data_7HCC
# 
_entry.id   7HCC 
# 
_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   7HCC         pdb_00007hcc 10.2210/pdb7hcc/pdb 
WWPDB D_1001407294 ?            ?                   
# 
_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                        7HCC 
_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 '3-{2-[(5-amino-1,3,4-thiadiazol-2-yl)sulfanyl]ethyl}-1,3-benzoxazol-2(3H)-one' 294.353   1   ? ? ? ? 
3 water       nat water                                                                           18.015    413 ? ? ? ? 
# 
_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 '3-{2-[(5-amino-1,3,4-thiadiazol-2-yl)sulfanyl]ethyl}-1,3-benzoxazol-2(3H)-one' A1A41 
3 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 
A1A41 non-polymer         . '3-{2-[(5-amino-1,3,4-thiadiazol-2-yl)sulfanyl]ethyl}-1,3-benzoxazol-2(3H)-one' ? 'C11 H10 N4 O2 S2' 
294.353 
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 
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 A1A41 1   201 201  A1A41 LA1 A . 
D 3 HOH   1   301 196  HOH   HOH A . 
D 3 HOH   2   302 292  HOH   HOH A . 
D 3 HOH   3   303 209  HOH   HOH A . 
D 3 HOH   4   304 1295 HOH   HOH A . 
D 3 HOH   5   305 625  HOH   HOH A . 
D 3 HOH   6   306 5    HOH   HOH A . 
D 3 HOH   7   307 151  HOH   HOH A . 
D 3 HOH   8   308 76   HOH   HOH A . 
D 3 HOH   9   309 109  HOH   HOH A . 
D 3 HOH   10  310 662  HOH   HOH A . 
D 3 HOH   11  311 229  HOH   HOH A . 
D 3 HOH   12  312 236  HOH   HOH A . 
D 3 HOH   13  313 964  HOH   HOH A . 
D 3 HOH   14  314 124  HOH   HOH A . 
D 3 HOH   15  315 225  HOH   HOH A . 
D 3 HOH   16  316 136  HOH   HOH A . 
D 3 HOH   17  317 241  HOH   HOH A . 
D 3 HOH   18  318 192  HOH   HOH A . 
D 3 HOH   19  319 15   HOH   HOH A . 
D 3 HOH   20  320 153  HOH   HOH A . 
D 3 HOH   21  321 1301 HOH   HOH A . 
D 3 HOH   22  322 337  HOH   HOH A . 
D 3 HOH   23  323 247  HOH   HOH A . 
D 3 HOH   24  324 164  HOH   HOH A . 
D 3 HOH   25  325 1300 HOH   HOH A . 
D 3 HOH   26  326 140  HOH   HOH A . 
D 3 HOH   27  327 320  HOH   HOH A . 
D 3 HOH   28  328 105  HOH   HOH A . 
D 3 HOH   29  329 661  HOH   HOH A . 
D 3 HOH   30  330 469  HOH   HOH A . 
D 3 HOH   31  331 3    HOH   HOH A . 
D 3 HOH   32  332 393  HOH   HOH A . 
D 3 HOH   33  333 86   HOH   HOH A . 
D 3 HOH   34  334 630  HOH   HOH A . 
D 3 HOH   35  335 42   HOH   HOH A . 
D 3 HOH   36  336 93   HOH   HOH A . 
D 3 HOH   37  337 354  HOH   HOH A . 
D 3 HOH   38  338 396  HOH   HOH A . 
D 3 HOH   39  339 165  HOH   HOH A . 
D 3 HOH   40  340 102  HOH   HOH A . 
D 3 HOH   41  341 92   HOH   HOH A . 
D 3 HOH   42  342 296  HOH   HOH A . 
D 3 HOH   43  343 162  HOH   HOH A . 
D 3 HOH   44  344 36   HOH   HOH A . 
D 3 HOH   45  345 17   HOH   HOH A . 
D 3 HOH   46  346 66   HOH   HOH A . 
D 3 HOH   47  347 2    HOH   HOH A . 
D 3 HOH   48  348 139  HOH   HOH A . 
D 3 HOH   49  349 186  HOH   HOH A . 
D 3 HOH   50  350 1290 HOH   HOH A . 
D 3 HOH   51  351 19   HOH   HOH A . 
D 3 HOH   52  352 45   HOH   HOH A . 
D 3 HOH   53  353 81   HOH   HOH A . 
D 3 HOH   54  354 169  HOH   HOH A . 
D 3 HOH   55  355 138  HOH   HOH A . 
D 3 HOH   56  356 159  HOH   HOH A . 
D 3 HOH   57  357 57   HOH   HOH A . 
D 3 HOH   58  358 939  HOH   HOH A . 
D 3 HOH   59  359 1296 HOH   HOH A . 
D 3 HOH   60  360 46   HOH   HOH A . 
D 3 HOH   61  361 5    HOH   HOH A . 
D 3 HOH   62  362 461  HOH   HOH A . 
D 3 HOH   63  363 49   HOH   HOH A . 
D 3 HOH   64  364 56   HOH   HOH A . 
D 3 HOH   65  365 134  HOH   HOH A . 
D 3 HOH   66  366 1283 HOH   HOH A . 
D 3 HOH   67  367 155  HOH   HOH A . 
D 3 HOH   68  368 78   HOH   HOH A . 
D 3 HOH   69  369 39   HOH   HOH A . 
D 3 HOH   70  370 218  HOH   HOH A . 
D 3 HOH   71  371 154  HOH   HOH A . 
D 3 HOH   72  372 18   HOH   HOH A . 
D 3 HOH   73  373 27   HOH   HOH A . 
D 3 HOH   74  374 21   HOH   HOH A . 
D 3 HOH   75  375 35   HOH   HOH A . 
D 3 HOH   76  376 1310 HOH   HOH A . 
D 3 HOH   77  377 405  HOH   HOH A . 
D 3 HOH   78  378 409  HOH   HOH A . 
D 3 HOH   79  379 26   HOH   HOH A . 
D 3 HOH   80  380 148  HOH   HOH A . 
D 3 HOH   81  381 116  HOH   HOH A . 
D 3 HOH   82  382 366  HOH   HOH A . 
D 3 HOH   83  383 83   HOH   HOH A . 
D 3 HOH   84  384 199  HOH   HOH A . 
D 3 HOH   85  385 4    HOH   HOH A . 
D 3 HOH   86  386 33   HOH   HOH A . 
D 3 HOH   87  387 58   HOH   HOH A . 
D 3 HOH   88  388 24   HOH   HOH A . 
D 3 HOH   89  389 333  HOH   HOH A . 
D 3 HOH   90  390 67   HOH   HOH A . 
D 3 HOH   91  391 1309 HOH   HOH A . 
D 3 HOH   92  392 85   HOH   HOH A . 
D 3 HOH   93  393 1313 HOH   HOH A . 
D 3 HOH   94  394 1308 HOH   HOH A . 
D 3 HOH   95  395 1275 HOH   HOH A . 
D 3 HOH   96  396 303  HOH   HOH A . 
D 3 HOH   97  397 12   HOH   HOH A . 
D 3 HOH   98  398 6    HOH   HOH A . 
D 3 HOH   99  399 132  HOH   HOH A . 
D 3 HOH   100 400 1315 HOH   HOH A . 
D 3 HOH   101 401 74   HOH   HOH A . 
D 3 HOH   102 402 3    HOH   HOH A . 
D 3 HOH   103 403 397  HOH   HOH A . 
D 3 HOH   104 404 493  HOH   HOH A . 
D 3 HOH   105 405 34   HOH   HOH A . 
D 3 HOH   106 406 1279 HOH   HOH A . 
D 3 HOH   107 407 582  HOH   HOH A . 
D 3 HOH   108 408 68   HOH   HOH A . 
D 3 HOH   109 409 278  HOH   HOH A . 
D 3 HOH   110 410 96   HOH   HOH A . 
D 3 HOH   111 411 1289 HOH   HOH A . 
D 3 HOH   112 412 351  HOH   HOH A . 
D 3 HOH   113 413 53   HOH   HOH A . 
D 3 HOH   114 414 1068 HOH   HOH A . 
D 3 HOH   115 415 125  HOH   HOH A . 
D 3 HOH   116 416 8    HOH   HOH A . 
D 3 HOH   117 417 381  HOH   HOH A . 
D 3 HOH   118 418 1222 HOH   HOH A . 
D 3 HOH   119 419 121  HOH   HOH A . 
D 3 HOH   120 420 115  HOH   HOH A . 
D 3 HOH   121 421 95   HOH   HOH A . 
D 3 HOH   122 422 122  HOH   HOH A . 
D 3 HOH   123 423 212  HOH   HOH A . 
D 3 HOH   124 424 25   HOH   HOH A . 
D 3 HOH   125 425 2    HOH   HOH A . 
D 3 HOH   126 426 123  HOH   HOH A . 
D 3 HOH   127 427 281  HOH   HOH A . 
D 3 HOH   128 428 7    HOH   HOH A . 
D 3 HOH   129 429 156  HOH   HOH A . 
D 3 HOH   130 430 51   HOH   HOH A . 
D 3 HOH   131 431 40   HOH   HOH A . 
D 3 HOH   132 432 195  HOH   HOH A . 
D 3 HOH   133 433 71   HOH   HOH A . 
D 3 HOH   134 434 70   HOH   HOH A . 
D 3 HOH   135 435 16   HOH   HOH A . 
D 3 HOH   136 436 1    HOH   HOH A . 
D 3 HOH   137 437 73   HOH   HOH A . 
D 3 HOH   138 438 80   HOH   HOH A . 
D 3 HOH   139 439 6    HOH   HOH A . 
D 3 HOH   140 440 952  HOH   HOH A . 
D 3 HOH   141 441 94   HOH   HOH A . 
D 3 HOH   142 442 4    HOH   HOH A . 
D 3 HOH   143 443 97   HOH   HOH A . 
D 3 HOH   144 444 944  HOH   HOH A . 
D 3 HOH   145 445 188  HOH   HOH A . 
D 3 HOH   146 446 576  HOH   HOH A . 
D 3 HOH   147 447 1094 HOH   HOH A . 
D 3 HOH   148 448 104  HOH   HOH A . 
D 3 HOH   149 449 1238 HOH   HOH A . 
D 3 HOH   150 450 1286 HOH   HOH A . 
D 3 HOH   151 451 330  HOH   HOH A . 
D 3 HOH   152 452 1189 HOH   HOH A . 
D 3 HOH   153 453 79   HOH   HOH A . 
D 3 HOH   154 454 1119 HOH   HOH A . 
D 3 HOH   155 455 107  HOH   HOH A . 
D 3 HOH   156 456 509  HOH   HOH A . 
D 3 HOH   157 457 1134 HOH   HOH A . 
D 3 HOH   158 458 163  HOH   HOH A . 
D 3 HOH   159 459 756  HOH   HOH A . 
D 3 HOH   160 460 408  HOH   HOH A . 
D 3 HOH   161 461 726  HOH   HOH A . 
D 3 HOH   162 462 126  HOH   HOH A . 
D 3 HOH   163 463 361  HOH   HOH A . 
D 3 HOH   164 464 801  HOH   HOH A . 
D 3 HOH   165 465 556  HOH   HOH A . 
D 3 HOH   166 466 319  HOH   HOH A . 
D 3 HOH   167 467 280  HOH   HOH A . 
D 3 HOH   168 468 63   HOH   HOH A . 
D 3 HOH   169 469 1276 HOH   HOH A . 
D 3 HOH   170 470 250  HOH   HOH A . 
D 3 HOH   171 471 1307 HOH   HOH A . 
D 3 HOH   172 472 342  HOH   HOH A . 
D 3 HOH   173 473 1287 HOH   HOH A . 
D 3 HOH   174 474 1306 HOH   HOH A . 
D 3 HOH   175 475 695  HOH   HOH A . 
D 3 HOH   176 476 919  HOH   HOH A . 
D 3 HOH   177 477 674  HOH   HOH A . 
D 3 HOH   178 478 370  HOH   HOH A . 
D 3 HOH   179 479 267  HOH   HOH A . 
D 3 HOH   180 480 202  HOH   HOH A . 
D 3 HOH   181 481 135  HOH   HOH A . 
D 3 HOH   182 482 224  HOH   HOH A . 
D 3 HOH   183 483 309  HOH   HOH A . 
D 3 HOH   184 484 318  HOH   HOH A . 
D 3 HOH   185 485 521  HOH   HOH A . 
D 3 HOH   186 486 1299 HOH   HOH A . 
D 3 HOH   187 487 805  HOH   HOH A . 
D 3 HOH   188 488 263  HOH   HOH A . 
D 3 HOH   189 489 152  HOH   HOH A . 
D 3 HOH   190 490 711  HOH   HOH A . 
D 3 HOH   191 491 331  HOH   HOH A . 
D 3 HOH   192 492 315  HOH   HOH A . 
D 3 HOH   193 493 1314 HOH   HOH A . 
D 3 HOH   194 494 941  HOH   HOH A . 
D 3 HOH   195 495 1071 HOH   HOH A . 
D 3 HOH   196 496 208  HOH   HOH A . 
D 3 HOH   197 497 356  HOH   HOH A . 
D 3 HOH   198 498 350  HOH   HOH A . 
D 3 HOH   199 499 180  HOH   HOH A . 
D 3 HOH   200 500 371  HOH   HOH A . 
D 3 HOH   201 501 363  HOH   HOH A . 
D 3 HOH   202 502 313  HOH   HOH A . 
D 3 HOH   203 503 326  HOH   HOH A . 
D 3 HOH   204 504 429  HOH   HOH A . 
D 3 HOH   205 505 185  HOH   HOH A . 
D 3 HOH   206 506 1284 HOH   HOH A . 
D 3 HOH   207 507 772  HOH   HOH A . 
D 3 HOH   208 508 376  HOH   HOH A . 
D 3 HOH   209 509 1074 HOH   HOH A . 
D 3 HOH   210 510 1292 HOH   HOH A . 
D 3 HOH   211 511 346  HOH   HOH A . 
D 3 HOH   212 512 1078 HOH   HOH A . 
E 3 HOH   1   201 64   HOH   HOH B . 
E 3 HOH   2   202 358  HOH   HOH B . 
E 3 HOH   3   203 398  HOH   HOH B . 
E 3 HOH   4   204 654  HOH   HOH B . 
E 3 HOH   5   205 364  HOH   HOH B . 
E 3 HOH   6   206 1249 HOH   HOH B . 
E 3 HOH   7   207 900  HOH   HOH B . 
E 3 HOH   8   208 758  HOH   HOH B . 
E 3 HOH   9   209 549  HOH   HOH B . 
E 3 HOH   10  210 240  HOH   HOH B . 
E 3 HOH   11  211 743  HOH   HOH B . 
E 3 HOH   12  212 264  HOH   HOH B . 
E 3 HOH   13  213 120  HOH   HOH B . 
E 3 HOH   14  214 353  HOH   HOH B . 
E 3 HOH   15  215 50   HOH   HOH B . 
E 3 HOH   16  216 276  HOH   HOH B . 
E 3 HOH   17  217 531  HOH   HOH B . 
E 3 HOH   18  218 232  HOH   HOH B . 
E 3 HOH   19  219 452  HOH   HOH B . 
E 3 HOH   20  220 131  HOH   HOH B . 
E 3 HOH   21  221 343  HOH   HOH B . 
E 3 HOH   22  222 723  HOH   HOH B . 
E 3 HOH   23  223 282  HOH   HOH B . 
E 3 HOH   24  224 332  HOH   HOH B . 
E 3 HOH   25  225 54   HOH   HOH B . 
E 3 HOH   26  226 205  HOH   HOH B . 
E 3 HOH   27  227 444  HOH   HOH B . 
E 3 HOH   28  228 272  HOH   HOH B . 
E 3 HOH   29  229 1278 HOH   HOH B . 
E 3 HOH   30  230 75   HOH   HOH B . 
E 3 HOH   31  231 128  HOH   HOH B . 
E 3 HOH   32  232 127  HOH   HOH B . 
E 3 HOH   33  233 1312 HOH   HOH B . 
E 3 HOH   34  234 82   HOH   HOH B . 
E 3 HOH   35  235 69   HOH   HOH B . 
E 3 HOH   36  236 1140 HOH   HOH B . 
E 3 HOH   37  237 110  HOH   HOH B . 
E 3 HOH   38  238 300  HOH   HOH B . 
E 3 HOH   39  239 1    HOH   HOH B . 
E 3 HOH   40  240 181  HOH   HOH B . 
E 3 HOH   41  241 14   HOH   HOH B . 
E 3 HOH   42  242 129  HOH   HOH B . 
E 3 HOH   43  243 325  HOH   HOH B . 
E 3 HOH   44  244 60   HOH   HOH B . 
E 3 HOH   45  245 30   HOH   HOH B . 
E 3 HOH   46  246 133  HOH   HOH B . 
E 3 HOH   47  247 9    HOH   HOH B . 
E 3 HOH   48  248 52   HOH   HOH B . 
E 3 HOH   49  249 166  HOH   HOH B . 
E 3 HOH   50  250 143  HOH   HOH B . 
E 3 HOH   51  251 231  HOH   HOH B . 
E 3 HOH   52  252 31   HOH   HOH B . 
E 3 HOH   53  253 347  HOH   HOH B . 
E 3 HOH   54  254 144  HOH   HOH B . 
E 3 HOH   55  255 150  HOH   HOH B . 
E 3 HOH   56  256 47   HOH   HOH B . 
E 3 HOH   57  257 41   HOH   HOH B . 
E 3 HOH   58  258 302  HOH   HOH B . 
E 3 HOH   59  259 172  HOH   HOH B . 
E 3 HOH   60  260 72   HOH   HOH B . 
E 3 HOH   61  261 10   HOH   HOH B . 
E 3 HOH   62  262 59   HOH   HOH B . 
E 3 HOH   63  263 61   HOH   HOH B . 
E 3 HOH   64  264 62   HOH   HOH B . 
E 3 HOH   65  265 20   HOH   HOH B . 
E 3 HOH   66  266 103  HOH   HOH B . 
E 3 HOH   67  267 391  HOH   HOH B . 
E 3 HOH   68  268 243  HOH   HOH B . 
E 3 HOH   69  269 11   HOH   HOH B . 
E 3 HOH   70  270 1106 HOH   HOH B . 
E 3 HOH   71  271 271  HOH   HOH B . 
E 3 HOH   72  272 77   HOH   HOH B . 
E 3 HOH   73  273 175  HOH   HOH B . 
E 3 HOH   74  274 84   HOH   HOH B . 
E 3 HOH   75  275 242  HOH   HOH B . 
E 3 HOH   76  276 252  HOH   HOH B . 
E 3 HOH   77  277 221  HOH   HOH B . 
E 3 HOH   78  278 114  HOH   HOH B . 
E 3 HOH   79  279 117  HOH   HOH B . 
E 3 HOH   80  280 22   HOH   HOH B . 
E 3 HOH   81  281 43   HOH   HOH B . 
E 3 HOH   82  282 1305 HOH   HOH B . 
E 3 HOH   83  283 1277 HOH   HOH B . 
E 3 HOH   84  284 106  HOH   HOH B . 
E 3 HOH   85  285 287  HOH   HOH B . 
E 3 HOH   86  286 13   HOH   HOH B . 
E 3 HOH   87  287 416  HOH   HOH B . 
E 3 HOH   88  288 147  HOH   HOH B . 
E 3 HOH   89  289 1066 HOH   HOH B . 
E 3 HOH   90  290 387  HOH   HOH B . 
E 3 HOH   91  291 137  HOH   HOH B . 
E 3 HOH   92  292 635  HOH   HOH B . 
E 3 HOH   93  293 297  HOH   HOH B . 
E 3 HOH   94  294 99   HOH   HOH B . 
E 3 HOH   95  295 160  HOH   HOH B . 
E 3 HOH   96  296 316  HOH   HOH B . 
E 3 HOH   97  297 299  HOH   HOH B . 
E 3 HOH   98  298 89   HOH   HOH B . 
E 3 HOH   99  299 88   HOH   HOH B . 
E 3 HOH   100 300 32   HOH   HOH B . 
E 3 HOH   101 301 235  HOH   HOH B . 
E 3 HOH   102 302 216  HOH   HOH B . 
E 3 HOH   103 303 112  HOH   HOH B . 
E 3 HOH   104 304 141  HOH   HOH B . 
E 3 HOH   105 305 704  HOH   HOH B . 
E 3 HOH   106 306 118  HOH   HOH B . 
E 3 HOH   107 307 220  HOH   HOH B . 
E 3 HOH   108 308 341  HOH   HOH B . 
E 3 HOH   109 309 142  HOH   HOH B . 
E 3 HOH   110 310 37   HOH   HOH B . 
E 3 HOH   111 311 215  HOH   HOH B . 
E 3 HOH   112 312 48   HOH   HOH B . 
E 3 HOH   113 313 101  HOH   HOH B . 
E 3 HOH   114 314 1291 HOH   HOH B . 
E 3 HOH   115 315 170  HOH   HOH B . 
E 3 HOH   116 316 91   HOH   HOH B . 
E 3 HOH   117 317 311  HOH   HOH B . 
E 3 HOH   118 318 182  HOH   HOH B . 
E 3 HOH   119 319 161  HOH   HOH B . 
E 3 HOH   120 320 23   HOH   HOH B . 
E 3 HOH   121 321 38   HOH   HOH B . 
E 3 HOH   122 322 44   HOH   HOH B . 
E 3 HOH   123 323 1274 HOH   HOH B . 
E 3 HOH   124 324 339  HOH   HOH B . 
E 3 HOH   125 325 28   HOH   HOH B . 
E 3 HOH   126 326 1126 HOH   HOH B . 
E 3 HOH   127 327 177  HOH   HOH B . 
E 3 HOH   128 328 100  HOH   HOH B . 
E 3 HOH   129 329 717  HOH   HOH B . 
E 3 HOH   130 330 55   HOH   HOH B . 
E 3 HOH   131 331 29   HOH   HOH B . 
E 3 HOH   132 332 445  HOH   HOH B . 
E 3 HOH   133 333 1285 HOH   HOH B . 
E 3 HOH   134 334 334  HOH   HOH B . 
E 3 HOH   135 335 98   HOH   HOH B . 
E 3 HOH   136 336 197  HOH   HOH B . 
E 3 HOH   137 337 234  HOH   HOH B . 
E 3 HOH   138 338 207  HOH   HOH B . 
E 3 HOH   139 339 65   HOH   HOH B . 
E 3 HOH   140 340 1294 HOH   HOH B . 
E 3 HOH   141 341 619  HOH   HOH B . 
E 3 HOH   142 342 178  HOH   HOH B . 
E 3 HOH   143 343 1293 HOH   HOH B . 
E 3 HOH   144 344 362  HOH   HOH B . 
E 3 HOH   145 345 90   HOH   HOH B . 
E 3 HOH   146 346 463  HOH   HOH B . 
E 3 HOH   147 347 960  HOH   HOH B . 
E 3 HOH   148 348 191  HOH   HOH B . 
E 3 HOH   149 349 1304 HOH   HOH B . 
E 3 HOH   150 350 335  HOH   HOH B . 
E 3 HOH   151 351 623  HOH   HOH B . 
E 3 HOH   152 352 304  HOH   HOH B . 
E 3 HOH   153 353 1046 HOH   HOH B . 
E 3 HOH   154 354 1280 HOH   HOH B . 
E 3 HOH   155 355 541  HOH   HOH B . 
E 3 HOH   156 356 290  HOH   HOH B . 
E 3 HOH   157 357 203  HOH   HOH B . 
E 3 HOH   158 358 87   HOH   HOH B . 
E 3 HOH   159 359 389  HOH   HOH B . 
E 3 HOH   160 360 1077 HOH   HOH B . 
E 3 HOH   161 361 479  HOH   HOH B . 
E 3 HOH   162 362 283  HOH   HOH B . 
E 3 HOH   163 363 718  HOH   HOH B . 
E 3 HOH   164 364 1072 HOH   HOH B . 
E 3 HOH   165 365 1316 HOH   HOH B . 
E 3 HOH   166 366 898  HOH   HOH B . 
E 3 HOH   167 367 667  HOH   HOH B . 
E 3 HOH   168 368 340  HOH   HOH B . 
E 3 HOH   169 369 373  HOH   HOH B . 
E 3 HOH   170 370 291  HOH   HOH B . 
E 3 HOH   171 371 615  HOH   HOH B . 
E 3 HOH   172 372 190  HOH   HOH B . 
E 3 HOH   173 373 1303 HOH   HOH B . 
E 3 HOH   174 374 310  HOH   HOH B . 
E 3 HOH   175 375 149  HOH   HOH B . 
E 3 HOH   176 376 431  HOH   HOH B . 
E 3 HOH   177 377 1163 HOH   HOH B . 
E 3 HOH   178 378 1173 HOH   HOH B . 
E 3 HOH   179 379 183  HOH   HOH B . 
E 3 HOH   180 380 1000 HOH   HOH B . 
E 3 HOH   181 381 418  HOH   HOH B . 
E 3 HOH   182 382 1311 HOH   HOH B . 
E 3 HOH   183 383 176  HOH   HOH B . 
E 3 HOH   184 384 424  HOH   HOH B . 
E 3 HOH   185 385 1298 HOH   HOH B . 
E 3 HOH   186 386 470  HOH   HOH B . 
E 3 HOH   187 387 248  HOH   HOH B . 
E 3 HOH   188 388 491  HOH   HOH B . 
E 3 HOH   189 389 265  HOH   HOH B . 
E 3 HOH   190 390 981  HOH   HOH B . 
E 3 HOH   191 391 184  HOH   HOH B . 
E 3 HOH   192 392 360  HOH   HOH B . 
E 3 HOH   193 393 410  HOH   HOH B . 
E 3 HOH   194 394 355  HOH   HOH B . 
E 3 HOH   195 395 314  HOH   HOH B . 
E 3 HOH   196 396 274  HOH   HOH B . 
E 3 HOH   197 397 566  HOH   HOH B . 
E 3 HOH   198 398 157  HOH   HOH B . 
E 3 HOH   199 399 792  HOH   HOH B . 
E 3 HOH   200 400 321  HOH   HOH B . 
E 3 HOH   201 401 558  HOH   HOH B . 
# 
loop_
_software.pdbx_ordinal 
_software.name 
_software.version 
_software.date 
_software.type 
_software.contact_author 
_software.contact_author_email 
_software.classification 
_software.location 
_software.language 
_software.citation_id 
1 PHENIX      1.21.1_5286    ?               package 'Paul D. Adams'   PDAdams@lbl.gov                         refinement        
http://www.phenix-online.org/                                                C++ ? 
2 Aimless     0.7.15         02/11/23        program 'Phil Evans'      ?                                       'data scaling'    
http://www.mrc-lmb.cam.ac.uk/harry/pre/aimless.html                          ?   ? 
3 PDB_EXTRACT 3.28           'Apr. 15, 2021' package PDB               deposit@deposit.rcsb.org                'data extraction' 
http://sw-tools.pdb.org/apps/PDB_EXTRACT/                                    C++ ? 
4 XDS         'Jun 30, 2023' 'Jun. 30, 2023' program 'Wolfgang Kabsch' Wolfgang.Kabsch@mpimf-heidelberg.mpg.de 'data reduction'  
http://xds.mpimf-heidelberg.mpg.de                                           ?   ? 
5 PHASER      2.8.3          'May 17, 2020'  program 'Randy J. Read'   cimr-phaser@lists.cam.ac.uk             phasing           
https://www.phaser.cimr.cam.ac.uk/index.php/Phaser_Crystallographic_Software ?   ? 
# 
_cell.entry_id           7HCC 
_cell.length_a           88.733 
_cell.length_b           88.733 
_cell.length_c           39.550 
_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                         7HCC 
_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          7HCC 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_Matthews      2.14 
_exptl_crystal.density_percent_sol   42.65 
_exptl_crystal.density_meas          ? 
_exptl_crystal.description           ? 
_exptl_crystal.preparation           ? 
# 
_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.pdbx_serial_crystal_experiment   ? 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               PIXEL 
_diffrn_detector.type                   'DECTRIS PILATUS3 6M' 
_diffrn_detector.pdbx_collection_date   2022-06-29 
_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                     7HCC 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             44.370 
_reflns.d_resolution_high            1.020 
_reflns.number_obs                   156119 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         99.700 
_reflns.pdbx_Rmerge_I_obs            0.044 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        16.400 
_reflns.B_iso_Wilson_estimate        11.010 
_reflns.pdbx_redundancy              6.500 
_reflns.pdbx_Rrim_I_all              0.048 
_reflns.pdbx_Rpim_I_all              0.019 
_reflns.pdbx_CC_half                 0.999 
_reflns.pdbx_netI_over_av_sigmaI     ? 
_reflns.pdbx_number_measured_all     1008973 
_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                      ? 
_reflns.pdbx_CC_star                 ? 
# 
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 
_reflns_shell.pdbx_CC_star 
1 1 1.020 1.040  ? 43363 7613 ? 0.654 ? ? ? 5.700 ? 1.700  ? ? ? ? ? ? 98.200 0.720 0.295 0.885 ? 
1 2 5.590 44.370 ? 7106  1032 ? 0.025 ? ? ? 6.900 ? 48.900 ? ? ? ? ? ? 99.400 0.027 0.010 0.999 ? 
# 
_refine.entry_id                                 7HCC 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_d_res_high                            1.0200 
_refine.ls_d_res_low                             44.3700 
_refine.pdbx_ls_sigma_F                          1.370 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.ls_percent_reflns_obs                    99.6400 
_refine.ls_number_reflns_obs                     156054 
_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                          0.1379 
_refine.ls_R_factor_R_work                       0.1373 
_refine.ls_wR_factor_R_work                      ? 
_refine.ls_R_factor_R_free                       0.1501 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_percent_reflns_R_free                 4.8300 
_refine.ls_number_reflns_R_free                  7531 
_refine.ls_number_reflns_R_work                  148523 
_refine.ls_R_factor_R_free_error                 ? 
_refine.B_iso_mean                               17.4600 
_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                            0.0800 
_refine.overall_SU_B                             ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.pdbx_solvent_vdw_probe_radii             1.1000 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.B_iso_max                                62.130 
_refine.B_iso_min                                7.900 
_refine.pdbx_overall_phase_error                 14.4400 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_R_factor_R_free_error_details         ? 
# 
_refine_hist.cycle_id                         final 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.d_res_high                       1.0200 
_refine_hist.d_res_low                        44.3700 
_refine_hist.pdbx_number_atoms_ligand         29 
_refine_hist.number_atoms_solvent             413 
_refine_hist.number_atoms_total               2984 
_refine_hist.pdbx_number_residues_total       336 
_refine_hist.pdbx_B_iso_mean_ligand           26.27 
_refine_hist.pdbx_B_iso_mean_solvent          27.76 
_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 
_refine_ls_shell.R_factor_obs 
1.0200 1.0300  30 97.0000  4866 . 0.2568 0.2671 . 200 0.0000 5066 . 'X-RAY DIFFRACTION' . 
1.0300 1.0400  30 100.0000 4930 . 0.2099 0.2129 . 280 0.0000 5210 . 'X-RAY DIFFRACTION' . 
1.0400 1.0600  30 100.0000 4878 . 0.1870 0.1929 . 277 0.0000 5155 . 'X-RAY DIFFRACTION' . 
1.0600 1.0700  30 100.0000 4925 . 0.1808 0.1904 . 277 0.0000 5202 . 'X-RAY DIFFRACTION' . 
1.0700 1.0800  30 100.0000 4912 . 0.1685 0.1782 . 235 0.0000 5147 . 'X-RAY DIFFRACTION' . 
1.0800 1.1000  30 100.0000 4995 . 0.1584 0.1879 . 240 0.0000 5235 . 'X-RAY DIFFRACTION' . 
1.1000 1.1100  30 100.0000 4872 . 0.1462 0.1632 . 264 0.0000 5136 . 'X-RAY DIFFRACTION' . 
1.1100 1.1300  30 100.0000 4996 . 0.1378 0.1492 . 214 0.0000 5210 . 'X-RAY DIFFRACTION' . 
1.1300 1.1500  30 100.0000 4906 . 0.1310 0.1423 . 247 0.0000 5153 . 'X-RAY DIFFRACTION' . 
1.1500 1.1700  30 100.0000 4972 . 0.1236 0.1455 . 260 0.0000 5232 . 'X-RAY DIFFRACTION' . 
1.1700 1.1900  30 100.0000 4928 . 0.1218 0.1494 . 243 0.0000 5171 . 'X-RAY DIFFRACTION' . 
1.1900 1.2100  30 100.0000 4885 . 0.1150 0.1529 . 275 0.0000 5160 . 'X-RAY DIFFRACTION' . 
1.2100 1.2300  30 100.0000 5024 . 0.1151 0.1277 . 219 0.0000 5243 . 'X-RAY DIFFRACTION' . 
1.2300 1.2600  30 100.0000 4909 . 0.1177 0.1376 . 249 0.0000 5158 . 'X-RAY DIFFRACTION' . 
1.2600 1.2900  30 100.0000 4944 . 0.1179 0.1351 . 247 0.0000 5191 . 'X-RAY DIFFRACTION' . 
1.2900 1.3200  30 100.0000 4946 . 0.1177 0.1336 . 268 0.0000 5214 . 'X-RAY DIFFRACTION' . 
1.3200 1.3500  30 100.0000 4946 . 0.1215 0.1390 . 253 0.0000 5199 . 'X-RAY DIFFRACTION' . 
1.3500 1.3800  30 100.0000 4939 . 0.1224 0.1401 . 257 0.0000 5196 . 'X-RAY DIFFRACTION' . 
1.3800 1.4300  30 100.0000 4964 . 0.1209 0.1451 . 241 0.0000 5205 . 'X-RAY DIFFRACTION' . 
1.4300 1.4700  30 100.0000 4963 . 0.1173 0.1335 . 250 0.0000 5213 . 'X-RAY DIFFRACTION' . 
1.4700 1.5200  30 100.0000 4978 . 0.1158 0.1332 . 237 0.0000 5215 . 'X-RAY DIFFRACTION' . 
1.5200 1.5800  30 100.0000 4964 . 0.1183 0.1281 . 261 0.0000 5225 . 'X-RAY DIFFRACTION' . 
1.5800 1.6600  30 100.0000 4945 . 0.1190 0.1370 . 262 0.0000 5207 . 'X-RAY DIFFRACTION' . 
1.6600 1.7400  30 100.0000 5012 . 0.1264 0.1393 . 206 0.0000 5218 . 'X-RAY DIFFRACTION' . 
1.7400 1.8500  30 100.0000 4934 . 0.1303 0.1312 . 294 0.0000 5228 . 'X-RAY DIFFRACTION' . 
1.8500 2.0000  30 99.0000  4951 . 0.1340 0.1300 . 241 0.0000 5192 . 'X-RAY DIFFRACTION' . 
2.0000 2.2000  30 99.0000  4937 . 0.1361 0.1454 . 286 0.0000 5223 . 'X-RAY DIFFRACTION' . 
2.2000 2.5200  30 99.0000  4990 . 0.1389 0.1433 . 252 0.0000 5242 . 'X-RAY DIFFRACTION' . 
2.5200 3.1700  30 99.0000  4987 . 0.1507 0.1587 . 250 0.0000 5237 . 'X-RAY DIFFRACTION' . 
3.1700 44.3700 30 99.0000  5125 . 0.1477 0.1722 . 246 0.0000 5371 . 'X-RAY DIFFRACTION' . 
# 
_struct.entry_id                  7HCC 
_struct.title                     
'PanDDA analysis group deposition -- Crystal structure of SARS-CoV-2 NSP3 macrodomain in complex with AVI-0000296' 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_details        ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HCC 
_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 3 ? 
# 
_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 7HCC A 3 ? 169 ? P0DTD1 1025 ? 1191 ? 3 169 
2 1 7HCC 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 7HCC SER A 1 ? UNP P0DTD1 ? ? 'expression tag' 1 1 
1 7HCC MET A 2 ? UNP P0DTD1 ? ? 'expression tag' 2 2 
2 7HCC SER B 1 ? UNP P0DTD1 ? ? 'expression tag' 1 3 
2 7HCC 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 
2 1 B,E   
# 
_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 VAL A 95  ? O VAL A 95  
AA2 2 3 O CYS A 92  ? O CYS A 92  N LEU A 83  ? N LEU A 83  
AA3 1 2 N LEU B 10  ? N LEU B 10  O ILE B 18  ? O ILE B 18  
AA3 2 3 N TYR B 17  ? N TYR B 17  O LEU B 153 ? O LEU B 153 
AA3 3 4 O TYR B 152 ? O TYR B 152 N LEU B 122 ? N LEU B 122 
AA4 1 2 N ASN B 37  ? N ASN B 37  O LEU B 93  ? O LEU B 93  
AA4 2 3 O HIS B 94  ? O HIS B 94  N CYS B 81  ? N CYS B 81  
# 
_pdbx_entry_details.entry_id                   7HCC 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
_pdbx_validate_symm_contact.id                1 
_pdbx_validate_symm_contact.PDB_model_num     1 
_pdbx_validate_symm_contact.auth_atom_id_1    O 
_pdbx_validate_symm_contact.auth_asym_id_1    A 
_pdbx_validate_symm_contact.auth_comp_id_1    ASP 
_pdbx_validate_symm_contact.auth_seq_id_1     66 
_pdbx_validate_symm_contact.PDB_ins_code_1    ? 
_pdbx_validate_symm_contact.label_alt_id_1    ? 
_pdbx_validate_symm_contact.site_symmetry_1   1_555 
_pdbx_validate_symm_contact.auth_atom_id_2    HG 
_pdbx_validate_symm_contact.auth_asym_id_2    B 
_pdbx_validate_symm_contact.auth_comp_id_2    SER 
_pdbx_validate_symm_contact.auth_seq_id_2     1 
_pdbx_validate_symm_contact.PDB_ins_code_2    ? 
_pdbx_validate_symm_contact.label_alt_id_2    B 
_pdbx_validate_symm_contact.site_symmetry_2   2_655 
_pdbx_validate_symm_contact.dist              1.59 
# 
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 ? ? 55.04 -133.02 
2 1 HIS B 86 ? ? 56.96 -127.78 
# 
_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 511 ? 5.95 . 
2 1 O ? A HOH 512 ? 7.60 . 
3 1 O ? B HOH 401 ? 6.32 . 
# 
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 
A1A41 N2   N Y N 1   
A1A41 C3   C N N 2   
A1A41 C6   C Y N 3   
A1A41 C9   C Y N 4   
A1A41 C1   C Y N 5   
A1A41 C10  C Y N 6   
A1A41 C11  C Y N 7   
A1A41 C2   C Y N 8   
A1A41 C4   C N N 9   
A1A41 C5   C N N 10  
A1A41 C7   C Y N 11  
A1A41 C8   C Y N 12  
A1A41 N1   N N N 13  
A1A41 N3   N Y N 14  
A1A41 N4   N N N 15  
A1A41 O1   O N N 16  
A1A41 O2   O N N 17  
A1A41 S1   S N N 18  
A1A41 S2   S Y N 19  
A1A41 H4   H N N 20  
A1A41 H3   H N N 21  
A1A41 H9   H N N 22  
A1A41 H10  H N N 23  
A1A41 H5   H N N 24  
A1A41 H6   H N N 25  
A1A41 H7   H N N 26  
A1A41 H8   H N N 27  
A1A41 H2   H N N 28  
A1A41 H1   H N N 29  
ALA   N    N N N 30  
ALA   CA   C N S 31  
ALA   C    C N N 32  
ALA   O    O N N 33  
ALA   CB   C N N 34  
ALA   OXT  O N N 35  
ALA   H    H N N 36  
ALA   H2   H N N 37  
ALA   HA   H N N 38  
ALA   HB1  H N N 39  
ALA   HB2  H N N 40  
ALA   HB3  H N N 41  
ALA   HXT  H N N 42  
ARG   N    N N N 43  
ARG   CA   C N S 44  
ARG   C    C N N 45  
ARG   O    O N N 46  
ARG   CB   C N N 47  
ARG   CG   C N N 48  
ARG   CD   C N N 49  
ARG   NE   N N N 50  
ARG   CZ   C N N 51  
ARG   NH1  N N N 52  
ARG   NH2  N N N 53  
ARG   OXT  O N N 54  
ARG   H    H N N 55  
ARG   H2   H N N 56  
ARG   HA   H N N 57  
ARG   HB2  H N N 58  
ARG   HB3  H N N 59  
ARG   HG2  H N N 60  
ARG   HG3  H N N 61  
ARG   HD2  H N N 62  
ARG   HD3  H N N 63  
ARG   HE   H N N 64  
ARG   HH11 H N N 65  
ARG   HH12 H N N 66  
ARG   HH21 H N N 67  
ARG   HH22 H N N 68  
ARG   HXT  H N N 69  
ASN   N    N N N 70  
ASN   CA   C N S 71  
ASN   C    C N N 72  
ASN   O    O N N 73  
ASN   CB   C N N 74  
ASN   CG   C N N 75  
ASN   OD1  O N N 76  
ASN   ND2  N N N 77  
ASN   OXT  O N N 78  
ASN   H    H N N 79  
ASN   H2   H N N 80  
ASN   HA   H N N 81  
ASN   HB2  H N N 82  
ASN   HB3  H N N 83  
ASN   HD21 H N N 84  
ASN   HD22 H N N 85  
ASN   HXT  H N N 86  
ASP   N    N N N 87  
ASP   CA   C N S 88  
ASP   C    C N N 89  
ASP   O    O N N 90  
ASP   CB   C N N 91  
ASP   CG   C N N 92  
ASP   OD1  O N N 93  
ASP   OD2  O N N 94  
ASP   OXT  O N N 95  
ASP   H    H N N 96  
ASP   H2   H N N 97  
ASP   HA   H N N 98  
ASP   HB2  H N N 99  
ASP   HB3  H N N 100 
ASP   HD2  H N N 101 
ASP   HXT  H N N 102 
CYS   N    N N N 103 
CYS   CA   C N R 104 
CYS   C    C N N 105 
CYS   O    O N N 106 
CYS   CB   C N N 107 
CYS   SG   S N N 108 
CYS   OXT  O N N 109 
CYS   H    H N N 110 
CYS   H2   H N N 111 
CYS   HA   H N N 112 
CYS   HB2  H N N 113 
CYS   HB3  H N N 114 
CYS   HG   H N N 115 
CYS   HXT  H N N 116 
GLN   N    N N N 117 
GLN   CA   C N S 118 
GLN   C    C N N 119 
GLN   O    O N N 120 
GLN   CB   C N N 121 
GLN   CG   C N N 122 
GLN   CD   C N N 123 
GLN   OE1  O N N 124 
GLN   NE2  N N N 125 
GLN   OXT  O N N 126 
GLN   H    H N N 127 
GLN   H2   H N N 128 
GLN   HA   H N N 129 
GLN   HB2  H N N 130 
GLN   HB3  H N N 131 
GLN   HG2  H N N 132 
GLN   HG3  H N N 133 
GLN   HE21 H N N 134 
GLN   HE22 H N N 135 
GLN   HXT  H N N 136 
GLU   N    N N N 137 
GLU   CA   C N S 138 
GLU   C    C N N 139 
GLU   O    O N N 140 
GLU   CB   C N N 141 
GLU   CG   C N N 142 
GLU   CD   C N N 143 
GLU   OE1  O N N 144 
GLU   OE2  O N N 145 
GLU   OXT  O N N 146 
GLU   H    H N N 147 
GLU   H2   H N N 148 
GLU   HA   H N N 149 
GLU   HB2  H N N 150 
GLU   HB3  H N N 151 
GLU   HG2  H N N 152 
GLU   HG3  H N N 153 
GLU   HE2  H N N 154 
GLU   HXT  H N N 155 
GLY   N    N N N 156 
GLY   CA   C N N 157 
GLY   C    C N N 158 
GLY   O    O N N 159 
GLY   OXT  O N N 160 
GLY   H    H N N 161 
GLY   H2   H N N 162 
GLY   HA2  H N N 163 
GLY   HA3  H N N 164 
GLY   HXT  H N N 165 
HIS   N    N N N 166 
HIS   CA   C N S 167 
HIS   C    C N N 168 
HIS   O    O N N 169 
HIS   CB   C N N 170 
HIS   CG   C Y N 171 
HIS   ND1  N Y N 172 
HIS   CD2  C Y N 173 
HIS   CE1  C Y N 174 
HIS   NE2  N Y N 175 
HIS   OXT  O N N 176 
HIS   H    H N N 177 
HIS   H2   H N N 178 
HIS   HA   H N N 179 
HIS   HB2  H N N 180 
HIS   HB3  H N N 181 
HIS   HD1  H N N 182 
HIS   HD2  H N N 183 
HIS   HE1  H N N 184 
HIS   HE2  H N N 185 
HIS   HXT  H N N 186 
HOH   O    O N N 187 
HOH   H1   H N N 188 
HOH   H2   H N N 189 
ILE   N    N N N 190 
ILE   CA   C N S 191 
ILE   C    C N N 192 
ILE   O    O N N 193 
ILE   CB   C N S 194 
ILE   CG1  C N N 195 
ILE   CG2  C N N 196 
ILE   CD1  C N N 197 
ILE   OXT  O N N 198 
ILE   H    H N N 199 
ILE   H2   H N N 200 
ILE   HA   H N N 201 
ILE   HB   H N N 202 
ILE   HG12 H N N 203 
ILE   HG13 H N N 204 
ILE   HG21 H N N 205 
ILE   HG22 H N N 206 
ILE   HG23 H N N 207 
ILE   HD11 H N N 208 
ILE   HD12 H N N 209 
ILE   HD13 H N N 210 
ILE   HXT  H N N 211 
LEU   N    N N N 212 
LEU   CA   C N S 213 
LEU   C    C N N 214 
LEU   O    O N N 215 
LEU   CB   C N N 216 
LEU   CG   C N N 217 
LEU   CD1  C N N 218 
LEU   CD2  C N N 219 
LEU   OXT  O N N 220 
LEU   H    H N N 221 
LEU   H2   H N N 222 
LEU   HA   H N N 223 
LEU   HB2  H N N 224 
LEU   HB3  H N N 225 
LEU   HG   H N N 226 
LEU   HD11 H N N 227 
LEU   HD12 H N N 228 
LEU   HD13 H N N 229 
LEU   HD21 H N N 230 
LEU   HD22 H N N 231 
LEU   HD23 H N N 232 
LEU   HXT  H N N 233 
LYS   N    N N N 234 
LYS   CA   C N S 235 
LYS   C    C N N 236 
LYS   O    O N N 237 
LYS   CB   C N N 238 
LYS   CG   C N N 239 
LYS   CD   C N N 240 
LYS   CE   C N N 241 
LYS   NZ   N N N 242 
LYS   OXT  O N N 243 
LYS   H    H N N 244 
LYS   H2   H N N 245 
LYS   HA   H N N 246 
LYS   HB2  H N N 247 
LYS   HB3  H N N 248 
LYS   HG2  H N N 249 
LYS   HG3  H N N 250 
LYS   HD2  H N N 251 
LYS   HD3  H N N 252 
LYS   HE2  H N N 253 
LYS   HE3  H N N 254 
LYS   HZ1  H N N 255 
LYS   HZ2  H N N 256 
LYS   HZ3  H N N 257 
LYS   HXT  H N N 258 
MET   N    N N N 259 
MET   CA   C N S 260 
MET   C    C N N 261 
MET   O    O N N 262 
MET   CB   C N N 263 
MET   CG   C N N 264 
MET   SD   S N N 265 
MET   CE   C N N 266 
MET   OXT  O N N 267 
MET   H    H N N 268 
MET   H2   H N N 269 
MET   HA   H N N 270 
MET   HB2  H N N 271 
MET   HB3  H N N 272 
MET   HG2  H N N 273 
MET   HG3  H N N 274 
MET   HE1  H N N 275 
MET   HE2  H N N 276 
MET   HE3  H N N 277 
MET   HXT  H N N 278 
PHE   N    N N N 279 
PHE   CA   C N S 280 
PHE   C    C N N 281 
PHE   O    O N N 282 
PHE   CB   C N N 283 
PHE   CG   C Y N 284 
PHE   CD1  C Y N 285 
PHE   CD2  C Y N 286 
PHE   CE1  C Y N 287 
PHE   CE2  C Y N 288 
PHE   CZ   C Y N 289 
PHE   OXT  O N N 290 
PHE   H    H N N 291 
PHE   H2   H N N 292 
PHE   HA   H N N 293 
PHE   HB2  H N N 294 
PHE   HB3  H N N 295 
PHE   HD1  H N N 296 
PHE   HD2  H N N 297 
PHE   HE1  H N N 298 
PHE   HE2  H N N 299 
PHE   HZ   H N N 300 
PHE   HXT  H N N 301 
PRO   N    N N N 302 
PRO   CA   C N S 303 
PRO   C    C N N 304 
PRO   O    O N N 305 
PRO   CB   C N N 306 
PRO   CG   C N N 307 
PRO   CD   C N N 308 
PRO   OXT  O N N 309 
PRO   H    H N N 310 
PRO   HA   H N N 311 
PRO   HB2  H N N 312 
PRO   HB3  H N N 313 
PRO   HG2  H N N 314 
PRO   HG3  H N N 315 
PRO   HD2  H N N 316 
PRO   HD3  H N N 317 
PRO   HXT  H N N 318 
SER   N    N N N 319 
SER   CA   C N S 320 
SER   C    C N N 321 
SER   O    O N N 322 
SER   CB   C N N 323 
SER   OG   O N N 324 
SER   OXT  O N N 325 
SER   H    H N N 326 
SER   H2   H N N 327 
SER   HA   H N N 328 
SER   HB2  H N N 329 
SER   HB3  H N N 330 
SER   HG   H N N 331 
SER   HXT  H N N 332 
THR   N    N N N 333 
THR   CA   C N S 334 
THR   C    C N N 335 
THR   O    O N N 336 
THR   CB   C N R 337 
THR   OG1  O N N 338 
THR   CG2  C N N 339 
THR   OXT  O N N 340 
THR   H    H N N 341 
THR   H2   H N N 342 
THR   HA   H N N 343 
THR   HB   H N N 344 
THR   HG1  H N N 345 
THR   HG21 H N N 346 
THR   HG22 H N N 347 
THR   HG23 H N N 348 
THR   HXT  H N N 349 
TYR   N    N N N 350 
TYR   CA   C N S 351 
TYR   C    C N N 352 
TYR   O    O N N 353 
TYR   CB   C N N 354 
TYR   CG   C Y N 355 
TYR   CD1  C Y N 356 
TYR   CD2  C Y N 357 
TYR   CE1  C Y N 358 
TYR   CE2  C Y N 359 
TYR   CZ   C Y N 360 
TYR   OH   O N N 361 
TYR   OXT  O N N 362 
TYR   H    H N N 363 
TYR   H2   H N N 364 
TYR   HA   H N N 365 
TYR   HB2  H N N 366 
TYR   HB3  H N N 367 
TYR   HD1  H N N 368 
TYR   HD2  H N N 369 
TYR   HE1  H N N 370 
TYR   HE2  H N N 371 
TYR   HH   H N N 372 
TYR   HXT  H N N 373 
VAL   N    N N N 374 
VAL   CA   C N S 375 
VAL   C    C N N 376 
VAL   O    O N N 377 
VAL   CB   C N N 378 
VAL   CG1  C N N 379 
VAL   CG2  C N N 380 
VAL   OXT  O N N 381 
VAL   H    H N N 382 
VAL   H2   H N N 383 
VAL   HA   H N N 384 
VAL   HB   H N N 385 
VAL   HG11 H N N 386 
VAL   HG12 H N N 387 
VAL   HG13 H N N 388 
VAL   HG21 H N N 389 
VAL   HG22 H N N 390 
VAL   HG23 H N N 391 
VAL   HXT  H N N 392 
# 
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 
A1A41 N2  N3   sing Y N 1   
A1A41 N2  C1   doub Y N 2   
A1A41 N1  C1   sing N N 3   
A1A41 N3  C2   doub Y N 4   
A1A41 C1  S2   sing Y N 5   
A1A41 C2  S2   sing Y N 6   
A1A41 C2  S1   sing N N 7   
A1A41 S1  C3   sing N N 8   
A1A41 C3  C4   sing N N 9   
A1A41 C9  C10  doub Y N 10  
A1A41 C9  C8   sing Y N 11  
A1A41 C10 C11  sing Y N 12  
A1A41 C8  C7   doub Y N 13  
A1A41 C4  N4   sing N N 14  
A1A41 C11 N4   sing N N 15  
A1A41 C11 C6   doub Y N 16  
A1A41 N4  C5   sing N N 17  
A1A41 C7  C6   sing Y N 18  
A1A41 C6  O2   sing N N 19  
A1A41 C5  O2   sing N N 20  
A1A41 C5  O1   doub N N 21  
A1A41 C3  H4   sing N N 22  
A1A41 C3  H3   sing N N 23  
A1A41 C9  H9   sing N N 24  
A1A41 C10 H10  sing N N 25  
A1A41 C4  H5   sing N N 26  
A1A41 C4  H6   sing N N 27  
A1A41 C7  H7   sing N N 28  
A1A41 C8  H8   sing N N 29  
A1A41 N1  H2   sing N N 30  
A1A41 N1  H1   sing N N 31  
ALA   N   CA   sing N N 32  
ALA   N   H    sing N N 33  
ALA   N   H2   sing N N 34  
ALA   CA  C    sing N N 35  
ALA   CA  CB   sing N N 36  
ALA   CA  HA   sing N N 37  
ALA   C   O    doub N N 38  
ALA   C   OXT  sing N N 39  
ALA   CB  HB1  sing N N 40  
ALA   CB  HB2  sing N N 41  
ALA   CB  HB3  sing N N 42  
ALA   OXT HXT  sing N N 43  
ARG   N   CA   sing N N 44  
ARG   N   H    sing N N 45  
ARG   N   H2   sing N N 46  
ARG   CA  C    sing N N 47  
ARG   CA  CB   sing N N 48  
ARG   CA  HA   sing N N 49  
ARG   C   O    doub N N 50  
ARG   C   OXT  sing N N 51  
ARG   CB  CG   sing N N 52  
ARG   CB  HB2  sing N N 53  
ARG   CB  HB3  sing N N 54  
ARG   CG  CD   sing N N 55  
ARG   CG  HG2  sing N N 56  
ARG   CG  HG3  sing N N 57  
ARG   CD  NE   sing N N 58  
ARG   CD  HD2  sing N N 59  
ARG   CD  HD3  sing N N 60  
ARG   NE  CZ   sing N N 61  
ARG   NE  HE   sing N N 62  
ARG   CZ  NH1  sing N N 63  
ARG   CZ  NH2  doub N N 64  
ARG   NH1 HH11 sing N N 65  
ARG   NH1 HH12 sing N N 66  
ARG   NH2 HH21 sing N N 67  
ARG   NH2 HH22 sing N N 68  
ARG   OXT HXT  sing N N 69  
ASN   N   CA   sing N N 70  
ASN   N   H    sing N N 71  
ASN   N   H2   sing N N 72  
ASN   CA  C    sing N N 73  
ASN   CA  CB   sing N N 74  
ASN   CA  HA   sing N N 75  
ASN   C   O    doub N N 76  
ASN   C   OXT  sing N N 77  
ASN   CB  CG   sing N N 78  
ASN   CB  HB2  sing N N 79  
ASN   CB  HB3  sing N N 80  
ASN   CG  OD1  doub N N 81  
ASN   CG  ND2  sing N N 82  
ASN   ND2 HD21 sing N N 83  
ASN   ND2 HD22 sing N N 84  
ASN   OXT HXT  sing N N 85  
ASP   N   CA   sing N N 86  
ASP   N   H    sing N N 87  
ASP   N   H2   sing N N 88  
ASP   CA  C    sing N N 89  
ASP   CA  CB   sing N N 90  
ASP   CA  HA   sing N N 91  
ASP   C   O    doub N N 92  
ASP   C   OXT  sing N N 93  
ASP   CB  CG   sing N N 94  
ASP   CB  HB2  sing N N 95  
ASP   CB  HB3  sing N N 96  
ASP   CG  OD1  doub N N 97  
ASP   CG  OD2  sing N N 98  
ASP   OD2 HD2  sing N N 99  
ASP   OXT HXT  sing N N 100 
CYS   N   CA   sing N N 101 
CYS   N   H    sing N N 102 
CYS   N   H2   sing N N 103 
CYS   CA  C    sing N N 104 
CYS   CA  CB   sing N N 105 
CYS   CA  HA   sing N N 106 
CYS   C   O    doub N N 107 
CYS   C   OXT  sing N N 108 
CYS   CB  SG   sing N N 109 
CYS   CB  HB2  sing N N 110 
CYS   CB  HB3  sing N N 111 
CYS   SG  HG   sing N N 112 
CYS   OXT HXT  sing N N 113 
GLN   N   CA   sing N N 114 
GLN   N   H    sing N N 115 
GLN   N   H2   sing N N 116 
GLN   CA  C    sing N N 117 
GLN   CA  CB   sing N N 118 
GLN   CA  HA   sing N N 119 
GLN   C   O    doub N N 120 
GLN   C   OXT  sing N N 121 
GLN   CB  CG   sing N N 122 
GLN   CB  HB2  sing N N 123 
GLN   CB  HB3  sing N N 124 
GLN   CG  CD   sing N N 125 
GLN   CG  HG2  sing N N 126 
GLN   CG  HG3  sing N N 127 
GLN   CD  OE1  doub N N 128 
GLN   CD  NE2  sing N N 129 
GLN   NE2 HE21 sing N N 130 
GLN   NE2 HE22 sing N N 131 
GLN   OXT HXT  sing N N 132 
GLU   N   CA   sing N N 133 
GLU   N   H    sing N N 134 
GLU   N   H2   sing N N 135 
GLU   CA  C    sing N N 136 
GLU   CA  CB   sing N N 137 
GLU   CA  HA   sing N N 138 
GLU   C   O    doub N N 139 
GLU   C   OXT  sing N N 140 
GLU   CB  CG   sing N N 141 
GLU   CB  HB2  sing N N 142 
GLU   CB  HB3  sing N N 143 
GLU   CG  CD   sing N N 144 
GLU   CG  HG2  sing N N 145 
GLU   CG  HG3  sing N N 146 
GLU   CD  OE1  doub N N 147 
GLU   CD  OE2  sing N N 148 
GLU   OE2 HE2  sing N N 149 
GLU   OXT HXT  sing N N 150 
GLY   N   CA   sing N N 151 
GLY   N   H    sing N N 152 
GLY   N   H2   sing N N 153 
GLY   CA  C    sing N N 154 
GLY   CA  HA2  sing N N 155 
GLY   CA  HA3  sing N N 156 
GLY   C   O    doub N N 157 
GLY   C   OXT  sing N N 158 
GLY   OXT HXT  sing N N 159 
HIS   N   CA   sing N N 160 
HIS   N   H    sing N N 161 
HIS   N   H2   sing N N 162 
HIS   CA  C    sing N N 163 
HIS   CA  CB   sing N N 164 
HIS   CA  HA   sing N N 165 
HIS   C   O    doub N N 166 
HIS   C   OXT  sing N N 167 
HIS   CB  CG   sing N N 168 
HIS   CB  HB2  sing N N 169 
HIS   CB  HB3  sing N N 170 
HIS   CG  ND1  sing Y N 171 
HIS   CG  CD2  doub Y N 172 
HIS   ND1 CE1  doub Y N 173 
HIS   ND1 HD1  sing N N 174 
HIS   CD2 NE2  sing Y N 175 
HIS   CD2 HD2  sing N N 176 
HIS   CE1 NE2  sing Y N 177 
HIS   CE1 HE1  sing N N 178 
HIS   NE2 HE2  sing N N 179 
HIS   OXT HXT  sing N N 180 
HOH   O   H1   sing N N 181 
HOH   O   H2   sing N N 182 
ILE   N   CA   sing N N 183 
ILE   N   H    sing N N 184 
ILE   N   H2   sing N N 185 
ILE   CA  C    sing N N 186 
ILE   CA  CB   sing N N 187 
ILE   CA  HA   sing N N 188 
ILE   C   O    doub N N 189 
ILE   C   OXT  sing N N 190 
ILE   CB  CG1  sing N N 191 
ILE   CB  CG2  sing N N 192 
ILE   CB  HB   sing N N 193 
ILE   CG1 CD1  sing N N 194 
ILE   CG1 HG12 sing N N 195 
ILE   CG1 HG13 sing N N 196 
ILE   CG2 HG21 sing N N 197 
ILE   CG2 HG22 sing N N 198 
ILE   CG2 HG23 sing N N 199 
ILE   CD1 HD11 sing N N 200 
ILE   CD1 HD12 sing N N 201 
ILE   CD1 HD13 sing N N 202 
ILE   OXT HXT  sing N N 203 
LEU   N   CA   sing N N 204 
LEU   N   H    sing N N 205 
LEU   N   H2   sing N N 206 
LEU   CA  C    sing N N 207 
LEU   CA  CB   sing N N 208 
LEU   CA  HA   sing N N 209 
LEU   C   O    doub N N 210 
LEU   C   OXT  sing N N 211 
LEU   CB  CG   sing N N 212 
LEU   CB  HB2  sing N N 213 
LEU   CB  HB3  sing N N 214 
LEU   CG  CD1  sing N N 215 
LEU   CG  CD2  sing N N 216 
LEU   CG  HG   sing N N 217 
LEU   CD1 HD11 sing N N 218 
LEU   CD1 HD12 sing N N 219 
LEU   CD1 HD13 sing N N 220 
LEU   CD2 HD21 sing N N 221 
LEU   CD2 HD22 sing N N 222 
LEU   CD2 HD23 sing N N 223 
LEU   OXT HXT  sing N N 224 
LYS   N   CA   sing N N 225 
LYS   N   H    sing N N 226 
LYS   N   H2   sing N N 227 
LYS   CA  C    sing N N 228 
LYS   CA  CB   sing N N 229 
LYS   CA  HA   sing N N 230 
LYS   C   O    doub N N 231 
LYS   C   OXT  sing N N 232 
LYS   CB  CG   sing N N 233 
LYS   CB  HB2  sing N N 234 
LYS   CB  HB3  sing N N 235 
LYS   CG  CD   sing N N 236 
LYS   CG  HG2  sing N N 237 
LYS   CG  HG3  sing N N 238 
LYS   CD  CE   sing N N 239 
LYS   CD  HD2  sing N N 240 
LYS   CD  HD3  sing N N 241 
LYS   CE  NZ   sing N N 242 
LYS   CE  HE2  sing N N 243 
LYS   CE  HE3  sing N N 244 
LYS   NZ  HZ1  sing N N 245 
LYS   NZ  HZ2  sing N N 246 
LYS   NZ  HZ3  sing N N 247 
LYS   OXT HXT  sing N N 248 
MET   N   CA   sing N N 249 
MET   N   H    sing N N 250 
MET   N   H2   sing N N 251 
MET   CA  C    sing N N 252 
MET   CA  CB   sing N N 253 
MET   CA  HA   sing N N 254 
MET   C   O    doub N N 255 
MET   C   OXT  sing N N 256 
MET   CB  CG   sing N N 257 
MET   CB  HB2  sing N N 258 
MET   CB  HB3  sing N N 259 
MET   CG  SD   sing N N 260 
MET   CG  HG2  sing N N 261 
MET   CG  HG3  sing N N 262 
MET   SD  CE   sing N N 263 
MET   CE  HE1  sing N N 264 
MET   CE  HE2  sing N N 265 
MET   CE  HE3  sing N N 266 
MET   OXT HXT  sing N N 267 
PHE   N   CA   sing N N 268 
PHE   N   H    sing N N 269 
PHE   N   H2   sing N N 270 
PHE   CA  C    sing N N 271 
PHE   CA  CB   sing N N 272 
PHE   CA  HA   sing N N 273 
PHE   C   O    doub N N 274 
PHE   C   OXT  sing N N 275 
PHE   CB  CG   sing N N 276 
PHE   CB  HB2  sing N N 277 
PHE   CB  HB3  sing N N 278 
PHE   CG  CD1  doub Y N 279 
PHE   CG  CD2  sing Y N 280 
PHE   CD1 CE1  sing Y N 281 
PHE   CD1 HD1  sing N N 282 
PHE   CD2 CE2  doub Y N 283 
PHE   CD2 HD2  sing N N 284 
PHE   CE1 CZ   doub Y N 285 
PHE   CE1 HE1  sing N N 286 
PHE   CE2 CZ   sing Y N 287 
PHE   CE2 HE2  sing N N 288 
PHE   CZ  HZ   sing N N 289 
PHE   OXT HXT  sing N N 290 
PRO   N   CA   sing N N 291 
PRO   N   CD   sing N N 292 
PRO   N   H    sing N N 293 
PRO   CA  C    sing N N 294 
PRO   CA  CB   sing N N 295 
PRO   CA  HA   sing N N 296 
PRO   C   O    doub N N 297 
PRO   C   OXT  sing N N 298 
PRO   CB  CG   sing N N 299 
PRO   CB  HB2  sing N N 300 
PRO   CB  HB3  sing N N 301 
PRO   CG  CD   sing N N 302 
PRO   CG  HG2  sing N N 303 
PRO   CG  HG3  sing N N 304 
PRO   CD  HD2  sing N N 305 
PRO   CD  HD3  sing N N 306 
PRO   OXT HXT  sing N N 307 
SER   N   CA   sing N N 308 
SER   N   H    sing N N 309 
SER   N   H2   sing N N 310 
SER   CA  C    sing N N 311 
SER   CA  CB   sing N N 312 
SER   CA  HA   sing N N 313 
SER   C   O    doub N N 314 
SER   C   OXT  sing N N 315 
SER   CB  OG   sing N N 316 
SER   CB  HB2  sing N N 317 
SER   CB  HB3  sing N N 318 
SER   OG  HG   sing N N 319 
SER   OXT HXT  sing N N 320 
THR   N   CA   sing N N 321 
THR   N   H    sing N N 322 
THR   N   H2   sing N N 323 
THR   CA  C    sing N N 324 
THR   CA  CB   sing N N 325 
THR   CA  HA   sing N N 326 
THR   C   O    doub N N 327 
THR   C   OXT  sing N N 328 
THR   CB  OG1  sing N N 329 
THR   CB  CG2  sing N N 330 
THR   CB  HB   sing N N 331 
THR   OG1 HG1  sing N N 332 
THR   CG2 HG21 sing N N 333 
THR   CG2 HG22 sing N N 334 
THR   CG2 HG23 sing N N 335 
THR   OXT HXT  sing N N 336 
TYR   N   CA   sing N N 337 
TYR   N   H    sing N N 338 
TYR   N   H2   sing N N 339 
TYR   CA  C    sing N N 340 
TYR   CA  CB   sing N N 341 
TYR   CA  HA   sing N N 342 
TYR   C   O    doub N N 343 
TYR   C   OXT  sing N N 344 
TYR   CB  CG   sing N N 345 
TYR   CB  HB2  sing N N 346 
TYR   CB  HB3  sing N N 347 
TYR   CG  CD1  doub Y N 348 
TYR   CG  CD2  sing Y N 349 
TYR   CD1 CE1  sing Y N 350 
TYR   CD1 HD1  sing N N 351 
TYR   CD2 CE2  doub Y N 352 
TYR   CD2 HD2  sing N N 353 
TYR   CE1 CZ   doub Y N 354 
TYR   CE1 HE1  sing N N 355 
TYR   CE2 CZ   sing Y N 356 
TYR   CE2 HE2  sing N N 357 
TYR   CZ  OH   sing N N 358 
TYR   OH  HH   sing N N 359 
TYR   OXT HXT  sing N N 360 
VAL   N   CA   sing N N 361 
VAL   N   H    sing N N 362 
VAL   N   H2   sing N N 363 
VAL   CA  C    sing N N 364 
VAL   CA  CB   sing N N 365 
VAL   CA  HA   sing N N 366 
VAL   C   O    doub N N 367 
VAL   C   OXT  sing N N 368 
VAL   CB  CG1  sing N N 369 
VAL   CB  CG2  sing N N 370 
VAL   CB  HB   sing N N 371 
VAL   CG1 HG11 sing N N 372 
VAL   CG1 HG12 sing N N 373 
VAL   CG1 HG13 sing N N 374 
VAL   CG2 HG21 sing N N 375 
VAL   CG2 HG22 sing N N 376 
VAL   CG2 HG23 sing N N 377 
VAL   OXT HXT  sing N N 378 
# 
_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                    7HCC 
_atom_sites.fract_transf_matrix[1][1]   0.011270 
_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]   0.011270 
_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]   0.025284 
_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   ? 19.672 -16.295 22.193  0.88 42.05 ?  3   VAL   A N    1 
ATOM   2    N N    B VAL   A 1 3   ? 19.736 -16.168 22.235  0.12 39.14 ?  3   VAL   A N    1 
ATOM   3    C CA   A VAL   A 1 3   ? 18.719 -15.215 22.420  0.88 41.62 ?  3   VAL   A CA   1 
ATOM   4    C CA   B VAL   A 1 3   ? 18.745 -15.133 22.502  0.12 38.91 ?  3   VAL   A CA   1 
ATOM   5    C C    A VAL   A 1 3   ? 19.363 -13.868 22.114  0.88 39.96 ?  3   VAL   A C    1 
ATOM   6    C C    B VAL   A 1 3   ? 19.342 -13.754 22.251  0.12 37.70 ?  3   VAL   A C    1 
ATOM   7    O O    A VAL   A 1 3   ? 20.509 -13.619 22.492  0.88 40.29 ?  3   VAL   A O    1 
ATOM   8    O O    B VAL   A 1 3   ? 20.409 -13.428 22.771  0.12 37.92 ?  3   VAL   A O    1 
ATOM   9    C CB   A VAL   A 1 3   ? 18.145 -15.267 23.854  0.88 42.48 ?  3   VAL   A CB   1 
ATOM   10   C CB   B VAL   A 1 3   ? 18.189 -15.247 23.934  0.12 39.67 ?  3   VAL   A CB   1 
ATOM   11   C CG1  A VAL   A 1 3   ? 17.126 -14.154 24.069  0.88 42.73 ?  3   VAL   A CG1  1 
ATOM   12   C CG1  B VAL   A 1 3   ? 17.145 -14.168 24.187  0.12 39.89 ?  3   VAL   A CG1  1 
ATOM   13   C CG2  A VAL   A 1 3   ? 17.515 -16.628 24.119  0.88 42.69 ?  3   VAL   A CG2  1 
ATOM   14   C CG2  B VAL   A 1 3   ? 17.602 -16.631 24.166  0.12 39.90 ?  3   VAL   A CG2  1 
ATOM   15   H HA   A VAL   A 1 3   ? 17.977 -15.319 21.811  0.88 49.94 ?  3   VAL   A HA   1 
ATOM   16   H HA   B VAL   A 1 3   ? 18.002 -15.244 21.892  0.12 46.69 ?  3   VAL   A HA   1 
ATOM   17   H HB   A VAL   A 1 3   ? 18.864 -15.141 24.493  0.88 50.97 ?  3   VAL   A HB   1 
ATOM   18   H HB   B VAL   A 1 3   ? 18.912 -15.118 24.567  0.12 47.61 ?  3   VAL   A HB   1 
ATOM   19   H HG11 A VAL   A 1 3   ? 16.651 -14.317 24.900  0.88 51.27 ?  3   VAL   A HG11 1 
ATOM   20   H HG11 B VAL   A 1 3   ? 16.676 -14.372 25.011  0.12 47.88 ?  3   VAL   A HG11 1 
ATOM   21   H HG12 A VAL   A 1 3   ? 17.588 -13.303 24.117  0.88 51.27 ?  3   VAL   A HG12 1 
ATOM   22   H HG12 B VAL   A 1 3   ? 17.588 -13.309 24.264  0.12 47.88 ?  3   VAL   A HG12 1 
ATOM   23   H HG13 A VAL   A 1 3   ? 16.500 -14.152 23.329  0.88 51.27 ?  3   VAL   A HG13 1 
ATOM   24   H HG13 B VAL   A 1 3   ? 16.519 -14.155 23.446  0.12 47.88 ?  3   VAL   A HG13 1 
ATOM   25   H HG21 A VAL   A 1 3   ? 17.101 -16.620 24.996  0.88 51.23 ?  3   VAL   A HG21 1 
ATOM   26   H HG21 B VAL   A 1 3   ? 17.194 -16.657 25.046  0.12 47.88 ?  3   VAL   A HG21 1 
ATOM   27   H HG22 A VAL   A 1 3   ? 16.846 -16.803 23.439  0.88 51.23 ?  3   VAL   A HG22 1 
ATOM   28   H HG22 B VAL   A 1 3   ? 16.933 -16.808 23.486  0.12 47.88 ?  3   VAL   A HG22 1 
ATOM   29   H HG23 A VAL   A 1 3   ? 18.206 -17.308 24.085  0.88 51.23 ?  3   VAL   A HG23 1 
ATOM   30   H HG23 B VAL   A 1 3   ? 18.312 -17.289 24.111  0.12 47.88 ?  3   VAL   A HG23 1 
ATOM   31   N N    A ASN   A 1 4   ? 18.627 -13.008 21.409  0.88 37.52 ?  4   ASN   A N    1 
ATOM   32   N N    B ASN   A 1 4   ? 18.650 -12.948 21.448  0.12 36.09 ?  4   ASN   A N    1 
ATOM   33   C CA   A ASN   A 1 4   ? 19.076 -11.654 21.111  0.88 34.82 ?  4   ASN   A CA   1 
ATOM   34   C CA   B ASN   A 1 4   ? 19.066 -11.582 21.159  0.12 34.33 ?  4   ASN   A CA   1 
ATOM   35   C C    A ASN   A 1 4   ? 17.921 -10.687 21.350  0.88 32.42 ?  4   ASN   A C    1 
ATOM   36   C C    B ASN   A 1 4   ? 17.921 -10.630 21.482  0.12 32.60 ?  4   ASN   A C    1 
ATOM   37   O O    A ASN   A 1 4   ? 16.796 -11.093 21.660  0.88 32.01 ?  4   ASN   A O    1 
ATOM   38   O O    B ASN   A 1 4   ? 16.841 -11.042 21.915  0.12 32.67 ?  4   ASN   A O    1 
ATOM   39   C CB   A ASN   A 1 4   ? 19.662 -11.552 19.695  0.88 34.25 ?  4   ASN   A CB   1 
ATOM   40   C CB   B ASN   A 1 4   ? 19.523 -11.421 19.703  0.12 34.17 ?  4   ASN   A CB   1 
ATOM   41   C CG   A ASN   A 1 4   ? 18.675 -11.948 18.620  0.88 33.44 ?  4   ASN   A CG   1 
ATOM   42   C CG   B ASN   A 1 4   ? 18.474 -11.865 18.707  0.12 33.97 ?  4   ASN   A CG   1 
ATOM   43   O OD1  A ASN   A 1 4   ? 17.553 -11.445 18.575  0.88 33.12 ?  4   ASN   A OD1  1 
ATOM   44   O OD1  B ASN   A 1 4   ? 17.413 -11.252 18.590  0.12 33.91 ?  4   ASN   A OD1  1 
ATOM   45   N ND2  A ASN   A 1 4   ? 19.090 -12.857 17.742  0.88 33.31 ?  4   ASN   A ND2  1 
ATOM   46   N ND2  B ASN   A 1 4   ? 18.772 -12.928 17.970  0.12 33.94 ?  4   ASN   A ND2  1 
ATOM   47   H H    A ASN   A 1 4   ? 17.852 -13.193 21.082  0.88 45.02 ?  4   ASN   A H    1 
ATOM   48   H H    B ASN   A 1 4   ? 17.917 -13.176 21.056  0.12 43.31 ?  4   ASN   A H    1 
ATOM   49   H HA   A ASN   A 1 4   ? 19.783 -11.425 21.728  0.88 41.79 ?  4   ASN   A HA   1 
ATOM   50   H HA   B ASN   A 1 4   ? 19.812 -11.356 21.729  0.12 41.20 ?  4   ASN   A HA   1 
ATOM   51   H HB2  A ASN   A 1 4   ? 19.930 -10.635 19.529  0.88 41.10 ?  4   ASN   A HB2  1 
ATOM   52   H HB2  B ASN   A 1 4   ? 19.720 -10.486 19.536  0.12 41.01 ?  4   ASN   A HB2  1 
ATOM   53   H HB3  A ASN   A 1 4   ? 20.429 -12.140 19.630  0.88 41.10 ?  4   ASN   A HB3  1 
ATOM   54   H HB3  B ASN   A 1 4   ? 20.317 -11.957 19.564  0.12 41.01 ?  4   ASN   A HB3  1 
ATOM   55   H HD21 A ASN   A 1 4   ? 18.570 -13.117 17.108  0.88 39.97 ?  4   ASN   A HD21 1 
ATOM   56   H HD21 B ASN   A 1 4   ? 18.211 -13.217 17.387  0.12 40.73 ?  4   ASN   A HD21 1 
ATOM   57   H HD22 A ASN   A 1 4   ? 19.884 -13.185 17.806  0.88 39.97 ?  4   ASN   A HD22 1 
ATOM   58   H HD22 B ASN   A 1 4   ? 19.526 -13.327 18.079  0.12 40.73 ?  4   ASN   A HD22 1 
ATOM   59   N N    A SER   A 1 5   ? 18.206 -9.392  21.202  0.88 30.05 ?  5   SER   A N    1 
ATOM   60   N N    B SER   A 1 5   ? 18.166 -9.339  21.265  0.12 30.65 ?  5   SER   A N    1 
ATOM   61   C CA   A SER   A 1 5   ? 17.276 -8.330  21.567  0.88 28.07 ?  5   SER   A CA   1 
ATOM   62   C CA   B SER   A 1 5   ? 17.202 -8.300  21.596  0.12 28.64 ?  5   SER   A CA   1 
ATOM   63   C C    A SER   A 1 5   ? 16.399 -7.865  20.406  0.88 25.60 ?  5   SER   A C    1 
ATOM   64   C C    B SER   A 1 5   ? 16.333 -7.885  20.416  0.12 26.02 ?  5   SER   A C    1 
ATOM   65   O O    A SER   A 1 5   ? 15.639 -6.907  20.567  0.88 25.81 ?  5   SER   A O    1 
ATOM   66   O O    B SER   A 1 5   ? 15.509 -6.978  20.568  0.12 26.21 ?  5   SER   A O    1 
ATOM   67   C CB   A SER   A 1 5   ? 18.040 -7.137  22.150  0.88 28.72 ?  5   SER   A CB   1 
ATOM   68   C CB   B SER   A 1 5   ? 17.915 -7.068  22.166  0.12 29.08 ?  5   SER   A CB   1 
ATOM   69   O OG   A SER   A 1 5   ? 19.028 -6.681  21.245  0.88 28.99 ?  5   SER   A OG   1 
ATOM   70   O OG   B SER   A 1 5   ? 18.705 -6.430  21.178  0.12 29.29 ?  5   SER   A OG   1 
ATOM   71   H H    A SER   A 1 5   ? 18.950 -9.100  20.881  0.88 36.07 ?  5   SER   A H    1 
ATOM   72   H H    B SER   A 1 5   ? 18.895 -9.038  20.920  0.12 36.78 ?  5   SER   A H    1 
ATOM   73   H HA   A SER   A 1 5   ? 16.691 -8.658  22.263  0.88 33.69 ?  5   SER   A HA   1 
ATOM   74   H HA   B SER   A 1 5   ? 16.614 -8.637  22.290  0.12 34.37 ?  5   SER   A HA   1 
ATOM   75   H HB2  A SER   A 1 5   ? 17.417 -6.412  22.324  0.88 34.46 ?  5   SER   A HB2  1 
ATOM   76   H HB2  B SER   A 1 5   ? 17.247 -6.442  22.494  0.12 34.90 ?  5   SER   A HB2  1 
ATOM   77   H HB3  A SER   A 1 5   ? 18.470 -7.407  22.979  0.88 34.46 ?  5   SER   A HB3  1 
ATOM   78   H HB3  B SER   A 1 5   ? 18.491 -7.344  22.896  0.12 34.90 ?  5   SER   A HB3  1 
ATOM   79   H HG   A SER   A 1 5   ? 19.446 -6.028  21.576  0.88 34.79 ?  5   SER   A HG   1 
ATOM   80   H HG   B SER   A 1 5   ? 19.081 -5.752  21.505  0.12 35.15 ?  5   SER   A HG   1 
ATOM   81   N N    . PHE   A 1 6   ? 16.487 -8.511  19.248  1.00 22.96 ?  6   PHE   A N    1 
ATOM   82   C CA   . PHE   A 1 6   ? 15.608 -8.176  18.133  1.00 18.76 ?  6   PHE   A CA   1 
ATOM   83   C C    . PHE   A 1 6   ? 14.180 -8.565  18.498  1.00 18.83 ?  6   PHE   A C    1 
ATOM   84   O O    . PHE   A 1 6   ? 13.925 -9.697  18.919  1.00 19.96 ?  6   PHE   A O    1 
ATOM   85   C CB   . PHE   A 1 6   ? 16.043 -8.904  16.864  1.00 16.71 ?  6   PHE   A CB   1 
ATOM   86   C CG   . PHE   A 1 6   ? 17.306 -8.359  16.249  1.00 15.53 ?  6   PHE   A CG   1 
ATOM   87   C CD1  . PHE   A 1 6   ? 17.296 -7.162  15.551  1.00 15.44 ?  6   PHE   A CD1  1 
ATOM   88   C CD2  . PHE   A 1 6   ? 18.495 -9.056  16.354  1.00 15.98 ?  6   PHE   A CD2  1 
ATOM   89   C CE1  . PHE   A 1 6   ? 18.456 -6.669  14.979  1.00 15.72 ?  6   PHE   A CE1  1 
ATOM   90   C CE2  . PHE   A 1 6   ? 19.653 -8.573  15.784  1.00 16.30 ?  6   PHE   A CE2  1 
ATOM   91   C CZ   . PHE   A 1 6   ? 19.635 -7.377  15.094  1.00 16.00 ?  6   PHE   A CZ   1 
ATOM   92   H H    A PHE   A 1 6   ? 17.042 -9.147  19.085  0.88 27.55 ?  6   PHE   A H    1 
ATOM   93   H H    B PHE   A 1 6   ? 17.074 -9.116  19.083  0.12 27.55 ?  6   PHE   A H    1 
ATOM   94   H HA   . PHE   A 1 6   ? 15.634 -7.224  17.974  1.00 22.52 ?  6   PHE   A HA   1 
ATOM   95   H HB2  . PHE   A 1 6   ? 16.191 -9.841  17.075  1.00 20.05 ?  6   PHE   A HB2  1 
ATOM   96   H HB3  . PHE   A 1 6   ? 15.333 -8.830  16.206  1.00 20.05 ?  6   PHE   A HB3  1 
ATOM   97   H HD1  . PHE   A 1 6   ? 16.501 -6.684  15.470  1.00 18.53 ?  6   PHE   A HD1  1 
ATOM   98   H HD2  . PHE   A 1 6   ? 18.511 -9.863  16.816  1.00 19.18 ?  6   PHE   A HD2  1 
ATOM   99   H HE1  . PHE   A 1 6   ? 18.439 -5.861  14.515  1.00 18.87 ?  6   PHE   A HE1  1 
ATOM   100  H HE2  . PHE   A 1 6   ? 20.448 -9.047  15.866  1.00 19.56 ?  6   PHE   A HE2  1 
ATOM   101  H HZ   . PHE   A 1 6   ? 20.416 -7.042  14.712  1.00 19.20 ?  6   PHE   A HZ   1 
ATOM   102  N N    A SER   A 1 7   ? 13.250 -7.628  18.323  0.88 18.07 ?  7   SER   A N    1 
ATOM   103  N N    B SER   A 1 7   ? 13.246 -7.627  18.351  0.12 18.95 ?  7   SER   A N    1 
ATOM   104  C CA   A SER   A 1 7   ? 11.882 -7.781  18.796  0.88 19.15 ?  7   SER   A CA   1 
ATOM   105  C CA   B SER   A 1 7   ? 11.876 -7.830  18.806  0.12 19.13 ?  7   SER   A CA   1 
ATOM   106  C C    A SER   A 1 7   ? 10.889 -7.493  17.678  0.88 17.82 ?  7   SER   A C    1 
ATOM   107  C C    B SER   A 1 7   ? 10.886 -7.488  17.702  0.12 18.23 ?  7   SER   A C    1 
ATOM   108  O O    A SER   A 1 7   ? 11.117 -6.617  16.840  0.88 17.88 ?  7   SER   A O    1 
ATOM   109  O O    B SER   A 1 7   ? 11.112 -6.578  16.900  0.12 18.33 ?  7   SER   A O    1 
ATOM   110  C CB   A SER   A 1 7   ? 11.622 -6.823  19.966  0.88 21.70 ?  7   SER   A CB   1 
ATOM   111  C CB   B SER   A 1 7   ? 11.570 -6.982  20.051  0.12 20.10 ?  7   SER   A CB   1 
ATOM   112  O OG   A SER   A 1 7   ? 10.271 -6.870  20.379  0.88 23.77 ?  7   SER   A OG   1 
ATOM   113  O OG   B SER   A 1 7   ? 10.226 -7.152  20.463  0.12 20.76 ?  7   SER   A OG   1 
ATOM   114  H H    A SER   A 1 7   ? 13.393 -6.881  17.925  0.88 21.68 ?  7   SER   A H    1 
ATOM   115  H H    B SER   A 1 7   ? 13.382 -6.861  17.988  0.12 22.74 ?  7   SER   A H    1 
ATOM   116  H HA   A SER   A 1 7   ? 11.739 -8.689  19.107  0.88 22.98 ?  7   SER   A HA   1 
ATOM   117  H HA   B SER   A 1 7   ? 11.748 -8.760  19.042  0.12 22.95 ?  7   SER   A HA   1 
ATOM   118  H HB2  A SER   A 1 7   ? 12.191 -7.074  20.713  0.88 26.04 ?  7   SER   A HB2  1 
ATOM   119  H HB2  B SER   A 1 7   ? 12.157 -7.258  20.774  0.12 24.12 ?  7   SER   A HB2  1 
ATOM   120  H HB3  A SER   A 1 7   ? 11.826 -5.918  19.686  0.88 26.04 ?  7   SER   A HB3  1 
ATOM   121  H HB3  B SER   A 1 7   ? 11.719 -6.047  19.843  0.12 24.12 ?  7   SER   A HB3  1 
ATOM   122  H HG   A SER   A 1 7   ? 10.146 -6.349  21.027  0.88 28.53 ?  7   SER   A HG   1 
ATOM   123  H HG   B SER   A 1 7   ? 10.081 -7.957  20.652  0.12 24.92 ?  7   SER   A HG   1 
ATOM   124  N N    . GLY   A 1 8   ? 9.780  -8.232  17.673  1.00 17.34 ?  8   GLY   A N    1 
ATOM   125  C CA   . GLY   A 1 8   ? 8.709  -7.972  16.732  1.00 16.92 ?  8   GLY   A CA   1 
ATOM   126  C C    . GLY   A 1 8   ? 8.909  -8.504  15.334  1.00 15.86 ?  8   GLY   A C    1 
ATOM   127  O O    . GLY   A 1 8   ? 8.168  -8.103  14.429  1.00 16.87 ?  8   GLY   A O    1 
ATOM   128  H H    A GLY   A 1 8   ? 9.629  -8.887  18.208  0.88 20.81 ?  8   GLY   A H    1 
ATOM   129  H H    B GLY   A 1 8   ? 9.632  -8.897  18.196  0.12 20.81 ?  8   GLY   A H    1 
ATOM   130  H HA2  . GLY   A 1 8   ? 7.891  -8.359  17.078  1.00 20.31 ?  8   GLY   A HA2  1 
ATOM   131  H HA3  . GLY   A 1 8   ? 8.579  -7.012  16.667  1.00 20.31 ?  8   GLY   A HA3  1 
ATOM   132  N N    . TYR   A 1 9   ? 9.884  -9.383  15.117  1.00 14.37 ?  9   TYR   A N    1 
ATOM   133  C CA   . TYR   A 1 9   ? 10.137 -9.932  13.793  1.00 13.10 ?  9   TYR   A CA   1 
ATOM   134  C C    . TYR   A 1 9   ? 9.254  -11.145 13.521  1.00 13.13 ?  9   TYR   A C    1 
ATOM   135  O O    . TYR   A 1 9   ? 8.958  -11.949 14.413  1.00 14.93 ?  9   TYR   A O    1 
ATOM   136  C CB   . TYR   A 1 9   ? 11.613 -10.335 13.632  1.00 13.28 ?  9   TYR   A CB   1 
ATOM   137  C CG   . TYR   A 1 9   ? 12.532 -9.148  13.471  1.00 13.14 ?  9   TYR   A CG   1 
ATOM   138  C CD1  . TYR   A 1 9   ? 12.859 -8.352  14.556  1.00 13.87 ?  9   TYR   A CD1  1 
ATOM   139  C CD2  . TYR   A 1 9   ? 13.048 -8.807  12.229  1.00 12.75 ?  9   TYR   A CD2  1 
ATOM   140  C CE1  . TYR   A 1 9   ? 13.676 -7.246  14.415  1.00 14.24 ?  9   TYR   A CE1  1 
ATOM   141  C CE2  . TYR   A 1 9   ? 13.866 -7.703  12.076  1.00 13.20 ?  9   TYR   A CE2  1 
ATOM   142  C CZ   . TYR   A 1 9   ? 14.173 -6.925  13.171  1.00 14.22 ?  9   TYR   A CZ   1 
ATOM   143  O OH   . TYR   A 1 9   ? 14.974 -5.828  13.022  1.00 15.30 ?  9   TYR   A OH   1 
ATOM   144  H H    . TYR   A 1 9   ? 10.423 -9.669  15.725  1.00 17.25 ?  9   TYR   A H    1 
ATOM   145  H HA   . TYR   A 1 9   ? 9.945  -9.251  13.126  1.00 15.73 ?  9   TYR   A HA   1 
ATOM   146  H HB2  . TYR   A 1 9   ? 11.897 -10.835 14.413  1.00 15.94 ?  9   TYR   A HB2  1 
ATOM   147  H HB3  . TYR   A 1 9   ? 11.696 -10.887 12.838  1.00 15.94 ?  9   TYR   A HB3  1 
ATOM   148  H HD1  . TYR   A 1 9   ? 12.509 -8.566  15.395  1.00 16.64 ?  9   TYR   A HD1  1 
ATOM   149  H HD2  . TYR   A 1 9   ? 12.839 -9.329  11.486  1.00 15.30 ?  9   TYR   A HD2  1 
ATOM   150  H HE1  . TYR   A 1 9   ? 13.880 -6.725  15.157  1.00 17.09 ?  9   TYR   A HE1  1 
ATOM   151  H HE2  . TYR   A 1 9   ? 14.212 -7.487  11.239  1.00 15.84 ?  9   TYR   A HE2  1 
ATOM   152  H HH   . TYR   A 1 9   ? 15.091 -5.453  13.768  1.00 18.36 ?  9   TYR   A HH   1 
ATOM   153  N N    . LEU   A 1 10  ? 8.850  -11.274 12.264  1.00 12.46 ?  10  LEU   A N    1 
ATOM   154  C CA   . LEU   A 1 10  ? 8.243  -12.496 11.764  1.00 12.05 ?  10  LEU   A CA   1 
ATOM   155  C C    . LEU   A 1 10  ? 9.361  -13.429 11.303  1.00 11.34 ?  10  LEU   A C    1 
ATOM   156  O O    . LEU   A 1 10  ? 10.315 -12.998 10.646  1.00 12.05 ?  10  LEU   A O    1 
ATOM   157  C CB   . LEU   A 1 10  ? 7.324  -12.156 10.590  1.00 13.54 ?  10  LEU   A CB   1 
ATOM   158  C CG   . LEU   A 1 10  ? 6.600  -13.337 9.937   1.00 16.05 ?  10  LEU   A CG   1 
ATOM   159  C CD1  . LEU   A 1 10  ? 5.527  -13.906 10.856  1.00 18.66 ?  10  LEU   A CD1  1 
ATOM   160  C CD2  . LEU   A 1 10  ? 6.017  -12.954 8.584   1.00 18.83 ?  10  LEU   A CD2  1 
ATOM   161  H H    . LEU   A 1 10  ? 8.928  -10.653 11.664  1.00 14.95 ?  10  LEU   A H    1 
ATOM   162  H HA   . LEU   A 1 10  ? 7.722  -12.920 12.471  1.00 14.47 ?  10  LEU   A HA   1 
ATOM   163  H HB2  . LEU   A 1 10  ? 6.645  -11.534 10.900  1.00 16.25 ?  10  LEU   A HB2  1 
ATOM   164  H HB3  . LEU   A 1 10  ? 7.859  -11.731 9.903   1.00 16.25 ?  10  LEU   A HB3  1 
ATOM   165  H HG   . LEU   A 1 10  ? 7.245  -14.043 9.785   1.00 19.27 ?  10  LEU   A HG   1 
ATOM   166  H HD11 . LEU   A 1 10  ? 5.138  -14.689 10.438  1.00 22.40 ?  10  LEU   A HD11 1 
ATOM   167  H HD12 . LEU   A 1 10  ? 5.933  -14.153 11.704  1.00 22.40 ?  10  LEU   A HD12 1 
ATOM   168  H HD13 . LEU   A 1 10  ? 4.845  -13.233 11.002  1.00 22.40 ?  10  LEU   A HD13 1 
ATOM   169  H HD21 . LEU   A 1 10  ? 5.568  -13.726 8.208   1.00 22.59 ?  10  LEU   A HD21 1 
ATOM   170  H HD22 . LEU   A 1 10  ? 5.388  -12.229 8.708   1.00 22.59 ?  10  LEU   A HD22 1 
ATOM   171  H HD23 . LEU   A 1 10  ? 6.740  -12.673 8.003   1.00 22.59 ?  10  LEU   A HD23 1 
ATOM   172  N N    . LYS   A 1 11  ? 9.252  -14.704 11.667  1.00 11.53 ?  11  LYS   A N    1 
ATOM   173  C CA   . LYS   A 1 11  ? 10.252 -15.701 11.309  1.00 11.34 ?  11  LYS   A CA   1 
ATOM   174  C C    . LYS   A 1 11  ? 9.894  -16.276 9.946   1.00 11.42 ?  11  LYS   A C    1 
ATOM   175  O O    . LYS   A 1 11  ? 8.818  -16.858 9.786   1.00 13.53 ?  11  LYS   A O    1 
ATOM   176  C CB   . LYS   A 1 11  ? 10.272 -16.792 12.375  1.00 11.24 ?  11  LYS   A CB   1 
ATOM   177  C CG   . LYS   A 1 11  ? 11.312 -17.876 12.182  1.00 11.38 ?  11  LYS   A CG   1 
ATOM   178  C CD   . LYS   A 1 11  ? 11.392 -18.742 13.439  1.00 12.04 ?  11  LYS   A CD   1 
ATOM   179  C CE   . LYS   A 1 11  ? 12.377 -19.894 13.303  1.00 12.03 ?  11  LYS   A CE   1 
ATOM   180  N NZ   . LYS   A 1 11  ? 13.757 -19.429 13.031  1.00 12.19 ?  11  LYS   A NZ   1 
ATOM   181  H H    . LYS   A 1 11  ? 8.589  -15.018 12.120  1.00 13.84 ?  11  LYS   A H    1 
ATOM   182  H HA   . LYS   A 1 11  ? 11.125 -15.283 11.257  1.00 13.61 ?  11  LYS   A HA   1 
ATOM   183  H HB2  . LYS   A 1 11  ? 10.441 -16.374 13.233  1.00 13.49 ?  11  LYS   A HB2  1 
ATOM   184  H HB3  . LYS   A 1 11  ? 9.400  -17.219 12.389  1.00 13.49 ?  11  LYS   A HB3  1 
ATOM   185  H HG2  . LYS   A 1 11  ? 11.057 -18.439 11.432  1.00 13.65 ?  11  LYS   A HG2  1 
ATOM   186  H HG3  . LYS   A 1 11  ? 12.177 -17.471 12.026  1.00 13.65 ?  11  LYS   A HG3  1 
ATOM   187  H HD2  . LYS   A 1 11  ? 11.672 -18.186 14.183  1.00 14.45 ?  11  LYS   A HD2  1 
ATOM   188  H HD3  . LYS   A 1 11  ? 10.512 -19.114 13.619  1.00 14.45 ?  11  LYS   A HD3  1 
ATOM   189  H HE2  . LYS   A 1 11  ? 12.389 -20.399 14.134  1.00 14.43 ?  11  LYS   A HE2  1 
ATOM   190  H HE3  . LYS   A 1 11  ? 12.100 -20.466 12.571  1.00 14.43 ?  11  LYS   A HE3  1 
ATOM   191  H HZ1  . LYS   A 1 11  ? 14.289 -20.125 12.877  1.00 14.63 ?  11  LYS   A HZ1  1 
ATOM   192  H HZ2  . LYS   A 1 11  ? 13.764 -18.899 12.315  1.00 14.63 ?  11  LYS   A HZ2  1 
ATOM   193  H HZ3  . LYS   A 1 11  ? 14.071 -18.974 13.728  1.00 14.63 ?  11  LYS   A HZ3  1 
ATOM   194  N N    . LEU   A 1 12  ? 10.782 -16.117 8.963   1.00 10.68 ?  12  LEU   A N    1 
ATOM   195  C CA   . LEU   A 1 12  ? 10.519 -16.686 7.646   1.00 11.29 ?  12  LEU   A CA   1 
ATOM   196  C C    . LEU   A 1 12  ? 11.092 -18.086 7.495   1.00 11.01 ?  12  LEU   A C    1 
ATOM   197  O O    . LEU   A 1 12  ? 10.455 -18.948 6.880   1.00 11.64 ?  12  LEU   A O    1 
ATOM   198  C CB   . LEU   A 1 12  ? 11.082 -15.788 6.542   1.00 11.99 ?  12  LEU   A CB   1 
ATOM   199  C CG   . LEU   A 1 12  ? 10.421 -14.418 6.378   1.00 12.85 ?  12  LEU   A CG   1 
ATOM   200  C CD1  . LEU   A 1 12  ? 11.175 -13.611 5.337   1.00 13.73 ?  12  LEU   A CD1  1 
ATOM   201  C CD2  . LEU   A 1 12  ? 8.960  -14.561 5.991   1.00 13.64 ?  12  LEU   A CD2  1 
ATOM   202  H H    . LEU   A 1 12  ? 11.533 -15.689 9.028   1.00 12.82 ?  12  LEU   A H    1 
ATOM   203  H HA   . LEU   A 1 12  ? 9.559  -16.744 7.518   1.00 13.55 ?  12  LEU   A HA   1 
ATOM   204  H HB2  . LEU   A 1 12  ? 12.021 -15.633 6.723   1.00 14.39 ?  12  LEU   A HB2  1 
ATOM   205  H HB3  . LEU   A 1 12  ? 10.991 -16.254 5.695   1.00 14.39 ?  12  LEU   A HB3  1 
ATOM   206  H HG   . LEU   A 1 12  ? 10.464 -13.937 7.217   1.00 15.43 ?  12  LEU   A HG   1 
ATOM   207  H HD11 . LEU   A 1 12  ? 10.751 -12.744 5.235   1.00 16.48 ?  12  LEU   A HD11 1 
ATOM   208  H HD12 . LEU   A 1 12  ? 12.094 -13.496 5.631   1.00 16.48 ?  12  LEU   A HD12 1 
ATOM   209  H HD13 . LEU   A 1 12  ? 11.159 -14.088 4.491   1.00 16.48 ?  12  LEU   A HD13 1 
ATOM   210  H HD21 . LEU   A 1 12  ? 8.604  -13.690 5.753   1.00 16.37 ?  12  LEU   A HD21 1 
ATOM   211  H HD22 . LEU   A 1 12  ? 8.889  -15.163 5.232   1.00 16.37 ?  12  LEU   A HD22 1 
ATOM   212  H HD23 . LEU   A 1 12  ? 8.466  -14.924 6.744   1.00 16.37 ?  12  LEU   A HD23 1 
ATOM   213  N N    . THR   A 1 13  ? 12.304 -18.301 8.005   1.00 10.93 ?  13  THR   A N    1 
ATOM   214  C CA   . THR   A 1 13  ? 12.992 -19.581 7.905   1.00 11.31 ?  13  THR   A CA   1 
ATOM   215  C C    . THR   A 1 13  ? 13.770 -19.809 9.193   1.00 11.12 ?  13  THR   A C    1 
ATOM   216  O O    . THR   A 1 13  ? 13.684 -19.032 10.148  1.00 11.40 ?  13  THR   A O    1 
ATOM   217  C CB   . THR   A 1 13  ? 13.957 -19.616 6.715   1.00 11.93 ?  13  THR   A CB   1 
ATOM   218  O OG1  . THR   A 1 13  ? 15.025 -18.705 6.971   1.00 12.12 ?  13  THR   A OG1  1 
ATOM   219  C CG2  . THR   A 1 13  ? 13.273 -19.256 5.406   1.00 13.47 ?  13  THR   A CG2  1 
ATOM   220  H H    . THR   A 1 13  ? 12.760 -17.700 8.417   1.00 13.12 ?  13  THR   A H    1 
ATOM   221  H HA   . THR   A 1 13  ? 12.341 -20.294 7.802   1.00 13.58 ?  13  THR   A HA   1 
ATOM   222  H HB   . THR   A 1 13  ? 14.318 -20.511 6.627   1.00 14.32 ?  13  THR   A HB   1 
ATOM   223  H HG1  . THR   A 1 13  ? 15.688 -19.114 7.275   1.00 14.55 ?  13  THR   A HG1  1 
ATOM   224  H HG21 . THR   A 1 13  ? 13.887 -19.391 4.665   1.00 16.17 ?  13  THR   A HG21 1 
ATOM   225  H HG22 . THR   A 1 13  ? 12.495 -19.821 5.272   1.00 16.17 ?  13  THR   A HG22 1 
ATOM   226  H HG23 . THR   A 1 13  ? 12.993 -18.330 5.418   1.00 16.17 ?  13  THR   A HG23 1 
ATOM   227  N N    . ASP   A 1 14  ? 14.567 -20.875 9.203   1.00 11.65 ?  14  ASP   A N    1 
ATOM   228  C CA   . ASP   A 1 14  ? 15.416 -21.155 10.353  1.00 12.01 ?  14  ASP   A CA   1 
ATOM   229  C C    . ASP   A 1 14  ? 16.254 -19.942 10.748  1.00 11.50 ?  14  ASP   A C    1 
ATOM   230  O O    . ASP   A 1 14  ? 16.493 -19.713 11.938  1.00 12.95 ?  14  ASP   A O    1 
ATOM   231  C CB   . ASP   A 1 14  ? 16.334 -22.332 10.041  1.00 14.27 ?  14  ASP   A CB   1 
ATOM   232  C CG   . ASP   A 1 14  ? 17.219 -22.687 11.204  1.00 18.36 ?  14  ASP   A CG   1 
ATOM   233  O OD1  . ASP   A 1 14  ? 16.679 -23.123 12.244  1.00 19.56 ?  14  ASP   A OD1  1 
ATOM   234  O OD2  . ASP   A 1 14  ? 18.447 -22.522 11.073  1.00 21.66 -1 14  ASP   A OD2  1 
ATOM   235  H H    . ASP   A 1 14  ? 14.636 -21.438 8.559   1.00 13.98 ?  14  ASP   A H    1 
ATOM   236  H HA   . ASP   A 1 14  ? 14.855 -21.397 11.108  1.00 14.42 ?  14  ASP   A HA   1 
ATOM   237  H HB2  . ASP   A 1 14  ? 15.782 -23.107 9.814   1.00 17.13 ?  14  ASP   A HB2  1 
ATOM   238  H HB3  . ASP   A 1 14  ? 16.899 -22.104 9.292   1.00 17.13 ?  14  ASP   A HB3  1 
ATOM   239  N N    . ASN   A 1 15  ? 16.722 -19.159 9.764   1.00 11.01 ?  15  ASN   A N    1 
ATOM   240  C CA   . ASN   A 1 15  ? 17.716 -18.124 10.026  1.00 11.39 ?  15  ASN   A CA   1 
ATOM   241  C C    . ASN   A 1 15  ? 17.345 -16.729 9.539   1.00 11.80 ?  15  ASN   A C    1 
ATOM   242  O O    . ASN   A 1 15  ? 18.110 -15.797 9.799   1.00 13.47 ?  15  ASN   A O    1 
ATOM   243  C CB   . ASN   A 1 15  ? 19.083 -18.523 9.435   1.00 11.36 ?  15  ASN   A CB   1 
ATOM   244  C CG   . ASN   A 1 15  ? 19.065 -18.612 7.925   1.00 11.55 ?  15  ASN   A CG   1 
ATOM   245  O OD1  . ASN   A 1 15  ? 18.338 -19.426 7.351   1.00 12.50 ?  15  ASN   A OD1  1 
ATOM   246  N ND2  . ASN   A 1 15  ? 19.854 -17.771 7.269   1.00 11.83 ?  15  ASN   A ND2  1 
ATOM   247  H H    . ASN   A 1 15  ? 16.475 -19.212 8.948   1.00 13.21 ?  15  ASN   A H    1 
ATOM   248  H HA   . ASN   A 1 15  ? 17.840 -18.063 10.985  1.00 13.68 ?  15  ASN   A HA   1 
ATOM   249  H HB2  . ASN   A 1 15  ? 19.745 -17.858 9.689   1.00 13.64 ?  15  ASN   A HB2  1 
ATOM   250  H HB3  . ASN   A 1 15  ? 19.340 -19.393 9.781   1.00 13.64 ?  15  ASN   A HB3  1 
ATOM   251  H HD21 . ASN   A 1 15  ? 19.875 -17.781 6.407   1.00 14.19 ?  15  ASN   A HD21 1 
ATOM   252  H HD22 . ASN   A 1 15  ? 20.352 -17.214 7.700   1.00 14.19 ?  15  ASN   A HD22 1 
ATOM   253  N N    . VAL   A 1 16  ? 16.210 -16.547 8.866   1.00 11.27 ?  16  VAL   A N    1 
ATOM   254  C CA   . VAL   A 1 16  ? 15.828 -15.258 8.300   1.00 10.99 ?  16  VAL   A CA   1 
ATOM   255  C C    . VAL   A 1 16  ? 14.551 -14.769 8.974   1.00 10.70 ?  16  VAL   A C    1 
ATOM   256  O O    . VAL   A 1 16  ? 13.547 -15.493 9.041   1.00 10.81 ?  16  VAL   A O    1 
ATOM   257  C CB   . VAL   A 1 16  ? 15.655 -15.323 6.773   1.00 11.68 ?  16  VAL   A CB   1 
ATOM   258  C CG1  . VAL   A 1 16  ? 15.218 -13.965 6.221   1.00 12.57 ?  16  VAL   A CG1  1 
ATOM   259  C CG2  . VAL   A 1 16  ? 16.942 -15.782 6.098   1.00 13.02 ?  16  VAL   A CG2  1 
ATOM   260  H H    . VAL   A 1 16  ? 15.634 -17.169 8.732   1.00 13.53 ?  16  VAL   A H    1 
ATOM   261  H HA   . VAL   A 1 16  ? 16.532 -14.613 8.489   1.00 13.19 ?  16  VAL   A HA   1 
ATOM   262  H HB   . VAL   A 1 16  ? 14.966 -15.968 6.563   1.00 14.02 ?  16  VAL   A HB   1 
ATOM   263  H HG11 . VAL   A 1 16  ? 15.310 -13.975 5.254   1.00 15.09 ?  16  VAL   A HG11 1 
ATOM   264  H HG12 . VAL   A 1 16  ? 14.292 -13.808 6.461   1.00 15.09 ?  16  VAL   A HG12 1 
ATOM   265  H HG13 . VAL   A 1 16  ? 15.782 -13.272 6.598   1.00 15.09 ?  16  VAL   A HG13 1 
ATOM   266  H HG21 . VAL   A 1 16  ? 16.821 -15.757 5.134   1.00 15.63 ?  16  VAL   A HG21 1 
ATOM   267  H HG22 . VAL   A 1 16  ? 17.666 -15.187 6.352   1.00 15.63 ?  16  VAL   A HG22 1 
ATOM   268  H HG23 . VAL   A 1 16  ? 17.146 -16.686 6.381   1.00 15.63 ?  16  VAL   A HG23 1 
ATOM   269  N N    . TYR   A 1 17  ? 14.591 -13.512 9.415   1.00 10.59 ?  17  TYR   A N    1 
ATOM   270  C CA   . TYR   A 1 17  ? 13.517 -12.832 10.121  1.00 10.49 ?  17  TYR   A CA   1 
ATOM   271  C C    . TYR   A 1 17  ? 13.251 -11.504 9.426   1.00 10.93 ?  17  TYR   A C    1 
ATOM   272  O O    . TYR   A 1 17  ? 14.153 -10.938 8.806   1.00 11.29 ?  17  TYR   A O    1 
ATOM   273  C CB   . TYR   A 1 17  ? 13.949 -12.569 11.569  1.00 11.03 ?  17  TYR   A CB   1 
ATOM   274  C CG   . TYR   A 1 17  ? 14.139 -13.835 12.378  1.00 11.81 ?  17  TYR   A CG   1 
ATOM   275  C CD1  . TYR   A 1 17  ? 15.298 -14.594 12.273  1.00 12.65 ?  17  TYR   A CD1  1 
ATOM   276  C CD2  . TYR   A 1 17  ? 13.146 -14.284 13.234  1.00 12.04 ?  17  TYR   A CD2  1 
ATOM   277  C CE1  . TYR   A 1 17  ? 15.461 -15.766 13.002  1.00 13.06 ?  17  TYR   A CE1  1 
ATOM   278  C CE2  . TYR   A 1 17  ? 13.301 -15.455 13.970  1.00 12.56 ?  17  TYR   A CE2  1 
ATOM   279  C CZ   . TYR   A 1 17  ? 14.460 -16.190 13.853  1.00 12.88 ?  17  TYR   A CZ   1 
ATOM   280  O OH   . TYR   A 1 17  ? 14.619 -17.347 14.583  1.00 13.69 ?  17  TYR   A OH   1 
ATOM   281  H H    . TYR   A 1 17  ? 15.278 -13.001 9.297   1.00 12.71 ?  17  TYR   A H    1 
ATOM   282  H HA   . TYR   A 1 17  ? 12.711 -13.375 10.109  1.00 12.59 ?  17  TYR   A HA   1 
ATOM   283  H HB2  . TYR   A 1 17  ? 14.790 -12.092 11.560  1.00 13.24 ?  17  TYR   A HB2  1 
ATOM   284  H HB3  . TYR   A 1 17  ? 13.269 -12.038 12.003  1.00 13.24 ?  17  TYR   A HB3  1 
ATOM   285  H HD1  . TYR   A 1 17  ? 15.975 -14.319 11.697  1.00 15.18 ?  17  TYR   A HD1  1 
ATOM   286  H HD2  . TYR   A 1 17  ? 12.360 -13.798 13.320  1.00 14.45 ?  17  TYR   A HD2  1 
ATOM   287  H HE1  . TYR   A 1 17  ? 16.248 -16.263 12.919  1.00 15.67 ?  17  TYR   A HE1  1 
ATOM   288  H HE2  . TYR   A 1 17  ? 12.627 -15.740 14.544  1.00 15.07 ?  17  TYR   A HE2  1 
ATOM   289  H HH   . TYR   A 1 17  ? 13.891 -17.554 14.952  1.00 16.43 ?  17  TYR   A HH   1 
ATOM   290  N N    . ILE   A 1 18  ? 12.019 -10.989 9.531   1.00 11.25 ?  18  ILE   A N    1 
ATOM   291  C CA   . ILE   A 1 18  ? 11.636 -9.779  8.804   1.00 11.70 ?  18  ILE   A CA   1 
ATOM   292  C C    . ILE   A 1 18  ? 10.684 -8.923  9.633   1.00 12.10 ?  18  ILE   A C    1 
ATOM   293  O O    . ILE   A 1 18  ? 9.849  -9.436  10.386  1.00 12.57 ?  18  ILE   A O    1 
ATOM   294  C CB   . ILE   A 1 18  ? 11.049 -10.145 7.420   1.00 12.16 ?  18  ILE   A CB   1 
ATOM   295  C CG1  . ILE   A 1 18  ? 10.995 -8.929  6.497   1.00 12.98 ?  18  ILE   A CG1  1 
ATOM   296  C CG2  . ILE   A 1 18  ? 9.692  -10.842 7.564   1.00 12.80 ?  18  ILE   A CG2  1 
ATOM   297  C CD1  . ILE   A 1 18  ? 10.713 -9.298  5.065   1.00 14.97 ?  18  ILE   A CD1  1 
ATOM   298  H H    . ILE   A 1 18  ? 11.387 -11.337 10.004  1.00 13.50 ?  18  ILE   A H    1 
ATOM   299  H HA   . ILE   A 1 18  ? 12.443 -9.259  8.648   1.00 14.04 ?  18  ILE   A HA   1 
ATOM   300  H HB   . ILE   A 1 18  ? 11.653 -10.782 7.014   1.00 14.60 ?  18  ILE   A HB   1 
ATOM   301  H HG12 . ILE   A 1 18  ? 10.298 -8.333  6.795   1.00 15.59 ?  18  ILE   A HG12 1 
ATOM   302  H HG13 . ILE   A 1 18  ? 11.856 -8.479  6.520   1.00 15.59 ?  18  ILE   A HG13 1 
ATOM   303  H HG21 . ILE   A 1 18  ? 9.428  -11.199 6.700   1.00 15.37 ?  18  ILE   A HG21 1 
ATOM   304  H HG22 . ILE   A 1 18  ? 9.774  -11.562 8.207   1.00 15.37 ?  18  ILE   A HG22 1 
ATOM   305  H HG23 . ILE   A 1 18  ? 9.033  -10.198 7.870   1.00 15.37 ?  18  ILE   A HG23 1 
ATOM   306  H HD11 . ILE   A 1 18  ? 10.761 -8.495  4.518   1.00 17.97 ?  18  ILE   A HD11 1 
ATOM   307  H HD12 . ILE   A 1 18  ? 11.374 -9.940  4.764   1.00 17.97 ?  18  ILE   A HD12 1 
ATOM   308  H HD13 . ILE   A 1 18  ? 9.825  -9.682  5.006   1.00 17.97 ?  18  ILE   A HD13 1 
ATOM   309  N N    . LYS   A 1 19  ? 10.799 -7.602  9.466   1.00 12.56 ?  19  LYS   A N    1 
ATOM   310  C CA   . LYS   A 1 19  ? 9.989  -6.649  10.217  1.00 14.08 ?  19  LYS   A CA   1 
ATOM   311  C C    . LYS   A 1 19  ? 9.773  -5.400  9.374   1.00 14.51 ?  19  LYS   A C    1 
ATOM   312  O O    . LYS   A 1 19  ? 10.664 -4.994  8.624   1.00 14.44 ?  19  LYS   A O    1 
ATOM   313  C CB   . LYS   A 1 19  ? 10.709 -6.278  11.521  1.00 15.10 ?  19  LYS   A CB   1 
ATOM   314  C CG   . LYS   A 1 19  ? 9.955  -5.382  12.490  1.00 17.03 ?  19  LYS   A CG   1 
ATOM   315  C CD   . LYS   A 1 19  ? 10.865 -5.072  13.675  1.00 18.55 ?  19  LYS   A CD   1 
ATOM   316  C CE   . LYS   A 1 19  ? 10.226 -4.148  14.695  1.00 19.43 ?  19  LYS   A CE   1 
ATOM   317  N NZ   . LYS   A 1 19  ? 11.141 -3.929  15.853  1.00 19.64 ?  19  LYS   A NZ   1 
ATOM   318  H H    . LYS   A 1 19  ? 11.354 -7.228  8.918   1.00 15.07 ?  19  LYS   A H    1 
ATOM   319  H HA   . LYS   A 1 19  ? 9.130  -7.048  10.431  1.00 16.90 ?  19  LYS   A HA   1 
ATOM   320  H HB2  . LYS   A 1 19  ? 10.914 -7.099  11.996  1.00 18.13 ?  19  LYS   A HB2  1 
ATOM   321  H HB3  . LYS   A 1 19  ? 11.534 -5.826  11.292  1.00 18.13 ?  19  LYS   A HB3  1 
ATOM   322  H HG2  . LYS   A 1 19  ? 9.716  -4.551  12.052  1.00 20.44 ?  19  LYS   A HG2  1 
ATOM   323  H HG3  . LYS   A 1 19  ? 9.163  -5.841  12.814  1.00 20.44 ?  19  LYS   A HG3  1 
ATOM   324  H HD2  . LYS   A 1 19  ? 11.088 -5.903  14.125  1.00 22.26 ?  19  LYS   A HD2  1 
ATOM   325  H HD3  . LYS   A 1 19  ? 11.671 -4.646  13.348  1.00 22.26 ?  19  LYS   A HD3  1 
ATOM   326  H HE2  . LYS   A 1 19  ? 10.045 -3.288  14.282  1.00 23.32 ?  19  LYS   A HE2  1 
ATOM   327  H HE3  . LYS   A 1 19  ? 9.406  -4.545  15.024  1.00 23.32 ?  19  LYS   A HE3  1 
ATOM   328  H HZ1  . LYS   A 1 19  ? 10.709 -3.510  16.508  1.00 23.57 ?  19  LYS   A HZ1  1 
ATOM   329  H HZ2  . LYS   A 1 19  ? 11.439 -4.711  16.157  1.00 23.57 ?  19  LYS   A HZ2  1 
ATOM   330  H HZ3  . LYS   A 1 19  ? 11.836 -3.434  15.603  1.00 23.57 ?  19  LYS   A HZ3  1 
ATOM   331  N N    . ASN   A 1 20  ? 8.591  -4.797  9.489   1.00 15.36 ?  20  ASN   A N    1 
ATOM   332  C CA   . ASN   A 1 20  ? 8.354  -3.471  8.929   1.00 16.92 ?  20  ASN   A CA   1 
ATOM   333  C C    . ASN   A 1 20  ? 8.969  -2.465  9.890   1.00 17.17 ?  20  ASN   A C    1 
ATOM   334  O O    . ASN   A 1 20  ? 8.445  -2.243  10.986  1.00 18.52 ?  20  ASN   A O    1 
ATOM   335  C CB   . ASN   A 1 20  ? 6.855  -3.236  8.750   1.00 18.33 ?  20  ASN   A CB   1 
ATOM   336  C CG   . ASN   A 1 20  ? 6.514  -1.801  8.359   1.00 20.28 ?  20  ASN   A CG   1 
ATOM   337  O OD1  . ASN   A 1 20  ? 5.558  -1.225  8.874   1.00 22.56 ?  20  ASN   A OD1  1 
ATOM   338  N ND2  . ASN   A 1 20  ? 7.286  -1.225  7.445   1.00 20.69 ?  20  ASN   A ND2  1 
ATOM   339  H H    . ASN   A 1 20  ? 7.910  -5.140  9.888   1.00 18.43 ?  20  ASN   A H    1 
ATOM   340  H HA   . ASN   A 1 20  ? 8.792  -3.395  8.069   1.00 20.30 ?  20  ASN   A HA   1 
ATOM   341  H HB2  . ASN   A 1 20  ? 6.528  -3.820  8.051   1.00 22.00 ?  20  ASN   A HB2  1 
ATOM   342  H HB3  . ASN   A 1 20  ? 6.405  -3.436  9.586   1.00 22.00 ?  20  ASN   A HB3  1 
ATOM   343  H HD21 . ASN   A 1 20  ? 7.128  -0.418  7.199   1.00 24.83 ?  20  ASN   A HD21 1 
ATOM   344  H HD22 . ASN   A 1 20  ? 7.945  -1.659  7.105   1.00 24.83 ?  20  ASN   A HD22 1 
ATOM   345  N N    . ALA   A 1 21  ? 10.105 -1.887  9.507   1.00 17.11 ?  21  ALA   A N    1 
ATOM   346  C CA   . ALA   A 1 21  ? 10.793 -0.976  10.408  1.00 17.15 ?  21  ALA   A CA   1 
ATOM   347  C C    . ALA   A 1 21  ? 11.765 -0.111  9.625   1.00 16.54 ?  21  ALA   A C    1 
ATOM   348  O O    . ALA   A 1 21  ? 12.211 -0.472  8.533   1.00 17.15 ?  21  ALA   A O    1 
ATOM   349  C CB   . ALA   A 1 21  ? 11.527 -1.739  11.512  1.00 18.83 ?  21  ALA   A CB   1 
ATOM   350  H H    . ALA   A 1 21  ? 10.488 -2.000  8.743   1.00 20.53 ?  21  ALA   A H    1 
ATOM   351  H HA   . ALA   A 1 21  ? 10.138 -0.393  10.827  1.00 20.59 ?  21  ALA   A HA   1 
ATOM   352  H HB1  . ALA   A 1 21  ? 11.917 -1.100  12.123  1.00 22.59 ?  21  ALA   A HB1  1 
ATOM   353  H HB2  . ALA   A 1 21  ? 10.884 -2.297  11.984  1.00 22.59 ?  21  ALA   A HB2  1 
ATOM   354  H HB3  . ALA   A 1 21  ? 12.211 -2.291  11.112  1.00 22.59 ?  21  ALA   A HB3  1 
ATOM   355  N N    . ASP   A 1 22  ? 12.062 1.052   10.209  1.00 16.49 ?  22  ASP   A N    1 
ATOM   356  C CA   . ASP   A 1 22  ? 13.100 1.953   9.733   1.00 16.52 ?  22  ASP   A CA   1 
ATOM   357  C C    . ASP   A 1 22  ? 14.432 1.444   10.270  1.00 15.17 ?  22  ASP   A C    1 
ATOM   358  O O    . ASP   A 1 22  ? 14.640 1.418   11.487  1.00 16.11 ?  22  ASP   A O    1 
ATOM   359  C CB   . ASP   A 1 22  ? 12.799 3.347   10.284  1.00 18.86 ?  22  ASP   A CB   1 
ATOM   360  C CG   . ASP   A 1 22  ? 13.760 4.408   9.783   1.00 21.07 ?  22  ASP   A CG   1 
ATOM   361  O OD1  . ASP   A 1 22  ? 14.863 4.057   9.323   1.00 21.31 ?  22  ASP   A OD1  1 
ATOM   362  O OD2  . ASP   A 1 22  ? 13.419 5.607   9.874   1.00 23.03 -1 22  ASP   A OD2  1 
ATOM   363  H H    . ASP   A 1 22  ? 11.649 1.346   10.910  1.00 19.79 ?  22  ASP   A H    1 
ATOM   364  H HA   . ASP   A 1 22  ? 13.114 1.973   8.764   1.00 19.82 ?  22  ASP   A HA   1 
ATOM   365  H HB2  . ASP   A 1 22  ? 11.894 3.596   10.036  1.00 22.63 ?  22  ASP   A HB2  1 
ATOM   366  H HB3  . ASP   A 1 22  ? 12.876 3.321   11.253  1.00 22.63 ?  22  ASP   A HB3  1 
ATOM   367  N N    . ILE   A 1 23  ? 15.324 1.020   9.369   1.00 14.81 ?  23  ILE   A N    1 
ATOM   368  C CA   . ILE   A 1 23  ? 16.588 0.417   9.790   1.00 14.01 ?  23  ILE   A CA   1 
ATOM   369  C C    . ILE   A 1 23  ? 17.395 1.366   10.667  1.00 14.11 ?  23  ILE   A C    1 
ATOM   370  O O    . ILE   A 1 23  ? 18.127 0.920   11.559  1.00 14.32 ?  23  ILE   A O    1 
ATOM   371  C CB   . ILE   A 1 23  ? 17.382 -0.096  8.566   1.00 13.35 ?  23  ILE   A CB   1 
ATOM   372  C CG1  . ILE   A 1 23  ? 18.542 -0.990  9.012   1.00 13.42 ?  23  ILE   A CG1  1 
ATOM   373  C CG2  . ILE   A 1 23  ? 17.859 1.060   7.693   1.00 13.57 ?  23  ILE   A CG2  1 
ATOM   374  C CD1  . ILE   A 1 23  ? 19.266 -1.680  7.862   1.00 13.51 ?  23  ILE   A CD1  1 
ATOM   375  H H    . ILE   A 1 23  ? 15.211 1.063   8.524   1.00 17.77 ?  23  ILE   A H    1 
ATOM   376  H HA   . ILE   A 1 23  ? 16.383 -0.356  10.337  1.00 16.81 ?  23  ILE   A HA   1 
ATOM   377  H HB   . ILE   A 1 23  ? 16.780 -0.639  8.035   1.00 16.02 ?  23  ILE   A HB   1 
ATOM   378  H HG12 . ILE   A 1 23  ? 19.192 -0.450  9.487   1.00 16.10 ?  23  ILE   A HG12 1 
ATOM   379  H HG13 . ILE   A 1 23  ? 18.198 -1.682  9.600   1.00 16.10 ?  23  ILE   A HG13 1 
ATOM   380  H HG21 . ILE   A 1 23  ? 18.213 0.702   6.862   1.00 16.29 ?  23  ILE   A HG21 1 
ATOM   381  H HG22 . ILE   A 1 23  ? 17.106 1.643   7.504   1.00 16.29 ?  23  ILE   A HG22 1 
ATOM   382  H HG23 . ILE   A 1 23  ? 18.549 1.551   8.163   1.00 16.29 ?  23  ILE   A HG23 1 
ATOM   383  H HD11 . ILE   A 1 23  ? 19.927 -2.289  8.225   1.00 16.22 ?  23  ILE   A HD11 1 
ATOM   384  H HD12 . ILE   A 1 23  ? 18.618 -2.172  7.333   1.00 16.22 ?  23  ILE   A HD12 1 
ATOM   385  H HD13 . ILE   A 1 23  ? 19.698 -1.008  7.313   1.00 16.22 ?  23  ILE   A HD13 1 
ATOM   386  N N    . VAL   A 1 24  ? 17.268 2.678   10.445  1.00 15.22 ?  24  VAL   A N    1 
ATOM   387  C CA   . VAL   A 1 24  ? 17.956 3.649   11.294  1.00 16.41 ?  24  VAL   A CA   1 
ATOM   388  C C    . VAL   A 1 24  ? 17.452 3.549   12.727  1.00 16.62 ?  24  VAL   A C    1 
ATOM   389  O O    . VAL   A 1 24  ? 18.239 3.491   13.680  1.00 16.58 ?  24  VAL   A O    1 
ATOM   390  C CB   . VAL   A 1 24  ? 17.777 5.070   10.732  1.00 17.67 ?  24  VAL   A CB   1 
ATOM   391  C CG1  . VAL   A 1 24  ? 18.310 6.107   11.716  1.00 18.83 ?  24  VAL   A CG1  1 
ATOM   392  C CG2  . VAL   A 1 24  ? 18.463 5.197   9.383   1.00 18.62 ?  24  VAL   A CG2  1 
ATOM   393  H H    . VAL   A 1 24  ? 16.801 3.024   9.816   1.00 18.27 ?  24  VAL   A H    1 
ATOM   394  H HA   . VAL   A 1 24  ? 18.905 3.450   11.300  1.00 19.69 ?  24  VAL   A HA   1 
ATOM   395  H HB   . VAL   A 1 24  ? 16.832 5.241   10.601  1.00 21.20 ?  24  VAL   A HB   1 
ATOM   396  H HG11 . VAL   A 1 24  ? 18.436 6.946   11.247  1.00 22.61 ?  24  VAL   A HG11 1 
ATOM   397  H HG12 . VAL   A 1 24  ? 17.666 6.223   12.432  1.00 22.61 ?  24  VAL   A HG12 1 
ATOM   398  H HG13 . VAL   A 1 24  ? 19.156 5.796   12.073  1.00 22.61 ?  24  VAL   A HG13 1 
ATOM   399  H HG21 . VAL   A 1 24  ? 18.315 6.089   9.034   1.00 22.34 ?  24  VAL   A HG21 1 
ATOM   400  H HG22 . VAL   A 1 24  ? 19.415 5.041   9.497   1.00 22.34 ?  24  VAL   A HG22 1 
ATOM   401  H HG23 . VAL   A 1 24  ? 18.092 4.538   8.775   1.00 22.34 ?  24  VAL   A HG23 1 
ATOM   402  N N    . GLU   A 1 25  ? 16.128 3.532   12.898  1.00 17.82 ?  25  GLU   A N    1 
ATOM   403  C CA   . GLU   A 1 25  ? 15.551 3.447   14.236  1.00 19.55 ?  25  GLU   A CA   1 
ATOM   404  C C    . GLU   A 1 25  ? 15.814 2.083   14.863  1.00 18.34 ?  25  GLU   A C    1 
ATOM   405  O O    . GLU   A 1 25  ? 16.075 1.989   16.067  1.00 19.04 ?  25  GLU   A O    1 
ATOM   406  C CB   . GLU   A 1 25  ? 14.054 3.758   14.181  1.00 22.16 ?  25  GLU   A CB   1 
ATOM   407  C CG   . GLU   A 1 25  ? 13.757 5.194   13.773  1.00 25.38 ?  25  GLU   A CG   1 
ATOM   408  C CD   . GLU   A 1 25  ? 14.479 6.206   14.644  1.00 28.36 ?  25  GLU   A CD   1 
ATOM   409  O OE1  . GLU   A 1 25  ? 14.519 6.009   15.878  1.00 29.41 ?  25  GLU   A OE1  1 
ATOM   410  O OE2  . GLU   A 1 25  ? 15.025 7.184   14.093  1.00 29.62 -1 25  GLU   A OE2  1 
ATOM   411  H H    . GLU   A 1 25  ? 15.551 3.565   12.262  1.00 21.39 ?  25  GLU   A H    1 
ATOM   412  H HA   . GLU   A 1 25  ? 15.974 4.106   14.802  1.00 23.47 ?  25  GLU   A HA   1 
ATOM   413  H HB2  . GLU   A 1 25  ? 13.629 3.174   13.533  1.00 26.60 ?  25  GLU   A HB2  1 
ATOM   414  H HB3  . GLU   A 1 25  ? 13.665 3.615   15.058  1.00 26.60 ?  25  GLU   A HB3  1 
ATOM   415  H HG2  . GLU   A 1 25  ? 14.053 5.331   12.860  1.00 30.46 ?  25  GLU   A HG2  1 
ATOM   416  H HG3  . GLU   A 1 25  ? 12.800 5.352   13.840  1.00 30.46 ?  25  GLU   A HG3  1 
ATOM   417  N N    A GLU   A 1 26  ? 15.757 1.017   14.061  0.88 18.05 ?  26  GLU   A N    1 
ATOM   418  N N    B GLU   A 1 26  ? 15.766 1.019   14.058  0.12 17.97 ?  26  GLU   A N    1 
ATOM   419  C CA   A GLU   A 1 26  ? 16.076 -0.313  14.574  0.88 17.69 ?  26  GLU   A CA   1 
ATOM   420  C CA   B GLU   A 1 26  ? 16.078 -0.313  14.569  0.12 17.71 ?  26  GLU   A CA   1 
ATOM   421  C C    A GLU   A 1 26  ? 17.508 -0.365  15.090  0.88 16.32 ?  26  GLU   A C    1 
ATOM   422  C C    B GLU   A 1 26  ? 17.509 -0.376  15.082  0.12 16.54 ?  26  GLU   A C    1 
ATOM   423  O O    A GLU   A 1 26  ? 17.773 -0.891  16.176  0.88 16.34 ?  26  GLU   A O    1 
ATOM   424  O O    B GLU   A 1 26  ? 17.772 -0.912  16.165  0.12 16.64 ?  26  GLU   A O    1 
ATOM   425  C CB   A GLU   A 1 26  ? 15.887 -1.359  13.474  0.88 19.52 ?  26  GLU   A CB   1 
ATOM   426  C CB   B GLU   A 1 26  ? 15.863 -1.355  13.471  0.12 18.66 ?  26  GLU   A CB   1 
ATOM   427  C CG   A GLU   A 1 26  ? 14.486 -1.900  13.320  0.88 22.01 ?  26  GLU   A CG   1 
ATOM   428  C CG   B GLU   A 1 26  ? 14.450 -1.892  13.394  0.12 19.66 ?  26  GLU   A CG   1 
ATOM   429  C CD   A GLU   A 1 26  ? 14.017 -2.689  14.531  0.88 23.06 ?  26  GLU   A CD   1 
ATOM   430  C CD   B GLU   A 1 26  ? 14.059 -2.684  14.625  0.12 20.34 ?  26  GLU   A CD   1 
ATOM   431  O OE1  A GLU   A 1 26  ? 14.468 -3.842  14.767  0.88 23.34 ?  26  GLU   A OE1  1 
ATOM   432  O OE1  B GLU   A 1 26  ? 14.813 -3.602  15.010  0.12 20.50 ?  26  GLU   A OE1  1 
ATOM   433  O OE2  A GLU   A 1 26  ? 13.173 -2.139  15.249  0.88 24.02 -1 26  GLU   A OE2  1 
ATOM   434  O OE2  B GLU   A 1 26  ? 13.000 -2.383  15.213  0.12 20.71 -1 26  GLU   A OE2  1 
ATOM   435  H H    A GLU   A 1 26  ? 15.552 1.040   13.227  0.88 21.66 ?  26  GLU   A H    1 
ATOM   436  H H    B GLU   A 1 26  ? 15.567 1.042   13.223  0.12 21.57 ?  26  GLU   A H    1 
ATOM   437  H HA   A GLU   A 1 26  ? 15.482 -0.525  15.307  0.88 21.23 ?  26  GLU   A HA   1 
ATOM   438  H HA   B GLU   A 1 26  ? 15.485 -0.518  15.307  0.12 21.25 ?  26  GLU   A HA   1 
ATOM   439  H HB2  A GLU   A 1 26  ? 16.141 -0.961  12.626  0.88 23.43 ?  26  GLU   A HB2  1 
ATOM   440  H HB2  B GLU   A 1 26  ? 16.071 -0.952  12.612  0.12 22.40 ?  26  GLU   A HB2  1 
ATOM   441  H HB3  A GLU   A 1 26  ? 16.468 -2.112  13.664  0.88 23.43 ?  26  GLU   A HB3  1 
ATOM   442  H HB3  B GLU   A 1 26  ? 16.456 -2.105  13.630  0.12 22.40 ?  26  GLU   A HB3  1 
ATOM   443  H HG2  A GLU   A 1 26  ? 13.879 -1.151  13.184  0.88 26.41 ?  26  GLU   A HG2  1 
ATOM   444  H HG2  B GLU   A 1 26  ? 13.838 -1.148  13.307  0.12 23.60 ?  26  GLU   A HG2  1 
ATOM   445  H HG3  A GLU   A 1 26  ? 14.456 -2.490  12.555  0.88 26.41 ?  26  GLU   A HG3  1 
ATOM   446  H HG3  B GLU   A 1 26  ? 14.379 -2.479  12.626  0.12 23.60 ?  26  GLU   A HG3  1 
ATOM   447  N N    . ALA   A 1 27  ? 18.451 0.168   14.312  1.00 15.29 ?  27  ALA   A N    1 
ATOM   448  C CA   . ALA   A 1 27  ? 19.848 0.133   14.727  1.00 14.85 ?  27  ALA   A CA   1 
ATOM   449  C C    . ALA   A 1 27  ? 20.061 0.934   16.006  1.00 16.21 ?  27  ALA   A C    1 
ATOM   450  O O    . ALA   A 1 27  ? 20.746 0.479   16.928  1.00 16.39 ?  27  ALA   A O    1 
ATOM   451  C CB   . ALA   A 1 27  ? 20.741 0.658   13.603  1.00 14.21 ?  27  ALA   A CB   1 
ATOM   452  H H    A ALA   A 1 27  ? 18.310 0.549   13.555  0.88 18.35 ?  27  ALA   A H    1 
ATOM   453  H H    B ALA   A 1 27  ? 18.309 0.562   13.561  0.12 18.35 ?  27  ALA   A H    1 
ATOM   454  H HA   . ALA   A 1 27  ? 20.102 -0.784  14.906  1.00 17.82 ?  27  ALA   A HA   1 
ATOM   455  H HB1  . ALA   A 1 27  ? 21.669 0.629   13.895  1.00 17.06 ?  27  ALA   A HB1  1 
ATOM   456  H HB2  . ALA   A 1 27  ? 20.627 0.097   12.820  1.00 17.06 ?  27  ALA   A HB2  1 
ATOM   457  H HB3  . ALA   A 1 27  ? 20.492 1.571   13.396  1.00 17.06 ?  27  ALA   A HB3  1 
ATOM   458  N N    . LYS   A 1 28  ? 19.469 2.128   16.087  1.00 18.48 ?  28  LYS   A N    1 
ATOM   459  C CA   . LYS   A 1 28  ? 19.629 2.945   17.287  1.00 21.67 ?  28  LYS   A CA   1 
ATOM   460  C C    . LYS   A 1 28  ? 19.090 2.241   18.525  1.00 22.30 ?  28  LYS   A C    1 
ATOM   461  O O    . LYS   A 1 28  ? 19.657 2.384   19.614  1.00 23.88 ?  28  LYS   A O    1 
ATOM   462  C CB   . LYS   A 1 28  ? 18.963 4.310   17.098  1.00 24.10 ?  28  LYS   A CB   1 
ATOM   463  C CG   . LYS   A 1 28  ? 19.753 5.244   16.193  1.00 26.40 ?  28  LYS   A CG   1 
ATOM   464  C CD   . LYS   A 1 28  ? 19.271 6.681   16.283  1.00 29.14 ?  28  LYS   A CD   1 
ATOM   465  C CE   . LYS   A 1 28  ? 17.922 6.861   15.615  1.00 31.14 ?  28  LYS   A CE   1 
ATOM   466  N NZ   . LYS   A 1 28  ? 17.532 8.298   15.553  1.00 32.38 ?  28  LYS   A NZ   1 
ATOM   467  H H    . LYS   A 1 28  ? 18.982 2.478   15.476  1.00 22.18 ?  28  LYS   A H    1 
ATOM   468  H HA   . LYS   A 1 28  ? 20.572 3.101   17.436  1.00 26.01 ?  28  LYS   A HA   1 
ATOM   469  H HB2  . LYS   A 1 28  ? 18.088 4.183   16.702  1.00 28.92 ?  28  LYS   A HB2  1 
ATOM   470  H HB3  . LYS   A 1 28  ? 18.875 4.742   17.963  1.00 28.92 ?  28  LYS   A HB3  1 
ATOM   471  H HG2  . LYS   A 1 28  ? 20.687 5.223   16.453  1.00 31.68 ?  28  LYS   A HG2  1 
ATOM   472  H HG3  . LYS   A 1 28  ? 19.656 4.951   15.274  1.00 31.68 ?  28  LYS   A HG3  1 
ATOM   473  H HD2  . LYS   A 1 28  ? 19.184 6.933   17.216  1.00 34.97 ?  28  LYS   A HD2  1 
ATOM   474  H HD3  . LYS   A 1 28  ? 19.909 7.261   15.838  1.00 34.97 ?  28  LYS   A HD3  1 
ATOM   475  H HE2  . LYS   A 1 28  ? 17.965 6.518   14.709  1.00 37.37 ?  28  LYS   A HE2  1 
ATOM   476  H HE3  . LYS   A 1 28  ? 17.247 6.385   16.123  1.00 37.37 ?  28  LYS   A HE3  1 
ATOM   477  H HZ1  . LYS   A 1 28  ? 16.740 8.381   15.158  1.00 38.86 ?  28  LYS   A HZ1  1 
ATOM   478  H HZ2  . LYS   A 1 28  ? 17.484 8.635   16.375  1.00 38.86 ?  28  LYS   A HZ2  1 
ATOM   479  H HZ3  . LYS   A 1 28  ? 18.137 8.757   15.088  1.00 38.86 ?  28  LYS   A HZ3  1 
ATOM   480  N N    . LYS   A 1 29  ? 18.012 1.470   18.380  1.00 22.54 ?  29  LYS   A N    1 
ATOM   481  C CA   . LYS   A 1 29  ? 17.425 0.773   19.521  1.00 24.30 ?  29  LYS   A CA   1 
ATOM   482  C C    . LYS   A 1 29  ? 18.234 -0.463  19.898  1.00 22.79 ?  29  LYS   A C    1 
ATOM   483  O O    . LYS   A 1 29  ? 18.536 -0.686  21.076  1.00 23.67 ?  29  LYS   A O    1 
ATOM   484  C CB   . LYS   A 1 29  ? 15.987 0.370   19.186  1.00 27.43 ?  29  LYS   A CB   1 
ATOM   485  C CG   . LYS   A 1 29  ? 15.243 -0.303  20.327  1.00 30.94 ?  29  LYS   A CG   1 
ATOM   486  C CD   . LYS   A 1 29  ? 14.874 0.699   21.405  1.00 34.12 ?  29  LYS   A CD   1 
ATOM   487  C CE   . LYS   A 1 29  ? 13.996 0.069   22.471  1.00 36.26 ?  29  LYS   A CE   1 
ATOM   488  N NZ   . LYS   A 1 29  ? 13.545 1.069   23.477  1.00 37.55 ?  29  LYS   A NZ   1 
ATOM   489  H H    . LYS   A 1 29  ? 17.602 1.338   17.635  1.00 27.05 ?  29  LYS   A H    1 
ATOM   490  H HA   . LYS   A 1 29  ? 17.403 1.367   20.285  1.00 29.16 ?  29  LYS   A HA   1 
ATOM   491  H HB2  . LYS   A 1 29  ? 15.489 1.165   18.942  1.00 32.92 ?  29  LYS   A HB2  1 
ATOM   492  H HB3  . LYS   A 1 29  ? 16.002 -0.249  18.440  1.00 32.92 ?  29  LYS   A HB3  1 
ATOM   493  H HG2  . LYS   A 1 29  ? 14.425 -0.697  19.986  1.00 37.13 ?  29  LYS   A HG2  1 
ATOM   494  H HG3  . LYS   A 1 29  ? 15.802 -0.990  20.726  1.00 37.13 ?  29  LYS   A HG3  1 
ATOM   495  H HD2  . LYS   A 1 29  ? 15.683 1.026   21.830  1.00 40.95 ?  29  LYS   A HD2  1 
ATOM   496  H HD3  . LYS   A 1 29  ? 14.386 1.435   21.003  1.00 40.95 ?  29  LYS   A HD3  1 
ATOM   497  H HE2  . LYS   A 1 29  ? 13.210 -0.316  22.051  1.00 43.51 ?  29  LYS   A HE2  1 
ATOM   498  H HE3  . LYS   A 1 29  ? 14.499 -0.620  22.933  1.00 43.51 ?  29  LYS   A HE3  1 
ATOM   499  H HZ1  . LYS   A 1 29  ? 13.033 0.675   24.089  1.00 45.07 ?  29  LYS   A HZ1  1 
ATOM   500  H HZ2  . LYS   A 1 29  ? 14.250 1.434   23.879  1.00 45.07 ?  29  LYS   A HZ2  1 
ATOM   501  H HZ3  . LYS   A 1 29  ? 13.076 1.711   23.076  1.00 45.07 ?  29  LYS   A HZ3  1 
ATOM   502  N N    . VAL   A 1 30  ? 18.581 -1.282  18.906  1.00 21.19 ?  30  VAL   A N    1 
ATOM   503  C CA   . VAL   A 1 30  ? 19.211 -2.569  19.173  1.00 20.33 ?  30  VAL   A CA   1 
ATOM   504  C C    . VAL   A 1 30  ? 20.719 -2.430  19.389  1.00 19.09 ?  30  VAL   A C    1 
ATOM   505  O O    . VAL   A 1 30  ? 21.301 -3.149  20.207  1.00 19.45 ?  30  VAL   A O    1 
ATOM   506  C CB   . VAL   A 1 30  ? 18.875 -3.531  18.019  1.00 21.05 ?  30  VAL   A CB   1 
ATOM   507  C CG1  . VAL   A 1 30  ? 19.611 -4.847  18.176  1.00 21.50 ?  30  VAL   A CG1  1 
ATOM   508  C CG2  . VAL   A 1 30  ? 17.369 -3.765  17.943  1.00 21.74 ?  30  VAL   A CG2  1 
ATOM   509  H H    . VAL   A 1 30  ? 18.450 -1.121  18.069  1.00 25.44 ?  30  VAL   A H    1 
ATOM   510  H HA   . VAL   A 1 30  ? 18.824 -2.940  19.979  1.00 24.40 ?  30  VAL   A HA   1 
ATOM   511  H HB   . VAL   A 1 30  ? 19.154 -3.131  17.180  1.00 25.26 ?  30  VAL   A HB   1 
ATOM   512  H HG11 . VAL   A 1 30  ? 19.242 -5.488  17.548  1.00 25.81 ?  30  VAL   A HG11 1 
ATOM   513  H HG12 . VAL   A 1 30  ? 20.551 -4.707  17.991  1.00 25.81 ?  30  VAL   A HG12 1 
ATOM   514  H HG13 . VAL   A 1 30  ? 19.489 -5.166  19.082  1.00 25.81 ?  30  VAL   A HG13 1 
ATOM   515  H HG21 . VAL   A 1 30  ? 17.185 -4.417  17.248  1.00 26.09 ?  30  VAL   A HG21 1 
ATOM   516  H HG22 . VAL   A 1 30  ? 17.059 -4.098  18.799  1.00 26.09 ?  30  VAL   A HG22 1 
ATOM   517  H HG23 . VAL   A 1 30  ? 16.929 -2.926  17.733  1.00 26.09 ?  30  VAL   A HG23 1 
ATOM   518  N N    . LYS   A 1 31  ? 21.369 -1.509  18.689  1.00 17.75 ?  31  LYS   A N    1 
ATOM   519  C CA   . LYS   A 1 31  ? 22.825 -1.421  18.649  1.00 18.23 ?  31  LYS   A CA   1 
ATOM   520  C C    . LYS   A 1 31  ? 23.429 -2.778  18.277  1.00 16.65 ?  31  LYS   A C    1 
ATOM   521  O O    . LYS   A 1 31  ? 24.220 -3.345  19.036  1.00 17.83 ?  31  LYS   A O    1 
ATOM   522  C CB   . LYS   A 1 31  ? 23.405 -0.903  19.958  1.00 23.10 ?  31  LYS   A CB   1 
ATOM   523  C CG   . LYS   A 1 31  ? 22.749 0.377   20.454  1.00 29.30 ?  31  LYS   A CG   1 
ATOM   524  C CD   . LYS   A 1 31  ? 23.782 1.412   20.873  1.00 33.79 ?  31  LYS   A CD   1 
ATOM   525  C CE   . LYS   A 1 31  ? 23.158 2.507   21.727  1.00 36.72 ?  31  LYS   A CE   1 
ATOM   526  N NZ   . LYS   A 1 31  ? 22.029 3.197   21.044  1.00 38.48 ?  31  LYS   A NZ   1 
ATOM   527  H H    . LYS   A 1 31  ? 20.975 -0.903  18.226  1.00 21.30 ?  31  LYS   A H    1 
ATOM   528  H HA   . LYS   A 1 31  ? 23.067 -0.796  17.956  1.00 21.87 ?  31  LYS   A HA   1 
ATOM   529  H HB2  . LYS   A 1 31  ? 23.295 -1.581  20.641  1.00 27.73 ?  31  LYS   A HB2  1 
ATOM   530  H HB3  . LYS   A 1 31  ? 24.350 -0.721  19.826  1.00 27.73 ?  31  LYS   A HB3  1 
ATOM   531  H HG2  . LYS   A 1 31  ? 22.211 0.757   19.741  1.00 35.17 ?  31  LYS   A HG2  1 
ATOM   532  H HG3  . LYS   A 1 31  ? 22.193 0.174   21.222  1.00 35.17 ?  31  LYS   A HG3  1 
ATOM   533  H HD2  . LYS   A 1 31  ? 24.477 0.979   21.393  1.00 40.55 ?  31  LYS   A HD2  1 
ATOM   534  H HD3  . LYS   A 1 31  ? 24.162 1.824   20.080  1.00 40.55 ?  31  LYS   A HD3  1 
ATOM   535  H HE2  . LYS   A 1 31  ? 22.818 2.114   22.546  1.00 44.07 ?  31  LYS   A HE2  1 
ATOM   536  H HE3  . LYS   A 1 31  ? 23.834 3.171   21.933  1.00 44.07 ?  31  LYS   A HE3  1 
ATOM   537  H HZ1  . LYS   A 1 31  ? 21.700 3.836   21.570  1.00 46.17 ?  31  LYS   A HZ1  1 
ATOM   538  H HZ2  . LYS   A 1 31  ? 22.311 3.564   20.284  1.00 46.17 ?  31  LYS   A HZ2  1 
ATOM   539  H HZ3  . LYS   A 1 31  ? 21.382 2.613   20.860  1.00 46.17 ?  31  LYS   A HZ3  1 
ATOM   540  N N    . PRO   A 1 32  ? 23.067 -3.320  17.120  1.00 14.72 ?  32  PRO   A N    1 
ATOM   541  C CA   . PRO   A 1 32  ? 23.544 -4.652  16.750  1.00 14.94 ?  32  PRO   A CA   1 
ATOM   542  C C    . PRO   A 1 32  ? 25.045 -4.656  16.534  1.00 14.66 ?  32  PRO   A C    1 
ATOM   543  O O    . PRO   A 1 32  ? 25.677 -3.621  16.308  1.00 14.76 ?  32  PRO   A O    1 
ATOM   544  C CB   . PRO   A 1 32  ? 22.806 -4.932  15.437  1.00 15.39 ?  32  PRO   A CB   1 
ATOM   545  C CG   . PRO   A 1 32  ? 22.596 -3.570  14.847  1.00 14.16 ?  32  PRO   A CG   1 
ATOM   546  C CD   . PRO   A 1 32  ? 22.317 -2.683  16.026  1.00 14.09 ?  32  PRO   A CD   1 
ATOM   547  H HA   . PRO   A 1 32  ? 23.304 -5.311  17.416  1.00 17.93 ?  32  PRO   A HA   1 
ATOM   548  H HB2  . PRO   A 1 32  ? 23.356 -5.484  14.853  1.00 18.47 ?  32  PRO   A HB2  1 
ATOM   549  H HB3  . PRO   A 1 32  ? 21.957 -5.369  15.620  1.00 18.47 ?  32  PRO   A HB3  1 
ATOM   550  H HG2  . PRO   A 1 32  ? 23.396 -3.295  14.379  1.00 16.99 ?  32  PRO   A HG2  1 
ATOM   551  H HG3  . PRO   A 1 32  ? 21.834 -3.597  14.242  1.00 16.99 ?  32  PRO   A HG3  1 
ATOM   552  H HD2  . PRO   A 1 32  ? 22.657 -1.792  15.849  1.00 16.91 ?  32  PRO   A HD2  1 
ATOM   553  H HD3  . PRO   A 1 32  ? 21.370 -2.675  16.221  1.00 16.91 ?  32  PRO   A HD3  1 
ATOM   554  N N    . THR   A 1 33  ? 25.614 -5.859  16.584  1.00 14.78 ?  33  THR   A N    1 
ATOM   555  C CA   . THR   A 1 33  ? 27.024 -6.011  16.252  1.00 14.97 ?  33  THR   A CA   1 
ATOM   556  C C    . THR   A 1 33  ? 27.302 -5.552  14.828  1.00 13.33 ?  33  THR   A C    1 
ATOM   557  O O    . THR   A 1 33  ? 28.330 -4.910  14.567  1.00 13.52 ?  33  THR   A O    1 
ATOM   558  C CB   . THR   A 1 33  ? 27.447 -7.465  16.459  1.00 16.69 ?  33  THR   A CB   1 
ATOM   559  O OG1  . THR   A 1 33  ? 27.218 -7.823  17.825  1.00 18.42 ?  33  THR   A OG1  1 
ATOM   560  C CG2  . THR   A 1 33  ? 28.924 -7.659  16.128  1.00 17.86 ?  33  THR   A CG2  1 
ATOM   561  H H    . THR   A 1 33  ? 25.215 -6.591  16.796  1.00 17.74 ?  33  THR   A H    1 
ATOM   562  H HA   . THR   A 1 33  ? 27.553 -5.464  16.849  1.00 17.97 ?  33  THR   A HA   1 
ATOM   563  H HB   . THR   A 1 33  ? 26.929 -8.051  15.884  1.00 20.03 ?  33  THR   A HB   1 
ATOM   564  H HG1  . THR   A 1 33  ? 27.712 -7.356  18.331  1.00 22.11 ?  33  THR   A HG1  1 
ATOM   565  H HG21 . THR   A 1 33  ? 29.224 -8.530  16.432  1.00 21.43 ?  33  THR   A HG21 1 
ATOM   566  H HG22 . THR   A 1 33  ? 29.062 -7.598  15.169  1.00 21.43 ?  33  THR   A HG22 1 
ATOM   567  H HG23 . THR   A 1 33  ? 29.453 -6.975  16.567  1.00 21.43 ?  33  THR   A HG23 1 
ATOM   568  N N    . VAL   A 1 34  ? 26.394 -5.856  13.898  1.00 12.08 ?  34  VAL   A N    1 
ATOM   569  C CA   . VAL   A 1 34  ? 26.566 -5.510  12.489  1.00 11.00 ?  34  VAL   A CA   1 
ATOM   570  C C    . VAL   A 1 34  ? 25.259 -4.950  11.943  1.00 10.62 ?  34  VAL   A C    1 
ATOM   571  O O    . VAL   A 1 34  ? 24.217 -5.617  12.007  1.00 11.25 ?  34  VAL   A O    1 
ATOM   572  C CB   . VAL   A 1 34  ? 27.007 -6.715  11.637  1.00 11.79 ?  34  VAL   A CB   1 
ATOM   573  C CG1  . VAL   A 1 34  ? 27.176 -6.297  10.181  1.00 12.02 ?  34  VAL   A CG1  1 
ATOM   574  C CG2  . VAL   A 1 34  ? 28.301 -7.327  12.174  1.00 12.90 ?  34  VAL   A CG2  1 
ATOM   575  H H    . VAL   A 1 34  ? 25.658 -6.273  14.062  1.00 14.50 ?  34  VAL   A H    1 
ATOM   576  H HA   . VAL   A 1 34  ? 27.243 -4.820  12.410  1.00 13.20 ?  34  VAL   A HA   1 
ATOM   577  H HB   . VAL   A 1 34  ? 26.317 -7.393  11.671  1.00 14.15 ?  34  VAL   A HB   1 
ATOM   578  H HG11 . VAL   A 1 34  ? 27.664 -6.991  9.709   1.00 14.42 ?  34  VAL   A HG11 1 
ATOM   579  H HG12 . VAL   A 1 34  ? 26.305 -6.173  9.778   1.00 14.42 ?  34  VAL   A HG12 1 
ATOM   580  H HG13 . VAL   A 1 34  ? 27.680 -5.465  10.147  1.00 14.42 ?  34  VAL   A HG13 1 
ATOM   581  H HG21 . VAL   A 1 34  ? 28.581 -8.046  11.583  1.00 15.48 ?  34  VAL   A HG21 1 
ATOM   582  H HG22 . VAL   A 1 34  ? 28.989 -6.643  12.207  1.00 15.48 ?  34  VAL   A HG22 1 
ATOM   583  H HG23 . VAL   A 1 34  ? 28.142 -7.678  13.064  1.00 15.48 ?  34  VAL   A HG23 1 
ATOM   584  N N    . VAL   A 1 35  ? 25.318 -3.741  11.381  1.00 10.07 ?  35  VAL   A N    1 
ATOM   585  C CA   . VAL   A 1 35  ? 24.274 -3.227  10.504  1.00 9.59  ?  35  VAL   A CA   1 
ATOM   586  C C    . VAL   A 1 35  ? 24.821 -3.220  9.086   1.00 9.01  ?  35  VAL   A C    1 
ATOM   587  O O    . VAL   A 1 35  ? 25.963 -2.807  8.852   1.00 9.83  ?  35  VAL   A O    1 
ATOM   588  C CB   . VAL   A 1 35  ? 23.744 -1.837  10.926  1.00 10.34 ?  35  VAL   A CB   1 
ATOM   589  C CG1  . VAL   A 1 35  ? 24.810 -0.739  10.788  1.00 11.00 ?  35  VAL   A CG1  1 
ATOM   590  C CG2  . VAL   A 1 35  ? 22.494 -1.478  10.120  1.00 11.04 ?  35  VAL   A CG2  1 
ATOM   591  H H    . VAL   A 1 35  ? 25.965 -3.187  11.494  1.00 12.09 ?  35  VAL   A H    1 
ATOM   592  H HA   . VAL   A 1 35  ? 23.517 -3.840  10.527  1.00 11.51 ?  35  VAL   A HA   1 
ATOM   593  H HB   . VAL   A 1 35  ? 23.479 -1.872  11.857  1.00 12.41 ?  35  VAL   A HB   1 
ATOM   594  H HG11 . VAL   A 1 35  ? 24.469 0.089   11.168  1.00 13.21 ?  35  VAL   A HG11 1 
ATOM   595  H HG12 . VAL   A 1 35  ? 25.609 -1.013  11.266  1.00 13.21 ?  35  VAL   A HG12 1 
ATOM   596  H HG13 . VAL   A 1 35  ? 25.018 -0.606  9.849   1.00 13.21 ?  35  VAL   A HG13 1 
ATOM   597  H HG21 . VAL   A 1 35  ? 22.143 -0.630  10.432  1.00 13.25 ?  35  VAL   A HG21 1 
ATOM   598  H HG22 . VAL   A 1 35  ? 22.731 -1.408  9.178   1.00 13.25 ?  35  VAL   A HG22 1 
ATOM   599  H HG23 . VAL   A 1 35  ? 21.828 -2.175  10.239  1.00 13.25 ?  35  VAL   A HG23 1 
ATOM   600  N N    . VAL   A 1 36  ? 24.001 -3.666  8.140   1.00 8.64  ?  36  VAL   A N    1 
ATOM   601  C CA   . VAL   A 1 36  ? 24.371 -3.671  6.733   1.00 8.49  ?  36  VAL   A CA   1 
ATOM   602  C C    . VAL   A 1 36  ? 23.909 -2.376  6.081   1.00 8.60  ?  36  VAL   A C    1 
ATOM   603  O O    . VAL   A 1 36  ? 22.751 -1.962  6.237   1.00 9.41  ?  36  VAL   A O    1 
ATOM   604  C CB   . VAL   A 1 36  ? 23.760 -4.883  6.010   1.00 8.74  ?  36  VAL   A CB   1 
ATOM   605  C CG1  . VAL   A 1 36  ? 24.012 -4.801  4.524   1.00 9.17  ?  36  VAL   A CG1  1 
ATOM   606  C CG2  . VAL   A 1 36  ? 24.301 -6.182  6.581   1.00 9.50  ?  36  VAL   A CG2  1 
ATOM   607  H H    . VAL   A 1 36  ? 23.209 -3.983  8.289   1.00 10.37 ?  36  VAL   A H    1 
ATOM   608  H HA   . VAL   A 1 36  ? 25.343 -3.734  6.659   1.00 10.19 ?  36  VAL   A HA   1 
ATOM   609  H HB   . VAL   A 1 36  ? 22.804 -4.876  6.151   1.00 10.49 ?  36  VAL   A HB   1 
ATOM   610  H HG11 . VAL   A 1 36  ? 23.870 -5.676  4.130   1.00 11.01 ?  36  VAL   A HG11 1 
ATOM   611  H HG12 . VAL   A 1 36  ? 23.394 -4.162  4.131   1.00 11.01 ?  36  VAL   A HG12 1 
