? 0.1983 0.1947 0.2115 0.0108  0.0468  0.0184  111 SER   B OG  
5832 N N   . ALA   B 112 ? 0.1401 0.1353 0.1917 0.0102  0.0223  0.0055  112 ALA   B N   
5833 C CA  . ALA   B 112 ? 0.1372 0.1361 0.1851 0.0038  0.0113  -0.0018 112 ALA   B CA  
5834 C C   . ALA   B 112 ? 0.1287 0.1260 0.1694 0.0067  0.0056  -0.0028 112 ALA   B C   
5835 O O   . ALA   B 112 ? 0.1309 0.1321 0.1748 -0.0046 0.0068  -0.0042 112 ALA   B O   
5836 C CB  . ALA   B 112 ? 0.1396 0.1438 0.1862 0.0086  0.0096  0.0020  112 ALA   B CB  
5842 N N   . TYR   B 113 ? 0.1305 0.1184 0.1824 0.0041  0.0102  0.0018  113 TYR   B N   
5843 C CA  . TYR   B 113 ? 0.1243 0.1212 0.1731 0.0005  0.0123  -0.0041 113 TYR   B CA  
5844 C C   . TYR   B 113 ? 0.1236 0.1150 0.1697 -0.0062 0.0050  -0.0019 113 TYR   B C   
5845 O O   . TYR   B 113 ? 0.1282 0.1202 0.1697 -0.0017 0.0065  -0.0075 113 TYR   B O   
5846 C CB  . TYR   B 113 ? 0.1297 0.1187 0.1731 0.0013  0.0119  0.0059  113 TYR   B CB  
5847 C CG  . TYR   B 113 ? 0.1292 0.1189 0.1818 -0.0023 0.0080  0.0047  113 TYR   B CG  
5848 C CD1 . TYR   B 113 ? 0.1382 0.1219 0.1913 -0.0036 0.0147  0.0155  113 TYR   B CD1 
5849 C CD2 . TYR   B 113 ? 0.1433 0.1183 0.1835 -0.0037 0.0151  0.0051  113 TYR   B CD2 
5850 C CE1 . TYR   B 113 ? 0.1412 0.1271 0.1867 -0.0009 0.0197  0.0038  113 TYR   B CE1 
5851 C CE2 . TYR   B 113 ? 0.1493 0.1173 0.1893 0.0033  0.0124  0.0087  113 TYR   B CE2 
5852 C CZ  . TYR   B 113 ? 0.1375 0.1205 0.1955 0.0058  0.0086  0.0008  113 TYR   B CZ  
5853 O OH  . TYR   B 113 ? 0.1469 0.1172 0.2251 0.0091  0.0182  0.0043  113 TYR   B OH  
5863 N N   . GLU   B 114 ? 0.1270 0.1161 0.1831 -0.0002 0.0106  0.0033  114 GLU   B N   
5864 C CA  . GLU   B 114 ? 0.1219 0.1136 0.1799 0.0011  0.0053  -0.0013 114 GLU   B CA  
5865 C C   . GLU   B 114 ? 0.1244 0.1163 0.1713 0.0006  0.0090  -0.0048 114 GLU   B C   
5866 O O   . GLU   B 114 ? 0.1279 0.1200 0.1853 0.0017  0.0023  0.0061  114 GLU   B O   
5867 C CB  . GLU   B 114 ? 0.1231 0.1206 0.1846 -0.0009 0.0095  0.0047  114 GLU   B CB  
5868 C CG  . GLU   B 114 ? 0.1312 0.1195 0.2010 -0.0014 0.0129  -0.0002 114 GLU   B CG  
5869 C CD  . GLU   B 114 ? 0.1329 0.1268 0.2011 -0.0053 0.0052  -0.0035 114 GLU   B CD  
5870 O OE1 . GLU   B 114 ? 0.1313 0.1413 0.1937 -0.0066 0.0125  -0.0025 114 GLU   B OE1 
5871 O OE2 . GLU   B 114 ? 0.1339 0.1462 0.2222 -0.0141 0.0134  0.0021  114 GLU   B OE2 
5878 N N   . ASN   B 115 ? 0.1252 0.1164 0.1622 0.0005  0.0022  -0.0017 115 ASN   B N   
5879 C CA  . ASN   B 115 ? 0.1259 0.1187 0.1536 -0.0040 0.0053  -0.0038 115 ASN   B CA  
5880 C C   . ASN   B 115 ? 0.1236 0.1175 0.1658 -0.0026 -0.0081 -0.0053 115 ASN   B C   
5881 O O   . ASN   B 115 ? 0.1320 0.1193 0.1725 -0.0061 -0.0026 -0.0010 115 ASN   B O   
5882 C CB  . ASN   B 115 ? 0.1349 0.1354 0.1655 -0.0077 0.0096  0.0032  115 ASN   B CB  
5883 C CG  . ASN   B 115 ? 0.1451 0.1382 0.1648 -0.0015 0.0010  -0.0039 115 ASN   B CG  
5884 O OD1 . ASN   B 115 ? 0.1805 0.1461 0.1907 -0.0080 0.0052  -0.0163 115 ASN   B OD1 
5885 N ND2 . ASN   B 115 ? 0.1411 0.1462 0.1597 -0.0000 0.0054  0.0000  115 ASN   B ND2 
5892 N N   . PHE   B 116 ? 0.1273 0.1174 0.1540 -0.0070 -0.0010 0.0011  116 PHE   B N   
5893 C CA  . PHE   B 116 ? 0.1291 0.1155 0.1595 -0.0084 -0.0020 0.0033  116 PHE   B CA  
5894 C C   . PHE   B 116 ? 0.1323 0.1068 0.1649 -0.0070 -0.0033 -0.0008 116 PHE   B C   
5895 O O   . PHE   B 116 ? 0.1376 0.1192 0.1691 0.0006  -0.0091 0.0006  116 PHE   B O   
5896 C CB  . PHE   B 116 ? 0.1281 0.1219 0.1607 -0.0040 -0.0089 0.0000  116 PHE   B CB  
5897 C CG  . PHE   B 116 ? 0.1228 0.1151 0.1662 -0.0079 -0.0098 -0.0014 116 PHE   B CG  
5898 C CD1 . PHE   B 116 ? 0.1280 0.1170 0.1716 -0.0023 -0.0029 -0.0012 116 PHE   B CD1 
5899 C CD2 . PHE   B 116 ? 0.1296 0.1231 0.1613 -0.0027 -0.0015 -0.0079 116 PHE   B CD2 
5900 C CE1 . PHE   B 116 ? 0.1317 0.1290 0.1726 -0.0028 -0.0066 0.0038  116 PHE   B CE1 
5901 C CE2 . PHE   B 116 ? 0.1315 0.1203 0.1693 -0.0005 -0.0006 -0.0049 116 PHE   B CE2 
5902 C CZ  . PHE   B 116 ? 0.1222 0.1287 0.1647 -0.0050 -0.0010 0.0012  116 PHE   B CZ  
5912 N N   . ASN   B 117 ? 0.1257 0.1152 0.1736 -0.0044 -0.0063 0.0040  117 ASN   B N   
5913 C CA  . ASN   B 117 ? 0.1335 0.1155 0.1706 -0.0003 -0.0131 -0.0022 117 ASN   B CA  
5914 C C   . ASN   B 117 ? 0.1423 0.1171 0.1864 0.0015  -0.0161 -0.0049 117 ASN   B C   
5915 O O   . ASN   B 117 ? 0.1491 0.1266 0.2146 -0.0010 -0.0390 0.0091  117 ASN   B O   
5916 C CB  . ASN   B 117 ? 0.1316 0.1227 0.1772 0.0078  -0.0136 -0.0053 117 ASN   B CB  
5917 C CG  . ASN   B 117 ? 0.1316 0.1262 0.1812 0.0041  -0.0129 -0.0036 117 ASN   B CG  
5918 O OD1 . ASN   B 117 ? 0.1531 0.1275 0.2000 -0.0099 0.0003  -0.0111 117 ASN   B OD1 
5919 N ND2 . ASN   B 117 ? 0.1378 0.1291 0.1826 0.0016  -0.0020 -0.0095 117 ASN   B ND2 
5926 N N   . GLN   B 118 ? 0.1393 0.1118 0.1859 -0.0032 -0.0151 -0.0026 118 GLN   B N   
5927 C CA  . GLN   B 118 ? 0.1431 0.1194 0.1882 0.0064  -0.0145 -0.0066 118 GLN   B CA  
5928 C C   . GLN   B 118 ? 0.1491 0.1161 0.1991 0.0030  -0.0136 -0.0008 118 GLN   B C   
5929 O O   . GLN   B 118 ? 0.1645 0.1161 0.2349 -0.0052 -0.0022 -0.0028 118 GLN   B O   
5930 C CB  . GLN   B 118 ? 0.1503 0.1224 0.2007 0.0043  -0.0189 -0.0057 118 GLN   B CB  
5931 C CG  . GLN   B 118 ? 0.1597 0.1304 0.1888 0.0088  -0.0134 -0.0155 118 GLN   B CG  
5932 C CD  . GLN   B 118 ? 0.1598 0.1246 0.1927 0.0053  -0.0180 -0.0171 118 GLN   B CD  
5933 O OE1 . GLN   B 118 ? 0.1678 0.1243 0.2162 0.0069  -0.0036 -0.0038 118 GLN   B OE1 
5934 N NE2 . GLN   B 118 ? 0.1689 0.1259 0.1933 0.0060  -0.0189 -0.0032 118 GLN   B NE2 
5943 N N   . HIS   B 119 ? 0.1491 0.1187 0.1671 -0.0071 -0.0119 0.0040  119 HIS   B N   
5944 C CA  . HIS   B 119 ? 0.1566 0.1252 0.1631 -0.0035 -0.0168 0.0031  119 HIS   B CA  
5945 C C   . HIS   B 119 ? 0.1574 0.1292 0.1623 -0.0024 -0.0234 0.0065  119 HIS   B C   
5946 O O   . HIS   B 119 ? 0.1714 0.1308 0.1783 -0.0242 -0.0172 0.0080  119 HIS   B O   
5947 C CB  . HIS   B 119 ? 0.1559 0.1393 0.1657 0.0036  -0.0149 0.0018  119 HIS   B CB  
5948 C CG  . HIS   B 119 ? 0.1643 0.1651 0.1893 0.0142  -0.0422 -0.0194 119 HIS   B CG  
5949 N ND1 . HIS   B 119 ? 0.1742 0.1770 0.2288 0.0099  -0.0510 -0.0383 119 HIS   B ND1 
5950 C CD2 . HIS   B 119 ? 0.1833 0.1869 0.1965 0.0375  -0.0461 -0.0202 119 HIS   B CD2 
5951 C CE1 . HIS   B 119 ? 0.1932 0.1930 0.2266 0.0228  -0.0584 -0.0472 119 HIS   B CE1 
5952 N NE2 . HIS   B 119 ? 0.1982 0.2037 0.2135 0.0363  -0.0463 -0.0386 119 HIS   B NE2 
5960 N N   . GLU   B 120 ? 0.1718 0.1298 0.1674 -0.0116 -0.0334 0.0116  120 GLU   B N   
5961 C CA  . GLU   B 120 ? 0.2008 0.1489 0.1774 -0.0003 -0.0447 0.0240  120 GLU   B CA  
5962 C C   . GLU   B 120 ? 0.1810 0.1366 0.1581 -0.0133 -0.0314 0.0224  120 GLU   B C   
5963 O O   . GLU   B 120 ? 0.1771 0.1474 0.1731 -0.0170 -0.0425 0.0137  120 GLU   B O   
5964 C CB  . GLU   B 120 ? 0.2641 0.1797 0.2452 0.0154  -0.0734 0.0535  120 GLU   B CB  
5965 C CG  . GLU   B 120 ? 0.3169 0.2505 0.3488 0.0248  -0.0952 0.0691  120 GLU   B CG  
5966 C CD  . GLU   B 120 ? 0.3663 0.3210 0.4465 0.0232  -0.1018 0.0850  120 GLU   B CD  
5967 O OE1 . GLU   B 120 ? 0.3835 0.3428 0.4802 0.0182  -0.0943 0.0969  120 GLU   B OE1 
5968 O OE2 . GLU   B 120 ? 0.3820 0.3454 0.4922 0.0216  -0.1002 0.0821  120 GLU   B OE2 
5975 N N   . VAL   B 121 ? 0.1755 0.1342 0.1559 -0.0160 -0.0184 0.0154  121 VAL   B N   
5976 C CA  . VAL   B 121 ? 0.1707 0.1445 0.1486 -0.0168 -0.0236 0.0092  121 VAL   B CA  
5977 C C   . VAL   B 121 ? 0.1633 0.1342 0.1558 -0.0218 -0.0182 0.0115  121 VAL   B C   
5978 O O   . VAL   B 121 ? 0.1738 0.1318 0.1595 -0.0260 -0.0255 0.0051  121 VAL   B O   
5979 C CB  . VAL   B 121 ? 0.1919 0.1799 0.1561 -0.0039 -0.0216 0.0186  121 VAL   B CB  
5980 C CG1 . VAL   B 121 ? 0.2033 0.1893 0.1778 -0.0122 -0.0083 0.0211  121 VAL   B CG1 
5981 C CG2 . VAL   B 121 ? 0.2125 0.2037 0.1706 0.0084  -0.0068 0.0061  121 VAL   B CG2 
5991 N N   . LEU   B 122 ? 0.1538 0.1305 0.1443 -0.0163 -0.0225 0.0094  122 LEU   B N   
5992 C CA  . LEU   B 122 ? 0.1462 0.1367 0.1353 -0.0183 -0.0165 0.0052  122 LEU   B CA  
5993 C C   . LEU   B 122 ? 0.1441 0.1204 0.1408 -0.0216 -0.0169 0.0074  122 LEU   B C   
5994 O O   . LEU   B 122 ? 0.1568 0.1295 0.1666 -0.0255 -0.0290 -0.0002 122 LEU   B O   
5995 C CB  . LEU   B 122 ? 0.1637 0.1470 0.1629 -0.0095 -0.0216 0.0175  122 LEU   B CB  
5996 C CG  . LEU   B 122 ? 0.1550 0.1537 0.1694 -0.0119 -0.0056 0.0106  122 LEU   B CG  
5997 C CD1 . LEU   B 122 ? 0.1564 0.1712 0.1740 -0.0145 -0.0159 0.0108  122 LEU   B CD1 
5998 C CD2 . LEU   B 122 ? 0.1468 0.1601 0.1506 -0.0051 -0.0050 0.0038  122 LEU   B CD2 
6010 N N   . LEU   B 123 ? 0.1477 0.1209 0.1373 -0.0185 -0.0167 0.0078  123 LEU   B N   
6011 C CA  . LEU   B 123 ? 0.1486 0.1186 0.1296 -0.0253 -0.0216 0.0058  123 LEU   B CA  
6012 C C   . LEU   B 123 ? 0.1374 0.1155 0.1256 -0.0224 -0.0135 -0.0017 123 LEU   B C   
6013 O O   . LEU   B 123 ? 0.1528 0.1243 0.1328 -0.0282 -0.0123 0.0008  123 LEU   B O   
6014 C CB  . LEU   B 123 ? 0.1506 0.1252 0.1455 -0.0257 -0.0104 -0.0036 123 LEU   B CB  
6015 C CG  . LEU   B 123 ? 0.1537 0.1305 0.1572 -0.0095 -0.0010 0.0071  123 LEU   B CG  
6016 C CD1 . LEU   B 123 ? 0.1589 0.1352 0.1613 -0.0117 0.0037  -0.0065 123 LEU   B CD1 
6017 C CD2 . LEU   B 123 ? 0.1567 0.1377 0.1732 -0.0124 0.0010  0.0127  123 LEU   B CD2 
6029 N N   . ALA   B 124 ? 0.1354 0.1196 0.1265 -0.0183 -0.0068 0.0007  124 ALA   B N   
6030 C CA  . ALA   B 124 ? 0.1345 0.1189 0.1369 -0.0129 -0.0066 -0.0043 124 ALA   B CA  
6031 C C   . ALA   B 124 ? 0.1308 0.1198 0.1308 -0.0183 -0.0073 -0.0059 124 ALA   B C   
6032 O O   . ALA   B 124 ? 0.1423 0.1251 0.1424 -0.0128 -0.0050 0.0046  124 ALA   B O   
6033 C CB  . ALA   B 124 ? 0.1493 0.1205 0.1398 -0.0100 0.0066  -0.0040 124 ALA   B CB  
6039 N N   . PRO   B 125 ? 0.1394 0.1253 0.1275 -0.0148 -0.0096 0.0034  125 PRO   B N   
6040 C CA  . PRO   B 125 ? 0.1439 0.1223 0.1449 -0.0132 -0.0092 0.0124  125 PRO   B CA  
6041 C C   . PRO   B 125 ? 0.1396 0.1206 0.1607 -0.0147 -0.0107 0.0039  125 PRO   B C   
6042 O O   . PRO   B 125 ? 0.1383 0.1185 0.1800 -0.0060 -0.0014 0.0057  125 PRO   B O   
6043 C CB  . PRO   B 125 ? 0.1544 0.1418 0.1657 -0.0175 -0.0178 0.0244  125 PRO   B CB  
6044 C CG  . PRO   B 125 ? 0.1565 0.1507 0.1506 -0.0266 -0.0177 0.0222  125 PRO   B CG  
6045 C CD  . PRO   B 125 ? 0.1507 0.1397 0.1384 -0.0253 -0.0043 0.0031  125 PRO   B CD  
6053 N N   . LEU   B 126 ? 0.1449 0.1180 0.1844 -0.0120 0.0086  0.0148  126 LEU   B N   
6054 C CA  . LEU   B 126 ? 0.1500 0.1229 0.1797 -0.0125 0.0154  0.0105  126 LEU   B CA  
6055 C C   . LEU   B 126 ? 0.1450 0.1305 0.1818 -0.0018 0.0109  0.0146  126 LEU   B C   
6056 O O   . LEU   B 126 ? 0.1660 0.1627 0.1969 0.0172  -0.0088 -0.0080 126 LEU   B O   
6057 C CB  . LEU   B 126 ? 0.1666 0.1286 0.2032 -0.0192 0.0251  0.0105  126 LEU   B CB  
6058 C CG  . LEU   B 126 ? 0.1843 0.1378 0.2163 -0.0253 0.0232  -0.0113 126 LEU   B CG  
6059 C CD1 . LEU   B 126 ? 0.2002 0.1420 0.2590 -0.0243 0.0192  -0.0126 126 LEU   B CD1 
6060 C CD2 . LEU   B 126 ? 0.1791 0.1491 0.2136 -0.0334 0.0082  -0.0146 126 LEU   B CD2 
6072 N N   . LEU   B 127 ? 0.1446 0.1216 0.1894 0.0006  0.0208  0.0070  127 LEU   B N   
6073 C CA  . LEU   B 127 ? 0.1475 0.1315 0.1919 -0.0091 0.0194  0.0123  127 LEU   B CA  
6074 C C   . LEU   B 127 ? 0.1420 0.1316 0.1898 -0.0032 0.0167  0.0125  127 LEU   B C   
6075 O O   . LEU   B 127 ? 0.1443 0.1363 0.1911 -0.0121 0.0097  0.0155  127 LEU   B O   
6076 C CB  . LEU   B 127 ? 0.1620 0.1338 0.1938 -0.0037 0.0258  0.0164  127 LEU   B CB  
6077 C CG  . LEU   B 127 ? 0.1690 0.1337 0.2032 -0.0018 0.0214  0.0086  127 LEU   B CG  
6078 C CD1 . LEU   B 127 ? 0.1775 0.1297 0.2074 0.0028  0.0118  -0.0008 127 LEU   B CD1 
6079 C CD2 . LEU   B 127 ? 0.1690 0.1469 0.2095 -0.0016 0.0212  0.0230  127 LEU   B CD2 
6091 N N   . SER   B 128 ? 0.1447 0.1276 0.1872 0.0016  0.0007  0.0122  128 SER   B N   
6092 C CA  . SER   B 128 ? 0.1601 0.1348 0.1837 0.0068  -0.0043 0.0168  128 SER   B CA  
6093 C C   . SER   B 128 ? 0.1731 0.1420 0.1982 0.0056  -0.0177 0.0155  128 SER   B C   
6094 O O   . SER   B 128 ? 0.1853 0.1460 0.2291 0.0053  -0.0120 0.0312  128 SER   B O   
6095 C CB  . SER   B 128 ? 0.1749 0.1372 0.1838 0.0046  0.0059  0.0218  128 SER   B CB  
6096 O OG  . SER   B 128 ? 0.1774 0.1477 0.1941 0.0130  0.0140  0.0259  128 SER   B OG  
6102 N N   . ALA   B 129 ? 0.1814 0.1462 0.2101 0.0247  -0.0120 0.0050  129 ALA   B N   
6103 C CA  . ALA   B 129 ? 0.2007 0.1487 0.2178 0.0292  -0.0039 -0.0032 129 ALA   B CA  
6104 C C   . ALA   B 129 ? 0.1900 0.1419 0.2142 0.0233  0.0127  -0.0030 129 ALA   B C   
6105 O O   . ALA   B 129 ? 0.1778 0.1494 0.2193 0.0198  -0.0029 0.0060  129 ALA   B O   
6106 C CB  . ALA   B 129 ? 0.2268 0.1705 0.2574 0.0356  0.0008  -0.0040 129 ALA   B CB  
6112 N N   . GLY   B 130 ? 0.1824 0.1440 0.2272 0.0278  0.0092  -0.0046 130 GLY   B N   
6113 C CA  . GLY   B 130 ? 0.1823 0.1507 0.2235 0.0267  0.0216  -0.0018 130 GLY   B CA  
6114 C C   . GLY   B 130 ? 0.1854 0.1523 0.2192 0.0178  0.0109  0.0026  130 GLY   B C   
6115 O O   . GLY   B 130 ? 0.1990 0.1613 0.2362 0.0191  -0.0008 0.0098  130 GLY   B O   
6119 N N   . ILE   B 131 ? 0.1850 0.1698 0.2232 0.0269  0.0077  0.0110  131 ILE   B N   
6120 C CA  . ILE   B 131 ? 0.1980 0.1881 0.2281 0.0278  -0.0075 0.0200  131 ILE   B CA  
6121 C C   . ILE   B 131 ? 0.2118 0.1817 0.1970 0.0202  -0.0111 0.0223  131 ILE   B C   
6122 O O   . ILE   B 131 ? 0.2374 0.2028 0.2080 0.0215  -0.0275 0.0287  131 ILE   B O   
6123 C CB  . ILE   B 131 ? 0.1928 0.2283 0.2612 0.0245  -0.0181 0.0250  131 ILE   B CB  
6124 C CG1 . ILE   B 131 ? 0.1986 0.2500 0.2669 -0.0038 -0.0080 0.0261  131 ILE   B CG1 
6125 C CG2 . ILE   B 131 ? 0.1962 0.2460 0.2871 0.0353  -0.0169 0.0130  131 ILE   B CG2 
6126 C CD1 . ILE   B 131 ? 0.2189 0.2676 0.2797 -0.0171 -0.0170 0.0329  131 ILE   B CD1 
6138 N N   . PHE   B 132 ? 0.1946 0.1601 0.1758 0.0150  0.0091  0.0167  132 PHE   B N   
6139 C CA  . PHE   B 132 ? 0.2072 0.1626 0.1839 0.0042  0.0275  0.0091  132 PHE   B CA  
6140 C C   . PHE   B 132 ? 0.2257 0.1766 0.1902 0.0044  0.0327  0.0090  132 PHE   B C   
6141 O O   . PHE   B 132 ? 0.2450 0.2013 0.2151 -0.0018 0.0486  0.0070  132 PHE   B O   
6142 C CB  . PHE   B 132 ? 0.1929 0.1579 0.1711 0.0117  0.0308  0.0178  132 PHE   B CB  
6143 C CG  . PHE   B 132 ? 0.1854 0.1601 0.1741 0.0179  0.0265  0.0195  132 PHE   B CG  
6144 C CD1 . PHE   B 132 ? 0.1981 0.1581 0.2079 0.0165  0.0353  0.0200  132 PHE   B CD1 
6145 C CD2 . PHE   B 132 ? 0.1866 0.1682 0.1528 0.0229  0.0250  0.0266  132 PHE   B CD2 
6146 C CE1 . PHE   B 132 ? 0.2009 0.1636 0.2242 0.0112  0.0334  0.0228  132 PHE   B CE1 
6147 C CE2 . PHE   B 132 ? 0.1949 0.1651 0.1672 0.0224  0.0230  0.0164  132 PHE   B CE2 
6148 C CZ  . PHE   B 132 ? 0.1992 0.1649 0.2058 0.0114  0.0174  0.0242  132 PHE   B CZ  
6158 N N   . GLY   B 133 ? 0.2243 0.1631 0.1894 -0.0001 0.0237  0.0291  133 GLY   B N   
6159 C CA  . GLY   B 133 ? 0.2381 0.1763 0.2008 -0.0160 0.0155  0.0411  133 GLY   B CA  
6160 C C   . GLY   B 133 ? 0.2404 0.1830 0.2096 -0.0266 0.0233  0.0451  133 GLY   B C   
6161 O O   . GLY   B 133 ? 0.2609 0.2026 0.2501 -0.0412 0.0235  0.0579  133 GLY   B O   
6165 N N   . ALA   B 134 ? 0.2223 0.1789 0.1992 -0.0291 0.0243  0.0262  134 ALA   B N   
6166 C CA  . ALA   B 134 ? 0.2192 0.1792 0.2155 -0.0228 0.0196  0.0072  134 ALA   B CA  
6167 C C   . ALA   B 134 ? 0.2268 0.1662 0.2148 -0.0144 0.0209  0.0161  134 ALA   B C   
6168 O O   . ALA   B 134 ? 0.2322 0.1864 0.2277 -0.0065 0.0206  0.0094  134 ALA   B O   
6169 C CB  . ALA   B 134 ? 0.2106 0.1875 0.2363 -0.0183 0.0198  0.0034  134 ALA   B CB  
6175 N N   . ASP   B 135 ? 0.2399 0.1618 0.2165 -0.0222 0.0082  0.0220  135 ASP   B N   
6176 C CA  . ASP   B 135 ? 0.2530 0.1534 0.2309 -0.0153 -0.0057 0.0220  135 ASP   B CA  
6177 C C   . ASP   B 135 ? 0.2345 0.1388 0.2129 -0.0028 -0.0025 0.0209  135 ASP   B C   
6178 O O   . ASP   B 135 ? 0.2244 0.1375 0.2237 -0.0051 0.0012  0.0250  135 ASP   B O   
6179 C CB  . ASP   B 135 ? 0.2839 0.1666 0.2513 -0.0334 -0.0089 0.0280  135 ASP   B CB  
6180 C CG  . ASP   B 135 ? 0.3106 0.1700 0.2968 -0.0563 -0.0038 0.0257  135 ASP   B CG  
6181 O OD1 . ASP   B 135 ? 0.3208 0.1610 0.2908 -0.0407 -0.0126 0.0208  135 ASP   B OD1 
6182 O OD2 . ASP   B 135 ? 0.3309 0.2072 0.3584 -0.0685 -0.0012 0.0055  135 ASP   B OD2 
6187 N N   . PRO   B 136 ? 0.2262 0.1490 0.2232 0.0138  -0.0161 0.0129  136 PRO   B N   
6188 C CA  . PRO   B 136 ? 0.2054 0.1402 0.2237 0.0175  -0.0147 0.0039  136 PRO   B CA  
6189 C C   . PRO   B 136 ? 0.1892 0.1303 0.2253 0.0120  -0.0060 0.0009  136 PRO   B C   
6190 O O   . PRO   B 136 ? 0.1687 0.1274 0.2208 0.0086  -0.0015 0.0010  136 PRO   B O   
6191 C CB  . PRO   B 136 ? 0.2136 0.1644 0.2320 0.0318  -0.0150 -0.0066 136 PRO   B CB  
6192 C CG  . PRO   B 136 ? 0.2350 0.1750 0.2554 0.0336  -0.0150 -0.0004 136 PRO   B CG  
6193 C CD  . PRO   B 136 ? 0.2324 0.1646 0.2457 0.0339  -0.0115 0.0136  136 PRO   B CD  
6201 N N   . ILE   B 137 ? 0.1981 0.1256 0.2382 0.0151  -0.0068 0.0022  137 ILE   B N   
6202 C CA  . ILE   B 137 ? 0.2026 0.1297 0.2527 -0.0080 -0.0028 -0.0018 137 ILE   B CA  
6203 C C   . ILE   B 137 ? 0.1861 0.1305 0.2391 -0.0087 0.0060  0.0079  137 ILE   B C   
6204 O O   . ILE   B 137 ? 0.1787 0.1331 0.2418 -0.0103 0.0010  0.0034  137 ILE   B O   
6205 C CB  . ILE   B 137 ? 0.2327 0.1321 0.3030 -0.0038 -0.0102 -0.0048 137 ILE   B CB  
6206 C CG1 . ILE   B 137 ? 0.2557 0.1451 0.3577 0.0039  -0.0074 -0.0179 137 ILE   B CG1 
6207 C CG2 . ILE   B 137 ? 0.2367 0.1344 0.3134 -0.0306 -0.0080 0.0025  137 ILE   B CG2 
6208 C CD1 . ILE   B 137 ? 0.2741 0.1744 0.4035 0.0145  -0.0077 -0.0111 137 ILE   B CD1 
6220 N N   . HIS   B 138 ? 0.1976 0.1346 0.2317 -0.0020 0.0158  0.0169  138 HIS   B N   
6221 C CA  . HIS   B 138 ? 0.2028 0.1406 0.2268 -0.0021 0.0255  0.0124  138 HIS   B CA  
6222 C C   . HIS   B 138 ? 0.1845 0.1370 0.2338 -0.0052 0.0282  0.0195  138 HIS   B C   
6223 O O   . HIS   B 138 ? 0.1772 0.1462 0.2490 0.0011  0.0264  0.0273  138 HIS   B O   
6224 C CB  . HIS   B 138 ? 0.2252 0.1512 0.2435 -0.0006 0.0396  0.0077  138 HIS   B CB  
6225 C CG  . HIS   B 138 ? 0.2428 0.1715 0.2530 -0.0068 0.0594  0.0209  138 HIS   B CG  
6226 N ND1 . HIS   B 138 ? 0.2494 0.1924 0.2705 -0.0057 0.0759  0.0150  138 HIS   B ND1 
6227 C CD2 . HIS   B 138 ? 0.2536 0.1821 0.2422 -0.0087 0.0624  0.0099  138 HIS   B CD2 
6228 C CE1 . HIS   B 138 ? 0.2559 0.1934 0.2709 -0.0069 0.0737  0.0134  138 HIS   B CE1 
6229 N NE2 . HIS   B 138 ? 0.2610 0.1844 0.2487 -0.0017 0.0683  0.0060  138 HIS   B NE2 
6237 N N   . SER   B 139 ? 0.1769 0.1253 0.2326 0.0045  0.0217  0.0088  139 SER   B N   
6238 C CA  . SER   B 139 ? 0.1726 0.1204 0.2122 0.0029  0.0201  -0.0046 139 SER   B CA  
6239 C C   . SER   B 139 ? 0.1539 0.1209 0.1969 -0.0032 0.0122  -0.0004 139 SER   B C   
6240 O O   . SER   B 139 ? 0.1526 0.1160 0.2112 -0.0013 0.0037  0.0041  139 SER   B O   
6241 C CB  . SER   B 139 ? 0.1808 0.1198 0.2134 0.0029  0.0097  0.0035  139 SER   B CB  
6242 O OG  . SER   B 139 ? 0.1840 0.1245 0.2180 -0.0032 -0.0050 0.0149  139 SER   B OG  
6248 N N   . LEU   B 140 ? 0.1479 0.1126 0.2014 -0.0061 0.0114  -0.0019 140 LEU   B N   
6249 C CA  . LEU   B 140 ? 0.1481 0.1190 0.2024 -0.0010 0.0055  0.0032  140 LEU   B CA  
6250 C C   . LEU   B 140 ? 0.1459 0.1233 0.2106 -0.0036 0.0003  0.0007  140 LEU   B C   
6251 O O   . LEU   B 140 ? 0.1449 0.1245 0.2193 -0.0005 -0.0072 0.0058  140 LEU   B O   
6252 C CB  . LEU   B 140 ? 0.1456 0.1185 0.2160 -0.0103 0.0101  -0.0059 140 LEU   B CB  
6253 C CG  . LEU   B 140 ? 0.1585 0.1209 0.2078 -0.0117 0.0016  0.0009  140 LEU   B CG  
6254 C CD1 . LEU   B 140 ? 0.1718 0.1300 0.2296 -0.0085 0.0027  -0.0047 140 LEU   B CD1 
6255 C CD2 . LEU   B 140 ? 0.1767 0.1274 0.2125 -0.0082 -0.0004 -0.0104 140 LEU   B CD2 
6267 N N   . ARG   B 141 ? 0.1443 0.1191 0.2363 -0.0061 0.0125  -0.0031 141 ARG   B N   
6268 C CA  . ARG   B 141 ? 0.1435 0.1201 0.2785 -0.0120 0.0236  -0.0033 141 ARG   B CA  
6269 C C   . ARG   B 141 ? 0.1379 0.1231 0.2587 -0.0128 0.0122  -0.0017 141 ARG   B C   
6270 O O   . ARG   B 141 ? 0.1456 0.1240 0.2508 -0.0114 0.0002  -0.0185 141 ARG   B O   
6271 C CB  . ARG   B 141 ? 0.1634 0.1345 0.3096 -0.0170 0.0380  -0.0019 141 ARG   B CB  
6272 C CG  . ARG   B 141 ? 0.1948 0.1665 0.3398 -0.0264 0.0450  0.0025  141 ARG   B CG  