ATOM   612  H HG13 . VAL   A 1 36  ? 24.926 -4.515  4.370   1.00 11.01 ?  36  VAL   A HG13 1 
ATOM   613  H HG21 . VAL   A 1 36  ? 23.907 -6.933  6.102   1.00 11.41 ?  36  VAL   A HG21 1 
ATOM   614  H HG22 . VAL   A 1 36  ? 25.267 -6.204  6.479   1.00 11.41 ?  36  VAL   A HG22 1 
ATOM   615  H HG23 . VAL   A 1 36  ? 24.070 -6.243  7.523   1.00 11.41 ?  36  VAL   A HG23 1 
ATOM   616  N N    . ASN   A 1 37  ? 24.813 -1.752  5.328   1.00 8.34  ?  37  ASN   A N    1 
ATOM   617  C CA   . ASN   A 1 37  ? 24.476 -0.621  4.481   1.00 8.25  ?  37  ASN   A CA   1 
ATOM   618  C C    . ASN   A 1 37  ? 24.330 -1.076  3.036   1.00 8.27  ?  37  ASN   A C    1 
ATOM   619  O O    . ASN   A 1 37  ? 25.104 -1.909  2.546   1.00 8.88  ?  37  ASN   A O    1 
ATOM   620  C CB   . ASN   A 1 37  ? 25.554 0.453   4.566   1.00 8.71  ?  37  ASN   A CB   1 
ATOM   621  C CG   . ASN   A 1 37  ? 25.229 1.663   3.726   1.00 8.99  ?  37  ASN   A CG   1 
ATOM   622  O OD1  . ASN   A 1 37  ? 24.057 2.015   3.563   1.00 9.51  ?  37  ASN   A OD1  1 
ATOM   623  N ND2  . ASN   A 1 37  ? 26.257 2.311   3.191   1.00 9.16  ?  37  ASN   A ND2  1 
ATOM   624  H H    . ASN   A 1 37  ? 25.648 -1.970  5.298   1.00 10.01 ?  37  ASN   A H    1 
ATOM   625  H HA   . ASN   A 1 37  ? 23.638 -0.235  4.778   1.00 9.91  ?  37  ASN   A HA   1 
ATOM   626  H HB2  . ASN   A 1 37  ? 25.644 0.747   5.488   1.00 10.46 ?  37  ASN   A HB2  1 
ATOM   627  H HB3  . ASN   A 1 37  ? 26.399 0.085   4.255   1.00 10.46 ?  37  ASN   A HB3  1 
ATOM   628  H HD21 . ASN   A 1 37  ? 26.117 3.003   2.697   1.00 10.99 ?  37  ASN   A HD21 1 
ATOM   629  H HD22 . ASN   A 1 37  ? 27.056 2.040   3.323   1.00 10.99 ?  37  ASN   A HD22 1 
ATOM   630  N N    . ALA   A 1 38  ? 23.323 -0.511  2.365   1.00 8.83  ?  38  ALA   A N    1 
ATOM   631  C CA   . ALA   A 1 38  ? 23.114 -0.660  0.926   1.00 9.09  ?  38  ALA   A CA   1 
ATOM   632  C C    . ALA   A 1 38  ? 24.028 0.326   0.202   1.00 8.94  ?  38  ALA   A C    1 
ATOM   633  O O    . ALA   A 1 38  ? 23.618 1.409   -0.227  1.00 9.58  ?  38  ALA   A O    1 
ATOM   634  C CB   . ALA   A 1 38  ? 21.651 -0.398  0.589   1.00 10.51 ?  38  ALA   A CB   1 
ATOM   635  H H    . ALA   A 1 38  ? 22.730 -0.016  2.742   1.00 10.59 ?  38  ALA   A H    1 
ATOM   636  H HA   . ALA   A 1 38  ? 23.341 -1.564  0.651   1.00 10.91 ?  38  ALA   A HA   1 
ATOM   637  H HB1  . ALA   A 1 38  ? 21.521 -0.506  -0.366  1.00 12.61 ?  38  ALA   A HB1  1 
ATOM   638  H HB2  . ALA   A 1 38  ? 21.096 -1.035  1.071   1.00 12.61 ?  38  ALA   A HB2  1 
ATOM   639  H HB3  . ALA   A 1 38  ? 21.422 0.505   0.856   1.00 12.61 ?  38  ALA   A HB3  1 
ATOM   640  N N    . ALA   A 1 39  ? 25.295 -0.061  0.069   1.00 9.19  ?  39  ALA   A N    1 
ATOM   641  C CA   . ALA   A 1 39  ? 26.345 0.816   -0.419  1.00 9.03  ?  39  ALA   A CA   1 
ATOM   642  C C    . ALA   A 1 39  ? 26.464 0.759   -1.937  1.00 8.97  ?  39  ALA   A C    1 
ATOM   643  O O    . ALA   A 1 39  ? 25.981 -0.162  -2.597  1.00 9.39  ?  39  ALA   A O    1 
ATOM   644  C CB   . ALA   A 1 39  ? 27.678 0.411   0.211   1.00 10.26 ?  39  ALA   A CB   1 
ATOM   645  H H    . ALA   A 1 39  ? 25.575 -0.859  0.261   1.00 11.03 ?  39  ALA   A H    1 
ATOM   646  H HA   . ALA   A 1 39  ? 26.139 1.728   -0.160  1.00 10.83 ?  39  ALA   A HA   1 
ATOM   647  H HB1  . ALA   A 1 39  ? 28.369 1.006   -0.118  1.00 12.32 ?  39  ALA   A HB1  1 
ATOM   648  H HB2  . ALA   A 1 39  ? 27.603 0.493   1.176   1.00 12.32 ?  39  ALA   A HB2  1 
ATOM   649  H HB3  . ALA   A 1 39  ? 27.876 -0.502  -0.032  1.00 12.32 ?  39  ALA   A HB3  1 
ATOM   650  N N    . ASN   A 1 40  ? 27.138 1.767   -2.489  1.00 9.28  ?  40  ASN   A N    1 
ATOM   651  C CA   . ASN   A 1 40  ? 27.654 1.719   -3.851  1.00 9.81  ?  40  ASN   A CA   1 
ATOM   652  C C    . ASN   A 1 40  ? 29.181 1.612   -3.813  1.00 9.26  ?  40  ASN   A C    1 
ATOM   653  O O    . ASN   A 1 40  ? 29.800 1.708   -2.752  1.00 9.34  ?  40  ASN   A O    1 
ATOM   654  C CB   . ASN   A 1 40  ? 27.158 2.908   -4.692  1.00 10.34 ?  40  ASN   A CB   1 
ATOM   655  C CG   . ASN   A 1 40  ? 27.544 4.255   -4.110  1.00 11.29 ?  40  ASN   A CG   1 
ATOM   656  O OD1  . ASN   A 1 40  ? 28.718 4.510   -3.822  1.00 12.64 ?  40  ASN   A OD1  1 
ATOM   657  N ND2  . ASN   A 1 40  ? 26.553 5.132   -3.948  1.00 12.17 ?  40  ASN   A ND2  1 
ATOM   658  H H    . ASN   A 1 40  ? 27.316 2.503   -2.087  1.00 11.14 ?  40  ASN   A H    1 
ATOM   659  H HA   . ASN   A 1 40  ? 27.319 0.914   -4.278  1.00 11.77 ?  40  ASN   A HA   1 
ATOM   660  H HB2  . ASN   A 1 40  ? 27.534 2.840   -5.587  1.00 12.41 ?  40  ASN   A HB2  1 
ATOM   661  H HB3  . ASN   A 1 40  ? 26.188 2.872   -4.747  1.00 12.41 ?  40  ASN   A HB3  1 
ATOM   662  H HD21 . ASN   A 1 40  ? 26.723 5.916   -3.633  1.00 14.61 ?  40  ASN   A HD21 1 
ATOM   663  H HD22 . ASN   A 1 40  ? 25.749 4.922   -4.164  1.00 14.61 ?  40  ASN   A HD22 1 
ATOM   664  N N    . VAL   A 1 41  ? 29.788 1.378   -4.980  1.00 9.65  ?  41  VAL   A N    1 
ATOM   665  C CA   . VAL   A 1 41  ? 31.218 1.068   -5.019  1.00 10.25 ?  41  VAL   A CA   1 
ATOM   666  C C    . VAL   A 1 41  ? 32.079 2.218   -4.541  1.00 10.42 ?  41  VAL   A C    1 
ATOM   667  O O    . VAL   A 1 41  ? 33.226 1.994   -4.135  1.00 10.77 ?  41  VAL   A O    1 
ATOM   668  C CB   . VAL   A 1 41  ? 31.688 0.587   -6.410  1.00 11.44 ?  41  VAL   A CB   1 
ATOM   669  C CG1  . VAL   A 1 41  ? 31.000 -0.714  -6.792  1.00 12.04 ?  41  VAL   A CG1  1 
ATOM   670  C CG2  . VAL   A 1 41  ? 31.491 1.659   -7.482  1.00 12.34 ?  41  VAL   A CG2  1 
ATOM   671  H H    . VAL   A 1 41  ? 29.397 1.381   -5.750  1.00 11.58 ?  41  VAL   A H    1 
ATOM   672  H HA   . VAL   A 1 41  ? 31.375 0.333   -4.406  1.00 12.30 ?  41  VAL   A HA   1 
ATOM   673  H HB   . VAL   A 1 41  ? 32.638 0.396   -6.361  1.00 13.73 ?  41  VAL   A HB   1 
ATOM   674  H HG11 . VAL   A 1 41  ? 31.335 -1.017  -7.650  1.00 14.45 ?  41  VAL   A HG11 1 
ATOM   675  H HG12 . VAL   A 1 41  ? 31.185 -1.387  -6.112  1.00 14.45 ?  41  VAL   A HG12 1 
ATOM   676  H HG13 . VAL   A 1 41  ? 30.041 -0.565  -6.847  1.00 14.45 ?  41  VAL   A HG13 1 
ATOM   677  H HG21 . VAL   A 1 41  ? 31.731 1.287   -8.346  1.00 14.81 ?  41  VAL   A HG21 1 
ATOM   678  H HG22 . VAL   A 1 41  ? 30.562 1.932   -7.487  1.00 14.81 ?  41  VAL   A HG22 1 
ATOM   679  H HG23 . VAL   A 1 41  ? 32.061 2.414   -7.277  1.00 14.81 ?  41  VAL   A HG23 1 
ATOM   680  N N    . TYR   A 1 42  ? 31.572 3.450   -4.612  1.00 10.23 ?  42  TYR   A N    1 
ATOM   681  C CA   . TYR   A 1 42  ? 32.310 4.635   -4.193  1.00 10.11 ?  42  TYR   A CA   1 
ATOM   682  C C    . TYR   A 1 42  ? 32.056 5.004   -2.742  1.00 9.99  ?  42  TYR   A C    1 
ATOM   683  O O    . TYR   A 1 42  ? 32.623 5.991   -2.255  1.00 10.56 ?  42  TYR   A O    1 
ATOM   684  C CB   . TYR   A 1 42  ? 31.963 5.826   -5.105  1.00 11.09 ?  42  TYR   A CB   1 
ATOM   685  C CG   . TYR   A 1 42  ? 32.149 5.521   -6.577  1.00 12.28 ?  42  TYR   A CG   1 
ATOM   686  C CD1  . TYR   A 1 42  ? 33.412 5.321   -7.112  1.00 12.91 ?  42  TYR   A CD1  1 
ATOM   687  C CD2  . TYR   A 1 42  ? 31.059 5.404   -7.425  1.00 13.62 ?  42  TYR   A CD2  1 
ATOM   688  C CE1  . TYR   A 1 42  ? 33.583 5.020   -8.455  1.00 13.33 ?  42  TYR   A CE1  1 
ATOM   689  C CE2  . TYR   A 1 42  ? 31.221 5.111   -8.768  1.00 14.66 ?  42  TYR   A CE2  1 
ATOM   690  C CZ   . TYR   A 1 42  ? 32.484 4.919   -9.278  1.00 14.29 ?  42  TYR   A CZ   1 
ATOM   691  O OH   . TYR   A 1 42  ? 32.645 4.624   -10.615 1.00 15.97 ?  42  TYR   A OH   1 
ATOM   692  H H    . TYR   A 1 42  ? 30.784 3.626   -4.919  1.00 12.28 ?  42  TYR   A H    1 
ATOM   693  H HA   . TYR   A 1 42  ? 33.257 4.463   -4.293  1.00 12.14 ?  42  TYR   A HA   1 
ATOM   694  H HB2  . TYR   A 1 42  ? 31.036 6.075   -4.969  1.00 13.31 ?  42  TYR   A HB2  1 
ATOM   695  H HB3  . TYR   A 1 42  ? 32.542 6.575   -4.883  1.00 13.31 ?  42  TYR   A HB3  1 
ATOM   696  H HD1  . TYR   A 1 42  ? 34.158 5.381   -6.560  1.00 15.50 ?  42  TYR   A HD1  1 
ATOM   697  H HD2  . TYR   A 1 42  ? 30.202 5.537   -7.089  1.00 16.34 ?  42  TYR   A HD2  1 
ATOM   698  H HE1  . TYR   A 1 42  ? 34.438 4.888   -8.801  1.00 16.00 ?  42  TYR   A HE1  1 
ATOM   699  H HE2  . TYR   A 1 42  ? 30.479 5.045   -9.327  1.00 17.59 ?  42  TYR   A HE2  1 
ATOM   700  H HH   . TYR   A 1 42  ? 33.464 4.528   -10.793 1.00 19.17 ?  42  TYR   A HH   1 
ATOM   701  N N    . LEU   A 1 43  ? 31.208 4.240   -2.049  1.00 9.63  ?  43  LEU   A N    1 
ATOM   702  C CA   . LEU   A 1 43  ? 30.768 4.569   -0.693  1.00 9.43  ?  43  LEU   A CA   1 
ATOM   703  C C    . LEU   A 1 43  ? 30.285 6.016   -0.593  1.00 9.49  ?  43  LEU   A C    1 
ATOM   704  O O    . LEU   A 1 43  ? 30.546 6.715   0.388   1.00 10.53 ?  43  LEU   A O    1 
ATOM   705  C CB   . LEU   A 1 43  ? 31.834 4.257   0.356   1.00 9.72  ?  43  LEU   A CB   1 
ATOM   706  C CG   . LEU   A 1 43  ? 32.313 2.806   0.441   1.00 10.01 ?  43  LEU   A CG   1 
ATOM   707  C CD1  . LEU   A 1 43  ? 33.375 2.696   1.525   1.00 10.94 ?  43  LEU   A CD1  1 
ATOM   708  C CD2  . LEU   A 1 43  ? 31.166 1.832   0.698   1.00 10.63 ?  43  LEU   A CD2  1 
ATOM   709  H H    . LEU   A 1 43  ? 30.857 3.509   -2.351  1.00 11.56 ?  43  LEU   A H    1 
ATOM   710  H HA   . LEU   A 1 43  ? 30.004 4.008   -0.486  1.00 11.32 ?  43  LEU   A HA   1 
ATOM   711  H HB2  . LEU   A 1 43  ? 32.611 4.805   0.175   1.00 11.67 ?  43  LEU   A HB2  1 
ATOM   712  H HB3  . LEU   A 1 43  ? 31.473 4.485   1.227   1.00 11.67 ?  43  LEU   A HB3  1 
ATOM   713  H HG   . LEU   A 1 43  ? 32.729 2.561   -0.401  1.00 12.01 ?  43  LEU   A HG   1 
ATOM   714  H HD11 . LEU   A 1 43  ? 33.680 1.775   1.581   1.00 13.14 ?  43  LEU   A HD11 1 
ATOM   715  H HD12 . LEU   A 1 43  ? 34.119 3.277   1.303   1.00 13.14 ?  43  LEU   A HD12 1 
ATOM   716  H HD13 . LEU   A 1 43  ? 32.989 2.965   2.375   1.00 13.14 ?  43  LEU   A HD13 1 
ATOM   717  H HD21 . LEU   A 1 43  ? 31.532 0.943   0.843   1.00 12.76 ?  43  LEU   A HD21 1 
ATOM   718  H HD22 . LEU   A 1 43  ? 30.679 2.119   1.486   1.00 12.76 ?  43  LEU   A HD22 1 
ATOM   719  H HD23 . LEU   A 1 43  ? 30.579 1.825   -0.072  1.00 12.76 ?  43  LEU   A HD23 1 
ATOM   720  N N    . LYS   A 1 44  ? 29.556 6.460   -1.616  1.00 9.64  ?  44  LYS   A N    1 
ATOM   721  C CA   . LYS   A 1 44  ? 28.914 7.774   -1.609  1.00 10.04 ?  44  LYS   A CA   1 
ATOM   722  C C    . LYS   A 1 44  ? 27.491 7.584   -1.100  1.00 9.46  ?  44  LYS   A C    1 
ATOM   723  O O    . LYS   A 1 44  ? 26.616 7.084   -1.814  1.00 10.35 ?  44  LYS   A O    1 
ATOM   724  C CB   . LYS   A 1 44  ? 28.945 8.405   -2.994  1.00 12.40 ?  44  LYS   A CB   1 
ATOM   725  C CG   . LYS   A 1 44  ? 30.316 8.892   -3.425  1.00 15.80 ?  44  LYS   A CG   1 
ATOM   726  C CD   . LYS   A 1 44  ? 30.984 9.774   -2.372  1.00 21.63 ?  44  LYS   A CD   1 
ATOM   727  C CE   . LYS   A 1 44  ? 32.280 10.364  -2.892  1.00 24.72 ?  44  LYS   A CE   1 
ATOM   728  N NZ   . LYS   A 1 44  ? 33.164 10.844  -1.797  1.00 26.77 ?  44  LYS   A NZ   1 
ATOM   729  H H    . LYS   A 1 44  ? 29.416 6.008   -2.334  1.00 11.57 ?  44  LYS   A H    1 
ATOM   730  H HA   . LYS   A 1 44  ? 29.371 8.352   -0.979  1.00 12.05 ?  44  LYS   A HA   1 
ATOM   731  H HB2  . LYS   A 1 44  ? 28.646 7.752   -3.644  1.00 14.89 ?  44  LYS   A HB2  1 
ATOM   732  H HB3  . LYS   A 1 44  ? 28.345 9.170   -3.000  1.00 14.89 ?  44  LYS   A HB3  1 
ATOM   733  H HG2  . LYS   A 1 44  ? 30.889 8.129   -3.588  1.00 18.97 ?  44  LYS   A HG2  1 
ATOM   734  H HG3  . LYS   A 1 44  ? 30.226 9.419   -4.239  1.00 18.97 ?  44  LYS   A HG3  1 
ATOM   735  H HD2  . LYS   A 1 44  ? 30.380 10.494  -2.130  1.00 25.96 ?  44  LYS   A HD2  1 
ATOM   736  H HD3  . LYS   A 1 44  ? 31.193 9.233   -1.593  1.00 25.96 ?  44  LYS   A HD3  1 
ATOM   737  H HE2  . LYS   A 1 44  ? 32.759 9.683   -3.389  1.00 29.67 ?  44  LYS   A HE2  1 
ATOM   738  H HE3  . LYS   A 1 44  ? 32.074 11.115  -3.467  1.00 29.67 ?  44  LYS   A HE3  1 
ATOM   739  H HZ1  . LYS   A 1 44  ? 33.912 11.184  -2.139  1.00 32.12 ?  44  LYS   A HZ1  1 
ATOM   740  H HZ2  . LYS   A 1 44  ? 32.749 11.476  -1.326  1.00 32.12 ?  44  LYS   A HZ2  1 
ATOM   741  H HZ3  . LYS   A 1 44  ? 33.373 10.171  -1.255  1.00 32.12 ?  44  LYS   A HZ3  1 
ATOM   742  N N    . HIS   A 1 45  ? 27.261 7.972   0.149   1.00 9.27  ?  45  HIS   A N    1 
ATOM   743  C CA   . HIS   A 1 45  ? 26.024 7.627   0.845   1.00 9.35  ?  45  HIS   A CA   1 
ATOM   744  C C    . HIS   A 1 45  ? 25.000 8.752   0.691   1.00 10.11 ?  45  HIS   A C    1 
ATOM   745  O O    . HIS   A 1 45  ? 24.682 9.481   1.629   1.00 11.60 ?  45  HIS   A O    1 
ATOM   746  C CB   . HIS   A 1 45  ? 26.316 7.356   2.307   1.00 9.44  ?  45  HIS   A CB   1 
ATOM   747  C CG   . HIS   A 1 45  ? 27.431 6.392   2.529   1.00 8.79  ?  45  HIS   A CG   1 
ATOM   748  N ND1  . HIS   A 1 45  ? 27.423 5.105   2.029   1.00 9.29  ?  45  HIS   A ND1  1 
ATOM   749  C CD2  . HIS   A 1 45  ? 28.597 6.541   3.201   1.00 9.25  ?  45  HIS   A CD2  1 
ATOM   750  C CE1  . HIS   A 1 45  ? 28.545 4.507   2.393   1.00 9.08  ?  45  HIS   A CE1  1 
ATOM   751  N NE2  . HIS   A 1 45  ? 29.273 5.354   3.103   1.00 9.26  ?  45  HIS   A NE2  1 
ATOM   752  H H    . HIS   A 1 45  ? 27.807 8.442   0.621   1.00 11.12 ?  45  HIS   A H    1 
ATOM   753  H HA   . HIS   A 1 45  ? 25.648 6.822   0.455   1.00 11.22 ?  45  HIS   A HA   1 
ATOM   754  H HB2  . HIS   A 1 45  ? 26.549 8.193   2.741   1.00 11.33 ?  45  HIS   A HB2  1 
ATOM   755  H HB3  . HIS   A 1 45  ? 25.516 6.988   2.722   1.00 11.33 ?  45  HIS   A HB3  1 
ATOM   756  H HD2  . HIS   A 1 45  ? 28.890 7.308   3.643   1.00 11.11 ?  45  HIS   A HD2  1 
ATOM   757  H HE1  . HIS   A 1 45  ? 28.779 3.630   2.191   1.00 10.89 ?  45  HIS   A HE1  1 
ATOM   758  H HE2  . HIS   A 1 45  ? 30.046 5.186   3.445   1.00 11.12 ?  45  HIS   A HE2  1 
ATOM   759  N N    . GLY   A 1 46  ? 24.465 8.870   -0.518  1.00 11.42 ?  46  GLY   A N    1 
ATOM   760  C CA   . GLY   A 1 46  ? 23.658 10.031  -0.847  1.00 12.05 ?  46  GLY   A CA   1 
ATOM   761  C C    . GLY   A 1 46  ? 22.177 9.905   -0.561  1.00 11.74 ?  46  GLY   A C    1 
ATOM   762  O O    . GLY   A 1 46  ? 21.511 10.895  -0.239  1.00 12.77 ?  46  GLY   A O    1 
ATOM   763  H H    . GLY   A 1 46  ? 24.541 8.300   -1.152  1.00 13.71 ?  46  GLY   A H    1 
ATOM   764  H HA2  . GLY   A 1 46  ? 23.982 10.796  -0.345  1.00 14.46 ?  46  GLY   A HA2  1 
ATOM   765  H HA3  . GLY   A 1 46  ? 23.752 10.227  -1.788  1.00 14.46 ?  46  GLY   A HA3  1 
ATOM   766  N N    . GLY   A 1 47  ? 21.640 8.699   -0.705  1.00 11.65 ?  47  GLY   A N    1 
ATOM   767  C CA   . GLY   A 1 47  ? 20.205 8.501   -0.633  1.00 12.25 ?  47  GLY   A CA   1 
ATOM   768  C C    . GLY   A 1 47  ? 19.875 7.060   -0.315  1.00 11.45 ?  47  GLY   A C    1 
ATOM   769  O O    . GLY   A 1 47  ? 20.757 6.225   -0.105  1.00 11.54 ?  47  GLY   A O    1 
ATOM   770  H H    . GLY   A 1 47  ? 22.086 7.977   -0.828  1.00 13.98 ?  47  GLY   A H    1 
ATOM   771  H HA2  . GLY   A 1 47  ? 19.820 9.068   0.057   1.00 14.70 ?  47  GLY   A HA2  1 
ATOM   772  H HA3  . GLY   A 1 47  ? 19.798 8.728   -1.483  1.00 14.70 ?  47  GLY   A HA3  1 
ATOM   773  N N    . GLY   A 1 48  ? 18.579 6.768   -0.300  1.00 11.82 ?  48  GLY   A N    1 
ATOM   774  C CA   . GLY   A 1 48  ? 18.140 5.445   0.090   1.00 11.75 ?  48  GLY   A CA   1 
ATOM   775  C C    . GLY   A 1 48  ? 18.584 5.119   1.503   1.00 10.75 ?  48  GLY   A C    1 
ATOM   776  O O    . GLY   A 1 48  ? 18.720 5.996   2.367   1.00 11.26 ?  48  GLY   A O    1 
ATOM   777  H H    . GLY   A 1 48  ? 17.943 7.312   -0.503  1.00 14.18 ?  48  GLY   A H    1 
ATOM   778  H HA2  . GLY   A 1 48  ? 17.172 5.387   0.043   1.00 14.10 ?  48  GLY   A HA2  1 
ATOM   779  H HA3  . GLY   A 1 48  ? 18.519 4.782   -0.510  1.00 14.10 ?  48  GLY   A HA3  1 
ATOM   780  N N    . VAL   A 1 49  ? 18.812 3.826   1.742   1.00 10.17 ?  49  VAL   A N    1 
ATOM   781  C CA   . VAL   A 1 49  ? 19.285 3.374   3.048   1.00 10.09 ?  49  VAL   A CA   1 
ATOM   782  C C    . VAL   A 1 49  ? 20.605 4.047   3.413   1.00 8.92  ?  49  VAL   A C    1 
ATOM   783  O O    . VAL   A 1 49  ? 20.809 4.453   4.562   1.00 9.44  ?  49  VAL   A O    1 
ATOM   784  C CB   . VAL   A 1 49  ? 19.399 1.836   3.062   1.00 11.57 ?  49  VAL   A CB   1 
ATOM   785  C CG1  . VAL   A 1 49  ? 20.166 1.359   4.293   1.00 12.40 ?  49  VAL   A CG1  1 
ATOM   786  C CG2  . VAL   A 1 49  ? 18.017 1.195   2.995   1.00 13.56 ?  49  VAL   A CG2  1 
ATOM   787  H H    . VAL   A 1 49  ? 18.701 3.192   1.167   1.00 12.21 ?  49  VAL   A H    1 
ATOM   788  H HA   . VAL   A 1 49  ? 18.629 3.620   3.719   1.00 12.11 ?  49  VAL   A HA   1 
ATOM   789  H HB   . VAL   A 1 49  ? 19.893 1.547   2.278   1.00 13.89 ?  49  VAL   A HB   1 
ATOM   790  H HG11 . VAL   A 1 49  ? 19.987 0.415   4.427   1.00 14.89 ?  49  VAL   A HG11 1 
ATOM   791  H HG12 . VAL   A 1 49  ? 21.110 1.503   4.153   1.00 14.89 ?  49  VAL   A HG12 1 
ATOM   792  H HG13 . VAL   A 1 49  ? 19.858 1.863   5.065   1.00 14.89 ?  49  VAL   A HG13 1 
ATOM   793  H HG21 . VAL   A 1 49  ? 18.112 0.228   3.006   1.00 16.27 ?  49  VAL   A HG21 1 
ATOM   794  H HG22 . VAL   A 1 49  ? 17.498 1.481   3.764   1.00 16.27 ?  49  VAL   A HG22 1 
ATOM   795  H HG23 . VAL   A 1 49  ? 17.577 1.473   2.177   1.00 16.27 ?  49  VAL   A HG23 1 
ATOM   796  N N    . ALA   A 1 50  ? 21.531 4.131   2.460   1.00 8.78  ?  50  ALA   A N    1 
ATOM   797  C CA   . ALA   A 1 50  ? 22.848 4.684   2.760   1.00 8.68  ?  50  ALA   A CA   1 
ATOM   798  C C    . ALA   A 1 50  ? 22.753 6.139   3.194   1.00 8.55  ?  50  ALA   A C    1 
ATOM   799  O O    . ALA   A 1 50  ? 23.392 6.554   4.170   1.00 9.10  ?  50  ALA   A O    1 
ATOM   800  C CB   . ALA   A 1 50  ? 23.754 4.555   1.540   1.00 8.99  ?  50  ALA   A CB   1 
ATOM   801  H H    . ALA   A 1 50  ? 21.420 3.883   1.640   1.00 10.55 ?  50  ALA   A H    1 
ATOM   802  H HA   . ALA   A 1 50  ? 23.243 4.183   3.486   1.00 10.42 ?  50  ALA   A HA   1 
ATOM   803  H HB1  . ALA   A 1 50  ? 24.622 4.927   1.754   1.00 10.79 ?  50  ALA   A HB1  1 
ATOM   804  H HB2  . ALA   A 1 50  ? 23.839 3.619   1.306   1.00 10.79 ?  50  ALA   A HB2  1 
ATOM   805  H HB3  . ALA   A 1 50  ? 23.357 5.046   0.800   1.00 10.79 ?  50  ALA   A HB3  1 
ATOM   806  N N    . GLY   A 1 51  ? 21.973 6.936   2.468   1.00 8.93  ?  51  GLY   A N    1 
ATOM   807  C CA   . GLY   A 1 51  ? 21.822 8.325   2.852   1.00 9.56  ?  51  GLY   A CA   1 
ATOM   808  C C    . GLY   A 1 51  ? 21.223 8.469   4.236   1.00 9.35  ?  51  GLY   A C    1 
ATOM   809  O O    . GLY   A 1 51  ? 21.614 9.351   5.004   1.00 9.90  ?  51  GLY   A O    1 
ATOM   810  H H    . GLY   A 1 51  ? 21.534 6.702   1.762   1.00 10.72 ?  51  GLY   A H    1 
ATOM   811  H HA2  . GLY   A 1 51  ? 22.689 8.760   2.845   1.00 11.48 ?  51  GLY   A HA2  1 
ATOM   812  H HA3  . GLY   A 1 51  ? 21.244 8.778   2.217   1.00 11.48 ?  51  GLY   A HA3  1 
ATOM   813  N N    . ALA   A 1 52  ? 20.259 7.604   4.568   1.00 9.47  ?  52  ALA   A N    1 
ATOM   814  C CA   . ALA   A 1 52  ? 19.622 7.658   5.879   1.00 10.10 ?  52  ALA   A CA   1 
ATOM   815  C C    . ALA   A 1 52  ? 20.581 7.236   6.988   1.00 9.32  ?  52  ALA   A C    1 
ATOM   816  O O    . ALA   A 1 52  ? 20.658 7.887   8.034   1.00 10.20 ?  52  ALA   A O    1 
ATOM   817  C CB   . ALA   A 1 52  ? 18.358 6.792   5.879   1.00 11.48 ?  52  ALA   A CB   1 
ATOM   818  H H    . ALA   A 1 52  ? 19.972 6.969   4.057   1.00 11.37 ?  52  ALA   A H    1 
ATOM   819  H HA   . ALA   A 1 52  ? 19.355 8.569   6.052   1.00 12.12 ?  52  ALA   A HA   1 
ATOM   820  H HB1  . ALA   A 1 52  ? 17.941 6.843   6.755   1.00 13.78 ?  52  ALA   A HB1  1 
ATOM   821  H HB2  . ALA   A 1 52  ? 17.745 7.130   5.204   1.00 13.78 ?  52  ALA   A HB2  1 
ATOM   822  H HB3  . ALA   A 1 52  ? 18.597 5.875   5.679   1.00 13.78 ?  52  ALA   A HB3  1 
ATOM   823  N N    . LEU   A 1 53  ? 21.307 6.131   6.793   1.00 9.00  ?  53  LEU   A N    1 
ATOM   824  C CA   . LEU   A 1 53  ? 22.277 5.714   7.804   1.00 9.36  ?  53  LEU   A CA   1 
ATOM   825  C C    . LEU   A 1 53  ? 23.335 6.789   8.002   1.00 8.88  ?  53  LEU   A C    1 
ATOM   826  O O    . LEU   A 1 53  ? 23.678 7.142   9.136   1.00 9.87  ?  53  LEU   A O    1 
ATOM   827  C CB   . LEU   A 1 53  ? 22.934 4.384   7.418   1.00 9.77  ?  53  LEU   A CB   1 
ATOM   828  C CG   . LEU   A 1 53  ? 22.060 3.124   7.474   1.00 10.48 ?  53  LEU   A CG   1 
ATOM   829  C CD1  . LEU   A 1 53  ? 22.800 1.946   6.865   1.00 11.44 ?  53  LEU   A CD1  1 
ATOM   830  C CD2  . LEU   A 1 53  ? 21.642 2.796   8.897   1.00 12.08 ?  53  LEU   A CD2  1 
ATOM   831  H H    . LEU   A 1 53  ? 21.259 5.614   6.102   1.00 10.81 ?  53  LEU   A H    1 
ATOM   832  H HA   . LEU   A 1 53  ? 21.820 5.587   8.649   1.00 11.24 ?  53  LEU   A HA   1 
ATOM   833  H HB2  . LEU   A 1 53  ? 23.264 4.460   6.510   1.00 11.73 ?  53  LEU   A HB2  1 
ATOM   834  H HB3  . LEU   A 1 53  ? 23.685 4.231   8.016   1.00 11.73 ?  53  LEU   A HB3  1 
ATOM   835  H HG   . LEU   A 1 53  ? 21.257 3.271   6.950   1.00 12.57 ?  53  LEU   A HG   1 
ATOM   836  H HD11 . LEU   A 1 53  ? 22.231 1.159   6.909   1.00 13.73 ?  53  LEU   A HD11 1 
ATOM   837  H HD12 . LEU   A 1 53  ? 23.011 2.148   5.941   1.00 13.73 ?  53  LEU   A HD12 1 
ATOM   838  H HD13 . LEU   A 1 53  ? 23.615 1.791   7.366   1.00 13.73 ?  53  LEU   A HD13 1 
ATOM   839  H HD21 . LEU   A 1 53  ? 21.109 1.983   8.892   1.00 14.50 ?  53  LEU   A HD21 1 
ATOM   840  H HD22 . LEU   A 1 53  ? 22.436 2.663   9.438   1.00 14.50 ?  53  LEU   A HD22 1 
ATOM   841  H HD23 . LEU   A 1 53  ? 21.118 3.530   9.251   1.00 14.50 ?  53  LEU   A HD23 1 
ATOM   842  N N    . ASN   A 1 54  ? 23.854 7.336   6.904   1.00 8.71  ?  54  ASN   A N    1 
ATOM   843  C CA   . ASN   A 1 54  ? 24.910 8.330   7.037   1.00 8.59  ?  54  ASN   A CA   1 
ATOM   844  C C    . ASN   A 1 54  ? 24.406 9.579   7.762   1.00 9.14  ?  54  ASN   A C    1 
ATOM   845  O O    . ASN   A 1 54  ? 25.097 10.129  8.632   1.00 9.68  ?  54  ASN   A O    1 
ATOM   846  C CB   . ASN   A 1 54  ? 25.479 8.691   5.675   1.00 8.94  ?  54  ASN   A CB   1 
ATOM   847  C CG   . ASN   A 1 54  ? 26.491 9.795   5.782   1.00 9.23  ?  54  ASN   A CG   1 
ATOM   848  O OD1  . ASN   A 1 54  ? 27.495 9.657   6.491   1.00 9.43  ?  54  ASN   A OD1  1 
ATOM   849  N ND2  . ASN   A 1 54  ? 26.227 10.915  5.125   1.00 10.24 ?  54  ASN   A ND2  1 
ATOM   850  H H    . ASN   A 1 54  ? 23.613 7.152   6.096   1.00 10.46 ?  54  ASN   A H    1 
ATOM   851  H HA   . ASN   A 1 54  ? 25.623 7.949   7.565   1.00 10.31 ?  54  ASN   A HA   1 
ATOM   852  H HB2  . ASN   A 1 54  ? 25.918 7.902   5.298   1.00 10.73 ?  54  ASN   A HB2  1 
ATOM   853  H HB3  . ASN   A 1 54  ? 24.761 8.977   5.090   1.00 10.73 ?  54  ASN   A HB3  1 
ATOM   854  H HD21 . ASN   A 1 54  ? 26.776 11.573  5.164   1.00 12.29 ?  54  ASN   A HD21 1 
ATOM   855  H HD22 . ASN   A 1 54  ? 25.510 10.978  4.653   1.00 12.29 ?  54  ASN   A HD22 1 
ATOM   856  N N    . LYS   A 1 55  ? 23.193 10.033  7.425   1.00 9.29  ?  55  LYS   A N    1 
ATOM   857  C CA   . LYS   A 1 55  ? 22.614 11.190  8.097   1.00 9.69  ?  55  LYS   A CA   1 
ATOM   858  C C    . LYS   A 1 55  ? 22.520 10.952  9.597   1.00 10.06 ?  55  LYS   A C    1 
ATOM   859  O O    . LYS   A 1 55  ? 22.795 11.853  10.399  1.00 10.73 ?  55  LYS   A O    1 
ATOM   860  C CB   . LYS   A 1 55  ? 21.238 11.493  7.492   1.00 10.63 ?  55  LYS   A CB   1 
ATOM   861  C CG   . LYS   A 1 55  ? 20.497 12.656  8.133   1.00 11.81 ?  55  LYS   A CG   1 
ATOM   862  C CD   . LYS   A 1 55  ? 19.171 12.914  7.416   1.00 12.82 ?  55  LYS   A CD   1 
ATOM   863  C CE   . LYS   A 1 55  ? 18.369 14.029  8.062   1.00 14.60 ?  55  LYS   A CE   1 
ATOM   864  N NZ   . LYS   A 1 55  ? 17.024 14.166  7.429   1.00 15.56 ?  55  LYS   A NZ   1 
ATOM   865  H H    . LYS   A 1 55  ? 22.680 9.679   6.824   1.00 11.15 ?  55  LYS   A H    1 
ATOM   866  H HA   . LYS   A 1 55  ? 23.184 11.956  7.947   1.00 11.63 ?  55  LYS   A HA   1 
ATOM   867  H HB2  . LYS   A 1 55  ? 21.354 11.708  6.553   1.00 12.76 ?  55  LYS   A HB2  1 
ATOM   868  H HB3  . LYS   A 1 55  ? 20.679 10.707  7.579   1.00 12.76 ?  55  LYS   A HB3  1 
ATOM   869  H HG2  . LYS   A 1 55  ? 20.302 12.442  9.061   1.00 14.18 ?  55  LYS   A HG2  1 
ATOM   870  H HG3  . LYS   A 1 55  ? 21.037 13.456  8.076   1.00 14.18 ?  55  LYS   A HG3  1 
ATOM   871  H HD2  . LYS   A 1 55  ? 19.354 13.165  6.497   1.00 15.39 ?  55  LYS   A HD2  1 
ATOM   872  H HD3  . LYS   A 1 55  ? 18.636 12.104  7.439   1.00 15.39 ?  55  LYS   A HD3  1 
ATOM   873  H HE2  . LYS   A 1 55  ? 18.245 13.831  9.004   1.00 17.52 ?  55  LYS   A HE2  1 
ATOM   874  H HE3  . LYS   A 1 55  ? 18.843 14.869  7.955   1.00 17.52 ?  55  LYS   A HE3  1 
ATOM   875  H HZ1  . LYS   A 1 55  ? 16.455 14.547  8.000   1.00 18.67 ?  55  LYS   A HZ1  1 
ATOM   876  H HZ2  . LYS   A 1 55  ? 17.077 14.670  6.699   1.00 18.67 ?  55  LYS   A HZ2  1 
ATOM   877  H HZ3  . LYS   A 1 55  ? 16.707 13.363  7.206   1.00 18.67 ?  55  LYS   A HZ3  1 
ATOM   878  N N    . ALA   A 1 56  ? 22.139 9.737   9.995   1.00 10.38 ?  56  ALA   A N    1 
ATOM   879  C CA   . ALA   A 1 56  ? 22.017 9.406   11.408  1.00 11.17 ?  56  ALA   A CA   1 
ATOM   880  C C    . ALA   A 1 56  ? 23.360 9.440   12.131  1.00 10.96 ?  56  ALA   A C    1 
ATOM   881  O O    . ALA   A 1 56  ? 23.385 9.642   13.349  1.00 12.49 ?  56  ALA   A O    1 
ATOM   882  C CB   . ALA   A 1 56  ? 21.344 8.039   11.572  1.00 12.26 ?  56  ALA   A CB   1 
ATOM   883  H H    . ALA   A 1 56  ? 21.940 9.094   9.462   1.00 12.45 ?  56  ALA   A H    1 
ATOM   884  H HA   . ALA   A 1 56  ? 21.445 10.060  11.831  1.00 13.41 ?  56  ALA   A HA   1 
ATOM   885  H HB1  . ALA   A 1 56  ? 21.270 7.834   12.520  1.00 14.71 ?  56  ALA   A HB1  1 
ATOM   886  H HB2  . ALA   A 1 56  ? 20.459 8.072   11.175  1.00 14.71 ?  56  ALA   A HB2  1 
ATOM   887  H HB3  . ALA   A 1 56  ? 21.880 7.363   11.130  1.00 14.71 ?  56  ALA   A HB3  1 
ATOM   888  N N    . THR   A 1 57  ? 24.473 9.258   11.413  1.00 10.07 ?  57  THR   A N    1 
ATOM   889  C CA   . THR   A 1 57  ? 25.814 9.384   11.988  1.00 10.47 ?  57  THR   A CA   1 
ATOM   890  C C    . THR   A 1 57  ? 26.363 10.804  11.918  1.00 10.51 ?  57  THR   A C    1 
ATOM   891  O O    . THR   A 1 57  ? 27.546 11.014  12.216  1.00 11.14 ?  57  THR   A O    1 
ATOM   892  C CB   . THR   A 1 57  ? 26.825 8.438   11.310  1.00 10.26 ?  57  THR   A CB   1 
ATOM   893  O OG1  . THR   A 1 57  ? 27.208 8.944   10.020  1.00 10.09 ?  57  THR   A OG1  1 
ATOM   894  C CG2  . THR   A 1 57  ? 26.293 7.016   11.199  1.00 10.58 ?  57  THR   A CG2  1 
ATOM   895  H H    . THR   A 1 57  ? 24.475 9.043   10.576  1.00 12.09 ?  57  THR   A H    1 
ATOM   896  H HA   . THR   A 1 57  ? 25.768 9.126   12.923  1.00 12.56 ?  57  THR   A HA   1 
ATOM   897  H HB   . THR   A 1 57  ? 27.620 8.393   11.869  1.00 12.32 ?  57  THR   A HB   1 
ATOM   898  H HG1  . THR   A 1 57  ? 26.532 9.008   9.529   1.00 12.11 ?  57  THR   A HG1  1 
ATOM   899  H HG21 . THR   A 1 57  ? 26.976 6.427   10.838  1.00 12.70 ?  57  THR   A HG21 1 
ATOM   900  H HG22 . THR   A 1 57  ? 26.029 6.687   12.074  1.00 12.70 ?  57  THR   A HG22 1 
ATOM   901  H HG23 . THR   A 1 57  ? 25.520 6.993   10.613  1.00 12.70 ?  57  THR   A HG23 1 
ATOM   902  N N    . ASN   A 1 58  ? 25.550 11.778  11.515  1.00 10.86 ?  58  ASN   A N    1 
ATOM   903  C CA   . ASN   A 1 58  ? 26.011 13.160  11.418  1.00 12.01 ?  58  ASN   A CA   1 
ATOM   904  C C    . ASN   A 1 58  ? 27.156 13.286  10.410  1.00 10.65 ?  58  ASN   A C    1 
ATOM   905  O O    . ASN   A 1 58  ? 28.055 14.112  10.573  1.00 11.52 ?  58  ASN   A O    1 
ATOM   906  C CB   . ASN   A 1 58  ? 26.393 13.692  12.813  1.00 14.49 ?  58  ASN   A CB   1 
ATOM   907  C CG   . ASN   A 1 58  ? 26.811 15.148  12.814  1.00 17.68 ?  58  ASN   A CG   1 
ATOM   908  O OD1  . ASN   A 1 58  ? 26.185 15.982  12.170  1.00 19.20 ?  58  ASN   A OD1  1 
ATOM   909  N ND2  . ASN   A 1 58  ? 27.866 15.462  13.567  1.00 19.04 ?  58  ASN   A ND2  1 
ATOM   910  H H    . ASN   A 1 58  ? 24.730 11.654  11.281  1.00 13.04 ?  58  ASN   A H    1 
ATOM   911  H HA   . ASN   A 1 58  ? 25.275 13.695  11.091  1.00 14.41 ?  58  ASN   A HA   1 
ATOM   912  H HB2  . ASN   A 1 58  ? 25.622 13.595  13.402  1.00 17.40 ?  58  ASN   A HB2  1 
ATOM   913  H HB3  . ASN   A 1 58  ? 27.132 13.172  13.159  1.00 17.40 ?  58  ASN   A HB3  1 
ATOM   914  H HD21 . ASN   A 1 58  ? 28.137 16.277  13.606  1.00 22.85 ?  58  ASN   A HD21 1 
ATOM   915  H HD22 . ASN   A 1 58  ? 28.274 14.850  14.009  1.00 22.85 ?  58  ASN   A HD22 1 
ATOM   916  N N    . ASN   A 1 59  ? 27.133 12.470  9.355   1.00 10.07 ?  59  ASN   A N    1 
ATOM   917  C CA   . ASN   A 1 59  ? 28.107 12.445  8.257   1.00 9.75  ?  59  ASN   A CA   1 
ATOM   918  C C    . ASN   A 1 59  ? 29.426 11.768  8.642   1.00 9.61  ?  59  ASN   A C    1 
ATOM   919  O O    . ASN   A 1 59  ? 30.345 11.729  7.814   1.00 9.88  ?  59  ASN   A O    1 
ATOM   920  C CB   . ASN   A 1 59  ? 28.388 13.833  7.655   1.00 10.11 ?  59  ASN   A CB   1 
ATOM   921  C CG   . ASN   A 1 59  ? 28.745 13.770  6.186   1.00 10.38 ?  59  ASN   A CG   1 
ATOM   922  O OD1  . ASN   A 1 59  ? 28.036 13.148  5.390   1.00 10.77 ?  59  ASN   A OD1  1 
ATOM   923  N ND2  . ASN   A 1 59  ? 29.834 14.434  5.810   1.00 11.02 ?  59  ASN   A ND2  1 
ATOM   924  H H    . ASN   A 1 59  ? 26.515 11.880  9.238   1.00 12.09 ?  59  ASN   A H    1 
ATOM   925  H HA   . ASN   A 1 59  ? 27.725 11.913  7.543   1.00 11.70 ?  59  ASN   A HA   1 
ATOM   926  H HB2  . ASN   A 1 59  ? 27.597 14.387  7.740   1.00 12.13 ?  59  ASN   A HB2  1 
ATOM   927  H HB3  . ASN   A 1 59  ? 29.133 14.242  8.121   1.00 12.13 ?  59  ASN   A HB3  1 
ATOM   928  H HD21 . ASN   A 1 59  ? 30.084 14.432  4.985   1.00 13.23 ?  59  ASN   A HD21 1 
ATOM   929  H HD22 . ASN   A 1 59  ? 30.310 14.859  6.394   1.00 13.23 ?  59  ASN   A HD22 1 
ATOM   930  N N    . ALA   A 1 60  ? 29.554 11.221  9.851   1.00 9.64  ?  60  ALA   A N    1 
ATOM   931  C CA   . ALA   A 1 60  ? 30.792 10.535  10.208  1.00 9.91  ?  60  ALA   A CA   1 
ATOM   932  C C    . ALA   A 1 60  ? 31.017 9.300   9.342   1.00 9.78  ?  60  ALA   A C    1 
ATOM   933  O O    . ALA   A 1 60  ? 32.162 8.979   9.004   1.00 10.34 ?  60  ALA   A O    1 
ATOM   934  C CB   . ALA   A 1 60  ? 30.785 10.168  11.690  1.00 10.85 ?  60  ALA   A CB   1 
ATOM   935  H H    . ALA   A 1 60  ? 28.955 11.232  10.468  1.00 11.57 ?  60  ALA   A H    1 
ATOM   936  H HA   . ALA   A 1 60  ? 31.538 11.141  10.057  1.00 11.89 ?  60  ALA   A HA   1 
ATOM   937  H HB1  . ALA   A 1 60  ? 31.616 9.717   11.908  1.00 13.02 ?  60  ALA   A HB1  1 
ATOM   938  H HB2  . ALA   A 1 60  ? 30.703 10.980  12.217  1.00 13.02 ?  60  ALA   A HB2  1 
ATOM   939  H HB3  . ALA   A 1 60  ? 30.033 9.583   11.866  1.00 13.02 ?  60  ALA   A HB3  1 
ATOM   940  N N    . MET   A 1 61  ? 29.946 8.604   8.961   1.00 9.39  ?  61  MET   A N    1 
ATOM   941  C CA   . MET   A 1 61  ? 30.090 7.470   8.055   1.00 9.31  ?  61  MET   A CA   1 
ATOM   942  C C    . MET   A 1 61  ? 30.720 7.899   6.732   1.00 9.24  ?  61  MET   A C    1 
ATOM   943  O O    . MET   A 1 61  ? 31.611 7.220   6.209   1.00 9.45  ?  61  MET   A O    1 
ATOM   944  C CB   . MET   A 1 61  ? 28.726 6.809   7.838   1.00 9.29  ?  61  MET   A CB   1 
ATOM   945  C CG   . MET   A 1 61  ? 28.738 5.655   6.850   1.00 9.91  ?  61  MET   A CG   1 
ATOM   946  S SD   . MET   A 1 61  ? 27.112 4.916   6.625   1.00 10.89 ?  61  MET   A SD   1 
ATOM   947  C CE   . MET   A 1 61  ? 26.938 4.025   8.171   1.00 12.36 ?  61  MET   A CE   1 
ATOM   948  H H    . MET   A 1 61  ? 29.140 8.770   9.209   1.00 11.28 ?  61  MET   A H    1 
ATOM   949  H HA   . MET   A 1 61  ? 30.667 6.815   8.473   1.00 11.18 ?  61  MET   A HA   1 
ATOM   950  H HB2  . MET   A 1 61  ? 28.410 6.463   8.687   1.00 11.15 ?  61  MET   A HB2  1 
ATOM   951  H HB3  . MET   A 1 61  ? 28.106 7.474   7.505   1.00 11.15 ?  61  MET   A HB3  1 
ATOM   952  H HG2  . MET   A 1 61  ? 29.030 5.972   5.982   1.00 11.90 ?  61  MET   A HG2  1 
ATOM   953  H HG3  . MET   A 1 61  ? 29.333 4.961   7.170   1.00 11.90 ?  61  MET   A HG3  1 
ATOM   954  H HE1  . MET   A 1 61  ? 26.095 3.547   8.170   1.00 14.84 ?  61  MET   A HE1  1 
ATOM   955  H HE2  . MET   A 1 61  ? 27.674 3.400   8.260   1.00 14.84 ?  61  MET   A HE2  1 
ATOM   956  H HE3  . MET   A 1 61  ? 26.955 4.661   8.906   1.00 14.84 ?  61  MET   A HE3  1 
ATOM   957  N N    . GLN   A 1 62  ? 30.274 9.030   6.179   1.00 9.01  ?  62  GLN   A N    1 
ATOM   958  C CA   . GLN   A 1 62  ? 30.832 9.509   4.918   1.00 9.52  ?  62  GLN   A CA   1 
ATOM   959  C C    . GLN   A 1 62  ? 32.303 9.883   5.060   1.00 9.48  ?  62  GLN   A C    1 
ATOM   960  O O    . GLN   A 1 62  ? 33.111 9.582   4.175   1.00 10.01 ?  62  GLN   A O    1 
ATOM   961  C CB   . GLN   A 1 62  ? 30.026 10.699  4.393   1.00 9.51  ?  62  GLN   A CB   1 
ATOM   962  C CG   . GLN   A 1 62  ? 30.401 11.068  2.971   1.00 9.52  ?  62  GLN   A CG   1 
ATOM   963  C CD   . GLN   A 1 62  ? 30.071 9.940   2.021   1.00 9.80  ?  62  GLN   A CD   1 
ATOM   964  O OE1  . GLN   A 1 62  ? 28.895 9.635   1.812   1.00 10.37 ?  62  GLN   A OE1  1 
ATOM   965  N NE2  . GLN   A 1 62  ? 31.090 9.272   1.491   1.00 10.44 ?  62  GLN   A NE2  1 
ATOM   966  H H    . GLN   A 1 62  ? 29.657 9.527   6.510   1.00 10.82 ?  62  GLN   A H    1 
ATOM   967  H HA   . GLN   A 1 62  ? 30.775 8.792   4.266   1.00 11.43 ?  62  GLN   A HA   1 
ATOM   968  H HB2  . GLN   A 1 62  ? 29.085 10.478  4.411   1.00 11.41 ?  62  GLN   A HB2  1 
ATOM   969  H HB3  . GLN   A 1 62  ? 30.200 11.470  4.958   1.00 11.41 ?  62  GLN   A HB3  1 
ATOM   970  H HG2  . GLN   A 1 62  ? 29.897 11.848  2.700   1.00 11.42 ?  62  GLN   A HG2  1 
ATOM   971  H HG3  . GLN   A 1 62  ? 31.353 11.242  2.920   1.00 11.42 ?  62  GLN   A HG3  1 
ATOM   972  H HE21 . GLN   A 1 62  ? 31.899 9.503   1.673   1.00 12.53 ?  62  GLN   A HE21 1 
ATOM   973  H HE22 . GLN   A 1 62  ? 30.942 8.618   0.952   1.00 12.53 ?  62  GLN   A HE22 1 
ATOM   974  N N    . VAL   A 1 63  ? 32.665 10.560  6.153   1.00 9.76  ?  63  VAL   A N    1 
ATOM   975  C CA   . VAL   A 1 63  ? 34.057 10.953  6.364   1.00 10.68 ?  63  VAL   A CA   1 
ATOM   976  C C    . VAL   A 1 63  ? 34.954 9.719   6.418   1.00 10.32 ?  63  VAL   A C    1 
ATOM   977  O O    . VAL   A 1 63  ? 36.005 9.657   5.766   1.00 10.90 ?  63  VAL   A O    1 
ATOM   978  C CB   . VAL   A 1 63  ? 34.172 11.819  7.632   1.00 12.32 ?  63  VAL   A CB   1 
ATOM   979  C CG1  . VAL   A 1 63  ? 35.623 12.054  7.994   1.00 14.01 ?  63  VAL   A CG1  1 
ATOM   980  C CG2  . VAL   A 1 63  ? 33.440 13.152  7.433   1.00 12.89 ?  63  VAL   A CG2  1 
ATOM   981  H H    . VAL   A 1 63  ? 32.121 10.800  6.782   1.00 11.72 ?  63  VAL   A H    1 
ATOM   982  H HA   . VAL   A 1 63  ? 34.337 11.491  5.614   1.00 12.82 ?  63  VAL   A HA   1 
ATOM   983  H HB   . VAL   A 1 63  ? 33.752 11.355  8.373   1.00 14.78 ?  63  VAL   A HB   1 
ATOM   984  H HG11 . VAL   A 1 63  ? 35.675 12.785  8.628   1.00 16.81 ?  63  VAL   A HG11 1 
ATOM   985  H HG12 . VAL   A 1 63  ? 35.989 11.247  8.388   1.00 16.81 ?  63  VAL   A HG12 1 
ATOM   986  H HG13 . VAL   A 1 63  ? 36.115 12.282  7.187   1.00 16.81 ?  63  VAL   A HG13 1 
ATOM   987  H HG21 . VAL   A 1 63  ? 33.536 13.690  8.236   1.00 15.47 ?  63  VAL   A HG21 1 
ATOM   988  H HG22 . VAL   A 1 63  ? 33.829 13.618  6.676   1.00 15.47 ?  63  VAL   A HG22 1 
ATOM   989  H HG23 . VAL   A 1 63  ? 32.500 12.977  7.265   1.00 15.47 ?  63  VAL   A HG23 1 
ATOM   990  N N    . GLU   A 1 64  ? 34.540 8.710   7.183   1.00 10.29 ?  64  GLU   A N    1 
ATOM   991  C CA   . GLU   A 1 64  ? 35.305 7.475   7.275   1.00 10.21 ?  64  GLU   A CA   1 
ATOM   992  C C    . GLU   A 1 64  ? 35.387 6.784   5.919   1.00 9.89  ?  64  GLU   A C    1 
ATOM   993  O O    . GLU   A 1 64  ? 36.437 6.244   5.541   1.00 10.42 ?  64  GLU   A O    1 
ATOM   994  C CB   . GLU   A 1 64  ? 34.630 6.568   8.301   1.00 10.94 ?  64  GLU   A CB   1 
ATOM   995  C CG   . GLU   A 1 64  ? 35.281 5.218   8.445   1.00 11.76 ?  64  GLU   A CG   1 
ATOM   996  C CD   . GLU   A 1 64  ? 34.407 4.225   9.179   1.00 12.45 ?  64  GLU   A CD   1 
ATOM   997  O OE1  . GLU   A 1 64  ? 33.165 4.322   9.062   1.00 13.30 ?  64  GLU   A OE1  1 
ATOM   998  O OE2  . GLU   A 1 64  ? 34.965 3.331   9.859   1.00 12.83 -1 64  GLU   A OE2  1 
ATOM   999  H H    . GLU   A 1 64  ? 33.812 8.710   7.642   1.00 12.35 ?  64  GLU   A H    1 
ATOM   1000 H HA   . GLU   A 1 64  ? 36.205 7.678   7.579   1.00 12.26 ?  64  GLU   A HA   1 
ATOM   1001 H HB2  . GLU   A 1 64  ? 34.664 7.007   9.170   1.00 13.14 ?  64  GLU   A HB2  1 
ATOM   1002 H HB3  . GLU   A 1 64  ? 33.710 6.436   8.037   1.00 13.14 ?  64  GLU   A HB3  1 
ATOM   1003 H HG2  . GLU   A 1 64  ? 35.476 4.850   7.567   1.00 14.11 ?  64  GLU   A HG2  1 
ATOM   1004 H HG3  . GLU   A 1 64  ? 36.105 5.316   8.948   1.00 14.11 ?  64  GLU   A HG3  1 
ATOM   1005 N N    . SER   A 1 65  ? 34.271 6.779   5.185   1.00 9.62  ?  65  SER   A N    1 
ATOM   1006 C CA   . SER   A 1 65  ? 34.218 6.125   3.882   1.00 9.46  ?  65  SER   A CA   1 
ATOM   1007 C C    . SER   A 1 65  ? 35.136 6.802   2.873   1.00 9.80  ?  65  SER   A C    1 
ATOM   1008 O O    . SER   A 1 65  ? 35.769 6.128   2.054   1.00 10.55 ?  65  SER   A O    1 
ATOM   1009 C CB   . SER   A 1 65  ? 32.785 6.140   3.355   1.00 9.60  ?  65  SER   A CB   1 
ATOM   1010 O OG   . SER   A 1 65  ? 31.935 5.319   4.140   1.00 10.30 ?  65  SER   A OG   1 
ATOM   1011 H H    . SER   A 1 65  ? 33.539 7.150   5.421   1.00 11.54 ?  65  SER   A H    1 
ATOM   1012 H HA   . SER   A 1 65  ? 34.502 5.203   3.973   1.00 11.36 ?  65  SER   A HA   1 
ATOM   1013 H HB2  . SER   A 1 65  ? 32.450 7.049   3.379   1.00 11.53 ?  65  SER   A HB2  1 
ATOM   1014 H HB3  . SER   A 1 65  ? 32.785 5.812   2.443   1.00 11.53 ?  65  SER   A HB3  1 
ATOM   1015 H HG   . SER   A 1 65  ? 31.929 5.589   4.938   1.00 12.36 ?  65  SER   A HG   1 
ATOM   1016 N N    . ASP   A 1 66  ? 35.206 8.135   2.898   1.00 9.95  ?  66  ASP   A N    1 
ATOM   1017 C CA   . ASP   A 1 66  ? 36.060 8.840   1.949   1.00 10.92 ?  66  ASP   A CA   1 
ATOM   1018 C C    . ASP   A 1 66  ? 37.524 8.482   2.176   1.00 11.01 ?  66  ASP   A C    1 
ATOM   1019 O O    . ASP   A 1 66  ? 38.292 8.323   1.219   1.00 11.81 ?  66  ASP   A O    1 
ATOM   1020 C CB   . ASP   A 1 66  ? 35.842 10.347  2.066   1.00 12.11 ?  66  ASP   A CB   1 
ATOM   1021 C CG   . ASP   A 1 66  ? 34.509 10.812  1.461   1.00 13.94 ?  66  ASP   A CG   1 
ATOM   1022 O OD1  . ASP   A 1 66  ? 33.792 10.018  0.814   1.00 13.95 ?  66  ASP   A OD1  1 
ATOM   1023 O OD2  . ASP   A 1 66  ? 34.193 12.004  1.628   1.00 16.87 -1 66  ASP   A OD2  1 
ATOM   1024 H H    . ASP   A 1 66  ? 34.764 8.645   3.435   1.00 11.95 ?  66  ASP   A H    1 
ATOM   1025 H HA   . ASP   A 1 66  ? 35.820 8.573   1.049   1.00 13.11 ?  66  ASP   A HA   1 
ATOM   1026 H HB2  . ASP   A 1 66  ? 35.835 10.593  3.004   1.00 14.54 ?  66  ASP   A HB2  1 
ATOM   1027 H HB3  . ASP   A 1 66  ? 36.566 10.805  1.609   1.00 14.54 ?  66  ASP   A HB3  1 
ATOM   1028 N N    . ASP   A 1 67  ? 37.927 8.343   3.438   1.00 10.86 ?  67  ASP   A N    1 
ATOM   1029 C CA   . ASP   A 1 67  ? 39.285 7.900   3.729   1.00 11.95 ?  67  ASP   A CA   1 
ATOM   1030 C C    . ASP   A 1 67  ? 39.506 6.466   3.255   1.00 11.74 ?  67  ASP   A C    1 
ATOM   1031 O O    . ASP   A 1 67  ? 40.568 6.142   2.712   1.00 12.40 ?  67  ASP   A O    1 
ATOM   1032 C CB   . ASP   A 1 67  ? 39.556 8.029   5.226   1.00 13.32 ?  67  ASP   A CB   1 
ATOM   1033 C CG   . ASP   A 1 67  ? 40.859 7.374   5.645   1.00 14.46 ?  67  ASP   A CG   1 
ATOM   1034 O OD1  . ASP   A 1 67  ? 41.929 8.012   5.513   1.00 17.05 ?  67  ASP   A OD1  1 
ATOM   1035 O OD2  . ASP   A 1 67  ? 40.806 6.211   6.104   1.00 14.16 -1 67  ASP   A OD2  1 
ATOM   1036 H H    . ASP   A 1 67  ? 37.439 8.493   4.127   1.00 13.04 ?  67  ASP   A H    1 
ATOM   1037 H HA   . ASP   A 1 67  ? 39.910 8.468   3.256   1.00 14.35 ?  67  ASP   A HA   1 
ATOM   1038 H HB2  . ASP   A 1 67  ? 39.602 8.966   5.453   1.00 15.99 ?  67  ASP   A HB2  1 
ATOM   1039 H HB3  . ASP   A 1 67  ? 38.832 7.600   5.712   1.00 15.99 ?  67  ASP   A HB3  1 
ATOM   1040 N N    . TYR   A 1 68  ? 38.515 5.589   3.450   1.00 10.99 ?  68  TYR   A N    1 
ATOM   1041 C CA   . TYR   A 1 68  ? 38.636 4.212   2.972   1.00 11.31 ?  68  TYR   A CA   1 
ATOM   1042 C C    . TYR   A 1 68  ? 38.873 4.170   1.465   1.00 11.07 ?  68  TYR   A C    1 
ATOM   1043 O O    . TYR   A 1 68  ? 39.745 3.435   0.983   1.00 11.53 ?  68  TYR   A O    1 
ATOM   1044 C CB   . TYR   A 1 68  ? 37.390 3.385   3.354   1.00 11.93 ?  68  TYR   A CB   1 
ATOM   1045 C CG   . TYR   A 1 68  ? 37.417 1.997   2.721   1.00 13.26 ?  68  TYR   A CG   1 
ATOM   1046 C CD1  . TYR   A 1 68  ? 36.954 1.806   1.424   1.00 14.62 ?  68  TYR   A CD1  1 
ATOM   1047 C CD2  . TYR   A 1 68  ? 37.965 0.909   3.385   1.00 14.99 ?  68  TYR   A CD2  1 
ATOM   1048 C CE1  . TYR   A 1 68  ? 37.020 0.587   0.809   1.00 15.89 ?  68  TYR   A CE1  1 
ATOM   1049 C CE2  . TYR   A 1 68  ? 38.023 -0.345  2.773   1.00 15.55 ?  68  TYR   A CE2  1 
ATOM   1050 C CZ   . TYR   A 1 68  ? 37.557 -0.479  1.484   1.00 16.14 ?  68  TYR   A CZ   1 
ATOM   1051 O OH   . TYR   A 1 68  ? 37.634 -1.691  0.860   1.00 17.49 ?  68  TYR   A OH   1 
ATOM   1052 H H    . TYR   A 1 68  ? 37.771 5.761   3.855   1.00 13.20 ?  68  TYR   A H    1 
ATOM   1053 H HA   . TYR   A 1 68  ? 39.399 3.801   3.400   1.00 13.58 ?  68  TYR   A HA   1 
ATOM   1054 H HB2  . TYR   A 1 68  ? 37.363 3.273   4.316   1.00 14.33 ?  68  TYR   A HB2  1 
ATOM   1055 H HB3  . TYR   A 1 68  ? 36.593 3.842   3.045   1.00 14.33 ?  68  TYR   A HB3  1 
ATOM   1056 H HD1  . TYR   A 1 68  ? 36.601 2.535   0.957   1.00 17.54 ?  68  TYR   A HD1  1 
ATOM   1057 H HD2  . TYR   A 1 68  ? 38.294 1.016   4.245   1.00 18.00 ?  68  TYR   A HD2  1 
ATOM   1058 H HE1  . TYR   A 1 68  ? 36.695 0.486   -0.059  1.00 19.07 ?  68  TYR   A HE1  1 
ATOM   1059 H HE2  . TYR   A 1 68  ? 38.390 -1.073  3.213   1.00 18.67 ?  68  TYR   A HE2  1 
ATOM   1060 H HH   . TYR   A 1 68  ? 37.964 -2.262  1.382   1.00 20.99 ?  68  TYR   A HH   1 
ATOM   1061 N N    . ILE   A 1 69  ? 38.083 4.931   0.700   1.00 10.69 ?  69  ILE   A N    1 
ATOM   1062 C CA   . ILE   A 1 69  ? 38.211 4.920   -0.756  1.00 10.90 ?  69  ILE   A CA   1 
ATOM   1063 C C    . ILE   A 1 69  ? 39.539 5.533   -1.190  1.00 10.85 ?  69  ILE   A C    1 
ATOM   1064 O O    . ILE   A 1 69  ? 40.182 5.046   -2.126  1.00 11.25 ?  69  ILE   A O    1 
ATOM   1065 C CB   . ILE   A 1 69  ? 37.010 5.631   -1.414  1.00 11.69 ?  69  ILE   A CB   1 
ATOM   1066 C CG1  . ILE   A 1 69  ? 35.698 4.888   -1.138  1.00 12.32 ?  69  ILE   A CG1  1 
ATOM   1067 C CG2  . ILE   A 1 69  ? 37.244 5.813   -2.916  1.00 13.14 ?  69  ILE   A CG2  1 
ATOM   1068 C CD1  . ILE   A 1 69  ? 35.532 3.601   -1.918  1.00 12.80 ?  69  ILE   A CD1  1 
ATOM   1069 H H    . ILE   A 1 69  ? 37.473 5.458   0.999   1.00 12.84 ?  69  ILE   A H    1 
ATOM   1070 H HA   . ILE   A 1 69  ? 38.205 3.998   -1.056  1.00 13.08 ?  69  ILE   A HA   1 
ATOM   1071 H HB   . ILE   A 1 69  ? 36.937 6.510   -1.019  1.00 14.03 ?  69  ILE   A HB   1 
ATOM   1072 H HG12 . ILE   A 1 69  ? 35.661 4.667   -0.193  1.00 14.79 ?  69  ILE   A HG12 1 
ATOM   1073 H HG13 . ILE   A 1 69  ? 34.959 5.471   -1.366  1.00 14.79 ?  69  ILE   A HG13 1 
ATOM   1074 H HG21 . ILE   A 1 69  ? 36.394 6.013   -3.344  1.00 15.77 ?  69  ILE   A HG21 1 
ATOM   1075 H HG22 . ILE   A 1 69  ? 37.860 6.552   -3.054  1.00 15.77 ?  69  ILE   A HG22 1 
ATOM   1076 H HG23 . ILE   A 1 69  ? 37.614 4.998   -3.284  1.00 15.77 ?  69  ILE   A HG23 1 
ATOM   1077 H HD11 . ILE   A 1 69  ? 34.744 3.139   -1.593  1.00 15.36 ?  69  ILE   A HD11 1 
ATOM   1078 H HD12 . ILE   A 1 69  ? 35.425 3.813   -2.859  1.00 15.36 ?  69  ILE   A HD12 1 
ATOM   1079 H HD13 . ILE   A 1 69  ? 36.316 3.047   -1.789  1.00 15.36 ?  69  ILE   A HD13 1 
ATOM   1080 N N    . ALA   A 1 70  ? 39.961 6.615   -0.536  1.00 11.22 ?  70  ALA   A N    1 
ATOM   1081 C CA   . ALA   A 1 70  ? 41.234 7.225   -0.896  1.00 12.16 ?  70  ALA   A CA   1 
ATOM   1082 C C    . ALA   A 1 70  ? 42.384 6.239   -0.731  1.00 12.26 ?  70  ALA   A C    1 
ATOM   1083 O O    . ALA   A 1 70  ? 43.346 6.271   -1.503  1.00 14.08 ?  70  ALA   A O    1 
ATOM   1084 C CB   . ALA   A 1 70  ? 41.474 8.477   -0.052  1.00 12.66 ?  70  ALA   A CB   1 
ATOM   1085 H H    . ALA   A 1 70  ? 39.535 7.005   0.099   1.00 13.47 ?  70  ALA   A H    1 
ATOM   1086 H HA   . ALA   A 1 70  ? 41.201 7.496   -1.827  1.00 14.59 ?  70  ALA   A HA   1 
ATOM   1087 H HB1  . ALA   A 1 70  ? 42.328 8.867   -0.306  1.00 15.19 ?  70  ALA   A HB1  1 
ATOM   1088 H HB2  . ALA   A 1 70  ? 40.761 9.111   -0.215  1.00 15.19 ?  70  ALA   A HB2  1 
ATOM   1089 H HB3  . ALA   A 1 70  ? 41.493 8.228   0.884   1.00 15.19 ?  70  ALA   A HB3  1 
ATOM   1090 N N    . THR   A 1 71  ? 42.289 5.343   0.248   1.00 11.71 ?  71  THR   A N    1 
ATOM   1091 C CA   . THR   A 1 71  ? 43.345 4.366   0.496   1.00 13.30 ?  71  THR   A CA   1 
ATOM   1092 C C    . THR   A 1 71  ? 43.225 3.141   -0.400  1.00 13.34 ?  71  THR   A C    1 
ATOM   1093 O O    . THR   A 1 71  ? 44.239 2.644   -0.910  1.00 15.24 ?  71  THR   A O    1 
ATOM   1094 C CB   . THR   A 1 71  ? 43.285 3.918   1.953   1.00 15.05 ?  71  THR   A CB   1 
ATOM   1095 O OG1  . THR   A 1 71  ? 43.541 5.041   2.800   1.00 16.44 ?  71  THR   A OG1  1 
ATOM   1096 C CG2  . THR   A 1 71  ? 44.301 2.810   2.229   1.00 16.47 ?  71  THR   A CG2  1 
ATOM   1097 H H    . THR   A 1 71  ? 41.621 5.273   0.780   1.00 14.06 ?  71  THR   A H    1 
ATOM   1098 H HA   . THR   A 1 71  ? 44.208 4.771   0.329   1.00 15.96 ?  71  THR   A HA   1 
ATOM   1099 H HB   . THR   A 1 71  ? 42.400 3.565   2.139   1.00 18.06 ?  71  THR   A HB   1 
ATOM   1100 H HG1  . THR   A 1 71  ? 42.962 5.631   2.665   1.00 19.73 ?  71  THR   A HG1  1 
ATOM   1101 H HG21 . THR   A 1 71  ? 44.450 2.732   3.185   1.00 19.76 ?  71  THR   A HG21 1 
ATOM   1102 H HG22 . THR   A 1 71  ? 43.977 1.959   1.893   1.00 19.76 ?  71  THR   A HG22 1 
ATOM   1103 H HG23 . THR   A 1 71  ? 45.146 3.019   1.798   1.00 19.76 ?  71  THR   A HG23 1 
ATOM   1104 N N    . ASN   A 1 72  ? 42.003 2.630   -0.585  1.00 12.42 ?  72  ASN   A N    1 
ATOM   1105 C CA   . ASN   A 1 72  ? 41.784 1.306   -1.149  1.00 12.55 ?  72  ASN   A CA   1 
ATOM   1106 C C    . ASN   A 1 72  ? 41.162 1.298   -2.532  1.00 12.95 ?  72  ASN   A C    1 
ATOM   1107 O O    . ASN   A 1 72  ? 41.171 0.246   -3.184  1.00 14.25 ?  72  ASN   A O    1 
ATOM   1108 C CB   . ASN   A 1 72  ? 40.896 0.485   -0.207  1.00 13.35 ?  72  ASN   A CB   1 
ATOM   1109 C CG   . ASN   A 1 72  ? 41.514 0.333   1.157   1.00 14.21 ?  72  ASN   A CG   1 
ATOM   1110 O OD1  . ASN   A 1 72  ? 41.055 0.928   2.131   1.00 15.84 ?  72  ASN   A OD1  1 
ATOM   1111 N ND2  . ASN   A 1 72  ? 42.576 -0.442  1.236   1.00 15.15 ?  72  ASN   A ND2  1 
ATOM   1112 H H    . ASN   A 1 72  ? 41.269 3.045   -0.388  1.00 14.91 ?  72  ASN   A H    1 
ATOM   1113 H HA   . ASN   A 1 72  ? 42.634 0.855   -1.217  1.00 15.06 ?  72  ASN   A HA   1 
ATOM   1114 H HB2  . ASN   A 1 72  ? 40.038 0.928   -0.107  1.00 16.03 ?  72  ASN   A HB2  1 
ATOM   1115 H HB3  . ASN   A 1 72  ? 40.770 -0.403  -0.582  1.00 16.03 ?  72  ASN   A HB3  1 
ATOM   1116 H HD21 . ASN   A 1 72  ? 42.970 -0.553  1.993   1.00 18.18 ?  72  ASN   A HD21 1 
ATOM   1117 H HD22 . ASN   A 1 72  ? 42.876 -0.833  0.533   1.00 18.18 ?  72  ASN   A HD22 1 
ATOM   1118 N N    . GLY   A 1 73  ? 40.609 2.413   -2.989  1.00 12.38 ?  73  GLY   A N    1 
ATOM   1119 C CA   . GLY   A 1 73  ? 39.871 2.433   -4.224  1.00 12.13 ?  73  GLY   A CA   1 
ATOM   1120 C C    . GLY   A 1 73  ? 38.479 1.856   -4.053  1.00 11.49 ?  73  GLY   A C    1 
ATOM   1121 O O    . GLY   A 1 73  ? 38.094 1.397   -2.971  1.00 12.28 ?  73  GLY   A O    1 
ATOM   1122 H H    . GLY   A 1 73  ? 40.647 3.183   -2.595  1.00 14.86 ?  73  GLY   A H    1 
ATOM   1123 H HA2  . GLY   A 1 73  ? 39.791 3.349   -4.543  1.00 14.56 ?  73  GLY   A HA2  1 
ATOM   1124 H HA3  . GLY   A 1 73  ? 40.345 1.916   -4.897  1.00 14.56 ?  73  GLY   A HA3  1 
ATOM   1125 N N    . PRO   A 1 74  ? 37.700 1.871   -5.134  1.00 11.71 ?  74  PRO   A N    1 
ATOM   1126 C CA   . PRO   A 1 74  ? 36.302 1.440   -5.050  1.00 11.91 ?  74  PRO   A CA   1 
ATOM   1127 C C    . PRO   A 1 74  ? 36.155 -0.043  -4.740  1.00 11.34 ?  74  PRO   A C    1 
ATOM   1128 O O    . PRO   A 1 74  ? 37.024 -0.870  -5.031  1.00 12.39 ?  74  PRO   A O    1 
ATOM   1129 C CB   . PRO   A 1 74  ? 35.749 1.752   -6.447  1.00 13.63 ?  74  PRO   A CB   1 
ATOM   1130 C CG   . PRO   A 1 74  ? 36.696 2.750   -7.037  1.00 16.03 ?  74  PRO   A CG   1 
ATOM   1131 C CD   . PRO   A 1 74  ? 38.037 2.401   -6.467  1.00 13.85 ?  74  PRO   A CD   1 
ATOM   1132 H HA   . PRO   A 1 74  ? 35.822 1.963   -4.386  1.00 14.29 ?  74  PRO   A HA   1 
ATOM   1133 H HB2  . PRO   A 1 74  ? 35.727 0.941   -6.977  1.00 16.36 ?  74  PRO   A HB2  1 
ATOM   1134 H HB3  . PRO   A 1 74  ? 34.857 2.132   -6.367  1.00 16.36 ?  74  PRO   A HB3  1 
ATOM   1135 H HG2  . PRO   A 1 74  ? 36.704 2.666   -8.003  1.00 19.23 ?  74  PRO   A HG2  1 
ATOM   1136 H HG3  . PRO   A 1 74  ? 36.437 3.646   -6.773  1.00 19.23 ?  74  PRO   A HG3  1 
ATOM   1137 H HD2  . PRO   A 1 74  ? 38.470 1.718   -7.006  1.00 16.63 ?  74  PRO   A HD2  1 
ATOM   1138 H HD3  . PRO   A 1 74  ? 38.588 3.198   -6.398  1.00 16.63 ?  74  PRO   A HD3  1 
ATOM   1139 N N    . LEU   A 1 75  ? 35.013 -0.368  -4.145  1.00 10.56 ?  75  LEU   A N    1 
ATOM   1140 C CA   . LEU   A 1 75  ? 34.610 -1.756  -3.998  1.00 10.33 ?  75  LEU   A CA   1 
ATOM   1141 C C    . LEU   A 1 75  ? 34.214 -2.331  -5.356  1.00 10.58 ?  75  LEU   A C    1 
ATOM   1142 O O    . LEU   A 1 75  ? 34.090 -1.617  -6.355  1.00 12.18 ?  75  LEU   A O    1 
ATOM   1143 C CB   . LEU   A 1 75  ? 33.423 -1.874  -3.039  1.00 10.51 ?  75  LEU   A CB   1 
ATOM   1144 C CG   . LEU   A 1 75  ? 33.642 -1.453  -1.586  1.00 12.24 ?  75  LEU   A CG   1 
ATOM   1145 C CD1  . LEU   A 1 75  ? 32.366 -1.653  -0.771  1.00 14.01 ?  75  LEU   A CD1  1 
ATOM   1146 C CD2  . LEU   A 1 75  ? 34.795 -2.182  -0.949  1.00 15.61 ?  75  LEU   A CD2  1 
ATOM   1147 H H    . LEU   A 1 75  ? 34.450 0.201   -3.826  1.00 12.67 ?  75  LEU   A H    1 
ATOM   1148 H HA   . LEU   A 1 75  ? 35.347 -2.270  -3.649  1.00 12.40 ?  75  LEU   A HA   1 
ATOM   1149 H HB2  . LEU   A 1 75  ? 32.699 -1.330  -3.385  1.00 12.62 ?  75  LEU   A HB2  1 
ATOM   1150 H HB3  . LEU   A 1 75  ? 33.142 -2.803  -3.025  1.00 12.62 ?  75  LEU   A HB3  1 
ATOM   1151 H HG   . LEU   A 1 75  ? 33.855 -0.507  -1.571  1.00 14.69 ?  75  LEU   A HG   1 
ATOM   1152 H HD11 . LEU   A 1 75  ? 32.532 -1.375  0.144   1.00 16.82 ?  75  LEU   A HD11 1 
ATOM   1153 H HD12 . LEU   A 1 75  ? 31.660 -1.110  -1.157  1.00 16.82 ?  75  LEU   A HD12 1 
ATOM   1154 H HD13 . LEU   A 1 75  ? 32.118 -2.587  -0.795  1.00 16.82 ?  75  LEU   A HD13 1 
ATOM   1155 H HD21 . LEU   A 1 75  ? 34.848 -1.934  -0.013  1.00 18.74 ?  75  LEU   A HD21 1 
ATOM   1156 H HD22 . LEU   A 1 75  ? 34.651 -3.137  -1.032  1.00 18.74 ?  75  LEU   A HD22 1 
ATOM   1157 H HD23 . LEU   A 1 75  ? 35.619 -1.932  -1.401  1.00 18.74 ?  75  LEU   A HD23 1 
ATOM   1158 N N    . LYS   A 1 76  ? 34.031 -3.650  -5.379  1.00 11.27 ?  76  LYS   A N    1 
ATOM   1159 C CA   . LYS   A 1 76  ? 33.427 -4.360  -6.499  1.00 11.89 ?  76  LYS   A CA   1 
ATOM   1160 C C    . LYS   A 1 76  ? 31.918 -4.446  -6.293  1.00 10.65 ?  76  LYS   A C    1 
ATOM   1161 O O    . LYS   A 1 76  ? 31.446 -4.572  -5.164  1.00 10.58 ?  76  LYS   A O    1 
ATOM   1162 C CB   . LYS   A 1 76  ? 33.971 -5.796  -6.565  1.00 13.65 ?  76  LYS   A CB   1 
ATOM   1163 C CG   . LYS   A 1 76  ? 35.481 -5.905  -6.770  1.00 15.34 ?  76  LYS   A CG   1 
ATOM   1164 C CD   . LYS   A 1 76  ? 35.996 -7.316  -6.562  1.00 16.61 ?  76  LYS   A CD   1 
ATOM   1165 C CE   . LYS   A 1 76  ? 37.499 -7.381  -6.749  1.00 18.91 ?  76  LYS   A CE   1 
ATOM   1166 N NZ   . LYS   A 1 76  ? 38.024 -8.746  -6.540  1.00 20.05 ?  76  LYS   A NZ   1 
ATOM   1167 H H    . LYS   A 1 76  ? 34.260 -4.172  -4.733  1.00 13.53 ?  76  LYS   A H    1 
ATOM   1168 H HA   . LYS   A 1 76  ? 33.618 -3.905  -7.334  1.00 14.27 ?  76  LYS   A HA   1 
ATOM   1169 H HB2  . LYS   A 1 76  ? 33.757 -6.248  -5.735  1.00 16.38 ?  76  LYS   A HB2  1 
ATOM   1170 H HB3  . LYS   A 1 76  ? 33.543 -6.255  -7.306  1.00 16.38 ?  76  LYS   A HB3  1 
ATOM   1171 H HG2  . LYS   A 1 76  ? 35.697 -5.632  -7.676  1.00 18.41 ?  76  LYS   A HG2  1 
ATOM   1172 H HG3  . LYS   A 1 76  ? 35.928 -5.322  -6.134  1.00 18.41 ?  76  LYS   A HG3  1 
ATOM   1173 H HD2  . LYS   A 1 76  ? 35.786 -7.606  -5.660  1.00 19.94 ?  76  LYS   A HD2  1 
ATOM   1174 H HD3  . LYS   A 1 76  ? 35.580 -7.908  -7.210  1.00 19.94 ?  76  LYS   A HD3  1 
ATOM   1175 H HE2  . LYS   A 1 76  ? 37.718 -7.107  -7.653  1.00 22.70 ?  76  LYS   A HE2  1 
ATOM   1176 H HE3  . LYS   A 1 76  ? 37.923 -6.792  -6.107  1.00 22.70 ?  76  LYS   A HE3  1 
ATOM   1177 H HZ1  . LYS   A 1 76  ? 38.905 -8.758  -6.656  1.00 24.06 ?  76  LYS   A HZ1  1 
ATOM   1178 H HZ2  . LYS   A 1 76  ? 37.837 -9.024  -5.714  1.00 24.06 ?  76  LYS   A HZ2  1 
ATOM   1179 H HZ3  . LYS   A 1 76  ? 37.650 -9.311  -7.122  1.00 24.06 ?  76  LYS   A HZ3  1 
ATOM   1180 N N    . VAL   A 1 77  ? 31.157 -4.417  -7.392  1.00 10.91 ?  77  VAL   A N    1 
ATOM   1181 C CA   . VAL   A 1 77  ? 29.751 -4.801  -7.300  1.00 10.76 ?  77  VAL   A CA   1 
ATOM   1182 C C    . VAL   A 1 77  ? 29.686 -6.253  -6.858  1.00 10.17 ?  77  VAL   A C    1 
ATOM   1183 O O    . VAL   A 1 77  ? 30.343 -7.123  -7.441  1.00 10.67 ?  77  VAL   A O    1 
ATOM   1184 C CB   . VAL   A 1 77  ? 29.023 -4.581  -8.634  1.00 12.07 ?  77  VAL   A CB   1 
ATOM   1185 C CG1  . VAL   A 1 77  ? 27.567 -5.019  -8.521  1.00 12.79 ?  77  VAL   A CG1  1 
ATOM   1186 C CG2  . VAL   A 1 77  ? 29.107 -3.124  -9.050  1.00 13.83 ?  77  VAL   A CG2  1 
ATOM   1187 H H    . VAL   A 1 77  ? 31.429 -4.182  -8.173  1.00 13.10 ?  77  VAL   A H    1 
ATOM   1188 H HA   . VAL   A 1 77  ? 29.320 -4.257  -6.623  1.00 12.92 ?  77  VAL   A HA   1 
ATOM   1189 H HB   . VAL   A 1 77  ? 29.453 -5.115  -9.321  1.00 14.48 ?  77  VAL   A HB   1 
ATOM   1190 H HG11 . VAL   A 1 77  ? 27.089 -4.717  -9.307  1.00 15.35 ?  77  VAL   A HG11 1 
ATOM   1191 H HG12 . VAL   A 1 77  ? 27.532 -5.986  -8.461  1.00 15.35 ?  77  VAL   A HG12 1 
ATOM   1192 H HG13 . VAL   A 1 77  ? 27.182 -4.622  -7.725  1.00 15.35 ?  77  VAL   A HG13 1 
ATOM   1193 H HG21 . VAL   A 1 77  ? 28.595 -3.001  -9.863  1.00 16.60 ?  77  VAL   A HG21 1 
ATOM   1194 H HG22 . VAL   A 1 77  ? 28.737 -2.574  -8.339  1.00 16.60 ?  77  VAL   A HG22 1 
ATOM   1195 H HG23 . VAL   A 1 77  ? 30.034 -2.888  -9.201  1.00 16.60 ?  77  VAL   A HG23 1 
ATOM   1196 N N    . GLY   A 1 78  ? 28.905 -6.520  -5.810  1.00 10.16 ?  78  GLY   A N    1 
ATOM   1197 C CA   . GLY   A 1 78  ? 28.889 -7.809  -5.154  1.00 10.48 ?  78  GLY   A CA   1 
ATOM   1198 C C    . GLY   A 1 78  ? 29.819 -7.911  -3.965  1.00 9.88  ?  78  GLY   A C    1 
ATOM   1199 O O    . GLY   A 1 78  ? 29.765 -8.918  -3.243  1.00 10.38 ?  78  GLY   A O    1 
ATOM   1200 H H    . GLY   A 1 78  ? 28.360 -5.948  -5.458  1.00 12.20 ?  78  GLY   A H    1 
ATOM   1201 H HA2  . GLY   A 1 78  ? 27.990 -7.999  -4.850  1.00 12.58 ?  78  GLY   A HA2  1 
ATOM   1202 H HA3  . GLY   A 1 78  ? 29.144 -8.490  -5.795  1.00 12.58 ?  78  GLY   A HA3  1 
ATOM   1203 N N    . GLY   A 1 79  ? 30.672 -6.909  -3.742  1.00 10.00 ?  79  GLY   A N    1 
ATOM   1204 C CA   . GLY   A 1 79  ? 31.641 -6.928  -2.671  1.00 10.28 ?  79  GLY   A CA   1 
ATOM   1205 C C    . GLY   A 1 79  ? 31.194 -6.136  -1.454  1.00 9.56  ?  79  GLY   A C    1 
ATOM   1206 O O    . GLY   A 1 79  ? 30.071 -5.630  -1.373  1.00 10.12 ?  79  GLY   A O    1 
ATOM   1207 H H    . GLY   A 1 79  ? 30.707 -6.193  -4.218  1.00 12.01 ?  79  GLY   A H    1 
ATOM   1208 H HA2  . GLY   A 1 79  ? 31.799 -7.852  -2.400  1.00 12.34 ?  79  GLY   A HA2  1 
ATOM   1209 H HA3  . GLY   A 1 79  ? 32.478 -6.560  -2.986  1.00 12.34 ?  79  GLY   A HA3  1 
ATOM   1210 N N    . SER   A 1 80  ? 32.104 -6.039  -0.486  1.00 10.33 ?  80  SER   A N    1 
ATOM   1211 C CA   . SER   A 1 80  ? 31.787 -5.412  0.786   1.00 9.74  ?  80  SER   A CA   1 
ATOM   1212 C C    . SER   A 1 80  ? 33.063 -4.964  1.480   1.00 9.80  ?  80  SER   A C    1 
ATOM   1213 O O    . SER   A 1 80  ? 34.175 -5.386  1.141   1.00 11.24 ?  80  SER   A O    1 
ATOM   1214 C CB   . SER   A 1 80  ? 31.034 -6.373  1.710   1.00 10.69 ?  80  SER   A CB   1 
ATOM   1215 O OG   . SER   A 1 80  ? 31.872 -7.423  2.168   1.00 12.57 ?  80  SER   A OG   1 
ATOM   1216 H H    . SER   A 1 80  ? 32.916 -6.315  -0.552  1.00 12.40 ?  80  SER   A H    1 
ATOM   1217 H HA   . SER   A 1 80  ? 31.233 -4.635  0.617   1.00 11.70 ?  80  SER   A HA   1 
ATOM   1218 H HB2  . SER   A 1 80  ? 30.706 -5.880  2.475   1.00 12.84 ?  80  SER   A HB2  1 
ATOM   1219 H HB3  . SER   A 1 80  ? 30.290 -6.758  1.221   1.00 12.84 ?  80  SER   A HB3  1 
ATOM   1220 H HG   . SER   A 1 80  ? 32.163 -7.862  1.510   1.00 15.09 ?  80  SER   A HG   1 
ATOM   1221 N N    . CYS   A 1 81  ? 32.878 -4.114  2.485   1.00 9.48  ?  81  CYS   A N    1 
ATOM   1222 C CA   . CYS   A 1 81  ? 33.933 -3.833  3.444   1.00 9.61  ?  81  CYS   A CA   1 
ATOM   1223 C C    . CYS   A 1 81  ? 33.295 -3.595  4.803   1.00 9.35  ?  81  CYS   A C    1 
ATOM   1224 O O    . CYS   A 1 81  ? 32.127 -3.204  4.898   1.00 10.47 ?  81  CYS   A O    1 
ATOM   1225 C CB   . CYS   A 1 81  ? 34.803 -2.644  3.021   1.00 10.42 ?  81  CYS   A CB   1 
ATOM   1226 S SG   . CYS   A 1 81  ? 33.911 -1.068  3.047   1.00 10.67 ?  81  CYS   A SG   1 
ATOM   1227 H H    . CYS   A 1 81  ? 32.141 -3.684  2.633   1.00 11.38 ?  81  CYS   A H    1 
ATOM   1228 H HA   . CYS   A 1 81  ? 34.506 -4.607  3.512   1.00 11.54 ?  81  CYS   A HA   1 
ATOM   1229 H HB2  . CYS   A 1 81  ? 35.557 -2.575  3.625   1.00 12.51 ?  81  CYS   A HB2  1 
ATOM   1230 H HB3  . CYS   A 1 81  ? 35.120 -2.794  2.113   1.00 12.51 ?  81  CYS   A HB3  1 
ATOM   1231 H HG   . CYS   A 1 81  ? 34.658 -0.188  2.704   1.00 12.80 ?  81  CYS   A HG   1 
ATOM   1232 N N    . VAL   A 1 82  ? 34.069 -3.856  5.853   1.00 9.62  ?  82  VAL   A N    1 
ATOM   1233 C CA   . VAL   A 1 82  ? 33.647 -3.621  7.226   1.00 10.34 ?  82  VAL   A CA   1 
ATOM   1234 C C    . VAL   A 1 82  ? 34.249 -2.308  7.700   1.00 10.31 ?  82  VAL   A C    1 
ATOM   1235 O O    . VAL   A 1 82  ? 35.473 -2.136  7.682   1.00 11.48 ?  82  VAL   A O    1 
ATOM   1236 C CB   . VAL   A 1 82  ? 34.071 -4.767  8.156   1.00 11.77 ?  82  VAL   A CB   1 
ATOM   1237 C CG1  . VAL   A 1 82  ? 33.629 -4.471  9.581   1.00 13.17 ?  82  VAL   A CG1  1 
ATOM   1238 C CG2  . VAL   A 1 82  ? 33.501 -6.090  7.680   1.00 12.75 ?  82  VAL   A CG2  1 
ATOM   1239 H H    . VAL   A 1 82  ? 34.868 -4.179  5.790   1.00 11.54 ?  82  VAL   A H    1 
ATOM   1240 H HA   . VAL   A 1 82  ? 32.681 -3.543  7.255   1.00 12.41 ?  82  VAL   A HA   1 
ATOM   1241 H HB   . VAL   A 1 82  ? 35.037 -4.836  8.153   1.00 14.13 ?  82  VAL   A HB   1 
ATOM   1242 H HG11 . VAL   A 1 82  ? 33.702 -5.283  10.108  1.00 15.81 ?  82  VAL   A HG11 1 
ATOM   1243 H HG12 . VAL   A 1 82  ? 34.197 -3.781  9.957   1.00 15.81 ?  82  VAL   A HG12 1 
ATOM   1244 H HG13 . VAL   A 1 82  ? 32.705 -4.171  9.570   1.00 15.81 ?  82  VAL   A HG13 1 
ATOM   1245 H HG21 . VAL   A 1 82  ? 33.750 -6.785  8.307   1.00 15.31 ?  82  VAL   A HG21 1 
ATOM   1246 H HG22 . VAL   A 1 82  ? 32.533 -6.017  7.635   1.00 15.31 ?  82  VAL   A HG22 1 
ATOM   1247 H HG23 . VAL   A 1 82  ? 33.858 -6.289  6.801   1.00 15.31 ?  82  VAL   A HG23 1 
ATOM   1248 N N    . LEU   A 1 83  ? 33.397 -1.391  8.139   1.00 10.09 ?  83  LEU   A N    1 
ATOM   1249 C CA   . LEU   A 1 83  ? 33.821 -0.126  8.719   1.00 10.11 ?  83  LEU   A CA   1 
ATOM   1250 C C    . LEU   A 1 83  ? 33.107 0.051   10.056  1.00 10.10 ?  83  LEU   A C    1 
ATOM   1251 O O    . LEU   A 1 83  ? 32.385 -0.837  10.523  1.00 10.56 ?  83  LEU   A O    1 
ATOM   1252 C CB   . LEU   A 1 83  ? 33.570 1.037   7.744   1.00 10.63 ?  83  LEU   A CB   1 
ATOM   1253 C CG   . LEU   A 1 83  ? 34.461 1.039   6.494   1.00 11.52 ?  83  LEU   A CG   1 
ATOM   1254 C CD1  . LEU   A 1 83  ? 34.016 2.088   5.496   1.00 11.91 ?  83  LEU   A CD1  1 
ATOM   1255 C CD2  . LEU   A 1 83  ? 35.935 1.235   6.856   1.00 12.40 ?  83  LEU   A CD2  1 
ATOM   1256 H H    . LEU   A 1 83  ? 32.541 -1.482  8.103   1.00 12.11 ?  83  LEU   A H    1 
ATOM   1257 H HA   . LEU   A 1 83  ? 34.772 -0.161  8.891   1.00 12.14 ?  83  LEU   A HA   1 
ATOM   1258 H HB2  . LEU   A 1 83  ? 32.648 1.001   7.441   1.00 12.76 ?  83  LEU   A HB2  1 
ATOM   1259 H HB3  . LEU   A 1 83  ? 33.721 1.875   8.211   1.00 12.76 ?  83  LEU   A HB3  1 
ATOM   1260 H HG   . LEU   A 1 83  ? 34.386 0.176   6.064   1.00 13.83 ?  83  LEU   A HG   1 
ATOM   1261 H HD11 . LEU   A 1 83  ? 34.601 2.051   4.721   1.00 14.29 ?  83  LEU   A HD11 1 
ATOM   1262 H HD12 . LEU   A 1 83  ? 33.104 1.896   5.229   1.00 14.29 ?  83  LEU   A HD12 1 
ATOM   1263 H HD13 . LEU   A 1 83  ? 34.067 2.961   5.910   1.00 14.29 ?  83  LEU   A HD13 1 
ATOM   1264 H HD21 . LEU   A 1 83  ? 36.448 1.376   6.042   1.00 14.88 ?  83  LEU   A HD21 1 
ATOM   1265 H HD22 . LEU   A 1 83  ? 36.023 2.010   7.435   1.00 14.88 ?  83  LEU   A HD22 1 
ATOM   1266 H HD23 . LEU   A 1 83  ? 36.262 0.444   7.314   1.00 14.88 ?  83  LEU   A HD23 1 
ATOM   1267 N N    . SER   A 1 84  ? 33.324 1.199   10.688  1.00 10.63 ?  84  SER   A N    1 
ATOM   1268 C CA   . SER   A 1 84  ? 32.689 1.454   11.969  1.00 10.74 ?  84  SER   A CA   1 
ATOM   1269 C C    . SER   A 1 84  ? 31.173 1.528   11.825  1.00 10.68 ?  84  SER   A C    1 
ATOM   1270 O O    . SER   A 1 84  ? 30.643 1.987   10.815  1.00 11.22 ?  84  SER   A O    1 
ATOM   1271 C CB   . SER   A 1 84  ? 33.181 2.779   12.538  1.00 12.18 ?  84  SER   A CB   1 
ATOM   1272 O OG   . SER   A 1 84  ? 32.543 3.057   13.772  1.00 12.92 ?  84  SER   A OG   1 
ATOM   1273 H H    . SER   A 1 84  ? 33.824 1.843   10.390  1.00 12.76 ?  84  SER   A H    1 
ATOM   1274 H HA   . SER   A 1 84  ? 32.915 0.743   12.582  1.00 12.89 ?  84  SER   A HA   1 
ATOM   1275 H HB2  . SER   A 1 84  ? 34.141 2.731   12.674  1.00 14.62 ?  84  SER   A HB2  1 
ATOM   1276 H HB3  . SER   A 1 84  ? 32.972 3.492   11.913  1.00 14.62 ?  84  SER   A HB3  1 
ATOM   1277 H HG   . SER   A 1 84  ? 32.826 3.781   14.086  1.00 15.51 ?  84  SER   A HG   1 
ATOM   1278 N N    . GLY   A 1 85  ? 30.473 1.107   12.871  1.00 11.40 ?  85  GLY   A N    1 
ATOM   1279 C CA   . GLY   A 1 85  ? 29.050 1.341   12.958  1.00 12.20 ?  85  GLY   A CA   1 
ATOM   1280 C C    . GLY   A 1 85  ? 28.673 2.646   13.612  1.00 11.60 ?  85  GLY   A C    1 
ATOM   1281 O O    . GLY   A 1 85  ? 27.482 2.950   13.729  1.00 12.08 ?  85  GLY   A O    1 
ATOM   1282 H H    . GLY   A 1 85  ? 30.808 0.683   13.541  1.00 13.69 ?  85  GLY   A H    1 
ATOM   1283 H HA2  . GLY   A 1 85  ? 28.675 1.332   12.063  1.00 14.64 ?  85  GLY   A HA2  1 
ATOM   1284 H HA3  . GLY   A 1 85  ? 28.644 0.628   13.464  1.00 14.64 ?  85  GLY   A HA3  1 
ATOM   1285 N N    . HIS   A 1 86  ? 29.651 3.432   14.048  1.00 11.31 ?  86  HIS   A N    1 
ATOM   1286 C CA   . HIS   A 1 86  ? 29.412 4.764   14.619  1.00 11.96 ?  86  HIS   A CA   1 
ATOM   1287 C C    . HIS   A 1 86  ? 28.424 4.631   15.771  1.00 12.65 ?  86  HIS   A C    1 
ATOM   1288 O O    . HIS   A 1 86  ? 28.612 3.756   16.633  1.00 13.85 ?  86  HIS   A O    1 
ATOM   1289 C CB   . HIS   A 1 86  ? 29.025 5.735   13.511  1.00 12.05 ?  86  HIS   A CB   1 
ATOM   1290 C CG   . HIS   A 1 86  ? 30.078 5.849   12.470  1.00 12.19 ?  86  HIS   A CG   1 
ATOM   1291 N ND1  . HIS   A 1 86  ? 31.158 6.694   12.606  1.00 13.21 ?  86  HIS   A ND1  1 
ATOM   1292 C CD2  . HIS   A 1 86  ? 30.270 5.168   11.319  1.00 12.26 ?  86  HIS   A CD2  1 
ATOM   1293 C CE1  . HIS   A 1 86  ? 31.955 6.546   11.564  1.00 12.95 ?  86  HIS   A CE1  1 
ATOM   1294 N NE2  . HIS   A 1 86  ? 31.441 5.626   10.769  1.00 12.43 ?  86  HIS   A NE2  1 
ATOM   1295 H H    . HIS   A 1 86  ? 30.481 3.219   14.037  1.00 13.58 ?  86  HIS   A H    1 
ATOM   1296 H HA   . HIS   A 1 86  ? 30.244 5.090   14.995  1.00 14.35 ?  86  HIS   A HA   1 
ATOM   1297 H HB2  . HIS   A 1 86  ? 28.209 5.431   13.084  1.00 14.47 ?  86  HIS   A HB2  1 
ATOM   1298 H HB3  . HIS   A 1 86  ? 28.883 6.622   13.893  1.00 14.47 ?  86  HIS   A HB3  1 
ATOM   1299 H HD2  . HIS   A 1 86  ? 29.713 4.512   10.965  1.00 14.72 ?  86  HIS   A HD2  1 
ATOM   1300 H HE1  . HIS   A 1 86  ? 32.741 7.018   11.404  1.00 15.54 ?  86  HIS   A HE1  1 
ATOM   1301 H HE2  . HIS   A 1 86  ? 31.781 5.361   10.022  1.00 14.92 ?  86  HIS   A HE2  1 
ATOM   1302 N N    . ASN   A 1 87  ? 27.400 5.472   15.840  1.00 13.42 ?  87  ASN   A N    1 
ATOM   1303 C CA   . ASN   A 1 87  ? 26.402 5.448   16.894  1.00 14.41 ?  87  ASN   A CA   1 
ATOM   1304 C C    . ASN   A 1 87  ? 25.282 4.453   16.626  1.00 15.60 ?  87  ASN   A C    1 
ATOM   1305 O O    . ASN   A 1 87  ? 24.332 4.397   17.412  1.00 17.93 ?  87  ASN   A O    1 
ATOM   1306 C CB   . ASN   A 1 87  ? 25.805 6.851   17.069  1.00 15.60 ?  87  ASN   A CB   1 
ATOM   1307 C CG   . ASN   A 1 87  ? 25.292 7.440   15.760  1.00 16.22 ?  87  ASN   A CG   1 
ATOM   1308 O OD1  . ASN   A 1 87  ? 25.925 7.315   14.714  1.00 16.95 ?  87  ASN   A OD1  1 
ATOM   1309 N ND2  . ASN   A 1 87  ? 24.144 8.095   15.820  1.00 17.31 ?  87  ASN   A ND2  1 
ATOM   1310 H H    . ASN   A 1 87  ? 27.256 6.090   15.263  1.00 16.10 ?  87  ASN   A H    1 
ATOM   1311 H HA   . ASN   A 1 87  ? 26.825 5.201   17.731  1.00 17.29 ?  87  ASN   A HA   1 
ATOM   1312 H HB2  . ASN   A 1 87  ? 25.058 6.803   17.693  1.00 18.72 ?  87  ASN   A HB2  1 
ATOM   1313 H HB3  . ASN   A 1 87  ? 26.487 7.443   17.423  1.00 18.72 ?  87  ASN   A HB3  1 
ATOM   1314 H HD21 . ASN   A 1 87  ? 23.816 8.449   15.110  1.00 20.78 ?  87  ASN   A HD21 1 
ATOM   1315 H HD22 . ASN   A 1 87  ? 23.728 8.169   16.570  1.00 20.78 ?  87  ASN   A HD22 1 
ATOM   1316 N N    . LEU   A 1 88  ? 25.368 3.665   15.557  1.00 14.77 ?  88  LEU   A N    1 
ATOM   1317 C CA   . LEU   A 1 88  ? 24.275 2.790   15.152  1.00 14.71 ?  88  LEU   A CA   1 
ATOM   1318 C C    . LEU   A 1 88  ? 24.507 1.319   15.465  1.00 14.34 ?  88  LEU   A C    1 
ATOM   1319 O O    . LEU   A 1 88  ? 23.536 0.576   15.639  1.00 15.46 ?  88  LEU   A O    1 
ATOM   1320 C CB   . LEU   A 1 88  ? 24.036 2.931   13.646  1.00 15.75 ?  88  LEU   A CB   1 
ATOM   1321 C CG   . LEU   A 1 88  ? 23.735 4.345   13.148  1.00 17.66 ?  88  LEU   A CG   1 
ATOM   1322 C CD1  . LEU   A 1 88  ? 23.563 4.351   11.639  1.00 18.15 ?  88  LEU   A CD1  1 
ATOM   1323 C CD2  . LEU   A 1 88  ? 22.498 4.914   13.833  1.00 19.49 ?  88  LEU   A CD2  1 
ATOM   1324 H H    . LEU   A 1 88  ? 26.061 3.625   15.050  1.00 17.72 ?  88  LEU   A H    1 
ATOM   1325 H HA   . LEU   A 1 88  ? 23.470 3.065   15.610  1.00 17.65 ?  88  LEU   A HA   1 
ATOM   1326 H HB2  . LEU   A 1 88  ? 24.823 2.623   13.176  1.00 18.90 ?  88  LEU   A HB2  1 
ATOM   1327 H HB3  . LEU   A 1 88  ? 23.276 2.378   13.406  1.00 18.90 ?  88  LEU   A HB3  1 
ATOM   1328 H HG   . LEU   A 1 88  ? 24.485 4.922   13.359  1.00 21.20 ?  88  LEU   A HG   1 
ATOM   1329 H HD11 . LEU   A 1 88  ? 23.406 5.261   11.340  1.00 21.78 ?  88  LEU   A HD11 1 
ATOM   1330 H HD12 . LEU   A 1 88  ? 24.370 4.003   11.227  1.00 21.78 ?  88  LEU   A HD12 1 
ATOM   1331 H HD13 . LEU   A 1 88  ? 22.806 3.791   11.405  1.00 21.78 ?  88  LEU   A HD13 1 
ATOM   1332 H HD21 . LEU   A 1 88  ? 22.265 5.757   13.412  1.00 23.39 ?  88  LEU   A HD21 1 
ATOM   1333 H HD22 . LEU   A 1 88  ? 21.769 4.284   13.740  1.00 23.39 ?  88  LEU   A HD22 1 
ATOM   1334 H HD23 . LEU   A 1 88  ? 22.698 5.057   14.771  1.00 23.39 ?  88  LEU   A HD23 1 
ATOM   1335 N N    . ALA   A 1 89  ? 25.761 0.886   15.530  1.00 13.27 ?  89  ALA   A N    1 
ATOM   1336 C CA   . ALA   A 1 89  ? 26.114 -0.523  15.625  1.00 12.91 ?  89  ALA   A CA   1 
ATOM   1337 C C    . ALA   A 1 89  ? 27.597 -0.576  15.945  1.00 13.37 ?  89  ALA   A C    1 
ATOM   1338 O O    . ALA   A 1 89  ? 28.301 0.427   15.835  1.00 14.17 ?  89  ALA   A O    1 
ATOM   1339 C CB   . ALA   A 1 89  ? 25.842 -1.237  14.301  1.00 12.55 ?  89  ALA   A CB   1 
ATOM   1340 H H    . ALA   A 1 89  ? 26.446 1.408   15.516  1.00 15.92 ?  89  ALA   A H    1 
ATOM   1341 H HA   . ALA   A 1 89  ? 25.609 -0.949  16.337  1.00 15.50 ?  89  ALA   A HA   1 
ATOM   1342 H HB1  . ALA   A 1 89  ? 26.104 -2.169  14.386  1.00 15.07 ?  89  ALA   A HB1  1 
ATOM   1343 H HB2  . ALA   A 1 89  ? 24.895 -1.179  14.097  1.00 15.07 ?  89  ALA   A HB2  1 
ATOM   1344 H HB3  . ALA   A 1 89  ? 26.359 -0.812  13.601  1.00 15.07 ?  89  ALA   A HB3  1 
ATOM   1345 N N    . LYS   A 1 90  ? 28.084 -1.754  16.329  1.00 13.79 ?  90  LYS   A N    1 
ATOM   1346 C CA   . LYS   A 1 90  ? 29.528 -1.898  16.474  1.00 14.42 ?  90  LYS   A CA   1 
ATOM   1347 C C    . LYS   A 1 90  ? 30.221 -1.708  15.128  1.00 13.50 ?  90  LYS   A C    1 
ATOM   1348 O O    . LYS   A 1 90  ? 31.152 -0.897  14.997  1.00 14.77 ?  90  LYS   A O    1 
ATOM   1349 C CB   . LYS   A 1 90  ? 29.872 -3.254  17.095  1.00 17.06 ?  90  LYS   A CB   1 
ATOM   1350 C CG   . LYS   A 1 90  ? 31.353 -3.410  17.413  1.00 20.99 ?  90  LYS   A CG   1 
ATOM   1351 C CD   . LYS   A 1 90  ? 31.604 -4.638  18.275  1.00 25.13 ?  90  LYS   A CD   1 
ATOM   1352 C CE   . LYS   A 1 90  ? 33.023 -4.667  18.825  1.00 28.18 ?  90  LYS   A CE   1 
ATOM   1353 N NZ   . LYS   A 1 90  ? 34.031 -5.011  17.788  1.00 30.01 ?  90  LYS   A NZ   1 
ATOM   1354 H H    . LYS   A 1 90  ? 27.619 -2.455  16.503  1.00 16.55 ?  90  LYS   A H    1 
ATOM   1355 H HA   . LYS   A 1 90  ? 29.853 -1.209  17.072  1.00 17.31 ?  90  LYS   A HA   1 
ATOM   1356 H HB2  . LYS   A 1 90  ? 29.375 -3.354  17.925  1.00 20.48 ?  90  LYS   A HB2  1 
ATOM   1357 H HB3  . LYS   A 1 90  ? 29.622 -3.957  16.477  1.00 20.48 ?  90  LYS   A HB3  1 
ATOM   1358 H HG2  . LYS   A 1 90  ? 31.850 -3.511  16.587  1.00 25.20 ?  90  LYS   A HG2  1 
ATOM   1359 H HG3  . LYS   A 1 90  ? 31.661 -2.629  17.899  1.00 25.20 ?  90  LYS   A HG3  1 
ATOM   1360 H HD2  . LYS   A 1 90  ? 30.989 -4.634  19.026  1.00 30.16 ?  90  LYS   A HD2  1 
ATOM   1361 H HD3  . LYS   A 1 90  ? 31.471 -5.437  17.740  1.00 30.16 ?  90  LYS   A HD3  1 
ATOM   1362 H HE2  . LYS   A 1 90  ? 33.243 -3.791  19.180  1.00 33.82 ?  90  LYS   A HE2  1 
ATOM   1363 H HE3  . LYS   A 1 90  ? 33.076 -5.332  19.530  1.00 33.82 ?  90  LYS   A HE3  1 
ATOM   1364 H HZ1  . LYS   A 1 90  ? 34.843 -5.047  18.152  1.00 36.02 ?  90  LYS   A HZ1  1 
ATOM   1365 H HZ2  . LYS   A 1 90  ? 33.841 -5.804  17.430  1.00 36.02 ?  90  LYS   A HZ2  1 
ATOM   1366 H HZ3  . LYS   A 1 90  ? 34.030 -4.396  17.146  1.00 36.02 ?  90  LYS   A HZ3  1 
ATOM   1367 N N    . HIS   A 1 91  ? 29.749 -2.424  14.108  1.00 11.63 ?  91  HIS   A N    1 
ATOM   1368 C CA   . HIS   A 1 91  ? 30.316 -2.397  12.773  1.00 11.17 ?  91  HIS   A CA   1 
ATOM   1369 C C    . HIS   A 1 91  ? 29.220 -2.121  11.759  1.00 10.20 ?  91  HIS   A C    1 
ATOM   1370 O O    . HIS   A 1 91  ? 28.055 -2.484  11.959  1.00 10.94 ?  91  HIS   A O    1 
ATOM   1371 C CB   . HIS   A 1 91  ? 30.915 -3.764  12.399  1.00 13.60 ?  91  HIS   A CB   1 
ATOM   1372 C CG   . HIS   A 1 91  ? 31.894 -4.295  13.397  1.00 17.99 ?  91  HIS   A CG   1 
ATOM   1373 N ND1  . HIS   A 1 91  ? 33.167 -3.787  13.535  1.00 20.15 ?  91  HIS   A ND1  1 
ATOM   1374 C CD2  . HIS   A 1 91  ? 31.792 -5.301  14.299  1.00 19.93 ?  91  HIS   A CD2  1 
ATOM   1375 C CE1  . HIS   A 1 91  ? 33.806 -4.452  14.481  1.00 20.88 ?  91  HIS   A CE1  1 
ATOM   1376 N NE2  . HIS   A 1 91  ? 32.993 -5.377  14.961  1.00 21.19 ?  91  HIS   A NE2  1 
ATOM   1377 H H    . HIS   A 1 91  ? 29.077 -2.969  14.178  1.00 13.96 ?  91  HIS   A H    1 
ATOM   1378 H HA   . HIS   A 1 91  ? 31.002 -1.723  12.709  1.00 13.41 ?  91  HIS   A HA   1 
ATOM   1379 H HB2  . HIS   A 1 91  ? 30.199 -4.415  12.321  1.00 16.33 ?  91  HIS   A HB2  1 
ATOM   1380 H HB3  . HIS   A 1 91  ? 31.378 -3.684  11.550  1.00 16.33 ?  91  HIS   A HB3  1 
ATOM   1381 H HD1  . HIS   A 1 91  ? 33.497 -3.138  13.075  1.00 24.19 ?  91  HIS   A HD1  1 
ATOM   1382 H HD2  . HIS   A 1 91  ? 31.052 -5.840  14.446  1.00 23.92 ?  91  HIS   A HD2  1 
ATOM   1383 H HE1  . HIS   A 1 91  ? 34.682 -4.292  14.762  1.00 25.06 ?  91  HIS   A HE1  1 
ATOM   1384 N N    . CYS   A 1 92  ? 29.619 -1.513  10.645  1.00 9.90  ?  92  CYS   A N    1 
ATOM   1385 C CA   . CYS   A 1 92  ? 28.779 -1.430  9.460   1.00 9.86  ?  92  CYS   A CA   1 
ATOM   1386 C C    . CYS   A 1 92  ? 29.420 -2.250  8.351   1.00 9.25  ?  92  CYS   A C    1 
ATOM   1387 O O    . CYS   A 1 92  ? 30.575 -2.004  7.977   1.00 10.00 ?  92  CYS   A O    1 
ATOM   1388 C CB   . CYS   A 1 92  ? 28.571 0.014   9.002   1.00 10.43 ?  92  CYS   A CB   1 
ATOM   1389 S SG   . CYS   A 1 92  ? 27.537 0.128   7.510   1.00 9.83  ?  92  CYS   A SG   1 
ATOM   1390 H H    . CYS   A 1 92  ? 30.386 -1.129  10.554  1.00 11.88 ?  92  CYS   A H    1 
ATOM   1391 H HA   . CYS   A 1 92  ? 27.912 -1.812  9.658   1.00 11.84 ?  92  CYS   A HA   1 
ATOM   1392 H HB2  . CYS   A 1 92  ? 28.131 0.513   9.708   1.00 12.52 ?  92  CYS   A HB2  1 
ATOM   1393 H HB3  . CYS   A 1 92  ? 29.431 0.412   8.799   1.00 12.52 ?  92  CYS   A HB3  1 
ATOM   1394 H HG   . CYS   A 1 92  ? 27.402 1.281   7.215   1.00 11.80 ?  92  CYS   A HG   1 
ATOM   1395 N N    . LEU   A 1 93  ? 28.675 -3.227  7.845   1.00 9.10  ?  93  LEU   A N    1 
ATOM   1396 C CA   . LEU   A 1 93  ? 29.070 -3.986  6.667   1.00 8.82  ?  93  LEU   A CA   1 
ATOM   1397 C C    . LEU   A 1 93  ? 28.468 -3.288  5.453   1.00 8.41  ?  93  LEU   A C    1 
ATOM   1398 O O    . LEU   A 1 93  ? 27.253 -3.351  5.225   1.00 8.74  ?  93  LEU   A O    1 
ATOM   1399 C CB   . LEU   A 1 93  ? 28.586 -5.431  6.776   1.00 9.23  ?  93  LEU   A CB   1 
ATOM   1400 C CG   . LEU   A 1 93  ? 28.964 -6.326  5.597   1.00 9.64  ?  93  LEU   A CG   1 
ATOM   1401 C CD1  . LEU   A 1 93  ? 30.468 -6.582  5.584   1.00 10.82 ?  93  LEU   A CD1  1 
ATOM   1402 C CD2  . LEU   A 1 93  ? 28.192 -7.651  5.630   1.00 10.50 ?  93  LEU   A CD2  1 
ATOM   1403 H H    . LEU   A 1 93  ? 27.920 -3.471  8.178   1.00 10.93 ?  93  LEU   A H    1 
ATOM   1404 H HA   . LEU   A 1 93  ? 30.035 -3.984  6.588   1.00 10.59 ?  93  LEU   A HA   1 
ATOM   1405 H HB2  . LEU   A 1 93  ? 28.966 -5.822  7.581   1.00 11.08 ?  93  LEU   A HB2  1 
ATOM   1406 H HB3  . LEU   A 1 93  ? 27.618 -5.427  6.845   1.00 11.08 ?  93  LEU   A HB3  1 
ATOM   1407 H HG   . LEU   A 1 93  ? 28.738 -5.875  4.776   1.00 11.57 ?  93  LEU   A HG   1 
ATOM   1408 H HD11 . LEU   A 1 93  ? 30.683 -7.204  4.875   1.00 12.99 ?  93  LEU   A HD11 1 
ATOM   1409 H HD12 . LEU   A 1 93  ? 30.934 -5.741  5.439   1.00 12.99 ?  93  LEU   A HD12 1 
ATOM   1410 H HD13 . LEU   A 1 93  ? 30.738 -6.957  6.443   1.00 12.99 ?  93  LEU   A HD13 1 
ATOM   1411 H HD21 . LEU   A 1 93  ? 28.464 -8.191  4.867   1.00 12.60 ?  93  LEU   A HD21 1 
ATOM   1412 H HD22 . LEU   A 1 93  ? 28.396 -8.120  6.453   1.00 12.60 ?  93  LEU   A HD22 1 
ATOM   1413 H HD23 . LEU   A 1 93  ? 27.243 -7.465  5.579   1.00 12.60 ?  93  LEU   A HD23 1 
ATOM   1414 N N    . HIS   A 1 94  ? 29.316 -2.591  4.699   1.00 8.45  ?  94  HIS   A N    1 
ATOM   1415 C CA   . HIS   A 1 94  ? 28.889 -1.917  3.478   1.00 8.35  ?  94  HIS   A CA   1 
ATOM   1416 C C    . HIS   A 1 94  ? 28.891 -2.951  2.365   1.00 8.44  ?  94  HIS   A C    1 
ATOM   1417 O O    . HIS   A 1 94  ? 29.954 -3.467  2.010   1.00 10.01 ?  94  HIS   A O    1 
ATOM   1418 C CB   . HIS   A 1 94  ? 29.847 -0.775  3.145   1.00 8.72  ?  94  HIS   A CB   1 
ATOM   1419 C CG   . HIS   A 1 94  ? 29.843 0.318   4.160   1.00 8.73  ?  94  HIS   A CG   1 
ATOM   1420 N ND1  . HIS   A 1 94  ? 28.966 1.381   4.110   1.00 9.01  ?  94  HIS   A ND1  1 
ATOM   1421 C CD2  . HIS   A 1 94  ? 30.586 0.487   5.277   1.00 9.46  ?  94  HIS   A CD2  1 
ATOM   1422 C CE1  . HIS   A 1 94  ? 29.184 2.162   5.152   1.00 9.19  ?  94  HIS   A CE1  1 
ATOM   1423 N NE2  . HIS   A 1 94  ? 30.161 1.644   5.875   1.00 9.60  ?  94  HIS   A NE2  1 
ATOM   1424 H H    . HIS   A 1 94  ? 30.155 -2.491  4.873   1.00 10.14 ?  94  HIS   A H    1 
ATOM   1425 H HA   . HIS   A 1 94  ? 27.989 -1.567  3.585   1.00 10.02 ?  94  HIS   A HA   1 
ATOM   1426 H HB2  . HIS   A 1 94  ? 30.744 -1.128  3.088   1.00 10.47 ?  94  HIS   A HB2  1 
ATOM   1427 H HB3  . HIS   A 1 94  ? 29.584 -0.390  2.292   1.00 10.47 ?  94  HIS   A HB3  1 
ATOM   1428 H HD2  . HIS   A 1 94  ? 31.260 -0.074  5.580   1.00 11.36 ?  94  HIS   A HD2  1 
ATOM   1429 H HE1  . HIS   A 1 94  ? 28.720 2.947   5.342   1.00 11.03 ?  94  HIS   A HE1  1 
ATOM   1430 H HE2  . HIS   A 1 94  ? 30.478 1.983   6.598   1.00 11.53 ?  94  HIS   A HE2  1 
ATOM   1431 N N    . VAL   A 1 95  ? 27.718 -3.271  1.822   1.00 7.90  ?  95  VAL   A N    1 
ATOM   1432 C CA   . VAL   A 1 95  ? 27.574 -4.304  0.797   1.00 8.26  ?  95  VAL   A CA   1 
ATOM   1433 C C    . VAL   A 1 95  ? 27.024 -3.664  -0.464  1.00 7.97  ?  95  VAL   A C    1 
ATOM   1434 O O    . VAL   A 1 95  ? 26.023 -2.940  -0.406  1.00 8.88  ?  95  VAL   A O    1 
ATOM   1435 C CB   . VAL   A 1 95  ? 26.644 -5.447  1.249   1.00 8.95  ?  95  VAL   A CB   1 
ATOM   1436 C CG1  . VAL   A 1 95  ? 26.539 -6.496  0.153   1.00 9.94  ?  95  VAL   A CG1  1 
ATOM   1437 C CG2  . VAL   A 1 95  ? 27.151 -6.064  2.533   1.00 9.31  ?  95  VAL   A CG2  1 
ATOM   1438 H H    . VAL   A 1 95  ? 26.970 -2.899  2.036   1.00 9.48  ?  95  VAL   A H    1 
ATOM   1439 H HA   . VAL   A 1 95  ? 28.441 -4.681  0.593   1.00 9.92  ?  95  VAL   A HA   1 
ATOM   1440 H HB   . VAL   A 1 95  ? 25.759 -5.095  1.414   1.00 10.75 ?  95  VAL   A HB   1 
ATOM   1441 H HG11 . VAL   A 1 95  ? 26.130 -7.301  0.520   1.00 11.93 ?  95  VAL   A HG11 1 
ATOM   1442 H HG12 . VAL   A 1 95  ? 25.987 -6.155  -0.570  1.00 11.93 ?  95  VAL   A HG12 1 
ATOM   1443 H HG13 . VAL   A 1 95  ? 27.426 -6.707  -0.179  1.00 11.93 ?  95  VAL   A HG13 1 
ATOM   1444 H HG21 . VAL   A 1 95  ? 26.597 -6.828  2.757   1.00 11.17 ?  95  VAL   A HG21 1 
ATOM   1445 H HG22 . VAL   A 1 95  ? 28.070 -6.347  2.407   1.00 11.17 ?  95  VAL   A HG22 1 
ATOM   1446 H HG23 . VAL   A 1 95  ? 27.102 -5.401  3.240   1.00 11.17 ?  95  VAL   A HG23 1 
ATOM   1447 N N    . VAL   A 1 96  ? 27.650 -3.949  -1.602  1.00 8.21  ?  96  VAL   A N    1 
ATOM   1448 C CA   . VAL   A 1 96  ? 27.241 -3.384  -2.883  1.00 8.77  ?  96  VAL   A CA   1 
ATOM   1449 C C    . VAL   A 1 96  ? 26.429 -4.427  -3.642  1.00 9.04  ?  96  VAL   A C    1 
ATOM   1450 O O    . VAL   A 1 96  ? 26.980 -5.361  -4.235  1.00 10.04 ?  96  VAL   A O    1 
ATOM   1451 C CB   . VAL   A 1 96  ? 28.437 -2.915  -3.709  1.00 9.38  ?  96  VAL   A CB   1 
ATOM   1452 C CG1  . VAL   A 1 96  ? 27.938 -2.267  -4.984  1.00 9.60  ?  96  VAL   A CG1  1 
ATOM   1453 C CG2  . VAL   A 1 96  ? 29.296 -1.948  -2.906  1.00 10.16 ?  96  VAL   A CG2  1 
ATOM   1454 H H    . VAL   A 1 96  ? 28.336 -4.470  -1.659  1.00 9.85  ?  96  VAL   A H    1 
ATOM   1455 H HA   . VAL   A 1 96  ? 26.673 -2.616  -2.725  1.00 10.53 ?  96  VAL   A HA   1 
ATOM   1456 H HB   . VAL   A 1 96  ? 28.986 -3.678  -3.951  1.00 11.26 ?  96  VAL   A HB   1 
ATOM   1457 H HG11 . VAL   A 1 96  ? 28.682 -1.802  -5.407  1.00 11.52 ?  96  VAL   A HG11 1 
ATOM   1458 H HG12 . VAL   A 1 96  ? 27.599 -2.950  -5.576  1.00 11.52 ?  96  VAL   A HG12 1 
ATOM   1459 H HG13 . VAL   A 1 96  ? 27.241 -1.633  -4.761  1.00 11.52 ?  96  VAL   A HG13 1 
ATOM   1460 H HG21 . VAL   A 1 96  ? 29.996 -1.595  -3.472  1.00 12.20 ?  96  VAL   A HG21 1 
ATOM   1461 H HG22 . VAL   A 1 96  ? 28.734 -1.222  -2.583  1.00 12.20 ?  96  VAL   A HG22 1 
ATOM   1462 H HG23 . VAL   A 1 96  ? 29.683 -2.419  -2.151  1.00 12.20 ?  96  VAL   A HG23 1 
ATOM   1463 N N    . GLY   A 1 97  ? 25.111 -4.272  -3.648  1.00 9.28  ?  97  GLY   A N    1 
ATOM   1464 C CA   . GLY   A 1 97  ? 24.285 -5.029  -4.554  1.00 9.66  ?  97  GLY   A CA   1 
ATOM   1465 C C    . GLY   A 1 97  ? 24.286 -4.379  -5.924  1.00 9.97  ?  97  GLY   A C    1 
ATOM   1466 O O    . GLY   A 1 97  ? 24.580 -3.186  -6.063  1.00 10.84 ?  97  GLY   A O    1 
ATOM   1467 H H    . GLY   A 1 97  ? 24.674 -3.732  -3.132  1.00 11.13 ?  97  GLY   A H    1 
ATOM   1468 H HA2  . GLY   A 1 97  ? 24.627 -5.932  -4.623  1.00 11.60 ?  97  GLY   A HA2  1 
ATOM   1469 H HA3  . GLY   A 1 97  ? 23.373 -5.062  -4.220  1.00 11.60 ?  97  GLY   A HA3  1 
ATOM   1470 N N    . PRO   A 1 98  ? 23.949 -5.138  -6.965  1.00 9.98  ?  98  PRO   A N    1 
ATOM   1471 C CA   . PRO   A 1 98  ? 23.841 -4.535  -8.297  1.00 11.28 ?  98  PRO   A CA   1 
ATOM   1472 C C    . PRO   A 1 98  ? 22.731 -3.495  -8.345  1.00 11.31 ?  98  PRO   A C    1 
ATOM   1473 O O    . PRO   A 1 98  ? 21.656 -3.669  -7.766  1.00 11.41 ?  98  PRO   A O    1 
ATOM   1474 C CB   . PRO   A 1 98  ? 23.530 -5.734  -9.202  1.00 11.69 ?  98  PRO   A CB   1 
ATOM   1475 C CG   . PRO   A 1 98  ? 22.892 -6.740  -8.284  1.00 11.85 ?  98  PRO   A CG   1 
ATOM   1476 C CD   . PRO   A 1 98  ? 23.621 -6.576  -6.977  1.00 10.64 ?  98  PRO   A CD   1 
ATOM   1477 H HA   . PRO   A 1 98  ? 24.685 -4.135  -8.559  1.00 13.54 ?  98  PRO   A HA   1 
ATOM   1478 H HB2  . PRO   A 1 98  ? 22.910 -5.464  -9.897  1.00 14.03 ?  98  PRO   A HB2  1 
ATOM   1479 H HB3  . PRO   A 1 98  ? 24.349 -6.083  -9.580  1.00 14.03 ?  98  PRO   A HB3  1 
ATOM   1480 H HG2  . PRO   A 1 98  ? 21.951 -6.536  -8.178  1.00 14.22 ?  98  PRO   A HG2  1 
ATOM   1481 H HG3  . PRO   A 1 98  ? 23.019 -7.631  -8.638  1.00 14.22 ?  98  PRO   A HG3  1 
ATOM   1482 H HD2  . PRO   A 1 98  ? 23.037 -6.800  -6.232  1.00 12.77 ?  98  PRO   A HD2  1 
ATOM   1483 H HD3  . PRO   A 1 98  ? 24.430 -7.112  -6.965  1.00 12.77 ?  98  PRO   A HD3  1 
ATOM   1484 N N    . ASN   A 1 99  ? 23.001 -2.398  -9.046  1.00 12.57 ?  99  ASN   A N    1 
ATOM   1485 C CA   . ASN   A 1 99  ? 22.024 -1.337  -9.261  1.00 13.68 ?  99  ASN   A CA   1 
ATOM   1486 C C    . ASN   A 1 99  ? 21.450 -1.518  -10.662 1.00 15.00 ?  99  ASN   A C    1 
ATOM   1487 O O    . ASN   A 1 99  ? 22.147 -1.311  -11.662 1.00 16.69 ?  99  ASN   A O    1 
ATOM   1488 C CB   . ASN   A 1 99  ? 22.670 0.037   -9.086  1.00 14.62 ?  99  ASN   A CB   1 
ATOM   1489 C CG   . ASN   A 1 99  ? 21.653 1.181   -9.072  1.00 15.30 ?  99  ASN   A CG   1 
ATOM   1490 O OD1  . ASN   A 1 99  ? 20.634 1.131   -9.761  1.00 15.91 ?  99  ASN   A OD1  1 
ATOM   1491 N ND2  . ASN   A 1 99  ? 21.940 2.221   -8.291  1.00 15.95 ?  99  ASN   A ND2  1 
ATOM   1492 H H    . ASN   A 1 99  ? 23.766 -2.239  -9.402  1.00 15.08 ?  99  ASN   A H    1 
ATOM   1493 H HA   . ASN   A 1 99  ? 21.304 -1.423  -8.608  1.00 16.42 ?  99  ASN   A HA   1 
ATOM   1494 H HB2  . ASN   A 1 99  ? 23.156 0.058   -8.248  1.00 17.54 ?  99  ASN   A HB2  1 
ATOM   1495 H HB3  . ASN   A 1 99  ? 23.279 0.189   -9.826  1.00 17.54 ?  99  ASN   A HB3  1 
ATOM   1496 H HD21 . ASN   A 1 99  ? 21.403 2.890   -8.248  1.00 19.14 ?  99  ASN   A HD21 1 
ATOM   1497 H HD22 . ASN   A 1 99  ? 22.665 2.221   -7.826  1.00 19.14 ?  99  ASN   A HD22 1 
ATOM   1498 N N    . VAL   A 1 100 ? 20.181 -1.928  -10.725 1.00 15.58 ?  100 VAL   A N    1 
ATOM   1499 C CA   . VAL   A 1 100 ? 19.527 -2.150  -12.009 1.00 17.63 ?  100 VAL   A CA   1 
ATOM   1500 C C    . VAL   A 1 100 ? 19.445 -0.856  -12.803 1.00 18.19 ?  100 VAL   A C    1 
ATOM   1501 O O    . VAL   A 1 100 ? 19.502 -0.871  -14.038 1.00 19.37 ?  100 VAL   A O    1 
ATOM   1502 C CB   . VAL   A 1 100 ? 18.143 -2.797  -11.791 1.00 19.29 ?  100 VAL   A CB   1 
ATOM   1503 C CG1  . VAL   A 1 100 ? 17.418 -2.989  -13.116 1.00 20.21 ?  100 VAL   A CG1  1 
ATOM   1504 C CG2  . VAL   A 1 100 ? 18.297 -4.125  -11.073 1.00 20.13 ?  100 VAL   A CG2  1 
ATOM   1505 H H    . VAL   A 1 100 ? 19.676 -2.083  -10.037 1.00 18.69 ?  100 VAL   A H    1 
ATOM   1506 H HA   . VAL   A 1 100 ? 20.060 -2.771  -12.522 1.00 21.16 ?  100 VAL   A HA   1 
ATOM   1507 H HB   . VAL   A 1 100 ? 17.600 -2.214  -11.238 1.00 23.15 ?  100 VAL   A HB   1 
ATOM   1508 H HG11 . VAL   A 1 100 ? 16.638 -3.548  -12.972 1.00 24.26 ?  100 VAL   A HG11 1 
ATOM   1509 H HG12 . VAL   A 1 100 ? 17.142 -2.124  -13.459 1.00 24.26 ?  100 VAL   A HG12 1 
ATOM   1510 H HG13 . VAL   A 1 100 ? 18.018 -3.419  -13.746 1.00 24.26 ?  100 VAL   A HG13 1 
ATOM   1511 H HG21 . VAL   A 1 100 ? 17.431 -4.558  -11.022 1.00 24.16 ?  100 VAL   A HG21 1 
ATOM   1512 H HG22 . VAL   A 1 100 ? 18.917 -4.681  -11.571 1.00 24.16 ?  100 VAL   A HG22 1 
ATOM   1513 H HG23 . VAL   A 1 100 ? 18.640 -3.962  -10.181 1.00 24.16 ?  100 VAL   A HG23 1 
ATOM   1514 N N    . ASN   A 1 101 ? 19.315 0.281   -12.122 1.00 19.76 ?  101 ASN   A N    1 
ATOM   1515 C CA   . ASN   A 1 101 ? 19.287 1.560   -12.822 1.00 21.73 ?  101 ASN   A CA   1 
ATOM   1516 C C    . ASN   A 1 101 ? 20.654 1.963   -13.379 1.00 23.35 ?  101 ASN   A C    1 
ATOM   1517 O O    . ASN   A 1 101 ? 20.749 3.003   -14.044 1.00 25.36 ?  101 ASN   A O    1 
ATOM   1518 C CB   . ASN   A 1 101 ? 18.678 2.624   -11.906 1.00 21.85 ?  101 ASN   A CB   1 
ATOM   1519 C CG   . ASN   A 1 101 ? 17.310 2.210   -11.378 1.00 21.56 ?  101 ASN   A CG   1 
ATOM   1520 O OD1  . ASN   A 1 101 ? 16.468 1.707   -12.128 1.00 22.18 ?  101 ASN   A OD1  1 
ATOM   1521 N ND2  . ASN   A 1 101 ? 17.089 2.397   -10.082 1.00 21.30 ?  101 ASN   A ND2  1 
ATOM   1522 H H    . ASN   A 1 101 ? 19.237 0.339   -11.267 1.00 23.72 ?  101 ASN   A H    1 
ATOM   1523 H HA   . ASN   A 1 101 ? 18.696 1.474   -13.580 1.00 26.08 ?  101 ASN   A HA   1 
ATOM   1524 H HB2  . ASN   A 1 101 ? 19.262 2.774   -11.148 1.00 26.22 ?  101 ASN   A HB2  1 
ATOM   1525 H HB3  . ASN   A 1 101 ? 18.569 3.452   -12.408 1.00 26.22 ?  101 ASN   A HB3  1 
ATOM   1526 H HD21 . ASN   A 1 101 ? 16.331 2.179   -9.740  1.00 25.57 ?  101 ASN   A HD21 1 
ATOM   1527 H HD22 . ASN   A 1 101 ? 17.698 2.750   -9.589  1.00 25.57 ?  101 ASN   A HD22 1 
ATOM   1528 N N    . LYS   A 1 102 ? 21.694 1.157   -13.142 1.00 24.44 ?  102 LYS   A N    1 
ATOM   1529 C CA   . LYS   A 1 102 ? 22.980 1.280   -13.818 1.00 25.46 ?  102 LYS   A CA   1 
ATOM   1530 C C    . LYS   A 1 102 ? 23.235 0.137   -14.794 1.00 25.54 ?  102 LYS   A C    1 
ATOM   1531 O O    . LYS   A 1 102 ? 24.317 0.076   -15.385 1.00 26.16 ?  102 LYS   A O    1 
ATOM   1532 C CB   . LYS   A 1 102 ? 24.124 1.322   -12.795 1.00 27.07 ?  102 LYS   A CB   1 
ATOM   1533 C CG   . LYS   A 1 102 ? 24.048 2.470   -11.802 1.00 28.37 ?  102 LYS   A CG   1 
ATOM   1534 C CD   . LYS   A 1 102 ? 25.196 2.410   -10.798 1.00 29.93 ?  102 LYS   A CD   1 
ATOM   1535 C CE   . LYS   A 1 102 ? 25.131 3.562   -9.804  1.00 31.32 ?  102 LYS   A CE   1 
ATOM   1536 N NZ   . LYS   A 1 102 ? 26.211 3.480   -8.778  1.00 32.00 ?  102 LYS   A NZ   1 
ATOM   1537 H H    . LYS   A 1 102 ? 21.674 0.504   -12.580 1.00 29.33 ?  102 LYS   A H    1 
ATOM   1538 H HA   . LYS   A 1 102 ? 22.996 2.111   -14.314 1.00 30.56 ?  102 LYS   A HA   1 
ATOM   1539 H HB2  . LYS   A 1 102 ? 24.118 0.495   -12.288 1.00 32.48 ?  102 LYS   A HB2  1 
ATOM   1540 H HB3  . LYS   A 1 102 ? 24.965 1.404   -13.274 1.00 32.48 ?  102 LYS   A HB3  1 
ATOM   1541 H HG2  . LYS   A 1 102 ? 24.105 3.311   -12.281 1.00 34.04 ?  102 LYS   A HG2  1 
ATOM   1542 H HG3  . LYS   A 1 102 ? 23.212 2.415   -11.314 1.00 34.04 ?  102 LYS   A HG3  1 
ATOM   1543 H HD2  . LYS   A 1 102 ? 25.144 1.577   -10.302 1.00 35.92 ?  102 LYS   A HD2  1 
ATOM   1544 H HD3  . LYS   A 1 102 ? 26.040 2.465   -11.273 1.00 35.92 ?  102 LYS   A HD3  1 
ATOM   1545 H HE2  . LYS   A 1 102 ? 25.231 4.400   -10.283 1.00 37.59 ?  102 LYS   A HE2  1 
ATOM   1546 H HE3  . LYS   A 1 102 ? 24.275 3.539   -9.347  1.00 37.59 ?  102 LYS   A HE3  1 
ATOM   1547 H HZ1  . LYS   A 1 102 ? 26.147 4.164   -8.213  1.00 38.40 ?  102 LYS   A HZ1  1 
ATOM   1548 H HZ2  . LYS   A 1 102 ? 26.138 2.719   -8.320  1.00 38.40 ?  102 LYS   A HZ2  1 
ATOM   1549 H HZ3  . LYS   A 1 102 ? 27.008 3.503   -9.173  1.00 38.40 ?  102 LYS   A HZ3  1 
ATOM   1550 N N    A GLY   A 1 103 ? 22.282 -0.776  -14.965 0.88 25.47 ?  103 GLY   A N    1 
ATOM   1551 N N    B GLY   A 1 103 ? 22.274 -0.766  -14.975 0.12 26.07 ?  103 GLY   A N    1 
ATOM   1552 C CA   A GLY   A 1 103 ? 22.461 -1.895  -15.871 0.88 25.10 ?  103 GLY   A CA   1 
ATOM   1553 C CA   B GLY   A 1 103 ? 22.443 -1.871  -15.896 0.12 26.24 ?  103 GLY   A CA   1 
ATOM   1554 C C    A GLY   A 1 103 ? 23.308 -3.027  -15.336 0.88 24.76 ?  103 GLY   A C    1 
ATOM   1555 C C    B GLY   A 1 103 ? 23.328 -2.984  -15.392 0.12 26.19 ?  103 GLY   A C    1 
ATOM   1556 O O    A GLY   A 1 103 ? 23.800 -3.843  -16.122 0.88 26.04 ?  103 GLY   A O    1 
ATOM   1557 O O    B GLY   A 1 103 ? 23.905 -3.714  -16.204 0.12 26.58 ?  103 GLY   A O    1 
ATOM   1558 H H    A GLY   A 1 103 ? 21.522 -0.768  -14.565 0.88 30.57 ?  103 GLY   A H    1 
ATOM   1559 H H    B GLY   A 1 103 ? 21.518 -0.761  -14.570 0.12 31.28 ?  103 GLY   A H    1 
ATOM   1560 H HA2  A GLY   A 1 103 ? 21.590 -2.255  -16.098 0.88 30.12 ?  103 GLY   A HA2  1 
ATOM   1561 H HA2  B GLY   A 1 103 ? 21.572 -2.244  -16.106 0.12 31.49 ?  103 GLY   A HA2  1 
ATOM   1562 H HA3  A GLY   A 1 103 ? 22.872 -1.570  -16.689 0.88 30.12 ?  103 GLY   A HA3  1 
ATOM   1563 H HA3  B GLY   A 1 103 ? 22.835 -1.541  -16.718 0.12 31.49 ?  103 GLY   A HA3  1 
ATOM   1564 N N    A GLU   A 1 104 ? 23.486 -3.116  -14.023 0.88 22.58 ?  104 GLU   A N    1 
ATOM   1565 N N    B GLU   A 1 104 ? 23.457 -3.142  -14.079 0.12 25.49 ?  104 GLU   A N    1 
ATOM   1566 C CA   A GLU   A 1 104 ? 24.379 -4.109  -13.444 0.88 21.06 ?  104 GLU   A CA   1 
ATOM   1567 C CA   B GLU   A 1 104 ? 24.366 -4.127  -13.517 0.12 24.77 ?  104 GLU   A CA   1 
ATOM   1568 C C    A GLU   A 1 104 ? 23.699 -5.474  -13.339 0.88 21.33 ?  104 GLU   A C    1 
ATOM   1569 C C    B GLU   A 1 104 ? 23.697 -5.492  -13.395 0.12 24.74 ?  104 GLU   A C    1 
ATOM   1570 O O    A GLU   A 1 104 ? 22.481 -5.582  -13.168 0.88 22.11 ?  104 GLU   A O    1 
ATOM   1571 O O    B GLU   A 1 104 ? 22.480 -5.603  -13.226 0.12 24.63 ?  104 GLU   A O    1 
ATOM   1572 C CB   A GLU   A 1 104 ? 24.900 -3.616  -12.090 0.88 19.67 ?  104 GLU   A CB   1 
ATOM   1573 C CB   B GLU   A 1 104 ? 24.893 -3.652  -12.162 0.12 24.12 ?  104 GLU   A CB   1 
ATOM   1574 C CG   A GLU   A 1 104 ? 25.831 -2.410  -12.265 0.88 19.48 ?  104 GLU   A CG   1 
ATOM   1575 C CG   B GLU   A 1 104 ? 25.818 -2.446  -12.281 0.12 23.70 ?  104 GLU   A CG   1 
ATOM   1576 C CD   A GLU   A 1 104 ? 26.168 -1.645  -10.997 0.88 18.61 ?  104 GLU   A CD   1 
ATOM   1577 C CD   B GLU   A 1 104 ? 26.119 -1.795  -10.944 0.12 23.38 ?  104 GLU   A CD   1 
ATOM   1578 O OE1  A GLU   A 1 104 ? 25.580 -1.908  -9.929  0.88 17.44 ?  104 GLU   A OE1  1 
ATOM   1579 O OE1  B GLU   A 1 104 ? 25.510 -2.196  -9.931  0.12 23.27 ?  104 GLU   A OE1  1 
ATOM   1580 O OE2  A GLU   A 1 104 ? 27.040 -0.751  -11.094 0.88 19.34 -1 104 GLU   A OE2  1 
ATOM   1581 O OE2  B GLU   A 1 104 ? 26.968 -0.879  -10.908 0.12 23.40 -1 104 GLU   A OE2  1 
ATOM   1582 H H    A GLU   A 1 104 ? 23.102 -2.607  -13.449 0.88 27.09 ?  104 GLU   A H    1 
ATOM   1583 H H    B GLU   A 1 104 ? 23.030 -2.679  -13.488 0.12 30.59 ?  104 GLU   A H    1 
ATOM   1584 H HA   A GLU   A 1 104 ? 25.144 -4.210  -14.031 0.88 25.27 ?  104 GLU   A HA   1 
ATOM   1585 H HA   B GLU   A 1 104 ? 25.124 -4.224  -14.110 0.12 29.72 ?  104 GLU   A HA   1 
ATOM   1586 H HB2  A GLU   A 1 104 ? 24.151 -3.351  -11.536 0.88 23.61 ?  104 GLU   A HB2  1 
ATOM   1587 H HB2  B GLU   A 1 104 ? 24.144 -3.401  -11.600 0.12 28.95 ?  104 GLU   A HB2  1 
ATOM   1588 H HB3  A GLU   A 1 104 ? 25.400 -4.331  -11.664 0.88 23.61 ?  104 GLU   A HB3  1 
ATOM   1589 H HB3  B GLU   A 1 104 ? 25.393 -4.372  -11.747 0.12 28.95 ?  104 GLU   A HB3  1 
ATOM   1590 H HG2  A GLU   A 1 104 ? 26.666 -2.720  -12.642 0.88 23.38 ?  104 GLU   A HG2  1 
ATOM   1591 H HG2  B GLU   A 1 104 ? 26.661 -2.732  -12.670 0.12 28.45 ?  104 GLU   A HG2  1 
ATOM   1592 H HG3  A GLU   A 1 104 ? 25.409 -1.781  -12.867 0.88 23.38 ?  104 GLU   A HG3  1 
ATOM   1593 H HG3  B GLU   A 1 104 ? 25.400 -1.784  -12.857 0.12 28.45 ?  104 GLU   A HG3  1 
ATOM   1594 N N    A ASP   A 1 105 ? 24.515 -6.521  -13.444 0.88 22.12 ?  105 ASP   A N    1 
ATOM   1595 N N    B ASP   A 1 105 ? 24.520 -6.535  -13.484 0.12 24.98 ?  105 ASP   A N    1 
ATOM   1596 C CA   A ASP   A 1 105 ? 24.025 -7.889  -13.573 0.88 23.56 ?  105 ASP   A CA   1 
ATOM   1597 C CA   B ASP   A 1 105 ? 24.031 -7.906  -13.554 0.12 25.31 ?  105 ASP   A CA   1 
ATOM   1598 C C    A ASP   A 1 105 ? 23.347 -8.338  -12.283 0.88 21.21 ?  105 ASP   A C    1 
ATOM   1599 C C    B ASP   A 1 105 ? 23.321 -8.286  -12.261 0.12 24.65 ?  105 ASP   A C    1 
ATOM   1600 O O    A ASP   A 1 105 ? 23.984 -8.399  -11.229 0.88 19.15 ?  105 ASP   A O    1 
ATOM   1601 O O    B ASP   A 1 105 ? 23.901 -8.197  -11.174 0.12 24.49 ?  105 ASP   A O    1 
ATOM   1602 C CB   A ASP   A 1 105 ? 25.207 -8.799  -13.901 0.88 27.19 ?  105 ASP   A CB   1 
ATOM   1603 C CB   B ASP   A 1 105 ? 25.217 -8.839  -13.801 0.12 26.27 ?  105 ASP   A CB   1 
ATOM   1604 C CG   A ASP   A 1 105 ? 24.793 -10.232 -14.147 0.88 30.42 ?  105 ASP   A CG   1 
ATOM   1605 C CG   B ASP   A 1 105 ? 24.794 -10.280 -13.990 0.12 27.14 ?  105 ASP   A CG   1 
ATOM   1606 O OD1  A ASP   A 1 105 ? 23.575 -10.495 -14.213 0.88 31.15 ?  105 ASP   A OD1  1 
ATOM   1607 O OD1  B ASP   A 1 105 ? 23.585 -10.520 -14.189 0.12 27.43 ?  105 ASP   A OD1  1 
ATOM   1608 O OD2  A ASP   A 1 105 ? 25.691 -11.094 -14.277 0.88 32.15 -1 105 ASP   A OD2  1 
ATOM   1609 O OD2  B ASP   A 1 105 ? 25.668 -11.171 -13.938 0.12 27.56 -1 105 ASP   A OD2  1 
ATOM   1610 H H    A ASP   A 1 105 ? 25.374 -6.460  -13.442 0.88 26.55 ?  105 ASP   A H    1 
ATOM   1611 H H    B ASP   A 1 105 ? 25.375 -6.472  -13.499 0.12 29.97 ?  105 ASP   A H    1 
ATOM   1612 H HA   A ASP   A 1 105 ? 23.383 -7.940  -14.295 0.88 28.27 ?  105 ASP   A HA   1 
ATOM   1613 H HA   B ASP   A 1 105 ? 23.409 -8.000  -14.292 0.12 30.38 ?  105 ASP   A HA   1 
ATOM   1614 H HB2  A ASP   A 1 105 ? 25.646 -8.469  -14.703 0.88 32.64 ?  105 ASP   A HB2  1 
ATOM   1615 H HB2  B ASP   A 1 105 ? 25.682 -8.555  -14.606 0.12 31.53 ?  105 ASP   A HB2  1 
ATOM   1616 H HB3  A ASP   A 1 105 ? 25.830 -8.789  -13.157 0.88 32.64 ?  105 ASP   A HB3  1 
ATOM   1617 H HB3  B ASP   A 1 105 ? 25.820 -8.796  -13.041 0.12 31.53 ?  105 ASP   A HB3  1 
ATOM   1618 N N    A ILE   A 1 106 ? 22.059 -8.676  -12.369 0.88 21.21 ?  106 ILE   A N    1 
ATOM   1619 N N    B ILE   A 1 106 ? 22.059 -8.713  -12.378 0.12 24.15 ?  106 ILE   A N    1 
ATOM   1620 C CA   A ILE   A 1 106 ? 21.313 -9.075  -11.182 0.88 20.80 ?  106 ILE   A CA   1 
ATOM   1621 C CA   B ILE   A 1 106 ? 21.309 -9.131  -11.199 0.12 23.65 ?  106 ILE   A CA   1 
ATOM   1622 C C    A ILE   A 1 106 ? 21.853 -10.363 -10.586 0.88 19.57 ?  106 ILE   A C    1 
ATOM   1623 C C    B ILE   A 1 106 ? 21.862 -10.421 -10.609 0.12 23.08 ?  106 ILE   A C    1 
ATOM   1624 O O    A ILE   A 1 106 ? 21.648 -10.619 -9.396  0.88 18.85 ?  106 ILE   A O    1 
ATOM   1625 O O    B ILE   A 1 106 ? 21.642 -10.698 -9.424  0.12 22.93 ?  106 ILE   A O    1 
ATOM   1626 C CB   A ILE   A 1 106 ? 19.798 -9.157  -11.487 0.88 22.69 ?  106 ILE   A CB   1 
ATOM   1627 C CB   B ILE   A 1 106 ? 19.799 -9.242  -11.499 0.12 23.89 ?  106 ILE   A CB   1 
ATOM   1628 C CG1  A ILE   A 1 106 ? 18.983 -9.205  -10.191 0.88 23.60 ?  106 ILE   A CG1  1 
ATOM   1629 C CG1  B ILE   A 1 106 ? 18.985 -9.203  -10.202 0.12 23.99 ?  106 ILE   A CG1  1 
ATOM   1630 C CG2  A ILE   A 1 106 ? 19.488 -10.376 -12.337 0.88 23.53 ?  106 ILE   A CG2  1 
ATOM   1631 C CG2  B ILE   A 1 106 ? 19.490 -10.528 -12.245 0.12 24.04 ?  106 ILE   A CG2  1 
ATOM   1632 C CD1  A ILE   A 1 106 ? 19.135 -7.973  -9.323  0.88 24.08 ?  106 ILE   A CD1  1 
ATOM   1633 C CD1  B ILE   A 1 106 ? 19.179 -7.939  -9.392  0.12 23.97 ?  106 ILE   A CD1  1 
ATOM   1634 H H    A ILE   A 1 106 ? 21.609 -8.680  -13.091 0.88 25.45 ?  106 ILE   A H    1 
ATOM   1635 H H    B ILE   A 1 106 ? 21.623 -8.757  -13.116 0.12 28.98 ?  106 ILE   A H    1 
ATOM   1636 H HA   A ILE   A 1 106 ? 21.440 -8.396  -10.510 0.88 24.97 ?  106 ILE   A HA   1 
ATOM   1637 H HA   B ILE   A 1 106 ? 21.423 -8.449  -10.526 0.12 28.38 ?  106 ILE   A HA   1 
ATOM   1638 H HB   A ILE   A 1 106 ? 19.543 -8.361  -11.981 0.88 27.23 ?  106 ILE   A HB   1 
ATOM   1639 H HB   B ILE   A 1 106 ? 19.532 -8.491  -12.052 0.12 28.68 ?  106 ILE   A HB   1 
ATOM   1640 H HG12 A ILE   A 1 106 ? 18.043 -9.289  -10.416 0.88 28.32 ?  106 ILE   A HG12 1 
ATOM   1641 H HG12 B ILE   A 1 106 ? 18.041 -9.269  -10.420 0.12 28.80 ?  106 ILE   A HG12 1 
ATOM   1642 H HG13 A ILE   A 1 106 ? 19.266 -9.971  -9.669  0.88 28.32 ?  106 ILE   A HG13 1 
ATOM   1643 H HG13 B ILE   A 1 106 ? 19.245 -9.953  -9.646  0.12 28.80 ?  106 ILE   A HG13 1 
ATOM   1644 H HG21 A ILE   A 1 106 ? 18.599 -10.279 -12.712 0.88 28.24 ?  106 ILE   A HG21 1 
ATOM   1645 H HG21 B ILE   A 1 106 ? 18.616 -10.451 -12.660 0.12 28.85 ?  106 ILE   A HG21 1 
ATOM   1646 H HG22 A ILE   A 1 106 ? 20.144 -10.436 -13.046 0.88 28.24 ?  106 ILE   A HG22 1 
ATOM   1647 H HG22 B ILE   A 1 106 ? 20.168 -10.667 -12.922 0.12 28.85 ?  106 ILE   A HG22 1 
ATOM   1648 H HG23 A ILE   A 1 106 ? 19.529 -11.167 -11.778 0.88 28.24 ?  106 ILE   A HG23 1 
ATOM   1649 H HG23 B ILE   A 1 106 ? 19.492 -11.268 -11.617 0.12 28.85 ?  106 ILE   A HG23 1 
ATOM   1650 H HD11 A ILE   A 1 106 ? 18.415 -7.952  -8.677  0.88 28.89 ?  106 ILE   A HD11 1 
ATOM   1651 H HD11 B ILE   A 1 106 ? 18.425 -7.830  -8.795  0.12 28.76 ?  106 ILE   A HD11 1 
ATOM   1652 H HD12 A ILE   A 1 106 ? 19.990 -8.014  -8.862  0.88 28.89 ?  106 ILE   A HD12 1 
ATOM   1653 H HD12 B ILE   A 1 106 ? 19.999 -8.016  -8.878  0.12 28.76 ?  106 ILE   A HD12 1 
ATOM   1654 H HD13 A ILE   A 1 106 ? 19.100 -7.184  -9.886  0.88 28.89 ?  106 ILE   A HD13 1 
ATOM   1655 H HD13 B ILE   A 1 106 ? 19.236 -7.183  -9.998  0.12 28.76 ?  106 ILE   A HD13 1 
ATOM   1656 N N    A GLN   A 1 107 ? 22.557 -11.178 -11.383 0.88 20.30 ?  107 GLN   A N    1 
ATOM   1657 N N    B GLN   A 1 107 ? 22.579 -11.221 -11.403 0.12 22.80 ?  107 GLN   A N    1 
ATOM   1658 C CA   A GLN   A 1 107 ? 23.184 -12.383 -10.847 0.88 22.51 ?  107 GLN   A CA   1 
ATOM   1659 C CA   B GLN   A 1 107 ? 23.218 -12.415 -10.863 0.12 22.60 ?  107 GLN   A CA   1 
ATOM   1660 C C    A GLN   A 1 107 ? 24.159 -12.044 -9.728  0.88 20.34 ?  107 GLN   A C    1 
ATOM   1661 C C    B GLN   A 1 107 ? 24.229 -12.073 -9.776  0.12 19.91 ?  107 GLN   A C    1 
ATOM   1662 O O    A GLN   A 1 107 ? 24.389 -12.865 -8.832  0.88 21.62 ?  107 GLN   A O    1 
ATOM   1663 O O    B GLN   A 1 107 ? 24.564 -12.939 -8.961  0.12 20.24 ?  107 GLN   A O    1 
ATOM   1664 C CB   A GLN   A 1 107 ? 23.896 -13.147 -11.969 0.88 26.69 ?  107 GLN   A CB   1 
ATOM   1665 C CB   B GLN   A 1 107 ? 23.901 -13.207 -11.982 0.12 24.97 ?  107 GLN   A CB   1 
ATOM   1666 C CG   A GLN   A 1 107 ? 23.027 -13.397 -13.197 0.88 31.19 ?  107 GLN   A CG   1 
ATOM   1667 C CG   B GLN   A 1 107 ? 23.015 -13.475 -13.191 0.12 27.20 ?  107 GLN   A CG   1 
ATOM   1668 C CD   A GLN   A 1 107 ? 21.759 -14.160 -12.873 0.88 34.73 ?  107 GLN   A CD   1 
ATOM   1669 C CD   B GLN   A 1 107 ? 21.684 -14.096 -12.818 0.12 28.98 ?  107 GLN   A CD   1 
ATOM   1670 O OE1  A GLN   A 1 107 ? 21.796 -15.200 -12.214 0.88 36.05 ?  107 GLN   A OE1  1 
ATOM   1671 O OE1  B GLN   A 1 107 ? 21.624 -15.043 -12.034 0.12 29.63 ?  107 GLN   A OE1  1 
ATOM   1672 N NE2  A GLN   A 1 107 ? 20.625 -13.642 -13.330 0.88 35.83 ?  107 GLN   A NE2  1 
ATOM   1673 N NE2  B GLN   A 1 107 ? 20.606 -13.558 -13.377 0.12 29.59 ?  107 GLN   A NE2  1 
ATOM   1674 H H    A GLN   A 1 107 ? 22.685 -11.055 -12.224 0.88 24.36 ?  107 GLN   A H    1 
ATOM   1675 H H    B GLN   A 1 107 ? 22.706 -11.093 -12.243 0.12 27.36 ?  107 GLN   A H    1 
ATOM   1676 H HA   A GLN   A 1 107 ? 22.504 -12.968 -10.481 0.88 27.01 ?  107 GLN   A HA   1 
ATOM   1677 H HA   B GLN   A 1 107 ? 22.541 -12.984 -10.468 0.12 27.12 ?  107 GLN   A HA   1 
ATOM   1678 H HB2  A GLN   A 1 107 ? 24.672 -12.640 -12.259 0.88 32.04 ?  107 GLN   A HB2  1 
ATOM   1679 H HB2  B GLN   A 1 107 ? 24.675 -12.711 -12.290 0.12 29.96 ?  107 GLN   A HB2  1 
ATOM   1680 H HB3  A GLN   A 1 107 ? 24.181 -14.015 -11.636 0.88 32.04 ?  107 GLN   A HB3  1 
ATOM   1681 H HB3  B GLN   A 1 107 ? 24.181 -14.066 -11.630 0.12 29.96 ?  107 GLN   A HB3  1 
ATOM   1682 H HG2  A GLN   A 1 107 ? 22.773 -12.547 -13.588 0.88 37.43 ?  107 GLN   A HG2  1 
ATOM   1683 H HG2  B GLN   A 1 107 ? 22.837 -12.640 -13.648 0.12 32.65 ?  107 GLN   A HG2  1 
ATOM   1684 H HG3  A GLN   A 1 107 ? 23.534 -13.916 -13.841 0.88 37.43 ?  107 GLN   A HG3  1 
ATOM   1685 H HG3  B GLN   A 1 107 ? 23.475 -14.086 -13.788 0.12 32.65 ?  107 GLN   A HG3  1 
ATOM   1686 H HE21 A GLN   A 1 107 ? 20.637 -12.913 -13.786 0.88 43.00 ?  107 GLN   A HE21 1 
ATOM   1687 H HE21 B GLN   A 1 107 ? 20.688 -12.895 -13.919 0.12 35.51 ?  107 GLN   A HE21 1 
ATOM   1688 H HE22 A GLN   A 1 107 ? 19.878 -14.039 -13.173 0.88 43.00 ?  107 GLN   A HE22 1 
ATOM   1689 H HE22 B GLN   A 1 107 ? 19.827 -13.874 -13.198 0.12 35.51 ?  107 GLN   A HE22 1 
ATOM   1690 N N    . LEU   A 1 108 ? 24.718 -10.830 -9.744  1.00 17.07 ?  108 LEU   A N    1 
ATOM   1691 C CA   . LEU   A 1 108 ? 25.631 -10.405 -8.693  1.00 14.09 ?  108 LEU   A CA   1 
ATOM   1692 C C    . LEU   A 1 108 ? 24.933 -10.245 -7.352  1.00 12.32 ?  108 LEU   A C    1 
ATOM   1693 O O    . LEU   A 1 108 ? 25.614 -10.094 -6.335  1.00 12.68 ?  108 LEU   A O    1 
ATOM   1694 C CB   . LEU   A 1 108 ? 26.340 -9.105  -9.094  1.00 13.70 ?  108 LEU   A CB   1 
ATOM   1695 C CG   . LEU   A 1 108 ? 27.340 -9.292  -10.237 1.00 15.34 ?  108 LEU   A CG   1 
ATOM   1696 C CD1  . LEU   A 1 108 ? 27.810 -7.957  -10.782 1.00 16.24 ?  108 LEU   A CD1  1 
ATOM   1697 C CD2  . LEU   A 1 108 ? 28.533 -10.120 -9.779  1.00 17.35 ?  108 LEU   A CD2  1 
ATOM   1698 H H    A LEU   A 1 108 ? 24.581 -10.243 -10.352 0.88 20.49 ?  108 LEU   A H    1 
ATOM   1699 H H    B LEU   A 1 108 ? 24.540 -10.226 -10.323 0.12 20.49 ?  108 LEU   A H    1 
ATOM   1700 H HA   . LEU   A 1 108 ? 26.307 -11.088 -8.577  1.00 16.92 ?  108 LEU   A HA   1 
ATOM   1701 H HB2  . LEU   A 1 108 ? 25.676 -8.460  -9.383  1.00 16.45 ?  108 LEU   A HB2  1 
ATOM   1702 H HB3  . LEU   A 1 108 ? 26.824 -8.762  -8.329  1.00 16.45 ?  108 LEU   A HB3  1 
ATOM   1703 H HG   . LEU   A 1 108 ? 26.907 -9.772  -10.961 1.00 18.41 ?  108 LEU   A HG   1 
ATOM   1704 H HD11 . LEU   A 1 108 ? 28.410 -8.113  -11.530 1.00 19.49 ?  108 LEU   A HD11 1 
ATOM   1705 H HD12 . LEU   A 1 108 ? 27.040 -7.447  -11.078 1.00 19.49 ?  108 LEU   A HD12 1 
ATOM   1706 H HD13 . LEU   A 1 108 ? 28.276 -7.475  -10.081 1.00 19.49 ?  108 LEU   A HD13 1 
ATOM   1707 H HD21 . LEU   A 1 108 ? 29.231 -10.063 -10.447 1.00 20.83 ?  108 LEU   A HD21 1 
ATOM   1708 H HD22 . LEU   A 1 108 ? 28.852 -9.768  -8.933  1.00 20.83 ?  108 LEU   A HD22 1 
ATOM   1709 H HD23 . LEU   A 1 108 ? 28.253 -11.042 -9.668  1.00 20.83 ?  108 LEU   A HD23 1 
ATOM   1710 N N    . LEU   A 1 109 ? 23.602 -10.303 -7.315  1.00 11.80 ?  109 LEU   A N    1 
ATOM   1711 C CA   . LEU   A 1 109 ? 22.905 -10.184 -6.040  1.00 11.16 ?  109 LEU   A CA   1 
ATOM   1712 C C    . LEU   A 1 109 ? 23.256 -11.336 -5.103  1.00 10.28 ?  109 LEU   A C    1 
ATOM   1713 O O    . LEU   A 1 109 ? 23.394 -11.138 -3.889  1.00 10.85 ?  109 LEU   A O    1 
ATOM   1714 C CB   . LEU   A 1 109 ? 21.402 -10.103 -6.289  1.00 11.66 ?  109 LEU   A CB   1 
ATOM   1715 C CG   . LEU   A 1 109 ? 20.519 -9.821  -5.077  1.00 11.91 ?  109 LEU   A CG   1 
ATOM   1716 C CD1  . LEU   A 1 109 ? 20.952 -8.544  -4.369  1.00 12.47 ?  109 LEU   A CD1  1 
ATOM   1717 C CD2  . LEU   A 1 109 ? 19.061 -9.729  -5.500  1.00 12.92 ?  109 LEU   A CD2  1 
ATOM   1718 H H    . LEU   A 1 109 ? 23.087 -10.416 -7.995  1.00 14.16 ?  109 LEU   A H    1 
ATOM   1719 H HA   . LEU   A 1 109 ? 23.185 -9.360  -5.614  1.00 13.40 ?  109 LEU   A HA   1 
ATOM   1720 H HB2  . LEU   A 1 109 ? 21.240 -9.392  -6.930  1.00 13.99 ?  109 LEU   A HB2  1 
ATOM   1721 H HB3  . LEU   A 1 109 ? 21.110 -10.945 -6.664  1.00 13.99 ?  109 LEU   A HB3  1 
ATOM   1722 H HG   . LEU   A 1 109 ? 20.600 -10.551 -4.449  1.00 14.29 ?  109 LEU   A HG   1 
ATOM   1723 H HD11 . LEU   A 1 109 ? 20.287 -8.301  -3.708  1.00 14.97 ?  109 LEU   A HD11 1 
ATOM   1724 H HD12 . LEU   A 1 109 ? 21.809 -8.695  -3.937  1.00 14.97 ?  109 LEU   A HD12 1 
ATOM   1725 H HD13 . LEU   A 1 109 ? 21.039 -7.829  -5.025  1.00 14.97 ?  109 LEU   A HD13 1 