6273 C CD  . ARG   B 141 ? 0.2465 0.1876 0.3400 -0.0192 0.0406  -0.0136 141 ARG   B CD  
6274 N NE  . ARG   B 141 ? 0.2820 0.1890 0.3374 -0.0372 0.0524  -0.0203 141 ARG   B NE  
6275 C CZ  . ARG   B 141 ? 0.2946 0.1661 0.3278 -0.0352 0.0628  -0.0374 141 ARG   B CZ  
6276 N NH1 . ARG   B 141 ? 0.3154 0.1627 0.3175 -0.0318 0.0636  -0.0368 141 ARG   B NH1 
6277 N NH2 . ARG   B 141 ? 0.3141 0.1801 0.3432 -0.0137 0.0475  -0.0288 141 ARG   B NH2 
6291 N N   . VAL   B 142 ? 0.1414 0.1190 0.2389 -0.0094 0.0094  -0.0068 142 VAL   B N   
6292 C CA  . VAL   B 142 ? 0.1452 0.1220 0.2364 -0.0044 0.0179  -0.0044 142 VAL   B CA  
6293 C C   . VAL   B 142 ? 0.1390 0.1190 0.2406 0.0035  0.0161  -0.0090 142 VAL   B C   
6294 O O   . VAL   B 142 ? 0.1439 0.1221 0.2567 0.0020  0.0080  -0.0052 142 VAL   B O   
6295 C CB  . VAL   B 142 ? 0.1495 0.1277 0.2353 0.0006  0.0264  0.0059  142 VAL   B CB  
6296 C CG1 . VAL   B 142 ? 0.1546 0.1308 0.2478 0.0074  0.0262  -0.0039 142 VAL   B CG1 
6297 C CG2 . VAL   B 142 ? 0.1743 0.1300 0.2419 0.0035  0.0293  0.0073  142 VAL   B CG2 
6307 N N   . CYS   B 143 ? 0.1321 0.1211 0.2279 0.0002  0.0116  0.0007  143 CYS   B N   
6308 C CA  . CYS   B 143 ? 0.1350 0.1203 0.2285 -0.0052 0.0121  -0.0031 143 CYS   B CA  
6309 C C   . CYS   B 143 ? 0.1309 0.1208 0.2321 -0.0045 0.0067  -0.0020 143 CYS   B C   
6310 O O   . CYS   B 143 ? 0.1363 0.1228 0.2284 -0.0041 0.0004  -0.0029 143 CYS   B O   
6311 C CB  . CYS   B 143 ? 0.1372 0.1255 0.2220 -0.0079 0.0054  -0.0055 143 CYS   B CB  
6312 S SG  . CYS   B 143 ? 0.1417 0.1428 0.2108 -0.0037 0.0039  0.0018  143 CYS   B SG  
6318 N N   . VAL   B 144 ? 0.1345 0.1206 0.2403 -0.0049 -0.0052 -0.0005 144 VAL   B N   
6319 C CA  . VAL   B 144 ? 0.1433 0.1320 0.2590 -0.0134 -0.0063 -0.0162 144 VAL   B CA  
6320 C C   . VAL   B 144 ? 0.1419 0.1356 0.2601 -0.0089 -0.0093 0.0020  144 VAL   B C   
6321 O O   . VAL   B 144 ? 0.1524 0.1599 0.2781 0.0050  -0.0030 0.0204  144 VAL   B O   
6322 C CB  . VAL   B 144 ? 0.1681 0.1506 0.3183 -0.0088 -0.0204 -0.0271 144 VAL   B CB  
6323 C CG1 . VAL   B 144 ? 0.1942 0.1988 0.3453 -0.0046 -0.0276 -0.0163 144 VAL   B CG1 
6324 C CG2 . VAL   B 144 ? 0.1843 0.1446 0.3157 0.0002  -0.0378 -0.0421 144 VAL   B CG2 
6334 N N   . ASP   B 145 ? 0.1391 0.1301 0.2677 -0.0080 -0.0063 -0.0141 145 ASP   B N   
6335 C CA  . ASP   B 145 ? 0.1397 0.1385 0.2920 -0.0032 0.0009  -0.0119 145 ASP   B CA  
6336 C C   . ASP   B 145 ? 0.1340 0.1354 0.2887 -0.0052 -0.0015 -0.0044 145 ASP   B C   
6337 O O   . ASP   B 145 ? 0.1344 0.1474 0.3439 -0.0059 0.0092  -0.0245 145 ASP   B O   
6338 C CB  . ASP   B 145 ? 0.1514 0.1450 0.3380 -0.0113 0.0234  0.0014  145 ASP   B CB  
6339 C CG  . ASP   B 145 ? 0.1695 0.1474 0.3803 -0.0260 0.0282  0.0022  145 ASP   B CG  
6340 O OD1 . ASP   B 145 ? 0.1735 0.1503 0.3898 -0.0244 -0.0077 -0.0094 145 ASP   B OD1 
6341 O OD2 . ASP   B 145 ? 0.2053 0.1566 0.4117 -0.0310 0.0474  0.0055  145 ASP   B OD2 
6346 N N   . THR   B 146 ? 0.1284 0.1226 0.2443 -0.0076 0.0012  -0.0009 146 THR   B N   
6347 C CA  . THR   B 146 ? 0.1356 0.1197 0.2309 -0.0056 0.0075  -0.0013 146 THR   B CA  
6348 C C   . THR   B 146 ? 0.1355 0.1193 0.2154 -0.0050 0.0038  -0.0036 146 THR   B C   
6349 O O   . THR   B 146 ? 0.1442 0.1232 0.2286 -0.0018 0.0029  -0.0020 146 THR   B O   
6350 C CB  . THR   B 146 ? 0.1411 0.1187 0.2296 -0.0015 0.0118  -0.0014 146 THR   B CB  
6351 O OG1 . THR   B 146 ? 0.1421 0.1205 0.2407 -0.0043 0.0212  0.0019  146 THR   B OG1 
6352 C CG2 . THR   B 146 ? 0.1515 0.1314 0.2230 0.0026  0.0108  -0.0017 146 THR   B CG2 
6360 N N   . VAL   B 147 ? 0.1425 0.1215 0.1978 -0.0045 0.0078  -0.0026 147 VAL   B N   
6361 C CA  . VAL   B 147 ? 0.1421 0.1269 0.1960 -0.0076 -0.0065 -0.0018 147 VAL   B CA  
6362 C C   . VAL   B 147 ? 0.1371 0.1247 0.2018 -0.0153 -0.0121 -0.0064 147 VAL   B C   
6363 O O   . VAL   B 147 ? 0.1514 0.1320 0.2097 -0.0134 -0.0259 -0.0171 147 VAL   B O   
6364 C CB  . VAL   B 147 ? 0.1444 0.1321 0.1796 -0.0068 -0.0079 -0.0061 147 VAL   B CB  
6365 C CG1 . VAL   B 147 ? 0.1420 0.1399 0.1801 -0.0067 -0.0062 -0.0008 147 VAL   B CG1 
6366 C CG2 . VAL   B 147 ? 0.1503 0.1366 0.1855 -0.0074 -0.0005 -0.0025 147 VAL   B CG2 
6376 N N   . ARG   B 148 ? 0.1379 0.1246 0.1947 -0.0105 -0.0130 -0.0143 148 ARG   B N   
6377 C CA  . ARG   B 148 ? 0.1442 0.1333 0.2030 -0.0061 -0.0270 -0.0149 148 ARG   B CA  
6378 C C   . ARG   B 148 ? 0.1515 0.1448 0.1942 -0.0094 -0.0307 -0.0043 148 ARG   B C   
6379 O O   . ARG   B 148 ? 0.1688 0.1719 0.1991 -0.0224 -0.0387 -0.0014 148 ARG   B O   
6380 C CB  . ARG   B 148 ? 0.1502 0.1434 0.2145 -0.0007 -0.0285 -0.0235 148 ARG   B CB  
6381 C CG  . ARG   B 148 ? 0.1481 0.1626 0.2103 -0.0035 -0.0281 -0.0378 148 ARG   B CG  
6382 C CD  . ARG   B 148 ? 0.1590 0.1827 0.2195 0.0112  -0.0322 -0.0466 148 ARG   B CD  
6383 N NE  . ARG   B 148 ? 0.1613 0.1852 0.2128 0.0311  -0.0282 -0.0372 148 ARG   B NE  
6384 C CZ  . ARG   B 148 ? 0.1574 0.1723 0.1939 0.0211  -0.0237 -0.0279 148 ARG   B CZ  
6385 N NH1 . ARG   B 148 ? 0.1511 0.1723 0.2034 0.0005  -0.0077 -0.0176 148 ARG   B NH1 
6386 N NH2 . ARG   B 148 ? 0.1797 0.1509 0.2026 0.0250  -0.0237 -0.0200 148 ARG   B NH2 
6400 N N   . THR   B 149 ? 0.1524 0.1377 0.1803 -0.0098 -0.0279 -0.0006 149 THR   B N   
6401 C CA  . THR   B 149 ? 0.1605 0.1390 0.1711 -0.0105 -0.0195 0.0059  149 THR   B CA  
6402 C C   . THR   B 149 ? 0.1604 0.1360 0.1661 -0.0161 -0.0226 0.0008  149 THR   B C   
6403 O O   . THR   B 149 ? 0.1651 0.1378 0.1814 -0.0180 -0.0172 0.0022  149 THR   B O   
6404 C CB  . THR   B 149 ? 0.1588 0.1366 0.1805 -0.0137 -0.0240 0.0034  149 THR   B CB  
6405 O OG1 . THR   B 149 ? 0.1568 0.1400 0.1847 -0.0194 -0.0271 -0.0038 149 THR   B OG1 
6406 C CG2 . THR   B 149 ? 0.1666 0.1431 0.2044 -0.0031 -0.0213 0.0077  149 THR   B CG2 
6414 N N   . ASN   B 150 ? 0.1678 0.1343 0.1617 -0.0112 -0.0303 0.0011  150 ASN   B N   
6415 C CA  . ASN   B 150 ? 0.1740 0.1528 0.1600 -0.0197 -0.0263 -0.0011 150 ASN   B CA  
6416 C C   . ASN   B 150 ? 0.1624 0.1443 0.1654 -0.0138 -0.0243 -0.0026 150 ASN   B C   
6417 O O   . ASN   B 150 ? 0.1693 0.1404 0.1972 -0.0278 -0.0417 0.0003  150 ASN   B O   
6418 C CB  . ASN   B 150 ? 0.1941 0.1798 0.1726 -0.0171 -0.0343 0.0131  150 ASN   B CB  
6419 C CG  . ASN   B 150 ? 0.2227 0.2266 0.2046 -0.0170 -0.0454 0.0239  150 ASN   B CG  
6420 O OD1 . ASN   B 150 ? 0.2323 0.2480 0.2197 -0.0264 -0.0691 0.0220  150 ASN   B OD1 
6421 N ND2 . ASN   B 150 ? 0.2389 0.2481 0.2403 -0.0080 -0.0465 0.0602  150 ASN   B ND2 
6428 N N   . VAL   B 151 ? 0.1535 0.1392 0.1616 -0.0192 -0.0223 -0.0025 151 VAL   B N   
6429 C CA  . VAL   B 151 ? 0.1471 0.1407 0.1587 -0.0181 -0.0215 0.0019  151 VAL   B CA  
6430 C C   . VAL   B 151 ? 0.1521 0.1351 0.1618 -0.0240 -0.0256 0.0000  151 VAL   B C   
6431 O O   . VAL   B 151 ? 0.1570 0.1419 0.1869 -0.0241 -0.0241 -0.0143 151 VAL   B O   
6432 C CB  . VAL   B 151 ? 0.1729 0.1536 0.1779 0.0004  -0.0162 -0.0058 151 VAL   B CB  
6433 C CG1 . VAL   B 151 ? 0.1862 0.1557 0.1997 -0.0083 -0.0102 -0.0168 151 VAL   B CG1 
6434 C CG2 . VAL   B 151 ? 0.1812 0.1696 0.1648 0.0086  -0.0155 0.0059  151 VAL   B CG2 
6444 N N   . TYR   B 152 ? 0.1522 0.1264 0.1527 -0.0242 -0.0209 -0.0058 152 TYR   B N   
6445 C CA  . TYR   B 152 ? 0.1540 0.1404 0.1376 -0.0264 -0.0169 -0.0100 152 TYR   B CA  
6446 C C   . TYR   B 152 ? 0.1520 0.1265 0.1323 -0.0181 -0.0064 -0.0071 152 TYR   B C   
6447 O O   . TYR   B 152 ? 0.1592 0.1292 0.1532 -0.0247 -0.0176 -0.0028 152 TYR   B O   
6448 C CB  . TYR   B 152 ? 0.1668 0.1547 0.1411 -0.0254 -0.0094 0.0048  152 TYR   B CB  
6449 C CG  . TYR   B 152 ? 0.1793 0.1614 0.1447 -0.0330 -0.0170 0.0071  152 TYR   B CG  
6450 C CD1 . TYR   B 152 ? 0.1936 0.1722 0.1464 -0.0256 -0.0201 0.0097  152 TYR   B CD1 
6451 C CD2 . TYR   B 152 ? 0.2006 0.1767 0.1480 -0.0319 -0.0112 0.0054  152 TYR   B CD2 
6452 C CE1 . TYR   B 152 ? 0.2160 0.1933 0.1541 -0.0205 -0.0294 0.0195  152 TYR   B CE1 
6453 C CE2 . TYR   B 152 ? 0.2189 0.1979 0.1537 -0.0279 -0.0158 0.0079  152 TYR   B CE2 
6454 C CZ  . TYR   B 152 ? 0.2249 0.2138 0.1430 -0.0240 -0.0408 0.0219  152 TYR   B CZ  
6455 O OH  . TYR   B 152 ? 0.2498 0.2491 0.1738 -0.0143 -0.0507 0.0185  152 TYR   B OH  
6465 N N   . LEU   B 153 ? 0.1517 0.1243 0.1466 -0.0241 -0.0162 -0.0067 153 LEU   B N   
6466 C CA  . LEU   B 153 ? 0.1507 0.1226 0.1324 -0.0168 -0.0090 -0.0073 153 LEU   B CA  
6467 C C   . LEU   B 153 ? 0.1544 0.1225 0.1404 -0.0218 -0.0046 -0.0142 153 LEU   B C   
6468 O O   . LEU   B 153 ? 0.1565 0.1437 0.1614 -0.0130 -0.0095 -0.0271 153 LEU   B O   
6469 C CB  . LEU   B 153 ? 0.1508 0.1235 0.1448 -0.0195 -0.0060 -0.0065 153 LEU   B CB  
6470 C CG  . LEU   B 153 ? 0.1522 0.1335 0.1687 -0.0202 0.0004  -0.0032 153 LEU   B CG  
6471 C CD1 . LEU   B 153 ? 0.1538 0.1424 0.1792 -0.0275 -0.0015 0.0047  153 LEU   B CD1 
6472 C CD2 . LEU   B 153 ? 0.1520 0.1473 0.1849 -0.0250 0.0058  -0.0027 153 LEU   B CD2 
6484 N N   . ALA   B 154 ? 0.1496 0.1222 0.1539 -0.0069 -0.0105 -0.0102 154 ALA   B N   
6485 C CA  . ALA   B 154 ? 0.1580 0.1300 0.1725 0.0003  -0.0120 -0.0187 154 ALA   B CA  
6486 C C   . ALA   B 154 ? 0.1668 0.1353 0.1756 -0.0020 -0.0224 -0.0233 154 ALA   B C   
6487 O O   . ALA   B 154 ? 0.2030 0.1413 0.1933 0.0056  -0.0093 -0.0095 154 ALA   B O   
6488 C CB  . ALA   B 154 ? 0.1551 0.1492 0.2151 -0.0050 -0.0134 -0.0256 154 ALA   B CB  
6494 N N   . VAL   B 155 ? 0.1429 0.1282 0.1903 -0.0026 -0.0061 -0.0092 155 VAL   B N   
6495 C CA  . VAL   B 155 ? 0.1338 0.1334 0.2062 -0.0035 -0.0111 -0.0030 155 VAL   B CA  
6496 C C   . VAL   B 155 ? 0.1402 0.1337 0.1909 -0.0034 -0.0169 -0.0172 155 VAL   B C   
6497 O O   . VAL   B 155 ? 0.1601 0.1536 0.2199 0.0101  -0.0135 -0.0374 155 VAL   B O   
6498 C CB  . VAL   B 155 ? 0.1407 0.1424 0.2496 -0.0072 -0.0153 0.0031  155 VAL   B CB  
6499 C CG1 . VAL   B 155 ? 0.1487 0.1338 0.2508 -0.0115 -0.0195 0.0041  155 VAL   B CG1 
6500 C CG2 . VAL   B 155 ? 0.1372 0.1563 0.2843 -0.0041 -0.0141 0.0278  155 VAL   B CG2 
6510 N N   . PHE   B 156 ? 0.1335 0.1387 0.2088 0.0053  -0.0092 -0.0164 156 PHE   B N   
6511 C CA  . PHE   B 156 ? 0.1408 0.1490 0.2411 0.0090  -0.0099 -0.0198 156 PHE   B CA  