ATOM   1726 H HD21 . LEU   A 1 109 ? 18.528 -9.423  -4.746  1.00 15.51 ?  109 LEU   A HD21 1 
ATOM   1727 H HD22 . LEU   A 1 109 ? 18.976 -9.104  -6.235  1.00 15.51 ?  109 LEU   A HD22 1 
ATOM   1728 H HD23 . LEU   A 1 109 ? 18.754 -10.610 -5.779  1.00 15.51 ?  109 LEU   A HD23 1 
ATOM   1729 N N    . LYS   A 1 110 ? 23.410 -12.549 -5.641  1.00 10.16 ?  110 LYS   A N    1 
ATOM   1730 C CA   . LYS   A 1 110 ? 23.794 -13.668 -4.785  1.00 10.03 ?  110 LYS   A CA   1 
ATOM   1731 C C    . LYS   A 1 110 ? 25.179 -13.444 -4.187  1.00 9.65  ?  110 LYS   A C    1 
ATOM   1732 O O    . LYS   A 1 110 ? 25.382 -13.645 -2.985  1.00 9.75  ?  110 LYS   A O    1 
ATOM   1733 C CB   . LYS   A 1 110 ? 23.716 -14.989 -5.554  1.00 10.82 ?  110 LYS   A CB   1 
ATOM   1734 C CG   . LYS   A 1 110 ? 23.924 -16.205 -4.653  1.00 11.11 ?  110 LYS   A CG   1 
ATOM   1735 C CD   . LYS   A 1 110 ? 23.688 -17.524 -5.372  1.00 11.95 ?  110 LYS   A CD   1 
ATOM   1736 C CE   . LYS   A 1 110 ? 23.790 -18.706 -4.420  1.00 12.90 ?  110 LYS   A CE   1 
ATOM   1737 N NZ   . LYS   A 1 110 ? 22.605 -18.835 -3.535  1.00 13.36 ?  110 LYS   A NZ   1 
ATOM   1738 H H    . LYS   A 1 110 ? 23.295 -12.746 -6.470  1.00 12.20 ?  110 LYS   A H    1 
ATOM   1739 H HA   . LYS   A 1 110 ? 23.159 -13.724 -4.050  1.00 12.04 ?  110 LYS   A HA   1 
ATOM   1740 H HB2  . LYS   A 1 110 ? 22.840 -15.065 -5.965  1.00 12.99 ?  110 LYS   A HB2  1 
ATOM   1741 H HB3  . LYS   A 1 110 ? 24.405 -14.997 -6.234  1.00 12.99 ?  110 LYS   A HB3  1 
ATOM   1742 H HG2  . LYS   A 1 110 ? 24.835 -16.198 -4.322  1.00 13.34 ?  110 LYS   A HG2  1 
ATOM   1743 H HG3  . LYS   A 1 110 ? 23.302 -16.152 -3.909  1.00 13.34 ?  110 LYS   A HG3  1 
ATOM   1744 H HD2  . LYS   A 1 110 ? 22.804 -17.520 -5.762  1.00 14.34 ?  110 LYS   A HD2  1 
ATOM   1745 H HD3  . LYS   A 1 110 ? 24.363 -17.631 -6.061  1.00 14.34 ?  110 LYS   A HD3  1 
ATOM   1746 H HE2  . LYS   A 1 110 ? 23.870 -19.520 -4.934  1.00 15.48 ?  110 LYS   A HE2  1 
ATOM   1747 H HE3  . LYS   A 1 110 ? 24.571 -18.589 -3.853  1.00 15.48 ?  110 LYS   A HE3  1 
ATOM   1748 H HZ1  . LYS   A 1 110 ? 22.700 -19.534 -2.996  1.00 16.03 ?  110 LYS   A HZ1  1 
ATOM   1749 H HZ2  . LYS   A 1 110 ? 22.509 -18.099 -3.042  1.00 16.03 ?  110 LYS   A HZ2  1 
ATOM   1750 H HZ3  . LYS   A 1 110 ? 21.870 -18.946 -4.028  1.00 16.03 ?  110 LYS   A HZ3  1 
ATOM   1751 N N    . SER   A 1 111 ? 26.136 -13.000 -5.006  1.00 9.95  ?  111 SER   A N    1 
ATOM   1752 C CA   . SER   A 1 111 ? 27.466 -12.691 -4.492  1.00 10.05 ?  111 SER   A CA   1 
ATOM   1753 C C    . SER   A 1 111 ? 27.398 -11.651 -3.380  1.00 9.53  ?  111 SER   A C    1 
ATOM   1754 O O    . SER   A 1 111 ? 28.103 -11.755 -2.370  1.00 10.30 ?  111 SER   A O    1 
ATOM   1755 C CB   . SER   A 1 111 ? 28.357 -12.196 -5.631  1.00 11.33 ?  111 SER   A CB   1 
ATOM   1756 O OG   . SER   A 1 111 ? 28.470 -13.178 -6.646  1.00 13.69 ?  111 SER   A OG   1 
ATOM   1757 H H    . SER   A 1 111 ? 26.035 -12.874 -5.849  1.00 11.94 ?  111 SER   A H    1 
ATOM   1758 H HA   . SER   A 1 111 ? 27.859 -13.498 -4.128  1.00 12.06 ?  111 SER   A HA   1 
ATOM   1759 H HB2  . SER   A 1 111 ? 27.959 -11.397 -6.016  1.00 13.60 ?  111 SER   A HB2  1 
ATOM   1760 H HB3  . SER   A 1 111 ? 29.233 -11.988 -5.274  1.00 13.60 ?  111 SER   A HB3  1 
ATOM   1761 H HG   . SER   A 1 111 ? 28.982 -12.888 -7.258  1.00 16.43 ?  111 SER   A HG   1 
ATOM   1762 N N    . ALA   A 1 112 ? 26.554 -10.635 -3.554  1.00 9.64  ?  112 ALA   A N    1 
ATOM   1763 C CA   . ALA   A 1 112 ? 26.409 -9.599  -2.535  1.00 9.52  ?  112 ALA   A CA   1 
ATOM   1764 C C    . ALA   A 1 112 ? 25.934 -10.197 -1.215  1.00 9.41  ?  112 ALA   A C    1 
ATOM   1765 O O    . ALA   A 1 112 ? 26.486 -9.904  -0.147  1.00 9.65  ?  112 ALA   A O    1 
ATOM   1766 C CB   . ALA   A 1 112 ? 25.450 -8.512  -3.029  1.00 10.10 ?  112 ALA   A CB   1 
ATOM   1767 H H    . ALA   A 1 112 ? 26.059 -10.516 -4.245  1.00 11.57 ?  112 ALA   A H    1 
ATOM   1768 H HA   . ALA   A 1 112 ? 27.268 -9.180  -2.378  1.00 11.42 ?  112 ALA   A HA   1 
ATOM   1769 H HB1  . ALA   A 1 112 ? 25.369 -7.820  -2.347  1.00 12.12 ?  112 ALA   A HB1  1 
ATOM   1770 H HB2  . ALA   A 1 112 ? 25.797 -8.125  -3.846  1.00 12.12 ?  112 ALA   A HB2  1 
ATOM   1771 H HB3  . ALA   A 1 112 ? 24.577 -8.905  -3.194  1.00 12.12 ?  112 ALA   A HB3  1 
ATOM   1772 N N    . TYR   A 1 113 ? 24.907 -11.050 -1.267  1.00 9.42  ?  113 TYR   A N    1 
ATOM   1773 C CA   . TYR   A 1 113 ? 24.401 -11.657 -0.041  1.00 9.21  ?  113 TYR   A CA   1 
ATOM   1774 C C    . TYR   A 1 113 ? 25.409 -12.602 0.602   1.00 8.88  ?  113 TYR   A C    1 
ATOM   1775 O O    . TYR   A 1 113 ? 25.370 -12.790 1.821   1.00 9.51  ?  113 TYR   A O    1 
ATOM   1776 C CB   . TYR   A 1 113 ? 23.090 -12.396 -0.312  1.00 9.73  ?  113 TYR   A CB   1 
ATOM   1777 C CG   . TYR   A 1 113 ? 21.863 -11.518 -0.209  1.00 9.72  ?  113 TYR   A CG   1 
ATOM   1778 C CD1  . TYR   A 1 113 ? 21.501 -10.937 1.002   1.00 9.75  ?  113 TYR   A CD1  1 
ATOM   1779 C CD2  . TYR   A 1 113 ? 21.054 -11.281 -1.314  1.00 9.83  ?  113 TYR   A CD2  1 
ATOM   1780 C CE1  . TYR   A 1 113 ? 20.366 -10.147 1.111   1.00 9.98  ?  113 TYR   A CE1  1 
ATOM   1781 C CE2  . TYR   A 1 113 ? 19.905 -10.490 -1.213  1.00 10.11 ?  113 TYR   A CE2  1 
ATOM   1782 C CZ   . TYR   A 1 113 ? 19.573 -9.928  0.002   1.00 9.77  ?  113 TYR   A CZ   1 
ATOM   1783 O OH   . TYR   A 1 113 ? 18.445 -9.146  0.134   1.00 10.71 ?  113 TYR   A OH   1 
ATOM   1784 H H    . TYR   A 1 113 ? 24.499 -11.289 -1.984  1.00 11.30 ?  113 TYR   A H    1 
ATOM   1785 H HA   . TYR   A 1 113 ? 24.218 -10.952 0.600   1.00 11.06 ?  113 TYR   A HA   1 
ATOM   1786 H HB2  . TYR   A 1 113 ? 23.113 -12.756 -1.210  1.00 11.68 ?  113 TYR   A HB2  1 
ATOM   1787 H HB3  . TYR   A 1 113 ? 22.993 -13.111 0.331   1.00 11.68 ?  113 TYR   A HB3  1 
ATOM   1788 H HD1  . TYR   A 1 113 ? 22.030 -11.084 1.754   1.00 11.71 ?  113 TYR   A HD1  1 
ATOM   1789 H HD2  . TYR   A 1 113 ? 21.270 -11.665 -2.129  1.00 11.80 ?  113 TYR   A HD2  1 
ATOM   1790 H HE1  . TYR   A 1 113 ? 20.142 -9.764  1.931   1.00 11.98 ?  113 TYR   A HE1  1 
ATOM   1791 H HE2  . TYR   A 1 113 ? 19.367 -10.337 -1.956  1.00 12.14 ?  113 TYR   A HE2  1 
ATOM   1792 H HH   . TYR   A 1 113 ? 18.052 -9.088  -0.612  1.00 12.85 ?  113 TYR   A HH   1 
ATOM   1793 N N    . GLU   A 1 114 ? 26.306 -13.213 -0.182  1.00 9.27  ?  114 GLU   A N    1 
ATOM   1794 C CA   . GLU   A 1 114 ? 27.297 -14.111 0.411   1.00 9.42  ?  114 GLU   A CA   1 
ATOM   1795 C C    . GLU   A 1 114 ? 28.149 -13.401 1.460   1.00 9.26  ?  114 GLU   A C    1 
ATOM   1796 O O    . GLU   A 1 114 ? 28.627 -14.037 2.407   1.00 9.64  ?  114 GLU   A O    1 
ATOM   1797 C CB   . GLU   A 1 114 ? 28.162 -14.746 -0.685  1.00 9.55  ?  114 GLU   A CB   1 
ATOM   1798 C CG   . GLU   A 1 114 ? 27.401 -15.803 -1.456  1.00 9.99  ?  114 GLU   A CG   1 
ATOM   1799 C CD   . GLU   A 1 114 ? 28.103 -16.330 -2.699  1.00 10.64 ?  114 GLU   A CD   1 
ATOM   1800 O OE1  . GLU   A 1 114 ? 29.055 -15.698 -3.199  1.00 10.95 ?  114 GLU   A OE1  1 
ATOM   1801 O OE2  . GLU   A 1 114 ? 27.660 -17.393 -3.193  1.00 11.77 -1 114 GLU   A OE2  1 
ATOM   1802 H H    . GLU   A 1 114 ? 26.361 -13.118 -1.040  1.00 11.12 ?  114 GLU   A H    1 
ATOM   1803 H HA   . GLU   A 1 114 ? 26.826 -14.828 0.852   1.00 11.31 ?  114 GLU   A HA   1 
ATOM   1804 H HB2  . GLU   A 1 114 ? 28.447 -14.062 -1.315  1.00 11.46 ?  114 GLU   A HB2  1 
ATOM   1805 H HB3  . GLU   A 1 114 ? 28.935 -15.169 -0.281  1.00 11.46 ?  114 GLU   A HB3  1 
ATOM   1806 H HG2  . GLU   A 1 114 ? 27.243 -16.560 -0.873  1.00 11.99 ?  114 GLU   A HG2  1 
ATOM   1807 H HG3  . GLU   A 1 114 ? 26.551 -15.429 -1.740  1.00 11.99 ?  114 GLU   A HG3  1 
ATOM   1808 N N    . ASN   A 1 115 ? 28.331 -12.082 1.329   1.00 9.24  ?  115 ASN   A N    1 
ATOM   1809 C CA   . ASN   A 1 115 ? 29.090 -11.346 2.336   1.00 9.63  ?  115 ASN   A CA   1 
ATOM   1810 C C    . ASN   A 1 115 ? 28.474 -11.486 3.722   1.00 9.33  ?  115 ASN   A C    1 
ATOM   1811 O O    . ASN   A 1 115 ? 29.190 -11.413 4.727   1.00 9.68  ?  115 ASN   A O    1 
ATOM   1812 C CB   . ASN   A 1 115 ? 29.181 -9.868  1.958   1.00 9.87  ?  115 ASN   A CB   1 
ATOM   1813 C CG   . ASN   A 1 115 ? 29.977 -9.640  0.698   1.00 10.78 ?  115 ASN   A CG   1 
ATOM   1814 O OD1  . ASN   A 1 115 ? 31.197 -9.729  0.708   1.00 13.99 ?  115 ASN   A OD1  1 
ATOM   1815 N ND2  . ASN   A 1 115 ? 29.295 -9.347  -0.393  1.00 10.29 ?  115 ASN   A ND2  1 
ATOM   1816 H H    . ASN   A 1 115 ? 28.027 -11.600 0.682   1.00 11.09 ?  115 ASN   A H    1 
ATOM   1817 H HA   . ASN   A 1 115 ? 29.986 -11.702 2.375   1.00 11.56 ?  115 ASN   A HA   1 
ATOM   1818 H HB2  . ASN   A 1 115 ? 28.284 -9.520  1.823   1.00 11.85 ?  115 ASN   A HB2  1 
ATOM   1819 H HB3  . ASN   A 1 115 ? 29.614 -9.386  2.683   1.00 11.85 ?  115 ASN   A HB3  1 
ATOM   1820 H HD21 . ASN   A 1 115 ? 29.706 -9.205  -1.133  1.00 12.35 ?  115 ASN   A HD21 1 
ATOM   1821 H HD22 . ASN   A 1 115 ? 28.434 -9.308  -0.364  1.00 12.35 ?  115 ASN   A HD22 1 
ATOM   1822 N N    . PHE   A 1 116 ? 27.149 -11.655 3.804   1.00 9.24  ?  116 PHE   A N    1 
ATOM   1823 C CA   . PHE   A 1 116 ? 26.508 -11.765 5.110   1.00 9.58  ?  116 PHE   A CA   1 
ATOM   1824 C C    . PHE   A 1 116 ? 26.992 -12.996 5.874   1.00 9.65  ?  116 PHE   A C    1 
ATOM   1825 O O    . PHE   A 1 116 ? 26.920 -13.016 7.103   1.00 9.97  ?  116 PHE   A O    1 
ATOM   1826 C CB   . PHE   A 1 116 ? 24.980 -11.896 4.976   1.00 9.66  ?  116 PHE   A CB   1 
ATOM   1827 C CG   . PHE   A 1 116 ? 24.221 -10.646 4.521   1.00 9.33  ?  116 PHE   A CG   1 
ATOM   1828 C CD1  . PHE   A 1 116 ? 24.787 -9.619  3.778   1.00 9.28  ?  116 PHE   A CD1  1 
ATOM   1829 C CD2  . PHE   A 1 116 ? 22.865 -10.547 4.849   1.00 10.00 ?  116 PHE   A CD2  1 
ATOM   1830 C CE1  . PHE   A 1 116 ? 24.014 -8.536  3.372   1.00 9.86  ?  116 PHE   A CE1  1 
ATOM   1831 C CE2  . PHE   A 1 116 ? 22.092 -9.476  4.452   1.00 10.25 ?  116 PHE   A CE2  1 
ATOM   1832 C CZ   . PHE   A 1 116 ? 22.661 -8.463  3.714   1.00 9.79  ?  116 PHE   A CZ   1 
ATOM   1833 H H    . PHE   A 1 116 ? 26.609 -11.703 3.130   1.00 11.09 ?  116 PHE   A H    1 
ATOM   1834 H HA   . PHE   A 1 116 ? 26.700 -10.973 5.635   1.00 11.49 ?  116 PHE   A HA   1 
ATOM   1835 H HB2  . PHE   A 1 116 ? 24.791 -12.599 4.331   1.00 11.60 ?  116 PHE   A HB2  1 
ATOM   1836 H HB3  . PHE   A 1 116 ? 24.622 -12.156 5.840   1.00 11.60 ?  116 PHE   A HB3  1 
ATOM   1837 H HD1  . PHE   A 1 116 ? 25.682 -9.676  3.538   1.00 11.15 ?  116 PHE   A HD1  1 
ATOM   1838 H HD2  . PHE   A 1 116 ? 22.468 -11.237 5.340   1.00 12.01 ?  116 PHE   A HD2  1 
ATOM   1839 H HE1  . PHE   A 1 116 ? 24.405 -7.857  2.877   1.00 11.83 ?  116 PHE   A HE1  1 
ATOM   1840 H HE2  . PHE   A 1 116 ? 21.193 -9.439  4.690   1.00 12.30 ?  116 PHE   A HE2  1 
ATOM   1841 H HZ   . PHE   A 1 116 ? 22.151 -7.732  3.453   1.00 11.75 ?  116 PHE   A HZ   1 
ATOM   1842 N N    . ASN   A 1 117 ? 27.429 -14.043 5.168   1.00 9.63  ?  117 ASN   A N    1 
ATOM   1843 C CA   . ASN   A 1 117 ? 27.797 -15.288 5.833   1.00 9.85  ?  117 ASN   A CA   1 
ATOM   1844 C C    . ASN   A 1 117 ? 29.062 -15.169 6.661   1.00 10.32 ?  117 ASN   A C    1 
ATOM   1845 O O    . ASN   A 1 117 ? 29.369 -16.093 7.423   1.00 11.12 ?  117 ASN   A O    1 
ATOM   1846 C CB   . ASN   A 1 117 ? 27.909 -16.408 4.804   1.00 9.97  ?  117 ASN   A CB   1 
ATOM   1847 C CG   . ASN   A 1 117 ? 26.554 -16.796 4.272   1.00 10.05 ?  117 ASN   A CG   1 
ATOM   1848 O OD1  . ASN   A 1 117 ? 25.587 -16.840 5.033   1.00 10.89 ?  117 ASN   A OD1  1 
ATOM   1849 N ND2  . ASN   A 1 117 ? 26.461 -17.052 2.978   1.00 9.94  ?  117 ASN   A ND2  1 
ATOM   1850 H H    . ASN   A 1 117 ? 27.511 -14.055 4.311   1.00 11.56 ?  117 ASN   A H    1 
ATOM   1851 H HA   . ASN   A 1 117 ? 27.077 -15.524 6.438   1.00 11.83 ?  117 ASN   A HA   1 
ATOM   1852 H HB2  . ASN   A 1 117 ? 28.458 -16.110 4.061   1.00 11.97 ?  117 ASN   A HB2  1 
ATOM   1853 H HB3  . ASN   A 1 117 ? 28.304 -17.187 5.224   1.00 11.97 ?  117 ASN   A HB3  1 
ATOM   1854 H HD21 . ASN   A 1 117 ? 25.706 -17.270 2.634   1.00 11.93 ?  117 ASN   A HD21 1 
ATOM   1855 H HD22 . ASN   A 1 117 ? 27.162 -16.996 2.477   1.00 11.93 ?  117 ASN   A HD22 1 
ATOM   1856 N N    . GLN   A 1 118 ? 29.790 -14.060 6.541   1.00 10.45 ?  118 GLN   A N    1 
ATOM   1857 C CA   . GLN   A 1 118 ? 30.970 -13.821 7.360   1.00 10.90 ?  118 GLN   A CA   1 
ATOM   1858 C C    . GLN   A 1 118 ? 30.632 -13.247 8.731   1.00 10.76 ?  118 GLN   A C    1 
ATOM   1859 O O    . GLN   A 1 118 ? 31.549 -12.954 9.509   1.00 12.35 ?  118 GLN   A O    1 
ATOM   1860 C CB   . GLN   A 1 118 ? 31.951 -12.908 6.619   1.00 11.15 ?  118 GLN   A CB   1 
ATOM   1861 C CG   . GLN   A 1 118 ? 32.431 -13.495 5.295   1.00 11.20 ?  118 GLN   A CG   1 
ATOM   1862 C CD   . GLN   A 1 118 ? 33.253 -14.762 5.473   1.00 11.37 ?  118 GLN   A CD   1 
ATOM   1863 O OE1  . GLN   A 1 118 ? 34.115 -14.838 6.357   1.00 12.19 ?  118 GLN   A OE1  1 
ATOM   1864 N NE2  . GLN   A 1 118 ? 33.003 -15.757 4.622   1.00 11.67 ?  118 GLN   A NE2  1 
ATOM   1865 H H    . GLN   A 1 118 ? 29.612 -13.421 5.988   1.00 12.54 ?  118 GLN   A H    1 
ATOM   1866 H HA   . GLN   A 1 118 ? 31.409 -14.672 7.504   1.00 13.08 ?  118 GLN   A HA   1 
ATOM   1867 H HB2  . GLN   A 1 118 ? 31.517 -12.062 6.436   1.00 13.38 ?  118 GLN   A HB2  1 
ATOM   1868 H HB3  . GLN   A 1 118 ? 32.729 -12.768 7.182   1.00 13.38 ?  118 GLN   A HB3  1 
ATOM   1869 H HG2  . GLN   A 1 118 ? 31.658 -13.709 4.746   1.00 13.44 ?  118 GLN   A HG2  1 
ATOM   1870 H HG3  . GLN   A 1 118 ? 32.982 -12.838 4.841   1.00 13.44 ?  118 GLN   A HG3  1 
ATOM   1871 H HE21 . GLN   A 1 118 ? 32.393 -15.667 4.015   1.00 14.01 ?  118 GLN   A HE21 1 
ATOM   1872 H HE22 . GLN   A 1 118 ? 33.440 -16.494 4.678   1.00 14.01 ?  118 GLN   A HE22 1 
ATOM   1873 N N    . HIS   A 1 119 ? 29.346 -13.097 9.049   1.00 10.35 ?  119 HIS   A N    1 
ATOM   1874 C CA   . HIS   A 1 119 ? 28.899 -12.495 10.300  1.00 10.89 ?  119 HIS   A CA   1 
ATOM   1875 C C    . HIS   A 1 119 ? 27.761 -13.321 10.872  1.00 10.90 ?  119 HIS   A C    1 
ATOM   1876 O O    . HIS   A 1 119 ? 26.806 -13.637 10.159  1.00 11.65 ?  119 HIS   A O    1 
ATOM   1877 C CB   . HIS   A 1 119 ? 28.440 -11.062 10.036  1.00 11.61 ?  119 HIS   A CB   1 
ATOM   1878 C CG   . HIS   A 1 119 ? 29.515 -10.246 9.419   1.00 13.03 ?  119 HIS   A CG   1 
ATOM   1879 N ND1  . HIS   A 1 119 ? 30.495 -9.641  10.171  1.00 15.52 ?  119 HIS   A ND1  1 
ATOM   1880 C CD2  . HIS   A 1 119 ? 29.846 -10.043 8.124   1.00 14.17 ?  119 HIS   A CD2  1 
ATOM   1881 C CE1  . HIS   A 1 119 ? 31.353 -9.045  9.362   1.00 15.92 ?  119 HIS   A CE1  1 
ATOM   1882 N NE2  . HIS   A 1 119 ? 30.989 -9.284  8.115   1.00 15.83 ?  119 HIS   A NE2  1 
ATOM   1883 H H    . HIS   A 1 119 ? 28.694 -13.353 8.547   1.00 12.42 ?  119 HIS   A H    1 
ATOM   1884 H HA   . HIS   A 1 119 ? 29.633 -12.482 10.940  1.00 13.07 ?  119 HIS   A HA   1 
ATOM   1885 H HB2  . HIS   A 1 119 ? 27.684 -11.081 9.431   1.00 13.94 ?  119 HIS   A HB2  1 
ATOM   1886 H HB3  . HIS   A 1 119 ? 28.190 -10.651 10.877  1.00 13.94 ?  119 HIS   A HB3  1 
ATOM   1887 H HD2  . HIS   A 1 119 ? 29.379 -10.350 7.379   1.00 17.00 ?  119 HIS   A HD2  1 
ATOM   1888 H HE1  . HIS   A 1 119 ? 32.089 -8.542  9.624   1.00 19.10 ?  119 HIS   A HE1  1 
ATOM   1889 H HE2  . HIS   A 1 119 ? 31.386 -8.986  7.411   1.00 19.01 ?  119 HIS   A HE2  1 
ATOM   1890 N N    . GLU   A 1 120 ? 27.855 -13.648 12.160  1.00 11.67 ?  120 GLU   A N    1 
ATOM   1891 C CA   . GLU   A 1 120 ? 26.902 -14.585 12.750  1.00 13.52 ?  120 GLU   A CA   1 
ATOM   1892 C C    . GLU   A 1 120 ? 25.490 -14.014 12.825  1.00 12.02 ?  120 GLU   A C    1 
ATOM   1893 O O    . GLU   A 1 120 ? 24.515 -14.770 12.702  1.00 12.35 ?  120 GLU   A O    1 
ATOM   1894 C CB   . GLU   A 1 120 ? 27.377 -15.011 14.140  1.00 18.62 ?  120 GLU   A CB   1 
ATOM   1895 C CG   . GLU   A 1 120 ? 28.559 -15.964 14.123  1.00 26.28 ?  120 GLU   A CG   1 
ATOM   1896 C CD   . GLU   A 1 120 ? 28.748 -16.671 15.450  1.00 33.70 ?  120 GLU   A CD   1 
ATOM   1897 O OE1  . GLU   A 1 120 ? 28.334 -16.112 16.489  1.00 35.67 ?  120 GLU   A OE1  1 
ATOM   1898 O OE2  . GLU   A 1 120 ? 29.300 -17.792 15.454  1.00 37.65 -1 120 GLU   A OE2  1 
ATOM   1899 H H    . GLU   A 1 120 ? 28.456 -13.355 12.705  1.00 14.01 ?  120 GLU   A H    1 
ATOM   1900 H HA   . GLU   A 1 120 ? 26.869 -15.381 12.203  1.00 16.23 ?  120 GLU   A HA   1 
ATOM   1901 H HB2  . GLU   A 1 120 ? 27.644 -14.225 14.640  1.00 22.34 ?  120 GLU   A HB2  1 
ATOM   1902 H HB3  . GLU   A 1 120 ? 26.649 -15.460 14.599  1.00 22.34 ?  120 GLU   A HB3  1 
ATOM   1903 H HG2  . GLU   A 1 120 ? 28.418 -16.640 13.441  1.00 31.54 ?  120 GLU   A HG2  1 
ATOM   1904 H HG3  . GLU   A 1 120 ? 29.370 -15.466 13.935  1.00 31.54 ?  120 GLU   A HG3  1 
ATOM   1905 N N    . VAL   A 1 121 ? 25.362 -12.705 13.054  1.00 11.42 ?  121 VAL   A N    1 
ATOM   1906 C CA   . VAL   A 1 121 ? 24.072 -12.034 13.198  1.00 11.77 ?  121 VAL   A CA   1 
ATOM   1907 C C    . VAL   A 1 121 ? 24.180 -10.653 12.559  1.00 10.72 ?  121 VAL   A C    1 
ATOM   1908 O O    . VAL   A 1 121 ? 25.157 -9.932  12.790  1.00 11.66 ?  121 VAL   A O    1 
ATOM   1909 C CB   . VAL   A 1 121 ? 23.667 -11.885 14.682  1.00 14.45 ?  121 VAL   A CB   1 
ATOM   1910 C CG1  . VAL   A 1 121 ? 22.297 -11.227 14.799  1.00 15.21 ?  121 VAL   A CG1  1 
ATOM   1911 C CG2  . VAL   A 1 121 ? 23.674 -13.219 15.401  1.00 16.75 ?  121 VAL   A CG2  1 
ATOM   1912 H H    . VAL   A 1 121 ? 26.030 -12.168 13.132  1.00 13.70 ?  121 VAL   A H    1 
ATOM   1913 H HA   . VAL   A 1 121 ? 23.387 -12.543 12.740  1.00 14.13 ?  121 VAL   A HA   1 
ATOM   1914 H HB   . VAL   A 1 121 ? 24.307 -11.310 15.125  1.00 17.35 ?  121 VAL   A HB   1 
ATOM   1915 H HG11 . VAL   A 1 121 ? 21.991 -11.298 15.717  1.00 18.25 ?  121 VAL   A HG11 1 
ATOM   1916 H HG12 . VAL   A 1 121 ? 22.371 -10.293 14.548  1.00 18.25 ?  121 VAL   A HG12 1 
ATOM   1917 H HG13 . VAL   A 1 121 ? 21.677 -11.682 14.208  1.00 18.25 ?  121 VAL   A HG13 1 
ATOM   1918 H HG21 . VAL   A 1 121 ? 23.344 -13.093 16.310  1.00 20.11 ?  121 VAL   A HG21 1 
ATOM   1919 H HG22 . VAL   A 1 121 ? 23.092 -13.840 14.930  1.00 20.11 ?  121 VAL   A HG22 1 
ATOM   1920 H HG23 . VAL   A 1 121 ? 24.577 -13.566 15.426  1.00 20.11 ?  121 VAL   A HG23 1 
ATOM   1921 N N    . LEU   A 1 122 ? 23.158 -10.261 11.790  1.00 10.42 ?  122 LEU   A N    1 
ATOM   1922 C CA   . LEU   A 1 122 ? 23.156 -8.965  11.113  1.00 10.41 ?  122 LEU   A CA   1 
ATOM   1923 C C    . LEU   A 1 122 ? 21.757 -8.377  11.090  1.00 10.13 ?  122 LEU   A C    1 
ATOM   1924 O O    . LEU   A 1 122 ? 20.767 -9.100  10.957  1.00 11.40 ?  122 LEU   A O    1 
ATOM   1925 C CB   . LEU   A 1 122 ? 23.565 -9.057  9.635   1.00 12.02 ?  122 LEU   A CB   1 
ATOM   1926 C CG   . LEU   A 1 122 ? 24.770 -9.903  9.253   1.00 11.77 ?  122 LEU   A CG   1 
ATOM   1927 C CD1  . LEU   A 1 122 ? 24.376 -11.361 9.034   1.00 12.56 ?  122 LEU   A CD1  1 
ATOM   1928 C CD2  . LEU   A 1 122 ? 25.433 -9.332  8.014   1.00 11.33 ?  122 LEU   A CD2  1 
ATOM   1929 H H    . LEU   A 1 122 ? 22.449 -10.728 11.641  1.00 12.50 ?  122 LEU   A H    1 
ATOM   1930 H HA   . LEU   A 1 122 ? 23.754 -8.347  11.568  1.00 12.50 ?  122 LEU   A HA   1 
ATOM   1931 H HB2  . LEU   A 1 122 ? 22.816 -9.410  9.140   1.00 14.43 ?  122 LEU   A HB2  1 
ATOM   1932 H HB3  . LEU   A 1 122 ? 23.755 -8.156  9.323   1.00 14.43 ?  122 LEU   A HB3  1 
ATOM   1933 H HG   . LEU   A 1 122 ? 25.427 -9.876  9.969   1.00 14.13 ?  122 LEU   A HG   1 
ATOM   1934 H HD11 . LEU   A 1 122 ? 25.154 -11.866 8.751   1.00 15.08 ?  122 LEU   A HD11 1 
ATOM   1935 H HD12 . LEU   A 1 122 ? 24.035 -11.722 9.869   1.00 15.08 ?  122 LEU   A HD12 1 
ATOM   1936 H HD13 . LEU   A 1 122 ? 23.688 -11.403 8.351   1.00 15.08 ?  122 LEU   A HD13 1 
ATOM   1937 H HD21 . LEU   A 1 122 ? 26.174 -9.905  7.752   1.00 13.60 ?  122 LEU   A HD21 1 
ATOM   1938 H HD22 . LEU   A 1 122 ? 24.782 -9.292  7.296   1.00 13.60 ?  122 LEU   A HD22 1 
ATOM   1939 H HD23 . LEU   A 1 122 ? 25.763 -8.441  8.211   1.00 13.60 ?  122 LEU   A HD23 1 
ATOM   1940 N N    . LEU   A 1 123 ? 21.697 -7.046  11.182  1.00 9.89  ?  123 LEU   A N    1 
ATOM   1941 C CA   . LEU   A 1 123 ? 20.523 -6.253  10.826  1.00 9.83  ?  123 LEU   A CA   1 
ATOM   1942 C C    . LEU   A 1 123 ? 20.754 -5.707  9.423   1.00 9.27  ?  123 LEU   A C    1 
ATOM   1943 O O    . LEU   A 1 123 ? 21.802 -5.113  9.166   1.00 10.07 ?  123 LEU   A O    1 
ATOM   1944 C CB   . LEU   A 1 123 ? 20.392 -5.088  11.807  1.00 10.23 ?  123 LEU   A CB   1 
ATOM   1945 C CG   . LEU   A 1 123 ? 19.344 -4.023  11.478  1.00 11.14 ?  123 LEU   A CG   1 
ATOM   1946 C CD1  . LEU   A 1 123 ? 17.947 -4.627  11.478  1.00 11.91 ?  123 LEU   A CD1  1 
ATOM   1947 C CD2  . LEU   A 1 123 ? 19.435 -2.858  12.459  1.00 11.94 ?  123 LEU   A CD2  1 
ATOM   1948 H H    . LEU   A 1 123 ? 22.352 -6.558  11.454  1.00 11.88 ?  123 LEU   A H    1 
ATOM   1949 H HA   . LEU   A 1 123 ? 19.715 -6.795  10.848  1.00 11.80 ?  123 LEU   A HA   1 
ATOM   1950 H HB2  . LEU   A 1 123 ? 20.163 -5.447  12.682  1.00 12.28 ?  123 LEU   A HB2  1 
ATOM   1951 H HB3  . LEU   A 1 123 ? 21.246 -4.636  11.861  1.00 12.28 ?  123 LEU   A HB3  1 
ATOM   1952 H HG   . LEU   A 1 123 ? 19.510 -3.673  10.589  1.00 13.37 ?  123 LEU   A HG   1 
ATOM   1953 H HD11 . LEU   A 1 123 ? 17.297 -3.930  11.320  1.00 14.29 ?  123 LEU   A HD11 1 
ATOM   1954 H HD12 . LEU   A 1 123 ? 17.892 -5.300  10.779  1.00 14.29 ?  123 LEU   A HD12 1 
ATOM   1955 H HD13 . LEU   A 1 123 ? 17.784 -5.043  12.343  1.00 14.29 ?  123 LEU   A HD13 1 
ATOM   1956 H HD21 . LEU   A 1 123 ? 18.760 -2.201  12.230  1.00 14.34 ?  123 LEU   A HD21 1 
ATOM   1957 H HD22 . LEU   A 1 123 ? 19.277 -3.194  13.357  1.00 14.34 ?  123 LEU   A HD22 1 
ATOM   1958 H HD23 . LEU   A 1 123 ? 20.317 -2.467  12.400  1.00 14.34 ?  123 LEU   A HD23 1 
ATOM   1959 N N    . ALA   A 1 124 ? 19.795 -5.894  8.516   1.00 9.22  ?  124 ALA   A N    1 
ATOM   1960 C CA   . ALA   A 1 124 ? 20.067 -5.586  7.119   1.00 9.44  ?  124 ALA   A CA   1 
ATOM   1961 C C    . ALA   A 1 124 ? 18.819 -5.126  6.385   1.00 9.23  ?  124 ALA   A C    1 
ATOM   1962 O O    . ALA   A 1 124 ? 17.697 -5.505  6.750   1.00 10.00 ?  124 ALA   A O    1 
ATOM   1963 C CB   . ALA   A 1 124 ? 20.641 -6.811  6.395   1.00 9.80  ?  124 ALA   A CB   1 
ATOM   1964 H H    . ALA   A 1 124 ? 19.002 -6.188  8.673   1.00 11.07 ?  124 ALA   A H    1 
ATOM   1965 H HA   . ALA   A 1 124 ? 20.739 -4.885  7.084   1.00 11.33 ?  124 ALA   A HA   1 
ATOM   1966 H HB1  . ALA   A 1 124 ? 20.823 -6.581  5.468   1.00 11.76 ?  124 ALA   A HB1  1 
ATOM   1967 H HB2  . ALA   A 1 124 ? 21.470 -7.085  6.829   1.00 11.76 ?  124 ALA   A HB2  1 
ATOM   1968 H HB3  . ALA   A 1 124 ? 19.999 -7.536  6.434   1.00 11.76 ?  124 ALA   A HB3  1 
ATOM   1969 N N    . PRO   A 1 125 ? 18.993 -4.353  5.320   1.00 9.25  ?  125 PRO   A N    1 
ATOM   1970 C CA   . PRO   A 1 125 ? 17.925 -4.116  4.353   1.00 9.92  ?  125 PRO   A CA   1 
ATOM   1971 C C    . PRO   A 1 125 ? 17.983 -5.185  3.265   1.00 9.79  ?  125 PRO   A C    1 
ATOM   1972 O O    . PRO   A 1 125 ? 18.949 -5.942  3.152   1.00 10.41 ?  125 PRO   A O    1 
ATOM   1973 C CB   . PRO   A 1 125 ? 18.340 -2.765  3.762   1.00 10.10 ?  125 PRO   A CB   1 
ATOM   1974 C CG   . PRO   A 1 125 ? 19.849 -2.901  3.671   1.00 10.39 ?  125 PRO   A CG   1 
ATOM   1975 C CD   . PRO   A 1 125 ? 20.254 -3.706  4.900   1.00 9.97  ?  125 PRO   A CD   1 
ATOM   1976 H HA   . PRO   A 1 125 ? 17.049 -4.075  4.771   1.00 11.91 ?  125 PRO   A HA   1 
ATOM   1977 H HB2  . PRO   A 1 125 ? 17.935 -2.650  2.885   1.00 12.12 ?  125 PRO   A HB2  1 
ATOM   1978 H HB3  . PRO   A 1 125 ? 18.081 -2.046  4.362   1.00 12.12 ?  125 PRO   A HB3  1 
ATOM   1979 H HG2  . PRO   A 1 125 ? 20.082 -3.374  2.855   1.00 12.48 ?  125 PRO   A HG2  1 
ATOM   1980 H HG3  . PRO   A 1 125 ? 20.253 -2.020  3.682   1.00 12.48 ?  125 PRO   A HG3  1 
ATOM   1981 H HD2  . PRO   A 1 125 ? 20.920 -4.372  4.663   1.00 11.97 ?  125 PRO   A HD2  1 
ATOM   1982 H HD3  . PRO   A 1 125 ? 20.581 -3.112  5.597   1.00 11.97 ?  125 PRO   A HD3  1 
ATOM   1983 N N    . LEU   A 1 126 ? 16.934 -5.221  2.448   1.00 10.10 ?  126 LEU   A N    1 
ATOM   1984 C CA   . LEU   A 1 126 ? 16.959 -6.060  1.255   1.00 10.38 ?  126 LEU   A CA   1 
ATOM   1985 C C    . LEU   A 1 126 ? 17.894 -5.455  0.214   1.00 10.16 ?  126 LEU   A C    1 
ATOM   1986 O O    . LEU   A 1 126 ? 17.681 -4.332  -0.252  1.00 10.92 ?  126 LEU   A O    1 
ATOM   1987 C CB   . LEU   A 1 126 ? 15.561 -6.215  0.673   1.00 11.46 ?  126 LEU   A CB   1 
ATOM   1988 C CG   . LEU   A 1 126 ? 14.641 -7.162  1.433   1.00 13.03 ?  126 LEU   A CG   1 
ATOM   1989 C CD1  . LEU   A 1 126 ? 13.227 -7.014  0.907   1.00 14.53 ?  126 LEU   A CD1  1 
ATOM   1990 C CD2  . LEU   A 1 126 ? 15.107 -8.605  1.302   1.00 13.25 ?  126 LEU   A CD2  1 
ATOM   1991 H H    . LEU   A 1 126 ? 16.208 -4.771  2.558   1.00 12.13 ?  126 LEU   A H    1 
ATOM   1992 H HA   . LEU   A 1 126 ? 17.292 -6.935  1.488   1.00 12.46 ?  126 LEU   A HA   1 
ATOM   1993 H HB2  . LEU   A 1 126 ? 15.131 -5.346  0.659   1.00 13.76 ?  126 LEU   A HB2  1 
ATOM   1994 H HB3  . LEU   A 1 126 ? 15.638 -6.553  -0.232  1.00 13.76 ?  126 LEU   A HB3  1 
ATOM   1995 H HG   . LEU   A 1 126 ? 14.638 -6.927  2.374   1.00 15.64 ?  126 LEU   A HG   1 
ATOM   1996 H HD11 . LEU   A 1 126 ? 12.646 -7.627  1.385   1.00 17.44 ?  126 LEU   A HD11 1 
ATOM   1997 H HD12 . LEU   A 1 126 ? 12.933 -6.102  1.044   1.00 17.44 ?  126 LEU   A HD12 1 
ATOM   1998 H HD13 . LEU   A 1 126 ? 13.221 -7.227  -0.041  1.00 17.44 ?  126 LEU   A HD13 1 
ATOM   1999 H HD21 . LEU   A 1 126 ? 14.436 -9.193  1.677   1.00 15.90 ?  126 LEU   A HD21 1 
ATOM   2000 H HD22 . LEU   A 1 126 ? 15.240 -8.809  0.362   1.00 15.90 ?  126 LEU   A HD22 1 
ATOM   2001 H HD23 . LEU   A 1 126 ? 15.946 -8.710  1.781   1.00 15.90 ?  126 LEU   A HD23 1 
ATOM   2002 N N    . LEU   A 1 127 ? 18.926 -6.202  -0.161  1.00 10.20 ?  127 LEU   A N    1 
ATOM   2003 C CA   . LEU   A 1 127 ? 19.910 -5.701  -1.105  1.00 10.07 ?  127 LEU   A CA   1 
ATOM   2004 C C    . LEU   A 1 127 ? 19.290 -5.494  -2.476  1.00 9.73  ?  127 LEU   A C    1 
ATOM   2005 O O    . LEU   A 1 127 ? 18.449 -6.273  -2.935  1.00 10.27 ?  127 LEU   A O    1 
ATOM   2006 C CB   . LEU   A 1 127 ? 21.084 -6.672  -1.214  1.00 10.71 ?  127 LEU   A CB   1 
ATOM   2007 C CG   . LEU   A 1 127 ? 21.890 -6.913  0.055   1.00 11.27 ?  127 LEU   A CG   1 
ATOM   2008 C CD1  . LEU   A 1 127 ? 23.000 -7.907  -0.237  1.00 11.92 ?  127 LEU   A CD1  1 
ATOM   2009 C CD2  . LEU   A 1 127 ? 22.469 -5.627  0.590   1.00 12.28 ?  127 LEU   A CD2  1 
ATOM   2010 H H    . LEU   A 1 127 ? 19.080 -7.002  0.128   1.00 12.25 ?  127 LEU   A H    1 
ATOM   2011 H HA   . LEU   A 1 127 ? 20.246 -4.849  -0.788  1.00 12.08 ?  127 LEU   A HA   1 
ATOM   2012 H HB2  . LEU   A 1 127 ? 20.742 -7.529  -1.506  1.00 12.85 ?  127 LEU   A HB2  1 
ATOM   2013 H HB3  . LEU   A 1 127 ? 21.698 -6.325  -1.879  1.00 12.85 ?  127 LEU   A HB3  1 
ATOM   2014 H HG   . LEU   A 1 127 ? 21.312 -7.296  0.737   1.00 13.53 ?  127 LEU   A HG   1 
ATOM   2015 H HD11 . LEU   A 1 127 ? 23.505 -8.069  0.578   1.00 14.30 ?  127 LEU   A HD11 1 
ATOM   2016 H HD12 . LEU   A 1 127 ? 22.609 -8.738  -0.552  1.00 14.30 ?  127 LEU   A HD12 1 
ATOM   2017 H HD13 . LEU   A 1 127 ? 23.584 -7.538  -0.917  1.00 14.30 ?  127 LEU   A HD13 1 
ATOM   2018 H HD21 . LEU   A 1 127 ? 23.081 -5.836  1.316   1.00 14.74 ?  127 LEU   A HD21 1 
ATOM   2019 H HD22 . LEU   A 1 127 ? 22.950 -5.180  -0.125  1.00 14.74 ?  127 LEU   A HD22 1 
ATOM   2020 H HD23 . LEU   A 1 127 ? 21.752 -5.065  0.912   1.00 14.74 ?  127 LEU   A HD23 1 
ATOM   2021 N N    . SER   A 1 128 ? 19.728 -4.430  -3.132  1.00 9.56  ?  128 SER   A N    1 
ATOM   2022 C CA   . SER   A 1 128 ? 19.317 -4.025  -4.467  1.00 9.77  ?  128 SER   A CA   1 
ATOM   2023 C C    . SER   A 1 128 ? 17.864 -3.566  -4.546  1.00 10.13 ?  128 SER   A C    1 
ATOM   2024 O O    . SER   A 1 128 ? 17.400 -3.255  -5.643  1.00 11.52 ?  128 SER   A O    1 
ATOM   2025 C CB   . SER   A 1 128 ? 19.639 -5.063  -5.551  1.00 10.15 ?  128 SER   A CB   1 
ATOM   2026 O OG   . SER   A 1 128 ? 21.047 -5.269  -5.626  1.00 10.78 ?  128 SER   A OG   1 
ATOM   2027 H H    . SER   A 1 128 ? 20.319 -3.896  -2.800  1.00 11.47 ?  128 SER   A H    1 
ATOM   2028 H HA   . SER   A 1 128 ? 19.844 -3.250  -4.686  1.00 11.73 ?  128 SER   A HA   1 
ATOM   2029 H HB2  . SER   A 1 128 ? 19.201 -5.899  -5.339  1.00 12.18 ?  128 SER   A HB2  1 
ATOM   2030 H HB3  . SER   A 1 128 ? 19.313 -4.729  -6.410  1.00 12.18 ?  128 SER   A HB3  1 
ATOM   2031 H HG   . SER   A 1 128 ? 21.431 -4.544  -5.819  1.00 12.93 ?  128 SER   A HG   1 
ATOM   2032 N N    . ALA   A 1 129 ? 17.150 -3.481  -3.423  1.00 10.69 ?  129 ALA   A N    1 
ATOM   2033 C CA   . ALA   A 1 129 ? 15.790 -2.964  -3.409  1.00 11.23 ?  129 ALA   A CA   1 
ATOM   2034 C C    . ALA   A 1 129 ? 15.809 -1.435  -3.406  1.00 10.94 ?  129 ALA   A C    1 
ATOM   2035 O O    . ALA   A 1 129 ? 16.859 -0.793  -3.514  1.00 10.79 ?  129 ALA   A O    1 
ATOM   2036 C CB   . ALA   A 1 129 ? 15.019 -3.522  -2.211  1.00 12.81 ?  129 ALA   A CB   1 
ATOM   2037 H H    . ALA   A 1 129 ? 17.440 -3.713  -2.640  1.00 12.83 ?  129 ALA   A H    1 
ATOM   2038 H HA   . ALA   A 1 129 ? 15.341 -3.256  -4.213  1.00 13.47 ?  129 ALA   A HA   1 
ATOM   2039 H HB1  . ALA   A 1 129 ? 14.110 -3.176  -2.233  1.00 15.37 ?  129 ALA   A HB1  1 
ATOM   2040 H HB2  . ALA   A 1 129 ? 15.005 -4.488  -2.267  1.00 15.37 ?  129 ALA   A HB2  1 
ATOM   2041 H HB3  . ALA   A 1 129 ? 15.457 -3.242  -1.393  1.00 15.37 ?  129 ALA   A HB3  1 
ATOM   2042 N N    . GLY   A 1 130 ? 14.623 -0.839  -3.308  1.00 12.10 ?  130 GLY   A N    1 
ATOM   2043 C CA   . GLY   A 1 130 ? 14.541 0.612   -3.260  1.00 12.50 ?  130 GLY   A CA   1 
ATOM   2044 C C    . GLY   A 1 130 ? 15.132 1.224   -4.512  1.00 11.99 ?  130 GLY   A C    1 
ATOM   2045 O O    . GLY   A 1 130 ? 14.873 0.773   -5.633  1.00 12.29 ?  130 GLY   A O    1 
ATOM   2046 H H    . GLY   A 1 130 ? 13.866 -1.247  -3.271  1.00 14.52 ?  130 GLY   A H    1 
ATOM   2047 H HA2  . GLY   A 1 130 ? 13.609 0.883   -3.179  1.00 15.00 ?  130 GLY   A HA2  1 
ATOM   2048 H HA3  . GLY   A 1 130 ? 15.027 0.942   -2.490  1.00 15.00 ?  130 GLY   A HA3  1 
ATOM   2049 N N    . ILE   A 1 131 ? 15.951 2.265   -4.323  1.00 11.81 ?  131 ILE   A N    1 
ATOM   2050 C CA   . ILE   A 1 131 ? 16.503 3.008   -5.452  1.00 11.70 ?  131 ILE   A CA   1 
ATOM   2051 C C    . ILE   A 1 131 ? 17.514 2.215   -6.266  1.00 11.19 ?  131 ILE   A C    1 
ATOM   2052 O O    . ILE   A 1 131 ? 17.938 2.695   -7.326  1.00 12.16 ?  131 ILE   A O    1 
ATOM   2053 C CB   . ILE   A 1 131 ? 17.091 4.371   -5.028  1.00 12.89 ?  131 ILE   A CB   1 
ATOM   2054 C CG1  . ILE   A 1 131 ? 18.353 4.198   -4.174  1.00 13.82 ?  131 ILE   A CG1  1 
ATOM   2055 C CG2  . ILE   A 1 131 ? 16.040 5.202   -4.298  1.00 13.50 ?  131 ILE   A CG2  1 
ATOM   2056 C CD1  . ILE   A 1 131 ? 19.010 5.523   -3.787  1.00 15.40 ?  131 ILE   A CD1  1 
ATOM   2057 H H    . ILE   A 1 131 ? 16.184 2.561   -3.550  1.00 14.17 ?  131 ILE   A H    1 
ATOM   2058 H HA   . ILE   A 1 131 ? 15.771 3.206   -6.047  1.00 14.04 ?  131 ILE   A HA   1 
ATOM   2059 H HB   . ILE   A 1 131 ? 17.340 4.850   -5.833  1.00 15.47 ?  131 ILE   A HB   1 
ATOM   2060 H HG12 . ILE   A 1 131 ? 18.121 3.735   -3.357  1.00 16.59 ?  131 ILE   A HG12 1 
ATOM   2061 H HG13 . ILE   A 1 131 ? 19.009 3.687   -4.672  1.00 16.59 ?  131 ILE   A HG13 1 
ATOM   2062 H HG21 . ILE   A 1 131 ? 16.365 6.111   -4.199  1.00 16.21 ?  131 ILE   A HG21 1 
ATOM   2063 H HG22 . ILE   A 1 131 ? 15.222 5.201   -4.819  1.00 16.21 ?  131 ILE   A HG22 1 
ATOM   2064 H HG23 . ILE   A 1 131 ? 15.877 4.811   -3.426  1.00 16.21 ?  131 ILE   A HG23 1 
ATOM   2065 H HD11 . ILE   A 1 131 ? 19.864 5.341   -3.363  1.00 18.48 ?  131 ILE   A HD11 1 
ATOM   2066 H HD12 . ILE   A 1 131 ? 19.146 6.056   -4.586  1.00 18.48 ?  131 ILE   A HD12 1 
ATOM   2067 H HD13 . ILE   A 1 131 ? 18.431 5.998   -3.169  1.00 18.48 ?  131 ILE   A HD13 1 
ATOM   2068 N N    . PHE   A 1 132 ? 17.910 1.016   -5.817  1.00 10.77 ?  132 PHE   A N    1 
ATOM   2069 C CA   . PHE   A 1 132 ? 18.760 0.163   -6.639  1.00 11.16 ?  132 PHE   A CA   1 
ATOM   2070 C C    . PHE   A 1 132 ? 17.977 -0.593  -7.710  1.00 11.84 ?  132 PHE   A C    1 
ATOM   2071 O O    . PHE   A 1 132 ? 18.594 -1.228  -8.570  1.00 13.00 ?  132 PHE   A O    1 
ATOM   2072 C CB   . PHE   A 1 132 ? 19.569 -0.816  -5.778  1.00 10.89 ?  132 PHE   A CB   1 
ATOM   2073 C CG   . PHE   A 1 132 ? 20.792 -0.210  -5.121  1.00 10.51 ?  132 PHE   A CG   1 
ATOM   2074 C CD1  . PHE   A 1 132 ? 20.676 0.821   -4.206  1.00 11.72 ?  132 PHE   A CD1  1 
ATOM   2075 C CD2  . PHE   A 1 132 ? 22.055 -0.717  -5.386  1.00 11.49 ?  132 PHE   A CD2  1 
ATOM   2076 C CE1  . PHE   A 1 132 ? 21.802 1.355   -3.593  1.00 12.00 ?  132 PHE   A CE1  1 
ATOM   2077 C CE2  . PHE   A 1 132 ? 23.180 -0.188  -4.774  1.00 11.98 ?  132 PHE   A CE2  1 
ATOM   2078 C CZ   . PHE   A 1 132 ? 23.051 0.847   -3.874  1.00 11.99 ?  132 PHE   A CZ   1 
ATOM   2079 H H    . PHE   A 1 132 ? 17.701 0.683   -5.046  1.00 12.92 ?  132 PHE   A H    1 
ATOM   2080 H HA   . PHE   A 1 132 ? 19.398 0.730   -7.092  1.00 13.40 ?  132 PHE   A HA   1 
ATOM   2081 H HB2  . PHE   A 1 132 ? 18.995 -1.156  -5.070  1.00 13.07 ?  132 PHE   A HB2  1 
ATOM   2082 H HB3  . PHE   A 1 132 ? 19.865 -1.553  -6.337  1.00 13.07 ?  132 PHE   A HB3  1 
ATOM   2083 H HD1  . PHE   A 1 132 ? 19.837 1.166   -4.006  1.00 14.07 ?  132 PHE   A HD1  1 
ATOM   2084 H HD2  . PHE   A 1 132 ? 22.149 -1.422  -5.995  1.00 13.79 ?  132 PHE   A HD2  1 
ATOM   2085 H HE1  . PHE   A 1 132 ? 21.712 2.054   -2.986  1.00 14.41 ?  132 PHE   A HE1  1 
ATOM   2086 H HE2  . PHE   A 1 132 ? 24.020 -0.534  -4.975  1.00 14.37 ?  132 PHE   A HE2  1 
ATOM   2087 H HZ   . PHE   A 1 132 ? 23.805 1.208   -3.469  1.00 14.39 ?  132 PHE   A HZ   1 
ATOM   2088 N N    . GLY   A 1 133 ? 16.647 -0.560  -7.679  1.00 12.30 ?  133 GLY   A N    1 
ATOM   2089 C CA   . GLY   A 1 133 ? 15.858 -0.936  -8.834  1.00 12.94 ?  133 GLY   A CA   1 
ATOM   2090 C C    . GLY   A 1 133 ? 15.494 -2.399  -8.993  1.00 13.01 ?  133 GLY   A C    1 
ATOM   2091 O O    . GLY   A 1 133 ? 14.795 -2.728  -9.959  1.00 14.66 ?  133 GLY   A O    1 
ATOM   2092 H H    . GLY   A 1 133 ? 16.176 -0.322  -6.996  1.00 14.76 ?  133 GLY   A H    1 
ATOM   2093 H HA2  . GLY   A 1 133 ? 15.025 -0.444  -8.811  1.00 15.53 ?  133 GLY   A HA2  1 
ATOM   2094 H HA3  . GLY   A 1 133 ? 16.338 -0.664  -9.633  1.00 15.53 ?  133 GLY   A HA3  1 
ATOM   2095 N N    . ALA   A 1 134 ? 15.945 -3.291  -8.113  1.00 12.26 ?  134 ALA   A N    1 
ATOM   2096 C CA   . ALA   A 1 134 ? 15.587 -4.691  -8.275  1.00 12.80 ?  134 ALA   A CA   1 
ATOM   2097 C C    . ALA   A 1 134 ? 14.228 -4.972  -7.640  1.00 13.21 ?  134 ALA   A C    1 
ATOM   2098 O O    . ALA   A 1 134 ? 13.695 -4.178  -6.857  1.00 14.53 ?  134 ALA   A O    1 
ATOM   2099 C CB   . ALA   A 1 134 ? 16.654 -5.604  -7.669  1.00 13.74 ?  134 ALA   A CB   1 
ATOM   2100 H H    . ALA   A 1 134 ? 16.462 -3.113  -7.439  1.00 14.71 ?  134 ALA   A H    1 
ATOM   2101 H HA   . ALA   A 1 134 ? 15.535 -4.890  -9.225  1.00 15.36 ?  134 ALA   A HA   1 
ATOM   2102 H HB1  . ALA   A 1 134 ? 16.389 -6.526  -7.804  1.00 16.49 ?  134 ALA   A HB1  1 
ATOM   2103 H HB2  . ALA   A 1 134 ? 17.505 -5.437  -8.110  1.00 16.49 ?  134 ALA   A HB2  1 
ATOM   2104 H HB3  . ALA   A 1 134 ? 16.731 -5.414  -6.723  1.00 16.49 ?  134 ALA   A HB3  1 
ATOM   2105 N N    . ASP   A 1 135 ? 13.668 -6.120  -8.001  1.00 14.18 ?  135 ASP   A N    1 
ATOM   2106 C CA   . ASP   A 1 135 ? 12.410 -6.581  -7.425  1.00 15.65 ?  135 ASP   A CA   1 
ATOM   2107 C C    . ASP   A 1 135 ? 12.659 -7.043  -5.993  1.00 14.75 ?  135 ASP   A C    1 
ATOM   2108 O O    . ASP   A 1 135 ? 13.431 -7.988  -5.787  1.00 14.24 ?  135 ASP   A O    1 
ATOM   2109 C CB   . ASP   A 1 135 ? 11.902 -7.744  -8.273  1.00 18.61 ?  135 ASP   A CB   1 
ATOM   2110 C CG   . ASP   A 1 135 ? 10.622 -8.368  -7.733  1.00 21.68 ?  135 ASP   A CG   1 
ATOM   2111 O OD1  . ASP   A 1 135 ? 10.077 -7.871  -6.725  1.00 22.13 ?  135 ASP   A OD1  1 
ATOM   2112 O OD2  . ASP   A 1 135 ? 10.158 -9.359  -8.336  1.00 24.80 -1 135 ASP   A OD2  1 
ATOM   2113 H H    . ASP   A 1 135 ? 13.999 -6.653  -8.588  1.00 17.03 ?  135 ASP   A H    1 
ATOM   2114 H HA   . ASP   A 1 135 ? 11.755 -5.863  -7.446  1.00 18.78 ?  135 ASP   A HA   1 
ATOM   2115 H HB2  . ASP   A 1 135 ? 11.719 -7.421  -9.170  1.00 22.33 ?  135 ASP   A HB2  1 
ATOM   2116 H HB3  . ASP   A 1 135 ? 12.588 -8.428  -8.303  1.00 22.33 ?  135 ASP   A HB3  1 
ATOM   2117 N N    . PRO   A 1 136 ? 12.059 -6.409  -4.982  1.00 14.99 ?  136 PRO   A N    1 
ATOM   2118 C CA   . PRO   A 1 136 ? 12.325 -6.833  -3.595  1.00 14.98 ?  136 PRO   A CA   1 
ATOM   2119 C C    . PRO   A 1 136 ? 11.889 -8.259  -3.291  1.00 13.84 ?  136 PRO   A C    1 
ATOM   2120 O O    . PRO   A 1 136 ? 12.482 -8.907  -2.419  1.00 13.47 ?  136 PRO   A O    1 
ATOM   2121 C CB   . PRO   A 1 136 ? 11.552 -5.800  -2.759  1.00 16.30 ?  136 PRO   A CB   1 
ATOM   2122 C CG   . PRO   A 1 136 ? 10.508 -5.263  -3.687  1.00 17.70 ?  136 PRO   A CG   1 
ATOM   2123 C CD   . PRO   A 1 136 ? 11.126 -5.271  -5.046  1.00 16.37 ?  136 PRO   A CD   1 
ATOM   2124 H HA   . PRO   A 1 136 ? 13.274 -6.746  -3.396  1.00 17.98 ?  136 PRO   A HA   1 
ATOM   2125 H HB2  . PRO   A 1 136 ? 11.146 -6.238  -1.997  1.00 19.57 ?  136 PRO   A HB2  1 
ATOM   2126 H HB3  . PRO   A 1 136 ? 12.156 -5.095  -2.472  1.00 19.57 ?  136 PRO   A HB3  1 
ATOM   2127 H HG2  . PRO   A 1 136 ? 9.731  -5.840  -3.668  1.00 21.25 ?  136 PRO   A HG2  1 
ATOM   2128 H HG3  . PRO   A 1 136 ? 10.276 -4.360  -3.427  1.00 21.25 ?  136 PRO   A HG3  1 
ATOM   2129 H HD2  . PRO   A 1 136 ? 10.448 -5.432  -5.725  1.00 19.64 ?  136 PRO   A HD2  1 
ATOM   2130 H HD3  . PRO   A 1 136 ? 11.603 -4.442  -5.214  1.00 19.64 ?  136 PRO   A HD3  1 
ATOM   2131 N N    . ILE   A 1 137 ? 10.859 -8.766  -3.971  1.00 14.13 ?  137 ILE   A N    1 
ATOM   2132 C CA   . ILE   A 1 137 ? 10.473 -10.163 -3.784  1.00 14.79 ?  137 ILE   A CA   1 
ATOM   2133 C C    . ILE   A 1 137 ? 11.615 -11.079 -4.203  1.00 13.95 ?  137 ILE   A C    1 
ATOM   2134 O O    . ILE   A 1 137 ? 11.921 -12.072 -3.530  1.00 14.06 ?  137 ILE   A O    1 
ATOM   2135 C CB   . ILE   A 1 137 ? 9.175  -10.469 -4.555  1.00 16.44 ?  137 ILE   A CB   1 
ATOM   2136 C CG1  . ILE   A 1 137 ? 8.002  -9.653  -4.000  1.00 18.68 ?  137 ILE   A CG1  1 
ATOM   2137 C CG2  . ILE   A 1 137 ? 8.858  -11.958 -4.496  1.00 17.09 ?  137 ILE   A CG2  1 
ATOM   2138 C CD1  . ILE   A 1 137 ? 6.716  -9.829  -4.777  1.00 20.54 ?  137 ILE   A CD1  1 
ATOM   2139 H H    . ILE   A 1 137 ? 10.382 -8.329  -4.536  1.00 16.96 ?  137 ILE   A H    1 
ATOM   2140 H HA   . ILE   A 1 137 ? 10.305 -10.316 -2.844  1.00 17.75 ?  137 ILE   A HA   1 
ATOM   2141 H HB   . ILE   A 1 137 ? 9.300  -10.220 -5.481  1.00 19.73 ?  137 ILE   A HB   1 
ATOM   2142 H HG12 . ILE   A 1 137 ? 7.835  -9.921  -3.082  1.00 22.42 ?  137 ILE   A HG12 1 
ATOM   2143 H HG13 . ILE   A 1 137 ? 8.235  -8.708  -4.025  1.00 22.42 ?  137 ILE   A HG13 1 
ATOM   2144 H HG21 . ILE   A 1 137 ? 8.086  -12.144 -5.051  1.00 20.51 ?  137 ILE   A HG21 1 
ATOM   2145 H HG22 . ILE   A 1 137 ? 9.609  -12.464 -4.827  1.00 20.51 ?  137 ILE   A HG22 1 
ATOM   2146 H HG23 . ILE   A 1 137 ? 8.670  -12.200 -3.577  1.00 20.51 ?  137 ILE   A HG23 1 
ATOM   2147 H HD11 . ILE   A 1 137 ? 6.000  -9.474  -4.239  1.00 24.66 ?  137 ILE   A HD11 1 
ATOM   2148 H HD12 . ILE   A 1 137 ? 6.783  -9.346  -5.616  1.00 24.66 ?  137 ILE   A HD12 1 
ATOM   2149 H HD13 . ILE   A 1 137 ? 6.552  -10.769 -4.946  1.00 24.66 ?  137 ILE   A HD13 1 
ATOM   2150 N N    . HIS   A 1 138 ? 12.257 -10.762 -5.328  1.00 13.89 ?  138 HIS   A N    1 
ATOM   2151 C CA   . HIS   A 1 138 ? 13.415 -11.534 -5.764  1.00 13.67 ?  138 HIS   A CA   1 
ATOM   2152 C C    . HIS   A 1 138 ? 14.569 -11.405 -4.777  1.00 12.74 ?  138 HIS   A C    1 
ATOM   2153 O O    . HIS   A 1 138 ? 15.237 -12.396 -4.455  1.00 13.03 ?  138 HIS   A O    1 
ATOM   2154 C CB   . HIS   A 1 138 ? 13.829 -11.091 -7.166  1.00 14.29 ?  138 HIS   A CB   1 
ATOM   2155 C CG   . HIS   A 1 138 ? 15.096 -11.725 -7.641  1.00 15.19 ?  138 HIS   A CG   1 
ATOM   2156 N ND1  . HIS   A 1 138 ? 15.206 -13.077 -7.886  1.00 16.58 ?  138 HIS   A ND1  1 
ATOM   2157 C CD2  . HIS   A 1 138 ? 16.313 -11.193 -7.901  1.00 15.57 ?  138 HIS   A CD2  1 
ATOM   2158 C CE1  . HIS   A 1 138 ? 16.436 -13.349 -8.283  1.00 16.86 ?  138 HIS   A CE1  1 
ATOM   2159 N NE2  . HIS   A 1 138 ? 17.128 -12.224 -8.301  1.00 16.19 ?  138 HIS   A NE2  1 
ATOM   2160 H H    . HIS   A 1 138 ? 12.043 -10.107 -5.850  1.00 16.67 ?  138 HIS   A H    1 
ATOM   2161 H HA   . HIS   A 1 138 ? 13.162 -12.467 -5.815  1.00 16.41 ?  138 HIS   A HA   1 
ATOM   2162 H HB2  . HIS   A 1 138 ? 13.123 -11.329 -7.794  1.00 17.15 ?  138 HIS   A HB2  1 
ATOM   2163 H HB3  . HIS   A 1 138 ? 13.956 -10.130 -7.171  1.00 17.15 ?  138 HIS   A HB3  1 
ATOM   2164 H HD1  . HIS   A 1 138 ? 14.572 -13.653 -7.796  1.00 19.90 ?  138 HIS   A HD1  1 
ATOM   2165 H HD2  . HIS   A 1 138 ? 16.547 -10.297 -7.828  1.00 18.69 ?  138 HIS   A HD2  1 
ATOM   2166 H HE1  . HIS   A 1 138 ? 16.761 -14.189 -8.511  1.00 20.23 ?  138 HIS   A HE1  1 
ATOM   2167 N N    . SER   A 1 139 ? 14.813 -10.195 -4.277  1.00 12.29 ?  139 SER   A N    1 
ATOM   2168 C CA   . SER   A 1 139 ? 15.895 -10.013 -3.322  1.00 11.92 ?  139 SER   A CA   1 
ATOM   2169 C C    . SER   A 1 139 ? 15.683 -10.860 -2.074  1.00 11.51 ?  139 SER   A C    1 
ATOM   2170 O O    . SER   A 1 139 ? 16.635 -11.452 -1.553  1.00 11.39 ?  139 SER   A O    1 
ATOM   2171 C CB   . SER   A 1 139 ? 16.037 -8.537  -2.965  1.00 12.20 ?  139 SER   A CB   1 
ATOM   2172 O OG   . SER   A 1 139 ? 17.123 -8.382  -2.075  1.00 12.29 ?  139 SER   A OG   1 
ATOM   2173 H H    . SER   A 1 139 ? 14.372 -9.480  -4.471  1.00 14.76 ?  139 SER   A H    1 
ATOM   2174 H HA   . SER   A 1 139 ? 16.725 -10.294 -3.735  1.00 14.30 ?  139 SER   A HA   1 
ATOM   2175 H HB2  . SER   A 1 139 ? 16.206 -8.019  -3.772  1.00 14.65 ?  139 SER   A HB2  1 
ATOM   2176 H HB3  . SER   A 1 139 ? 15.227 -8.224  -2.532  1.00 14.65 ?  139 SER   A HB3  1 
ATOM   2177 H HG   . SER   A 1 139 ? 17.227 -7.577  -1.870  1.00 14.75 ?  139 SER   A HG   1 
ATOM   2178 N N    . LEU   A 1 140 ? 14.447 -10.928 -1.577  1.00 11.57 ?  140 LEU   A N    1 
ATOM   2179 C CA   . LEU   A 1 140 ? 14.176 -11.749 -0.401  1.00 11.11 ?  140 LEU   A CA   1 
ATOM   2180 C C    . LEU   A 1 140 ? 14.431 -13.225 -0.691  1.00 11.15 ?  140 LEU   A C    1 
ATOM   2181 O O    . LEU   A 1 140 ? 14.978 -13.948 0.151   1.00 11.64 ?  140 LEU   A O    1 
ATOM   2182 C CB   . LEU   A 1 140 ? 12.741 -11.518 0.071   1.00 11.38 ?  140 LEU   A CB   1 
ATOM   2183 C CG   . LEU   A 1 140 ? 12.280 -12.375 1.250   1.00 12.04 ?  140 LEU   A CG   1 
ATOM   2184 C CD1  . LEU   A 1 140 ? 13.182 -12.190 2.459   1.00 12.06 ?  140 LEU   A CD1  1 
ATOM   2185 C CD2  . LEU   A 1 140 ? 10.827 -12.054 1.607   1.00 13.01 ?  140 LEU   A CD2  1 
ATOM   2186 H H    . LEU   A 1 140 ? 13.763 -10.512 -1.893  1.00 13.88 ?  140 LEU   A H    1 
ATOM   2187 H HA   . LEU   A 1 140 ? 14.772 -11.480 0.315   1.00 13.33 ?  140 LEU   A HA   1 
ATOM   2188 H HB2  . LEU   A 1 140 ? 12.651 -10.593 0.336   1.00 13.66 ?  140 LEU   A HB2  1 
ATOM   2189 H HB3  . LEU   A 1 140 ? 12.144 -11.704 -0.670  1.00 13.66 ?  140 LEU   A HB3  1 
ATOM   2190 H HG   . LEU   A 1 140 ? 12.313 -13.310 0.993   1.00 14.45 ?  140 LEU   A HG   1 
ATOM   2191 H HD11 . LEU   A 1 140 ? 12.800 -12.671 3.211   1.00 14.48 ?  140 LEU   A HD11 1 
ATOM   2192 H HD12 . LEU   A 1 140 ? 14.059 -12.547 2.251   1.00 14.48 ?  140 LEU   A HD12 1 
ATOM   2193 H HD13 . LEU   A 1 140 ? 13.243 -11.247 2.663   1.00 14.48 ?  140 LEU   A HD13 1 
ATOM   2194 H HD21 . LEU   A 1 140 ? 10.555 -12.613 2.357   1.00 15.62 ?  140 LEU   A HD21 1 
ATOM   2195 H HD22 . LEU   A 1 140 ? 10.758 -11.120 1.851   1.00 15.62 ?  140 LEU   A HD22 1 
ATOM   2196 H HD23 . LEU   A 1 140 ? 10.261 -12.241 0.841   1.00 15.62 ?  140 LEU   A HD23 1 
ATOM   2197 N N    . ARG   A 1 141 ? 14.039 -13.687 -1.880  1.00 11.48 ?  141 ARG   A N    1 
ATOM   2198 C CA   . ARG   A 1 141 ? 14.279 -15.073 -2.266  1.00 12.76 ?  141 ARG   A CA   1 
ATOM   2199 C C    . ARG   A 1 141 ? 15.772 -15.380 -2.281  1.00 11.86 ?  141 ARG   A C    1 
ATOM   2200 O O    . ARG   A 1 141 ? 16.218 -16.396 -1.733  1.00 12.07 ?  141 ARG   A O    1 
ATOM   2201 C CB   . ARG   A 1 141 ? 13.665 -15.313 -3.646  1.00 15.05 ?  141 ARG   A CB   1 
ATOM   2202 C CG   . ARG   A 1 141 ? 13.661 -16.750 -4.110  1.00 18.20 ?  141 ARG   A CG   1 
ATOM   2203 C CD   . ARG   A 1 141 ? 12.627 -17.539 -3.363  1.00 20.34 ?  141 ARG   A CD   1 
ATOM   2204 N NE   . ARG   A 1 141 ? 13.234 -18.330 -2.306  1.00 20.86 ?  141 ARG   A NE   1 
ATOM   2205 C CZ   . ARG   A 1 141 ? 12.551 -18.903 -1.324  1.00 21.40 ?  141 ARG   A CZ   1 
ATOM   2206 N NH1  . ARG   A 1 141 ? 11.254 -18.692 -1.170  1.00 21.46 ?  141 ARG   A NH1  1 
ATOM   2207 N NH2  . ARG   A 1 141 ? 13.186 -19.699 -0.471  1.00 21.88 ?  141 ARG   A NH2  1 
ATOM   2208 H H    . ARG   A 1 141 ? 13.632 -13.219 -2.478  1.00 13.79 ?  141 ARG   A H    1 
ATOM   2209 H HA   . ARG   A 1 141 ? 13.853 -15.665 -1.631  1.00 15.31 ?  141 ARG   A HA   1 
ATOM   2210 H HB2  . ARG   A 1 141 ? 12.748 -15.001 -3.633  1.00 18.07 ?  141 ARG   A HB2  1 
ATOM   2211 H HB3  . ARG   A 1 141 ? 14.171 -14.799 -4.296  1.00 18.07 ?  141 ARG   A HB3  1 
ATOM   2212 H HG2  . ARG   A 1 141 ? 13.451 -16.783 -5.058  1.00 21.85 ?  141 ARG   A HG2  1 
ATOM   2213 H HG3  . ARG   A 1 141 ? 14.532 -17.150 -3.947  1.00 21.85 ?  141 ARG   A HG3  1 
ATOM   2214 H HD2  . ARG   A 1 141 ? 11.988 -16.932 -2.957  1.00 24.41 ?  141 ARG   A HD2  1 
ATOM   2215 H HD3  . ARG   A 1 141 ? 12.173 -18.137 -3.979  1.00 24.41 ?  141 ARG   A HD3  1 
ATOM   2216 H HE   . ARG   A 1 141 ? 14.066 -18.528 -2.381  1.00 25.04 ?  141 ARG   A HE   1 
ATOM   2217 H HH11 . ARG   A 1 141 ? 10.827 -18.189 -1.723  1.00 25.76 ?  141 ARG   A HH11 1 
ATOM   2218 H HH12 . ARG   A 1 141 ? 10.830 -19.073 -0.525  1.00 25.76 ?  141 ARG   A HH12 1 
ATOM   2219 H HH21 . ARG   A 1 141 ? 14.030 -19.838 -0.559  1.00 26.27 ?  141 ARG   A HH21 1 
ATOM   2220 H HH22 . ARG   A 1 141 ? 12.756 -20.067 0.177   1.00 26.27 ?  141 ARG   A HH22 1 
ATOM   2221 N N    . VAL   A 1 142 ? 16.565 -14.504 -2.905  1.00 11.49 ?  142 VAL   A N    1 
ATOM   2222 C CA   . VAL   A 1 142 ? 18.010 -14.716 -2.936  1.00 11.50 ?  142 VAL   A CA   1 
ATOM   2223 C C    . VAL   A 1 142 ? 18.580 -14.705 -1.525  1.00 10.69 ?  142 VAL   A C    1 
ATOM   2224 O O    . VAL   A 1 142 ? 19.438 -15.525 -1.179  1.00 11.21 ?  142 VAL   A O    1 
ATOM   2225 C CB   . VAL   A 1 142 ? 18.704 -13.691 -3.853  1.00 11.63 ?  142 VAL   A CB   1 
ATOM   2226 C CG1  . VAL   A 1 142 ? 20.210 -13.895 -3.813  1.00 11.58 ?  142 VAL   A CG1  1 
ATOM   2227 C CG2  . VAL   A 1 142 ? 18.203 -13.824 -5.281  1.00 13.11 ?  142 VAL   A CG2  1 
ATOM   2228 H H    . VAL   A 1 142 ? 16.299 -13.786 -3.306  1.00 13.79 ?  142 VAL   A H    1 
ATOM   2229 H HA   . VAL   A 1 142 ? 18.180 -15.588 -3.314  1.00 13.81 ?  142 VAL   A HA   1 
ATOM   2230 H HB   . VAL   A 1 142 ? 18.512 -12.786 -3.543  1.00 13.96 ?  142 VAL   A HB   1 
ATOM   2231 H HG11 . VAL   A 1 142 ? 20.617 -13.399 -4.544  1.00 13.89 ?  142 VAL   A HG11 1 
ATOM   2232 H HG12 . VAL   A 1 142 ? 20.557 -13.565 -2.966  1.00 13.89 ?  142 VAL   A HG12 1 
ATOM   2233 H HG13 . VAL   A 1 142 ? 20.404 -14.837 -3.906  1.00 13.89 ?  142 VAL   A HG13 1 
ATOM   2234 H HG21 . VAL   A 1 142 ? 18.674 -13.187 -5.843  1.00 15.73 ?  142 VAL   A HG21 1 
ATOM   2235 H HG22 . VAL   A 1 142 ? 18.381 -14.727 -5.588  1.00 15.73 ?  142 VAL   A HG22 1 
ATOM   2236 H HG23 . VAL   A 1 142 ? 17.254 -13.646 -5.299  1.00 15.73 ?  142 VAL   A HG23 1 
ATOM   2237 N N    . CYS   A 1 143 ? 18.111 -13.786 -0.683  1.00 10.61 ?  143 CYS   A N    1 
ATOM   2238 C CA   . CYS   A 1 143 ? 18.578 -13.741 0.698   1.00 10.52 ?  143 CYS   A CA   1 
ATOM   2239 C C    . CYS   A 1 143 ? 18.358 -15.082 1.385   1.00 10.47 ?  143 CYS   A C    1 
ATOM   2240 O O    . CYS   A 1 143 ? 19.282 -15.662 1.964   1.00 10.56 ?  143 CYS   A O    1 
ATOM   2241 C CB   . CYS   A 1 143 ? 17.835 -12.637 1.447   1.00 11.12 ?  143 CYS   A CB   1 
ATOM   2242 S SG   . CYS   A 1 143 ? 18.329 -12.456 3.170   1.00 11.43 ?  143 CYS   A SG   1 
ATOM   2243 H H    . CYS   A 1 143 ? 17.530 -13.188 -0.885  1.00 12.74 ?  143 CYS   A H    1 
ATOM   2244 H HA   . CYS   A 1 143 ? 19.527 -13.547 0.711   1.00 12.63 ?  143 CYS   A HA   1 
ATOM   2245 H HB2  . CYS   A 1 143 ? 17.998 -11.794 0.997   1.00 13.34 ?  143 CYS   A HB2  1 
ATOM   2246 H HB3  . CYS   A 1 143 ? 16.890 -12.837 1.431   1.00 13.34 ?  143 CYS   A HB3  1 
ATOM   2247 H HG   . CYS   A 1 143 ? 17.737 -11.527 3.643   1.00 13.71 ?  143 CYS   A HG   1 
ATOM   2248 N N    . VAL   A 1 144 ? 17.129 -15.589 1.331   1.00 10.91 ?  144 VAL   A N    1 
ATOM   2249 C CA   . VAL   A 1 144 ? 16.794 -16.824 2.030   1.00 12.08 ?  144 VAL   A CA   1 
ATOM   2250 C C    . VAL   A 1 144 ? 17.609 -17.993 1.497   1.00 11.98 ?  144 VAL   A C    1 
ATOM   2251 O O    . VAL   A 1 144 ? 17.978 -18.902 2.251   1.00 12.46 ?  144 VAL   A O    1 
ATOM   2252 C CB   . VAL   A 1 144 ? 15.279 -17.072 1.918   1.00 15.01 ?  144 VAL   A CB   1 
ATOM   2253 C CG1  . VAL   A 1 144 ? 14.924 -18.502 2.262   1.00 16.87 ?  144 VAL   A CG1  1 
ATOM   2254 C CG2  . VAL   A 1 144 ? 14.527 -16.079 2.799   1.00 15.13 ?  144 VAL   A CG2  1 
ATOM   2255 H H    . VAL   A 1 144 ? 16.470 -15.231 0.901   1.00 13.09 ?  144 VAL   A H    1 
ATOM   2256 H HA   . VAL   A 1 144 ? 17.001 -16.716 2.967   1.00 14.50 ?  144 VAL   A HA   1 
ATOM   2257 H HB   . VAL   A 1 144 ? 14.999 -16.910 1.001   1.00 18.01 ?  144 VAL   A HB   1 
ATOM   2258 H HG11 . VAL   A 1 144 ? 13.972 -18.555 2.451   1.00 20.25 ?  144 VAL   A HG11 1 
ATOM   2259 H HG12 . VAL   A 1 144 ? 15.140 -19.073 1.509   1.00 20.25 ?  144 VAL   A HG12 1 
ATOM   2260 H HG13 . VAL   A 1 144 ? 15.428 -18.772 3.044   1.00 20.25 ?  144 VAL   A HG13 1 
ATOM   2261 H HG21 . VAL   A 1 144 ? 13.571 -16.245 2.727   1.00 18.16 ?  144 VAL   A HG21 1 
ATOM   2262 H HG22 . VAL   A 1 144 ? 14.811 -16.190 3.719   1.00 18.16 ?  144 VAL   A HG22 1 
ATOM   2263 H HG23 . VAL   A 1 144 ? 14.722 -15.174 2.501   1.00 18.16 ?  144 VAL   A HG23 1 
ATOM   2264 N N    . ASP   A 1 145 ? 17.880 -18.005 0.195   1.00 12.18 ?  145 ASP   A N    1 
ATOM   2265 C CA   . ASP   A 1 145 ? 18.590 -19.107 -0.441  1.00 12.78 ?  145 ASP   A CA   1 
ATOM   2266 C C    . ASP   A 1 145 ? 20.108 -18.956 -0.408  1.00 12.39 ?  145 ASP   A C    1 
ATOM   2267 O O    . ASP   A 1 145 ? 20.813 -19.848 -0.894  1.00 14.60 ?  145 ASP   A O    1 
ATOM   2268 C CB   . ASP   A 1 145 ? 18.136 -19.252 -1.895  1.00 14.30 ?  145 ASP   A CB   1 
ATOM   2269 C CG   . ASP   A 1 145 ? 16.682 -19.674 -2.017  1.00 16.45 ?  145 ASP   A CG   1 
ATOM   2270 O OD1  . ASP   A 1 145 ? 16.118 -20.211 -1.038  1.00 16.98 ?  145 ASP   A OD1  1 
ATOM   2271 O OD2  . ASP   A 1 145 ? 16.101 -19.473 -3.102  1.00 17.85 -1 145 ASP   A OD2  1 
ATOM   2272 H H    . ASP   A 1 145 ? 17.641 -17.381 -0.351  1.00 14.62 ?  145 ASP   A H    1 
ATOM   2273 H HA   . ASP   A 1 145 ? 18.363 -19.928 0.020   1.00 15.33 ?  145 ASP   A HA   1 
ATOM   2274 H HB2  . ASP   A 1 145 ? 18.245 -18.403 -2.349  1.00 17.16 ?  145 ASP   A HB2  1 
ATOM   2275 H HB3  . ASP   A 1 145 ? 18.672 -19.934 -2.326  1.00 17.16 ?  145 ASP   A HB3  1 
ATOM   2276 N N    . THR   A 1 146 ? 20.627 -17.864 0.141   1.00 10.86 ?  146 THR   A N    1 
ATOM   2277 C CA   . THR   A 1 146 ? 22.065 -17.604 0.156   1.00 10.49 ?  146 THR   A CA   1 
ATOM   2278 C C    . THR   A 1 146 ? 22.626 -17.420 1.553   1.00 10.18 ?  146 THR   A C    1 
ATOM   2279 O O    . THR   A 1 146 ? 23.705 -17.943 1.858   1.00 11.26 ?  146 THR   A O    1 
ATOM   2280 C CB   . THR   A 1 146 ? 22.386 -16.351 -0.681  1.00 10.49 ?  146 THR   A CB   1 
ATOM   2281 O OG1  . THR   A 1 146 ? 21.855 -16.514 -1.996  1.00 11.18 ?  146 THR   A OG1  1 
ATOM   2282 C CG2  . THR   A 1 146 ? 23.885 -16.114 -0.772  1.00 11.20 ?  146 THR   A CG2  1 
ATOM   2283 H H    . THR   A 1 146 ? 20.161 -17.237 0.513   1.00 13.03 ?  146 THR   A H    1 
ATOM   2284 H HA   . THR   A 1 146 ? 22.523 -18.354 -0.248  1.00 12.60 ?  146 THR   A HA   1 
ATOM   2285 H HB   . THR   A 1 146 ? 21.984 -15.573 -0.266  1.00 12.59 ?  146 THR   A HB   1 
ATOM   2286 H HG1  . THR   A 1 146 ? 21.018 -16.589 -1.962  1.00 13.42 ?  146 THR   A HG1  1 
ATOM   2287 H HG21 . THR   A 1 146 ? 24.073 -15.445 -1.449  1.00 13.45 ?  146 THR   A HG21 1 
ATOM   2288 H HG22 . THR   A 1 146 ? 24.226 -15.802 0.081   1.00 13.45 ?  146 THR   A HG22 1 
ATOM   2289 H HG23 . THR   A 1 146 ? 24.337 -16.938 -1.012  1.00 13.45 ?  146 THR   A HG23 1 
ATOM   2290 N N    . VAL   A 1 147 ? 21.945 -16.651 2.393   1.00 10.17 ?  147 VAL   A N    1 
ATOM   2291 C CA   . VAL   A 1 147 ? 22.435 -16.353 3.730   1.00 10.18 ?  147 VAL   A CA   1 
ATOM   2292 C C    . VAL   A 1 147 ? 22.121 -17.526 4.644   1.00 10.66 ?  147 VAL   A C    1 
ATOM   2293 O O    . VAL   A 1 147 ? 20.978 -18.002 4.700   1.00 11.05 ?  147 VAL   A O    1 
ATOM   2294 C CB   . VAL   A 1 147 ? 21.814 -15.049 4.253   1.00 10.56 ?  147 VAL   A CB   1 
ATOM   2295 C CG1  . VAL   A 1 147 ? 22.355 -14.733 5.629   1.00 11.57 ?  147 VAL   A CG1  1 
ATOM   2296 C CG2  . VAL   A 1 147 ? 22.078 -13.901 3.284   1.00 10.78 ?  147 VAL   A CG2  1 
ATOM   2297 H H    . VAL   A 1 147 ? 21.182 -16.291 2.214   1.00 12.21 ?  147 VAL   A H    1 
ATOM   2298 H HA   . VAL   A 1 147 ? 23.397 -16.238 3.696   1.00 12.22 ?  147 VAL   A HA   1 
ATOM   2299 H HB   . VAL   A 1 147 ? 20.856 -15.161 4.330   1.00 12.67 ?  147 VAL   A HB   1 
ATOM   2300 H HG11 . VAL   A 1 147 ? 22.105 -13.830 5.867   1.00 13.89 ?  147 VAL   A HG11 1 
ATOM   2301 H HG12 . VAL   A 1 147 ? 21.980 -15.361 6.268   1.00 13.89 ?  147 VAL   A HG12 1 
ATOM   2302 H HG13 . VAL   A 1 147 ? 23.322 -14.817 5.614   1.00 13.89 ?  147 VAL   A HG13 1 
ATOM   2303 H HG21 . VAL   A 1 147 ? 21.749 -13.074 3.677   1.00 12.94 ?  147 VAL   A HG21 1 
ATOM   2304 H HG22 . VAL   A 1 147 ? 23.033 -13.831 3.126   1.00 12.94 ?  147 VAL   A HG22 1 
ATOM   2305 H HG23 . VAL   A 1 147 ? 21.615 -14.075 2.451   1.00 12.94 ?  147 VAL   A HG23 1 
ATOM   2306 N N    . ARG   A 1 148 ? 23.150 -17.997 5.352   1.00 10.77 ?  148 ARG   A N    1 
ATOM   2307 C CA   . ARG   A 1 148 ? 23.022 -19.074 6.317   1.00 10.98 ?  148 ARG   A CA   1 
ATOM   2308 C C    . ARG   A 1 148 ? 23.157 -18.597 7.751   1.00 11.23 ?  148 ARG   A C    1 
ATOM   2309 O O    . ARG   A 1 148 ? 22.760 -19.319 8.672   1.00 12.72 ?  148 ARG   A O    1 
ATOM   2310 C CB   . ARG   A 1 148 ? 24.058 -20.170 6.034   1.00 11.69 ?  148 ARG   A CB   1 
ATOM   2311 C CG   . ARG   A 1 148 ? 23.882 -20.808 4.669   1.00 12.96 ?  148 ARG   A CG   1 
ATOM   2312 C CD   . ARG   A 1 148 ? 24.968 -21.838 4.361   1.00 13.97 ?  148 ARG   A CD   1 
ATOM   2313 N NE   . ARG   A 1 148 ? 26.302 -21.251 4.378   1.00 13.52 ?  148 ARG   A NE   1 
ATOM   2314 C CZ   . ARG   A 1 148 ? 26.805 -20.511 3.398   1.00 12.98 ?  148 ARG   A CZ   1 
ATOM   2315 N NH1  . ARG   A 1 148 ? 26.123 -20.274 2.289   1.00 13.43 ?  148 ARG   A NH1  1 
ATOM   2316 N NH2  . ARG   A 1 148 ? 28.022 -19.988 3.538   1.00 13.43 ?  148 ARG   A NH2  1 
ATOM   2317 H H    . ARG   A 1 148 ? 23.959 -17.695 5.279   1.00 12.92 ?  148 ARG   A H    1 
ATOM   2318 H HA   . ARG   A 1 148 ? 22.146 -19.468 6.223   1.00 13.18 ?  148 ARG   A HA   1 
ATOM   2319 H HB2  . ARG   A 1 148 ? 24.947 -19.791 6.075   1.00 14.03 ?  148 ARG   A HB2  1 
ATOM   2320 H HB3  . ARG   A 1 148 ? 23.965 -20.871 6.702   1.00 14.03 ?  148 ARG   A HB3  1 
ATOM   2321 H HG2  . ARG   A 1 148 ? 23.020 -21.254 4.637   1.00 15.56 ?  148 ARG   A HG2  1 
ATOM   2322 H HG3  . ARG   A 1 148 ? 23.921 -20.114 3.991   1.00 15.56 ?  148 ARG   A HG3  1 
ATOM   2323 H HD2  . ARG   A 1 148 ? 24.939 -22.540 5.030   1.00 16.77 ?  148 ARG   A HD2  1 
ATOM   2324 H HD3  . ARG   A 1 148 ? 24.809 -22.214 3.479   1.00 16.77 ?  148 ARG   A HD3  1 
ATOM   2325 H HE   . ARG   A 1 148 ? 26.795 -21.393 5.064   1.00 16.22 ?  148 ARG   A HE   1 
ATOM   2326 H HH11 . ARG   A 1 148 ? 25.338 -20.602 2.184   1.00 16.12 ?  148 ARG   A HH11 1 
ATOM   2327 H HH12 . ARG   A 1 148 ? 26.471 -19.787 1.668   1.00 16.12 ?  148 ARG   A HH12 1 
ATOM   2328 H HH21 . ARG   A 1 148 ? 28.468 -20.127 4.256   1.00 16.12 ?  148 ARG   A HH21 1 
ATOM   2329 H HH22 . ARG   A 1 148 ? 28.355 -19.500 2.911   1.00 16.12 ?  148 ARG   A HH22 1 
ATOM   2330 N N    . THR   A 1 149 ? 23.701 -17.404 7.959   1.00 10.82 ?  149 THR   A N    1 
ATOM   2331 C CA   . THR   A 1 149 ? 23.783 -16.810 9.276   1.00 11.10 ?  149 THR   A CA   1 
ATOM   2332 C C    . THR   A 1 149 ? 22.457 -16.118 9.594   1.00 10.71 ?  149 THR   A C    1 
ATOM   2333 O O    . THR   A 1 149 ? 21.512 -16.122 8.796   1.00 11.54 ?  149 THR   A O    1 
ATOM   2334 C CB   . THR   A 1 149 ? 24.978 -15.871 9.332   1.00 11.64 ?  149 THR   A CB   1 
ATOM   2335 O OG1  . THR   A 1 149 ? 24.845 -14.928 8.269   1.00 11.80 ?  149 THR   A OG1  1 
ATOM   2336 C CG2  . THR   A 1 149 ? 26.288 -16.658 9.180   1.00 12.42 ?  149 THR   A CG2  1 
ATOM   2337 H H    . THR   A 1 149 ? 24.044 -16.912 7.337   1.00 12.98 ?  149 THR   A H    1 
ATOM   2338 H HA   . THR   A 1 149 ? 23.917 -17.513 9.930   1.00 13.32 ?  149 THR   A HA   1 
ATOM   2339 H HB   . THR   A 1 149 ? 24.988 -15.412 10.184  1.00 13.97 ?  149 THR   A HB   1 
ATOM   2340 H HG1  . THR   A 1 149 ? 25.495 -14.393 8.276   1.00 14.16 ?  149 THR   A HG1  1 
ATOM   2341 H HG21 . THR   A 1 149 ? 27.046 -16.056 9.243   1.00 14.91 ?  149 THR   A HG21 1 
ATOM   2342 H HG22 . THR   A 1 149 ? 26.360 -17.327 9.881   1.00 14.91 ?  149 THR   A HG22 1 
ATOM   2343 H HG23 . THR   A 1 149 ? 26.313 -17.105 8.318   1.00 14.91 ?  149 THR   A HG23 1 
ATOM   2344 N N    . ASN   A 1 150 ? 22.351 -15.567 10.795  1.00 10.98 ?  150 ASN   A N    1 
ATOM   2345 C CA   . ASN   A 1 150 ? 21.071 -15.070 11.299  1.00 11.76 ?  150 ASN   A CA   1 
ATOM   2346 C C    . ASN   A 1 150 ? 20.877 -13.627 10.852  1.00 11.05 ?  150 ASN   A C    1 
ATOM   2347 O O    . ASN   A 1 150 ? 21.608 -12.730 11.289  1.00 12.85 ?  150 ASN   A O    1 
ATOM   2348 C CB   . ASN   A 1 150 ? 21.037 -15.193 12.816  1.00 14.31 ?  150 ASN   A CB   1 
ATOM   2349 C CG   . ASN   A 1 150 ? 20.878 -16.624 13.269  1.00 18.88 ?  150 ASN   A CG   1 
ATOM   2350 O OD1  . ASN   A 1 150 ? 20.259 -17.434 12.580  1.00 20.62 ?  150 ASN   A OD1  1 
ATOM   2351 N ND2  . ASN   A 1 150 ? 21.450 -16.952 14.421  1.00 21.21 ?  150 ASN   A ND2  1 
ATOM   2352 H H    . ASN   A 1 150 ? 23.010 -15.469 11.341  1.00 13.17 ?  150 ASN   A H    1 
ATOM   2353 H HA   . ASN   A 1 150 ? 20.353 -15.607 10.934  1.00 14.12 ?  150 ASN   A HA   1 
ATOM   2354 H HB2  . ASN   A 1 150 ? 21.870 -14.854 13.184  1.00 17.18 ?  150 ASN   A HB2  1 
ATOM   2355 H HB3  . ASN   A 1 150 ? 20.288 -14.686 13.161  1.00 17.18 ?  150 ASN   A HB3  1 
ATOM   2356 H HD21 . ASN   A 1 150 ? 21.390 -17.758 14.721  1.00 25.45 ?  150 ASN   A HD21 1 
ATOM   2357 H HD22 . ASN   A 1 150 ? 21.879 -16.360 14.875  1.00 25.45 ?  150 ASN   A HD22 1 
ATOM   2358 N N    . VAL   A 1 151 ? 19.890 -13.397 9.990   1.00 10.65 ?  151 VAL   A N    1 
ATOM   2359 C CA   . VAL   A 1 151 ? 19.671 -12.083 9.404   1.00 10.90 ?  151 VAL   A CA   1 
ATOM   2360 C C    . VAL   A 1 151 ? 18.287 -11.569 9.776   1.00 10.64 ?  151 VAL   A C    1 
ATOM   2361 O O    . VAL   A 1 151 ? 17.281 -12.282 9.640   1.00 11.83 ?  151 VAL   A O    1 
ATOM   2362 C CB   . VAL   A 1 151 ? 19.951 -12.059 7.887   1.00 12.12 ?  151 VAL   A CB   1 
ATOM   2363 C CG1  . VAL   A 1 151 ? 19.119 -13.075 7.136   1.00 13.36 ?  151 VAL   A CG1  1 
ATOM   2364 C CG2  . VAL   A 1 151 ? 19.747 -10.654 7.325   1.00 12.68 ?  151 VAL   A CG2  1 
ATOM   2365 H H    . VAL   A 1 151 ? 19.337 -13.998 9.724   1.00 12.79 ?  151 VAL   A H    1 
ATOM   2366 H HA   . VAL   A 1 151 ? 20.312 -11.474 9.801   1.00 13.08 ?  151 VAL   A HA   1 
ATOM   2367 H HB   . VAL   A 1 151 ? 20.884 -12.293 7.741   1.00 14.55 ?  151 VAL   A HB   1 
ATOM   2368 H HG11 . VAL   A 1 151 ? 19.314 -13.014 6.187   1.00 16.04 ?  151 VAL   A HG11 1 
ATOM   2369 H HG12 . VAL   A 1 151 ? 19.338 -13.967 7.458   1.00 16.04 ?  151 VAL   A HG12 1 
ATOM   2370 H HG13 . VAL   A 1 151 ? 18.178 -12.893 7.292   1.00 16.04 ?  151 VAL   A HG13 1 
ATOM   2371 H HG21 . VAL   A 1 151 ? 20.070 -10.629 6.409   1.00 15.21 ?  151 VAL   A HG21 1 
ATOM   2372 H HG22 . VAL   A 1 151 ? 18.803 -10.436 7.347   1.00 15.21 ?  151 VAL   A HG22 1 
ATOM   2373 H HG23 . VAL   A 1 151 ? 20.247 -10.022 7.866   1.00 15.21 ?  151 VAL   A HG23 1 
ATOM   2374 N N    . TYR   A 1 152 ? 18.268 -10.324 10.258  1.00 10.49 ?  152 TYR   A N    1 
ATOM   2375 C CA   . TYR   A 1 152 ? 17.077 -9.593  10.654  1.00 10.30 ?  152 TYR   A CA   1 
ATOM   2376 C C    . TYR   A 1 152 ? 16.883 -8.488  9.626   1.00 10.23 ?  152 TYR   A C    1 
ATOM   2377 O O    . TYR   A 1 152 ? 17.658 -7.525  9.580   1.00 10.71 ?  152 TYR   A O    1 
ATOM   2378 C CB   . TYR   A 1 152 ? 17.262 -9.050  12.070  1.00 10.77 ?  152 TYR   A CB   1 
ATOM   2379 C CG   . TYR   A 1 152 ? 17.236 -10.180 13.066  1.00 11.31 ?  152 TYR   A CG   1 
ATOM   2380 C CD1  . TYR   A 1 152 ? 18.378 -10.914 13.353  1.00 12.74 ?  152 TYR   A CD1  1 
ATOM   2381 C CD2  . TYR   A 1 152 ? 16.052 -10.553 13.678  1.00 11.61 ?  152 TYR   A CD2  1 
ATOM   2382 C CE1  . TYR   A 1 152 ? 18.345 -11.979 14.236  1.00 14.01 ?  152 TYR   A CE1  1 
ATOM   2383 C CE2  . TYR   A 1 152 ? 16.004 -11.624 14.563  1.00 12.88 ?  152 TYR   A CE2  1 
ATOM   2384 C CZ   . TYR   A 1 152 ? 17.156 -12.332 14.836  1.00 13.76 ?  152 TYR   A CZ   1 
ATOM   2385 O OH   . TYR   A 1 152 ? 17.127 -13.401 15.711  1.00 15.84 ?  152 TYR   A OH   1 
ATOM   2386 H H    . TYR   A 1 152 ? 18.986 -9.851  10.352  1.00 12.59 ?  152 TYR   A H    1 
ATOM   2387 H HA   . TYR   A 1 152 ? 16.308 -10.182 10.636  1.00 12.37 ?  152 TYR   A HA   1 
ATOM   2388 H HB2  . TYR   A 1 152 ? 18.116 -8.604  12.141  1.00 12.92 ?  152 TYR   A HB2  1 
ATOM   2389 H HB3  . TYR   A 1 152 ? 16.538 -8.441  12.282  1.00 12.92 ?  152 TYR   A HB3  1 
ATOM   2390 H HD1  . TYR   A 1 152 ? 19.180 -10.684 12.944  1.00 15.29 ?  152 TYR   A HD1  1 
ATOM   2391 H HD2  . TYR   A 1 152 ? 15.268 -10.086 13.491  1.00 13.93 ?  152 TYR   A HD2  1 
ATOM   2392 H HE1  . TYR   A 1 152 ? 19.123 -12.454 14.424  1.00 16.81 ?  152 TYR   A HE1  1 
ATOM   2393 H HE2  . TYR   A 1 152 ? 15.200 -11.856 14.973  1.00 15.46 ?  152 TYR   A HE2  1 
ATOM   2394 H HH   . TYR   A 1 152 ? 16.347 -13.495 16.016  1.00 19.02 ?  152 TYR   A HH   1 
ATOM   2395 N N    . LEU   A 1 153 ? 15.873 -8.650  8.780   1.00 10.27 ?  153 LEU   A N    1 
ATOM   2396 C CA   . LEU   A 1 153 ? 15.605 -7.739  7.679   1.00 10.72 ?  153 LEU   A CA   1 
ATOM   2397 C C    . LEU   A 1 153 ? 14.612 -6.670  8.101   1.00 11.21 ?  153 LEU   A C    1 
ATOM   2398 O O    . LEU   A 1 153 ? 13.523 -6.978  8.599   1.00 12.26 ?  153 LEU   A O    1 
ATOM   2399 C CB   . LEU   A 1 153 ? 15.028 -8.504  6.489   1.00 10.95 ?  153 LEU   A CB   1 
ATOM   2400 C CG   . LEU   A 1 153 ? 15.958 -9.521  5.828   1.00 11.14 ?  153 LEU   A CG   1 
ATOM   2401 C CD1  . LEU   A 1 153 ? 15.168 -10.414 4.882   1.00 11.87 ?  153 LEU   A CD1  1 
ATOM   2402 C CD2  . LEU   A 1 153 ? 17.086 -8.819  5.088   1.00 11.77 ?  153 LEU   A CD2  1 
ATOM   2403 H H    . LEU   A 1 153 ? 15.310 -9.301  8.831   1.00 12.32 ?  153 LEU   A H    1 
ATOM   2404 H HA   . LEU   A 1 153 ? 16.432 -7.313  7.411   1.00 12.87 ?  153 LEU   A HA   1 
ATOM   2405 H HB2  . LEU   A 1 153 ? 14.240 -8.979  6.787   1.00 13.15 ?  153 LEU   A HB2  1 
ATOM   2406 H HB3  . LEU   A 1 153 ? 14.777 -7.855  5.810   1.00 13.15 ?  153 LEU   A HB3  1 
ATOM   2407 H HG   . LEU   A 1 153 ? 16.357 -10.078 6.517   1.00 13.37 ?  153 LEU   A HG   1 
ATOM   2408 H HD11 . LEU   A 1 153 ? 15.750 -11.120 4.560   1.00 14.25 ?  153 LEU   A HD11 1 
ATOM   2409 H HD12 . LEU   A 1 153 ? 14.421 -10.794 5.365   1.00 14.25 ?  153 LEU   A HD12 1 
ATOM   2410 H HD13 . LEU   A 1 153 ? 14.851 -9.878  4.140   1.00 14.25 ?  153 LEU   A HD13 1 
ATOM   2411 H HD21 . LEU   A 1 153 ? 17.644 -9.489  4.664   1.00 14.12 ?  153 LEU   A HD21 1 
ATOM   2412 H HD22 . LEU   A 1 153 ? 16.703 -8.232  4.420   1.00 14.12 ?  153 LEU   A HD22 1 
ATOM   2413 H HD23 . LEU   A 1 153 ? 17.610 -8.306  5.722   1.00 14.12 ?  153 LEU   A HD23 1 
ATOM   2414 N N    . ALA   A 1 154 ? 14.980 -5.417  7.860   1.00 11.22 ?  154 ALA   A N    1 
ATOM   2415 C CA   . ALA   A 1 154 ? 14.122 -4.267  8.107   1.00 12.46 ?  154 ALA   A CA   1 
ATOM   2416 C C    . ALA   A 1 154 ? 13.619 -3.750  6.768   1.00 12.56 ?  154 ALA   A C    1 
ATOM   2417 O O    . ALA   A 1 154 ? 14.419 -3.395  5.894   1.00 13.63 ?  154 ALA   A O    1 
ATOM   2418 C CB   . ALA   A 1 154 ? 14.890 -3.162  8.831   1.00 13.14 ?  154 ALA   A CB   1 
ATOM   2419 H H    . ALA   A 1 154 ? 15.749 -5.201  7.532   1.00 13.46 ?  154 ALA   A H    1 
ATOM   2420 H HA   . ALA   A 1 154 ? 13.366 -4.527  8.655   1.00 14.96 ?  154 ALA   A HA   1 
ATOM   2421 H HB1  . ALA   A 1 154 ? 14.301 -2.407  8.984   1.00 15.77 ?  154 ALA   A HB1  1 
ATOM   2422 H HB2  . ALA   A 1 154 ? 15.221 -3.499  9.678   1.00 15.77 ?  154 ALA   A HB2  1 
ATOM   2423 H HB3  . ALA   A 1 154 ? 15.643 -2.880  8.277   1.00 15.77 ?  154 ALA   A HB3  1 
ATOM   2424 N N    . VAL   A 1 155 ? 12.298 -3.688  6.622   1.00 13.19 ?  155 VAL   A N    1 
ATOM   2425 C CA   . VAL   A 1 155 ? 11.641 -3.204  5.413   1.00 14.21 ?  155 VAL   A CA   1 
ATOM   2426 C C    . VAL   A 1 155 ? 10.898 -1.924  5.776   1.00 16.15 ?  155 VAL   A C    1 
ATOM   2427 O O    . VAL   A 1 155 ? 9.970  -1.954  6.591   1.00 16.40 ?  155 VAL   A O    1 
ATOM   2428 C CB   . VAL   A 1 155 ? 10.691 -4.259  4.826   1.00 14.03 ?  155 VAL   A CB   1 
ATOM   2429 C CG1  . VAL   A 1 155 ? 9.978  -3.704  3.606   1.00 15.24 ?  155 VAL   A CG1  1 
ATOM   2430 C CG2  . VAL   A 1 155 ? 11.466 -5.527  4.466   1.00 14.75 ?  155 VAL   A CG2  1 
ATOM   2431 H H    . VAL   A 1 155 ? 11.743 -3.941  7.233   1.00 15.83 ?  155 VAL   A H    1 
ATOM   2432 H HA   . VAL   A 1 155 ? 12.311 -2.991  4.749   1.00 17.06 ?  155 VAL   A HA   1 
ATOM   2433 H HB   . VAL   A 1 155 ? 10.022 -4.493  5.493   1.00 16.84 ?  155 VAL   A HB   1 
ATOM   2434 H HG11 . VAL   A 1 155 ? 9.537  -4.432  3.142   1.00 18.30 ?  155 VAL   A HG11 1 
ATOM   2435 H HG12 . VAL   A 1 155 ? 9.318  -3.050  3.893   1.00 18.30 ?  155 VAL   A HG12 1 
ATOM   2436 H HG13 . VAL   A 1 155 ? 10.629 -3.285  3.025   1.00 18.30 ?  155 VAL   A HG13 1 
ATOM   2437 H HG21 . VAL   A 1 155 ? 10.860 -6.164  4.059   1.00 17.70 ?  155 VAL   A HG21 1 
ATOM   2438 H HG22 . VAL   A 1 155 ? 12.172 -5.296  3.841   1.00 17.70 ?  155 VAL   A HG22 1 
ATOM   2439 H HG23 . VAL   A 1 155 ? 11.852 -5.905  5.273   1.00 17.70 ?  155 VAL   A HG23 1 
ATOM   2440 N N    . PHE   A 1 156 ? 11.313 -0.803  5.176   1.00 18.05 ?  156 PHE   A N    1 
ATOM   2441 C CA   . PHE   A 1 156 ? 10.767 0.502   5.547   1.00 20.16 ?  156 PHE   A CA   1 
ATOM   2442 C C    . PHE   A 1 156 ? 9.295  0.635   5.173   1.00 20.29 ?  156 PHE   A C    1 
ATOM   2443 O O    . PHE   A 1 156 ? 8.494  1.167   5.953   1.00 21.33 ?  156 PHE   A O    1 
ATOM   2444 C CB   . PHE   A 1 156 ? 11.585 1.597   4.862   1.00 21.63 ?  156 PHE   A CB   1 
ATOM   2445 C CG   . PHE   A 1 156 ? 11.122 2.989   5.170   1.00 23.27 ?  156 PHE   A CG   1 
ATOM   2446 C CD1  . PHE   A 1 156 ? 11.075 3.437   6.477   1.00 24.32 ?  156 PHE   A CD1  1 
ATOM   2447 C CD2  . PHE   A 1 156 ? 10.758 3.856   4.150   1.00 24.01 ?  156 PHE   A CD2  1 
ATOM   2448 C CE1  . PHE   A 1 156 ? 10.658 4.721   6.767   1.00 25.37 ?  156 PHE   A CE1  1 
ATOM   2449 C CE2  . PHE   A 1 156 ? 10.340 5.143   4.432   1.00 25.15 ?  156 PHE   A CE2  1 
ATOM   2450 C CZ   . PHE   A 1 156 ? 10.294 5.577   5.743   1.00 25.53 ?  156 PHE   A CZ   1 
ATOM   2451 H H    . PHE   A 1 156 ? 11.913 -0.776  4.562   1.00 21.67 ?  156 PHE   A H    1 
ATOM   2452 H HA   . PHE   A 1 156 ? 10.850 0.621   6.505   1.00 24.19 ?  156 PHE   A HA   1 
ATOM   2453 H HB2  . PHE   A 1 156 ? 12.510 1.524   5.150   1.00 25.96 ?  156 PHE   A HB2  1 
ATOM   2454 H HB3  . PHE   A 1 156 ? 11.532 1.473   3.902   1.00 25.96 ?  156 PHE   A HB3  1 
ATOM   2455 H HD1  . PHE   A 1 156 ? 11.322 2.864   7.168   1.00 29.19 ?  156 PHE   A HD1  1 
ATOM   2456 H HD2  . PHE   A 1 156 ? 10.789 3.563   3.267   1.00 28.81 ?  156 PHE   A HD2  1 
ATOM   2457 H HE1  . PHE   A 1 156 ? 10.626 5.014   7.649   1.00 30.44 ?  156 PHE   A HE1  1 
ATOM   2458 H HE2  . PHE   A 1 156 ? 10.092 5.714   3.740   1.00 30.19 ?  156 PHE   A HE2  1 
ATOM   2459 H HZ   . PHE   A 1 156 ? 10.009 6.443   5.936   1.00 30.64 ?  156 PHE   A HZ   1 
ATOM   2460 N N    . ASP   A 1 157 ? 8.927  0.185   3.980   1.00 19.91 ?  157 ASP   A N    1 
ATOM   2461 C CA   . ASP   A 1 157 ? 7.599  0.424   3.429   1.00 20.91 ?  157 ASP   A CA   1 
ATOM   2462 C C    . ASP   A 1 157 ? 6.625  -0.643  3.919   1.00 20.51 ?  157 ASP   A C    1 
ATOM   2463 O O    . ASP   A 1 157 ? 6.829  -1.836  3.667   1.00 19.53 ?  157 ASP   A O    1 
ATOM   2464 C CB   . ASP   A 1 157 ? 7.673  0.405   1.906   1.00 22.69 ?  157 ASP   A CB   1 
ATOM   2465 C CG   . ASP   A 1 157 ? 6.392  0.883   1.264   1.00 24.97 ?  157 ASP   A CG   1 
ATOM   2466 O OD1  . ASP   A 1 157 ? 6.112  2.097   1.320   1.00 27.02 ?  157 ASP   A OD1  1 
ATOM   2467 O OD2  . ASP   A 1 157 ? 5.647  0.044   0.720   1.00 25.14 -1 157 ASP   A OD2  1 
ATOM   2468 H H    . ASP   A 1 157 ? 9.443  -0.266  3.459   1.00 23.89 ?  157 ASP   A H    1 
ATOM   2469 H HA   . ASP   A 1 157 ? 7.279  1.293   3.717   1.00 25.10 ?  157 ASP   A HA   1 
ATOM   2470 H HB2  . ASP   A 1 157 ? 8.412  0.970   1.622   1.00 27.23 ?  157 ASP   A HB2  1 
ATOM   2471 H HB3  . ASP   A 1 157 ? 7.824  -0.504  1.608   1.00 27.23 ?  157 ASP   A HB3  1 
ATOM   2472 N N    . LYS   A 1 158 ? 5.558  -0.212  4.601   1.00 21.58 ?  158 LYS   A N    1 
ATOM   2473 C CA   . LYS   A 1 158 ? 4.594  -1.159  5.158   1.00 22.42 ?  158 LYS   A CA   1 
ATOM   2474 C C    . LYS   A 1 158 ? 3.891  -1.947  4.059   1.00 21.36 ?  158 LYS   A C    1 
ATOM   2475 O O    . LYS   A 1 158 ? 3.717  -3.168  4.170   1.00 21.37 ?  158 LYS   A O    1 
ATOM   2476 C CB   . LYS   A 1 158 ? 3.584  -0.414  6.036   1.00 24.13 ?  158 LYS   A CB   1 
ATOM   2477 C CG   . LYS   A 1 158 ? 2.381  -1.246  6.480   1.00 25.93 ?  158 LYS   A CG   1 
ATOM   2478 C CD   . LYS   A 1 158 ? 2.783  -2.469  7.302   1.00 27.43 ?  158 LYS   A CD   1 
ATOM   2479 C CE   . LYS   A 1 158 ? 1.547  -3.206  7.809   1.00 28.42 ?  158 LYS   A CE   1 
ATOM   2480 N NZ   . LYS   A 1 158 ? 1.874  -4.514  8.443   1.00 29.00 ?  158 LYS   A NZ   1 
ATOM   2481 H H    . LYS   A 1 158 ? 5.379  0.614   4.752   1.00 25.89 ?  158 LYS   A H    1 
ATOM   2482 H HA   . LYS   A 1 158 ? 5.067  -1.788  5.726   1.00 26.91 ?  158 LYS   A HA   1 
ATOM   2483 H HB2  . LYS   A 1 158 ? 4.037  -0.104  6.840   1.00 28.96 ?  158 LYS   A HB2  1 
ATOM   2484 H HB3  . LYS   A 1 158 ? 3.247  0.352   5.543   1.00 28.96 ?  158 LYS   A HB3  1 
ATOM   2485 H HG2  . LYS   A 1 158 ? 1.807  -0.692  7.031   1.00 31.12 ?  158 LYS   A HG2  1 
ATOM   2486 H HG3  . LYS   A 1 158 ? 1.892  -1.549  5.699   1.00 31.12 ?  158 LYS   A HG3  1 
ATOM   2487 H HD2  . LYS   A 1 158 ? 3.298  -3.073  6.747   1.00 32.92 ?  158 LYS   A HD2  1 
ATOM   2488 H HD3  . LYS   A 1 158 ? 3.307  -2.180  8.067   1.00 32.92 ?  158 LYS   A HD3  1 
ATOM   2489 H HE2  . LYS   A 1 158 ? 1.098  -2.654  8.468   1.00 34.11 ?  158 LYS   A HE2  1 
ATOM   2490 H HE3  . LYS   A 1 158 ? 0.954  -3.374  7.060   1.00 34.11 ?  158 LYS   A HE3  1 
ATOM   2491 H HZ1  . LYS   A 1 158 ? 1.128  -4.909  8.723   1.00 34.81 ?  158 LYS   A HZ1  1 
ATOM   2492 H HZ2  . LYS   A 1 158 ? 2.280  -5.044  7.855   1.00 34.81 ?  158 LYS   A HZ2  1 
ATOM   2493 H HZ3  . LYS   A 1 158 ? 2.414  -4.387  9.139   1.00 34.81 ?  158 LYS   A HZ3  1 
ATOM   2494 N N    A ASN   A 1 159 ? 3.472  -1.266  2.991   0.88 22.35 ?  159 ASN   A N    1 
ATOM   2495 N N    B ASN   A 1 159 ? 3.477  -1.269  2.986   0.12 20.91 ?  159 ASN   A N    1 
ATOM   2496 C CA   A ASN   A 1 159 ? 2.824  -1.967  1.891   0.88 22.91 ?  159 ASN   A CA   1 
ATOM   2497 C CA   B ASN   A 1 159 ? 2.823  -1.969  1.886   0.12 20.63 ?  159 ASN   A CA   1 
ATOM   2498 C C    A ASN   A 1 159 ? 3.742  -3.035  1.306   0.88 21.46 ?  159 ASN   A C    1 
ATOM   2499 C C    B ASN   A 1 159 ? 3.738  -3.030  1.289   0.12 20.17 ?  159 ASN   A C    1 
ATOM   2500 O O    A ASN   A 1 159 ? 3.307  -4.162  1.038   0.88 21.25 ?  159 ASN   A O    1 
ATOM   2501 O O    B ASN   A 1 159 ? 3.293  -4.139  0.972   0.12 20.07 ?  159 ASN   A O    1 
ATOM   2502 C CB   A ASN   A 1 159 ? 2.372  -0.963  0.829   0.88 25.53 ?  159 ASN   A CB   1 
ATOM   2503 C CB   B ASN   A 1 159 ? 2.381  -0.975  0.812   0.12 21.03 ?  159 ASN   A CB   1 
ATOM   2504 C CG   A ASN   A 1 159 ? 1.170  -0.156  1.275   0.88 28.26 ?  159 ASN   A CG   1 
ATOM   2505 C CG   B ASN   A 1 159 ? 0.891  -0.703  0.848   0.12 21.45 ?  159 ASN   A CG   1 
ATOM   2506 O OD1  A ASN   A 1 159 ? 0.294  -0.673  1.965   0.88 29.50 ?  159 ASN   A OD1  1 
ATOM   2507 O OD1  B ASN   A 1 159 ? 0.295  -0.592  1.920   0.12 21.73 ?  159 ASN   A OD1  1 
ATOM   2508 N ND2  A ASN   A 1 159 ? 1.121  1.117   0.888   0.88 29.23 ?  159 ASN   A ND2  1 
ATOM   2509 N ND2  B ASN   A 1 159 ? 0.277  -0.607  -0.326  0.12 21.42 ?  159 ASN   A ND2  1 
ATOM   2510 H H    A ASN   A 1 159 ? 3.557  -0.418  2.885   0.88 26.82 ?  159 ASN   A H    1 
ATOM   2511 H H    B ASN   A 1 159 ? 3.564  -0.422  2.878   0.12 25.10 ?  159 ASN   A H    1 
ATOM   2512 H HA   A ASN   A 1 159 ? 2.035  -2.413  2.231   0.88 27.50 ?  159 ASN   A HA   1 
ATOM   2513 H HA   B ASN   A 1 159 ? 2.032  -2.416  2.223   0.12 24.76 ?  159 ASN   A HA   1 
ATOM   2514 H HB2  A ASN   A 1 159 ? 3.094  -0.344  0.645   0.88 30.64 ?  159 ASN   A HB2  1 
ATOM   2515 H HB2  B ASN   A 1 159 ? 2.842  -0.132  0.948   0.12 25.24 ?  159 ASN   A HB2  1 
ATOM   2516 H HB3  A ASN   A 1 159 ? 2.127  -1.443  0.023   0.88 30.64 ?  159 ASN   A HB3  1 
ATOM   2517 H HB3  B ASN   A 1 159 ? 2.598  -1.335  -0.061  0.12 25.24 ?  159 ASN   A HB3  1 
ATOM   2518 H HD21 A ASN   A 1 159 ? 0.458  1.614   1.119   0.88 35.07 ?  159 ASN   A HD21 1 
ATOM   2519 H HD21 B ASN   A 1 159 ? -0.569 -0.456  -0.361  0.12 25.71 ?  159 ASN   A HD21 1 
ATOM   2520 H HD22 A ASN   A 1 159 ? 1.757  1.443   0.412   0.88 35.07 ?  159 ASN   A HD22 1 
ATOM   2521 H HD22 B ASN   A 1 159 ? 0.727  -0.694  -1.054  0.12 25.71 ?  159 ASN   A HD22 1 
ATOM   2522 N N    . LEU   A 1 160 ? 5.024  -2.711  1.132   1.00 19.92 ?  160 LEU   A N    1 
ATOM   2523 C CA   . LEU   A 1 160 ? 5.964  -3.695  0.608   1.00 19.12 ?  160 LEU   A CA   1 
ATOM   2524 C C    . LEU   A 1 160 ? 6.161  -4.843  1.587   1.00 18.14 ?  160 LEU   A C    1 
ATOM   2525 O O    . LEU   A 1 160 ? 6.195  -6.013  1.183   1.00 18.61 ?  160 LEU   A O    1 
ATOM   2526 C CB   . LEU   A 1 160 ? 7.299  -3.028  0.288   1.00 18.98 ?  160 LEU   A CB   1 
ATOM   2527 C CG   . LEU   A 1 160 ? 8.389  -4.008  -0.142  1.00 19.41 ?  160 LEU   A CG   1 
ATOM   2528 C CD1  . LEU   A 1 160 ? 7.945  -4.771  -1.373  1.00 20.01 ?  160 LEU   A CD1  1 
ATOM   2529 C CD2  . LEU   A 1 160 ? 9.700  -3.290  -0.395  1.00 19.69 ?  160 LEU   A CD2  1 
ATOM   2530 H H    A LEU   A 1 160 ? 5.369  -1.943  1.316   0.88 23.91 ?  160 LEU   A H    1 
ATOM   2531 H H    B LEU   A 1 160 ? 5.369  -1.944  1.322   0.12 23.91 ?  160 LEU   A H    1 
ATOM   2532 H HA   . LEU   A 1 160 ? 5.606  -4.059  -0.212  1.00 22.95 ?  160 LEU   A HA   1 
ATOM   2533 H HB2  . LEU   A 1 160 ? 7.168  -2.386  -0.434  1.00 22.78 ?  160 LEU   A HB2  1 
ATOM   2534 H HB3  . LEU   A 1 160 ? 7.616  -2.567  1.080   1.00 22.78 ?  160 LEU   A HB3  1 
ATOM   2535 H HG   . LEU   A 1 160 ? 8.541  -4.648  0.568   1.00 23.29 ?  160 LEU   A HG   1 
ATOM   2536 H HD11 . LEU   A 1 160 ? 8.686  -5.302  -1.693  1.00 24.01 ?  160 LEU   A HD11 1 
ATOM   2537 H HD12 . LEU   A 1 160 ? 7.202  -5.349  -1.137  1.00 24.01 ?  160 LEU   A HD12 1 
ATOM   2538 H HD13 . LEU   A 1 160 ? 7.668  -4.137  -2.054  1.00 24.01 ?  160 LEU   A HD13 1 
ATOM   2539 H HD21 . LEU   A 1 160 ? 10.369 -3.940  -0.663  1.00 23.64 ?  160 LEU   A HD21 1 
ATOM   2540 H HD22 . LEU   A 1 160 ? 9.573  -2.636  -1.101  1.00 23.64 ?  160 LEU   A HD22 1 
ATOM   2541 H HD23 . LEU   A 1 160 ? 9.980  -2.845  0.421   1.00 23.64 ?  160 LEU   A HD23 1 
ATOM   2542 N N    . TYR   A 1 161 ? 6.310  -4.528  2.874   1.00 17.27 ?  161 TYR   A N    1 
ATOM   2543 C CA   . TYR   A 1 161 ? 6.449  -5.574  3.882   1.00 16.80 ?  161 TYR   A CA   1 
ATOM   2544 C C    . TYR   A 1 161 ? 5.305  -6.580  3.792   1.00 17.02 ?  161 TYR   A C    1 
ATOM   2545 O O    . TYR   A 1 161 ? 5.523  -7.795  3.783   1.00 16.91 ?  161 TYR   A O    1 
ATOM   2546 C CB   . TYR   A 1 161 ? 6.517  -4.945  5.276   1.00 17.02 ?  161 TYR   A CB   1 
ATOM   2547 C CG   . TYR   A 1 161 ? 6.421  -5.966  6.375   1.00 16.28 ?  161 TYR   A CG   1 
ATOM   2548 C CD1  . TYR   A 1 161 ? 7.546  -6.647  6.811   1.00 15.98 ?  161 TYR   A CD1  1 
ATOM   2549 C CD2  . TYR   A 1 161 ? 5.201  -6.265  6.969   1.00 16.58 ?  161 TYR   A CD2  1 
ATOM   2550 C CE1  . TYR   A 1 161 ? 7.463  -7.597  7.808   1.00 16.28 ?  161 TYR   A CE1  1 
ATOM   2551 C CE2  . TYR   A 1 161 ? 5.107  -7.210  7.967   1.00 16.35 ?  161 TYR   A CE2  1 
ATOM   2552 C CZ   . TYR   A 1 161 ? 6.241  -7.880  8.383   1.00 16.73 ?  161 TYR   A CZ   1 
ATOM   2553 O OH   . TYR   A 1 161 ? 6.162  -8.834  9.378   1.00 17.88 ?  161 TYR   A OH   1 
ATOM   2554 H H    . TYR   A 1 161 ? 6.326  -3.727  3.188   1.00 20.73 ?  161 TYR   A H    1 
ATOM   2555 H HA   . TYR   A 1 161 ? 7.276  -6.051  3.733   1.00 20.16 ?  161 TYR   A HA   1 
ATOM   2556 H HB2  . TYR   A 1 161 ? 7.363  -4.480  5.372   1.00 20.43 ?  161 TYR   A HB2  1 
ATOM   2557 H HB3  . TYR   A 1 161 ? 5.782  -4.321  5.381   1.00 20.43 ?  161 TYR   A HB3  1 
ATOM   2558 H HD1  . TYR   A 1 161 ? 8.370  -6.461  6.424   1.00 19.18 ?  161 TYR   A HD1  1 
ATOM   2559 H HD2  . TYR   A 1 161 ? 4.432  -5.821  6.691   1.00 19.91 ?  161 TYR   A HD2  1 
ATOM   2560 H HE1  . TYR   A 1 161 ? 8.228  -8.046  8.092   1.00 19.54 ?  161 TYR   A HE1  1 
ATOM   2561 H HE2  . TYR   A 1 161 ? 4.279  -7.403  8.357   1.00 19.62 ?  161 TYR   A HE2  1 
ATOM   2562 H HH   . TYR   A 1 161 ? 5.361  -8.909  9.643   1.00 21.46 ?  161 TYR   A HH   1 
ATOM   2563 N N    . ASP   A 1 162 ? 4.069  -6.087  3.720   1.00 18.00 ?  162 ASP   A N    1 
ATOM   2564 C CA   . ASP   A 1 162 ? 2.922  -6.991  3.662   1.00 18.77 ?  162 ASP   A CA   1 
ATOM   2565 C C    . ASP   A 1 162 ? 2.958  -7.845  2.400   1.00 18.94 ?  162 ASP   A C    1 
ATOM   2566 O O    . ASP   A 1 162 ? 2.596  -9.029  2.430   1.00 19.44 ?  162 ASP   A O    1 
ATOM   2567 C CB   . ASP   A 1 162 ? 1.614  -6.196  3.729   1.00 19.96 ?  162 ASP   A CB   1 
ATOM   2568 C CG   . ASP   A 1 162 ? 1.320  -5.644  5.112   1.00 21.52 ?  162 ASP   A CG   1 
ATOM   2569 O OD1  . ASP   A 1 162 ? 1.981  -6.047  6.086   1.00 22.63 ?  162 ASP   A OD1  1 
ATOM   2570 O OD2  . ASP   A 1 162 ? 0.398  -4.804  5.221   1.00 23.04 -1 162 ASP   A OD2  1 
ATOM   2571 H H    . ASP   A 1 162 ? 3.868  -5.255  3.709   1.00 21.61 ?  162 ASP   A H    1 
ATOM   2572 H HA   . ASP   A 1 162 ? 2.946  -7.594  4.422   1.00 22.53 ?  162 ASP   A HA   1 
ATOM   2573 H HB2  . ASP   A 1 162 ? 1.668  -5.447  3.123   1.00 23.96 ?  162 ASP   A HB2  1 
ATOM   2574 H HB3  . ASP   A 1 162 ? 0.877  -6.776  3.491   1.00 23.96 ?  162 ASP   A HB3  1 
ATOM   2575 N N    . LYS   A 1 163 ? 3.389  -7.265  1.278   1.00 20.07 ?  163 LYS   A N    1 
ATOM   2576 C CA   . LYS   A 1 163 ? 3.478  -8.035  0.042   1.00 20.78 ?  163 LYS   A CA   1 
ATOM   2577 C C    . LYS   A 1 163 ? 4.569  -9.096  0.126   1.00 19.78 ?  163 LYS   A C    1 
ATOM   2578 O O    . LYS   A 1 163 ? 4.403  -10.205 -0.394  1.00 20.56 ?  163 LYS   A O    1 
ATOM   2579 C CB   . LYS   A 1 163 ? 3.727  -7.102  -1.142  1.00 23.92 ?  163 LYS   A CB   1 
ATOM   2580 C CG   . LYS   A 1 163 ? 3.768  -7.815  -2.482  1.00 27.56 ?  163 LYS   A CG   1 
ATOM   2581 C CD   . LYS   A 1 163 ? 4.159  -6.871  -3.603  1.00 31.52 ?  163 LYS   A CD   1 
ATOM   2582 C CE   . LYS   A 1 163 ? 4.008  -7.536  -4.962  1.00 34.58 ?  163 LYS   A CE   1 
ATOM   2583 N NZ   . LYS   A 1 163 ? 4.661  -6.753  -6.045  1.00 35.69 ?  163 LYS   A NZ   1 
ATOM   2584 H H    . LYS   A 1 163 ? 3.631  -6.438  1.210   1.00 24.09 ?  163 LYS   A H    1 
ATOM   2585 H HA   . LYS   A 1 163 ? 2.630  -8.481  -0.106  1.00 24.95 ?  163 LYS   A HA   1 
ATOM   2586 H HB2  . LYS   A 1 163 ? 3.013  -6.443  -1.181  1.00 28.71 ?  163 LYS   A HB2  1 
ATOM   2587 H HB3  . LYS   A 1 163 ? 4.578  -6.656  -1.018  1.00 28.71 ?  163 LYS   A HB3  1 
ATOM   2588 H HG2  . LYS   A 1 163 ? 4.423  -8.529  -2.449  1.00 33.07 ?  163 LYS   A HG2  1 
ATOM   2589 H HG3  . LYS   A 1 163 ? 2.888  -8.176  -2.678  1.00 33.07 ?  163 LYS   A HG3  1 
ATOM   2590 H HD2  . LYS   A 1 163 ? 3.580  -6.091  -3.581  1.00 37.83 ?  163 LYS   A HD2  1 
ATOM   2591 H HD3  . LYS   A 1 163 ? 5.085  -6.605  -3.491  1.00 37.83 ?  163 LYS   A HD3  1 
ATOM   2592 H HE2  . LYS   A 1 163 ? 4.402  -8.421  -4.940  1.00 41.50 ?  163 LYS   A HE2  1 
ATOM   2593 H HE3  . LYS   A 1 163 ? 3.067  -7.606  -5.171  1.00 41.50 ?  163 LYS   A HE3  1 
ATOM   2594 H HZ1  . LYS   A 1 163 ? 4.558  -7.170  -6.825  1.00 42.83 ?  163 LYS   A HZ1  1 
ATOM   2595 H HZ2  . LYS   A 1 163 ? 4.293  -5.945  -6.098  1.00 42.83 ?  163 LYS   A HZ2  1 
ATOM   2596 H HZ3  . LYS   A 1 163 ? 5.531  -6.665  -5.877  1.00 42.83 ?  163 LYS   A HZ3  1 
ATOM   2597 N N    . LEU   A 1 164 ? 5.697  -8.769  0.762   1.00 17.86 ?  164 LEU   A N    1 
ATOM   2598 C CA   . LEU   A 1 164 ? 6.784  -9.735  0.902   1.00 16.90 ?  164 LEU   A CA   1 
ATOM   2599 C C    . LEU   A 1 164 ? 6.357  -10.923 1.753   1.00 16.63 ?  164 LEU   A C    1 
ATOM   2600 O O    . LEU   A 1 164 ? 6.661  -12.077 1.428   1.00 16.91 ?  164 LEU   A O    1 
ATOM   2601 C CB   . LEU   A 1 164 ? 7.993  -9.050  1.533   1.00 16.43 ?  164 LEU   A CB   1 
ATOM   2602 C CG   . LEU   A 1 164 ? 8.743  -8.059  0.644   1.00 16.47 ?  164 LEU   A CG   1 
ATOM   2603 C CD1  . LEU   A 1 164 ? 9.659  -7.184  1.485   1.00 16.21 ?  164 LEU   A CD1  1 
ATOM   2604 C CD2  . LEU   A 1 164 ? 9.535  -8.783  -0.432  1.00 17.23 ?  164 LEU   A CD2  1 
ATOM   2605 H H    . LEU   A 1 164 ? 5.853  -8.000  1.119   1.00 21.43 ?  164 LEU   A H    1 
ATOM   2606 H HA   . LEU   A 1 164 ? 7.037  -10.061 0.028   1.00 20.28 ?  164 LEU   A HA   1 
ATOM   2607 H HB2  . LEU   A 1 164 ? 7.697  -8.561  2.316   1.00 19.72 ?  164 LEU   A HB2  1 
ATOM   2608 H HB3  . LEU   A 1 164 ? 8.628  -9.731  1.798   1.00 19.72 ?  164 LEU   A HB3  1 
ATOM   2609 H HG   . LEU   A 1 164 ? 8.104  -7.478  0.205   1.00 19.77 ?  164 LEU   A HG   1 
ATOM   2610 H HD11 . LEU   A 1 164 ? 10.135 -6.566  0.904   1.00 19.46 ?  164 LEU   A HD11 1 
ATOM   2611 H HD12 . LEU   A 1 164 ? 9.125  -6.686  2.125   1.00 19.46 ?  164 LEU   A HD12 1 
ATOM   2612 H HD13 . LEU   A 1 164 ? 10.296 -7.747  1.956   1.00 19.46 ?  164 LEU   A HD13 1 
ATOM   2613 H HD21 . LEU   A 1 164 ? 10.036 -8.130  -0.949  1.00 20.68 ?  164 LEU   A HD21 1 
ATOM   2614 H HD22 . LEU   A 1 164 ? 10.145 -9.407  -0.011  1.00 20.68 ?  164 LEU   A HD22 1 
ATOM   2615 H HD23 . LEU   A 1 164 ? 8.919  -9.258  -1.010  1.00 20.68 ?  164 LEU   A HD23 1 
ATOM   2616 N N    . VAL   A 1 165 ? 5.667  -10.655 2.860   1.00 16.30 ?  165 VAL   A N    1 
ATOM   2617 C CA   . VAL   A 1 165 ? 5.193  -11.731 3.722   1.00 16.44 ?  165 VAL   A CA   1 
ATOM   2618 C C    . VAL   A 1 165 ? 4.156  -12.575 2.994   1.00 16.42 ?  165 VAL   A C    1 
ATOM   2619 O O    . VAL   A 1 165 ? 4.248  -13.808 2.955   1.00 16.25 ?  165 VAL   A O    1 
ATOM   2620 C CB   . VAL   A 1 165 ? 4.634  -11.144 5.031   1.00 17.01 ?  165 VAL   A CB   1 
ATOM   2621 C CG1  . VAL   A 1 165 ? 3.883  -12.205 5.823   1.00 17.60 ?  165 VAL   A CG1  1 
ATOM   2622 C CG2  . VAL   A 1 165 ? 5.754  -10.528 5.858   1.00 17.64 ?  165 VAL   A CG2  1 
ATOM   2623 H H    . VAL   A 1 165 ? 5.458  -9.867  3.132   1.00 19.57 ?  165 VAL   A H    1 
ATOM   2624 H HA   . VAL   A 1 165 ? 5.938  -12.307 3.951   1.00 19.73 ?  165 VAL   A HA   1 
ATOM   2625 H HB   . VAL   A 1 165 ? 4.006  -10.437 4.815   1.00 20.42 ?  165 VAL   A HB   1 
ATOM   2626 H HG11 . VAL   A 1 165 ? 3.788  -11.902 6.741   1.00 21.12 ?  165 VAL   A HG11 1 
ATOM   2627 H HG12 . VAL   A 1 165 ? 3.004  -12.331 5.428   1.00 21.12 ?  165 VAL   A HG12 1 
ATOM   2628 H HG13 . VAL   A 1 165 ? 4.384  -13.031 5.798   1.00 21.12 ?  165 VAL   A HG13 1 
ATOM   2629 H HG21 . VAL   A 1 165 ? 5.382  -10.166 6.679   1.00 21.17 ?  165 VAL   A HG21 1 
ATOM   2630 H HG22 . VAL   A 1 165 ? 6.409  -11.212 6.066   1.00 21.17 ?  165 VAL   A HG22 1 
ATOM   2631 H HG23 . VAL   A 1 165 ? 6.171  -9.816  5.345   1.00 21.17 ?  165 VAL   A HG23 1 
ATOM   2632 N N    . SER   A 1 166 ? 3.152  -11.921 2.403   1.00 17.20 ?  166 SER   A N    1 
ATOM   2633 C CA   . SER   A 1 166 ? 2.022  -12.653 1.842   1.00 18.42 ?  166 SER   A CA   1 
ATOM   2634 C C    . SER   A 1 166 ? 2.421  -13.497 0.642   1.00 19.22 ?  166 SER   A C    1 
ATOM   2635 O O    . SER   A 1 166 ? 1.760  -14.502 0.349   1.00 20.96 ?  166 SER   A O    1 
ATOM   2636 C CB   . SER   A 1 166 ? 0.907  -11.683 1.446   1.00 20.52 ?  166 SER   A CB   1 
ATOM   2637 O OG   . SER   A 1 166 ? 0.307  -11.089 2.584   1.00 23.01 ?  166 SER   A OG   1 
ATOM   2638 H H    . SER   A 1 166 ? 3.100  -11.071 2.323   1.00 20.65 ?  166 SER   A H    1 
ATOM   2639 H HA   . SER   A 1 166 ? 1.660  -13.251 2.515   1.00 22.10 ?  166 SER   A HA   1 
ATOM   2640 H HB2  . SER   A 1 166 ? 1.274  -10.993 0.873   1.00 24.63 ?  166 SER   A HB2  1 
ATOM   2641 H HB3  . SER   A 1 166 ? 0.212  -12.170 0.970   1.00 24.63 ?  166 SER   A HB3  1 
ATOM   2642 H HG   . SER   A 1 166 ? -0.282 -10.539 2.350   1.00 27.61 ?  166 SER   A HG   1 
ATOM   2643 N N    . SER   A 1 167 ? 3.480  -13.110 -0.066  1.00 18.66 ?  167 SER   A N    1 
ATOM   2644 C CA   . SER   A 1 167 ? 3.925  -13.833 -1.247  1.00 19.48 ?  167 SER   A CA   1 
ATOM   2645 C C    . SER   A 1 167 ? 5.087  -14.774 -0.963  1.00 19.14 ?  167 SER   A C    1 
ATOM   2646 O O    . SER   A 1 167 ? 5.596  -15.403 -1.896  1.00 20.31 ?  167 SER   A O    1 
ATOM   2647 C CB   . SER   A 1 167 ? 4.321  -12.846 -2.354  1.00 20.40 ?  167 SER   A CB   1 
ATOM   2648 O OG   . SER   A 1 167 ? 5.394  -12.013 -1.939  1.00 20.58 ?  167 SER   A OG   1 
ATOM   2649 H H    . SER   A 1 167 ? 3.960  -12.420 0.123   1.00 22.39 ?  167 SER   A H    1 
ATOM   2650 H HA   . SER   A 1 167 ? 3.185  -14.362 -1.582  1.00 23.38 ?  167 SER   A HA   1 
ATOM   2651 H HB2  . SER   A 1 167 ? 4.599  -13.348 -3.136  1.00 24.48 ?  167 SER   A HB2  1 
ATOM   2652 H HB3  . SER   A 1 167 ? 3.551  -12.294 -2.575  1.00 24.48 ?  167 SER   A HB3  1 
ATOM   2653 H HG   . SER   A 1 167 ? 5.156  -11.559 -1.268  1.00 24.70 ?  167 SER   A HG   1 
ATOM   2654 N N    . PHE   A 1 168 ? 5.517  -14.893 0.291   1.00 18.11 ?  168 PHE   A N    1 
ATOM   2655 C CA   . PHE   A 1 168 ? 6.699  -15.690 0.590   1.00 18.57 ?  168 PHE   A CA   1 
ATOM   2656 C C    . PHE   A 1 168 ? 6.387  -17.176 0.505   1.00 21.35 ?  168 PHE   A C    1 
ATOM   2657 O O    . PHE   A 1 168 ? 5.437  -17.663 1.127   1.00 22.40 ?  168 PHE   A O    1 
ATOM   2658 C CB   . PHE   A 1 168 ? 7.234  -15.378 1.983   1.00 16.96 ?  168 PHE   A CB   1 
ATOM   2659 C CG   . PHE   A 1 168 ? 8.498  -16.123 2.302   1.00 15.97 ?  168 PHE   A CG   1 
ATOM   2660 C CD1  . PHE   A 1 168 ? 9.678  -15.771 1.684   1.00 16.62 ?  168 PHE   A CD1  1 
ATOM   2661 C CD2  . PHE   A 1 168 ? 8.505  -17.196 3.182   1.00 15.61 ?  168 PHE   A CD2  1 
ATOM   2662 C CE1  . PHE   A 1 168 ? 10.846 -16.450 1.948   1.00 16.35 ?  168 PHE   A CE1  1 
ATOM   2663 C CE2  . PHE   A 1 168 ? 9.682  -17.878 3.452   1.00 16.03 ?  168 PHE   A CE2  1 
ATOM   2664 C CZ   . PHE   A 1 168 ? 10.851 -17.502 2.830   1.00 16.26 ?  168 PHE   A CZ   1 
ATOM   2665 H H    . PHE   A 1 168 ? 5.151  -14.521 0.975   1.00 21.74 ?  168 PHE   A H    1 
ATOM   2666 H HA   . PHE   A 1 168 ? 7.393  -15.485 -0.058  1.00 22.29 ?  168 PHE   A HA   1 
ATOM   2667 H HB2  . PHE   A 1 168 ? 7.423  -14.428 2.040   1.00 20.36 ?  168 PHE   A HB2  1 
ATOM   2668 H HB3  . PHE   A 1 168 ? 6.564  -15.623 2.638   1.00 20.36 ?  168 PHE   A HB3  1 
ATOM   2669 H HD1  . PHE   A 1 168 ? 9.690  -15.059 1.086   1.00 19.95 ?  168 PHE   A HD1  1 
ATOM   2670 H HD2  . PHE   A 1 168 ? 7.714  -17.451 3.602   1.00 18.73 ?  168 PHE   A HD2  1 
ATOM   2671 H HE1  . PHE   A 1 168 ? 11.640 -16.196 1.531   1.00 19.63 ?  168 PHE   A HE1  1 
ATOM   2672 H HE2  . PHE   A 1 168 ? 9.676  -18.593 4.049   1.00 19.24 ?  168 PHE   A HE2  1 
ATOM   2673 H HZ   . PHE   A 1 168 ? 11.643 -17.960 3.010   1.00 19.52 ?  168 PHE   A HZ   1 
ATOM   2674 N N    . LEU   A 1 169 ? 7.217  -17.902 -0.236  1.00 25.82 ?  169 LEU   A N    1 
ATOM   2675 C CA   . LEU   A 1 169 ? 7.039  -19.335 -0.380  1.00 32.24 ?  169 LEU   A CA   1 
ATOM   2676 C C    . LEU   A 1 169 ? 7.957  -20.059 0.595   1.00 34.71 ?  169 LEU   A C    1 
ATOM   2677 O O    . LEU   A 1 169 ? 7.525  -20.481 1.669   1.00 35.57 ?  169 LEU   A O    1 
ATOM   2678 C CB   . LEU   A 1 169 ? 7.334  -19.768 -1.818  1.00 35.22 ?  169 LEU   A CB   1 
ATOM   2679 C CG   . LEU   A 1 169 ? 6.997  -21.217 -2.178  1.00 37.52 ?  169 LEU   A CG   1 
ATOM   2680 C CD1  . LEU   A 1 169 ? 5.598  -21.578 -1.705  1.00 38.24 ?  169 LEU   A CD1  1 
ATOM   2681 C CD2  . LEU   A 1 169 ? 7.125  -21.429 -3.679  1.00 38.20 ?  169 LEU   A CD2  1 
ATOM   2682 O OXT  . LEU   A 1 169 ? 9.150  -20.224 0.339   1.00 34.99 -1 169 LEU   A OXT  1 
ATOM   2683 H H    . LEU   A 1 169 ? 7.896  -17.587 -0.663  1.00 30.99 ?  169 LEU   A H    1 
ATOM   2684 H HA   . LEU   A 1 169 ? 6.120  -19.557 -0.171  1.00 38.69 ?  169 LEU   A HA   1 
ATOM   2685 H HB2  . LEU   A 1 169 ? 6.826  -19.200 -2.415  1.00 42.27 ?  169 LEU   A HB2  1 
ATOM   2686 H HB3  . LEU   A 1 169 ? 8.281  -19.645 -1.983  1.00 42.27 ?  169 LEU   A HB3  1 
ATOM   2687 H HG   . LEU   A 1 169 ? 7.627  -21.810 -1.738  1.00 45.02 ?  169 LEU   A HG   1 
ATOM   2688 H HD11 . LEU   A 1 169 ? 5.325  -22.403 -2.132  1.00 45.89 ?  169 LEU   A HD11 1 
ATOM   2689 H HD12 . LEU   A 1 169 ? 5.611  -21.693 -0.741  1.00 45.89 ?  169 LEU   A HD12 1 
ATOM   2690 H HD13 . LEU   A 1 169 ? 4.990  -20.862 -1.947  1.00 45.89 ?  169 LEU   A HD13 1 
ATOM   2691 H HD21 . LEU   A 1 169 ? 6.915  -22.353 -3.886  1.00 45.84 ?  169 LEU   A HD21 1 
ATOM   2692 H HD22 . LEU   A 1 169 ? 6.503  -20.839 -4.134  1.00 45.84 ?  169 LEU   A HD22 1 
ATOM   2693 H HD23 . LEU   A 1 169 ? 8.033  -21.226 -3.951  1.00 45.84 ?  169 LEU   A HD23 1 
ATOM   2694 N N    A SER   B 1 1   ? 50.790 -9.232  -23.789 0.88 26.86 ?  1   SER   B N    1 
ATOM   2695 N N    B SER   B 1 1   ? 50.759 -9.220  -23.755 0.12 26.62 ?  1   SER   B N    1 
ATOM   2696 C CA   A SER   B 1 1   ? 51.250 -10.278 -22.854 0.88 26.64 ?  1   SER   B CA   1 
ATOM   2697 C CA   B SER   B 1 1   ? 51.253 -10.230 -22.795 0.12 26.60 ?  1   SER   B CA   1 
ATOM   2698 C C    A SER   B 1 1   ? 50.162 -11.314 -22.606 0.88 25.62 ?  1   SER   B C    1 
ATOM   2699 C C    B SER   B 1 1   ? 50.200 -11.306 -22.585 0.12 26.44 ?  1   SER   B C    1 
ATOM   2700 O O    A SER   B 1 1   ? 48.971 -11.110 -22.900 0.88 25.28 ?  1   SER   B O    1 
ATOM   2701 O O    B SER   B 1 1   ? 49.053 -11.161 -23.011 0.12 26.36 ?  1   SER   B O    1 
ATOM   2702 C CB   A SER   B 1 1   ? 51.688 -9.666  -21.525 0.88 27.10 ?  1   SER   B CB   1 
ATOM   2703 C CB   B SER   B 1 1   ? 51.607 -9.574  -21.464 0.12 26.53 ?  1   SER   B CB   1 
ATOM   2704 O OG   A SER   B 1 1   ? 50.570 -9.436  -20.689 0.88 29.06 ?  1   SER   B OG   1 
ATOM   2705 O OG   B SER   B 1 1   ? 50.484 -9.546  -20.603 0.12 26.80 ?  1   SER   B OG   1 
ATOM   2706 H H1   A SER   B 1 1   ? 50.682 -9.592  -24.593 0.88 32.24 ?  1   SER   B H1   1 
ATOM   2707 H H1   B SER   B 1 1   ? 51.453 -8.775  -24.085 0.12 31.95 ?  1   SER   B H1   1 
ATOM   2708 H H2   A SER   B 1 1   ? 50.022 -8.904  -23.497 0.88 32.24 ?  1   SER   B H2   1 
ATOM   2709 H H2   B SER   B 1 1   ? 50.325 -9.632  -24.410 0.12 31.95 ?  1   SER   B H2   1 
ATOM   2710 H H3   A SER   B 1 1   ? 51.403 -8.590  -23.825 0.88 32.24 ?  1   SER   B H3   1 
ATOM   2711 H H3   B SER   B 1 1   ? 50.215 -8.662  -23.333 0.12 31.95 ?  1   SER   B H3   1 
ATOM   2712 H HA   A SER   B 1 1   ? 52.016 -10.721 -23.250 0.88 31.97 ?  1   SER   B HA   1 
ATOM   2713 H HA   B SER   B 1 1   ? 52.046 -10.641 -23.161 0.12 31.92 ?  1   SER   B HA   1 
ATOM   2714 H HB2  A SER   B 1 1   ? 52.291 -10.283 -21.083 0.88 32.53 ?  1   SER   B HB2  1 
ATOM   2715 H HB2  B SER   B 1 1   ? 52.324 -10.080 -21.054 0.12 31.84 ?  1   SER   B HB2  1 
ATOM   2716 H HB3  A SER   B 1 1   ? 52.139 -8.824  -21.696 0.88 32.53 ?  1   SER   B HB3  1 
ATOM   2717 H HB3  B SER   B 1 1   ? 51.895 -8.662  -21.627 0.12 31.84 ?  1   SER   B HB3  1 
ATOM   2718 H HG   A SER   B 1 1   ? 50.806 -8.979  -20.024 0.88 34.88 ?  1   SER   B HG   1 
ATOM   2719 H HG   B SER   B 1 1   ? 50.612 -8.989  -19.991 0.12 32.16 ?  1   SER   B HG   1 
ATOM   2720 N N    A MET   B 1 2   ? 50.599 -12.430 -22.041 0.88 25.28 ?  2   MET   B N    1 
ATOM   2721 N N    B MET   B 1 2   ? 50.597 -12.384 -21.916 0.12 26.24 ?  2   MET   B N    1 
ATOM   2722 C CA   A MET   B 1 2   ? 49.777 -13.618 -21.870 0.88 25.38 ?  2   MET   B CA   1 
ATOM   2723 C CA   B MET   B 1 2   ? 49.768 -13.573 -21.763 0.12 25.97 ?  2   MET   B CA   1 
ATOM   2724 C C    A MET   B 1 2   ? 49.528 -13.805 -20.380 0.88 23.11 ?  2   MET   B C    1 
ATOM   2725 C C    B MET   B 1 2   ? 49.492 -13.788 -20.282 0.12 24.14 ?  2   MET   B C    1 
ATOM   2726 O O    A MET   B 1 2   ? 50.459 -14.099 -19.624 0.88 23.46 ?  2   MET   B O    1 
ATOM   2727 O O    B MET   B 1 2   ? 50.385 -14.200 -19.532 0.12 24.31 ?  2   MET   B O    1 
ATOM   2728 C CB   A MET   B 1 2   ? 50.513 -14.817 -22.456 0.88 29.15 ?  2   MET   B CB   1 
ATOM   2729 C CB   B MET   B 1 2   ? 50.489 -14.775 -22.360 0.12 27.58 ?  2   MET   B CB   1 
ATOM   2730 C CG   A MET   B 1 2   ? 49.653 -16.041 -22.711 0.88 32.46 ?  2   MET   B CG   1 
ATOM   2731 C CG   B MET   B 1 2   ? 49.587 -15.935 -22.739 0.12 28.97 ?  2   MET   B CG   1 
ATOM   2732 S SD   A MET   B 1 2   ? 50.504 -17.243 -23.750 0.88 35.74 ?  2   MET   B SD   1 
ATOM   2733 S SD   B MET   B 1 2   ? 50.455 -17.132 -23.763 0.12 30.16 ?  2   MET   B SD   1 
ATOM   2734 C CE   A MET   B 1 2   ? 51.111 -16.165 -25.038 0.88 35.83 ?  2   MET   B CE   1 
ATOM   2735 C CE   B MET   B 1 2   ? 51.320 -16.025 -24.873 0.12 30.48 ?  2   MET   B CE   1 
ATOM   2736 H H    A MET   B 1 2   ? 51.399 -12.534 -21.737 0.88 30.34 ?  2   MET   B H    1 
ATOM   2737 H H    B MET   B 1 2   ? 51.368 -12.454 -21.543 0.12 31.50 ?  2   MET   B H    1 
ATOM   2738 H HA   A MET   B 1 2   ? 48.934 -13.517 -22.337 0.88 30.46 ?  2   MET   B HA   1 
ATOM   2739 H HA   B MET   B 1 2   ? 48.934 -13.456 -22.243 0.12 31.17 ?  2   MET   B HA   1 
ATOM   2740 H HB2  A MET   B 1 2   ? 50.900 -14.523 -23.290 0.88 34.99 ?  2   MET   B HB2  1 
ATOM   2741 H HB2  B MET   B 1 2   ? 50.947 -14.448 -23.145 0.12 33.10 ?  2   MET   B HB2  1 
ATOM   2742 H HB3  A MET   B 1 2   ? 51.215 -15.091 -21.851 0.88 34.99 ?  2   MET   B HB3  1 
ATOM   2743 H HB3  B MET   B 1 2   ? 51.134 -15.117 -21.727 0.12 33.10 ?  2   MET   B HB3  1 
ATOM   2744 H HG2  A MET   B 1 2   ? 49.443 -16.461 -21.860 0.88 38.95 ?  2   MET   B HG2  1 
ATOM   2745 H HG2  B MET   B 1 2   ? 49.293 -16.385 -21.932 0.12 34.77 ?  2   MET   B HG2  1 
ATOM   2746 H HG3  A MET   B 1 2   ? 48.839 -15.783 -23.169 0.88 38.95 ?  2   MET   B HG3  1 
ATOM   2747 H HG3  B MET   B 1 2   ? 48.823 -15.611 -23.236 0.12 34.77 ?  2   MET   B HG3  1 
ATOM   2748 H HE1  A MET   B 1 2   ? 51.260 -16.691 -25.827 0.88 43.00 ?  2   MET   B HE1  1 
ATOM   2749 H HE1  B MET   B 1 2   ? 51.557 -16.513 -25.662 0.12 36.57 ?  2   MET   B HE1  1 
ATOM   2750 H HE2  A MET   B 1 2   ? 50.438 -15.484 -25.207 0.88 43.00 ?  2   MET   B HE2  1 
ATOM   2751 H HE2  B MET   B 1 2   ? 50.735 -15.280 -25.104 0.12 36.57 ?  2   MET   B HE2  1 
ATOM   2752 H HE3  A MET   B 1 2   ? 51.940 -15.744 -24.749 0.88 43.00 ?  2   MET   B HE3  1 
ATOM   2753 H HE3  B MET   B 1 2   ? 52.120 -15.692 -24.428 0.12 36.57 ?  2   MET   B HE3  1 
ATOM   2754 N N    A VAL   B 1 3   ? 48.279 -13.614 -19.961 0.88 21.04 ?  3   VAL   B N    1 
ATOM   2755 N N    B VAL   B 1 3   ? 48.262 -13.507 -19.864 0.12 22.08 ?  3   VAL   B N    1 
ATOM   2756 C CA   A VAL   B 1 3   ? 47.858 -13.851 -18.587 0.88 19.71 ?  3   VAL   B CA   1 
ATOM   2757 C CA   B VAL   B 1 3   ? 47.819 -13.765 -18.501 0.12 20.02 ?  3   VAL   B CA   1 
ATOM   2758 C C    A VAL   B 1 3   ? 46.628 -14.749 -18.612 0.88 17.83 ?  3   VAL   B C    1 
ATOM   2759 C C    B VAL   B 1 3   ? 46.579 -14.646 -18.549 0.12 17.90 ?  3   VAL   B C    1 
ATOM   2760 O O    A VAL   B 1 3   ? 45.894 -14.814 -19.601 0.88 18.34 ?  3   VAL   B O    1 
ATOM   2761 O O    B VAL   B 1 3   ? 45.786 -14.591 -19.494 0.12 17.82 ?  3   VAL   B O    1 
ATOM   2762 C CB   A VAL   B 1 3   ? 47.570 -12.538 -17.820 0.88 21.42 ?  3   VAL   B CB   1 
ATOM   2763 C CB   B VAL   B 1 3   ? 47.540 -12.468 -17.710 0.12 20.23 ?  3   VAL   B CB   1 
ATOM   2764 C CG1  A VAL   B 1 3   ? 48.835 -11.683 -17.723 0.88 22.16 ?  3   VAL   B CG1  1 
ATOM   2765 C CG1  B VAL   B 1 3   ? 48.800 -11.619 -17.611 0.12 20.32 ?  3   VAL   B CG1  1 
ATOM   2766 C CG2  A VAL   B 1 3   ? 46.436 -11.765 -18.481 0.88 22.12 ?  3   VAL   B CG2  1 
ATOM   2767 C CG2  B VAL   B 1 3   ? 46.404 -11.685 -18.348 0.12 20.32 ?  3   VAL   B CG2  1 
ATOM   2768 H H    A VAL   B 1 3   ? 47.641 -13.348 -20.471 0.88 25.25 ?  3   VAL   B H    1 
ATOM   2769 H H    B VAL   B 1 3   ? 47.660 -13.155 -20.367 0.12 26.50 ?  3   VAL   B H    1 
ATOM   2770 H HA   A VAL   B 1 3   ? 48.558 -14.322 -18.110 0.88 23.66 ?  3   VAL   B HA   1 
ATOM   2771 H HA   B VAL   B 1 3   ? 48.514 -14.252 -18.035 0.12 24.03 ?  3   VAL   B HA   1 
ATOM   2772 H HB   A VAL   B 1 3   ? 47.295 -12.752 -16.916 0.88 25.71 ?  3   VAL   B HB   1 
ATOM   2773 H HB   B VAL   B 1 3   ? 47.270 -12.705 -16.809 0.12 24.27 ?  3   VAL   B HB   1 
ATOM   2774 H HG11 A VAL   B 1 3   ? 48.633 -10.871 -17.231 0.88 26.60 ?  3   VAL   B HG11 1 
ATOM   2775 H HG11 B VAL   B 1 3   ? 48.604 -10.824 -17.092 0.12 24.39 ?  3   VAL   B HG11 1 
ATOM   2776 H HG12 A VAL   B 1 3   ? 49.522 -12.187 -17.259 0.88 26.60 ?  3   VAL   B HG12 1 
ATOM   2777 H HG12 B VAL   B 1 3   ? 49.495 -12.136 -17.175 0.12 24.39 ?  3   VAL   B HG12 1 
ATOM   2778 H HG13 A VAL   B 1 3   ? 49.136 -11.460 -18.618 0.88 26.60 ?  3   VAL   B HG13 1 
ATOM   2779 H HG13 B VAL   B 1 3   ? 49.084 -11.370 -18.504 0.12 24.39 ?  3   VAL   B HG13 1 
ATOM   2780 H HG21 A VAL   B 1 3   ? 46.381 -10.883 -18.083 0.88 26.55 ?  3   VAL   B HG21 1 
ATOM   2781 H HG21 B VAL   B 1 3   ? 46.351 -10.813 -17.929 0.12 24.39 ?  3   VAL   B HG21 1 
ATOM   2782 H HG22 A VAL   B 1 3   ? 46.616 -11.690 -19.430 0.88 26.55 ?  3   VAL   B HG22 1 
ATOM   2783 H HG22 B VAL   B 1 3   ? 46.583 -11.587 -19.296 0.12 24.39 ?  3   VAL   B HG22 1 
ATOM   2784 H HG23 A VAL   B 1 3   ? 45.604 -12.244 -18.338 0.88 26.55 ?  3   VAL   B HG23 1 
ATOM   2785 H HG23 B VAL   B 1 3   ? 45.573 -12.167 -18.216 0.12 24.39 ?  3   VAL   B HG23 1 
ATOM   2786 N N    . ASN   B 1 4   ? 46.415 -15.462 -17.509 1.00 15.99 ?  4   ASN   B N    1 
ATOM   2787 C CA   . ASN   B 1 4   ? 45.283 -16.382 -17.400 1.00 14.74 ?  4   ASN   B CA   1 
ATOM   2788 C C    . ASN   B 1 4   ? 45.233 -17.344 -18.587 1.00 14.86 ?  4   ASN   B C    1 
ATOM   2789 O O    . ASN   B 1 4   ? 44.173 -17.603 -19.156 1.00 15.72 ?  4   ASN   B O    1 
ATOM   2790 C CB   . ASN   B 1 4   ? 43.959 -15.632 -17.236 1.00 13.82 ?  4   ASN   B CB   1 
ATOM   2791 C CG   . ASN   B 1 4   ? 43.912 -14.816 -15.962 1.00 13.04 ?  4   ASN   B CG   1 
ATOM   2792 O OD1  . ASN   B 1 4   ? 44.204 -15.322 -14.881 1.00 12.79 ?  4   ASN   B OD1  1 
ATOM   2793 N ND2  . ASN   B 1 4   ? 43.563 -13.540 -16.083 1.00 13.95 ?  4   ASN   B ND2  1 
ATOM   2794 H H    A ASN   B 1 4   ? 46.918 -15.441 -16.812 0.88 19.19 ?  4   ASN   B H    1 
ATOM   2795 H H    B ASN   B 1 4   ? 46.952 -15.495 -16.838 0.12 19.19 ?  4   ASN   B H    1 
ATOM   2796 H HA   . ASN   B 1 4   ? 45.411 -16.919 -16.603 1.00 17.69 ?  4   ASN   B HA   1 
ATOM   2797 H HB2  . ASN   B 1 4   ? 43.839 -15.029 -17.984 1.00 16.59 ?  4   ASN   B HB2  1 
ATOM   2798 H HB3  . ASN   B 1 4   ? 43.233 -16.278 -17.209 1.00 16.59 ?  4   ASN   B HB3  1 
ATOM   2799 H HD21 . ASN   B 1 4   ? 43.520 -13.037 -15.385 1.00 16.74 ?  4   ASN   B HD21 1 
ATOM   2800 H HD22 . ASN   B 1 4   ? 43.365 -13.219 -16.855 1.00 16.74 ?  4   ASN   B HD22 1 
ATOM   2801 N N    . SER   B 1 5   ? 46.396 -17.868 -18.971 1.00 15.34 ?  5   SER   B N    1 
ATOM   2802 C CA   . SER   B 1 5   ? 46.496 -18.781 -20.110 1.00 17.71 ?  5   SER   B CA   1 
ATOM   2803 C C    . SER   B 1 5   ? 46.477 -20.222 -19.608 1.00 19.24 ?  5   SER   B C    1 
ATOM   2804 O O    . SER   B 1 5   ? 47.473 -20.940 -19.629 1.00 22.00 ?  5   SER   B O    1 
ATOM   2805 C CB   . SER   B 1 5   ? 47.754 -18.486 -20.921 1.00 19.17 ?  5   SER   B CB   1 
ATOM   2806 O OG   . SER   B 1 5   ? 48.926 -18.766 -20.172 1.00 21.76 ?  5   SER   B OG   1 
ATOM   2807 H H    . SER   B 1 5   ? 47.152 -17.704 -18.589 1.00 18.41 ?  5   SER   B H    1 
ATOM   2808 H HA   . SER   B 1 5   ? 45.732 -18.652 -20.690 1.00 21.26 ?  5   SER   B HA   1 
ATOM   2809 H HB2  . SER   B 1 5   ? 47.750 -19.032 -21.725 1.00 23.00 ?  5   SER   B HB2  1 
ATOM   2810 H HB3  . SER   B 1 5   ? 47.740 -17.548 -21.161 1.00 23.00 ?  5   SER   B HB3  1 
ATOM   2811 H HG   . SER   B 1 5   ? 48.965 -19.588 -19.999 1.00 26.12 ?  5   SER   B HG   1 
ATOM   2812 N N    . PHE   B 1 6   ? 45.304 -20.628 -19.138 1.00 19.04 ?  6   PHE   B N    1 
ATOM   2813 C CA   . PHE   B 1 6   ? 45.111 -21.982 -18.642 1.00 18.55 ?  6   PHE   B CA   1 
ATOM   2814 C C    . PHE   B 1 6   ? 45.026 -22.950 -19.812 1.00 21.74 ?  6   PHE   B C    1 
ATOM   2815 O O    . PHE   B 1 6   ? 44.369 -22.670 -20.818 1.00 23.82 ?  6   PHE   B O    1 
ATOM   2816 C CB   . PHE   B 1 6   ? 43.829 -22.054 -17.815 1.00 16.73 ?  6   PHE   B CB   1 
ATOM   2817 C CG   . PHE   B 1 6   ? 43.850 -21.187 -16.584 1.00 14.95 ?  6   PHE   B CG   1 
ATOM   2818 C CD1  . PHE   B 1 6   ? 44.365 -21.672 -15.397 1.00 13.94 ?  6   PHE   B CD1  1 
ATOM   2819 C CD2  . PHE   B 1 6   ? 43.354 -19.888 -16.614 1.00 14.51 ?  6   PHE   B CD2  1 
ATOM   2820 C CE1  . PHE   B 1 6   ? 44.381 -20.884 -14.255 1.00 13.54 ?  6   PHE   B CE1  1 
ATOM   2821 C CE2  . PHE   B 1 6   ? 43.374 -19.093 -15.479 1.00 14.80 ?  6   PHE   B CE2  1 
ATOM   2822 C CZ   . PHE   B 1 6   ? 43.896 -19.585 -14.301 1.00 13.81 ?  6   PHE   B CZ   1 
ATOM   2823 H H    . PHE   B 1 6   ? 44.601 -20.137 -19.098 1.00 22.86 ?  6   PHE   B H    1 
ATOM   2824 H HA   . PHE   B 1 6   ? 45.860 -22.238 -18.082 1.00 22.26 ?  6   PHE   B HA   1 
ATOM   2825 H HB2  . PHE   B 1 6   ? 43.084 -21.770 -18.365 1.00 20.08 ?  6   PHE   B HB2  1 
ATOM   2826 H HB3  . PHE   B 1 6   ? 43.693 -22.972 -17.526 1.00 20.08 ?  6   PHE   B HB3  1 
ATOM   2827 H HD1  . PHE   B 1 6   ? 44.703 -22.538 -15.358 1.00 16.74 ?  6   PHE   B HD1  1 
ATOM   2828 H HD2  . PHE   B 1 6   ? 43.004 -19.551 -17.406 1.00 17.42 ?  6   PHE   B HD2  1 
ATOM   2829 H HE1  . PHE   B 1 6   ? 44.741 -21.215 -13.460 1.00 16.25 ?  6   PHE   B HE1  1 
ATOM   2830 H HE2  . PHE   B 1 6   ? 43.039 -18.224 -15.511 1.00 17.76 ?  6   PHE   B HE2  1 
ATOM   2831 H HZ   . PHE   B 1 6   ? 43.908 -19.055 -13.535 1.00 16.57 ?  6   PHE   B HZ   1 
ATOM   2832 N N    . SER   B 1 7   ? 45.707 -24.089 -19.680 1.00 22.68 ?  7   SER   B N    1 
ATOM   2833 C CA   . SER   B 1 7   ? 45.787 -25.073 -20.751 1.00 24.94 ?  7   SER   B CA   1 
ATOM   2834 C C    . SER   B 1 7   ? 45.741 -26.479 -20.171 1.00 24.27 ?  7   SER   B C    1 
ATOM   2835 O O    . SER   B 1 7   ? 46.336 -26.752 -19.125 1.00 25.38 ?  7   SER   B O    1 
ATOM   2836 C CB   . SER   B 1 7   ? 47.078 -24.893 -21.564 1.00 27.86 ?  7   SER   B CB   1 
ATOM   2837 O OG   . SER   B 1 7   ? 47.119 -25.788 -22.662 1.00 29.75 ?  7   SER   B OG   1 
ATOM   2838 H H    . SER   B 1 7   ? 46.138 -24.315 -18.968 1.00 27.22 ?  7   SER   B H    1 
ATOM   2839 H HA   . SER   B 1 7   ? 45.032 -24.966 -21.346 1.00 29.93 ?  7   SER   B HA   1 