6512 C C   . PHE   B 156 ? 0.1425 0.1477 0.2710 0.0132  -0.0160 -0.0379 156 PHE   B C   
6513 O O   . PHE   B 156 ? 0.1640 0.1659 0.3005 0.0313  -0.0061 -0.0385 156 PHE   B O   
6514 C CB  . PHE   B 156 ? 0.1403 0.1431 0.2349 0.0035  -0.0158 -0.0102 156 PHE   B CB  
6515 C CG  . PHE   B 156 ? 0.1441 0.1541 0.2448 0.0026  -0.0143 0.0112  156 PHE   B CG  
6516 C CD1 . PHE   B 156 ? 0.1543 0.1803 0.2831 0.0093  -0.0057 0.0362  156 PHE   B CD1 
6517 C CD2 . PHE   B 156 ? 0.1488 0.1675 0.2371 0.0114  -0.0196 0.0100  156 PHE   B CD2 
6518 C CE1 . PHE   B 156 ? 0.1610 0.2000 0.2979 0.0066  -0.0036 0.0345  156 PHE   B CE1 
6519 C CE2 . PHE   B 156 ? 0.1572 0.1867 0.2711 0.0137  -0.0128 0.0166  156 PHE   B CE2 
6520 C CZ  . PHE   B 156 ? 0.1501 0.1981 0.2883 0.0128  -0.0182 0.0207  156 PHE   B CZ  
6530 N N   . ASP   B 157 ? 0.1407 0.1417 0.2963 0.0106  -0.0244 -0.0231 157 ASP   B N   
6531 C CA  . ASP   B 157 ? 0.1509 0.1471 0.3289 0.0092  -0.0352 -0.0243 157 ASP   B CA  
6532 C C   . ASP   B 157 ? 0.1502 0.1441 0.3309 0.0108  -0.0252 -0.0487 157 ASP   B C   
6533 O O   . ASP   B 157 ? 0.1437 0.1440 0.3158 0.0084  -0.0228 -0.0368 157 ASP   B O   
6534 C CB  . ASP   B 157 ? 0.1718 0.1647 0.3452 0.0005  -0.0498 -0.0098 157 ASP   B CB  
6535 C CG  . ASP   B 157 ? 0.2119 0.1837 0.3703 0.0022  -0.0360 -0.0117 157 ASP   B CG  
6536 O OD1 . ASP   B 157 ? 0.2204 0.1818 0.3926 0.0164  -0.0277 -0.0089 157 ASP   B OD1 
6537 O OD2 . ASP   B 157 ? 0.2440 0.2092 0.3907 -0.0017 -0.0171 -0.0049 157 ASP   B OD2 
6542 N N   . LYS   B 158 ? 0.1508 0.1674 0.3381 0.0096  -0.0089 -0.0676 158 LYS   B N   
6543 C CA  . LYS   B 158 ? 0.1620 0.1900 0.3452 0.0069  0.0054  -0.0833 158 LYS   B CA  
6544 C C   . LYS   B 158 ? 0.1602 0.1705 0.3453 0.0070  0.0026  -0.0756 158 LYS   B C   
6545 O O   . LYS   B 158 ? 0.1652 0.1722 0.3440 -0.0037 -0.0002 -0.0822 158 LYS   B O   
6546 C CB  . LYS   B 158 ? 0.1838 0.2355 0.3479 0.0057  0.0190  -0.1074 158 LYS   B CB  
6547 C CG  . LYS   B 158 ? 0.2164 0.2874 0.3578 0.0061  0.0275  -0.1278 158 LYS   B CG  
6548 C CD  . LYS   B 158 ? 0.2443 0.3471 0.3730 0.0048  0.0363  -0.1288 158 LYS   B CD  
6549 C CE  . LYS   B 158 ? 0.2644 0.3790 0.3898 0.0121  0.0422  -0.1278 158 LYS   B CE  
6550 N NZ  . LYS   B 158 ? 0.2554 0.4043 0.3916 0.0150  0.0484  -0.1252 158 LYS   B NZ  
6564 N N   . ASN   B 159 ? 0.1677 0.1668 0.3633 0.0077  -0.0170 -0.0624 159 ASN   B N   
6565 C CA  . ASN   B 159 ? 0.1820 0.1600 0.3721 0.0136  -0.0399 -0.0537 159 ASN   B CA  
6566 C C   . ASN   B 159 ? 0.1694 0.1450 0.3526 0.0115  -0.0479 -0.0415 159 ASN   B C   
6567 O O   . ASN   B 159 ? 0.1726 0.1416 0.3622 -0.0036 -0.0483 -0.0304 159 ASN   B O   
6568 C CB  . ASN   B 159 ? 0.2003 0.1751 0.3958 0.0234  -0.0411 -0.0455 159 ASN   B CB  
6569 C CG  . ASN   B 159 ? 0.2280 0.1939 0.4205 0.0327  -0.0466 -0.0603 159 ASN   B CG  
6570 O OD1 . ASN   B 159 ? 0.2427 0.2072 0.4323 0.0424  -0.0403 -0.0662 159 ASN   B OD1 
6571 N ND2 . ASN   B 159 ? 0.2282 0.2016 0.4345 0.0356  -0.0544 -0.0560 159 ASN   B ND2 
6578 N N   . LEU   B 160 ? 0.1590 0.1473 0.3387 0.0090  -0.0443 -0.0424 160 LEU   B N   
6579 C CA  . LEU   B 160 ? 0.1469 0.1460 0.3056 0.0138  -0.0396 -0.0201 160 LEU   B CA  
6580 C C   . LEU   B 160 ? 0.1431 0.1415 0.2911 0.0033  -0.0247 -0.0248 160 LEU   B C   
6581 O O   . LEU   B 160 ? 0.1370 0.1420 0.2800 -0.0006 -0.0255 -0.0159 160 LEU   B O   
6582 C CB  . LEU   B 160 ? 0.1517 0.1548 0.2954 0.0103  -0.0332 -0.0155 160 LEU   B CB  
6583 C CG  . LEU   B 160 ? 0.1551 0.1690 0.2763 0.0115  -0.0318 -0.0101 160 LEU   B CG  
6584 C CD1 . LEU   B 160 ? 0.1693 0.1851 0.2849 -0.0052 -0.0107 -0.0059 160 LEU   B CD1 
6585 C CD2 . LEU   B 160 ? 0.1600 0.1727 0.2778 0.0102  -0.0336 -0.0175 160 LEU   B CD2 
6597 N N   . TYR   B 161 ? 0.1405 0.1488 0.2865 -0.0038 -0.0085 -0.0446 161 TYR   B N   
6598 C CA  . TYR   B 161 ? 0.1496 0.1439 0.2760 -0.0117 0.0092  -0.0515 161 TYR   B CA  
6599 C C   . TYR   B 161 ? 0.1537 0.1456 0.2779 -0.0146 0.0187  -0.0402 161 TYR   B C   
6600 O O   . TYR   B 161 ? 0.1634 0.1422 0.2598 -0.0150 0.0065  -0.0392 161 TYR   B O   
6601 C CB  . TYR   B 161 ? 0.1689 0.1575 0.2770 -0.0228 0.0292  -0.0585 161 TYR   B CB  
6602 C CG  . TYR   B 161 ? 0.1969 0.1580 0.2729 -0.0280 0.0327  -0.0545 161 TYR   B CG  
6603 C CD1 . TYR   B 161 ? 0.2057 0.1525 0.2663 -0.0405 0.0347  -0.0513 161 TYR   B CD1 
6604 C CD2 . TYR   B 161 ? 0.2206 0.1676 0.2751 -0.0248 0.0271  -0.0563 161 TYR   B CD2 
6605 C CE1 . TYR   B 161 ? 0.2245 0.1701 0.2672 -0.0393 0.0376  -0.0449 161 TYR   B CE1 
6606 C CE2 . TYR   B 161 ? 0.2403 0.1774 0.2795 -0.0338 0.0340  -0.0469 161 TYR   B CE2 
6607 C CZ  . TYR   B 161 ? 0.2385 0.1856 0.2688 -0.0463 0.0375  -0.0368 161 TYR   B CZ  
6608 O OH  . TYR   B 161 ? 0.2654 0.2150 0.2912 -0.0445 0.0332  -0.0360 161 TYR   B OH  
6618 N N   . ASP   B 162 ? 0.1614 0.1475 0.3011 -0.0076 0.0063  -0.0558 162 ASP   B N   
6619 C CA  . ASP   B 162 ? 0.1723 0.1505 0.3056 -0.0026 -0.0052 -0.0586 162 ASP   B CA  
6620 C C   . ASP   B 162 ? 0.1710 0.1420 0.2914 -0.0081 -0.0104 -0.0481 162 ASP   B C   
6621 O O   . ASP   B 162 ? 0.1751 0.1489 0.2883 -0.0174 -0.0194 -0.0333 162 ASP   B O   
6622 C CB  . ASP   B 162 ? 0.1926 0.1642 0.3232 0.0019  -0.0049 -0.0764 162 ASP   B CB  
6623 C CG  . ASP   B 162 ? 0.1975 0.1848 0.3404 0.0094  -0.0055 -0.0827 162 ASP   B CG  
6624 O OD1 . ASP   B 162 ? 0.1956 0.2087 0.3318 0.0068  0.0054  -0.0801 162 ASP   B OD1 
6625 O OD2 . ASP   B 162 ? 0.2145 0.2106 0.3621 0.0257  0.0018  -0.0757 162 ASP   B OD2 
6630 N N   . LYS   B 163 ? 0.1714 0.1337 0.2772 -0.0058 -0.0186 -0.0330 163 LYS   B N   
6631 C CA  . LYS   B 163 ? 0.1752 0.1421 0.2764 -0.0163 -0.0216 -0.0144 163 LYS   B CA  
6632 C C   . LYS   B 163 ? 0.1489 0.1357 0.2619 -0.0174 -0.0213 -0.0048 163 LYS   B C   
6633 O O   . LYS   B 163 ? 0.1506 0.1466 0.2826 -0.0218 -0.0236 -0.0075 163 LYS   B O   
6634 C CB  . LYS   B 163 ? 0.2211 0.1729 0.3222 -0.0088 -0.0285 0.0052  163 LYS   B CB  
6635 C CG  . LYS   B 163 ? 0.3022 0.2518 0.3923 -0.0155 -0.0209 0.0078  163 LYS   B CG  
6636 C CD  . LYS   B 163 ? 0.3758 0.3348 0.4659 -0.0248 -0.0183 0.0057  163 LYS   B CD  
6637 C CE  . LYS   B 163 ? 0.4310 0.4036 0.5176 -0.0325 -0.0160 0.0049  163 LYS   B CE  
6638 N NZ  . LYS   B 163 ? 0.4664 0.4456 0.5486 -0.0360 -0.0150 0.0002  163 LYS   B NZ  
6652 N N   . LEU   B 164 ? 0.1335 0.1314 0.2442 -0.0116 -0.0209 -0.0038 164 LEU   B N   
6653 C CA  . LEU   B 164 ? 0.1416 0.1336 0.2338 -0.0071 -0.0176 -0.0058 164 LEU   B CA  
6654 C C   . LEU   B 164 ? 0.1479 0.1325 0.2320 -0.0169 -0.0283 0.0017  164 LEU   B C   
6655 O O   . LEU   B 164 ? 0.1473 0.1545 0.2418 -0.0139 -0.0245 0.0030  164 LEU   B O   
6656 C CB  . LEU   B 164 ? 0.1392 0.1285 0.2239 -0.0076 -0.0157 -0.0095 164 LEU   B CB  
6657 C CG  . LEU   B 164 ? 0.1451 0.1424 0.2328 -0.0078 -0.0070 -0.0044 164 LEU   B CG  
6658 C CD1 . LEU   B 164 ? 0.1542 0.1377 0.2510 -0.0119 -0.0200 -0.0133 164 LEU   B CD1 
6659 C CD2 . LEU   B 164 ? 0.1696 0.1879 0.2485 -0.0081 0.0047  -0.0230 164 LEU   B CD2 
6671 N N   . VAL   B 165 ? 0.1774 0.1380 0.2435 -0.0256 -0.0279 -0.0158 165 VAL   B N   
6672 C CA  . VAL   B 165 ? 0.2103 0.1528 0.2552 -0.0298 -0.0536 -0.0115 165 VAL   B CA  
6673 C C   . VAL   B 165 ? 0.2407 0.1665 0.2732 -0.0430 -0.0790 -0.0091 165 VAL   B C   
6674 O O   . VAL   B 165 ? 0.2572 0.1863 0.2722 -0.0521 -0.0809 -0.0004 165 VAL   B O   
6675 C CB  . VAL   B 165 ? 0.2309 0.1669 0.2574 -0.0100 -0.0292 -0.0153 165 VAL   B CB  
6676 C CG1 . VAL   B 165 ? 0.2518 0.1758 0.2890 -0.0094 -0.0282 -0.0224 165 VAL   B CG1 
6677 C CG2 . VAL   B 165 ? 0.2267 0.1733 0.2512 -0.0118 -0.0155 -0.0170 165 VAL   B CG2 
6687 N N   . SER   B 166 ? 0.2494 0.1579 0.3179 -0.0407 -0.0822 -0.0221 166 SER   B N   
6688 C CA  . SER   B 166 ? 0.2417 0.1563 0.3776 -0.0423 -0.0708 -0.0276 166 SER   B CA  
6689 C C   . SER   B 166 ? 0.2273 0.1664 0.3930 -0.0404 -0.0710 -0.0109 166 SER   B C   
6690 O O   . SER   B 166 ? 0.2290 0.1880 0.4160 -0.0543 -0.0796 -0.0285 166 SER   B O   
6691 C CB  . SER   B 166 ? 0.2374 0.1613 0.4081 -0.0282 -0.0640 -0.0420 166 SER   B CB  
6692 O OG  . SER   B 166 ? 0.2197 0.1566 0.4202 -0.0211 -0.0608 -0.0216 166 SER   B OG  
6698 N N   . SER   B 167 ? 0.2078 0.1572 0.3697 -0.0405 -0.0733 0.0306  167 SER   B N   
6699 C CA  . SER   B 167 ? 0.2005 0.1639 0.3488 -0.0397 -0.0545 0.0348  167 SER   B CA  
6700 C C   . SER   B 167 ? 0.1943 0.1706 0.3232 -0.0486 -0.0485 0.0539  167 SER   B C   
6701 O O   . SER   B 167 ? 0.1947 0.1803 0.3217 -0.0541 -0.0464 0.0462  167 SER   B O   
6702 C CB  . SER   B 167 ? 0.1907 0.1724 0.3452 -0.0366 -0.0247 0.0439  167 SER   B CB  
6703 O OG  . SER   B 167 ? 0.1847 0.1839 0.3339 -0.0241 -0.0135 0.0395  167 SER   B OG  
6709 N N   . PHE   B 168 ? 0.1998 0.1754 0.3117 -0.0433 -0.0397 0.0674  168 PHE   B N   
6710 C CA  . PHE   B 168 ? 0.2037 0.1731 0.2957 -0.0500 -0.0350 0.0426  168 PHE   B CA  
6711 C C   . PHE   B 168 ? 0.1770 0.1574 0.2413 -0.0244 -0.0108 0.0219  168 PHE   B C   
6712 O O   . PHE   B 168 ? 0.2026 0.1491 0.2467 0.0009  -0.0047 0.0006  168 PHE   B O   
6713 C CB  . PHE   B 168 ? 0.2156 0.1801 0.3105 -0.0601 -0.0504 0.0540  168 PHE   B CB  
6714 C CG  . PHE   B 168 ? 0.2409 0.1650 0.3049 -0.0588 -0.0592 0.0290  168 PHE   B CG  
6715 C CD1 . PHE   B 168 ? 0.2737 0.1658 0.3182 -0.0545 -0.0668 0.0206  168 PHE   B CD1 
6716 C CD2 . PHE   B 168 ? 0.2262 0.1627 0.3102 -0.0508 -0.0596 0.0397  168 PHE   B CD2 
6717 C CE1 . PHE   B 168 ? 0.2849 0.1791 0.3255 -0.0396 -0.0617 0.0314  168 PHE   B CE1 
6718 C CE2 . PHE   B 168 ? 0.2485 0.1708 0.3113 -0.0344 -0.0720 0.0341  168 PHE   B CE2 
6719 C CZ  . PHE   B 168 ? 0.2718 0.1656 0.3212 -0.0246 -0.0707 0.0429  168 PHE   B CZ  
6729 N N   . LEU   B 169 ? 0.1788 0.1683 0.2430 -0.0064 0.0010  -0.0063 169 LEU   B N   
6730 C CA  . LEU   B 169 ? 0.2096 0.1970 0.2910 -0.0076 -0.0037 -0.0438 169 LEU   B CA  
6731 C C   . LEU   B 169 ? 0.2371 0.2215 0.3468 0.0069  0.0023  -0.0681 169 LEU   B C   
6732 O O   . LEU   B 169 ? 0.2627 0.2502 0.3971 0.0021  -0.0008 -0.0829 169 LEU   B O   
6733 C CB  . LEU   B 169 ? 0.2408 0.2435 0.3131 -0.0151 -0.0111 -0.0198 169 LEU   B CB  