ATOM   2840 H HB2  . SER   B 1 7   ? 47.115 -23.982 -21.899 1.00 33.43 ?  7   SER   B HB2  1 
ATOM   2841 H HB3  . SER   B 1 7   ? 47.841 -25.063 -20.989 1.00 33.43 ?  7   SER   B HB3  1 
ATOM   2842 H HG   . SER   B 1 7   ? 47.831 -25.677 -23.096 1.00 35.70 ?  7   SER   B HG   1 
ATOM   2843 N N    . GLY   B 1 8   ? 45.030 -27.370 -20.862 1.00 24.03 ?  8   GLY   B N    1 
ATOM   2844 C CA   . GLY   B 1 8   ? 45.002 -28.767 -20.484 1.00 23.32 ?  8   GLY   B CA   1 
ATOM   2845 C C    . GLY   B 1 8   ? 44.067 -29.106 -19.351 1.00 22.04 ?  8   GLY   B C    1 
ATOM   2846 O O    . GLY   B 1 8   ? 44.211 -30.176 -18.746 1.00 23.50 ?  8   GLY   B O    1 
ATOM   2847 H H    . GLY   B 1 8   ? 44.558 -27.180 -21.553 1.00 28.84 ?  8   GLY   B H    1 
ATOM   2848 H HA2  . GLY   B 1 8   ? 44.738 -29.293 -21.254 1.00 27.98 ?  8   GLY   B HA2  1 
ATOM   2849 H HA3  . GLY   B 1 8   ? 45.893 -29.041 -20.223 1.00 27.98 ?  8   GLY   B HA3  1 
ATOM   2850 N N    . TYR   B 1 9   ? 43.098 -28.245 -19.050 1.00 19.95 ?  9   TYR   B N    1 
ATOM   2851 C CA   . TYR   B 1 9   ? 42.149 -28.524 -17.987 1.00 17.74 ?  9   TYR   B CA   1 
ATOM   2852 C C    . TYR   B 1 9   ? 40.965 -29.316 -18.511 1.00 17.08 ?  9   TYR   B C    1 
ATOM   2853 O O    . TYR   B 1 9   ? 40.554 -29.178 -19.667 1.00 19.38 ?  9   TYR   B O    1 
ATOM   2854 C CB   . TYR   B 1 9   ? 41.642 -27.236 -17.342 1.00 17.23 ?  9   TYR   B CB   1 
ATOM   2855 C CG   . TYR   B 1 9   ? 42.661 -26.609 -16.427 1.00 16.63 ?  9   TYR   B CG   1 
ATOM   2856 C CD1  . TYR   B 1 9   ? 43.760 -25.944 -16.946 1.00 17.15 ?  9   TYR   B CD1  1 
ATOM   2857 C CD2  . TYR   B 1 9   ? 42.543 -26.701 -15.047 1.00 15.96 ?  9   TYR   B CD2  1 
ATOM   2858 C CE1  . TYR   B 1 9   ? 44.707 -25.381 -16.121 1.00 17.49 ?  9   TYR   B CE1  1 
ATOM   2859 C CE2  . TYR   B 1 9   ? 43.487 -26.142 -14.212 1.00 16.38 ?  9   TYR   B CE2  1 
ATOM   2860 C CZ   . TYR   B 1 9   ? 44.568 -25.480 -14.757 1.00 17.35 ?  9   TYR   B CZ   1 
ATOM   2861 O OH   . TYR   B 1 9   ? 45.513 -24.926 -13.932 1.00 18.30 ?  9   TYR   B OH   1 
ATOM   2862 H H    . TYR   B 1 9   ? 42.957 -27.503 -19.461 1.00 23.94 ?  9   TYR   B H    1 
ATOM   2863 H HA   . TYR   B 1 9   ? 42.580 -29.053 -17.303 1.00 21.29 ?  9   TYR   B HA   1 
ATOM   2864 H HB2  . TYR   B 1 9   ? 41.413 -26.593 -18.032 1.00 20.68 ?  9   TYR   B HB2  1 
ATOM   2865 H HB3  . TYR   B 1 9   ? 40.863 -27.452 -16.812 1.00 20.68 ?  9   TYR   B HB3  1 
ATOM   2866 H HD1  . TYR   B 1 9   ? 43.858 -25.877 -17.869 1.00 20.58 ?  9   TYR   B HD1  1 
ATOM   2867 H HD2  . TYR   B 1 9   ? 41.813 -27.150 -14.679 1.00 19.15 ?  9   TYR   B HD2  1 
ATOM   2868 H HE1  . TYR   B 1 9   ? 45.435 -24.937 -16.484 1.00 21.00 ?  9   TYR   B HE1  1 
ATOM   2869 H HE2  . TYR   B 1 9   ? 43.388 -26.211 -13.288 1.00 19.66 ?  9   TYR   B HE2  1 
ATOM   2870 H HH   . TYR   B 1 9   ? 46.107 -24.554 -14.389 1.00 21.96 ?  9   TYR   B HH   1 
ATOM   2871 N N    . LEU   B 1 10  ? 40.434 -30.164 -17.640 1.00 15.17 ?  10  LEU   B N    1 
ATOM   2872 C CA   . LEU   B 1 10  ? 39.223 -30.915 -17.917 1.00 15.06 ?  10  LEU   B CA   1 
ATOM   2873 C C    . LEU   B 1 10  ? 38.033 -30.146 -17.358 1.00 14.69 ?  10  LEU   B C    1 
ATOM   2874 O O    . LEU   B 1 10  ? 38.044 -29.728 -16.197 1.00 14.60 ?  10  LEU   B O    1 
ATOM   2875 C CB   . LEU   B 1 10  ? 39.318 -32.289 -17.256 1.00 16.06 ?  10  LEU   B CB   1 
ATOM   2876 C CG   . LEU   B 1 10  ? 38.169 -33.232 -17.592 1.00 17.76 ?  10  LEU   B CG   1 
ATOM   2877 C CD1  . LEU   B 1 10  ? 38.304 -33.751 -19.019 1.00 19.10 ?  10  LEU   B CD1  1 
ATOM   2878 C CD2  . LEU   B 1 10  ? 38.093 -34.373 -16.594 1.00 19.13 ?  10  LEU   B CD2  1 
ATOM   2879 H H    . LEU   B 1 10  ? 40.765 -30.328 -16.861 1.00 18.21 ?  10  LEU   B H    1 
ATOM   2880 H HA   . LEU   B 1 10  ? 39.109 -31.034 -18.872 1.00 18.08 ?  10  LEU   B HA   1 
ATOM   2881 H HB2  . LEU   B 1 10  ? 40.142 -32.719 -17.540 1.00 19.27 ?  10  LEU   B HB2  1 
ATOM   2882 H HB3  . LEU   B 1 10  ? 39.330 -32.174 -16.291 1.00 19.27 ?  10  LEU   B HB3  1 
ATOM   2883 H HG   . LEU   B 1 10  ? 37.335 -32.742 -17.537 1.00 21.32 ?  10  LEU   B HG   1 
ATOM   2884 H HD11 . LEU   B 1 10  ? 37.592 -34.386 -19.191 1.00 22.92 ?  10  LEU   B HD11 1 
ATOM   2885 H HD12 . LEU   B 1 10  ? 38.233 -33.002 -19.632 1.00 22.92 ?  10  LEU   B HD12 1 
ATOM   2886 H HD13 . LEU   B 1 10  ? 39.166 -34.181 -19.118 1.00 22.92 ?  10  LEU   B HD13 1 
ATOM   2887 H HD21 . LEU   B 1 10  ? 37.357 -34.954 -16.839 1.00 22.96 ?  10  LEU   B HD21 1 
ATOM   2888 H HD22 . LEU   B 1 10  ? 38.927 -34.863 -16.613 1.00 22.96 ?  10  LEU   B HD22 1 
ATOM   2889 H HD23 . LEU   B 1 10  ? 37.943 -34.003 -15.710 1.00 22.96 ?  10  LEU   B HD23 1 
ATOM   2890 N N    . LYS   B 1 11  ? 37.011 -29.965 -18.184 1.00 15.78 ?  11  LYS   B N    1 
ATOM   2891 C CA   . LYS   B 1 11  ? 35.816 -29.243 -17.775 1.00 17.50 ?  11  LYS   B CA   1 
ATOM   2892 C C    . LYS   B 1 11  ? 34.922 -30.161 -16.949 1.00 16.92 ?  11  LYS   B C    1 
ATOM   2893 O O    . LYS   B 1 11  ? 34.518 -31.230 -17.420 1.00 18.67 ?  11  LYS   B O    1 
ATOM   2894 C CB   . LYS   B 1 11  ? 35.082 -28.756 -19.022 1.00 20.73 ?  11  LYS   B CB   1 
ATOM   2895 C CG   . LYS   B 1 11  ? 33.915 -27.824 -18.760 1.00 23.96 ?  11  LYS   B CG   1 
ATOM   2896 C CD   . LYS   B 1 11  ? 33.191 -27.497 -20.061 1.00 26.79 ?  11  LYS   B CD   1 
ATOM   2897 C CE   . LYS   B 1 11  ? 32.152 -26.409 -19.867 1.00 28.92 ?  11  LYS   B CE   1 
ATOM   2898 N NZ   . LYS   B 1 11  ? 32.782 -25.103 -19.542 1.00 30.10 ?  11  LYS   B NZ   1 
ATOM   2899 H H    . LYS   B 1 11  ? 36.982 -30.261 -18.992 1.00 18.93 ?  11  LYS   B H    1 
ATOM   2900 H HA   . LYS   B 1 11  ? 36.066 -28.475 -17.237 1.00 21.01 ?  11  LYS   B HA   1 
ATOM   2901 H HB2  . LYS   B 1 11  ? 35.713 -28.281 -19.587 1.00 24.88 ?  11  LYS   B HB2  1 
ATOM   2902 H HB3  . LYS   B 1 11  ? 34.738 -29.527 -19.499 1.00 24.88 ?  11  LYS   B HB3  1 
ATOM   2903 H HG2  . LYS   B 1 11  ? 33.285 -28.252 -18.160 1.00 28.76 ?  11  LYS   B HG2  1 
ATOM   2904 H HG3  . LYS   B 1 11  ? 34.242 -26.996 -18.375 1.00 28.76 ?  11  LYS   B HG3  1 
ATOM   2905 H HD2  . LYS   B 1 11  ? 33.836 -27.188 -20.717 1.00 32.15 ?  11  LYS   B HD2  1 
ATOM   2906 H HD3  . LYS   B 1 11  ? 32.741 -28.294 -20.385 1.00 32.15 ?  11  LYS   B HD3  1 
ATOM   2907 H HE2  . LYS   B 1 11  ? 31.640 -26.306 -20.685 1.00 34.71 ?  11  LYS   B HE2  1 
ATOM   2908 H HE3  . LYS   B 1 11  ? 31.566 -26.656 -19.134 1.00 34.71 ?  11  LYS   B HE3  1 
ATOM   2909 H HZ1  . LYS   B 1 11  ? 32.160 -24.469 -19.495 1.00 36.12 ?  11  LYS   B HZ1  1 
ATOM   2910 H HZ2  . LYS   B 1 11  ? 33.204 -25.154 -18.761 1.00 36.12 ?  11  LYS   B HZ2  1 
ATOM   2911 H HZ3  . LYS   B 1 11  ? 33.369 -24.884 -20.175 1.00 36.12 ?  11  LYS   B HZ3  1 
ATOM   2912 N N    . LEU   B 1 12  ? 34.611 -29.747 -15.721 1.00 15.28 ?  12  LEU   B N    1 
ATOM   2913 C CA   . LEU   B 1 12  ? 33.650 -30.452 -14.879 1.00 15.21 ?  12  LEU   B CA   1 
ATOM   2914 C C    . LEU   B 1 12  ? 32.256 -29.848 -14.966 1.00 15.14 ?  12  LEU   B C    1 
ATOM   2915 O O    . LEU   B 1 12  ? 31.269 -30.569 -15.128 1.00 15.73 ?  12  LEU   B O    1 
ATOM   2916 C CB   . LEU   B 1 12  ? 34.115 -30.461 -13.420 1.00 14.65 ?  12  LEU   B CB   1 
ATOM   2917 C CG   . LEU   B 1 12  ? 35.445 -31.150 -13.137 1.00 14.62 ?  12  LEU   B CG   1 
ATOM   2918 C CD1  . LEU   B 1 12  ? 35.750 -31.107 -11.649 1.00 14.89 ?  12  LEU   B CD1  1 
ATOM   2919 C CD2  . LEU   B 1 12  ? 35.446 -32.584 -13.658 1.00 15.72 ?  12  LEU   B CD2  1 
ATOM   2920 H H    . LEU   B 1 12  ? 34.949 -29.048 -15.351 1.00 18.34 ?  12  LEU   B H    1 
ATOM   2921 H HA   . LEU   B 1 12  ? 33.586 -31.370 -15.181 1.00 18.26 ?  12  LEU   B HA   1 
ATOM   2922 H HB2  . LEU   B 1 12  ? 34.195 -29.543 -13.122 1.00 17.59 ?  12  LEU   B HB2  1 
ATOM   2923 H HB3  . LEU   B 1 12  ? 33.439 -30.914 -12.892 1.00 17.59 ?  12  LEU   B HB3  1 
ATOM   2924 H HG   . LEU   B 1 12  ? 36.151 -30.666 -13.596 1.00 17.54 ?  12  LEU   B HG   1 
ATOM   2925 H HD11 . LEU   B 1 12  ? 36.600 -31.548 -11.487 1.00 17.87 ?  12  LEU   B HD11 1 
ATOM   2926 H HD12 . LEU   B 1 12  ? 35.797 -30.183 -11.361 1.00 17.87 ?  12  LEU   B HD12 1 
ATOM   2927 H HD13 . LEU   B 1 12  ? 35.043 -31.568 -11.169 1.00 17.87 ?  12  LEU   B HD13 1 
ATOM   2928 H HD21 . LEU   B 1 12  ? 36.240 -33.035 -13.334 1.00 18.87 ?  12  LEU   B HD21 1 
ATOM   2929 H HD22 . LEU   B 1 12  ? 34.652 -33.035 -13.337 1.00 18.87 ?  12  LEU   B HD22 1 
ATOM   2930 H HD23 . LEU   B 1 12  ? 35.449 -32.566 -14.629 1.00 18.87 ?  12  LEU   B HD23 1 
ATOM   2931 N N    . THR   B 1 13  ? 32.164 -28.529 -14.851 1.00 15.14 ?  13  THR   B N    1 
ATOM   2932 C CA   . THR   B 1 13  ? 30.934 -27.781 -15.046 1.00 15.26 ?  13  THR   B CA   1 
ATOM   2933 C C    . THR   B 1 13  ? 31.259 -26.575 -15.920 1.00 16.91 ?  13  THR   B C    1 
ATOM   2934 O O    . THR   B 1 13  ? 32.401 -26.380 -16.351 1.00 17.32 ?  13  THR   B O    1 
ATOM   2935 C CB   . THR   B 1 13  ? 30.341 -27.318 -13.710 1.00 15.16 ?  13  THR   B CB   1 
ATOM   2936 O OG1  . THR   B 1 13  ? 31.184 -26.297 -13.158 1.00 15.03 ?  13  THR   B OG1  1 
ATOM   2937 C CG2  . THR   B 1 13  ? 30.235 -28.479 -12.727 1.00 15.86 ?  13  THR   B CG2  1 
ATOM   2938 H H    . THR   B 1 13  ? 32.831 -28.025 -14.651 1.00 18.17 ?  13  THR   B H    1 
ATOM   2939 H HA   . THR   B 1 13  ? 30.279 -28.338 -15.500 1.00 18.32 ?  13  THR   B HA   1 
ATOM   2940 H HB   . THR   B 1 13  ? 29.449 -26.958 -13.858 1.00 18.20 ?  13  THR   B HB   1 
ATOM   2941 H HG1  . THR   B 1 13  ? 30.872 -25.537 -13.344 1.00 18.03 ?  13  THR   B HG1  1 
ATOM   2942 H HG21 . THR   B 1 13  ? 29.715 -28.213 -11.953 1.00 19.03 ?  13  THR   B HG21 1 
ATOM   2943 H HG22 . THR   B 1 13  ? 29.801 -29.236 -13.152 1.00 19.03 ?  13  THR   B HG22 1 
ATOM   2944 H HG23 . THR   B 1 13  ? 31.120 -28.748 -12.435 1.00 19.03 ?  13  THR   B HG23 1 
ATOM   2945 N N    A ASP   B 1 14  ? 30.244 -25.750 -16.174 0.88 18.07 ?  14  ASP   B N    1 
ATOM   2946 N N    B ASP   B 1 14  ? 30.246 -25.742 -16.165 0.12 17.66 ?  14  ASP   B N    1 
ATOM   2947 C CA   A ASP   B 1 14  ? 30.445 -24.584 -17.024 0.88 19.66 ?  14  ASP   B CA   1 
ATOM   2948 C CA   B ASP   B 1 14  ? 30.438 -24.580 -17.027 0.12 18.40 ?  14  ASP   B CA   1 
ATOM   2949 C C    A ASP   B 1 14  ? 31.523 -23.654 -16.486 0.88 18.02 ?  14  ASP   B C    1 
ATOM   2950 C C    B ASP   B 1 14  ? 31.458 -23.596 -16.469 0.12 17.05 ?  14  ASP   B C    1 
ATOM   2951 O O    A ASP   B 1 14  ? 32.128 -22.911 -17.269 0.88 19.60 ?  14  ASP   B O    1 
ATOM   2952 O O    B ASP   B 1 14  ? 31.947 -22.744 -17.219 0.12 17.36 ?  14  ASP   B O    1 
ATOM   2953 C CB   A ASP   B 1 14  ? 29.131 -23.819 -17.187 0.88 23.46 ?  14  ASP   B CB   1 
ATOM   2954 C CB   B ASP   B 1 14  ? 29.107 -23.862 -17.261 0.12 20.38 ?  14  ASP   B CB   1 
ATOM   2955 C CG   A ASP   B 1 14  ? 28.185 -24.487 -18.160 0.88 27.56 ?  14  ASP   B CG   1 
ATOM   2956 C CG   B ASP   B 1 14  ? 28.203 -24.609 -18.224 0.12 22.11 ?  14  ASP   B CG   1 
ATOM   2957 O OD1  A ASP   B 1 14  ? 28.601 -25.447 -18.844 0.88 29.05 ?  14  ASP   B OD1  1 
ATOM   2958 O OD1  B ASP   B 1 14  ? 28.729 -25.327 -19.101 0.12 22.72 ?  14  ASP   B OD1  1 
ATOM   2959 O OD2  A ASP   B 1 14  ? 27.019 -24.051 -18.238 0.88 29.09 -1 14  ASP   B OD2  1 
ATOM   2960 O OD2  B ASP   B 1 14  ? 26.967 -24.478 -18.106 0.12 22.65 -1 14  ASP   B OD2  1 
ATOM   2961 H H    A ASP   B 1 14  ? 29.446 -25.837 -15.860 0.88 21.68 ?  14  ASP   B H    1 
ATOM   2962 H H    B ASP   B 1 14  ? 29.451 -25.826 -15.849 0.12 21.19 ?  14  ASP   B H    1 
ATOM   2963 H HA   A ASP   B 1 14  ? 30.723 -24.882 -17.902 0.88 23.60 ?  14  ASP   B HA   1 
ATOM   2964 H HA   B ASP   B 1 14  ? 30.763 -24.885 -17.887 0.12 22.08 ?  14  ASP   B HA   1 
ATOM   2965 H HB2  A ASP   B 1 14  ? 28.680 -23.766 -16.331 0.88 28.15 ?  14  ASP   B HB2  1 
ATOM   2966 H HB2  B ASP   B 1 14  ? 28.637 -23.781 -16.418 0.12 24.46 ?  14  ASP   B HB2  1 
ATOM   2967 H HB3  A ASP   B 1 14  ? 29.317 -22.928 -17.522 0.88 28.15 ?  14  ASP   B HB3  1 
ATOM   2968 H HB3  B ASP   B 1 14  ? 29.288 -22.979 -17.626 0.12 24.46 ?  14  ASP   B HB3  1 
ATOM   2969 N N    . ASN   B 1 15  ? 31.783 -23.679 -15.176 1.00 15.43 ?  15  ASN   B N    1 
ATOM   2970 C CA   . ASN   B 1 15  ? 32.741 -22.759 -14.576 1.00 13.42 ?  15  ASN   B CA   1 
ATOM   2971 C C    . ASN   B 1 15  ? 33.837 -23.410 -13.741 1.00 12.37 ?  15  ASN   B C    1 
ATOM   2972 O O    . ASN   B 1 15  ? 34.675 -22.681 -13.202 1.00 12.92 ?  15  ASN   B O    1 
ATOM   2973 C CB   . ASN   B 1 15  ? 32.026 -21.709 -13.712 1.00 13.66 ?  15  ASN   B CB   1 
ATOM   2974 C CG   . ASN   B 1 15  ? 31.412 -22.310 -12.470 1.00 13.45 ?  15  ASN   B CG   1 
ATOM   2975 O OD1  . ASN   B 1 15  ? 30.468 -23.106 -12.552 1.00 15.11 ?  15  ASN   B OD1  1 
ATOM   2976 N ND2  . ASN   B 1 15  ? 31.943 -21.955 -11.313 1.00 12.87 ?  15  ASN   B ND2  1 
ATOM   2977 H H    A ASN   B 1 15  ? 31.408 -24.218 -14.617 0.88 18.51 ?  15  ASN   B H    1 
ATOM   2978 H H    B ASN   B 1 15  ? 31.445 -24.251 -14.626 0.12 18.51 ?  15  ASN   B H    1 
ATOM   2979 H HA   . ASN   B 1 15  ? 33.185 -22.277 -15.285 1.00 16.10 ?  15  ASN   B HA   1 
ATOM   2980 H HB2  . ASN   B 1 15  ? 32.672 -21.033 -13.438 1.00 16.39 ?  15  ASN   B HB2  1 
ATOM   2981 H HB3  . ASN   B 1 15  ? 31.318 -21.293 -14.231 1.00 16.39 ?  15  ASN   B HB3  1 
ATOM   2982 H HD21 . ASN   B 1 15  ? 31.625 -22.269 -10.578 1.00 15.44 ?  15  ASN   B HD21 1 
ATOM   2983 H HD22 . ASN   B 1 15  ? 32.603 -21.400 -11.290 1.00 15.44 ?  15  ASN   B HD22 1 
ATOM   2984 N N    . VAL   B 1 16  ? 33.863 -24.735 -13.610 1.00 12.28 ?  16  VAL   B N    1 
ATOM   2985 C CA   . VAL   B 1 16  ? 34.861 -25.428 -12.801 1.00 11.80 ?  16  VAL   B CA   1 
ATOM   2986 C C    . VAL   B 1 16  ? 35.657 -26.367 -13.695 1.00 11.96 ?  16  VAL   B C    1 
ATOM   2987 O O    . VAL   B 1 16  ? 35.081 -27.231 -14.371 1.00 13.15 ?  16  VAL   B O    1 
ATOM   2988 C CB   . VAL   B 1 16  ? 34.229 -26.198 -11.628 1.00 12.36 ?  16  VAL   B CB   1 
ATOM   2989 C CG1  . VAL   B 1 16  ? 35.308 -26.934 -10.835 1.00 12.65 ?  16  VAL   B CG1  1 
ATOM   2990 C CG2  . VAL   B 1 16  ? 33.437 -25.257 -10.730 1.00 13.22 ?  16  VAL   B CG2  1 
ATOM   2991 H H    . VAL   B 1 16  ? 33.297 -25.267 -13.985 1.00 14.75 ?  16  VAL   B H    1 
ATOM   2992 H HA   . VAL   B 1 16  ? 35.476 -24.775 -12.429 1.00 14.16 ?  16  VAL   B HA   1 
ATOM   2993 H HB   . VAL   B 1 16  ? 33.616 -26.863 -11.983 1.00 14.84 ?  16  VAL   B HB   1 
ATOM   2994 H HG11 . VAL   B 1 16  ? 34.928 -27.231 -9.993  1.00 15.18 ?  16  VAL   B HG11 1 
ATOM   2995 H HG12 . VAL   B 1 16  ? 35.616 -27.697 -11.346 1.00 15.18 ?  16  VAL   B HG12 1 
ATOM   2996 H HG13 . VAL   B 1 16  ? 36.044 -26.325 -10.667 1.00 15.18 ?  16  VAL   B HG13 1 
ATOM   2997 H HG21 . VAL   B 1 16  ? 33.087 -25.760 -9.979  1.00 15.86 ?  16  VAL   B HG21 1 
ATOM   2998 H HG22 . VAL   B 1 16  ? 34.024 -24.554 -10.415 1.00 15.86 ?  16  VAL   B HG22 1 
ATOM   2999 H HG23 . VAL   B 1 16  ? 32.707 -24.875 -11.242 1.00 15.86 ?  16  VAL   B HG23 1 
ATOM   3000 N N    . TYR   B 1 17  ? 36.982 -26.202 -13.672 1.00 12.38 ?  17  TYR   B N    1 
ATOM   3001 C CA   . TYR   B 1 17  ? 37.927 -26.958 -14.478 1.00 12.47 ?  17  TYR   B CA   1 
ATOM   3002 C C    . TYR   B 1 17  ? 38.972 -27.569 -13.558 1.00 11.83 ?  17  TYR   B C    1 
ATOM   3003 O O    . TYR   B 1 17  ? 39.249 -27.036 -12.480 1.00 12.30 ?  17  TYR   B O    1 
ATOM   3004 C CB   . TYR   B 1 17  ? 38.642 -26.034 -15.471 1.00 14.55 ?  17  TYR   B CB   1 
ATOM   3005 C CG   . TYR   B 1 17  ? 37.717 -25.267 -16.379 1.00 17.22 ?  17  TYR   B CG   1 
ATOM   3006 C CD1  . TYR   B 1 17  ? 37.125 -24.080 -15.964 1.00 18.27 ?  17  TYR   B CD1  1 
ATOM   3007 C CD2  . TYR   B 1 17  ? 37.432 -25.732 -17.654 1.00 19.13 ?  17  TYR   B CD2  1 
ATOM   3008 C CE1  . TYR   B 1 17  ? 36.273 -23.377 -16.796 1.00 19.76 ?  17  TYR   B CE1  1 
ATOM   3009 C CE2  . TYR   B 1 17  ? 36.586 -25.036 -18.495 1.00 20.63 ?  17  TYR   B CE2  1 
ATOM   3010 C CZ   . TYR   B 1 17  ? 36.007 -23.862 -18.060 1.00 20.96 ?  17  TYR   B CZ   1 
ATOM   3011 O OH   . TYR   B 1 17  ? 35.165 -23.169 -18.896 1.00 22.48 ?  17  TYR   B OH   1 
ATOM   3012 H H    . TYR   B 1 17  ? 37.381 -25.615 -13.172 1.00 14.86 ?  17  TYR   B H    1 
ATOM   3013 H HA   . TYR   B 1 17  ? 37.470 -27.666 -14.962 1.00 14.97 ?  17  TYR   B HA   1 
ATOM   3014 H HB2  . TYR   B 1 17  ? 39.178 -25.394 -14.978 1.00 17.46 ?  17  TYR   B HB2  1 
ATOM   3015 H HB3  . TYR   B 1 17  ? 39.212 -26.574 -16.035 1.00 17.46 ?  17  TYR   B HB3  1 
ATOM   3016 H HD1  . TYR   B 1 17  ? 37.305 -23.753 -15.113 1.00 21.92 ?  17  TYR   B HD1  1 
ATOM   3017 H HD2  . TYR   B 1 17  ? 37.817 -26.525 -17.951 1.00 22.96 ?  17  TYR   B HD2  1 
ATOM   3018 H HE1  . TYR   B 1 17  ? 35.884 -22.582 -16.507 1.00 23.71 ?  17  TYR   B HE1  1 
ATOM   3019 H HE2  . TYR   B 1 17  ? 36.398 -25.360 -19.348 1.00 24.76 ?  17  TYR   B HE2  1 
ATOM   3020 H HH   . TYR   B 1 17  ? 35.084 -23.570 -19.629 1.00 26.98 ?  17  TYR   B HH   1 
ATOM   3021 N N    . ILE   B 1 18  ? 39.586 -28.672 -13.994 1.00 11.76 ?  18  ILE   B N    1 
ATOM   3022 C CA   . ILE   B 1 18  ? 40.515 -29.397 -13.133 1.00 11.81 ?  18  ILE   B CA   1 
ATOM   3023 C C    . ILE   B 1 18  ? 41.677 -29.946 -13.952 1.00 12.17 ?  18  ILE   B C    1 
ATOM   3024 O O    . ILE   B 1 18  ? 41.515 -30.340 -15.112 1.00 13.30 ?  18  ILE   B O    1 
ATOM   3025 C CB   . ILE   B 1 18  ? 39.761 -30.492 -12.333 1.00 12.47 ?  18  ILE   B CB   1 
ATOM   3026 C CG1  . ILE   B 1 18  ? 40.615 -31.043 -11.187 1.00 12.98 ?  18  ILE   B CG1  1 
ATOM   3027 C CG2  . ILE   B 1 18  ? 39.262 -31.609 -13.257 1.00 12.87 ?  18  ILE   B CG2  1 
ATOM   3028 C CD1  . ILE   B 1 18  ? 39.793 -31.829 -10.168 1.00 14.51 ?  18  ILE   B CD1  1 
ATOM   3029 H H    . ILE   B 1 18  ? 39.487 -29.016 -14.778 1.00 14.11 ?  18  ILE   B H    1 
ATOM   3030 H HA   . ILE   B 1 18  ? 40.882 -28.781 -12.485 1.00 14.17 ?  18  ILE   B HA   1 
ATOM   3031 H HB   . ILE   B 1 18  ? 38.977 -30.082 -11.936 1.00 14.96 ?  18  ILE   B HB   1 
ATOM   3032 H HG12 . ILE   B 1 18  ? 41.289 -31.634 -11.548 1.00 15.59 ?  18  ILE   B HG12 1 
ATOM   3033 H HG13 . ILE   B 1 18  ? 41.031 -30.300 -10.722 1.00 15.59 ?  18  ILE   B HG13 1 
ATOM   3034 H HG21 . ILE   B 1 18  ? 38.671 -32.195 -12.757 1.00 15.44 ?  18  ILE   B HG21 1 
ATOM   3035 H HG22 . ILE   B 1 18  ? 38.782 -31.211 -13.999 1.00 15.44 ?  18  ILE   B HG22 1 
ATOM   3036 H HG23 . ILE   B 1 18  ? 40.024 -32.112 -13.586 1.00 15.44 ?  18  ILE   B HG23 1 
ATOM   3037 H HD11 . ILE   B 1 18  ? 40.373 -32.111 -9.443  1.00 17.42 ?  18  ILE   B HD11 1 
ATOM   3038 H HD12 . ILE   B 1 18  ? 39.085 -31.261 -9.822  1.00 17.42 ?  18  ILE   B HD12 1 
ATOM   3039 H HD13 . ILE   B 1 18  ? 39.407 -32.606 -10.603 1.00 17.42 ?  18  ILE   B HD13 1 
ATOM   3040 N N    . LYS   B 1 19  ? 42.857 -29.980 -13.332 1.00 12.65 ?  19  LYS   B N    1 
ATOM   3041 C CA   . LYS   B 1 19  ? 44.066 -30.461 -13.986 1.00 13.35 ?  19  LYS   B CA   1 
ATOM   3042 C C    . LYS   B 1 19  ? 44.962 -31.134 -12.958 1.00 13.08 ?  19  LYS   B C    1 
ATOM   3043 O O    . LYS   B 1 19  ? 45.046 -30.692 -11.809 1.00 13.07 ?  19  LYS   B O    1 
ATOM   3044 C CB   . LYS   B 1 19  ? 44.841 -29.300 -14.625 1.00 14.86 ?  19  LYS   B CB   1 
ATOM   3045 C CG   . LYS   B 1 19  ? 46.043 -29.708 -15.457 1.00 16.86 ?  19  LYS   B CG   1 
ATOM   3046 C CD   . LYS   B 1 19  ? 46.760 -28.472 -15.989 1.00 18.62 ?  19  LYS   B CD   1 
ATOM   3047 C CE   . LYS   B 1 19  ? 47.915 -28.840 -16.898 1.00 20.53 ?  19  LYS   B CE   1 
ATOM   3048 N NZ   . LYS   B 1 19  ? 48.675 -27.646 -17.356 1.00 21.55 ?  19  LYS   B NZ   1 
ATOM   3049 H H    . LYS   B 1 19  ? 42.977 -29.725 -12.516 1.00 15.18 ?  19  LYS   B H    1 
ATOM   3050 H HA   . LYS   B 1 19  ? 43.831 -31.106 -14.672 1.00 16.02 ?  19  LYS   B HA   1 
ATOM   3051 H HB2  . LYS   B 1 19  ? 44.233 -28.816 -15.204 1.00 17.83 ?  19  LYS   B HB2  1 
ATOM   3052 H HB3  . LYS   B 1 19  ? 45.151 -28.714 -13.916 1.00 17.83 ?  19  LYS   B HB3  1 
ATOM   3053 H HG2  . LYS   B 1 19  ? 46.659 -30.212 -14.906 1.00 20.24 ?  19  LYS   B HG2  1 
ATOM   3054 H HG3  . LYS   B 1 19  ? 45.743 -30.242 -16.210 1.00 20.24 ?  19  LYS   B HG3  1 
ATOM   3055 H HD2  . LYS   B 1 19  ? 46.131 -27.932 -16.495 1.00 22.35 ?  19  LYS   B HD2  1 
ATOM   3056 H HD3  . LYS   B 1 19  ? 47.110 -27.961 -15.241 1.00 22.35 ?  19  LYS   B HD3  1 
ATOM   3057 H HE2  . LYS   B 1 19  ? 48.523 -29.422 -16.417 1.00 24.64 ?  19  LYS   B HE2  1 
ATOM   3058 H HE3  . LYS   B 1 19  ? 47.567 -29.298 -17.681 1.00 24.64 ?  19  LYS   B HE3  1 
ATOM   3059 H HZ1  . LYS   B 1 19  ? 49.321 -27.894 -17.917 1.00 25.86 ?  19  LYS   B HZ1  1 
ATOM   3060 H HZ2  . LYS   B 1 19  ? 48.130 -27.081 -17.776 1.00 25.86 ?  19  LYS   B HZ2  1 
ATOM   3061 H HZ3  . LYS   B 1 19  ? 49.040 -27.232 -16.659 1.00 25.86 ?  19  LYS   B HZ3  1 
ATOM   3062 N N    . ASN   B 1 20  ? 45.647 -32.188 -13.388 1.00 14.16 ?  20  ASN   B N    1 
ATOM   3063 C CA   . ASN   B 1 20  ? 46.690 -32.812 -12.581 1.00 15.12 ?  20  ASN   B CA   1 
ATOM   3064 C C    . ASN   B 1 20  ? 47.953 -31.983 -12.776 1.00 15.63 ?  20  ASN   B C    1 
ATOM   3065 O O    . ASN   B 1 20  ? 48.600 -32.056 -13.824 1.00 17.46 ?  20  ASN   B O    1 
ATOM   3066 C CB   . ASN   B 1 20  ? 46.883 -34.259 -13.026 1.00 16.43 ?  20  ASN   B CB   1 
ATOM   3067 C CG   . ASN   B 1 20  ? 48.046 -34.954 -12.335 1.00 17.83 ?  20  ASN   B CG   1 
ATOM   3068 O OD1  . ASN   B 1 20  ? 48.729 -35.782 -12.942 1.00 19.84 ?  20  ASN   B OD1  1 
ATOM   3069 N ND2  . ASN   B 1 20  ? 48.265 -34.641 -11.067 1.00 17.39 ?  20  ASN   B ND2  1 
ATOM   3070 H H    . ASN   B 1 20  ? 45.528 -32.563 -14.154 1.00 17.00 ?  20  ASN   B H    1 
ATOM   3071 H HA   . ASN   B 1 20  ? 46.429 -32.798 -11.647 1.00 18.15 ?  20  ASN   B HA   1 
ATOM   3072 H HB2  . ASN   B 1 20  ? 46.078 -34.761 -12.826 1.00 19.72 ?  20  ASN   B HB2  1 
ATOM   3073 H HB3  . ASN   B 1 20  ? 47.053 -34.272 -13.981 1.00 19.72 ?  20  ASN   B HB3  1 
ATOM   3074 H HD21 . ASN   B 1 20  ? 48.914 -35.004 -10.640 1.00 20.87 ?  20  ASN   B HD21 1 
ATOM   3075 H HD22 . ASN   B 1 20  ? 47.762 -34.062 -10.669 1.00 20.87 ?  20  ASN   B HD22 1 
ATOM   3076 N N    . ALA   B 1 21  ? 48.303 -31.177 -11.772 1.00 15.29 ?  21  ALA   B N    1 
ATOM   3077 C CA   . ALA   B 1 21  ? 49.399 -30.233 -11.925 1.00 15.85 ?  21  ALA   B CA   1 
ATOM   3078 C C    . ALA   B 1 21  ? 49.861 -29.745 -10.560 1.00 15.15 ?  21  ALA   B C    1 
ATOM   3079 O O    . ALA   B 1 21  ? 49.117 -29.778 -9.574  1.00 15.24 ?  21  ALA   B O    1 
ATOM   3080 C CB   . ALA   B 1 21  ? 48.981 -29.049 -12.798 1.00 17.17 ?  21  ALA   B CB   1 
ATOM   3081 H H    . ALA   B 1 21  ? 47.919 -31.158 -10.999 1.00 18.35 ?  21  ALA   B H    1 
ATOM   3082 H HA   . ALA   B 1 21  ? 50.141 -30.681 -12.355 1.00 19.03 ?  21  ALA   B HA   1 
ATOM   3083 H HB1  . ALA   B 1 21  ? 49.755 -28.494 -12.956 1.00 20.60 ?  21  ALA   B HB1  1 
ATOM   3084 H HB2  . ALA   B 1 21  ? 48.637 -29.389 -13.639 1.00 20.60 ?  21  ALA   B HB2  1 
ATOM   3085 H HB3  . ALA   B 1 21  ? 48.290 -28.545 -12.339 1.00 20.60 ?  21  ALA   B HB3  1 
ATOM   3086 N N    . ASP   B 1 22  ? 51.118 -29.298 -10.535 1.00 14.63 ?  22  ASP   B N    1 
ATOM   3087 C CA   . ASP   B 1 22  ? 51.728 -28.614 -9.400  1.00 14.14 ?  22  ASP   B CA   1 
ATOM   3088 C C    . ASP   B 1 22  ? 51.329 -27.143 -9.472  1.00 12.70 ?  22  ASP   B C    1 
ATOM   3089 O O    . ASP   B 1 22  ? 51.656 -26.460 -10.447 1.00 12.88 ?  22  ASP   B O    1 
ATOM   3090 C CB   . ASP   B 1 22  ? 53.244 -28.791 -9.548  1.00 15.85 ?  22  ASP   B CB   1 
ATOM   3091 C CG   . ASP   B 1 22  ? 54.067 -28.046 -8.499  1.00 17.66 ?  22  ASP   B CG   1 
ATOM   3092 O OD1  . ASP   B 1 22  ? 53.696 -26.936 -8.083  1.00 17.99 ?  22  ASP   B OD1  1 
ATOM   3093 O OD2  . ASP   B 1 22  ? 55.138 -28.571 -8.115  1.00 19.98 -1 22  ASP   B OD2  1 
ATOM   3094 H H    . ASP   B 1 22  ? 51.660 -29.387 -11.201 1.00 17.56 ?  22  ASP   B H    1 
ATOM   3095 H HA   . ASP   B 1 22  ? 51.429 -29.007 -8.561  1.00 16.97 ?  22  ASP   B HA   1 
ATOM   3096 H HB2  . ASP   B 1 22  ? 53.461 -29.730 -9.479  1.00 19.02 ?  22  ASP   B HB2  1 
ATOM   3097 H HB3  . ASP   B 1 22  ? 53.510 -28.451 -10.418 1.00 19.02 ?  22  ASP   B HB3  1 
ATOM   3098 N N    . ILE   B 1 23  ? 50.615 -26.657 -8.452  1.00 12.16 ?  23  ILE   B N    1 
ATOM   3099 C CA   . ILE   B 1 23  ? 50.024 -25.319 -8.519  1.00 11.45 ?  23  ILE   B CA   1 
ATOM   3100 C C    . ILE   B 1 23  ? 51.081 -24.228 -8.655  1.00 11.43 ?  23  ILE   B C    1 
ATOM   3101 O O    . ILE   B 1 23  ? 50.821 -23.188 -9.268  1.00 11.14 ?  23  ILE   B O    1 
ATOM   3102 C CB   . ILE   B 1 23  ? 49.080 -25.086 -7.324  1.00 12.01 ?  23  ILE   B CB   1 
ATOM   3103 C CG1  . ILE   B 1 23  ? 48.255 -23.813 -7.524  1.00 12.88 ?  23  ILE   B CG1  1 
ATOM   3104 C CG2  . ILE   B 1 23  ? 49.848 -25.055 -6.016  1.00 13.12 ?  23  ILE   B CG2  1 
ATOM   3105 C CD1  . ILE   B 1 23  ? 47.121 -23.661 -6.528  1.00 13.58 ?  23  ILE   B CD1  1 
ATOM   3106 H H    . ILE   B 1 23  ? 50.466 -27.081 -7.718  1.00 14.60 ?  23  ILE   B H    1 
ATOM   3107 H HA   . ILE   B 1 23  ? 49.479 -25.281 -9.318  1.00 13.74 ?  23  ILE   B HA   1 
ATOM   3108 H HB   . ILE   B 1 23  ? 48.461 -25.833 -7.289  1.00 14.41 ?  23  ILE   B HB   1 
ATOM   3109 H HG12 . ILE   B 1 23  ? 48.839 -23.042 -7.430  1.00 15.46 ?  23  ILE   B HG12 1 
ATOM   3110 H HG13 . ILE   B 1 23  ? 47.871 -23.823 -8.417  1.00 15.46 ?  23  ILE   B HG13 1 
ATOM   3111 H HG21 . ILE   B 1 23  ? 49.214 -25.045 -5.280  1.00 15.75 ?  23  ILE   B HG21 1 
ATOM   3112 H HG22 . ILE   B 1 23  ? 50.404 -25.848 -5.959  1.00 15.75 ?  23  ILE   B HG22 1 
ATOM   3113 H HG23 . ILE   B 1 23  ? 50.399 -24.260 -5.991  1.00 15.75 ?  23  ILE   B HG23 1 
ATOM   3114 H HD11 . ILE   B 1 23  ? 46.599 -22.880 -6.761  1.00 16.30 ?  23  ILE   B HD11 1 
ATOM   3115 H HD12 . ILE   B 1 23  ? 46.563 -24.457 -6.569  1.00 16.30 ?  23  ILE   B HD12 1 
ATOM   3116 H HD13 . ILE   B 1 23  ? 47.493 -23.564 -5.640  1.00 16.30 ?  23  ILE   B HD13 1 
ATOM   3117 N N    . VAL   B 1 24  ? 52.275 -24.433 -8.096  1.00 11.85 ?  24  VAL   B N    1 
ATOM   3118 C CA   . VAL   B 1 24  ? 53.351 -23.453 -8.260  1.00 12.20 ?  24  VAL   B CA   1 
ATOM   3119 C C    . VAL   B 1 24  ? 53.802 -23.398 -9.714  1.00 12.34 ?  24  VAL   B C    1 
ATOM   3120 O O    . VAL   B 1 24  ? 53.945 -22.318 -10.303 1.00 13.05 ?  24  VAL   B O    1 
ATOM   3121 C CB   . VAL   B 1 24  ? 54.529 -23.778 -7.319  1.00 13.34 ?  24  VAL   B CB   1 
ATOM   3122 C CG1  . VAL   B 1 24  ? 55.742 -22.899 -7.639  1.00 14.35 ?  24  VAL   B CG1  1 
ATOM   3123 C CG2  . VAL   B 1 24  ? 54.117 -23.606 -5.878  1.00 14.44 ?  24  VAL   B CG2  1 
ATOM   3124 H H    . VAL   B 1 24  ? 52.488 -25.121 -7.625  1.00 14.23 ?  24  VAL   B H    1 
ATOM   3125 H HA   . VAL   B 1 24  ? 53.016 -22.579 -8.022  1.00 14.64 ?  24  VAL   B HA   1 
ATOM   3126 H HB   . VAL   B 1 24  ? 54.790 -24.704 -7.443  1.00 16.01 ?  24  VAL   B HB   1 
ATOM   3127 H HG11 . VAL   B 1 24  ? 56.340 -22.899 -6.873  1.00 17.22 ?  24  VAL   B HG11 1 
ATOM   3128 H HG12 . VAL   B 1 24  ? 56.199 -23.263 -8.412  1.00 17.22 ?  24  VAL   B HG12 1 
ATOM   3129 H HG13 . VAL   B 1 24  ? 55.439 -21.997 -7.819  1.00 17.22 ?  24  VAL   B HG13 1 
ATOM   3130 H HG21 . VAL   B 1 24  ? 54.841 -23.898 -5.304  1.00 17.33 ?  24  VAL   B HG21 1 
ATOM   3131 H HG22 . VAL   B 1 24  ? 53.922 -22.670 -5.717  1.00 17.33 ?  24  VAL   B HG22 1 
ATOM   3132 H HG23 . VAL   B 1 24  ? 53.325 -24.142 -5.710  1.00 17.33 ?  24  VAL   B HG23 1 
ATOM   3133 N N    . GLU   B 1 25  ? 54.061 -24.567 -10.306 1.00 13.33 ?  25  GLU   B N    1 
ATOM   3134 C CA   . GLU   B 1 25  ? 54.457 -24.604 -11.708 1.00 14.86 ?  25  GLU   B CA   1 
ATOM   3135 C C    . GLU   B 1 25  ? 53.352 -24.059 -12.599 1.00 13.80 ?  25  GLU   B C    1 
ATOM   3136 O O    . GLU   B 1 25  ? 53.621 -23.350 -13.576 1.00 14.70 ?  25  GLU   B O    1 
ATOM   3137 C CB   . GLU   B 1 25  ? 54.843 -26.029 -12.102 1.00 18.63 ?  25  GLU   B CB   1 
ATOM   3138 C CG   . GLU   B 1 25  ? 56.131 -26.493 -11.440 1.00 24.20 ?  25  GLU   B CG   1 
ATOM   3139 C CD   . GLU   B 1 25  ? 57.254 -25.472 -11.547 1.00 29.22 ?  25  GLU   B CD   1 
ATOM   3140 O OE1  . GLU   B 1 25  ? 57.617 -25.098 -12.682 1.00 31.11 ?  25  GLU   B OE1  1 
ATOM   3141 O OE2  . GLU   B 1 25  ? 57.762 -25.026 -10.492 1.00 31.05 -1 25  GLU   B OE2  1 
ATOM   3142 H H    . GLU   B 1 25  ? 54.012 -25.337 -9.924  1.00 16.00 ?  25  GLU   B H    1 
ATOM   3143 H HA   . GLU   B 1 25  ? 55.219 -24.026 -11.834 1.00 17.83 ?  25  GLU   B HA   1 
ATOM   3144 H HB2  . GLU   B 1 25  ? 54.134 -26.639 -11.833 1.00 22.36 ?  25  GLU   B HB2  1 
ATOM   3145 H HB3  . GLU   B 1 25  ? 54.965 -26.073 -13.064 1.00 22.36 ?  25  GLU   B HB3  1 
ATOM   3146 H HG2  . GLU   B 1 25  ? 55.970 -26.633 -10.499 1.00 29.04 ?  25  GLU   B HG2  1 
ATOM   3147 H HG3  . GLU   B 1 25  ? 56.423 -27.316 -11.862 1.00 29.04 ?  25  GLU   B HG3  1 
ATOM   3148 N N    . GLU   B 1 26  ? 52.100 -24.369 -12.266 1.00 12.88 ?  26  GLU   B N    1 
ATOM   3149 C CA   . GLU   B 1 26  ? 50.977 -23.839 -13.033 1.00 13.41 ?  26  GLU   B CA   1 
ATOM   3150 C C    . GLU   B 1 26  ? 50.929 -22.321 -12.948 1.00 12.74 ?  26  GLU   B C    1 
ATOM   3151 O O    . GLU   B 1 26  ? 50.738 -21.639 -13.959 1.00 14.10 ?  26  GLU   B O    1 
ATOM   3152 C CB   . GLU   B 1 26  ? 49.661 -24.425 -12.519 1.00 15.37 ?  26  GLU   B CB   1 
ATOM   3153 C CG   . GLU   B 1 26  ? 49.244 -25.715 -13.183 1.00 18.80 ?  26  GLU   B CG   1 
ATOM   3154 C CD   . GLU   B 1 26  ? 48.980 -25.566 -14.677 1.00 20.34 ?  26  GLU   B CD   1 
ATOM   3155 O OE1  . GLU   B 1 26  ? 47.998 -24.903 -15.080 1.00 20.52 ?  26  GLU   B OE1  1 
ATOM   3156 O OE2  . GLU   B 1 26  ? 49.760 -26.133 -15.454 1.00 22.66 -1 26  GLU   B OE2  1 
ATOM   3157 H H    . GLU   B 1 26  ? 51.870 -24.879 -11.607 1.00 15.45 ?  26  GLU   B H    1 
ATOM   3158 H HA   . GLU   B 1 26  ? 51.080 -24.087 -13.963 1.00 16.10 ?  26  GLU   B HA   1 
ATOM   3159 H HB2  . GLU   B 1 26  ? 49.745 -24.599 -11.568 1.00 18.44 ?  26  GLU   B HB2  1 
ATOM   3160 H HB3  . GLU   B 1 26  ? 48.952 -23.777 -12.668 1.00 18.44 ?  26  GLU   B HB3  1 
ATOM   3161 H HG2  . GLU   B 1 26  ? 49.956 -26.357 -13.067 1.00 22.57 ?  26  GLU   B HG2  1 
ATOM   3162 H HG3  . GLU   B 1 26  ? 48.428 -26.033 -12.768 1.00 22.57 ?  26  GLU   B HG3  1 
ATOM   3163 N N    . ALA   B 1 27  ? 51.073 -21.776 -11.738 1.00 11.91 ?  27  ALA   B N    1 
ATOM   3164 C CA   . ALA   B 1 27  ? 51.034 -20.326 -11.582 1.00 12.46 ?  27  ALA   B CA   1 
ATOM   3165 C C    . ALA   B 1 27  ? 52.105 -19.656 -12.431 1.00 13.23 ?  27  ALA   B C    1 
ATOM   3166 O O    . ALA   B 1 27  ? 51.843 -18.651 -13.107 1.00 14.00 ?  27  ALA   B O    1 
ATOM   3167 C CB   . ALA   B 1 27  ? 51.192 -19.953 -10.109 1.00 12.81 ?  27  ALA   B CB   1 
ATOM   3168 H H    . ALA   B 1 27  ? 51.190 -22.216 -11.006 1.00 14.30 ?  27  ALA   B H    1 
ATOM   3169 H HA   . ALA   B 1 27  ? 50.175 -20.000 -11.879 1.00 14.95 ?  27  ALA   B HA   1 
ATOM   3170 H HB1  . ALA   B 1 27  ? 51.158 -18.988 -10.020 1.00 15.37 ?  27  ALA   B HB1  1 
ATOM   3171 H HB2  . ALA   B 1 27  ? 50.463 -20.354 -9.603  1.00 15.37 ?  27  ALA   B HB2  1 
ATOM   3172 H HB3  . ALA   B 1 27  ? 52.040 -20.287 -9.782  1.00 15.37 ?  27  ALA   B HB3  1 
ATOM   3173 N N    . LYS   B 1 28  ? 53.322 -20.200 -12.417 1.00 14.59 ?  28  LYS   B N    1 
ATOM   3174 C CA   . LYS   B 1 28  ? 54.398 -19.573 -13.174 1.00 16.77 ?  28  LYS   B CA   1 
ATOM   3175 C C    . LYS   B 1 28  ? 54.150 -19.647 -14.675 1.00 17.49 ?  28  LYS   B C    1 
ATOM   3176 O O    . LYS   B 1 28  ? 54.563 -18.743 -15.412 1.00 18.72 ?  28  LYS   B O    1 
ATOM   3177 C CB   . LYS   B 1 28  ? 55.751 -20.177 -12.786 1.00 19.55 ?  28  LYS   B CB   1 
ATOM   3178 C CG   . LYS   B 1 28  ? 56.151 -19.864 -11.349 1.00 22.28 ?  28  LYS   B CG   1 
ATOM   3179 C CD   . LYS   B 1 28  ? 57.575 -20.292 -11.025 1.00 26.52 ?  28  LYS   B CD   1 
ATOM   3180 C CE   . LYS   B 1 28  ? 57.668 -21.778 -10.760 1.00 29.97 ?  28  LYS   B CE   1 
ATOM   3181 N NZ   . LYS   B 1 28  ? 59.022 -22.157 -10.265 1.00 31.12 ?  28  LYS   B NZ   1 
ATOM   3182 H H    . LYS   B 1 28  ? 53.549 -20.908 -11.985 1.00 17.51 ?  28  LYS   B H    1 
ATOM   3183 H HA   . LYS   B 1 28  ? 54.429 -18.631 -12.942 1.00 20.13 ?  28  LYS   B HA   1 
ATOM   3184 H HB2  . LYS   B 1 28  ? 55.710 -21.138 -12.882 1.00 23.47 ?  28  LYS   B HB2  1 
ATOM   3185 H HB3  . LYS   B 1 28  ? 56.439 -19.814 -13.370 1.00 23.47 ?  28  LYS   B HB3  1 
ATOM   3186 H HG2  . LYS   B 1 28  ? 56.082 -18.906 -11.205 1.00 26.74 ?  28  LYS   B HG2  1 
ATOM   3187 H HG3  . LYS   B 1 28  ? 55.550 -20.332 -10.750 1.00 26.74 ?  28  LYS   B HG3  1 
ATOM   3188 H HD2  . LYS   B 1 28  ? 58.149 -20.080 -11.778 1.00 31.83 ?  28  LYS   B HD2  1 
ATOM   3189 H HD3  . LYS   B 1 28  ? 57.874 -19.820 -10.232 1.00 31.83 ?  28  LYS   B HD3  1 
ATOM   3190 H HE2  . LYS   B 1 28  ? 57.016 -22.024 -10.084 1.00 35.97 ?  28  LYS   B HE2  1 
ATOM   3191 H HE3  . LYS   B 1 28  ? 57.497 -22.264 -11.582 1.00 35.97 ?  28  LYS   B HE3  1 
ATOM   3192 H HZ1  . LYS   B 1 28  ? 59.057 -23.033 -10.113 1.00 37.34 ?  28  LYS   B HZ1  1 
ATOM   3193 H HZ2  . LYS   B 1 28  ? 59.638 -21.943 -10.870 1.00 37.34 ?  28  LYS   B HZ2  1 
ATOM   3194 H HZ3  . LYS   B 1 28  ? 59.200 -21.726 -9.506  1.00 37.34 ?  28  LYS   B HZ3  1 
ATOM   3195 N N    . LYS   B 1 29  ? 53.456 -20.685 -15.143 1.00 18.39 ?  29  LYS   B N    1 
ATOM   3196 C CA   . LYS   B 1 29  ? 53.178 -20.820 -16.569 1.00 20.97 ?  29  LYS   B CA   1 
ATOM   3197 C C    . LYS   B 1 29  ? 51.921 -20.070 -17.006 1.00 19.79 ?  29  LYS   B C    1 
ATOM   3198 O O    . LYS   B 1 29  ? 51.920 -19.436 -18.067 1.00 21.21 ?  29  LYS   B O    1 
ATOM   3199 C CB   . LYS   B 1 29  ? 53.054 -22.300 -16.937 1.00 25.39 ?  29  LYS   B CB   1 
ATOM   3200 C CG   . LYS   B 1 29  ? 52.921 -22.561 -18.426 1.00 29.53 ?  29  LYS   B CG   1 
ATOM   3201 C CD   . LYS   B 1 29  ? 53.119 -24.033 -18.753 1.00 32.82 ?  29  LYS   B CD   1 
ATOM   3202 C CE   . LYS   B 1 29  ? 52.007 -24.896 -18.174 1.00 35.14 ?  29  LYS   B CE   1 
ATOM   3203 N NZ   . LYS   B 1 29  ? 52.205 -26.339 -18.490 1.00 36.38 ?  29  LYS   B NZ   1 
ATOM   3204 H H    . LYS   B 1 29  ? 53.135 -21.326 -14.653 1.00 22.07 ?  29  LYS   B H    1 
ATOM   3205 H HA   . LYS   B 1 29  ? 53.927 -20.456 -17.062 1.00 25.17 ?  29  LYS   B HA   1 
ATOM   3206 H HB2  . LYS   B 1 29  ? 53.848 -22.765 -16.626 1.00 30.47 ?  29  LYS   B HB2  1 
ATOM   3207 H HB3  . LYS   B 1 29  ? 52.270 -22.664 -16.502 1.00 30.47 ?  29  LYS   B HB3  1 
ATOM   3208 H HG2  . LYS   B 1 29  ? 52.034 -22.303 -18.718 1.00 35.44 ?  29  LYS   B HG2  1 
ATOM   3209 H HG3  . LYS   B 1 29  ? 53.595 -22.051 -18.903 1.00 35.44 ?  29  LYS   B HG3  1 
ATOM   3210 H HD2  . LYS   B 1 29  ? 53.123 -24.147 -19.716 1.00 39.39 ?  29  LYS   B HD2  1 
ATOM   3211 H HD3  . LYS   B 1 29  ? 53.962 -24.332 -18.377 1.00 39.39 ?  29  LYS   B HD3  1 
ATOM   3212 H HE2  . LYS   B 1 29  ? 51.992 -24.798 -17.209 1.00 42.18 ?  29  LYS   B HE2  1 
ATOM   3213 H HE3  . LYS   B 1 29  ? 51.157 -24.616 -18.551 1.00 42.18 ?  29  LYS   B HE3  1 
ATOM   3214 H HZ1  . LYS   B 1 29  ? 51.543 -26.821 -18.141 1.00 43.66 ?  29  LYS   B HZ1  1 
ATOM   3215 H HZ2  . LYS   B 1 29  ? 52.217 -26.459 -19.372 1.00 43.66 ?  29  LYS   B HZ2  1 
ATOM   3216 H HZ3  . LYS   B 1 29  ? 52.978 -26.622 -18.150 1.00 43.66 ?  29  LYS   B HZ3  1 
ATOM   3217 N N    . VAL   B 1 30  ? 50.848 -20.146 -16.213 1.00 18.23 ?  30  VAL   B N    1 
ATOM   3218 C CA   . VAL   B 1 30  ? 49.556 -19.564 -16.586 1.00 18.54 ?  30  VAL   B CA   1 
ATOM   3219 C C    . VAL   B 1 30  ? 49.543 -18.048 -16.433 1.00 17.26 ?  30  VAL   B C    1 
ATOM   3220 O O    . VAL   B 1 30  ? 48.801 -17.349 -17.141 1.00 18.14 ?  30  VAL   B O    1 
ATOM   3221 C CB   . VAL   B 1 30  ? 48.449 -20.201 -15.722 1.00 20.20 ?  30  VAL   B CB   1 
ATOM   3222 C CG1  . VAL   B 1 30  ? 47.163 -19.381 -15.779 1.00 20.28 ?  30  VAL   B CG1  1 
ATOM   3223 C CG2  . VAL   B 1 30  ? 48.196 -21.642 -16.143 1.00 21.02 ?  30  VAL   B CG2  1 
ATOM   3224 H H    . VAL   B 1 30  ? 50.832 -20.560 -15.449 1.00 21.88 ?  30  VAL   B H    1 
ATOM   3225 H HA   . VAL   B 1 30  ? 49.369 -19.791 -17.512 1.00 22.25 ?  30  VAL   B HA   1 
ATOM   3226 H HB   . VAL   B 1 30  ? 48.742 -20.223 -14.798 1.00 24.24 ?  30  VAL   B HB   1 
ATOM   3227 H HG11 . VAL   B 1 30  ? 46.418 -19.958 -15.548 1.00 24.34 ?  30  VAL   B HG11 1 
ATOM   3228 H HG12 . VAL   B 1 30  ? 47.219 -18.653 -15.143 1.00 24.34 ?  30  VAL   B HG12 1 
ATOM   3229 H HG13 . VAL   B 1 30  ? 47.039 -19.042 -16.675 1.00 24.34 ?  30  VAL   B HG13 1 
ATOM   3230 H HG21 . VAL   B 1 30  ? 47.499 -22.022 -15.579 1.00 25.23 ?  30  VAL   B HG21 1 
ATOM   3231 H HG22 . VAL   B 1 30  ? 47.907 -21.655 -17.070 1.00 25.23 ?  30  VAL   B HG22 1 
ATOM   3232 H HG23 . VAL   B 1 30  ? 49.013 -22.151 -16.043 1.00 25.23 ?  30  VAL   B HG23 1 
ATOM   3233 N N    . LYS   B 1 31  ? 50.325 -17.528 -15.499 1.00 16.85 ?  31  LYS   B N    1 
ATOM   3234 C CA   . LYS   B 1 31  ? 50.340 -16.116 -15.145 1.00 17.44 ?  31  LYS   B CA   1 
ATOM   3235 C C    . LYS   B 1 31  ? 48.940 -15.651 -14.744 1.00 15.23 ?  31  LYS   B C    1 
ATOM   3236 O O    . LYS   B 1 31  ? 48.384 -14.735 -15.363 1.00 16.22 ?  31  LYS   B O    1 
ATOM   3237 C CB   . LYS   B 1 31  ? 50.953 -15.294 -16.286 1.00 20.48 ?  31  LYS   B CB   1 
ATOM   3238 C CG   . LYS   B 1 31  ? 52.377 -15.735 -16.641 1.00 23.27 ?  31  LYS   B CG   1 
ATOM   3239 C CD   . LYS   B 1 31  ? 52.980 -14.893 -17.749 1.00 26.13 ?  31  LYS   B CD   1 
ATOM   3240 C CE   . LYS   B 1 31  ? 54.455 -15.198 -17.927 1.00 28.62 ?  31  LYS   B CE   1 
ATOM   3241 N NZ   . LYS   B 1 31  ? 55.221 -14.880 -16.690 1.00 29.69 ?  31  LYS   B NZ   1 
ATOM   3242 H H    . LYS   B 1 31  ? 50.876 -18.003 -15.048 1.00 20.23 ?  31  LYS   B H    1 
ATOM   3243 H HA   . LYS   B 1 31  ? 50.907 -16.020 -14.377 1.00 20.93 ?  31  LYS   B HA   1 
ATOM   3244 H HB2  . LYS   B 1 31  ? 50.405 -15.389 -17.081 1.00 24.58 ?  31  LYS   B HB2  1 
ATOM   3245 H HB3  . LYS   B 1 31  ? 50.986 -14.367 -16.012 1.00 24.58 ?  31  LYS   B HB3  1 
ATOM   3246 H HG2  . LYS   B 1 31  ? 52.936 -15.652 -15.853 1.00 27.93 ?  31  LYS   B HG2  1 
ATOM   3247 H HG3  . LYS   B 1 31  ? 52.360 -16.660 -16.939 1.00 27.93 ?  31  LYS   B HG3  1 
ATOM   3248 H HD2  . LYS   B 1 31  ? 52.525 -15.090 -18.581 1.00 31.36 ?  31  LYS   B HD2  1 
ATOM   3249 H HD3  . LYS   B 1 31  ? 52.886 -13.956 -17.524 1.00 31.36 ?  31  LYS   B HD3  1 
ATOM   3250 H HE2  . LYS   B 1 31  ? 54.569 -16.143 -18.121 1.00 34.34 ?  31  LYS   B HE2  1 
ATOM   3251 H HE3  . LYS   B 1 31  ? 54.809 -14.660 -18.652 1.00 34.34 ?  31  LYS   B HE3  1 
ATOM   3252 H HZ1  . LYS   B 1 31  ? 56.094 -14.946 -16.848 1.00 35.64 ?  31  LYS   B HZ1  1 
ATOM   3253 H HZ2  . LYS   B 1 31  ? 55.037 -14.051 -16.425 1.00 35.64 ?  31  LYS   B HZ2  1 
ATOM   3254 H HZ3  . LYS   B 1 31  ? 55.001 -15.447 -16.040 1.00 35.64 ?  31  LYS   B HZ3  1 
ATOM   3255 N N    . PRO   B 1 32  ? 48.342 -16.252 -13.709 1.00 13.08 ?  32  PRO   B N    1 
ATOM   3256 C CA   . PRO   B 1 32  ? 46.963 -15.903 -13.342 1.00 12.12 ?  32  PRO   B CA   1 
ATOM   3257 C C    . PRO   B 1 32  ? 46.877 -14.559 -12.636 1.00 12.10 ?  32  PRO   B C    1 
ATOM   3258 O O    . PRO   B 1 32  ? 47.800 -14.133 -11.937 1.00 13.56 ?  32  PRO   B O    1 
ATOM   3259 C CB   . PRO   B 1 32  ? 46.577 -17.024 -12.370 1.00 12.57 ?  32  PRO   B CB   1 
ATOM   3260 C CG   . PRO   B 1 32  ? 47.888 -17.361 -11.698 1.00 12.67 ?  32  PRO   B CG   1 
ATOM   3261 C CD   . PRO   B 1 32  ? 48.927 -17.238 -12.776 1.00 13.09 ?  32  PRO   B CD   1 
ATOM   3262 H HA   . PRO   B 1 32  ? 46.377 -15.924 -14.120 1.00 14.55 ?  32  PRO   B HA   1 
ATOM   3263 H HB2  . PRO   B 1 32  ? 45.927 -16.698 -11.726 1.00 15.08 ?  32  PRO   B HB2  1 
ATOM   3264 H HB3  . PRO   B 1 32  ? 46.229 -17.790 -12.857 1.00 15.08 ?  32  PRO   B HB3  1 
ATOM   3265 H HG2  . PRO   B 1 32  ? 48.060 -16.725 -10.983 1.00 15.21 ?  32  PRO   B HG2  1 
ATOM   3266 H HG3  . PRO   B 1 32  ? 47.859 -18.265 -11.350 1.00 15.21 ?  32  PRO   B HG3  1 
ATOM   3267 H HD2  . PRO   B 1 32  ? 49.756 -16.896 -12.406 1.00 15.71 ?  32  PRO   B HD2  1 
ATOM   3268 H HD3  . PRO   B 1 32  ? 49.055 -18.091 -13.214 1.00 15.71 ?  32  PRO   B HD3  1 
ATOM   3269 N N    . THR   B 1 33  ? 45.724 -13.907 -12.805 1.00 11.71 ?  33  THR   B N    1 
ATOM   3270 C CA   . THR   B 1 33  ? 45.428 -12.731 -11.995 1.00 12.01 ?  33  THR   B CA   1 
ATOM   3271 C C    . THR   B 1 33  ? 45.383 -13.086 -10.514 1.00 11.56 ?  33  THR   B C    1 
ATOM   3272 O O    . THR   B 1 33  ? 45.853 -12.308 -9.671  1.00 12.75 ?  33  THR   B O    1 
ATOM   3273 C CB   . THR   B 1 33  ? 44.108 -12.099 -12.441 1.00 12.66 ?  33  THR   B CB   1 
ATOM   3274 O OG1  . THR   B 1 33  ? 44.151 -11.841 -13.847 1.00 12.89 ?  33  THR   B OG1  1 
ATOM   3275 C CG2  . THR   B 1 33  ? 43.862 -10.793 -11.699 1.00 14.00 ?  33  THR   B CG2  1 
ATOM   3276 H H    . THR   B 1 33  ? 45.104 -14.130 -13.367 1.00 14.06 ?  33  THR   B H    1 
ATOM   3277 H HA   . THR   B 1 33  ? 46.129 -12.081 -12.129 1.00 14.41 ?  33  THR   B HA   1 
ATOM   3278 H HB   . THR   B 1 33  ? 43.373 -12.705 -12.247 1.00 15.19 ?  33  THR   B HB   1 
ATOM   3279 H HG1  . THR   B 1 33  ? 43.423 -11.482 -14.099 1.00 15.47 ?  33  THR   B HG1  1 
ATOM   3280 H HG21 . THR   B 1 33  ? 43.103 -10.332 -12.085 1.00 16.80 ?  33  THR   B HG21 1 
ATOM   3281 H HG22 . THR   B 1 33  ? 43.685 -10.971 -10.764 1.00 16.80 ?  33  THR   B HG22 1 
ATOM   3282 H HG23 . THR   B 1 33  ? 44.646 -10.224 -11.771 1.00 16.80 ?  33  THR   B HG23 1 
ATOM   3283 N N    . VAL   B 1 34  ? 44.834 -14.257 -10.177 1.00 10.93 ?  34  VAL   B N    1 
ATOM   3284 C CA   . VAL   B 1 34  ? 44.645 -14.659 -8.787  1.00 10.42 ?  34  VAL   B CA   1 
ATOM   3285 C C    . VAL   B 1 34  ? 45.073 -16.109 -8.622  1.00 9.60  ?  34  VAL   B C    1 
ATOM   3286 O O    . VAL   B 1 34  ? 44.559 -16.994 -9.314  1.00 10.48 ?  34  VAL   B O    1 
ATOM   3287 C CB   . VAL   B 1 34  ? 43.176 -14.518 -8.340  1.00 11.85 ?  34  VAL   B CB   1 
ATOM   3288 C CG1  . VAL   B 1 34  ? 43.017 -14.978 -6.898  1.00 12.32 ?  34  VAL   B CG1  1 
ATOM   3289 C CG2  . VAL   B 1 34  ? 42.674 -13.093 -8.525  1.00 12.73 ?  34  VAL   B CG2  1 
ATOM   3290 H H    . VAL   B 1 34  ? 44.571 -14.848 -10.745 1.00 13.12 ?  34  VAL   B H    1 
ATOM   3291 H HA   . VAL   B 1 34  ? 45.199 -14.105 -8.211  1.00 12.50 ?  34  VAL   B HA   1 
ATOM   3292 H HB   . VAL   B 1 34  ? 42.630 -15.094 -8.898  1.00 14.22 ?  34  VAL   B HB   1 
ATOM   3293 H HG11 . VAL   B 1 34  ? 42.169 -14.655 -6.557  1.00 14.78 ?  34  VAL   B HG11 1 
ATOM   3294 H HG12 . VAL   B 1 34  ? 43.035 -15.948 -6.869  1.00 14.78 ?  34  VAL   B HG12 1 
ATOM   3295 H HG13 . VAL   B 1 34  ? 43.744 -14.617 -6.368  1.00 14.78 ?  34  VAL   B HG13 1 
ATOM   3296 H HG21 . VAL   B 1 34  ? 41.756 -13.041 -8.214  1.00 15.28 ?  34  VAL   B HG21 1 
ATOM   3297 H HG22 . VAL   B 1 34  ? 43.233 -12.491 -8.013  1.00 15.28 ?  34  VAL   B HG22 1 
ATOM   3298 H HG23 . VAL   B 1 34  ? 42.714 -12.862 -9.468  1.00 15.28 ?  34  VAL   B HG23 1 
ATOM   3299 N N    . VAL   B 1 35  ? 45.980 -16.356 -7.682  1.00 9.34  ?  35  VAL   B N    1 
ATOM   3300 C CA   . VAL   B 1 35  ? 46.221 -17.697 -7.164  1.00 9.18  ?  35  VAL   B CA   1 
ATOM   3301 C C    . VAL   B 1 35  ? 45.682 -17.756 -5.742  1.00 8.86  ?  35  VAL   B C    1 
ATOM   3302 O O    . VAL   B 1 35  ? 45.895 -16.831 -4.950  1.00 9.37  ?  35  VAL   B O    1 
ATOM   3303 C CB   . VAL   B 1 35  ? 47.706 -18.117 -7.245  1.00 10.05 ?  35  VAL   B CB   1 
ATOM   3304 C CG1  . VAL   B 1 35  ? 48.599 -17.277 -6.323  1.00 10.61 ?  35  VAL   B CG1  1 
ATOM   3305 C CG2  . VAL   B 1 35  ? 47.856 -19.612 -6.940  1.00 10.46 ?  35  VAL   B CG2  1 
ATOM   3306 H H    . VAL   B 1 35  ? 46.479 -15.749 -7.326  1.00 11.21 ?  35  VAL   B H    1 
ATOM   3307 H HA   . VAL   B 1 35  ? 45.710 -18.326 -7.694  1.00 11.02 ?  35  VAL   B HA   1 
ATOM   3308 H HB   . VAL   B 1 35  ? 48.013 -17.979 -8.155  1.00 12.06 ?  35  VAL   B HB   1 
ATOM   3309 H HG11 . VAL   B 1 35  ? 49.526 -17.496 -6.500  1.00 12.73 ?  35  VAL   B HG11 1 
ATOM   3310 H HG12 . VAL   B 1 35  ? 48.436 -16.340 -6.498  1.00 12.73 ?  35  VAL   B HG12 1 
ATOM   3311 H HG13 . VAL   B 1 35  ? 48.380 -17.485 -5.399  1.00 12.73 ?  35  VAL   B HG13 1 
ATOM   3312 H HG21 . VAL   B 1 35  ? 48.783 -19.869 -7.041  1.00 12.55 ?  35  VAL   B HG21 1 
ATOM   3313 H HG22 . VAL   B 1 35  ? 47.561 -19.785 -6.030  1.00 12.55 ?  35  VAL   B HG22 1 
ATOM   3314 H HG23 . VAL   B 1 35  ? 47.304 -20.123 -7.561  1.00 12.55 ?  35  VAL   B HG23 1 
ATOM   3315 N N    . VAL   B 1 36  ? 44.970 -18.838 -5.426  1.00 8.78  ?  36  VAL   B N    1 
ATOM   3316 C CA   . VAL   B 1 36  ? 44.421 -19.046 -4.096  1.00 8.58  ?  36  VAL   B CA   1 
ATOM   3317 C C    . VAL   B 1 36  ? 45.431 -19.807 -3.247  1.00 8.15  ?  36  VAL   B C    1 
ATOM   3318 O O    . VAL   B 1 36  ? 45.970 -20.838 -3.671  1.00 9.37  ?  36  VAL   B O    1 
ATOM   3319 C CB   . VAL   B 1 36  ? 43.088 -19.809 -4.172  1.00 9.05  ?  36  VAL   B CB   1 
ATOM   3320 C CG1  . VAL   B 1 36  ? 42.584 -20.171 -2.781  1.00 9.62  ?  36  VAL   B CG1  1 
ATOM   3321 C CG2  . VAL   B 1 36  ? 42.055 -18.982 -4.919  1.00 9.77  ?  36  VAL   B CG2  1 
ATOM   3322 H H    . VAL   B 1 36  ? 44.800 -19.477 -5.977  1.00 10.54 ?  36  VAL   B H    1 
ATOM   3323 H HA   . VAL   B 1 36  ? 44.257 -18.186 -3.680  1.00 10.30 ?  36  VAL   B HA   1 
ATOM   3324 H HB   . VAL   B 1 36  ? 43.223 -20.631 -4.668  1.00 10.86 ?  36  VAL   B HB   1 
ATOM   3325 H HG11 . VAL   B 1 36  ? 41.647 -20.407 -2.839  1.00 11.54 ?  36  VAL   B HG11 1 
ATOM   3326 H HG12 . VAL   B 1 36  ? 43.097 -20.914 -2.441  1.00 11.54 ?  36  VAL   B HG12 1 
ATOM   3327 H HG13 . VAL   B 1 36  ? 42.690 -19.396 -2.201  1.00 11.54 ?  36  VAL   B HG13 1 
ATOM   3328 H HG21 . VAL   B 1 36  ? 41.217 -19.467 -4.943  1.00 11.73 ?  36  VAL   B HG21 1 
ATOM   3329 H HG22 . VAL   B 1 36  ? 41.937 -18.135 -4.462  1.00 11.73 ?  36  VAL   B HG22 1 
ATOM   3330 H HG23 . VAL   B 1 36  ? 42.370 -18.823 -5.826  1.00 11.73 ?  36  VAL   B HG23 1 
ATOM   3331 N N    . ASN   B 1 37  ? 45.656 -19.315 -2.032  1.00 8.70  ?  37  ASN   B N    1 
ATOM   3332 C CA   . ASN   B 1 37  ? 46.408 -20.041 -1.023  1.00 9.03  ?  37  ASN   B CA   1 
ATOM   3333 C C    . ASN   B 1 37  ? 45.460 -20.713 -0.037  1.00 8.89  ?  37  ASN   B C    1 
ATOM   3334 O O    . ASN   B 1 37  ? 44.451 -20.136 0.376   1.00 9.70  ?  37  ASN   B O    1 
ATOM   3335 C CB   . ASN   B 1 37  ? 47.336 -19.094 -0.264  1.00 9.31  ?  37  ASN   B CB   1 
ATOM   3336 C CG   . ASN   B 1 37  ? 48.187 -19.811 0.752   1.00 9.33  ?  37  ASN   B CG   1 
ATOM   3337 O OD1  . ASN   B 1 37  ? 48.532 -20.982 0.568   1.00 10.24 ?  37  ASN   B OD1  1 
ATOM   3338 N ND2  . ASN   B 1 37  ? 48.531 -19.122 1.831   1.00 9.79  ?  37  ASN   B ND2  1 
ATOM   3339 H H    . ASN   B 1 37  ? 45.376 -18.547 -1.759  1.00 10.44 ?  37  ASN   B H    1 
ATOM   3340 H HA   . ASN   B 1 37  ? 46.943 -20.732 -1.444  1.00 10.84 ?  37  ASN   B HA   1 
ATOM   3341 H HB2  . ASN   B 1 37  ? 47.928 -18.666 -0.896  1.00 11.17 ?  37  ASN   B HB2  1 
ATOM   3342 H HB3  . ASN   B 1 37  ? 46.805 -18.437 0.204   1.00 11.17 ?  37  ASN   B HB3  1 
ATOM   3343 H HD21 . ASN   B 1 37  ? 49.010 -19.495 2.442   1.00 11.75 ?  37  ASN   B HD21 1 
ATOM   3344 H HD22 . ASN   B 1 37  ? 48.265 -18.318 1.931   1.00 11.75 ?  37  ASN   B HD22 1 
ATOM   3345 N N    . ALA   B 1 38  ? 45.807 -21.943 0.340   1.00 9.29  ?  38  ALA   B N    1 
ATOM   3346 C CA   . ALA   B 1 38  ? 45.153 -22.687 1.417   1.00 9.60  ?  38  ALA   B CA   1 
ATOM   3347 C C    . ALA   B 1 38  ? 45.743 -22.212 2.742   1.00 9.38  ?  38  ALA   B C    1 
ATOM   3348 O O    . ALA   B 1 38  ? 46.644 -22.826 3.325   1.00 10.63 ?  38  ALA   B O    1 
ATOM   3349 C CB   . ALA   B 1 38  ? 45.359 -24.182 1.223   1.00 10.91 ?  38  ALA   B CB   1 
ATOM   3350 H H    . ALA   B 1 38  ? 46.457 -22.381 -0.013  1.00 11.16 ?  38  ALA   B H    1 
ATOM   3351 H HA   . ALA   B 1 38  ? 44.201 -22.498 1.417   1.00 11.53 ?  38  ALA   B HA   1 
ATOM   3352 H HB1  . ALA   B 1 38  ? 44.913 -24.660 1.948   1.00 13.09 ?  38  ALA   B HB1  1 
ATOM   3353 H HB2  . ALA   B 1 38  ? 44.971 -24.446 0.375   1.00 13.09 ?  38  ALA   B HB2  1 
ATOM   3354 H HB3  . ALA   B 1 38  ? 46.304 -24.379 1.236   1.00 13.09 ?  38  ALA   B HB3  1 
ATOM   3355 N N    . ALA   B 1 39  ? 45.225 -21.076 3.209   1.00 9.32  ?  39  ALA   B N    1 
ATOM   3356 C CA   . ALA   B 1 39  ? 45.772 -20.344 4.340   1.00 9.75  ?  39  ALA   B CA   1 
ATOM   3357 C C    . ALA   B 1 39  ? 45.150 -20.792 5.659   1.00 9.59  ?  39  ALA   B C    1 
ATOM   3358 O O    . ALA   B 1 39  ? 44.122 -21.472 5.703   1.00 10.56 ?  39  ALA   B O    1 
ATOM   3359 C CB   . ALA   B 1 39  ? 45.540 -18.841 4.151   1.00 10.42 ?  39  ALA   B CB   1 
ATOM   3360 H H    . ALA   B 1 39  ? 44.528 -20.701 2.869   1.00 11.19 ?  39  ALA   B H    1 
ATOM   3361 H HA   . ALA   B 1 39  ? 46.724 -20.501 4.389   1.00 11.70 ?  39  ALA   B HA   1 
ATOM   3362 H HB1  . ALA   B 1 39  ? 45.911 -18.367 4.913   1.00 12.51 ?  39  ALA   B HB1  1 
ATOM   3363 H HB2  . ALA   B 1 39  ? 45.984 -18.556 3.337   1.00 12.51 ?  39  ALA   B HB2  1 
ATOM   3364 H HB3  . ALA   B 1 39  ? 44.588 -18.672 4.086   1.00 12.51 ?  39  ALA   B HB3  1 
ATOM   3365 N N    . ASN   B 1 40  ? 45.791 -20.373 6.747   1.00 10.37 ?  40  ASN   B N    1 
ATOM   3366 C CA   . ASN   B 1 40  ? 45.230 -20.431 8.087   1.00 11.07 ?  40  ASN   B CA   1 
ATOM   3367 C C    . ASN   B 1 40  ? 45.051 -19.006 8.614   1.00 10.80 ?  40  ASN   B C    1 
ATOM   3368 O O    . ASN   B 1 40  ? 45.460 -18.025 7.985   1.00 10.80 ?  40  ASN   B O    1 
ATOM   3369 C CB   . ASN   B 1 40  ? 46.084 -21.307 9.022   1.00 12.23 ?  40  ASN   B CB   1 
ATOM   3370 C CG   . ASN   B 1 40  ? 47.539 -20.904 9.040   1.00 13.14 ?  40  ASN   B CG   1 
ATOM   3371 O OD1  . ASN   B 1 40  ? 47.859 -19.722 9.096   1.00 14.94 ?  40  ASN   B OD1  1 
ATOM   3372 N ND2  . ASN   B 1 40  ? 48.432 -21.883 9.000   1.00 13.24 ?  40  ASN   B ND2  1 
ATOM   3373 H H    . ASN   B 1 40  ? 46.588 -20.052 6.730   1.00 12.44 ?  40  ASN   B H    1 
ATOM   3374 H HA   . ASN   B 1 40  ? 44.350 -20.830 8.043   1.00 13.28 ?  40  ASN   B HA   1 
ATOM   3375 H HB2  . ASN   B 1 40  ? 45.742 -21.229 9.928   1.00 14.68 ?  40  ASN   B HB2  1 
ATOM   3376 H HB3  . ASN   B 1 40  ? 46.031 -22.226 8.725   1.00 14.68 ?  40  ASN   B HB3  1 
ATOM   3377 H HD21 . ASN   B 1 40  ? 49.274 -21.703 9.007   1.00 15.90 ?  40  ASN   B HD21 1 
ATOM   3378 H HD22 . ASN   B 1 40  ? 48.170 -22.703 8.962   1.00 15.90 ?  40  ASN   B HD22 1 
ATOM   3379 N N    . VAL   B 1 41  ? 44.398 -18.883 9.771   1.00 11.23 ?  41  VAL   B N    1 
ATOM   3380 C CA   . VAL   B 1 41  ? 43.939 -17.562 10.212  1.00 11.96 ?  41  VAL   B CA   1 
ATOM   3381 C C    . VAL   B 1 41  ? 45.090 -16.612 10.520  1.00 11.69 ?  41  VAL   B C    1 
ATOM   3382 O O    . VAL   B 1 41  ? 44.916 -15.390 10.439  1.00 11.92 ?  41  VAL   B O    1 
ATOM   3383 C CB   . VAL   B 1 41  ? 42.953 -17.639 11.395  1.00 13.39 ?  41  VAL   B CB   1 
ATOM   3384 C CG1  . VAL   B 1 41  ? 41.668 -18.330 10.980  1.00 14.03 ?  41  VAL   B CG1  1 
ATOM   3385 C CG2  . VAL   B 1 41  ? 43.593 -18.317 12.596  1.00 14.44 ?  41  VAL   B CG2  1 
ATOM   3386 H H    . VAL   B 1 41  ? 44.217 -19.525 10.307  1.00 13.48 ?  41  VAL   B H    1 
ATOM   3387 H HA   . VAL   B 1 41  ? 43.450 -17.163 9.478   1.00 14.36 ?  41  VAL   B HA   1 
ATOM   3388 H HB   . VAL   B 1 41  ? 42.721 -16.736 11.663  1.00 16.08 ?  41  VAL   B HB   1 
ATOM   3389 H HG11 . VAL   B 1 41  ? 41.052 -18.335 11.731  1.00 16.84 ?  41  VAL   B HG11 1 
ATOM   3390 H HG12 . VAL   B 1 41  ? 41.275 -17.850 10.235  1.00 16.84 ?  41  VAL   B HG12 1 
ATOM   3391 H HG13 . VAL   B 1 41  ? 41.871 -19.242 10.715  1.00 16.84 ?  41  VAL   B HG13 1 
ATOM   3392 H HG21 . VAL   B 1 41  ? 42.947 -18.355 13.318  1.00 17.33 ?  41  VAL   B HG21 1 
ATOM   3393 H HG22 . VAL   B 1 41  ? 43.860 -19.216 12.346  1.00 17.33 ?  41  VAL   B HG22 1 
ATOM   3394 H HG23 . VAL   B 1 41  ? 44.369 -17.806 12.872  1.00 17.33 ?  41  VAL   B HG23 1 
ATOM   3395 N N    . TYR   B 1 42  ? 46.258 -17.128 10.902  1.00 12.08 ?  42  TYR   B N    1 
ATOM   3396 C CA   . TYR   B 1 42  ? 47.412 -16.279 11.173  1.00 12.80 ?  42  TYR   B CA   1 
ATOM   3397 C C    . TYR   B 1 42  ? 48.379 -16.206 9.997   1.00 11.92 ?  42  TYR   B C    1 
ATOM   3398 O O    . TYR   B 1 42  ? 49.468 -15.638 10.134  1.00 12.88 ?  42  TYR   B O    1 
ATOM   3399 C CB   . TYR   B 1 42  ? 48.110 -16.681 12.479  1.00 14.65 ?  42  TYR   B CB   1 
ATOM   3400 C CG   . TYR   B 1 42  ? 47.515 -15.990 13.699  1.00 14.87 ?  42  TYR   B CG   1 
ATOM   3401 C CD1  . TYR   B 1 42  ? 47.747 -14.639 13.934  1.00 14.22 ?  42  TYR   B CD1  1 
ATOM   3402 C CD2  . TYR   B 1 42  ? 46.718 -16.680 14.601  1.00 16.41 ?  42  TYR   B CD2  1 
ATOM   3403 C CE1  . TYR   B 1 42  ? 47.207 -13.996 15.034  1.00 15.33 ?  42  TYR   B CE1  1 
ATOM   3404 C CE2  . TYR   B 1 42  ? 46.173 -16.044 15.706  1.00 16.78 ?  42  TYR   B CE2  1 
ATOM   3405 C CZ   . TYR   B 1 42  ? 46.420 -14.700 15.918  1.00 17.11 ?  42  TYR   B CZ   1 
ATOM   3406 O OH   . TYR   B 1 42  ? 45.889 -14.057 17.016  1.00 19.84 ?  42  TYR   B OH   1 
ATOM   3407 H H    . TYR   B 1 42  ? 46.404 -17.972 11.003  1.00 14.50 ?  42  TYR   B H    1 
ATOM   3408 H HA   . TYR   B 1 42  ? 47.084 -15.380 11.306  1.00 15.36 ?  42  TYR   B HA   1 
ATOM   3409 H HB2  . TYR   B 1 42  ? 48.023 -17.638 12.603  1.00 17.58 ?  42  TYR   B HB2  1 
ATOM   3410 H HB3  . TYR   B 1 42  ? 49.047 -16.436 12.422  1.00 17.58 ?  42  TYR   B HB3  1 
ATOM   3411 H HD1  . TYR   B 1 42  ? 48.281 -14.157 13.336  1.00 17.07 ?  42  TYR   B HD1  1 
ATOM   3412 H HD2  . TYR   B 1 42  ? 46.548 -17.584 14.459  1.00 19.69 ?  42  TYR   B HD2  1 
ATOM   3413 H HE1  . TYR   B 1 42  ? 47.380 -13.094 15.175  1.00 18.39 ?  42  TYR   B HE1  1 
ATOM   3414 H HE2  . TYR   B 1 42  ? 45.644 -16.523 16.300  1.00 20.13 ?  42  TYR   B HE2  1 
ATOM   3415 H HH   . TYR   B 1 42  ? 46.128 -13.255 17.012  1.00 23.81 ?  42  TYR   B HH   1 
ATOM   3416 N N    . LEU   B 1 43  ? 47.983 -16.720 8.836   1.00 10.86 ?  43  LEU   B N    1 
ATOM   3417 C CA   . LEU   B 1 43  ? 48.796 -16.642 7.626   1.00 10.78 ?  43  LEU   B CA   1 
ATOM   3418 C C    . LEU   B 1 43  ? 50.211 -17.150 7.877   1.00 11.11 ?  43  LEU   B C    1 
ATOM   3419 O O    . LEU   B 1 43  ? 51.192 -16.550 7.433   1.00 11.91 ?  43  LEU   B O    1 
ATOM   3420 C CB   . LEU   B 1 43  ? 48.808 -15.231 7.036   1.00 10.92 ?  43  LEU   B CB   1 
ATOM   3421 C CG   . LEU   B 1 43  ? 47.447 -14.631 6.661   1.00 11.05 ?  43  LEU   B CG   1 
ATOM   3422 C CD1  . LEU   B 1 43  ? 47.648 -13.228 6.102   1.00 12.39 ?  43  LEU   B CD1  1 
ATOM   3423 C CD2  . LEU   B 1 43  ? 46.702 -15.517 5.673   1.00 11.37 ?  43  LEU   B CD2  1 
ATOM   3424 H H    . LEU   B 1 43  ? 47.239 -17.140 8.720   1.00 13.03 ?  43  LEU   B H    1 
ATOM   3425 H HA   . LEU   B 1 43  ? 48.399 -17.225 6.958   1.00 12.94 ?  43  LEU   B HA   1 
ATOM   3426 H HB2  . LEU   B 1 43  ? 49.217 -14.635 7.681   1.00 13.11 ?  43  LEU   B HB2  1 
ATOM   3427 H HB3  . LEU   B 1 43  ? 49.342 -15.248 6.227   1.00 13.11 ?  43  LEU   B HB3  1 
ATOM   3428 H HG   . LEU   B 1 43  ? 46.906 -14.558 7.461   1.00 13.27 ?  43  LEU   B HG   1 
ATOM   3429 H HD11 . LEU   B 1 43  ? 46.784 -12.852 5.868   1.00 14.88 ?  43  LEU   B HD11 1 
ATOM   3430 H HD12 . LEU   B 1 43  ? 48.073 -12.675 6.780   1.00 14.88 ?  43  LEU   B HD12 1 
ATOM   3431 H HD13 . LEU   B 1 43  ? 48.212 -13.276 5.315   1.00 14.88 ?  43  LEU   B HD13 1 
ATOM   3432 H HD21 . LEU   B 1 43  ? 45.903 -15.056 5.373   1.00 13.64 ?  43  LEU   B HD21 1 
ATOM   3433 H HD22 . LEU   B 1 43  ? 47.280 -15.705 4.917   1.00 13.64 ?  43  LEU   B HD22 1 
ATOM   3434 H HD23 . LEU   B 1 43  ? 46.456 -16.347 6.115   1.00 13.64 ?  43  LEU   B HD23 1 
ATOM   3435 N N    . LYS   B 1 44  ? 50.315 -18.272 8.591   1.00 11.07 ?  44  LYS   B N    1 
ATOM   3436 C CA   . LYS   B 1 44  ? 51.583 -18.953 8.818   1.00 11.58 ?  44  LYS   B CA   1 
ATOM   3437 C C    . LYS   B 1 44  ? 51.694 -20.064 7.783   1.00 11.17 ?  44  LYS   B C    1 
ATOM   3438 O O    . LYS   B 1 44  ? 50.996 -21.081 7.867   1.00 12.52 ?  44  LYS   B O    1 
ATOM   3439 C CB   . LYS   B 1 44  ? 51.652 -19.476 10.250  1.00 13.42 ?  44  LYS   B CB   1 
ATOM   3440 C CG   . LYS   B 1 44  ? 51.841 -18.374 11.281  1.00 16.29 ?  44  LYS   B CG   1 
ATOM   3441 C CD   . LYS   B 1 44  ? 53.034 -17.500 10.893  1.00 19.45 ?  44  LYS   B CD   1 
ATOM   3442 C CE   . LYS   B 1 44  ? 53.517 -16.622 12.019  1.00 21.96 ?  44  LYS   B CE   1 
ATOM   3443 N NZ   . LYS   B 1 44  ? 54.684 -15.797 11.614  1.00 23.23 ?  44  LYS   B NZ   1 
ATOM   3444 H H    . LYS   B 1 44  ? 49.644 -18.658 8.967   1.00 13.29 ?  44  LYS   B H    1 
ATOM   3445 H HA   . LYS   B 1 44  ? 52.312 -18.335 8.655   1.00 13.90 ?  44  LYS   B HA   1 
ATOM   3446 H HB2  . LYS   B 1 44  ? 50.821 -19.936 10.455  1.00 16.11 ?  44  LYS   B HB2  1 
ATOM   3447 H HB3  . LYS   B 1 44  ? 52.397 -20.088 10.325  1.00 16.11 ?  44  LYS   B HB3  1 
ATOM   3448 H HG2  . LYS   B 1 44  ? 51.047 -17.821 11.317  1.00 19.55 ?  44  LYS   B HG2  1 
ATOM   3449 H HG3  . LYS   B 1 44  ? 52.019 -18.773 12.150  1.00 19.55 ?  44  LYS   B HG3  1 
ATOM   3450 H HD2  . LYS   B 1 44  ? 53.764 -18.079 10.608  1.00 23.34 ?  44  LYS   B HD2  1 
ATOM   3451 H HD3  . LYS   B 1 44  ? 52.769 -16.921 10.161  1.00 23.34 ?  44  LYS   B HD3  1 
ATOM   3452 H HE2  . LYS   B 1 44  ? 52.805 -16.018 12.263  1.00 26.36 ?  44  LYS   B HE2  1 
ATOM   3453 H HE3  . LYS   B 1 44  ? 53.774 -17.176 12.771  1.00 26.36 ?  44  LYS   B HE3  1 
ATOM   3454 H HZ1  . LYS   B 1 44  ? 54.944 -15.286 12.294  1.00 27.88 ?  44  LYS   B HZ1  1 
ATOM   3455 H HZ2  . LYS   B 1 44  ? 55.359 -16.319 11.367  1.00 27.88 ?  44  LYS   B HZ2  1 
ATOM   3456 H HZ3  . LYS   B 1 44  ? 54.461 -15.271 10.928  1.00 27.88 ?  44  LYS   B HZ3  1 
ATOM   3457 N N    . HIS   B 1 45  ? 52.548 -19.844 6.786   1.00 10.80 ?  45  HIS   B N    1 
ATOM   3458 C CA   . HIS   B 1 45  ? 52.569 -20.676 5.584   1.00 11.29 ?  45  HIS   B CA   1 
ATOM   3459 C C    . HIS   B 1 45  ? 53.589 -21.798 5.744   1.00 13.64 ?  45  HIS   B C    1 
ATOM   3460 O O    . HIS   B 1 45  ? 54.653 -21.810 5.132   1.00 15.87 ?  45  HIS   B O    1 
ATOM   3461 C CB   . HIS   B 1 45  ? 52.877 -19.823 4.365   1.00 11.06 ?  45  HIS   B CB   1 
ATOM   3462 C CG   . HIS   B 1 45  ? 52.009 -18.616 4.260   1.00 10.91 ?  45  HIS   B CG   1 
ATOM   3463 N ND1  . HIS   B 1 45  ? 50.631 -18.690 4.234   1.00 11.32 ?  45  HIS   B ND1  1 
ATOM   3464 C CD2  . HIS   B 1 45  ? 52.326 -17.303 4.192   1.00 11.91 ?  45  HIS   B CD2  1 
ATOM   3465 C CE1  . HIS   B 1 45  ? 50.142 -17.467 4.136   1.00 10.94 ?  45  HIS   B CE1  1 
ATOM   3466 N NE2  . HIS   B 1 45  ? 51.146 -16.608 4.111   1.00 11.44 ?  45  HIS   B NE2  1 
ATOM   3467 H H    . HIS   B 1 45  ? 53.123 -19.204 6.775   1.00 12.96 ?  45  HIS   B H    1 
ATOM   3468 H HA   . HIS   B 1 45  ? 51.694 -21.077 5.458   1.00 13.56 ?  45  HIS   B HA   1 
ATOM   3469 H HB2  . HIS   B 1 45  ? 53.798 -19.530 4.408   1.00 13.27 ?  45  HIS   B HB2  1 
ATOM   3470 H HB3  . HIS   B 1 45  ? 52.741 -20.361 3.564   1.00 13.27 ?  45  HIS   B HB3  1 
ATOM   3471 H HD2  . HIS   B 1 45  ? 53.183 -16.939 4.194   1.00 14.29 ?  45  HIS   B HD2  1 
ATOM   3472 H HE1  . HIS   B 1 45  ? 49.239 -17.246 4.091   1.00 13.13 ?  45  HIS   B HE1  1 
ATOM   3473 H HE2  . HIS   B 1 45  ? 51.070 -15.752 4.058   1.00 13.73 ?  45  HIS   B HE2  1 
ATOM   3474 N N    A GLY   B 1 46  ? 53.226 -22.770 6.574   0.88 14.26 ?  46  GLY   B N    1 
ATOM   3475 N N    B GLY   B 1 46  ? 53.233 -22.759 6.591   0.12 14.48 ?  46  GLY   B N    1 
ATOM   3476 C CA   A GLY   B 1 46  ? 54.151 -23.830 6.928   0.88 15.78 ?  46  GLY   B CA   1 
ATOM   3477 C CA   B GLY   B 1 46  ? 54.146 -23.830 6.933   0.12 15.35 ?  46  GLY   B CA   1 
ATOM   3478 C C    A GLY   B 1 46  ? 54.187 -25.023 5.994   0.88 17.40 ?  46  GLY   B C    1 
ATOM   3479 C C    B GLY   B 1 46  ? 54.175 -24.985 5.953   0.12 16.30 ?  46  GLY   B C    1 
ATOM   3480 O O    A GLY   B 1 46  ? 55.249 -25.394 5.484   0.88 20.29 ?  46  GLY   B O    1 
ATOM   3481 O O    B GLY   B 1 46  ? 55.218 -25.278 5.360   0.12 16.68 ?  46  GLY   B O    1 
ATOM   3482 H H    A GLY   B 1 46  ? 52.457 -22.822 6.962   0.88 17.11 ?  46  GLY   B H    1 
ATOM   3483 H H    B GLY   B 1 46  ? 52.467 -22.804 6.985   0.12 17.38 ?  46  GLY   B H    1 
ATOM   3484 H HA2  A GLY   B 1 46  ? 55.047 -23.460 6.973   0.88 18.94 ?  46  GLY   B HA2  1 
ATOM   3485 H HA2  B GLY   B 1 46  ? 55.043 -23.468 6.995   0.12 18.43 ?  46  GLY   B HA2  1 
ATOM   3486 H HA3  A GLY   B 1 46  ? 53.922 -24.164 7.808   0.88 18.94 ?  46  GLY   B HA3  1 
ATOM   3487 H HA3  B GLY   B 1 46  ? 53.904 -24.182 7.804   0.12 18.43 ?  46  GLY   B HA3  1 
ATOM   3488 N N    . GLY   B 1 47  ? 53.034 -25.649 5.769   1.00 16.90 ?  47  GLY   B N    1 
ATOM   3489 C CA   . GLY   B 1 47  ? 52.968 -26.901 5.049   1.00 14.70 ?  47  GLY   B CA   1 
ATOM   3490 C C    . GLY   B 1 47  ? 52.049 -26.866 3.843   1.00 12.78 ?  47  GLY   B C    1 
ATOM   3491 O O    . GLY   B 1 47  ? 51.396 -25.862 3.551   1.00 12.86 ?  47  GLY   B O    1 
ATOM   3492 H H    A GLY   B 1 47  ? 52.270 -25.371 6.051   0.88 20.28 ?  47  GLY   B H    1 
ATOM   3493 H H    B GLY   B 1 47  ? 52.271 -25.383 6.067   0.12 20.28 ?  47  GLY   B H    1 
ATOM   3494 H HA2  . GLY   B 1 47  ? 53.855 -27.149 4.745   1.00 17.65 ?  47  GLY   B HA2  1 
ATOM   3495 H HA3  . GLY   B 1 47  ? 52.654 -27.594 5.652   1.00 17.65 ?  47  GLY   B HA3  1 
ATOM   3496 N N    . GLY   B 1 48  ? 52.011 -28.000 3.146   1.00 11.89 ?  48  GLY   B N    1 
ATOM   3497 C CA   . GLY   B 1 48  ? 51.085 -28.146 2.042   1.00 11.80 ?  48  GLY   B CA   1 
ATOM   3498 C C    . GLY   B 1 48  ? 51.226 -27.036 1.028   1.00 11.29 ?  48  GLY   B C    1 
ATOM   3499 O O    . GLY   B 1 48  ? 52.332 -26.575 0.715   1.00 11.69 ?  48  GLY   B O    1 
ATOM   3500 H H    . GLY   B 1 48  ? 52.518 -28.677 3.286   1.00 14.28 ?  48  GLY   B H    1 
ATOM   3501 H HA2  . GLY   B 1 48  ? 51.245 -28.996 1.599   1.00 14.16 ?  48  GLY   B HA2  1 
ATOM   3502 H HA3  . GLY   B 1 48  ? 50.176 -28.143 2.380   1.00 14.16 ?  48  GLY   B HA3  1 
ATOM   3503 N N    . VAL   B 1 49  ? 50.079 -26.606 0.497   1.00 11.13 ?  49  VAL   B N    1 
ATOM   3504 C CA   . VAL   B 1 49  ? 50.060 -25.580 -0.542  1.00 11.26 ?  49  VAL   B CA   1 
ATOM   3505 C C    . VAL   B 1 49  ? 50.719 -24.294 -0.053  1.00 10.55 ?  49  VAL   B C    1 
ATOM   3506 O O    . VAL   B 1 49  ? 51.512 -23.676 -0.773  1.00 11.18 ?  49  VAL   B O    1 
ATOM   3507 C CB   . VAL   B 1 49  ? 48.619 -25.328 -1.023  1.00 12.39 ?  49  VAL   B CB   1 
ATOM   3508 C CG1  . VAL   B 1 49  ? 48.559 -24.074 -1.885  1.00 12.51 ?  49  VAL   B CG1  1 
ATOM   3509 C CG2  . VAL   B 1 49  ? 48.086 -26.532 -1.782  1.00 14.05 ?  49  VAL   B CG2  1 
ATOM   3510 H H    . VAL   B 1 49  ? 49.296 -26.893 0.717   1.00 13.36 ?  49  VAL   B H    1 
ATOM   3511 H HA   . VAL   B 1 49  ? 50.566 -25.896 -1.305  1.00 13.52 ?  49  VAL   B HA   1 
ATOM   3512 H HB   . VAL   B 1 49  ? 48.048 -25.184 -0.253  1.00 14.87 ?  49  VAL   B HB   1 
ATOM   3513 H HG11 . VAL   B 1 49  ? 47.739 -24.085 -2.404  1.00 15.02 ?  49  VAL   B HG11 1 
ATOM   3514 H HG12 . VAL   B 1 49  ? 48.571 -23.290 -1.310  1.00 15.02 ?  49  VAL   B HG12 1 
ATOM   3515 H HG13 . VAL   B 1 49  ? 49.325 -24.060 -2.480  1.00 15.02 ?  49  VAL   B HG13 1 
ATOM   3516 H HG21 . VAL   B 1 49  ? 47.179 -26.348 -2.072  1.00 16.86 ?  49  VAL   B HG21 1 
ATOM   3517 H HG22 . VAL   B 1 49  ? 48.653 -26.692 -2.555  1.00 16.86 ?  49  VAL   B HG22 1 
ATOM   3518 H HG23 . VAL   B 1 49  ? 48.099 -27.303 -1.197  1.00 16.86 ?  49  VAL   B HG23 1 
ATOM   3519 N N    . ALA   B 1 50  ? 50.378 -23.851 1.161   1.00 10.21 ?  50  ALA   B N    1 
ATOM   3520 C CA   . ALA   B 1 50  ? 50.898 -22.575 1.642   1.00 10.09 ?  50  ALA   B CA   1 
ATOM   3521 C C    . ALA   B 1 50  ? 52.416 -22.606 1.746   1.00 10.42 ?  50  ALA   B C    1 
ATOM   3522 O O    . ALA   B 1 50  ? 53.092 -21.638 1.376   1.00 10.40 ?  50  ALA   B O    1 
ATOM   3523 C CB   . ALA   B 1 50  ? 50.267 -22.215 2.987   1.00 10.65 ?  50  ALA   B CB   1 
ATOM   3524 H H    . ALA   B 1 50  ? 49.866 -24.265 1.713   1.00 12.25 ?  50  ALA   B H    1 
ATOM   3525 H HA   . ALA   B 1 50  ? 50.667 -21.882 1.012   1.00 12.11 ?  50  ALA   B HA   1 
ATOM   3526 H HB1  . ALA   B 1 50  ? 50.621 -21.363 3.288   1.00 12.78 ?  50  ALA   B HB1  1 
ATOM   3527 H HB2  . ALA   B 1 50  ? 49.303 -22.149 2.875   1.00 12.78 ?  50  ALA   B HB2  1 
ATOM   3528 H HB3  . ALA   B 1 50  ? 50.474 -22.907 3.634   1.00 12.78 ?  50  ALA   B HB3  1 
ATOM   3529 N N    . GLY   B 1 51  ? 52.970 -23.701 2.261   1.00 10.95 ?  51  GLY   B N    1 
ATOM   3530 C CA   . GLY   B 1 51  ? 54.416 -23.806 2.330   1.00 11.59 ?  51  GLY   B CA   1 
ATOM   3531 C C    . GLY   B 1 51  ? 55.062 -23.754 0.960   1.00 11.19 ?  51  GLY   B C    1 
ATOM   3532 O O    . GLY   B 1 51  ? 56.103 -23.117 0.776   1.00 12.15 ?  51  GLY   B O    1 
ATOM   3533 H H    . GLY   B 1 51  ? 52.544 -24.381 2.571   1.00 13.14 ?  51  GLY   B H    1 
ATOM   3534 H HA2  . GLY   B 1 51  ? 54.772 -23.075 2.865   1.00 13.91 ?  51  GLY   B HA2  1 
ATOM   3535 H HA3  . GLY   B 1 51  ? 54.664 -24.642 2.756   1.00 13.91 ?  51  GLY   B HA3  1 
ATOM   3536 N N    . ALA   B 1 52  ? 54.451 -24.414 -0.021  1.00 11.13 ?  52  ALA   B N    1 
ATOM   3537 C CA   . ALA   B 1 52  ? 55.013 -24.421 -1.365  1.00 11.36 ?  52  ALA   B CA   1 
ATOM   3538 C C    . ALA   B 1 52  ? 54.935 -23.044 -2.014  1.00 11.00 ?  52  ALA   B C    1 
ATOM   3539 O O    . ALA   B 1 52  ? 55.904 -22.596 -2.645  1.00 11.61 ?  52  ALA   B O    1 
ATOM   3540 C CB   . ALA   B 1 52  ? 54.305 -25.464 -2.223  1.00 12.21 ?  52  ALA   B CB   1 
ATOM   3541 H H    . ALA   B 1 52  ? 53.718 -24.855 0.066   1.00 13.36 ?  52  ALA   B H    1 
ATOM   3542 H HA   . ALA   B 1 52  ? 55.949 -24.666 -1.308  1.00 13.64 ?  52  ALA   B HA   1 
ATOM   3543 H HB1  . ALA   B 1 52  ? 54.694 -25.455 -3.112  1.00 14.66 ?  52  ALA   B HB1  1 
ATOM   3544 H HB2  . ALA   B 1 52  ? 54.427 -26.339 -1.819  1.00 14.66 ?  52  ALA   B HB2  1 
ATOM   3545 H HB3  . ALA   B 1 52  ? 53.363 -25.249 -2.270  1.00 14.66 ?  52  ALA   B HB3  1 
ATOM   3546 N N    . LEU   B 1 53  ? 53.790 -22.364 -1.892  1.00 10.50 ?  53  LEU   B N    1 
ATOM   3547 C CA   . LEU   B 1 53  ? 53.678 -21.027 -2.460  1.00 10.72 ?  53  LEU   B CA   1 
ATOM   3548 C C    . LEU   B 1 53  ? 54.682 -20.088 -1.812  1.00 10.82 ?  53  LEU   B C    1 
ATOM   3549 O O    . LEU   B 1 53  ? 55.382 -19.337 -2.499  1.00 11.59 ?  53  LEU   B O    1 
ATOM   3550 C CB   . LEU   B 1 53  ? 52.254 -20.489 -2.287  1.00 11.16 ?  53  LEU   B CB   1 
ATOM   3551 C CG   . LEU   B 1 53  ? 51.125 -21.204 -3.036  1.00 11.60 ?  53  LEU   B CG   1 
ATOM   3552 C CD1  . LEU   B 1 53  ? 49.780 -20.585 -2.689  1.00 12.90 ?  53  LEU   B CD1  1 
ATOM   3553 C CD2  . LEU   B 1 53  ? 51.346 -21.177 -4.540  1.00 13.41 ?  53  LEU   B CD2  1 
ATOM   3554 H H    . LEU   B 1 53  ? 53.083 -22.649 -1.489  1.00 12.60 ?  53  LEU   B H    1 
ATOM   3555 H HA   . LEU   B 1 53  ? 53.872 -21.069 -3.410  1.00 12.87 ?  53  LEU   B HA   1 
ATOM   3556 H HB2  . LEU   B 1 53  ? 52.032 -20.527 -1.345  1.00 13.39 ?  53  LEU   B HB2  1 
ATOM   3557 H HB3  . LEU   B 1 53  ? 52.244 -19.567 -2.581  1.00 13.39 ?  53  LEU   B HB3  1 
ATOM   3558 H HG   . LEU   B 1 53  ? 51.098 -22.132 -2.756  1.00 13.92 ?  53  LEU   B HG   1 
ATOM   3559 H HD11 . LEU   B 1 53  ? 49.080 -21.055 -3.172  1.00 15.48 ?  53  LEU   B HD11 1 
ATOM   3560 H HD12 . LEU   B 1 53  ? 49.631 -20.668 -1.733  1.00 15.48 ?  53  LEU   B HD12 1 
ATOM   3561 H HD13 . LEU   B 1 53  ? 49.786 -19.650 -2.942  1.00 15.48 ?  53  LEU   B HD13 1 
ATOM   3562 H HD21 . LEU   B 1 53  ? 50.605 -21.622 -4.979  1.00 16.09 ?  53  LEU   B HD21 1 
ATOM   3563 H HD22 . LEU   B 1 53  ? 51.400 -20.255 -4.835  1.00 16.09 ?  53  LEU   B HD22 1 
ATOM   3564 H HD23 . LEU   B 1 53  ? 52.175 -21.639 -4.745  1.00 16.09 ?  53  LEU   B HD23 1 
ATOM   3565 N N    . ASN   B 1 54  ? 54.774 -20.118 -0.484  1.00 10.38 ?  54  ASN   B N    1 
ATOM   3566 C CA   . ASN   B 1 54  ? 55.688 -19.207 0.189   1.00 11.11 ?  54  ASN   B CA   1 
ATOM   3567 C C    . ASN   B 1 54  ? 57.130 -19.480 -0.216  1.00 11.32 ?  54  ASN   B C    1 
ATOM   3568 O O    . ASN   B 1 54  ? 57.904 -18.543 -0.450  1.00 11.84 ?  54  ASN   B O    1 
ATOM   3569 C CB   . ASN   B 1 54  ? 55.532 -19.295 1.700   1.00 11.73 ?  54  ASN   B CB   1 
ATOM   3570 C CG   . ASN   B 1 54  ? 56.504 -18.381 2.417   1.00 11.98 ?  54  ASN   B CG   1 
ATOM   3571 O OD1  . ASN   B 1 54  ? 56.519 -17.172 2.179   1.00 11.88 ?  54  ASN   B OD1  1 
ATOM   3572 N ND2  . ASN   B 1 54  ? 57.345 -18.954 3.268   1.00 13.23 ?  54  ASN   B ND2  1 
ATOM   3573 H H    . ASN   B 1 54  ? 54.330 -20.643 0.034   1.00 12.46 ?  54  ASN   B H    1 
ATOM   3574 H HA   . ASN   B 1 54  ? 55.473 -18.299 -0.080  1.00 13.33 ?  54  ASN   B HA   1 
ATOM   3575 H HB2  . ASN   B 1 54  ? 54.629 -19.025 1.942   1.00 14.08 ?  54  ASN   B HB2  1 
ATOM   3576 H HB3  . ASN   B 1 54  ? 55.698 -20.203 1.987   1.00 14.08 ?  54  ASN   B HB3  1 
ATOM   3577 H HD21 . ASN   B 1 54  ? 57.920 -18.474 3.693   1.00 15.89 ?  54  ASN   B HD21 1 
ATOM   3578 H HD22 . ASN   B 1 54  ? 57.316 -19.803 3.400   1.00 15.89 ?  54  ASN   B HD22 1 
ATOM   3579 N N    . LYS   B 1 55  ? 57.514 -20.756 -0.292  1.00 11.97 ?  55  LYS   B N    1 
ATOM   3580 C CA   . LYS   B 1 55  ? 58.872 -21.091 -0.705  1.00 12.94 ?  55  LYS   B CA   1 
ATOM   3581 C C    . LYS   B 1 55  ? 59.173 -20.549 -2.096  1.00 12.48 ?  55  LYS   B C    1 
ATOM   3582 O O    . LYS   B 1 55  ? 60.272 -20.044 -2.348  1.00 13.11 ?  55  LYS   B O    1 
ATOM   3583 C CB   . LYS   B 1 55  ? 59.068 -22.605 -0.653  1.00 14.34 ?  55  LYS   B CB   1 
ATOM   3584 C CG   . LYS   B 1 55  ? 60.459 -23.059 -1.045  1.00 18.01 ?  55  LYS   B CG   1 
ATOM   3585 C CD   . LYS   B 1 55  ? 60.622 -24.561 -0.894  1.00 21.25 ?  55  LYS   B CD   1 
ATOM   3586 C CE   . LYS   B 1 55  ? 60.610 -24.988 0.571   1.00 24.10 ?  55  LYS   B CE   1 
ATOM   3587 N NZ   . LYS   B 1 55  ? 60.977 -26.415 0.743   1.00 25.28 ?  55  LYS   B NZ   1 
ATOM   3588 H H    . LYS   B 1 55  ? 57.014 -21.432 -0.113  1.00 14.36 ?  55  LYS   B H    1 
ATOM   3589 H HA   . LYS   B 1 55  ? 59.500 -20.688 -0.087  1.00 15.53 ?  55  LYS   B HA   1 
ATOM   3590 H HB2  . LYS   B 1 55  ? 58.901 -22.904 0.255   1.00 17.22 ?  55  LYS   B HB2  1 
ATOM   3591 H HB3  . LYS   B 1 55  ? 58.440 -23.024 -1.259  1.00 17.22 ?  55  LYS   B HB3  1 
ATOM   3592 H HG2  . LYS   B 1 55  ? 60.624 -22.831 -1.973  1.00 21.61 ?  55  LYS   B HG2  1 
ATOM   3593 H HG3  . LYS   B 1 55  ? 61.113 -22.624 -0.473  1.00 21.61 ?  55  LYS   B HG3  1 
ATOM   3594 H HD2  . LYS   B 1 55  ? 59.890 -25.011 -1.345  1.00 25.51 ?  55  LYS   B HD2  1 
ATOM   3595 H HD3  . LYS   B 1 55  ? 61.471 -24.834 -1.280  1.00 25.51 ?  55  LYS   B HD3  1 
ATOM   3596 H HE2  . LYS   B 1 55  ? 61.249 -24.443 1.061   1.00 28.92 ?  55  LYS   B HE2  1 
ATOM   3597 H HE3  . LYS   B 1 55  ? 59.718 -24.855 0.930   1.00 28.92 ?  55  LYS   B HE3  1 
ATOM   3598 H HZ1  . LYS   B 1 55  ? 60.924 -26.638 1.603   1.00 30.34 ?  55  LYS   B HZ1  1 
ATOM   3599 H HZ2  . LYS   B 1 55  ? 60.419 -26.927 0.276   1.00 30.34 ?  55  LYS   B HZ2  1 
ATOM   3600 H HZ3  . LYS   B 1 55  ? 61.806 -26.551 0.456   1.00 30.34 ?  55  LYS   B HZ3  1 
ATOM   3601 N N    . ALA   B 1 56  ? 58.203 -20.629 -3.010  1.00 12.20 ?  56  ALA   B N    1 
ATOM   3602 C CA   . ALA   B 1 56  ? 58.423 -20.122 -4.359  1.00 12.93 ?  56  ALA   B CA   1 
ATOM   3603 C C    . ALA   B 1 56  ? 58.698 -18.626 -4.355  1.00 12.54 ?  56  ALA   B C    1 
ATOM   3604 O O    . ALA   B 1 56  ? 59.420 -18.126 -5.226  1.00 13.68 ?  56  ALA   B O    1 
ATOM   3605 C CB   . ALA   B 1 56  ? 57.229 -20.450 -5.254  1.00 14.13 ?  56  ALA   B CB   1 
ATOM   3606 H H    . ALA   B 1 56  ? 57.418 -20.958 -2.875  1.00 14.65 ?  56  ALA   B H    1 
ATOM   3607 H HA   . ALA   B 1 56  ? 59.201 -20.557 -4.732  1.00 15.51 ?  56  ALA   B HA   1 
ATOM   3608 H HB1  . ALA   B 1 56  ? 57.402 -20.110 -6.149  1.00 16.96 ?  56  ALA   B HB1  1 
ATOM   3609 H HB2  . ALA   B 1 56  ? 57.117 -21.413 -5.286  1.00 16.96 ?  56  ALA   B HB2  1 
ATOM   3610 H HB3  . ALA   B 1 56  ? 56.434 -20.034 -4.891  1.00 16.96 ?  56  ALA   B HB3  1 
ATOM   3611 N N    . THR   B 1 57  ? 58.132 -17.896 -3.391  1.00 12.47 ?  57  THR   B N    1 
ATOM   3612 C CA   . THR   B 1 57  ? 58.367 -16.462 -3.260  1.00 12.47 ?  57  THR   B CA   1 
ATOM   3613 C C    . THR   B 1 57  ? 59.618 -16.138 -2.451  1.00 13.38 ?  57  THR   B C    1 
ATOM   3614 O O    . THR   B 1 57  ? 59.849 -14.964 -2.136  1.00 13.78 ?  57  THR   B O    1 
ATOM   3615 C CB   . THR   B 1 57  ? 57.163 -15.746 -2.620  1.00 12.00 ?  57  THR   B CB   1 
ATOM   3616 O OG1  . THR   B 1 57  ? 57.147 -15.968 -1.201  1.00 12.15 ?  57  THR   B OG1  1 
ATOM   3617 C CG2  . THR   B 1 57  ? 55.842 -16.179 -3.258  1.00 12.31 ?  57  THR   B CG2  1 
ATOM   3618 H H    . THR   B 1 57  ? 57.589 -18.212 -2.801  1.00 14.97 ?  57  THR   B H    1 
ATOM   3619 H HA   . THR   B 1 57  ? 58.484 -16.089 -4.147  1.00 14.97 ?  57  THR   B HA   1 
ATOM   3620 H HB   . THR   B 1 57  ? 57.253 -14.794 -2.782  1.00 14.41 ?  57  THR   B HB   1 
ATOM   3621 H HG1  . THR   B 1 57  ? 57.079 -16.790 -1.045  1.00 14.58 ?  57  THR   B HG1  1 
ATOM   3622 H HG21 . THR   B 1 57  ? 55.113 -15.641 -2.916  1.00 14.77 ?  57  THR   B HG21 1 
ATOM   3623 H HG22 . THR   B 1 57  ? 55.886 -16.076 -4.222  1.00 14.77 ?  57  THR   B HG22 1 
ATOM   3624 H HG23 . THR   B 1 57  ? 55.665 -17.112 -3.054  1.00 14.77 ?  57  THR   B HG23 1 
ATOM   3625 N N    . ASN   B 1 58  ? 60.416 -17.143 -2.095  1.00 13.98 ?  58  ASN   B N    1 
ATOM   3626 C CA   . ASN   B 1 58  ? 61.613 -16.932 -1.284  1.00 16.47 ?  58  ASN   B CA   1 
ATOM   3627 C C    . ASN   B 1 58  ? 61.270 -16.228 0.029   1.00 14.64 ?  58  ASN   B C    1 
ATOM   3628 O O    . ASN   B 1 58  ? 61.999 -15.351 0.498   1.00 15.25 ?  58  ASN   B O    1 
ATOM   3629 C CB   . ASN   B 1 58  ? 62.695 -16.178 -2.061  1.00 23.30 ?  58  ASN   B CB   1 
ATOM   3630 C CG   . ASN   B 1 58  ? 64.061 -16.293 -1.415  1.00 31.22 ?  58  ASN   B CG   1 
ATOM   3631 O OD1  . ASN   B 1 58  ? 64.361 -17.279 -0.742  1.00 33.64 ?  58  ASN   B OD1  1 
ATOM   3632 N ND2  . ASN   B 1 58  ? 64.898 -15.280 -1.615  1.00 34.73 ?  58  ASN   B ND2  1 
ATOM   3633 H H    . ASN   B 1 58  ? 60.278 -17.972 -2.303  1.00 16.78 ?  58  ASN   B H    1 
ATOM   3634 H HA   . ASN   B 1 58  ? 61.978 -17.804 -1.060  1.00 19.77 ?  58  ASN   B HA   1 
ATOM   3635 H HB2  . ASN   B 1 58  ? 62.754 -16.545 -2.959  1.00 27.97 ?  58  ASN   B HB2  1 
ATOM   3636 H HB3  . ASN   B 1 58  ? 62.461 -15.240 -2.100  1.00 27.97 ?  58  ASN   B HB3  1 
ATOM   3637 H HD21 . ASN   B 1 58  ? 65.686 -15.298 -1.272  1.00 41.68 ?  58  ASN   B HD21 1 
ATOM   3638 H HD22 . ASN   B 1 58  ? 64.651 -14.607 -2.090  1.00 41.68 ?  58  ASN   B HD22 1 
ATOM   3639 N N    . ASN   B 1 59  ? 60.147 -16.619 0.629   1.00 13.51 ?  59  ASN   B N    1 
ATOM   3640 C CA   . ASN   B 1 59  ? 59.670 -16.150 1.930   1.00 13.51 ?  59  ASN   B CA   1 
ATOM   3641 C C    . ASN   B 1 59  ? 59.075 -14.744 1.879   1.00 12.80 ?  59  ASN   B C    1 
ATOM   3642 O O    . ASN   B 1 59  ? 58.646 -14.240 2.925   1.00 13.15 ?  59  ASN   B O    1 
ATOM   3643 C CB   . ASN   B 1 59  ? 60.740 -16.209 3.035   1.00 14.66 ?  59  ASN   B CB   1 
ATOM   3644 C CG   . ASN   B 1 59  ? 60.148 -16.396 4.414   1.00 15.73 ?  59  ASN   B CG   1 
ATOM   3645 O OD1  . ASN   B 1 59  ? 59.317 -17.278 4.630   1.00 16.17 ?  59  ASN   B OD1  1 
ATOM   3646 N ND2  . ASN   B 1 59  ? 60.570 -15.563 5.357   1.00 16.30 ?  59  ASN   B ND2  1 
ATOM   3647 H H    . ASN   B 1 59  ? 59.614 -17.198 0.282   1.00 16.21 ?  59  ASN   B H    1 
ATOM   3648 H HA   . ASN   B 1 59  ? 58.960 -16.746 2.210   1.00 16.22 ?  59  ASN   B HA   1 
ATOM   3649 H HB2  . ASN   B 1 59  ? 61.334 -16.956 2.869   1.00 17.59 ?  59  ASN   B HB2  1 
ATOM   3650 H HB3  . ASN   B 1 59  ? 61.240 -15.380 3.042   1.00 17.59 ?  59  ASN   B HB3  1 
ATOM   3651 H HD21 . ASN   B 1 59  ? 60.263 -15.627 6.160   1.00 19.56 ?  59  ASN   B HD21 1 
ATOM   3652 H HD22 . ASN   B 1 59  ? 61.151 -14.958 5.168   1.00 19.56 ?  59  ASN   B HD22 1 
ATOM   3653 N N    . ALA   B 1 60  ? 59.014 -14.096 0.711   1.00 12.63 ?  60  ALA   B N    1 
ATOM   3654 C CA   . ALA   B 1 60  ? 58.412 -12.766 0.647   1.00 12.64 ?  60  ALA   B CA   1 
ATOM   3655 C C    . ALA   B 1 60  ? 56.942 -12.794 1.043   1.00 11.93 ?  60  ALA   B C    1 
ATOM   3656 O O    . ALA   B 1 60  ? 56.441 -11.841 1.654   1.00 12.52 ?  60  ALA   B O    1 
ATOM   3657 C CB   . ALA   B 1 60  ? 58.579 -12.174 -0.753  1.00 13.53 ?  60  ALA   B CB   1 
ATOM   3658 H H    . ALA   B 1 60  ? 59.308 -14.400 -0.035  1.00 15.15 ?  60  ALA   B H    1 
ATOM   3659 H HA   . ALA   B 1 60  ? 58.873 -12.187 1.271   1.00 15.17 ?  60  ALA   B HA   1 
ATOM   3660 H HB1  . ALA   B 1 60  ? 58.177 -11.293 -0.773  1.00 16.24 ?  60  ALA   B HB1  1 
ATOM   3661 H HB2  . ALA   B 1 60  ? 59.528 -12.108 -0.956  1.00 16.24 ?  60  ALA   B HB2  1 
ATOM   3662 H HB3  . ALA   B 1 60  ? 58.145 -12.754 -1.398  1.00 16.24 ?  60  ALA   B HB3  1 
ATOM   3663 N N    . MET   B 1 61  ? 56.236 -13.869 0.700   1.00 11.53 ?  61  MET   B N    1 
ATOM   3664 C CA   . MET   B 1 61  ? 54.841 -13.990 1.095   1.00 11.36 ?  61  MET   B CA   1 
ATOM   3665 C C    . MET   B 1 61  ? 54.705 -14.003 2.616   1.00 11.34 ?  61  MET   B C    1 
ATOM   3666 O O    . MET   B 1 61  ? 53.807 -13.357 3.169   1.00 11.29 ?  61  MET   B O    1 
ATOM   3667 C CB   . MET   B 1 61  ? 54.261 -15.257 0.467   1.00 10.93 ?  61  MET   B CB   1 
ATOM   3668 C CG   . MET   B 1 61  ? 52.823 -15.554 0.883   1.00 11.04 ?  61  MET   B CG   1 
ATOM   3669 S SD   . MET   B 1 61  ? 52.181 -17.053 0.123   1.00 11.90 ?  61  MET   B SD   1 
ATOM   3670 C CE   . MET   B 1 61  ? 51.939 -16.470 -1.554  1.00 13.07 ?  61  MET   B CE   1 
ATOM   3671 H H    . MET   B 1 61  ? 56.539 -14.534 0.242   1.00 13.84 ?  61  MET   B H    1 
ATOM   3672 H HA   . MET   B 1 61  ? 54.347 -13.234 0.737   1.00 13.63 ?  61  MET   B HA   1 
ATOM   3673 H HB2  . MET   B 1 61  ? 54.273 -15.163 -0.501  1.00 13.12 ?  61  MET   B HB2  1 
ATOM   3674 H HB3  . MET   B 1 61  ? 54.806 -16.015 0.727   1.00 13.12 ?  61  MET   B HB3  1 
ATOM   3675 H HG2  . MET   B 1 61  ? 52.785 -15.672 1.845   1.00 13.25 ?  61  MET   B HG2  1 
ATOM   3676 H HG3  . MET   B 1 61  ? 52.255 -14.814 0.616   1.00 13.25 ?  61  MET   B HG3  1 
ATOM   3677 H HE1  . MET   B 1 61  ? 51.548 -17.183 -2.084  1.00 15.69 ?  61  MET   B HE1  1 
ATOM   3678 H HE2  . MET   B 1 61  ? 51.345 -15.704 -1.542  1.00 15.69 ?  61  MET   B HE2  1 
ATOM   3679 H HE3  . MET   B 1 61  ? 52.799 -16.216 -1.929  1.00 15.69 ?  61  MET   B HE3  1 
ATOM   3680 N N    . GLN   B 1 62  ? 55.588 -14.724 3.315   1.00 11.22 ?  62  GLN   B N    1 
ATOM   3681 C CA   . GLN   B 1 62  ? 55.484 -14.785 4.770   1.00 11.60 ?  62  GLN   B CA   1 
ATOM   3682 C C    . GLN   B 1 62  ? 55.766 -13.432 5.408   1.00 11.86 ?  62  GLN   B C    1 
ATOM   3683 O O    . GLN   B 1 62  ? 55.086 -13.036 6.362   1.00 12.13 ?  62  GLN   B O    1 
ATOM   3684 C CB   . GLN   B 1 62  ? 56.437 -15.838 5.330   1.00 11.75 ?  62  GLN   B CB   1 
ATOM   3685 C CG   . GLN   B 1 62  ? 56.221 -16.107 6.808   1.00 12.08 ?  62  GLN   B CG   1 
ATOM   3686 C CD   . GLN   B 1 62  ? 54.852 -16.706 7.058   1.00 11.78 ?  62  GLN   B CD   1 
ATOM   3687 O OE1  . GLN   B 1 62  ? 54.601 -17.859 6.710   1.00 12.28 ?  62  GLN   B OE1  1 
ATOM   3688 N NE2  . GLN   B 1 62  ? 53.942 -15.913 7.612   1.00 12.28 ?  62  GLN   B NE2  1 
ATOM   3689 H H    . GLN   B 1 62  ? 56.233 -15.177 2.972   1.00 13.46 ?  62  GLN   B H    1 
ATOM   3690 H HA   . GLN   B 1 62  ? 54.578 -15.041 5.003   1.00 13.92 ?  62  GLN   B HA   1 
ATOM   3691 H HB2  . GLN   B 1 62  ? 56.306 -16.671 4.851   1.00 14.10 ?  62  GLN   B HB2  1 
ATOM   3692 H HB3  . GLN   B 1 62  ? 57.350 -15.529 5.211   1.00 14.10 ?  62  GLN   B HB3  1 
ATOM   3693 H HG2  . GLN   B 1 62  ? 56.891 -16.737 7.116   1.00 14.50 ?  62  GLN   B HG2  1 
ATOM   3694 H HG3  . GLN   B 1 62  ? 56.289 -15.275 7.301   1.00 14.50 ?  62  GLN   B HG3  1 
ATOM   3695 H HE21 . GLN   B 1 62  ? 54.151 -15.108 7.833   1.00 14.74 ?  62  GLN   B HE21 1 
ATOM   3696 H HE22 . GLN   B 1 62  ? 53.153 -16.212 7.767   1.00 14.74 ?  62  GLN   B HE22 1 
ATOM   3697 N N    . VAL   B 1 63  ? 56.775 -12.713 4.912   1.00 12.41 ?  63  VAL   B N    1 
ATOM   3698 C CA   . VAL   B 1 63  ? 57.084 -11.398 5.469   1.00 13.14 ?  63  VAL   B CA   1 
ATOM   3699 C C    . VAL   B 1 63  ? 55.894 -10.463 5.291   1.00 12.55 ?  63  VAL   B C    1 
ATOM   3700 O O    . VAL   B 1 63  ? 55.485 -9.756  6.223   1.00 13.11 ?  63  VAL   B O    1 
ATOM   3701 C CB   . VAL   B 1 63  ? 58.372 -10.837 4.841   1.00 14.51 ?  63  VAL   B CB   1 
ATOM   3702 C CG1  . VAL   B 1 63  ? 58.602 -9.397  5.288   1.00 15.12 ?  63  VAL   B CG1  1 
ATOM   3703 C CG2  . VAL   B 1 63  ? 59.559 -11.709 5.224   1.00 15.30 ?  63  VAL   B CG2  1 
ATOM   3704 H H    . VAL   B 1 63  ? 57.283 -12.959 4.261   1.00 14.89 ?  63  VAL   B H    1 
ATOM   3705 H HA   . VAL   B 1 63  ? 57.242 -11.497 6.418   1.00 15.77 ?  63  VAL   B HA   1 
ATOM   3706 H HB   . VAL   B 1 63  ? 58.293 -10.846 3.876   1.00 17.41 ?  63  VAL   B HB   1 
ATOM   3707 H HG11 . VAL   B 1 63  ? 59.518 -9.148  5.094   1.00 18.15 ?  63  VAL   B HG11 1 
ATOM   3708 H HG12 . VAL   B 1 63  ? 57.991 -8.816  4.810   1.00 18.15 ?  63  VAL   B HG12 1 
ATOM   3709 H HG13 . VAL   B 1 63  ? 58.440 -9.336  6.244   1.00 18.15 ?  63  VAL   B HG13 1 
ATOM   3710 H HG21 . VAL   B 1 63  ? 60.367 -11.332 4.840   1.00 18.36 ?  63  VAL   B HG21 1 
ATOM   3711 H HG22 . VAL   B 1 63  ? 59.635 -11.731 6.193   1.00 18.36 ?  63  VAL   B HG22 1 
ATOM   3712 H HG23 . VAL   B 1 63  ? 59.418 -12.605 4.884   1.00 18.36 ?  63  VAL   B HG23 1 
ATOM   3713 N N    . GLU   B 1 64  ? 55.320 -10.449 4.087   1.00 12.22 ?  64  GLU   B N    1 
ATOM   3714 C CA   . GLU   B 1 64  ? 54.152 -9.613  3.819   1.00 11.84 ?  64  GLU   B CA   1 
ATOM   3715 C C    . GLU   B 1 64  ? 52.974 -10.018 4.700   1.00 11.52 ?  64  GLU   B C    1 
ATOM   3716 O O    . GLU   B 1 64  ? 52.232 -9.161  5.205   1.00 12.07 ?  64  GLU   B O    1 
ATOM   3717 C CB   . GLU   B 1 64  ? 53.787 -9.748  2.340   1.00 12.05 ?  64  GLU   B CB   1 
ATOM   3718 C CG   . GLU   B 1 64  ? 52.520 -9.019  1.923   1.00 12.30 ?  64  GLU   B CG   1 
ATOM   3719 C CD   . GLU   B 1 64  ? 51.981 -9.505  0.584   1.00 13.16 ?  64  GLU   B CD   1 
ATOM   3720 O OE1  . GLU   B 1 64  ? 52.166 -10.706 0.251   1.00 14.32 ?  64  GLU   B OE1  1 
ATOM   3721 O OE2  . GLU   B 1 64  ? 51.355 -8.685  -0.134  1.00 14.03 -1 64  GLU   B OE2  1 
ATOM   3722 H H    . GLU   B 1 64  ? 55.595 -10.909 3.410   1.00 14.67 ?  64  GLU   B H    1 
ATOM   3723 H HA   . GLU   B 1 64  ? 54.371 -8.686  3.998   1.00 14.22 ?  64  GLU   B HA   1 
ATOM   3724 H HB2  . GLU   B 1 64  ? 54.516 -9.386  1.805   1.00 14.46 ?  64  GLU   B HB2  1 
ATOM   3725 H HB3  . GLU   B 1 64  ? 53.671 -10.686 2.134   1.00 14.46 ?  64  GLU   B HB3  1 
ATOM   3726 H HG2  . GLU   B 1 64  ? 51.826 -9.160  2.590   1.00 14.77 ?  64  GLU   B HG2  1 
ATOM   3727 H HG3  . GLU   B 1 64  ? 52.710 -8.072  1.845   1.00 14.77 ?  64  GLU   B HG3  1 
ATOM   3728 N N    . SER   B 1 65  ? 52.790 -11.327 4.887   1.00 11.33 ?  65  SER   B N    1 
ATOM   3729 C CA   . SER   B 1 65  ? 51.684 -11.837 5.688   1.00 11.30 ?  65  SER   B CA   1 
ATOM   3730 C C    . SER   B 1 65  ? 51.820 -11.439 7.151   1.00 11.41 ?  65  SER   B C    1 
ATOM   3731 O O    . SER   B 1 65  ? 50.827 -11.064 7.790   1.00 11.81 ?  65  SER   B O    1 
ATOM   3732 C CB   . SER   B 1 65  ? 51.601 -13.358 5.555   1.00 11.46 ?  65  SER   B CB   1 
ATOM   3733 O OG   . SER   B 1 65  ? 51.254 -13.748 4.235   1.00 11.86 ?  65  SER   B OG   1 
ATOM   3734 H H    . SER   B 1 65  ? 53.301 -11.944 4.564   1.00 13.60 ?  65  SER   B H    1 
ATOM   3735 H HA   . SER   B 1 65  ? 50.854 -11.462 5.352   1.00 13.56 ?  65  SER   B HA   1 
ATOM   3736 H HB2  . SER   B 1 65  ? 52.462 -13.741 5.774   1.00 13.76 ?  65  SER   B HB2  1 
ATOM   3737 H HB3  . SER   B 1 65  ? 50.925 -13.689 6.167   1.00 13.76 ?  65  SER   B HB3  1 
ATOM   3738 H HG   . SER   B 1 65  ? 51.828 -13.458 3.687   1.00 14.23 ?  65  SER   B HG   1 
ATOM   3739 N N    . ASP   B 1 66  ? 53.032 -11.539 7.707   1.00 11.81 ?  66  ASP   B N    1 
ATOM   3740 C CA   . ASP   B 1 66  ? 53.233 -11.150 9.100   1.00 12.17 ?  66  ASP   B CA   1 
ATOM   3741 C C    . ASP   B 1 66  ? 52.916 -9.673  9.308   1.00 12.27 ?  66  ASP   B C    1 
ATOM   3742 O O    . ASP   B 1 66  ? 52.343 -9.290  10.334  1.00 12.97 ?  66  ASP   B O    1 
ATOM   3743 C CB   . ASP   B 1 66  ? 54.668 -11.451 9.535   1.00 13.70 ?  66  ASP   B CB   1 
ATOM   3744 C CG   . ASP   B 1 66  ? 54.940 -12.939 9.695   1.00 15.60 ?  66  ASP   B CG   1 
ATOM   3745 O OD1  . ASP   B 1 66  ? 53.989 -13.748 9.608   1.00 16.12 ?  66  ASP   B OD1  1 
ATOM   3746 O OD2  . ASP   B 1 66  ? 56.116 -13.301 9.916   1.00 17.95 -1 66  ASP   B OD2  1 
ATOM   3747 H H    . ASP   B 1 66  ? 53.735 -11.830 7.309   1.00 14.17 ?  66  ASP   B H    1 
ATOM   3748 H HA   . ASP   B 1 66  ? 52.637 -11.661 9.667   1.00 14.61 ?  66  ASP   B HA   1 
ATOM   3749 H HB2  . ASP   B 1 66  ? 55.281 -11.106 8.867   1.00 16.44 ?  66  ASP   B HB2  1 
ATOM   3750 H HB3  . ASP   B 1 66  ? 54.837 -11.019 10.390  1.00 16.44 ?  66  ASP   B HB3  1 
ATOM   3751 N N    . ASP   B 1 67  ? 53.285 -8.826  8.347   1.00 12.11 ?  67  ASP   B N    1 
ATOM   3752 C CA   . ASP   B 1 67  ? 52.935 -7.414  8.444   1.00 12.73 ?  67  ASP   B CA   1 
ATOM   3753 C C    . ASP   B 1 67  ? 51.423 -7.209  8.364   1.00 12.54 ?  67  ASP   B C    1 
ATOM   3754 O O    . ASP   B 1 67  ? 50.859 -6.406  9.116   1.00 13.09 ?  67  ASP   B O    1 
ATOM   3755 C CB   . ASP   B 1 67  ? 53.652 -6.635  7.348   1.00 14.05 ?  67  ASP   B CB   1 
ATOM   3756 C CG   . ASP   B 1 67  ? 53.234 -5.194  7.315   1.00 15.49 ?  67  ASP   B CG   1 
ATOM   3757 O OD1  . ASP   B 1 67  ? 53.743 -4.395  8.133   1.00 16.46 ?  67  ASP   B OD1  1 
ATOM   3758 O OD2  . ASP   B 1 67  ? 52.370 -4.875  6.482   1.00 16.68 -1 67  ASP   B OD2  1 
ATOM   3759 H H    . ASP   B 1 67  ? 53.737 -9.038  7.645   1.00 14.54 ?  67  ASP   B H    1 
ATOM   3760 H HA   . ASP   B 1 67  ? 53.239 -7.071  9.296   1.00 15.27 ?  67  ASP   B HA   1 
ATOM   3761 H HB2  . ASP   B 1 67  ? 54.609 -6.664  7.506   1.00 16.87 ?  67  ASP   B HB2  1 
ATOM   3762 H HB3  . ASP   B 1 67  ? 53.448 -7.034  6.485   1.00 16.87 ?  67  ASP   B HB3  1 
ATOM   3763 N N    . TYR   B 1 68  ? 50.746 -7.945  7.475   1.00 12.17 ?  68  TYR   B N    1 
ATOM   3764 C CA   . TYR   B 1 68  ? 49.288 -7.870  7.408   1.00 12.76 ?  68  TYR   B CA   1 
ATOM   3765 C C    . TYR   B 1 68  ? 48.654 -8.216  8.752   1.00 12.32 ?  68  TYR   B C    1 
ATOM   3766 O O    . TYR   B 1 68  ? 47.722 -7.538  9.203   1.00 12.91 ?  68  TYR   B O    1 
ATOM   3767 C CB   . TYR   B 1 68  ? 48.751 -8.803  6.316   1.00 13.67 ?  68  TYR   B CB   1 
ATOM   3768 C CG   . TYR   B 1 68  ? 47.244 -8.952  6.373   1.00 14.57 ?  68  TYR   B CG   1 
ATOM   3769 C CD1  . TYR   B 1 68  ? 46.652 -9.910  7.188   1.00 15.39 ?  68  TYR   B CD1  1 
ATOM   3770 C CD2  . TYR   B 1 68  ? 46.418 -8.112  5.647   1.00 15.69 ?  68  TYR   B CD2  1 
ATOM   3771 C CE1  . TYR   B 1 68  ? 45.284 -10.029 7.275   1.00 16.65 ?  68  TYR   B CE1  1 
ATOM   3772 C CE2  . TYR   B 1 68  ? 45.036 -8.231  5.721   1.00 16.21 ?  68  TYR   B CE2  1 
ATOM   3773 C CZ   . TYR   B 1 68  ? 44.486 -9.189  6.538   1.00 16.58 ?  68  TYR   B CZ   1 
ATOM   3774 O OH   . TYR   B 1 68  ? 43.118 -9.302  6.624   1.00 17.45 ?  68  TYR   B OH   1 
ATOM   3775 H H    . TYR   B 1 68  ? 51.102 -8.495  6.914   1.00 14.61 ?  68  TYR   B H    1 
ATOM   3776 H HA   . TYR   B 1 68  ? 49.032 -6.966  7.185   1.00 15.32 ?  68  TYR   B HA   1 
ATOM   3777 H HB2  . TYR   B 1 68  ? 48.982 -8.437  5.451   1.00 16.40 ?  68  TYR   B HB2  1 
ATOM   3778 H HB3  . TYR   B 1 68  ? 49.145 -9.681  6.427   1.00 16.40 ?  68  TYR   B HB3  1 
ATOM   3779 H HD1  . TYR   B 1 68  ? 47.188 -10.482 7.691   1.00 18.47 ?  68  TYR   B HD1  1 
ATOM   3780 H HD2  . TYR   B 1 68  ? 46.796 -7.458  5.110   1.00 18.83 ?  68  TYR   B HD2  1 
ATOM   3781 H HE1  . TYR   B 1 68  ? 44.900 -10.686 7.815   1.00 19.98 ?  68  TYR   B HE1  1 
ATOM   3782 H HE2  . TYR   B 1 68  ? 44.490 -7.662  5.231   1.00 19.45 ?  68  TYR   B HE2  1 
ATOM   3783 H HH   . TYR   B 1 68  ? 42.741 -8.745  6.114   1.00 20.95 ?  68  TYR   B HH   1 
ATOM   3784 N N    . ILE   B 1 69  ? 49.135 -9.282  9.396   1.00 12.08 ?  69  ILE   B N    1 
ATOM   3785 C CA   . ILE   B 1 69  ? 48.580 -9.710  10.676  1.00 12.65 ?  69  ILE   B CA   1 
ATOM   3786 C C    . ILE   B 1 69  ? 48.836 -8.663  11.751  1.00 12.41 ?  69  ILE   B C    1 
ATOM   3787 O O    . ILE   B 1 69  ? 47.969 -8.388  12.585  1.00 12.83 ?  69  ILE   B O    1 
ATOM   3788 C CB   . ILE   B 1 69  ? 49.157 -11.086 11.067  1.00 13.63 ?  69  ILE   B CB   1 
ATOM   3789 C CG1  . ILE   B 1 69  ? 48.631 -12.189 10.137  1.00 13.93 ?  69  ILE   B CG1  1 
ATOM   3790 C CG2  . ILE   B 1 69  ? 48.877 -11.399 12.531  1.00 14.75 ?  69  ILE   B CG2  1 
ATOM   3791 C CD1  . ILE   B 1 69  ? 47.160 -12.516 10.302  1.00 13.92 ?  69  ILE   B CD1  1 
ATOM   3792 H H    . ILE   B 1 69  ? 49.784 -9.771  9.117   1.00 14.50 ?  69  ILE   B H    1 
ATOM   3793 H HA   . ILE   B 1 69  ? 47.621 -9.806  10.585  1.00 15.19 ?  69  ILE   B HA   1 
ATOM   3794 H HB   . ILE   B 1 69  ? 50.120 -11.043 10.958  1.00 16.36 ?  69  ILE   B HB   1 
ATOM   3795 H HG12 . ILE   B 1 69  ? 48.769 -11.907 9.219   1.00 16.72 ?  69  ILE   B HG12 1 
ATOM   3796 H HG13 . ILE   B 1 69  ? 49.135 -13.000 10.306  1.00 16.72 ?  69  ILE   B HG13 1 
ATOM   3797 H HG21 . ILE   B 1 69  ? 49.023 -12.348 12.680  1.00 17.71 ?  69  ILE   B HG21 1 
ATOM   3798 H HG22 . ILE   B 1 69  ? 49.481 -10.886 13.090  1.00 17.71 ?  69  ILE   B HG22 1 
ATOM   3799 H HG23 . ILE   B 1 69  ? 47.957 -11.172 12.735  1.00 17.71 ?  69  ILE   B HG23 1 
ATOM   3800 H HD11 . ILE   B 1 69  ? 46.925 -13.220 9.678   1.00 16.71 ?  69  ILE   B HD11 1 
ATOM   3801 H HD12 . ILE   B 1 69  ? 47.002 -12.818 11.211  1.00 16.71 ?  69  ILE   B HD12 1 
ATOM   3802 H HD13 . ILE   B 1 69  ? 46.634 -11.724 10.120  1.00 16.71 ?  69  ILE   B HD13 1 
ATOM   3803 N N    . ALA   B 1 70  ? 50.033 -8.077  11.768  1.00 12.45 ?  70  ALA   B N    1 
ATOM   3804 C CA   . ALA   B 1 70  ? 50.316 -7.040  12.754  1.00 12.47 ?  70  ALA   B CA   1 
ATOM   3805 C C    . ALA   B 1 70  ? 49.319 -5.893  12.646  1.00 12.70 ?  70  ALA   B C    1 
ATOM   3806 O O    . ALA   B 1 70  ? 48.878 -5.346  13.662  1.00 13.06 ?  70  ALA   B O    1 
ATOM   3807 C CB   . ALA   B 1 70  ? 51.749 -6.534  12.583  1.00 13.31 ?  70  ALA   B CB   1 
ATOM   3808 H H    . ALA   B 1 70  ? 50.675 -8.255  11.234  1.00 14.94 ?  70  ALA   B H    1 
ATOM   3809 H HA   . ALA   B 1 70  ? 50.242 -7.417  13.645  1.00 14.97 ?  70  ALA   B HA   1 
ATOM   3810 H HB1  . ALA   B 1 70  ? 51.936 -5.869  13.265  1.00 15.98 ?  70  ALA   B HB1  1 
ATOM   3811 H HB2  . ALA   B 1 70  ? 52.362 -7.282  12.677  1.00 15.98 ?  70  ALA   B HB2  1 
ATOM   3812 H HB3  . ALA   B 1 70  ? 51.844 -6.141  11.701  1.00 15.98 ?  70  ALA   B HB3  1 
ATOM   3813 N N    . THR   B 1 71  ? 48.944 -5.522  11.424  1.00 13.22 ?  71  THR   B N    1 
ATOM   3814 C CA   . THR   B 1 71  ? 48.048 -4.388  11.223  1.00 14.16 ?  71  THR   B CA   1 
ATOM   3815 C C    . THR   B 1 71  ? 46.583 -4.761  11.429  1.00 14.61 ?  71  THR   B C    1 
ATOM   3816 O O    . THR   B 1 71  ? 45.802 -3.947  11.941  1.00 16.38 ?  71  THR   B O    1 
ATOM   3817 C CB   . THR   B 1 71  ? 48.256 -3.820  9.818   1.00 16.24 ?  71  THR   B CB   1 
ATOM   3818 O OG1  . THR   B 1 71  ? 49.581 -3.290  9.712   1.00 18.13 ?  71  THR   B OG1  1 
ATOM   3819 C CG2  . THR   B 1 71  ? 47.237 -2.729  9.505   1.00 17.39 ?  71  THR   B CG2  1 
ATOM   3820 H H    . THR   B 1 71  ? 49.193 -5.909  10.701  1.00 15.87 ?  71  THR   B H    1 
ATOM   3821 H HA   . THR   B 1 71  ? 48.271 -3.691  11.861  1.00 17.00 ?  71  THR   B HA   1 
ATOM   3822 H HB   . THR   B 1 71  ? 48.156 -4.525  9.164   1.00 19.49 ?  71  THR   B HB   1 
ATOM   3823 H HG1  . THR   B 1 71  ? 49.706 -2.955  8.947   1.00 21.76 ?  71  THR   B HG1  1 
ATOM   3824 H HG21 . THR   B 1 71  ? 47.539 -2.200  8.748   1.00 20.87 ?  71  THR   B HG21 1 
ATOM   3825 H HG22 . THR   B 1 71  ? 46.380 -3.125  9.289   1.00 20.87 ?  71  THR   B HG22 1 
ATOM   3826 H HG23 . THR   B 1 71  ? 47.132 -2.142  10.271  1.00 20.87 ?  71  THR   B HG23 1 
ATOM   3827 N N    . ASN   B 1 72  ? 46.190 -5.974  11.032  1.00 14.31 ?  72  ASN   B N    1 
ATOM   3828 C CA   . ASN   B 1 72  ? 44.785 -6.331  10.903  1.00 14.66 ?  72  ASN   B CA   1 
ATOM   3829 C C    . ASN   B 1 72  ? 44.312 -7.434  11.837  1.00 15.07 ?  72  ASN   B C    1 
ATOM   3830 O O    . ASN   B 1 72  ? 43.097 -7.596  11.997  1.00 16.15 ?  72  ASN   B O    1 
ATOM   3831 C CB   . ASN   B 1 72  ? 44.477 -6.754  9.459   1.00 15.52 ?  72  ASN   B CB   1 
ATOM   3832 C CG   . ASN   B 1 72  ? 44.750 -5.650  8.470   1.00 16.48 ?  72  ASN   B CG   1 
ATOM   3833 O OD1  . ASN   B 1 72  ? 45.769 -5.650  7.777   1.00 17.90 ?  72  ASN   B OD1  1 
ATOM   3834 N ND2  . ASN   B 1 72  ? 43.858 -4.678  8.424   1.00 18.12 ?  72  ASN   B ND2  1 
ATOM   3835 H H    . ASN   B 1 72  ? 46.733 -6.613  10.821  1.00 17.17 ?  72  ASN   B H    1 
ATOM   3836 H HA   . ASN   B 1 72  ? 44.255 -5.543  11.089  1.00 17.59 ?  72  ASN   B HA   1 
ATOM   3837 H HB2  . ASN   B 1 72  ? 45.036 -7.514  9.223   1.00 18.62 ?  72  ASN   B HB2  1 
ATOM   3838 H HB3  . ASN   B 1 72  ? 43.542 -6.996  9.392   1.00 18.62 ?  72  ASN   B HB3  1 
ATOM   3839 H HD21 . ASN   B 1 72  ? 43.962 -4.022  7.877   1.00 21.74 ?  72  ASN   B HD21 1 
ATOM   3840 H HD22 . ASN   B 1 72  ? 43.159 -4.710  8.926   1.00 21.74 ?  72  ASN   B HD22 1 
ATOM   3841 N N    . GLY   B 1 73  ? 45.212 -8.190  12.453  1.00 14.58 ?  73  GLY   B N    1 
ATOM   3842 C CA   . GLY   B 1 73  ? 44.816 -9.328  13.244  1.00 14.11 ?  73  GLY   B CA   1 
ATOM   3843 C C    . GLY   B 1 73  ? 44.455 -10.512 12.373  1.00 12.90 ?  73  GLY   B C    1 
ATOM   3844 O O    . GLY   B 1 73  ? 44.436 -10.428 11.142  1.00 12.90 ?  73  GLY   B O    1 
ATOM   3845 H H    . GLY   B 1 73  ? 46.063 -8.060  12.423  1.00 17.50 ?  73  GLY   B H    1 
ATOM   3846 H HA2  . GLY   B 1 73  ? 45.543 -9.584  13.832  1.00 16.94 ?  73  GLY   B HA2  1 
ATOM   3847 H HA3  . GLY   B 1 73  ? 44.046 -9.094  13.789  1.00 16.94 ?  73  GLY   B HA3  1 
ATOM   3848 N N    . PRO   B 1 74  ? 44.150 -11.638 13.006  1.00 13.04 ?  74  PRO   B N    1 
ATOM   3849 C CA   . PRO   B 1 74  ? 43.905 -12.868 12.252  1.00 12.77 ?  74  PRO   B CA   1 
ATOM   3850 C C    . PRO   B 1 74  ? 42.601 -12.814 11.467  1.00 12.27 ?  74  PRO   B C    1 
ATOM   3851 O O    . PRO   B 1 74  ? 41.658 -12.081 11.790  1.00 13.36 ?  74  PRO   B O    1 
ATOM   3852 C CB   . PRO   B 1 74  ? 43.841 -13.941 13.345  1.00 13.85 ?  74  PRO   B CB   1 
ATOM   3853 C CG   . PRO   B 1 74  ? 43.386 -13.205 14.557  1.00 15.34 ?  74  PRO   B CG   1 
ATOM   3854 C CD   . PRO   B 1 74  ? 44.031 -11.849 14.458  1.00 14.68 ?  74  PRO   B CD   1 
ATOM   3855 H HA   . PRO   B 1 74  ? 44.648 -13.052 11.650  1.00 15.32 ?  74  PRO   B HA   1 
ATOM   3856 H HB2  . PRO   B 1 74  ? 43.202 -14.626 13.092  1.00 16.62 ?  74  PRO   B HB2  1 
ATOM   3857 H HB3  . PRO   B 1 74  ? 44.722 -14.324 13.481  1.00 16.62 ?  74  PRO   B HB3  1 
ATOM   3858 H HG2  . PRO   B 1 74  ? 42.419 -13.129 14.546  1.00 18.41 ?  74  PRO   B HG2  1 
ATOM   3859 H HG3  . PRO   B 1 74  ? 43.686 -13.672 15.351  1.00 18.41 ?  74  PRO   B HG3  1 
ATOM   3860 H HD2  . PRO   B 1 74  ? 43.456 -11.173 14.856  1.00 17.62 ?  74  PRO   B HD2  1 
ATOM   3861 H HD3  . PRO   B 1 74  ? 44.907 -11.857 14.871  1.00 17.62 ?  74  PRO   B HD3  1 
ATOM   3862 N N    . LEU   B 1 75  ? 42.569 -13.625 10.413  1.00 11.36 ?  75  LEU   B N    1 
ATOM   3863 C CA   . LEU   B 1 75  ? 41.353 -13.843 9.651   1.00 11.54 ?  75  LEU   B CA   1 
ATOM   3864 C C    . LEU   B 1 75  ? 40.384 -14.708 10.455  1.00 12.01 ?  75  LEU   B C    1 
ATOM   3865 O O    . LEU   B 1 75  ? 40.727 -15.265 11.500  1.00 13.15 ?  75  LEU   B O    1 
ATOM   3866 C CB   . LEU   B 1 75  ? 41.676 -14.551 8.334   1.00 11.73 ?  75  LEU   B CB   1 
ATOM   3867 C CG   . LEU   B 1 75  ? 42.542 -13.807 7.311   1.00 13.67 ?  75  LEU   B CG   1 
ATOM   3868 C CD1  . LEU   B 1 75  ? 42.727 -14.646 6.048   1.00 15.04 ?  75  LEU   B CD1  1 
ATOM   3869 C CD2  . LEU   B 1 75  ? 41.982 -12.449 6.962   1.00 16.76 ?  75  LEU   B CD2  1 
ATOM   3870 H H    . LEU   B 1 75  ? 43.246 -14.067 10.115  1.00 13.64 ?  75  LEU   B H    1 
ATOM   3871 H HA   . LEU   B 1 75  ? 40.926 -12.995 9.456   1.00 13.85 ?  75  LEU   B HA   1 
ATOM   3872 H HB2  . LEU   B 1 75  ? 42.137 -15.378 8.542   1.00 14.08 ?  75  LEU   B HB2  1 
ATOM   3873 H HB3  . LEU   B 1 75  ? 40.838 -14.760 7.890   1.00 14.08 ?  75  LEU   B HB3  1 
ATOM   3874 H HG   . LEU   B 1 75  ? 43.422 -13.672 7.693   1.00 16.40 ?  75  LEU   B HG   1 
ATOM   3875 H HD11 . LEU   B 1 75  ? 43.281 -14.155 5.417   1.00 18.05 ?  75  LEU   B HD11 1 
ATOM   3876 H HD12 . LEU   B 1 75  ? 43.161 -15.483 6.281   1.00 18.05 ?  75  LEU   B HD12 1 
ATOM   3877 H HD13 . LEU   B 1 75  ? 41.860 -14.824 5.652   1.00 18.05 ?  75  LEU   B HD13 1 
ATOM   3878 H HD21 . LEU   B 1 75  ? 42.528 -12.051 6.268   1.00 20.11 ?  75  LEU   B HD21 1 
ATOM   3879 H HD22 . LEU   B 1 75  ? 41.071 -12.556 6.649   1.00 20.11 ?  75  LEU   B HD22 1 
ATOM   3880 H HD23 . LEU   B 1 75  ? 41.997 -11.892 7.756   1.00 20.11 ?  75  LEU   B HD23 1 
ATOM   3881 N N    . LYS   B 1 76  ? 39.155 -14.811 9.948   1.00 13.04 ?  76  LYS   B N    1 
ATOM   3882 C CA   . LYS   B 1 76  ? 38.174 -15.778 10.424  1.00 14.30 ?  76  LYS   B CA   1 
ATOM   3883 C C    . LYS   B 1 76  ? 38.258 -17.042 9.573   1.00 12.67 ?  76  LYS   B C    1 
ATOM   3884 O O    . LYS   B 1 76  ? 38.526 -16.976 8.374   1.00 12.41 ?  76  LYS   B O    1 
ATOM   3885 C CB   . LYS   B 1 76  ? 36.753 -15.212 10.267  1.00 17.27 ?  76  LYS   B CB   1 
ATOM   3886 C CG   . LYS   B 1 76  ? 36.505 -13.811 10.846  1.00 19.77 ?  76  LYS   B CG   1 
ATOM   3887 C CD   . LYS   B 1 76  ? 35.100 -13.286 10.506  1.00 21.32 ?  76  LYS   B CD   1 
ATOM   3888 C CE   . LYS   B 1 76  ? 34.838 -11.923 11.129  1.00 23.24 ?  76  LYS   B CE   1 
ATOM   3889 N NZ   . LYS   B 1 76  ? 33.521 -11.362 10.720  1.00 23.91 ?  76  LYS   B NZ   1 
ATOM   3890 H H    . LYS   B 1 76  ? 38.862 -14.319 9.311   1.00 15.65 ?  76  LYS   B H    1 
ATOM   3891 H HA   . LYS   B 1 76  ? 38.332 -16.003 11.356  1.00 17.16 ?  76  LYS   B HA   1 
ATOM   3892 H HB2  . LYS   B 1 76  ? 36.544 -15.172 9.320   1.00 20.73 ?  76  LYS   B HB2  1 
ATOM   3893 H HB3  . LYS   B 1 76  ? 36.132 -15.816 10.706  1.00 20.73 ?  76  LYS   B HB3  1 
ATOM   3894 H HG2  . LYS   B 1 76  ? 36.590 -13.845 11.811  1.00 23.72 ?  76  LYS   B HG2  1 
ATOM   3895 H HG3  . LYS   B 1 76  ? 37.155 -13.193 10.474  1.00 23.72 ?  76  LYS   B HG3  1 
ATOM   3896 H HD2  . LYS   B 1 76  ? 35.015 -13.198 9.543   1.00 25.58 ?  76  LYS   B HD2  1 
ATOM   3897 H HD3  . LYS   B 1 76  ? 34.436 -13.906 10.844  1.00 25.58 ?  76  LYS   B HD3  1 
ATOM   3898 H HE2  . LYS   B 1 76  ? 34.842 -12.010 12.096  1.00 27.90 ?  76  LYS   B HE2  1 
ATOM   3899 H HE3  . LYS   B 1 76  ? 35.531 -11.305 10.848  1.00 27.90 ?  76  LYS   B HE3  1 
ATOM   3900 H HZ1  . LYS   B 1 76  ? 33.397 -10.566 11.101  1.00 28.69 ?  76  LYS   B HZ1  1 
ATOM   3901 H HZ2  . LYS   B 1 76  ? 33.492 -11.265 9.836   1.00 28.69 ?  76  LYS   B HZ2  1 
ATOM   3902 H HZ3  . LYS   B 1 76  ? 32.865 -11.908 10.973  1.00 28.69 ?  76  LYS   B HZ3  1 
ATOM   3903 N N    . VAL   B 1 77  ? 38.014 -18.201 10.194  1.00 13.15 ?  77  VAL   B N    1 
ATOM   3904 C CA   . VAL   B 1 77  ? 37.801 -19.408 9.400   1.00 13.29 ?  77  VAL   B CA   1 
ATOM   3905 C C    . VAL   B 1 77  ? 36.609 -19.169 8.485   1.00 12.03 ?  77  VAL   B C    1 
ATOM   3906 O O    . VAL   B 1 77  ? 35.545 -18.717 8.931   1.00 12.26 ?  77  VAL   B O    1 
ATOM   3907 C CB   . VAL   B 1 77  ? 37.605 -20.636 10.300  1.00 14.54 ?  77  VAL   B CB   1 
ATOM   3908 C CG1  . VAL   B 1 77  ? 37.326 -21.866 9.445   1.00 15.22 ?  77  VAL   B CG1  1 
ATOM   3909 C CG2  . VAL   B 1 77  ? 38.835 -20.861 11.175  1.00 15.99 ?  77  VAL   B CG2  1 
ATOM   3910 H H    . VAL   B 1 77  ? 37.974 -18.311 11.042  1.00 15.78 ?  77  VAL   B H    1 
ATOM   3911 H HA   . VAL   B 1 77  ? 38.576 -19.564 8.841   1.00 15.96 ?  77  VAL   B HA   1 
ATOM   3912 H HB   . VAL   B 1 77  ? 36.839 -20.487 10.882  1.00 17.46 ?  77  VAL   B HB   1 
ATOM   3913 H HG11 . VAL   B 1 77  ? 37.379 -22.657 10.006  1.00 18.26 ?  77  VAL   B HG11 1 
ATOM   3914 H HG12 . VAL   B 1 77  ? 36.433 -21.797 9.066   1.00 18.26 ?  77  VAL   B HG12 1 
ATOM   3915 H HG13 . VAL   B 1 77  ? 37.983 -21.916 8.738   1.00 18.26 ?  77  VAL   B HG13 1 
ATOM   3916 H HG21 . VAL   B 1 77  ? 38.702 -21.667 11.697  1.00 19.19 ?  77  VAL   B HG21 1 
ATOM   3917 H HG22 . VAL   B 1 77  ? 39.609 -20.956 10.603  1.00 19.19 ?  77  VAL   B HG22 1 
ATOM   3918 H HG23 . VAL   B 1 77  ? 38.945 -20.098 11.764  1.00 19.19 ?  77  VAL   B HG23 1 
ATOM   3919 N N    . GLY   B 1 78  ? 36.792 -19.441 7.195   1.00 11.48 ?  78  GLY   B N    1 
ATOM   3920 C CA   . GLY   B 1 78  ? 35.815 -19.116 6.179   1.00 11.07 ?  78  GLY   B CA   1 
ATOM   3921 C C    . GLY   B 1 78  ? 36.061 -17.796 5.486   1.00 10.86 ?  78  GLY   B C    1 
ATOM   3922 O O    . GLY   B 1 78  ? 35.388 -17.503 4.492   1.00 11.30 ?  78  GLY   B O    1 
ATOM   3923 H H    . GLY   B 1 78  ? 37.494 -19.827 6.881   1.00 13.78 ?  78  GLY   B H    1 
ATOM   3924 H HA2  . GLY   B 1 78  ? 35.810 -19.811 5.506   1.00 13.29 ?  78  GLY   B HA2  1 
ATOM   3925 H HA3  . GLY   B 1 78  ? 34.934 -19.078 6.584   1.00 13.29 ?  78  GLY   B HA3  1 
ATOM   3926 N N    . GLY   B 1 79  ? 37.007 -16.995 5.981   1.00 11.09 ?  79  GLY   B N    1 
ATOM   3927 C CA   . GLY   B 1 79  ? 37.310 -15.699 5.414   1.00 10.86 ?  79  GLY   B CA   1 
ATOM   3928 C C    . GLY   B 1 79  ? 38.546 -15.714 4.524   1.00 10.46 ?  79  GLY   B C    1 
ATOM   3929 O O    . GLY   B 1 79  ? 39.159 -16.749 4.262   1.00 10.82 ?  79  GLY   B O    1 
ATOM   3930 H H    . GLY   B 1 79  ? 37.500 -17.194 6.653   1.00 13.31 ?  79  GLY   B H    1 
ATOM   3931 H HA2  . GLY   B 1 79  ? 36.560 -15.391 4.881   1.00 13.04 ?  79  GLY   B HA2  1 
ATOM   3932 H HA3  . GLY   B 1 79  ? 37.458 -15.061 6.130   1.00 13.04 ?  79  GLY   B HA3  1 
ATOM   3933 N N    . SER   B 1 80  ? 38.911 -14.514 4.060   1.00 10.50 ?  80  SER   B N    1 
ATOM   3934 C CA   . SER   B 1 80  ? 40.012 -14.376 3.118   1.00 10.56 ?  80  SER   B CA   1 
ATOM   3935 C C    . SER   B 1 80  ? 40.587 -12.969 3.181   1.00 10.54 ?  80  SER   B C    1 
ATOM   3936 O O    . SER   B 1 80  ? 39.970 -12.041 3.706   1.00 11.73 ?  80  SER   B O    1 
ATOM   3937 C CB   . SER   B 1 80  ? 39.565 -14.663 1.681   1.00 11.01 ?  80  SER   B CB   1 
ATOM   3938 O OG   . SER   B 1 80  ? 38.722 -13.636 1.183   1.00 12.27 ?  80  SER   B OG   1 
ATOM   3939 H H    . SER   B 1 80  ? 38.539 -13.771 4.277   1.00 12.61 ?  80  SER   B H    1 
ATOM   3940 H HA   . SER   B 1 80  ? 40.708 -15.004 3.357   1.00 12.67 ?  80  SER   B HA   1 
ATOM   3941 H HB2  . SER   B 1 80  ? 40.344 -14.726 1.110   1.00 13.22 ?  80  SER   B HB2  1 
ATOM   3942 H HB3  . SER   B 1 80  ? 39.075 -15.501 1.665   1.00 13.22 ?  80  SER   B HB3  1 
ATOM   3943 H HG   . SER   B 1 80  ? 38.033 -13.571 1.666   1.00 14.73 ?  80  SER   B HG   1 
ATOM   3944 N N    . CYS   B 1 81  ? 41.772 -12.820 2.595   1.00 10.10 ?  81  CYS   B N    1 
ATOM   3945 C CA   . CYS   B 1 81  ? 42.316 -11.506 2.289   1.00 10.31 ?  81  CYS   B CA   1 
ATOM   3946 C C    . CYS   B 1 81  ? 43.091 -11.585 0.983   1.00 9.59  ?  81  CYS   B C    1 
ATOM   3947 O O    . CYS   B 1 81  ? 43.608 -12.644 0.609   1.00 10.80 ?  81  CYS   B O    1 
ATOM   3948 C CB   . CYS   B 1 81  ? 43.209 -10.958 3.414   1.00 11.19 ?  81  CYS   B CB   1 
ATOM   3949 S SG   . CYS   B 1 81  ? 44.730 -11.888 3.657   1.00 11.48 ?  81  CYS   B SG   1 
ATOM   3950 H H    . CYS   B 1 81  ? 42.284 -13.471 2.354   1.00 12.13 ?  81  CYS   B H    1 
ATOM   3951 H HA   . CYS   B 1 81  ? 41.583 -10.882 2.162   1.00 12.37 ?  81  CYS   B HA   1 
ATOM   3952 H HB2  . CYS   B 1 81  ? 43.453 -10.043 3.205   1.00 13.43 ?  81  CYS   B HB2  1 
ATOM   3953 H HB3  . CYS   B 1 81  ? 42.707 -10.979 4.247   1.00 13.43 ?  81  CYS   B HB3  1 