6734 C CG  . LEU   B 169 ? 0.2905 0.2755 0.3496 -0.0061 -0.0087 -0.0135 169 LEU   B CG  
6735 C CD1 . LEU   B 169 ? 0.3000 0.2912 0.3509 -0.0063 -0.0084 -0.0028 169 LEU   B CD1 
6736 C CD2 . LEU   B 169 ? 0.2830 0.2786 0.3471 0.0080  0.0049  -0.0212 169 LEU   B CD2 
6737 O OXT . LEU   B 169 ? 0.2534 0.2361 0.3523 0.0325  0.0060  -0.0673 169 LEU   B OXT 
6749 S S   B DMS   C .   ? 0.5241 0.2198 0.3564 -0.0027 0.0822  0.1031  301 DMS   A S   
6750 O O   B DMS   C .   ? 0.5194 0.2202 0.3309 -0.0140 0.0918  0.1092  301 DMS   A O   
6751 C C1  B DMS   C .   ? 0.5276 0.2446 0.3912 -0.0194 0.1006  0.0899  301 DMS   A C1  
6752 C C2  B DMS   C .   ? 0.5285 0.2395 0.3744 -0.0125 0.0881  0.0865  301 DMS   A C2  
6759 N N2  B A1BBS D .   ? 0.1581 0.1428 0.1354 -0.0131 0.0039  0.0259  302 A1BBS A N2  
6760 C C3  B A1BBS D .   ? 0.2490 0.2287 0.2091 -0.0203 -0.0017 0.0274  302 A1BBS A C3  
6761 C C6  B A1BBS D .   ? 0.2180 0.1560 0.1815 -0.0355 -0.0095 0.0505  302 A1BBS A C6  
6762 C C9  B A1BBS D .   ? 0.1501 0.1376 0.1463 -0.0013 -0.0013 0.0275  302 A1BBS A C9  
6763 C C12 B A1BBS D .   ? 0.1575 0.1316 0.1667 -0.0135 -0.0098 0.0285  302 A1BBS A C12 
6764 C C1  B A1BBS D .   ? 0.2232 0.2012 0.1809 -0.0388 -0.0199 0.0387  302 A1BBS A C1  
6765 C C10 B A1BBS D .   ? 0.1595 0.1436 0.1509 -0.0119 -0.0052 0.0347  302 A1BBS A C10 
6766 C C11 B A1BBS D .   ? 0.1695 0.1406 0.1692 -0.0134 -0.0035 0.0422  302 A1BBS A C11 
6767 C C13 B A1BBS D .   ? 0.2248 0.1790 0.1715 -0.0378 -0.0011 0.0431  302 A1BBS A C13 
6768 C C2  B A1BBS D .   ? 0.2401 0.2260 0.2017 -0.0271 -0.0235 0.0279  302 A1BBS A C2  
6769 C C4  B A1BBS D .   ? 0.2429 0.1948 0.1880 -0.0267 0.0032  0.0403  302 A1BBS A C4  
6770 C C5  B A1BBS D .   ? 0.2421 0.1779 0.1820 -0.0263 -0.0065 0.0482  302 A1BBS A C5  
6771 C C7  B A1BBS D .   ? 0.1678 0.1456 0.1452 -0.0218 0.0020  0.0420  302 A1BBS A C7  
6772 C C8  B A1BBS D .   ? 0.1535 0.1441 0.1215 -0.0030 0.0132  0.0304  302 A1BBS A C8  
6773 N N1  B A1BBS D .   ? 0.2001 0.1508 0.1637 -0.0324 -0.0029 0.0485  302 A1BBS A N1  
6774 N N3  B A1BBS D .   ? 0.1492 0.1389 0.1358 -0.0022 0.0121  0.0344  302 A1BBS A N3  
6775 N N4  B A1BBS D .   ? 0.1545 0.1366 0.1573 -0.0022 -0.0107 0.0247  302 A1BBS A N4  
6776 O O1  B A1BBS D .   ? 0.2056 0.2062 0.1731 -0.0447 -0.0177 0.0575  302 A1BBS A O1  
6793 O O   . HOH   E .   ? 0.2711 0.2373 0.3295 -0.0066 0.0288  0.0846  401 HOH   A O   
6794 O O   . HOH   E .   ? 0.3000 0.3028 0.1886 0.0053  0.0486  0.0651  402 HOH   A O   
6795 O O   A HOH   E .   ? 0.3674 0.1726 0.3429 0.0105  -0.0590 0.0176  403 HOH   A O   
6796 O O   . HOH   E .   ? 0.5892 0.6388 0.6066 0.0484  -0.0676 0.1457  404 HOH   A O   
6797 O O   . HOH   E .   ? 0.5279 0.4361 0.4549 0.1691  -0.1246 -0.0453 405 HOH   A O   
6798 O O   . HOH   E .   ? 0.2968 0.3490 0.5018 0.0286  -0.1254 0.0133  406 HOH   A O   
6799 O O   A HOH   E .   ? 0.3052 0.4037 0.2972 -0.0433 -0.0193 0.1032  407 HOH   A O   
6800 O O   . HOH   E .   ? 0.5417 0.4299 0.3397 0.1677  -0.1100 0.0256  408 HOH   A O   
6801 O O   . HOH   E .   ? 0.5103 0.4891 0.5742 -0.0568 0.1286  0.2091  409 HOH   A O   
6802 O O   . HOH   E .   ? 0.4153 0.3700 0.4150 -0.0631 -0.0450 -0.0709 410 HOH   A O   
6803 O O   A HOH   E .   ? 0.3110 0.2724 0.3168 0.0028  0.0318  0.0236  411 HOH   A O   
6804 O O   . HOH   E .   ? 0.2349 0.4423 0.5290 -0.0473 0.0665  -0.1156 412 HOH   A O   
6805 O O   . HOH   E .   ? 0.3134 0.2755 0.5742 -0.0237 -0.1355 0.1399  413 HOH   A O   
6806 O O   . HOH   E .   ? 0.3016 0.2572 0.7495 -0.0657 0.0846  -0.0949 414 HOH   A O   
6807 O O   . HOH   E .   ? 0.7306 0.4638 0.6509 -0.1061 -0.0865 -0.0590 415 HOH   A O   
6808 O O   . HOH   E .   ? 0.3745 0.5022 0.4283 0.1315  0.1022  -0.0270 416 HOH   A O   
6809 O O   . HOH   E .   ? 0.4336 0.5686 0.3577 -0.1067 0.1183  0.0254  417 HOH   A O   
6810 O O   B HOH   E .   ? 0.2085 0.1794 0.3375 -0.0202 -0.0656 0.0755  418 HOH   A O   
6811 O O   A HOH   E .   ? 0.2803 0.2991 0.1922 -0.0192 -0.0150 0.0375  419 HOH   A O   
6812 O O   . HOH   E .   ? 0.2167 0.1796 0.2367 0.0265  -0.0346 0.0101  420 HOH   A O   
6813 O O   . HOH   E .   ? 0.4200 0.3763 0.4127 -0.1762 -0.0729 0.1821  421 HOH   A O   
6814 O O   . HOH   E .   ? 0.2117 0.5602 0.3763 0.1341  0.0361  0.1239  422 HOH   A O   
6815 O O   . HOH   E .   ? 0.2259 0.1943 0.3708 -0.0562 0.0327  -0.0459 423 HOH   A O   
6816 O O   . HOH   E .   ? 0.3471 0.3649 0.3796 -0.1051 -0.0167 0.1454  424 HOH   A O   
6817 O O   . HOH   E .   ? 0.5718 0.5653 0.4585 -0.1651 -0.0475 0.2513  425 HOH   A O   
6818 O O   . HOH   E .   ? 0.6535 0.5965 0.8316 -0.1236 -0.0258 0.2346  426 HOH   A O   
6819 O O   . HOH   E .   ? 0.6604 0.6006 0.3344 0.0049  -0.1238 0.1370  427 HOH   A O   
6820 O O   . HOH   E .   ? 0.3772 0.4007 0.3549 0.0209  0.1549  0.0820  428 HOH   A O   
6821 O O   . HOH   E .   ? 0.5320 0.6151 0.3064 0.0956  -0.1197 -0.1064 429 HOH   A O   
6822 O O   . HOH   E .   ? 0.2095 0.2308 0.6828 0.0372  -0.0931 -0.0997 430 HOH   A O   
6823 O O   . HOH   E .   ? 0.6278 0.4739 0.3622 0.2707  -0.1508 -0.1208 431 HOH   A O   
6824 O O   . HOH   E .   ? 0.5779 0.3912 0.2950 0.0652  0.0528  0.1116  432 HOH   A O   
6825 O O   B HOH   E .   ? 0.3887 0.7223 0.5116 -0.1610 -0.1362 0.0201  433 HOH   A O   
6826 O O   . HOH   E .   ? 0.3267 0.4303 0.2610 0.0378  0.0714  0.0281  434 HOH   A O   
6827 O O   . HOH   E .   ? 1.0412 1.0244 0.7569 -0.0736 -0.0525 -0.1089 435 HOH   A O   
6828 O O   B HOH   E .   ? 0.4201 0.2323 0.2157 -0.0860 -0.0848 0.0519  436 HOH   A O   
6829 O O   . HOH   E .   ? 0.5411 0.2016 0.7078 0.0700  -0.0684 -0.0487 437 HOH   A O   
6830 O O   . HOH   E .   ? 0.3779 0.2719 0.3040 -0.0619 0.0295  -0.0563 438 HOH   A O   
6831 O O   . HOH   E .   ? 0.2221 0.2790 0.2213 -0.0461 -0.0196 0.1054  439 HOH   A O   
6832 O O   . HOH   E .   ? 0.2342 0.2286 0.2495 0.0553  0.0229  0.0372  440 HOH   A O   
6833 O O   . HOH   E .   ? 0.5300 0.7349 0.4430 0.2362  -0.0158 0.0095  441 HOH   A O   
6834 O O   . HOH   E .   ? 0.1605 0.1508 0.2512 -0.0265 0.0076  -0.0084 442 HOH   A O   
6835 O O   . HOH   E .   ? 0.4949 0.1883 0.4543 0.0511  -0.0665 0.0656  443 HOH   A O   
6836 O O   . HOH   E .   ? 0.4268 0.3247 0.4969 0.0088  0.1716  0.0021  444 HOH   A O   
6837 O O   . HOH   E .   ? 0.3574 0.4203 0.4579 -0.1461 -0.1215 0.0015  445 HOH   A O   
6838 O O   . HOH   E .   ? 0.4460 0.4367 0.4961 0.0091  0.2179  -0.0537 446 HOH   A O   
6839 O O   . HOH   E .   ? 0.1663 0.1896 0.2564 0.0005  -0.0273 -0.0577 447 HOH   A O   
6840 O O   . HOH   E .   ? 0.2288 0.3851 0.4706 -0.0212 -0.0816 0.1161  448 HOH   A O   
6841 O O   . HOH   E .   ? 0.4729 0.2893 0.3986 -0.1688 0.1792  -0.0552 449 HOH   A O   
6842 O O   B HOH   E .   ? 0.1523 0.1934 0.1988 0.0202  -0.0082 -0.0391 450 HOH   A O   
6843 O O   B HOH   E .   ? 0.1377 0.1715 0.1672 0.0080  0.0115  0.0389  451 HOH   A O   
6844 O O   . HOH   E .   ? 0.5182 0.4625 0.4406 -0.0861 -0.1128 -0.0822 452 HOH   A O   
6845 O O   . HOH   E .   ? 0.1466 0.2143 0.2215 0.0039  -0.0078 0.0530  453 HOH   A O   
6846 O O   . HOH   E .   ? 0.2690 0.3463 0.3089 -0.0331 0.1205  -0.0535 454 HOH   A O   
6847 O O   . HOH   E .   ? 0.2457 0.4561 0.3667 0.1086  -0.0484 0.0364  455 HOH   A O   
6848 O O   . HOH   E .   ? 0.3284 0.3480 0.5432 -0.0711 -0.0920 -0.1557 456 HOH   A O   
6849 O O   A HOH   E .   ? 0.2816 0.3550 0.3040 0.0910  0.0472  -0.0365 457 HOH   A O   
6850 O O   . HOH   E .   ? 0.4183 0.2004 0.2227 0.1095  0.0221  0.0121  458 HOH   A O   
6851 O O   A HOH   E .   ? 0.1684 0.3441 0.2410 0.1170  0.0462  0.0300  459 HOH   A O   
6852 O O   A HOH   E .   ? 0.2636 0.3395 0.3497 0.0420  -0.0306 -0.0457 460 HOH   A O   
6853 O O   . HOH   E .   ? 0.1959 0.2532 0.4303 0.0005  0.0528  0.0613  461 HOH   A O   
6854 O O   . HOH   E .   ? 0.3679 0.3631 0.2628 -0.0588 0.0033  0.0324  462 HOH   A O   
6855 O O   . HOH   E .   ? 0.3021 0.2055 0.2080 0.0186  0.0495  0.0019  463 HOH   A O   
6856 O O   . HOH   E .   ? 0.6045 0.4456 0.5681 0.1376  0.0127  -0.1155 464 HOH   A O   
6857 O O   . HOH   E .   ? 0.3955 0.3529 0.2066 -0.1016 -0.0235 -0.0818 465 HOH   A O   
6858 O O   A HOH   E .   ? 0.1710 0.1676 0.1663 0.0186  0.0013  -0.0073 466 HOH   A O   
6859 O O   . HOH   E .   ? 0.1960 0.1898 0.2571 0.0197  -0.0231 0.0192  467 HOH   A O   
6860 O O   . HOH   E .   ? 0.3004 0.4682 0.4195 -0.0715 0.0532  -0.0783 468 HOH   A O   
6861 O O   A HOH   E .   ? 0.1548 0.1714 0.3289 -0.0308 -0.0504 0.0026  469 HOH   A O   
6862 O O   . HOH   E .   ? 0.1427 0.1460 0.2024 -0.0051 -0.0269 0.0069  470 HOH   A O   
6863 O O   . HOH   E .   ? 0.2854 0.4788 0.3277 0.0613  -0.0717 0.0117  471 HOH   A O   
6864 O O   . HOH   E .   ? 0.3874 0.7402 0.4814 -0.0749 -0.1416 0.0341  472 HOH   A O   
6865 O O   . HOH   E .   ? 0.1563 0.1316 0.2283 -0.0052 0.0118  -0.0135 473 HOH   A O   
6866 O O   . HOH   E .   ? 0.1521 0.1831 0.2406 0.0103  -0.0041 0.0025  474 HOH   A O   
6867 O O   . HOH   E .   ? 0.1385 0.1277 0.1448 -0.0029 0.0124  0.0044  475 HOH   A O   
6868 O O   . HOH   E .   ? 0.2086 0.2071 0.3252 0.0249  0.0713  0.0076  476 HOH   A O   
6869 O O   B HOH   E .   ? 0.5460 0.3694 0.5113 0.2310  0.0491  0.1285  477 HOH   A O   
6870 O O   . HOH   E .   ? 0.1922 0.3066 0.4857 0.0262  0.0753  -0.1377 478 HOH   A O   
6871 O O   B HOH   E .   ? 0.4126 0.3536 0.2572 -0.0932 -0.1293 0.1245  479 HOH   A O   
6872 O O   B HOH   E .   ? 0.2963 0.2874 0.3566 0.0985  0.0312  0.0006  480 HOH   A O   
6873 O O   . HOH   E .   ? 0.2439 0.2040 0.2289 -0.0425 0.0070  0.0467  481 HOH   A O   
6874 O O   . HOH   E .   ? 0.1487 0.1547 0.1520 -0.0062 -0.0117 -0.0035 482 HOH   A O   
6875 O O   . HOH   E .   ? 0.3974 0.4101 0.3989 0.1908  0.0882  0.0340  483 HOH   A O   
6876 O O   . HOH   E .   ? 0.4007 0.2141 0.5111 -0.1037 0.0957  0.0331  484 HOH   A O   
6877 O O   . HOH   E .   ? 0.2705 0.3874 0.3130 0.0589  0.0940  0.1765  485 HOH   A O   
6878 O O   . HOH   E .   ? 0.1894 0.1867 0.2231 -0.0343 0.0180  0.0234  486 HOH   A O   
6879 O O   . HOH   E .   ? 0.2098 0.2274 0.2237 -0.0134 -0.0330 0.0427  487 HOH   A O   
6880 O O   . HOH   E .   ? 0.2524 0.1892 0.1901 -0.0427 0.0342  0.0270  488 HOH   A O   
6881 O O   . HOH   E .   ? 0.3131 0.5537 0.4084 0.0961  0.0701  -0.0957 489 HOH   A O   
6882 O O   . HOH   E .   ? 0.3096 0.2783 0.1983 0.0372  0.0658  0.0146  490 HOH   A O   
6883 O O   . HOH   E .   ? 0.3736 0.3359 0.3306 -0.0769 0.1567  0.0287  491 HOH   A O   
6884 O O   . HOH   E .   ? 0.1685 0.1679 0.2948 -0.0133 0.0234  0.0320  492 HOH   A O   
6885 O O   A HOH   E .   ? 0.2259 0.3005 0.1912 0.0325  0.0627  0.0909  493 HOH   A O   
6886 O O   A HOH   E .   ? 0.2178 0.2988 0.2314 -0.0246 -0.0525 0.0280  494 HOH   A O   
6887 O O   . HOH   E .   ? 0.7518 0.7554 0.7868 -0.0771 -0.0610 -0.0303 495 HOH   A O   
6888 O O   . HOH   E .   ? 0.6887 0.3163 0.4076 -0.1615 -0.0060 0.0965  496 HOH   A O   
6889 O O   . HOH   E .   ? 0.1785 0.1918 0.3391 0.0285  0.0895  0.0841  497 HOH   A O   
6890 O O   . HOH   E .   ? 0.3234 0.2285 0.3358 -0.0056 -0.0364 0.0859  498 HOH   A O   
6891 O O   . HOH   E .   ? 0.2914 0.4755 0.4917 -0.0345 0.1574  -0.0355 499 HOH   A O   
6892 O O   . HOH   E .   ? 0.2626 0.3907 0.3793 -0.0343 0.1359  -0.0623 500 HOH   A O   
6893 O O   . HOH   E .   ? 0.2837 0.1888 0.2921 -0.0195 0.0200  0.0256  501 HOH   A O   
6894 O O   A HOH   E .   ? 0.1647 0.1397 0.1404 0.0112  -0.0408 0.0274  502 HOH   A O   
6895 O O   A HOH   E .   ? 0.3222 0.2572 0.3107 0.0597  0.0989  0.0567  503 HOH   A O   
6896 O O   . HOH   E .   ? 0.2148 0.2652 0.3409 -0.0095 -0.0223 0.1405  504 HOH   A O   
6897 O O   . HOH   E .   ? 0.1684 0.1272 0.1630 -0.0130 0.0070  0.0011  505 HOH   A O   
6898 O O   . HOH   E .   ? 0.2362 0.1643 0.1500 -0.0015 0.0159  0.0144  506 HOH   A O   
6899 O O   . HOH   E .   ? 0.6684 0.6546 0.5076 0.1151  -0.1150 -0.0847 507 HOH   A O   
6900 O O   . HOH   E .   ? 0.5779 0.3058 0.2663 -0.1512 0.0591  0.0401  508 HOH   A O   
6901 O O   A HOH   E .   ? 0.3779 0.4217 0.3403 -0.0163 -0.0157 0.0575  509 HOH   A O   
6902 O O   A HOH   E .   ? 0.1432 0.1038 0.1591 0.0376  -0.0451 -0.0404 510 HOH   A O   
6903 O O   . HOH   E .   ? 0.2421 0.2443 0.4964 0.0072  -0.0941 -0.0268 511 HOH   A O   
6904 O O   B HOH   E .   ? 0.2762 0.1701 0.5618 0.0084  -0.1764 0.0191  512 HOH   A O   
6905 O O   . HOH   E .   ? 0.4950 0.2561 0.5645 -0.0826 0.0041  0.0017  513 HOH   A O   
6906 O O   . HOH   E .   ? 0.4743 0.4383 0.1948 -0.1072 0.0567  0.0731  514 HOH   A O   
6907 O O   . HOH   E .   ? 0.3926 0.6111 0.3543 -0.0700 -0.0054 0.0477  515 HOH   A O   
6908 O O   . HOH   E .   ? 0.3179 0.2454 0.2096 -0.0607 -0.0754 0.0165  516 HOH   A O   
6909 O O   . HOH   E .   ? 0.2209 0.1759 0.3655 -0.0020 -0.0369 0.0003  517 HOH   A O   
6910 O O   . HOH   E .   ? 0.5336 0.6549 0.4030 0.0009  0.2574  -0.0710 518 HOH   A O   
6911 O O   . HOH   E .   ? 0.2047 0.2974 0.2499 0.0113  -0.0313 0.0541  519 HOH   A O   
6912 O O   A HOH   E .   ? 0.3406 0.3140 0.2271 -0.0093 0.0420  0.0925  520 HOH   A O   
6913 O O   . HOH   E .   ? 0.4164 0.5045 0.4431 -0.0762 -0.0602 0.0037  521 HOH   A O   
6914 O O   A HOH   E .   ? 0.0987 0.1869 0.2034 -0.0176 0.0608  0.0406  522 HOH   A O   
6915 O O   . HOH   E .   ? 0.2071 0.2989 0.3300 -0.0051 0.0061  0.0295  523 HOH   A O   
6916 O O   . HOH   E .   ? 0.3548 0.1288 0.2067 0.0154  -0.0802 0.0088  524 HOH   A O   
6917 O O   . HOH   E .   ? 0.1497 0.1491 0.1906 0.0142  -0.0293 0.0184  525 HOH   A O   
6918 O O   . HOH   E .   ? 0.1770 0.2394 0.3476 -0.0382 0.0201  0.0040  526 HOH   A O   
6919 O O   . HOH   E .   ? 0.2871 0.5347 0.1714 -0.0213 0.0565  0.0168  527 HOH   A O   
6920 O O   . HOH   E .   ? 0.4234 0.8589 0.5853 -0.0975 -0.1167 0.2053  528 HOH   A O   
6921 O O   A HOH   E .   ? 0.3280 0.2765 0.2989 0.0357  0.0277  -0.0089 529 HOH   A O   
6922 O O   . HOH   E .   ? 0.4310 0.6592 0.3230 -0.1027 -0.0485 0.1349  530 HOH   A O   
6923 O O   . HOH   E .   ? 0.2298 0.4298 0.2368 0.1559  -0.0190 -0.0040 531 HOH   A O   
6924 O O   . HOH   E .   ? 0.5630 0.7175 0.5620 0.2908  0.1764  0.0194  532 HOH   A O   
6925 O O   . HOH   E .   ? 0.3859 0.2373 0.5147 -0.0838 -0.2238 0.1330  533 HOH   A O   
6926 O O   . HOH   E .   ? 0.4686 0.4603 0.6393 -0.0277 -0.1199 -0.1248 534 HOH   A O   
6927 O O   . HOH   E .   ? 0.3213 0.3569 0.6307 -0.0079 0.0289  -0.0639 535 HOH   A O   
6928 O O   . HOH   E .   ? 0.1638 0.1764 0.3426 0.0022  -0.0047 -0.0037 536 HOH   A O   
6929 O O   . HOH   E .   ? 0.6089 0.6843 0.7512 0.2956  -0.1251 0.0305  537 HOH   A O   
6930 O O   A HOH   E .   ? 0.3555 0.4818 0.4498 -0.0957 -0.0528 0.0105  538 HOH   A O   
6931 O O   A HOH   E .   ? 0.4342 0.4798 0.3320 0.1529  -0.1243 0.0801  539 HOH   A O   
6932 O O   B HOH   E .   ? 0.3273 0.3128 0.2659 0.1370  0.0118  0.0346  540 HOH   A O   
6933 O O   . HOH   E .   ? 0.3968 0.2652 0.1899 -0.0625 0.0723  0.0809  541 HOH   A O   
6934 O O   B HOH   E .   ? 0.6836 0.2975 0.4045 -0.0798 -0.0858 0.0034  542 HOH   A O   
6935 O O   A HOH   E .   ? 0.1043 0.1292 0.1328 -0.0047 -0.0006 -0.0632 543 HOH   A O   
6936 O O   . HOH   E .   ? 0.6001 0.3549 0.4735 0.1333  -0.1175 0.0741  544 HOH   A O   
6937 O O   B HOH   E .   ? 0.6773 0.5144 0.5042 -0.1315 0.0616  0.0324  545 HOH   A O   
6938 O O   B HOH   E .   ? 0.3790 0.7474 0.4266 -0.1044 0.0622  0.0895  546 HOH   A O   
6939 O O   . HOH   E .   ? 0.2537 0.1740 0.2967 0.0057  0.0169  -0.0002 547 HOH   A O   
6940 O O   . HOH   E .   ? 0.2145 0.2139 0.4929 -0.0272 -0.1288 0.0550  548 HOH   A O   
6941 O O   . HOH   E .   ? 0.7964 0.8002 0.7269 0.0928  0.0080  -0.0563 549 HOH   A O   
6942 O O   B HOH   E .   ? 0.5120 0.3405 0.2248 -0.1161 -0.1110 -0.0030 550 HOH   A O   
6943 O O   . HOH   E .   ? 0.2040 0.2747 0.2599 0.0131  -0.0209 -0.0525 551 HOH   A O   
6944 O O   . HOH   E .   ? 0.4346 0.3977 0.3191 0.2456  -0.0591 -0.0482 552 HOH   A O   
6945 O O   . HOH   E .   ? 0.7737 0.7766 0.8827 -0.0283 -0.0875 0.2546  553 HOH   A O   
6946 O O   B HOH   E .   ? 0.4966 0.2064 0.2803 0.0661  -0.1263 -0.0402 554 HOH   A O   
6947 O O   B HOH   E .   ? 0.5587 0.3017 0.2152 -0.1681 0.1134  -0.0607 555 HOH   A O   
6948 O O   B HOH   E .   ? 0.1631 0.4967 0.2482 -0.0130 -0.0394 -0.1195 556 HOH   A O   
6949 O O   . HOH   E .   ? 0.2384 0.2225 0.2827 0.0055  0.0007  0.0345  557 HOH   A O   
6950 O O   A HOH   E .   ? 0.2548 0.2823 0.2288 -0.0461 -0.0199 -0.0642 558 HOH   A O   
6951 O O   A HOH   E .   ? 0.3812 0.3049 0.3093 0.0590  0.0697  0.0958  559 HOH   A O   
6952 O O   . HOH   E .   ? 0.3270 0.4937 0.5894 0.0821  0.0396  -0.1518 560 HOH   A O   
6953 O O   B HOH   E .   ? 0.2018 0.2133 0.2861 0.0162  -0.0267 0.0272  561 HOH   A O   
6954 O O   . HOH   E .   ? 0.3874 0.3226 0.4543 0.0275  0.0554  0.0060  562 HOH   A O   
6955 O O   . HOH   E .   ? 0.8167 0.7456 0.4666 -0.0244 -0.0893 -0.0022 563 HOH   A O   
6956 O O   A HOH   E .   ? 0.4240 0.3602 0.3337 0.0192  0.1238  0.0562  564 HOH   A O   
6957 O O   . HOH   E .   ? 0.6956 0.6739 0.8000 -0.1301 0.0316  -0.1318 565 HOH   A O   
6958 O O   . HOH   E .   ? 0.6687 0.6290 0.5344 -0.1165 0.0541  0.1037  566 HOH   A O   
6959 O O   . HOH   E .   ? 0.3250 0.3081 0.5587 -0.0324 -0.0204 -0.1359 567 HOH   A O   
6960 O O   . HOH   E .   ? 0.6819 0.6216 0.7935 -0.0932 -0.1347 0.0270  568 HOH   A O   
6961 O O   . HOH   E .   ? 0.4166 0.5196 0.5346 0.2087  -0.1081 0.1338  569 HOH   A O   
6962 O O   . HOH   E .   ? 0.3857 0.4516 0.4380 0.0754  -0.0017 0.0676  570 HOH   A O   
6963 O O   . HOH   E .   ? 0.4914 0.3732 0.5352 0.0760  0.1045  0.1022  571 HOH   A O   
6964 O O   . HOH   E .   ? 0.3500 0.4720 0.4785 -0.0444 -0.0211 -0.0594 572 HOH   A O   
6965 O O   . HOH   E .   ? 0.3077 0.5220 0.4674 -0.1368 0.0646  -0.0662 573 HOH   A O   
6966 O O   . HOH   E .   ? 0.6242 0.2904 0.7408 -0.0221 -0.0203 0.1673  574 HOH   A O   
6967 O O   . HOH   E .   ? 0.2801 0.4766 0.4836 0.0443  0.0295  -0.1566 575 HOH   A O   
6968 O O   . HOH   E .   ? 0.4407 0.5293 0.4541 0.0259  -0.0544 0.1462  576 HOH   A O   
6969 O O   . HOH   E .   ? 0.3980 0.4951 0.3869 0.0322  -0.0829 -0.1160 577 HOH   A O   
6970 O O   . HOH   E .   ? 0.6939 0.7174 0.6098 0.0276  0.0611  0.3316  578 HOH   A O   
6971 O O   . HOH   E .   ? 0.4334 0.5820 0.4082 -0.0579 -0.0597 0.2285  579 HOH   A O   
6972 O O   B HOH   E .   ? 0.4541 0.3775 0.4538 0.0601  -0.0702 -0.0279 580 HOH   A O   
6973 O O   . HOH   E .   ? 0.3043 0.2669 0.4005 -0.0963 0.0564  -0.0389 581 HOH   A O   
6974 O O   . HOH   E .   ? 0.5991 0.4857 0.5863 0.0781  0.2300  0.1352  582 HOH   A O   
6975 O O   A HOH   E .   ? 0.2230 0.1984 0.3392 0.0542  -0.1246 -0.0434 583 HOH   A O   
6976 O O   . HOH   E .   ? 0.2841 0.4246 0.3910 0.1031  0.0510  0.0603  584 HOH   A O   
6977 O O   . HOH   E .   ? 0.5787 0.6702 0.6404 0.2141  -0.0398 -0.0635 585 HOH   A O   
6978 O O   . HOH   E .   ? 0.3426 0.1976 0.2654 0.0421  -0.0922 -0.0335 586 HOH   A O   
6979 O O   . HOH   E .   ? 0.7471 0.6260 0.7354 -0.1293 -0.1163 -0.1341 587 HOH   A O   
6980 O O   . HOH   E .   ? 0.5834 0.5976 0.3401 0.0891  -0.0198 0.0500  588 HOH   A O   
6981 O O   . HOH   E .   ? 0.4187 0.7266 0.6597 -0.1347 -0.1103 0.0822  589 HOH   A O   
6982 O O   . HOH   E .   ? 0.3747 0.4741 0.4918 -0.1849 -0.0029 0.0432  590 HOH   A O   
6983 O O   . HOH   E .   ? 0.7393 0.5890 0.8215 0.0049  0.1083  -0.0682 591 HOH   A O   
6984 O O   . HOH   E .   ? 0.5174 0.5065 0.5842 -0.0337 -0.0637 -0.1156 592 HOH   A O   
6985 O O   . HOH   E .   ? 0.5805 0.4334 0.3576 -0.0408 0.0565  0.0203  593 HOH   A O   
6986 O O   . HOH   E .   ? 0.2649 0.3598 0.2735 0.0785  0.0262  0.0572  594 HOH   A O   
6987 O O   . HOH   E .   ? 0.7239 0.3560 0.3645 -0.0955 -0.0492 0.0734  595 HOH   A O   
6988 O O   B HOH   E .   ? 0.3889 0.2056 0.2763 0.0479  0.0087  -0.0000 596 HOH   A O   
6989 O O   B HOH   E .   ? 0.3141 0.2170 0.3234 0.0092  -0.0892 -0.0340 597 HOH   A O   
6990 O O   . HOH   E .   ? 0.8311 0.3655 0.3320 -0.0246 -0.1216 -0.0328 598 HOH   A O   
6991 O O   . HOH   E .   ? 0.5147 0.5803 0.3912 0.0104  -0.1031 -0.0478 599 HOH   A O   
6992 O O   . HOH   E .   ? 0.3738 0.4365 0.5728 0.0246  0.1518  0.2315  600 HOH   A O   
6993 O O   . HOH   E .   ? 0.3163 0.4627 0.3907 0.0279  -0.0420 -0.0669 601 HOH   A O   
6994 O O   B HOH   E .   ? 0.6314 0.6546 0.4156 -0.1090 -0.0574 0.0391  602 HOH   A O   
6995 O O   . HOH   E .   ? 0.2866 0.5037 0.3859 0.1103  0.1201  0.2367  603 HOH   A O   