ATOM   3954 H HG   . CYS   B 1 81  ? 45.354 -11.397 4.557   1.00 13.78 ?  81  CYS   B HG   1 
ATOM   3955 N N    . VAL   B 1 82  ? 43.187 -10.442 0.307   1.00 10.01 ?  82  VAL   B N    1 
ATOM   3956 C CA   . VAL   B 1 82  ? 43.954 -10.312 -0.929  1.00 10.21 ?  82  VAL   B CA   1 
ATOM   3957 C C    . VAL   B 1 82  ? 45.293 -9.670  -0.609  1.00 10.50 ?  82  VAL   B C    1 
ATOM   3958 O O    . VAL   B 1 82  ? 45.344 -8.554  -0.074  1.00 11.66 ?  82  VAL   B O    1 
ATOM   3959 C CB   . VAL   B 1 82  ? 43.205 -9.475  -1.977  1.00 11.59 ?  82  VAL   B CB   1 
ATOM   3960 C CG1  . VAL   B 1 82  ? 44.055 -9.315  -3.231  1.00 12.90 ?  82  VAL   B CG1  1 
ATOM   3961 C CG2  . VAL   B 1 82  ? 41.855 -10.095 -2.304  1.00 12.56 ?  82  VAL   B CG2  1 
ATOM   3962 H H    . VAL   B 1 82  ? 42.799 -9.706  0.545   1.00 12.02 ?  82  VAL   B H    1 
ATOM   3963 H HA   . VAL   B 1 82  ? 44.112 -11.189 -1.304  1.00 12.25 ?  82  VAL   B HA   1 
ATOM   3964 H HB   . VAL   B 1 82  ? 43.039 -8.589  -1.619  1.00 13.91 ?  82  VAL   B HB   1 
ATOM   3965 H HG11 . VAL   B 1 82  ? 43.492 -9.010  -3.961  1.00 15.49 ?  82  VAL   B HG11 1 
ATOM   3966 H HG12 . VAL   B 1 82  ? 44.752 -8.660  -3.062  1.00 15.49 ?  82  VAL   B HG12 1 
ATOM   3967 H HG13 . VAL   B 1 82  ? 44.451 -10.170 -3.457  1.00 15.49 ?  82  VAL   B HG13 1 
ATOM   3968 H HG21 . VAL   B 1 82  ? 41.417 -9.569  -2.995  1.00 15.07 ?  82  VAL   B HG21 1 
ATOM   3969 H HG22 . VAL   B 1 82  ? 41.990 -11.004 -2.622  1.00 15.07 ?  82  VAL   B HG22 1 
ATOM   3970 H HG23 . VAL   B 1 82  ? 41.306 -10.106 -1.504  1.00 15.07 ?  82  VAL   B HG23 1 
ATOM   3971 N N    . LEU   B 1 83  ? 46.375 -10.350 -0.977  1.00 10.10 ?  83  LEU   B N    1 
ATOM   3972 C CA   . LEU   B 1 83  ? 47.725 -9.828  -0.852  1.00 10.06 ?  83  LEU   B CA   1 
ATOM   3973 C C    . LEU   B 1 83  ? 48.430 -9.965  -2.199  1.00 10.09 ?  83  LEU   B C    1 
ATOM   3974 O O    . LEU   B 1 83  ? 47.833 -10.381 -3.196  1.00 10.20 ?  83  LEU   B O    1 
ATOM   3975 C CB   . LEU   B 1 83  ? 48.475 -10.505 0.301   1.00 10.84 ?  83  LEU   B CB   1 
ATOM   3976 C CG   . LEU   B 1 83  ? 47.960 -10.150 1.700   1.00 12.15 ?  83  LEU   B CG   1 
ATOM   3977 C CD1  . LEU   B 1 83  ? 48.594 -11.014 2.776   1.00 12.67 ?  83  LEU   B CD1  1 
ATOM   3978 C CD2  . LEU   B 1 83  ? 48.176 -8.669  2.019   1.00 12.96 ?  83  LEU   B CD2  1 
ATOM   3979 H H    . LEU   B 1 83  ? 46.343 -11.143 -1.313  1.00 12.12 ?  83  LEU   B H    1 
ATOM   3980 H HA   . LEU   B 1 83  ? 47.671 -8.883  -0.655  1.00 12.07 ?  83  LEU   B HA   1 
ATOM   3981 H HB2  . LEU   B 1 83  ? 48.407 -11.463 0.200   1.00 13.01 ?  83  LEU   B HB2  1 
ATOM   3982 H HB3  . LEU   B 1 83  ? 49.408 -10.237 0.260   1.00 13.01 ?  83  LEU   B HB3  1 
ATOM   3983 H HG   . LEU   B 1 83  ? 47.006 -10.312 1.722   1.00 14.59 ?  83  LEU   B HG   1 
ATOM   3984 H HD11 . LEU   B 1 83  ? 48.230 -10.761 3.641   1.00 15.21 ?  83  LEU   B HD11 1 
ATOM   3985 H HD12 . LEU   B 1 83  ? 48.386 -11.946 2.594   1.00 15.21 ?  83  LEU   B HD12 1 
ATOM   3986 H HD13 . LEU   B 1 83  ? 49.553 -10.882 2.769   1.00 15.21 ?  83  LEU   B HD13 1 
ATOM   3987 H HD21 . LEU   B 1 83  ? 47.979 -8.515  2.956   1.00 15.55 ?  83  LEU   B HD21 1 
ATOM   3988 H HD22 . LEU   B 1 83  ? 49.098 -8.436  1.831   1.00 15.55 ?  83  LEU   B HD22 1 
ATOM   3989 H HD23 . LEU   B 1 83  ? 47.582 -8.137  1.465   1.00 15.55 ?  83  LEU   B HD23 1 
ATOM   3990 N N    . SER   B 1 84  ? 49.706 -9.593  -2.245  1.00 11.08 ?  84  SER   B N    1 
ATOM   3991 C CA   . SER   B 1 84  ? 50.443 -9.697  -3.496  1.00 11.50 ?  84  SER   B CA   1 
ATOM   3992 C C    . SER   B 1 84  ? 50.598 -11.153 -3.922  1.00 10.97 ?  84  SER   B C    1 
ATOM   3993 O O    . SER   B 1 84  ? 50.709 -12.060 -3.096  1.00 10.87 ?  84  SER   B O    1 
ATOM   3994 C CB   . SER   B 1 84  ? 51.835 -9.090  -3.343  1.00 13.42 ?  84  SER   B CB   1 
ATOM   3995 O OG   . SER   B 1 84  ? 52.590 -9.304  -4.519  1.00 15.21 ?  84  SER   B OG   1 
ATOM   3996 H H    . SER   B 1 84  ? 50.157 -9.277  -1.582  1.00 13.30 ?  84  SER   B H    1 
ATOM   3997 H HA   . SER   B 1 84  ? 49.971 -9.221  -4.194  1.00 13.80 ?  84  SER   B HA   1 
ATOM   3998 H HB2  . SER   B 1 84  ? 51.748 -8.133  -3.187  1.00 16.11 ?  84  SER   B HB2  1 
ATOM   3999 H HB3  . SER   B 1 84  ? 52.289 -9.507  -2.596  1.00 16.11 ?  84  SER   B HB3  1 
ATOM   4000 H HG   . SER   B 1 84  ? 53.354 -8.960  -4.440  1.00 18.26 ?  84  SER   B HG   1 
ATOM   4001 N N    . GLY   B 1 85  ? 50.660 -11.365 -5.232  1.00 12.05 ?  85  GLY   B N    1 
ATOM   4002 C CA   . GLY   B 1 85  ? 51.007 -12.656 -5.778  1.00 12.65 ?  85  GLY   B CA   1 
ATOM   4003 C C    . GLY   B 1 85  ? 52.479 -12.858 -6.073  1.00 11.78 ?  85  GLY   B C    1 
ATOM   4004 O O    . GLY   B 1 85  ? 52.855 -13.935 -6.540  1.00 12.19 ?  85  GLY   B O    1 
ATOM   4005 H H    . GLY   B 1 85  ? 50.514 -10.764 -5.825  1.00 14.46 ?  85  GLY   B H    1 
ATOM   4006 H HA2  . GLY   B 1 85  ? 50.732 -13.345 -5.154  1.00 15.18 ?  85  GLY   B HA2  1 
ATOM   4007 H HA3  . GLY   B 1 85  ? 50.522 -12.787 -6.603  1.00 15.18 ?  85  GLY   B HA3  1 
ATOM   4008 N N    . HIS   B 1 86  ? 53.331 -11.862 -5.836  1.00 11.60 ?  86  HIS   B N    1 
ATOM   4009 C CA   . HIS   B 1 86  ? 54.792 -12.033 -5.924  1.00 11.66 ?  86  HIS   B CA   1 
ATOM   4010 C C    . HIS   B 1 86  ? 55.162 -12.539 -7.317  1.00 11.53 ?  86  HIS   B C    1 
ATOM   4011 O O    . HIS   B 1 86  ? 54.773 -11.920 -8.320  1.00 12.38 ?  86  HIS   B O    1 
ATOM   4012 C CB   . HIS   B 1 86  ? 55.275 -12.885 -4.754  1.00 11.88 ?  86  HIS   B CB   1 
ATOM   4013 C CG   . HIS   B 1 86  ? 54.961 -12.287 -3.426  1.00 12.23 ?  86  HIS   B CG   1 
ATOM   4014 N ND1  . HIS   B 1 86  ? 55.782 -11.366 -2.812  1.00 13.68 ?  86  HIS   B ND1  1 
ATOM   4015 C CD2  . HIS   B 1 86  ? 53.887 -12.438 -2.615  1.00 12.50 ?  86  HIS   B CD2  1 
ATOM   4016 C CE1  . HIS   B 1 86  ? 55.230 -10.985 -1.675  1.00 13.59 ?  86  HIS   B CE1  1 
ATOM   4017 N NE2  . HIS   B 1 86  ? 54.080 -11.618 -1.532  1.00 12.77 ?  86  HIS   B NE2  1 
ATOM   4018 H H    . HIS   B 1 86  ? 53.092 -11.066 -5.623  1.00 13.93 ?  86  HIS   B H    1 
ATOM   4019 H HA   . HIS   B 1 86  ? 55.203 -11.162 -5.825  1.00 14.00 ?  86  HIS   B HA   1 
ATOM   4020 H HB2  . HIS   B 1 86  ? 54.857 -13.757 -4.800  1.00 14.26 ?  86  HIS   B HB2  1 
ATOM   4021 H HB3  . HIS   B 1 86  ? 56.243 -12.983 -4.814  1.00 14.26 ?  86  HIS   B HB3  1 
ATOM   4022 H HD2  . HIS   B 1 86  ? 53.154 -12.991 -2.767  1.00 15.00 ?  86  HIS   B HD2  1 
ATOM   4023 H HE1  . HIS   B 1 86  ? 55.598 -10.383 -1.070  1.00 16.31 ?  86  HIS   B HE1  1 
ATOM   4024 H HE2  . HIS   B 1 86  ? 53.546 -11.542 -0.863  1.00 15.32 ?  86  HIS   B HE2  1 
ATOM   4025 N N    . ASN   B 1 87  ? 55.923 -13.625 -7.432  1.00 11.99 ?  87  ASN   B N    1 
ATOM   4026 C CA   . ASN   B 1 87  ? 56.317 -14.198 -8.711  1.00 12.64 ?  87  ASN   B CA   1 
ATOM   4027 C C    . ASN   B 1 87  ? 55.334 -15.240 -9.215  1.00 12.14 ?  87  ASN   B C    1 
ATOM   4028 O O    . ASN   B 1 87  ? 55.647 -15.950 -10.176 1.00 13.97 ?  87  ASN   B O    1 
ATOM   4029 C CB   . ASN   B 1 87  ? 57.713 -14.824 -8.602  1.00 14.27 ?  87  ASN   B CB   1 
ATOM   4030 C CG   . ASN   B 1 87  ? 57.776 -15.942 -7.571  1.00 15.22 ?  87  ASN   B CG   1 
ATOM   4031 O OD1  . ASN   B 1 87  ? 57.139 -15.874 -6.516  1.00 14.48 ?  87  ASN   B OD1  1 
ATOM   4032 N ND2  . ASN   B 1 87  ? 58.529 -16.993 -7.885  1.00 17.20 ?  87  ASN   B ND2  1 
ATOM   4033 H H    . ASN   B 1 87  ? 56.230 -14.065 -6.759  1.00 14.39 ?  87  ASN   B H    1 
ATOM   4034 H HA   . ASN   B 1 87  ? 56.359 -13.491 -9.371  1.00 15.17 ?  87  ASN   B HA   1 
ATOM   4035 H HB2  . ASN   B 1 87  ? 57.961 -15.195 -9.464  1.00 17.12 ?  87  ASN   B HB2  1 
ATOM   4036 H HB3  . ASN   B 1 87  ? 58.345 -14.137 -8.342  1.00 17.12 ?  87  ASN   B HB3  1 
ATOM   4037 H HD21 . ASN   B 1 87  ? 58.599 -17.648 -7.337  1.00 20.65 ?  87  ASN   B HD21 1 
ATOM   4038 H HD22 . ASN   B 1 87  ? 58.954 -17.008 -8.634  1.00 20.65 ?  87  ASN   B HD22 1 
ATOM   4039 N N    . LEU   B 1 88  ? 54.156 -15.338 -8.599  1.00 11.37 ?  88  LEU   B N    1 
ATOM   4040 C CA   . LEU   B 1 88  ? 53.175 -16.365 -8.930  1.00 11.68 ?  88  LEU   B CA   1 
ATOM   4041 C C    . LEU   B 1 88  ? 51.941 -15.845 -9.647  1.00 11.37 ?  88  LEU   B C    1 
ATOM   4042 O O    . LEU   B 1 88  ? 51.340 -16.588 -10.432 1.00 13.25 ?  88  LEU   B O    1 
ATOM   4043 C CB   . LEU   B 1 88  ? 52.706 -17.060 -7.648  1.00 12.50 ?  88  LEU   B CB   1 
ATOM   4044 C CG   . LEU   B 1 88  ? 53.824 -17.704 -6.838  1.00 15.08 ?  88  LEU   B CG   1 
ATOM   4045 C CD1  . LEU   B 1 88  ? 53.325 -18.045 -5.445  1.00 16.59 ?  88  LEU   B CD1  1 
ATOM   4046 C CD2  . LEU   B 1 88  ? 54.324 -18.940 -7.555  1.00 18.13 ?  88  LEU   B CD2  1 
ATOM   4047 H H    . LEU   B 1 88  ? 53.900 -14.816 -7.962  1.00 13.65 ?  88  LEU   B H    1 
ATOM   4048 H HA   . LEU   B 1 88  ? 53.590 -17.031 -9.493  1.00 14.01 ?  88  LEU   B HA   1 
ATOM   4049 H HB2  . LEU   B 1 88  ? 52.267 -16.409 -7.078  1.00 15.01 ?  88  LEU   B HB2  1 
ATOM   4050 H HB3  . LEU   B 1 88  ? 52.076 -17.761 -7.885  1.00 15.01 ?  88  LEU   B HB3  1 
ATOM   4051 H HG   . LEU   B 1 88  ? 54.563 -17.078 -6.753  1.00 18.10 ?  88  LEU   B HG   1 
ATOM   4052 H HD11 . LEU   B 1 88  ? 53.944 -18.664 -5.030  1.00 19.91 ?  88  LEU   B HD11 1 
ATOM   4053 H HD12 . LEU   B 1 88  ? 53.271 -17.229 -4.921  1.00 19.91 ?  88  LEU   B HD12 1 
ATOM   4054 H HD13 . LEU   B 1 88  ? 52.448 -18.449 -5.518  1.00 19.91 ?  88  LEU   B HD13 1 
ATOM   4055 H HD21 . LEU   B 1 88  ? 54.992 -19.374 -7.003  1.00 21.76 ?  88  LEU   B HD21 1 
ATOM   4056 H HD22 . LEU   B 1 88  ? 53.577 -19.538 -7.707  1.00 21.76 ?  88  LEU   B HD22 1 
ATOM   4057 H HD23 . LEU   B 1 88  ? 54.716 -18.676 -8.403  1.00 21.76 ?  88  LEU   B HD23 1 
ATOM   4058 N N    . ALA   B 1 89  ? 51.534 -14.610 -9.378  1.00 10.87 ?  89  ALA   B N    1 
ATOM   4059 C CA   . ALA   B 1 89  ? 50.244 -14.115 -9.830  1.00 10.30 ?  89  ALA   B CA   1 
ATOM   4060 C C    . ALA   B 1 89  ? 50.213 -12.625 -9.544  1.00 10.86 ?  89  ALA   B C    1 
ATOM   4061 O O    . ALA   B 1 89  ? 51.051 -12.107 -8.805  1.00 11.62 ?  89  ALA   B O    1 
ATOM   4062 C CB   . ALA   B 1 89  ? 49.105 -14.802 -9.079  1.00 10.64 ?  89  ALA   B CB   1 
ATOM   4063 H H    . ALA   B 1 89  ? 51.982 -14.035 -8.919  1.00 13.04 ?  89  ALA   B H    1 
ATOM   4064 H HA   . ALA   B 1 89  ? 50.138 -14.263 -10.784 1.00 12.37 ?  89  ALA   B HA   1 
ATOM   4065 H HB1  . ALA   B 1 89  ? 48.256 -14.472 -9.421  1.00 12.77 ?  89  ALA   B HB1  1 
ATOM   4066 H HB2  . ALA   B 1 89  ? 49.165 -15.761 -9.226  1.00 12.77 ?  89  ALA   B HB2  1 
ATOM   4067 H HB3  . ALA   B 1 89  ? 49.183 -14.606 -8.137  1.00 12.77 ?  89  ALA   B HB3  1 
ATOM   4068 N N    . LYS   B 1 90  ? 49.224 -11.935 -10.107 1.00 11.63 ?  90  LYS   B N    1 
ATOM   4069 C CA   . LYS   B 1 90  ? 49.032 -10.548 -9.706  1.00 11.89 ?  90  LYS   B CA   1 
ATOM   4070 C C    . LYS   B 1 90  ? 48.709 -10.473 -8.218  1.00 11.72 ?  90  LYS   B C    1 
ATOM   4071 O O    . LYS   B 1 90  ? 49.346 -9.723  -7.465  1.00 13.11 ?  90  LYS   B O    1 
ATOM   4072 C CB   . LYS   B 1 90  ? 47.952 -9.890  -10.564 1.00 13.54 ?  90  LYS   B CB   1 
ATOM   4073 C CG   . LYS   B 1 90  ? 47.639 -8.452  -10.178 1.00 14.41 ?  90  LYS   B CG   1 
ATOM   4074 C CD   . LYS   B 1 90  ? 48.834 -7.537  -10.289 1.00 16.90 ?  90  LYS   B CD   1 
ATOM   4075 C CE   . LYS   B 1 90  ? 48.397 -6.113  -10.020 1.00 18.88 ?  90  LYS   B CE   1 
ATOM   4076 N NZ   . LYS   B 1 90  ? 49.545 -5.176  -9.945  1.00 18.93 ?  90  LYS   B NZ   1 
ATOM   4077 H H    . LYS   B 1 90  ? 48.674 -12.237 -10.698 1.00 13.96 ?  90  LYS   B H    1 
ATOM   4078 H HA   . LYS   B 1 90  ? 49.859 -10.069 -9.855  1.00 14.27 ?  90  LYS   B HA   1 
ATOM   4079 H HB2  . LYS   B 1 90  ? 48.249 -9.887  -11.490 1.00 16.26 ?  90  LYS   B HB2  1 
ATOM   4080 H HB3  . LYS   B 1 90  ? 47.134 -10.404 -10.489 1.00 16.26 ?  90  LYS   B HB3  1 
ATOM   4081 H HG2  . LYS   B 1 90  ? 46.947 -8.112  -10.765 1.00 17.29 ?  90  LYS   B HG2  1 
ATOM   4082 H HG3  . LYS   B 1 90  ? 47.327 -8.431  -9.257  1.00 17.29 ?  90  LYS   B HG3  1 
ATOM   4083 H HD2  . LYS   B 1 90  ? 49.502 -7.785  -9.629  1.00 20.28 ?  90  LYS   B HD2  1 
ATOM   4084 H HD3  . LYS   B 1 90  ? 49.203 -7.588  -11.184 1.00 20.28 ?  90  LYS   B HD3  1 
ATOM   4085 H HE2  . LYS   B 1 90  ? 47.816 -5.814  -10.740 1.00 22.66 ?  90  LYS   B HE2  1 
ATOM   4086 H HE3  . LYS   B 1 90  ? 47.924 -6.073  -9.175  1.00 22.66 ?  90  LYS   B HE3  1 
ATOM   4087 H HZ1  . LYS   B 1 90  ? 49.257 -4.346  -9.789  1.00 22.72 ?  90  LYS   B HZ1  1 
ATOM   4088 H HZ2  . LYS   B 1 90  ? 50.095 -5.417  -9.288  1.00 22.72 ?  90  LYS   B HZ2  1 
ATOM   4089 H HZ3  . LYS   B 1 90  ? 49.996 -5.181  -10.714 1.00 22.72 ?  90  LYS   B HZ3  1 
ATOM   4090 N N    . HIS   B 1 91  ? 47.755 -11.294 -7.773  1.00 10.30 ?  91  HIS   B N    1 
ATOM   4091 C CA   . HIS   B 1 91  ? 47.298 -11.321 -6.396  1.00 10.24 ?  91  HIS   B CA   1 
ATOM   4092 C C    . HIS   B 1 91  ? 47.298 -12.750 -5.882  1.00 9.42  ?  91  HIS   B C    1 
ATOM   4093 O O    . HIS   B 1 91  ? 47.065 -13.702 -6.635  1.00 10.20 ?  91  HIS   B O    1 
ATOM   4094 C CB   . HIS   B 1 91  ? 45.847 -10.843 -6.274  1.00 11.78 ?  91  HIS   B CB   1 
ATOM   4095 C CG   . HIS   B 1 91  ? 45.629 -9.439  -6.721  1.00 15.43 ?  91  HIS   B CG   1 
ATOM   4096 N ND1  . HIS   B 1 91  ? 46.216 -8.359  -6.099  1.00 18.03 ?  91  HIS   B ND1  1 
ATOM   4097 C CD2  . HIS   B 1 91  ? 44.862 -8.933  -7.713  1.00 17.91 ?  91  HIS   B CD2  1 
ATOM   4098 C CE1  . HIS   B 1 91  ? 45.833 -7.246  -6.699  1.00 18.86 ?  91  HIS   B CE1  1 
ATOM   4099 N NE2  . HIS   B 1 91  ? 45.006 -7.567  -7.679  1.00 19.07 ?  91  HIS   B NE2  1 
ATOM   4100 H H    . HIS   B 1 91  ? 47.344 -11.859 -8.275  1.00 12.36 ?  91  HIS   B H    1 
ATOM   4101 H HA   . HIS   B 1 91  ? 47.874 -10.768 -5.836  1.00 12.29 ?  91  HIS   B HA   1 
ATOM   4102 H HB2  . HIS   B 1 91  ? 45.285 -11.415 -6.814  1.00 14.14 ?  91  HIS   B HB2  1 
ATOM   4103 H HB3  . HIS   B 1 91  ? 45.579 -10.901 -5.342  1.00 14.14 ?  91  HIS   B HB3  1 
ATOM   4104 H HD1  . HIS   B 1 91  ? 46.753 -8.400  -5.425  1.00 21.64 ?  91  HIS   B HD1  1 
ATOM   4105 H HD2  . HIS   B 1 91  ? 44.341 -9.413  -8.311  1.00 21.49 ?  91  HIS   B HD2  1 
ATOM   4106 H HE1  . HIS   B 1 91  ? 46.097 -6.382  -6.465  1.00 22.63 ?  91  HIS   B HE1  1 
ATOM   4107 N N    . CYS   B 1 92  ? 47.494 -12.885 -4.578  1.00 9.57  ?  92  CYS   B N    1 
ATOM   4108 C CA   . CYS   B 1 92  ? 47.201 -14.124 -3.869  1.00 9.30  ?  92  CYS   B CA   1 
ATOM   4109 C C    . CYS   B 1 92  ? 45.983 -13.898 -2.985  1.00 8.95  ?  92  CYS   B C    1 
ATOM   4110 O O    . CYS   B 1 92  ? 45.982 -13.003 -2.130  1.00 10.01 ?  92  CYS   B O    1 
ATOM   4111 C CB   . CYS   B 1 92  ? 48.384 -14.574 -3.015  1.00 9.90  ?  92  CYS   B CB   1 
ATOM   4112 S SG   . CYS   B 1 92  ? 48.029 -16.121 -2.125  1.00 9.93  ?  92  CYS   B SG   1 
ATOM   4113 H H    . CYS   B 1 92  ? 47.809 -12.262 -4.067  1.00 11.49 ?  92  CYS   B H    1 
ATOM   4114 H HA   . CYS   B 1 92  ? 47.002 -14.822 -4.513  1.00 11.16 ?  92  CYS   B HA   1 
ATOM   4115 H HB2  . CYS   B 1 92  ? 49.151 -14.716 -3.584  1.00 11.89 ?  92  CYS   B HB2  1 
ATOM   4116 H HB3  . CYS   B 1 92  ? 48.572 -13.887 -2.356  1.00 11.89 ?  92  CYS   B HB3  1 
ATOM   4117 H HG   . CYS   B 1 92  ? 49.005 -16.429 -1.499  1.00 11.91 ?  92  CYS   B HG   1 
ATOM   4118 N N    . LEU   B 1 93  ? 44.947 -14.704 -3.202  1.00 8.95  ?  93  LEU   B N    1 
ATOM   4119 C CA   . LEU   B 1 93  ? 43.774 -14.724 -2.337  1.00 9.13  ?  93  LEU   B CA   1 
ATOM   4120 C C    . LEU   B 1 93  ? 44.002 -15.792 -1.273  1.00 8.58  ?  93  LEU   B C    1 
ATOM   4121 O O    . LEU   B 1 93  ? 43.959 -16.993 -1.567  1.00 9.14  ?  93  LEU   B O    1 
ATOM   4122 C CB   . LEU   B 1 93  ? 42.511 -15.013 -3.146  1.00 9.43  ?  93  LEU   B CB   1 
ATOM   4123 C CG   . LEU   B 1 93  ? 41.213 -15.041 -2.339  1.00 10.40 ?  93  LEU   B CG   1 
ATOM   4124 C CD1  . LEU   B 1 93  ? 40.858 -13.650 -1.837  1.00 10.75 ?  93  LEU   B CD1  1 
ATOM   4125 C CD2  . LEU   B 1 93  ? 40.094 -15.627 -3.180  1.00 10.76 ?  93  LEU   B CD2  1 
ATOM   4126 H H    . LEU   B 1 93  ? 44.903 -15.278 -3.852  1.00 10.74 ?  93  LEU   B H    1 
ATOM   4127 H HA   . LEU   B 1 93  ? 43.681 -13.864 -1.903  1.00 10.96 ?  93  LEU   B HA   1 
ATOM   4128 H HB2  . LEU   B 1 93  ? 42.416 -14.320 -3.821  1.00 11.32 ?  93  LEU   B HB2  1 
ATOM   4129 H HB3  . LEU   B 1 93  ? 42.606 -15.874 -3.574  1.00 11.32 ?  93  LEU   B HB3  1 
ATOM   4130 H HG   . LEU   B 1 93  ? 41.336 -15.611 -1.564  1.00 12.48 ?  93  LEU   B HG   1 
ATOM   4131 H HD11 . LEU   B 1 93  ? 40.007 -13.689 -1.379  1.00 12.90 ?  93  LEU   B HD11 1 
ATOM   4132 H HD12 . LEU   B 1 93  ? 41.551 -13.347 -1.228  1.00 12.90 ?  93  LEU   B HD12 1 
ATOM   4133 H HD13 . LEU   B 1 93  ? 40.802 -13.048 -2.596  1.00 12.90 ?  93  LEU   B HD13 1 
ATOM   4134 H HD21 . LEU   B 1 93  ? 39.275 -15.631 -2.658  1.00 12.91 ?  93  LEU   B HD21 1 
ATOM   4135 H HD22 . LEU   B 1 93  ? 39.975 -15.082 -3.974  1.00 12.91 ?  93  LEU   B HD22 1 
ATOM   4136 H HD23 . LEU   B 1 93  ? 40.328 -16.533 -3.432  1.00 12.91 ?  93  LEU   B HD23 1 
ATOM   4137 N N    . HIS   B 1 94  ? 44.280 -15.358 -0.051  1.00 8.61  ?  94  HIS   B N    1 
ATOM   4138 C CA   . HIS   B 1 94  ? 44.494 -16.266 1.067   1.00 8.79  ?  94  HIS   B CA   1 
ATOM   4139 C C    . HIS   B 1 94  ? 43.131 -16.622 1.640   1.00 9.06  ?  94  HIS   B C    1 
ATOM   4140 O O    . HIS   B 1 94  ? 42.458 -15.752 2.190   1.00 10.68 ?  94  HIS   B O    1 
ATOM   4141 C CB   . HIS   B 1 94  ? 45.362 -15.592 2.127   1.00 9.49  ?  94  HIS   B CB   1 
ATOM   4142 C CG   . HIS   B 1 94  ? 46.746 -15.289 1.656   1.00 9.47  ?  94  HIS   B CG   1 
ATOM   4143 N ND1  . HIS   B 1 94  ? 47.775 -16.202 1.739   1.00 9.53  ?  94  HIS   B ND1  1 
ATOM   4144 C CD2  . HIS   B 1 94  ? 47.255 -14.181 1.064   1.00 9.83  ?  94  HIS   B CD2  1 
ATOM   4145 C CE1  . HIS   B 1 94  ? 48.866 -15.654 1.234   1.00 9.92  ?  94  HIS   B CE1  1 
ATOM   4146 N NE2  . HIS   B 1 94  ? 48.579 -14.431 0.815   1.00 10.05 ?  94  HIS   B NE2  1 
ATOM   4147 H H    . HIS   B 1 94  ? 44.349 -14.523 0.161   1.00 10.34 ?  94  HIS   B H    1 
ATOM   4148 H HA   . HIS   B 1 94  ? 44.932 -17.073 0.761   1.00 10.55 ?  94  HIS   B HA   1 
ATOM   4149 H HB2  . HIS   B 1 94  ? 44.948 -14.756 2.389   1.00 11.39 ?  94  HIS   B HB2  1 
ATOM   4150 H HB3  . HIS   B 1 94  ? 45.433 -16.181 2.895   1.00 11.39 ?  94  HIS   B HB3  1 
ATOM   4151 H HD2  . HIS   B 1 94  ? 46.797 -13.398 0.867   1.00 11.80 ?  94  HIS   B HD2  1 
ATOM   4152 H HE1  . HIS   B 1 94  ? 49.699 -16.068 1.177   1.00 11.90 ?  94  HIS   B HE1  1 
ATOM   4153 H HE2  . HIS   B 1 94  ? 49.135 -13.888 0.447   1.00 12.06 ?  94  HIS   B HE2  1 
ATOM   4154 N N    . VAL   B 1 95  ? 42.705 -17.877 1.490   1.00 9.13  ?  95  VAL   B N    1 
ATOM   4155 C CA   . VAL   B 1 95  ? 41.382 -18.321 1.925   1.00 9.20  ?  95  VAL   B CA   1 
ATOM   4156 C C    . VAL   B 1 95  ? 41.553 -19.359 3.020   1.00 9.14  ?  95  VAL   B C    1 
ATOM   4157 O O    . VAL   B 1 95  ? 42.324 -20.311 2.858   1.00 9.85  ?  95  VAL   B O    1 
ATOM   4158 C CB   . VAL   B 1 95  ? 40.565 -18.919 0.763   1.00 9.56  ?  95  VAL   B CB   1 
ATOM   4159 C CG1  . VAL   B 1 95  ? 39.185 -19.368 1.245   1.00 10.46 ?  95  VAL   B CG1  1 
ATOM   4160 C CG2  . VAL   B 1 95  ? 40.439 -17.931 -0.373  1.00 9.87  ?  95  VAL   B CG2  1 
ATOM   4161 H H    . VAL   B 1 95  ? 43.170 -18.503 1.127   1.00 10.96 ?  95  VAL   B H    1 
ATOM   4162 H HA   . VAL   B 1 95  ? 40.886 -17.571 2.291   1.00 11.04 ?  95  VAL   B HA   1 
ATOM   4163 H HB   . VAL   B 1 95  ? 41.025 -19.698 0.424   1.00 11.47 ?  95  VAL   B HB   1 
ATOM   4164 H HG11 . VAL   B 1 95  ? 38.627 -19.566 0.472   1.00 12.55 ?  95  VAL   B HG11 1 
ATOM   4165 H HG12 . VAL   B 1 95  ? 39.280 -20.166 1.789   1.00 12.55 ?  95  VAL   B HG12 1 
ATOM   4166 H HG13 . VAL   B 1 95  ? 38.780 -18.657 1.765   1.00 12.55 ?  95  VAL   B HG13 1 
ATOM   4167 H HG21 . VAL   B 1 95  ? 39.861 -18.310 -1.053  1.00 11.84 ?  95  VAL   B HG21 1 
ATOM   4168 H HG22 . VAL   B 1 95  ? 40.057 -17.109 -0.031  1.00 11.84 ?  95  VAL   B HG22 1 
ATOM   4169 H HG23 . VAL   B 1 95  ? 41.320 -17.765 -0.737  1.00 11.84 ?  95  VAL   B HG23 1 
ATOM   4170 N N    . VAL   B 1 96  ? 40.818 -19.195 4.114   1.00 9.63  ?  96  VAL   B N    1 
ATOM   4171 C CA   . VAL   B 1 96  ? 40.899 -20.111 5.250   1.00 10.13 ?  96  VAL   B CA   1 
ATOM   4172 C C    . VAL   B 1 96  ? 39.712 -21.073 5.200   1.00 10.30 ?  96  VAL   B C    1 
ATOM   4173 O O    . VAL   B 1 96  ? 38.592 -20.720 5.578   1.00 11.17 ?  96  VAL   B O    1 
ATOM   4174 C CB   . VAL   B 1 96  ? 40.945 -19.365 6.586   1.00 10.75 ?  96  VAL   B CB   1 
ATOM   4175 C CG1  . VAL   B 1 96  ? 41.116 -20.359 7.728   1.00 11.54 ?  96  VAL   B CG1  1 
ATOM   4176 C CG2  . VAL   B 1 96  ? 42.060 -18.334 6.598   1.00 11.54 ?  96  VAL   B CG2  1 
ATOM   4177 H H    . VAL   B 1 96  ? 40.257 -18.555 4.228   1.00 11.55 ?  96  VAL   B H    1 
ATOM   4178 H HA   . VAL   B 1 96  ? 41.714 -20.637 5.178   1.00 12.16 ?  96  VAL   B HA   1 
ATOM   4179 H HB   . VAL   B 1 96  ? 40.103 -18.903 6.720   1.00 12.90 ?  96  VAL   B HB   1 
ATOM   4180 H HG11 . VAL   B 1 96  ? 41.302 -19.868 8.548   1.00 13.86 ?  96  VAL   B HG11 1 
ATOM   4181 H HG12 . VAL   B 1 96  ? 40.299 -20.870 7.835   1.00 13.86 ?  96  VAL   B HG12 1 
ATOM   4182 H HG13 . VAL   B 1 96  ? 41.856 -20.951 7.527   1.00 13.86 ?  96  VAL   B HG13 1 
ATOM   4183 H HG21 . VAL   B 1 96  ? 42.109 -17.927 7.479   1.00 13.85 ?  96  VAL   B HG21 1 
ATOM   4184 H HG22 . VAL   B 1 96  ? 42.899 -18.768 6.387   1.00 13.85 ?  96  VAL   B HG22 1 
ATOM   4185 H HG23 . VAL   B 1 96  ? 41.865 -17.651 5.934   1.00 13.85 ?  96  VAL   B HG23 1 
ATOM   4186 N N    . GLY   B 1 97  ? 39.951 -22.307 4.767   1.00 10.52 ?  97  GLY   B N    1 
ATOM   4187 C CA   . GLY   B 1 97  ? 38.977 -23.361 4.926   1.00 10.94 ?  97  GLY   B CA   1 
ATOM   4188 C C    . GLY   B 1 97  ? 39.098 -23.971 6.306   1.00 11.74 ?  97  GLY   B C    1 
ATOM   4189 O O    . GLY   B 1 97  ? 40.135 -23.845 6.967   1.00 12.21 ?  97  GLY   B O    1 
ATOM   4190 H H    . GLY   B 1 97  ? 40.683 -22.554 4.377   1.00 12.63 ?  97  GLY   B H    1 
ATOM   4191 H HA2  . GLY   B 1 97  ? 38.086 -22.994 4.809   1.00 13.13 ?  97  GLY   B HA2  1 
ATOM   4192 H HA3  . GLY   B 1 97  ? 39.123 -24.048 4.255   1.00 13.13 ?  97  GLY   B HA3  1 
ATOM   4193 N N    . PRO   B 1 98  ? 38.051 -24.655 6.766   1.00 12.31 ?  98  PRO   B N    1 
ATOM   4194 C CA   . PRO   B 1 98  ? 38.142 -25.350 8.054   1.00 13.31 ?  98  PRO   B CA   1 
ATOM   4195 C C    . PRO   B 1 98  ? 39.168 -26.470 8.013   1.00 12.87 ?  98  PRO   B C    1 
ATOM   4196 O O    . PRO   B 1 98  ? 39.277 -27.204 7.030   1.00 13.04 ?  98  PRO   B O    1 
ATOM   4197 C CB   . PRO   B 1 98  ? 36.726 -25.898 8.256   1.00 13.71 ?  98  PRO   B CB   1 
ATOM   4198 C CG   . PRO   B 1 98  ? 36.172 -26.027 6.878   1.00 13.06 ?  98  PRO   B CG   1 
ATOM   4199 C CD   . PRO   B 1 98  ? 36.739 -24.851 6.126   1.00 12.45 ?  98  PRO   B CD   1 
ATOM   4200 H HA   . PRO   B 1 98  ? 38.363 -24.728 8.760   1.00 15.98 ?  98  PRO   B HA   1 
ATOM   4201 H HB2  . PRO   B 1 98  ? 36.770 -26.766 8.689   1.00 16.45 ?  98  PRO   B HB2  1 
ATOM   4202 H HB3  . PRO   B 1 98  ? 36.205 -25.274 8.778   1.00 16.45 ?  98  PRO   B HB3  1 
ATOM   4203 H HG2  . PRO   B 1 98  ? 36.468 -26.863 6.482   1.00 15.67 ?  98  PRO   B HG2  1 
ATOM   4204 H HG3  . PRO   B 1 98  ? 35.207 -25.982 6.908   1.00 15.67 ?  98  PRO   B HG3  1 
ATOM   4205 H HD2  . PRO   B 1 98  ? 36.845 -25.069 5.182   1.00 14.94 ?  98  PRO   B HD2  1 
ATOM   4206 H HD3  . PRO   B 1 98  ? 36.186 -24.065 6.247   1.00 14.94 ?  98  PRO   B HD3  1 
ATOM   4207 N N    . ASN   B 1 99  ? 39.914 -26.599 9.101   1.00 13.89 ?  99  ASN   B N    1 
ATOM   4208 C CA   . ASN   B 1 99  ? 40.892 -27.669 9.266   1.00 14.41 ?  99  ASN   B CA   1 
ATOM   4209 C C    . ASN   B 1 99  ? 40.252 -28.759 10.127  1.00 16.09 ?  99  ASN   B C    1 
ATOM   4210 O O    . ASN   B 1 99  ? 40.155 -28.625 11.349  1.00 17.05 ?  99  ASN   B O    1 
ATOM   4211 C CB   . ASN   B 1 99  ? 42.165 -27.116 9.893   1.00 14.99 ?  99  ASN   B CB   1 
ATOM   4212 C CG   . ASN   B 1 99  ? 43.297 -28.121 9.889   1.00 16.11 ?  99  ASN   B CG   1 
ATOM   4213 O OD1  . ASN   B 1 99  ? 43.075 -29.318 10.044  1.00 17.05 ?  99  ASN   B OD1  1 
ATOM   4214 N ND2  . ASN   B 1 99  ? 44.518 -27.640 9.700   1.00 16.71 ?  99  ASN   B ND2  1 
ATOM   4215 H H    . ASN   B 1 99  ? 39.870 -26.069 9.776   1.00 16.67 ?  99  ASN   B H    1 
ATOM   4216 H HA   . ASN   B 1 99  ? 41.112 -28.050 8.402   1.00 17.29 ?  99  ASN   B HA   1 
ATOM   4217 H HB2  . ASN   B 1 99  ? 42.450 -26.339 9.397   1.00 18.00 ?  99  ASN   B HB2  1 
ATOM   4218 H HB3  . ASN   B 1 99  ? 41.981 -26.874 10.817  1.00 18.00 ?  99  ASN   B HB3  1 
ATOM   4219 H HD21 . ASN   B 1 99  ? 45.193 -28.170 9.691   1.00 20.05 ?  99  ASN   B HD21 1 
ATOM   4220 H HD22 . ASN   B 1 99  ? 44.632 -26.793 9.596   1.00 20.05 ?  99  ASN   B HD22 1 
ATOM   4221 N N    A VAL   B 1 100 ? 39.801 -29.835 9.476   0.88 17.89 ?  100 VAL   B N    1 
ATOM   4222 N N    B VAL   B 1 100 ? 39.806 -29.837 9.475   0.12 18.16 ?  100 VAL   B N    1 
ATOM   4223 C CA   A VAL   B 1 100 ? 39.180 -30.943 10.199  0.88 20.55 ?  100 VAL   B CA   1 
ATOM   4224 C CA   B VAL   B 1 100 ? 39.185 -30.947 10.195  0.12 20.27 ?  100 VAL   B CA   1 
ATOM   4225 C C    A VAL   B 1 100 ? 40.176 -31.615 11.137  0.88 20.88 ?  100 VAL   B C    1 
ATOM   4226 C C    B VAL   B 1 100 ? 40.179 -31.602 11.144  0.12 21.00 ?  100 VAL   B C    1 
ATOM   4227 O O    A VAL   B 1 100 ? 39.792 -32.132 12.194  0.88 21.81 ?  100 VAL   B O    1 
ATOM   4228 O O    B VAL   B 1 100 ? 39.800 -32.084 12.219  0.12 21.23 ?  100 VAL   B O    1 
ATOM   4229 C CB   A VAL   B 1 100 ? 38.549 -31.940 9.205   0.88 23.22 ?  100 VAL   B CB   1 
ATOM   4230 C CB   B VAL   B 1 100 ? 38.575 -31.956 9.200   0.12 21.46 ?  100 VAL   B CB   1 
ATOM   4231 C CG1  A VAL   B 1 100 ? 38.071 -33.192 9.924   0.88 24.32 ?  100 VAL   B CG1  1 
ATOM   4232 C CG1  B VAL   B 1 100 ? 38.020 -33.172 9.932   0.12 21.89 ?  100 VAL   B CG1  1 
ATOM   4233 C CG2  A VAL   B 1 100 ? 37.397 -31.286 8.455   0.88 23.89 ?  100 VAL   B CG2  1 
ATOM   4234 C CG2  B VAL   B 1 100 ? 37.487 -31.289 8.375   0.12 21.87 ?  100 VAL   B CG2  1 
ATOM   4235 H H    A VAL   B 1 100 ? 39.833 -29.939 8.623   0.88 21.47 ?  100 VAL   B H    1 
ATOM   4236 H H    B VAL   B 1 100 ? 39.848 -29.945 8.623   0.12 21.80 ?  100 VAL   B H    1 
ATOM   4237 H HA   A VAL   B 1 100 ? 38.462 -30.589 10.742  0.88 24.66 ?  100 VAL   B HA   1 
ATOM   4238 H HA   B VAL   B 1 100 ? 38.458 -30.599 10.733  0.12 24.33 ?  100 VAL   B HA   1 
ATOM   4239 H HB   A VAL   B 1 100 ? 39.216 -32.206 8.556   0.88 27.86 ?  100 VAL   B HB   1 
ATOM   4240 H HB   B VAL   B 1 100 ? 39.266 -32.264 8.594   0.12 25.75 ?  100 VAL   B HB   1 
ATOM   4241 H HG11 A VAL   B 1 100 ? 37.487 -33.692 9.330   0.88 29.19 ?  100 VAL   B HG11 1 
ATOM   4242 H HG11 B VAL   B 1 100 ? 37.466 -33.682 9.318   0.12 26.28 ?  100 VAL   B HG11 1 
ATOM   4243 H HG12 A VAL   B 1 100 ? 38.838 -33.736 10.163  0.88 29.19 ?  100 VAL   B HG12 1 
ATOM   4244 H HG12 B VAL   B 1 100 ? 38.756 -33.722 10.243  0.12 26.28 ?  100 VAL   B HG12 1 
ATOM   4245 H HG13 A VAL   B 1 100 ? 37.584 -32.935 10.722  0.88 29.19 ?  100 VAL   B HG13 1 
ATOM   4246 H HG13 B VAL   B 1 100 ? 37.486 -32.872 10.684  0.12 26.28 ?  100 VAL   B HG13 1 
ATOM   4247 H HG21 A VAL   B 1 100 ? 37.022 -31.930 7.832   0.88 28.67 ?  100 VAL   B HG21 1 
ATOM   4248 H HG21 B VAL   B 1 100 ? 37.093 -31.946 7.781   0.12 26.24 ?  100 VAL   B HG21 1 
ATOM   4249 H HG22 A VAL   B 1 100 ? 36.719 -31.012 9.093   0.88 28.67 ?  100 VAL   B HG22 1 
ATOM   4250 H HG22 B VAL   B 1 100 ? 36.810 -30.935 8.974   0.12 26.24 ?  100 VAL   B HG22 1 
ATOM   4251 H HG23 A VAL   B 1 100 ? 37.731 -30.516 7.973   0.88 28.67 ?  100 VAL   B HG23 1 
ATOM   4252 H HG23 B VAL   B 1 100 ? 37.881 -30.569 7.859   0.12 26.24 ?  100 VAL   B HG23 1 
ATOM   4253 N N    . ASN   B 1 101 ? 41.460 -31.636 10.769  1.00 21.42 ?  101 ASN   B N    1 
ATOM   4254 C CA   . ASN   B 1 101 ? 42.482 -32.178 11.662  1.00 23.70 ?  101 ASN   B CA   1 
ATOM   4255 C C    . ASN   B 1 101 ? 42.641 -31.347 12.930  1.00 25.86 ?  101 ASN   B C    1 
ATOM   4256 O O    . ASN   B 1 101 ? 43.238 -31.829 13.902  1.00 26.66 ?  101 ASN   B O    1 
ATOM   4257 C CB   . ASN   B 1 101 ? 43.821 -32.305 10.929  1.00 23.85 ?  101 ASN   B CB   1 
ATOM   4258 C CG   . ASN   B 1 101 ? 43.817 -33.424 9.906   1.00 23.77 ?  101 ASN   B CG   1 
ATOM   4259 O OD1  . ASN   B 1 101 ? 43.154 -34.442 10.090  1.00 24.66 ?  101 ASN   B OD1  1 
ATOM   4260 N ND2  . ASN   B 1 101 ? 44.555 -33.238 8.818   1.00 23.68 ?  101 ASN   B ND2  1 
ATOM   4261 H H    A ASN   B 1 101 ? 41.754 -31.361 10.009  0.88 25.71 ?  101 ASN   B H    1 
ATOM   4262 H H    B ASN   B 1 101 ? 41.754 -31.359 10.010  0.12 25.71 ?  101 ASN   B H    1 
ATOM   4263 H HA   . ASN   B 1 101 ? 42.214 -33.064 11.931  1.00 28.45 ?  101 ASN   B HA   1 
ATOM   4264 H HB2  . ASN   B 1 101 ? 44.017 -31.478 10.464  1.00 28.63 ?  101 ASN   B HB2  1 
ATOM   4265 H HB3  . ASN   B 1 101 ? 44.519 -32.493 11.577  1.00 28.63 ?  101 ASN   B HB3  1 
ATOM   4266 H HD21 . ASN   B 1 101 ? 44.585 -33.846 8.210   1.00 28.42 ?  101 ASN   B HD21 1 
ATOM   4267 H HD22 . ASN   B 1 101 ? 45.002 -32.511 8.721   1.00 28.42 ?  101 ASN   B HD22 1 
ATOM   4268 N N    A LYS   B 1 102 ? 42.132 -30.114 12.937  0.88 27.12 ?  102 LYS   B N    1 
ATOM   4269 N N    B LYS   B 1 102 ? 42.121 -30.119 12.946  0.12 27.32 ?  102 LYS   B N    1 
ATOM   4270 C CA   A LYS   B 1 102 ? 42.134 -29.253 14.113  0.88 29.03 ?  102 LYS   B CA   1 
ATOM   4271 C CA   B LYS   B 1 102 ? 42.081 -29.293 14.145  0.12 28.69 ?  102 LYS   B CA   1 
ATOM   4272 C C    A LYS   B 1 102 ? 40.772 -29.197 14.794  0.88 28.67 ?  102 LYS   B C    1 
ATOM   4273 C C    B LYS   B 1 102 ? 40.709 -29.289 14.807  0.12 28.51 ?  102 LYS   B C    1 
ATOM   4274 O O    A LYS   B 1 102 ? 40.585 -28.399 15.718  0.88 29.42 ?  102 LYS   B O    1 
ATOM   4275 O O    B LYS   B 1 102 ? 40.515 -28.578 15.798  0.12 28.70 ?  102 LYS   B O    1 
ATOM   4276 C CB   A LYS   B 1 102 ? 42.560 -27.832 13.736  0.88 31.82 ?  102 LYS   B CB   1 
ATOM   4277 C CB   B LYS   B 1 102 ? 42.494 -27.853 13.818  0.12 30.19 ?  102 LYS   B CB   1 
ATOM   4278 C CG   A LYS   B 1 102 ? 44.034 -27.659 13.404  0.88 34.38 ?  102 LYS   B CG   1 
ATOM   4279 C CG   B LYS   B 1 102 ? 43.952 -27.688 13.423  0.12 31.46 ?  102 LYS   B CG   1 
ATOM   4280 C CD   A LYS   B 1 102 ? 44.323 -26.212 13.023  0.88 36.85 ?  102 LYS   B CD   1 
ATOM   4281 C CD   B LYS   B 1 102 ? 44.251 -26.245 13.047  0.12 32.59 ?  102 LYS   B CD   1 
ATOM   4282 C CE   A LYS   B 1 102 ? 45.805 -25.960 12.799  0.88 38.80 ?  102 LYS   B CE   1 
ATOM   4283 C CE   B LYS   B 1 102 ? 45.724 -26.037 12.738  0.12 33.44 ?  102 LYS   B CE   1 
ATOM   4284 N NZ   A LYS   B 1 102 ? 46.068 -24.544 12.408  0.88 39.93 ?  102 LYS   B NZ   1 
ATOM   4285 N NZ   B LYS   B 1 102 ? 46.007 -24.634 12.328  0.12 33.89 ?  102 LYS   B NZ   1 
ATOM   4286 H H    A LYS   B 1 102 ? 41.763 -29.745 12.251  0.88 32.54 ?  102 LYS   B H    1 
ATOM   4287 H H    B LYS   B 1 102 ? 41.773 -29.736 12.258  0.12 32.79 ?  102 LYS   B H    1 
ATOM   4288 H HA   A LYS   B 1 102 ? 42.785 -29.595 14.747  0.88 34.84 ?  102 LYS   B HA   1 
ATOM   4289 H HA   B LYS   B 1 102 ? 42.719 -29.641 14.785  0.12 34.43 ?  102 LYS   B HA   1 
ATOM   4290 H HB2  A LYS   B 1 102 ? 42.052 -27.554 12.959  0.88 38.19 ?  102 LYS   B HB2  1 
ATOM   4291 H HB2  B LYS   B 1 102 ? 41.954 -27.533 13.080  0.12 36.23 ?  102 LYS   B HB2  1 
ATOM   4292 H HB3  A LYS   B 1 102 ? 42.360 -27.243 14.481  0.88 38.19 ?  102 LYS   B HB3  1 
ATOM   4293 H HB3  B LYS   B 1 102 ? 42.340 -27.300 14.600  0.12 36.23 ?  102 LYS   B HB3  1 
ATOM   4294 H HG2  A LYS   B 1 102 ? 44.571 -27.885 14.180  0.88 41.26 ?  102 LYS   B HG2  1 
ATOM   4295 H HG2  B LYS   B 1 102 ? 44.519 -27.933 14.171  0.12 37.75 ?  102 LYS   B HG2  1 
ATOM   4296 H HG3  A LYS   B 1 102 ? 44.267 -28.226 12.653  0.88 41.26 ?  102 LYS   B HG3  1 
ATOM   4297 H HG3  B LYS   B 1 102 ? 44.144 -28.250 12.656  0.12 37.75 ?  102 LYS   B HG3  1 
ATOM   4298 H HD2  A LYS   B 1 102 ? 43.854 -25.999 12.201  0.88 44.23 ?  102 LYS   B HD2  1 
ATOM   4299 H HD2  B LYS   B 1 102 ? 43.740 -26.007 12.257  0.12 39.12 ?  102 LYS   B HD2  1 
ATOM   4300 H HD3  A LYS   B 1 102 ? 44.023 -25.628 13.738  0.88 44.23 ?  102 LYS   B HD3  1 
ATOM   4301 H HD3  B LYS   B 1 102 ? 44.012 -25.665 13.788  0.12 39.12 ?  102 LYS   B HD3  1 
ATOM   4302 H HE2  A LYS   B 1 102 ? 46.289 -26.143 13.620  0.88 46.56 ?  102 LYS   B HE2  1 
ATOM   4303 H HE2  B LYS   B 1 102 ? 46.247 -26.232 13.532  0.12 40.13 ?  102 LYS   B HE2  1 
ATOM   4304 H HE3  A LYS   B 1 102 ? 46.124 -26.536 12.086  0.88 46.56 ?  102 LYS   B HE3  1 
ATOM   4305 H HE3  B LYS   B 1 102 ? 45.984 -26.625 12.012  0.12 40.13 ?  102 LYS   B HE3  1 
ATOM   4306 H HZ1  A LYS   B 1 102 ? 46.940 -24.419 12.282  0.88 47.92 ?  102 LYS   B HZ1  1 
ATOM   4307 H HZ1  B LYS   B 1 102 ? 46.874 -24.538 12.153  0.12 40.68 ?  102 LYS   B HZ1  1 
ATOM   4308 H HZ2  A LYS   B 1 102 ? 45.637 -24.351 11.653  0.88 47.92 ?  102 LYS   B HZ2  1 
ATOM   4309 H HZ2  B LYS   B 1 102 ? 45.540 -24.431 11.598  0.12 40.68 ?  102 LYS   B HZ2  1 
ATOM   4310 H HZ3  A LYS   B 1 102 ? 45.787 -23.994 13.049  0.88 47.92 ?  102 LYS   B HZ3  1 
ATOM   4311 H HZ3  B LYS   B 1 102 ? 45.780 -24.074 12.981  0.12 40.68 ?  102 LYS   B HZ3  1 
ATOM   4312 N N    A GLY   B 1 103 ? 39.813 -30.004 14.346  0.88 27.82 ?  103 GLY   B N    1 
ATOM   4313 N N    B GLY   B 1 103 ? 39.757 -30.060 14.285  0.12 28.12 ?  103 GLY   B N    1 
ATOM   4314 C CA   A GLY   B 1 103 ? 38.493 -30.031 14.942  0.88 27.77 ?  103 GLY   B CA   1 
ATOM   4315 C CA   B GLY   B 1 103 ? 38.428 -30.120 14.858  0.12 27.71 ?  103 GLY   B CA   1 
ATOM   4316 C C    A GLY   B 1 103 ? 37.535 -28.977 14.433  0.88 26.83 ?  103 GLY   B C    1 
ATOM   4317 C C    B GLY   B 1 103 ? 37.497 -29.009 14.435  0.12 27.15 ?  103 GLY   B C    1 
ATOM   4318 O O    A GLY   B 1 103 ? 36.417 -28.878 14.951  0.88 27.54 ?  103 GLY   B O    1 
ATOM   4319 O O    B GLY   B 1 103 ? 36.463 -28.806 15.079  0.12 27.30 ?  103 GLY   B O    1 
ATOM   4320 H H    A GLY   B 1 103 ? 39.911 -30.548 13.692  0.88 33.38 ?  103 GLY   B H    1 
ATOM   4321 H H    B GLY   B 1 103 ? 39.864 -30.563 13.598  0.12 33.74 ?  103 GLY   B H    1 
ATOM   4322 H HA2  A GLY   B 1 103 ? 38.094 -30.898 14.771  0.88 33.33 ?  103 GLY   B HA2  1 
ATOM   4323 H HA2  B GLY   B 1 103 ? 38.021 -30.966 14.612  0.12 33.26 ?  103 GLY   B HA2  1 
ATOM   4324 H HA3  A GLY   B 1 103 ? 38.581 -29.929 15.905  0.88 33.33 ?  103 GLY   B HA3  1 
ATOM   4325 H HA3  B GLY   B 1 103 ? 38.500 -30.093 15.824  0.12 33.26 ?  103 GLY   B HA3  1 
ATOM   4326 N N    A GLU   B 1 104 ? 37.927 -28.194 13.432  0.88 25.15 ?  104 GLU   B N    1 
ATOM   4327 N N    B GLU   B 1 104 ? 37.824 -28.283 13.370  0.12 26.36 ?  104 GLU   B N    1 
ATOM   4328 C CA   A GLU   B 1 104 ? 37.084 -27.109 12.956  0.88 23.47 ?  104 GLU   B CA   1 
ATOM   4329 C CA   B GLU   B 1 104 ? 36.990 -27.176 12.927  0.12 25.60 ?  104 GLU   B CA   1 
ATOM   4330 C C    A GLU   B 1 104 ? 35.917 -27.652 12.132  0.88 24.19 ?  104 GLU   B C    1 
ATOM   4331 C C    B GLU   B 1 104 ? 35.833 -27.682 12.073  0.12 25.63 ?  104 GLU   B C    1 
ATOM   4332 O O    A GLU   B 1 104 ? 35.976 -28.742 11.553  0.88 25.28 ?  104 GLU   B O    1 
ATOM   4333 O O    B GLU   B 1 104 ? 35.931 -28.709 11.395  0.12 25.67 ?  104 GLU   B O    1 
ATOM   4334 C CB   A GLU   B 1 104 ? 37.920 -26.109 12.160  0.88 21.98 ?  104 GLU   B CB   1 
ATOM   4335 C CB   B GLU   B 1 104 ? 37.831 -26.160 12.153  0.12 24.92 ?  104 GLU   B CB   1 
ATOM   4336 C CG   A GLU   B 1 104 ? 39.025 -25.498 13.008  0.88 20.96 ?  104 GLU   B CG   1 
ATOM   4337 C CG   B GLU   B 1 104 ? 38.939 -25.544 12.996  0.12 24.39 ?  104 GLU   B CG   1 
ATOM   4338 C CD   A GLU   B 1 104 ? 39.964 -24.603 12.236  0.88 19.83 ?  104 GLU   B CD   1 
ATOM   4339 C CD   B GLU   B 1 104 ? 39.859 -24.644 12.196  0.12 24.00 ?  104 GLU   B CD   1 
ATOM   4340 O OE1  A GLU   B 1 104 ? 39.958 -24.630 10.986  0.88 17.89 ?  104 GLU   B OE1  1 
ATOM   4341 O OE1  B GLU   B 1 104 ? 39.760 -24.639 10.951  0.12 23.79 ?  104 GLU   B OE1  1 
ATOM   4342 O OE2  A GLU   B 1 104 ? 40.717 -23.864 12.900  0.88 21.02 -1 104 GLU   B OE2  1 
ATOM   4343 O OE2  B GLU   B 1 104 ? 40.684 -23.940 12.816  0.12 24.01 -1 104 GLU   B OE2  1 
ATOM   4344 H H    A GLU   B 1 104 ? 38.678 -28.268 13.021  0.88 30.19 ?  104 GLU   B H    1 
ATOM   4345 H H    B GLU   B 1 104 ? 38.526 -28.408 12.890  0.12 31.64 ?  104 GLU   B H    1 
ATOM   4346 H HA   A GLU   B 1 104 ? 36.719 -26.640 13.725  0.88 28.17 ?  104 GLU   B HA   1 
ATOM   4347 H HA   B GLU   B 1 104 ? 36.619 -26.729 13.701  0.12 30.72 ?  104 GLU   B HA   1 
ATOM   4348 H HB2  A GLU   B 1 104 ? 38.331 -26.561 11.408  0.88 26.38 ?  104 GLU   B HB2  1 
ATOM   4349 H HB2  B GLU   B 1 104 ? 38.244 -26.602 11.394  0.12 29.90 ?  104 GLU   B HB2  1 
ATOM   4350 H HB3  A GLU   B 1 104 ? 37.346 -25.391 11.848  0.88 26.38 ?  104 GLU   B HB3  1 
ATOM   4351 H HB3  B GLU   B 1 104 ? 37.256 -25.441 11.845  0.12 29.90 ?  104 GLU   B HB3  1 
ATOM   4352 H HG2  A GLU   B 1 104 ? 38.626 -24.958 13.709  0.88 25.16 ?  104 GLU   B HG2  1 
ATOM   4353 H HG2  B GLU   B 1 104 ? 38.539 -25.011 13.702  0.12 29.28 ?  104 GLU   B HG2  1 
ATOM   4354 H HG3  A GLU   B 1 104 ? 39.556 -26.207 13.402  0.88 25.16 ?  104 GLU   B HG3  1 
ATOM   4355 H HG3  B GLU   B 1 104 ? 39.473 -26.256 13.385  0.12 29.28 ?  104 GLU   B HG3  1 
ATOM   4356 N N    A ASP   B 1 105 ? 34.843 -26.867 12.089  0.88 24.22 ?  105 ASP   B N    1 
ATOM   4357 N N    B ASP   B 1 105 ? 34.726 -26.943 12.115  0.12 25.69 ?  105 ASP   B N    1 
ATOM   4358 C CA   A ASP   B 1 105 ? 33.568 -27.330 11.555  0.88 24.80 ?  105 ASP   B CA   1 
ATOM   4359 C CA   B ASP   B 1 105 ? 33.479 -27.402 11.515  0.12 25.87 ?  105 ASP   B CA   1 
ATOM   4360 C C    A ASP   B 1 105 ? 33.614 -27.364 10.031  0.88 23.29 ?  105 ASP   B C    1 
ATOM   4361 C C    B ASP   B 1 105 ? 33.597 -27.415 9.995   0.12 25.20 ?  105 ASP   B C    1 
ATOM   4362 O O    A ASP   B 1 105 ? 33.747 -26.321 9.381   0.88 22.53 ?  105 ASP   B O    1 
ATOM   4363 O O    B ASP   B 1 105 ? 33.849 -26.378 9.372   0.12 25.02 ?  105 ASP   B O    1 
ATOM   4364 C CB   A ASP   B 1 105 ? 32.445 -26.412 12.037  0.88 27.52 ?  105 ASP   B CB   1 
ATOM   4365 C CB   B ASP   B 1 105 ? 32.332 -26.495 11.956  0.12 26.63 ?  105 ASP   B CB   1 
ATOM   4366 C CG   A ASP   B 1 105 ? 31.065 -26.938 11.677  0.88 29.96 ?  105 ASP   B CG   1 
ATOM   4367 C CG   B ASP   B 1 105 ? 30.970 -27.094 11.661  0.12 27.37 ?  105 ASP   B CG   1 
ATOM   4368 O OD1  A ASP   B 1 105 ? 30.979 -27.979 10.992  0.88 30.24 ?  105 ASP   B OD1  1 
ATOM   4369 O OD1  B ASP   B 1 105 ? 30.911 -28.119 10.950  0.12 27.60 ?  105 ASP   B OD1  1 
ATOM   4370 O OD2  A ASP   B 1 105 ? 30.061 -26.316 12.090  0.88 31.39 -1 105 ASP   B OD2  1 
ATOM   4371 O OD2  B ASP   B 1 105 ? 29.959 -26.545 12.147  0.12 27.62 -1 105 ASP   B OD2  1 
ATOM   4372 H H    A ASP   B 1 105 ? 34.834 -26.052 12.362  0.88 29.07 ?  105 ASP   B H    1 
ATOM   4373 H H    B ASP   B 1 105 ? 34.672 -26.169 12.485  0.12 30.83 ?  105 ASP   B H    1 
ATOM   4374 H HA   A ASP   B 1 105 ? 33.391 -28.227 11.878  0.88 29.76 ?  105 ASP   B HA   1 
ATOM   4375 H HA   B ASP   B 1 105 ? 33.287 -28.304 11.814  0.12 31.05 ?  105 ASP   B HA   1 
ATOM   4376 H HB2  A ASP   B 1 105 ? 32.499 -26.330 13.004  0.88 33.03 ?  105 ASP   B HB2  1 
ATOM   4377 H HB2  B ASP   B 1 105 ? 32.399 -26.343 12.913  0.12 31.96 ?  105 ASP   B HB2  1 
ATOM   4378 H HB3  A ASP   B 1 105 ? 32.556 -25.538 11.628  0.88 33.03 ?  105 ASP   B HB3  1 
ATOM   4379 H HB3  B ASP   B 1 105 ? 32.394 -25.651 11.482  0.12 31.96 ?  105 ASP   B HB3  1 
ATOM   4380 N N    A ILE   B 1 106 ? 33.482 -28.566 9.463   0.88 22.90 ?  106 ILE   B N    1 
ATOM   4381 N N    B ILE   B 1 106 ? 33.409 -28.597 9.400   0.12 24.65 ?  106 ILE   B N    1 
ATOM   4382 C CA   A ILE   B 1 106 ? 33.477 -28.735 8.015   0.88 22.19 ?  106 ILE   B CA   1 
ATOM   4383 C CA   B ILE   B 1 106 ? 33.445 -28.737 7.949   0.12 24.15 ?  106 ILE   B CA   1 
ATOM   4384 C C    A ILE   B 1 106 ? 32.378 -27.909 7.351   0.88 21.20 ?  106 ILE   B C    1 
ATOM   4385 C C    B ILE   B 1 106 ? 32.351 -27.917 7.277   0.12 23.61 ?  106 ILE   B C    1 
ATOM   4386 O O    A ILE   B 1 106 ? 32.483 -27.573 6.167   0.88 20.37 ?  106 ILE   B O    1 
ATOM   4387 O O    B ILE   B 1 106 ? 32.446 -27.622 6.080   0.12 23.48 ?  106 ILE   B O    1 
ATOM   4388 C CB   A ILE   B 1 106 ? 33.380 -30.241 7.677   0.88 23.40 ?  106 ILE   B CB   1 
ATOM   4389 C CB   B ILE   B 1 106 ? 33.363 -30.234 7.571   0.12 24.29 ?  106 ILE   B CB   1 
ATOM   4390 C CG1  A ILE   B 1 106 ? 33.620 -30.486 6.187   0.88 24.07 ?  106 ILE   B CG1  1 
ATOM   4391 C CG1  B ILE   B 1 106 ? 33.637 -30.440 6.078   0.12 24.31 ?  106 ILE   B CG1  1 
ATOM   4392 C CG2  A ILE   B 1 106 ? 32.029 -30.804 8.110   0.88 24.27 ?  106 ILE   B CG2  1 
ATOM   4393 C CG2  B ILE   B 1 106 ? 32.004 -30.811 7.950   0.12 24.47 ?  106 ILE   B CG2  1 
ATOM   4394 C CD1  A ILE   B 1 106 ? 34.982 -30.035 5.716   0.88 24.26 ?  106 ILE   B CD1  1 
ATOM   4395 C CD1  B ILE   B 1 106 ? 34.994 -29.938 5.635   0.12 24.30 ?  106 ILE   B CD1  1 
ATOM   4396 H H    A ILE   B 1 106 ? 33.404 -29.298 9.903   0.88 27.48 ?  106 ILE   B H    1 
ATOM   4397 H H    B ILE   B 1 106 ? 33.271 -29.332 9.819   0.12 29.58 ?  106 ILE   B H    1 
ATOM   4398 H HA   A ILE   B 1 106 ? 34.325 -28.414 7.674   0.88 26.63 ?  106 ILE   B HA   1 
ATOM   4399 H HA   B ILE   B 1 106 ? 34.295 -28.399 7.635   0.12 28.98 ?  106 ILE   B HA   1 
ATOM   4400 H HB   A ILE   B 1 106 ? 34.071 -30.710 8.173   0.88 28.08 ?  106 ILE   B HB   1 
ATOM   4401 H HB   B ILE   B 1 106 ? 34.043 -30.711 8.069   0.12 29.15 ?  106 ILE   B HB   1 
ATOM   4402 H HG12 A ILE   B 1 106 ? 33.549 -31.440 6.011   0.88 28.89 ?  106 ILE   B HG12 1 
ATOM   4403 H HG12 B ILE   B 1 106 ? 33.597 -31.391 5.882   0.12 29.17 ?  106 ILE   B HG12 1 
ATOM   4404 H HG13 A ILE   B 1 106 ? 32.953 -30.008 5.675   0.88 28.89 ?  106 ILE   B HG13 1 
ATOM   4405 H HG13 B ILE   B 1 106 ? 32.963 -29.972 5.564   0.12 29.17 ?  106 ILE   B HG13 1 
ATOM   4406 H HG21 A ILE   B 1 106 ? 32.039 -31.768 7.999   0.88 29.12 ?  106 ILE   B HG21 1 
ATOM   4407 H HG21 B ILE   B 1 106 ? 32.023 -31.773 7.824   0.12 29.36 ?  106 ILE   B HG21 1 
ATOM   4408 H HG22 A ILE   B 1 106 ? 31.880 -30.582 9.043   0.88 29.12 ?  106 ILE   B HG22 1 
ATOM   4409 H HG22 B ILE   B 1 106 ? 31.822 -30.604 8.880   0.12 29.36 ?  106 ILE   B HG22 1 
ATOM   4410 H HG23 A ILE   B 1 106 ? 31.332 -30.415 7.561   0.88 29.12 ?  106 ILE   B HG23 1 
ATOM   4411 H HG23 B ILE   B 1 106 ? 31.322 -30.418 7.384   0.12 29.36 ?  106 ILE   B HG23 1 
ATOM   4412 H HD11 A ILE   B 1 106 ? 35.166 -30.435 4.853   0.88 29.11 ?  106 ILE   B HD11 1 
ATOM   4413 H HD11 B ILE   B 1 106 ? 35.200 -30.316 4.767   0.12 29.16 ?  106 ILE   B HD11 1 
ATOM   4414 H HD12 A ILE   B 1 106 ? 34.987 -29.068 5.640   0.88 29.11 ?  106 ILE   B HD12 1 
ATOM   4415 H HD12 B ILE   B 1 106 ? 34.969 -28.970 5.577   0.12 29.16 ?  106 ILE   B HD12 1 
ATOM   4416 H HD13 A ILE   B 1 106 ? 35.650 -30.321 6.360   0.88 29.11 ?  106 ILE   B HD13 1 
ATOM   4417 H HD13 B ILE   B 1 106 ? 35.660 -30.216 6.283   0.12 29.16 ?  106 ILE   B HD13 1 
ATOM   4418 N N    A GLN   B 1 107 ? 31.331 -27.547 8.094   0.88 22.14 ?  107 GLN   B N    1 
ATOM   4419 N N    B GLN   B 1 107 ? 31.310 -27.536 8.021   0.12 23.30 ?  107 GLN   B N    1 
ATOM   4420 C CA   A GLN   B 1 107 ? 30.254 -26.744 7.524   0.88 22.68 ?  107 GLN   B CA   1 
ATOM   4421 C CA   B GLN   B 1 107 ? 30.238 -26.724 7.457   0.12 22.94 ?  107 GLN   B CA   1 
ATOM   4422 C C    A GLN   B 1 107 ? 30.740 -25.389 7.017   0.88 20.67 ?  107 GLN   B C    1 
ATOM   4423 C C    B GLN   B 1 107 ? 30.730 -25.355 7.004   0.12 20.68 ?  107 GLN   B C    1 
ATOM   4424 O O    A GLN   B 1 107 ? 30.098 -24.804 6.139   0.88 21.59 ?  107 GLN   B O    1 
ATOM   4425 O O    B GLN   B 1 107 ? 30.078 -24.721 6.168   0.12 20.80 ?  107 GLN   B O    1 
ATOM   4426 C CB   A GLN   B 1 107 ? 29.147 -26.562 8.567   0.88 26.21 ?  107 GLN   B CB   1 
ATOM   4427 C CB   B GLN   B 1 107 ? 29.115 -26.571 8.488   0.12 24.88 ?  107 GLN   B CB   1 
ATOM   4428 C CG   A GLN   B 1 107 ? 27.818 -26.071 8.006   0.88 29.97 ?  107 GLN   B CG   1 
ATOM   4429 C CG   B GLN   B 1 107 ? 27.804 -26.028 7.931   0.12 26.65 ?  107 GLN   B CG   1 
ATOM   4430 C CD   A GLN   B 1 107 ? 27.729 -24.557 7.932   0.88 32.77 ?  107 GLN   B CD   1 
ATOM   4431 C CD   B GLN   B 1 107 ? 27.720 -24.514 7.986   0.12 28.03 ?  107 GLN   B CD   1 
ATOM   4432 O OE1  A GLN   B 1 107 ? 28.568 -23.844 8.486   0.88 33.69 ?  107 GLN   B OE1  1 
ATOM   4433 O OE1  B GLN   B 1 107 ? 28.566 -23.853 8.590   0.12 28.49 ?  107 GLN   B OE1  1 
ATOM   4434 N NE2  A GLN   B 1 107 ? 26.703 -24.059 7.248   0.88 33.68 ?  107 GLN   B NE2  1 
ATOM   4435 N NE2  B GLN   B 1 107 ? 26.692 -23.957 7.358   0.12 28.51 ?  107 GLN   B NE2  1 
ATOM   4436 H H    A GLN   B 1 107 ? 31.228 -27.748 8.919   0.88 26.57 ?  107 GLN   B H    1 
ATOM   4437 H H    B GLN   B 1 107 ? 31.200 -27.739 8.846   0.12 27.97 ?  107 GLN   B H    1 
ATOM   4438 H HA   A GLN   B 1 107 ? 29.875 -27.227 6.771   0.88 27.22 ?  107 GLN   B HA   1 
ATOM   4439 H HA   B GLN   B 1 107 ? 29.870 -27.182 6.685   0.12 27.53 ?  107 GLN   B HA   1 
ATOM   4440 H HB2  A GLN   B 1 107 ? 28.985 -27.415 8.996   0.88 31.45 ?  107 GLN   B HB2  1 
ATOM   4441 H HB2  B GLN   B 1 107 ? 28.928 -27.440 8.870   0.12 29.86 ?  107 GLN   B HB2  1 
ATOM   4442 H HB3  A GLN   B 1 107 ? 29.447 -25.918 9.228   0.88 31.45 ?  107 GLN   B HB3  1 
ATOM   4443 H HB3  B GLN   B 1 107 ? 29.413 -25.967 9.186   0.12 29.86 ?  107 GLN   B HB3  1 
ATOM   4444 H HG2  A GLN   B 1 107 ? 27.703 -26.419 7.109   0.88 35.97 ?  107 GLN   B HG2  1 
ATOM   4445 H HG2  B GLN   B 1 107 ? 27.718 -26.297 7.003   0.12 31.99 ?  107 GLN   B HG2  1 
ATOM   4446 H HG3  A GLN   B 1 107 ? 27.098 -26.389 8.577   0.88 35.97 ?  107 GLN   B HG3  1 
ATOM   4447 H HG3  B GLN   B 1 107 ? 27.066 -26.392 8.449   0.12 31.99 ?  107 GLN   B HG3  1 
ATOM   4448 H HE21 A GLN   B 1 107 ? 26.136 -24.588 6.873   0.88 40.42 ?  107 GLN   B HE21 1 
ATOM   4449 H HE21 B GLN   B 1 107 ? 26.120 -24.451 6.945   0.12 34.21 ?  107 GLN   B HE21 1 
ATOM   4450 H HE22 A GLN   B 1 107 ? 26.604 -23.207 7.180   0.88 40.42 ?  107 GLN   B HE22 1 
ATOM   4451 H HE22 B GLN   B 1 107 ? 26.598 -23.103 7.363   0.12 34.21 ?  107 GLN   B HE22 1 
ATOM   4452 N N    . LEU   B 1 108 ? 31.864 -24.885 7.530   1.00 18.37 ?  108 LEU   B N    1 
ATOM   4453 C CA   . LEU   B 1 108 ? 32.415 -23.591 7.122   1.00 16.21 ?  108 LEU   B CA   1 
ATOM   4454 C C    . LEU   B 1 108 ? 33.063 -23.617 5.746   1.00 14.11 ?  108 LEU   B C    1 
ATOM   4455 O O    . LEU   B 1 108 ? 33.494 -22.563 5.258   1.00 13.81 ?  108 LEU   B O    1 
ATOM   4456 C CB   . LEU   B 1 108 ? 33.425 -23.111 8.162   1.00 16.71 ?  108 LEU   B CB   1 
ATOM   4457 C CG   . LEU   B 1 108 ? 32.802 -22.652 9.479   1.00 18.01 ?  108 LEU   B CG   1 
ATOM   4458 C CD1  . LEU   B 1 108 ? 33.844 -22.552 10.578  1.00 18.23 ?  108 LEU   B CD1  1 
ATOM   4459 C CD2  . LEU   B 1 108 ? 32.113 -21.314 9.280   1.00 19.24 ?  108 LEU   B CD2  1 
ATOM   4460 H H    A LEU   B 1 108 ? 32.328 -25.281 8.132   0.88 22.04 ?  108 LEU   B H    1 
ATOM   4461 H H    B LEU   B 1 108 ? 32.324 -25.294 8.127   0.12 22.04 ?  108 LEU   B H    1 
ATOM   4462 H HA   . LEU   B 1 108 ? 31.692 -22.949 7.094   1.00 19.46 ?  108 LEU   B HA   1 
ATOM   4463 H HB2  . LEU   B 1 108 ? 34.034 -23.839 8.365   1.00 20.06 ?  108 LEU   B HB2  1 
ATOM   4464 H HB3  . LEU   B 1 108 ? 33.918 -22.364 7.794   1.00 20.06 ?  108 LEU   B HB3  1 
ATOM   4465 H HG   . LEU   B 1 108 ? 32.132 -23.297 9.758   1.00 21.62 ?  108 LEU   B HG   1 
ATOM   4466 H HD11 . LEU   B 1 108 ? 33.405 -22.295 11.407  1.00 21.87 ?  108 LEU   B HD11 1 
ATOM   4467 H HD12 . LEU   B 1 108 ? 34.274 -23.414 10.686  1.00 21.87 ?  108 LEU   B HD12 1 
ATOM   4468 H HD13 . LEU   B 1 108 ? 34.499 -21.881 10.332  1.00 21.87 ?  108 LEU   B HD13 1 
ATOM   4469 H HD21 . LEU   B 1 108 ? 31.827 -20.976 10.142  1.00 23.09 ?  108 LEU   B HD21 1 
ATOM   4470 H HD22 . LEU   B 1 108 ? 32.739 -20.696 8.873   1.00 23.09 ?  108 LEU   B HD22 1 
ATOM   4471 H HD23 . LEU   B 1 108 ? 31.345 -21.437 8.701   1.00 23.09 ?  108 LEU   B HD23 1 
ATOM   4472 N N    . LEU   B 1 109 ? 33.131 -24.785 5.112   1.00 13.11 ?  109 LEU   B N    1 
ATOM   4473 C CA   . LEU   B 1 109 ? 33.760 -24.887 3.804   1.00 12.26 ?  109 LEU   B CA   1 
ATOM   4474 C C    . LEU   B 1 109 ? 32.994 -24.102 2.744   1.00 11.77 ?  109 LEU   B C    1 
ATOM   4475 O O    . LEU   B 1 109 ? 33.605 -23.508 1.849   1.00 11.81 ?  109 LEU   B O    1 
ATOM   4476 C CB   . LEU   B 1 109 ? 33.885 -26.360 3.420   1.00 12.46 ?  109 LEU   B CB   1 
ATOM   4477 C CG   . LEU   B 1 109 ? 34.667 -26.696 2.153   1.00 12.39 ?  109 LEU   B CG   1 
ATOM   4478 C CD1  . LEU   B 1 109 ? 36.045 -26.050 2.174   1.00 12.65 ?  109 LEU   B CD1  1 
ATOM   4479 C CD2  . LEU   B 1 109 ? 34.782 -28.207 2.000   1.00 13.08 ?  109 LEU   B CD2  1 
ATOM   4480 H H    . LEU   B 1 109 ? 32.828 -25.529 5.415   1.00 15.74 ?  109 LEU   B H    1 
ATOM   4481 H HA   . LEU   B 1 109 ? 34.653 -24.515 3.854   1.00 14.71 ?  109 LEU   B HA   1 
ATOM   4482 H HB2  . LEU   B 1 109 ? 34.326 -26.826 4.149   1.00 14.96 ?  109 LEU   B HB2  1 
ATOM   4483 H HB3  . LEU   B 1 109 ? 32.994 -26.724 3.306   1.00 14.96 ?  109 LEU   B HB3  1 
ATOM   4484 H HG   . LEU   B 1 109 ? 34.183 -26.359 1.379   1.00 14.88 ?  109 LEU   B HG   1 
ATOM   4485 H HD11 . LEU   B 1 109 ? 36.575 -26.408 1.445   1.00 15.18 ?  109 LEU   B HD11 1 
ATOM   4486 H HD12 . LEU   B 1 109 ? 35.945 -25.092 2.070   1.00 15.18 ?  109 LEU   B HD12 1 
ATOM   4487 H HD13 . LEU   B 1 109 ? 36.472 -26.251 3.022   1.00 15.18 ?  109 LEU   B HD13 1 
ATOM   4488 H HD21 . LEU   B 1 109 ? 35.352 -28.406 1.240   1.00 15.70 ?  109 LEU   B HD21 1 
ATOM   4489 H HD22 . LEU   B 1 109 ? 35.168 -28.577 2.808   1.00 15.70 ?  109 LEU   B HD22 1 
ATOM   4490 H HD23 . LEU   B 1 109 ? 33.897 -28.580 1.854   1.00 15.70 ?  109 LEU   B HD23 1 
ATOM   4491 N N    . LYS   B 1 110 ? 31.660 -24.077 2.824   1.00 11.73 ?  110 LYS   B N    1 
ATOM   4492 C CA   . LYS   B 1 110 ? 30.898 -23.311 1.841   1.00 11.20 ?  110 LYS   B CA   1 
ATOM   4493 C C    . LYS   B 1 110 ? 31.237 -21.825 1.931   1.00 10.93 ?  110 LYS   B C    1 
ATOM   4494 O O    . LYS   B 1 110 ? 31.488 -21.174 0.912   1.00 10.93 ?  110 LYS   B O    1 
ATOM   4495 C CB   . LYS   B 1 110 ? 29.396 -23.560 1.996   1.00 11.98 ?  110 LYS   B CB   1 
ATOM   4496 C CG   . LYS   B 1 110 ? 28.590 -22.930 0.869   1.00 12.37 ?  110 LYS   B CG   1 
ATOM   4497 C CD   . LYS   B 1 110 ? 27.134 -23.372 0.887   1.00 12.77 ?  110 LYS   B CD   1 
ATOM   4498 C CE   . LYS   B 1 110 ? 26.364 -22.845 -0.325  1.00 13.52 ?  110 LYS   B CE   1 
ATOM   4499 N NZ   . LYS   B 1 110 ? 26.691 -23.567 -1.586  1.00 13.64 ?  110 LYS   B NZ   1 
ATOM   4500 H H    . LYS   B 1 110 ? 31.191 -24.491 3.412   1.00 14.08 ?  110 LYS   B H    1 
ATOM   4501 H HA   . LYS   B 1 110 ? 31.151 -23.613 0.954   1.00 13.45 ?  110 LYS   B HA   1 
ATOM   4502 H HB2  . LYS   B 1 110 ? 29.227 -24.518 1.984   1.00 14.38 ?  110 LYS   B HB2  1 
ATOM   4503 H HB3  . LYS   B 1 110 ? 29.092 -23.180 2.833   1.00 14.38 ?  110 LYS   B HB3  1 
ATOM   4504 H HG2  . LYS   B 1 110 ? 28.605 -21.964 0.962   1.00 14.85 ?  110 LYS   B HG2  1 
ATOM   4505 H HG3  . LYS   B 1 110 ? 28.966 -23.189 0.015   1.00 14.85 ?  110 LYS   B HG3  1 
ATOM   4506 H HD2  . LYS   B 1 110 ? 27.092 -24.343 0.875   1.00 15.33 ?  110 LYS   B HD2  1 
ATOM   4507 H HD3  . LYS   B 1 110 ? 26.703 -23.032 1.690   1.00 15.33 ?  110 LYS   B HD3  1 
ATOM   4508 H HE2  . LYS   B 1 110 ? 25.413 -22.945 -0.163  1.00 16.23 ?  110 LYS   B HE2  1 
ATOM   4509 H HE3  . LYS   B 1 110 ? 26.583 -21.911 -0.453  1.00 16.23 ?  110 LYS   B HE3  1 
ATOM   4510 H HZ1  . LYS   B 1 110 ? 26.223 -23.230 -2.261  1.00 16.37 ?  110 LYS   B HZ1  1 
ATOM   4511 H HZ2  . LYS   B 1 110 ? 27.559 -23.490 -1.765  1.00 16.37 ?  110 LYS   B HZ2  1 
ATOM   4512 H HZ3  . LYS   B 1 110 ? 26.491 -24.433 -1.501  1.00 16.37 ?  110 LYS   B HZ3  1 
ATOM   4513 N N    . SER   B 1 111 ? 31.266 -21.274 3.150   1.00 11.45 ?  111 SER   B N    1 
ATOM   4514 C CA   . SER   B 1 111 ? 31.655 -19.876 3.326   1.00 11.47 ?  111 SER   B CA   1 
ATOM   4515 C C    . SER   B 1 111 ? 33.034 -19.613 2.737   1.00 10.83 ?  111 SER   B C    1 
ATOM   4516 O O    . SER   B 1 111 ? 33.257 -18.580 2.092   1.00 11.12 ?  111 SER   B O    1 
ATOM   4517 C CB   . SER   B 1 111 ? 31.643 -19.515 4.811   1.00 12.68 ?  111 SER   B CB   1 
ATOM   4518 O OG   . SER   B 1 111 ? 30.332 -19.528 5.332   1.00 14.45 ?  111 SER   B OG   1 
ATOM   4519 H H    . SER   B 1 111 ? 31.069 -21.688 3.880   1.00 13.74 ?  111 SER   B H    1 
ATOM   4520 H HA   . SER   B 1 111 ? 31.020 -19.308 2.870   1.00 13.77 ?  111 SER   B HA   1 
ATOM   4521 H HB2  . SER   B 1 111 ? 32.181 -20.157 5.300   1.00 15.22 ?  111 SER   B HB2  1 
ATOM   4522 H HB3  . SER   B 1 111 ? 32.009 -18.625 4.923   1.00 15.22 ?  111 SER   B HB3  1 
ATOM   4523 H HG   . SER   B 1 111 ? 30.341 -19.331 6.155   1.00 17.34 ?  111 SER   B HG   1 
ATOM   4524 N N    . ALA   B 1 112 ? 33.974 -20.535 2.955   1.00 10.88 ?  112 ALA   B N    1 
ATOM   4525 C CA   . ALA   B 1 112 ? 35.316 -20.364 2.409   1.00 10.70 ?  112 ALA   B CA   1 
ATOM   4526 C C    . ALA   B 1 112 ? 35.278 -20.258 0.889   1.00 10.05 ?  112 ALA   B C    1 
ATOM   4527 O O    . ALA   B 1 112 ? 35.905 -19.370 0.301   1.00 10.54 ?  112 ALA   B O    1 
ATOM   4528 C CB   . ALA   B 1 112 ? 36.225 -21.507 2.869   1.00 11.49 ?  112 ALA   B CB   1 
ATOM   4529 H H    . ALA   B 1 112 ? 33.865 -21.256 3.419   1.00 13.06 ?  112 ALA   B H    1 
ATOM   4530 H HA   . ALA   B 1 112 ? 35.689 -19.537 2.754   1.00 12.85 ?  112 ALA   B HA   1 
ATOM   4531 H HB1  . ALA   B 1 112 ? 37.115 -21.365 2.504   1.00 13.79 ?  112 ALA   B HB1  1 
ATOM   4532 H HB2  . ALA   B 1 112 ? 36.267 -21.505 3.840   1.00 13.79 ?  112 ALA   B HB2  1 
ATOM   4533 H HB3  . ALA   B 1 112 ? 35.865 -22.346 2.553   1.00 13.79 ?  112 ALA   B HB3  1 
ATOM   4534 N N    . TYR   B 1 113 ? 34.544 -21.159 0.228   1.00 10.01 ?  113 TYR   B N    1 
ATOM   4535 C CA   . TYR   B 1 113 ? 34.470 -21.109 -1.227  1.00 9.63  ?  113 TYR   B CA   1 
ATOM   4536 C C    . TYR   B 1 113 ? 33.762 -19.861 -1.740  1.00 9.60  ?  113 TYR   B C    1 
ATOM   4537 O O    . TYR   B 1 113 ? 34.037 -19.425 -2.861  1.00 9.69  ?  113 TYR   B O    1 
ATOM   4538 C CB   . TYR   B 1 113 ? 33.802 -22.372 -1.775  1.00 10.23 ?  113 TYR   B CB   1 
ATOM   4539 C CG   . TYR   B 1 113 ? 34.762 -23.516 -2.036  1.00 10.61 ?  113 TYR   B CG   1 
ATOM   4540 C CD1  . TYR   B 1 113 ? 35.757 -23.409 -3.002  1.00 11.05 ?  113 TYR   B CD1  1 
ATOM   4541 C CD2  . TYR   B 1 113 ? 34.661 -24.710 -1.337  1.00 10.92 ?  113 TYR   B CD2  1 
ATOM   4542 C CE1  . TYR   B 1 113 ? 36.636 -24.446 -3.251  1.00 10.89 ?  113 TYR   B CE1  1 
ATOM   4543 C CE2  . TYR   B 1 113 ? 35.531 -25.760 -1.584  1.00 11.02 ?  113 TYR   B CE2  1 
ATOM   4544 C CZ   . TYR   B 1 113 ? 36.512 -25.625 -2.544  1.00 11.18 ?  113 TYR   B CZ   1 
ATOM   4545 O OH   . TYR   B 1 113 ? 37.391 -26.645 -2.818  1.00 11.78 ?  113 TYR   B OH   1 
ATOM   4546 H H    . TYR   B 1 113 ? 34.085 -21.790 0.596   1.00 12.02 ?  113 TYR   B H    1 
ATOM   4547 H HA   . TYR   B 1 113 ? 35.373 -21.088 -1.569  1.00 11.56 ?  113 TYR   B HA   1 
ATOM   4548 H HB2  . TYR   B 1 113 ? 33.142 -22.687 -1.135  1.00 12.28 ?  113 TYR   B HB2  1 
ATOM   4549 H HB3  . TYR   B 1 113 ? 33.365 -22.157 -2.614  1.00 12.28 ?  113 TYR   B HB3  1 
ATOM   4550 H HD1  . TYR   B 1 113 ? 35.841 -22.614 -3.484  1.00 13.26 ?  113 TYR   B HD1  1 
ATOM   4551 H HD2  . TYR   B 1 113 ? 33.995 -24.807 -0.698  1.00 13.11 ?  113 TYR   B HD2  1 
ATOM   4552 H HE1  . TYR   B 1 113 ? 37.298 -24.353 -3.907  1.00 13.07 ?  113 TYR   B HE1  1 
ATOM   4553 H HE2  . TYR   B 1 113 ? 35.445 -26.553 -1.114  1.00 13.23 ?  113 TYR   B HE2  1 
ATOM   4554 H HH   . TYR   B 1 113 ? 37.214 -27.311 -2.337  1.00 14.14 ?  113 TYR   B HH   1 
ATOM   4555 N N    . GLU   B 1 114 ? 32.841 -19.286 -0.959  1.00 9.84  ?  114 GLU   B N    1 
ATOM   4556 C CA   . GLU   B 1 114 ? 32.155 -18.077 -1.409  1.00 9.87  ?  114 GLU   B CA   1 
ATOM   4557 C C    . GLU   B 1 114 ? 33.132 -16.948 -1.700  1.00 9.70  ?  114 GLU   B C    1 
ATOM   4558 O O    . GLU   B 1 114 ? 32.853 -16.094 -2.545  1.00 9.98  ?  114 GLU   B O    1 
ATOM   4559 C CB   . GLU   B 1 114 ? 31.088 -17.658 -0.394  1.00 10.42 ?  114 GLU   B CB   1 
ATOM   4560 C CG   . GLU   B 1 114 ? 29.879 -18.577 -0.456  1.00 10.46 ?  114 GLU   B CG   1 
ATOM   4561 C CD   . GLU   B 1 114 ? 28.861 -18.391 0.657   1.00 10.63 ?  114 GLU   B CD   1 
ATOM   4562 O OE1  . GLU   B 1 114 ? 29.155 -17.776 1.704   1.00 11.07 ?  114 GLU   B OE1  1 
ATOM   4563 O OE2  . GLU   B 1 114 ? 27.739 -18.922 0.492   1.00 11.61 -1 114 GLU   B OE2  1 
ATOM   4564 H H    . GLU   B 1 114 ? 32.595 -19.577 -0.185  1.00 11.81 ?  114 GLU   B H    1 
ATOM   4565 H HA   . GLU   B 1 114 ? 31.699 -18.275 -2.234  1.00 11.84 ?  114 GLU   B HA   1 
ATOM   4566 H HB2  . GLU   B 1 114 ? 31.459 -17.703 0.505   1.00 12.51 ?  114 GLU   B HB2  1 
ATOM   4567 H HB3  . GLU   B 1 114 ? 30.792 -16.757 -0.588  1.00 12.51 ?  114 GLU   B HB3  1 
ATOM   4568 H HG2  . GLU   B 1 114 ? 29.425 -18.433 -1.297  1.00 12.55 ?  114 GLU   B HG2  1 
ATOM   4569 H HG3  . GLU   B 1 114 ? 30.194 -19.499 -0.413  1.00 12.55 ?  114 GLU   B HG3  1 
ATOM   4570 N N    . ASN   B 1 115 ? 34.295 -16.941 -1.044  1.00 9.59  ?  115 ASN   B N    1 
ATOM   4571 C CA   . ASN   B 1 115 ? 35.284 -15.908 -1.341  1.00 9.70  ?  115 ASN   B CA   1 
ATOM   4572 C C    . ASN   B 1 115 ? 35.699 -15.928 -2.805  1.00 9.37  ?  115 ASN   B C    1 
ATOM   4573 O O    . ASN   B 1 115 ? 36.086 -14.888 -3.354  1.00 10.14 ?  115 ASN   B O    1 
ATOM   4574 C CB   . ASN   B 1 115 ? 36.524 -16.090 -0.464  1.00 10.13 ?  115 ASN   B CB   1 
ATOM   4575 C CG   . ASN   B 1 115 ? 36.262 -15.826 0.997   1.00 10.75 ?  115 ASN   B CG   1 
ATOM   4576 O OD1  . ASN   B 1 115 ? 36.256 -14.680 1.439   1.00 12.76 ?  115 ASN   B OD1  1 
ATOM   4577 N ND2  . ASN   B 1 115 ? 36.097 -16.894 1.771   1.00 10.93 ?  115 ASN   B ND2  1 
ATOM   4578 H H    . ASN   B 1 115 ? 34.531 -17.500 -0.428  1.00 11.51 ?  115 ASN   B H    1 
ATOM   4579 H HA   . ASN   B 1 115 ? 34.908 -15.035 -1.145  1.00 11.64 ?  115 ASN   B HA   1 
ATOM   4580 H HB2  . ASN   B 1 115 ? 36.846 -16.999 -0.552  1.00 12.16 ?  115 ASN   B HB2  1 
ATOM   4581 H HB3  . ASN   B 1 115 ? 37.212 -15.467 -0.753  1.00 12.16 ?  115 ASN   B HB3  1 
ATOM   4582 H HD21 . ASN   B 1 115 ? 35.954 -16.796 2.615   1.00 13.12 ?  115 ASN   B HD21 1 
ATOM   4583 H HD22 . ASN   B 1 115 ? 36.125 -17.683 1.431   1.00 13.12 ?  115 ASN   B HD22 1 
ATOM   4584 N N    . PHE   B 1 116 ? 35.676 -17.105 -3.444  1.00 9.16  ?  116 PHE   B N    1 
ATOM   4585 C CA   . PHE   B 1 116 ? 36.106 -17.199 -4.837  1.00 9.60  ?  116 PHE   B CA   1 
ATOM   4586 C C    . PHE   B 1 116 ? 35.205 -16.372 -5.748  1.00 9.09  ?  116 PHE   B C    1 
ATOM   4587 O O    . PHE   B 1 116 ? 35.638 -15.941 -6.821  1.00 9.75  ?  116 PHE   B O    1 
ATOM   4588 C CB   . PHE   B 1 116 ? 36.069 -18.647 -5.360  1.00 9.39  ?  116 PHE   B CB   1 
ATOM   4589 C CG   . PHE   B 1 116 ? 37.139 -19.598 -4.816  1.00 9.37  ?  116 PHE   B CG   1 
ATOM   4590 C CD1  . PHE   B 1 116 ? 37.798 -19.406 -3.611  1.00 10.14 ?  116 PHE   B CD1  1 
ATOM   4591 C CD2  . PHE   B 1 116 ? 37.442 -20.736 -5.552  1.00 9.92  ?  116 PHE   B CD2  1 
ATOM   4592 C CE1  . PHE   B 1 116 ? 38.735 -20.342 -3.158  1.00 10.16 ?  116 PHE   B CE1  1 
ATOM   4593 C CE2  . PHE   B 1 116 ? 38.371 -21.670 -5.107  1.00 9.79  ?  116 PHE   B CE2  1 
ATOM   4594 C CZ   . PHE   B 1 116 ? 39.014 -21.472 -3.912  1.00 9.93  ?  116 PHE   B CZ   1 
ATOM   4595 H H    . PHE   B 1 116 ? 35.420 -17.852 -3.096  1.00 10.99 ?  116 PHE   B H    1 
ATOM   4596 H HA   . PHE   B 1 116 ? 37.012 -16.869 -4.921  1.00 11.52 ?  116 PHE   B HA   1 
ATOM   4597 H HB2  . PHE   B 1 116 ? 35.201 -19.027 -5.139  1.00 11.27 ?  116 PHE   B HB2  1 
ATOM   4598 H HB3  . PHE   B 1 116 ? 36.166 -18.623 -6.326  1.00 11.27 ?  116 PHE   B HB3  1 
ATOM   4599 H HD1  . PHE   B 1 116 ? 37.600 -18.656 -3.095  1.00 12.17 ?  116 PHE   B HD1  1 
ATOM   4600 H HD2  . PHE   B 1 116 ? 37.000 -20.889 -6.357  1.00 11.90 ?  116 PHE   B HD2  1 
ATOM   4601 H HE1  . PHE   B 1 116 ? 39.174 -20.201 -2.352  1.00 12.19 ?  116 PHE   B HE1  1 
ATOM   4602 H HE2  . PHE   B 1 116 ? 38.561 -22.421 -5.620  1.00 11.76 ?  116 PHE   B HE2  1 
ATOM   4603 H HZ   . PHE   B 1 116 ? 39.650 -22.079 -3.615  1.00 11.92 ?  116 PHE   B HZ   1 
ATOM   4604 N N    . ASN   B 1 117 ? 33.939 -16.164 -5.362  1.00 9.63  ?  117 ASN   B N    1 
ATOM   4605 C CA   . ASN   B 1 117 ? 32.994 -15.465 -6.232  1.00 9.97  ?  117 ASN   B CA   1 
ATOM   4606 C C    . ASN   B 1 117 ? 33.305 -13.985 -6.381  1.00 10.03 ?  117 ASN   B C    1 
ATOM   4607 O O    . ASN   B 1 117 ? 32.705 -13.328 -7.237  1.00 11.18 ?  117 ASN   B O    1 
ATOM   4608 C CB   . ASN   B 1 117 ? 31.569 -15.684 -5.745  1.00 10.15 ?  117 ASN   B CB   1 
ATOM   4609 C CG   . ASN   B 1 117 ? 31.118 -17.096 -5.994  1.00 10.28 ?  117 ASN   B CG   1 
ATOM   4610 O OD1  . ASN   B 1 117 ? 31.462 -17.688 -7.018  1.00 11.34 ?  117 ASN   B OD1  1 
ATOM   4611 N ND2  . ASN   B 1 117 ? 30.388 -17.665 -5.049  1.00 10.52 ?  117 ASN   B ND2  1 
ATOM   4612 H H    . ASN   B 1 117 ? 33.610 -16.414 -4.604  1.00 11.56 ?  117 ASN   B H    1 
ATOM   4613 H HA   . ASN   B 1 117 ? 33.056 -15.863 -7.111  1.00 11.96 ?  117 ASN   B HA   1 
ATOM   4614 H HB2  . ASN   B 1 117 ? 31.523 -15.512 -4.789  1.00 12.19 ?  117 ASN   B HB2  1 
ATOM   4615 H HB3  . ASN   B 1 117 ? 30.974 -15.079 -6.219  1.00 12.19 ?  117 ASN   B HB3  1 
ATOM   4616 H HD21 . ASN   B 1 117 ? 30.107 -18.470 -5.146  1.00 12.63 ?  117 ASN   B HD21 1 
ATOM   4617 H HD22 . ASN   B 1 117 ? 30.170 -17.217 -4.343  1.00 12.63 ?  117 ASN   B HD22 1 
ATOM   4618 N N    . GLN   B 1 118 ? 34.239 -13.457 -5.600  1.00 9.97  ?  118 GLN   B N    1 
ATOM   4619 C CA   . GLN   B 1 118 ? 34.665 -12.070 -5.737  1.00 10.64 ?  118 GLN   B CA   1 
ATOM   4620 C C    . GLN   B 1 118 ? 35.733 -11.878 -6.809  1.00 10.59 ?  118 GLN   B C    1 
ATOM   4621 O O    . GLN   B 1 118 ? 36.204 -10.748 -6.988  1.00 12.17 ?  118 GLN   B O    1 
ATOM   4622 C CB   . GLN   B 1 118 ? 35.145 -11.541 -4.384  1.00 11.30 ?  118 GLN   B CB   1 
ATOM   4623 C CG   . GLN   B 1 118 ? 34.059 -11.584 -3.317  1.00 11.24 ?  118 GLN   B CG   1 
ATOM   4624 C CD   . GLN   B 1 118 ? 32.884 -10.681 -3.647  1.00 11.16 ?  118 GLN   B CD   1 
ATOM   4625 O OE1  . GLN   B 1 118 ? 33.070 -9.537  -4.080  1.00 11.91 ?  118 GLN   B OE1  1 
ATOM   4626 N NE2  . GLN   B 1 118 ? 31.670 -11.175 -3.439  1.00 11.91 ?  118 GLN   B NE2  1 
ATOM   4627 H H    . GLN   B 1 118 ? 34.656 -13.886 -4.977  1.00 11.97 ?  118 GLN   B H    1 
ATOM   4628 H HA   . GLN   B 1 118 ? 33.899 -11.543 -6.006  1.00 12.77 ?  118 GLN   B HA   1 
ATOM   4629 H HB2  . GLN   B 1 118 ? 35.891 -12.073 -4.079  1.00 13.56 ?  118 GLN   B HB2  1 
ATOM   4630 H HB3  . GLN   B 1 118 ? 35.421 -10.612 -4.489  1.00 13.56 ?  118 GLN   B HB3  1 
ATOM   4631 H HG2  . GLN   B 1 118 ? 33.730 -12.493 -3.241  1.00 13.49 ?  118 GLN   B HG2  1 
ATOM   4632 H HG3  . GLN   B 1 118 ? 34.437 -11.295 -2.472  1.00 13.49 ?  118 GLN   B HG3  1 
ATOM   4633 H HE21 . GLN   B 1 118 ? 31.579 -11.975 -3.136  1.00 14.30 ?  118 GLN   B HE21 1 
ATOM   4634 H HE22 . GLN   B 1 118 ? 30.981 -10.697 -3.612  1.00 14.30 ?  118 GLN   B HE22 1 
ATOM   4635 N N    . HIS   B 1 119 ? 36.087 -12.932 -7.547  1.00 10.00 ?  119 HIS   B N    1 
ATOM   4636 C CA   . HIS   B 1 119 ? 37.129 -12.881 -8.565  1.00 10.52 ?  119 HIS   B CA   1 
ATOM   4637 C C    . HIS   B 1 119 ? 36.651 -13.618 -9.803  1.00 10.52 ?  119 HIS   B C    1 
ATOM   4638 O O    . HIS   B 1 119 ? 36.150 -14.739 -9.701  1.00 11.25 ?  119 HIS   B O    1 
ATOM   4639 C CB   . HIS   B 1 119 ? 38.415 -13.506 -8.020  1.00 11.15 ?  119 HIS   B CB   1 
ATOM   4640 C CG   . HIS   B 1 119 ? 38.896 -12.811 -6.793  1.00 12.21 ?  119 HIS   B CG   1 
ATOM   4641 N ND1  . HIS   B 1 119 ? 39.681 -11.679 -6.847  1.00 14.00 ?  119 HIS   B ND1  1 
ATOM   4642 C CD2  . HIS   B 1 119 ? 38.613 -13.016 -5.486  1.00 13.52 ?  119 HIS   B CD2  1 
ATOM   4643 C CE1  . HIS   B 1 119 ? 39.896 -11.242 -5.619  1.00 15.11 ?  119 HIS   B CE1  1 
ATOM   4644 N NE2  . HIS   B 1 119 ? 39.255 -12.032 -4.776  1.00 15.10 ?  119 HIS   B NE2  1 
ATOM   4645 H H    . HIS   B 1 119 ? 35.717 -13.709 -7.481  1.00 12.00 ?  119 HIS   B H    1 
ATOM   4646 H HA   . HIS   B 1 119 ? 37.305 -11.957 -8.807  1.00 12.63 ?  119 HIS   B HA   1 
ATOM   4647 H HB2  . HIS   B 1 119 ? 38.249 -14.433 -7.802  1.00 13.38 ?  119 HIS   B HB2  1 
ATOM   4648 H HB3  . HIS   B 1 119 ? 39.108 -13.439 -8.699  1.00 13.38 ?  119 HIS   B HB3  1 
ATOM   4649 H HD2  . HIS   B 1 119 ? 38.092 -13.702 -5.137  1.00 16.23 ?  119 HIS   B HD2  1 
ATOM   4650 H HE1  . HIS   B 1 119 ? 40.419 -10.509 -5.384  1.00 18.14 ?  119 HIS   B HE1  1 
ATOM   4651 H HE2  . HIS   B 1 119 ? 39.263 -11.960 -3.918  1.00 18.12 ?  119 HIS   B HE2  1 
ATOM   4652 N N    . GLU   B 1 120 ? 36.802 -12.997 -10.972 1.00 10.88 ?  120 GLU   B N    1 
ATOM   4653 C CA   . GLU   B 1 120 ? 36.212 -13.576 -12.175 1.00 12.34 ?  120 GLU   B CA   1 
ATOM   4654 C C    . GLU   B 1 120 ? 36.887 -14.875 -12.592 1.00 11.21 ?  120 GLU   B C    1 
ATOM   4655 O O    . GLU   B 1 120 ? 36.223 -15.749 -13.161 1.00 11.40 ?  120 GLU   B O    1 
ATOM   4656 C CB   . GLU   B 1 120 ? 36.221 -12.564 -13.317 1.00 16.25 ?  120 GLU   B CB   1 
ATOM   4657 C CG   . GLU   B 1 120 ? 35.244 -11.422 -13.098 1.00 22.20 ?  120 GLU   B CG   1 
ATOM   4658 C CD   . GLU   B 1 120 ? 35.075 -10.537 -14.314 1.00 27.78 ?  120 GLU   B CD   1 
ATOM   4659 O OE1  . GLU   B 1 120 ? 36.087 -10.249 -14.989 1.00 29.67 ?  120 GLU   B OE1  1 
ATOM   4660 O OE2  . GLU   B 1 120 ? 33.929 -10.126 -14.589 1.00 30.16 -1 120 GLU   B OE2  1 
ATOM   4661 H H    . GLU   B 1 120 ? 37.228 -12.258 -11.097 1.00 13.06 ?  120 GLU   B H    1 
ATOM   4662 H HA   . GLU   B 1 120 ? 35.289 -13.787 -11.989 1.00 14.81 ?  120 GLU   B HA   1 
ATOM   4663 H HB2  . GLU   B 1 120 ? 37.107 -12.182 -13.403 1.00 19.51 ?  120 GLU   B HB2  1 
ATOM   4664 H HB3  . GLU   B 1 120 ? 35.972 -13.011 -14.143 1.00 19.51 ?  120 GLU   B HB3  1 
ATOM   4665 H HG2  . GLU   B 1 120 ? 34.375 -11.789 -12.870 1.00 26.64 ?  120 GLU   B HG2  1 
ATOM   4666 H HG3  . GLU   B 1 120 ? 35.569 -10.863 -12.378 1.00 26.64 ?  120 GLU   B HG3  1 
ATOM   4667 N N    . VAL   B 1 121 ? 38.187 -15.018 -12.331 1.00 10.76 ?  121 VAL   B N    1 
ATOM   4668 C CA   . VAL   B 1 121 ? 38.932 -16.227 -12.676 1.00 10.72 ?  121 VAL   B CA   1 
ATOM   4669 C C    . VAL   B 1 121 ? 40.045 -16.429 -11.654 1.00 10.22 ?  121 VAL   B C    1 
ATOM   4670 O O    . VAL   B 1 121 ? 40.719 -15.473 -11.256 1.00 11.10 ?  121 VAL   B O    1 
ATOM   4671 C CB   . VAL   B 1 121 ? 39.448 -16.187 -14.135 1.00 12.63 ?  121 VAL   B CB   1 
ATOM   4672 C CG1  . VAL   B 1 121 ? 40.315 -14.958 -14.393 1.00 13.68 ?  121 VAL   B CG1  1 
ATOM   4673 C CG2  . VAL   B 1 121 ? 40.190 -17.466 -14.483 1.00 13.76 ?  121 VAL   B CG2  1 
ATOM   4674 H H    . VAL   B 1 121 ? 38.671 -14.416 -11.952 1.00 12.91 ?  121 VAL   B H    1 
ATOM   4675 H HA   . VAL   B 1 121 ? 38.329 -16.980 -12.611 1.00 12.87 ?  121 VAL   B HA   1 
ATOM   4676 H HB   . VAL   B 1 121 ? 38.682 -16.130 -14.731 1.00 15.16 ?  121 VAL   B HB   1 
ATOM   4677 H HG11 . VAL   B 1 121 ? 40.622 -14.975 -15.314 1.00 16.42 ?  121 VAL   B HG11 1 
ATOM   4678 H HG12 . VAL   B 1 121 ? 39.783 -14.160 -14.240 1.00 16.42 ?  121 VAL   B HG12 1 
ATOM   4679 H HG13 . VAL   B 1 121 ? 41.072 -14.973 -13.791 1.00 16.42 ?  121 VAL   B HG13 1 
ATOM   4680 H HG21 . VAL   B 1 121 ? 40.390 -17.469 -15.435 1.00 16.51 ?  121 VAL   B HG21 1 
ATOM   4681 H HG22 . VAL   B 1 121 ? 41.018 -17.502 -13.976 1.00 16.51 ?  121 VAL   B HG22 1 
ATOM   4682 H HG23 . VAL   B 1 121 ? 39.633 -18.227 -14.263 1.00 16.51 ?  121 VAL   B HG23 1 
ATOM   4683 N N    . LEU   B 1 122 ? 40.227 -17.681 -11.220 1.00 9.85  ?  122 LEU   B N    1 
ATOM   4684 C CA   . LEU   B 1 122 ? 41.207 -18.029 -10.196 1.00 9.62  ?  122 LEU   B CA   1 
ATOM   4685 C C    . LEU   B 1 122 ? 41.862 -19.362 -10.521 1.00 9.36  ?  122 LEU   B C    1 
ATOM   4686 O O    . LEU   B 1 122 ? 41.205 -20.283 -11.024 1.00 10.75 ?  122 LEU   B O    1 
ATOM   4687 C CB   . LEU   B 1 122 ? 40.553 -18.254 -8.822  1.00 11.44 ?  122 LEU   B CB   1 
ATOM   4688 C CG   . LEU   B 1 122 ? 39.523 -17.239 -8.328  1.00 11.42 ?  122 LEU   B CG   1 
ATOM   4689 C CD1  . LEU   B 1 122 ? 38.125 -17.602 -8.801  1.00 12.62 ?  122 LEU   B CD1  1 
ATOM   4690 C CD2  . LEU   B 1 122 ? 39.579 -17.145 -6.820  1.00 11.00 ?  122 LEU   B CD2  1 
ATOM   4691 H H    . LEU   B 1 122 ? 39.785 -18.360 -11.514 1.00 11.82 ?  122 LEU   B H    1 
ATOM   4692 H HA   . LEU   B 1 122 ? 41.885 -17.334 -10.125 1.00 11.55 ?  122 LEU   B HA   1 
ATOM   4693 H HB2  . LEU   B 1 122 ? 40.108 -19.112 -8.848  1.00 13.73 ?  122 LEU   B HB2  1 
ATOM   4694 H HB3  . LEU   B 1 122 ? 41.259 -18.279 -8.162  1.00 13.73 ?  122 LEU   B HB3  1 
ATOM   4695 H HG   . LEU   B 1 122 ? 39.741 -16.364 -8.688  1.00 13.71 ?  122 LEU   B HG   1 
ATOM   4696 H HD11 . LEU   B 1 122 ? 37.494 -16.955 -8.444  1.00 15.15 ?  122 LEU   B HD11 1 
ATOM   4697 H HD12 . LEU   B 1 122 ? 38.102 -17.581 -9.770  1.00 15.15 ?  122 LEU   B HD12 1 
ATOM   4698 H HD13 . LEU   B 1 122 ? 37.904 -18.489 -8.482  1.00 15.15 ?  122 LEU   B HD13 1 
ATOM   4699 H HD21 . LEU   B 1 122 ? 38.896 -16.529 -6.512  1.00 13.21 ?  122 LEU   B HD21 1 
ATOM   4700 H HD22 . LEU   B 1 122 ? 39.429 -18.024 -6.440  1.00 13.21 ?  122 LEU   B HD22 1 
ATOM   4701 H HD23 . LEU   B 1 122 ? 40.458 -16.818 -6.555  1.00 13.21 ?  122 LEU   B HD23 1 
ATOM   4702 N N    . LEU   B 1 123 ? 43.151 -19.468 -10.170 1.00 9.17  ?  123 LEU   B N    1 
ATOM   4703 C CA   . LEU   B 1 123 ? 43.865 -20.738 -10.047 1.00 9.60  ?  123 LEU   B CA   1 
ATOM   4704 C C    . LEU   B 1 123 ? 43.838 -21.136 -8.575  1.00 9.31  ?  123 LEU   B C    1 
ATOM   4705 O O    . LEU   B 1 123 ? 44.185 -20.314 -7.718  1.00 9.74  ?  123 LEU   B O    1 
ATOM   4706 C CB   . LEU   B 1 123 ? 45.314 -20.559 -10.509 1.00 9.90  ?  123 LEU   B CB   1 
ATOM   4707 C CG   . LEU   B 1 123 ? 46.257 -21.740 -10.269 1.00 10.46 ?  123 LEU   B CG   1 
ATOM   4708 C CD1  . LEU   B 1 123 ? 45.822 -22.973 -11.049 1.00 10.98 ?  123 LEU   B CD1  1 
ATOM   4709 C CD2  . LEU   B 1 123 ? 47.679 -21.345 -10.633 1.00 11.45 ?  123 LEU   B CD2  1 
ATOM   4710 H H    . LEU   B 1 123 ? 43.649 -18.789 -9.975  1.00 11.00 ?  123 LEU   B H    1 
ATOM   4711 H HA   . LEU   B 1 123 ? 43.429 -21.424 -10.579 1.00 11.53 ?  123 LEU   B HA   1 
ATOM   4712 H HB2  . LEU   B 1 123 ? 45.305 -20.390 -11.465 1.00 11.88 ?  123 LEU   B HB2  1 
ATOM   4713 H HB3  . LEU   B 1 123 ? 45.687 -19.797 -10.050 1.00 11.88 ?  123 LEU   B HB3  1 
ATOM   4714 H HG   . LEU   B 1 123 ? 46.249 -21.971 -9.328  1.00 12.56 ?  123 LEU   B HG   1 
ATOM   4715 H HD11 . LEU   B 1 123 ? 46.459 -23.686 -10.893 1.00 13.18 ?  123 LEU   B HD11 1 
ATOM   4716 H HD12 . LEU   B 1 123 ? 44.940 -23.242 -10.745 1.00 13.18 ?  123 LEU   B HD12 1 
ATOM   4717 H HD13 . LEU   B 1 123 ? 45.793 -22.754 -11.994 1.00 13.18 ?  123 LEU   B HD13 1 
ATOM   4718 H HD21 . LEU   B 1 123 ? 48.270 -22.098 -10.479 1.00 13.74 ?  123 LEU   B HD21 1 
ATOM   4719 H HD22 . LEU   B 1 123 ? 47.708 -21.088 -11.570 1.00 13.74 ?  123 LEU   B HD22 1 
ATOM   4720 H HD23 . LEU   B 1 123 ? 47.949 -20.594 -10.079 1.00 13.74 ?  123 LEU   B HD23 1 
ATOM   4721 N N    . ALA   B 1 124 ? 43.408 -22.369 -8.272  1.00 9.33  ?  124 ALA   B N    1 
ATOM   4722 C CA   . ALA   B 1 124 ? 43.150 -22.695 -6.877  1.00 9.54  ?  124 ALA   B CA   1 
ATOM   4723 C C    . ALA   B 1 124 ? 43.418 -24.154 -6.548  1.00 9.21  ?  124 ALA   B C    1 
ATOM   4724 O O    . ALA   B 1 124 ? 43.294 -25.025 -7.419  1.00 9.82  ?  124 ALA   B O    1 
ATOM   4725 C CB   . ALA   B 1 124 ? 41.696 -22.380 -6.504  1.00 10.22 ?  124 ALA   B CB   1 
ATOM   4726 H H    . ALA   B 1 124 ? 43.255 -23.008 -8.835  1.00 11.20 ?  124 ALA   B H    1 
ATOM   4727 H HA   . ALA   B 1 124 ? 43.727 -22.146 -6.328  1.00 11.45 ?  124 ALA   B HA   1 
ATOM   4728 H HB1  . ALA   B 1 124 ? 41.549 -22.603 -5.571  1.00 12.27 ?  124 ALA   B HB1  1 
ATOM   4729 H HB2  . ALA   B 1 124 ? 41.534 -21.432 -6.644  1.00 12.27 ?  124 ALA   B HB2  1 
ATOM   4730 H HB3  . ALA   B 1 124 ? 41.102 -22.901 -7.066  1.00 12.27 ?  124 ALA   B HB3  1 
ATOM   4731 N N    . PRO   B 1 125 ? 43.722 -24.449 -5.288  1.00 9.49  ?  125 PRO   B N    1 
ATOM   4732 C CA   . PRO   B 1 125 ? 43.664 -25.816 -4.771  1.00 10.16 ?  125 PRO   B CA   1 
ATOM   4733 C C    . PRO   B 1 125 ? 42.265 -26.094 -4.224  1.00 10.08 ?  125 PRO   B C    1 
ATOM   4734 O O    . PRO   B 1 125 ? 41.466 -25.181 -4.015  1.00 10.84 ?  125 PRO   B O    1 
ATOM   4735 C CB   . PRO   B 1 125 ? 44.654 -25.743 -3.605  1.00 11.13 ?  125 PRO   B CB   1 
ATOM   4736 C CG   . PRO   B 1 125 ? 44.397 -24.360 -3.026  1.00 11.36 ?  125 PRO   B CG   1 
ATOM   4737 C CD   . PRO   B 1 125 ? 44.053 -23.482 -4.223  1.00 10.19 ?  125 PRO   B CD   1 
ATOM   4738 H HA   . PRO   B 1 125 ? 43.935 -26.480 -5.424  1.00 12.19 ?  125 PRO   B HA   1 
ATOM   4739 H HB2  . PRO   B 1 125 ? 44.457 -26.434 -2.951  1.00 13.37 ?  125 PRO   B HB2  1 
ATOM   4740 H HB3  . PRO   B 1 125 ? 45.564 -25.820 -3.931  1.00 13.37 ?  125 PRO   B HB3  1 
ATOM   4741 H HG2  . PRO   B 1 125 ? 43.653 -24.391 -2.404  1.00 13.63 ?  125 PRO   B HG2  1 
ATOM   4742 H HG3  . PRO   B 1 125 ? 45.198 -24.032 -2.580  1.00 13.63 ?  125 PRO   B HG3  1 
ATOM   4743 H HD2  . PRO   B 1 125 ? 43.290 -22.918 -4.027  1.00 12.23 ?  125 PRO   B HD2  1 
ATOM   4744 H HD3  . PRO   B 1 125 ? 44.828 -22.946 -4.481  1.00 12.23 ?  125 PRO   B HD3  1 
ATOM   4745 N N    . LEU   B 1 126 ? 41.997 -27.375 -3.952  1.00 10.96 ?  126 LEU   B N    1 
ATOM   4746 C CA   . LEU   B 1 126 ? 40.775 -27.743 -3.244  1.00 11.34 ?  126 LEU   B CA   1 
ATOM   4747 C C    . LEU   B 1 126 ? 40.889 -27.346 -1.778  1.00 11.57 ?  126 LEU   B C    1 
ATOM   4748 O O    . LEU   B 1 126 ? 41.780 -27.812 -1.061  1.00 13.26 ?  126 LEU   B O    1 
ATOM   4749 C CB   . LEU   B 1 126 ? 40.516 -29.241 -3.366  1.00 12.66 ?  126 LEU   B CB   1 
ATOM   4750 C CG   . LEU   B 1 126 ? 39.986 -29.708 -4.722  1.00 13.42 ?  126 LEU   B CG   1 
ATOM   4751 C CD1  . LEU   B 1 126 ? 40.035 -31.218 -4.823  1.00 15.12 ?  126 LEU   B CD1  1 
ATOM   4752 C CD2  . LEU   B 1 126 ? 38.568 -29.206 -4.957  1.00 13.65 ?  126 LEU   B CD2  1 
ATOM   4753 H H    . LEU   B 1 126 ? 42.505 -28.041 -4.156  1.00 13.16 ?  126 LEU   B H    1 
ATOM   4754 H HA   . LEU   B 1 126 ? 40.026 -27.267 -3.633  1.00 13.61 ?  126 LEU   B HA   1 
ATOM   4755 H HB2  . LEU   B 1 126 ? 41.346 -29.711 -3.204  1.00 15.20 ?  126 LEU   B HB2  1 
ATOM   4756 H HB3  . LEU   B 1 126 ? 39.860 -29.494 -2.699  1.00 15.20 ?  126 LEU   B HB3  1 
ATOM   4757 H HG   . LEU   B 1 126 ? 40.550 -29.347 -5.425  1.00 16.11 ?  126 LEU   B HG   1 
ATOM   4758 H HD11 . LEU   B 1 126 ? 39.692 -31.492 -5.690  1.00 18.15 ?  126 LEU   B HD11 1 
ATOM   4759 H HD12 . LEU   B 1 126 ? 40.951 -31.515 -4.721  1.00 18.15 ?  126 LEU   B HD12 1 
ATOM   4760 H HD13 . LEU   B 1 126 ? 39.483 -31.600 -4.119  1.00 18.15 ?  126 LEU   B HD13 1 
ATOM   4761 H HD21 . LEU   B 1 126 ? 38.215 -29.617 -5.761  1.00 16.38 ?  126 LEU   B HD21 1 
ATOM   4762 H HD22 . LEU   B 1 126 ? 38.019 -29.442 -4.194  1.00 16.38 ?  126 LEU   B HD22 1 
ATOM   4763 H HD23 . LEU   B 1 126 ? 38.588 -28.240 -5.063  1.00 16.38 ?  126 LEU   B HD23 1 
ATOM   4764 N N    . LEU   B 1 127 ? 39.966 -26.507 -1.323  1.00 11.20 ?  127 LEU   B N    1 
ATOM   4765 C CA   . LEU   B 1 127 ? 40.017 -26.018 0.045   1.00 11.50 ?  127 LEU   B CA   1 
ATOM   4766 C C    . LEU   B 1 127 ? 39.740 -27.139 1.039   1.00 11.17 ?  127 LEU   B C    1 
ATOM   4767 O O    . LEU   B 1 127 ? 38.917 -28.033 0.805   1.00 11.37 ?  127 LEU   B O    1 
ATOM   4768 C CB   . LEU   B 1 127 ? 38.995 -24.900 0.252   1.00 12.21 ?  127 LEU   B CB   1 
ATOM   4769 C CG   . LEU   B 1 127 ? 39.179 -23.628 -0.575  1.00 12.67 ?  127 LEU   B CG   1 
ATOM   4770 C CD1  . LEU   B 1 127 ? 38.051 -22.664 -0.250  1.00 12.65 ?  127 LEU   B CD1  1 
ATOM   4771 C CD2  . LEU   B 1 127 ? 40.538 -22.984 -0.325  1.00 13.07 ?  127 LEU   B CD2  1 
ATOM   4772 H H    . LEU   B 1 127 ? 39.300 -26.200 -1.783  1.00 13.45 ?  127 LEU   B H    1 
ATOM   4773 H HA   . LEU   B 1 127 ? 40.902 -25.657 0.224   1.00 13.80 ?  127 LEU   B HA   1 
ATOM   4774 H HB2  . LEU   B 1 127 ? 38.116 -25.250 0.044   1.00 14.65 ?  127 LEU   B HB2  1 
ATOM   4775 H HB3  . LEU   B 1 127 ? 39.019 -24.634 1.186   1.00 14.65 ?  127 LEU   B HB3  1 
ATOM   4776 H HG   . LEU   B 1 127 ? 39.112 -23.845 -1.516  1.00 15.21 ?  127 LEU   B HG   1 
ATOM   4777 H HD11 . LEU   B 1 127 ? 38.165 -21.850 -0.771  1.00 15.19 ?  127 LEU   B HD11 1 
ATOM   4778 H HD12 . LEU   B 1 127 ? 37.201 -23.076 -0.467  1.00 15.19 ?  127 LEU   B HD12 1 
ATOM   4779 H HD13 . LEU   B 1 127 ? 38.080 -22.449 0.698   1.00 15.19 ?  127 LEU   B HD13 1 
ATOM   4780 H HD21 . LEU   B 1 127 ? 40.574 -22.129 -0.780  1.00 15.69 ?  127 LEU   B HD21 1 
ATOM   4781 H HD22 . LEU   B 1 127 ? 40.654 -22.855 0.631   1.00 15.69 ?  127 LEU   B HD22 1 
ATOM   4782 H HD23 . LEU   B 1 127 ? 41.229 -23.572 -0.664  1.00 15.69 ?  127 LEU   B HD23 1 
ATOM   4783 N N    . SER   B 1 128 ? 40.428 -27.061 2.170   1.00 11.20 ?  128 SER   B N    1 
ATOM   4784 C CA   . SER   B 1 128 ? 40.317 -27.977 3.295   1.00 11.64 ?  128 SER   B CA   1 
ATOM   4785 C C    . SER   B 1 128 ? 40.806 -29.385 2.971   1.00 12.77 ?  128 SER   B C    1 
ATOM   4786 O O    . SER   B 1 128 ? 40.716 -30.268 3.828   1.00 13.96 ?  128 SER   B O    1 
ATOM   4787 C CB   . SER   B 1 128 ? 38.916 -27.986 3.924   1.00 12.16 ?  128 SER   B CB   1 
ATOM   4788 O OG   . SER   B 1 128 ? 38.607 -26.715 4.482   1.00 12.80 ?  128 SER   B OG   1 
ATOM   4789 H H    . SER   B 1 128 ? 41.007 -26.437 2.316   1.00 13.44 ?  128 SER   B H    1 
ATOM   4790 H HA   . SER   B 1 128 ? 40.910 -27.639 3.983   1.00 13.97 ?  128 SER   B HA   1 
ATOM   4791 H HB2  . SER   B 1 128 ? 38.261 -28.214 3.247   1.00 14.59 ?  128 SER   B HB2  1 
ATOM   4792 H HB3  . SER   B 1 128 ? 38.898 -28.664 4.634   1.00 14.59 ?  128 SER   B HB3  1 
ATOM   4793 H HG   . SER   B 1 128 ? 39.177 -26.527 5.072   1.00 15.36 ?  128 SER   B HG   1 
ATOM   4794 N N    . ALA   B 1 129 ? 41.369 -29.612 1.782   1.00 13.46 ?  129 ALA   B N    1 
ATOM   4795 C CA   . ALA   B 1 129 ? 41.914 -30.913 1.432   1.00 14.63 ?  129 ALA   B CA   1 
ATOM   4796 C C    . ALA   B 1 129 ? 43.309 -31.082 2.023   1.00 13.80 ?  129 ALA   B C    1 
ATOM   4797 O O    . ALA   B 1 129 ? 43.867 -30.177 2.658   1.00 13.65 ?  129 ALA   B O    1 
ATOM   4798 C CB   . ALA   B 1 129 ? 41.956 -31.084 -0.083  1.00 16.40 ?  129 ALA   B CB   1 
ATOM   4799 H H    . ALA   B 1 129 ? 41.450 -29.024 1.158   1.00 16.16 ?  129 ALA   B H    1 
ATOM   4800 H HA   . ALA   B 1 129 ? 41.347 -31.606 1.799   1.00 17.56 ?  129 ALA   B HA   1 
ATOM   4801 H HB1  . ALA   B 1 129 ? 42.313 -31.962 -0.293  1.00 19.68 ?  129 ALA   B HB1  1 
ATOM   4802 H HB2  . ALA   B 1 129 ? 41.056 -31.000 -0.433  1.00 19.68 ?  129 ALA   B HB2  1 
ATOM   4803 H HB3  . ALA   B 1 129 ? 42.525 -30.396 -0.463  1.00 19.68 ?  129 ALA   B HB3  1 
ATOM   4804 N N    . GLY   B 1 130 ? 43.870 -32.269 1.806   1.00 13.89 ?  130 GLY   B N    1 
ATOM   4805 C CA   . GLY   B 1 130 ? 45.259 -32.507 2.151   1.00 14.49 ?  130 GLY   B CA   1 
ATOM   4806 C C    . GLY   B 1 130 ? 45.482 -32.409 3.642   1.00 14.47 ?  130 GLY   B C    1 
ATOM   4807 O O    . GLY   B 1 130 ? 44.790 -33.051 4.444   1.00 15.28 ?  130 GLY   B O    1 
ATOM   4808 H H    . GLY   B 1 130 ? 43.473 -32.945 1.450   1.00 16.67 ?  130 GLY   B H    1 
ATOM   4809 H HA2  . GLY   B 1 130 ? 45.522 -33.397 1.858   1.00 17.39 ?  130 GLY   B HA2  1 
ATOM   4810 H HA3  . GLY   B 1 130 ? 45.826 -31.858 1.707   1.00 17.39 ?  130 GLY   B HA3  1 
ATOM   4811 N N    . ILE   B 1 131 ? 46.450 -31.571 4.025   1.00 14.77 ?  131 ILE   B N    1 
ATOM   4812 C CA   . ILE   B 1 131 ? 46.808 -31.440 5.432   1.00 15.49 ?  131 ILE   B CA   1 
ATOM   4813 C C    . ILE   B 1 131 ? 45.689 -30.847 6.271   1.00 14.72 ?  131 ILE   B C    1 
ATOM   4814 O O    . ILE   B 1 131 ? 45.769 -30.910 7.502   1.00 16.14 ?  131 ILE   B O    1 
ATOM   4815 C CB   . ILE   B 1 131 ? 48.127 -30.660 5.632   1.00 17.48 ?  131 ILE   B CB   1 
ATOM   4816 C CG1  . ILE   B 1 131 ? 47.957 -29.182 5.254   1.00 18.19 ?  131 ILE   B CG1  1 
ATOM   4817 C CG2  . ILE   B 1 131 ? 49.254 -31.301 4.828   1.00 18.62 ?  131 ILE   B CG2  1 
ATOM   4818 C CD1  . ILE   B 1 131 ? 49.169 -28.323 5.579   1.00 19.15 ?  131 ILE   B CD1  1 
ATOM   4819 H H    . ILE   B 1 131 ? 46.910 -31.078 3.492   1.00 17.72 ?  131 ILE   B H    1 
ATOM   4820 H HA   . ILE   B 1 131 ? 46.959 -32.332 5.776   1.00 18.59 ?  131 ILE   B HA   1 
ATOM   4821 H HB   . ILE   B 1 131 ? 48.361 -30.707 6.571   1.00 20.98 ?  131 ILE   B HB   1 
ATOM   4822 H HG12 . ILE   B 1 131 ? 47.794 -29.122 4.300   1.00 21.83 ?  131 ILE   B HG12 1 
ATOM   4823 H HG13 . ILE   B 1 131 ? 47.201 -28.813 5.739   1.00 21.83 ?  131 ILE   B HG13 1 
ATOM   4824 H HG21 . ILE   B 1 131 ? 50.094 -30.898 5.094   1.00 22.35 ?  131 ILE   B HG21 1 
ATOM   4825 H HG22 . ILE   B 1 131 ? 49.266 -32.251 5.010   1.00 22.35 ?  131 ILE   B HG22 1 
ATOM   4826 H HG23 . ILE   B 1 131 ? 49.092 -31.144 3.885   1.00 22.35 ?  131 ILE   B HG23 1 
ATOM   4827 H HD11 . ILE   B 1 131 ? 48.950 -27.394 5.404   1.00 22.99 ?  131 ILE   B HD11 1 
ATOM   4828 H HD12 . ILE   B 1 131 ? 49.393 -28.438 6.516   1.00 22.99 ?  131 ILE   B HD12 1 
ATOM   4829 H HD13 . ILE   B 1 131 ? 49.911 -28.601 5.023   1.00 22.99 ?  131 ILE   B HD13 1 
ATOM   4830 N N    . PHE   B 1 132 ? 44.654 -30.277 5.643   1.00 13.72 ?  132 PHE   B N    1 
ATOM   4831 C CA   . PHE   B 1 132 ? 43.493 -29.773 6.371   1.00 13.87 ?  132 PHE   B CA   1 
ATOM   4832 C C    . PHE   B 1 132 ? 42.468 -30.861 6.695   1.00 14.94 ?  132 PHE   B C    1 
ATOM   4833 O O    . PHE   B 1 132 ? 41.558 -30.610 7.493   1.00 16.77 ?  132 PHE   B O    1 
ATOM   4834 C CB   . PHE   B 1 132 ? 42.821 -28.640 5.585   1.00 13.09 ?  132 PHE   B CB   1 
ATOM   4835 C CG   . PHE   B 1 132 ? 43.515 -27.297 5.702   1.00 13.02 ?  132 PHE   B CG   1 
ATOM   4836 C CD1  . PHE   B 1 132 ? 44.809 -27.106 5.233   1.00 14.30 ?  132 PHE   B CD1  1 
ATOM   4837 C CD2  . PHE   B 1 132 ? 42.840 -26.209 6.235   1.00 12.87 ?  132 PHE   B CD2  1 
ATOM   4838 C CE1  . PHE   B 1 132 ? 45.422 -25.861 5.329   1.00 14.75 ?  132 PHE   B CE1  1 
ATOM   4839 C CE2  . PHE   B 1 132 ? 43.445 -24.964 6.329   1.00 13.54 ?  132 PHE   B CE2  1 
ATOM   4840 C CZ   . PHE   B 1 132 ? 44.736 -24.793 5.874   1.00 14.42 ?  132 PHE   B CZ   1 
ATOM   4841 H H    . PHE   B 1 132 ? 44.603 -30.172 4.789   1.00 16.47 ?  132 PHE   B H    1 
ATOM   4842 H HA   . PHE   B 1 132 ? 43.800 -29.398 7.209   1.00 16.65 ?  132 PHE   B HA   1 
ATOM   4843 H HB2  . PHE   B 1 132 ? 42.813 -28.876 4.647   1.00 15.71 ?  132 PHE   B HB2  1 
ATOM   4844 H HB3  . PHE   B 1 132 ? 41.914 -28.531 5.908   1.00 15.71 ?  132 PHE   B HB3  1 
ATOM   4845 H HD1  . PHE   B 1 132 ? 45.276 -27.823 4.868   1.00 17.16 ?  132 PHE   B HD1  1 
ATOM   4846 H HD2  . PHE   B 1 132 ? 41.968 -26.318 6.543   1.00 15.44 ?  132 PHE   B HD2  1 
ATOM   4847 H HE1  . PHE   B 1 132 ? 46.295 -25.750 5.024   1.00 17.70 ?  132 PHE   B HE1  1 
ATOM   4848 H HE2  . PHE   B 1 132 ? 42.983 -24.245 6.700   1.00 16.25 ?  132 PHE   B HE2  1 
ATOM   4849 H HZ   . PHE   B 1 132 ? 45.149 -23.959 5.942   1.00 17.31 ?  132 PHE   B HZ   1 
ATOM   4850 N N    . GLY   B 1 133 ? 42.573 -32.050 6.092   1.00 14.55 ?  133 GLY   B N    1 
ATOM   4851 C CA   . GLY   B 1 133 ? 41.868 -33.223 6.581   1.00 15.42 ?  133 GLY   B CA   1 
ATOM   4852 C C    . GLY   B 1 133 ? 40.472 -33.485 6.049   1.00 15.84 ?  133 GLY   B C    1 
ATOM   4853 O O    . GLY   B 1 133 ? 39.875 -34.496 6.433   1.00 17.91 ?  133 GLY   B O    1 
ATOM   4854 H H    . GLY   B 1 133 ? 43.059 -32.195 5.395   1.00 17.46 ?  133 GLY   B H    1 
ATOM   4855 H HA2  . GLY   B 1 133 ? 42.405 -34.002 6.380   1.00 18.50 ?  133 GLY   B HA2  1 
ATOM   4856 H HA3  . GLY   B 1 133 ? 41.803 -33.153 7.546   1.00 18.50 ?  133 GLY   B HA3  1 
ATOM   4857 N N    . ALA   B 1 134 ? 39.917 -32.625 5.202   1.00 15.06 ?  134 ALA   B N    1 
ATOM   4858 C CA   . ALA   B 1 134 ? 38.590 -32.899 4.673   1.00 15.33 ?  134 ALA   B CA   1 
ATOM   4859 C C    . ALA   B 1 134 ? 38.672 -33.885 3.513   1.00 15.23 ?  134 ALA   B C    1 
ATOM   4860 O O    . ALA   B 1 134 ? 39.724 -34.070 2.895   1.00 16.42 ?  134 ALA   B O    1 
ATOM   4861 C CB   . ALA   B 1 134 ? 37.913 -31.608 4.212   1.00 15.94 ?  134 ALA   B CB   1 
ATOM   4862 H H    . ALA   B 1 134 ? 40.279 -31.890 4.926   1.00 18.07 ?  134 ALA   B H    1 
ATOM   4863 H HA   . ALA   B 1 134 ? 38.045 -33.292 5.373   1.00 18.40 ?  134 ALA   B HA   1 
ATOM   4864 H HB1  . ALA   B 1 134 ? 37.026 -31.821 3.881   1.00 19.13 ?  134 ALA   B HB1  1 
ATOM   4865 H HB2  . ALA   B 1 134 ? 37.849 -31.000 4.965   1.00 19.13 ?  134 ALA   B HB2  1 
ATOM   4866 H HB3  . ALA   B 1 134 ? 38.444 -31.209 3.507   1.00 19.13 ?  134 ALA   B HB3  1 
ATOM   4867 N N    . ASP   B 1 135 ? 37.541 -34.517 3.224   1.00 15.18 ?  135 ASP   B N    1 
ATOM   4868 C CA   . ASP   B 1 135 ? 37.443 -35.413 2.079   1.00 15.84 ?  135 ASP   B CA   1 
ATOM   4869 C C    . ASP   B 1 135 ? 37.541 -34.579 0.808   1.00 15.07 ?  135 ASP   B C    1 
ATOM   4870 O O    . ASP   B 1 135 ? 36.688 -33.712 0.585   1.00 15.05 ?  135 ASP   B O    1 
ATOM   4871 C CB   . ASP   B 1 135 ? 36.100 -36.142 2.134   1.00 17.46 ?  135 ASP   B CB   1 
ATOM   4872 C CG   . ASP   B 1 135 ? 35.907 -37.122 0.988   1.00 19.55 ?  135 ASP   B CG   1 
ATOM   4873 O OD1  . ASP   B 1 135 ? 36.776 -37.184 0.093   1.00 19.37 ?  135 ASP   B OD1  1 
ATOM   4874 O OD2  . ASP   B 1 135 ? 34.885 -37.848 0.994   1.00 22.48 -1 135 ASP   B OD2  1 
ATOM   4875 H H    . ASP   B 1 135 ? 36.813 -34.444 3.677   1.00 18.22 ?  135 ASP   B H    1 
ATOM   4876 H HA   . ASP   B 1 135 ? 38.160 -36.067 2.110   1.00 19.01 ?  135 ASP   B HA   1 
ATOM   4877 H HB2  . ASP   B 1 135 ? 36.051 -36.640 2.962   1.00 20.95 ?  135 ASP   B HB2  1 
ATOM   4878 H HB3  . ASP   B 1 135 ? 35.390 -35.485 2.095   1.00 20.95 ?  135 ASP   B HB3  1 
ATOM   4879 N N    . PRO   B 1 136 ? 38.550 -34.786 -0.041  1.00 15.06 ?  136 PRO   B N    1 
ATOM   4880 C CA   . PRO   B 1 136 ? 38.652 -33.959 -1.255  1.00 14.34 ?  136 PRO   B CA   1 
ATOM   4881 C C    . PRO   B 1 136 ? 37.464 -34.107 -2.184  1.00 13.57 ?  136 PRO   B C    1 
ATOM   4882 O O    . PRO   B 1 136 ? 37.142 -33.161 -2.913  1.00 12.90 ?  136 PRO   B O    1 
ATOM   4883 C CB   . PRO   B 1 136 ? 39.958 -34.441 -1.903  1.00 15.51 ?  136 PRO   B CB   1 
ATOM   4884 C CG   . PRO   B 1 136 ? 40.150 -35.829 -1.368  1.00 16.37 ?  136 PRO   B CG   1 
ATOM   4885 C CD   . PRO   B 1 136 ? 39.630 -35.783 0.037   1.00 16.04 ?  136 PRO   B CD   1 
ATOM   4886 H HA   . PRO   B 1 136 ? 38.747 -33.022 -1.018  1.00 17.22 ?  136 PRO   B HA   1 
ATOM   4887 H HB2  . PRO   B 1 136 ? 39.861 -34.454 -2.870  1.00 18.61 ?  136 PRO   B HB2  1 
ATOM   4888 H HB3  . PRO   B 1 136 ? 40.690 -33.864 -1.638  1.00 18.61 ?  136 PRO   B HB3  1 
ATOM   4889 H HG2  . PRO   B 1 136 ? 39.640 -36.459 -1.901  1.00 19.65 ?  136 PRO   B HG2  1 
ATOM   4890 H HG3  . PRO   B 1 136 ? 41.092 -36.055 -1.376  1.00 19.65 ?  136 PRO   B HG3  1 
ATOM   4891 H HD2  . PRO   B 1 136 ? 39.269 -36.645 0.296   1.00 19.25 ?  136 PRO   B HD2  1 
ATOM   4892 H HD3  . PRO   B 1 136 ? 40.320 -35.486 0.652   1.00 19.25 ?  136 PRO   B HD3  1 
ATOM   4893 N N    . ILE   B 1 137 ? 36.809 -35.271 -2.191  1.00 13.99 ?  137 ILE   B N    1 
ATOM   4894 C CA   . ILE   B 1 137 ? 35.594 -35.440 -2.983  1.00 14.61 ?  137 ILE   B CA   1 
ATOM   4895 C C    . ILE   B 1 137 ? 34.522 -34.472 -2.507  1.00 14.06 ?  137 ILE   B C    1 
ATOM   4896 O O    . ILE   B 1 137 ? 33.808 -33.860 -3.311  1.00 13.74 ?  137 ILE   B O    1 
ATOM   4897 C CB   . ILE   B 1 137 ? 35.120 -36.907 -2.928  1.00 16.63 ?  137 ILE   B CB   1 
ATOM   4898 C CG1  . ILE   B 1 137 ? 36.087 -37.803 -3.703  1.00 18.84 ?  137 ILE   B CG1  1 
ATOM   4899 C CG2  . ILE   B 1 137 ? 33.708 -37.040 -3.482  1.00 17.30 ?  137 ILE   B CG2  1 
ATOM   4900 C CD1  . ILE   B 1 137 ? 35.793 -39.286 -3.571  1.00 21.09 ?  137 ILE   B CD1  1 
ATOM   4901 H H    . ILE   B 1 137 ? 37.046 -35.972 -1.754  1.00 16.79 ?  137 ILE   B H    1 
ATOM   4902 H HA   . ILE   B 1 137 ? 35.790 -35.230 -3.910  1.00 17.54 ?  137 ILE   B HA   1 
ATOM   4903 H HB   . ILE   B 1 137 ? 35.112 -37.192 -2.005  1.00 19.96 ?  137 ILE   B HB   1 
ATOM   4904 H HG12 . ILE   B 1 137 ? 36.039 -37.576 -4.646  1.00 22.62 ?  137 ILE   B HG12 1 
ATOM   4905 H HG13 . ILE   B 1 137 ? 36.985 -37.650 -3.374  1.00 22.62 ?  137 ILE   B HG13 1 
ATOM   4906 H HG21 . ILE   B 1 137 ? 33.491 -37.981 -3.589  1.00 20.76 ?  137 ILE   B HG21 1 
ATOM   4907 H HG22 . ILE   B 1 137 ? 33.082 -36.638 -2.861  1.00 20.76 ?  137 ILE   B HG22 1 
ATOM   4908 H HG23 . ILE   B 1 137 ? 33.661 -36.594 -4.341  1.00 20.76 ?  137 ILE   B HG23 1 
ATOM   4909 H HD11 . ILE   B 1 137 ? 36.533 -39.781 -3.949  1.00 25.31 ?  137 ILE   B HD11 1 
ATOM   4910 H HD12 . ILE   B 1 137 ? 35.689 -39.506 -2.632  1.00 25.31 ?  137 ILE   B HD12 1 
ATOM   4911 H HD13 . ILE   B 1 137 ? 34.977 -39.496 -4.053  1.00 25.31 ?  137 ILE   B HD13 1 
ATOM   4912 N N    . HIS   B 1 138 ? 34.395 -34.318 -1.192  1.00 13.91 ?  138 HIS   B N    1 
ATOM   4913 C CA   . HIS   B 1 138 ? 33.439 -33.358 -0.660  1.00 14.27 ?  138 HIS   B CA   1 
ATOM   4914 C C    . HIS   B 1 138 ? 33.858 -31.927 -0.971  1.00 13.29 ?  138 HIS   B C    1 
ATOM   4915 O O    . HIS   B 1 138 ? 33.011 -31.085 -1.288  1.00 13.73 ?  138 HIS   B O    1 
ATOM   4916 C CB   . HIS   B 1 138 ? 33.292 -33.551 0.842   1.00 15.58 ?  138 HIS   B CB   1 
ATOM   4917 C CG   . HIS   B 1 138 ? 32.361 -32.569 1.472   1.00 16.69 ?  138 HIS   B CG   1 
ATOM   4918 N ND1  . HIS   B 1 138 ? 31.020 -32.511 1.159   1.00 17.99 ?  138 HIS   B ND1  1 
ATOM   4919 C CD2  . HIS   B 1 138 ? 32.580 -31.587 2.377   1.00 17.42 ?  138 HIS   B CD2  1 
ATOM   4920 C CE1  . HIS   B 1 138 ? 30.449 -31.544 1.855   1.00 18.09 ?  138 HIS   B CE1  1 
ATOM   4921 N NE2  . HIS   B 1 138 ? 31.374 -30.970 2.604   1.00 17.68 ?  138 HIS   B NE2  1 
ATOM   4922 H H    . HIS   B 1 138 ? 34.846 -34.748 -0.601  1.00 16.69 ?  138 HIS   B H    1 
ATOM   4923 H HA   . HIS   B 1 138 ? 32.573 -33.520 -1.071  1.00 17.13 ?  138 HIS   B HA   1 
ATOM   4924 H HB2  . HIS   B 1 138 ? 32.943 -34.442 1.012   1.00 18.70 ?  138 HIS   B HB2  1 
ATOM   4925 H HB3  . HIS   B 1 138 ? 34.158 -33.450 1.258   1.00 18.70 ?  138 HIS   B HB3  1 
ATOM   4926 H HD1  . HIS   B 1 138 ? 30.615 -33.029 0.600   1.00 21.59 ?  138 HIS   B HD1  1 
ATOM   4927 H HD2  . HIS   B 1 138 ? 33.387 -31.376 2.779   1.00 20.91 ?  138 HIS   B HD2  1 
ATOM   4928 H HE1  . HIS   B 1 138 ? 29.545 -31.314 1.824   1.00 21.71 ?  138 HIS   B HE1  1 
ATOM   4929 N N    . SER   B 1 139 ? 35.152 -31.625 -0.882  1.00 12.88 ?  139 SER   B N    1 
ATOM   4930 C CA   . SER   B 1 139 ? 35.593 -30.275 -1.205  1.00 12.51 ?  139 SER   B CA   1 
ATOM   4931 C C    . SER   B 1 139 ? 35.252 -29.921 -2.644  1.00 11.60 ?  139 SER   B C    1 
ATOM   4932 O O    . SER   B 1 139 ? 34.813 -28.801 -2.923  1.00 11.76 ?  139 SER   B O    1 
ATOM   4933 C CB   . SER   B 1 139 ? 37.089 -30.139 -0.945  1.00 12.85 ?  139 SER   B CB   1 
ATOM   4934 O OG   . SER   B 1 139 ? 37.504 -28.806 -1.198  1.00 12.97 ?  139 SER   B OG   1 
ATOM   4935 H H    . SER   B 1 139 ? 35.770 -32.171 -0.652  1.00 15.46 ?  139 SER   B H    1 
ATOM   4936 H HA   . SER   B 1 139 ? 35.128 -29.652 -0.633  1.00 15.01 ?  139 SER   B HA   1 
ATOM   4937 H HB2  . SER   B 1 139 ? 37.268 -30.354 -0.016  1.00 15.42 ?  139 SER   B HB2  1 
ATOM   4938 H HB3  . SER   B 1 139 ? 37.572 -30.747 -1.527  1.00 15.42 ?  139 SER   B HB3  1 
ATOM   4939 H HG   . SER   B 1 139 ? 38.332 -28.734 -1.061  1.00 15.57 ?  139 SER   B HG   1 
ATOM   4940 N N    . LEU   B 1 140 ? 35.437 -30.862 -3.571  1.00 11.66 ?  140 LEU   B N    1 
ATOM   4941 C CA   . LEU   B 1 140 ? 35.071 -30.609 -4.959  1.00 11.54 ?  140 LEU   B CA   1 
ATOM   4942 C C    . LEU   B 1 140 ? 33.567 -30.382 -5.091  1.00 11.67 ?  140 LEU   B C    1 
ATOM   4943 O O    . LEU   B 1 140 ? 33.128 -29.493 -5.827  1.00 11.70 ?  140 LEU   B O    1 
ATOM   4944 C CB   . LEU   B 1 140 ? 35.542 -31.770 -5.838  1.00 11.90 ?  140 LEU   B CB   1 
ATOM   4945 C CG   . LEU   B 1 140 ? 35.175 -31.658 -7.312  1.00 12.01 ?  140 LEU   B CG   1 
ATOM   4946 C CD1  . LEU   B 1 140 ? 35.747 -30.380 -7.914  1.00 12.57 ?  140 LEU   B CD1  1 
ATOM   4947 C CD2  . LEU   B 1 140 ? 35.657 -32.878 -8.063  1.00 12.85 ?  140 LEU   B CD2  1 
ATOM   4948 H H    . LEU   B 1 140 ? 35.766 -31.641 -3.427  1.00 13.99 ?  140 LEU   B H    1 
ATOM   4949 H HA   . LEU   B 1 140 ? 35.523 -29.804 -5.262  1.00 13.85 ?  140 LEU   B HA   1 
ATOM   4950 H HB2  . LEU   B 1 140 ? 36.513 -31.825 -5.785  1.00 14.28 ?  140 LEU   B HB2  1 
ATOM   4951 H HB3  . LEU   B 1 140 ? 35.153 -32.591 -5.504  1.00 14.28 ?  140 LEU   B HB3  1 
ATOM   4952 H HG   . LEU   B 1 140 ? 34.210 -31.613 -7.392  1.00 14.41 ?  140 LEU   B HG   1 
ATOM   4953 H HD11 . LEU   B 1 140 ? 35.619 -30.402 -8.874  1.00 15.09 ?  140 LEU   B HD11 1 
ATOM   4954 H HD12 . LEU   B 1 140 ? 35.282 -29.614 -7.538  1.00 15.09 ?  140 LEU   B HD12 1 
ATOM   4955 H HD13 . LEU   B 1 140 ? 36.692 -30.327 -7.706  1.00 15.09 ?  140 LEU   B HD13 1 
ATOM   4956 H HD21 . LEU   B 1 140 ? 35.409 -32.785 -8.997  1.00 15.43 ?  140 LEU   B HD21 1 
ATOM   4957 H HD22 . LEU   B 1 140 ? 36.617 -32.942 -7.977  1.00 15.43 ?  140 LEU   B HD22 1 
ATOM   4958 H HD23 . LEU   B 1 140 ? 35.231 -33.662 -7.685  1.00 15.43 ?  140 LEU   B HD23 1 
ATOM   4959 N N    . ARG   B 1 141 ? 32.769 -31.173 -4.371  1.00 11.92 ?  141 ARG   B N    1 
ATOM   4960 C CA   . ARG   B 1 141 ? 31.319 -30.998 -4.353  1.00 13.04 ?  141 ARG   B CA   1 
ATOM   4961 C C    . ARG   B 1 141 ? 30.944 -29.587 -3.922  1.00 12.25 ?  141 ARG   B C    1 
ATOM   4962 O O    . ARG   B 1 141 ? 30.138 -28.909 -4.576  1.00 12.29 ?  141 ARG   B O    1 
ATOM   4963 C CB   . ARG   B 1 141 ? 30.740 -32.028 -3.375  1.00 14.91 ?  141 ARG   B CB   1 
ATOM   4964 C CG   . ARG   B 1 141 ? 29.272 -31.915 -3.048  1.00 17.24 ?  141 ARG   B CG   1 
ATOM   4965 C CD   . ARG   B 1 141 ? 28.465 -32.551 -4.119  1.00 19.26 ?  141 ARG   B CD   1 
ATOM   4966 N NE   . ARG   B 1 141 ? 28.207 -31.632 -5.217  1.00 19.60 ?  141 ARG   B NE   1 
ATOM   4967 C CZ   . ARG   B 1 141 ? 28.220 -31.968 -6.499  1.00 19.19 ?  141 ARG   B CZ   1 
ATOM   4968 N NH1  . ARG   B 1 141 ? 28.650 -33.154 -6.902  1.00 19.05 ?  141 ARG   B NH1  1 
ATOM   4969 N NH2  . ARG   B 1 141 ? 27.791 -31.089 -7.401  1.00 20.11 ?  141 ARG   B NH2  1 
ATOM   4970 H H    . ARG   B 1 141 ? 33.052 -31.818 -3.880  1.00 14.31 ?  141 ARG   B H    1 
ATOM   4971 H HA   . ARG   B 1 141 ? 30.957 -31.165 -5.236  1.00 15.65 ?  141 ARG   B HA   1 
ATOM   4972 H HB2  . ARG   B 1 141 ? 30.895 -32.915 -3.744  1.00 17.90 ?  141 ARG   B HB2  1 
ATOM   4973 H HB3  . ARG   B 1 141 ? 31.224 -31.954 -2.539  1.00 17.90 ?  141 ARG   B HB3  1 
ATOM   4974 H HG2  . ARG   B 1 141 ? 29.098 -32.374 -2.213  1.00 20.69 ?  141 ARG   B HG2  1 
ATOM   4975 H HG3  . ARG   B 1 141 ? 29.016 -30.981 -2.976  1.00 20.69 ?  141 ARG   B HG3  1 
ATOM   4976 H HD2  . ARG   B 1 141 ? 28.943 -33.326 -4.460  1.00 23.12 ?  141 ARG   B HD2  1 
ATOM   4977 H HD3  . ARG   B 1 141 ? 27.617 -32.830 -3.749  1.00 23.12 ?  141 ARG   B HD3  1 
ATOM   4978 H HE   . ARG   B 1 141 ? 28.017 -30.816 -5.017  1.00 23.52 ?  141 ARG   B HE   1 
ATOM   4979 H HH11 . ARG   B 1 141 ? 28.919 -33.736 -6.333  1.00 22.86 ?  141 ARG   B HH11 1 
ATOM   4980 H HH12 . ARG   B 1 141 ? 28.656 -33.340 -7.739  1.00 22.86 ?  141 ARG   B HH12 1 
ATOM   4981 H HH21 . ARG   B 1 141 ? 27.517 -30.311 -7.151  1.00 24.14 ?  141 ARG   B HH21 1 
ATOM   4982 H HH22 . ARG   B 1 141 ? 27.814 -31.284 -8.238  1.00 24.14 ?  141 ARG   B HH22 1 
ATOM   4983 N N    . VAL   B 1 142 ? 31.493 -29.142 -2.795  1.00 11.98 ?  142 VAL   B N    1 
ATOM   4984 C CA   . VAL   B 1 142 ? 31.161 -27.809 -2.308  1.00 11.77 ?  142 VAL   B CA   1 
ATOM   4985 C C    . VAL   B 1 142 ? 31.633 -26.751 -3.299  1.00 11.82 ?  142 VAL   B C    1 
ATOM   4986 O O    . VAL   B 1 142 ? 30.930 -25.766 -3.555  1.00 12.12 ?  142 VAL   B O    1 
ATOM   4987 C CB   . VAL   B 1 142 ? 31.713 -27.585 -0.887  1.00 12.66 ?  142 VAL   B CB   1 
ATOM   4988 C CG1  . VAL   B 1 142 ? 31.397 -26.166 -0.412  1.00 12.76 ?  142 VAL   B CG1  1 
ATOM   4989 C CG2  . VAL   B 1 142 ? 31.129 -28.610 0.077   1.00 13.41 ?  142 VAL   B CG2  1 
ATOM   4990 H H    . VAL   B 1 142 ? 32.051 -29.579 -2.308  1.00 14.38 ?  142 VAL   B H    1 
ATOM   4991 H HA   . VAL   B 1 142 ? 30.201 -27.738 -2.251  1.00 14.13 ?  142 VAL   B HA   1 
ATOM   4992 H HB   . VAL   B 1 142 ? 32.679 -27.693 -0.894  1.00 15.20 ?  142 VAL   B HB   1 
ATOM   4993 H HG11 . VAL   B 1 142 ? 31.586 -26.102 0.537   1.00 15.32 ?  142 VAL   B HG11 1 
ATOM   4994 H HG12 . VAL   B 1 142 ? 31.953 -25.537 -0.901  1.00 15.32 ?  142 VAL   B HG12 1 
ATOM   4995 H HG13 . VAL   B 1 142 ? 30.461 -25.981 -0.577  1.00 15.32 ?  142 VAL   B HG13 1 
ATOM   4996 H HG21 . VAL   B 1 142 ? 31.456 -28.421 0.971   1.00 16.10 ?  142 VAL   B HG21 1 
ATOM   4997 H HG22 . VAL   B 1 142 ? 30.162 -28.541 0.056   1.00 16.10 ?  142 VAL   B HG22 1 
ATOM   4998 H HG23 . VAL   B 1 142 ? 31.407 -29.495 -0.199  1.00 16.10 ?  142 VAL   B HG23 1 
ATOM   4999 N N    . CYS   B 1 143 ? 32.814 -26.948 -3.889  1.00 11.29 ?  143 CYS   B N    1 
ATOM   5000 C CA   . CYS   B 1 143 ? 33.305 -26.006 -4.890  1.00 11.37 ?  143 CYS   B CA   1 
ATOM   5001 C C    . CYS   B 1 143 ? 32.302 -25.855 -6.028  1.00 11.23 ?  143 CYS   B C    1 
ATOM   5002 O O    . CYS   B 1 143 ? 31.899 -24.742 -6.380  1.00 11.60 ?  143 CYS   B O    1 
ATOM   5003 C CB   . CYS   B 1 143 ? 34.658 -26.485 -5.421  1.00 11.85 ?  143 CYS   B CB   1 
ATOM   5004 S SG   . CYS   B 1 143 ? 35.408 -25.388 -6.637  1.00 12.20 ?  143 CYS   B SG   1 
ATOM   5005 H H    . CYS   B 1 143 ? 33.342 -27.611 -3.732  1.00 13.55 ?  143 CYS   B H    1 
ATOM   5006 H HA   . CYS   B 1 143 ? 33.431 -25.138 -4.479  1.00 13.64 ?  143 CYS   B HA   1 
ATOM   5007 H HB2  . CYS   B 1 143 ? 35.278 -26.569 -4.681  1.00 14.22 ?  143 CYS   B HB2  1 
ATOM   5008 H HB3  . CYS   B 1 143 ? 34.539 -27.350 -5.841  1.00 14.22 ?  143 CYS   B HB3  1 
ATOM   5009 H HG   . CYS   B 1 143 ? 36.480 -25.820 -6.959  1.00 14.64 ?  143 CYS   B HG   1 
ATOM   5010 N N    . VAL   B 1 144 ? 31.897 -26.973 -6.625  1.00 11.59 ?  144 VAL   B N    1 
ATOM   5011 C CA   . VAL   B 1 144 ? 30.987 -26.911 -7.764  1.00 12.76 ?  144 VAL   B CA   1 
ATOM   5012 C C    . VAL   B 1 144 ? 29.647 -26.305 -7.380  1.00 12.57 ?  144 VAL   B C    1 
ATOM   5013 O O    . VAL   B 1 144 ? 29.026 -25.599 -8.185  1.00 13.79 ?  144 VAL   B O    1 
ATOM   5014 C CB   . VAL   B 1 144 ? 30.833 -28.318 -8.359  1.00 15.11 ?  144 VAL   B CB   1 
ATOM   5015 C CG1  . VAL   B 1 144 ? 29.577 -28.425 -9.218  1.00 17.73 ?  144 VAL   B CG1  1 
ATOM   5016 C CG2  . VAL   B 1 144 ? 32.086 -28.701 -9.135  1.00 15.38 ?  144 VAL   B CG2  1 
ATOM   5017 H H    . VAL   B 1 144 ? 32.137 -27.770 -6.401  1.00 13.91 ?  144 VAL   B H    1 
ATOM   5018 H HA   . VAL   B 1 144 ? 31.376 -26.346 -8.448  1.00 15.31 ?  144 VAL   B HA   1 
ATOM   5019 H HB   . VAL   B 1 144 ? 30.740 -28.953 -7.632  1.00 18.14 ?  144 VAL   B HB   1 
ATOM   5020 H HG11 . VAL   B 1 144 ? 29.665 -29.199 -9.800  1.00 21.28 ?  144 VAL   B HG11 1 
ATOM   5021 H HG12 . VAL   B 1 144 ? 28.810 -28.537 -8.639  1.00 21.28 ?  144 VAL   B HG12 1 
ATOM   5022 H HG13 . VAL   B 1 144 ? 29.489 -27.623 -9.751  1.00 21.28 ?  144 VAL   B HG13 1 
ATOM   5023 H HG21 . VAL   B 1 144 ? 31.974 -29.594 -9.497  1.00 18.45 ?  144 VAL   B HG21 1 
ATOM   5024 H HG22 . VAL   B 1 144 ? 32.216 -28.066 -9.858  1.00 18.45 ?  144 VAL   B HG22 1 
ATOM   5025 H HG23 . VAL   B 1 144 ? 32.847 -28.679 -8.535  1.00 18.45 ?  144 VAL   B HG23 1 
ATOM   5026 N N    . ASP   B 1 145 ? 29.184 -26.554 -6.160  1.00 12.59 ?  145 ASP   B N    1 
ATOM   5027 C CA   . ASP   B 1 145 ? 27.879 -26.084 -5.720  1.00 13.37 ?  145 ASP   B CA   1 
ATOM   5028 C C    . ASP   B 1 145 ? 27.908 -24.662 -5.176  1.00 12.94 ?  145 ASP   B C    1 
ATOM   5029 O O    . ASP   B 1 145 ? 26.846 -24.122 -4.850  1.00 14.82 ?  145 ASP   B O    1 
ATOM   5030 C CB   . ASP   B 1 145 ? 27.303 -27.008 -4.638  1.00 14.70 ?  145 ASP   B CB   1 
ATOM   5031 C CG   . ASP   B 1 145 ? 26.933 -28.381 -5.158  1.00 16.37 ?  145 ASP   B CG   1 
ATOM   5032 O OD1  . ASP   B 1 145 ? 26.817 -28.564 -6.387  1.00 16.91 ?  145 ASP   B OD1  1 
ATOM   5033 O OD2  . ASP   B 1 145 ? 26.745 -29.280 -4.314  1.00 18.75 -1 145 ASP   B OD2  1 
ATOM   5034 H H    . ASP   B 1 145 ? 29.619 -26.991 -5.559  1.00 15.11 ?  145 ASP   B H    1 
ATOM   5035 H HA   . ASP   B 1 145 ? 27.277 -26.082 -6.474  1.00 16.05 ?  145 ASP   B HA   1 
ATOM   5036 H HB2  . ASP   B 1 145 ? 27.960 -27.128 -3.942  1.00 17.65 ?  145 ASP   B HB2  1 
ATOM   5037 H HB3  . ASP   B 1 145 ? 26.500 -26.599 -4.276  1.00 17.65 ?  145 ASP   B HB3  1 
ATOM   5038 N N    . THR   B 1 146 ? 29.083 -24.045 -5.061  1.00 11.46 ?  146 THR   B N    1 
ATOM   5039 C CA   . THR   B 1 146 ? 29.219 -22.723 -4.453  1.00 11.09 ?  146 THR   B CA   1 
ATOM   5040 C C    . THR   B 1 146 ? 29.850 -21.693 -5.373  1.00 11.00 ?  146 THR   B C    1 
ATOM   5041 O O    . THR   B 1 146 ? 29.393 -20.537 -5.417  1.00 11.46 ?  146 THR   B O    1 
ATOM   5042 C CB   . THR   B 1 146 ? 30.047 -22.831 -3.163  1.00 11.71 ?  146 THR   B CB   1 
ATOM   5043 O OG1  . THR   B 1 146 ? 29.475 -23.827 -2.307  1.00 11.87 ?  146 THR   B OG1  1 
ATOM   5044 C CG2  . THR   B 1 146 ? 30.113 -21.497 -2.438  1.00 11.99 ?  146 THR   B CG2  1 
ATOM   5045 H H    . THR   B 1 146 ? 29.836 -24.378 -5.327  1.00 13.75 ?  146 THR   B H    1 
ATOM   5046 H HA   . THR   B 1 146 ? 28.348 -22.396 -4.208  1.00 13.32 ?  146 THR   B HA   1 
ATOM   5047 H HB   . THR   B 1 146 ? 30.958 -23.088 -3.387  1.00 14.05 ?  146 THR   B HB   1 
ATOM   5048 H HG1  . THR   B 1 146 ? 29.512 -24.583 -2.688  1.00 14.24 ?  146 THR   B HG1  1 
ATOM   5049 H HG21 . THR   B 1 146 ? 30.470 -21.622 -1.546  1.00 14.39 ?  146 THR   B HG21 1 
ATOM   5050 H HG22 . THR   B 1 146 ? 30.690 -20.882 -2.922  1.00 14.39 ?  146 THR   B HG22 1 
ATOM   5051 H HG23 . THR   B 1 146 ? 29.227 -21.112 -2.373  1.00 14.39 ?  146 THR   B HG23 1 
ATOM   5052 N N    . VAL   B 1 147 ? 30.911 -22.066 -6.079  1.00 11.10 ?  147 VAL   B N    1 
ATOM   5053 C CA   . VAL   B 1 147 ? 31.634 -21.120 -6.916  1.00 10.68 ?  147 VAL   B CA   1 
ATOM   5054 C C    . VAL   B 1 147 ? 30.902 -20.986 -8.239  1.00 10.95 ?  147 VAL   B C    1 
ATOM   5055 O O    . VAL   B 1 147 ? 30.535 -21.987 -8.869  1.00 11.78 ?  147 VAL   B O    1 
ATOM   5056 C CB   . VAL   B 1 147 ? 33.087 -21.576 -7.118  1.00 11.12 ?  147 VAL   B CB   1 
ATOM   5057 C CG1  . VAL   B 1 147 ? 33.851 -20.551 -7.929  1.00 11.31 ?  147 VAL   B CG1  1 
ATOM   5058 C CG2  . VAL   B 1 147 ? 33.760 -21.798 -5.774  1.00 11.23 ?  147 VAL   B CG2  1 
ATOM   5059 H H    . VAL   B 1 147 ? 31.239 -22.865 -6.091  1.00 13.33 ?  147 VAL   B H    1 
ATOM   5060 H HA   . VAL   B 1 147 ? 31.652 -20.254 -6.486  1.00 12.82 ?  147 VAL   B HA   1 
ATOM   5061 H HB   . VAL   B 1 147 ? 33.103 -22.417 -7.605  1.00 13.35 ?  147 VAL   B HB   1 
ATOM   5062 H HG11 . VAL   B 1 147 ? 34.797 -20.777 -7.918  1.00 13.57 ?  147 VAL   B HG11 1 
ATOM   5063 H HG12 . VAL   B 1 147 ? 33.523 -20.555 -8.840  1.00 13.57 ?  147 VAL   B HG12 1 
ATOM   5064 H HG13 . VAL   B 1 147 ? 33.721 -19.675 -7.531  1.00 13.57 ?  147 VAL   B HG13 1 
ATOM   5065 H HG21 . VAL   B 1 147 ? 34.705 -21.980 -5.915  1.00 13.48 ?  147 VAL   B HG21 1 
ATOM   5066 H HG22 . VAL   B 1 147 ? 33.658 -20.998 -5.235  1.00 13.48 ?  147 VAL   B HG22 1 