6996 O O   . HOH   E .   ? 0.2541 0.2744 0.7005 0.0015  -0.1508 0.0418  604 HOH   A O   
6997 O O   . HOH   E .   ? 0.4593 0.3461 0.2121 -0.0813 0.1059  -0.0178 605 HOH   A O   
6998 O O   . HOH   E .   ? 0.5524 0.5439 0.5138 0.0157  -0.1276 -0.0359 606 HOH   A O   
6999 O O   . HOH   E .   ? 0.4840 0.4643 0.4181 -0.0351 -0.0195 0.0282  607 HOH   A O   
7000 O O   . HOH   E .   ? 0.4756 0.4889 0.6046 0.0363  -0.0739 -0.0251 608 HOH   A O   
7001 O O   . HOH   E .   ? 0.7381 0.6062 0.4903 -0.0378 0.1026  0.0858  609 HOH   A O   
7002 O O   . HOH   E .   ? 0.5485 0.6254 0.7431 0.1066  0.1319  -0.1320 610 HOH   A O   
7003 O O   . HOH   E .   ? 0.4215 0.3341 0.4720 -0.0217 0.1694  0.0756  611 HOH   A O   
7004 O O   . HOH   E .   ? 0.3269 0.2094 0.5546 -0.0038 0.0700  0.0361  612 HOH   A O   
7005 O O   . HOH   E .   ? 0.3500 0.3199 0.5372 0.0459  0.1013  -0.0719 613 HOH   A O   
7006 O O   . HOH   E .   ? 0.2408 0.3346 0.3647 0.0532  -0.0654 0.0145  614 HOH   A O   
7007 O O   . HOH   E .   ? 0.4459 0.8730 0.4833 -0.0644 -0.0173 0.1628  615 HOH   A O   
7008 O O   . HOH   E .   ? 0.4723 0.2708 0.4876 -0.1348 0.0556  0.0417  616 HOH   A O   
7009 O O   B HOH   E .   ? 0.2132 0.2399 0.1714 0.0716  0.0005  0.0197  617 HOH   A O   
7010 O O   . HOH   E .   ? 0.6702 0.2611 0.5728 -0.0462 0.0525  0.1113  618 HOH   A O   
7011 O O   . HOH   E .   ? 0.2751 0.4784 0.3819 0.0715  -0.0157 0.0285  619 HOH   A O   
7012 O O   . HOH   E .   ? 0.6278 0.5647 0.6586 -0.1103 -0.0394 -0.0183 620 HOH   A O   
7013 O O   . HOH   E .   ? 0.6094 0.7722 0.5059 0.1366  -0.0213 0.0870  621 HOH   A O   
7014 O O   B HOH   E .   ? 0.4870 0.3858 0.6761 0.0856  -0.0861 0.0692  622 HOH   A O   
7015 O O   . HOH   E .   ? 0.6754 0.8458 0.5300 0.0371  -0.1372 0.0375  623 HOH   A O   
7016 O O   . HOH   E .   ? 0.3371 0.2905 0.5223 0.0301  0.0688  0.1087  624 HOH   A O   
7017 O O   . HOH   E .   ? 0.5386 0.6704 0.5435 0.2944  -0.1037 0.1003  625 HOH   A O   
7018 O O   . HOH   E .   ? 0.5554 0.7930 0.5830 -0.1005 -0.1123 -0.1146 626 HOH   A O   
7019 O O   A HOH   E .   ? 0.2717 0.3812 0.2322 0.0529  0.0018  -0.0749 627 HOH   A O   
7020 O O   . HOH   E .   ? 0.4465 0.7312 0.4339 0.1860  -0.0271 -0.0962 628 HOH   A O   
7021 O O   . HOH   E .   ? 0.5192 0.6509 0.5244 -0.0811 -0.0616 0.0413  629 HOH   A O   
7022 O O   . HOH   E .   ? 0.6154 0.5419 0.5533 0.0329  0.0227  -0.0334 630 HOH   A O   
7023 O O   . HOH   E .   ? 0.4135 0.4644 0.6399 0.0180  -0.0938 0.2947  631 HOH   A O   
7024 O O   . HOH   F .   ? 0.2576 0.2293 0.3291 0.0022  0.1004  0.0217  201 HOH   B O   
7025 O O   . HOH   F .   ? 0.2270 0.5504 0.4652 0.0209  0.0815  -0.1984 202 HOH   B O   
7026 O O   . HOH   F .   ? 0.3706 0.4136 0.5749 -0.0578 0.0879  -0.0937 203 HOH   B O   
7027 O O   . HOH   F .   ? 0.6361 0.4626 0.2923 0.1050  -0.0846 -0.1299 204 HOH   B O   
7028 O O   . HOH   F .   ? 0.4610 0.4903 0.4960 -0.1380 0.1347  -0.1499 205 HOH   B O   
7029 O O   . HOH   F .   ? 0.2433 0.2823 0.2769 0.0735  0.0208  -0.0485 206 HOH   B O   
7030 O O   . HOH   F .   ? 0.4550 0.4277 0.6973 -0.0274 -0.1478 0.2860  207 HOH   B O   
7031 O O   . HOH   F .   ? 0.5069 0.2997 0.3496 -0.0355 0.0122  -0.1036 208 HOH   B O   
7032 O O   . HOH   F .   ? 0.6664 0.2839 0.4373 0.0098  0.0967  -0.0315 209 HOH   B O   
7033 O O   . HOH   F .   ? 0.3444 0.6197 0.3566 0.0898  0.0070  0.2251  210 HOH   B O   
7034 O O   . HOH   F .   ? 0.6388 0.5958 0.3610 0.2615  -0.1317 -0.1040 211 HOH   B O   
7035 O O   . HOH   F .   ? 0.3495 0.2142 0.5329 0.0232  0.2160  0.0889  212 HOH   B O   
7036 O O   . HOH   F .   ? 0.6311 0.5585 0.6699 0.1311  0.1420  0.0956  213 HOH   B O   
7037 O O   . HOH   F .   ? 0.4553 0.4902 0.3825 0.0814  0.0271  -0.1685 214 HOH   B O   
7038 O O   . HOH   F .   ? 0.5243 0.4400 0.2907 -0.0003 -0.1205 0.0849  215 HOH   B O   
7039 O O   . HOH   F .   ? 0.1566 0.1912 0.2470 -0.0168 -0.0002 0.0071  216 HOH   B O   
7040 O O   . HOH   F .   ? 0.4619 0.4566 0.3952 0.1894  -0.0524 0.0170  217 HOH   B O   
7041 O O   . HOH   F .   ? 0.2891 0.3175 0.6367 0.0830  -0.1016 0.0208  218 HOH   B O   
7042 O O   . HOH   F .   ? 0.3061 0.3167 0.4608 0.0294  -0.1200 0.0103  219 HOH   B O   
7043 O O   . HOH   F .   ? 0.3762 0.5193 0.4705 0.2480  0.0657  -0.0116 220 HOH   B O   
7044 O O   . HOH   F .   ? 0.3599 0.2513 0.4060 0.0574  -0.0174 -0.0638 221 HOH   B O   
7045 O O   . HOH   F .   ? 0.2539 0.1757 0.2523 -0.0260 0.0982  0.0015  222 HOH   B O   
7046 O O   . HOH   F .   ? 0.5908 0.2964 0.4704 -0.1786 0.0393  0.0000  223 HOH   B O   
7047 O O   . HOH   F .   ? 0.3505 0.3875 0.4934 -0.1313 0.0177  0.0154  224 HOH   B O   
7048 O O   . HOH   F .   ? 0.2770 0.4140 0.5173 0.0444  0.0776  0.1012  225 HOH   B O   
7049 O O   . HOH   F .   ? 0.2182 0.2130 0.3558 -0.0350 -0.0028 -0.0262 226 HOH   B O   
7050 O O   . HOH   F .   ? 0.5329 0.7116 0.4189 0.3444  0.0033  0.0641  227 HOH   B O   
7051 O O   . HOH   F .   ? 0.4850 0.2058 0.3326 -0.0040 -0.1049 0.0152  228 HOH   B O   
7052 O O   . HOH   F .   ? 0.4296 0.3452 0.3266 -0.0757 0.0349  -0.0377 229 HOH   B O   
7053 O O   . HOH   F .   ? 0.2225 0.1363 0.3602 0.0167  -0.0926 -0.0248 230 HOH   B O   
7054 O O   . HOH   F .   ? 0.2910 0.2835 0.3082 0.0294  0.0433  -0.1156 231 HOH   B O   
7055 O O   . HOH   F .   ? 0.2449 0.3879 0.3107 -0.0508 -0.0667 -0.0779 232 HOH   B O   
7056 O O   . HOH   F .   ? 0.2919 0.3148 0.2310 -0.0736 0.0326  -0.0351 233 HOH   B O   
7057 O O   . HOH   F .   ? 0.1779 0.1972 0.2731 -0.0161 0.0051  -0.0033 234 HOH   B O   
7058 O O   . HOH   F .   ? 0.3786 0.3440 0.3320 0.0192  0.0845  -0.0172 235 HOH   B O   
7059 O O   . HOH   F .   ? 0.3231 0.2130 0.4509 -0.0082 0.1611  -0.0037 236 HOH   B O   
7060 O O   . HOH   F .   ? 0.5119 0.3001 0.4388 -0.2193 -0.0068 0.0050  237 HOH   B O   
7061 O O   . HOH   F .   ? 0.4167 0.1844 0.2148 0.0556  -0.1047 -0.0309 238 HOH   B O   
7062 O O   . HOH   F .   ? 0.3954 0.3227 0.4071 0.0704  -0.0984 -0.1924 239 HOH   B O   
7063 O O   . HOH   F .   ? 0.1497 0.1479 0.1528 -0.0095 -0.0046 0.0044  240 HOH   B O   
7064 O O   . HOH   F .   ? 0.2420 0.3628 0.2235 -0.0823 0.0214  0.0636  241 HOH   B O   
7065 O O   . HOH   F .   ? 0.5256 0.4121 0.2289 -0.0092 0.0302  -0.0704 242 HOH   B O   
7066 O O   . HOH   F .   ? 0.3016 0.1761 0.5769 0.0023  -0.1552 -0.0356 243 HOH   B O   
7067 O O   . HOH   F .   ? 0.2368 0.2077 0.1765 0.0055  -0.0111 -0.0013 244 HOH   B O   
7068 O O   . HOH   F .   ? 0.1815 0.2735 0.2468 0.0444  0.0388  0.0938  245 HOH   B O   
7069 O O   . HOH   F .   ? 0.2550 0.2250 0.2593 0.0917  -0.0860 -0.0814 246 HOH   B O   
7070 O O   . HOH   F .   ? 0.2228 0.2298 0.2686 -0.0462 0.0215  -0.0178 247 HOH   B O   
7071 O O   . HOH   F .   ? 0.2487 0.4286 0.4816 0.0960  -0.0725 -0.1065 248 HOH   B O   
7072 O O   . HOH   F .   ? 0.1492 0.1306 0.1479 0.0028  0.0006  0.0024  249 HOH   B O   
7073 O O   . HOH   F .   ? 0.2012 0.3671 0.2390 -0.0241 -0.0107 0.0482  250 HOH   B O   
7074 O O   . HOH   F .   ? 0.1650 0.1409 0.2600 -0.0099 0.0101  -0.0185 251 HOH   B O   
7075 O O   . HOH   F .   ? 0.3483 0.3868 0.3574 -0.0053 -0.1158 0.0318  252 HOH   B O   
7076 O O   . HOH   F .   ? 0.2269 0.2004 0.2153 -0.0249 -0.0570 0.0123  253 HOH   B O   
7077 O O   . HOH   F .   ? 0.2166 0.1986 0.4721 0.0197  -0.0764 -0.0702 254 HOH   B O   
7078 O O   . HOH   F .   ? 0.3449 0.3359 0.2136 0.0148  0.0819  -0.0070 255 HOH   B O   
7079 O O   . HOH   F .   ? 0.5182 0.6683 0.2867 -0.0120 0.0572  -0.0189 256 HOH   B O   
7080 O O   . HOH   F .   ? 0.1638 0.1690 0.2719 -0.0171 -0.0140 0.0093  257 HOH   B O   
7081 O O   . HOH   F .   ? 0.2570 0.2847 0.2469 -0.0338 -0.0801 0.0019  258 HOH   B O   
7082 O O   . HOH   F .   ? 0.1453 0.1604 0.2046 -0.0005 0.0040  0.0032  259 HOH   B O   
7083 O O   . HOH   F .   ? 0.2002 0.1495 0.2156 -0.0297 -0.0096 0.0121  260 HOH   B O   
7084 O O   . HOH   F .   ? 0.2072 0.1553 0.2152 -0.0229 -0.0421 0.0238  261 HOH   B O   
7085 O O   . HOH   F .   ? 0.2856 0.2382 0.2887 0.0836  0.0900  0.0244  262 HOH   B O   
7086 O O   . HOH   F .   ? 0.3124 0.2423 0.2966 -0.0442 0.0289  -0.0333 263 HOH   B O   
7087 O O   . HOH   F .   ? 0.2442 0.2810 0.2430 -0.0489 -0.0665 -0.0359 264 HOH   B O   
7088 O O   . HOH   F .   ? 0.4703 0.5453 0.6216 0.0655  -0.1091 -0.1102 265 HOH   B O   
7089 O O   . HOH   F .   ? 0.4946 0.5546 0.5307 0.1027  -0.1478 -0.0320 266 HOH   B O   
7090 O O   . HOH   F .   ? 0.2816 0.4060 0.3133 0.0054  0.1086  0.0133  267 HOH   B O   
7091 O O   . HOH   F .   ? 0.2905 0.2129 0.4761 0.0104  0.0754  0.0358  268 HOH   B O   
7092 O O   . HOH   F .   ? 0.2260 0.3343 0.3224 -0.0389 0.0533  -0.1223 269 HOH   B O   
7093 O O   . HOH   F .   ? 0.3474 0.4209 0.5371 0.0235  0.1298  -0.0714 270 HOH   B O   
7094 O O   . HOH   F .   ? 0.4472 0.3968 0.2508 -0.0116 0.0942  -0.0484 271 HOH   B O   
7095 O O   . HOH   F .   ? 0.2285 0.2504 0.2033 0.0657  -0.0217 -0.0048 272 HOH   B O   
7096 O O   . HOH   F .   ? 0.5542 0.7090 0.3052 0.0207  -0.0999 0.1943  273 HOH   B O   
7097 O O   . HOH   F .   ? 0.4054 0.2616 0.3117 -0.0545 0.0512  -0.0792 274 HOH   B O   
7098 O O   . HOH   F .   ? 0.2271 0.2222 0.1812 0.0194  0.0014  0.0029  275 HOH   B O   
7099 O O   . HOH   F .   ? 0.1888 0.1824 0.1638 -0.0431 -0.0376 0.0077  276 HOH   B O   
7100 O O   . HOH   F .   ? 0.2740 0.3606 0.3331 -0.0730 -0.0457 -0.0197 277 HOH   B O   
7101 O O   . HOH   F .   ? 0.6419 0.5071 0.4787 0.1211  0.0413  -0.0840 278 HOH   B O   
7102 O O   . HOH   F .   ? 0.1721 0.1435 0.4660 -0.0057 -0.0206 -0.0103 279 HOH   B O   
7103 O O   . HOH   F .   ? 0.2776 0.1962 0.2941 -0.0639 0.0350  -0.0277 280 HOH   B O   
7104 O O   . HOH   F .   ? 0.4595 0.2948 0.4486 -0.0846 0.0660  0.0941  281 HOH   B O   
7105 O O   . HOH   F .   ? 0.6053 0.3842 0.2772 0.2719  0.0685  0.0538  282 HOH   B O   
7106 O O   . HOH   F .   ? 0.3804 0.2799 0.2093 0.0454  -0.0830 -0.0306 283 HOH   B O   
7107 O O   . HOH   F .   ? 0.3044 0.7022 0.6461 0.0560  -0.1064 -0.0524 284 HOH   B O   
7108 O O   . HOH   F .   ? 0.3243 0.3562 0.4840 0.1057  -0.0442 -0.0942 285 HOH   B O   
7109 O O   . HOH   F .   ? 0.1670 0.1562 0.3303 -0.0104 -0.0052 -0.0048 286 HOH   B O   
7110 O O   . HOH   F .   ? 0.3418 0.2174 0.3634 -0.0335 -0.1450 0.0515  287 HOH   B O   
7111 O O   . HOH   F .   ? 0.1619 0.1509 0.1688 0.0054  0.0086  0.0039  288 HOH   B O   
7112 O O   . HOH   F .   ? 0.3757 0.6671 0.3365 0.1516  -0.1004 0.0134  289 HOH   B O   
7113 O O   . HOH   F .   ? 0.2401 0.2591 0.3163 0.0137  -0.0716 0.0356  290 HOH   B O   
7114 O O   . HOH   F .   ? 0.2144 0.5627 0.4165 -0.0439 -0.0271 -0.1176 291 HOH   B O   
7115 O O   . HOH   F .   ? 0.4353 0.4479 0.2070 0.0005  0.0541  0.0379  292 HOH   B O   
7116 O O   . HOH   F .   ? 0.2581 0.4603 0.5364 -0.0734 -0.1330 0.1075  293 HOH   B O   
7117 O O   . HOH   F .   ? 0.1672 0.1912 0.2852 0.0205  -0.0038 0.0264  294 HOH   B O   
7118 O O   . HOH   F .   ? 0.1636 0.1986 0.1619 -0.0113 -0.0159 0.0066  295 HOH   B O   
7119 O O   . HOH   F .   ? 0.1694 0.3515 0.4283 0.0156  0.0190  -0.1522 296 HOH   B O   
7120 O O   . HOH   F .   ? 0.4117 0.3602 0.3821 -0.0420 -0.0956 0.0256  297 HOH   B O   
7121 O O   . HOH   F .   ? 0.1995 0.3164 0.4851 0.0032  -0.0615 0.0022  298 HOH   B O   
7122 O O   . HOH   F .   ? 0.5276 0.3032 0.2647 -0.1979 0.1042  -0.0134 299 HOH   B O   
7123 O O   . HOH   F .   ? 0.2284 0.2906 0.5514 0.0690  -0.0474 -0.1220 300 HOH   B O   
7124 O O   . HOH   F .   ? 0.3291 0.4257 0.3569 -0.1600 0.1162  -0.0954 301 HOH   B O   
7125 O O   . HOH   F .   ? 0.4637 0.3751 0.2495 0.1196  -0.0768 0.0559  302 HOH   B O   
7126 O O   . HOH   F .   ? 0.3001 0.2954 0.2443 -0.0309 0.0256  -0.1270 303 HOH   B O   
7127 O O   . HOH   F .   ? 0.3239 0.2952 0.4820 -0.0424 -0.0934 0.1395  304 HOH   B O   
7128 O O   . HOH   F .   ? 0.2151 0.2124 0.1657 -0.0085 0.0313  0.0079  305 HOH   B O   
7129 O O   . HOH   F .   ? 0.3320 0.1822 0.4007 0.0698  0.1467  0.0647  306 HOH   B O   
7130 O O   . HOH   F .   ? 0.2674 0.6451 0.2332 0.0896  -0.0434 -0.0691 307 HOH   B O   
7131 O O   . HOH   F .   ? 0.4821 0.3542 0.2859 0.0702  -0.0180 -0.0658 308 HOH   B O   
7132 O O   . HOH   F .   ? 0.2094 0.1574 0.3124 0.0294  -0.1048 -0.0142 309 HOH   B O   
7133 O O   . HOH   F .   ? 0.5699 0.5086 0.4400 -0.1107 0.0095  0.0450  310 HOH   B O   
7134 O O   . HOH   F .   ? 0.1593 0.1877 0.2698 -0.0233 -0.0107 0.0009  311 HOH   B O   
7135 O O   . HOH   F .   ? 0.2353 0.1665 0.2596 -0.0183 -0.0224 -0.0076 312 HOH   B O   
7136 O O   . HOH   F .   ? 0.1711 0.1583 0.2303 0.0044  -0.0010 0.0101  313 HOH   B O   
7137 O O   . HOH   F .   ? 0.4326 0.2210 0.3277 0.1403  0.1372  0.0372  314 HOH   B O   
7138 O O   . HOH   F .   ? 0.5496 0.4422 0.5426 0.0747  0.1486  -0.0034 315 HOH   B O   
7139 O O   . HOH   F .   ? 0.2553 0.1466 0.2535 -0.0130 -0.0321 0.0295  316 HOH   B O   
7140 O O   . HOH   F .   ? 0.2850 0.3132 0.4659 -0.0668 -0.1549 0.1420  317 HOH   B O   
7141 O O   . HOH   F .   ? 0.2765 0.3121 0.3871 -0.0462 0.1358  -0.0793 318 HOH   B O   
7142 O O   . HOH   F .   ? 0.1709 0.1502 0.3295 0.0086  0.0034  0.0015  319 HOH   B O   
7143 O O   . HOH   F .   ? 0.2613 0.2270 0.2284 0.0101  -0.0173 0.0197  320 HOH   B O   
7144 O O   . HOH   F .   ? 0.1631 0.2672 0.2285 -0.0087 -0.0167 0.0536  321 HOH   B O   
7145 O O   . HOH   F .   ? 0.5018 0.4369 0.2239 0.0642  -0.0592 -0.0650 322 HOH   B O   
7146 O O   . HOH   F .   ? 0.4689 0.4743 0.5938 0.0991  -0.0162 0.1164  323 HOH   B O   
7147 O O   . HOH   F .   ? 0.7308 0.1960 0.3606 -0.0018 -0.1157 0.0024  324 HOH   B O   
7148 O O   . HOH   F .   ? 0.2858 0.6666 0.5256 -0.1385 -0.0580 0.1067  325 HOH   B O   
7149 O O   . HOH   F .   ? 0.5340 0.2596 0.3095 0.0573  0.0008  0.0667  326 HOH   B O   
7150 O O   . HOH   F .   ? 0.6972 0.5425 0.5554 0.3017  -0.0095 -0.0295 327 HOH   B O   
7151 O O   . HOH   F .   ? 0.4557 0.3501 0.4875 0.1299  0.1969  0.1779  328 HOH   B O   
7152 O O   . HOH   F .   ? 0.1579 0.1761 0.3141 -0.0101 -0.0050 -0.0228 329 HOH   B O   
7153 O O   . HOH   F .   ? 0.1903 0.1892 0.2684 0.0328  0.0395  0.0175  330 HOH   B O   
7154 O O   . HOH   F .   ? 0.1892 0.2910 0.2846 0.0478  -0.0207 -0.0824 331 HOH   B O   
7155 O O   . HOH   F .   ? 0.5540 0.3960 0.3726 -0.0065 0.1196  0.1584  332 HOH   B O   
7156 O O   . HOH   F .   ? 0.2770 0.2006 0.4128 -0.0161 -0.0087 0.0228  333 HOH   B O   
7157 O O   . HOH   F .   ? 0.2316 0.2567 0.5067 -0.0570 -0.0124 0.1346  334 HOH   B O   
7158 O O   . HOH   F .   ? 0.5907 0.3288 0.3884 0.0173  0.0749  -0.1506 335 HOH   B O   
7159 O O   . HOH   F .   ? 0.4581 0.3775 0.6648 0.1067  -0.0156 0.1139  336 HOH   B O   
7160 O O   . HOH   F .   ? 0.3714 0.3610 0.7663 -0.0283 -0.1019 0.1741  337 HOH   B O   
7161 O O   . HOH   F .   ? 0.1744 0.1456 0.2169 0.0069  -0.0203 0.0067  338 HOH   B O   
7162 O O   . HOH   F .   ? 0.5967 0.3910 0.4700 -0.0466 -0.0935 -0.0708 339 HOH   B O   
7163 O O   . HOH   F .   ? 0.4301 0.6984 0.3489 -0.0601 0.0083  0.1438  340 HOH   B O   
7164 O O   . HOH   F .   ? 0.7120 0.5867 0.3572 0.0657  -0.0525 0.1697  341 HOH   B O   
7165 O O   . HOH   F .   ? 0.5269 0.5706 0.3616 -0.0518 -0.1074 0.0256  342 HOH   B O   
7166 O O   . HOH   F .   ? 0.4494 0.4335 0.3291 0.0977  -0.1200 -0.1161 343 HOH   B O   
7167 O O   . HOH   F .   ? 0.2459 0.5217 0.5965 -0.0444 -0.0496 -0.0421 344 HOH   B O   
7168 O O   . HOH   F .   ? 0.2633 0.2051 0.3640 0.0508  -0.0789 -0.0650 345 HOH   B O   
7169 O O   . HOH   F .   ? 0.4973 0.5699 0.4541 -0.1179 0.0754  0.0158  346 HOH   B O   
7170 O O   . HOH   F .   ? 0.2177 0.1915 0.2955 -0.0197 0.0609  -0.0105 347 HOH   B O   
7171 O O   . HOH   F .   ? 0.4740 0.3492 0.5650 -0.0928 0.1153  0.1107  348 HOH   B O   
7172 O O   . HOH   F .   ? 0.3252 0.2334 0.4003 -0.0263 -0.0775 -0.0378 349 HOH   B O   
7173 O O   . HOH   F .   ? 0.4432 0.5244 0.4000 -0.1353 -0.1003 -0.0815 350 HOH   B O   
7174 O O   . HOH   F .   ? 0.4297 0.6105 0.6067 0.0196  -0.0993 0.0290  351 HOH   B O   
7175 O O   . HOH   F .   ? 0.4901 0.7044 0.7457 0.1394  0.0363  -0.0334 352 HOH   B O   
7176 O O   . HOH   F .   ? 0.3235 0.4080 0.4912 -0.1166 0.0330  -0.0103 353 HOH   B O   
7177 O O   . HOH   F .   ? 0.2527 0.3574 0.5239 0.0294  0.0402  0.0165  354 HOH   B O   
7178 O O   . HOH   F .   ? 0.2154 0.5634 0.3217 0.1237  -0.0360 -0.1172 355 HOH   B O   
7179 O O   . HOH   F .   ? 0.3973 0.2258 0.3683 -0.0812 0.0549  -0.0999 356 HOH   B O   
7180 O O   . HOH   F .   ? 0.4690 0.5497 0.4505 0.1774  -0.1026 0.1203  357 HOH   B O   
7181 O O   . HOH   F .   ? 0.4784 0.3696 0.4131 0.0643  0.1619  -0.0410 358 HOH   B O   
7182 O O   . HOH   F .   ? 0.4672 0.3148 0.3608 -0.1337 -0.0734 0.0081  359 HOH   B O   
7183 O O   . HOH   F .   ? 0.5657 0.3353 0.6350 -0.0411 -0.1408 -0.0173 360 HOH   B O   
7184 O O   . HOH   F .   ? 0.5099 0.4217 0.6732 -0.0219 0.1077  0.1413  361 HOH   B O   
7185 O O   . HOH   F .   ? 0.4980 0.6021 0.3533 0.1459  -0.0696 0.0468  362 HOH   B O   
7186 O O   . HOH   F .   ? 0.6597 0.5537 0.5490 -0.0113 0.0989  0.0693  363 HOH   B O   
7187 O O   . HOH   F .   ? 0.2227 0.3417 0.5976 -0.0490 -0.0716 -0.0465 364 HOH   B O   
7188 O O   . HOH   F .   ? 0.5986 0.2358 0.3425 0.0062  0.0117  0.0892  365 HOH   B O   
7189 O O   . HOH   F .   ? 0.4262 0.3333 0.4950 -0.0014 -0.1632 0.0722  366 HOH   B O   
7190 O O   . HOH   F .   ? 0.6010 0.6608 0.3943 0.1547  -0.1356 0.0819  367 HOH   B O   
7191 O O   . HOH   F .   ? 0.6209 0.5035 0.4565 0.1158  0.1381  0.0050  368 HOH   B O   
7192 O O   . HOH   F .   ? 0.5387 0.6322 0.5168 -0.1025 -0.1111 -0.0933 369 HOH   B O   
7193 O O   . HOH   F .   ? 0.5138 0.3637 0.3913 0.0049  -0.1220 0.0267  370 HOH   B O   
7194 O O   . HOH   F .   ? 0.4619 0.4957 0.5587 0.2191  0.0401  0.0508  371 HOH   B O   
7195 O O   . HOH   F .   ? 0.8509 0.7565 0.6046 0.1534  -0.0923 -0.0049 372 HOH   B O   
7196 O O   . HOH   F .   ? 0.4987 0.3088 0.5610 -0.1367 -0.0833 0.0164  373 HOH   B O   
7197 O O   . HOH   F .   ? 0.5658 0.4600 0.3676 -0.0616 -0.1179 -0.0893 374 HOH   B O   
7198 O O   . HOH   F .   ? 0.2652 0.3944 0.3757 0.0544  -0.0588 -0.0624 375 HOH   B O   
7199 O O   . HOH   F .   ? 0.3999 0.5009 0.4489 -0.0756 -0.0841 0.0298  376 HOH   B O   
7200 O O   . HOH   F .   ? 0.4039 0.4239 0.2248 -0.0164 0.0562  -0.0147 377 HOH   B O   
7201 O O   . HOH   F .   ? 0.3924 0.6047 0.6285 0.1131  -0.0723 0.1995  378 HOH   B O   
7202 O O   . HOH   F .   ? 0.4881 0.7006 0.6456 0.1375  0.0086  0.2614  379 HOH   B O   
7203 O O   . HOH   F .   ? 0.5653 0.7141 0.7335 -0.0710 0.0976  0.0848  380 HOH   B O   
7204 O O   . HOH   F .   ? 0.7361 0.3774 0.5748 -0.0670 -0.1210 0.0050  381 HOH   B O   
7205 O O   . HOH   F .   ? 0.3276 0.7272 0.4808 0.1984  0.0892  0.1629  382 HOH   B O   
7206 O O   . HOH   F .   ? 0.2741 0.2664 0.2977 0.0010  0.0074  0.0028  383 HOH   B O   
7207 O O   . HOH   F .   ? 0.5776 0.5960 0.4239 -0.1245 0.0131  -0.1405 384 HOH   B O   
7208 O O   . HOH   F .   ? 0.5572 0.4298 0.4990 -0.0979 -0.0426 0.1090  385 HOH   B O   
7209 O O   . HOH   F .   ? 0.6735 0.4519 0.4713 0.0625  0.0572  -0.1341 386 HOH   B O   
7210 O O   . HOH   F .   ? 0.6647 0.5706 0.4524 0.2391  0.0924  0.0156  387 HOH   B O   
7211 O O   . HOH   F .   ? 0.5439 0.4255 0.3445 0.0624  0.1089  -0.0261 388 HOH   B O   
7212 O O   . HOH   F .   ? 0.2834 0.3966 0.3482 -0.0423 -0.1064 -0.0482 389 HOH   B O   
7213 O O   . HOH   F .   ? 0.4054 0.2433 0.3560 0.0944  -0.0640 -0.0224 390 HOH   B O   
7214 O O   . HOH   F .   ? 0.4987 0.2281 0.5348 -0.0711 0.0445  0.0749  391 HOH   B O   
7215 O O   . HOH   F .   ? 0.2485 0.5102 0.6097 -0.1317 -0.0595 0.0116  392 HOH   B O   
7216 O O   . HOH   F .   ? 0.5476 0.3631 0.4229 0.0425  0.0352  0.0342  393 HOH   B O   
7217 O O   . HOH   F .   ? 0.6463 0.7818 0.8420 0.2890  -0.1175 0.2551  394 HOH   B O   
7218 O O   . HOH   F .   ? 0.4515 0.4563 0.3424 0.0296  0.0684  0.0338  395 HOH   B O   
7219 O O   . HOH   F .   ? 0.2003 0.3012 0.5809 -0.0606 -0.0671 0.0642  396 HOH   B O   
7220 O O   . HOH   F .   ? 0.3263 0.4167 0.3340 0.0428  0.0123  -0.0538 397 HOH   B O   
7221 O O   . HOH   F .   ? 0.4787 0.5998 0.4494 0.1655  -0.0530 -0.1165 398 HOH   B O   
7222 O O   . HOH   F .   ? 0.5837 0.3570 0.2943 -0.1587 -0.0591 0.0797  399 HOH   B O   
7223 O O   . HOH   F .   ? 0.5820 0.5314 0.3994 0.2061  -0.0502 -0.0228 400 HOH   B O   
# 