ATOM   5067 H HG23 . VAL   B 1 147 ? 33.344 -22.552 -5.330  1.00 13.48 ?  147 VAL   B HG23 1 
ATOM   5068 N N    . ARG   B 1 148 ? 30.693 -19.740 -8.656  1.00 10.99 ?  148 ARG   B N    1 
ATOM   5069 C CA   . ARG   B 1 148 ? 30.071 -19.416 -9.926  1.00 11.12 ?  148 ARG   B CA   1 
ATOM   5070 C C    . ARG   B 1 148 ? 31.022 -18.738 -10.899 1.00 11.08 ?  148 ARG   B C    1 
ATOM   5071 O O    . ARG   B 1 148 ? 30.736 -18.719 -12.099 1.00 12.46 ?  148 ARG   B O    1 
ATOM   5072 C CB   . ARG   B 1 148 ? 28.834 -18.532 -9.701  1.00 11.68 ?  148 ARG   B CB   1 
ATOM   5073 C CG   . ARG   B 1 148 ? 27.757 -19.238 -8.887  1.00 12.53 ?  148 ARG   B CG   1 
ATOM   5074 C CD   . ARG   B 1 148 ? 26.556 -18.349 -8.581  1.00 13.36 ?  148 ARG   B CD   1 
ATOM   5075 N NE   . ARG   B 1 148 ? 26.941 -17.151 -7.847  1.00 13.01 ?  148 ARG   B NE   1 
ATOM   5076 C CZ   . ARG   B 1 148 ? 27.240 -17.121 -6.555  1.00 12.29 ?  148 ARG   B CZ   1 
ATOM   5077 N NH1  . ARG   B 1 148 ? 27.167 -18.207 -5.800  1.00 12.45 ?  148 ARG   B NH1  1 
ATOM   5078 N NH2  . ARG   B 1 148 ? 27.626 -15.972 -6.005  1.00 12.42 ?  148 ARG   B NH2  1 
ATOM   5079 H H    . ARG   B 1 148 ? 30.915 -19.044 -8.195  1.00 13.19 ?  148 ARG   B H    1 
ATOM   5080 H HA   . ARG   B 1 148 ? 29.770 -20.238 -10.335 1.00 13.35 ?  148 ARG   B HA   1 
ATOM   5081 H HB2  . ARG   B 1 148 ? 29.097 -17.731 -9.221  1.00 14.02 ?  148 ARG   B HB2  1 
ATOM   5082 H HB3  . ARG   B 1 148 ? 28.454 -18.295 -10.561 1.00 14.02 ?  148 ARG   B HB3  1 
ATOM   5083 H HG2  . ARG   B 1 148 ? 27.435 -20.006 -9.385  1.00 15.04 ?  148 ARG   B HG2  1 
ATOM   5084 H HG3  . ARG   B 1 148 ? 28.133 -19.527 -8.042  1.00 15.04 ?  148 ARG   B HG3  1 
ATOM   5085 H HD2  . ARG   B 1 148 ? 26.142 -18.071 -9.413  1.00 16.03 ?  148 ARG   B HD2  1 
ATOM   5086 H HD3  . ARG   B 1 148 ? 25.918 -18.843 -8.040  1.00 16.03 ?  148 ARG   B HD3  1 
ATOM   5087 H HE   . ARG   B 1 148 ? 26.986 -16.411 -8.282  1.00 15.62 ?  148 ARG   B HE   1 
ATOM   5088 H HH11 . ARG   B 1 148 ? 26.914 -18.956 -6.139  1.00 14.94 ?  148 ARG   B HH11 1 
ATOM   5089 H HH12 . ARG   B 1 148 ? 27.358 -18.162 -4.961  1.00 14.94 ?  148 ARG   B HH12 1 
ATOM   5090 H HH21 . ARG   B 1 148 ? 27.680 -15.262 -6.487  1.00 14.90 ?  148 ARG   B HH21 1 
ATOM   5091 H HH22 . ARG   B 1 148 ? 27.820 -15.938 -5.169  1.00 14.90 ?  148 ARG   B HH22 1 
ATOM   5092 N N    . THR   B 1 149 ? 32.130 -18.186 -10.414 1.00 11.18 ?  149 THR   B N    1 
ATOM   5093 C CA   . THR   B 1 149 ? 33.166 -17.627 -11.265 1.00 11.18 ?  149 THR   B CA   1 
ATOM   5094 C C    . THR   B 1 149 ? 34.055 -18.764 -11.768 1.00 10.79 ?  149 THR   B C    1 
ATOM   5095 O O    . THR   B 1 149 ? 33.872 -19.932 -11.416 1.00 11.36 ?  149 THR   B O    1 
ATOM   5096 C CB   . THR   B 1 149 ? 33.938 -16.574 -10.484 1.00 11.35 ?  149 THR   B CB   1 
ATOM   5097 O OG1  . THR   B 1 149 ? 34.394 -17.170 -9.266  1.00 11.32 ?  149 THR   B OG1  1 
ATOM   5098 C CG2  . THR   B 1 149 ? 33.044 -15.377 -10.184 1.00 12.03 ?  149 THR   B CG2  1 
ATOM   5099 H H    . THR   B 1 149 ? 32.301 -18.115 -9.576  1.00 13.42 ?  149 THR   B H    1 
ATOM   5100 H HA   . THR   B 1 149 ? 32.754 -17.199 -12.033 1.00 13.42 ?  149 THR   B HA   1 
ATOM   5101 H HB   . THR   B 1 149 ? 34.697 -16.275 -11.006 1.00 13.62 ?  149 THR   B HB   1 
ATOM   5102 H HG1  . THR   B 1 149 ? 34.816 -16.595 -8.813  1.00 13.58 ?  149 THR   B HG1  1 
ATOM   5103 H HG21 . THR   B 1 149 ? 33.549 -14.700 -9.708  1.00 14.44 ?  149 THR   B HG21 1 
ATOM   5104 H HG22 . THR   B 1 149 ? 32.712 -14.995 -11.014 1.00 14.44 ?  149 THR   B HG22 1 
ATOM   5105 H HG23 . THR   B 1 149 ? 32.290 -15.651 -9.641  1.00 14.44 ?  149 THR   B HG23 1 
ATOM   5106 N N    . ASN   B 1 150 ? 35.015 -18.440 -12.622 1.00 11.06 ?  150 ASN   B N    1 
ATOM   5107 C CA   . ASN   B 1 150 ? 35.780 -19.464 -13.322 1.00 11.39 ?  150 ASN   B CA   1 
ATOM   5108 C C    . ASN   B 1 150 ? 36.944 -19.912 -12.449 1.00 10.99 ?  150 ASN   B C    1 
ATOM   5109 O O    . ASN   B 1 150 ? 37.868 -19.137 -12.183 1.00 12.09 ?  150 ASN   B O    1 
ATOM   5110 C CB   . ASN   B 1 150 ? 36.254 -18.924 -14.664 1.00 12.96 ?  150 ASN   B CB   1 
ATOM   5111 C CG   . ASN   B 1 150 ? 35.111 -18.703 -15.616 1.00 15.74 ?  150 ASN   B CG   1 
ATOM   5112 O OD1  . ASN   B 1 150 ? 34.217 -19.536 -15.715 1.00 16.97 ?  150 ASN   B OD1  1 
ATOM   5113 N ND2  . ASN   B 1 150 ? 35.110 -17.569 -16.295 1.00 17.35 ?  150 ASN   B ND2  1 
ATOM   5114 H H    . ASN   B 1 150 ? 35.251 -17.631 -12.808 1.00 13.27 ?  150 ASN   B H    1 
ATOM   5115 H HA   . ASN   B 1 150 ? 35.204 -20.230 -13.489 1.00 13.67 ?  150 ASN   B HA   1 
ATOM   5116 H HB2  . ASN   B 1 150 ? 36.699 -18.073 -14.524 1.00 15.55 ?  150 ASN   B HB2  1 
ATOM   5117 H HB3  . ASN   B 1 150 ? 36.863 -19.559 -15.066 1.00 15.55 ?  150 ASN   B HB3  1 
ATOM   5118 H HD21 . ASN   B 1 150 ? 34.476 -17.396 -16.853 1.00 20.82 ?  150 ASN   B HD21 1 
ATOM   5119 H HD22 . ASN   B 1 150 ? 35.753 -17.004 -16.194 1.00 20.82 ?  150 ASN   B HD22 1 
ATOM   5120 N N    . VAL   B 1 151 ? 36.905 -21.161 -12.001 1.00 10.63 ?  151 VAL   B N    1 
ATOM   5121 C CA   . VAL   B 1 151 ? 37.925 -21.689 -11.110 1.00 10.68 ?  151 VAL   B CA   1 
ATOM   5122 C C    . VAL   B 1 151 ? 38.636 -22.857 -11.781 1.00 10.59 ?  151 VAL   B C    1 
ATOM   5123 O O    . VAL   B 1 151 ? 37.998 -23.794 -12.284 1.00 11.69 ?  151 VAL   B O    1 
ATOM   5124 C CB   . VAL   B 1 151 ? 37.367 -22.028 -9.714  1.00 12.01 ?  151 VAL   B CB   1 
ATOM   5125 C CG1  . VAL   B 1 151 ? 36.203 -23.022 -9.794  1.00 13.16 ?  151 VAL   B CG1  1 
ATOM   5126 C CG2  . VAL   B 1 151 ? 38.483 -22.525 -8.806  1.00 12.78 ?  151 VAL   B CG2  1 
ATOM   5127 H H    . VAL   B 1 151 ? 36.285 -21.726 -12.204 1.00 12.76 ?  151 VAL   B H    1 
ATOM   5128 H HA   . VAL   B 1 151 ? 38.590 -20.993 -10.981 1.00 12.82 ?  151 VAL   B HA   1 
ATOM   5129 H HB   . VAL   B 1 151 ? 37.024 -21.209 -9.321  1.00 14.42 ?  151 VAL   B HB   1 
ATOM   5130 H HG11 . VAL   B 1 151 ? 35.890 -23.213 -8.895  1.00 15.80 ?  151 VAL   B HG11 1 
ATOM   5131 H HG12 . VAL   B 1 151 ? 35.483 -22.626 -10.314 1.00 15.80 ?  151 VAL   B HG12 1 
ATOM   5132 H HG13 . VAL   B 1 151 ? 36.507 -23.837 -10.220 1.00 15.80 ?  151 VAL   B HG13 1 
ATOM   5133 H HG21 . VAL   B 1 151 ? 38.140 -22.596 -7.900  1.00 15.34 ?  151 VAL   B HG21 1 
ATOM   5134 H HG22 . VAL   B 1 151 ? 38.781 -23.395 -9.115  1.00 15.34 ?  151 VAL   B HG22 1 
ATOM   5135 H HG23 . VAL   B 1 151 ? 39.219 -21.893 -8.830  1.00 15.34 ?  151 VAL   B HG23 1 
ATOM   5136 N N    . TYR   B 1 152 ? 39.966 -22.765 -11.801 1.00 10.27 ?  152 TYR   B N    1 
ATOM   5137 C CA   . TYR   B 1 152 ? 40.868 -23.746 -12.385 1.00 10.65 ?  152 TYR   B CA   1 
ATOM   5138 C C    . TYR   B 1 152 ? 41.589 -24.424 -11.226 1.00 9.98  ?  152 TYR   B C    1 
ATOM   5139 O O    . TYR   B 1 152 ? 42.434 -23.810 -10.567 1.00 10.45 ?  152 TYR   B O    1 
ATOM   5140 C CB   . TYR   B 1 152 ? 41.838 -23.039 -13.335 1.00 11.25 ?  152 TYR   B CB   1 
ATOM   5141 C CG   . TYR   B 1 152 ? 41.158 -22.581 -14.601 1.00 11.55 ?  152 TYR   B CG   1 
ATOM   5142 C CD1  . TYR   B 1 152 ? 40.482 -21.365 -14.662 1.00 12.29 ?  152 TYR   B CD1  1 
ATOM   5143 C CD2  . TYR   B 1 152 ? 41.169 -23.383 -15.731 1.00 12.75 ?  152 TYR   B CD2  1 
ATOM   5144 C CE1  . TYR   B 1 152 ? 39.839 -20.968 -15.819 1.00 13.54 ?  152 TYR   B CE1  1 
ATOM   5145 C CE2  . TYR   B 1 152 ? 40.536 -22.997 -16.886 1.00 13.61 ?  152 TYR   B CE2  1 
ATOM   5146 C CZ   . TYR   B 1 152 ? 39.875 -21.787 -16.932 1.00 14.06 ?  152 TYR   B CZ   1 
ATOM   5147 O OH   . TYR   B 1 152 ? 39.245 -21.415 -18.094 1.00 16.34 ?  152 TYR   B OH   1 
ATOM   5148 H H    . TYR   B 1 152 ? 40.396 -22.101 -11.453 1.00 12.32 ?  152 TYR   B H    1 
ATOM   5149 H HA   . TYR   B 1 152 ? 40.364 -24.412 -12.882 1.00 12.79 ?  152 TYR   B HA   1 
ATOM   5150 H HB2  . TYR   B 1 152 ? 42.205 -22.261 -12.886 1.00 13.51 ?  152 TYR   B HB2  1 
ATOM   5151 H HB3  . TYR   B 1 152 ? 42.553 -23.650 -13.574 1.00 13.51 ?  152 TYR   B HB3  1 
ATOM   5152 H HD1  . TYR   B 1 152 ? 40.457 -20.816 -13.910 1.00 14.75 ?  152 TYR   B HD1  1 
ATOM   5153 H HD2  . TYR   B 1 152 ? 41.610 -24.204 -15.704 1.00 15.30 ?  152 TYR   B HD2  1 
ATOM   5154 H HE1  . TYR   B 1 152 ? 39.396 -20.154 -15.853 1.00 16.25 ?  152 TYR   B HE1  1 
ATOM   5155 H HE2  . TYR   B 1 152 ? 40.555 -23.548 -17.636 1.00 16.34 ?  152 TYR   B HE2  1 
ATOM   5156 H HH   . TYR   B 1 152 ? 38.882 -20.666 -17.993 1.00 19.61 ?  152 TYR   B HH   1 
ATOM   5157 N N    . LEU   B 1 153 ? 41.227 -25.681 -10.965 1.00 10.32 ?  153 LEU   B N    1 
ATOM   5158 C CA   . LEU   B 1 153 ? 41.727 -26.435 -9.825  1.00 9.97  ?  153 LEU   B CA   1 
ATOM   5159 C C    . LEU   B 1 153 ? 42.957 -27.237 -10.218 1.00 10.28 ?  153 LEU   B C    1 
ATOM   5160 O O    . LEU   B 1 153 ? 42.937 -27.970 -11.209 1.00 11.48 ?  153 LEU   B O    1 
ATOM   5161 C CB   . LEU   B 1 153 ? 40.644 -27.391 -9.322  1.00 10.82 ?  153 LEU   B CB   1 
ATOM   5162 C CG   . LEU   B 1 153 ? 39.391 -26.737 -8.744  1.00 11.26 ?  153 LEU   B CG   1 
ATOM   5163 C CD1  . LEU   B 1 153 ? 38.294 -27.778 -8.599  1.00 11.90 ?  153 LEU   B CD1  1 
ATOM   5164 C CD2  . LEU   B 1 153 ? 39.699 -26.092 -7.400  1.00 11.71 ?  153 LEU   B CD2  1 
ATOM   5165 H H    . LEU   B 1 153 ? 40.661 -26.127 -11.447 1.00 12.39 ?  153 LEU   B H    1 
ATOM   5166 H HA   . LEU   B 1 153 ? 41.955 -25.827 -9.112  1.00 11.96 ?  153 LEU   B HA   1 
ATOM   5167 H HB2  . LEU   B 1 153 ? 40.357 -27.954 -10.058 1.00 12.99 ?  153 LEU   B HB2  1 
ATOM   5168 H HB3  . LEU   B 1 153 ? 41.024 -27.947 -8.622  1.00 12.99 ?  153 LEU   B HB3  1 
ATOM   5169 H HG   . LEU   B 1 153 ? 39.078 -26.042 -9.346  1.00 13.51 ?  153 LEU   B HG   1 
ATOM   5170 H HD11 . LEU   B 1 153 ? 37.493 -27.342 -8.265  1.00 14.29 ?  153 LEU   B HD11 1 
ATOM   5171 H HD12 . LEU   B 1 153 ? 38.123 -28.170 -9.465  1.00 14.29 ?  153 LEU   B HD12 1 
ATOM   5172 H HD13 . LEU   B 1 153 ? 38.589 -28.454 -7.973  1.00 14.29 ?  153 LEU   B HD13 1 
ATOM   5173 H HD21 . LEU   B 1 153 ? 38.885 -25.723 -7.027  1.00 14.05 ?  153 LEU   B HD21 1 
ATOM   5174 H HD22 . LEU   B 1 153 ? 40.061 -26.768 -6.802  1.00 14.05 ?  153 LEU   B HD22 1 
ATOM   5175 H HD23 . LEU   B 1 153 ? 40.354 -25.386 -7.529  1.00 14.05 ?  153 LEU   B HD23 1 
ATOM   5176 N N    . ALA   B 1 154 ? 44.010 -27.128 -9.416  1.00 10.36 ?  154 ALA   B N    1 
ATOM   5177 C CA   . ALA   B 1 154 ? 45.239 -27.886 -9.604  1.00 11.37 ?  154 ALA   B CA   1 
ATOM   5178 C C    . ALA   B 1 154 ? 45.310 -28.963 -8.530  1.00 11.98 ?  154 ALA   B C    1 
ATOM   5179 O O    . ALA   B 1 154 ? 45.226 -28.666 -7.332  1.00 13.52 ?  154 ALA   B O    1 
ATOM   5180 C CB   . ALA   B 1 154 ? 46.461 -26.970 -9.538  1.00 12.71 ?  154 ALA   B CB   1 
ATOM   5181 H H    . ALA   B 1 154 ? 44.031 -26.600 -8.734  1.00 12.44 ?  154 ALA   B H    1 
ATOM   5182 H HA   . ALA   B 1 154 ? 45.225 -28.313 -10.469 1.00 13.65 ?  154 ALA   B HA   1 
ATOM   5183 H HB1  . ALA   B 1 154 ? 47.262 -27.502 -9.664  1.00 15.25 ?  154 ALA   B HB1  1 
ATOM   5184 H HB2  . ALA   B 1 154 ? 46.396 -26.300 -10.238 1.00 15.25 ?  154 ALA   B HB2  1 
ATOM   5185 H HB3  . ALA   B 1 154 ? 46.489 -26.534 -8.669  1.00 15.25 ?  154 ALA   B HB3  1 
ATOM   5186 N N    . VAL   B 1 155 ? 45.439 -30.210 -8.963  1.00 11.50 ?  155 VAL   B N    1 
ATOM   5187 C CA   . VAL   B 1 155 ? 45.541 -31.356 -8.071  1.00 11.62 ?  155 VAL   B CA   1 
ATOM   5188 C C    . VAL   B 1 155 ? 46.881 -32.024 -8.350  1.00 11.66 ?  155 VAL   B C    1 
ATOM   5189 O O    . VAL   B 1 155 ? 47.118 -32.513 -9.462  1.00 13.19 ?  155 VAL   B O    1 
ATOM   5190 C CB   . VAL   B 1 155 ? 44.385 -32.350 -8.277  1.00 13.05 ?  155 VAL   B CB   1 
ATOM   5191 C CG1  . VAL   B 1 155 ? 44.561 -33.556 -7.367  1.00 13.15 ?  155 VAL   B CG1  1 
ATOM   5192 C CG2  . VAL   B 1 155 ? 43.043 -31.672 -8.020  1.00 13.98 ?  155 VAL   B CG2  1 
ATOM   5193 H H    . VAL   B 1 155 ? 45.473 -30.422 -9.796  1.00 13.80 ?  155 VAL   B H    1 
ATOM   5194 H HA   . VAL   B 1 155 ? 45.528 -31.059 -7.148  1.00 13.95 ?  155 VAL   B HA   1 
ATOM   5195 H HB   . VAL   B 1 155 ? 44.392 -32.661 -9.197  1.00 15.66 ?  155 VAL   B HB   1 
ATOM   5196 H HG11 . VAL   B 1 155 ? 43.734 -34.062 -7.346  1.00 15.78 ?  155 VAL   B HG11 1 
ATOM   5197 H HG12 . VAL   B 1 155 ? 45.278 -34.115 -7.711  1.00 15.78 ?  155 VAL   B HG12 1 
ATOM   5198 H HG13 . VAL   B 1 155 ? 44.783 -33.249 -6.473  1.00 15.78 ?  155 VAL   B HG13 1 
ATOM   5199 H HG21 . VAL   B 1 155 ? 42.334 -32.326 -8.122  1.00 16.78 ?  155 VAL   B HG21 1 
ATOM   5200 H HG22 . VAL   B 1 155 ? 43.038 -31.318 -7.116  1.00 16.78 ?  155 VAL   B HG22 1 
ATOM   5201 H HG23 . VAL   B 1 155 ? 42.924 -30.952 -8.658  1.00 16.78 ?  155 VAL   B HG23 1 
ATOM   5202 N N    . PHE   B 1 156 ? 47.745 -32.069 -7.334  1.00 12.16 ?  156 PHE   B N    1 
ATOM   5203 C CA   . PHE   B 1 156 ? 49.126 -32.516 -7.534  1.00 13.15 ?  156 PHE   B CA   1 
ATOM   5204 C C    . PHE   B 1 156 ? 49.230 -34.014 -7.817  1.00 13.98 ?  156 PHE   B C    1 
ATOM   5205 O O    . PHE   B 1 156 ? 49.969 -34.437 -8.719  1.00 15.72 ?  156 PHE   B O    1 
ATOM   5206 C CB   . PHE   B 1 156 ? 49.949 -32.146 -6.302  1.00 13.17 ?  156 PHE   B CB   1 
ATOM   5207 C CG   . PHE   B 1 156 ? 51.370 -32.611 -6.357  1.00 13.81 ?  156 PHE   B CG   1 
ATOM   5208 C CD1  . PHE   B 1 156 ? 52.252 -32.065 -7.267  1.00 15.74 ?  156 PHE   B CD1  1 
ATOM   5209 C CD2  . PHE   B 1 156 ? 51.826 -33.581 -5.487  1.00 14.37 ?  156 PHE   B CD2  1 
ATOM   5210 C CE1  . PHE   B 1 156 ? 53.570 -32.476 -7.316  1.00 16.81 ?  156 PHE   B CE1  1 
ATOM   5211 C CE2  . PHE   B 1 156 ? 53.142 -34.001 -5.531  1.00 15.87 ?  156 PHE   B CE2  1 
ATOM   5212 C CZ   . PHE   B 1 156 ? 54.011 -33.448 -6.450  1.00 16.49 ?  156 PHE   B CZ   1 
ATOM   5213 H H    . PHE   B 1 156 ? 47.558 -31.845 -6.523  1.00 14.60 ?  156 PHE   B H    1 
ATOM   5214 H HA   . PHE   B 1 156 ? 49.498 -32.043 -8.290  1.00 15.78 ?  156 PHE   B HA   1 
ATOM   5215 H HB2  . PHE   B 1 156 ? 49.960 -31.180 -6.212  1.00 15.81 ?  156 PHE   B HB2  1 
ATOM   5216 H HB3  . PHE   B 1 156 ? 49.540 -32.544 -5.518  1.00 15.81 ?  156 PHE   B HB3  1 
ATOM   5217 H HD1  . PHE   B 1 156 ? 51.960 -31.403 -7.853  1.00 18.89 ?  156 PHE   B HD1  1 
ATOM   5218 H HD2  . PHE   B 1 156 ? 51.239 -33.960 -4.869  1.00 17.25 ?  156 PHE   B HD2  1 
ATOM   5219 H HE1  . PHE   B 1 156 ? 54.155 -32.100 -7.936  1.00 20.17 ?  156 PHE   B HE1  1 
ATOM   5220 H HE2  . PHE   B 1 156 ? 53.437 -34.664 -4.946  1.00 19.05 ?  156 PHE   B HE2  1 
ATOM   5221 H HZ   . PHE   B 1 156 ? 54.895 -33.734 -6.481  1.00 19.79 ?  156 PHE   B HZ   1 
ATOM   5222 N N    . ASP   B 1 157 ? 48.553 -34.836 -7.026  1.00 14.21 ?  157 ASP   B N    1 
ATOM   5223 C CA   . ASP   B 1 157 ? 48.700 -36.284 -7.121  1.00 15.47 ?  157 ASP   B CA   1 
ATOM   5224 C C    . ASP   B 1 157 ? 47.788 -36.826 -8.217  1.00 15.41 ?  157 ASP   B C    1 
ATOM   5225 O O    . ASP   B 1 157 ? 46.562 -36.707 -8.124  1.00 14.76 ?  157 ASP   B O    1 
ATOM   5226 C CB   . ASP   B 1 157 ? 48.336 -36.897 -5.775  1.00 17.14 ?  157 ASP   B CB   1 
ATOM   5227 C CG   . ASP   B 1 157 ? 48.480 -38.405 -5.755  1.00 19.03 ?  157 ASP   B CG   1 
ATOM   5228 O OD1  . ASP   B 1 157 ? 48.822 -39.008 -6.798  1.00 19.39 ?  157 ASP   B OD1  1 
ATOM   5229 O OD2  . ASP   B 1 157 ? 48.264 -38.990 -4.674  1.00 21.15 -1 157 ASP   B OD2  1 
ATOM   5230 H H    . ASP   B 1 157 ? 47.999 -34.582 -6.423  1.00 17.06 ?  157 ASP   B H    1 
ATOM   5231 H HA   . ASP   B 1 157 ? 49.622 -36.513 -7.334  1.00 18.56 ?  157 ASP   B HA   1 
ATOM   5232 H HB2  . ASP   B 1 157 ? 48.911 -36.519 -5.093  1.00 20.57 ?  157 ASP   B HB2  1 
ATOM   5233 H HB3  . ASP   B 1 157 ? 47.409 -36.686 -5.578  1.00 20.57 ?  157 ASP   B HB3  1 
ATOM   5234 N N    . LYS   B 1 158 ? 48.389 -37.449 -9.239  1.00 16.46 ?  158 LYS   B N    1 
ATOM   5235 C CA   . LYS   B 1 158 ? 47.617 -38.054 -10.326 1.00 17.37 ?  158 LYS   B CA   1 
ATOM   5236 C C    . LYS   B 1 158 ? 46.559 -39.021 -9.803  1.00 16.97 ?  158 LYS   B C    1 
ATOM   5237 O O    . LYS   B 1 158 ? 45.459 -39.113 -10.361 1.00 17.23 ?  158 LYS   B O    1 
ATOM   5238 C CB   . LYS   B 1 158 ? 48.567 -38.769 -11.295 1.00 18.76 ?  158 LYS   B CB   1 
ATOM   5239 C CG   . LYS   B 1 158 ? 47.890 -39.664 -12.326 1.00 20.71 ?  158 LYS   B CG   1 
ATOM   5240 C CD   . LYS   B 1 158 ? 47.048 -38.875 -13.305 1.00 23.12 ?  158 LYS   B CD   1 
ATOM   5241 C CE   . LYS   B 1 158 ? 46.427 -39.788 -14.349 1.00 24.91 ?  158 LYS   B CE   1 
ATOM   5242 N NZ   . LYS   B 1 158 ? 45.386 -39.086 -15.154 1.00 25.04 ?  158 LYS   B NZ   1 
ATOM   5243 H H    . LYS   B 1 158 ? 49.243 -37.537 -9.325  1.00 19.76 ?  158 LYS   B H    1 
ATOM   5244 H HA   . LYS   B 1 158 ? 47.166 -37.352 -10.821 1.00 20.85 ?  158 LYS   B HA   1 
ATOM   5245 H HB2  . LYS   B 1 158 ? 49.073 -38.099 -11.787 1.00 22.52 ?  158 LYS   B HB2  1 
ATOM   5246 H HB3  . LYS   B 1 158 ? 49.176 -39.322 -10.785 1.00 22.52 ?  158 LYS   B HB3  1 
ATOM   5247 H HG2  . LYS   B 1 158 ? 48.575 -40.128 -12.833 1.00 24.86 ?  158 LYS   B HG2  1 
ATOM   5248 H HG3  . LYS   B 1 158 ? 47.321 -40.314 -11.883 1.00 24.86 ?  158 LYS   B HG3  1 
ATOM   5249 H HD2  . LYS   B 1 158 ? 46.334 -38.426 -12.827 1.00 27.74 ?  158 LYS   B HD2  1 
ATOM   5250 H HD3  . LYS   B 1 158 ? 47.608 -38.228 -13.761 1.00 27.74 ?  158 LYS   B HD3  1 
ATOM   5251 H HE2  . LYS   B 1 158 ? 47.117 -40.100 -14.953 1.00 29.89 ?  158 LYS   B HE2  1 
ATOM   5252 H HE3  . LYS   B 1 158 ? 46.007 -40.543 -13.904 1.00 29.89 ?  158 LYS   B HE3  1 
ATOM   5253 H HZ1  . LYS   B 1 158 ? 45.037 -39.642 -15.755 1.00 30.05 ?  158 LYS   B HZ1  1 
ATOM   5254 H HZ2  . LYS   B 1 158 ? 44.735 -38.792 -14.622 1.00 30.05 ?  158 LYS   B HZ2  1 
ATOM   5255 H HZ3  . LYS   B 1 158 ? 45.747 -38.391 -15.578 1.00 30.05 ?  158 LYS   B HZ3  1 
ATOM   5256 N N    . ASN   B 1 159 ? 46.876 -39.777 -8.751  1.00 17.40 ?  159 ASN   B N    1 
ATOM   5257 C CA   . ASN   B 1 159 ? 45.919 -40.760 -8.253  1.00 18.08 ?  159 ASN   B CA   1 
ATOM   5258 C C    . ASN   B 1 159 ? 44.722 -40.094 -7.577  1.00 17.19 ?  159 ASN   B C    1 
ATOM   5259 O O    . ASN   B 1 159 ? 43.592 -40.588 -7.699  1.00 17.38 ?  159 ASN   B O    1 
ATOM   5260 C CB   . ASN   B 1 159 ? 46.617 -41.755 -7.330  1.00 19.73 ?  159 ASN   B CB   1 
ATOM   5261 C CG   . ASN   B 1 159 ? 47.665 -42.572 -8.054  1.00 21.78 ?  159 ASN   B CG   1 
ATOM   5262 O OD1  . ASN   B 1 159 ? 47.424 -43.075 -9.155  1.00 22.41 ?  159 ASN   B OD1  1 
ATOM   5263 N ND2  . ASN   B 1 159 ? 48.838 -42.699 -7.450  1.00 22.62 ?  159 ASN   B ND2  1 
ATOM   5264 H H    . ASN   B 1 159 ? 47.613 -39.734 -8.320  1.00 20.89 ?  159 ASN   B H    1 
ATOM   5265 H HA   . ASN   B 1 159 ? 45.577 -41.258 -9.011  1.00 21.70 ?  159 ASN   B HA   1 
ATOM   5266 H HB2  . ASN   B 1 159 ? 47.054 -41.273 -6.614  1.00 23.68 ?  159 ASN   B HB2  1 
ATOM   5267 H HB3  . ASN   B 1 159 ? 45.957 -42.368 -6.971  1.00 23.68 ?  159 ASN   B HB3  1 
ATOM   5268 H HD21 . ASN   B 1 159 ? 49.469 -43.155 -7.823  1.00 27.14 ?  159 ASN   B HD21 1 
ATOM   5269 H HD22 . ASN   B 1 159 ? 48.969 -42.340 -6.681  1.00 27.14 ?  159 ASN   B HD22 1 
ATOM   5270 N N    . LEU   B 1 160 ? 44.931 -38.964 -6.889  1.00 16.32 ?  160 LEU   B N    1 
ATOM   5271 C CA   . LEU   B 1 160 ? 43.796 -38.231 -6.341  1.00 15.23 ?  160 LEU   B CA   1 
ATOM   5272 C C    . LEU   B 1 160 ? 43.002 -37.563 -7.452  1.00 14.63 ?  160 LEU   B C    1 
ATOM   5273 O O    . LEU   B 1 160 ? 41.764 -37.576 -7.438  1.00 14.00 ?  160 LEU   B O    1 
ATOM   5274 C CB   . LEU   B 1 160 ? 44.265 -37.202 -5.312  1.00 14.63 ?  160 LEU   B CB   1 
ATOM   5275 C CG   . LEU   B 1 160 ? 43.140 -36.313 -4.764  1.00 14.40 ?  160 LEU   B CG   1 
ATOM   5276 C CD1  . LEU   B 1 160 ? 42.024 -37.141 -4.140  1.00 15.25 ?  160 LEU   B CD1  1 
ATOM   5277 C CD2  . LEU   B 1 160 ? 43.680 -35.318 -3.753  1.00 14.83 ?  160 LEU   B CD2  1 
ATOM   5278 H H    . LEU   B 1 160 ? 45.703 -38.610 -6.736  1.00 19.59 ?  160 LEU   B H    1 
ATOM   5279 H HA   . LEU   B 1 160 ? 43.211 -38.857 -5.894  1.00 18.28 ?  160 LEU   B HA   1 
ATOM   5280 H HB2  . LEU   B 1 160 ? 44.669 -37.674 -4.564  1.00 17.56 ?  160 LEU   B HB2  1 
ATOM   5281 H HB3  . LEU   B 1 160 ? 44.929 -36.625 -5.727  1.00 17.56 ?  160 LEU   B HB3  1 
ATOM   5282 H HG   . LEU   B 1 160 ? 42.758 -35.805 -5.494  1.00 17.29 ?  160 LEU   B HG   1 
ATOM   5283 H HD11 . LEU   B 1 160 ? 41.393 -36.543 -3.712  1.00 18.31 ?  160 LEU   B HD11 1 
ATOM   5284 H HD12 . LEU   B 1 160 ? 41.579 -37.650 -4.836  1.00 18.31 ?  160 LEU   B HD12 1 
ATOM   5285 H HD13 . LEU   B 1 160 ? 42.407 -37.744 -3.482  1.00 18.31 ?  160 LEU   B HD13 1 
ATOM   5286 H HD21 . LEU   B 1 160 ? 42.954 -34.747 -3.455  1.00 17.80 ?  160 LEU   B HD21 1 
ATOM   5287 H HD22 . LEU   B 1 160 ? 44.050 -35.801 -2.998  1.00 17.80 ?  160 LEU   B HD22 1 
ATOM   5288 H HD23 . LEU   B 1 160 ? 44.370 -34.781 -4.173  1.00 17.80 ?  160 LEU   B HD23 1 
ATOM   5289 N N    . TYR   B 1 161 ? 43.701 -36.991 -8.434  1.00 14.71 ?  161 TYR   B N    1 
ATOM   5290 C CA   . TYR   B 1 161 ? 43.031 -36.424 -9.598  1.00 14.42 ?  161 TYR   B CA   1 
ATOM   5291 C C    . TYR   B 1 161 ? 42.089 -37.446 -10.227 1.00 14.13 ?  161 TYR   B C    1 
ATOM   5292 O O    . TYR   B 1 161 ? 40.918 -37.151 -10.491 1.00 13.86 ?  161 TYR   B O    1 
ATOM   5293 C CB   . TYR   B 1 161 ? 44.077 -35.945 -10.610 1.00 14.84 ?  161 TYR   B CB   1 
ATOM   5294 C CG   . TYR   B 1 161 ? 43.500 -35.476 -11.921 1.00 15.24 ?  161 TYR   B CG   1 
ATOM   5295 C CD1  . TYR   B 1 161 ? 43.093 -34.160 -12.083 1.00 15.16 ?  161 TYR   B CD1  1 
ATOM   5296 C CD2  . TYR   B 1 161 ? 43.348 -36.346 -12.994 1.00 16.13 ?  161 TYR   B CD2  1 
ATOM   5297 C CE1  . TYR   B 1 161 ? 42.559 -33.721 -13.270 1.00 16.28 ?  161 TYR   B CE1  1 
ATOM   5298 C CE2  . TYR   B 1 161 ? 42.809 -35.916 -14.187 1.00 17.14 ?  161 TYR   B CE2  1 
ATOM   5299 C CZ   . TYR   B 1 161 ? 42.417 -34.602 -14.320 1.00 17.18 ?  161 TYR   B CZ   1 
ATOM   5300 O OH   . TYR   B 1 161 ? 41.878 -34.154 -15.502 1.00 19.13 ?  161 TYR   B OH   1 
ATOM   5301 H H    . TYR   B 1 161 ? 44.560 -36.930 -8.455  1.00 17.66 ?  161 TYR   B H    1 
ATOM   5302 H HA   . TYR   B 1 161 ? 42.507 -35.661 -9.322  1.00 17.30 ?  161 TYR   B HA   1 
ATOM   5303 H HB2  . TYR   B 1 161 ? 44.569 -35.201 -10.221 1.00 17.82 ?  161 TYR   B HB2  1 
ATOM   5304 H HB3  . TYR   B 1 161 ? 44.689 -36.672 -10.802 1.00 17.82 ?  161 TYR   B HB3  1 
ATOM   5305 H HD1  . TYR   B 1 161 ? 43.190 -33.557 -11.377 1.00 18.20 ?  161 TYR   B HD1  1 
ATOM   5306 H HD2  . TYR   B 1 161 ? 43.610 -37.232 -12.907 1.00 19.36 ?  161 TYR   B HD2  1 
ATOM   5307 H HE1  . TYR   B 1 161 ? 42.295 -32.830 -13.361 1.00 19.54 ?  161 TYR   B HE1  1 
ATOM   5308 H HE2  . TYR   B 1 161 ? 42.712 -36.504 -14.899 1.00 20.57 ?  161 TYR   B HE2  1 
ATOM   5309 H HH   . TYR   B 1 161 ? 41.847 -34.784 -16.057 1.00 22.95 ?  161 TYR   B HH   1 
ATOM   5310 N N    . ASP   B 1 162 ? 42.588 -38.664 -10.459 1.00 14.59 ?  162 ASP   B N    1 
ATOM   5311 C CA   . ASP   B 1 162 ? 41.763 -39.702 -11.069 1.00 15.24 ?  162 ASP   B CA   1 
ATOM   5312 C C    . ASP   B 1 162 ? 40.556 -40.038 -10.200 1.00 14.81 ?  162 ASP   B C    1 
ATOM   5313 O O    . ASP   B 1 162 ? 39.451 -40.251 -10.716 1.00 15.14 ?  162 ASP   B O    1 
ATOM   5314 C CB   . ASP   B 1 162 ? 42.597 -40.963 -11.317 1.00 16.92 ?  162 ASP   B CB   1 
ATOM   5315 C CG   . ASP   B 1 162 ? 43.593 -40.804 -12.453 1.00 18.06 ?  162 ASP   B CG   1 
ATOM   5316 O OD1  . ASP   B 1 162 ? 43.454 -39.856 -13.251 1.00 18.34 ?  162 ASP   B OD1  1 
ATOM   5317 O OD2  . ASP   B 1 162 ? 44.503 -41.653 -12.558 1.00 19.96 -1 162 ASP   B OD2  1 
ATOM   5318 H H    . ASP   B 1 162 ? 43.391 -38.909 -10.272 1.00 17.52 ?  162 ASP   B H    1 
ATOM   5319 H HA   . ASP   B 1 162 ? 41.437 -39.384 -11.923 1.00 18.29 ?  162 ASP   B HA   1 
ATOM   5320 H HB2  . ASP   B 1 162 ? 43.100 -41.171 -10.515 1.00 20.31 ?  162 ASP   B HB2  1 
ATOM   5321 H HB3  . ASP   B 1 162 ? 42.005 -41.694 -11.541 1.00 20.31 ?  162 ASP   B HB3  1 
ATOM   5322 N N    . LYS   B 1 163 ? 40.746 -40.114 -8.882  1.00 14.60 ?  163 LYS   B N    1 
ATOM   5323 C CA   . LYS   B 1 163 ? 39.621 -40.397 -7.997  1.00 15.15 ?  163 LYS   B CA   1 
ATOM   5324 C C    . LYS   B 1 163 ? 38.576 -39.290 -8.059  1.00 13.74 ?  163 LYS   B C    1 
ATOM   5325 O O    . LYS   B 1 163 ? 37.368 -39.560 -8.066  1.00 14.92 ?  163 LYS   B O    1 
ATOM   5326 C CB   . LYS   B 1 163 ? 40.107 -40.588 -6.562  1.00 18.13 ?  163 LYS   B CB   1 
ATOM   5327 C CG   . LYS   B 1 163 ? 39.013 -41.085 -5.639  1.00 24.31 ?  163 LYS   B CG   1 
ATOM   5328 C CD   . LYS   B 1 163 ? 39.485 -41.273 -4.212  1.00 30.45 ?  163 LYS   B CD   1 
ATOM   5329 C CE   . LYS   B 1 163 ? 38.401 -41.953 -3.385  1.00 34.73 ?  163 LYS   B CE   1 
ATOM   5330 N NZ   . LYS   B 1 163 ? 38.504 -41.640 -1.934  1.00 37.42 ?  163 LYS   B NZ   1 
ATOM   5331 H H    . LYS   B 1 163 ? 41.504 -40.005 -8.487  1.00 17.52 ?  163 LYS   B H    1 
ATOM   5332 H HA   . LYS   B 1 163 ? 39.201 -41.220 -8.283  1.00 18.18 ?  163 LYS   B HA   1 
ATOM   5333 H HB2  . LYS   B 1 163 ? 40.826 -41.240 -6.556  1.00 21.76 ?  163 LYS   B HB2  1 
ATOM   5334 H HB3  . LYS   B 1 163 ? 40.427 -39.739 -6.220  1.00 21.76 ?  163 LYS   B HB3  1 
ATOM   5335 H HG2  . LYS   B 1 163 ? 38.288 -40.442 -5.631  1.00 29.17 ?  163 LYS   B HG2  1 
ATOM   5336 H HG3  . LYS   B 1 163 ? 38.692 -41.942 -5.964  1.00 29.17 ?  163 LYS   B HG3  1 
ATOM   5337 H HD2  . LYS   B 1 163 ? 40.276 -41.835 -4.203  1.00 36.55 ?  163 LYS   B HD2  1 
ATOM   5338 H HD3  . LYS   B 1 163 ? 39.677 -40.409 -3.817  1.00 36.55 ?  163 LYS   B HD3  1 
ATOM   5339 H HE2  . LYS   B 1 163 ? 37.530 -41.664 -3.700  1.00 41.68 ?  163 LYS   B HE2  1 
ATOM   5340 H HE3  . LYS   B 1 163 ? 38.484 -42.914 -3.490  1.00 41.68 ?  163 LYS   B HE3  1 
ATOM   5341 H HZ1  . LYS   B 1 163 ? 37.854 -42.054 -1.488  1.00 44.91 ?  163 LYS   B HZ1  1 
ATOM   5342 H HZ2  . LYS   B 1 163 ? 39.290 -41.912 -1.620  1.00 44.91 ?  163 LYS   B HZ2  1 
ATOM   5343 H HZ3  . LYS   B 1 163 ? 38.428 -40.762 -1.807  1.00 44.91 ?  163 LYS   B HZ3  1 
ATOM   5344 N N    . LEU   B 1 164 ? 39.027 -38.035 -8.108  1.00 12.65 ?  164 LEU   B N    1 
ATOM   5345 C CA   . LEU   B 1 164 ? 38.115 -36.897 -8.153  1.00 12.22 ?  164 LEU   B CA   1 
ATOM   5346 C C    . LEU   B 1 164 ? 37.327 -36.873 -9.457  1.00 12.50 ?  164 LEU   B C    1 
ATOM   5347 O O    . LEU   B 1 164 ? 36.106 -36.676 -9.454  1.00 13.74 ?  164 LEU   B O    1 
ATOM   5348 C CB   . LEU   B 1 164 ? 38.912 -35.603 -7.991  1.00 12.11 ?  164 LEU   B CB   1 
ATOM   5349 C CG   . LEU   B 1 164 ? 39.450 -35.330 -6.592  1.00 12.85 ?  164 LEU   B CG   1 
ATOM   5350 C CD1  . LEU   B 1 164 ? 40.538 -34.267 -6.655  1.00 13.10 ?  164 LEU   B CD1  1 
ATOM   5351 C CD2  . LEU   B 1 164 ? 38.340 -34.898 -5.661  1.00 14.64 ?  164 LEU   B CD2  1 
ATOM   5352 H H    . LEU   B 1 164 ? 39.862 -37.815 -8.118  1.00 15.18 ?  164 LEU   B H    1 
ATOM   5353 H HA   . LEU   B 1 164 ? 37.489 -36.963 -7.421  1.00 14.66 ?  164 LEU   B HA   1 
ATOM   5354 H HB2  . LEU   B 1 164 ? 39.673 -35.633 -8.595  1.00 14.53 ?  164 LEU   B HB2  1 
ATOM   5355 H HB3  . LEU   B 1 164 ? 38.340 -34.859 -8.233  1.00 14.53 ?  164 LEU   B HB3  1 
ATOM   5356 H HG   . LEU   B 1 164 ? 39.848 -36.138 -6.241  1.00 15.43 ?  164 LEU   B HG   1 
ATOM   5357 H HD11 . LEU   B 1 164 ? 40.867 -34.093 -5.758  1.00 15.73 ?  164 LEU   B HD11 1 
ATOM   5358 H HD12 . LEU   B 1 164 ? 41.268 -34.589 -7.213  1.00 15.73 ?  164 LEU   B HD12 1 
ATOM   5359 H HD13 . LEU   B 1 164 ? 40.171 -33.453 -7.035  1.00 15.73 ?  164 LEU   B HD13 1 
ATOM   5360 H HD21 . LEU   B 1 164 ? 38.719 -34.672 -4.799  1.00 17.57 ?  164 LEU   B HD21 1 
ATOM   5361 H HD22 . LEU   B 1 164 ? 37.890 -34.126 -6.039  1.00 17.57 ?  164 LEU   B HD22 1 
ATOM   5362 H HD23 . LEU   B 1 164 ? 37.711 -35.632 -5.565  1.00 17.57 ?  164 LEU   B HD23 1 
ATOM   5363 N N    . VAL   B 1 165 ? 38.014 -37.040 -10.587 1.00 13.74 ?  165 VAL   B N    1 
ATOM   5364 C CA   . VAL   B 1 165 ? 37.352 -36.974 -11.886 1.00 14.83 ?  165 VAL   B CA   1 
ATOM   5365 C C    . VAL   B 1 165 ? 36.434 -38.173 -12.073 1.00 16.30 ?  165 VAL   B C    1 
ATOM   5366 O O    . VAL   B 1 165 ? 35.275 -38.035 -12.483 1.00 17.14 ?  165 VAL   B O    1 
ATOM   5367 C CB   . VAL   B 1 165 ? 38.395 -36.885 -13.015 1.00 15.88 ?  165 VAL   B CB   1 
ATOM   5368 C CG1  . VAL   B 1 165 ? 37.725 -36.991 -14.369 1.00 17.19 ?  165 VAL   B CG1  1 
ATOM   5369 C CG2  . VAL   B 1 165 ? 39.192 -35.599 -12.904 1.00 15.98 ?  165 VAL   B CG2  1 
ATOM   5370 H H    . VAL   B 1 165 ? 38.860 -37.183 -10.628 1.00 16.49 ?  165 VAL   B H    1 
ATOM   5371 H HA   . VAL   B 1 165 ? 36.806 -36.176 -11.925 1.00 17.80 ?  165 VAL   B HA   1 
ATOM   5372 H HB   . VAL   B 1 165 ? 39.017 -37.623 -12.929 1.00 19.05 ?  165 VAL   B HB   1 
ATOM   5373 H HG11 . VAL   B 1 165 ? 38.342 -36.688 -15.050 1.00 20.63 ?  165 VAL   B HG11 1 
ATOM   5374 H HG12 . VAL   B 1 165 ? 37.488 -37.919 -14.529 1.00 20.63 ?  165 VAL   B HG12 1 
ATOM   5375 H HG13 . VAL   B 1 165 ? 36.929 -36.440 -14.371 1.00 20.63 ?  165 VAL   B HG13 1 
ATOM   5376 H HG21 . VAL   B 1 165 ? 39.825 -35.552 -13.639 1.00 19.18 ?  165 VAL   B HG21 1 
ATOM   5377 H HG22 . VAL   B 1 165 ? 38.583 -34.843 -12.946 1.00 19.18 ?  165 VAL   B HG22 1 
ATOM   5378 H HG23 . VAL   B 1 165 ? 39.668 -35.590 -12.058 1.00 19.18 ?  165 VAL   B HG23 1 
ATOM   5379 N N    . SER   B 1 166 ? 36.945 -39.370 -11.771 1.00 17.12 ?  166 SER   B N    1 
ATOM   5380 C CA   . SER   B 1 166 ? 36.193 -40.584 -12.052 1.00 18.36 ?  166 SER   B CA   1 
ATOM   5381 C C    . SER   B 1 166 ? 34.937 -40.676 -11.198 1.00 18.78 ?  166 SER   B C    1 
ATOM   5382 O O    . SER   B 1 166 ? 33.965 -41.301 -11.619 1.00 20.27 ?  166 SER   B O    1 
ATOM   5383 C CB   . SER   B 1 166 ? 37.067 -41.832 -11.883 1.00 19.29 ?  166 SER   B CB   1 
ATOM   5384 O OG   . SER   B 1 166 ? 37.428 -42.047 -10.530 1.00 19.47 ?  166 SER   B OG   1 
ATOM   5385 H H    . SER   B 1 166 ? 37.718 -39.503 -11.411 1.00 20.55 ?  166 SER   B H    1 
ATOM   5386 H HA   . SER   B 1 166 ? 35.910 -40.561 -12.978 1.00 22.03 ?  166 SER   B HA   1 
ATOM   5387 H HB2  . SER   B 1 166 ? 36.573 -42.606 -12.202 1.00 23.16 ?  166 SER   B HB2  1 
ATOM   5388 H HB3  . SER   B 1 166 ? 37.875 -41.722 -12.412 1.00 23.16 ?  166 SER   B HB3  1 
ATOM   5389 H HG   . SER   B 1 166 ? 37.866 -41.391 -10.245 1.00 23.36 ?  166 SER   B HG   1 
ATOM   5390 N N    . SER   B 1 167 ? 34.922 -40.062 -10.016 1.00 17.62 ?  167 SER   B N    1 
ATOM   5391 C CA   . SER   B 1 167 ? 33.769 -40.121 -9.127  1.00 17.07 ?  167 SER   B CA   1 
ATOM   5392 C C    . SER   B 1 167 ? 32.852 -38.904 -9.231  1.00 16.92 ?  167 SER   B C    1 
ATOM   5393 O O    . SER   B 1 167 ? 31.776 -38.904 -8.621  1.00 17.03 ?  167 SER   B O    1 
ATOM   5394 C CB   . SER   B 1 167 ? 34.217 -40.298 -7.670  1.00 16.84 ?  167 SER   B CB   1 
ATOM   5395 O OG   . SER   B 1 167 ? 34.883 -39.140 -7.190  1.00 16.74 ?  167 SER   B OG   1 
ATOM   5396 H H    . SER   B 1 167 ? 35.577 -39.605 -9.707  1.00 21.15 ?  167 SER   B H    1 
ATOM   5397 H HA   . SER   B 1 167 ? 33.241 -40.902 -9.364  1.00 20.49 ?  167 SER   B HA   1 
ATOM   5398 H HB2  . SER   B 1 167 ? 33.432 -40.467 -7.121  1.00 20.21 ?  167 SER   B HB2  1 
ATOM   5399 H HB3  . SER   B 1 167 ? 34.819 -41.062 -7.618  1.00 20.21 ?  167 SER   B HB3  1 
ATOM   5400 H HG   . SER   B 1 167 ? 35.562 -38.995 -7.662  1.00 20.09 ?  167 SER   B HG   1 
ATOM   5401 N N    . PHE   B 1 168 ? 33.232 -37.874 -9.990  1.00 16.60 ?  168 PHE   B N    1 
ATOM   5402 C CA   . PHE   B 1 168 ? 32.404 -36.671 -10.054 1.00 16.34 ?  168 PHE   B CA   1 
ATOM   5403 C C    . PHE   B 1 168 ? 31.081 -36.930 -10.771 1.00 14.47 ?  168 PHE   B C    1 
ATOM   5404 O O    . PHE   B 1 168 ? 30.048 -36.332 -10.423 1.00 15.17 ?  168 PHE   B O    1 
ATOM   5405 C CB   . PHE   B 1 168 ? 33.164 -35.541 -10.745 1.00 16.81 ?  168 PHE   B CB   1 
ATOM   5406 C CG   . PHE   B 1 168 ? 32.369 -34.285 -10.862 1.00 16.99 ?  168 PHE   B CG   1 
ATOM   5407 C CD1  . PHE   B 1 168 ? 32.064 -33.544 -9.730  1.00 18.06 ?  168 PHE   B CD1  1 
ATOM   5408 C CD2  . PHE   B 1 168 ? 31.900 -33.853 -12.087 1.00 16.51 ?  168 PHE   B CD2  1 
ATOM   5409 C CE1  . PHE   B 1 168 ? 31.314 -32.389 -9.817  1.00 18.89 ?  168 PHE   B CE1  1 
ATOM   5410 C CE2  . PHE   B 1 168 ? 31.155 -32.687 -12.188 1.00 17.60 ?  168 PHE   B CE2  1 
ATOM   5411 C CZ   . PHE   B 1 168 ? 30.858 -31.956 -11.049 1.00 17.98 ?  168 PHE   B CZ   1 
ATOM   5412 H H    . PHE   B 1 168 ? 33.952 -37.846 -10.463 1.00 19.93 ?  168 PHE   B H    1 
ATOM   5413 H HA   . PHE   B 1 168 ? 32.201 -36.386 -9.153  1.00 19.61 ?  168 PHE   B HA   1 
ATOM   5414 H HB2  . PHE   B 1 168 ? 33.964 -35.340 -10.231 1.00 20.18 ?  168 PHE   B HB2  1 
ATOM   5415 H HB3  . PHE   B 1 168 ? 33.409 -35.822 -11.639 1.00 20.18 ?  168 PHE   B HB3  1 
ATOM   5416 H HD1  . PHE   B 1 168 ? 32.367 -33.835 -8.899  1.00 21.68 ?  168 PHE   B HD1  1 
ATOM   5417 H HD2  . PHE   B 1 168 ? 32.098 -34.339 -12.854 1.00 19.82 ?  168 PHE   B HD2  1 
ATOM   5418 H HE1  . PHE   B 1 168 ? 31.118 -31.901 -9.050  1.00 22.67 ?  168 PHE   B HE1  1 
ATOM   5419 H HE2  . PHE   B 1 168 ? 30.846 -32.402 -13.019 1.00 21.12 ?  168 PHE   B HE2  1 
ATOM   5420 H HZ   . PHE   B 1 168 ? 30.353 -31.177 -11.115 1.00 21.58 ?  168 PHE   B HZ   1 
ATOM   5421 N N    . LEU   B 1 169 ? 31.095 -37.816 -11.762 1.00 15.08 ?  169 LEU   B N    1 
ATOM   5422 C CA   . LEU   B 1 169 ? 29.912 -38.111 -12.555 1.00 17.72 ?  169 LEU   B CA   1 
ATOM   5423 C C    . LEU   B 1 169 ? 29.911 -39.548 -13.059 1.00 20.50 ?  169 LEU   B C    1 
ATOM   5424 O O    . LEU   B 1 169 ? 29.017 -39.964 -13.797 1.00 22.73 ?  169 LEU   B O    1 
ATOM   5425 C CB   . LEU   B 1 169 ? 29.832 -37.155 -13.744 1.00 19.50 ?  169 LEU   B CB   1 
ATOM   5426 C CG   . LEU   B 1 169 ? 28.567 -36.303 -13.831 1.00 22.29 ?  169 LEU   B CG   1 
ATOM   5427 C CD1  . LEU   B 1 169 ? 28.530 -35.567 -15.157 1.00 23.38 ?  169 LEU   B CD1  1 
ATOM   5428 C CD2  . LEU   B 1 169 ? 27.322 -37.152 -13.648 1.00 22.62 ?  169 LEU   B CD2  1 
ATOM   5429 O OXT  . LEU   B 1 169 ? 30.812 -40.319 -12.745 1.00 21.22 -1 169 LEU   B OXT  1 
ATOM   5430 H H    . LEU   B 1 169 ? 31.792 -38.266 -12.000 1.00 18.10 ?  169 LEU   B H    1 
ATOM   5431 H HA   . LEU   B 1 169 ? 29.130 -37.985 -12.001 1.00 21.27 ?  169 LEU   B HA   1 
ATOM   5432 H HB2  . LEU   B 1 169 ? 30.586 -36.545 -13.700 1.00 23.40 ?  169 LEU   B HB2  1 
ATOM   5433 H HB3  . LEU   B 1 169 ? 29.884 -37.673 -14.562 1.00 23.40 ?  169 LEU   B HB3  1 
ATOM   5434 H HG   . LEU   B 1 169 ? 28.584 -35.639 -13.123 1.00 26.75 ?  169 LEU   B HG   1 
ATOM   5435 H HD11 . LEU   B 1 169 ? 27.732 -35.017 -15.188 1.00 28.06 ?  169 LEU   B HD11 1 
ATOM   5436 H HD12 . LEU   B 1 169 ? 29.320 -35.011 -15.230 1.00 28.06 ?  169 LEU   B HD12 1 
ATOM   5437 H HD13 . LEU   B 1 169 ? 28.512 -36.218 -15.875 1.00 28.06 ?  169 LEU   B HD13 1 
ATOM   5438 H HD21 . LEU   B 1 169 ? 26.567 -36.701 -14.051 1.00 27.15 ?  169 LEU   B HD21 1 
ATOM   5439 H HD22 . LEU   B 1 169 ? 27.462 -38.013 -14.076 1.00 27.15 ?  169 LEU   B HD22 1 
ATOM   5440 H HD23 . LEU   B 1 169 ? 27.166 -37.278 -12.700 1.00 27.15 ?  169 LEU   B HD23 1 
HETATM 5441 N N2   B A1A41 C 2 .   ? 24.914 -9.264  17.819  0.12 23.07 ?  201 A1A41 A N2   1 
HETATM 5442 C C3   B A1A41 C 2 .   ? 22.151 -6.175  20.367  0.12 24.15 ?  201 A1A41 A C3   1 
HETATM 5443 C C6   B A1A41 C 2 .   ? 24.315 -9.720  22.012  0.12 25.56 ?  201 A1A41 A C6   1 
HETATM 5444 C C9   B A1A41 C 2 .   ? 26.604 -8.127  21.592  0.12 25.47 ?  201 A1A41 A C9   1 
HETATM 5445 C C1   B A1A41 C 2 .   ? 24.575 -10.534 18.149  0.12 23.02 ?  201 A1A41 A C1   1 
HETATM 5446 C C10  B A1A41 C 2 .   ? 25.347 -7.516  21.642  0.12 25.46 ?  201 A1A41 A C10  1 
HETATM 5447 C C11  B A1A41 C 2 .   ? 24.210 -8.301  21.850  0.12 25.45 ?  201 A1A41 A C11  1 
HETATM 5448 C C2   B A1A41 C 2 .   ? 22.863 -8.659  18.733  0.12 23.29 ?  201 A1A41 A C2   1 
HETATM 5449 C C4   B A1A41 C 2 .   ? 22.221 -6.639  21.843  0.12 24.74 ?  201 A1A41 A C4   1 
HETATM 5450 C C5   B A1A41 C 2 .   ? 22.156 -9.149  22.156  0.12 25.61 ?  201 A1A41 A C5   1 
HETATM 5451 C C7   B A1A41 C 2 .   ? 25.571 -10.357 21.965  0.12 25.53 ?  201 A1A41 A C7   1 
HETATM 5452 C C8   B A1A41 C 2 .   ? 26.716 -9.529  21.751  0.12 25.49 ?  201 A1A41 A C8   1 
HETATM 5453 N N1   B A1A41 C 2 .   ? 25.376 -11.652 17.906  0.12 23.10 ?  201 A1A41 A N1   1 
HETATM 5454 N N3   B A1A41 C 2 .   ? 24.015 -8.323  18.132  0.12 23.18 ?  201 A1A41 A N3   1 
HETATM 5455 N N4   B A1A41 C 2 .   ? 22.881 -8.029  21.948  0.12 25.29 ?  201 A1A41 A N4   1 
HETATM 5456 O O1   B A1A41 C 2 .   ? 20.914 -9.259  22.292  0.12 25.79 ?  201 A1A41 A O1   1 
HETATM 5457 O O2   B A1A41 C 2 .   ? 23.007 -10.246 22.205  0.12 25.62 ?  201 A1A41 A O2   1 
HETATM 5458 S S1   B A1A41 C 2 .   ? 21.589 -7.517  19.201  0.12 23.56 ?  201 A1A41 A S1   1 
HETATM 5459 S S2   B A1A41 C 2 .   ? 22.916 -10.477 18.944  0.12 23.13 ?  201 A1A41 A S2   1 
HETATM 5460 H H4   B A1A41 C 2 .   ? 21.427 -5.376  20.250  0.12 28.99 ?  201 A1A41 A H4   1 
HETATM 5461 H H3   B A1A41 C 2 .   ? 23.134 -5.803  20.016  0.12 28.99 ?  201 A1A41 A H3   1 
HETATM 5462 H H9   B A1A41 C 2 .   ? 27.483 -7.484  21.427  0.12 30.56 ?  201 A1A41 A H9   1 
HETATM 5463 H H10  B A1A41 C 2 .   ? 25.188 -6.424  21.525  0.12 30.56 ?  201 A1A41 A H10  1 
HETATM 5464 H H5   B A1A41 C 2 .   ? 21.217 -6.766  22.302  0.12 29.70 ?  201 A1A41 A H5   1 
HETATM 5465 H H6   B A1A41 C 2 .   ? 22.833 -6.006  22.496  0.12 29.70 ?  201 A1A41 A H6   1 
HETATM 5466 H H7   B A1A41 C 2 .   ? 25.697 -11.440 22.084  0.12 30.64 ?  201 A1A41 A H7   1 
HETATM 5467 H H8   B A1A41 C 2 .   ? 27.728 -9.985  21.706  0.12 30.59 ?  201 A1A41 A H8   1 
HETATM 5468 H H2   B A1A41 C 2 .   ? 25.741 -11.855 17.015  0.12 27.73 ?  201 A1A41 A H2   1 
HETATM 5469 H H1   B A1A41 C 2 .   ? 25.620 -12.302 18.614  0.12 27.73 ?  201 A1A41 A H1   1 
HETATM 5470 O O    . HOH   D 3 .   ? 4.768  3.911   0.697   1.00 23.89 ?  301 HOH   A O    1 
HETATM 5471 O O    . HOH   D 3 .   ? 14.801 -4.668  20.570  1.00 39.12 ?  302 HOH   A O    1 
HETATM 5472 O O    . HOH   D 3 .   ? 15.149 -12.235 18.750  1.00 27.07 ?  303 HOH   A O    1 
HETATM 5473 O O    . HOH   D 3 .   ? 28.227 -6.350  19.552  1.00 42.25 ?  304 HOH   A O    1 
HETATM 5474 O O    . HOH   D 3 .   ? 34.386 -1.882  12.495  1.00 35.59 ?  305 HOH   A O    1 
HETATM 5475 O O    B HOH   D 3 .   ? 27.572 -11.407 16.708  0.12 28.07 ?  306 HOH   A O    1 
HETATM 5476 O O    . HOH   D 3 .   ? 19.833 -12.494 -9.034  1.00 24.55 ?  307 HOH   A O    1 
HETATM 5477 O O    . HOH   D 3 .   ? 42.437 10.517  5.138   1.00 19.01 ?  308 HOH   A O    1 
HETATM 5478 O O    . HOH   D 3 .   ? 28.888 0.437   -9.733  1.00 20.02 ?  309 HOH   A O    1 
HETATM 5479 O O    . HOH   D 3 .   ? 8.037  -21.499 3.989   1.00 43.58 ?  310 HOH   A O    1 
HETATM 5480 O O    . HOH   D 3 .   ? 12.207 0.256   14.952  1.00 30.79 ?  311 HOH   A O    1 
HETATM 5481 O O    . HOH   D 3 .   ? 36.127 -5.078  -0.583  1.00 26.37 ?  312 HOH   A O    1 
HETATM 5482 O O    . HOH   D 3 .   ? 28.256 -0.131  -13.347 1.00 32.45 ?  313 HOH   A O    1 
HETATM 5483 O O    . HOH   D 3 .   ? 30.236 -13.281 -8.598  1.00 18.62 ?  314 HOH   A O    1 
HETATM 5484 O O    . HOH   D 3 .   ? 33.981 -1.009  -8.926  1.00 25.86 ?  315 HOH   A O    1 
HETATM 5485 O O    . HOH   D 3 .   ? 14.760 -14.042 16.713  1.00 19.19 ?  316 HOH   A O    1 
HETATM 5486 O O    . HOH   D 3 .   ? 27.278 13.754  2.908   1.00 24.19 ?  317 HOH   A O    1 
HETATM 5487 O O    . HOH   D 3 .   ? 14.142 -4.544  -11.798 1.00 27.94 ?  318 HOH   A O    1 
HETATM 5488 O O    . HOH   D 3 .   ? 26.477 -19.354 -1.824  1.00 13.03 ?  319 HOH   A O    1 
HETATM 5489 O O    . HOH   D 3 .   ? 17.125 -18.062 15.161  1.00 22.07 ?  320 HOH   A O    1 
HETATM 5490 O O    . HOH   D 3 .   ? 11.578 -10.838 -10.046 1.00 38.30 ?  321 HOH   A O    1 
HETATM 5491 O O    . HOH   D 3 .   ? 18.877 -22.006 6.912   1.00 29.60 ?  322 HOH   A O    1 
HETATM 5492 O O    . HOH   D 3 .   ? 0.719  -4.561  0.385   1.00 29.87 ?  323 HOH   A O    1 
HETATM 5493 O O    . HOH   D 3 .   ? 37.563 2.771   10.165  1.00 26.89 ?  324 HOH   A O    1 
HETATM 5494 O O    . HOH   D 3 .   ? 22.517 5.299   19.159  1.00 40.02 ?  325 HOH   A O    1 
HETATM 5495 O O    . HOH   D 3 .   ? 31.014 -18.178 7.759   1.00 18.17 ?  326 HOH   A O    1 
HETATM 5496 O O    . HOH   D 3 .   ? 20.623 -19.737 -5.092  1.00 28.03 ?  327 HOH   A O    1 
HETATM 5497 O O    . HOH   D 3 .   ? 7.966  -12.652 -0.838  1.00 20.21 ?  328 HOH   A O    1 
HETATM 5498 O O    . HOH   D 3 .   ? 9.155  -10.195 19.392  1.00 37.23 ?  329 HOH   A O    1 
HETATM 5499 O O    . HOH   D 3 .   ? 38.265 10.108  7.149   1.00 33.42 ?  330 HOH   A O    1 
HETATM 5500 O O    B HOH   D 3 .   ? 19.942 -4.219  22.268  0.12 9.72  ?  331 HOH   A O    1 
HETATM 5501 O O    . HOH   D 3 .   ? 3.594  -9.437  9.927   1.00 31.40 ?  332 HOH   A O    1 
HETATM 5502 O O    . HOH   D 3 .   ? 6.955  -8.196  11.882  1.00 19.75 ?  333 HOH   A O    1 
HETATM 5503 O O    . HOH   D 3 .   ? 18.669 -19.407 13.542  1.00 31.12 ?  334 HOH   A O    1 
HETATM 5504 O O    . HOH   D 3 .   ? 38.565 4.937   6.947   1.00 14.51 ?  335 HOH   A O    1 
HETATM 5505 O O    . HOH   D 3 .   ? 26.818 11.378  1.672   1.00 15.11 ?  336 HOH   A O    1 
HETATM 5506 O O    . HOH   D 3 .   ? 42.565 4.280   5.358   1.00 30.01 ?  337 HOH   A O    1 
HETATM 5507 O O    . HOH   D 3 .   ? 22.316 -19.253 11.358  1.00 31.16 ?  338 HOH   A O    1 
HETATM 5508 O O    . HOH   D 3 .   ? 44.310 7.078   6.452   1.00 25.25 ?  339 HOH   A O    1 
HETATM 5509 O O    . HOH   D 3 .   ? 31.669 8.195   14.830  1.00 22.90 ?  340 HOH   A O    1 
HETATM 5510 O O    . HOH   D 3 .   ? 39.745 -1.013  -5.243  1.00 18.94 ?  341 HOH   A O    1 
HETATM 5511 O O    . HOH   D 3 .   ? 15.575 11.933  8.050   1.00 24.24 ?  342 HOH   A O    1 
HETATM 5512 O O    . HOH   D 3 .   ? 37.403 11.861  4.951   1.00 27.99 ?  343 HOH   A O    1 
HETATM 5513 O O    . HOH   D 3 .   ? 17.543 -1.708  0.505   1.00 15.69 ?  344 HOH   A O    1 
HETATM 5514 O O    . HOH   D 3 .   ? 21.227 -2.411  -2.050  1.00 14.41 ?  345 HOH   A O    1 
HETATM 5515 O O    . HOH   D 3 .   ? 35.771 -12.698 6.788   1.00 14.76 ?  346 HOH   A O    1 
HETATM 5516 O O    . HOH   D 3 .   ? 23.995 -2.105  -2.055  1.00 9.59  ?  347 HOH   A O    1 
HETATM 5517 O O    . HOH   D 3 .   ? 17.175 -17.849 -5.038  1.00 25.60 ?  348 HOH   A O    1 
HETATM 5518 O O    . HOH   D 3 .   ? 16.483 -22.069 0.952   1.00 25.85 ?  349 HOH   A O    1 
HETATM 5519 O O    . HOH   D 3 .   ? -0.622 -8.521  2.281   1.00 39.40 ?  350 HOH   A O    1 
HETATM 5520 O O    . HOH   D 3 .   ? 31.064 -13.950 -2.520  1.00 12.38 ?  351 HOH   A O    1 
HETATM 5521 O O    . HOH   D 3 .   ? 33.665 -7.184  4.239   1.00 15.61 ?  352 HOH   A O    1 
HETATM 5522 O O    . HOH   D 3 .   ? 31.774 -9.355  -6.671  1.00 20.23 ?  353 HOH   A O    1 
HETATM 5523 O O    . HOH   D 3 .   ? 14.355 -21.281 -4.254  1.00 29.50 ?  354 HOH   A O    1 
HETATM 5524 O O    . HOH   D 3 .   ? 21.925 -21.944 8.433   1.00 25.47 ?  355 HOH   A O    1 
HETATM 5525 O O    . HOH   D 3 .   ? 43.881 8.434   -3.145  1.00 25.35 ?  356 HOH   A O    1 
HETATM 5526 O O    . HOH   D 3 .   ? 9.830  -21.383 5.721   1.00 17.10 ?  357 HOH   A O    1 
HETATM 5527 O O    . HOH   D 3 .   ? 37.261 -2.862  9.672   1.00 37.88 ?  358 HOH   A O    1 
HETATM 5528 O O    . HOH   D 3 .   ? 19.645 -11.184 24.208  1.00 62.13 ?  359 HOH   A O    1 
HETATM 5529 O O    . HOH   D 3 .   ? 27.528 -10.663 14.030  1.00 15.14 ?  360 HOH   A O    1 
HETATM 5530 O O    . HOH   D 3 .   ? 30.814 3.074   8.268   1.00 11.17 ?  361 HOH   A O    1 
HETATM 5531 O O    A HOH   D 3 .   ? 22.764 -12.115 21.878  0.88 34.30 ?  362 HOH   A O    1 
HETATM 5532 O O    . HOH   D 3 .   ? 17.020 -19.326 4.905   1.00 13.22 ?  363 HOH   A O    1 
HETATM 5533 O O    . HOH   D 3 .   ? 18.563 9.430   9.015   1.00 18.64 ?  364 HOH   A O    1 
HETATM 5534 O O    . HOH   D 3 .   ? 31.700 -7.262  -9.868  1.00 20.04 ?  365 HOH   A O    1 
HETATM 5535 O O    . HOH   D 3 .   ? 15.169 3.895   17.883  1.00 34.51 ?  366 HOH   A O    1 
HETATM 5536 O O    . HOH   D 3 .   ? 13.522 -15.260 -7.494  1.00 26.85 ?  367 HOH   A O    1 
HETATM 5537 O O    . HOH   D 3 .   ? 20.068 4.480   -7.560  1.00 17.71 ?  368 HOH   A O    1 
HETATM 5538 O O    . HOH   D 3 .   ? 13.290 -1.436  -6.545  1.00 16.25 ?  369 HOH   A O    1 
HETATM 5539 O O    . HOH   D 3 .   ? 43.344 7.821   2.639   1.00 24.59 ?  370 HOH   A O    1 
HETATM 5540 O O    . HOH   D 3 .   ? 24.743 -17.553 12.706  1.00 22.00 ?  371 HOH   A O    1 
HETATM 5541 O O    . HOH   D 3 .   ? 22.757 12.515  1.666   1.00 13.24 ?  372 HOH   A O    1 
HETATM 5542 O O    . HOH   D 3 .   ? 24.402 3.563   -1.825  1.00 14.27 ?  373 HOH   A O    1 
HETATM 5543 O O    . HOH   D 3 .   ? 14.609 -3.658  3.118   1.00 16.32 ?  374 HOH   A O    1 
HETATM 5544 O O    . HOH   D 3 .   ? 24.313 -7.835  14.454  1.00 15.68 ?  375 HOH   A O    1 
HETATM 5545 O O    . HOH   D 3 .   ? 28.452 -10.619 -14.054 1.00 38.87 ?  376 HOH   A O    1 
HETATM 5546 O O    . HOH   D 3 .   ? 8.866  -12.070 17.221  1.00 40.30 ?  377 HOH   A O    1 
HETATM 5547 O O    . HOH   D 3 .   ? -0.473 -3.133  3.126   1.00 37.11 ?  378 HOH   A O    1 
HETATM 5548 O O    . HOH   D 3 .   ? 25.686 -0.797  -7.338  1.00 13.88 ?  379 HOH   A O    1 
HETATM 5549 O O    . HOH   D 3 .   ? 13.995 -5.002  17.609  1.00 21.41 ?  380 HOH   A O    1 
HETATM 5550 O O    . HOH   D 3 .   ? 37.530 -2.020  5.753   1.00 25.94 ?  381 HOH   A O    1 
HETATM 5551 O O    . HOH   D 3 .   ? 21.202 10.290  15.017  1.00 31.58 ?  382 HOH   A O    1 
HETATM 5552 O O    . HOH   D 3 .   ? 30.684 1.840   16.703  1.00 20.13 ?  383 HOH   A O    1 
HETATM 5553 O O    . HOH   D 3 .   ? 23.907 -15.682 -9.167  1.00 28.95 ?  384 HOH   A O    1 
HETATM 5554 O O    . HOH   D 3 .   ? 18.943 -0.679  -1.601  1.00 11.43 ?  385 HOH   A O    1 
HETATM 5555 O O    . HOH   D 3 .   ? 14.240 0.512   6.802   1.00 18.82 ?  386 HOH   A O    1 
HETATM 5556 O O    . HOH   D 3 .   ? 32.788 -9.264  5.923   1.00 19.14 ?  387 HOH   A O    1 
HETATM 5557 O O    . HOH   D 3 .   ? 6.484  -5.632  11.196  1.00 19.58 ?  388 HOH   A O    1 
HETATM 5558 O O    . HOH   D 3 .   ? 21.808 -13.806 -8.119  1.00 33.07 ?  389 HOH   A O    1 
HETATM 5559 O O    . HOH   D 3 .   ? 20.579 -20.047 2.766   1.00 16.05 ?  390 HOH   A O    1 
HETATM 5560 O O    . HOH   D 3 .   ? 10.468 -22.208 -1.225  1.00 46.35 ?  391 HOH   A O    1 
HETATM 5561 O O    . HOH   D 3 .   ? 24.562 1.970   -7.010  1.00 17.40 ?  392 HOH   A O    1 
HETATM 5562 O O    . HOH   D 3 .   ? 15.854 2.081   24.808  1.00 49.36 ?  393 HOH   A O    1 
HETATM 5563 O O    . HOH   D 3 .   ? 27.263 -5.965  -14.023 1.00 35.10 ?  394 HOH   A O    1 
HETATM 5564 O O    . HOH   D 3 .   ? 14.409 -24.732 11.604  1.00 29.99 ?  395 HOH   A O    1 
HETATM 5565 O O    . HOH   D 3 .   ? 15.767 -0.945  5.309   1.00 22.36 ?  396 HOH   A O    1 
HETATM 5566 O O    . HOH   D 3 .   ? 23.457 11.353  4.113   1.00 10.94 ?  397 HOH   A O    1 
HETATM 5567 O O    . HOH   D 3 .   ? 21.346 3.156   -0.349  1.00 11.86 ?  398 HOH   A O    1 
HETATM 5568 O O    . HOH   D 3 .   ? 11.064 1.528   12.861  1.00 22.59 ?  399 HOH   A O    1 
HETATM 5569 O O    . HOH   D 3 .   ? 27.256 2.291   18.701  1.00 28.56 ?  400 HOH   A O    1 
HETATM 5570 O O    . HOH   D 3 .   ? 15.206 -21.618 14.209  1.00 15.40 ?  401 HOH   A O    1 
HETATM 5571 O O    . HOH   D 3 .   ? 26.920 4.153   -0.640  1.00 11.71 ?  402 HOH   A O    1 
HETATM 5572 O O    . HOH   D 3 .   ? 41.607 1.502   4.902   1.00 35.34 ?  403 HOH   A O    1 
HETATM 5573 O O    . HOH   D 3 .   ? 7.652  -6.298  -6.547  1.00 38.52 ?  404 HOH   A O    1 
HETATM 5574 O O    . HOH   D 3 .   ? 14.070 -23.110 7.425   1.00 15.78 ?  405 HOH   A O    1 
HETATM 5575 O O    . HOH   D 3 .   ? 44.903 -0.635  2.956   1.00 38.30 ?  406 HOH   A O    1 
HETATM 5576 O O    . HOH   D 3 .   ? 16.197 -14.193 20.326  1.00 36.31 ?  407 HOH   A O    1 
HETATM 5577 O O    . HOH   D 3 .   ? 38.091 -1.383  -2.001  1.00 18.07 ?  408 HOH   A O    1 
HETATM 5578 O O    . HOH   D 3 .   ? 16.243 16.636  8.769   1.00 25.23 ?  409 HOH   A O    1 
HETATM 5579 O O    . HOH   D 3 .   ? 15.159 -8.093  -9.552  1.00 20.20 ?  410 HOH   A O    1 
HETATM 5580 O O    . HOH   D 3 .   ? 18.578 -2.433  -16.326 1.00 40.13 ?  411 HOH   A O    1 
HETATM 5581 O O    . HOH   D 3 .   ? 6.720  -3.438  13.017  1.00 29.39 ?  412 HOH   A O    1 
HETATM 5582 O O    . HOH   D 3 .   ? 35.044 -5.215  -3.128  1.00 17.33 ?  413 HOH   A O    1 
HETATM 5583 O O    . HOH   D 3 .   ? 40.898 -8.242  -6.767  1.00 33.97 ?  414 HOH   A O    1 
HETATM 5584 O O    . HOH   D 3 .   ? 32.614 -4.289  -9.934  1.00 25.76 ?  415 HOH   A O    1 
HETATM 5585 O O    . HOH   D 3 .   ? 27.894 0.837   -7.155  1.00 12.85 ?  416 HOH   A O    1 
HETATM 5586 O O    . HOH   D 3 .   ? 5.198  2.620   5.281   1.00 30.29 ?  417 HOH   A O    1 
HETATM 5587 O O    . HOH   D 3 .   ? 22.701 8.079   18.376  1.00 39.05 ?  418 HOH   A O    1 
HETATM 5588 O O    A HOH   D 3 .   ? 30.111 -10.134 13.039  0.88 19.31 ?  419 HOH   A O    1 
HETATM 5589 O O    . HOH   D 3 .   ? 11.061 -0.388  2.046   1.00 23.48 ?  420 HOH   A O    1 
HETATM 5590 O O    . HOH   D 3 .   ? 36.743 -4.973  5.377   1.00 22.94 ?  421 HOH   A O    1 
HETATM 5591 O O    . HOH   D 3 .   ? 24.023 3.939   -4.843  1.00 21.08 ?  422 HOH   A O    1 
HETATM 5592 O O    . HOH   D 3 .   ? 27.150 -3.247  19.285  1.00 32.86 ?  423 HOH   A O    1 
HETATM 5593 O O    . HOH   D 3 .   ? 23.940 -20.304 -1.361  1.00 14.79 ?  424 HOH   A O    1 
HETATM 5594 O O    B HOH   D 3 .   ? 20.124 -8.374  24.988  0.12 13.87 ?  425 HOH   A O    1 
HETATM 5595 O O    . HOH   D 3 .   ? 30.384 -12.961 13.506  1.00 18.10 ?  426 HOH   A O    1 
HETATM 5596 O O    . HOH   D 3 .   ? 30.862 6.232   -12.324 1.00 30.01 ?  427 HOH   A O    1 
HETATM 5597 O O    . HOH   D 3 .   ? 16.007 6.933   3.051   1.00 14.30 ?  428 HOH   A O    1 
HETATM 5598 O O    . HOH   D 3 .   ? 32.585 -10.650 3.145   1.00 28.99 ?  429 HOH   A O    1 
HETATM 5599 O O    . HOH   D 3 .   ? 10.392 -13.766 -1.648  1.00 16.35 ?  430 HOH   A O    1 
HETATM 5600 O O    . HOH   D 3 .   ? 16.262 2.924   -1.450  1.00 15.49 ?  431 HOH   A O    1 
HETATM 5601 O O    . HOH   D 3 .   ? 14.484 -0.542  -11.998 1.00 25.33 ?  432 HOH   A O    1 
HETATM 5602 O O    A HOH   D 3 .   ? 23.684 -8.140  16.995  0.88 19.25 ?  433 HOH   A O    1 
HETATM 5603 O O    . HOH   D 3 .   ? 11.697 -10.786 17.084  1.00 21.04 ?  434 HOH   A O    1 
HETATM 5604 O O    . HOH   D 3 .   ? 18.878 2.010   -0.703  1.00 12.01 ?  435 HOH   A O    1 
HETATM 5605 O O    B HOH   D 3 .   ? 23.363 -13.895 22.186  0.12 38.61 ?  436 HOH   A O    1 
HETATM 5606 O O    . HOH   D 3 .   ? 37.707 -8.819  -3.504  1.00 23.01 ?  437 HOH   A O    1 
HETATM 5607 O O    . HOH   D 3 .   ? 23.328 -20.998 1.288   1.00 16.66 ?  438 HOH   A O    1 
HETATM 5608 O O    B HOH   D 3 .   ? 30.084 -10.090 13.178  0.12 17.38 ?  439 HOH   A O    1 
HETATM 5609 O O    . HOH   D 3 .   ? 9.486  -16.328 -2.016  1.00 38.31 ?  440 HOH   A O    1 
HETATM 5610 O O    . HOH   D 3 .   ? 34.413 -8.069  -0.575  1.00 26.87 ?  441 HOH   A O    1 
HETATM 5611 O O    B HOH   D 3 .   ? 21.649 -13.745 18.701  0.12 27.98 ?  442 HOH   A O    1 
HETATM 5612 O O    . HOH   D 3 .   ? 30.578 14.754  2.835   1.00 17.68 ?  443 HOH   A O    1 
HETATM 5613 O O    . HOH   D 3 .   ? 18.419 -16.108 16.459  1.00 32.84 ?  444 HOH   A O    1 
HETATM 5614 O O    . HOH   D 3 .   ? 23.210 7.580   -3.134  1.00 26.32 ?  445 HOH   A O    1 
HETATM 5615 O O    A HOH   D 3 .   ? 21.537 -14.740 18.034  0.88 38.36 ?  446 HOH   A O    1 
HETATM 5616 O O    . HOH   D 3 .   ? -1.385 -5.002  7.774   1.00 35.93 ?  447 HOH   A O    1 
HETATM 5617 O O    . HOH   D 3 .   ? 31.330 -12.776 -0.024  1.00 17.96 ?  448 HOH   A O    1 
HETATM 5618 O O    . HOH   D 3 .   ? 18.457 4.901   -15.072 1.00 46.14 ?  449 HOH   A O    1 
HETATM 5619 O O    A HOH   D 3 .   ? 21.370 -9.414  21.259  0.88 42.59 ?  450 HOH   A O    1 
HETATM 5620 O O    . HOH   D 3 .   ? 29.800 -16.066 10.562  1.00 32.39 ?  451 HOH   A O    1 
HETATM 5621 O O    A HOH   D 3 .   ? 20.572 -17.916 24.796  0.88 40.57 ?  452 HOH   A O    1 
HETATM 5622 O O    . HOH   D 3 .   ? 13.999 -0.356  3.480   1.00 22.08 ?  453 HOH   A O    1 
HETATM 5623 O O    . HOH   D 3 .   ? 27.759 7.065   -6.331  1.00 31.95 ?  454 HOH   A O    1 
HETATM 5624 O O    . HOH   D 3 .   ? 25.425 8.239   -4.741  1.00 21.62 ?  455 HOH   A O    1 
HETATM 5625 O O    . HOH   D 3 .   ? 32.501 -15.977 10.748  1.00 33.72 ?  456 HOH   A O    1 
HETATM 5626 O O    . HOH   D 3 .   ? 29.761 -1.965  -12.753 1.00 43.21 ?  457 HOH   A O    1 
HETATM 5627 O O    . HOH   D 3 .   ? 19.910 -17.378 -5.082  1.00 23.90 ?  458 HOH   A O    1 
HETATM 5628 O O    . HOH   D 3 .   ? 24.609 14.508  7.890   1.00 32.08 ?  459 HOH   A O    1 
HETATM 5629 O O    . HOH   D 3 .   ? 23.207 -22.350 -3.284  1.00 34.17 ?  460 HOH   A O    1 
HETATM 5630 O O    . HOH   D 3 .   ? 24.928 5.627   20.746  1.00 49.57 ?  461 HOH   A O    1 
HETATM 5631 O O    . HOH   D 3 .   ? 15.720 -21.548 3.688   1.00 20.61 ?  462 HOH   A O    1 
HETATM 5632 O O    . HOH   D 3 .   ? 26.919 11.627  -1.306  1.00 26.10 ?  463 HOH   A O    1 
HETATM 5633 O O    A HOH   D 3 .   ? 27.466 -11.402 16.597  0.88 31.67 ?  464 HOH   A O    1 
HETATM 5634 O O    . HOH   D 3 .   ? 39.629 -7.015  -3.564  1.00 41.64 ?  465 HOH   A O    1 
HETATM 5635 O O    . HOH   D 3 .   ? 18.722 10.767  11.361  1.00 29.01 ?  466 HOH   A O    1 
HETATM 5636 O O    . HOH   D 3 .   ? 21.960 5.267   -5.946  1.00 25.28 ?  467 HOH   A O    1 
HETATM 5637 O O    . HOH   D 3 .   ? 23.519 13.690  5.532   1.00 17.81 ?  468 HOH   A O    1 
HETATM 5638 O O    . HOH   D 3 .   ? 11.994 -13.414 16.372  1.00 35.94 ?  469 HOH   A O    1 
HETATM 5639 O O    . HOH   D 3 .   ? 25.837 10.780  -3.710  1.00 23.70 ?  470 HOH   A O    1 
HETATM 5640 O O    . HOH   D 3 .   ? 12.336 1.562   17.391  1.00 36.72 ?  471 HOH   A O    1 
HETATM 5641 O O    . HOH   D 3 .   ? 11.016 -15.023 -6.079  1.00 33.67 ?  472 HOH   A O    1 
HETATM 5642 O O    . HOH   D 3 .   ? 28.860 8.942   17.469  1.00 35.55 ?  473 HOH   A O    1 
HETATM 5643 O O    . HOH   D 3 .   ? 35.181 7.400   12.203  1.00 44.39 ?  474 HOH   A O    1 
HETATM 5644 O O    . HOH   D 3 .   ? 17.369 -18.738 19.793  1.00 44.55 ?  475 HOH   A O    1 
HETATM 5645 O O    . HOH   D 3 .   ? 30.853 0.673   19.135  1.00 34.31 ?  476 HOH   A O    1 
HETATM 5646 O O    . HOH   D 3 .   ? 40.913 -3.982  -0.354  1.00 34.20 ?  477 HOH   A O    1 
HETATM 5647 O O    . HOH   D 3 .   ? 18.132 -16.265 -8.759  1.00 38.35 ?  478 HOH   A O    1 
HETATM 5648 O O    . HOH   D 3 .   ? 14.048 -10.297 -10.857 1.00 29.66 ?  479 HOH   A O    1 
HETATM 5649 O O    . HOH   D 3 .   ? 16.806 -20.614 16.188  1.00 25.12 ?  480 HOH   A O    1 
HETATM 5650 O O    . HOH   D 3 .   ? 23.145 11.815  -4.053  1.00 17.68 ?  481 HOH   A O    1 
HETATM 5651 O O    . HOH   D 3 .   ? 15.730 -17.208 -6.981  1.00 30.59 ?  482 HOH   A O    1 
HETATM 5652 O O    . HOH   D 3 .   ? 41.677 9.272   -4.095  1.00 29.87 ?  483 HOH   A O    1 
HETATM 5653 O O    . HOH   D 3 .   ? 44.485 10.423  -1.617  1.00 30.60 ?  484 HOH   A O    1 
HETATM 5654 O O    . HOH   D 3 .   ? 28.510 -4.667  -12.343 1.00 34.32 ?  485 HOH   A O    1 
HETATM 5655 O O    A HOH   D 3 .   ? 23.347 -13.027 19.256  0.88 38.38 ?  486 HOH   A O    1 
HETATM 5656 O O    . HOH   D 3 .   ? 18.494 -23.226 1.962   1.00 42.57 ?  487 HOH   A O    1 
HETATM 5657 O O    . HOH   D 3 .   ? 40.478 -0.237  -7.836  1.00 32.54 ?  488 HOH   A O    1 
HETATM 5658 O O    . HOH   D 3 .   ? 19.980 -22.368 4.144   1.00 24.97 ?  489 HOH   A O    1 
HETATM 5659 O O    . HOH   D 3 .   ? 15.914 -6.786  -11.760 1.00 39.58 ?  490 HOH   A O    1 
HETATM 5660 O O    . HOH   D 3 .   ? 39.173 2.351   7.581   1.00 29.79 ?  491 HOH   A O    1 
HETATM 5661 O O    . HOH   D 3 .   ? 31.449 -0.605  -10.555 1.00 23.63 ?  492 HOH   A O    1 
HETATM 5662 O O    . HOH   D 3 .   ? 28.592 -7.895  -15.333 1.00 46.82 ?  493 HOH   A O    1 
HETATM 5663 O O    . HOH   D 3 .   ? 14.109 -25.400 8.900   1.00 26.83 ?  494 HOH   A O    1 
HETATM 5664 O O    . HOH   D 3 .   ? 30.677 -5.823  -11.814 1.00 41.24 ?  495 HOH   A O    1 
HETATM 5665 O O    . HOH   D 3 .   ? 16.153 -23.401 5.727   1.00 25.31 ?  496 HOH   A O    1 
HETATM 5666 O O    . HOH   D 3 .   ? 30.750 5.814   -14.665 1.00 33.78 ?  497 HOH   A O    1 
HETATM 5667 O O    . HOH   D 3 .   ? 23.149 -23.795 1.691   1.00 28.50 ?  498 HOH   A O    1 
HETATM 5668 O O    . HOH   D 3 .   ? 37.372 -6.683  7.526   1.00 23.34 ?  499 HOH   A O    1 
HETATM 5669 O O    . HOH   D 3 .   ? 28.949 14.434  0.949   1.00 40.81 ?  500 HOH   A O    1 
HETATM 5670 O O    . HOH   D 3 .   ? 39.568 -0.003  6.579   1.00 29.30 ?  501 HOH   A O    1 
HETATM 5671 O O    . HOH   D 3 .   ? 38.050 13.866  6.706   1.00 34.86 ?  502 HOH   A O    1 
HETATM 5672 O O    . HOH   D 3 .   ? 20.477 -16.077 -7.379  1.00 28.28 ?  503 HOH   A O    1 
HETATM 5673 O O    . HOH   D 3 .   ? 36.507 -6.488  10.100  1.00 37.00 ?  504 HOH   A O    1 
HETATM 5674 O O    . HOH   D 3 .   ? 22.024 -24.105 4.426   1.00 24.15 ?  505 HOH   A O    1 
HETATM 5675 O O    . HOH   D 3 .   ? 8.230  -3.018  -5.680  1.00 37.88 ?  506 HOH   A O    1 
HETATM 5676 O O    . HOH   D 3 .   ? 17.400 -6.622  -14.090 1.00 36.73 ?  507 HOH   A O    1 
HETATM 5677 O O    . HOH   D 3 .   ? 14.885 8.586   5.034   1.00 33.04 ?  508 HOH   A O    1 
HETATM 5678 O O    . HOH   D 3 .   ? 24.095 8.986   -7.231  1.00 33.42 ?  509 HOH   A O    1 
HETATM 5679 O O    . HOH   D 3 .   ? 15.953 -12.245 27.517  1.00 38.62 ?  510 HOH   A O    1 
HETATM 5680 O O    . HOH   D 3 .   ? 16.433 -21.108 18.821  1.00 30.89 ?  511 HOH   A O    1 
HETATM 5681 O O    . HOH   D 3 .   ? 14.636 -22.779 19.892  1.00 29.77 ?  512 HOH   A O    1 
HETATM 5682 O O    . HOH   E 3 .   ? 29.808 -22.429 5.411   1.00 18.38 ?  201 HOH   B O    1 
HETATM 5683 O O    . HOH   E 3 .   ? 48.133 -6.915  15.518  1.00 31.80 ?  202 HOH   B O    1 
HETATM 5684 O O    . HOH   E 3 .   ? 27.811 -41.723 -15.244 1.00 34.45 ?  203 HOH   B O    1 
HETATM 5685 O O    . HOH   E 3 .   ? 47.414 -7.432  -4.013  1.00 39.43 ?  204 HOH   B O    1 
HETATM 5686 O O    . HOH   E 3 .   ? 59.142 -18.756 6.741   1.00 34.56 ?  205 HOH   B O    1 
HETATM 5687 O O    . HOH   E 3 .   ? 37.893 -39.481 -0.333  1.00 38.72 ?  206 HOH   B O    1 
HETATM 5688 O O    . HOH   E 3 .   ? 49.371 -22.698 -19.838 1.00 45.62 ?  207 HOH   B O    1 
HETATM 5689 O O    . HOH   E 3 .   ? 41.369 -7.758  5.480   1.00 34.25 ?  208 HOH   B O    1 
HETATM 5690 O O    . HOH   E 3 .   ? 41.809 -35.850 -17.484 1.00 28.81 ?  209 HOH   B O    1 
HETATM 5691 O O    . HOH   E 3 .   ? 27.737 -29.165 -1.902  1.00 31.25 ?  210 HOH   B O    1 
HETATM 5692 O O    . HOH   E 3 .   ? 56.339 -19.742 7.249   1.00 32.15 ?  211 HOH   B O    1 
HETATM 5693 O O    . HOH   E 3 .   ? 58.211 -12.947 8.378   1.00 31.98 ?  212 HOH   B O    1 
HETATM 5694 O O    . HOH   E 3 .   ? 54.445 -9.340  -8.803  1.00 17.46 ?  213 HOH   B O    1 
HETATM 5695 O O    . HOH   E 3 .   ? 50.260 -3.361  7.148   1.00 32.48 ?  214 HOH   B O    1 
HETATM 5696 O O    . HOH   E 3 .   ? 30.210 -41.007 -8.194  1.00 15.10 ?  215 HOH   B O    1 
HETATM 5697 O O    . HOH   E 3 .   ? 29.772 -34.200 -0.470  1.00 31.56 ?  216 HOH   B O    1 
HETATM 5698 O O    . HOH   E 3 .   ? 52.889 -13.380 -20.432 1.00 36.10 ?  217 HOH   B O    1 
HETATM 5699 O O    . HOH   E 3 .   ? 29.927 -26.329 3.961   1.00 25.69 ?  218 HOH   B O    1 
HETATM 5700 O O    . HOH   E 3 .   ? 57.710 -24.420 4.968   1.00 31.76 ?  219 HOH   B O    1 
HETATM 5701 O O    . HOH   E 3 .   ? 50.730 -6.109  0.167   1.00 27.34 ?  220 HOH   B O    1 
HETATM 5702 O O    . HOH   E 3 .   ? 55.276 -16.359 -14.407 1.00 31.05 ?  221 HOH   B O    1 
HETATM 5703 O O    . HOH   E 3 .   ? 45.163 -34.925 6.821   1.00 37.04 ?  222 HOH   B O    1 
HETATM 5704 O O    . HOH   E 3 .   ? 35.933 -43.239 -8.644  1.00 30.03 ?  223 HOH   B O    1 
HETATM 5705 O O    . HOH   E 3 .   ? 56.724 -30.729 -7.837  1.00 32.26 ?  224 HOH   B O    1 
HETATM 5706 O O    . HOH   E 3 .   ? 57.365 -16.200 -12.237 1.00 18.10 ?  225 HOH   B O    1 
HETATM 5707 O O    . HOH   E 3 .   ? 30.860 -28.788 4.235   1.00 23.67 ?  226 HOH   B O    1 
HETATM 5708 O O    . HOH   E 3 .   ? 44.462 -7.267  2.131   1.00 33.20 ?  227 HOH   B O    1 
HETATM 5709 O O    . HOH   E 3 .   ? 39.332 -10.919 6.079   1.00 25.35 ?  228 HOH   B O    1 
HETATM 5710 O O    . HOH   E 3 .   ? 37.112 -19.755 -18.108 1.00 33.67 ?  229 HOH   B O    1 
HETATM 5711 O O    . HOH   E 3 .   ? 34.534 -36.343 -7.279  1.00 16.05 ?  230 HOH   B O    1 
HETATM 5712 O O    . HOH   E 3 .   ? 40.622 -16.092 14.078  1.00 23.59 ?  231 HOH   B O    1 
HETATM 5713 O O    . HOH   E 3 .   ? 41.364 -9.684  13.028  1.00 20.59 ?  232 HOH   B O    1 
HETATM 5714 O O    . HOH   E 3 .   ? 48.548 -36.448 -15.567 1.00 38.42 ?  233 HOH   B O    1 
HETATM 5715 O O    . HOH   E 3 .   ? 41.471 -39.116 -14.962 1.00 20.15 ?  234 HOH   B O    1 
HETATM 5716 O O    . HOH   E 3 .   ? 32.805 -43.756 -11.398 1.00 18.24 ?  235 HOH   B O    1 
HETATM 5717 O O    . HOH   E 3 .   ? 57.179 -26.800 -7.698  1.00 38.24 ?  236 HOH   B O    1 
HETATM 5718 O O    . HOH   E 3 .   ? 35.092 -7.999  -3.065  1.00 17.04 ?  237 HOH   B O    1 
HETATM 5719 O O    . HOH   E 3 .   ? 25.454 -26.008 -1.396  1.00 30.32 ?  238 HOH   B O    1 
HETATM 5720 O O    . HOH   E 3 .   ? 50.719 -12.978 -0.510  1.00 11.40 ?  239 HOH   B O    1 
HETATM 5721 O O    . HOH   E 3 .   ? 28.368 -19.644 -13.140 1.00 22.77 ?  240 HOH   B O    1 
HETATM 5722 O O    . HOH   E 3 .   ? 42.565 -25.385 2.585   1.00 14.13 ?  241 HOH   B O    1 
HETATM 5723 O O    . HOH   E 3 .   ? 43.106 -43.221 -8.320  1.00 26.93 ?  242 HOH   B O    1 
HETATM 5724 O O    . HOH   E 3 .   ? 46.353 -1.599  13.264  1.00 28.74 ?  243 HOH   B O    1 
HETATM 5725 O O    . HOH   E 3 .   ? 51.643 -6.516  4.397   1.00 18.67 ?  244 HOH   B O    1 
HETATM 5726 O O    . HOH   E 3 .   ? 39.483 -11.143 0.278   1.00 16.01 ?  245 HOH   B O    1 
HETATM 5727 O O    . HOH   E 3 .   ? 44.526 -27.834 -0.785  1.00 20.73 ?  246 HOH   B O    1 
HETATM 5728 O O    . HOH   E 3 .   ? 42.644 -22.888 3.794   1.00 10.66 ?  247 HOH   B O    1 
HETATM 5729 O O    . HOH   E 3 .   ? 57.605 -24.383 -3.888  1.00 20.78 ?  248 HOH   B O    1 
HETATM 5730 O O    . HOH   E 3 .   ? 44.996 -43.502 -10.564 1.00 26.94 ?  249 HOH   B O    1 
HETATM 5731 O O    . HOH   E 3 .   ? 43.187 -32.348 -17.139 1.00 21.29 ?  250 HOH   B O    1 
HETATM 5732 O O    . HOH   E 3 .   ? 51.535 -13.886 10.884  1.00 29.03 ?  251 HOH   B O    1 
HETATM 5733 O O    . HOH   E 3 .   ? 40.324 -12.739 -11.572 1.00 14.13 ?  252 HOH   B O    1 
HETATM 5734 O O    . HOH   E 3 .   ? 38.927 -12.092 12.322  1.00 33.24 ?  253 HOH   B O    1 
HETATM 5735 O O    . HOH   E 3 .   ? 34.179 -18.556 11.351  1.00 21.36 ?  254 HOH   B O    1 
HETATM 5736 O O    . HOH   E 3 .   ? 58.132 -10.608 -4.104  1.00 19.99 ?  255 HOH   B O    1 
HETATM 5737 O O    . HOH   E 3 .   ? 29.713 -25.206 -10.882 1.00 14.69 ?  256 HOH   B O    1 
HETATM 5738 O O    . HOH   E 3 .   ? 38.446 -11.053 -2.289  1.00 17.77 ?  257 HOH   B O    1 
HETATM 5739 O O    . HOH   E 3 .   ? 49.742 -0.552  10.246  1.00 31.87 ?  258 HOH   B O    1 
HETATM 5740 O O    . HOH   E 3 .   ? 34.849 -24.663 13.807  1.00 26.43 ?  259 HOH   B O    1 
HETATM 5741 O O    . HOH   E 3 .   ? 41.878 -23.558 9.259   1.00 15.70 ?  260 HOH   B O    1 
HETATM 5742 O O    . HOH   E 3 .   ? 30.852 -15.745 2.606   1.00 12.18 ?  261 HOH   B O    1 
HETATM 5743 O O    . HOH   E 3 .   ? 48.011 -22.778 5.771   1.00 15.69 ?  262 HOH   B O    1 
HETATM 5744 O O    . HOH   E 3 .   ? 57.489 -9.252  1.405   1.00 18.67 ?  263 HOH   B O    1 
HETATM 5745 O O    . HOH   E 3 .   ? 33.506 -17.033 7.997   1.00 18.11 ?  264 HOH   B O    1 
HETATM 5746 O O    . HOH   E 3 .   ? 49.323 -28.688 -6.986  1.00 14.22 ?  265 HOH   B O    1 
HETATM 5747 O O    . HOH   E 3 .   ? 27.146 -31.811 -10.046 1.00 19.56 ?  266 HOH   B O    1 
HETATM 5748 O O    . HOH   E 3 .   ? 50.983 -39.925 -8.357  1.00 27.66 ?  267 HOH   B O    1 
HETATM 5749 O O    . HOH   E 3 .   ? 28.468 -30.742 -14.858 1.00 27.35 ?  268 HOH   B O    1 
HETATM 5750 O O    . HOH   E 3 .   ? 43.378 -15.783 -12.224 1.00 12.94 ?  269 HOH   B O    1 
HETATM 5751 O O    . HOH   E 3 .   ? 57.112 -12.132 12.284  1.00 36.40 ?  270 HOH   B O    1 
HETATM 5752 O O    . HOH   E 3 .   ? 31.809 -17.962 -14.601 1.00 29.33 ?  271 HOH   B O    1 
HETATM 5753 O O    . HOH   E 3 .   ? 28.270 -34.336 -9.497  1.00 18.87 ?  272 HOH   B O    1 
HETATM 5754 O O    . HOH   E 3 .   ? 34.474 -12.794 2.576   1.00 24.44 ?  273 HOH   B O    1 
HETATM 5755 O O    . HOH   E 3 .   ? 56.953 -8.684  8.397   1.00 18.94 ?  274 HOH   B O    1 
HETATM 5756 O O    . HOH   E 3 .   ? 56.169 -23.459 -14.820 1.00 24.93 ?  275 HOH   B O    1 
HETATM 5757 O O    . HOH   E 3 .   ? 47.968 -24.448 -17.885 1.00 29.75 ?  276 HOH   B O    1 
HETATM 5758 O O    . HOH   E 3 .   ? 30.587 -42.231 -10.651 1.00 27.82 ?  277 HOH   B O    1 
HETATM 5759 O O    . HOH   E 3 .   ? 46.609 -31.247 -4.857  1.00 20.58 ?  278 HOH   B O    1 
HETATM 5760 O O    . HOH   E 3 .   ? 42.303 -9.896  9.324   1.00 20.07 ?  279 HOH   B O    1 
HETATM 5761 O O    . HOH   E 3 .   ? 48.405 -25.057 3.056   1.00 12.15 ?  280 HOH   B O    1 
HETATM 5762 O O    . HOH   E 3 .   ? 27.954 -22.896 -8.053  1.00 15.67 ?  281 HOH   B O    1 
HETATM 5763 O O    . HOH   E 3 .   ? 41.220 -5.501  11.497  1.00 42.29 ?  282 HOH   B O    1 
HETATM 5764 O O    . HOH   E 3 .   ? 34.896 -33.362 -19.285 1.00 26.68 ?  283 HOH   B O    1 
HETATM 5765 O O    . HOH   E 3 .   ? 33.530 -15.291 -14.006 1.00 19.57 ?  284 HOH   B O    1 
HETATM 5766 O O    . HOH   E 3 .   ? 46.856 -29.562 9.782   1.00 30.26 ?  285 HOH   B O    1 
HETATM 5767 O O    . HOH   E 3 .   ? 48.722 -20.058 5.881   1.00 13.07 ?  286 HOH   B O    1 
HETATM 5768 O O    . HOH   E 3 .   ? 42.794 -20.270 -20.794 1.00 33.85 ?  287 HOH   B O    1 
HETATM 5769 O O    . HOH   E 3 .   ? 42.398 -34.706 3.726   1.00 23.82 ?  288 HOH   B O    1 
HETATM 5770 O O    . HOH   E 3 .   ? 36.826 -12.780 -1.547  1.00 25.18 ?  289 HOH   B O    1 
HETATM 5771 O O    . HOH   E 3 .   ? 42.219 -10.042 -14.993 1.00 32.47 ?  290 HOH   B O    1 
HETATM 5772 O O    . HOH   E 3 .   ? 51.233 -37.567 -9.679  1.00 23.77 ?  291 HOH   B O    1 
HETATM 5773 O O    . HOH   E 3 .   ? 37.352 -35.682 7.159   1.00 31.85 ?  292 HOH   B O    1 
HETATM 5774 O O    . HOH   E 3 .   ? 35.094 -33.617 4.462   1.00 26.48 ?  293 HOH   B O    1 
HETATM 5775 O O    . HOH   E 3 .   ? 45.360 -33.367 -16.010 1.00 21.16 ?  294 HOH   B O    1 
HETATM 5776 O O    . HOH   E 3 .   ? 42.656 -12.260 -18.515 1.00 26.69 ?  295 HOH   B O    1 
HETATM 5777 O O    . HOH   E 3 .   ? 52.623 -35.594 -8.677  1.00 26.66 ?  296 HOH   B O    1 
HETATM 5778 O O    . HOH   E 3 .   ? 45.906 -40.376 -3.715  1.00 26.48 ?  297 HOH   B O    1 
HETATM 5779 O O    . HOH   E 3 .   ? 47.074 -33.967 -4.689  1.00 15.53 ?  298 HOH   B O    1 
HETATM 5780 O O    . HOH   E 3 .   ? 52.494 -10.448 12.989  1.00 21.11 ?  299 HOH   B O    1 
HETATM 5781 O O    . HOH   E 3 .   ? 40.225 -10.823 -9.565  1.00 15.75 ?  300 HOH   B O    1 
HETATM 5782 O O    . HOH   E 3 .   ? 27.545 -26.704 -15.700 1.00 31.32 ?  301 HOH   B O    1 
HETATM 5783 O O    . HOH   E 3 .   ? 59.749 -15.446 8.139   1.00 29.36 ?  302 HOH   B O    1 
HETATM 5784 O O    . HOH   E 3 .   ? 44.612 -27.467 1.918   1.00 14.36 ?  303 HOH   B O    1 
HETATM 5785 O O    . HOH   E 3 .   ? 57.679 -22.136 3.014   1.00 25.36 ?  304 HOH   B O    1 
HETATM 5786 O O    . HOH   E 3 .   ? 62.791 -20.250 -0.898  1.00 37.27 ?  305 HOH   B O    1 
HETATM 5787 O O    . HOH   E 3 .   ? 52.546 -29.212 -13.074 1.00 22.90 ?  306 HOH   B O    1 
HETATM 5788 O O    . HOH   E 3 .   ? 50.052 -24.584 5.818   1.00 32.11 ?  307 HOH   B O    1 
HETATM 5789 O O    . HOH   E 3 .   ? 43.515 -15.333 18.184  1.00 28.72 ?  308 HOH   B O    1 
HETATM 5790 O O    . HOH   E 3 .   ? 44.036 -29.359 -4.736  1.00 21.78 ?  309 HOH   B O    1 
HETATM 5791 O O    . HOH   E 3 .   ? 37.810 -10.240 -10.788 1.00 15.95 ?  310 HOH   B O    1 
HETATM 5792 O O    . HOH   E 3 .   ? 52.978 -15.953 -12.805 1.00 26.48 ?  311 HOH   B O    1 
HETATM 5793 O O    . HOH   E 3 .   ? 32.811 -34.593 -5.981  1.00 15.05 ?  312 HOH   B O    1 
HETATM 5794 O O    . HOH   E 3 .   ? 53.431 -30.207 4.482   1.00 17.88 ?  313 HOH   B O    1 
HETATM 5795 O O    . HOH   E 3 .   ? 48.143 -32.600 -16.684 1.00 43.03 ?  314 HOH   B O    1 
HETATM 5796 O O    . HOH   E 3 .   ? 62.640 -13.563 4.704   1.00 26.85 ?  315 HOH   B O    1 
HETATM 5797 O O    . HOH   E 3 .   ? 41.730 -8.091  1.340   1.00 23.75 ?  316 HOH   B O    1 
HETATM 5798 O O    . HOH   E 3 .   ? 37.512 -18.231 13.108  1.00 26.67 ?  317 HOH   B O    1 
HETATM 5799 O O    . HOH   E 3 .   ? 38.355 -9.351  -13.317 1.00 25.37 ?  318 HOH   B O    1 
HETATM 5800 O O    . HOH   E 3 .   ? 59.930 -17.150 -10.486 1.00 32.25 ?  319 HOH   B O    1 
HETATM 5801 O O    . HOH   E 3 .   ? 43.203 -21.449 10.633  1.00 14.33 ?  320 HOH   B O    1 
HETATM 5802 O O    . HOH   E 3 .   ? 25.948 -21.494 -3.571  1.00 14.79 ?  321 HOH   B O    1 
HETATM 5803 O O    . HOH   E 3 .   ? 38.340 -12.797 7.911   1.00 17.00 ?  322 HOH   B O    1 
HETATM 5804 O O    . HOH   E 3 .   ? 51.360 -32.887 -10.860 1.00 35.43 ?  323 HOH   B O    1 
HETATM 5805 O O    . HOH   E 3 .   ? 39.506 -23.409 -20.305 1.00 33.58 ?  324 HOH   B O    1 
HETATM 5806 O O    . HOH   E 3 .   ? 26.328 -21.038 -6.297  1.00 15.13 ?  325 HOH   B O    1 
HETATM 5807 O O    . HOH   E 3 .   ? 41.329 -24.487 15.769  1.00 41.68 ?  326 HOH   B O    1 
HETATM 5808 O O    . HOH   E 3 .   ? 37.160 -30.610 -21.109 1.00 29.26 ?  327 HOH   B O    1 
HETATM 5809 O O    . HOH   E 3 .   ? 44.588 -24.645 9.520   1.00 18.34 ?  328 HOH   B O    1 
HETATM 5810 O O    . HOH   E 3 .   ? 33.648 -31.147 11.049  1.00 34.25 ?  329 HOH   B O    1 
HETATM 5811 O O    . HOH   E 3 .   ? 43.129 -34.608 0.011   1.00 19.63 ?  330 HOH   B O    1 
HETATM 5812 O O    . HOH   E 3 .   ? 36.703 -12.431 4.257   1.00 18.35 ?  331 HOH   B O    1 
HETATM 5813 O O    . HOH   E 3 .   ? 45.766 -36.234 -16.169 1.00 31.75 ?  332 HOH   B O    1 
HETATM 5814 O O    . HOH   E 3 .   ? 51.720 -5.907  -7.933  1.00 42.53 ?  333 HOH   B O    1 
HETATM 5815 O O    . HOH   E 3 .   ? 27.958 -14.780 -9.478  1.00 32.70 ?  334 HOH   B O    1 
HETATM 5816 O O    . HOH   E 3 .   ? 47.176 -24.516 8.099   1.00 24.11 ?  335 HOH   B O    1 
HETATM 5817 O O    . HOH   E 3 .   ? 53.658 -12.520 -22.336 1.00 32.08 ?  336 HOH   B O    1 
HETATM 5818 O O    . HOH   E 3 .   ? 42.871 -43.451 -14.472 1.00 41.91 ?  337 HOH   B O    1 
HETATM 5819 O O    . HOH   E 3 .   ? 48.570 -11.877 -13.924 1.00 26.01 ?  338 HOH   B O    1 
HETATM 5820 O O    . HOH   E 3 .   ? 47.469 -27.446 1.953   1.00 13.94 ?  339 HOH   B O    1 
HETATM 5821 O O    . HOH   E 3 .   ? 44.178 -1.691  7.593   1.00 41.66 ?  340 HOH   B O    1 
HETATM 5822 O O    . HOH   E 3 .   ? 46.811 -19.926 12.266  1.00 29.57 ?  341 HOH   B O    1 
HETATM 5823 O O    . HOH   E 3 .   ? 37.083 -45.136 -9.862  1.00 34.81 ?  342 HOH   B O    1 
HETATM 5824 O O    . HOH   E 3 .   ? 37.012 -15.027 -16.537 1.00 37.59 ?  343 HOH   B O    1 
HETATM 5825 O O    . HOH   E 3 .   ? 28.872 -42.881 -12.407 1.00 37.11 ?  344 HOH   B O    1 
HETATM 5826 O O    . HOH   E 3 .   ? 32.986 -14.695 0.985   1.00 18.14 ?  345 HOH   B O    1 
HETATM 5827 O O    . HOH   E 3 .   ? 39.780 -44.244 -11.289 1.00 37.40 ?  346 HOH   B O    1 
HETATM 5828 O O    . HOH   E 3 .   ? 38.446 -12.259 -16.276 1.00 38.31 ?  347 HOH   B O    1 
HETATM 5829 O O    . HOH   E 3 .   ? 40.402 -43.435 -9.226  1.00 25.48 ?  348 HOH   B O    1 
HETATM 5830 O O    . HOH   E 3 .   ? 38.576 -22.375 15.015  1.00 37.92 ?  349 HOH   B O    1 
HETATM 5831 O O    . HOH   E 3 .   ? 27.771 -26.640 -0.631  1.00 27.67 ?  350 HOH   B O    1 
HETATM 5832 O O    . HOH   E 3 .   ? 33.755 -9.248  -8.839  1.00 29.07 ?  351 HOH   B O    1 
HETATM 5833 O O    . HOH   E 3 .   ? 55.636 -8.267  10.788  1.00 23.61 ?  352 HOH   B O    1 
HETATM 5834 O O    . HOH   E 3 .   ? 62.505 -20.172 -4.977  1.00 41.76 ?  353 HOH   B O    1 
HETATM 5835 O O    . HOH   E 3 .   ? 44.139 -37.296 -17.884 1.00 33.31 ?  354 HOH   B O    1 
HETATM 5836 O O    . HOH   E 3 .   ? 36.066 -8.569  -9.741  1.00 33.56 ?  355 HOH   B O    1 
HETATM 5837 O O    . HOH   E 3 .   ? 56.551 -7.288  3.070   1.00 29.64 ?  356 HOH   B O    1 
HETATM 5838 O O    . HOH   E 3 .   ? 23.211 -23.705 6.733   1.00 31.07 ?  357 HOH   B O    1 
HETATM 5839 O O    . HOH   E 3 .   ? 34.666 -10.339 7.418   1.00 23.51 ?  358 HOH   B O    1 
HETATM 5840 O O    . HOH   E 3 .   ? 61.488 -19.859 1.614   1.00 32.11 ?  359 HOH   B O    1 
HETATM 5841 O O    . HOH   E 3 .   ? 34.136 -7.816  11.411  1.00 40.28 ?  360 HOH   B O    1 
HETATM 5842 O O    . HOH   E 3 .   ? 43.175 -12.669 -21.239 1.00 37.42 ?  361 HOH   B O    1 
HETATM 5843 O O    . HOH   E 3 .   ? 40.234 -8.822  9.874   1.00 35.54 ?  362 HOH   B O    1 
HETATM 5844 O O    . HOH   E 3 .   ? 56.942 -21.522 -16.497 1.00 37.29 ?  363 HOH   B O    1 
HETATM 5845 O O    . HOH   E 3 .   ? 27.154 -25.960 -11.507 1.00 30.98 ?  364 HOH   B O    1 
HETATM 5846 O O    . HOH   E 3 .   ? 54.217 -5.749  2.982   1.00 35.66 ?  365 HOH   B O    1 
HETATM 5847 O O    . HOH   E 3 .   ? 32.459 -23.608 14.031  1.00 37.11 ?  366 HOH   B O    1 
HETATM 5848 O O    . HOH   E 3 .   ? 39.883 -7.074  7.820   1.00 38.41 ?  367 HOH   B O    1 
HETATM 5849 O O    . HOH   E 3 .   ? 36.224 -8.771  8.994   1.00 36.25 ?  368 HOH   B O    1 
HETATM 5850 O O    . HOH   E 3 .   ? 59.027 -10.498 9.097   1.00 35.11 ?  369 HOH   B O    1 
HETATM 5851 O O    . HOH   E 3 .   ? 40.049 -11.376 -13.994 1.00 30.26 ?  370 HOH   B O    1 
HETATM 5852 O O    . HOH   E 3 .   ? 48.433 -26.537 8.734   1.00 37.83 ?  371 HOH   B O    1 
HETATM 5853 O O    . HOH   E 3 .   ? 56.048 -7.831  -0.593  1.00 37.14 ?  372 HOH   B O    1 
HETATM 5854 O O    . HOH   E 3 .   ? 41.793 -9.997  -17.477 1.00 51.83 ?  373 HOH   B O    1 
HETATM 5855 O O    . HOH   E 3 .   ? 52.038 -12.928 13.301  1.00 31.21 ?  374 HOH   B O    1 
HETATM 5856 O O    . HOH   E 3 .   ? 38.019 -10.603 10.053  1.00 27.32 ?  375 HOH   B O    1 
HETATM 5857 O O    . HOH   E 3 .   ? 63.015 -12.367 6.894   1.00 34.94 ?  376 HOH   B O    1 
HETATM 5858 O O    . HOH   E 3 .   ? 44.082 -5.623  -3.546  1.00 38.80 ?  377 HOH   B O    1 
HETATM 5859 O O    . HOH   E 3 .   ? 41.834 -6.800  -4.863  1.00 44.65 ?  378 HOH   B O    1 
HETATM 5860 O O    . HOH   E 3 .   ? 36.513 -22.846 13.254  1.00 23.54 ?  379 HOH   B O    1 
HETATM 5861 O O    . HOH   E 3 .   ? 42.660 -17.086 -23.237 1.00 40.53 ?  380 HOH   B O    1 
HETATM 5862 O O    . HOH   E 3 .   ? 40.111 -7.660  3.214   1.00 33.02 ?  381 HOH   B O    1 
HETATM 5863 O O    . HOH   E 3 .   ? 39.735 -14.096 15.688  1.00 47.25 ?  382 HOH   B O    1 
HETATM 5864 O O    . HOH   E 3 .   ? 52.803 -29.902 7.106   1.00 22.27 ?  383 HOH   B O    1 
HETATM 5865 O O    . HOH   E 3 .   ? 60.445 -22.244 2.759   1.00 42.37 ?  384 HOH   B O    1 
HETATM 5866 O O    . HOH   E 3 .   ? 41.005 -9.807  15.772  1.00 43.43 ?  385 HOH   B O    1 
HETATM 5867 O O    . HOH   E 3 .   ? 35.393 -33.719 7.235   1.00 38.25 ?  386 HOH   B O    1 
HETATM 5868 O O    . HOH   E 3 .   ? 23.911 -20.851 -7.759  1.00 25.51 ?  387 HOH   B O    1 
HETATM 5869 O O    . HOH   E 3 .   ? 46.866 -5.354  2.912   1.00 38.35 ?  388 HOH   B O    1 
HETATM 5870 O O    . HOH   E 3 .   ? 35.288 -20.324 13.313  1.00 28.21 ?  389 HOH   B O    1 
HETATM 5871 O O    . HOH   E 3 .   ? 25.780 -18.943 -12.017 1.00 35.10 ?  390 HOH   B O    1 
HETATM 5872 O O    . HOH   E 3 .   ? 40.675 -6.645  -0.882  1.00 23.46 ?  391 HOH   B O    1 
HETATM 5873 O O    . HOH   E 3 .   ? 44.126 -31.781 -3.943  1.00 32.30 ?  392 HOH   B O    1 
HETATM 5874 O O    . HOH   E 3 .   ? 27.952 -27.124 2.189   1.00 30.13 ?  393 HOH   B O    1 
HETATM 5875 O O    . HOH   E 3 .   ? 26.602 -27.950 -13.545 1.00 34.17 ?  394 HOH   B O    1 
HETATM 5876 O O    . HOH   E 3 .   ? 50.598 -30.818 8.642   1.00 26.99 ?  395 HOH   B O    1 
HETATM 5877 O O    . HOH   E 3 .   ? 24.611 -20.661 -10.475 1.00 35.34 ?  396 HOH   B O    1 
HETATM 5878 O O    . HOH   E 3 .   ? 34.413 -33.491 9.562   1.00 31.84 ?  397 HOH   B O    1 
HETATM 5879 O O    . HOH   E 3 .   ? 26.848 -30.611 -12.736 1.00 26.16 ?  398 HOH   B O    1 
HETATM 5880 O O    . HOH   E 3 .   ? 45.797 -20.309 15.122  1.00 45.69 ?  399 HOH   B O    1 
HETATM 5881 O O    . HOH   E 3 .   ? 57.694 -6.472  -2.391  1.00 34.74 ?  400 HOH   B O    1 
HETATM 5882 O O    . HOH   E 3 .   ? 40.867 -11.841 -22.354 1.00 42.09 ?  401 HOH   B O    1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N   A VAL   A 3   ? 0.5158 0.4928 0.5890 -0.0099 -0.0296 0.0817  3   VAL   A N   
2    N N   B VAL   A 3   ? 0.4728 0.4750 0.5395 -0.0053 -0.0047 0.0093  3   VAL   A N   
3    C CA  A VAL   A 3   ? 0.5136 0.4906 0.5770 -0.0120 -0.0278 0.0808  3   VAL   A CA  
4    C CA  B VAL   A 3   ? 0.4709 0.4733 0.5342 -0.0061 -0.0043 0.0091  3   VAL   A CA  
5    C C   A VAL   A 3   ? 0.4984 0.4813 0.5385 -0.0187 -0.0321 0.0824  3   VAL   A C   
6    C C   B VAL   A 3   ? 0.4595 0.4648 0.5081 -0.0093 -0.0046 0.0089  3   VAL   A C   
7    O O   A VAL   A 3   ? 0.5005 0.4823 0.5482 -0.0162 -0.0343 0.0844  3   VAL   A O   
8    O O   B VAL   A 3   ? 0.4614 0.4663 0.5131 -0.0086 -0.0053 0.0094  3   VAL   A O   
9    C CB  A VAL   A 3   ? 0.5246 0.4962 0.5931 -0.0094 -0.0220 0.0791  3   VAL   A CB  
10   C CB  B VAL   A 3   ? 0.4783 0.4786 0.5503 -0.0044 -0.0035 0.0092  3   VAL   A CB  
11   C CG1 A VAL   A 3   ? 0.5290 0.4981 0.5963 -0.0083 -0.0209 0.0776  3   VAL   A CG1 
12   C CG1 B VAL   A 3   ? 0.4809 0.4803 0.5546 -0.0038 -0.0034 0.0090  3   VAL   A CG1 
13   C CG2 A VAL   A 3   ? 0.5280 0.4982 0.5958 -0.0089 -0.0193 0.0813  3   VAL   A CG2 
14   C CG2 B VAL   A 3   ? 0.4809 0.4805 0.5546 -0.0039 -0.0031 0.0097  3   VAL   A CG2 
31   N N   A ASN   A 4   ? 0.4780 0.4695 0.4780 -0.0278 -0.0341 0.0813  4   ASN   A N   
32   N N   B ASN   A 4   ? 0.4442 0.4533 0.4736 -0.0136 -0.0040 0.0078  4   ASN   A N   
33   C CA  A ASN   A 4   ? 0.4553 0.4563 0.4114 -0.0384 -0.0327 0.0771  4   ASN   A CA  
34   C CA  B ASN   A 4   ? 0.4273 0.4406 0.4367 -0.0189 -0.0025 0.0061  4   ASN   A CA  
35   C C   A ASN   A 4   ? 0.4249 0.4402 0.3666 -0.0504 -0.0182 0.0579  4   ASN   A C   
36   C C   B ASN   A 4   ? 0.4042 0.4249 0.4097 -0.0277 0.0032  0.0027  4   ASN   A C   
37   O O   A ASN   A 4   ? 0.4231 0.4387 0.3546 -0.0532 -0.0187 0.0643  4   ASN   A O   
38   O O   B ASN   A 4   ? 0.4049 0.4254 0.4109 -0.0271 0.0028  0.0041  4   ASN   A O   
39   C CB  A ASN   A 4   ? 0.4591 0.4574 0.3847 -0.0368 -0.0446 0.0901  4   ASN   A CB  
40   C CB  B ASN   A 4   ? 0.4317 0.4422 0.4244 -0.0162 -0.0059 0.0076  4   ASN   A CB  
41   C CG  A ASN   A 4   ? 0.4605 0.4558 0.3541 -0.0372 -0.0570 0.1044  4   ASN   A CG  
42   C CG  B ASN   A 4   ? 0.4348 0.4429 0.4129 -0.0144 -0.0091 0.0088  4   ASN   A CG  
43   O OD1 A ASN   A 4   ? 0.4620 0.4540 0.3426 -0.0374 -0.0658 0.1122  4   ASN   A OD1 
44   O OD1 B ASN   A 4   ? 0.4358 0.4428 0.4098 -0.0140 -0.0103 0.0093  4   ASN   A OD1 
45   N ND2 A ASN   A 4   ? 0.4591 0.4552 0.3512 -0.0360 -0.0578 0.1115  4   ASN   A ND2 
46   N ND2 B ASN   A 4   ? 0.4357 0.4431 0.4106 -0.0135 -0.0099 0.0096  4   ASN   A ND2 
59   N N   A SER   A 5   ? 0.3944 0.4199 0.3277 -0.0601 -0.0032 0.0352  5   SER   A N   
60   N N   B SER   A 5   ? 0.3790 0.4073 0.3781 -0.0379 0.0100  -0.0023 5   SER   A N   
61   C CA  A SER   A 5   ? 0.3644 0.4009 0.3014 -0.0672 0.0140  0.0096  5   SER   A CA  
62   C CA  B SER   A 5   ? 0.3531 0.3891 0.3459 -0.0481 0.0178  -0.0075 5   SER   A CA  
63   C C   A SER   A 5   ? 0.3324 0.3759 0.2644 -0.0640 0.0216  -0.0122 5   SER   A C   
64   C C   B SER   A 5   ? 0.3245 0.3667 0.2973 -0.0586 0.0271  -0.0121 5   SER   A C   
65   O O   A SER   A 5   ? 0.3367 0.3851 0.2590 -0.0552 0.0173  -0.0313 5   SER   A O   
66   O O   B SER   A 5   ? 0.3253 0.3680 0.3027 -0.0589 0.0252  -0.0153 5   SER   A O   
67   C CB  A SER   A 5   ? 0.3683 0.4074 0.3153 -0.0753 0.0242  0.0072  5   SER   A CB  
68   C CB  B SER   A 5   ? 0.3552 0.3923 0.3575 -0.0477 0.0164  -0.0077 5   SER   A CB  
69   O OG  A SER   A 5   ? 0.3711 0.4101 0.3203 -0.0800 0.0333  0.0084  5   SER   A OG  
70   O OG  B SER   A 5   ? 0.3562 0.3942 0.3625 -0.0477 0.0156  -0.0077 5   SER   A OG  
81   N N   . PHE   A 6   ? 0.2937 0.3404 0.2380 -0.0690 0.0373  -0.0135 6   PHE   A N   
82   C CA  . PHE   A 6   ? 0.2398 0.2834 0.1898 -0.0725 0.0480  -0.0042 6   PHE   A CA  
83   C C   . PHE   A 6   ? 0.2306 0.2758 0.2090 -0.0737 0.0604  -0.0017 6   PHE   A C   
84   O O   . PHE   A 6   ? 0.2387 0.2837 0.2360 -0.0769 0.0552  0.0198  6   PHE   A O   
85   C CB  . PHE   A 6   ? 0.2170 0.2461 0.1717 -0.0596 0.0370  0.0028  6   PHE   A CB  
86   C CG  . PHE   A 6   ? 0.2043 0.2227 0.1629 -0.0453 0.0292  0.0134  6   PHE   A CG  
87   C CD1 . PHE   A 6   ? 0.1995 0.2165 0.1706 -0.0411 0.0180  0.0244  6   PHE   A CD1 
88   C CD2 . PHE   A 6   ? 0.2089 0.2164 0.1817 -0.0253 0.0317  0.0064  6   PHE   A CD2 
89   C CE1 . PHE   A 6   ? 0.2040 0.2148 0.1786 -0.0367 0.0194  0.0251  6   PHE   A CE1 
90   C CE2 . PHE   A 6   ? 0.2103 0.2155 0.1935 -0.0217 0.0251  0.0022  6   PHE   A CE2 
91   C CZ  . PHE   A 6   ? 0.2092 0.2130 0.1857 -0.0329 0.0229  0.0093  6   PHE   A CZ  
102  N N   A SER   A 7   ? 0.2219 0.2668 0.1978 -0.0715 0.0771  -0.0089 7   SER   A N   
103  N N   B SER   A 7   ? 0.2251 0.2703 0.2246 -0.0693 0.0607  -0.0078 7   SER   A N   
104  C CA  A SER   A 7   ? 0.2324 0.2706 0.2244 -0.0598 0.0763  -0.0195 7   SER   A CA  
105  C CA  B SER   A 7   ? 0.2220 0.2638 0.2409 -0.0642 0.0604  -0.0130 7   SER   A CA  
106  C C   A SER   A 7   ? 0.2178 0.2396 0.2197 -0.0576 0.0789  -0.0151 7   SER   A C   
107  C C   B SER   A 7   ? 0.2125 0.2470 0.2331 -0.0608 0.0679  -0.0172 7   SER   A C   
108  O O   A SER   A 7   ? 0.2247 0.2261 0.2286 -0.0611 0.0755  -0.0071 7   SER   A O   
109  O O   B SER   A 7   ? 0.2148 0.2465 0.2352 -0.0613 0.0669  -0.0158 7   SER   A O   
110  C CB  A SER   A 7   ? 0.2594 0.3033 0.2618 -0.0420 0.0763  -0.0234 7   SER   A CB  
111  C CB  B SER   A 7   ? 0.2289 0.2725 0.2623 -0.0604 0.0538  -0.0117 7   SER   A CB  
112  O OG  A SER   A 7   ? 0.2784 0.3208 0.3041 -0.0328 0.0740  -0.0242 7   SER   A OG  
113  O OG  B SER   A 7   ? 0.2341 0.2778 0.2769 -0.0575 0.0497  -0.0098 7   SER   A OG  
124  N N   . GLY   A 8   ? 0.2011 0.2305 0.2273 -0.0583 0.0766  -0.0222 8   GLY   A N   
125  C CA  . GLY   A 8   ? 0.1906 0.2097 0.2425 -0.0416 0.0696  -0.0206 8   GLY   A CA  
126  C C   . GLY   A 8   ? 0.1752 0.1971 0.2303 -0.0313 0.0577  -0.0136 8   GLY   A C   
127  O O   . GLY   A 8   ? 0.1757 0.2019 0.2632 -0.0112 0.0472  -0.0302 8   GLY   A O   
132  N N   . TYR   A 9   ? 0.1574 0.1822 0.2063 -0.0264 0.0499  0.0048  9   TYR   A N   
133  C CA  . TYR   A 9   ? 0.1526 0.1666 0.1787 -0.0204 0.0415  0.0098  9   TYR   A CA  
134  C C   . TYR   A 9   ? 0.1582 0.1557 0.1849 -0.0184 0.0358  0.0314  9   TYR   A C   
135  O O   . TYR   A 9   ? 0.1863 0.1788 0.2023 -0.0294 0.0313  0.0302  9   TYR   A O   
136  C CB  . TYR   A 9   ? 0.1448 0.1722 0.1875 -0.0144 0.0294  0.0013  9   TYR   A CB  
137  C CG  . TYR   A 9   ? 0.1414 0.1750 0.1829 -0.0054 0.0340  -0.0039 9   TYR   A CG  
138  C CD1 . TYR   A 9   ? 0.1450 0.1866 0.1953 -0.0132 0.0418  -0.0055 9   TYR   A CD1 
139  C CD2 . TYR   A 9   ? 0.1363 0.1645 0.1836 -0.0020 0.0304  0.0102  9   TYR   A CD2 
140  C CE1 . TYR   A 9   ? 0.1492 0.1899 0.2020 -0.0131 0.0451  -0.0127 9   TYR   A CE1 
141  C CE2 . TYR   A 9   ? 0.1397 0.1740 0.1877 -0.0007 0.0430  -0.0012 9   TYR   A CE2 
142  C CZ  . TYR   A 9   ? 0.1457 0.1860 0.2085 -0.0200 0.0502  -0.0035 9   TYR   A CZ  
143  O OH  . TYR   A 9   ? 0.1561 0.2006 0.2247 -0.0356 0.0576  -0.0096 9   TYR   A OH  
153  N N   . LEU   A 10  ? 0.1439 0.1445 0.1850 -0.0122 0.0288  0.0274  10  LEU   A N   
154  C CA  . LEU   A 10  ? 0.1335 0.1434 0.1811 -0.0157 0.0180  0.0375  10  LEU   A CA  
155  C C   . LEU   A 10  ? 0.1266 0.1373 0.1671 -0.0147 0.0128  0.0370  10  LEU   A C   
156  O O   . LEU   A 10  ? 0.1323 0.1356 0.1898 -0.0174 0.0325  0.0385  10  LEU   A O   
157  C CB  . LEU   A 10  ? 0.1377 0.1552 0.2216 -0.0174 0.0028  0.0482  10  LEU   A CB  
158  C CG  . LEU   A 10  ? 0.1646 0.1698 0.2755 -0.0116 -0.0311 0.0631  10  LEU   A CG  
159  C CD1 . LEU   A 10  ? 0.1893 0.1877 0.3320 -0.0196 -0.0206 0.0590  10  LEU   A CD1 
160  C CD2 . LEU   A 10  ? 0.1982 0.2000 0.3171 0.0011  -0.0229 0.0429  10  LEU   A CD2 
172  N N   . LYS   A 11  ? 0.1295 0.1419 0.1666 -0.0173 0.0141  0.0358  11  LYS   A N   
173  C CA  . LYS   A 11  ? 0.1328 0.1390 0.1590 -0.0194 0.0125  0.0372  11  LYS   A CA  
174  C C   . LYS   A 11  ? 0.1317 0.1464 0.1558 -0.0252 0.0136  0.0346  11  LYS   A C   
175  O O   . LYS   A 11  ? 0.1438 0.1914 0.1787 -0.0551 0.0215  0.0113  11  LYS   A O   
176  C CB  . LYS   A 11  ? 0.1379 0.1314 0.1577 -0.0184 0.0117  0.0258  11  LYS   A CB  
177  C CG  . LYS   A 11  ? 0.1481 0.1319 0.1522 -0.0187 0.0183  0.0266  11  LYS   A CG  
178  C CD  . LYS   A 11  ? 0.1629 0.1374 0.1570 -0.0133 0.0161  0.0248  11  LYS   A CD  
179  C CE  . LYS   A 11  ? 0.1703 0.1337 0.1529 -0.0110 0.0162  0.0308  11  LYS   A CE  
180  N NZ  . LYS   A 11  ? 0.1704 0.1379 0.1549 -0.0001 0.0047  0.0239  11  LYS   A NZ  
194  N N   . LEU   A 12  ? 0.1223 0.1401 0.1434 -0.0235 0.0100  0.0274  12  LEU   A N   
195  C CA  . LEU   A 12  ? 0.1225 0.1580 0.1485 -0.0198 0.0063  0.0364  12  LEU   A CA  
196  C C   . LEU   A 12  ? 0.1308 0.1488 0.1387 -0.0240 0.0117  0.0343  12  LEU   A C   
197  O O   . LEU   A 12  ? 0.1380 0.1551 0.1490 -0.0229 0.0046  0.0224  12  LEU   A O   
198  C CB  . LEU   A 12  ? 0.1305 0.1587 0.1665 -0.0201 0.0028  0.0447  12  LEU   A CB  
199  C CG  . LEU   A 12  ? 0.1394 0.1659 0.1831 -0.0153 0.0147  0.0472  12  LEU   A CG  
200  C CD1 . LEU   A 12  ? 0.1558 0.1739 0.1919 -0.0039 0.0218  0.0567  12  LEU   A CD1 
201  C CD2 . LEU   A 12  ? 0.1420 0.1736 0.2025 -0.0058 0.0069  0.0407  12  LEU   A CD2 
213  N N   . THR   A 13  ? 0.1256 0.1410 0.1488 -0.0242 0.0095  0.0262  13  THR   A N   
214  C CA  . THR   A 13  ? 0.1320 0.1380 0.1599 -0.0222 0.0126  0.0193  13  THR   A CA  
215  C C   . THR   A 13  ? 0.1312 0.1320 0.1593 -0.0222 0.0091  0.0252  13  THR   A C   
216  O O   . THR   A 13  ? 0.1343 0.1346 0.1644 -0.0149 0.0110  0.0226  13  THR   A O   
217  C CB  . THR   A 13  ? 0.1399 0.1514 0.1621 -0.0173 0.0230  0.0247  13  THR   A CB  
218  O OG1 . THR   A 13  ? 0.1366 0.1511 0.1730 -0.0234 0.0140  0.0245  13  THR   A OG1 
219  C CG2 . THR   A 13  ? 0.1495 0.1737 0.1887 -0.0186 0.0219  0.0173  13  THR   A CG2 
227  N N   . ASP   A 14  ? 0.1350 0.1349 0.1727 -0.0189 0.0102  0.0271  14  ASP   A N   
228  C CA  . ASP   A 14  ? 0.1373 0.1404 0.1787 -0.0161 0.0084  0.0353  14  ASP   A CA  
229  C C   . ASP   A 14  ? 0.1332 0.1417 0.1619 -0.0135 -0.0006 0.0425  14  ASP   A C   
230  O O   . ASP   A 14  ? 0.1510 0.1601 0.1809 -0.0276 -0.0099 0.0457  14  ASP   A O   
231  C CB  . ASP   A 14  ? 0.1633 0.1502 0.2287 -0.0196 0.0100  0.0528  14  ASP   A CB  
232  C CG  . ASP   A 14  ? 0.1800 0.2003 0.3172 -0.0168 0.0078  0.0516  14  ASP   A CG  
233  O OD1 . ASP   A 14  ? 0.1930 0.2163 0.3339 -0.0028 -0.0019 0.0569  14  ASP   A OD1 
234  O OD2 . ASP   A 14  ? 0.2036 0.2455 0.3739 -0.0113 -0.0027 0.0368  14  ASP   A OD2 
239  N N   . ASN   A 15  ? 0.1294 0.1331 0.1557 -0.0149 0.0127  0.0394  15  ASN   A N   
240  C CA  . ASN   A 15  ? 0.1271 0.1335 0.1723 -0.0182 0.0013  0.0289  15  ASN   A CA  
241  C C   . ASN   A 15  ? 0.1251 0.1306 0.1928 -0.0173 0.0077  0.0298  15  ASN   A C   
242  O O   . ASN   A 15  ? 0.1276 0.1353 0.2489 -0.0169 -0.0117 0.0305  15  ASN   A O   
243  C CB  . ASN   A 15  ? 0.1260 0.1307 0.1749 -0.0097 0.0020  0.0258  15  ASN   A CB  
244  C CG  . ASN   A 15  ? 0.1266 0.1397 0.1724 -0.0047 0.0080  0.0211  15  ASN   A CG  
245  O OD1 . ASN   A 15  ? 0.1399 0.1455 0.1894 -0.0224 0.0045  0.0211  15  ASN   A OD1 
246  N ND2 . ASN   A 15  ? 0.1289 0.1521 0.1683 -0.0166 0.0175  0.0211  15  ASN   A ND2 
253  N N   . VAL   A 16  ? 0.1259 0.1274 0.1751 -0.0128 0.0096  0.0277  16  VAL   A N   
254  C CA  . VAL   A 16  ? 0.1267 0.1239 0.1670 -0.0108 0.0121  0.0315  16  VAL   A CA  
255  C C   . VAL   A 16  ? 0.1236 0.1289 0.1538 -0.0107 0.0075  0.0317  16  VAL   A C   
256  O O   . VAL   A 16  ? 0.1170 0.1256 0.1681 -0.0145 0.0154  0.0215  16  VAL   A O   
257  C CB  . VAL   A 16  ? 0.1409 0.1420 0.1611 0.0039  0.0228  0.0404  16  VAL   A CB  
258  C CG1 . VAL   A 16  ? 0.1531 0.1536 0.1709 0.0091  0.0257  0.0427  16  VAL   A CG1 
259  C CG2 . VAL   A 16  ? 0.1501 0.1601 0.1845 0.0070  0.0412  0.0346  16  VAL   A CG2 
269  N N   . TYR   A 17  ? 0.1227 0.1276 0.1519 -0.0078 0.0202  0.0281  17  TYR   A N   
270  C CA  . TYR   A 17  ? 0.1254 0.1284 0.1447 -0.0123 0.0209  0.0328  17  TYR   A CA  
271  C C   . TYR   A 17  ? 0.1251 0.1258 0.1645 -0.0101 0.0171  0.0275  17  TYR   A C   
272  O O   . TYR   A 17  ? 0.1211 0.1295 0.1783 -0.0098 0.0222  0.0364  17  TYR   A O   
273  C CB  . TYR   A 17  ? 0.1426 0.1280 0.1485 -0.0125 0.0166  0.0254  17  TYR   A CB  
274  C CG  . TYR   A 17  ? 0.1567 0.1376 0.1544 -0.0185 0.0066  0.0206  17  TYR   A CG  
275  C CD1 . TYR   A 17  ? 0.1638 0.1513 0.1655 -0.0053 0.0037  0.0258  17  TYR   A CD1 
276  C CD2 . TYR   A 17  ? 0.1664 0.1432 0.1480 -0.0276 0.0062  0.0244  17  TYR   A CD2 
277  C CE1 . TYR   A 17  ? 0.1774 0.1503 0.1684 -0.0060 -0.0081 0.0247  17  TYR   A CE1 
278  C CE2 . TYR   A 17  ? 0.1825 0.1449 0.1498 -0.0272 0.0016  0.0134  17  TYR   A CE2 
279  C CZ  . TYR   A 17  ? 0.1881 0.1429 0.1585 -0.0164 -0.0114 0.0286  17  TYR   A CZ  
280  O OH  . TYR   A 17  ? 0.2013 0.1496 0.1692 -0.0191 -0.0116 0.0331  17  TYR   A OH  
290  N N   . ILE   A 18  ? 0.1247 0.1288 0.1740 -0.0101 0.0189  0.0383  18  ILE   A N   
291  C CA  . ILE   A 18  ? 0.1274 0.1317 0.1853 -0.0072 0.0266  0.0325  18  ILE   A CA  
292  C C   . ILE   A 18  ? 0.1300 0.1360 0.1938 -0.0107 0.0244  0.0346  18  ILE   A C   
293  O O   . ILE   A 18  ? 0.1299 0.1471 0.2006 -0.0128 0.0355  0.0378  18  ILE   A O   
294  C CB  . ILE   A 18  ? 0.1407 0.1413 0.1802 -0.0025 0.0225  0.0565  18  ILE   A CB  
295  C CG1 . ILE   A 18  ? 0.1562 0.1523 0.1848 -0.0000 0.0051  0.0620  18  ILE   A CG1 
296  C CG2 . ILE   A 18  ? 0.1445 0.1493 0.1926 -0.0101 0.0168  0.0508  18  ILE   A CG2 
297  C CD1 . ILE   A 18  ? 0.1852 0.1706 0.2131 -0.0001 -0.0073 0.0659  18  ILE   A CD1 
309  N N   . LYS   A 19  ? 0.1340 0.1352 0.2079 -0.0057 0.0431  0.0339  19  LYS   A N   
310  C CA  . LYS   A 19  ? 0.1495 0.1449 0.2406 0.0026  0.0500  0.0406  19  LYS   A CA  
311  C C   . LYS   A 19  ? 0.1415 0.1429 0.2671 0.0092  0.0487  0.0456  19  LYS   A C   
312  O O   . LYS   A 19  ? 0.1381 0.1401 0.2703 0.0069  0.0365  0.0538  19  LYS   A O   
313  C CB  . LYS   A 19  ? 0.1605 0.1597 0.2536 -0.0009 0.0584  0.0277  19  LYS   A CB  
314  C CG  . LYS   A 19  ? 0.1976 0.1795 0.2699 0.0021  0.0549  0.0077  19  LYS   A CG  
315  C CD  . LYS   A 19  ? 0.2278 0.2035 0.2733 0.0039  0.0574  0.0108  19  LYS   A CD  
316  C CE  . LYS   A 19  ? 0.2466 0.2132 0.2786 -0.0047 0.0556  0.0077  19  LYS   A CE  
317  N NZ  . LYS   A 19  ? 0.2572 0.2185 0.2707 -0.0215 0.0631  -0.0001 19  LYS   A NZ  
331  N N   . ASN   A 20  ? 0.1478 0.1419 0.2939 0.0052  0.0448  0.0478  20  ASN   A N   
332  C CA  . ASN   A 20  ? 0.1661 0.1633 0.3133 0.0282  0.0555  0.0405  20  ASN   A CA  
333  C C   . ASN   A 20  ? 0.1860 0.1586 0.3077 0.0184  0.0641  0.0294  20  ASN   A C   
334  O O   . ASN   A 20  ? 0.2112 0.1759 0.3168 -0.0065 0.0655  0.0173  20  ASN   A O   
335  C CB  . ASN   A 20  ? 0.1713 0.1852 0.3399 0.0440  0.0583  0.0575  20  ASN   A CB  
336  C CG  . ASN   A 20  ? 0.1898 0.1985 0.3822 0.0549  0.0596  0.0684  20  ASN   A CG  
337  O OD1 . ASN   A 20  ? 0.2200 0.2137 0.4233 0.0657  0.0759  0.0640  20  ASN   A OD1 
338  N ND2 . ASN   A 20  ? 0.1970 0.1971 0.3921 0.0512  0.0446  0.0750  20  ASN   A ND2 
345  N N   . ALA   A 21  ? 0.1864 0.1580 0.3057 0.0153  0.0538  0.0238  21  ALA   A N   
346  C CA  . ALA   A 21  ? 0.1891 0.1601 0.3025 0.0060  0.0522  0.0280  21  ALA   A CA  
347  C C   . ALA   A 21  ? 0.1769 0.1615 0.2902 0.0067  0.0598  0.0271  21  ALA   A C   
348  O O   . ALA   A 21  ? 0.1836 0.1763 0.2918 0.0068  0.0548  0.0213  21  ALA   A O   
349  C CB  . ALA   A 21  ? 0.2152 0.1728 0.3273 -0.0053 0.0321  0.0420  21  ALA   A CB  
355  N N   . ASP   A 22  ? 0.1803 0.1588 0.2874 -0.0041 0.0608  0.0244  22  ASP   A N   
356  C CA  . ASP   A 22  ? 0.1800 0.1681 0.2794 -0.0041 0.0474  0.0232  22  ASP   A CA  
357  C C   . ASP   A 22  ? 0.1650 0.1803 0.2312 -0.0108 0.0507  0.0254  22  ASP   A C   
358  O O   . ASP   A 22  ? 0.1734 0.1993 0.2392 -0.0098 0.0611  0.0246  22  ASP   A O   
359  C CB  . ASP   A 22  ? 0.2070 0.1774 0.3322 -0.0039 0.0414  0.0198  22  ASP   A CB  
360  C CG  . ASP   A 22  ? 0.2279 0.1875 0.3851 -0.0095 0.0240  0.0313  22  ASP   A CG  
361  O OD1 . ASP   A 22  ? 0.2224 0.1889 0.3982 -0.0224 0.0151  0.0581  22  ASP   A OD1 
362  O OD2 . ASP   A 22  ? 0.2535 0.1997 0.4220 -0.0022 0.0233  0.0166  22  ASP   A OD2 
367  N N   . ILE   A 23  ? 0.1696 0.1816 0.2114 -0.0058 0.0466  0.0206  23  ILE   A N   
368  C CA  . ILE   A 23  ? 0.1663 0.1749 0.1910 -0.0114 0.0423  0.0285  23  ILE   A CA  
369  C C   . ILE   A 23  ? 0.1665 0.1840 0.1858 -0.0134 0.0553  0.0149  23  ILE   A C   
370  O O   . ILE   A 23  ? 0.1744 0.1869 0.1830 -0.0033 0.0520  0.0071  23  ILE   A O   
371  C CB  . ILE   A 23  ? 0.1714 0.1709 0.1648 -0.0064 0.0318  0.0246  23  ILE   A CB  
372  C CG1 . ILE   A 23  ? 0.1759 0.1739 0.1600 -0.0041 0.0255  0.0113  23  ILE   A CG1 
373  C CG2 . ILE   A 23  ? 0.1779 0.1669 0.1709 -0.0096 0.0275  0.0280  23  ILE   A CG2 
374  C CD1 . ILE   A 23  ? 0.1794 0.1701 0.1640 -0.0052 0.0174  0.0042  23  ILE   A CD1 
386  N N   . VAL   A 24  ? 0.1797 0.1888 0.2098 -0.0219 0.0571  0.0154  24  VAL   A N   
387  C CA  . VAL   A 24  ? 0.1969 0.1953 0.2312 -0.0263 0.0534  0.0079  24  VAL   A CA  
388  C C   . VAL   A 24  ? 0.2023 0.2015 0.2277 -0.0285 0.0604  -0.0026 24  VAL   A C   
389  O O   . VAL   A 24  ? 0.2117 0.1971 0.2213 -0.0217 0.0557  -0.0066 24  VAL   A O   
390  C CB  . VAL   A 24  ? 0.2069 0.2059 0.2586 -0.0291 0.0566  0.0157  24  VAL   A CB  
391  C CG1 . VAL   A 24  ? 0.2164 0.2154 0.2838 -0.0282 0.0529  0.0101  24  VAL   A CG1 
392  C CG2 . VAL   A 24  ? 0.2199 0.2184 0.2691 -0.0239 0.0706  0.0324  24  VAL   A CG2 
402  N N   . GLU   A 25  ? 0.2087 0.2306 0.2379 -0.0287 0.0796  -0.0074 25  GLU   A N   
403  C CA  . GLU   A 25  ? 0.2311 0.2620 0.2499 -0.0241 0.0939  -0.0103 25  GLU   A CA  
404  C C   . GLU   A 25  ? 0.2244 0.2612 0.2111 -0.0377 0.0941  -0.0096 25  GLU   A C   
405  O O   . GLU   A 25  ? 0.2365 0.2721 0.2149 -0.0373 0.0966  -0.0112 25  GLU   A O   
406  C CB  . GLU   A 25  ? 0.2590 0.2881 0.2949 -0.0138 0.1067  -0.0081 25  GLU   A CB  
407  C CG  . GLU   A 25  ? 0.2907 0.3169 0.3567 -0.0088 0.0940  -0.0064 25  GLU   A CG  
408  C CD  . GLU   A 25  ? 0.3181 0.3455 0.4141 -0.0067 0.0806  -0.0030 25  GLU   A CD  
409  O OE1 . GLU   A 25  ? 0.3305 0.3582 0.4287 -0.0024 0.0650  -0.0056 25  GLU   A OE1 
410  O OE2 . GLU   A 25  ? 0.3306 0.3526 0.4424 -0.0075 0.0753  -0.0106 25  GLU   A OE2 
417  N N   A GLU   A 26  ? 0.2154 0.2524 0.2180 -0.0539 0.0921  -0.0149 26  GLU   A N   
418  N N   B GLU   A 26  ? 0.2212 0.2533 0.2083 -0.0422 0.0783  -0.0100 26  GLU   A N   
419  C CA  A GLU   A 26  ? 0.2289 0.2467 0.1965 -0.0669 0.0842  -0.0069 26  GLU   A CA  
420  C CA  B GLU   A 26  ? 0.2214 0.2460 0.2055 -0.0458 0.0630  -0.0090 26  GLU   A CA  
421  C C   A GLU   A 26  ? 0.2207 0.2290 0.1703 -0.0639 0.0701  -0.0103 26  GLU   A C   
422  C C   B GLU   A 26  ? 0.2143 0.2305 0.1837 -0.0528 0.0631  -0.0090 26  GLU   A C   
423  O O   A GLU   A 26  ? 0.2258 0.2278 0.1673 -0.0705 0.0644  -0.0083 26  GLU   A O   
424  O O   B GLU   A 26  ? 0.2157 0.2322 0.1842 -0.0537 0.0621  -0.0085 26  GLU   A O   
425  C CB  A GLU   A 26  ? 0.2578 0.2468 0.2370 -0.0822 0.0730  0.0048  26  GLU   A CB  
426  C CB  B GLU   A 26  ? 0.2281 0.2528 0.2282 -0.0415 0.0464  -0.0087 26  GLU   A CB  
427  C CG  A GLU   A 26  ? 0.2854 0.2551 0.2958 -0.0892 0.0750  -0.0008 26  GLU   A CG  
428  C CG  B GLU   A 26  ? 0.2342 0.2590 0.2540 -0.0366 0.0325  -0.0105 26  GLU   A CG  
429  C CD  A GLU   A 26  ? 0.3002 0.2543 0.3218 -0.1037 0.0996  -0.0037 26  GLU   A CD  
430  C CD  B GLU   A 26  ? 0.2380 0.2636 0.2713 -0.0329 0.0235  -0.0135 26  GLU   A CD  
431  O OE1 A GLU   A 26  ? 0.2916 0.2820 0.3131 -0.0890 0.1298  -0.0539 26  GLU   A OE1 
432  O OE1 B GLU   A 26  ? 0.2352 0.2706 0.2733 -0.0286 0.0212  -0.0181 26  GLU   A OE1 
433  O OE2 A GLU   A 26  ? 0.3216 0.2535 0.3375 -0.1023 0.1033  0.0142  26  GLU   A OE2 
434  O OE2 B GLU   A 26  ? 0.2431 0.2627 0.2812 -0.0316 0.0200  -0.0168 26  GLU   A OE2 
447  N N   . ALA   A 27  ? 0.2040 0.2124 0.1645 -0.0600 0.0643  -0.0093 27  ALA   A N   
448  C CA  . ALA   A 27  ? 0.2118 0.2092 0.1433 -0.0541 0.0597  -0.0111 27  ALA   A CA  
449  C C   . ALA   A 27  ? 0.2439 0.2184 0.1537 -0.0585 0.0664  -0.0283 27  ALA   A C   
450  O O   . ALA   A 27  ? 0.2515 0.2152 0.1562 -0.0613 0.0524  -0.0271 27  ALA   A O   
451  C CB  . ALA   A 27  ? 0.1951 0.1997 0.1452 -0.0522 0.0474  -0.0115 27  ALA   A CB  
458  N N   . LYS   A 28  ? 0.2775 0.2429 0.1817 -0.0573 0.0645  -0.0609 28  LYS   A N   
459  C CA  . LYS   A 28  ? 0.3181 0.2836 0.2217 -0.0554 0.0623  -0.0772 28  LYS   A CA  
460  C C   . LYS   A 28  ? 0.3346 0.3152 0.1975 -0.0628 0.0708  -0.0656 28  LYS   A C   
461  O O   . LYS   A 28  ? 0.3410 0.3268 0.2394 -0.0654 0.0526  -0.0559 28  LYS   A O   
462  C CB  . LYS   A 28  ? 0.3395 0.3017 0.2744 -0.0434 0.0554  -0.0967 28  LYS   A CB  
463  C CG  . LYS   A 28  ? 0.3563 0.3184 0.3282 -0.0340 0.0488  -0.1006 28  LYS   A CG  
464  C CD  . LYS   A 28  ? 0.3712 0.3408 0.3950 -0.0253 0.0391  -0.0923 28  LYS   A CD  
465  C CE  . LYS   A 28  ? 0.3833 0.3584 0.4415 -0.0226 0.0319  -0.0901 28  LYS   A CE  
466  N NZ  . LYS   A 28  ? 0.3901 0.3670 0.4731 -0.0184 0.0297  -0.0911 28  LYS   A NZ  
480  N N   . LYS   A 29  ? 0.3392 0.3362 0.1808 -0.0683 0.0985  -0.0467 29  LYS   A N   
481  C CA  . LYS   A 29  ? 0.3531 0.3631 0.2070 -0.0709 0.1085  -0.0276 29  LYS   A CA  
482  C C   . LYS   A 29  ? 0.3455 0.3542 0.1662 -0.0777 0.0975  -0.0208 29  LYS   A C   
483  O O   . LYS   A 29  ? 0.3559 0.3671 0.1762 -0.0699 0.0886  -0.0191 29  LYS   A O   
484  C CB  . LYS   A 29  ? 0.3699 0.3974 0.2749 -0.0660 0.1255  -0.0150 29  LYS   A CB  
485  C CG  . LYS   A 29  ? 0.3903 0.4246 0.3605 -0.0623 0.1245  -0.0069 29  LYS   A CG  
486  C CD  . LYS   A 29  ? 0.4087 0.4475 0.4403 -0.0592 0.1186  -0.0035 29  LYS   A CD  
487  C CE  . LYS   A 29  ? 0.4190 0.4640 0.4946 -0.0565 0.1163  -0.0043 29  LYS   A CE  
488  N NZ  . LYS   A 29  ? 0.4267 0.4736 0.5266 -0.0551 0.1149  -0.0073 29  LYS   A NZ  
502  N N   . VAL   A 30  ? 0.3246 0.3300 0.1507 -0.0897 0.0878  -0.0179 30  VAL   A N   
503  C CA  . VAL   A 30  ? 0.3148 0.3095 0.1480 -0.0999 0.0656  0.0038  30  VAL   A CA  
504  C C   . VAL   A 30  ? 0.3118 0.2933 0.1202 -0.0941 0.0521  0.0097  30  VAL   A C   
505  O O   . VAL   A 30  ? 0.3220 0.2960 0.1210 -0.0954 0.0434  0.0115  30  VAL   A O   
506  C CB  . VAL   A 30  ? 0.3105 0.3051 0.1841 -0.1076 0.0413  0.0134  30  VAL   A CB  
507  C CG1 . VAL   A 30  ? 0.3156 0.3051 0.1962 -0.1082 0.0250  0.0208  30  VAL   A CG1 
508  C CG2 . VAL   A 30  ? 0.3086 0.3090 0.2085 -0.1119 0.0421  0.0160  30  VAL   A CG2 
518  N N   . LYS   A 31  ? 0.2963 0.2720 0.1060 -0.0960 0.0380  0.0009  31  LYS   A N   
519  C CA  . LYS   A 31  ? 0.3087 0.2703 0.1135 -0.0870 0.0136  -0.0121 31  LYS   A CA  
520  C C   . LYS   A 31  ? 0.2916 0.2487 0.0923 -0.0684 0.0126  0.0208  31  LYS   A C   
521  O O   . LYS   A 31  ? 0.2984 0.2596 0.1193 -0.0643 -0.0008 0.0388  31  LYS   A O   
522  C CB  . LYS   A 31  ? 0.3524 0.3076 0.2177 -0.0867 -0.0088 -0.0354 31  LYS   A CB  
523  C CG  . LYS   A 31  ? 0.4018 0.3541 0.3575 -0.0780 -0.0267 -0.0401 31  LYS   A CG  
524  C CD  . LYS   A 31  ? 0.4348 0.3846 0.4645 -0.0710 -0.0423 -0.0428 31  LYS   A CD  
525  C CE  . LYS   A 31  ? 0.4569 0.4079 0.5305 -0.0672 -0.0572 -0.0490 31  LYS   A CE  
526  N NZ  . LYS   A 31  ? 0.4737 0.4227 0.5655 -0.0661 -0.0661 -0.0541 31  LYS   A NZ  
540  N N   . PRO   A 32  ? 0.2578 0.2227 0.0789 -0.0550 0.0159  0.0152  32  PRO   A N   
541  C CA  . PRO   A 32  ? 0.2501 0.2077 0.1099 -0.0505 0.0023  0.0223  32  PRO   A CA  
542  C C   . PRO   A 32  ? 0.2438 0.2024 0.1107 -0.0423 -0.0103 0.0295  32  PRO   A C   
543  O O   . PRO   A 32  ? 0.2369 0.1972 0.1269 -0.0462 -0.0199 0.0358  32  PRO   A O   
544  C CB  . PRO   A 32  ? 0.2459 0.2153 0.1234 -0.0487 0.0011  0.0176  32  PRO   A CB  
545  C CG  . PRO   A 32  ? 0.2380 0.2192 0.0808 -0.0488 -0.0022 0.0137  32  PRO   A CG  
546  C CD  . PRO   A 32  ? 0.2417 0.2162 0.0776 -0.0532 0.0073  0.0159  32  PRO   A CD  
554  N N   . THR   A 33  ? 0.2524 0.2008 0.1085 -0.0392 -0.0071 0.0359  33  THR   A N   
555  C CA  . THR   A 33  ? 0.2478 0.2037 0.1174 -0.0269 -0.0203 0.0366  33  THR   A CA  
556  C C   . THR   A 33  ? 0.2130 0.1875 0.1058 -0.0280 -0.0200 0.0245  33  THR   A C   
557  O O   . THR   A 33  ? 0.2058 0.1932 0.1145 -0.0322 -0.0355 0.0271  33  THR   A O   
558  C CB  . THR   A 33  ? 0.2730 0.2233 0.1378 -0.0205 -0.0358 0.0574  33  THR   A CB  
559  O OG1 . THR   A 33  ? 0.2940 0.2362 0.1698 -0.0097 -0.0251 0.0766  33  THR   A OG1 
560  C CG2 . THR   A 33  ? 0.2767 0.2335 0.1685 -0.0128 -0.0448 0.0530  33  THR   A CG2 
568  N N   . VAL   A 34  ? 0.1875 0.1708 0.1007 -0.0292 -0.0157 0.0221  34  VAL   A N   
569  C CA  . VAL   A 34  ? 0.1701 0.1591 0.0886 -0.0253 -0.0041 0.0234  34  VAL   A CA  
570  C C   . VAL   A 34  ? 0.1592 0.1536 0.0908 -0.0215 0.0006  0.0157  34  VAL   A C   
571  O O   . VAL   A 34  ? 0.1658 0.1549 0.1069 -0.0305 0.0039  0.0224  34  VAL   A O   
572  C CB  . VAL   A 34  ? 0.1730 0.1571 0.1177 -0.0220 -0.0004 0.0142  34  VAL   A CB  
573  C CG1 . VAL   A 34  ? 0.1784 0.1614 0.1168 -0.0156 0.0089  0.0063  34  VAL   A CG1 
574  C CG2 . VAL   A 34  ? 0.1763 0.1684 0.1453 -0.0107 -0.0108 0.0142  34  VAL   A CG2 
584  N N   . VAL   A 35  ? 0.1487 0.1410 0.0931 -0.0244 -0.0058 0.0187  35  VAL   A N   
585  C CA  . VAL   A 35  ? 0.1419 0.1379 0.0845 -0.0195 -0.0016 0.0137  35  VAL   A CA  
586  C C   . VAL   A 35  ? 0.1309 0.1244 0.0869 -0.0142 0.0027  0.0151  35  VAL   A C   
587  O O   . VAL   A 35  ? 0.1249 0.1397 0.1088 -0.0234 0.0085  0.0082  35  VAL   A O   
588  C CB  . VAL   A 35  ? 0.1488 0.1483 0.0957 -0.0144 0.0132  -0.0003 35  VAL   A CB  
589  C CG1 . VAL   A 35  ? 0.1577 0.1478 0.1127 -0.0059 0.0035  -0.0098 35  VAL   A CG1 
590  C CG2 . VAL   A 35  ? 0.1490 0.1504 0.1201 -0.0117 0.0171  -0.0027 35  VAL   A CG2 
600  N N   . VAL   A 36  ? 0.1193 0.1295 0.0797 -0.0154 0.0065  0.0148  36  VAL   A N   
601  C CA  . VAL   A 36  ? 0.1147 0.1185 0.0893 -0.0107 0.0047  0.0088  36  VAL   A CA  
602  C C   . VAL   A 36  ? 0.1134 0.1177 0.0955 -0.0068 0.0081  0.0059  36  VAL   A C   
603  O O   . VAL   A 36  ? 0.1202 0.1174 0.1200 -0.0021 0.0199  0.0102  36  VAL   A O   
604  C CB  . VAL   A 36  ? 0.1166 0.1128 0.1026 -0.0098 0.0071  0.0076  36  VAL   A CB  
605  C CG1 . VAL   A 36  ? 0.1235 0.1146 0.1104 -0.0131 0.0050  -0.0002 36  VAL   A CG1 
606  C CG2 . VAL   A 36  ? 0.1285 0.1145 0.1181 -0.0059 -0.0019 0.0175  36  VAL   A CG2 
616  N N   . ASN   A 37  ? 0.1071 0.1137 0.0960 -0.0013 0.0065  0.0122  37  ASN   A N   
617  C CA  . ASN   A 37  ? 0.1091 0.1115 0.0930 -0.0010 0.0058  0.0141  37  ASN   A CA  
618  C C   . ASN   A 37  ? 0.1111 0.1073 0.0957 -0.0025 0.0119  0.0192  37  ASN   A C   
619  O O   . ASN   A 37  ? 0.1213 0.1204 0.0958 0.0073  0.0094  0.0055  37  ASN   A O   
620  C CB  . ASN   A 37  ? 0.1142 0.1101 0.1067 0.0034  -0.0003 0.0097  37  ASN   A CB  
621  C CG  . ASN   A 37  ? 0.1138 0.1116 0.1161 -0.0016 0.0061  0.0106  37  ASN   A CG  
622  O OD1 . ASN   A 37  ? 0.1128 0.1127 0.1357 0.0003  0.0059  0.0158  37  ASN   A OD1 
623  N ND2 . ASN   A 37  ? 0.1149 0.1168 0.1162 -0.0012 -0.0029 0.0219  37  ASN   A ND2 
630  N N   . ALA   A 38  ? 0.1106 0.1161 0.1087 0.0020  0.0076  0.0123  38  ALA   A N   
631  C CA  . ALA   A 38  ? 0.1175 0.1224 0.1054 0.0004  0.0006  0.0057  38  ALA   A CA  
632  C C   . ALA   A 38  ? 0.1144 0.1230 0.1023 0.0002  -0.0068 0.0005  38  ALA   A C   
633  O O   . ALA   A 38  ? 0.1185 0.1266 0.1190 0.0054  -0.0062 0.0074  38  ALA   A O   
634  C CB  . ALA   A 38  ? 0.1226 0.1523 0.1242 -0.0097 -0.0050 0.0055  38  ALA   A CB  
640  N N   . ALA   A 39  ? 0.1150 0.1190 0.1152 0.0017  -0.0005 0.0034  39  ALA   A N   
641  C CA  . ALA   A 39  ? 0.1185 0.1163 0.1081 0.0005  0.0046  0.0070  39  ALA   A CA  
642  C C   . ALA   A 39  ? 0.1184 0.1144 0.1080 0.0017  0.0038  0.0060  39  ALA   A C   
643  O O   . ALA   A 39  ? 0.1305 0.1182 0.1080 -0.0060 0.0109  0.0053  39  ALA   A O   
644  C CB  . ALA   A 39  ? 0.1198 0.1388 0.1314 -0.0023 -0.0068 -0.0004 39  ALA   A CB  
650  N N   . ASN   A 40  ? 0.1295 0.1210 0.1022 -0.0070 0.0223  0.0051  40  ASN   A N   
651  C CA  . ASN   A 40  ? 0.1371 0.1151 0.1206 -0.0024 0.0063  0.0036  40  ASN   A CA  
652  C C   . ASN   A 40  ? 0.1364 0.1103 0.1051 -0.0032 0.0262  0.0147  40  ASN   A C   
653  O O   . ASN   A 40  ? 0.1286 0.1109 0.1155 -0.0056 0.0199  0.0166  40  ASN   A O   
654  C CB  . ASN   A 40  ? 0.1467 0.1233 0.1228 0.0041  -0.0008 0.0068  40  ASN   A CB  
655  C CG  . ASN   A 40  ? 0.1533 0.1252 0.1506 0.0051  -0.0124 0.0099  40  ASN   A CG  
656  O OD1 . ASN   A 40  ? 0.1614 0.1293 0.1895 -0.0012 -0.0060 0.0039  40  ASN   A OD1 
657  N ND2 . ASN   A 40  ? 0.1592 0.1349 0.1684 0.0037  -0.0054 0.0031  40  ASN   A ND2 
664  N N   . VAL   A 41  ? 0.1450 0.1128 0.1089 -0.0050 0.0259  0.0099  41  VAL   A N   
665  C CA  . VAL   A 41  ? 0.1487 0.1208 0.1198 -0.0067 0.0354  0.0077  41  VAL   A CA  
666  C C   . VAL   A 41  ? 0.1442 0.1206 0.1310 -0.0023 0.0352  0.0080  41  VAL   A C   
667  O O   . VAL   A 41  ? 0.1450 0.1153 0.1490 -0.0008 0.0321  0.0064  41  VAL   A O   
668  C CB  . VAL   A 41  ? 0.1699 0.1326 0.1322 -0.0127 0.0497  0.0071  41  VAL   A CB  
669  C CG1 . VAL   A 41  ? 0.1796 0.1386 0.1394 -0.0130 0.0470  -0.0005 41  VAL   A CG1 
670  C CG2 . VAL   A 41  ? 0.1965 0.1426 0.1295 -0.0208 0.0540  0.0044  41  VAL   A CG2 
680  N N   . TYR   A 42  ? 0.1335 0.1167 0.1385 -0.0017 0.0322  0.0215  42  TYR   A N   
681  C CA  . TYR   A 42  ? 0.1333 0.1128 0.1381 -0.0082 0.0307  0.0227  42  TYR   A CA  
682  C C   . TYR   A 42  ? 0.1222 0.1141 0.1432 -0.0049 0.0232  0.0220  42  TYR   A C   
683  O O   . TYR   A 42  ? 0.1249 0.1172 0.1590 -0.0122 0.0207  0.0058  42  TYR   A O   
684  C CB  . TYR   A 42  ? 0.1551 0.1252 0.1411 -0.0058 0.0356  0.0261  42  TYR   A CB  
685  C CG  . TYR   A 42  ? 0.1778 0.1402 0.1484 -0.0074 0.0231  0.0303  42  TYR   A CG  
686  C CD1 . TYR   A 42  ? 0.1876 0.1499 0.1532 -0.0087 0.0286  0.0295  42  TYR   A CD1 
687  C CD2 . TYR   A 42  ? 0.1885 0.1615 0.1673 -0.0020 0.0146  0.0207  42  TYR   A CD2 
688  C CE1 . TYR   A 42  ? 0.1954 0.1578 0.1533 -0.0121 0.0385  0.0290  42  TYR   A CE1 
689  C CE2 . TYR   A 42  ? 0.2055 0.1741 0.1773 -0.0155 0.0186  0.0262  42  TYR   A CE2 
690  C CZ  . TYR   A 42  ? 0.2118 0.1721 0.1590 -0.0184 0.0319  0.0259  42  TYR   A CZ  
691  O OH  . TYR   A 42  ? 0.2295 0.1988 0.1784 -0.0298 0.0340  0.0161  42  TYR   A OH  
701  N N   . LEU   A 43  ? 0.1235 0.1142 0.1281 -0.0048 0.0116  0.0092  43  LEU   A N   
702  C CA  . LEU   A 43  ? 0.1189 0.1121 0.1272 -0.0060 0.0108  0.0068  43  LEU   A CA  
703  C C   . LEU   A 43  ? 0.1201 0.1148 0.1259 0.0001  0.0077  0.0065  43  LEU   A C   
704  O O   . LEU   A 43  ? 0.1358 0.1203 0.1438 0.0048  -0.0025 0.0035  43  LEU   A O   
705  C CB  . LEU   A 43  ? 0.1236 0.1127 0.1330 -0.0087 0.0079  0.0068  43  LEU   A CB  
706  C CG  . LEU   A 43  ? 0.1261 0.1125 0.1415 -0.0017 0.0089  0.0070  43  LEU   A CG  
707  C CD1 . LEU   A 43  ? 0.1330 0.1267 0.1561 0.0012  -0.0019 0.0151  43  LEU   A CD1 
708  C CD2 . LEU   A 43  ? 0.1418 0.1213 0.1408 -0.0059 0.0075  0.0211  43  LEU   A CD2 
720  N N   . LYS   A 44  ? 0.1216 0.1178 0.1269 0.0002  0.0089  0.0136  44  LYS   A N   
721  C CA  . LYS   A 44  ? 0.1372 0.1166 0.1277 -0.0045 0.0134  0.0167  44  LYS   A CA  
722  C C   . LYS   A 44  ? 0.1256 0.1188 0.1152 0.0009  0.0052  0.0119  44  LYS   A C   
723  O O   . LYS   A 44  ? 0.1325 0.1334 0.1274 0.0000  0.0015  -0.0007 44  LYS   A O   
724  C CB  . LYS   A 44  ? 0.1657 0.1304 0.1751 0.0015  0.0251  0.0312  44  LYS   A CB  
725  C CG  . LYS   A 44  ? 0.2037 0.1610 0.2357 -0.0068 0.0461  0.0424  44  LYS   A CG  
726  C CD  . LYS   A 44  ? 0.2479 0.2246 0.3494 -0.0091 0.0350  0.0325  44  LYS   A CD  
727  C CE  . LYS   A 44  ? 0.2617 0.2499 0.4276 -0.0082 0.0285  0.0330  44  LYS   A CE  
728  N NZ  . LYS   A 44  ? 0.2766 0.2789 0.4616 -0.0075 0.0260  0.0329  44  LYS   A NZ  
742  N N   . HIS   A 45  ? 0.1157 0.1165 0.1200 0.0016  0.0007  0.0141  45  HIS   A N   
743  C CA  . HIS   A 45  ? 0.1149 0.1172 0.1231 0.0031  -0.0074 0.0107  45  HIS   A CA  
744  C C   . HIS   A 45  ? 0.1200 0.1332 0.1308 0.0052  -0.0013 0.0109  45  HIS   A C   
745  O O   . HIS   A 45  ? 0.1383 0.1412 0.1610 0.0236  -0.0081 -0.0067 45  HIS   A O   
746  C CB  . HIS   A 45  ? 0.1160 0.1162 0.1264 0.0042  -0.0008 0.0063  45  HIS   A CB  
747  C CG  . HIS   A 45  ? 0.1130 0.1109 0.1102 -0.0062 0.0022  0.0078  45  HIS   A CG  
748  N ND1 . HIS   A 45  ? 0.1093 0.1165 0.1272 -0.0024 0.0019  0.0145  45  HIS   A ND1 
749  C CD2 . HIS   A 45  ? 0.1169 0.1174 0.1173 -0.0141 -0.0033 0.0146  45  HIS   A CD2 
750  C CE1 . HIS   A 45  ? 0.1139 0.1188 0.1121 -0.0053 0.0015  0.0165  45  HIS   A CE1 
751  N NE2 . HIS   A 45  ? 0.1136 0.1229 0.1153 -0.0080 -0.0038 0.0203  45  HIS   A NE2 
759  N N   . GLY   A 46  ? 0.1352 0.1478 0.1509 0.0173  -0.0113 0.0179  46  GLY   A N   
760  C CA  . GLY   A 46  ? 0.1414 0.1551 0.1611 0.0168  -0.0105 0.0278  46  GLY   A CA  
761  C C   . GLY   A 46  ? 0.1472 0.1426 0.1561 0.0291  -0.0213 0.0333  46  GLY   A C   
762  O O   . GLY   A 46  ? 0.1510 0.1478 0.1865 0.0253  -0.0334 0.0205  46  GLY   A O   
766  N N   . GLY   A 47  ? 0.1479 0.1426 0.1520 0.0286  -0.0160 0.0192  47  GLY   A N   
767  C CA  . GLY   A 47  ? 0.1513 0.1478 0.1663 0.0266  -0.0366 0.0163  47  GLY   A CA  
768  C C   . GLY   A 47  ? 0.1508 0.1371 0.1471 0.0253  -0.0399 -0.0001 47  GLY   A C   
769  O O   . GLY   A 47  ? 0.1506 0.1371 0.1507 0.0274  -0.0355 0.0080  47  GLY   A O   
773  N N   . GLY   A 48  ? 0.1499 0.1380 0.1611 0.0264  -0.0472 -0.0028 48  GLY   A N   
774  C CA  . GLY   A 48  ? 0.1467 0.1333 0.1664 0.0142  -0.0415 -0.0154 48  GLY   A CA  
775  C C   . GLY   A 48  ? 0.1280 0.1303 0.1503 0.0073  -0.0126 -0.0139 48  GLY   A C   
776  O O   . GLY   A 48  ? 0.1343 0.1272 0.1664 0.0085  -0.0160 -0.0194 48  GLY   A O   
780  N N   . VAL   A 49  ? 0.1193 0.1242 0.1429 -0.0050 -0.0068 -0.0091 49  VAL   A N   
781  C CA  . VAL   A 49  ? 0.1302 0.1196 0.1336 -0.0100 0.0141  -0.0067 49  VAL   A CA  
782  C C   . VAL   A 49  ? 0.1206 0.1099 0.1082 -0.0005 0.0067  -0.0011 49  VAL   A C   
783  O O   . VAL   A 49  ? 0.1259 0.1159 0.1171 -0.0076 0.0135  -0.0033 49  VAL   A O   
784  C CB  . VAL   A 49  ? 0.1588 0.1218 0.1591 -0.0155 0.0047  0.0031  49  VAL   A CB  
785  C CG1 . VAL   A 49  ? 0.1740 0.1262 0.1711 -0.0146 0.0017  0.0101  49  VAL   A CG1 
786  C CG2 . VAL   A 49  ? 0.1742 0.1387 0.2022 -0.0357 0.0001  -0.0028 49  VAL   A CG2 
796  N N   . ALA   A 50  ? 0.1186 0.1082 0.1070 -0.0030 -0.0065 0.0044  50  ALA   A N   
797  C CA  . ALA   A 50  ? 0.1139 0.1109 0.1051 -0.0026 -0.0054 0.0091  50  ALA   A CA  
798  C C   . ALA   A 50  ? 0.1099 0.1117 0.1032 -0.0025 -0.0041 0.0057  50  ALA   A C   
799  O O   . ALA   A 50  ? 0.1146 0.1151 0.1161 -0.0021 -0.0037 0.0040  50  ALA   A O   
800  C CB  . ALA   A 50  ? 0.1093 0.1126 0.1197 -0.0035 -0.0034 -0.0004 50  ALA   A CB  
806  N N   . GLY   A 51  ? 0.1170 0.1032 0.1192 0.0038  -0.0128 0.0017  51  GLY   A N   
807  C CA  . GLY   A 51  ? 0.1244 0.1067 0.1323 0.0079  -0.0133 0.0020  51  GLY   A CA  
808  C C   . GLY   A 51  ? 0.1156 0.1119 0.1277 0.0052  -0.0085 -0.0061 51  GLY   A C   
809  O O   . GLY   A 51  ? 0.1200 0.1165 0.1397 0.0004  -0.0069 -0.0098 51  GLY   A O   
813  N N   . ALA   A 52  ? 0.1148 0.1234 0.1218 0.0004  -0.0005 -0.0133 52  ALA   A N   
814  C CA  . ALA   A 52  ? 0.1173 0.1307 0.1357 -0.0004 0.0034  -0.0124 52  ALA   A CA  
815  C C   . ALA   A 52  ? 0.1143 0.1324 0.1073 -0.0102 0.0075  -0.0133 52  ALA   A C   
816  O O   . ALA   A 52  ? 0.1222 0.1360 0.1291 -0.0051 0.0090  -0.0188 52  ALA   A O   
817  C CB  . ALA   A 52  ? 0.1216 0.1568 0.1577 -0.0067 0.0009  -0.0104 52  ALA   A CB  
823  N N   . LEU   A 53  ? 0.1122 0.1242 0.1056 -0.0077 0.0021  -0.0076 53  LEU   A N   
824  C CA  . LEU   A 53  ? 0.1245 0.1268 0.1045 -0.0076 0.0027  0.0007  53  LEU   A CA  
825  C C   . LEU   A 53  ? 0.1235 0.1293 0.0846 0.0037  -0.0006 -0.0013 53  LEU   A C   
826  O O   . LEU   A 53  ? 0.1366 0.1379 0.1004 -0.0103 0.0034  0.0019  53  LEU   A O   
827  C CB  . LEU   A 53  ? 0.1327 0.1274 0.1111 -0.0085 0.0055  -0.0006 53  LEU   A CB  
828  C CG  . LEU   A 53  ? 0.1519 0.1285 0.1177 -0.0161 0.0053  0.0032  53  LEU   A CG  
829  C CD1 . LEU   A 53  ? 0.1670 0.1326 0.1352 -0.0029 0.0079  0.0045  53  LEU   A CD1 
830  C CD2 . LEU   A 53  ? 0.1790 0.1447 0.1351 -0.0262 0.0164  -0.0001 53  LEU   A CD2 
842  N N   . ASN   A 54  ? 0.1174 0.1222 0.0915 -0.0007 -0.0011 0.0057  54  ASN   A N   
843  C CA  . ASN   A 54  ? 0.1067 0.1188 0.1009 -0.0004 -0.0049 -0.0064 54  ASN   A CA  
844  C C   . ASN   A 54  ? 0.1145 0.1245 0.1082 -0.0082 -0.0009 -0.0012 54  ASN   A C   
845  O O   . ASN   A 54  ? 0.1189 0.1296 0.1194 -0.0050 -0.0086 -0.0096 54  ASN   A O   
846  C CB  . ASN   A 54  ? 0.1032 0.1201 0.1163 -0.0056 -0.0061 -0.0044 54  ASN   A CB  
847  C CG  . ASN   A 54  ? 0.1082 0.1200 0.1224 -0.0007 -0.0025 -0.0044 54  ASN   A CG  
848  O OD1 . ASN   A 54  ? 0.1120 0.1230 0.1232 -0.0000 -0.0088 -0.0015 54  ASN   A OD1 
849  N ND2 . ASN   A 54  ? 0.1155 0.1253 0.1484 -0.0083 -0.0147 0.0060  54  ASN   A ND2 
856  N N   . LYS   A 55  ? 0.1124 0.1198 0.1209 -0.0013 -0.0062 -0.0119 55  LYS   A N   
857  C CA  . LYS   A 55  ? 0.1225 0.1252 0.1205 0.0001  -0.0089 -0.0097 55  LYS   A CA  
858  C C   . LYS   A 55  ? 0.1188 0.1363 0.1273 -0.0010 -0.0014 -0.0186 55  LYS   A C   
859  O O   . LYS   A 55  ? 0.1295 0.1492 0.1290 0.0026  -0.0065 -0.0237 55  LYS   A O   
860  C CB  . LYS   A 55  ? 0.1333 0.1323 0.1384 0.0105  -0.0086 -0.0147 55  LYS   A CB  
861  C CG  . LYS   A 55  ? 0.1423 0.1563 0.1503 0.0172  -0.0176 -0.0190 55  LYS   A CG  
862  C CD  . LYS   A 55  ? 0.1482 0.1767 0.1624 0.0249  0.0007  -0.0196 55  LYS   A CD  
863  C CE  . LYS   A 55  ? 0.1642 0.2015 0.1890 0.0374  -0.0192 -0.0197 55  LYS   A CE  
864  N NZ  . LYS   A 55  ? 0.1692 0.2143 0.2075 0.0447  -0.0233 -0.0175 55  LYS   A NZ  
878  N N   . ALA   A 56  ? 0.1255 0.1454 0.1234 -0.0088 0.0081  -0.0188 56  ALA   A N   
879  C CA  . ALA   A 56  ? 0.1381 0.1612 0.1251 -0.0102 0.0058  -0.0101 56  ALA   A CA  
880  C C   . ALA   A 56  ? 0.1446 0.1709 0.1011 -0.0089 0.0119  -0.0169 56  ALA   A C   
881  O O   . ALA   A 56  ? 0.1497 0.2039 0.1211 0.0048  0.0112  -0.0136 56  ALA   A O   
882  C CB  . ALA   A 56  ? 0.1519 0.1788 0.1351 -0.0151 0.0104  -0.0049 56  ALA   A CB  
888  N N   . THR   A 57  ? 0.1299 0.1485 0.1043 -0.0059 0.0080  -0.0173 57  THR   A N   
889  C CA  . THR   A 57  ? 0.1340 0.1470 0.1167 -0.0058 0.0000  -0.0124 57  THR   A CA  
890  C C   . THR   A 57  ? 0.1326 0.1511 0.1158 -0.0054 -0.0065 -0.0187 57  THR   A C   
891  O O   . THR   A 57  ? 0.1322 0.1544 0.1366 -0.0050 -0.0128 -0.0223 57  THR   A O   
892  C CB  . THR   A 57  ? 0.1313 0.1458 0.1128 -0.0086 -0.0031 -0.0084 57  THR   A CB  
893  O OG1 . THR   A 57  ? 0.1234 0.1416 0.1184 -0.0033 -0.0014 -0.0049 57  THR   A OG1 
894  C CG2 . THR   A 57  ? 0.1355 0.1552 0.1114 -0.0083 -0.0002 -0.0002 57  THR   A CG2 
902  N N   . ASN   A 58  ? 0.1315 0.1474 0.1339 -0.0080 0.0027  -0.0286 58  ASN   A N   
903  C CA  . ASN   A 58  ? 0.1504 0.1432 0.1626 -0.0105 0.0083  -0.0361 58  ASN   A CA  
904  C C   . ASN   A 58  ? 0.1319 0.1309 0.1419 -0.0030 0.0006  -0.0239 58  ASN   A C   
905  O O   . ASN   A 58  ? 0.1334 0.1444 0.1597 -0.0126 -0.0036 -0.0265 58  ASN   A O   
906  C CB  . ASN   A 58  ? 0.1947 0.1636 0.1924 -0.0175 0.0249  -0.0499 58  ASN   A CB  
907  C CG  . ASN   A 58  ? 0.2354 0.1865 0.2499 -0.0155 0.0238  -0.0431 58  ASN   A CG  
908  O OD1 . ASN   A 58  ? 0.2583 0.1866 0.2846 0.0169  0.0502  -0.0381 58  ASN   A OD1 
909  N ND2 . ASN   A 58  ? 0.2473 0.2003 0.2756 -0.0196 0.0053  -0.0468 58  ASN   A ND2 
916  N N   . ASN   A 59  ? 0.1220 0.1282 0.1325 -0.0071 -0.0123 -0.0158 59  ASN   A N   
917  C CA  . ASN   A 59  ? 0.1221 0.1168 0.1315 -0.0055 -0.0058 -0.0104 59  ASN   A CA  
918  C C   . ASN   A 59  ? 0.1190 0.1214 0.1247 -0.0060 -0.0057 -0.0054 59  ASN   A C   
919  O O   . ASN   A 59  ? 0.1190 0.1259 0.1307 -0.0080 -0.0006 0.0008  59  ASN   A O   
920  C CB  . ASN   A 59  ? 0.1255 0.1156 0.1430 0.0024  -0.0196 -0.0157 59  ASN   A CB  
921  C CG  . ASN   A 59  ? 0.1286 0.1225 0.1433 -0.0025 -0.0273 -0.0002 59  ASN   A CG  
922  O OD1 . ASN   A 59  ? 0.1418 0.1351 0.1322 -0.0104 -0.0287 0.0079  59  ASN   A OD1 
923  N ND2 . ASN   A 59  ? 0.1366 0.1287 0.1534 -0.0114 -0.0193 0.0006  59  ASN   A ND2 
930  N N   . ALA   A 60  ? 0.1163 0.1291 0.1209 -0.0028 -0.0057 -0.0078 60  ALA   A N   
931  C CA  . ALA   A 60  ? 0.1171 0.1276 0.1316 -0.0020 -0.0114 -0.0028 60  ALA   A CA  
932  C C   . ALA   A 60  ? 0.1159 0.1197 0.1359 -0.0026 -0.0059 -0.0020 60  ALA   A C   
933  O O   . ALA   A 60  ? 0.1115 0.1257 0.1555 -0.0043 -0.0117 -0.0045 60  ALA   A O   
934  C CB  . ALA   A 60  ? 0.1304 0.1418 0.1400 -0.0044 -0.0190 -0.0194 60  ALA   A CB  
940  N N   . MET   A 61  ? 0.1143 0.1173 0.1252 -0.0049 -0.0063 -0.0036 61  MET   A N   
941  C CA  . MET   A 61  ? 0.1149 0.1159 0.1231 -0.0048 -0.0021 -0.0007 61  MET   A CA  
942  C C   . MET   A 61  ? 0.1133 0.1117 0.1260 -0.0050 -0.0013 -0.0049 61  MET   A C   
943  O O   . MET   A 61  ? 0.1173 0.1102 0.1316 -0.0040 0.0080  0.0034  61  MET   A O   
944  C CB  . MET   A 61  ? 0.1196 0.1183 0.1151 -0.0044 -0.0049 0.0011  61  MET   A CB  
945  C CG  . MET   A 61  ? 0.1204 0.1265 0.1297 -0.0016 -0.0001 -0.0042 61  MET   A CG  
946  S SD  . MET   A 61  ? 0.1237 0.1261 0.1637 -0.0115 -0.0007 -0.0202 61  MET   A SD  
947  C CE  . MET   A 61  ? 0.1458 0.1426 0.1814 -0.0152 0.0152  -0.0151 61  MET   A CE  
957  N N   . GLN   A 62  ? 0.1095 0.1125 0.1203 -0.0055 -0.0051 -0.0019 62  GLN   A N   
958  C CA  . GLN   A 62  ? 0.1177 0.1131 0.1310 -0.0030 -0.0020 -0.0018 62  GLN   A CA  
959  C C   . GLN   A 62  ? 0.1145 0.1091 0.1365 -0.0028 0.0049  -0.0005 62  GLN   A C   
960  O O   . GLN   A 62  ? 0.1181 0.1228 0.1392 -0.0047 0.0042  -0.0027 62  GLN   A O   
961  C CB  . GLN   A 62  ? 0.1162 0.1084 0.1365 -0.0032 -0.0019 0.0000  62  GLN   A CB  
962  C CG  . GLN   A 62  ? 0.1198 0.1085 0.1333 -0.0037 -0.0030 0.0076  62  GLN   A CG  
963  C CD  . GLN   A 62  ? 0.1280 0.1121 0.1323 -0.0022 0.0075  0.0099  62  GLN   A CD  
964  O OE1 . GLN   A 62  ? 0.1284 0.1247 0.1408 -0.0039 -0.0032 0.0024  62  GLN   A OE1 
965  N NE2 . GLN   A 62  ? 0.1373 0.1156 0.1437 -0.0001 0.0020  -0.0034 62  GLN   A NE2 
974  N N   . VAL   A 63  ? 0.1120 0.1126 0.1464 -0.0050 0.0039  -0.0168 63  VAL   A N   
975  C CA  . VAL   A 63  ? 0.1140 0.1230 0.1687 -0.0126 0.0007  -0.0179 63  VAL   A CA  
976  C C   . VAL   A 63  ? 0.1067 0.1243 0.1613 -0.0137 -0.0103 -0.0148 63  VAL   A C   
977  O O   . VAL   A 63  ? 0.1124 0.1271 0.1745 -0.0155 -0.0002 -0.0114 63  VAL   A O   
978  C CB  . VAL   A 63  ? 0.1269 0.1407 0.2004 -0.0151 -0.0029 -0.0390 63  VAL   A CB  
979  C CG1 . VAL   A 63  ? 0.1440 0.1644 0.2239 -0.0134 -0.0047 -0.0579 63  VAL   A CG1 
980  C CG2 . VAL   A 63  ? 0.1388 0.1326 0.2183 -0.0171 0.0198  -0.0396 63  VAL   A CG2 
990  N N   . GLU   A 64  ? 0.1109 0.1313 0.1487 -0.0039 -0.0047 -0.0106 64  GLU   A N   
991  C CA  . GLU   A 64  ? 0.1087 0.1279 0.1514 -0.0057 -0.0075 -0.0018 64  GLU   A CA  
992  C C   . GLU   A 64  ? 0.1093 0.1207 0.1459 -0.0053 0.0003  0.0006  64  GLU   A C   
993  O O   . GLU   A 64  ? 0.1177 0.1318 0.1465 0.0001  -0.0006 0.0006  64  GLU   A O   
994  C CB  . GLU   A 64  ? 0.1198 0.1402 0.1558 -0.0075 -0.0012 -0.0105 64  GLU   A CB  
995  C CG  . GLU   A 64  ? 0.1343 0.1448 0.1675 -0.0081 0.0025  -0.0084 64  GLU   A CG  
996  C CD  . GLU   A 64  ? 0.1472 0.1527 0.1733 -0.0141 0.0071  -0.0062 64  GLU   A CD  
997  O OE1 . GLU   A 64  ? 0.1461 0.1628 0.1966 -0.0209 0.0158  -0.0019 64  GLU   A OE1 
998  O OE2 . GLU   A 64  ? 0.1672 0.1502 0.1702 -0.0243 -0.0042 -0.0004 64  GLU   A OE2 
1005 N N   . SER   A 65  ? 0.1055 0.1230 0.1369 0.0017  0.0013  -0.0045 65  SER   A N   
1006 C CA  . SER   A 65  ? 0.1114 0.1181 0.1300 -0.0047 -0.0016 -0.0066 65  SER   A CA  
1007 C C   . SER   A 65  ? 0.1135 0.1232 0.1356 0.0009  -0.0055 -0.0004 65  SER   A C   
1008 O O   . SER   A 65  ? 0.1195 0.1317 0.1499 0.0001  0.0124  -0.0059 65  SER   A O   
1009 C CB  . SER   A 65  ? 0.1124 0.1176 0.1348 -0.0088 0.0067  0.0047  65  SER   A CB  
1010 O OG  . SER   A 65  ? 0.1135 0.1285 0.1492 -0.0066 -0.0052 0.0074  65  SER   A OG  
1016 N N   . ASP   A 66  ? 0.1146 0.1189 0.1447 -0.0006 0.0098  0.0042  66  ASP   A N   
1017 C CA  . ASP   A 66  ? 0.1239 0.1292 0.1619 -0.0022 0.0106  0.0162  66  ASP   A CA  
1018 C C   . ASP   A 66  ? 0.1216 0.1272 0.1694 -0.0066 0.0162  0.0192  66  ASP   A C   
1019 O O   . ASP   A 66  ? 0.1279 0.1388 0.1820 -0.0052 0.0227  0.0236  66  ASP   A O   
1020 C CB  . ASP   A 66  ? 0.1353 0.1410 0.1839 0.0027  0.0115  0.0257  66  ASP   A CB  
1021 C CG  . ASP   A 66  ? 0.1562 0.1556 0.2179 0.0039  -0.0021 0.0408  66  ASP   A CG  
1022 O OD1 . ASP   A 66  ? 0.1525 0.1823 0.1951 -0.0034 -0.0103 0.0429  66  ASP   A OD1 
1023 O OD2 . ASP   A 66  ? 0.1740 0.1628 0.3041 0.0195  -0.0214 0.0245  66  ASP   A OD2 
1028 N N   . ASP   A 67  ? 0.1115 0.1292 0.1720 -0.0035 0.0098  0.0158  67  ASP   A N   
1029 C CA  . ASP   A 67  ? 0.1197 0.1436 0.1908 -0.0041 0.0031  0.0230  67  ASP   A CA  
1030 C C   . ASP   A 67  ? 0.1198 0.1467 0.1795 -0.0024 0.0100  0.0202  67  ASP   A C   
1031 O O   . ASP   A 67  ? 0.1178 0.1527 0.2006 -0.0001 0.0266  0.0344  67  ASP   A O   
1032 C CB  . ASP   A 67  ? 0.1289 0.1568 0.2205 -0.0014 -0.0152 0.0261  67  ASP   A CB  
1033 C CG  . ASP   A 67  ? 0.1305 0.1695 0.2492 -0.0004 -0.0212 0.0288  67  ASP   A CG  
1034 O OD1 . ASP   A 67  ? 0.1330 0.1871 0.3277 -0.0084 -0.0379 0.0408  67  ASP   A OD1 
1035 O OD2 . ASP   A 67  ? 0.1307 0.1744 0.2329 0.0098  -0.0162 0.0252  67  ASP   A OD2 
1040 N N   . TYR   A 68  ? 0.1216 0.1351 0.1610 0.0010  0.0169  0.0244  68  TYR   A N   
1041 C CA  . TYR   A 68  ? 0.1297 0.1345 0.1657 0.0015  0.0229  0.0215  68  TYR   A CA  
1042 C C   . TYR   A 68  ? 0.1246 0.1317 0.1642 0.0004  0.0185  0.0195  68  TYR   A C   
1043 O O   . TYR   A 68  ? 0.1283 0.1348 0.1752 0.0088  0.0273  0.0208  68  TYR   A O   
1044 C CB  . TYR   A 68  ? 0.1362 0.1363 0.1810 0.0110  0.0323  0.0266  68  TYR   A CB  
1045 C CG  . TYR   A 68  ? 0.1401 0.1498 0.2141 0.0084  0.0564  0.0281  68  TYR   A CG  
1046 C CD1 . TYR   A 68  ? 0.1490 0.1589 0.2474 -0.0176 0.0447  -0.0010 68  TYR   A CD1 
1047 C CD2 . TYR   A 68  ? 0.1601 0.1503 0.2593 0.0146  0.0538  0.0385  68  TYR   A CD2 
1048 C CE1 . TYR   A 68  ? 0.1548 0.1661 0.2827 -0.0166 0.0493  -0.0102 68  TYR   A CE1 
1049 C CE2 . TYR   A 68  ? 0.1550 0.1528 0.2832 0.0073  0.0628  0.0188  68  TYR   A CE2 
1050 C CZ  . TYR   A 68  ? 0.1608 0.1576 0.2949 -0.0145 0.0556  -0.0085 68  TYR   A CZ  
1051 O OH  . TYR   A 68  ? 0.1899 0.1574 0.3171 -0.0107 0.0311  -0.0323 68  TYR   A OH  
1061 N N   . ILE   A 69  ? 0.1149 0.1262 0.1653 0.0044  0.0174  0.0165  69  ILE   A N   
1062 C CA  . ILE   A 69  ? 0.1242 0.1309 0.1589 0.0040  0.0153  0.0075  69  ILE   A CA  
1063 C C   . ILE   A 69  ? 0.1264 0.1324 0.1532 0.0036  0.0160  0.0208  69  ILE   A C   
1064 O O   . ILE   A 69  ? 0.1340 0.1433 0.1502 -0.0039 0.0210  0.0219  69  ILE   A O   
1065 C CB  . ILE   A 69  ? 0.1314 0.1503 0.1625 0.0038  0.0118  -0.0026 69  ILE   A CB  
1066 C CG1 . ILE   A 69  ? 0.1299 0.1630 0.1754 0.0091  0.0169  -0.0105 69  ILE   A CG1 
1067 C CG2 . ILE   A 69  ? 0.1536 0.1686 0.1771 0.0107  0.0027  -0.0102 69  ILE   A CG2 
1068 C CD1 . ILE   A 69  ? 0.1322 0.1703 0.1837 -0.0003 0.0142  -0.0162 69  ILE   A CD1 
1080 N N   . ALA   A 70  ? 0.1319 0.1316 0.1629 -0.0039 0.0181  0.0133  70  ALA   A N   
1081 C CA  . ALA   A 70  ? 0.1372 0.1452 0.1796 -0.0142 0.0297  0.0245  70  ALA   A CA  
1082 C C   . ALA   A 70  ? 0.1329 0.1608 0.1719 -0.0132 0.0278  0.0266  70  ALA   A C   
1083 O O   . ALA   A 70  ? 0.1520 0.1887 0.1943 0.0031  0.0480  0.0299  70  ALA   A O   
1084 C CB  . ALA   A 70  ? 0.1371 0.1413 0.2025 -0.0166 0.0261  0.0088  70  ALA   A CB  
1090 N N   . THR   A 71  ? 0.1266 0.1551 0.1633 -0.0038 0.0168  0.0209  71  THR   A N   
1091 C CA  . THR   A 71  ? 0.1380 0.1710 0.1963 0.0068  0.0254  0.0210  71  THR   A CA  
1092 C C   . THR   A 71  ? 0.1285 0.1665 0.2119 0.0133  0.0341  0.0178  71  THR   A C   
1093 O O   . THR   A 71  ? 0.1371 0.1923 0.2497 0.0096  0.0418  -0.0052 71  THR   A O   
1094 C CB  . THR   A 71  ? 0.1637 0.1927 0.2153 0.0171  -0.0107 0.0283  71  THR   A CB  
1095 O OG1 . THR   A 71  ? 0.1858 0.2108 0.2281 0.0119  -0.0344 0.0211  71  THR   A OG1 
1096 C CG2 . THR   A 71  ? 0.1777 0.2088 0.2392 0.0230  -0.0173 0.0370  71  THR   A CG2 
1104 N N   . ASN   A 72  ? 0.1310 0.1491 0.1919 0.0156  0.0253  0.0187  72  ASN   A N   
1105 C CA  . ASN   A 72  ? 0.1376 0.1472 0.1919 0.0202  0.0342  0.0243  72  ASN   A CA  
1106 C C   . ASN   A 72  ? 0.1491 0.1486 0.1943 0.0140  0.0481  0.0137  72  ASN   A C   
1107 O O   . ASN   A 72  ? 0.1650 0.1509 0.2257 0.0210  0.0461  0.0045  72  ASN   A O   
1108 C CB  . ASN   A 72  ? 0.1564 0.1539 0.1970 0.0166  0.0378  0.0241  72  ASN   A CB  
1109 C CG  . ASN   A 72  ? 0.1800 0.1639 0.1960 0.0279  0.0363  0.0310  72  ASN   A CG  
1110 O OD1 . ASN   A 72  ? 0.1970 0.1970 0.2077 0.0269  0.0420  0.0242  72  ASN   A OD1 
1111 N ND2 . ASN   A 72  ? 0.1940 0.1703 0.2112 0.0493  0.0166  0.0200  72  ASN   A ND2 
1118 N N   . GLY   A 73  ? 0.1514 0.1460 0.1731 0.0096  0.0436  0.0086  73  GLY   A N   
1119 C CA  . GLY   A 73  ? 0.1579 0.1431 0.1597 -0.0043 0.0403  0.0067  73  GLY   A CA  
1120 C C   . GLY   A 73  ? 0.1540 0.1313 0.1511 0.0011  0.0481  0.0220  73  GLY   A C   
1121 O O   . GLY   A 73  ? 0.1500 0.1405 0.1761 0.0087  0.0376  0.0292  73  GLY   A O   
1125 N N   . PRO   A 74  ? 0.1611 0.1340 0.1499 -0.0128 0.0430  0.0158  74  PRO   A N   
1126 C CA  . PRO   A 74  ? 0.1577 0.1342 0.1604 -0.0002 0.0432  0.0160  74  PRO   A CA  
1127 C C   . PRO   A 74  ? 0.1506 0.1211 0.1592 0.0041  0.0311  0.0040  74  PRO   A C   
1128 O O   . PRO   A 74  ? 0.1589 0.1251 0.1869 0.0018  0.0339  -0.0044 74  PRO   A O   
1129 C CB  . PRO   A 74  ? 0.1739 0.1643 0.1795 0.0024  0.0417  0.0309  74  PRO   A CB  
1130 C CG  . PRO   A 74  ? 0.1977 0.1902 0.2210 -0.0132 0.0322  0.0193  74  PRO   A CG  
1131 C CD  . PRO   A 74  ? 0.1832 0.1695 0.1737 -0.0210 0.0336  0.0048  74  PRO   A CD  
1139 N N   . LEU   A 75  ? 0.1412 0.1154 0.1446 0.0008  0.0299  0.0087  75  LEU   A N   
1140 C CA  . LEU   A 75  ? 0.1498 0.1175 0.1253 0.0021  0.0083  0.0031  75  LEU   A CA  
1141 C C   . LEU   A 75  ? 0.1575 0.1240 0.1206 0.0047  0.0134  0.0135  75  LEU   A C   
1142 O O   . LEU   A 75  ? 0.1960 0.1424 0.1242 0.0097  0.0074  0.0097  75  LEU   A O   
1143 C CB  . LEU   A 75  ? 0.1565 0.1277 0.1152 -0.0095 0.0102  0.0163  75  LEU   A CB  
1144 C CG  . LEU   A 75  ? 0.1734 0.1604 0.1312 -0.0343 0.0078  0.0139  75  LEU   A CG  
1145 C CD1 . LEU   A 75  ? 0.1844 0.2056 0.1423 -0.0334 0.0035  -0.0002 75  LEU   A CD1 
1146 C CD2 . LEU   A 75  ? 0.1987 0.1991 0.1953 -0.0130 0.0076  0.0130  75  LEU   A CD2 
1158 N N   . LYS   A 76  ? 0.1640 0.1259 0.1382 -0.0051 0.0117  -0.0011 76  LYS   A N   
1159 C CA  . LYS   A 76  ? 0.1596 0.1468 0.1453 -0.0063 0.0142  -0.0144 76  LYS   A CA  
1160 C C   . LYS   A 76  ? 0.1566 0.1306 0.1177 -0.0025 0.0162  -0.0065 76  LYS   A C   
1161 O O   . LYS   A 76  ? 0.1574 0.1286 0.1161 -0.0018 0.0183  0.0048  76  LYS   A O   
1162 C CB  . LYS   A 76  ? 0.1614 0.1695 0.1875 0.0051  0.0119  -0.0434 76  LYS   A CB  
1163 C CG  . LYS   A 76  ? 0.1696 0.1677 0.2455 0.0087  0.0140  -0.0372 76  LYS   A CG  
1164 C CD  . LYS   A 76  ? 0.1751 0.1687 0.2873 0.0125  0.0087  -0.0431 76  LYS   A CD  
1165 C CE  . LYS   A 76  ? 0.1861 0.1895 0.3430 0.0043  0.0149  -0.0476 76  LYS   A CE  
1166 N NZ  . LYS   A 76  ? 0.1875 0.1908 0.3834 -0.0083 0.0071  -0.0536 76  LYS   A NZ  
1180 N N   . VAL   A 77  ? 0.1648 0.1352 0.1145 -0.0017 0.0226  0.0088  77  VAL   A N   
1181 C CA  . VAL   A 77  ? 0.1568 0.1343 0.1179 0.0067  0.0176  0.0110  77  VAL   A CA  
1182 C C   . VAL   A 77  ? 0.1492 0.1291 0.1081 0.0104  0.0149  0.0015  77  VAL   A C   
1183 O O   . VAL   A 77  ? 0.1572 0.1344 0.1141 0.0136  0.0256  -0.0054 77  VAL   A O   
1184 C CB  . VAL   A 77  ? 0.1770 0.1541 0.1273 0.0052  0.0121  0.0171  77  VAL   A CB  
1185 C CG1 . VAL   A 77  ? 0.1729 0.1670 0.1460 0.0132  -0.0008 0.0053  77  VAL   A CG1 
1186 C CG2 . VAL   A 77  ? 0.2007 0.1700 0.1550 -0.0021 -0.0018 0.0223  77  VAL   A CG2 
1196 N N   . GLY   A 78  ? 0.1502 0.1285 0.1076 0.0044  0.0225  0.0051  78  GLY   A N   
1197 C CA  . GLY   A 78  ? 0.1441 0.1278 0.1262 0.0023  0.0243  0.0095  78  GLY   A CA  
1198 C C   . GLY   A 78  ? 0.1385 0.1203 0.1167 0.0029  0.0256  0.0079  78  GLY   A C   
1199 O O   . GLY   A 78  ? 0.1368 0.1276 0.1299 0.0023  0.0203  0.0225  78  GLY   A O   
1203 N N   . GLY   A 79  ? 0.1437 0.1183 0.1181 0.0029  0.0174  0.0125  79  GLY   A N   
1204 C CA  . GLY   A 79  ? 0.1404 0.1218 0.1286 0.0024  0.0157  0.0056  79  GLY   A CA  
1205 C C   . GLY   A 79  ? 0.1250 0.1156 0.1227 0.0006  0.0141  0.0026  79  GLY   A C   
1206 O O   . GLY   A 79  ? 0.1314 0.1273 0.1257 0.0190  0.0119  0.0060  79  GLY   A O   
1210 N N   . SER   A 80  ? 0.1177 0.1315 0.1434 0.0015  0.0160  -0.0060 80  SER   A N   
1211 C CA  . SER   A 80  ? 0.1179 0.1246 0.1278 -0.0010 0.0081  -0.0000 80  SER   A CA  
1212 C C   . SER   A 80  ? 0.1171 0.1262 0.1292 -0.0019 0.0059  0.0087  80  SER   A C   
1213 O O   . SER   A 80  ? 0.1152 0.1468 0.1652 0.0059  0.0148  0.0007  80  SER   A O   
1214 C CB  . SER   A 80  ? 0.1274 0.1268 0.1521 -0.0083 0.0032  0.0005  80  SER   A CB  
1215 O OG  . SER   A 80  ? 0.1557 0.1264 0.1957 0.0048  -0.0048 0.0126  80  SER   A OG  
1221 N N   . CYS   A 81  ? 0.1114 0.1243 0.1245 0.0017  0.0017  0.0035  81  CYS   A N   
1222 C CA  . CYS   A 81  ? 0.1108 0.1323 0.1221 -0.0035 -0.0078 0.0132  81  CYS   A CA  
1223 C C   . CYS   A 81  ? 0.1117 0.1245 0.1190 -0.0068 -0.0011 0.0172  81  CYS   A C   
1224 O O   . CYS   A 81  ? 0.1117 0.1482 0.1378 -0.0006 -0.0000 0.0302  81  CYS   A O   
1225 C CB  . CYS   A 81  ? 0.1187 0.1364 0.1409 -0.0115 -0.0005 0.0166  81  CYS   A CB  
1226 S SG  . CYS   A 81  ? 0.1375 0.1250 0.1428 -0.0117 0.0009  0.0098  81  CYS   A SG  
1232 N N   . VAL   A 82  ? 0.1166 0.1335 0.1153 0.0009  -0.0105 0.0094  82  VAL   A N   
1233 C CA  . VAL   A 82  ? 0.1304 0.1383 0.1241 0.0003  -0.0108 0.0184  82  VAL   A CA  
1234 C C   . VAL   A 82  ? 0.1236 0.1380 0.1302 -0.0007 -0.0110 0.0154  82  VAL   A C   
1235 O O   . VAL   A 82  ? 0.1198 0.1509 0.1653 0.0022  -0.0064 -0.0055 82  VAL   A O   
1236 C CB  . VAL   A 82  ? 0.1609 0.1446 0.1418 0.0055  -0.0053 0.0217  82  VAL   A CB  
1237 C CG1 . VAL   A 82  ? 0.1779 0.1608 0.1618 0.0105  0.0030  0.0196  82  VAL   A CG1 
1238 C CG2 . VAL   A 82  ? 0.1720 0.1459 0.1667 0.0018  -0.0074 0.0342  82  VAL   A CG2 
1248 N N   . LEU   A 83  ? 0.1224 0.1336 0.1273 -0.0066 -0.0092 0.0078  83  LEU   A N   
1249 C CA  . LEU   A 83  ? 0.1262 0.1396 0.1184 -0.0085 -0.0096 0.0043  83  LEU   A CA  
1250 C C   . LEU   A 83  ? 0.1335 0.1402 0.1100 -0.0075 -0.0136 0.0105  83  LEU   A C   
1251 O O   . LEU   A 83  ? 0.1396 0.1393 0.1224 -0.0109 -0.0031 0.0112  83  LEU   A O   
1252 C CB  . LEU   A 83  ? 0.1363 0.1441 0.1235 -0.0127 -0.0086 0.0100  83  LEU   A CB  
1253 C CG  . LEU   A 83  ? 0.1482 0.1545 0.1350 -0.0105 0.0028  0.0018  83  LEU   A CG  
1254 C CD1 . LEU   A 83  ? 0.1582 0.1538 0.1405 -0.0236 0.0016  0.0170  83  LEU   A CD1 
1255 C CD2 . LEU   A 83  ? 0.1409 0.1684 0.1618 -0.0113 0.0208  0.0156  83  LEU   A CD2 
1267 N N   . SER   A 84  ? 0.1451 0.1447 0.1143 -0.0115 -0.0097 0.0153  84  SER   A N   
1268 C CA  . SER   A 84  ? 0.1542 0.1477 0.1061 -0.0114 -0.0105 0.0089  84  SER   A CA  
1269 C C   . SER   A 84  ? 0.1587 0.1423 0.1047 -0.0141 0.0020  0.0041  84  SER   A C   
1270 O O   . SER   A 84  ? 0.1546 0.1605 0.1111 -0.0124 -0.0048 0.0023  84  SER   A O   
1271 C CB  . SER   A 84  ? 0.1613 0.1742 0.1272 -0.0097 -0.0054 -0.0014 84  SER   A CB  
1272 O OG  . SER   A 84  ? 0.1671 0.1913 0.1325 -0.0072 -0.0205 -0.0129 84  SER   A OG  
1278 N N   . GLY   A 85  ? 0.1718 0.1543 0.1072 -0.0165 0.0114  0.0011  85  GLY   A N   
1279 C CA  . GLY   A 85  ? 0.1758 0.1615 0.1263 -0.0219 0.0138  -0.0041 85  GLY   A CA  
1280 C C   . GLY   A 85  ? 0.1664 0.1677 0.1068 -0.0163 0.0034  -0.0018 85  GLY   A C   
1281 O O   . GLY   A 85  ? 0.1616 0.1795 0.1179 -0.0241 0.0136  -0.0131 85  GLY   A O   
1285 N N   . HIS   A 86  ? 0.1689 0.1544 0.1067 -0.0126 -0.0023 -0.0007 86  HIS   A N   
1286 C CA  . HIS   A 86  ? 0.1857 0.1648 0.1037 -0.0153 0.0035  -0.0011 86  HIS   A CA  
1287 C C   . HIS   A 86  ? 0.2060 0.1751 0.0996 -0.0150 -0.0070 -0.0069 86  HIS   A C   
1288 O O   . HIS   A 86  ? 0.2155 0.1955 0.1153 -0.0091 0.0052  -0.0041 86  HIS   A O   
1289 C CB  . HIS   A 86  ? 0.1813 0.1548 0.1218 -0.0109 0.0063  0.0004  86  HIS   A CB  
1290 C CG  . HIS   A 86  ? 0.1753 0.1558 0.1320 -0.0066 0.0132  0.0116  86  HIS   A CG  
1291 N ND1 . HIS   A 86  ? 0.1814 0.1617 0.1589 -0.0155 0.0079  0.0097  86  HIS   A ND1 
1292 C CD2 . HIS   A 86  ? 0.1790 0.1572 0.1296 0.0036  0.0087  0.0132  86  HIS   A CD2 
1293 C CE1 . HIS   A 86  ? 0.1796 0.1620 0.1504 -0.0098 0.0208  0.0118  86  HIS   A CE1 
1294 N NE2 . HIS   A 86  ? 0.1798 0.1585 0.1342 0.0050  0.0207  0.0251  86  HIS   A NE2 
1302 N N   . ASN   A 87  ? 0.2157 0.1827 0.1113 -0.0089 0.0149  -0.0122 87  ASN   A N   
1303 C CA  . ASN   A 87  ? 0.2356 0.1957 0.1162 -0.0068 0.0400  -0.0152 87  ASN   A CA  
1304 C C   . ASN   A 87  ? 0.2338 0.2084 0.1503 -0.0117 0.0568  -0.0008 87  ASN   A C   
1305 O O   . ASN   A 87  ? 0.2556 0.2270 0.1987 -0.0228 0.0869  -0.0068 87  ASN   A O   
1306 C CB  . ASN   A 87  ? 0.2545 0.2073 0.1309 0.0033  0.0398  -0.0137 87  ASN   A CB  
1307 C CG  . ASN   A 87  ? 0.2662 0.2145 0.1354 0.0125  0.0519  -0.0057 87  ASN   A CG  
1308 O OD1 . ASN   A 87  ? 0.2827 0.2110 0.1502 0.0295  0.0474  0.0096  87  ASN   A OD1 
1309 N ND2 . ASN   A 87  ? 0.2713 0.2378 0.1488 0.0128  0.0530  0.0015  87  ASN   A ND2 
1316 N N   . LEU   A 88  ? 0.2061 0.2049 0.1500 -0.0178 0.0327  0.0137  88  LEU   A N   
1317 C CA  . LEU   A 88  ? 0.1886 0.2029 0.1673 -0.0295 0.0294  0.0268  88  LEU   A CA  
1318 C C   . LEU   A 88  ? 0.1844 0.2037 0.1567 -0.0297 0.0252  0.0271  88  LEU   A C   
1319 O O   . LEU   A 88  ? 0.1862 0.2136 0.1877 -0.0264 0.0272  0.0505  88  LEU   A O   
1320 C CB  . LEU   A 88  ? 0.1929 0.2142 0.1912 -0.0401 -0.0073 0.0411  88  LEU   A CB  
1321 C CG  . LEU   A 88  ? 0.2127 0.2301 0.2284 -0.0422 -0.0217 0.0477  88  LEU   A CG  
1322 C CD1 . LEU   A 88  ? 0.2284 0.2391 0.2220 -0.0429 -0.0256 0.0342  88  LEU   A CD1 
1323 C CD2 . LEU   A 88  ? 0.2263 0.2422 0.2721 -0.0337 -0.0214 0.0409  88  LEU   A CD2 
1335 N N   . ALA   A 89  ? 0.1849 0.1898 0.1294 -0.0311 0.0215  0.0069  89  ALA   A N   
1336 C CA  . ALA   A 89  ? 0.1937 0.1868 0.1101 -0.0266 0.0127  0.0116  89  ALA   A CA  
1337 C C   . ALA   A 89  ? 0.1999 0.1900 0.1181 -0.0187 -0.0001 0.0022  89  ALA   A C   
1338 O O   . ALA   A 89  ? 0.1954 0.1869 0.1560 -0.0237 -0.0116 -0.0158 89  ALA   A O   
1339 C CB  . ALA   A 89  ? 0.1837 0.1864 0.1070 -0.0257 0.0083  0.0131  89  ALA   A CB  
1345 N N   . LYS   A 90  ? 0.2112 0.2038 0.1091 -0.0232 -0.0181 0.0156  90  LYS   A N   
1346 C CA  . LYS   A 90  ? 0.2174 0.2150 0.1156 -0.0223 -0.0303 0.0117  90  LYS   A CA  
1347 C C   . LYS   A 90  ? 0.1932 0.2005 0.1195 -0.0215 -0.0294 0.0034  90  LYS   A C   
1348 O O   . LYS   A 90  ? 0.1952 0.2163 0.1497 -0.0274 -0.0356 0.0018  90  LYS   A O   
1349 C CB  . LYS   A 90  ? 0.2446 0.2471 0.1567 -0.0149 -0.0386 0.0308  90  LYS   A CB  
1350 C CG  . LYS   A 90  ? 0.2708 0.2736 0.2532 -0.0105 -0.0363 0.0389  90  LYS   A CG  
1351 C CD  . LYS   A 90  ? 0.3010 0.3011 0.3528 -0.0079 -0.0222 0.0443  90  LYS   A CD  
1352 C CE  . LYS   A 90  ? 0.3269 0.3261 0.4177 -0.0068 -0.0116 0.0425  90  LYS   A CE  
1353 N NZ  . LYS   A 90  ? 0.3372 0.3380 0.4652 -0.0067 -0.0073 0.0382  90  LYS   A NZ  
1367 N N   . HIS   A 91  ? 0.1792 0.1721 0.0907 -0.0191 -0.0276 0.0098  91  HIS   A N   
1368 C CA  . HIS   A 91  ? 0.1678 0.1632 0.0935 -0.0148 -0.0244 0.0151  91  HIS   A CA  
1369 C C   . HIS   A 91  ? 0.1488 0.1544 0.0842 -0.0180 -0.0112 0.0150  91  HIS   A C   
1370 O O   . HIS   A 91  ? 0.1462 0.1649 0.1046 -0.0180 -0.0034 0.0163  91  HIS   A O   
1371 C CB  . HIS   A 91  ? 0.1844 0.1875 0.1450 0.0088  -0.0385 0.0085  91  HIS   A CB  
1372 C CG  . HIS   A 91  ? 0.2202 0.2351 0.2284 0.0187  -0.0649 0.0075  91  HIS   A CG  
1373 N ND1 . HIS   A 91  ? 0.2302 0.2635 0.2720 0.0193  -0.0709 -0.0065 91  HIS   A ND1 
1374 C CD2 . HIS   A 91  ? 0.2444 0.2572 0.2556 0.0249  -0.0756 0.0184  91  HIS   A CD2 
1375 C CE1 . HIS   A 91  ? 0.2394 0.2722 0.2818 0.0241  -0.0752 0.0043  91  HIS   A CE1 
1376 N NE2 . HIS   A 91  ? 0.2530 0.2709 0.2813 0.0296  -0.0762 0.0111  91  HIS   A NE2 
1384 N N   . CYS   A 92  ? 0.1369 0.1460 0.0931 -0.0149 -0.0096 0.0115  92  CYS   A N   
1385 C CA  . CYS   A 92  ? 0.1268 0.1375 0.1104 -0.0139 -0.0017 0.0060  92  CYS   A CA  
1386 C C   . CYS   A 92  ? 0.1174 0.1346 0.0993 -0.0128 0.0031  0.0122  92  CYS   A C   
1387 O O   . CYS   A 92  ? 0.1206 0.1421 0.1173 -0.0129 -0.0046 0.0078  92  CYS   A O   
1388 C CB  . CYS   A 92  ? 0.1298 0.1397 0.1268 -0.0050 0.0006  0.0123  92  CYS   A CB  
1389 S SG  . CYS   A 92  ? 0.1327 0.1299 0.1109 -0.0085 -0.0028 0.0077  92  CYS   A SG  
1395 N N   . LEU   A 93  ? 0.1168 0.1215 0.1075 -0.0089 0.0064  0.0122  93  LEU   A N   
1396 C CA  . LEU   A 93  ? 0.1112 0.1191 0.1049 -0.0056 0.0066  0.0090  93  LEU   A CA  
1397 C C   . LEU   A 93  ? 0.1091 0.1085 0.1022 -0.0021 0.0046  0.0049  93  LEU   A C   
1398 O O   . LEU   A 93  ? 0.1093 0.1182 0.1046 -0.0011 0.0014  0.0065  93  LEU   A O   
1399 C CB  . LEU   A 93  ? 0.1185 0.1175 0.1146 -0.0016 -0.0023 0.0150  93  LEU   A CB  
1400 C CG  . LEU   A 93  ? 0.1244 0.1195 0.1224 -0.0000 0.0005  0.0183  93  LEU   A CG  
1401 C CD1 . LEU   A 93  ? 0.1356 0.1207 0.1549 0.0014  0.0074  0.0087  93  LEU   A CD1 
1402 C CD2 . LEU   A 93  ? 0.1388 0.1237 0.1363 -0.0060 0.0003  0.0099  93  LEU   A CD2 
1414 N N   . HIS   A 94  ? 0.1085 0.1092 0.1034 -0.0013 0.0044  0.0081  94  HIS   A N   
1415 C CA  . HIS   A 94  ? 0.1070 0.1110 0.0991 -0.0032 -0.0016 0.0123  94  HIS   A CA  
1416 C C   . HIS   A 94  ? 0.1061 0.1093 0.1054 -0.0027 0.0018  0.0077  94  HIS   A C   
1417 O O   . HIS   A 94  ? 0.1047 0.1302 0.1456 0.0014  0.0029  -0.0110 94  HIS   A O   
1418 C CB  . HIS   A 94  ? 0.1115 0.1107 0.1093 0.0024  0.0008  0.0139  94  HIS   A CB  
1419 C CG  . HIS   A 94  ? 0.1113 0.1117 0.1085 -0.0055 -0.0051 0.0117  94  HIS   A CG  
1420 N ND1 . HIS   A 94  ? 0.1150 0.1105 0.1167 -0.0015 -0.0015 0.0125  94  HIS   A ND1 
1421 C CD2 . HIS   A 94  ? 0.1220 0.1208 0.1168 -0.0005 -0.0068 0.0061  94  HIS   A CD2 
1422 C CE1 . HIS   A 94  ? 0.1208 0.1125 0.1158 -0.0055 -0.0078 0.0044  94  HIS   A CE1 
1423 N NE2 . HIS   A 94  ? 0.1284 0.1144 0.1221 -0.0070 -0.0064 0.0026  94  HIS   A NE2 
1431 N N   . VAL   A 95  ? 0.1044 0.1055 0.0902 0.0004  0.0082  0.0016  95  VAL   A N   
1432 C CA  . VAL   A 95  ? 0.1129 0.1095 0.0916 -0.0004 0.0095  0.0094  95  VAL   A CA  
1433 C C   . VAL   A 95  ? 0.1136 0.1092 0.0801 -0.0111 0.0045  -0.0011 95  VAL   A C   
1434 O O   . VAL   A 95  ? 0.1203 0.1194 0.0977 0.0110  0.0077  0.0023  95  VAL   A O   
1435 C CB  . VAL   A 95  ? 0.1161 0.1126 0.1116 -0.0078 0.0026  0.0063  95  VAL   A CB  
1436 C CG1 . VAL   A 95  ? 0.1360 0.1218 0.1198 -0.0114 0.0029  -0.0058 95  VAL   A CG1 
1437 C CG2 . VAL   A 95  ? 0.1209 0.1130 0.1197 -0.0114 0.0061  0.0147  95  VAL   A CG2 
1447 N N   . VAL   A 96  ? 0.1167 0.1101 0.0850 -0.0011 0.0028  0.0108  96  VAL   A N   
1448 C CA  . VAL   A 96  ? 0.1202 0.1116 0.1014 0.0017  0.0100  0.0119  96  VAL   A CA  
1449 C C   . VAL   A 96  ? 0.1230 0.1196 0.1009 -0.0045 0.0114  0.0108  96  VAL   A C   
1450 O O   . VAL   A 96  ? 0.1339 0.1261 0.1216 -0.0047 0.0156  -0.0015 96  VAL   A O   
1451 C CB  . VAL   A 96  ? 0.1278 0.1190 0.1096 -0.0014 0.0198  0.0114  96  VAL   A CB  
1452 C CG1 . VAL   A 96  ? 0.1332 0.1282 0.1033 -0.0003 0.0138  0.0108  96  VAL   A CG1 
1453 C CG2 . VAL   A 96  ? 0.1299 0.1276 0.1287 -0.0081 0.0180  0.0094  96  VAL   A CG2 
1463 N N   . GLY   A 97  ? 0.1228 0.1231 0.1064 -0.0082 0.0104  0.0086  97  GLY   A N   
1464 C CA  . GLY   A 97  ? 0.1327 0.1344 0.0999 -0.0024 0.0041  0.0129  97  GLY   A CA  
1465 C C   . GLY   A 97  ? 0.1336 0.1488 0.0963 -0.0046 0.0043  0.0043  97  GLY   A C   
1466 O O   . GLY   A 97  ? 0.1460 0.1493 0.1164 -0.0066 0.0024  0.0153  97  GLY   A O   
1470 N N   . PRO   A 98  ? 0.1437 0.1544 0.0811 -0.0014 0.0004  0.0165  98  PRO   A N   
1471 C CA  . PRO   A 98  ? 0.1556 0.1748 0.0981 -0.0013 0.0027  0.0056  98  PRO   A CA  
1472 C C   . PRO   A 98  ? 0.1584 0.1783 0.0931 -0.0103 0.0007  0.0247  98  PRO   A C   
1473 O O   . PRO   A 98  ? 0.1523 0.1598 0.1215 -0.0066 -0.0039 0.0196  98  PRO   A O   
1474 C CB  . PRO   A 98  ? 0.1690 0.1838 0.0915 0.0052  -0.0015 -0.0039 98  PRO   A CB  
1475 C CG  . PRO   A 98  ? 0.1723 0.1681 0.1099 0.0043  -0.0076 -0.0078 98  PRO   A CG  
1476 C CD  . PRO   A 98  ? 0.1561 0.1536 0.0944 0.0058  -0.0044 0.0060  98  PRO   A CD  
1484 N N   . ASN   A 99  ? 0.1714 0.2007 0.1055 -0.0073 0.0005  0.0472  99  ASN   A N   
1485 C CA  . ASN   A 99  ? 0.1916 0.2141 0.1142 -0.0086 -0.0015 0.0636  99  ASN   A CA  
1486 C C   . ASN   A 99  ? 0.2065 0.2588 0.1045 -0.0234 0.0077  0.0672  99  ASN   A C   
1487 O O   . ASN   A 99  ? 0.2170 0.2928 0.1245 -0.0112 0.0006  0.0628  99  ASN   A O   
1488 C CB  . ASN   A 99  ? 0.1942 0.2035 0.1576 -0.0087 -0.0231 0.0689  99  ASN   A CB  
1489 C CG  . ASN   A 99  ? 0.1938 0.1995 0.1880 -0.0091 -0.0317 0.0531  99  ASN   A CG  
1490 O OD1 . ASN   A 99  ? 0.2061 0.2085 0.1900 -0.0012 -0.0361 0.0423  99  ASN   A OD1 
1491 N ND2 . ASN   A 99  ? 0.1904 0.1985 0.2171 -0.0072 -0.0346 0.0541  99  ASN   A ND2 
1498 N N   . VAL   A 100 ? 0.2196 0.2690 0.1032 -0.0416 -0.0171 0.0536  100 VAL   A N   
1499 C CA  . VAL   A 100 ? 0.2447 0.3019 0.1234 -0.0494 -0.0210 0.0473  100 VAL   A CA  
1500 C C   . VAL   A 100 ? 0.2513 0.3226 0.1173 -0.0516 -0.0331 0.0709  100 VAL   A C   
1501 O O   . VAL   A 100 ? 0.2592 0.3405 0.1362 -0.0481 -0.0155 0.0664  100 VAL   A O   
1502 C CB  . VAL   A 100 ? 0.2650 0.3038 0.1642 -0.0606 -0.0269 0.0336  100 VAL   A CB  
1503 C CG1 . VAL   A 100 ? 0.2676 0.3099 0.1903 -0.0664 -0.0219 0.0331  100 VAL   A CG1 
1504 C CG2 . VAL   A 100 ? 0.2773 0.3067 0.1807 -0.0661 -0.0251 0.0198  100 VAL   A CG2 
1514 N N   . ASN   A 101 ? 0.2604 0.3281 0.1623 -0.0549 -0.0432 0.1043  101 ASN   A N   
1515 C CA  . ASN   A 101 ? 0.2909 0.3382 0.1966 -0.0554 -0.0458 0.1252  101 ASN   A CA  
1516 C C   . ASN   A 101 ? 0.3112 0.3571 0.2189 -0.0571 -0.0123 0.1523  101 ASN   A C   
1517 O O   . ASN   A 101 ? 0.3299 0.3665 0.2671 -0.0557 -0.0150 0.1497  101 ASN   A O   
1518 C CB  . ASN   A 101 ? 0.2998 0.3284 0.2020 -0.0494 -0.0768 0.1097  101 ASN   A CB  
1519 C CG  . ASN   A 101 ? 0.3079 0.3196 0.1915 -0.0476 -0.0949 0.0738  101 ASN   A CG  
1520 O OD1 . ASN   A 101 ? 0.3069 0.3310 0.2050 -0.0379 -0.0871 0.0299  101 ASN   A OD1 
1521 N ND2 . ASN   A 101 ? 0.3161 0.3049 0.1884 -0.0583 -0.0936 0.0725  101 ASN   A ND2 
1528 N N   . LYS   A 102 ? 0.3079 0.3796 0.2410 -0.0668 0.0075  0.1460  102 LYS   A N   
1529 C CA  . LYS   A 102 ? 0.3175 0.3956 0.2545 -0.0656 0.0140  0.1307  102 LYS   A CA  
1530 C C   . LYS   A 102 ? 0.3269 0.4068 0.2367 -0.0485 0.0149  0.1128  102 LYS   A C   
1531 O O   . LYS   A 102 ? 0.3311 0.4231 0.2398 -0.0457 0.0215  0.1066  102 LYS   A O   
1532 C CB  . LYS   A 102 ? 0.3248 0.4021 0.3014 -0.0786 0.0081  0.1159  102 LYS   A CB  
1533 C CG  . LYS   A 102 ? 0.3327 0.4065 0.3386 -0.0878 -0.0014 0.0991  102 LYS   A CG  
1534 C CD  . LYS   A 102 ? 0.3464 0.4151 0.3757 -0.0879 -0.0127 0.0776  102 LYS   A CD  
1535 C CE  . LYS   A 102 ? 0.3590 0.4230 0.4081 -0.0849 -0.0222 0.0633  102 LYS   A CE  
1536 N NZ  . LYS   A 102 ? 0.3677 0.4277 0.4204 -0.0850 -0.0262 0.0527  102 LYS   A NZ  
1550 N N   A GLY   A 103 ? 0.3295 0.4156 0.2226 -0.0359 0.0026  0.0945  103 GLY   A N   
1551 N N   B GLY   A 103 ? 0.3295 0.3971 0.2639 -0.0393 0.0092  0.0911  103 GLY   A N   
1552 C CA  A GLY   A 103 ? 0.3317 0.4188 0.2030 -0.0258 0.0037  0.0789  103 GLY   A CA  
1553 C CA  B GLY   A 103 ? 0.3310 0.3862 0.2799 -0.0299 0.0051  0.0700  103 GLY   A CA  
1554 C C   A GLY   A 103 ? 0.3276 0.4215 0.1917 -0.0212 0.0110  0.0551  103 GLY   A C   
1555 C C   B GLY   A 103 ? 0.3306 0.3748 0.2896 -0.0218 0.0024  0.0495  103 GLY   A C   
1556 O O   A GLY   A 103 ? 0.3384 0.4314 0.2198 -0.0150 0.0118  0.0436  103 GLY   A O   
1557 O O   B GLY   A 103 ? 0.3331 0.3771 0.2999 -0.0201 0.0025  0.0461  103 GLY   A O   
1564 N N   A GLU   A 104 ? 0.3084 0.4097 0.1396 -0.0254 0.0157  0.0401  104 GLU   A N   
1565 N N   B GLU   A 104 ? 0.3262 0.3601 0.2820 -0.0167 0.0003  0.0340  104 GLU   A N   
1566 C CA  A GLU   A 104 ? 0.2854 0.3946 0.1202 -0.0358 0.0144  0.0303  104 GLU   A CA  
1567 C CA  B GLU   A 104 ? 0.3212 0.3454 0.2745 -0.0125 -0.0016 0.0197  104 GLU   A CA  
1568 C C   A GLU   A 104 ? 0.2823 0.3978 0.1306 -0.0408 0.0187  0.0146  104 GLU   A C   
1569 C C   B GLU   A 104 ? 0.3210 0.3412 0.2777 -0.0110 -0.0010 0.0112  104 GLU   A C   
1570 O O   A GLU   A 104 ? 0.2759 0.3952 0.1690 -0.0431 0.0113  0.0124  104 GLU   A O   
1571 O O   B GLU   A 104 ? 0.3204 0.3402 0.2752 -0.0110 -0.0019 0.0100  104 GLU   A O   
1572 C CB  A GLU   A 104 ? 0.2628 0.3757 0.1088 -0.0425 0.0152  0.0441  104 GLU   A CB  
1573 C CB  B GLU   A 104 ? 0.3161 0.3358 0.2646 -0.0101 -0.0037 0.0157  104 GLU   A CB  
1574 C CG  A GLU   A 104 ? 0.2499 0.3621 0.1281 -0.0451 0.0091  0.0526  104 GLU   A CG  
1575 C CG  B GLU   A 104 ? 0.3125 0.3283 0.2599 -0.0076 -0.0056 0.0125  104 GLU   A CG  
1576 C CD  A GLU   A 104 ? 0.2326 0.3479 0.1263 -0.0484 0.0111  0.0644  104 GLU   A CD  
1577 C CD  B GLU   A 104 ? 0.3098 0.3227 0.2559 -0.0054 -0.0067 0.0095  104 GLU   A CD  
1578 O OE1 A GLU   A 104 ? 0.2143 0.3370 0.1112 -0.0490 0.0039  0.0640  104 GLU   A OE1 
1579 O OE1 B GLU   A 104 ? 0.3087 0.3208 0.2545 -0.0041 -0.0073 0.0090  104 GLU   A OE1 
1580 O OE2 A GLU   A 104 ? 0.2451 0.3442 0.1457 -0.0509 0.0097  0.0809  104 GLU   A OE2 
1581 O OE2 B GLU   A 104 ? 0.3100 0.3208 0.2584 -0.0048 -0.0077 0.0075  104 GLU   A OE2 
1594 N N   A ASP   A 105 ? 0.2875 0.4044 0.1486 -0.0432 0.0347  -0.0049 105 ASP   A N   
1595 N N   B ASP   A 105 ? 0.3217 0.3386 0.2886 -0.0099 0.0010  0.0046  105 ASP   A N   
1596 C CA  A ASP   A 105 ? 0.2895 0.4087 0.1969 -0.0410 0.0412  -0.0333 105 ASP   A CA  
1597 C CA  B ASP   A 105 ? 0.3220 0.3361 0.3036 -0.0090 0.0026  -0.0020 105 ASP   A CA  
1598 C C   A ASP   A 105 ? 0.2549 0.3933 0.1578 -0.0475 0.0253  -0.0468 105 ASP   A C   
1599 C C   B ASP   A 105 ? 0.3157 0.3302 0.2904 -0.0105 0.0026  -0.0040 105 ASP   A C   
1600 O O   A ASP   A 105 ? 0.2315 0.3790 0.1170 -0.0482 0.0112  -0.0645 105 ASP   A O   
1601 O O   B ASP   A 105 ? 0.3150 0.3306 0.2848 -0.0096 0.0019  -0.0045 105 ASP   A O   
1602 C CB  A ASP   A 105 ? 0.3201 0.4287 0.2845 -0.0318 0.0576  -0.0473 105 ASP   A CB  
1603 C CB  B ASP   A 105 ? 0.3276 0.3391 0.3314 -0.0068 0.0040  -0.0062 105 ASP   A CB  
1604 C CG  A ASP   A 105 ? 0.3454 0.4446 0.3657 -0.0212 0.0597  -0.0653 105 ASP   A CG  
1605 C CG  B ASP   A 105 ? 0.3323 0.3417 0.3572 -0.0046 0.0039  -0.0101 105 ASP   A CG  
1606 O OD1 A ASP   A 105 ? 0.3547 0.4506 0.3783 -0.0197 0.0583  -0.0811 105 ASP   A OD1 
1607 O OD1 B ASP   A 105 ? 0.3338 0.3429 0.3653 -0.0042 0.0037  -0.0128 105 ASP   A OD1 
1608 O OD2 A ASP   A 105 ? 0.3581 0.4521 0.4113 -0.0184 0.0623  -0.0621 105 ASP   A OD2 
1609 O OD2 B ASP   A 105 ? 0.3349 0.3429 0.3694 -0.0044 0.0037  -0.0101 105 ASP   A OD2 
1618 N N   A ILE   A 106 ? 0.2413 0.3874 0.1771 -0.0518 -0.0000 -0.0485 106 ILE   A N   
1619 N N   B ILE   A 106 ? 0.3097 0.3235 0.2842 -0.0130 0.0024  -0.0054 106 ILE   A N   
1620 C CA  A ILE   A 106 ? 0.2179 0.3752 0.1973 -0.0603 -0.0192 -0.0624 106 ILE   A CA  
1621 C CA  B ILE   A 106 ? 0.3023 0.3163 0.2799 -0.0161 0.0031  -0.0079 106 ILE   A CA  
1622 C C   A ILE   A 106 ? 0.2009 0.3471 0.1956 -0.0745 -0.0177 -0.0799 106 ILE   A C   
1623 C C   B ILE   A 106 ? 0.2930 0.3071 0.2770 -0.0212 0.0080  -0.0126 106 ILE   A C   
1624 O O   A ILE   A 106 ? 0.1836 0.3342 0.1984 -0.0722 0.0048  -0.0874 106 ILE   A O   
1625 O O   B ILE   A 106 ? 0.2925 0.3064 0.2725 -0.0205 0.0083  -0.0120 106 ILE   A O   
1626 C CB  A ILE   A 106 ? 0.2211 0.3901 0.2508 -0.0466 -0.0344 -0.0376 106 ILE   A CB  
1627 C CB  B ILE   A 106 ? 0.3042 0.3182 0.2854 -0.0142 -0.0009 -0.0045 106 ILE   A CB  
1628 C CG1 A ILE   A 106 ? 0.2184 0.3921 0.2859 -0.0317 -0.0362 -0.0140 106 ILE   A CG1 
1629 C CG1 B ILE   A 106 ? 0.3037 0.3178 0.2902 -0.0124 -0.0026 -0.0010 106 ILE   A CG1 
1630 C CG2 A ILE   A 106 ? 0.2282 0.3971 0.2687 -0.0448 -0.0453 -0.0371 106 ILE   A CG2 
1631 C CG2 B ILE   A 106 ? 0.3061 0.3201 0.2872 -0.0140 -0.0026 -0.0043 106 ILE   A CG2 
1632 C CD1 A ILE   A 106 ? 0.2220 0.3881 0.3047 -0.0209 -0.0253 -0.0010 106 ILE   A CD1 
1633 C CD1 B ILE   A 106 ? 0.3033 0.3163 0.2910 -0.0110 -0.0025 0.0012  106 ILE   A CD1 
1656 N N   A GLN   A 107 ? 0.2191 0.3337 0.2185 -0.0737 -0.0134 -0.0889 107 GLN   A N   
1657 N N   B GLN   A 107 ? 0.2839 0.2981 0.2842 -0.0265 0.0138  -0.0193 107 GLN   A N   
1658 C CA  A GLN   A 107 ? 0.2453 0.3183 0.2917 -0.0578 0.0125  -0.0893 107 GLN   A CA  
1659 C CA  B GLN   A 107 ? 0.2734 0.2883 0.2971 -0.0310 0.0198  -0.0281 107 GLN   A CA  
1660 C C   A GLN   A 107 ? 0.2250 0.2686 0.2790 -0.0494 0.0310  -0.0629 107 GLN   A C   
1661 C C   B GLN   A 107 ? 0.2396 0.2595 0.2573 -0.0392 0.0282  -0.0379 107 GLN   A C   
1662 O O   A GLN   A 107 ? 0.2310 0.2578 0.3328 -0.0372 0.0410  -0.0620 107 GLN   A O   
1663 O O   B GLN   A 107 ? 0.2425 0.2599 0.2666 -0.0382 0.0291  -0.0364 107 GLN   A O   
1664 C CB  A GLN   A 107 ? 0.2835 0.3504 0.3804 -0.0609 0.0096  -0.0965 107 GLN   A CB  
1665 C CB  B GLN   A 107 ? 0.2942 0.3055 0.3490 -0.0294 0.0171  -0.0253 107 GLN   A CB  
1666 C CG  A GLN   A 107 ? 0.3239 0.3829 0.4781 -0.0606 0.0066  -0.0915 107 GLN   A CG  
1667 C CG  B GLN   A 107 ? 0.3126 0.3207 0.4003 -0.0276 0.0144  -0.0226 107 GLN   A CG  
1668 C CD  A GLN   A 107 ? 0.3565 0.4069 0.5563 -0.0614 0.0074  -0.0837 107 GLN   A CD  
1669 C CD  B GLN   A 107 ? 0.3266 0.3321 0.4425 -0.0261 0.0125  -0.0194 107 GLN   A CD  
1670 O OE1 A GLN   A 107 ? 0.3666 0.4143 0.5886 -0.0637 0.0082  -0.0816 107 GLN   A OE1 
1671 O OE1 B GLN   A 107 ? 0.3315 0.3360 0.4583 -0.0259 0.0122  -0.0189 107 GLN   A OE1 
1672 N NE2 A GLN   A 107 ? 0.3638 0.4155 0.5822 -0.0629 0.0065  -0.0851 107 GLN   A NE2 
1673 N NE2 B GLN   A 107 ? 0.3314 0.3361 0.4568 -0.0259 0.0117  -0.0188 107 GLN   A NE2 
1690 N N   . LEU   A 108 ? 0.2023 0.2295 0.2169 -0.0480 0.0331  -0.0518 108 LEU   A N   
1691 C CA  . LEU   A 108 ? 0.1765 0.1810 0.1780 -0.0214 0.0305  -0.0155 108 LEU   A CA  
1692 C C   . LEU   A 108 ? 0.1511 0.1440 0.1729 -0.0080 0.0183  0.0133  108 LEU   A C   
1693 O O   . LEU   A 108 ? 0.1468 0.1458 0.1892 -0.0022 0.0194  0.0127  108 LEU   A O   
1694 C CB  . LEU   A 108 ? 0.1800 0.1883 0.1524 -0.0256 0.0335  -0.0114 108 LEU   A CB  
1695 C CG  . LEU   A 108 ? 0.1972 0.2131 0.1725 -0.0215 0.0435  -0.0139 108 LEU   A CG  
1696 C CD1 . LEU   A 108 ? 0.2177 0.2227 0.1765 -0.0320 0.0513  -0.0148 108 LEU   A CD1 
1697 C CD2 . LEU   A 108 ? 0.2002 0.2366 0.2226 -0.0111 0.0357  -0.0049 108 LEU   A CD2 
1710 N N   . LEU   A 109 ? 0.1409 0.1442 0.1632 0.0021  0.0159  0.0235  109 LEU   A N   
1711 C CA  . LEU   A 109 ? 0.1377 0.1359 0.1505 -0.0024 0.0081  0.0176  109 LEU   A CA  
1712 C C   . LEU   A 109 ? 0.1291 0.1282 0.1332 -0.0088 0.0068  0.0091  109 LEU   A C   
1713 O O   . LEU   A 109 ? 0.1403 0.1203 0.1518 -0.0037 -0.0059 0.0024  109 LEU   A O   
1714 C CB  . LEU   A 109 ? 0.1401 0.1421 0.1607 0.0062  -0.0009 0.0313  109 LEU   A CB  
1715 C CG  . LEU   A 109 ? 0.1375 0.1476 0.1674 0.0036  0.0033  0.0344  109 LEU   A CG  
1716 C CD1 . LEU   A 109 ? 0.1423 0.1434 0.1881 -0.0016 0.0156  0.0168  109 LEU   A CD1 
1717 C CD2 . LEU   A 109 ? 0.1412 0.1647 0.1852 0.0047  0.0013  0.0340  109 LEU   A CD2 
1729 N N   . LYS   A 110 ? 0.1274 0.1234 0.1353 -0.0084 0.0006  0.0019  110 LYS   A N   
1730 C CA  . LYS   A 110 ? 0.1274 0.1185 0.1353 -0.0070 -0.0008 0.0077  110 LYS   A CA  
1731 C C   . LYS   A 110 ? 0.1304 0.1144 0.1218 -0.0086 0.0031  -0.0057 110 LYS   A C   
1732 O O   . LYS   A 110 ? 0.1247 0.1147 0.1309 -0.0082 0.0092  -0.0063 110 LYS   A O   
1733 C CB  . LYS   A 110 ? 0.1326 0.1233 0.1553 -0.0036 -0.0024 -0.0046 110 LYS   A CB  
1734 C CG  . LYS   A 110 ? 0.1341 0.1227 0.1654 -0.0027 -0.0028 -0.0101 110 LYS   A CG  
1735 C CD  . LYS   A 110 ? 0.1402 0.1293 0.1846 -0.0047 -0.0028 -0.0124 110 LYS   A CD  
1736 C CE  . LYS   A 110 ? 0.1494 0.1338 0.2069 -0.0086 0.0096  -0.0074 110 LYS   A CE  
1737 N NZ  . LYS   A 110 ? 0.1519 0.1329 0.2228 -0.0140 0.0143  -0.0036 110 LYS   A NZ  
1751 N N   . SER   A 111 ? 0.1275 0.1220 0.1284 -0.0038 0.0006  0.0012  111 SER   A N   
1752 C CA  . SER   A 111 ? 0.1229 0.1220 0.1367 0.0006  0.0037  0.0004  111 SER   A CA  
1753 C C   . SER   A 111 ? 0.1172 0.1166 0.1282 -0.0050 0.0080  0.0069  111 SER   A C   
1754 O O   . SER   A 111 ? 0.1286 0.1136 0.1493 -0.0043 0.0068  0.0062  111 SER   A O   
1755 C CB  . SER   A 111 ? 0.1344 0.1430 0.1529 -0.0071 0.0234  -0.0109 111 SER   A CB  
1756 O OG  . SER   A 111 ? 0.1866 0.1647 0.1688 0.0004  0.0311  -0.0100 111 SER   A OG  
1762 N N   . ALA   A 112 ? 0.1226 0.1079 0.1357 -0.0005 0.0114  0.0046  112 ALA   A N   
1763 C CA  . ALA   A 112 ? 0.1241 0.1094 0.1281 -0.0008 0.0136  0.0026  112 ALA   A CA  
1764 C C   . ALA   A 112 ? 0.1230 0.1067 0.1277 -0.0030 0.0113  -0.0041 112 ALA   A C   
1765 O O   . ALA   A 112 ? 0.1252 0.1050 0.1365 -0.0107 0.0096  0.0043  112 ALA   A O   
1766 C CB  . ALA   A 112 ? 0.1332 0.1144 0.1360 -0.0061 0.0111  0.0017  112 ALA   A CB  
1772 N N   . TYR   A 113 ? 0.1128 0.1098 0.1353 -0.0023 0.0077  0.0078  113 TYR   A N   
1773 C CA  . TYR   A 113 ? 0.1104 0.1085 0.1312 -0.0004 0.0112  0.0076  113 TYR   A CA  
1774 C C   . TYR   A 113 ? 0.1101 0.1074 0.1199 -0.0067 0.0053  0.0012  113 TYR   A C   
1775 O O   . TYR   A 113 ? 0.1147 0.1110 0.1355 -0.0021 0.0187  0.0004  113 TYR   A O   
1776 C CB  . TYR   A 113 ? 0.1140 0.1172 0.1385 -0.0017 0.0019  0.0127  113 TYR   A CB  
1777 C CG  . TYR   A 113 ? 0.1151 0.1195 0.1347 -0.0069 0.0033  0.0152  113 TYR   A CG  
1778 C CD1 . TYR   A 113 ? 0.1164 0.1255 0.1287 -0.0024 0.0046  0.0238  113 TYR   A CD1 
1779 C CD2 . TYR   A 113 ? 0.1201 0.1262 0.1271 -0.0092 0.0053  0.0172  113 TYR   A CD2 
1780 C CE1 . TYR   A 113 ? 0.1203 0.1346 0.1244 -0.0007 0.0071  0.0201  113 TYR   A CE1 
1781 C CE2 . TYR   A 113 ? 0.1218 0.1323 0.1302 -0.0090 -0.0015 0.0180  113 TYR   A CE2 
1782 C CZ  . TYR   A 113 ? 0.1148 0.1323 0.1242 0.0016  0.0110  0.0262  113 TYR   A CZ  
1783 O OH  . TYR   A 113 ? 0.1162 0.1428 0.1478 0.0117  0.0113  0.0334  113 TYR   A OH  
1793 N N   . GLU   A 114 ? 0.1120 0.1092 0.1310 -0.0044 0.0121  0.0063  114 GLU   A N   
1794 C CA  . GLU   A 114 ? 0.1138 0.1031 0.1411 0.0072  0.0052  0.0167  114 GLU   A CA  
1795 C C   . GLU   A 114 ? 0.1101 0.1094 0.1324 0.0053  0.0130  0.0094  114 GLU   A C   
1796 O O   . GLU   A 114 ? 0.1229 0.1115 0.1320 0.0009  0.0037  0.0057  114 GLU   A O   
1797 C CB  . GLU   A 114 ? 0.1161 0.1109 0.1357 -0.0013 0.0079  0.0081  114 GLU   A CB  
1798 C CG  . GLU   A 114 ? 0.1239 0.1150 0.1408 0.0016  0.0113  0.0003  114 GLU   A CG  
1799 C CD  . GLU   A 114 ? 0.1329 0.1186 0.1527 -0.0009 0.0076  0.0023  114 GLU   A CD  
1800 O OE1 . GLU   A 114 ? 0.1340 0.1164 0.1656 -0.0069 0.0186  -0.0047 114 GLU   A OE1 
1801 O OE2 . GLU   A 114 ? 0.1510 0.1222 0.1738 -0.0063 0.0130  -0.0182 114 GLU   A OE2 
1808 N N   . ASN   A 115 ? 0.1125 0.1112 0.1274 -0.0015 0.0096  0.0068  115 ASN   A N   
1809 C CA  . ASN   A 115 ? 0.1127 0.1172 0.1360 -0.0068 0.0107  0.0058  115 ASN   A CA  
1810 C C   . ASN   A 115 ? 0.1196 0.1118 0.1232 -0.0063 0.0051  0.0018  115 ASN   A C   
1811 O O   . ASN   A 115 ? 0.1219 0.1222 0.1236 -0.0091 0.0094  0.0065  115 ASN   A O   
1812 C CB  . ASN   A 115 ? 0.1210 0.1232 0.1309 -0.0126 0.0079  0.0038  115 ASN   A CB  
1813 C CG  . ASN   A 115 ? 0.1200 0.1454 0.1444 -0.0167 0.0199  0.0038  115 ASN   A CG  
1814 O OD1 . ASN   A 115 ? 0.1270 0.2337 0.1708 -0.0147 0.0231  0.0216  115 ASN   A OD1 
1815 N ND2 . ASN   A 115 ? 0.1241 0.1322 0.1345 -0.0143 0.0146  0.0081  115 ASN   A ND2 
1822 N N   . PHE   A 116 ? 0.1110 0.1140 0.1259 0.0000  0.0161  0.0125  116 PHE   A N   
1823 C CA  . PHE   A 116 ? 0.1150 0.1217 0.1271 -0.0012 0.0096  0.0101  116 PHE   A CA  
1824 C C   . PHE   A 116 ? 0.1126 0.1238 0.1302 -0.0040 0.0122  0.0165  116 PHE   A C   
1825 O O   . PHE   A 116 ? 0.1183 0.1298 0.1307 0.0048  0.0085  0.0212  116 PHE   A O   
1826 C CB  . PHE   A 116 ? 0.1164 0.1123 0.1385 -0.0020 0.0163  0.0075  116 PHE   A CB  
1827 C CG  . PHE   A 116 ? 0.1132 0.1133 0.1278 -0.0064 0.0120  0.0029  116 PHE   A CG  
1828 C CD1 . PHE   A 116 ? 0.1138 0.1104 0.1286 -0.0054 0.0096  0.0118  116 PHE   A CD1 
1829 C CD2 . PHE   A 116 ? 0.1214 0.1188 0.1399 -0.0051 0.0136  0.0125  116 PHE   A CD2 
1830 C CE1 . PHE   A 116 ? 0.1220 0.1108 0.1418 -0.0125 0.0064  0.0096  116 PHE   A CE1 
1831 C CE2 . PHE   A 116 ? 0.1190 0.1178 0.1526 -0.0037 0.0103  0.0082  116 PHE   A CE2 
1832 C CZ  . PHE   A 116 ? 0.1233 0.1081 0.1406 -0.0044 0.0001  0.0162  116 PHE   A CZ  
1842 N N   . ASN   A 117 ? 0.1144 0.1137 0.1378 -0.0009 0.0141  0.0152  117 ASN   A N   
1843 C CA  . ASN   A 117 ? 0.1160 0.1148 0.1437 0.0010  0.0094  0.0234  117 ASN   A CA  
1844 C C   . ASN   A 117 ? 0.1168 0.1270 0.1482 -0.0008 0.0128  0.0218  117 ASN   A C   
1845 O O   . ASN   A 117 ? 0.1235 0.1301 0.1688 -0.0048 -0.0053 0.0314  117 ASN   A O   
1846 C CB  . ASN   A 117 ? 0.1165 0.1162 0.1463 0.0020  0.0070  0.0194  117 ASN   A CB  
1847 C CG  . ASN   A 117 ? 0.1178 0.1203 0.1437 -0.0013 0.0130  0.0215  117 ASN   A CG  
1848 O OD1 . ASN   A 117 ? 0.1215 0.1421 0.1502 -0.0105 0.0167  0.0130  117 ASN   A OD1 
1849 N ND2 . ASN   A 117 ? 0.1106 0.1213 0.1458 0.0022  0.0095  0.0181  117 ASN   A ND2 
1856 N N   . GLN   A 118 ? 0.1132 0.1303 0.1535 -0.0059 0.0037  0.0233  118 GLN   A N   
1857 C CA  . GLN   A 118 ? 0.1211 0.1372 0.1558 -0.0032 -0.0010 0.0119  118 GLN   A CA  
1858 C C   . GLN   A 118 ? 0.1200 0.1421 0.1468 -0.0057 -0.0059 0.0178  118 GLN   A C   
1859 O O   . GLN   A 118 ? 0.1213 0.1713 0.1766 0.0022  -0.0116 -0.0009 118 GLN   A O   
1860 C CB  . GLN   A 118 ? 0.1189 0.1404 0.1643 -0.0019 0.0049  0.0145  118 GLN   A CB  
1861 C CG  . GLN   A 118 ? 0.1172 0.1402 0.1682 0.0000  0.0103  0.0212  118 GLN   A CG  
1862 C CD  . GLN   A 118 ? 0.1139 0.1407 0.1772 0.0025  0.0084  0.0176  118 GLN   A CD  
1863 O OE1 . GLN   A 118 ? 0.1246 0.1579 0.1808 0.0116  -0.0018 0.0063  118 GLN   A OE1 
1864 N NE2 . GLN   A 118 ? 0.1266 0.1387 0.1782 0.0054  0.0039  0.0187  118 GLN   A NE2 
1873 N N   . HIS   A 119 ? 0.1259 0.1358 0.1315 0.0013  -0.0051 0.0194  119 HIS   A N   
1874 C CA  . HIS   A 119 ? 0.1325 0.1440 0.1373 -0.0019 -0.0002 0.0214  119 HIS   A CA  
1875 C C   . HIS   A 119 ? 0.1419 0.1449 0.1273 -0.0056 0.0040  0.0196  119 HIS   A C   
1876 O O   . HIS   A 119 ? 0.1456 0.1567 0.1403 -0.0194 0.0015  0.0178  119 HIS   A O   
1877 C CB  . HIS   A 119 ? 0.1369 0.1403 0.1639 0.0001  0.0210  0.0237  119 HIS   A CB  
1878 C CG  . HIS   A 119 ? 0.1394 0.1432 0.2126 0.0054  0.0199  0.0325  119 HIS   A CG  
1879 N ND1 . HIS   A 119 ? 0.1491 0.1636 0.2770 -0.0080 0.0179  0.0235  119 HIS   A ND1 
1880 C CD2 . HIS   A 119 ? 0.1534 0.1533 0.2316 0.0151  0.0334  0.0477  119 HIS   A CD2 
1881 C CE1 . HIS   A 119 ? 0.1489 0.1648 0.2910 -0.0114 0.0319  0.0442  119 HIS   A CE1 
1882 N NE2 . HIS   A 119 ? 0.1619 0.1584 0.2813 0.0029  0.0467  0.0620  119 HIS   A NE2 
1890 N N   . GLU   A 120 ? 0.1483 0.1637 0.1313 -0.0005 0.0010  0.0344  120 GLU   A N   
1891 C CA  . GLU   A 120 ? 0.1670 0.1901 0.1567 0.0090  0.0003  0.0628  120 GLU   A CA  
1892 C C   . GLU   A 120 ? 0.1497 0.1737 0.1334 -0.0054 -0.0022 0.0531  120 GLU   A C   
1893 O O   . GLU   A 120 ? 0.1473 0.1687 0.1531 -0.0064 0.0012  0.0542  120 GLU   A O   
1894 C CB  . GLU   A 120 ? 0.2294 0.2601 0.2177 0.0353  -0.0068 0.1218  120 GLU   A CB  
1895 C CG  . GLU   A 120 ? 0.3186 0.3384 0.3415 0.0486  -0.0080 0.1293  120 GLU   A CG  
1896 C CD  . GLU   A 120 ? 0.4025 0.4073 0.4705 0.0566  0.0069  0.1157  120 GLU   A CD  
1897 O OE1 . GLU   A 120 ? 0.4269 0.4269 0.5015 0.0576  0.0110  0.1096  120 GLU   A OE1 
1898 O OE2 . GLU   A 120 ? 0.4523 0.4523 0.5261 0.0590  0.0143  0.1113  120 GLU   A OE2 
1905 N N   . VAL   A 121 ? 0.1466 0.1707 0.1164 -0.0056 0.0014  0.0413  121 VAL   A N   
1906 C CA  . VAL   A 121 ? 0.1548 0.1780 0.1145 -0.0060 0.0120  0.0413  121 VAL   A CA  
1907 C C   . VAL   A 121 ? 0.1426 0.1611 0.1036 -0.0111 0.0123  0.0281  121 VAL   A C   
1908 O O   . VAL   A 121 ? 0.1447 0.1692 0.1290 -0.0211 -0.0050 0.0191  121 VAL   A O   
1909 C CB  . VAL   A 121 ? 0.1937 0.2084 0.1471 0.0079  0.0260  0.0563  121 VAL   A CB  
1910 C CG1 . VAL   A 121 ? 0.2039 0.2262 0.1477 0.0177  0.0367  0.0532  121 VAL   A CG1 
1911 C CG2 . VAL   A 121 ? 0.2162 0.2261 0.1942 -0.0005 0.0204  0.0439  121 VAL   A CG2 
1921 N N   . LEU   A 122 ? 0.1356 0.1403 0.1200 -0.0109 0.0131  0.0307  122 LEU   A N   
1922 C CA  . LEU   A 122 ? 0.1417 0.1317 0.1223 -0.0149 0.0281  0.0191  122 LEU   A CA  
1923 C C   . LEU   A 122 ? 0.1391 0.1319 0.1139 -0.0168 0.0127  0.0163  122 LEU   A C   
1924 O O   . LEU   A 122 ? 0.1383 0.1397 0.1552 -0.0234 0.0109  0.0235  122 LEU   A O   
1925 C CB  . LEU   A 122 ? 0.1562 0.1403 0.1603 -0.0041 0.0169  0.0337  122 LEU   A CB  
1926 C CG  . LEU   A 122 ? 0.1577 0.1474 0.1421 -0.0036 0.0178  0.0224  122 LEU   A CG  
1927 C CD1 . LEU   A 122 ? 0.1769 0.1496 0.1508 -0.0088 0.0215  0.0256  122 LEU   A CD1 
1928 C CD2 . LEU   A 122 ? 0.1493 0.1385 0.1425 -0.0072 0.0274  0.0196  122 LEU   A CD2 
1940 N N   . LEU   A 123 ? 0.1347 0.1289 0.1123 -0.0163 0.0070  0.0168  123 LEU   A N   
1941 C CA  . LEU   A 123 ? 0.1319 0.1330 0.1085 -0.0168 0.0159  0.0192  123 LEU   A CA  
1942 C C   . LEU   A 123 ? 0.1253 0.1261 0.1007 -0.0108 0.0118  0.0199  123 LEU   A C   
1943 O O   . LEU   A 123 ? 0.1243 0.1446 0.1138 -0.0211 0.0055  0.0244  123 LEU   A O   
1944 C CB  . LEU   A 123 ? 0.1387 0.1439 0.1061 -0.0180 0.0210  0.0181  123 LEU   A CB  
1945 C CG  . LEU   A 123 ? 0.1431 0.1533 0.1269 -0.0157 0.0268  0.0106  123 LEU   A CG  
1946 C CD1 . LEU   A 123 ? 0.1459 0.1570 0.1495 -0.0034 0.0153  0.0013  123 LEU   A CD1 
1947 C CD2 . LEU   A 123 ? 0.1559 0.1573 0.1406 -0.0118 0.0188  -0.0039 123 LEU   A CD2 
1959 N N   . ALA   A 124 ? 0.1245 0.1239 0.1019 -0.0142 0.0078  0.0171  124 ALA   A N   
1960 C CA  . ALA   A 124 ? 0.1206 0.1269 0.1113 -0.0125 0.0044  0.0201  124 ALA   A CA  
1961 C C   . ALA   A 124 ? 0.1156 0.1239 0.1112 -0.0105 0.0073  0.0197  124 ALA   A C   
1962 O O   . ALA   A 124 ? 0.1169 0.1306 0.1325 -0.0110 0.0165  0.0306  124 ALA   A O   
1963 C CB  . ALA   A 124 ? 0.1210 0.1253 0.1259 -0.0117 0.0025  0.0153  124 ALA   A CB  
1969 N N   . PRO   A 125 ? 0.1153 0.1229 0.1131 -0.0098 0.0064  0.0326  125 PRO   A N   
1970 C CA  . PRO   A 125 ? 0.1276 0.1282 0.1211 -0.0049 0.0090  0.0242  125 PRO   A CA  
1971 C C   . PRO   A 125 ? 0.1177 0.1332 0.1210 -0.0119 0.0106  0.0287  125 PRO   A C   
1972 O O   . PRO   A 125 ? 0.1257 0.1304 0.1395 0.0004  -0.0027 0.0207  125 PRO   A O   
1973 C CB  . PRO   A 125 ? 0.1405 0.1257 0.1176 -0.0054 0.0082  0.0271  125 PRO   A CB  
1974 C CG  . PRO   A 125 ? 0.1388 0.1232 0.1330 -0.0144 0.0079  0.0257  125 PRO   A CG  
1975 C CD  . PRO   A 125 ? 0.1268 0.1278 0.1242 -0.0168 0.0072  0.0247  125 PRO   A CD  
1983 N N   . LEU   A 126 ? 0.1152 0.1483 0.1204 -0.0054 0.0021  0.0202  126 LEU   A N   
1984 C CA  . LEU   A 126 ? 0.1201 0.1457 0.1287 -0.0067 -0.0018 0.0251  126 LEU   A CA  
1985 C C   . LEU   A 126 ? 0.1243 0.1329 0.1288 0.0028  0.0001  0.0201  126 LEU   A C   
1986 O O   . LEU   A 126 ? 0.1382 0.1284 0.1483 0.0052  0.0160  0.0196  126 LEU   A O   
1987 C CB  . LEU   A 126 ? 0.1259 0.1636 0.1460 -0.0140 -0.0058 0.0230  126 LEU   A CB  
1988 C CG  . LEU   A 126 ? 0.1270 0.1872 0.1809 -0.0165 0.0093  0.0248  126 LEU   A CG  
1989 C CD1 . LEU   A 126 ? 0.1335 0.2024 0.2161 -0.0218 0.0052  0.0239  126 LEU   A CD1 
1990 C CD2 . LEU   A 126 ? 0.1393 0.1794 0.1847 -0.0261 0.0036  0.0348  126 LEU   A CD2 
2002 N N   . LEU   A 127 ? 0.1247 0.1338 0.1291 0.0051  0.0023  0.0232  127 LEU   A N   
2003 C CA  . LEU   A 127 ? 0.1195 0.1397 0.1232 0.0017  -0.0043 0.0199  127 LEU   A CA  
2004 C C   . LEU   A 127 ? 0.1227 0.1312 0.1157 -0.0003 -0.0014 0.0123  127 LEU   A C   
2005 O O   . LEU   A 127 ? 0.1311 0.1330 0.1260 -0.0106 -0.0054 0.0219  127 LEU   A O   
2006 C CB  . LEU   A 127 ? 0.1260 0.1535 0.1272 0.0057  0.0018  0.0214  127 LEU   A CB  
2007 C CG  . LEU   A 127 ? 0.1315 0.1657 0.1311 0.0139  -0.0057 0.0258  127 LEU   A CG  
2008 C CD1 . LEU   A 127 ? 0.1361 0.1664 0.1502 0.0101  -0.0065 0.0298  127 LEU   A CD1 
2009 C CD2 . LEU   A 127 ? 0.1502 0.1717 0.1447 0.0151  -0.0102 0.0167  127 LEU   A CD2 
2021 N N   . SER   A 128 ? 0.1259 0.1289 0.1083 -0.0068 -0.0056 0.0155  128 SER   A N   
2022 C CA  . SER   A 128 ? 0.1353 0.1292 0.1069 -0.0090 -0.0066 0.0192  128 SER   A CA  
2023 C C   . SER   A 128 ? 0.1466 0.1261 0.1121 0.0004  -0.0146 0.0220  128 SER   A C   
2024 O O   . SER   A 128 ? 0.1587 0.1434 0.1356 0.0000  -0.0240 0.0117  128 SER   A O   
2025 C CB  . SER   A 128 ? 0.1349 0.1408 0.1099 -0.0108 -0.0062 0.0200  128 SER   A CB  
2026 O OG  . SER   A 128 ? 0.1356 0.1500 0.1239 -0.0087 0.0009  0.0179  128 SER   A OG  
2032 N N   . ALA   A 129 ? 0.1337 0.1334 0.1390 0.0011  -0.0110 0.0273  129 ALA   A N   
2033 C CA  . ALA   A 129 ? 0.1323 0.1381 0.1561 -0.0014 -0.0086 0.0274  129 ALA   A CA  
2034 C C   . ALA   A 129 ? 0.1363 0.1363 0.1430 -0.0033 -0.0206 0.0142  129 ALA   A C   
2035 O O   . ALA   A 129 ? 0.1367 0.1391 0.1340 -0.0088 -0.0088 0.0250  129 ALA   A O   
2036 C CB  . ALA   A 129 ? 0.1389 0.1595 0.1881 0.0078  0.0021  0.0389  129 ALA   A CB  
2042 N N   . GLY   A 130 ? 0.1430 0.1361 0.1805 0.0016  -0.0028 0.0086  130 GLY   A N   
2043 C CA  . GLY   A 130 ? 0.1577 0.1385 0.1787 0.0033  0.0012  0.0040  130 GLY   A CA  
2044 C C   . GLY   A 130 ? 0.1605 0.1341 0.1611 0.0052  -0.0099 0.0050  130 GLY   A C   
2045 O O   . GLY   A 130 ? 0.1657 0.1351 0.1661 0.0025  -0.0255 0.0064  130 GLY   A O   
2049 N N   . ILE   A 131 ? 0.1694 0.1314 0.1478 -0.0010 -0.0130 0.0124  131 ILE   A N   
2050 C CA  . ILE   A 131 ? 0.1811 0.1295 0.1339 -0.0067 -0.0312 0.0086  131 ILE   A CA  
2051 C C   . ILE   A 131 ? 0.1706 0.1365 0.1180 -0.0110 -0.0263 0.0172  131 ILE   A C   
2052 O O   . ILE   A 131 ? 0.1778 0.1411 0.1429 -0.0036 -0.0212 0.0237  131 ILE   A O   
2053 C CB  . ILE   A 131 ? 0.2060 0.1420 0.1417 -0.0176 -0.0333 0.0004  131 ILE   A CB  
2054 C CG1 . ILE   A 131 ? 0.2191 0.1711 0.1350 -0.0275 -0.0330 0.0057  131 ILE   A CG1 
2055 C CG2 . ILE   A 131 ? 0.2198 0.1286 0.1647 -0.0084 -0.0235 -0.0140 131 ILE   A CG2 
2056 C CD1 . ILE   A 131 ? 0.2284 0.1866 0.1700 -0.0319 -0.0360 -0.0072 131 ILE   A CD1 
2068 N N   . PHE   A 132 ? 0.1601 0.1353 0.1137 -0.0008 -0.0145 0.0174  132 PHE   A N   
2069 C CA  . PHE   A 132 ? 0.1661 0.1453 0.1127 -0.0025 -0.0068 0.0114  132 PHE   A CA  
2070 C C   . PHE   A 132 ? 0.1751 0.1640 0.1107 0.0004  -0.0124 0.0114  132 PHE   A C   
2071 O O   . PHE   A 132 ? 0.1873 0.1820 0.1247 -0.0045 -0.0126 0.0096  132 PHE   A O   
2072 C CB  . PHE   A 132 ? 0.1620 0.1350 0.1166 0.0023  -0.0073 0.0168  132 PHE   A CB  
2073 C CG  . PHE   A 132 ? 0.1594 0.1336 0.1065 0.0057  -0.0145 0.0130  132 PHE   A CG  
2074 C CD1 . PHE   A 132 ? 0.1607 0.1491 0.1356 0.0086  -0.0111 -0.0019 132 PHE   A CD1 
2075 C CD2 . PHE   A 132 ? 0.1685 0.1465 0.1216 0.0096  -0.0144 0.0007  132 PHE   A CD2 
2076 C CE1 . PHE   A 132 ? 0.1620 0.1561 0.1380 0.0080  -0.0188 -0.0158 132 PHE   A CE1 
2077 C CE2 . PHE   A 132 ? 0.1619 0.1602 0.1330 0.0143  -0.0149 -0.0003 132 PHE   A CE2 
2078 C CZ  . PHE   A 132 ? 0.1560 0.1584 0.1413 0.0050  -0.0217 0.0022  132 PHE   A CZ  
2088 N N   . GLY   A 133 ? 0.1792 0.1615 0.1266 0.0008  -0.0325 0.0155  133 GLY   A N   
2089 C CA  . GLY   A 133 ? 0.1849 0.1678 0.1388 -0.0022 -0.0368 0.0029  133 GLY   A CA  
2090 C C   . GLY   A 133 ? 0.1857 0.1751 0.1336 -0.0059 -0.0398 -0.0015 133 GLY   A C   
2091 O O   . GLY   A 133 ? 0.2143 0.1923 0.1503 -0.0050 -0.0535 -0.0144 133 GLY   A O   
2095 N N   . ALA   A 134 ? 0.1718 0.1641 0.1299 -0.0140 -0.0286 -0.0040 134 ALA   A N   
2096 C CA  . ALA   A 134 ? 0.1653 0.1676 0.1535 -0.0111 -0.0239 -0.0046 134 ALA   A CA  
2097 C C   . ALA   A 134 ? 0.1689 0.1828 0.1502 -0.0078 -0.0202 0.0112  134 ALA   A C   
2098 O O   . ALA   A 134 ? 0.1834 0.1875 0.1813 -0.0050 0.0131  0.0140  134 ALA   A O   
2099 C CB  . ALA   A 134 ? 0.1708 0.1619 0.1892 -0.0099 -0.0262 -0.0092 134 ALA   A CB  
2105 N N   . ASP   A 135 ? 0.1762 0.1936 0.1692 -0.0207 -0.0289 0.0285  135 ASP   A N   
2106 C CA  . ASP   A 135 ? 0.1777 0.2116 0.2053 -0.0299 -0.0459 0.0467  135 ASP   A CA  
2107 C C   . ASP   A 135 ? 0.1651 0.1993 0.1961 -0.0221 -0.0291 0.0606  135 ASP   A C   
2108 O O   . ASP   A 135 ? 0.1599 0.1844 0.1967 -0.0264 -0.0321 0.0545  135 ASP   A O   
2109 C CB  . ASP   A 135 ? 0.2048 0.2480 0.2542 -0.0515 -0.0722 0.0379  135 ASP   A CB  
2110 C CG  . ASP   A 135 ? 0.2232 0.2848 0.3156 -0.0694 -0.0817 0.0270  135 ASP   A CG  
2111 O OD1 . ASP   A 135 ? 0.2151 0.3015 0.3244 -0.0715 -0.0864 0.0475  135 ASP   A OD1 
2112 O OD2 . ASP   A 135 ? 0.2604 0.3054 0.3767 -0.0720 -0.0504 0.0187  135 ASP   A OD2 
2117 N N   . PRO   A 136 ? 0.1549 0.2058 0.2089 -0.0043 -0.0147 0.0755  136 PRO   A N   
2118 C CA  . PRO   A 136 ? 0.1468 0.2049 0.2173 -0.0019 -0.0026 0.0632  136 PRO   A CA  
2119 C C   . PRO   A 136 ? 0.1223 0.1975 0.2060 0.0012  -0.0004 0.0536  136 PRO   A C   
2120 O O   . PRO   A 136 ? 0.1212 0.1936 0.1968 0.0012  0.0012  0.0474  136 PRO   A O   
2121 C CB  . PRO   A 136 ? 0.1713 0.2063 0.2419 0.0070  -0.0006 0.0701  136 PRO   A CB  
2122 C CG  . PRO   A 136 ? 0.1890 0.2201 0.2635 0.0121  -0.0024 0.0683  136 PRO   A CG  
2123 C CD  . PRO   A 136 ? 0.1719 0.2131 0.2368 0.0098  -0.0004 0.0834  136 PRO   A CD  
2131 N N   . ILE   A 137 ? 0.1234 0.1995 0.2140 0.0010  -0.0148 0.0490  137 ILE   A N   
2132 C CA  . ILE   A 137 ? 0.1284 0.2087 0.2248 -0.0119 -0.0201 0.0449  137 ILE   A CA  
2133 C C   . ILE   A 137 ? 0.1287 0.1979 0.2033 -0.0191 -0.0216 0.0448  137 ILE   A C   
2134 O O   . ILE   A 137 ? 0.1355 0.1958 0.2029 -0.0226 -0.0106 0.0408  137 ILE   A O   
2135 C CB  . ILE   A 137 ? 0.1367 0.2342 0.2538 -0.0155 -0.0369 0.0375  137 ILE   A CB  
2136 C CG1 . ILE   A 137 ? 0.1522 0.2632 0.2943 -0.0057 -0.0390 0.0369  137 ILE   A CG1 
2137 C CG2 . ILE   A 137 ? 0.1498 0.2344 0.2653 -0.0191 -0.0469 0.0316  137 ILE   A CG2 
2138 C CD1 . ILE   A 137 ? 0.1735 0.2844 0.3227 -0.0009 -0.0379 0.0409  137 ILE   A CD1 
2150 N N   . HIS   A 138 ? 0.1318 0.2063 0.1894 -0.0185 -0.0137 0.0405  138 HIS   A N   
2151 C CA  . HIS   A 138 ? 0.1420 0.2054 0.1720 -0.0195 -0.0174 0.0303  138 HIS   A CA  
2152 C C   . HIS   A 138 ? 0.1309 0.1907 0.1626 -0.0120 -0.0150 0.0374  138 HIS   A C   
2153 O O   . HIS   A 138 ? 0.1428 0.1879 0.1644 -0.0159 -0.0052 0.0269  138 HIS   A O   
2154 C CB  . HIS   A 138 ? 0.1600 0.2191 0.1639 -0.0177 -0.0198 0.0205  138 HIS   A CB  
2155 C CG  . HIS   A 138 ? 0.1759 0.2312 0.1701 -0.0242 -0.0184 0.0084  138 HIS   A CG  
2156 N ND1 . HIS   A 138 ? 0.1878 0.2441 0.1982 -0.0252 -0.0196 -0.0098 138 HIS   A ND1 
2157 C CD2 . HIS   A 138 ? 0.1790 0.2404 0.1723 -0.0183 -0.0130 0.0084  138 HIS   A CD2 
2158 C CE1 . HIS   A 138 ? 0.1935 0.2510 0.1960 -0.0165 -0.0217 -0.0091 138 HIS   A CE1 
2159 N NE2 . HIS   A 138 ? 0.1888 0.2509 0.1753 -0.0155 -0.0115 -0.0021 138 HIS   A NE2 
2167 N N   . SER   A 139 ? 0.1243 0.1753 0.1675 -0.0101 -0.0077 0.0469  139 SER   A N   
2168 C CA  . SER   A 139 ? 0.1204 0.1685 0.1639 -0.0116 -0.0071 0.0484  139 SER   A CA  
2169 C C   . SER   A 139 ? 0.1172 0.1577 0.1625 -0.0089 -0.0025 0.0353  139 SER   A C   
2170 O O   . SER   A 139 ? 0.1136 0.1514 0.1678 -0.0099 0.0033  0.0364  139 SER   A O   
2171 C CB  . SER   A 139 ? 0.1219 0.1661 0.1757 -0.0143 -0.0084 0.0517  139 SER   A CB  
2172 O OG  . SER   A 139 ? 0.1226 0.1637 0.1806 -0.0167 -0.0124 0.0563  139 SER   A OG  
2178 N N   . LEU   A 140 ? 0.1154 0.1601 0.1640 -0.0057 0.0002  0.0449  140 LEU   A N   
2179 C CA  . LEU   A 140 ? 0.1143 0.1549 0.1528 -0.0081 -0.0009 0.0430  140 LEU   A CA  
2180 C C   . LEU   A 140 ? 0.1109 0.1609 0.1519 -0.0116 0.0020  0.0356  140 LEU   A C   
2181 O O   . LEU   A 140 ? 0.1169 0.1569 0.1685 -0.0040 -0.0008 0.0325  140 LEU   A O   
2182 C CB  . LEU   A 140 ? 0.1146 0.1597 0.1580 -0.0086 0.0008  0.0414  140 LEU   A CB  
2183 C CG  . LEU   A 140 ? 0.1175 0.1716 0.1683 -0.0166 0.0074  0.0413  140 LEU   A CG  
2184 C CD1 . LEU   A 140 ? 0.1223 0.1760 0.1601 -0.0083 0.0074  0.0385  140 LEU   A CD1 
2185 C CD2 . LEU   A 140 ? 0.1217 0.1890 0.1838 -0.0161 0.0180  0.0480  140 LEU   A CD2 
2197 N N   . ARG   A 141 ? 0.1153 0.1649 0.1562 -0.0109 -0.0003 0.0312  141 ARG   A N   
2198 C CA  . ARG   A 141 ? 0.1317 0.1778 0.1751 -0.0206 -0.0110 0.0130  141 ARG   A CA  
2199 C C   . ARG   A 141 ? 0.1314 0.1575 0.1616 -0.0160 -0.0093 0.0130  141 ARG   A C   
2200 O O   . ARG   A 141 ? 0.1287 0.1523 0.1776 -0.0222 0.0071  0.0121  141 ARG   A O   
2201 C CB  . ARG   A 141 ? 0.1464 0.2064 0.2191 -0.0260 -0.0218 -0.0081 141 ARG   A CB  
2202 C CG  . ARG   A 141 ? 0.1834 0.2419 0.2663 -0.0226 -0.0182 -0.0153 141 ARG   A CG  
2203 C CD  . ARG   A 141 ? 0.2092 0.2643 0.2993 -0.0314 -0.0130 -0.0179 141 ARG   A CD  
2204 N NE  . ARG   A 141 ? 0.2002 0.2795 0.3129 -0.0383 -0.0237 -0.0194 141 ARG   A NE  
2205 C CZ  . ARG   A 141 ? 0.1949 0.2931 0.3250 -0.0484 -0.0112 -0.0147 141 ARG   A CZ  
2206 N NH1 . ARG   A 141 ? 0.1889 0.3016 0.3251 -0.0524 0.0031  -0.0320 141 ARG   A NH1 
2207 N NH2 . ARG   A 141 ? 0.1957 0.2967 0.3391 -0.0434 -0.0195 -0.0023 141 ARG   A NH2 
2221 N N   . VAL   A 142 ? 0.1236 0.1552 0.1577 -0.0122 -0.0052 0.0094  142 VAL   A N   
2222 C CA  . VAL   A 142 ? 0.1268 0.1520 0.1582 -0.0115 0.0066  0.0106  142 VAL   A CA  
2223 C C   . VAL   A 142 ? 0.1159 0.1446 0.1459 -0.0150 0.0039  0.0127  142 VAL   A C   
2224 O O   . VAL   A 142 ? 0.1215 0.1475 0.1570 -0.0026 0.0026  0.0131  142 VAL   A O   
2225 C CB  . VAL   A 142 ? 0.1358 0.1581 0.1480 -0.0133 0.0078  0.0183  142 VAL   A CB  
2226 C CG1 . VAL   A 142 ? 0.1336 0.1544 0.1518 -0.0137 0.0108  0.0092  142 VAL   A CG1 
2227 C CG2 . VAL   A 142 ? 0.1502 0.1791 0.1688 -0.0050 0.0006  0.0193  142 VAL   A CG2 
2237 N N   . CYS   A 143 ? 0.1159 0.1446 0.1427 -0.0128 -0.0004 0.0085  143 CYS   A N   
2238 C CA  . CYS   A 143 ? 0.1176 0.1355 0.1467 -0.0106 0.0059  0.0141  143 CYS   A CA  
2239 C C   . CYS   A 143 ? 0.1167 0.1331 0.1479 -0.0083 0.0058  0.0170  143 CYS   A C   
2240 O O   . CYS   A 143 ? 0.1150 0.1317 0.1545 -0.0052 0.0015  0.0171  143 CYS   A O   
2241 C CB  . CYS   A 143 ? 0.1284 0.1400 0.1541 -0.0062 0.0128  0.0219  143 CYS   A CB  
2242 S SG  . CYS   A 143 ? 0.1409 0.1449 0.1483 0.0029  0.0116  0.0165  143 CYS   A SG  
2248 N N   . VAL   A 144 ? 0.1126 0.1412 0.1608 -0.0072 0.0093  0.0253  144 VAL   A N   
2249 C CA  . VAL   A 144 ? 0.1208 0.1473 0.1910 -0.0113 0.0186  0.0247  144 VAL   A CA  
2250 C C   . VAL   A 144 ? 0.1227 0.1369 0.1955 -0.0157 -0.0027 0.0153  144 VAL   A C   
2251 O O   . VAL   A 144 ? 0.1364 0.1391 0.1981 -0.0024 -0.0062 0.0210  144 VAL   A O   
2252 C CB  . VAL   A 144 ? 0.1444 0.1682 0.2576 -0.0010 0.0319  0.0299  144 VAL   A CB  
2253 C CG1 . VAL   A 144 ? 0.1549 0.1866 0.2994 -0.0079 0.0155  0.0232  144 VAL   A CG1 
2254 C CG2 . VAL   A 144 ? 0.1354 0.1724 0.2671 -0.0025 0.0442  0.0441  144 VAL   A CG2 
2264 N N   . ASP   A 145 ? 0.1260 0.1385 0.1982 -0.0166 0.0032  0.0063  145 ASP   A N   
2265 C CA  . ASP   A 145 ? 0.1432 0.1416 0.2006 -0.0213 -0.0028 -0.0004 145 ASP   A CA  
2266 C C   . ASP   A 145 ? 0.1424 0.1361 0.1922 -0.0165 0.0047  -0.0123 145 ASP   A C   
2267 O O   . ASP   A 145 ? 0.1568 0.1485 0.2496 -0.0175 0.0036  -0.0422 145 ASP   A O   
2268 C CB  . ASP   A 145 ? 0.1552 0.1680 0.2201 -0.0267 -0.0159 0.0005  145 ASP   A CB  
2269 C CG  . ASP   A 145 ? 0.1753 0.2013 0.2485 -0.0434 -0.0273 0.0057  145 ASP   A CG  
2270 O OD1 . ASP   A 145 ? 0.1704 0.2120 0.2628 -0.0517 -0.0194 0.0056  145 ASP   A OD1 
2271 O OD2 . ASP   A 145 ? 0.2003 0.2245 0.2535 -0.0488 -0.0439 0.0071  145 ASP   A OD2 
2276 N N   . THR   A 146 ? 0.1256 0.1271 0.1598 -0.0109 0.0055  0.0034  146 THR   A N   
2277 C CA  . THR   A 146 ? 0.1229 0.1275 0.1483 -0.0028 0.0041  0.0054  146 THR   A CA  
2278 C C   . THR   A 146 ? 0.1164 0.1230 0.1475 0.0009  0.0085  0.0101  146 THR   A C   
2279 O O   . THR   A 146 ? 0.1310 0.1381 0.1588 0.0053  0.0003  0.0052  146 THR   A O   
2280 C CB  . THR   A 146 ? 0.1200 0.1335 0.1450 -0.0020 0.0034  0.0113  146 THR   A CB  
2281 O OG1 . THR   A 146 ? 0.1196 0.1504 0.1548 -0.0009 0.0022  0.0059  146 THR   A OG1 
2282 C CG2 . THR   A 146 ? 0.1214 0.1383 0.1661 -0.0095 0.0065  0.0102  146 THR   A CG2 
2290 N N   . VAL   A 147 ? 0.1134 0.1264 0.1466 0.0025  0.0099  0.0106  147 VAL   A N   
2291 C CA  . VAL   A 147 ? 0.1164 0.1280 0.1424 -0.0036 0.0203  0.0161  147 VAL   A CA  
2292 C C   . VAL   A 147 ? 0.1190 0.1230 0.1630 -0.0052 0.0163  0.0163  147 VAL   A C   
2293 O O   . VAL   A 147 ? 0.1207 0.1304 0.1688 -0.0138 0.0089  0.0138  147 VAL   A O   
2294 C CB  . VAL   A 147 ? 0.1302 0.1289 0.1420 -0.0115 0.0175  0.0202  147 VAL   A CB  
2295 C CG1 . VAL   A 147 ? 0.1632 0.1350 0.1415 -0.0065 0.0109  0.0266  147 VAL   A CG1 
2296 C CG2 . VAL   A 147 ? 0.1342 0.1322 0.1432 -0.0108 0.0118  0.0182  147 VAL   A CG2 
2306 N N   . ARG   A 148 ? 0.1195 0.1270 0.1626 -0.0082 0.0156  0.0255  148 ARG   A N   
2307 C CA  . ARG   A 148 ? 0.1238 0.1265 0.1667 -0.0085 0.0086  0.0331  148 ARG   A CA  
2308 C C   . ARG   A 148 ? 0.1391 0.1314 0.1563 -0.0117 0.0165  0.0422  148 ARG   A C   
2309 O O   . ARG   A 148 ? 0.1684 0.1396 0.1755 -0.0157 0.0203  0.0359  148 ARG   A O   
2310 C CB  . ARG   A 148 ? 0.1332 0.1261 0.1849 -0.0048 0.0212  0.0277  148 ARG   A CB  
2311 C CG  . ARG   A 148 ? 0.1524 0.1294 0.2106 -0.0042 0.0325  0.0148  148 ARG   A CG  
2312 C CD  . ARG   A 148 ? 0.1657 0.1308 0.2343 0.0004  0.0381  0.0264  148 ARG   A CD  
2313 N NE  . ARG   A 148 ? 0.1556 0.1341 0.2238 0.0067  0.0465  0.0321  148 ARG   A NE  
2314 C CZ  . ARG   A 148 ? 0.1535 0.1265 0.2132 0.0057  0.0453  0.0306  148 ARG   A CZ  
2315 N NH1 . ARG   A 148 ? 0.1608 0.1351 0.2144 -0.0019 0.0424  0.0075  148 ARG   A NH1 
2316 N NH2 . ARG   A 148 ? 0.1482 0.1458 0.2162 0.0156  0.0464  0.0333  148 ARG   A NH2 
2330 N N   . THR   A 149 ? 0.1356 0.1356 0.1397 -0.0116 0.0065  0.0343  149 THR   A N   
2331 C CA  . THR   A 149 ? 0.1361 0.1440 0.1416 -0.0129 0.0079  0.0354  149 THR   A CA  
2332 C C   . THR   A 149 ? 0.1333 0.1390 0.1347 -0.0190 0.0053  0.0376  149 THR   A C   
2333 O O   . THR   A 149 ? 0.1331 0.1473 0.1580 -0.0182 0.0073  0.0330  149 THR   A O   
2334 C CB  . THR   A 149 ? 0.1328 0.1503 0.1592 -0.0132 0.0101  0.0279  149 THR   A CB  
2335 O OG1 . THR   A 149 ? 0.1393 0.1407 0.1682 -0.0177 0.0063  0.0240  149 THR   A OG1 
2336 C CG2 . THR   A 149 ? 0.1321 0.1644 0.1755 -0.0065 0.0064  0.0315  149 THR   A CG2 
2344 N N   . ASN   A 150 ? 0.1335 0.1369 0.1467 -0.0070 0.0064  0.0362  150 ASN   A N   
2345 C CA  . ASN   A 150 ? 0.1494 0.1447 0.1527 -0.0070 0.0156  0.0345  150 ASN   A CA  
2346 C C   . ASN   A 150 ? 0.1304 0.1395 0.1500 -0.0137 0.0103  0.0297  150 ASN   A C   
2347 O O   . ASN   A 150 ? 0.1404 0.1482 0.1996 -0.0119 -0.0087 0.0242  150 ASN   A O   
2348 C CB  . ASN   A 150 ? 0.1924 0.1706 0.1809 -0.0123 0.0402  0.0514  150 ASN   A CB  
2349 C CG  . ASN   A 150 ? 0.2489 0.2078 0.2607 -0.0127 0.0131  0.0585  150 ASN   A CG  
2350 O OD1 . ASN   A 150 ? 0.2722 0.2198 0.2915 -0.0198 0.0088  0.0731  150 ASN   A OD1 
2351 N ND2 . ASN   A 150 ? 0.2770 0.2311 0.2977 -0.0064 0.0009  0.0616  150 ASN   A ND2 
2358 N N   . VAL   A 151 ? 0.1300 0.1262 0.1486 -0.0092 0.0053  0.0291  151 VAL   A N   
2359 C CA  . VAL   A 151 ? 0.1359 0.1285 0.1499 -0.0171 0.0102  0.0265  151 VAL   A CA  
2360 C C   . VAL   A 151 ? 0.1272 0.1233 0.1537 -0.0175 0.0145  0.0314  151 VAL   A C   
2361 O O   . VAL   A 151 ? 0.1345 0.1320 0.1829 -0.0135 0.0138  0.0272  151 VAL   A O   
2362 C CB  . VAL   A 151 ? 0.1642 0.1484 0.1479 0.0008  0.0134  0.0288  151 VAL   A CB  
2363 C CG1 . VAL   A 151 ? 0.1615 0.1730 0.1734 -0.0018 0.0094  0.0226  151 VAL   A CG1 
2364 C CG2 . VAL   A 151 ? 0.1769 0.1496 0.1551 0.0056  0.0249  0.0267  151 VAL   A CG2 
2374 N N   . TYR   A 152 ? 0.1258 0.1261 0.1467 -0.0126 0.0123  0.0300  152 TYR   A N   
2375 C CA  . TYR   A 152 ? 0.1266 0.1274 0.1374 -0.0117 0.0166  0.0245  152 TYR   A CA  
2376 C C   . TYR   A 152 ? 0.1221 0.1270 0.1394 -0.0152 0.0238  0.0252  152 TYR   A C   
2377 O O   . TYR   A 152 ? 0.1333 0.1309 0.1427 -0.0226 0.0197  0.0201  152 TYR   A O   
2378 C CB  . TYR   A 152 ? 0.1419 0.1331 0.1341 -0.0050 0.0284  0.0240  152 TYR   A CB  
2379 C CG  . TYR   A 152 ? 0.1536 0.1463 0.1299 -0.0114 0.0307  0.0256  152 TYR   A CG  
2380 C CD1 . TYR   A 152 ? 0.1630 0.1671 0.1540 -0.0007 0.0308  0.0374  152 TYR   A CD1 
2381 C CD2 . TYR   A 152 ? 0.1570 0.1560 0.1279 -0.0253 0.0215  0.0231  152 TYR   A CD2 
2382 C CE1 . TYR   A 152 ? 0.1855 0.1794 0.1672 -0.0009 0.0126  0.0462  152 TYR   A CE1 
2383 C CE2 . TYR   A 152 ? 0.1769 0.1717 0.1406 -0.0298 0.0213  0.0301  152 TYR   A CE2 
2384 C CZ  . TYR   A 152 ? 0.1976 0.1729 0.1522 -0.0184 0.0113  0.0470  152 TYR   A CZ  
2385 O OH  . TYR   A 152 ? 0.2273 0.1971 0.1777 -0.0081 0.0164  0.0620  152 TYR   A OH  
2395 N N   . LEU   A 153 ? 0.1195 0.1248 0.1457 -0.0174 0.0193  0.0319  153 LEU   A N   
2396 C CA  . LEU   A 153 ? 0.1220 0.1256 0.1598 -0.0093 0.0222  0.0319  153 LEU   A CA  
2397 C C   . LEU   A 153 ? 0.1256 0.1318 0.1684 -0.0074 0.0298  0.0288  153 LEU   A C   
2398 O O   . LEU   A 153 ? 0.1295 0.1398 0.1964 -0.0041 0.0383  0.0291  153 LEU   A O   
2399 C CB  . LEU   A 153 ? 0.1167 0.1297 0.1698 -0.0061 0.0091  0.0374  153 LEU   A CB  
2400 C CG  . LEU   A 153 ? 0.1216 0.1403 0.1613 -0.0095 0.0137  0.0297  153 LEU   A CG  
2401 C CD1 . LEU   A 153 ? 0.1338 0.1458 0.1715 -0.0080 0.0051  0.0251  153 LEU   A CD1 
2402 C CD2 . LEU   A 153 ? 0.1340 0.1438 0.1692 -0.0093 0.0293  0.0095  153 LEU   A CD2 
2414 N N   . ALA   A 154 ? 0.1246 0.1279 0.1736 -0.0037 0.0289  0.0344  154 ALA   A N   
2415 C CA  . ALA   A 154 ? 0.1405 0.1351 0.1978 -0.0015 0.0294  0.0319  154 ALA   A CA  
2416 C C   . ALA   A 154 ? 0.1337 0.1337 0.2098 0.0008  0.0259  0.0459  154 ALA   A C   
2417 O O   . ALA   A 154 ? 0.1453 0.1570 0.2155 -0.0014 0.0269  0.0564  154 ALA   A O   
2418 C CB  . ALA   A 154 ? 0.1522 0.1366 0.2104 0.0085  0.0199  0.0157  154 ALA   A CB  
2424 N N   . VAL   A 155 ? 0.1414 0.1384 0.2213 0.0091  0.0237  0.0511  155 VAL   A N   
2425 C CA  . VAL   A 155 ? 0.1502 0.1527 0.2371 0.0102  0.0201  0.0684  155 VAL   A CA  
2426 C C   . VAL   A 155 ? 0.1679 0.1604 0.2853 0.0187  0.0159  0.0796  155 VAL   A C   
2427 O O   . VAL   A 155 ? 0.1691 0.1660 0.2880 0.0319  0.0285  0.0660  155 VAL   A O   
2428 C CB  . VAL   A 155 ? 0.1504 0.1628 0.2200 0.0092  0.0114  0.0615  155 VAL   A CB  
2429 C CG1 . VAL   A 155 ? 0.1657 0.1769 0.2366 0.0117  0.0005  0.0656  155 VAL   A CG1 
2430 C CG2 . VAL   A 155 ? 0.1636 0.1724 0.2243 0.0193  0.0012  0.0524  155 VAL   A CG2 
2440 N N   . PHE   A 156 ? 0.1895 0.1691 0.3273 0.0159  0.0135  0.1021  156 PHE   A N   
2441 C CA  . PHE   A 156 ? 0.2143 0.1742 0.3773 0.0248  0.0122  0.1007  156 PHE   A CA  
2442 C C   . PHE   A 156 ? 0.2102 0.1793 0.3815 0.0373  0.0230  0.1041  156 PHE   A C   
2443 O O   . PHE   A 156 ? 0.2194 0.1892 0.4020 0.0381  0.0264  0.0787  156 PHE   A O   
2444 C CB  . PHE   A 156 ? 0.2411 0.1819 0.3987 0.0180  0.0013  0.1178  156 PHE   A CB  
2445 C CG  . PHE   A 156 ? 0.2702 0.1901 0.4237 0.0277  -0.0052 0.1086  156 PHE   A CG  
2446 C CD1 . PHE   A 156 ? 0.2831 0.2033 0.4376 0.0316  0.0007  0.0946  156 PHE   A CD1 
2447 C CD2 . PHE   A 156 ? 0.2842 0.1964 0.4316 0.0354  -0.0059 0.1193  156 PHE   A CD2 
2448 C CE1 . PHE   A 156 ? 0.2981 0.2122 0.4534 0.0331  0.0045  0.0849  156 PHE   A CE1 
2449 C CE2 . PHE   A 156 ? 0.3001 0.2076 0.4481 0.0420  -0.0028 0.0983  156 PHE   A CE2 
2450 C CZ  . PHE   A 156 ? 0.3027 0.2142 0.4531 0.0424  -0.0004 0.0798  156 PHE   A CZ  
2460 N N   . ASP   A 157 ? 0.2088 0.1868 0.3609 0.0303  0.0269  0.1250  157 ASP   A N   
2461 C CA  . ASP   A 157 ? 0.2233 0.2078 0.3634 0.0332  0.0184  0.1252  157 ASP   A CA  
2462 C C   . ASP   A 157 ? 0.2042 0.2170 0.3582 0.0378  0.0356  0.1226  157 ASP   A C   
2463 O O   . ASP   A 157 ? 0.1877 0.2078 0.3465 0.0349  0.0422  0.1267  157 ASP   A O   
2464 C CB  . ASP   A 157 ? 0.2558 0.2235 0.3826 0.0343  0.0037  0.1241  157 ASP   A CB  
2465 C CG  . ASP   A 157 ? 0.2891 0.2385 0.4211 0.0432  -0.0163 0.1225  157 ASP   A CG  
2466 O OD1 . ASP   A 157 ? 0.3205 0.2500 0.4562 0.0432  -0.0394 0.1041  157 ASP   A OD1 
2467 O OD2 . ASP   A 157 ? 0.2803 0.2364 0.4385 0.0416  -0.0116 0.1363  157 ASP   A OD2 
2472 N N   . LYS   A 158 ? 0.2105 0.2385 0.3708 0.0429  0.0395  0.1132  158 LYS   A N   
2473 C CA  . LYS   A 158 ? 0.2133 0.2618 0.3768 0.0503  0.0515  0.1107  158 LYS   A CA  
2474 C C   . LYS   A 158 ? 0.1897 0.2695 0.3526 0.0538  0.0433  0.1300  158 LYS   A C   
2475 O O   . LYS   A 158 ? 0.1842 0.2674 0.3603 0.0483  0.0493  0.1348  158 LYS   A O   
2476 C CB  . LYS   A 158 ? 0.2358 0.2769 0.4043 0.0525  0.0776  0.1004  158 LYS   A CB  
2477 C CG  . LYS   A 158 ? 0.2539 0.2959 0.4355 0.0567  0.1007  0.0933  158 LYS   A CG  
2478 C CD  . LYS   A 158 ? 0.2697 0.3136 0.4589 0.0545  0.1252  0.0969  158 LYS   A CD  
2479 C CE  . LYS   A 158 ? 0.2779 0.3253 0.4765 0.0519  0.1422  0.1044  158 LYS   A CE  
2480 N NZ  . LYS   A 158 ? 0.2808 0.3322 0.4890 0.0477  0.1461  0.1121  158 LYS   A NZ  
2494 N N   A ASN   A 159 ? 0.1912 0.2846 0.3734 0.0610  0.0257  0.1318  159 ASN   A N   
2495 N N   B ASN   A 159 ? 0.1892 0.2754 0.3300 0.0473  0.0319  0.1146  159 ASN   A N   
2496 C CA  A ASN   A 159 ? 0.1917 0.2990 0.3800 0.0607  0.0122  0.1415  159 ASN   A CA  
2497 C CA  B ASN   A 159 ? 0.1881 0.2803 0.3154 0.0403  0.0207  0.1023  159 ASN   A CA  
2498 C C   A ASN   A 159 ? 0.1710 0.2960 0.3483 0.0437  0.0137  0.1358  159 ASN   A C   
2499 C C   B ASN   A 159 ? 0.1753 0.2816 0.3096 0.0370  0.0144  0.1128  159 ASN   A C   
2500 O O   A ASN   A 159 ? 0.1576 0.3070 0.3428 0.0395  0.0006  0.1263  159 ASN   A O   
2501 O O   B ASN   A 159 ? 0.1762 0.2851 0.3012 0.0371  0.0118  0.1067  159 ASN   A O   
2502 C CB  A ASN   A 159 ? 0.2202 0.3189 0.4310 0.0637  0.0133  0.1473  159 ASN   A CB  
2503 C CB  B ASN   A 159 ? 0.1994 0.2827 0.3171 0.0359  0.0169  0.0815  159 ASN   A CB  
2504 C CG  A ASN   A 159 ? 0.2486 0.3381 0.4869 0.0562  0.0194  0.1413  159 ASN   A CG  
2505 C CG  B ASN   A 159 ? 0.2082 0.2838 0.3229 0.0310  0.0134  0.0638  159 ASN   A CG  
2506 O OD1 A ASN   A 159 ? 0.2600 0.3492 0.5115 0.0515  0.0285  0.1361  159 ASN   A OD1 
2507 O OD1 B ASN   A 159 ? 0.2136 0.2856 0.3264 0.0288  0.0149  0.0569  159 ASN   A OD1 
2508 N ND2 A ASN   A 159 ? 0.2575 0.3444 0.5086 0.0526  0.0211  0.1366  159 ASN   A ND2 
2509 N ND2 B ASN   A 159 ? 0.2094 0.2834 0.3212 0.0288  0.0089  0.0590  159 ASN   A ND2 
2522 N N   . LEU   A 160 ? 0.1605 0.2781 0.3182 0.0336  0.0071  0.1316  160 LEU   A N   
2523 C CA  . LEU   A 160 ? 0.1571 0.2641 0.3055 0.0192  0.0128  0.1265  160 LEU   A CA  
2524 C C   . LEU   A 160 ? 0.1394 0.2551 0.2945 0.0096  0.0227  0.1180  160 LEU   A C   
2525 O O   . LEU   A 160 ? 0.1339 0.2652 0.3079 -0.0012 0.0211  0.1124  160 LEU   A O   
2526 C CB  . LEU   A 160 ? 0.1691 0.2642 0.2877 0.0088  0.0136  0.1284  160 LEU   A CB  
2527 C CG  . LEU   A 160 ? 0.1824 0.2699 0.2850 -0.0090 0.0255  0.1121  160 LEU   A CG  
2528 C CD1 . LEU   A 160 ? 0.1952 0.2803 0.2847 -0.0135 0.0302  0.0978  160 LEU   A CD1 
2529 C CD2 . LEU   A 160 ? 0.1882 0.2701 0.2900 -0.0134 0.0326  0.0987  160 LEU   A CD2 
2542 N N   . TYR   A 161 ? 0.1376 0.2357 0.2830 0.0143  0.0254  0.1117  161 TYR   A N   
2543 C CA  . TYR   A 161 ? 0.1402 0.2197 0.2782 0.0153  0.0221  0.1120  161 TYR   A CA  
2544 C C   . TYR   A 161 ? 0.1311 0.2307 0.2849 0.0145  0.0188  0.1068  161 TYR   A C   
2545 O O   . TYR   A 161 ? 0.1258 0.2339 0.2829 0.0060  0.0189  0.0999  161 TYR   A O   
2546 C CB  . TYR   A 161 ? 0.1554 0.2036 0.2877 0.0154  0.0250  0.0946  161 TYR   A CB  
2547 C CG  . TYR   A 161 ? 0.1495 0.1929 0.2761 0.0141  0.0252  0.0738  161 TYR   A CG  
2548 C CD1 . TYR   A 161 ? 0.1409 0.1855 0.2807 0.0046  0.0199  0.0657  161 TYR   A CD1 
2549 C CD2 . TYR   A 161 ? 0.1527 0.2020 0.2754 0.0167  0.0174  0.0577  161 TYR   A CD2 
2550 C CE1 . TYR   A 161 ? 0.1502 0.1821 0.2862 0.0026  0.0135  0.0648  161 TYR   A CE1 
2551 C CE2 . TYR   A 161 ? 0.1565 0.1945 0.2701 0.0078  0.0158  0.0673  161 TYR   A CE2 
2552 C CZ  . TYR   A 161 ? 0.1665 0.1829 0.2862 -0.0016 0.0101  0.0737  161 TYR   A CZ  
2553 O OH  . TYR   A 161 ? 0.1841 0.1934 0.3019 -0.0091 -0.0023 0.0820  161 TYR   A OH  
2563 N N   . ASP   A 162 ? 0.1333 0.2474 0.3034 0.0133  0.0254  0.1056  162 ASP   A N   
2564 C CA  . ASP   A 162 ? 0.1310 0.2719 0.3105 0.0095  0.0269  0.1092  162 ASP   A CA  
2565 C C   . ASP   A 162 ? 0.1254 0.2868 0.3075 -0.0007 0.0269  0.1154  162 ASP   A C   
2566 O O   . ASP   A 162 ? 0.1275 0.2868 0.3244 -0.0093 0.0331  0.1033  162 ASP   A O   
2567 C CB  . ASP   A 162 ? 0.1415 0.2835 0.3333 0.0115  0.0392  0.0963  162 ASP   A CB  
2568 C CG  . ASP   A 162 ? 0.1575 0.3025 0.3576 0.0218  0.0529  0.0778  162 ASP   A CG  
2569 O OD1 . ASP   A 162 ? 0.1768 0.3132 0.3700 0.0124  0.0485  0.0749  162 ASP   A OD1 
2570 O OD2 . ASP   A 162 ? 0.1775 0.3128 0.3852 0.0405  0.0526  0.0595  162 ASP   A OD2 
2575 N N   . LYS   A 163 ? 0.1391 0.3078 0.3158 -0.0021 0.0007  0.1141  163 LYS   A N   
2576 C CA  . LYS   A 163 ? 0.1552 0.3258 0.3087 -0.0062 -0.0056 0.1129  163 LYS   A CA  
2577 C C   . LYS   A 163 ? 0.1429 0.3138 0.2948 -0.0094 0.0124  0.1078  163 LYS   A C   
2578 O O   . LYS   A 163 ? 0.1395 0.3299 0.3118 -0.0151 0.0067  0.0933  163 LYS   A O   
2579 C CB  . LYS   A 163 ? 0.2046 0.3568 0.3474 0.0031  -0.0270 0.1093  163 LYS   A CB  
2580 C CG  . LYS   A 163 ? 0.2622 0.3822 0.4027 0.0054  -0.0263 0.1019  163 LYS   A CG  
2581 C CD  . LYS   A 163 ? 0.3257 0.4077 0.4644 0.0082  -0.0298 0.0901  163 LYS   A CD  
2582 C CE  . LYS   A 163 ? 0.3754 0.4297 0.5089 0.0091  -0.0292 0.0824  163 LYS   A CE  
2583 N NZ  . LYS   A 163 ? 0.3897 0.4318 0.5343 0.0093  -0.0281 0.0806  163 LYS   A NZ  
2597 N N   . LEU   A 164 ? 0.1274 0.2809 0.2702 -0.0196 0.0098  0.1014  164 LEU   A N   
2598 C CA  . LEU   A 164 ? 0.1319 0.2570 0.2530 -0.0242 0.0169  0.0883  164 LEU   A CA  
2599 C C   . LEU   A 164 ? 0.1402 0.2504 0.2414 -0.0203 0.0218  0.0787  164 LEU   A C   
2600 O O   . LEU   A 164 ? 0.1479 0.2563 0.2383 -0.0250 0.0419  0.0556  164 LEU   A O   
2601 C CB  . LEU   A 164 ? 0.1323 0.2440 0.2479 -0.0227 0.0179  0.0859  164 LEU   A CB  
2602 C CG  . LEU   A 164 ? 0.1424 0.2392 0.2443 -0.0213 0.0201  0.0736  164 LEU   A CG  
2603 C CD1 . LEU   A 164 ? 0.1334 0.2319 0.2508 -0.0125 0.0159  0.0611  164 LEU   A CD1 
2604 C CD2 . LEU   A 164 ? 0.1632 0.2444 0.2470 -0.0248 0.0285  0.0653  164 LEU   A CD2 
2616 N N   . VAL   A 165 ? 0.1336 0.2445 0.2413 -0.0215 0.0221  0.0760  165 VAL   A N   
2617 C CA  . VAL   A 165 ? 0.1487 0.2412 0.2345 -0.0199 0.0280  0.0843  165 VAL   A CA  
2618 C C   . VAL   A 165 ? 0.1383 0.2510 0.2345 -0.0115 0.0266  0.0861  165 VAL   A C   
2619 O O   . VAL   A 165 ? 0.1368 0.2489 0.2317 -0.0126 0.0273  0.0825  165 VAL   A O   
2620 C CB  . VAL   A 165 ? 0.1676 0.2346 0.2442 -0.0249 0.0307  0.0722  165 VAL   A CB  
2621 C CG1 . VAL   A 165 ? 0.1756 0.2362 0.2567 -0.0240 0.0354  0.0671  165 VAL   A CG1 
2622 C CG2 . VAL   A 165 ? 0.1821 0.2370 0.2513 -0.0245 0.0258  0.0735  165 VAL   A CG2 
2632 N N   . SER   A 166 ? 0.1259 0.2653 0.2624 -0.0152 0.0301  0.0852  166 SER   A N   
2633 C CA  . SER   A 166 ? 0.1263 0.2951 0.2785 -0.0196 0.0237  0.0742  166 SER   A CA  
2634 C C   . SER   A 166 ? 0.1341 0.3212 0.2750 -0.0240 0.0051  0.0653  166 SER   A C   
2635 O O   . SER   A 166 ? 0.1541 0.3362 0.3063 -0.0336 0.0075  0.0370  166 SER   A O   
2636 C CB  . SER   A 166 ? 0.1490 0.3103 0.3203 -0.0035 0.0094  0.0582  166 SER   A CB  
2637 O OG  . SER   A 166 ? 0.1966 0.3218 0.3557 -0.0018 0.0057  0.0584  166 SER   A OG  
2643 N N   . SER   A 167 ? 0.1421 0.3301 0.2367 -0.0130 -0.0088 0.0737  167 SER   A N   
2644 C CA  . SER   A 167 ? 0.1669 0.3408 0.2324 -0.0057 -0.0139 0.0624  167 SER   A CA  
2645 C C   . SER   A 167 ? 0.1719 0.3365 0.2188 0.0035  -0.0091 0.0511  167 SER   A C   
2646 O O   . SER   A 167 ? 0.1950 0.3417 0.2349 0.0069  -0.0185 0.0435  167 SER   A O   
2647 C CB  . SER   A 167 ? 0.1807 0.3540 0.2403 0.0010  -0.0077 0.0688  167 SER   A CB  
2648 O OG  . SER   A 167 ? 0.1823 0.3593 0.2403 -0.0011 0.0183  0.0779  167 SER   A OG  
2654 N N   . PHE   A 168 ? 0.1615 0.3292 0.1974 0.0127  0.0019  0.0437  168 PHE   A N   
2655 C CA  . PHE   A 168 ? 0.1678 0.3255 0.2122 0.0087  0.0197  0.0276  168 PHE   A CA  
2656 C C   . PHE   A 168 ? 0.1931 0.3579 0.2603 -0.0014 0.0659  -0.0036 168 PHE   A C   
2657 O O   . PHE   A 168 ? 0.1919 0.3600 0.2992 -0.0169 0.0764  0.0041  168 PHE   A O   
2658 C CB  . PHE   A 168 ? 0.1634 0.2950 0.1860 0.0009  0.0021  0.0313  168 PHE   A CB  
2659 C CG  . PHE   A 168 ? 0.1589 0.2720 0.1759 -0.0085 -0.0031 0.0374  168 PHE   A CG  
2660 C CD1 . PHE   A 168 ? 0.1613 0.2722 0.1980 -0.0136 -0.0106 0.0545  168 PHE   A CD1 
2661 C CD2 . PHE   A 168 ? 0.1557 0.2621 0.1752 -0.0096 0.0088  0.0250  168 PHE   A CD2 
2662 C CE1 . PHE   A 168 ? 0.1504 0.2715 0.1995 -0.0152 -0.0074 0.0536  168 PHE   A CE1 
2663 C CE2 . PHE   A 168 ? 0.1612 0.2596 0.1883 -0.0131 0.0100  0.0329  168 PHE   A CE2 
2664 C CZ  . PHE   A 168 ? 0.1571 0.2648 0.1959 -0.0144 0.0005  0.0460  168 PHE   A CZ  
2674 N N   . LEU   A 169 ? 0.2588 0.3905 0.3317 -0.0106 0.0581  -0.0308 169 LEU   A N   
2675 C CA  . LEU   A 169 ? 0.3484 0.4281 0.4485 -0.0165 0.0161  -0.0439 169 LEU   A CA  
2676 C C   . LEU   A 169 ? 0.3825 0.4376 0.4988 -0.0218 0.0019  -0.0420 169 LEU   A C   
2677 O O   . LEU   A 169 ? 0.3965 0.4417 0.5134 -0.0225 -0.0006 -0.0429 169 LEU   A O   
2678 C CB  . LEU   A 169 ? 0.3931 0.4515 0.4937 -0.0191 -0.0078 -0.0556 169 LEU   A CB  
2679 C CG  . LEU   A 169 ? 0.4275 0.4687 0.5292 -0.0238 -0.0250 -0.0687 169 LEU   A CG  
2680 C CD1 . LEU   A 169 ? 0.4367 0.4736 0.5425 -0.0250 -0.0303 -0.0720 169 LEU   A CD1 
2681 C CD2 . LEU   A 169 ? 0.4369 0.4753 0.5393 -0.0260 -0.0296 -0.0737 169 LEU   A CD2 
2682 O OXT . LEU   A 169 ? 0.3825 0.4384 0.5084 -0.0246 0.0010  -0.0428 169 LEU   A OXT 
2694 N N   A SER   B 1   ? 0.3338 0.3420 0.3449 -0.1288 -0.0812 0.0525  1   SER   B N   
2695 N N   B SER   B 1   ? 0.3401 0.3392 0.3322 -0.0260 -0.0167 0.0106  1   SER   B N   
2696 C CA  A SER   B 1   ? 0.3215 0.3445 0.3461 -0.1330 -0.0889 0.0480  1   SER   B CA  
2697 C CA  B SER   B 1   ? 0.3379 0.3387 0.3339 -0.0263 -0.0162 0.0103  1   SER   B CA  
2698 C C   A SER   B 1   ? 0.2955 0.3468 0.3310 -0.1308 -0.0992 0.0706  1   SER   B C   
2699 C C   B SER   B 1   ? 0.3320 0.3372 0.3355 -0.0263 -0.0181 0.0147  1   SER   B C   
2700 O O   A SER   B 1   ? 0.3067 0.3474 0.3067 -0.1203 -0.0965 0.0682  1   SER   B O   
2701 O O   B SER   B 1   ? 0.3338 0.3375 0.3303 -0.0255 -0.0190 0.0137  1   SER   B O   
2702 C CB  A SER   B 1   ? 0.3321 0.3438 0.3539 -0.1361 -0.0746 0.0252  1   SER   B CB  
2703 C CB  B SER   B 1   ? 0.3400 0.3387 0.3292 -0.0261 -0.0133 0.0060  1   SER   B CB  
2704 O OG  A SER   B 1   ? 0.3502 0.3540 0.4000 -0.1293 -0.0601 0.0169  1   SER   B OG  
2705 O OG  B SER   B 1   ? 0.3423 0.3397 0.3362 -0.0261 -0.0117 0.0040  1   SER   B OG  
2720 N N   A MET   B 2   ? 0.2724 0.3496 0.3385 -0.1249 -0.0950 0.1119  2   MET   B N   
2721 N N   B MET   B 2   ? 0.3237 0.3342 0.3393 -0.0269 -0.0185 0.0220  2   MET   B N   
2722 C CA  A MET   B 2   ? 0.2562 0.3523 0.3558 -0.1016 -0.0954 0.1322  2   MET   B CA  
2723 C CA  B MET   B 2   ? 0.3139 0.3297 0.3433 -0.0266 -0.0191 0.0284  2   MET   B CA  
2724 C C   A MET   B 2   ? 0.2226 0.3262 0.3292 -0.0835 -0.0925 0.1591  2   MET   B C   
2725 C C   B MET   B 2   ? 0.2921 0.3121 0.3129 -0.0297 -0.0213 0.0364  2   MET   B C   
2726 O O   A MET   B 2   ? 0.2129 0.3400 0.3385 -0.0662 -0.0986 0.1559  2   MET   B O   
2727 O O   B MET   B 2   ? 0.2943 0.3154 0.3140 -0.0281 -0.0189 0.0347  2   MET   B O   
2728 C CB  A MET   B 2   ? 0.2864 0.3878 0.4336 -0.0814 -0.0834 0.1087  2   MET   B CB  
2729 C CB  B MET   B 2   ? 0.3256 0.3423 0.3802 -0.0224 -0.0174 0.0264  2   MET   B CB  
2730 C CG  A MET   B 2   ? 0.3132 0.4191 0.5010 -0.0609 -0.0691 0.0963  2   MET   B CG  
2731 C CG  B MET   B 2   ? 0.3353 0.3532 0.4122 -0.0187 -0.0161 0.0262  2   MET   B CG  
2732 S SD  A MET   B 2   ? 0.3412 0.4488 0.5681 -0.0429 -0.0558 0.0858  2   MET   B SD  
2733 S SD  B MET   B 2   ? 0.3435 0.3628 0.4397 -0.0153 -0.0157 0.0270  2   MET   B SD  
2734 C CE  A MET   B 2   ? 0.3428 0.4519 0.5666 -0.0429 -0.0485 0.0862  2   MET   B CE  
2735 C CE  B MET   B 2   ? 0.3457 0.3655 0.4467 -0.0151 -0.0148 0.0259  2   MET   B CE  
2754 N N   A VAL   B 3   ? 0.2026 0.2865 0.3104 -0.0874 -0.0815 0.1663  3   VAL   B N   
2755 N N   B VAL   B 3   ? 0.2667 0.2899 0.2823 -0.0350 -0.0265 0.0463  3   VAL   B N   
2756 C CA  A VAL   B 3   ? 0.1986 0.2475 0.3029 -0.0758 -0.0696 0.1488  3   VAL   B CA  
2757 C CA  B VAL   B 3   ? 0.2405 0.2662 0.2541 -0.0392 -0.0322 0.0556  3   VAL   B CA  
2758 C C   A VAL   B 3   ? 0.1845 0.2365 0.2565 -0.0653 -0.0691 0.1220  3   VAL   B C   
2759 C C   B VAL   B 3   ? 0.2099 0.2422 0.2280 -0.0457 -0.0449 0.0723  3   VAL   B C   
2760 O O   A VAL   B 3   ? 0.1905 0.2477 0.2585 -0.0646 -0.0733 0.1268  3   VAL   B O   
2761 O O   B VAL   B 3   ? 0.2108 0.2451 0.2210 -0.0440 -0.0431 0.0730  3   VAL   B O   
2762 C CB  A VAL   B 3   ? 0.2205 0.2401 0.3534 -0.0708 -0.0659 0.1272  3   VAL   B CB  
2763 C CB  B VAL   B 3   ? 0.2450 0.2670 0.2565 -0.0379 -0.0270 0.0484  3   VAL   B CB  
2764 C CG1 A VAL   B 3   ? 0.2306 0.2360 0.3754 -0.0724 -0.0643 0.1130  3   VAL   B CG1 
2765 C CG1 B VAL   B 3   ? 0.2469 0.2670 0.2582 -0.0376 -0.0255 0.0446  3   VAL   B CG1 
2766 C CG2 A VAL   B 3   ? 0.2237 0.2458 0.3709 -0.0638 -0.0610 0.1318  3   VAL   B CG2 
2767 C CG2 B VAL   B 3   ? 0.2463 0.2680 0.2578 -0.0370 -0.0254 0.0474  3   VAL   B CG2 
2786 N N   . ASN   B 4   ? 0.1793 0.2145 0.2139 -0.0546 -0.0609 0.0890  4   ASN   B N   
2787 C CA  . ASN   B 4   ? 0.1740 0.2051 0.1809 -0.0521 -0.0458 0.0484  4   ASN   B CA  
2788 C C   . ASN   B 4   ? 0.1798 0.2167 0.1681 -0.0529 -0.0297 0.0311  4   ASN   B C   
2789 O O   . ASN   B 4   ? 0.1821 0.2269 0.1883 -0.0505 -0.0224 0.0157  4   ASN   B O   
2790 C CB  . ASN   B 4   ? 0.1673 0.1956 0.1624 -0.0445 -0.0491 0.0389  4   ASN   B CB  
2791 C CG  . ASN   B 4   ? 0.1673 0.1807 0.1474 -0.0427 -0.0405 0.0273  4   ASN   B CG  
2792 O OD1 . ASN   B 4   ? 0.1695 0.1717 0.1447 -0.0382 -0.0429 0.0226  4   ASN   B OD1 
2793 N ND2 . ASN   B 4   ? 0.1868 0.1854 0.1578 -0.0219 -0.0305 0.0226  4   ASN   B ND2 
2801 N N   . SER   B 5   ? 0.1905 0.2306 0.1616 -0.0522 -0.0129 0.0312  5   SER   B N   
2802 C CA  . SER   B 5   ? 0.2154 0.2644 0.1932 -0.0379 0.0076  0.0335  5   SER   B CA  
2803 C C   . SER   B 5   ? 0.2290 0.2698 0.2323 -0.0520 0.0385  0.0326  5   SER   B C   
2804 O O   . SER   B 5   ? 0.2473 0.2713 0.3172 -0.0444 0.0679  0.0350  5   SER   B O   
2805 C CB  . SER   B 5   ? 0.2268 0.2851 0.2163 -0.0294 0.0080  0.0451  5   SER   B CB  
2806 O OG  . SER   B 5   ? 0.2450 0.3071 0.2748 -0.0238 0.0059  0.0448  5   SER   B OG  
2812 N N   . PHE   B 6   ? 0.2416 0.2849 0.1971 -0.0544 0.0435  0.0300  6   PHE   B N   
2813 C CA  . PHE   B 6   ? 0.2502 0.2856 0.1690 -0.0735 0.0442  0.0094  6   PHE   B CA  
2814 C C   . PHE   B 6   ? 0.3018 0.3152 0.2091 -0.0806 0.0629  -0.0141 6   PHE   B C   
2815 O O   . PHE   B 6   ? 0.3172 0.3428 0.2450 -0.0757 0.0423  -0.0297 6   PHE   B O   
2816 C CB  . PHE   B 6   ? 0.2212 0.2631 0.1513 -0.0654 0.0224  0.0065  6   PHE   B CB  
2817 C CG  . PHE   B 6   ? 0.1925 0.2326 0.1429 -0.0576 0.0081  0.0003  6   PHE   B CG  
2818 C CD1 . PHE   B 6   ? 0.1930 0.2079 0.1289 -0.0496 -0.0046 0.0026  6   PHE   B CD1 
2819 C CD2 . PHE   B 6   ? 0.1722 0.2309 0.1483 -0.0505 0.0140  0.0290  6   PHE   B CD2 
2820 C CE1 . PHE   B 6   ? 0.1857 0.1882 0.1405 -0.0414 -0.0088 0.0012  6   PHE   B CE1 
2821 C CE2 . PHE   B 6   ? 0.1731 0.2153 0.1738 -0.0372 0.0164  0.0272  6   PHE   B CE2 
2822 C CZ  . PHE   B 6   ? 0.1748 0.1930 0.1569 -0.0393 0.0073  0.0089  6   PHE   B CZ  
2832 N N   . SER   B 7   ? 0.3371 0.3018 0.2227 -0.0990 0.0971  -0.0362 7   SER   B N   
2833 C CA  . SER   B 7   ? 0.3703 0.3124 0.2648 -0.0982 0.1185  -0.0430 7   SER   B CA  
2834 C C   . SER   B 7   ? 0.3684 0.2940 0.2598 -0.0978 0.1322  -0.0522 7   SER   B C   
2835 O O   . SER   B 7   ? 0.3737 0.2972 0.2936 -0.0959 0.1270  -0.0561 7   SER   B O   
2836 C CB  . SER   B 7   ? 0.3952 0.3360 0.3273 -0.0944 0.1276  -0.0397 7   SER   B CB  
2837 O OG  . SER   B 7   ? 0.4096 0.3446 0.3760 -0.0915 0.1272  -0.0323 7   SER   B OG  
2843 N N   . GLY   B 8   ? 0.3651 0.2799 0.2680 -0.0869 0.1377  -0.0564 8   GLY   B N   
2844 C CA  . GLY   B 8   ? 0.3524 0.2612 0.2723 -0.0794 0.1346  -0.0619 8   GLY   B CA  
2845 C C   . GLY   B 8   ? 0.3310 0.2370 0.2695 -0.0763 0.1302  -0.0554 8   GLY   B C   
2846 O O   . GLY   B 8   ? 0.3394 0.2458 0.3077 -0.0689 0.1332  -0.0584 8   GLY   B O   
2850 N N   . TYR   B 9   ? 0.3068 0.2167 0.2344 -0.0658 0.1052  -0.0580 9   TYR   B N   
2851 C CA  . TYR   B 9   ? 0.2826 0.1929 0.1984 -0.0516 0.0741  -0.0433 9   TYR   B CA  
2852 C C   . TYR   B 9   ? 0.2767 0.1964 0.1760 -0.0468 0.0408  -0.0306 9   TYR   B C   
2853 O O   . TYR   B 9   ? 0.2948 0.2221 0.2193 -0.0486 0.0390  -0.0203 9   TYR   B O   
2854 C CB  . TYR   B 9   ? 0.2752 0.1759 0.2035 -0.0413 0.0655  -0.0404 9   TYR   B CB  
2855 C CG  . TYR   B 9   ? 0.2681 0.1607 0.2032 -0.0454 0.0646  -0.0436 9   TYR   B CG  
2856 C CD1 . TYR   B 9   ? 0.2721 0.1615 0.2179 -0.0631 0.0688  -0.0347 9   TYR   B CD1 
2857 C CD2 . TYR   B 9   ? 0.2523 0.1573 0.1967 -0.0422 0.0640  -0.0533 9   TYR   B CD2 
2858 C CE1 . TYR   B 9   ? 0.2668 0.1711 0.2268 -0.0707 0.0725  -0.0476 9   TYR   B CE1 
2859 C CE2 . TYR   B 9   ? 0.2541 0.1610 0.2073 -0.0446 0.0640  -0.0544 9   TYR   B CE2 
2860 C CZ  . TYR   B 9   ? 0.2589 0.1769 0.2232 -0.0610 0.0689  -0.0595 9   TYR   B CZ  
2861 O OH  . TYR   B 9   ? 0.2576 0.1953 0.2424 -0.0733 0.0653  -0.0740 9   TYR   B OH  
2871 N N   . LEU   B 10  ? 0.2542 0.1704 0.1518 -0.0382 0.0185  -0.0307 10  LEU   B N   
2872 C CA  . LEU   B 10  ? 0.2471 0.1649 0.1604 -0.0442 0.0003  -0.0351 10  LEU   B CA  
2873 C C   . LEU   B 10  ? 0.2294 0.1654 0.1635 -0.0487 -0.0101 -0.0315 10  LEU   B C   
2874 O O   . LEU   B 10  ? 0.2188 0.1702 0.1658 -0.0361 -0.0021 -0.0267 10  LEU   B O   
2875 C CB  . LEU   B 10  ? 0.2600 0.1660 0.1841 -0.0456 -0.0152 -0.0228 10  LEU   B CB  
2876 C CG  . LEU   B 10  ? 0.2776 0.1720 0.2254 -0.0407 -0.0404 -0.0090 10  LEU   B CG  
2877 C CD1 . LEU   B 10  ? 0.2873 0.1862 0.2521 -0.0402 -0.0419 -0.0088 10  LEU   B CD1 
2878 C CD2 . LEU   B 10  ? 0.2900 0.1790 0.2580 -0.0385 -0.0381 0.0083  10  LEU   B CD2 
2890 N N   . LYS   B 11  ? 0.2393 0.1906 0.1695 -0.0458 -0.0200 -0.0208 11  LYS   B N   
2891 C CA  . LYS   B 11  ? 0.2534 0.2163 0.1954 -0.0326 -0.0283 -0.0243 11  LYS   B CA  
2892 C C   . LYS   B 11  ? 0.2413 0.2007 0.2007 -0.0492 -0.0206 -0.0377 11  LYS   B C   
2893 O O   . LYS   B 11  ? 0.2571 0.2162 0.2361 -0.0642 -0.0186 -0.0698 11  LYS   B O   
2894 C CB  . LYS   B 11  ? 0.2798 0.2631 0.2448 -0.0041 -0.0310 -0.0135 11  LYS   B CB  
2895 C CG  . LYS   B 11  ? 0.3063 0.2943 0.3099 0.0120  -0.0277 -0.0090 11  LYS   B CG  
2896 C CD  . LYS   B 11  ? 0.3278 0.3158 0.3742 0.0191  -0.0235 -0.0079 11  LYS   B CD  
2897 C CE  . LYS   B 11  ? 0.3440 0.3306 0.4242 0.0177  -0.0219 -0.0071 11  LYS   B CE  
2898 N NZ  . LYS   B 11  ? 0.3524 0.3399 0.4514 0.0143  -0.0221 -0.0055 11  LYS   B NZ  
2912 N N   . LEU   B 12  ? 0.2111 0.1754 0.1941 -0.0441 -0.0157 -0.0409 12  LEU   B N   
2913 C CA  . LEU   B 12  ? 0.2009 0.1648 0.2122 -0.0427 -0.0162 -0.0355 12  LEU   B CA  
2914 C C   . LEU   B 12  ? 0.1906 0.1657 0.2190 -0.0470 -0.0276 -0.0318 12  LEU   B C   
2915 O O   . LEU   B 12  ? 0.1893 0.1700 0.2385 -0.0546 -0.0373 -0.0244 12  LEU   B O   
2916 C CB  . LEU   B 12  ? 0.2017 0.1460 0.2091 -0.0308 -0.0077 -0.0358 12  LEU   B CB  
2917 C CG  . LEU   B 12  ? 0.2014 0.1438 0.2101 -0.0322 -0.0108 -0.0273 12  LEU   B CG  
2918 C CD1 . LEU   B 12  ? 0.2128 0.1470 0.2058 -0.0212 -0.0148 -0.0140 12  LEU   B CD1 
2919 C CD2 . LEU   B 12  ? 0.2064 0.1543 0.2368 -0.0296 -0.0044 -0.0294 12  LEU   B CD2 
2931 N N   . THR   B 13  ? 0.1825 0.1697 0.2230 -0.0448 -0.0323 -0.0393 13  THR   B N   
2932 C CA  . THR   B 13  ? 0.1840 0.1761 0.2198 -0.0490 -0.0395 -0.0273 13  THR   B CA  
2933 C C   . THR   B 13  ? 0.2211 0.1888 0.2325 -0.0545 -0.0520 -0.0245 13  THR   B C   
2934 O O   . THR   B 13  ? 0.2343 0.1841 0.2396 -0.0506 -0.0171 -0.0268 13  THR   B O   
2935 C CB  . THR   B 13  ? 0.1719 0.1795 0.2246 -0.0464 -0.0390 -0.0194 13  THR   B CB  
2936 O OG1 . THR   B 13  ? 0.1708 0.1758 0.2242 -0.0385 -0.0254 -0.0191 13  THR   B OG1 
2937 C CG2 . THR   B 13  ? 0.1824 0.1873 0.2329 -0.0369 -0.0238 -0.0117 13  THR   B CG2 
2945 N N   A ASP   B 14  ? 0.2394 0.1993 0.2477 -0.0585 -0.0879 -0.0138 14  ASP   B N   
2946 N N   B ASP   B 14  ? 0.2270 0.1941 0.2499 -0.0529 -0.0547 -0.0176 14  ASP   B N   
2947 C CA  A ASP   B 14  ? 0.2535 0.2203 0.2733 -0.0578 -0.1043 0.0078  14  ASP   B CA  
2948 C CA  B ASP   B 14  ? 0.2318 0.2007 0.2665 -0.0509 -0.0556 -0.0092 14  ASP   B CA  
2949 C C   A ASP   B 14  ? 0.2423 0.2038 0.2384 -0.0639 -0.0809 0.0103  14  ASP   B C   
2950 C C   B ASP   B 14  ? 0.2206 0.1897 0.2375 -0.0515 -0.0613 -0.0042 14  ASP   B C   
2951 O O   A ASP   B 14  ? 0.2716 0.2255 0.2476 -0.0695 -0.0755 0.0253  14  ASP   B O   
2952 O O   B ASP   B 14  ? 0.2263 0.1935 0.2397 -0.0508 -0.0611 -0.0032 14  ASP   B O   
2953 C CB  A ASP   B 14  ? 0.2770 0.2606 0.3537 -0.0502 -0.1254 0.0159  14  ASP   B CB  
2954 C CB  B ASP   B 14  ? 0.2463 0.2172 0.3108 -0.0486 -0.0490 -0.0073 14  ASP   B CB  
2955 C CG  A ASP   B 14  ? 0.3079 0.2988 0.4402 -0.0381 -0.1208 0.0083  14  ASP   B CG  
2956 C CG  B ASP   B 14  ? 0.2603 0.2314 0.3484 -0.0459 -0.0419 -0.0078 14  ASP   B CG  
2957 O OD1 A ASP   B 14  ? 0.3257 0.3138 0.4642 -0.0385 -0.1157 -0.0078 14  ASP   B OD1 
2958 O OD1 B ASP   B 14  ? 0.2658 0.2384 0.3592 -0.0456 -0.0385 -0.0099 14  ASP   B OD1 
2959 O OD2 A ASP   B 14  ? 0.3135 0.3151 0.4768 -0.0347 -0.1190 0.0111  14  ASP   B OD2 
2960 O OD2 B ASP   B 14  ? 0.2648 0.2357 0.3600 -0.0459 -0.0409 -0.0070 14  ASP   B OD2 
2969 N N   . ASN   B 15  ? 0.2031 0.1751 0.2079 -0.0501 -0.0679 0.0025  15  ASN   B N   
2970 C CA  . ASN   B 15  ? 0.1652 0.1520 0.1925 -0.0279 -0.0409 -0.0045 15  ASN   B CA  
2971 C C   . ASN   B 15  ? 0.1514 0.1394 0.1791 -0.0183 -0.0317 -0.0094 15  ASN   B C   
2972 O O   . ASN   B 15  ? 0.1554 0.1369 0.1986 -0.0172 -0.0400 -0.0219 15  ASN   B O   
2973 C CB  . ASN   B 15  ? 0.1555 0.1501 0.2133 -0.0144 -0.0408 -0.0011 15  ASN   B CB  
2974 C CG  . ASN   B 15  ? 0.1444 0.1550 0.2115 -0.0204 -0.0145 -0.0004 15  ASN   B CG  
2975 O OD1 . ASN   B 15  ? 0.1544 0.1813 0.2386 -0.0379 -0.0182 0.0088  15  ASN   B OD1 
2976 N ND2 . ASN   B 15  ? 0.1484 0.1361 0.2043 -0.0114 0.0077  -0.0078 15  ASN   B ND2 
2984 N N   . VAL   B 16  ? 0.1529 0.1318 0.1820 -0.0240 -0.0427 -0.0078 16  VAL   B N   
2985 C CA  . VAL   B 16  ? 0.1516 0.1316 0.1652 -0.0259 -0.0269 -0.0239 16  VAL   B CA  
2986 C C   . VAL   B 16  ? 0.1510 0.1409 0.1625 -0.0310 -0.0257 -0.0189 16  VAL   B C   
2987 O O   . VAL   B 16  ? 0.1570 0.1563 0.1865 -0.0261 -0.0189 -0.0284 16  VAL   B O   
2988 C CB  . VAL   B 16  ? 0.1583 0.1352 0.1762 -0.0150 -0.0170 -0.0209 16  VAL   B CB  
2989 C CG1 . VAL   B 16  ? 0.1665 0.1364 0.1778 -0.0010 -0.0139 -0.0122 16  VAL   B CG1 
2990 C CG2 . VAL   B 16  ? 0.1607 0.1450 0.1965 -0.0045 -0.0102 -0.0158 16  VAL   B CG2 
3000 N N   . TYR   B 17  ? 0.1570 0.1507 0.1627 -0.0269 -0.0168 -0.0244 17  TYR   B N   
3001 C CA  . TYR   B 17  ? 0.1627 0.1606 0.1506 -0.0293 -0.0175 -0.0082 17  TYR   B CA  
3002 C C   . TYR   B 17  ? 0.1577 0.1402 0.1516 -0.0326 -0.0140 -0.0127 17  TYR   B C   
3003 O O   . TYR   B 17  ? 0.1631 0.1419 0.1626 -0.0240 -0.0241 -0.0312 17  TYR   B O   
3004 C CB  . TYR   B 17  ? 0.1879 0.1983 0.1666 -0.0181 -0.0137 0.0261  17  TYR   B CB  
3005 C CG  . TYR   B 17  ? 0.2163 0.2372 0.2008 -0.0106 -0.0207 0.0323  17  TYR   B CG  
3006 C CD1 . TYR   B 17  ? 0.2292 0.2484 0.2164 -0.0058 -0.0326 0.0392  17  TYR   B CD1 
3007 C CD2 . TYR   B 17  ? 0.2387 0.2632 0.2249 -0.0018 -0.0292 0.0279  17  TYR   B CD2 
3008 C CE1 . TYR   B 17  ? 0.2482 0.2692 0.2333 0.0011  -0.0431 0.0335  17  TYR   B CE1 
3009 C CE2 . TYR   B 17  ? 0.2562 0.2805 0.2472 0.0062  -0.0432 0.0330  17  TYR   B CE2 
3010 C CZ  . TYR   B 17  ? 0.2610 0.2862 0.2493 0.0102  -0.0534 0.0342  17  TYR   B CZ  
3011 O OH  . TYR   B 17  ? 0.2772 0.3040 0.2730 0.0202  -0.0590 0.0323  17  TYR   B OH  
3021 N N   . ILE   B 18  ? 0.1650 0.1396 0.1421 -0.0269 -0.0046 -0.0211 18  ILE   B N   
3022 C CA  . ILE   B 18  ? 0.1693 0.1366 0.1426 -0.0257 -0.0072 -0.0201 18  ILE   B CA  
3023 C C   . ILE   B 18  ? 0.1797 0.1394 0.1434 -0.0312 -0.0032 -0.0286 18  ILE   B C   
3024 O O   . ILE   B 18  ? 0.2014 0.1520 0.1518 -0.0291 0.0098  -0.0352 18  ILE   B O   
3025 C CB  . ILE   B 18  ? 0.1760 0.1401 0.1575 -0.0319 -0.0054 -0.0121 18  ILE   B CB  
3026 C CG1 . ILE   B 18  ? 0.1779 0.1479 0.1676 -0.0318 -0.0026 -0.0025 18  ILE   B CG1 
3027 C CG2 . ILE   B 18  ? 0.1767 0.1446 0.1676 -0.0344 -0.0044 -0.0108 18  ILE   B CG2 
3028 C CD1 . ILE   B 18  ? 0.1834 0.1728 0.1952 -0.0300 -0.0162 0.0153  18  ILE   B CD1 
3040 N N   . LYS   B 19  ? 0.1806 0.1407 0.1593 -0.0172 0.0233  -0.0304 19  LYS   B N   
3041 C CA  . LYS   B 19  ? 0.1864 0.1468 0.1739 -0.0182 0.0233  -0.0332 19  LYS   B CA  
3042 C C   . LYS   B 19  ? 0.1702 0.1483 0.1784 -0.0197 0.0300  -0.0423 19  LYS   B C   
3043 O O   . LYS   B 19  ? 0.1701 0.1527 0.1740 -0.0150 0.0241  -0.0396 19  LYS   B O   
3044 C CB  . LYS   B 19  ? 0.2108 0.1624 0.1913 -0.0231 0.0375  -0.0243 19  LYS   B CB  
3045 C CG  . LYS   B 19  ? 0.2326 0.1854 0.2225 -0.0281 0.0550  -0.0250 19  LYS   B CG  
3046 C CD  . LYS   B 19  ? 0.2576 0.2143 0.2357 -0.0338 0.0622  -0.0177 19  LYS   B CD  
3047 C CE  . LYS   B 19  ? 0.2818 0.2402 0.2580 -0.0343 0.0622  -0.0174 19  LYS   B CE  
3048 N NZ  . LYS   B 19  ? 0.2964 0.2562 0.2662 -0.0384 0.0655  -0.0147 19  LYS   B NZ  
3062 N N   . ASN   B 20  ? 0.1726 0.1546 0.2108 -0.0116 0.0349  -0.0563 20  ASN   B N   
3063 C CA  . ASN   B 20  ? 0.1739 0.1677 0.2329 -0.0050 0.0339  -0.0635 20  ASN   B CA  
3064 C C   . ASN   B 20  ? 0.1680 0.1889 0.2368 -0.0154 0.0454  -0.0722 20  ASN   B C   
3065 O O   . ASN   B 20  ? 0.1887 0.2230 0.2517 -0.0301 0.0470  -0.0730 20  ASN   B O   
3066 C CB  . ASN   B 20  ? 0.2005 0.1667 0.2571 0.0118  0.0230  -0.0649 20  ASN   B CB  
3067 C CG  . ASN   B 20  ? 0.2248 0.1768 0.2760 0.0388  0.0197  -0.0667 20  ASN   B CG  
3068 O OD1 . ASN   B 20  ? 0.2497 0.2022 0.3018 0.0531  0.0115  -0.0750 20  ASN   B OD1 
3069 N ND2 . ASN   B 20  ? 0.2192 0.1777 0.2639 0.0371  0.0169  -0.0615 20  ASN   B ND2 
3076 N N   . ALA   B 21  ? 0.1687 0.1754 0.2367 -0.0205 0.0452  -0.0585 21  ALA   B N   
3077 C CA  . ALA   B 21  ? 0.1772 0.1776 0.2476 -0.0245 0.0323  -0.0461 21  ALA   B CA  
3078 C C   . ALA   B 21  ? 0.1776 0.1546 0.2435 -0.0145 0.0359  -0.0341 21  ALA   B C   
3079 O O   . ALA   B 21  ? 0.1856 0.1479 0.2455 -0.0247 0.0391  -0.0294 21  ALA   B O   
3080 C CB  . ALA   B 21  ? 0.1930 0.2032 0.2560 -0.0352 0.0280  -0.0312 21  ALA   B CB  
3086 N N   . ASP   B 22  ? 0.1709 0.1445 0.2405 -0.0150 0.0260  -0.0294 22  ASP   B N   
3087 C CA  . ASP   B 22  ? 0.1698 0.1403 0.2273 -0.0062 0.0202  -0.0224 22  ASP   B CA  
3088 C C   . ASP   B 22  ? 0.1665 0.1384 0.1776 -0.0112 0.0160  -0.0148 22  ASP   B C   
3089 O O   . ASP   B 22  ? 0.1706 0.1387 0.1799 -0.0088 0.0106  -0.0038 22  ASP   B O   
3090 C CB  . ASP   B 22  ? 0.1793 0.1467 0.2761 -0.0048 0.0180  -0.0061 22  ASP   B CB  
3091 C CG  . ASP   B 22  ? 0.1886 0.1655 0.3168 0.0018  -0.0097 -0.0047 22  ASP   B CG  
3092 O OD1 . ASP   B 22  ? 0.2038 0.1653 0.3146 0.0066  -0.0284 -0.0061 22  ASP   B OD1 
3093 O OD2 . ASP   B 22  ? 0.1971 0.1974 0.3648 0.0093  -0.0245 -0.0137 22  ASP   B OD2 
3098 N N   . ILE   B 23  ? 0.1676 0.1349 0.1596 -0.0063 0.0056  0.0038  23  ILE   B N   
3099 C CA  . ILE   B 23  ? 0.1590 0.1314 0.1447 -0.0051 -0.0036 0.0061  23  ILE   B CA  
3100 C C   . ILE   B 23  ? 0.1504 0.1334 0.1503 -0.0038 -0.0061 0.0001  23  ILE   B C   
3101 O O   . ILE   B 23  ? 0.1412 0.1351 0.1468 -0.0086 -0.0031 0.0077  23  ILE   B O   
3102 C CB  . ILE   B 23  ? 0.1576 0.1405 0.1580 -0.0160 0.0027  0.0209  23  ILE   B CB  
3103 C CG1 . ILE   B 23  ? 0.1603 0.1531 0.1758 -0.0115 0.0095  0.0222  23  ILE   B CG1 
3104 C CG2 . ILE   B 23  ? 0.1675 0.1611 0.1701 -0.0130 -0.0013 0.0100  23  ILE   B CG2 
3105 C CD1 . ILE   B 23  ? 0.1611 0.1610 0.1938 -0.0055 0.0075  0.0151  23  ILE   B CD1 
3117 N N   . VAL   B 24  ? 0.1528 0.1334 0.1642 -0.0053 -0.0070 -0.0004 24  VAL   B N   
3118 C CA  . VAL   B 24  ? 0.1464 0.1401 0.1770 -0.0030 -0.0131 -0.0090 24  VAL   B CA  
3119 C C   . VAL   B 24  ? 0.1440 0.1442 0.1804 -0.0080 -0.0121 -0.0006 24  VAL   B C   
3120 O O   . VAL   B 24  ? 0.1428 0.1535 0.1995 -0.0136 -0.0068 0.0121  24  VAL   B O   
3121 C CB  . VAL   B 24  ? 0.1584 0.1582 0.1903 0.0062  -0.0260 -0.0028 24  VAL   B CB  
3122 C CG1 . VAL   B 24  ? 0.1598 0.1607 0.2245 -0.0005 -0.0204 -0.0082 24  VAL   B CG1 
3123 C CG2 . VAL   B 24  ? 0.1705 0.1844 0.1938 0.0086  -0.0228 -0.0104 24  VAL   B CG2 
3133 N N   . GLU   B 25  ? 0.1652 0.1558 0.1854 -0.0069 -0.0041 0.0025  25  GLU   B N   
3134 C CA  . GLU   B 25  ? 0.1809 0.1789 0.2049 0.0031  0.0097  -0.0019 25  GLU   B CA  
3135 C C   . GLU   B 25  ? 0.1738 0.1685 0.1820 -0.0083 0.0125  0.0059  25  GLU   B C   
3136 O O   . GLU   B 25  ? 0.1776 0.1835 0.1976 -0.0063 0.0183  0.0127  25  GLU   B O   
3137 C CB  . GLU   B 25  ? 0.2159 0.2261 0.2658 0.0269  0.0227  -0.0082 25  GLU   B CB  
3138 C CG  . GLU   B 25  ? 0.2510 0.2980 0.3705 0.0322  0.0216  -0.0113 25  GLU   B CG  
3139 C CD  . GLU   B 25  ? 0.2890 0.3613 0.4600 0.0285  0.0180  -0.0157 25  GLU   B CD  
3140 O OE1 . GLU   B 25  ? 0.3118 0.3815 0.4887 0.0325  0.0235  -0.0119 25  GLU   B OE1 
3141 O OE2 . GLU   B 25  ? 0.3099 0.3786 0.4913 0.0251  0.0113  -0.0254 25  GLU   B OE2 
3148 N N   . GLU   B 26  ? 0.1682 0.1607 0.1603 -0.0243 0.0102  0.0034  26  GLU   B N   
3149 C CA  . GLU   B 26  ? 0.1666 0.1734 0.1695 -0.0322 -0.0063 0.0000  26  GLU   B CA  
3150 C C   . GLU   B 26  ? 0.1529 0.1679 0.1632 -0.0215 0.0054  0.0163  26  GLU   B C   
3151 O O   . GLU   B 26  ? 0.1757 0.1891 0.1710 -0.0199 -0.0001 0.0264  26  GLU   B O   
3152 C CB  . GLU   B 26  ? 0.1949 0.1949 0.1940 -0.0467 -0.0009 0.0049  26  GLU   B CB  
3153 C CG  . GLU   B 26  ? 0.2340 0.2283 0.2521 -0.0486 0.0082  -0.0154 26  GLU   B CG  
3154 C CD  . GLU   B 26  ? 0.2582 0.2521 0.2624 -0.0643 0.0227  -0.0419 26  GLU   B CD  
3155 O OE1 . GLU   B 26  ? 0.2795 0.2355 0.2645 -0.0725 0.0635  -0.0407 26  GLU   B OE1 
3156 O OE2 . GLU   B 26  ? 0.2599 0.2925 0.3084 -0.0546 0.0158  -0.0288 26  GLU   B OE2 
3163 N N   . ALA   B 27  ? 0.1386 0.1539 0.1602 -0.0170 0.0100  0.0158  27  ALA   B N   
3164 C CA  . ALA   B 27  ? 0.1435 0.1503 0.1796 -0.0091 0.0015  0.0248  27  ALA   B CA  
3165 C C   . ALA   B 27  ? 0.1429 0.1579 0.2019 -0.0111 0.0179  0.0384  27  ALA   B C   
3166 O O   . ALA   B 27  ? 0.1562 0.1646 0.2111 -0.0017 0.0161  0.0400  27  ALA   B O   
3167 C CB  . ALA   B 27  ? 0.1615 0.1373 0.1879 -0.0147 0.0018  0.0246  27  ALA   B CB  
3173 N N   . LYS   B 28  ? 0.1381 0.1792 0.2370 -0.0168 0.0224  0.0600  28  LYS   B N   
3174 C CA  . LYS   B 28  ? 0.1583 0.2195 0.2595 -0.0076 0.0465  0.0847  28  LYS   B CA  
3175 C C   . LYS   B 28  ? 0.1792 0.2373 0.2479 0.0014  0.0629  0.0785  28  LYS   B C   
3176 O O   . LYS   B 28  ? 0.2054 0.2443 0.2614 -0.0017 0.0615  0.0777  28  LYS   B O   
3177 C CB  . LYS   B 28  ? 0.1792 0.2532 0.3105 -0.0004 0.0686  0.0993  28  LYS   B CB  
3178 C CG  . LYS   B 28  ? 0.2082 0.2933 0.3452 0.0085  0.0733  0.1122  28  LYS   B CG  
3179 C CD  . LYS   B 28  ? 0.2631 0.3469 0.3977 0.0164  0.0823  0.1126  28  LYS   B CD  
3180 C CE  . LYS   B 28  ? 0.3103 0.3855 0.4429 0.0241  0.0850  0.1160  28  LYS   B CE  
3181 N NZ  . LYS   B 28  ? 0.3245 0.3976 0.4602 0.0300  0.0848  0.1214  28  LYS   B NZ  
3195 N N   . LYS   B 29  ? 0.1947 0.2557 0.2484 0.0257  0.0638  0.0650  29  LYS   B N   
3196 C CA  . LYS   B 29  ? 0.2379 0.2871 0.2718 0.0256  0.0622  0.0595  29  LYS   B CA  
3197 C C   . LYS   B 29  ? 0.2338 0.2862 0.2321 0.0245  0.0559  0.0725  29  LYS   B C   
3198 O O   . LYS   B 29  ? 0.2537 0.3070 0.2451 0.0322  0.0498  0.0751  29  LYS   B O   
3199 C CB  . LYS   B 29  ? 0.2914 0.3246 0.3488 0.0207  0.0538  0.0450  29  LYS   B CB  
3200 C CG  . LYS   B 29  ? 0.3322 0.3533 0.4365 0.0153  0.0529  0.0417  29  LYS   B CG  
3201 C CD  . LYS   B 29  ? 0.3701 0.3765 0.5006 0.0082  0.0593  0.0370  29  LYS   B CD  
3202 C CE  . LYS   B 29  ? 0.3966 0.3956 0.5431 0.0025  0.0666  0.0339  29  LYS   B CE  
3203 N NZ  . LYS   B 29  ? 0.4072 0.3994 0.5757 -0.0000 0.0680  0.0319  29  LYS   B NZ  
3217 N N   . VAL   B 30  ? 0.2070 0.2678 0.2179 0.0111  0.0425  0.0748  30  VAL   B N   
3218 C CA  . VAL   B 30  ? 0.1943 0.2594 0.2505 -0.0037 0.0055  0.0764  30  VAL   B CA  
3219 C C   . VAL   B 30  ? 0.1667 0.2503 0.2387 -0.0074 0.0131  0.0932  30  VAL   B C   
3220 O O   . VAL   B 30  ? 0.1814 0.2663 0.2418 0.0031  0.0076  0.1037  30  VAL   B O   
3221 C CB  . VAL   B 30  ? 0.2052 0.2612 0.3010 -0.0196 -0.0205 0.0669  30  VAL   B CB  
3222 C CG1 . VAL   B 30  ? 0.2067 0.2684 0.2955 -0.0221 -0.0141 0.0621  30  VAL   B CG1 
3223 C CG2 . VAL   B 30  ? 0.2174 0.2605 0.3208 -0.0250 -0.0316 0.0583  30  VAL   B CG2 
3233 N N   . LYS   B 31  ? 0.1593 0.2155 0.2656 -0.0207 0.0088  0.1001  31  LYS   B N   
3234 C CA  . LYS   B 31  ? 0.1502 0.2089 0.3033 -0.0346 0.0021  0.0974  31  LYS   B CA  
3235 C C   . LYS   B 31  ? 0.1418 0.1760 0.2608 -0.0337 -0.0198 0.0809  31  LYS   B C   
3236 O O   . LYS   B 31  ? 0.1536 0.1916 0.2711 -0.0226 -0.0168 0.0947  31  LYS   B O   
3237 C CB  . LYS   B 31  ? 0.1731 0.2514 0.3537 -0.0300 0.0257  0.1068  31  LYS   B CB  
3238 C CG  . LYS   B 31  ? 0.1987 0.2934 0.3920 -0.0290 0.0415  0.1051  31  LYS   B CG  
3239 C CD  . LYS   B 31  ? 0.2297 0.3358 0.4273 -0.0251 0.0403  0.0970  31  LYS   B CD  
3240 C CE  . LYS   B 31  ? 0.2571 0.3656 0.4646 -0.0218 0.0298  0.0844  31  LYS   B CE  
3241 N NZ  . LYS   B 31  ? 0.2643 0.3834 0.4805 -0.0145 0.0193  0.0739  31  LYS   B NZ  
3255 N N   . PRO   B 32  ? 0.1528 0.1483 0.1960 -0.0297 -0.0372 0.0435  32  PRO   B N   
3256 C CA  . PRO   B 32  ? 0.1613 0.1427 0.1565 -0.0264 -0.0377 0.0300  32  PRO   B CA  
3257 C C   . PRO   B 32  ? 0.1723 0.1300 0.1574 -0.0297 -0.0482 0.0306  32  PRO   B C   
3258 O O   . PRO   B 32  ? 0.1861 0.1363 0.1929 -0.0336 -0.0604 0.0304  32  PRO   B O   
3259 C CB  . PRO   B 32  ? 0.1793 0.1376 0.1606 -0.0299 -0.0288 0.0145  32  PRO   B CB  
3260 C CG  . PRO   B 32  ? 0.1924 0.1279 0.1611 -0.0288 -0.0495 0.0181  32  PRO   B CG  
3261 C CD  . PRO   B 32  ? 0.1784 0.1350 0.1839 -0.0202 -0.0479 0.0271  32  PRO   B CD  
3269 N N   . THR   B 33  ? 0.1759 0.1251 0.1441 -0.0213 -0.0419 0.0176  33  THR   B N   
3270 C CA  . THR   B 33  ? 0.1794 0.1334 0.1435 -0.0265 -0.0414 0.0202  33  THR   B CA  
3271 C C   . THR   B 33  ? 0.1776 0.1262 0.1354 -0.0295 -0.0390 0.0131  33  THR   B C   
3272 O O   . THR   B 33  ? 0.2034 0.1306 0.1504 -0.0393 -0.0476 0.0171  33  THR   B O   
3273 C CB  . THR   B 33  ? 0.1889 0.1407 0.1513 -0.0112 -0.0450 0.0251  33  THR   B CB  
3274 O OG1 . THR   B 33  ? 0.1815 0.1509 0.1574 -0.0144 -0.0442 0.0325  33  THR   B OG1 
3275 C CG2 . THR   B 33  ? 0.2101 0.1501 0.1717 -0.0014 -0.0460 0.0255  33  THR   B CG2 
3283 N N   . VAL   B 34  ? 0.1641 0.1238 0.1276 -0.0290 -0.0324 0.0123  34  VAL   B N   
3284 C CA  . VAL   B 34  ? 0.1529 0.1201 0.1227 -0.0220 -0.0278 0.0071  34  VAL   B CA  
3285 C C   . VAL   B 34  ? 0.1412 0.1161 0.1073 -0.0235 -0.0178 0.0071  34  VAL   B C   
3286 O O   . VAL   B 34  ? 0.1594 0.1193 0.1195 -0.0223 -0.0299 0.0050  34  VAL   B O   
3287 C CB  . VAL   B 34  ? 0.1642 0.1283 0.1576 -0.0068 -0.0233 0.0027  34  VAL   B CB  
3288 C CG1 . VAL   B 34  ? 0.1653 0.1424 0.1602 -0.0066 -0.0100 -0.0044 34  VAL   B CG1 
3289 C CG2 . VAL   B 34  ? 0.1733 0.1352 0.1753 -0.0046 -0.0260 0.0001  34  VAL   B CG2 
3299 N N   . VAL   B 35  ? 0.1344 0.1123 0.1083 -0.0235 -0.0132 0.0063  35  VAL   B N   
3300 C CA  . VAL   B 35  ? 0.1322 0.1122 0.1045 -0.0167 -0.0090 0.0042  35  VAL   B CA  
3301 C C   . VAL   B 35  ? 0.1232 0.1095 0.1038 -0.0146 -0.0094 0.0014  35  VAL   B C   
3302 O O   . VAL   B 35  ? 0.1261 0.1154 0.1145 -0.0194 -0.0019 -0.0051 35  VAL   B O   
3303 C CB  . VAL   B 35  ? 0.1311 0.1342 0.1166 -0.0167 0.0035  0.0083  35  VAL   B CB  
3304 C CG1 . VAL   B 35  ? 0.1219 0.1460 0.1351 -0.0181 0.0020  -0.0012 35  VAL   B CG1 
3305 C CG2 . VAL   B 35  ? 0.1311 0.1310 0.1353 -0.0061 0.0015  0.0053  35  VAL   B CG2 
3315 N N   . VAL   B 36  ? 0.1267 0.1069 0.1000 -0.0146 -0.0081 0.0084  36  VAL   B N   
3316 C CA  . VAL   B 36  ? 0.1229 0.1058 0.0973 -0.0093 -0.0046 0.0048  36  VAL   B CA  
3317 C C   . VAL   B 36  ? 0.1192 0.1055 0.0848 -0.0117 -0.0003 -0.0009 36  VAL   B C   
3318 O O   . VAL   B 36  ? 0.1245 0.1155 0.1160 -0.0097 0.0013  -0.0078 36  VAL   B O   
3319 C CB  . VAL   B 36  ? 0.1229 0.1130 0.1079 -0.0124 -0.0037 0.0027  36  VAL   B CB  
3320 C CG1 . VAL   B 36  ? 0.1212 0.1230 0.1212 -0.0163 -0.0046 0.0047  36  VAL   B CG1 
3321 C CG2 . VAL   B 36  ? 0.1285 0.1180 0.1248 -0.0074 -0.0152 0.0072  36  VAL   B CG2 
3331 N N   . ASN   B 37  ? 0.1231 0.1148 0.0926 0.0017  -0.0046 0.0049  37  ASN   B N   
3332 C CA  . ASN   B 37  ? 0.1200 0.1144 0.1088 0.0033  -0.0066 0.0034  37  ASN   B CA  
3333 C C   . ASN   B 37  ? 0.1195 0.1160 0.1024 0.0051  -0.0051 -0.0027 37  ASN   B C   
3334 O O   . ASN   B 37  ? 0.1304 0.1233 0.1149 0.0045  0.0025  0.0064  37  ASN   B O   
3335 C CB  . ASN   B 37  ? 0.1221 0.1245 0.1071 0.0041  -0.0072 0.0015  37  ASN   B CB  
3336 C CG  . ASN   B 37  ? 0.1255 0.1199 0.1090 -0.0007 -0.0093 -0.0037 37  ASN   B CG  
3337 O OD1 . ASN   B 37  ? 0.1338 0.1278 0.1275 0.0119  -0.0101 -0.0018 37  ASN   B OD1 
3338 N ND2 . ASN   B 37  ? 0.1338 0.1148 0.1235 0.0032  -0.0139 0.0017  37  ASN   B ND2 
3345 N N   . ALA   B 38  ? 0.1292 0.1118 0.1122 0.0086  0.0023  -0.0016 38  ALA   B N   
3346 C CA  . ALA   B 38  ? 0.1411 0.1153 0.1085 0.0019  0.0095  0.0085  38  ALA   B CA  
3347 C C   . ALA   B 38  ? 0.1326 0.1122 0.1118 0.0019  0.0084  0.0077  38  ALA   B C   
3348 O O   . ALA   B 38  ? 0.1435 0.1271 0.1333 0.0100  0.0025  0.0069  38  ALA   B O   
3349 C CB  . ALA   B 38  ? 0.1653 0.1269 0.1222 -0.0070 0.0143  0.0062  38  ALA   B CB  
3355 N N   . ALA   B 39  ? 0.1334 0.1207 0.1000 0.0090  -0.0034 0.0026  39  ALA   B N   
3356 C CA  . ALA   B 39  ? 0.1435 0.1279 0.0990 0.0089  -0.0073 0.0029  39  ALA   B CA  
3357 C C   . ALA   B 39  ? 0.1459 0.1310 0.0875 0.0097  -0.0029 -0.0014 39  ALA   B C   
3358 O O   . ALA   B 39  ? 0.1448 0.1374 0.1191 0.0014  -0.0023 0.0063  39  ALA   B O   
3359 C CB  . ALA   B 39  ? 0.1450 0.1273 0.1236 -0.0047 0.0012  -0.0002 39  ALA   B CB  
3365 N N   . ASN   B 40  ? 0.1471 0.1491 0.0977 -0.0035 0.0017  -0.0019 40  ASN   B N   
3366 C CA  . ASN   B 40  ? 0.1531 0.1553 0.1121 0.0005  -0.0058 -0.0074 40  ASN   B CA  
3367 C C   . ASN   B 40  ? 0.1603 0.1572 0.0930 0.0063  -0.0062 -0.0004 40  ASN   B C   
3368 O O   . ASN   B 40  ? 0.1571 0.1462 0.1071 0.0058  -0.0077 0.0001  40  ASN   B O   
3369 C CB  . ASN   B 40  ? 0.1679 0.1609 0.1359 0.0075  -0.0099 0.0086  40  ASN   B CB  
3370 C CG  . ASN   B 40  ? 0.1680 0.1597 0.1714 0.0057  -0.0228 0.0085  40  ASN   B CG  
3371 O OD1 . ASN   B 40  ? 0.1658 0.1564 0.2454 0.0075  -0.0337 0.0094  40  ASN   B OD1 
3372 N ND2 . ASN   B 40  ? 0.1739 0.1611 0.1682 0.0061  -0.0133 0.0109  40  ASN   B ND2 
3379 N N   . VAL   B 41  ? 0.1711 0.1626 0.0931 0.0102  0.0070  0.0012  41  VAL   B N   
3380 C CA  . VAL   B 41  ? 0.1749 0.1740 0.1057 0.0113  0.0040  -0.0092 41  VAL   B CA  
3381 C C   . VAL   B 41  ? 0.1679 0.1715 0.1048 0.0177  -0.0055 -0.0132 41  VAL   B C   
3382 O O   . VAL   B 41  ? 0.1683 0.1682 0.1162 0.0155  -0.0075 -0.0148 41  VAL   B O   
3383 C CB  . VAL   B 41  ? 0.1897 0.1932 0.1260 -0.0029 0.0190  -0.0239 41  VAL   B CB  
3384 C CG1 . VAL   B 41  ? 0.1841 0.2014 0.1477 -0.0071 0.0291  -0.0226 41  VAL   B CG1 
3385 C CG2 . VAL   B 41  ? 0.2007 0.2122 0.1358 -0.0088 0.0240  -0.0255 41  VAL   B CG2 
3395 N N   . TYR   B 42  ? 0.1726 0.1691 0.1172 0.0186  -0.0173 -0.0030 42  TYR   B N   
3396 C CA  . TYR   B 42  ? 0.1797 0.1818 0.1248 0.0139  -0.0221 -0.0183 42  TYR   B CA  
3397 C C   . TYR   B 42  ? 0.1643 0.1606 0.1282 0.0190  -0.0221 -0.0178 42  TYR   B C   
3398 O O   . TYR   B 42  ? 0.1639 0.1691 0.1563 0.0143  -0.0285 -0.0203 42  TYR   B O   
3399 C CB  . TYR   B 42  ? 0.2031 0.2110 0.1425 0.0071  -0.0259 -0.0075 42  TYR   B CB  
3400 C CG  . TYR   B 42  ? 0.2036 0.2257 0.1357 0.0004  -0.0272 0.0049  42  TYR   B CG  
3401 C CD1 . TYR   B 42  ? 0.2009 0.2266 0.1130 -0.0055 -0.0116 -0.0035 42  TYR   B CD1 
3402 C CD2 . TYR   B 42  ? 0.2135 0.2363 0.1736 -0.0036 -0.0116 0.0113  42  TYR   B CD2 
3403 C CE1 . TYR   B 42  ? 0.2161 0.2435 0.1227 -0.0025 -0.0090 -0.0025 42  TYR   B CE1 
3404 C CE2 . TYR   B 42  ? 0.2188 0.2493 0.1693 -0.0034 0.0045  0.0195  42  TYR   B CE2 
3405 C CZ  . TYR   B 42  ? 0.2312 0.2607 0.1581 0.0097  0.0084  0.0076  42  TYR   B CZ  
3406 O OH  . TYR   B 42  ? 0.2636 0.2817 0.2084 0.0253  0.0220  0.0131  42  TYR   B OH  
3416 N N   . LEU   B 43  ? 0.1519 0.1429 0.1178 0.0102  -0.0152 -0.0150 43  LEU   B N   
3417 C CA  . LEU   B 43  ? 0.1529 0.1428 0.1140 0.0072  -0.0130 -0.0045 43  LEU   B CA  
3418 C C   . LEU   B 43  ? 0.1530 0.1465 0.1228 0.0073  -0.0099 -0.0018 43  LEU   B C   
3419 O O   . LEU   B 43  ? 0.1504 0.1531 0.1489 0.0094  -0.0153 0.0093  43  LEU   B O   
3420 C CB  . LEU   B 43  ? 0.1498 0.1366 0.1285 -0.0010 -0.0222 -0.0107 43  LEU   B CB  
3421 C CG  . LEU   B 43  ? 0.1526 0.1366 0.1308 0.0007  -0.0197 -0.0151 43  LEU   B CG  
3422 C CD1 . LEU   B 43  ? 0.1623 0.1428 0.1659 0.0029  -0.0357 -0.0104 43  LEU   B CD1 
3423 C CD2 . LEU   B 43  ? 0.1499 0.1388 0.1431 -0.0017 -0.0221 -0.0110 43  LEU   B CD2 
3435 N N   . LYS   B 44  ? 0.1498 0.1428 0.1280 0.0074  -0.0087 -0.0056 44  LYS   B N   
3436 C CA  . LYS   B 44  ? 0.1635 0.1534 0.1233 0.0106  -0.0133 0.0046  44  LYS   B CA  
3437 C C   . LYS   B 44  ? 0.1541 0.1465 0.1239 0.0111  -0.0095 -0.0021 44  LYS   B C   
3438 O O   . LYS   B 44  ? 0.1738 0.1452 0.1566 0.0072  -0.0001 -0.0001 44  LYS   B O   
3439 C CB  . LYS   B 44  ? 0.1883 0.1771 0.1446 0.0153  -0.0218 0.0021  44  LYS   B CB  
3440 C CG  . LYS   B 44  ? 0.2236 0.2053 0.1901 0.0120  -0.0421 -0.0016 44  LYS   B CG  
3441 C CD  . LYS   B 44  ? 0.2583 0.2275 0.2532 -0.0021 -0.0484 -0.0029 44  LYS   B CD  
3442 C CE  . LYS   B 44  ? 0.2868 0.2483 0.2993 -0.0036 -0.0509 0.0043  44  LYS   B CE  
3443 N NZ  . LYS   B 44  ? 0.2986 0.2573 0.3266 -0.0003 -0.0564 0.0152  44  LYS   B NZ  
3457 N N   . HIS   B 45  ? 0.1505 0.1443 0.1156 0.0052  -0.0095 0.0039  45  HIS   B N   
3458 C CA  . HIS   B 45  ? 0.1586 0.1432 0.1273 0.0116  -0.0071 -0.0005 45  HIS   B CA  
3459 C C   . HIS   B 45  ? 0.1824 0.1634 0.1724 0.0166  -0.0180 -0.0029 45  HIS   B C   
3460 O O   . HIS   B 45  ? 0.1921 0.1963 0.2145 0.0411  0.0106  0.0045  45  HIS   B O   
3461 C CB  . HIS   B 45  ? 0.1485 0.1469 0.1247 -0.0000 -0.0073 -0.0021 45  HIS   B CB  
3462 C CG  . HIS   B 45  ? 0.1510 0.1412 0.1223 -0.0011 -0.0050 -0.0037 45  HIS   B CG  
3463 N ND1 . HIS   B 45  ? 0.1536 0.1405 0.1361 0.0023  -0.0146 -0.0103 45  HIS   B ND1 
3464 C CD2 . HIS   B 45  ? 0.1608 0.1463 0.1453 -0.0040 -0.0119 -0.0004 45  HIS   B CD2 
3465 C CE1 . HIS   B 45  ? 0.1614 0.1314 0.1228 0.0007  -0.0239 -0.0120 45  HIS   B CE1 
3466 N NE2 . HIS   B 45  ? 0.1654 0.1411 0.1282 -0.0004 -0.0210 -0.0072 45  HIS   B NE2 
3474 N N   A GLY   B 46  ? 0.1936 0.1501 0.1981 0.0190  -0.0348 0.0064  46  GLY   B N   
3475 N N   B GLY   B 46  ? 0.1881 0.1713 0.1908 0.0139  -0.0213 0.0004  46  GLY   B N   
3476 C CA  A GLY   B 46  ? 0.2068 0.1627 0.2300 0.0180  -0.0371 0.0058  46  GLY   B CA  
3477 C CA  B GLY   B 46  ? 0.1940 0.1809 0.2084 0.0112  -0.0232 0.0011  46  GLY   B CA  
3478 C C   A GLY   B 46  ? 0.2044 0.1841 0.2728 0.0245  -0.0349 0.0027  46  GLY   B C   
3479 C C   B GLY   B 46  ? 0.1980 0.1913 0.2298 0.0113  -0.0233 0.0016  46  GLY   B C   
3480 O O   A GLY   B 46  ? 0.2151 0.2107 0.3452 0.0250  -0.0206 -0.0138 46  GLY   B O   
3481 O O   B GLY   B 46  ? 0.2003 0.1965 0.2369 0.0114  -0.0233 0.0052  46  GLY   B O   
3488 N N   . GLY   B 47  ? 0.1997 0.1982 0.2443 0.0079  -0.0179 -0.0038 47  GLY   B N   
3489 C CA  . GLY   B 47  ? 0.1858 0.1706 0.2022 0.0038  -0.0132 0.0008  47  GLY   B CA  
3490 C C   . GLY   B 47  ? 0.1678 0.1490 0.1687 0.0044  0.0005  0.0069  47  GLY   B C   
3491 O O   . GLY   B 47  ? 0.1791 0.1385 0.1709 0.0036  -0.0078 0.0085  47  GLY   B O   
3496 N N   . GLY   B 48  ? 0.1464 0.1389 0.1667 0.0068  -0.0085 0.0129  48  GLY   B N   
3497 C CA  . GLY   B 48  ? 0.1503 0.1299 0.1680 0.0010  0.0003  0.0071  48  GLY   B CA  
3498 C C   . GLY   B 48  ? 0.1436 0.1287 0.1566 0.0027  0.0058  0.0060  48  GLY   B C   
3499 O O   . GLY   B 48  ? 0.1437 0.1327 0.1676 0.0054  -0.0058 0.0082  48  GLY   B O   
3503 N N   . VAL   B 49  ? 0.1411 0.1377 0.1441 0.0113  0.0002  0.0081  49  VAL   B N   
3504 C CA  . VAL   B 49  ? 0.1458 0.1458 0.1364 0.0091  -0.0153 -0.0014 49  VAL   B CA  
3505 C C   . VAL   B 49  ? 0.1372 0.1379 0.1257 0.0139  -0.0065 0.0099  49  VAL   B C   
3506 O O   . VAL   B 49  ? 0.1445 0.1435 0.1367 0.0064  -0.0028 0.0087  49  VAL   B O   
3507 C CB  . VAL   B 49  ? 0.1448 0.1605 0.1654 0.0026  -0.0237 -0.0013 49  VAL   B CB  
3508 C CG1 . VAL   B 49  ? 0.1435 0.1657 0.1662 0.0081  -0.0299 0.0052  49  VAL   B CG1 
3509 C CG2 . VAL   B 49  ? 0.1666 0.1753 0.1918 -0.0050 -0.0375 -0.0074 49  VAL   B CG2 
3519 N N   . ALA   B 50  ? 0.1316 0.1311 0.1251 0.0068  -0.0032 0.0079  50  ALA   B N   
3520 C CA  . ALA   B 50  ? 0.1301 0.1260 0.1271 0.0076  -0.0053 0.0067  50  ALA   B CA  
3521 C C   . ALA   B 50  ? 0.1376 0.1283 0.1299 0.0083  -0.0044 0.0067  50  ALA   B C   
3522 O O   . ALA   B 50  ? 0.1371 0.1321 0.1260 0.0056  0.0003  0.0009  50  ALA   B O   
3523 C CB  . ALA   B 50  ? 0.1356 0.1276 0.1413 -0.0018 -0.0014 0.0112  50  ALA   B CB  
3529 N N   . GLY   B 51  ? 0.1377 0.1371 0.1413 0.0108  -0.0150 0.0075  51  GLY   B N   
3530 C CA  . GLY   B 51  ? 0.1395 0.1459 0.1550 0.0134  -0.0134 0.0076  51  GLY   B CA  
3531 C C   . GLY   B 51  ? 0.1350 0.1389 0.1512 0.0185  -0.0100 0.0074  51  GLY   B C   
3532 O O   . GLY   B 51  ? 0.1383 0.1482 0.1751 0.0126  -0.0087 0.0003  51  GLY   B O   
3536 N N   . ALA   B 52  ? 0.1392 0.1341 0.1495 0.0134  -0.0055 0.0107  52  ALA   B N   
3537 C CA  . ALA   B 52  ? 0.1428 0.1405 0.1484 0.0192  0.0012  -0.0011 52  ALA   B CA  
3538 C C   . ALA   B 52  ? 0.1352 0.1398 0.1429 0.0138  0.0075  0.0015  52  ALA   B C   
3539 O O   . ALA   B 52  ? 0.1418 0.1451 0.1544 0.0145  0.0077  0.0023  52  ALA   B O   
3540 C CB  . ALA   B 52  ? 0.1643 0.1462 0.1536 0.0058  0.0147  -0.0032 52  ALA   B CB  
3546 N N   . LEU   B 53  ? 0.1299 0.1356 0.1334 0.0165  0.0064  0.0020  53  LEU   B N   
3547 C CA  . LEU   B 53  ? 0.1300 0.1439 0.1336 0.0126  -0.0008 0.0083  53  LEU   B CA  
3548 C C   . LEU   B 53  ? 0.1361 0.1388 0.1361 0.0096  0.0051  0.0094  53  LEU   B C   
3549 O O   . LEU   B 53  ? 0.1380 0.1526 0.1496 0.0015  0.0042  0.0184  53  LEU   B O   
3550 C CB  . LEU   B 53  ? 0.1350 0.1489 0.1400 0.0090  0.0027  0.0178  53  LEU   B CB  
3551 C CG  . LEU   B 53  ? 0.1319 0.1615 0.1472 0.0054  -0.0027 0.0194  53  LEU   B CG  
3552 C CD1 . LEU   B 53  ? 0.1379 0.1838 0.1684 0.0149  -0.0070 0.0076  53  LEU   B CD1 
3553 C CD2 . LEU   B 53  ? 0.1464 0.1896 0.1735 -0.0095 -0.0116 -0.0093 53  LEU   B CD2 
3565 N N   . ASN   B 54  ? 0.1307 0.1328 0.1310 0.0052  0.0011  0.0099  54  ASN   B N   
3566 C CA  . ASN   B 54  ? 0.1358 0.1431 0.1432 0.0036  -0.0006 0.0012  54  ASN   B CA  
3567 C C   . ASN   B 54  ? 0.1370 0.1441 0.1488 0.0051  0.0017  0.0056  54  ASN   B C   
3568 O O   . ASN   B 54  ? 0.1360 0.1526 0.1611 -0.0013 0.0086  0.0010  54  ASN   B O   
3569 C CB  . ASN   B 54  ? 0.1415 0.1520 0.1521 0.0030  0.0039  0.0017  54  ASN   B CB  
3570 C CG  . ASN   B 54  ? 0.1376 0.1643 0.1534 0.0006  -0.0020 0.0001  54  ASN   B CG  
3571 O OD1 . ASN   B 54  ? 0.1312 0.1615 0.1586 -0.0051 -0.0083 -0.0120 54  ASN   B OD1 
3572 N ND2 . ASN   B 54  ? 0.1481 0.1813 0.1735 0.0020  -0.0259 0.0114  54  ASN   B ND2 
3579 N N   . LYS   B 55  ? 0.1346 0.1514 0.1687 0.0102  -0.0011 0.0032  55  LYS   B N   
3580 C CA  . LYS   B 55  ? 0.1439 0.1640 0.1837 0.0187  -0.0027 0.0068  55  LYS   B CA  
3581 C C   . LYS   B 55  ? 0.1357 0.1606 0.1780 0.0159  0.0027  -0.0014 55  LYS   B C   
3582 O O   . LYS   B 55  ? 0.1287 0.1738 0.1956 0.0143  0.0046  -0.0052 55  LYS   B O   
3583 C CB  . LYS   B 55  ? 0.1556 0.1701 0.2193 0.0299  0.0081  0.0199  55  LYS   B CB  
3584 C CG  . LYS   B 55  ? 0.1910 0.1968 0.2964 0.0343  0.0261  0.0296  55  LYS   B CG  
3585 C CD  . LYS   B 55  ? 0.2272 0.2195 0.3609 0.0423  0.0434  0.0369  55  LYS   B CD  
3586 C CE  . LYS   B 55  ? 0.2540 0.2398 0.4217 0.0431  0.0565  0.0347  55  LYS   B CE  
3587 N NZ  . LYS   B 55  ? 0.2586 0.2504 0.4516 0.0451  0.0489  0.0379  55  LYS   B NZ  
3601 N N   . ALA   B 56  ? 0.1328 0.1707 0.1603 0.0092  0.0043  -0.0054 56  ALA   B N   
3602 C CA  . ALA   B 56  ? 0.1498 0.1805 0.1608 0.0046  0.0064  -0.0035 56  ALA   B CA  
3603 C C   . ALA   B 56  ? 0.1450 0.1731 0.1582 0.0049  0.0135  0.0035  56  ALA   B C   
3604 O O   . ALA   B 56  ? 0.1604 0.1868 0.1727 0.0066  0.0265  0.0071  56  ALA   B O   
3605 C CB  . ALA   B 56  ? 0.1642 0.2027 0.1699 -0.0099 0.0068  -0.0076 56  ALA   B CB  
3611 N N   . THR   B 57  ? 0.1423 0.1648 0.1669 0.0083  0.0156  0.0086  57  THR   B N   
3612 C CA  . THR   B 57  ? 0.1447 0.1649 0.1643 0.0016  0.0202  0.0175  57  THR   B CA  
3613 C C   . THR   B 57  ? 0.1482 0.1736 0.1865 -0.0006 0.0246  0.0115  57  THR   B C   
3614 O O   . THR   B 57  ? 0.1558 0.1725 0.1952 -0.0124 0.0199  0.0071  57  THR   B O   
3615 C CB  . THR   B 57  ? 0.1501 0.1562 0.1498 0.0042  0.0197  0.0211  57  THR   B CB  
3616 O OG1 . THR   B 57  ? 0.1471 0.1488 0.1658 0.0059  0.0165  0.0109  57  THR   B OG1 
3617 C CG2 . THR   B 57  ? 0.1452 0.1660 0.1564 0.0042  0.0148  0.0191  57  THR   B CG2 
3625 N N   . ASN   B 58  ? 0.1330 0.1906 0.2077 -0.0123 0.0083  -0.0033 58  ASN   B N   
3626 C CA  . ASN   B 58  ? 0.1533 0.2317 0.2410 -0.0205 0.0320  -0.0008 58  ASN   B CA  
3627 C C   . ASN   B 58  ? 0.1356 0.2133 0.2074 -0.0158 0.0034  0.0009  58  ASN   B C   
3628 O O   . ASN   B 58  ? 0.1412 0.2230 0.2152 -0.0162 0.0056  -0.0046 58  ASN   B O   
3629 C CB  . ASN   B 58  ? 0.2363 0.3006 0.3485 -0.0298 0.0596  0.0045  58  ASN   B CB  
3630 C CG  . ASN   B 58  ? 0.3354 0.3673 0.4836 -0.0334 0.0689  0.0220  58  ASN   B CG  
3631 O OD1 . ASN   B 58  ? 0.3620 0.3850 0.5312 -0.0357 0.0707  0.0278  58  ASN   B OD1 
3632 N ND2 . ASN   B 58  ? 0.3950 0.3950 0.5296 -0.0362 0.0724  0.0244  58  ASN   B ND2 
3639 N N   . ASN   B 59  ? 0.1300 0.1930 0.1902 -0.0090 0.0047  0.0136  59  ASN   B N   
3640 C CA  . ASN   B 59  ? 0.1319 0.1951 0.1864 -0.0095 -0.0073 0.0203  59  ASN   B CA  
3641 C C   . ASN   B 59  ? 0.1286 0.1856 0.1721 -0.0115 -0.0131 0.0048  59  ASN   B C   
3642 O O   . ASN   B 59  ? 0.1368 0.1858 0.1770 -0.0106 -0.0112 0.0038  59  ASN   B O   
3643 C CB  . ASN   B 59  ? 0.1447 0.2141 0.1981 -0.0019 -0.0227 0.0160  59  ASN   B CB  
3644 C CG  . ASN   B 59  ? 0.1583 0.2305 0.2090 0.0012  -0.0352 0.0159  59  ASN   B CG  
3645 O OD1 . ASN   B 59  ? 0.1667 0.2368 0.2108 0.0003  -0.0236 0.0257  59  ASN   B OD1 
3646 N ND2 . ASN   B 59  ? 0.1619 0.2388 0.2187 -0.0099 -0.0339 0.0059  59  ASN   B ND2 
3653 N N   . ALA   B 60  ? 0.1373 0.1725 0.1699 -0.0081 -0.0005 0.0029  60  ALA   B N   
3654 C CA  . ALA   B 60  ? 0.1472 0.1604 0.1726 -0.0164 -0.0045 0.0058  60  ALA   B CA  
3655 C C   . ALA   B 60  ? 0.1421 0.1527 0.1583 -0.0107 -0.0078 0.0116  60  ALA   B C   
3656 O O   . ALA   B 60  ? 0.1481 0.1582 0.1693 -0.0150 -0.0019 -0.0024 60  ALA   B O   
3657 C CB  . ALA   B 60  ? 0.1636 0.1590 0.1915 -0.0163 0.0055  0.0085  60  ALA   B CB  
3663 N N   . MET   B 61  ? 0.1333 0.1465 0.1583 -0.0055 -0.0028 0.0104  61  MET   B N   
3664 C CA  . MET   B 61  ? 0.1303 0.1438 0.1573 -0.0044 -0.0112 0.0058  61  MET   B CA  
3665 C C   . MET   B 61  ? 0.1419 0.1385 0.1506 -0.0083 -0.0127 0.0071  61  MET   B C   
3666 O O   . MET   B 61  ? 0.1465 0.1399 0.1427 -0.0002 -0.0034 -0.0088 61  MET   B O   
3667 C CB  . MET   B 61  ? 0.1278 0.1444 0.1431 0.0029  -0.0074 -0.0009 61  MET   B CB  
3668 C CG  . MET   B 61  ? 0.1327 0.1470 0.1397 -0.0001 -0.0080 0.0023  61  MET   B CG  
3669 S SD  . MET   B 61  ? 0.1340 0.1482 0.1700 -0.0015 -0.0041 -0.0103 61  MET   B SD  
3670 C CE  . MET   B 61  ? 0.1390 0.1678 0.1900 -0.0022 -0.0020 -0.0237 61  MET   B CE  
3680 N N   . GLN   B 62  ? 0.1407 0.1432 0.1423 -0.0007 -0.0137 0.0091  62  GLN   B N   
3681 C CA  . GLN   B 62  ? 0.1404 0.1491 0.1512 0.0005  -0.0133 0.0007  62  GLN   B CA  
3682 C C   . GLN   B 62  ? 0.1393 0.1575 0.1538 -0.0014 -0.0220 -0.0063 62  GLN   B C   
3683 O O   . GLN   B 62  ? 0.1542 0.1528 0.1540 -0.0013 -0.0255 -0.0126 62  GLN   B O   
3684 C CB  . GLN   B 62  ? 0.1411 0.1538 0.1514 0.0010  -0.0136 0.0066  62  GLN   B CB  
3685 C CG  . GLN   B 62  ? 0.1400 0.1667 0.1524 0.0016  -0.0216 -0.0001 62  GLN   B CG  
3686 C CD  . GLN   B 62  ? 0.1441 0.1574 0.1462 0.0087  -0.0243 0.0089  62  GLN   B CD  
3687 O OE1 . GLN   B 62  ? 0.1473 0.1536 0.1658 0.0008  -0.0229 -0.0068 62  GLN   B OE1 
3688 N NE2 . GLN   B 62  ? 0.1472 0.1595 0.1599 0.0031  -0.0208 -0.0087 62  GLN   B NE2 
3697 N N   . VAL   B 63  ? 0.1384 0.1610 0.1720 -0.0080 -0.0155 -0.0105 63  VAL   B N   
3698 C CA  . VAL   B 63  ? 0.1503 0.1631 0.1857 -0.0130 -0.0245 -0.0065 63  VAL   B CA  
3699 C C   . VAL   B 63  ? 0.1519 0.1491 0.1758 -0.0137 -0.0225 -0.0093 63  VAL   B C   
3700 O O   . VAL   B 63  ? 0.1591 0.1487 0.1901 -0.0093 -0.0308 -0.0104 63  VAL   B O   
3701 C CB  . VAL   B 63  ? 0.1554 0.1746 0.2213 -0.0188 -0.0247 -0.0080 63  VAL   B CB  
3702 C CG1 . VAL   B 63  ? 0.1650 0.1789 0.2309 -0.0277 -0.0229 -0.0065 63  VAL   B CG1 
3703 C CG2 . VAL   B 63  ? 0.1512 0.1883 0.2418 -0.0138 -0.0267 -0.0106 63  VAL   B CG2 
3713 N N   . GLU   B 64  ? 0.1535 0.1397 0.1713 -0.0051 -0.0184 -0.0062 64  GLU   B N   
3714 C CA  . GLU   B 64  ? 0.1496 0.1367 0.1638 -0.0075 -0.0265 -0.0066 64  GLU   B CA  
3715 C C   . GLU   B 64  ? 0.1450 0.1363 0.1565 -0.0033 -0.0282 -0.0165 64  GLU   B C   
3716 O O   . GLU   B 64  ? 0.1565 0.1471 0.1551 -0.0107 -0.0232 -0.0136 64  GLU   B O   
3717 C CB  . GLU   B 64  ? 0.1515 0.1477 0.1586 -0.0108 -0.0238 0.0002  64  GLU   B CB  
3718 C CG  . GLU   B 64  ? 0.1556 0.1528 0.1590 -0.0220 -0.0227 -0.0120 64  GLU   B CG  
3719 C CD  . GLU   B 64  ? 0.1620 0.1705 0.1676 -0.0300 -0.0269 -0.0183 64  GLU   B CD  
3720 O OE1 . GLU   B 64  ? 0.1702 0.1921 0.1819 -0.0342 -0.0240 -0.0374 64  GLU   B OE1 
3721 O OE2 . GLU   B 64  ? 0.1771 0.1825 0.1734 -0.0292 -0.0394 -0.0106 64  GLU   B OE2 
3728 N N   . SER   B 65  ? 0.1441 0.1354 0.1510 -0.0048 -0.0131 -0.0167 65  SER   B N   
3729 C CA  . SER   B 65  ? 0.1424 0.1345 0.1524 -0.0005 -0.0128 -0.0123 65  SER   B CA  
3730 C C   . SER   B 65  ? 0.1458 0.1361 0.1516 -0.0022 -0.0184 -0.0144 65  SER   B C   
3731 O O   . SER   B 65  ? 0.1533 0.1440 0.1515 -0.0000 -0.0210 -0.0255 65  SER   B O   
3732 C CB  . SER   B 65  ? 0.1480 0.1388 0.1488 -0.0092 -0.0130 -0.0125 65  SER   B CB  
3733 O OG  . SER   B 65  ? 0.1521 0.1409 0.1576 -0.0089 -0.0121 -0.0209 65  SER   B OG  
3739 N N   . ASP   B 66  ? 0.1565 0.1429 0.1492 -0.0004 -0.0213 -0.0162 66  ASP   B N   
3740 C CA  . ASP   B 66  ? 0.1658 0.1532 0.1436 -0.0009 -0.0297 -0.0117 66  ASP   B CA  
3741 C C   . ASP   B 66  ? 0.1670 0.1584 0.1407 -0.0063 -0.0287 -0.0172 66  ASP   B C   
3742 O O   . ASP   B 66  ? 0.1709 0.1611 0.1608 0.0038  -0.0296 -0.0273 66  ASP   B O   
3743 C CB  . ASP   B 66  ? 0.1842 0.1692 0.1670 0.0107  -0.0421 -0.0154 66  ASP   B CB  
3744 C CG  . ASP   B 66  ? 0.2090 0.1878 0.1959 0.0194  -0.0586 -0.0002 66  ASP   B CG  
3745 O OD1 . ASP   B 66  ? 0.2287 0.1802 0.2036 0.0140  -0.0541 0.0025  66  ASP   B OD1 
3746 O OD2 . ASP   B 66  ? 0.2239 0.2124 0.2457 0.0370  -0.0554 -0.0047 66  ASP   B OD2 
3751 N N   . ASP   B 67  ? 0.1624 0.1503 0.1474 -0.0072 -0.0231 -0.0185 67  ASP   B N   
3752 C CA  . ASP   B 67  ? 0.1757 0.1465 0.1613 -0.0122 -0.0196 -0.0181 67  ASP   B CA  
3753 C C   . ASP   B 67  ? 0.1716 0.1416 0.1631 -0.0008 -0.0183 -0.0207 67  ASP   B C   
3754 O O   . ASP   B 67  ? 0.1778 0.1475 0.1721 -0.0010 -0.0135 -0.0253 67  ASP   B O   
3755 C CB  . ASP   B 67  ? 0.2016 0.1564 0.1760 -0.0192 -0.0310 -0.0098 67  ASP   B CB  
3756 C CG  . ASP   B 67  ? 0.2365 0.1644 0.1875 -0.0132 -0.0542 -0.0125 67  ASP   B CG  
3757 O OD1 . ASP   B 67  ? 0.2547 0.1688 0.2020 -0.0155 -0.0566 -0.0099 67  ASP   B OD1 
3758 O OD2 . ASP   B 67  ? 0.2534 0.1701 0.2102 -0.0006 -0.0674 -0.0065 67  ASP   B OD2 
3763 N N   . TYR   B 68  ? 0.1651 0.1461 0.1512 -0.0008 -0.0301 -0.0214 68  TYR   B N   
3764 C CA  . TYR   B 68  ? 0.1613 0.1589 0.1646 0.0048  -0.0333 -0.0329 68  TYR   B CA  
3765 C C   . TYR   B 68  ? 0.1526 0.1581 0.1574 0.0016  -0.0308 -0.0405 68  TYR   B C   
3766 O O   . TYR   B 68  ? 0.1568 0.1664 0.1673 0.0043  -0.0280 -0.0518 68  TYR   B O   
3767 C CB  . TYR   B 68  ? 0.1655 0.1793 0.1744 0.0088  -0.0373 -0.0437 68  TYR   B CB  
3768 C CG  . TYR   B 68  ? 0.1752 0.1938 0.1845 0.0129  -0.0266 -0.0622 68  TYR   B CG  
3769 C CD1 . TYR   B 68  ? 0.1763 0.1980 0.2102 -0.0065 -0.0294 -0.0714 68  TYR   B CD1 
3770 C CD2 . TYR   B 68  ? 0.1804 0.2123 0.2035 0.0212  -0.0367 -0.0571 68  TYR   B CD2 
3771 C CE1 . TYR   B 68  ? 0.1820 0.2164 0.2342 -0.0042 -0.0305 -0.0667 68  TYR   B CE1 
3772 C CE2 . TYR   B 68  ? 0.1839 0.2180 0.2140 0.0190  -0.0298 -0.0649 68  TYR   B CE2 
3773 C CZ  . TYR   B 68  ? 0.1772 0.2220 0.2307 0.0017  -0.0336 -0.0705 68  TYR   B CZ  
3774 O OH  . TYR   B 68  ? 0.1728 0.2381 0.2523 0.0012  -0.0362 -0.0601 68  TYR   B OH  
3784 N N   . ILE   B 69  ? 0.1552 0.1456 0.1581 0.0018  -0.0249 -0.0323 69  ILE   B N   
3785 C CA  . ILE   B 69  ? 0.1648 0.1521 0.1638 -0.0015 -0.0184 -0.0429 69  ILE   B CA  
3786 C C   . ILE   B 69  ? 0.1637 0.1502 0.1576 0.0076  -0.0285 -0.0297 69  ILE   B C   
3787 O O   . ILE   B 69  ? 0.1674 0.1644 0.1556 0.0037  -0.0197 -0.0340 69  ILE   B O   
3788 C CB  . ILE   B 69  ? 0.1727 0.1619 0.1834 -0.0028 0.0015  -0.0337 69  ILE   B CB  
3789 C CG1 . ILE   B 69  ? 0.1731 0.1670 0.1891 -0.0081 0.0025  -0.0347 69  ILE   B CG1 
3790 C CG2 . ILE   B 69  ? 0.1877 0.1692 0.2036 -0.0005 0.0060  -0.0257 69  ILE   B CG2 
3791 C CD1 . ILE   B 69  ? 0.1635 0.1708 0.1946 -0.0212 0.0036  -0.0333 69  ILE   B CD1 
3803 N N   . ALA   B 70  ? 0.1618 0.1532 0.1581 0.0071  -0.0394 -0.0263 70  ALA   B N   
3804 C CA  . ALA   B 70  ? 0.1675 0.1600 0.1464 0.0036  -0.0360 -0.0254 70  ALA   B CA  
3805 C C   . ALA   B 70  ? 0.1719 0.1552 0.1555 -0.0000 -0.0410 -0.0301 70  ALA   B C   
3806 O O   . ALA   B 70  ? 0.1806 0.1577 0.1581 0.0029  -0.0351 -0.0382 70  ALA   B O   
3807 C CB  . ALA   B 70  ? 0.1719 0.1794 0.1545 -0.0012 -0.0385 -0.0261 70  ALA   B CB  
3813 N N   . THR   B 71  ? 0.1758 0.1553 0.1713 0.0019  -0.0505 -0.0336 71  THR   B N   
3814 C CA  . THR   B 71  ? 0.1874 0.1589 0.1919 0.0087  -0.0646 -0.0316 71  THR   B CA  
3815 C C   . THR   B 71  ? 0.1825 0.1632 0.2094 0.0236  -0.0582 -0.0523 71  THR   B C   
3816 O O   . THR   B 71  ? 0.1976 0.1702 0.2543 0.0268  -0.0528 -0.0693 71  THR   B O   
3817 C CB  . THR   B 71  ? 0.2165 0.1800 0.2204 -0.0025 -0.0729 -0.0074 71  THR   B CB  
3818 O OG1 . THR   B 71  ? 0.2338 0.2054 0.2497 -0.0207 -0.0666 0.0177  71  THR   B OG1 
3819 C CG2 . THR   B 71  ? 0.2335 0.1797 0.2477 0.0010  -0.0644 0.0061  71  THR   B CG2 
3827 N N   . ASN   B 72  ? 0.1689 0.1653 0.2093 0.0132  -0.0530 -0.0678 72  ASN   B N   
3828 C CA  . ASN   B 72  ? 0.1719 0.1790 0.2060 0.0137  -0.0440 -0.0701 72  ASN   B CA  
3829 C C   . ASN   B 72  ? 0.1731 0.1902 0.2094 -0.0022 -0.0218 -0.0729 72  ASN   B C   
3830 O O   . ASN   B 72  ? 0.1713 0.2069 0.2353 0.0026  -0.0104 -0.0700 72  ASN   B O   
3831 C CB  . ASN   B 72  ? 0.1792 0.1922 0.2181 0.0132  -0.0538 -0.0614 72  ASN   B CB  
3832 C CG  . ASN   B 72  ? 0.1931 0.2071 0.2260 0.0287  -0.0657 -0.0373 72  ASN   B CG  
3833 O OD1 . ASN   B 72  ? 0.2184 0.2249 0.2368 0.0210  -0.0440 -0.0419 72  ASN   B OD1 
3834 N ND2 . ASN   B 72  ? 0.2077 0.2142 0.2664 0.0427  -0.0506 -0.0019 72  ASN   B ND2 
3841 N N   . GLY   B 73  ? 0.1762 0.1906 0.1870 -0.0022 -0.0246 -0.0658 73  GLY   B N   
3842 C CA  . GLY   B 73  ? 0.1718 0.1985 0.1659 -0.0041 -0.0228 -0.0498 73  GLY   B CA  
3843 C C   . GLY   B 73  ? 0.1671 0.1955 0.1277 0.0048  -0.0184 -0.0496 73  GLY   B C   
3844 O O   . GLY   B 73  ? 0.1635 0.1833 0.1433 0.0064  -0.0178 -0.0344 73  GLY   B O   
3848 N N   . PRO   B 74  ? 0.1665 0.2049 0.1241 0.0038  -0.0249 -0.0387 74  PRO   B N   
3849 C CA  . PRO   B 74  ? 0.1640 0.2044 0.1167 0.0089  -0.0176 -0.0285 74  PRO   B CA  
3850 C C   . PRO   B 74  ? 0.1514 0.1882 0.1268 0.0073  -0.0182 -0.0247 74  PRO   B C   
3851 O O   . PRO   B 74  ? 0.1566 0.1904 0.1606 0.0094  -0.0125 -0.0346 74  PRO   B O   
3852 C CB  . PRO   B 74  ? 0.1809 0.2250 0.1203 0.0075  -0.0194 -0.0224 74  PRO   B CB  
3853 C CG  . PRO   B 74  ? 0.1946 0.2331 0.1551 0.0050  -0.0144 -0.0204 74  PRO   B CG  
3854 C CD  . PRO   B 74  ? 0.1892 0.2235 0.1451 0.0064  -0.0157 -0.0332 74  PRO   B CD  
3862 N N   . LEU   B 75  ? 0.1450 0.1766 0.1102 0.0095  -0.0154 -0.0271 75  LEU   B N   
3863 C CA  . LEU   B 75  ? 0.1476 0.1743 0.1165 0.0036  -0.0150 -0.0108 75  LEU   B CA  
3864 C C   . LEU   B 75  ? 0.1540 0.1813 0.1210 0.0028  -0.0068 -0.0103 75  LEU   B C   
3865 O O   . LEU   B 75  ? 0.1728 0.1960 0.1308 -0.0014 -0.0088 -0.0032 75  LEU   B O   
3866 C CB  . LEU   B 75  ? 0.1585 0.1806 0.1065 -0.0065 -0.0194 0.0040  75  LEU   B CB  
3867 C CG  . LEU   B 75  ? 0.1905 0.1968 0.1319 -0.0267 -0.0065 -0.0013 75  LEU   B CG  
3868 C CD1 . LEU   B 75  ? 0.2227 0.2130 0.1358 -0.0333 0.0129  -0.0058 75  LEU   B CD1 
3869 C CD2 . LEU   B 75  ? 0.2217 0.2154 0.1996 -0.0195 0.0023  0.0021  75  LEU   B CD2 
3881 N N   . LYS   B 76  ? 0.1497 0.2007 0.1451 0.0016  -0.0006 -0.0067 76  LYS   B N   
3882 C CA  . LYS   B 76  ? 0.1615 0.2079 0.1739 -0.0059 0.0210  -0.0126 76  LYS   B CA  
3883 C C   . LYS   B 76  ? 0.1552 0.1885 0.1375 0.0057  0.0064  0.0035  76  LYS   B C   
3884 O O   . LYS   B 76  ? 0.1589 0.1742 0.1386 0.0028  0.0020  0.0054  76  LYS   B O   
3885 C CB  . LYS   B 76  ? 0.1846 0.2210 0.2506 -0.0096 0.0455  -0.0484 76  LYS   B CB  
3886 C CG  . LYS   B 76  ? 0.2031 0.2390 0.3089 0.0006  0.0330  -0.0572 76  LYS   B CG  
3887 C CD  . LYS   B 76  ? 0.2052 0.2482 0.3565 0.0084  0.0185  -0.0742 76  LYS   B CD  
3888 C CE  . LYS   B 76  ? 0.2094 0.2633 0.4104 0.0109  0.0040  -0.0834 76  LYS   B CE  
3889 N NZ  . LYS   B 76  ? 0.2077 0.2692 0.4315 0.0132  -0.0135 -0.0990 76  LYS   B NZ  
3903 N N   . VAL   B 77  ? 0.1635 0.1981 0.1381 0.0169  0.0063  0.0114  77  VAL   B N   
3904 C CA  . VAL   B 77  ? 0.1668 0.1890 0.1493 0.0194  0.0188  0.0299  77  VAL   B CA  
3905 C C   . VAL   B 77  ? 0.1539 0.1702 0.1329 0.0200  0.0158  0.0214  77  VAL   B C   
3906 O O   . VAL   B 77  ? 0.1570 0.1693 0.1396 0.0272  0.0254  0.0169  77  VAL   B O   
3907 C CB  . VAL   B 77  ? 0.1763 0.1979 0.1783 0.0181  0.0287  0.0463  77  VAL   B CB  
3908 C CG1 . VAL   B 77  ? 0.1852 0.1837 0.2093 0.0111  0.0325  0.0626  77  VAL   B CG1 
3909 C CG2 . VAL   B 77  ? 0.1893 0.2190 0.1993 0.0164  0.0153  0.0501  77  VAL   B CG2 
3919 N N   . GLY   B 78  ? 0.1505 0.1622 0.1235 0.0150  0.0158  0.0158  78  GLY   B N   
3920 C CA  . GLY   B 78  ? 0.1472 0.1548 0.1187 0.0145  0.0170  0.0079  78  GLY   B CA  
3921 C C   . GLY   B 78  ? 0.1448 0.1514 0.1165 0.0139  0.0114  0.0088  78  GLY   B C   
3922 O O   . GLY   B 78  ? 0.1520 0.1507 0.1267 0.0187  0.0182  0.0105  78  GLY   B O   
3926 N N   . GLY   B 79  ? 0.1393 0.1580 0.1242 0.0106  0.0112  0.0064  79  GLY   B N   
3927 C CA  . GLY   B 79  ? 0.1360 0.1501 0.1265 0.0129  0.0096  0.0039  79  GLY   B CA  
3928 C C   . GLY   B 79  ? 0.1299 0.1390 0.1286 0.0138  0.0087  -0.0006 79  GLY   B C   
3929 O O   . GLY   B 79  ? 0.1406 0.1371 0.1335 0.0120  0.0180  0.0138  79  GLY   B O   
3933 N N   . SER   B 80  ? 0.1311 0.1296 0.1384 0.0093  0.0162  -0.0022 80  SER   B N   
3934 C CA  . SER   B 80  ? 0.1295 0.1298 0.1417 0.0057  0.0105  0.0001  80  SER   B CA  
3935 C C   . SER   B 80  ? 0.1306 0.1280 0.1418 0.0094  -0.0008 -0.0039 80  SER   B C   
3936 O O   . SER   B 80  ? 0.1445 0.1282 0.1731 0.0126  0.0056  -0.0112 80  SER   B O   
3937 C CB  . SER   B 80  ? 0.1373 0.1373 0.1438 -0.0020 0.0039  0.0036  80  SER   B CB  
3938 O OG  . SER   B 80  ? 0.1443 0.1533 0.1685 0.0012  -0.0165 0.0110  80  SER   B OG  
3944 N N   . CYS   B 81  ? 0.1290 0.1175 0.1373 0.0038  -0.0014 -0.0087 81  CYS   B N   
3945 C CA  . CYS   B 81  ? 0.1368 0.1165 0.1385 0.0057  -0.0074 -0.0093 81  CYS   B CA  
3946 C C   . CYS   B 81  ? 0.1345 0.1146 0.1152 0.0019  -0.0093 -0.0063 81  CYS   B C   
3947 O O   . CYS   B 81  ? 0.1591 0.1187 0.1325 0.0109  -0.0030 -0.0101 81  CYS   B O   
3948 C CB  . CYS   B 81  ? 0.1492 0.1307 0.1453 -0.0034 -0.0104 -0.0083 81  CYS   B CB  
3949 S SG  . CYS   B 81  ? 0.1506 0.1489 0.1366 -0.0031 -0.0245 -0.0113 81  CYS   B SG  
3955 N N   . VAL   B 82  ? 0.1369 0.1130 0.1307 0.0028  -0.0095 -0.0049 82  VAL   B N   
3956 C CA  . VAL   B 82  ? 0.1412 0.1196 0.1269 -0.0019 -0.0084 -0.0026 82  VAL   B CA  
3957 C C   . VAL   B 82  ? 0.1492 0.1111 0.1385 0.0022  -0.0067 -0.0012 82  VAL   B C   
3958 O O   . VAL   B 82  ? 0.1589 0.1124 0.1716 -0.0005 -0.0059 -0.0171 82  VAL   B O   
3959 C CB  . VAL   B 82  ? 0.1519 0.1375 0.1509 0.0031  -0.0112 0.0032  82  VAL   B CB  
3960 C CG1 . VAL   B 82  ? 0.1695 0.1604 0.1603 0.0073  -0.0097 0.0201  82  VAL   B CG1 
3961 C CG2 . VAL   B 82  ? 0.1620 0.1531 0.1620 -0.0010 -0.0234 0.0057  82  VAL   B CG2 
3971 N N   . LEU   B 83  ? 0.1377 0.1135 0.1324 -0.0119 -0.0177 -0.0074 83  LEU   B N   
3972 C CA  . LEU   B 83  ? 0.1396 0.1210 0.1214 -0.0088 -0.0157 -0.0074 83  LEU   B CA  
3973 C C   . LEU   B 83  ? 0.1376 0.1209 0.1247 -0.0121 -0.0168 -0.0016 83  LEU   B C   
3974 O O   . LEU   B 83  ? 0.1419 0.1278 0.1177 -0.0138 -0.0118 0.0005  83  LEU   B O   
3975 C CB  . LEU   B 83  ? 0.1467 0.1339 0.1314 -0.0127 -0.0175 -0.0152 83  LEU   B CB  
3976 C CG  . LEU   B 83  ? 0.1644 0.1556 0.1417 -0.0134 -0.0099 -0.0108 83  LEU   B CG  
3977 C CD1 . LEU   B 83  ? 0.1755 0.1639 0.1421 -0.0137 -0.0212 -0.0075 83  LEU   B CD1 
3978 C CD2 . LEU   B 83  ? 0.1788 0.1577 0.1558 -0.0049 -0.0082 -0.0215 83  LEU   B CD2 
3990 N N   . SER   B 84  ? 0.1385 0.1328 0.1498 -0.0216 -0.0116 0.0024  84  SER   B N   
3991 C CA  . SER   B 84  ? 0.1443 0.1502 0.1424 -0.0226 -0.0111 0.0148  84  SER   B CA  
3992 C C   . SER   B 84  ? 0.1364 0.1670 0.1132 -0.0185 -0.0142 0.0199  84  SER   B C   
3993 O O   . SER   B 84  ? 0.1504 0.1518 0.1108 -0.0170 -0.0099 0.0017  84  SER   B O   
3994 C CB  . SER   B 84  ? 0.1631 0.1548 0.1920 -0.0284 0.0163  0.0132  84  SER   B CB  
3995 O OG  . SER   B 84  ? 0.1685 0.1683 0.2413 -0.0333 0.0170  0.0209  84  SER   B OG  
4001 N N   . GLY   B 85  ? 0.1380 0.1881 0.1316 -0.0241 -0.0107 0.0218  85  GLY   B N   
4002 C CA  . GLY   B 85  ? 0.1391 0.1971 0.1445 -0.0311 0.0058  -0.0021 85  GLY   B CA  
4003 C C   . GLY   B 85  ? 0.1397 0.1773 0.1306 -0.0420 0.0034  0.0040  85  GLY   B C   
4004 O O   . GLY   B 85  ? 0.1504 0.1796 0.1332 -0.0555 0.0175  -0.0098 85  GLY   B O   
4008 N N   . HIS   B 86  ? 0.1391 0.1613 0.1404 -0.0284 -0.0143 0.0160  86  HIS   B N   
4009 C CA  . HIS   B 86  ? 0.1398 0.1599 0.1435 -0.0300 -0.0178 0.0200  86  HIS   B CA  
4010 C C   . HIS   B 86  ? 0.1425 0.1676 0.1282 -0.0379 -0.0089 0.0331  86  HIS   B C   
4011 O O   . HIS   B 86  ? 0.1600 0.1758 0.1344 -0.0321 0.0058  0.0278  86  HIS   B O   
4012 C CB  . HIS   B 86  ? 0.1460 0.1619 0.1437 -0.0193 -0.0241 0.0105  86  HIS   B CB  
4013 C CG  . HIS   B 86  ? 0.1527 0.1707 0.1411 -0.0093 -0.0220 0.0130  86  HIS   B CG  
4014 N ND1 . HIS   B 86  ? 0.1686 0.1908 0.1603 -0.0185 -0.0275 -0.0065 86  HIS   B ND1 
4015 C CD2 . HIS   B 86  ? 0.1568 0.1731 0.1450 -0.0076 -0.0207 0.0111  86  HIS   B CD2 
4016 C CE1 . HIS   B 86  ? 0.1725 0.1886 0.1553 -0.0122 -0.0112 -0.0178 86  HIS   B CE1 
4017 N NE2 . HIS   B 86  ? 0.1670 0.1792 0.1388 0.0022  -0.0138 -0.0017 86  HIS   B NE2 
4025 N N   . ASN   B 87  ? 0.1433 0.1711 0.1412 -0.0324 -0.0062 0.0304  87  ASN   B N   
4026 C CA  . ASN   B 87  ? 0.1449 0.1853 0.1502 -0.0297 0.0192  0.0202  87  ASN   B CA  
4027 C C   . ASN   B 87  ? 0.1581 0.1711 0.1322 -0.0279 0.0256  0.0131  87  ASN   B C   
4028 O O   . ASN   B 87  ? 0.1813 0.1816 0.1678 -0.0270 0.0435  0.0093  87  ASN   B O   
4029 C CB  . ASN   B 87  ? 0.1463 0.2181 0.1777 -0.0245 0.0274  0.0171  87  ASN   B CB  
4030 C CG  . ASN   B 87  ? 0.1544 0.2347 0.1890 0.0076  0.0299  0.0317  87  ASN   B CG  
4031 O OD1 . ASN   B 87  ? 0.1524 0.2218 0.1758 0.0134  0.0417  0.0537  87  ASN   B OD1 
4032 N ND2 . ASN   B 87  ? 0.1879 0.2467 0.2190 0.0124  0.0358  0.0280  87  ASN   B ND2 
4039 N N   . LEU   B 88  ? 0.1495 0.1619 0.1208 -0.0312 0.0142  0.0090  88  LEU   B N   
4040 C CA  . LEU   B 88  ? 0.1585 0.1555 0.1296 -0.0285 0.0077  0.0008  88  LEU   B CA  
4041 C C   . LEU   B 88  ? 0.1600 0.1455 0.1266 -0.0350 0.0017  0.0014  88  LEU   B C   
4042 O O   . LEU   B 88  ? 0.1846 0.1582 0.1605 -0.0219 -0.0254 -0.0085 88  LEU   B O   
4043 C CB  . LEU   B 88  ? 0.1671 0.1612 0.1468 -0.0360 -0.0053 0.0148  88  LEU   B CB  
4044 C CG  . LEU   B 88  ? 0.2071 0.1943 0.1716 -0.0292 -0.0259 0.0367  88  LEU   B CG  
4045 C CD1 . LEU   B 88  ? 0.2179 0.2229 0.1894 -0.0418 -0.0207 0.0459  88  LEU   B CD1 
4046 C CD2 . LEU   B 88  ? 0.2416 0.2178 0.2295 0.0025  -0.0493 0.0196  88  LEU   B CD2 
4058 N N   . ALA   B 89  ? 0.1464 0.1427 0.1238 -0.0362 0.0137  0.0014  89  ALA   B N   
4059 C CA  . ALA   B 89  ? 0.1465 0.1419 0.1031 -0.0313 0.0003  0.0108  89  ALA   B CA  
4060 C C   . ALA   B 89  ? 0.1548 0.1434 0.1144 -0.0332 0.0161  0.0049  89  ALA   B C   
4061 O O   . ALA   B 89  ? 0.1384 0.1540 0.1490 -0.0347 0.0153  -0.0270 89  ALA   B O   
4062 C CB  . ALA   B 89  ? 0.1397 0.1411 0.1234 -0.0317 0.0011  0.0187  89  ALA   B CB  
4068 N N   . LYS   B 90  ? 0.1869 0.1350 0.1202 -0.0358 0.0006  0.0081  90  LYS   B N   
4069 C CA  . LYS   B 90  ? 0.2016 0.1307 0.1195 -0.0357 -0.0089 0.0077  90  LYS   B CA  
4070 C C   . LYS   B 90  ? 0.1869 0.1245 0.1339 -0.0400 -0.0064 -0.0059 90  LYS   B C   
4071 O O   . LYS   B 90  ? 0.2011 0.1445 0.1524 -0.0567 -0.0018 0.0023  90  LYS   B O   
4072 C CB  . LYS   B 90  ? 0.2224 0.1397 0.1525 -0.0309 0.0025  0.0165  90  LYS   B CB  
4073 C CG  . LYS   B 90  ? 0.2276 0.1542 0.1655 -0.0207 0.0305  0.0118  90  LYS   B CG  
4074 C CD  . LYS   B 90  ? 0.2516 0.1788 0.2116 -0.0169 0.0447  -0.0076 90  LYS   B CD  
4075 C CE  . LYS   B 90  ? 0.2630 0.1972 0.2572 -0.0221 0.0484  -0.0117 90  LYS   B CE  
4076 N NZ  . LYS   B 90  ? 0.2666 0.1934 0.2592 -0.0281 0.0570  -0.0064 90  LYS   B NZ  
4090 N N   . HIS   B 91  ? 0.1600 0.1163 0.1150 -0.0313 -0.0113 0.0002  91  HIS   B N   
4091 C CA  . HIS   B 91  ? 0.1490 0.1206 0.1195 -0.0225 -0.0110 -0.0035 91  HIS   B CA  
4092 C C   . HIS   B 91  ? 0.1365 0.1215 0.1000 -0.0273 -0.0057 -0.0020 91  HIS   B C   
4093 O O   . HIS   B 91  ? 0.1523 0.1262 0.1089 -0.0221 -0.0132 -0.0007 91  HIS   B O   
4094 C CB  . HIS   B 91  ? 0.1676 0.1213 0.1588 -0.0075 -0.0059 0.0045  91  HIS   B CB  
4095 C CG  . HIS   B 91  ? 0.2129 0.1430 0.2304 0.0053  0.0220  0.0213  91  HIS   B CG  
4096 N ND1 . HIS   B 91  ? 0.2417 0.1540 0.2896 0.0037  0.0298  0.0114  91  HIS   B ND1 
4097 C CD2 . HIS   B 91  ? 0.2298 0.1691 0.2815 0.0230  0.0100  0.0528  91  HIS   B CD2 
4098 C CE1 . HIS   B 91  ? 0.2464 0.1632 0.3070 0.0228  0.0289  0.0245  91  HIS   B CE1 
4099 N NE2 . HIS   B 91  ? 0.2409 0.1743 0.3094 0.0350  0.0231  0.0617  91  HIS   B NE2 
4107 N N   . CYS   B 92  ? 0.1340 0.1193 0.1105 -0.0239 -0.0081 -0.0038 92  CYS   B N   
4108 C CA  . CYS   B 92  ? 0.1292 0.1138 0.1104 -0.0199 -0.0028 -0.0016 92  CYS   B CA  
4109 C C   . CYS   B 92  ? 0.1293 0.1099 0.1008 -0.0099 -0.0066 -0.0022 92  CYS   B C   
4110 O O   . CYS   B 92  ? 0.1355 0.1207 0.1240 -0.0104 -0.0070 -0.0004 92  CYS   B O   
4111 C CB  . CYS   B 92  ? 0.1288 0.1255 0.1220 -0.0112 -0.0022 0.0034  92  CYS   B CB  
4112 S SG  . CYS   B 92  ? 0.1336 0.1296 0.1139 -0.0091 -0.0090 0.0040  92  CYS   B SG  
4118 N N   . LEU   B 93  ? 0.1209 0.1147 0.1045 -0.0114 -0.0019 -0.0035 93  LEU   B N   
4119 C CA  . LEU   B 93  ? 0.1252 0.1127 0.1091 -0.0017 -0.0075 0.0014  93  LEU   B CA  
4120 C C   . LEU   B 93  ? 0.1161 0.1109 0.0990 0.0007  -0.0082 0.0019  93  LEU   B C   
4121 O O   . LEU   B 93  ? 0.1231 0.1125 0.1119 -0.0033 -0.0021 -0.0003 93  LEU   B O   
4122 C CB  . LEU   B 93  ? 0.1251 0.1162 0.1170 -0.0018 -0.0065 -0.0023 93  LEU   B CB  
4123 C CG  . LEU   B 93  ? 0.1240 0.1304 0.1407 -0.0004 -0.0053 0.0106  93  LEU   B CG  
4124 C CD1 . LEU   B 93  ? 0.1294 0.1380 0.1409 0.0096  0.0026  -0.0033 93  LEU   B CD1 
4125 C CD2 . LEU   B 93  ? 0.1194 0.1318 0.1574 -0.0031 -0.0074 0.0039  93  LEU   B CD2 
4137 N N   . HIS   B 94  ? 0.1209 0.1075 0.0988 -0.0051 -0.0105 0.0000  94  HIS   B N   
4138 C CA  . HIS   B 94  ? 0.1206 0.1095 0.1039 0.0014  -0.0025 0.0011  94  HIS   B CA  
4139 C C   . HIS   B 94  ? 0.1189 0.1085 0.1171 -0.0007 -0.0007 0.0049  94  HIS   B C   
4140 O O   . HIS   B 94  ? 0.1229 0.1200 0.1628 -0.0024 0.0201  -0.0115 94  HIS   B O   
4141 C CB  . HIS   B 94  ? 0.1209 0.1200 0.1197 -0.0002 -0.0067 0.0013  94  HIS   B CB  
4142 C CG  . HIS   B 94  ? 0.1289 0.1141 0.1168 -0.0027 -0.0205 0.0035  94  HIS   B CG  
4143 N ND1 . HIS   B 94  ? 0.1315 0.1177 0.1127 -0.0068 -0.0155 -0.0001 94  HIS   B ND1 
4144 C CD2 . HIS   B 94  ? 0.1322 0.1159 0.1255 0.0006  -0.0187 0.0055  94  HIS   B CD2 
4145 C CE1 . HIS   B 94  ? 0.1331 0.1232 0.1204 -0.0094 -0.0211 0.0031  94  HIS   B CE1 
4146 N NE2 . HIS   B 94  ? 0.1256 0.1288 0.1273 -0.0146 -0.0156 0.0033  94  HIS   B NE2 
4154 N N   . VAL   B 95  ? 0.1134 0.1097 0.1239 0.0050  0.0014  0.0019  95  VAL   B N   
4155 C CA  . VAL   B 95  ? 0.1197 0.1157 0.1140 0.0048  0.0046  0.0067  95  VAL   B CA  
4156 C C   . VAL   B 95  ? 0.1259 0.1161 0.1054 0.0038  0.0095  0.0009  95  VAL   B C   
4157 O O   . VAL   B 95  ? 0.1260 0.1167 0.1315 0.0062  0.0090  0.0103  95  VAL   B O   
4158 C CB  . VAL   B 95  ? 0.1226 0.1202 0.1203 -0.0020 -0.0076 0.0023  95  VAL   B CB  
4159 C CG1 . VAL   B 95  ? 0.1371 0.1358 0.1245 -0.0085 -0.0030 0.0084  95  VAL   B CG1 
4160 C CG2 . VAL   B 95  ? 0.1305 0.1184 0.1259 0.0038  -0.0118 -0.0019 95  VAL   B CG2 
4170 N N   . VAL   B 96  ? 0.1361 0.1245 0.1052 0.0114  0.0125  0.0097  96  VAL   B N   
4171 C CA  . VAL   B 96  ? 0.1388 0.1366 0.1095 0.0101  0.0048  0.0127  96  VAL   B CA  
4172 C C   . VAL   B 96  ? 0.1414 0.1396 0.1105 0.0089  0.0083  0.0104  96  VAL   B C   
4173 O O   . VAL   B 96  ? 0.1414 0.1435 0.1394 0.0074  0.0121  -0.0002 96  VAL   B O   
4174 C CB  . VAL   B 96  ? 0.1453 0.1546 0.1085 0.0061  0.0034  0.0010  96  VAL   B CB  
4175 C CG1 . VAL   B 96  ? 0.1416 0.1721 0.1250 0.0115  0.0075  0.0050  96  VAL   B CG1 
4176 C CG2 . VAL   B 96  ? 0.1582 0.1579 0.1224 0.0098  0.0073  -0.0024 96  VAL   B CG2 
4186 N N   . GLY   B 97  ? 0.1447 0.1377 0.1175 0.0049  0.0066  0.0122  97  GLY   B N   
4187 C CA  . GLY   B 97  ? 0.1545 0.1388 0.1224 -0.0045 0.0070  0.0172  97  GLY   B CA  
4188 C C   . GLY   B 97  ? 0.1707 0.1461 0.1292 0.0026  -0.0004 0.0097  97  GLY   B C   
4189 O O   . GLY   B 97  ? 0.1768 0.1548 0.1324 0.0006  0.0037  0.0114  97  GLY   B O   
4193 N N   . PRO   B 98  ? 0.1806 0.1479 0.1391 0.0074  0.0251  0.0233  98  PRO   B N   
4194 C CA  . PRO   B 98  ? 0.1926 0.1627 0.1505 0.0144  0.0352  0.0229  98  PRO   B CA  
4195 C C   . PRO   B 98  ? 0.2029 0.1675 0.1186 0.0231  0.0278  0.0365  98  PRO   B C   
4196 O O   . PRO   B 98  ? 0.1941 0.1641 0.1374 0.0214  0.0303  0.0299  98  PRO   B O   
4197 C CB  . PRO   B 98  ? 0.1808 0.1660 0.1739 0.0085  0.0463  0.0281  98  PRO   B CB  
4198 C CG  . PRO   B 98  ? 0.1738 0.1572 0.1651 0.0104  0.0394  0.0289  98  PRO   B CG  
4199 C CD  . PRO   B 98  ? 0.1643 0.1518 0.1569 0.0146  0.0337  0.0243  98  PRO   B CD  
4207 N N   . ASN   B 99  ? 0.2173 0.1766 0.1339 0.0399  0.0269  0.0221  99  ASN   B N   
4208 C CA  . ASN   B 99  ? 0.2285 0.1802 0.1388 0.0463  0.0234  0.0324  99  ASN   B CA  
4209 C C   . ASN   B 99  ? 0.2481 0.2075 0.1559 0.0405  0.0409  0.0495  99  ASN   B C   
4210 O O   . ASN   B 99  ? 0.2641 0.2122 0.1716 0.0381  0.0289  0.0440  99  ASN   B O   
4211 C CB  . ASN   B 99  ? 0.2374 0.1779 0.1544 0.0443  0.0147  0.0345  99  ASN   B CB  
4212 C CG  . ASN   B 99  ? 0.2407 0.1902 0.1815 0.0410  0.0070  0.0345  99  ASN   B CG  
4213 O OD1 . ASN   B 99  ? 0.2459 0.1944 0.2076 0.0458  0.0003  0.0376  99  ASN   B OD1 
4214 N ND2 . ASN   B 99  ? 0.2408 0.1955 0.1985 0.0395  -0.0151 0.0254  99  ASN   B ND2 
4221 N N   A VAL   B 100 ? 0.2600 0.2229 0.1967 0.0231  0.0475  0.0655  100 VAL   B N   
4222 N N   B VAL   B 100 ? 0.2679 0.2238 0.1983 0.0342  0.0339  0.0607  100 VAL   B N   
4223 C CA  A VAL   B 100 ? 0.2867 0.2417 0.2524 0.0123  0.0485  0.0797  100 VAL   B CA  
4224 C CA  B VAL   B 100 ? 0.2901 0.2390 0.2410 0.0289  0.0254  0.0701  100 VAL   B CA  
4225 C C   A VAL   B 100 ? 0.3090 0.2449 0.2395 0.0210  0.0465  0.0999  100 VAL   B C   
4226 C C   B VAL   B 100 ? 0.3074 0.2453 0.2452 0.0311  0.0242  0.0881  100 VAL   B C   
4227 O O   A VAL   B 100 ? 0.3209 0.2562 0.2517 0.0176  0.0609  0.0953  100 VAL   B O   
4228 O O   B VAL   B 100 ? 0.3098 0.2486 0.2483 0.0295  0.0239  0.0886  100 VAL   B O   
4229 C CB  A VAL   B 100 ? 0.2954 0.2596 0.3271 -0.0092 0.0424  0.0826  100 VAL   B CB  
4230 C CB  B VAL   B 100 ? 0.2951 0.2470 0.2732 0.0218  0.0177  0.0626  100 VAL   B CB  
4231 C CG1 A VAL   B 100 ? 0.3022 0.2672 0.3548 -0.0093 0.0419  0.0824  100 VAL   B CG1 
4232 C CG1 B VAL   B 100 ? 0.2973 0.2496 0.2849 0.0208  0.0151  0.0603  100 VAL   B CG1 
4233 C CG2 A VAL   B 100 ? 0.2959 0.2651 0.3465 -0.0180 0.0459  0.0904  100 VAL   B CG2 
4234 C CG2 B VAL   B 100 ? 0.2968 0.2500 0.2840 0.0193  0.0158  0.0607  100 VAL   B CG2 
4253 N N   . ASN   B 101 ? 0.3220 0.2492 0.2427 0.0357  0.0251  0.1025  101 ASN   B N   
4254 C CA  . ASN   B 101 ? 0.3604 0.2707 0.2695 0.0459  0.0037  0.1098  101 ASN   B CA  
4255 C C   . ASN   B 101 ? 0.4004 0.3096 0.2724 0.0469  -0.0085 0.1071  101 ASN   B C   
4256 O O   . ASN   B 101 ? 0.4079 0.3216 0.2833 0.0544  -0.0114 0.0913  101 ASN   B O   
4257 C CB  . ASN   B 101 ? 0.3607 0.2606 0.2849 0.0421  0.0103  0.1075  101 ASN   B CB  
4258 C CG  . ASN   B 101 ? 0.3605 0.2512 0.2913 0.0399  0.0197  0.1120  101 ASN   B CG  
4259 O OD1 . ASN   B 101 ? 0.3664 0.2534 0.3170 0.0321  0.0401  0.1069  101 ASN   B OD1 
4260 N ND2 . ASN   B 101 ? 0.3575 0.2548 0.2874 0.0406  0.0152  0.0975  101 ASN   B ND2 
4268 N N   A LYS   B 102 ? 0.4278 0.3271 0.2754 0.0412  -0.0026 0.1057  102 LYS   B N   
4269 N N   B LYS   B 102 ? 0.4032 0.3276 0.3072 0.0383  -0.0073 0.0798  102 LYS   B N   
4270 C CA  A LYS   B 102 ? 0.4539 0.3545 0.2945 0.0298  0.0145  0.0866  102 LYS   B CA  
4271 C CA  B LYS   B 102 ? 0.4046 0.3453 0.3402 0.0291  -0.0024 0.0515  102 LYS   B CA  
4272 C C   A LYS   B 102 ? 0.4578 0.3568 0.2746 0.0303  0.0329  0.0946  102 LYS   B C   
4273 C C   B LYS   B 102 ? 0.3977 0.3467 0.3389 0.0242  0.0014  0.0388  102 LYS   B C   
4274 O O   A LYS   B 102 ? 0.4678 0.3628 0.2874 0.0329  0.0251  0.0840  102 LYS   B O   
4275 O O   B LYS   B 102 ? 0.3997 0.3490 0.3417 0.0238  0.0016  0.0353  102 LYS   B O   
4276 C CB  A LYS   B 102 ? 0.4738 0.3783 0.3570 0.0182  0.0208  0.0538  102 LYS   B CB  
4277 C CB  B LYS   B 102 ? 0.4118 0.3598 0.3756 0.0254  -0.0001 0.0367  102 LYS   B CB  
4278 C CG  A LYS   B 102 ? 0.4905 0.3995 0.4163 0.0106  0.0278  0.0257  102 LYS   B CG  
4279 C CG  B LYS   B 102 ? 0.4179 0.3716 0.4056 0.0226  0.0020  0.0247  102 LYS   B CG  
4280 C CD  A LYS   B 102 ? 0.5062 0.4168 0.4773 0.0045  0.0357  0.0053  102 LYS   B CD  
4281 C CD  B LYS   B 102 ? 0.4236 0.3810 0.4339 0.0205  0.0036  0.0158  102 LYS   B CD  
4282 C CE  A LYS   B 102 ? 0.5192 0.4292 0.5257 0.0001  0.0402  -0.0108 102 LYS   B CE  
4283 C CE  B LYS   B 102 ? 0.4283 0.3878 0.4544 0.0193  0.0046  0.0094  102 LYS   B CE  
4284 N NZ  A LYS   B 102 ? 0.5263 0.4366 0.5542 -0.0023 0.0406  -0.0206 102 LYS   B NZ  
4285 N NZ  B LYS   B 102 ? 0.4308 0.3912 0.4659 0.0188  0.0047  0.0060  102 LYS   B NZ  
4312 N N   A GLY   B 103 ? 0.4470 0.3499 0.2600 0.0268  0.0627  0.1056  103 GLY   B N   
4313 N N   B GLY   B 103 ? 0.3878 0.3440 0.3364 0.0202  0.0050  0.0307  103 GLY   B N   
4314 C CA  A GLY   B 103 ? 0.4351 0.3457 0.2744 0.0247  0.0866  0.0937  103 GLY   B CA  
4315 C CA  B GLY   B 103 ? 0.3778 0.3405 0.3347 0.0164  0.0079  0.0221  103 GLY   B CA  
4316 C C   A GLY   B 103 ? 0.4190 0.3362 0.2644 0.0192  0.1099  0.0830  103 GLY   B C   
4317 C C   B GLY   B 103 ? 0.3670 0.3357 0.3289 0.0123  0.0103  0.0145  103 GLY   B C   
4318 O O   A GLY   B 103 ? 0.4251 0.3446 0.2767 0.0176  0.1114  0.0841  103 GLY   B O   
4319 O O   B GLY   B 103 ? 0.3680 0.3370 0.3321 0.0125  0.0111  0.0135  103 GLY   B O   
4326 N N   A GLU   B 104 ? 0.3958 0.3153 0.2446 0.0155  0.1214  0.0629  104 GLU   B N   
4327 N N   B GLU   B 104 ? 0.3552 0.3290 0.3174 0.0079  0.0102  0.0083  104 GLU   B N   
4328 C CA  A GLU   B 104 ? 0.3731 0.2972 0.2213 0.0131  0.1224  0.0438  104 GLU   B CA  
4329 C CA  B GLU   B 104 ? 0.3441 0.3231 0.3054 0.0034  0.0097  0.0036  104 GLU   B CA  
4330 C C   A GLU   B 104 ? 0.3769 0.2985 0.2438 0.0035  0.1396  0.0347  104 GLU   B C   
4331 C C   B GLU   B 104 ? 0.3414 0.3234 0.3091 -0.0001 0.0136  0.0013  104 GLU   B C   
4332 O O   A GLU   B 104 ? 0.3819 0.3018 0.2769 -0.0018 0.1304  0.0248  104 GLU   B O   
4333 O O   B GLU   B 104 ? 0.3418 0.3240 0.3094 -0.0010 0.0137  0.0001  104 GLU   B O   
4334 C CB  A GLU   B 104 ? 0.3519 0.2769 0.2064 0.0205  0.0888  0.0260  104 GLU   B CB  
4335 C CB  B GLU   B 104 ? 0.3369 0.3172 0.2927 0.0021  0.0052  0.0013  104 GLU   B CB  
4336 C CG  A GLU   B 104 ? 0.3356 0.2643 0.1965 0.0250  0.0455  -0.0027 104 GLU   B CG  
4337 C CG  B GLU   B 104 ? 0.3315 0.3128 0.2826 0.0007  0.0007  -0.0013 104 GLU   B CG  
4338 C CD  A GLU   B 104 ? 0.3210 0.2505 0.1817 0.0268  0.0108  -0.0094 104 GLU   B CD  
4339 C CD  B GLU   B 104 ? 0.3281 0.3096 0.2744 -0.0008 -0.0025 -0.0020 104 GLU   B CD  
4340 O OE1 A GLU   B 104 ? 0.3004 0.2331 0.1462 0.0270  0.0226  -0.0016 104 GLU   B OE1 
4341 O OE1 B GLU   B 104 ? 0.3262 0.3076 0.2700 -0.0015 -0.0019 -0.0015 104 GLU   B OE1 
4342 O OE2 A GLU   B 104 ? 0.3289 0.2642 0.2057 0.0229  -0.0253 -0.0247 104 GLU   B OE2 
4343 O OE2 B GLU   B 104 ? 0.3279 0.3100 0.2745 -0.0015 -0.0059 -0.0037 104 GLU   B OE2 
4356 N N   A ASP   B 105 ? 0.3723 0.3014 0.2465 -0.0067 0.1598  0.0396  105 ASP   B N   
4357 N N   B ASP   B 105 ? 0.3385 0.3237 0.3138 -0.0028 0.0172  0.0010  105 ASP   B N   
4358 C CA  A ASP   B 105 ? 0.3722 0.3025 0.2675 -0.0167 0.1780  0.0312  105 ASP   B CA  
4359 C CA  B ASP   B 105 ? 0.3364 0.3239 0.3227 -0.0051 0.0201  0.0001  105 ASP   B CA  
4360 C C   A ASP   B 105 ? 0.3592 0.2712 0.2546 -0.0243 0.1708  0.0217  105 ASP   B C   
4361 C C   B ASP   B 105 ? 0.3310 0.3185 0.3081 -0.0058 0.0215  -0.0014 105 ASP   B C   
4362 O O   A ASP   B 105 ? 0.3428 0.2606 0.2525 -0.0229 0.1681  0.0181  105 ASP   B O   
4363 O O   B ASP   B 105 ? 0.3307 0.3180 0.3021 -0.0061 0.0218  -0.0012 105 ASP   B O   
4364 C CB  A ASP   B 105 ? 0.3837 0.3309 0.3312 -0.0109 0.1890  0.0164  105 ASP   B CB  
4365 C CB  B ASP   B 105 ? 0.3389 0.3286 0.3444 -0.0059 0.0219  -0.0002 105 ASP   B CB  
4366 C CG  A ASP   B 105 ? 0.3926 0.3513 0.3944 -0.0106 0.2055  0.0085  105 ASP   B CG  
4367 C CG  B ASP   B 105 ? 0.3412 0.3321 0.3666 -0.0070 0.0235  0.0001  105 ASP   B CG  
4368 O OD1 A ASP   B 105 ? 0.3934 0.3568 0.3987 -0.0207 0.2141  0.0190  105 ASP   B OD1 
4369 O OD1 B ASP   B 105 ? 0.3419 0.3335 0.3733 -0.0084 0.0240  0.0008  105 ASP   B OD1 
4370 O OD2 A ASP   B 105 ? 0.3981 0.3632 0.4313 -0.0047 0.2006  -0.0028 105 ASP   B OD2 
4371 O OD2 B ASP   B 105 ? 0.3417 0.3335 0.3741 -0.0072 0.0238  0.0003  105 ASP   B OD2 
4380 N N   A ILE   B 106 ? 0.3550 0.2489 0.2662 -0.0290 0.1547  0.0180  106 ILE   B N   
4381 N N   B ILE   B 106 ? 0.3254 0.3132 0.2980 -0.0055 0.0219  -0.0027 106 ILE   B N   
4382 C CA  A ILE   B 106 ? 0.3377 0.2250 0.2805 -0.0379 0.1563  0.0112  106 ILE   B CA  
4383 C CA  B ILE   B 106 ? 0.3182 0.3076 0.2918 -0.0051 0.0236  -0.0042 106 ILE   B CA  
4384 C C   A ILE   B 106 ? 0.3053 0.2219 0.2781 -0.0381 0.1540  -0.0079 106 ILE   B C   
4385 C C   B ILE   B 106 ? 0.3067 0.3016 0.2887 -0.0051 0.0273  -0.0076 106 ILE   B C   
4386 O O   A ILE   B 106 ? 0.2968 0.1982 0.2791 -0.0432 0.1468  -0.0156 106 ILE   B O   
4387 O O   B ILE   B 106 ? 0.3063 0.3007 0.2851 -0.0052 0.0241  -0.0087 106 ILE   B O   
4388 C CB  A ILE   B 106 ? 0.3585 0.2189 0.3118 -0.0408 0.1464  0.0247  106 ILE   B CB  
4389 C CB  B ILE   B 106 ? 0.3220 0.3082 0.2927 -0.0047 0.0219  -0.0024 106 ILE   B CB  
4390 C CG1 A ILE   B 106 ? 0.3688 0.2210 0.3248 -0.0260 0.1342  0.0208  106 ILE   B CG1 
4391 C CG1 B ILE   B 106 ? 0.3223 0.3073 0.2940 -0.0033 0.0203  -0.0013 106 ILE   B CG1 
4392 C CG2 A ILE   B 106 ? 0.3655 0.2199 0.3366 -0.0500 0.1452  0.0314  106 ILE   B CG2 
4393 C CG2 B ILE   B 106 ? 0.3243 0.3098 0.2956 -0.0049 0.0219  -0.0019 106 ILE   B CG2 
4394 C CD1 A ILE   B 106 ? 0.3718 0.2226 0.3273 -0.0127 0.1292  0.0273  106 ILE   B CD1 
4395 C CD1 B ILE   B 106 ? 0.3219 0.3066 0.2946 -0.0020 0.0195  -0.0000 106 ILE   B CD1 
4418 N N   A GLN   B 107 ? 0.2930 0.2496 0.2987 -0.0357 0.1395  -0.0135 107 GLN   B N   
4419 N N   B GLN   B 107 ? 0.2956 0.2964 0.2934 -0.0058 0.0338  -0.0098 107 GLN   B N   
4420 C CA  A GLN   B 107 ? 0.2758 0.2728 0.3132 -0.0367 0.1279  -0.0105 107 GLN   B CA  
4421 C CA  B GLN   B 107 ? 0.2834 0.2897 0.2985 -0.0063 0.0413  -0.0104 107 GLN   B CA  
4422 C C   A GLN   B 107 ? 0.2451 0.2560 0.2845 -0.0244 0.0902  -0.0193 107 GLN   B C   
4423 C C   B GLN   B 107 ? 0.2548 0.2663 0.2646 -0.0066 0.0556  -0.0144 107 GLN   B C   
4424 O O   A GLN   B 107 ? 0.2395 0.2573 0.3234 -0.0165 0.0632  -0.0349 107 GLN   B O   
4425 O O   B GLN   B 107 ? 0.2558 0.2680 0.2667 -0.0068 0.0517  -0.0180 107 GLN   B O   
4426 C CB  A GLN   B 107 ? 0.3047 0.3124 0.3787 -0.0376 0.1199  -0.0027 107 GLN   B CB  
4427 C CB  B GLN   B 107 ? 0.2988 0.3050 0.3416 -0.0054 0.0333  -0.0076 107 GLN   B CB  
4428 C CG  A GLN   B 107 ? 0.3382 0.3519 0.4485 -0.0312 0.0888  0.0029  107 GLN   B CG  
4429 C CG  B GLN   B 107 ? 0.3122 0.3183 0.3823 -0.0037 0.0247  -0.0045 107 GLN   B CG  
4430 C CD  A GLN   B 107 ? 0.3606 0.3804 0.5041 -0.0295 0.0670  0.0101  107 GLN   B CD  
4431 C CD  B GLN   B 107 ? 0.3216 0.3280 0.4155 -0.0029 0.0184  -0.0014 107 GLN   B CD  
4432 O OE1 A GLN   B 107 ? 0.3676 0.3901 0.5222 -0.0285 0.0689  0.0098  107 GLN   B OE1 
4433 O OE1 B GLN   B 107 ? 0.3247 0.3316 0.4264 -0.0027 0.0179  -0.0008 107 GLN   B OE1 
4434 N NE2 A GLN   B 107 ? 0.3693 0.3872 0.5233 -0.0253 0.0536  0.0170  107 GLN   B NE2 
4435 N NE2 B GLN   B 107 ? 0.3250 0.3310 0.4270 -0.0021 0.0156  0.0006  107 GLN   B NE2 
4452 N N   . LEU   B 108 ? 0.2237 0.2398 0.2344 -0.0054 0.0735  -0.0157 108 LEU   B N   
4453 C CA  . LEU   B 108 ? 0.2050 0.2107 0.2004 0.0176  0.0520  -0.0022 108 LEU   B CA  
4454 C C   . LEU   B 108 ? 0.1777 0.1715 0.1869 0.0228  0.0333  0.0171  108 LEU   B C   
4455 O O   . LEU   B 108 ? 0.1811 0.1609 0.1826 0.0237  0.0232  0.0098  108 LEU   B O   
4456 C CB  . LEU   B 108 ? 0.2231 0.2263 0.1857 0.0200  0.0547  -0.0060 108 LEU   B CB  
4457 C CG  . LEU   B 108 ? 0.2411 0.2554 0.1880 0.0254  0.0434  -0.0278 108 LEU   B CG  
4458 C CD1 . LEU   B 108 ? 0.2458 0.2697 0.1770 0.0182  0.0492  -0.0178 108 LEU   B CD1 
4459 C CD2 . LEU   B 108 ? 0.2575 0.2657 0.2078 0.0344  0.0315  -0.0419 108 LEU   B CD2 
4472 N N   . LEU   B 109 ? 0.1626 0.1552 0.1805 0.0170  0.0318  0.0151  109 LEU   B N   
4473 C CA  . LEU   B 109 ? 0.1486 0.1296 0.1874 0.0096  0.0306  0.0208  109 LEU   B CA  
4474 C C   . LEU   B 109 ? 0.1393 0.1206 0.1872 0.0045  0.0281  0.0156  109 LEU   B C   
4475 O O   . LEU   B 109 ? 0.1359 0.1233 0.1896 0.0056  0.0259  0.0253  109 LEU   B O   
4476 C CB  . LEU   B 109 ? 0.1577 0.1269 0.1889 0.0081  0.0200  0.0278  109 LEU   B CB  
4477 C CG  . LEU   B 109 ? 0.1571 0.1290 0.1848 0.0079  0.0111  0.0168  109 LEU   B CG  
4478 C CD1 . LEU   B 109 ? 0.1567 0.1383 0.1856 0.0174  0.0235  0.0173  109 LEU   B CD1 
4479 C CD2 . LEU   B 109 ? 0.1656 0.1367 0.1946 0.0079  0.0115  0.0094  109 LEU   B CD2 
4491 N N   . LYS   B 110 ? 0.1395 0.1243 0.1820 -0.0010 0.0283  0.0169  110 LYS   B N   
4492 C CA  . LYS   B 110 ? 0.1368 0.1199 0.1689 0.0008  0.0216  0.0116  110 LYS   B CA  
4493 C C   . LYS   B 110 ? 0.1324 0.1239 0.1591 0.0020  0.0215  0.0072  110 LYS   B C   
4494 O O   . LYS   B 110 ? 0.1286 0.1281 0.1585 -0.0044 0.0150  0.0003  110 LYS   B O   
4495 C CB  . LYS   B 110 ? 0.1394 0.1219 0.1939 0.0008  0.0204  0.0091  110 LYS   B CB  
4496 C CG  . LYS   B 110 ? 0.1385 0.1245 0.2070 -0.0024 0.0162  0.0095  110 LYS   B CG  
4497 C CD  . LYS   B 110 ? 0.1405 0.1277 0.2171 -0.0037 0.0114  -0.0002 110 LYS   B CD  
4498 C CE  . LYS   B 110 ? 0.1408 0.1426 0.2304 -0.0012 0.0159  -0.0002 110 LYS   B CE  
4499 N NZ  . LYS   B 110 ? 0.1393 0.1574 0.2216 0.0033  0.0087  -0.0093 110 LYS   B NZ  
4513 N N   . SER   B 111 ? 0.1399 0.1278 0.1673 -0.0032 0.0250  0.0113  111 SER   B N   
4514 C CA  . SER   B 111 ? 0.1445 0.1268 0.1645 0.0038  0.0188  0.0120  111 SER   B CA  
4515 C C   . SER   B 111 ? 0.1366 0.1225 0.1523 0.0003  0.0114  0.0078  111 SER   B C   
4516 O O   . SER   B 111 ? 0.1310 0.1266 0.1648 -0.0007 0.0074  0.0103  111 SER   B O   
4517 C CB  . SER   B 111 ? 0.1573 0.1478 0.1767 0.0016  0.0341  0.0196  111 SER   B CB  
4518 O OG  . SER   B 111 ? 0.1747 0.1900 0.1843 0.0059  0.0410  0.0165  111 SER   B OG  
4524 N N   . ALA   B 112 ? 0.1281 0.1278 0.1576 0.0047  0.0155  0.0154  112 ALA   B N   
4525 C CA  . ALA   B 112 ? 0.1241 0.1315 0.1512 0.0022  0.0070  0.0094  112 ALA   B CA  
4526 C C   . ALA   B 112 ? 0.1173 0.1250 0.1395 0.0004  0.0121  0.0012  112 ALA   B C   
4527 O O   . ALA   B 112 ? 0.1189 0.1263 0.1551 -0.0022 0.0073  -0.0002 112 ALA   B O   
4528 C CB  . ALA   B 112 ? 0.1336 0.1306 0.1723 0.0078  0.0070  0.0110  112 ALA   B CB  
4534 N N   . TYR   B 113 ? 0.1170 0.1123 0.1511 -0.0005 0.0076  0.0064  113 TYR   B N   
4535 C CA  . TYR   B 113 ? 0.1162 0.1085 0.1412 0.0006  0.0108  -0.0026 113 TYR   B CA  
4536 C C   . TYR   B 113 ? 0.1175 0.1056 0.1416 -0.0033 0.0073  -0.0019 113 TYR   B C   
4537 O O   . TYR   B 113 ? 0.1183 0.1101 0.1397 -0.0024 0.0063  -0.0001 113 TYR   B O   
4538 C CB  . TYR   B 113 ? 0.1251 0.1100 0.1535 0.0001  0.0136  0.0086  113 TYR   B CB  
4539 C CG  . TYR   B 113 ? 0.1243 0.1134 0.1655 -0.0022 0.0088  0.0084  113 TYR   B CG  
4540 C CD1 . TYR   B 113 ? 0.1299 0.1164 0.1735 -0.0067 0.0155  0.0150  113 TYR   B CD1 
4541 C CD2 . TYR   B 113 ? 0.1310 0.1136 0.1702 -0.0030 0.0104  0.0085  113 TYR   B CD2 
4542 C CE1 . TYR   B 113 ? 0.1271 0.1146 0.1721 0.0030  0.0187  0.0059  113 TYR   B CE1 
4543 C CE2 . TYR   B 113 ? 0.1373 0.1102 0.1712 0.0025  0.0111  0.0094  113 TYR   B CE2 
4544 C CZ  . TYR   B 113 ? 0.1292 0.1143 0.1813 0.0065  0.0096  -0.0001 113 TYR   B CZ  
4545 O OH  . TYR   B 113 ? 0.1374 0.1106 0.1995 0.0139  0.0192  0.0040  113 TYR   B OH  
4555 N N   . GLU   B 114 ? 0.1155 0.1040 0.1542 -0.0014 0.0141  0.0013  114 GLU   B N   
4556 C CA  . GLU   B 114 ? 0.1138 0.1078 0.1534 0.0006  0.0077  -0.0008 114 GLU   B CA  
4557 C C   . GLU   B 114 ? 0.1119 0.1114 0.1452 0.0008  0.0073  0.0027  114 GLU   B C   
4558 O O   . GLU   B 114 ? 0.1110 0.1131 0.1549 0.0027  0.0055  0.0088  114 GLU   B O   
4559 C CB  . GLU   B 114 ? 0.1181 0.1135 0.1645 -0.0016 0.0083  0.0016  114 GLU   B CB  
4560 C CG  . GLU   B 114 ? 0.1229 0.1141 0.1604 0.0003  0.0117  0.0041  114 GLU   B CG  
4561 C CD  . GLU   B 114 ? 0.1217 0.1168 0.1654 -0.0061 0.0121  0.0011  114 GLU   B CD  
4562 O OE1 . GLU   B 114 ? 0.1205 0.1354 0.1645 -0.0046 0.0232  0.0031  114 GLU   B OE1 
4563 O OE2 . GLU   B 114 ? 0.1211 0.1373 0.1827 -0.0159 0.0168  0.0031  114 GLU   B OE2 
4570 N N   . ASN   B 115 ? 0.1180 0.1055 0.1408 -0.0017 0.0027  0.0018  115 ASN   B N   
4571 C CA  . ASN   B 115 ? 0.1206 0.1136 0.1344 -0.0070 0.0039  0.0013  115 ASN   B CA  
4572 C C   . ASN   B 115 ? 0.1133 0.1099 0.1329 -0.0082 0.0011  -0.0003 115 ASN   B C   
4573 O O   . ASN   B 115 ? 0.1237 0.1158 0.1457 -0.0134 0.0021  0.0050  115 ASN   B O   
4574 C CB  . ASN   B 115 ? 0.1319 0.1248 0.1281 -0.0068 0.0050  0.0013  115 ASN   B CB  
4575 C CG  . ASN   B 115 ? 0.1411 0.1295 0.1378 0.0049  0.0003  0.0024  115 ASN   B CG  
4576 O OD1 . ASN   B 115 ? 0.1834 0.1391 0.1624 0.0037  0.0089  -0.0140 115 ASN   B OD1 
4577 N ND2 . ASN   B 115 ? 0.1339 0.1389 0.1426 -0.0035 0.0018  0.0066  115 ASN   B ND2 
4584 N N   . PHE   B 116 ? 0.1137 0.1133 0.1209 -0.0035 0.0023  0.0027  116 PHE   B N   
4585 C CA  . PHE   B 116 ? 0.1192 0.1126 0.1329 -0.0078 0.0001  0.0002  116 PHE   B CA  
4586 C C   . PHE   B 116 ? 0.1205 0.1025 0.1224 -0.0082 0.0018  0.0039  116 PHE   B C   
4587 O O   . PHE   B 116 ? 0.1211 0.1130 0.1363 -0.0015 0.0011  -0.0012 116 PHE   B O   
4588 C CB  . PHE   B 116 ? 0.1203 0.1089 0.1277 -0.0021 -0.0060 0.0020  116 PHE   B CB  
4589 C CG  . PHE   B 116 ? 0.1142 0.1110 0.1306 -0.0047 0.0036  -0.0003 116 PHE   B CG  
4590 C CD1 . PHE   B 116 ? 0.1247 0.1110 0.1496 -0.0019 0.0019  0.0000  116 PHE   B CD1 
4591 C CD2 . PHE   B 116 ? 0.1211 0.1199 0.1358 -0.0011 0.0050  -0.0045 116 PHE   B CD2 
4592 C CE1 . PHE   B 116 ? 0.1227 0.1171 0.1461 -0.0038 -0.0036 0.0043  116 PHE   B CE1 
4593 C CE2 . PHE   B 116 ? 0.1224 0.1173 0.1325 0.0032  0.0079  0.0012  116 PHE   B CE2 
4594 C CZ  . PHE   B 116 ? 0.1146 0.1191 0.1436 -0.0004 -0.0046 0.0086  116 PHE   B CZ  
4604 N N   . ASN   B 117 ? 0.1171 0.1061 0.1428 0.0003  -0.0014 -0.0010 117 ASN   B N   
4605 C CA  . ASN   B 117 ? 0.1236 0.1099 0.1452 0.0013  -0.0035 -0.0057 117 ASN   B CA  
4606 C C   . ASN   B 117 ? 0.1230 0.1080 0.1503 0.0049  0.0011  -0.0005 117 ASN   B C   
4607 O O   . ASN   B 117 ? 0.1325 0.1150 0.1773 -0.0018 -0.0198 0.0048  117 ASN   B O   
4608 C CB  . ASN   B 117 ? 0.1271 0.1138 0.1449 -0.0008 -0.0013 -0.0079 117 ASN   B CB  
4609 C CG  . ASN   B 117 ? 0.1232 0.1162 0.1513 0.0014  0.0009  -0.0068 117 ASN   B CG  
4610 O OD1 . ASN   B 117 ? 0.1406 0.1200 0.1701 -0.0128 0.0086  -0.0045 117 ASN   B OD1 
4611 N ND2 . ASN   B 117 ? 0.1242 0.1173 0.1584 -0.0022 0.0025  -0.0065 117 ASN   B ND2 
4618 N N   . GLN   B 118 ? 0.1220 0.1051 0.1518 -0.0030 -0.0112 -0.0018 118 GLN   B N   
4619 C CA  . GLN   B 118 ? 0.1283 0.1117 0.1644 0.0023  -0.0100 -0.0028 118 GLN   B CA  
4620 C C   . GLN   B 118 ? 0.1319 0.1094 0.1610 -0.0021 -0.0006 -0.0064 118 GLN   B C   
4621 O O   . GLN   B 118 ? 0.1535 0.1087 0.2000 -0.0074 0.0102  -0.0036 118 GLN   B O   
4622 C CB  . GLN   B 118 ? 0.1367 0.1201 0.1725 0.0048  -0.0120 -0.0046 118 GLN   B CB  
4623 C CG  . GLN   B 118 ? 0.1439 0.1188 0.1643 0.0114  -0.0104 -0.0150 118 GLN   B CG  
4624 C CD  . GLN   B 118 ? 0.1526 0.1146 0.1566 0.0038  -0.0021 -0.0174 118 GLN   B CD  
4625 O OE1 . GLN   B 118 ? 0.1599 0.1161 0.1764 0.0042  0.0112  -0.0007 118 GLN   B OE1 
4626 N NE2 . GLN   B 118 ? 0.1582 0.1151 0.1792 0.0022  -0.0104 0.0003  118 GLN   B NE2 
4635 N N   . HIS   B 119 ? 0.1303 0.1141 0.1354 -0.0065 -0.0056 0.0061  119 HIS   B N   
4636 C CA  . HIS   B 119 ? 0.1412 0.1264 0.1323 -0.0004 -0.0076 0.0042  119 HIS   B CA  
4637 C C   . HIS   B 119 ? 0.1396 0.1261 0.1339 -0.0022 -0.0135 0.0031  119 HIS   B C   
4638 O O   . HIS   B 119 ? 0.1524 0.1245 0.1507 -0.0245 -0.0089 0.0062  119 HIS   B O   
4639 C CB  . HIS   B 119 ? 0.1445 0.1392 0.1397 0.0041  -0.0190 0.0001  119 HIS   B CB  
4640 C CG  . HIS   B 119 ? 0.1473 0.1611 0.1555 0.0127  -0.0301 -0.0137 119 HIS   B CG  
4641 N ND1 . HIS   B 119 ? 0.1640 0.1775 0.1903 0.0011  -0.0362 -0.0373 119 HIS   B ND1 
4642 C CD2 . HIS   B 119 ? 0.1662 0.1777 0.1698 0.0358  -0.0393 -0.0217 119 HIS   B CD2 
4643 C CE1 . HIS   B 119 ? 0.1840 0.1876 0.2025 0.0168  -0.0448 -0.0456 119 HIS   B CE1 
4644 N NE2 . HIS   B 119 ? 0.1871 0.1977 0.1890 0.0292  -0.0413 -0.0378 119 HIS   B NE2 
4652 N N   . GLU   B 120 ? 0.1544 0.1271 0.1319 -0.0093 -0.0228 0.0135  120 GLU   B N   
4653 C CA  . GLU   B 120 ? 0.1845 0.1401 0.1442 -0.0014 -0.0349 0.0210  120 GLU   B CA  
4654 C C   . GLU   B 120 ? 0.1626 0.1295 0.1337 -0.0109 -0.0218 0.0233  120 GLU   B C   
4655 O O   . GLU   B 120 ? 0.1576 0.1432 0.1322 -0.0128 -0.0180 0.0079  120 GLU   B O   
4656 C CB  . GLU   B 120 ? 0.2424 0.1705 0.2046 0.0190  -0.0586 0.0417  120 GLU   B CB  
4657 C CG  . GLU   B 120 ? 0.2937 0.2404 0.3092 0.0259  -0.0754 0.0644  120 GLU   B CG  
4658 C CD  . GLU   B 120 ? 0.3353 0.3028 0.4174 0.0231  -0.0821 0.0784  120 GLU   B CD  
4659 O OE1 . GLU   B 120 ? 0.3522 0.3225 0.4527 0.0159  -0.0796 0.0903  120 GLU   B OE1 
4660 O OE2 . GLU   B 120 ? 0.3516 0.3252 0.4693 0.0225  -0.0812 0.0712  120 GLU   B OE2 
4667 N N   . VAL   B 121 ? 0.1520 0.1261 0.1308 -0.0170 -0.0123 0.0146  121 VAL   B N   
4668 C CA  . VAL   B 121 ? 0.1506 0.1358 0.1209 -0.0146 -0.0110 0.0125  121 VAL   B CA  
4669 C C   . VAL   B 121 ? 0.1423 0.1310 0.1151 -0.0190 -0.0110 0.0064  121 VAL   B C   
4670 O O   . VAL   B 121 ? 0.1523 0.1269 0.1425 -0.0248 -0.0170 -0.0018 121 VAL   B O   
4671 C CB  . VAL   B 121 ? 0.1727 0.1707 0.1366 0.0011  -0.0187 0.0177  121 VAL   B CB  
4672 C CG1 . VAL   B 121 ? 0.1767 0.1769 0.1660 -0.0040 -0.0072 0.0148  121 VAL   B CG1 
4673 C CG2 . VAL   B 121 ? 0.1953 0.1890 0.1383 0.0095  -0.0132 0.0106  121 VAL   B CG2 
4683 N N   . LEU   B 122 ? 0.1350 0.1241 0.1152 -0.0095 -0.0159 0.0028  122 LEU   B N   
4684 C CA  . LEU   B 122 ? 0.1263 0.1325 0.1068 -0.0136 -0.0098 -0.0004 122 LEU   B CA  
4685 C C   . LEU   B 122 ? 0.1254 0.1190 0.1113 -0.0238 -0.0029 0.0057  122 LEU   B C   
4686 O O   . LEU   B 122 ? 0.1366 0.1248 0.1471 -0.0278 -0.0128 0.0011  122 LEU   B O   
4687 C CB  . LEU   B 122 ? 0.1494 0.1459 0.1394 -0.0026 -0.0192 0.0031  122 LEU   B CB  
4688 C CG  . LEU   B 122 ? 0.1405 0.1474 0.1460 -0.0114 -0.0026 0.0026  122 LEU   B CG  
4689 C CD1 . LEU   B 122 ? 0.1484 0.1684 0.1626 -0.0182 -0.0021 -0.0002 122 LEU   B CD1 
4690 C CD2 . LEU   B 122 ? 0.1451 0.1467 0.1264 -0.0127 -0.0062 -0.0067 122 LEU   B CD2 
4702 N N   . LEU   B 123 ? 0.1265 0.1067 0.1151 -0.0213 -0.0012 0.0020  123 LEU   B N   
4703 C CA  . LEU   B 123 ? 0.1326 0.1173 0.1149 -0.0203 -0.0097 -0.0043 123 LEU   B CA  
4704 C C   . LEU   B 123 ? 0.1284 0.1115 0.1136 -0.0199 -0.0088 -0.0009 123 LEU   B C   
4705 O O   . LEU   B 123 ? 0.1403 0.1150 0.1148 -0.0263 -0.0099 0.0031  123 LEU   B O   
4706 C CB  . LEU   B 123 ? 0.1386 0.1175 0.1200 -0.0202 -0.0105 -0.0007 123 LEU   B CB  
4707 C CG  . LEU   B 123 ? 0.1376 0.1237 0.1363 -0.0135 -0.0022 0.0084  123 LEU   B CG  
4708 C CD1 . LEU   B 123 ? 0.1467 0.1274 0.1431 -0.0117 -0.0001 -0.0096 123 LEU   B CD1 
4709 C CD2 . LEU   B 123 ? 0.1470 0.1274 0.1605 -0.0089 -0.0001 0.0130  123 LEU   B CD2 
4721 N N   . ALA   B 124 ? 0.1291 0.1090 0.1165 -0.0184 -0.0007 -0.0034 124 ALA   B N   
4722 C CA  . ALA   B 124 ? 0.1243 0.1112 0.1269 -0.0128 -0.0015 -0.0093 124 ALA   B CA  
4723 C C   . ALA   B 124 ? 0.1204 0.1119 0.1178 -0.0134 -0.0069 -0.0062 124 ALA   B C   
4724 O O   . ALA   B 124 ? 0.1312 0.1154 0.1263 -0.0140 -0.0072 -0.0012 124 ALA   B O   
4725 C CB  . ALA   B 124 ? 0.1296 0.1203 0.1383 -0.0096 0.0073  -0.0030 124 ALA   B CB  
4731 N N   . PRO   B 125 ? 0.1324 0.1163 0.1120 -0.0131 -0.0107 0.0060  125 PRO   B N   
4732 C CA  . PRO   B 125 ? 0.1376 0.1159 0.1325 -0.0114 -0.0053 0.0140  125 PRO   B CA  
4733 C C   . PRO   B 125 ? 0.1321 0.1074 0.1434 -0.0087 -0.0028 0.0051  125 PRO   B C   
4734 O O   . PRO   B 125 ? 0.1363 0.1086 0.1670 -0.0085 0.0030  0.0116  125 PRO   B O   
4735 C CB  . PRO   B 125 ? 0.1397 0.1432 0.1401 -0.0178 -0.0147 0.0277  125 PRO   B CB  
4736 C CG  . PRO   B 125 ? 0.1462 0.1523 0.1331 -0.0294 -0.0153 0.0128  125 PRO   B CG  
4737 C CD  . PRO   B 125 ? 0.1417 0.1306 0.1149 -0.0291 -0.0051 0.0028  125 PRO   B CD  
4745 N N   . LEU   B 126 ? 0.1387 0.1075 0.1703 -0.0123 0.0131  0.0082  126 LEU   B N   
4746 C CA  . LEU   B 126 ? 0.1449 0.1163 0.1695 -0.0071 0.0157  0.0037  126 LEU   B CA  
4747 C C   . LEU   B 126 ? 0.1432 0.1236 0.1729 0.0025  0.0225  0.0097  126 LEU   B C   
4748 O O   . LEU   B 126 ? 0.1604 0.1512 0.1920 0.0168  0.0020  -0.0070 126 LEU   B O   
4749 C CB  . LEU   B 126 ? 0.1630 0.1206 0.1975 -0.0103 0.0251  0.0029  126 LEU   B CB  
4750 C CG  . LEU   B 126 ? 0.1789 0.1292 0.2017 -0.0197 0.0260  -0.0105 126 LEU   B CG  
4751 C CD1 . LEU   B 126 ? 0.1905 0.1394 0.2445 -0.0209 0.0172  -0.0197 126 LEU   B CD1 
4752 C CD2 . LEU   B 126 ? 0.1805 0.1442 0.1940 -0.0314 0.0196  -0.0042 126 LEU   B CD2 
4764 N N   . LEU   B 127 ? 0.1393 0.1166 0.1698 0.0006  0.0228  0.0084  127 LEU   B N   
4765 C CA  . LEU   B 127 ? 0.1377 0.1227 0.1765 -0.0026 0.0240  0.0153  127 LEU   B CA  
4766 C C   . LEU   B 127 ? 0.1348 0.1192 0.1705 -0.0019 0.0224  0.0121  127 LEU   B C   
4767 O O   . LEU   B 127 ? 0.1381 0.1229 0.1710 -0.0122 0.0106  0.0145  127 LEU   B O   
4768 C CB  . LEU   B 127 ? 0.1544 0.1251 0.1845 0.0039  0.0258  0.0207  127 LEU   B CB  
4769 C CG  . LEU   B 127 ? 0.1634 0.1264 0.1917 0.0030  0.0230  0.0157  127 LEU   B CG  
4770 C CD1 . LEU   B 127 ? 0.1654 0.1276 0.1878 0.0038  0.0151  0.0031  127 LEU   B CD1 
4771 C CD2 . LEU   B 127 ? 0.1623 0.1313 0.2030 -0.0088 0.0301  0.0224  127 LEU   B CD2 
4783 N N   . SER   B 128 ? 0.1430 0.1197 0.1628 0.0005  0.0064  0.0069  128 SER   B N   
4784 C CA  . SER   B 128 ? 0.1485 0.1296 0.1640 0.0056  -0.0041 0.0132  128 SER   B CA  
4785 C C   . SER   B 128 ? 0.1615 0.1354 0.1883 0.0091  -0.0209 0.0139  128 SER   B C   
4786 O O   . SER   B 128 ? 0.1765 0.1370 0.2171 0.0062  -0.0128 0.0288  128 SER   B O   
4787 C CB  . SER   B 128 ? 0.1597 0.1337 0.1686 0.0077  0.0009  0.0175  128 SER   B CB  
4788 O OG  . SER   B 128 ? 0.1679 0.1428 0.1754 0.0109  0.0111  0.0188  128 SER   B OG  
4794 N N   . ALA   B 129 ? 0.1730 0.1394 0.1990 0.0248  -0.0159 -0.0005 129 ALA   B N   
4795 C CA  . ALA   B 129 ? 0.1857 0.1479 0.2223 0.0274  -0.0180 -0.0097 129 ALA   B CA  
4796 C C   . ALA   B 129 ? 0.1737 0.1414 0.2092 0.0188  0.0010  -0.0023 129 ALA   B C   
4797 O O   . ALA   B 129 ? 0.1639 0.1468 0.2079 0.0128  -0.0085 0.0102  129 ALA   B O   
4798 C CB  . ALA   B 129 ? 0.2049 0.1698 0.2483 0.0320  -0.0074 -0.0195 129 ALA   B CB  
4804 N N   . GLY   B 130 ? 0.1721 0.1357 0.2198 0.0258  0.0075  -0.0044 130 GLY   B N   
4805 C CA  . GLY   B 130 ? 0.1774 0.1442 0.2289 0.0248  0.0207  -0.0047 130 GLY   B CA  
4806 C C   . GLY   B 130 ? 0.1817 0.1468 0.2214 0.0209  0.0179  0.0060  130 GLY   B C   
4807 O O   . GLY   B 130 ? 0.2005 0.1548 0.2253 0.0210  0.0152  0.0156  130 GLY   B O   
4811 N N   . ILE   B 131 ? 0.1727 0.1638 0.2246 0.0266  0.0143  0.0076  131 ILE   B N   
4812 C CA  . ILE   B 131 ? 0.1901 0.1775 0.2209 0.0267  -0.0015 0.0186  131 ILE   B CA  
4813 C C   . ILE   B 131 ? 0.2016 0.1663 0.1913 0.0162  -0.0069 0.0204  131 ILE   B C   
4814 O O   . ILE   B 131 ? 0.2266 0.1797 0.2070 0.0236  -0.0244 0.0164  131 ILE   B O   
4815 C CB  . ILE   B 131 ? 0.1930 0.2148 0.2563 0.0280  -0.0107 0.0211  131 ILE   B CB  
4816 C CG1 . ILE   B 131 ? 0.1959 0.2331 0.2621 0.0080  -0.0033 0.0240  131 ILE   B CG1 
4817 C CG2 . ILE   B 131 ? 0.1963 0.2304 0.2809 0.0338  -0.0048 0.0145  131 ILE   B CG2 
4818 C CD1 . ILE   B 131 ? 0.2046 0.2500 0.2731 -0.0102 -0.0060 0.0300  131 ILE   B CD1 
4830 N N   . PHE   B 132 ? 0.1884 0.1493 0.1838 0.0126  0.0090  0.0207  132 PHE   B N   
4831 C CA  . PHE   B 132 ? 0.1957 0.1505 0.1808 0.0069  0.0255  0.0100  132 PHE   B CA  
4832 C C   . PHE   B 132 ? 0.2130 0.1600 0.1948 0.0096  0.0312  0.0138  132 PHE   B C   
4833 O O   . PHE   B 132 ? 0.2333 0.1836 0.2203 0.0058  0.0440  0.0142  132 PHE   B O   
4834 C CB  . PHE   B 132 ? 0.1785 0.1456 0.1732 0.0139  0.0222  0.0198  132 PHE   B CB  
4835 C CG  . PHE   B 132 ? 0.1755 0.1495 0.1698 0.0171  0.0216  0.0130  132 PHE   B CG  
4836 C CD1 . PHE   B 132 ? 0.1806 0.1540 0.2086 0.0129  0.0227  0.0147  132 PHE   B CD1 
4837 C CD2 . PHE   B 132 ? 0.1800 0.1496 0.1593 0.0207  0.0196  0.0229  132 PHE   B CD2 
4838 C CE1 . PHE   B 132 ? 0.1852 0.1590 0.2161 0.0099  0.0198  0.0181  132 PHE   B CE1 
4839 C CE2 . PHE   B 132 ? 0.1853 0.1569 0.1722 0.0185  0.0116  0.0200  132 PHE   B CE2 
4840 C CZ  . PHE   B 132 ? 0.1889 0.1544 0.2047 0.0133  -0.0001 0.0273  132 PHE   B CZ  
4850 N N   . GLY   B 133 ? 0.2093 0.1481 0.1954 0.0118  0.0259  0.0266  133 GLY   B N   
4851 C CA  . GLY   B 133 ? 0.2196 0.1605 0.2057 -0.0086 0.0278  0.0364  133 GLY   B CA  
4852 C C   . GLY   B 133 ? 0.2222 0.1702 0.2095 -0.0232 0.0349  0.0354  133 GLY   B C   
4853 O O   . GLY   B 133 ? 0.2396 0.1870 0.2540 -0.0359 0.0323  0.0498  133 GLY   B O   
4857 N N   . ALA   B 134 ? 0.2065 0.1675 0.1982 -0.0250 0.0324  0.0169  134 ALA   B N   
4858 C CA  . ALA   B 134 ? 0.2001 0.1637 0.2188 -0.0192 0.0370  0.0051  134 ALA   B CA  
4859 C C   . ALA   B 134 ? 0.2059 0.1588 0.2138 -0.0118 0.0340  0.0187  134 ALA   B C   
4860 O O   . ALA   B 134 ? 0.2142 0.1796 0.2303 0.0002  0.0313  0.0129  134 ALA   B O   
4861 C CB  . ALA   B 134 ? 0.1973 0.1634 0.2449 -0.0130 0.0307  -0.0086 134 ALA   B CB  
4867 N N   . ASP   B 135 ? 0.2173 0.1524 0.2072 -0.0128 0.0138  0.0190  135 ASP   B N   
4868 C CA  . ASP   B 135 ? 0.2371 0.1472 0.2175 -0.0116 0.0013  0.0240  135 ASP   B CA  
4869 C C   . ASP   B 135 ? 0.2231 0.1397 0.2099 -0.0025 0.0024  0.0179  135 ASP   B C   
4870 O O   . ASP   B 135 ? 0.2161 0.1341 0.2216 -0.0035 0.0037  0.0209  135 ASP   B O   
4871 C CB  . ASP   B 135 ? 0.2633 0.1552 0.2448 -0.0291 0.0028  0.0261  135 ASP   B CB  
4872 C CG  . ASP   B 135 ? 0.2902 0.1616 0.2910 -0.0484 0.0016  0.0170  135 ASP   B CG  
4873 O OD1 . ASP   B 135 ? 0.2991 0.1492 0.2878 -0.0346 -0.0065 0.0164  135 ASP   B OD1 
4874 O OD2 . ASP   B 135 ? 0.3133 0.1989 0.3418 -0.0611 -0.0044 -0.0028 135 ASP   B OD2 
4879 N N   . PRO   B 136 ? 0.2151 0.1416 0.2154 0.0163  -0.0072 0.0140  136 PRO   B N   
4880 C CA  . PRO   B 136 ? 0.1960 0.1369 0.2121 0.0164  -0.0017 0.0061  136 PRO   B CA  
4881 C C   . PRO   B 136 ? 0.1749 0.1271 0.2137 0.0110  -0.0002 0.0043  136 PRO   B C   
4882 O O   . PRO   B 136 ? 0.1582 0.1262 0.2059 0.0078  -0.0004 0.0058  136 PRO   B O   
4883 C CB  . PRO   B 136 ? 0.2025 0.1581 0.2286 0.0296  -0.0062 -0.0012 136 PRO   B CB  
4884 C CG  . PRO   B 136 ? 0.2181 0.1605 0.2434 0.0335  -0.0087 -0.0017 136 PRO   B CG  
4885 C CD  . PRO   B 136 ? 0.2204 0.1546 0.2343 0.0368  -0.0060 0.0045  136 PRO   B CD  
4893 N N   . ILE   B 137 ? 0.1824 0.1187 0.2305 0.0089  -0.0096 0.0055  137 ILE   B N   
4894 C CA  . ILE   B 137 ? 0.1904 0.1173 0.2475 -0.0039 -0.0010 0.0024  137 ILE   B CA  
4895 C C   . ILE   B 137 ? 0.1838 0.1249 0.2257 -0.0074 0.0099  0.0112  137 ILE   B C   
4896 O O   . ILE   B 137 ? 0.1722 0.1238 0.2262 -0.0109 0.0081  0.0072  137 ILE   B O   
4897 C CB  . ILE   B 137 ? 0.2137 0.1251 0.2930 -0.0043 -0.0018 0.0037  137 ILE   B CB  
4898 C CG1 . ILE   B 137 ? 0.2438 0.1413 0.3309 0.0030  0.0043  -0.0137 137 ILE   B CG1 
4899 C CG2 . ILE   B 137 ? 0.2168 0.1305 0.3100 -0.0246 -0.0069 0.0114  137 ILE   B CG2 
4900 C CD1 . ILE   B 137 ? 0.2690 0.1665 0.3659 0.0135  0.0022  -0.0095 137 ILE   B CD1 
4912 N N   . HIS   B 138 ? 0.1897 0.1228 0.2159 -0.0065 0.0145  0.0126  138 HIS   B N   
4913 C CA  . HIS   B 138 ? 0.1930 0.1327 0.2163 -0.0043 0.0278  0.0100  138 HIS   B CA  
4914 C C   . HIS   B 138 ? 0.1742 0.1268 0.2040 -0.0010 0.0311  0.0148  138 HIS   B C   
4915 O O   . HIS   B 138 ? 0.1658 0.1356 0.2201 0.0027  0.0334  0.0315  138 HIS   B O   
4916 C CB  . HIS   B 138 ? 0.2140 0.1439 0.2342 -0.0047 0.0391  0.0098  138 HIS   B CB  
4917 C CG  . HIS   B 138 ? 0.2307 0.1647 0.2388 -0.0113 0.0538  0.0259  138 HIS   B CG  
4918 N ND1 . HIS   B 138 ? 0.2381 0.1847 0.2607 -0.0087 0.0680  0.0203  138 HIS   B ND1 
4919 C CD2 . HIS   B 138 ? 0.2453 0.1746 0.2421 -0.0124 0.0585  0.0188  138 HIS   B CD2 
4920 C CE1 . HIS   B 138 ? 0.2436 0.1821 0.2617 -0.0041 0.0718  0.0188  138 HIS   B CE1 
4921 N NE2 . HIS   B 138 ? 0.2521 0.1711 0.2487 -0.0017 0.0672  0.0130  138 HIS   B NE2 
4929 N N   . SER   B 139 ? 0.1717 0.1160 0.2017 0.0051  0.0235  0.0040  139 SER   B N   
4930 C CA  . SER   B 139 ? 0.1648 0.1138 0.1965 0.0043  0.0247  0.0006  139 SER   B CA  
4931 C C   . SER   B 139 ? 0.1441 0.1088 0.1878 0.0010  0.0228  0.0004  139 SER   B C   
4932 O O   . SER   B 139 ? 0.1471 0.1113 0.1883 -0.0008 0.0076  0.0045  139 SER   B O   
4933 C CB  . SER   B 139 ? 0.1742 0.1166 0.1975 0.0030  0.0055  0.0060  139 SER   B CB  
4934 O OG  . SER   B 139 ? 0.1771 0.1185 0.1972 -0.0028 -0.0062 0.0057  139 SER   B OG  
4940 N N   . LEU   B 140 ? 0.1471 0.1078 0.1880 -0.0030 0.0185  -0.0071 140 LEU   B N   
4941 C CA  . LEU   B 140 ? 0.1370 0.1085 0.1928 -0.0034 0.0138  -0.0009 140 LEU   B CA  
4942 C C   . LEU   B 140 ? 0.1336 0.1095 0.2003 -0.0036 0.0040  -0.0056 140 LEU   B C   
4943 O O   . LEU   B 140 ? 0.1348 0.1141 0.1958 -0.0014 0.0033  -0.0036 140 LEU   B O   
4944 C CB  . LEU   B 140 ? 0.1348 0.1072 0.2101 -0.0040 0.0182  -0.0063 140 LEU   B CB  
4945 C CG  . LEU   B 140 ? 0.1442 0.1139 0.1983 -0.0101 0.0086  0.0048  140 LEU   B CG  
4946 C CD1 . LEU   B 140 ? 0.1476 0.1262 0.2040 -0.0122 0.0128  -0.0031 140 LEU   B CD1 
4947 C CD2 . LEU   B 140 ? 0.1618 0.1215 0.2050 -0.0111 0.0015  -0.0073 140 LEU   B CD2 
4959 N N   . ARG   B 141 ? 0.1280 0.1151 0.2099 -0.0112 0.0084  -0.0064 141 ARG   B N   
4960 C CA  . ARG   B 141 ? 0.1339 0.1147 0.2469 -0.0146 0.0280  -0.0043 141 ARG   B CA  
4961 C C   . ARG   B 141 ? 0.1324 0.1136 0.2194 -0.0120 0.0185  -0.0032 141 ARG   B C   
4962 O O   . ARG   B 141 ? 0.1384 0.1163 0.2124 -0.0103 0.0113  -0.0092 141 ARG   B O   
4963 C CB  . ARG   B 141 ? 0.1532 0.1266 0.2869 -0.0185 0.0367  -0.0013 141 ARG   B CB  
4964 C CG  . ARG   B 141 ? 0.1834 0.1552 0.3163 -0.0236 0.0374  0.0059  141 ARG   B CG  
4965 C CD  . ARG   B 141 ? 0.2252 0.1797 0.3269 -0.0183 0.0193  -0.0039 141 ARG   B CD  
4966 N NE  . ARG   B 141 ? 0.2444 0.1786 0.3215 -0.0308 0.0268  -0.0119 141 ARG   B NE  
4967 C CZ  . ARG   B 141 ? 0.2557 0.1645 0.3091 -0.0249 0.0391  -0.0243 141 ARG   B CZ  
4968 N NH1 . ARG   B 141 ? 0.2666 0.1585 0.2986 -0.0222 0.0420  -0.0286 141 ARG   B NH1 
4969 N NH2 . ARG   B 141 ? 0.2685 0.1729 0.3228 -0.0115 0.0283  -0.0140 141 ARG   B NH2 
4983 N N   . VAL   B 142 ? 0.1373 0.1103 0.2077 -0.0093 0.0187  -0.0106 142 VAL   B N   
4984 C CA  . VAL   B 142 ? 0.1308 0.1146 0.2018 -0.0058 0.0217  -0.0092 142 VAL   B CA  
4985 C C   . VAL   B 142 ? 0.1307 0.1143 0.2042 -0.0014 0.0144  -0.0112 142 VAL   B C   
4986 O O   . VAL   B 142 ? 0.1354 0.1138 0.2114 0.0025  0.0160  -0.0027 142 VAL   B O   
4987 C CB  . VAL   B 142 ? 0.1460 0.1233 0.2118 0.0008  0.0231  0.0050  142 VAL   B CB  
4988 C CG1 . VAL   B 142 ? 0.1447 0.1180 0.2223 0.0052  0.0182  -0.0011 142 VAL   B CG1 
4989 C CG2 . VAL   B 142 ? 0.1696 0.1248 0.2153 0.0010  0.0253  0.0036  142 VAL   B CG2 
4999 N N   . CYS   B 143 ? 0.1291 0.1123 0.1874 -0.0035 0.0113  0.0012  143 CYS   B N   
5000 C CA  . CYS   B 143 ? 0.1248 0.1158 0.1913 -0.0058 0.0105  0.0046  143 CYS   B CA  
5001 C C   . CYS   B 143 ? 0.1217 0.1150 0.1901 -0.0058 0.0129  -0.0031 143 CYS   B C   
5002 O O   . CYS   B 143 ? 0.1293 0.1161 0.1955 -0.0046 0.0036  -0.0018 143 CYS   B O   
5003 C CB  . CYS   B 143 ? 0.1282 0.1235 0.1984 -0.0042 0.0084  0.0036  143 CYS   B CB  
5004 S SG  . CYS   B 143 ? 0.1344 0.1379 0.1911 -0.0049 0.0125  0.0023  143 CYS   B SG  
5010 N N   . VAL   B 144 ? 0.1265 0.1181 0.1958 -0.0047 0.0135  -0.0113 144 VAL   B N   
5011 C CA  . VAL   B 144 ? 0.1360 0.1284 0.2203 -0.0125 -0.0036 -0.0238 144 VAL   B CA  
5012 C C   . VAL   B 144 ? 0.1316 0.1256 0.2206 -0.0077 -0.0001 -0.0066 144 VAL   B C   
5013 O O   . VAL   B 144 ? 0.1441 0.1430 0.2368 0.0032  0.0038  0.0144  144 VAL   B O   
5014 C CB  . VAL   B 144 ? 0.1534 0.1379 0.2831 -0.0128 -0.0114 -0.0323 144 VAL   B CB  
5015 C CG1 . VAL   B 144 ? 0.1798 0.1738 0.3202 -0.0036 -0.0186 -0.0302 144 VAL   B CG1 
5016 C CG2 . VAL   B 144 ? 0.1634 0.1368 0.2841 -0.0021 -0.0219 -0.0394 144 VAL   B CG2 
5026 N N   . ASP   B 145 ? 0.1281 0.1193 0.2310 -0.0068 0.0019  -0.0125 145 ASP   B N   
5027 C CA  . ASP   B 145 ? 0.1299 0.1280 0.2502 -0.0056 0.0120  -0.0155 145 ASP   B CA  
5028 C C   . ASP   B 145 ? 0.1243 0.1291 0.2382 -0.0088 0.0166  -0.0124 145 ASP   B C   
5029 O O   . ASP   B 145 ? 0.1305 0.1437 0.2887 -0.0068 0.0159  -0.0294 145 ASP   B O   
5030 C CB  . ASP   B 145 ? 0.1457 0.1309 0.2822 -0.0124 0.0219  -0.0088 145 ASP   B CB  
5031 C CG  . ASP   B 145 ? 0.1618 0.1408 0.3196 -0.0194 0.0314  -0.0032 145 ASP   B CG  
5032 O OD1 . ASP   B 145 ? 0.1654 0.1478 0.3294 -0.0215 -0.0021 -0.0138 145 ASP   B OD1 
5033 O OD2 . ASP   B 145 ? 0.1924 0.1518 0.3680 -0.0226 0.0476  0.0070  145 ASP   B OD2 
5038 N N   . THR   B 146 ? 0.1176 0.1231 0.1947 -0.0076 0.0095  -0.0045 146 THR   B N   
5039 C CA  . THR   B 146 ? 0.1302 0.1135 0.1779 -0.0052 0.0163  -0.0047 146 THR   B CA  
5040 C C   . THR   B 146 ? 0.1279 0.1129 0.1773 -0.0022 0.0082  -0.0012 146 THR   B C   
5041 O O   . THR   B 146 ? 0.1306 0.1146 0.1902 -0.0040 0.0046  0.0010  146 THR   B O   
5042 C CB  . THR   B 146 ? 0.1347 0.1144 0.1958 -0.0013 0.0256  -0.0026 146 THR   B CB  
5043 O OG1 . THR   B 146 ? 0.1364 0.1143 0.2002 -0.0037 0.0206  0.0072  146 THR   B OG1 
5044 C CG2 . THR   B 146 ? 0.1432 0.1257 0.1867 -0.0023 0.0195  -0.0011 146 THR   B CG2 
5052 N N   . VAL   B 147 ? 0.1344 0.1207 0.1667 -0.0028 0.0166  0.0006  147 VAL   B N   
5053 C CA  . VAL   B 147 ? 0.1334 0.1149 0.1574 -0.0129 0.0068  -0.0026 147 VAL   B CA  
5054 C C   . VAL   B 147 ? 0.1251 0.1147 0.1763 -0.0147 -0.0004 -0.0083 147 VAL   B C   
5055 O O   . VAL   B 147 ? 0.1395 0.1248 0.1835 -0.0187 -0.0175 -0.0098 147 VAL   B O   
5056 C CB  . VAL   B 147 ? 0.1343 0.1281 0.1602 -0.0075 -0.0013 -0.0027 147 VAL   B CB  
5057 C CG1 . VAL   B 147 ? 0.1328 0.1420 0.1548 -0.0120 -0.0025 0.0036  147 VAL   B CG1 
5058 C CG2 . VAL   B 147 ? 0.1395 0.1264 0.1609 -0.0078 0.0001  0.0002  147 VAL   B CG2 
5068 N N   . ARG   B 148 ? 0.1277 0.1154 0.1743 -0.0095 -0.0102 -0.0126 148 ARG   B N   
5069 C CA  . ARG   B 148 ? 0.1296 0.1262 0.1668 -0.0068 -0.0178 -0.0138 148 ARG   B CA  
5070 C C   . ARG   B 148 ? 0.1358 0.1323 0.1531 -0.0065 -0.0161 -0.0082 148 ARG   B C   
5071 O O   . ARG   B 148 ? 0.1581 0.1602 0.1551 -0.0199 -0.0267 -0.0045 148 ARG   B O   
5072 C CB  . ARG   B 148 ? 0.1342 0.1362 0.1734 -0.0020 -0.0183 -0.0160 148 ARG   B CB  
5073 C CG  . ARG   B 148 ? 0.1363 0.1507 0.1892 -0.0093 -0.0146 -0.0301 148 ARG   B CG  
5074 C CD  . ARG   B 148 ? 0.1444 0.1649 0.1982 0.0038  -0.0171 -0.0273 148 ARG   B CD  
5075 N NE  . ARG   B 148 ? 0.1484 0.1598 0.1863 0.0178  -0.0193 -0.0265 148 ARG   B NE  
5076 C CZ  . ARG   B 148 ? 0.1424 0.1530 0.1716 0.0150  -0.0141 -0.0214 148 ARG   B CZ  
5077 N NH1 . ARG   B 148 ? 0.1379 0.1580 0.1771 -0.0022 0.0017  -0.0195 148 ARG   B NH1 
5078 N NH2 . ARG   B 148 ? 0.1597 0.1411 0.1709 0.0162  -0.0144 -0.0148 148 ARG   B NH2 
5092 N N   . THR   B 149 ? 0.1365 0.1269 0.1613 -0.0108 -0.0180 -0.0010 149 THR   B N   
5093 C CA  . THR   B 149 ? 0.1417 0.1322 0.1510 -0.0131 -0.0171 0.0042  149 THR   B CA  
5094 C C   . THR   B 149 ? 0.1432 0.1274 0.1394 -0.0128 -0.0175 0.0010  149 THR   B C   
5095 O O   . THR   B 149 ? 0.1511 0.1250 0.1556 -0.0161 -0.0081 -0.0037 149 THR   B O   
5096 C CB  . THR   B 149 ? 0.1442 0.1304 0.1565 -0.0143 -0.0146 -0.0018 149 THR   B CB  
5097 O OG1 . THR   B 149 ? 0.1452 0.1351 0.1498 -0.0217 -0.0198 -0.0008 149 THR   B OG1 
5098 C CG2 . THR   B 149 ? 0.1494 0.1321 0.1756 -0.0040 -0.0096 -0.0036 149 THR   B CG2 
5106 N N   . ASN   B 150 ? 0.1466 0.1269 0.1466 -0.0119 -0.0225 -0.0026 150 ASN   B N   
5107 C CA  . ASN   B 150 ? 0.1522 0.1396 0.1409 -0.0143 -0.0154 -0.0121 150 ASN   B CA  
5108 C C   . ASN   B 150 ? 0.1418 0.1321 0.1438 -0.0115 -0.0185 -0.0084 150 ASN   B C   
5109 O O   . ASN   B 150 ? 0.1519 0.1334 0.1743 -0.0194 -0.0395 0.0004  150 ASN   B O   
5110 C CB  . ASN   B 150 ? 0.1662 0.1724 0.1537 -0.0189 -0.0230 0.0026  150 ASN   B CB  
5111 C CG  . ASN   B 150 ? 0.1915 0.2167 0.1898 -0.0178 -0.0301 0.0226  150 ASN   B CG  
5112 O OD1 . ASN   B 150 ? 0.2027 0.2314 0.2107 -0.0280 -0.0485 0.0183  150 ASN   B OD1 
5113 N ND2 . ASN   B 150 ? 0.1996 0.2359 0.2236 -0.0057 -0.0352 0.0616  150 ASN   B ND2 
5120 N N   . VAL   B 151 ? 0.1333 0.1328 0.1377 -0.0129 -0.0211 -0.0019 151 VAL   B N   
5121 C CA  . VAL   B 151 ? 0.1306 0.1328 0.1423 -0.0201 -0.0159 -0.0045 151 VAL   B CA  
5122 C C   . VAL   B 151 ? 0.1358 0.1256 0.1410 -0.0254 -0.0147 -0.0074 151 VAL   B C   
5123 O O   . VAL   B 151 ? 0.1437 0.1353 0.1650 -0.0228 -0.0050 -0.0166 151 VAL   B O   
5124 C CB  . VAL   B 151 ? 0.1538 0.1484 0.1543 -0.0064 -0.0101 -0.0053 151 VAL   B CB  
5125 C CG1 . VAL   B 151 ? 0.1652 0.1466 0.1882 -0.0126 0.0022  -0.0160 151 VAL   B CG1 
5126 C CG2 . VAL   B 151 ? 0.1736 0.1661 0.1459 0.0053  -0.0097 0.0051  151 VAL   B CG2 
5136 N N   . TYR   B 152 ? 0.1333 0.1172 0.1395 -0.0213 -0.0124 -0.0077 152 TYR   B N   
5137 C CA  . TYR   B 152 ? 0.1386 0.1337 0.1325 -0.0235 -0.0062 -0.0115 152 TYR   B CA  
5138 C C   . TYR   B 152 ? 0.1326 0.1186 0.1281 -0.0165 -0.0042 -0.0080 152 TYR   B C   
5139 O O   . TYR   B 152 ? 0.1407 0.1220 0.1345 -0.0217 -0.0051 -0.0046 152 TYR   B O   
5140 C CB  . TYR   B 152 ? 0.1470 0.1437 0.1370 -0.0193 -0.0066 -0.0031 152 TYR   B CB  
5141 C CG  . TYR   B 152 ? 0.1629 0.1471 0.1289 -0.0297 -0.0087 -0.0015 152 TYR   B CG  
5142 C CD1 . TYR   B 152 ? 0.1751 0.1621 0.1296 -0.0157 -0.0152 0.0046  152 TYR   B CD1 
5143 C CD2 . TYR   B 152 ? 0.1824 0.1659 0.1361 -0.0293 -0.0088 0.0009  152 TYR   B CD2 
5144 C CE1 . TYR   B 152 ? 0.1904 0.1780 0.1459 -0.0171 -0.0196 0.0142  152 TYR   B CE1 
5145 C CE2 . TYR   B 152 ? 0.1958 0.1879 0.1335 -0.0290 -0.0123 -0.0008 152 TYR   B CE2 
5146 C CZ  . TYR   B 152 ? 0.2005 0.1986 0.1352 -0.0235 -0.0330 0.0170  152 TYR   B CZ  
5147 O OH  . TYR   B 152 ? 0.2230 0.2320 0.1658 -0.0132 -0.0338 0.0155  152 TYR   B OH  
5157 N N   . LEU   B 153 ? 0.1358 0.1189 0.1376 -0.0225 -0.0042 -0.0095 153 LEU   B N   
5158 C CA  . LEU   B 153 ? 0.1400 0.1155 0.1231 -0.0178 0.0032  -0.0110 153 LEU   B CA  
5159 C C   . LEU   B 153 ? 0.1375 0.1156 0.1374 -0.0194 -0.0034 -0.0139 153 LEU   B C   
5160 O O   . LEU   B 153 ? 0.1466 0.1371 0.1524 -0.0103 -0.0037 -0.0317 153 LEU   B O   
5161 C CB  . LEU   B 153 ? 0.1434 0.1152 0.1526 -0.0187 0.0039  -0.0096 153 LEU   B CB  
5162 C CG  . LEU   B 153 ? 0.1360 0.1245 0.1673 -0.0204 0.0002  -0.0016 153 LEU   B CG  
5163 C CD1 . LEU   B 153 ? 0.1420 0.1375 0.1729 -0.0212 0.0054  0.0014  153 LEU   B CD1 
5164 C CD2 . LEU   B 153 ? 0.1395 0.1344 0.1710 -0.0251 0.0095  -0.0043 153 LEU   B CD2 
5176 N N   . ALA   B 154 ? 0.1366 0.1168 0.1403 -0.0045 -0.0096 -0.0125 154 ALA   B N   
5177 C CA  . ALA   B 154 ? 0.1484 0.1260 0.1577 0.0040  -0.0132 -0.0227 154 ALA   B CA  
5178 C C   . ALA   B 154 ? 0.1604 0.1280 0.1668 0.0059  -0.0242 -0.0259 154 ALA   B C   
5179 O O   . ALA   B 154 ? 0.1911 0.1355 0.1873 0.0084  -0.0094 -0.0115 154 ALA   B O   
5180 C CB  . ALA   B 154 ? 0.1473 0.1479 0.1875 0.0009  -0.0112 -0.0269 154 ALA   B CB  
5186 N N   . VAL   B 155 ? 0.1350 0.1183 0.1835 -0.0005 -0.0066 -0.0158 155 VAL   B N   
5187 C CA  . VAL   B 155 ? 0.1287 0.1171 0.1957 -0.0003 -0.0093 -0.0053 155 VAL   B CA  
5188 C C   . VAL   B 155 ? 0.1306 0.1201 0.1922 -0.0008 -0.0076 -0.0177 155 VAL   B C   
5189 O O   . VAL   B 155 ? 0.1475 0.1409 0.2126 0.0072  -0.0075 -0.0339 155 VAL   B O   
5190 C CB  . VAL   B 155 ? 0.1353 0.1330 0.2274 -0.0004 -0.0140 0.0026  155 VAL   B CB  
5191 C CG1 . VAL   B 155 ? 0.1375 0.1299 0.2321 -0.0083 -0.0112 -0.0041 155 VAL   B CG1 
5192 C CG2 . VAL   B 155 ? 0.1303 0.1482 0.2527 -0.0023 -0.0109 0.0251  155 VAL   B CG2 
5202 N N   . PHE   B 156 ? 0.1231 0.1311 0.2078 0.0028  -0.0019 -0.0144 156 PHE   B N   
5203 C CA  . PHE   B 156 ? 0.1235 0.1397 0.2364 0.0058  -0.0057 -0.0139 156 PHE   B CA  
5204 C C   . PHE   B 156 ? 0.1270 0.1458 0.2584 0.0128  -0.0123 -0.0325 156 PHE   B C   
5205 O O   . PHE   B 156 ? 0.1478 0.1685 0.2808 0.0214  0.0020  -0.0340 156 PHE   B O   
5206 C CB  . PHE   B 156 ? 0.1315 0.1338 0.2351 -0.0030 -0.0163 -0.0038 156 PHE   B CB  
5207 C CG  . PHE   B 156 ? 0.1318 0.1430 0.2500 -0.0019 -0.0180 0.0104  156 PHE   B CG  
5208 C CD1 . PHE   B 156 ? 0.1392 0.1712 0.2876 0.0056  -0.0070 0.0439  156 PHE   B CD1 
5209 C CD2 . PHE   B 156 ? 0.1426 0.1519 0.2514 0.0065  -0.0289 0.0158  156 PHE   B CD2 
5210 C CE1 . PHE   B 156 ? 0.1432 0.1895 0.3059 0.0051  -0.0104 0.0464  156 PHE   B CE1 
5211 C CE2 . PHE   B 156 ? 0.1508 0.1760 0.2762 0.0121  -0.0216 0.0228  156 PHE   B CE2 
5212 C CZ  . PHE   B 156 ? 0.1408 0.1878 0.2980 0.0139  -0.0225 0.0307  156 PHE   B CZ  
5222 N N   . ASP   B 157 ? 0.1280 0.1336 0.2784 0.0103  -0.0229 -0.0175 157 ASP   B N   
5223 C CA  . ASP   B 157 ? 0.1385 0.1405 0.3087 0.0072  -0.0274 -0.0247 157 ASP   B CA  
5224 C C   . ASP   B 157 ? 0.1395 0.1349 0.3112 0.0094  -0.0255 -0.0424 157 ASP   B C   
5225 O O   . ASP   B 157 ? 0.1320 0.1376 0.2911 0.0032  -0.0227 -0.0329 157 ASP   B O   
5226 C CB  . ASP   B 157 ? 0.1656 0.1578 0.3280 0.0041  -0.0475 -0.0080 157 ASP   B CB  
5227 C CG  . ASP   B 157 ? 0.1997 0.1748 0.3487 -0.0017 -0.0331 -0.0051 157 ASP   B CG  
5228 O OD1 . ASP   B 157 ? 0.2052 0.1685 0.3631 0.0029  -0.0267 -0.0031 157 ASP   B OD1 
5229 O OD2 . ASP   B 157 ? 0.2312 0.1961 0.3763 -0.0049 -0.0140 -0.0018 157 ASP   B OD2 
5234 N N   . LYS   B 158 ? 0.1410 0.1581 0.3263 0.0084  -0.0145 -0.0630 158 LYS   B N   
5235 C CA  . LYS   B 158 ? 0.1539 0.1735 0.3326 0.0084  -0.0060 -0.0726 158 LYS   B CA  
5236 C C   . LYS   B 158 ? 0.1522 0.1601 0.3327 0.0107  -0.0081 -0.0690 158 LYS   B C   
5237 O O   . LYS   B 158 ? 0.1595 0.1606 0.3348 -0.0001 -0.0120 -0.0764 158 LYS   B O   
5238 C CB  . LYS   B 158 ? 0.1739 0.2068 0.3322 0.0104  0.0105  -0.0939 158 LYS   B CB  
5239 C CG  . LYS   B 158 ? 0.2054 0.2456 0.3360 0.0138  0.0191  -0.0976 158 LYS   B CG  
5240 C CD  . LYS   B 158 ? 0.2354 0.2923 0.3506 0.0132  0.0218  -0.0915 158 LYS   B CD  
5241 C CE  . LYS   B 158 ? 0.2557 0.3265 0.3642 0.0185  0.0215  -0.0858 158 LYS   B CE  
5242 N NZ  . LYS   B 158 ? 0.2511 0.3349 0.3654 0.0175  0.0230  -0.0815 158 LYS   B NZ  
5256 N N   . ASN   B 159 ? 0.1587 0.1552 0.3472 0.0090  -0.0161 -0.0538 159 ASN   B N   
5257 C CA  . ASN   B 159 ? 0.1734 0.1478 0.3657 0.0212  -0.0260 -0.0451 159 ASN   B CA  
5258 C C   . ASN   B 159 ? 0.1593 0.1367 0.3571 0.0150  -0.0384 -0.0374 159 ASN   B C   
5259 O O   . ASN   B 159 ? 0.1606 0.1363 0.3634 0.0005  -0.0384 -0.0336 159 ASN   B O   
5260 C CB  . ASN   B 159 ? 0.1952 0.1622 0.3923 0.0276  -0.0325 -0.0340 159 ASN   B CB  
5261 C CG  . ASN   B 159 ? 0.2202 0.1848 0.4226 0.0262  -0.0428 -0.0434 159 ASN   B CG  
5262 O OD1 . ASN   B 159 ? 0.2337 0.1950 0.4227 0.0328  -0.0422 -0.0546 159 ASN   B OD1 
5263 N ND2 . ASN   B 159 ? 0.2247 0.1959 0.4387 0.0304  -0.0516 -0.0375 159 ASN   B ND2 
5270 N N   . LEU   B 160 ? 0.1477 0.1352 0.3373 0.0075  -0.0375 -0.0268 160 LEU   B N   
5271 C CA  . LEU   B 160 ? 0.1439 0.1387 0.2962 0.0095  -0.0287 -0.0184 160 LEU   B CA  
5272 C C   . LEU   B 160 ? 0.1398 0.1300 0.2861 0.0010  -0.0221 -0.0320 160 LEU   B C   
5273 O O   . LEU   B 160 ? 0.1304 0.1351 0.2665 -0.0045 -0.0207 -0.0215 160 LEU   B O   
5274 C CB  . LEU   B 160 ? 0.1443 0.1420 0.2698 0.0062  -0.0284 -0.0126 160 LEU   B CB  
5275 C CG  . LEU   B 160 ? 0.1492 0.1549 0.2433 0.0108  -0.0293 -0.0066 160 LEU   B CG  
5276 C CD1 . LEU   B 160 ? 0.1615 0.1711 0.2470 0.0038  -0.0213 -0.0116 160 LEU   B CD1 
5277 C CD2 . LEU   B 160 ? 0.1546 0.1608 0.2482 0.0260  -0.0310 -0.0170 160 LEU   B CD2 
5289 N N   . TYR   B 161 ? 0.1349 0.1346 0.2896 -0.0034 -0.0065 -0.0360 161 TYR   B N   
5290 C CA  . TYR   B 161 ? 0.1397 0.1345 0.2736 -0.0103 0.0114  -0.0385 161 TYR   B CA  
5291 C C   . TYR   B 161 ? 0.1396 0.1374 0.2599 -0.0094 0.0171  -0.0324 161 TYR   B C   
5292 O O   . TYR   B 161 ? 0.1436 0.1347 0.2482 -0.0115 0.0070  -0.0307 161 TYR   B O   
5293 C CB  . TYR   B 161 ? 0.1513 0.1434 0.2693 -0.0160 0.0260  -0.0459 161 TYR   B CB  
5294 C CG  . TYR   B 161 ? 0.1717 0.1467 0.2606 -0.0209 0.0405  -0.0464 161 TYR   B CG  
5295 C CD1 . TYR   B 161 ? 0.1786 0.1427 0.2548 -0.0316 0.0305  -0.0466 161 TYR   B CD1 
5296 C CD2 . TYR   B 161 ? 0.1971 0.1600 0.2558 -0.0158 0.0333  -0.0478 161 TYR   B CD2 
5297 C CE1 . TYR   B 161 ? 0.1954 0.1566 0.2667 -0.0295 0.0290  -0.0425 161 TYR   B CE1 
5298 C CE2 . TYR   B 161 ? 0.2137 0.1690 0.2684 -0.0227 0.0313  -0.0416 161 TYR   B CE2 
5299 C CZ  . TYR   B 161 ? 0.2090 0.1718 0.2719 -0.0329 0.0274  -0.0346 161 TYR   B CZ  
5300 O OH  . TYR   B 161 ? 0.2367 0.1988 0.2912 -0.0378 0.0289  -0.0283 161 TYR   B OH  
5310 N N   . ASP   B 162 ? 0.1451 0.1355 0.2739 -0.0064 0.0019  -0.0466 162 ASP   B N   
5311 C CA  . ASP   B 162 ? 0.1612 0.1430 0.2748 -0.0035 -0.0046 -0.0532 162 ASP   B CA  
5312 C C   . ASP   B 162 ? 0.1588 0.1322 0.2718 -0.0083 -0.0040 -0.0489 162 ASP   B C   
5313 O O   . ASP   B 162 ? 0.1653 0.1403 0.2695 -0.0148 -0.0131 -0.0356 162 ASP   B O   
5314 C CB  . ASP   B 162 ? 0.1841 0.1604 0.2985 0.0016  -0.0031 -0.0698 162 ASP   B CB  
5315 C CG  . ASP   B 162 ? 0.1863 0.1831 0.3168 0.0062  -0.0006 -0.0789 162 ASP   B CG  
5316 O OD1 . ASP   B 162 ? 0.1845 0.2022 0.3099 0.0050  0.0121  -0.0705 162 ASP   B OD1 
5317 O OD2 . ASP   B 162 ? 0.2025 0.2026 0.3533 0.0192  0.0076  -0.0775 162 ASP   B OD2 
5322 N N   . LYS   B 163 ? 0.1567 0.1242 0.2738 -0.0111 -0.0183 -0.0340 163 LYS   B N   
5323 C CA  . LYS   B 163 ? 0.1684 0.1368 0.2705 -0.0204 -0.0163 -0.0149 163 LYS   B CA  
5324 C C   . LYS   B 163 ? 0.1404 0.1290 0.2527 -0.0178 -0.0203 -0.0030 163 LYS   B C   
5325 O O   . LYS   B 163 ? 0.1418 0.1393 0.2857 -0.0188 -0.0166 -0.0043 163 LYS   B O   
5326 C CB  . LYS   B 163 ? 0.2086 0.1691 0.3113 -0.0197 -0.0186 0.0036  163 LYS   B CB  
5327 C CG  . LYS   B 163 ? 0.2857 0.2530 0.3849 -0.0282 -0.0167 0.0099  163 LYS   B CG  
5328 C CD  . LYS   B 163 ? 0.3617 0.3384 0.4570 -0.0370 -0.0225 0.0065  163 LYS   B CD  
5329 C CE  . LYS   B 163 ? 0.4159 0.4002 0.5034 -0.0439 -0.0233 0.0078  163 LYS   B CE  
5330 N NZ  . LYS   B 163 ? 0.4425 0.4424 0.5370 -0.0468 -0.0239 0.0064  163 LYS   B NZ  
5344 N N   . LEU   B 164 ? 0.1243 0.1266 0.2297 -0.0141 -0.0166 -0.0059 164 LEU   B N   
5345 C CA  . LEU   B 164 ? 0.1306 0.1204 0.2132 -0.0091 -0.0208 -0.0004 164 LEU   B CA  
5346 C C   . LEU   B 164 ? 0.1351 0.1271 0.2127 -0.0134 -0.0266 -0.0077 164 LEU   B C   
5347 O O   . LEU   B 164 ? 0.1395 0.1445 0.2381 -0.0086 -0.0239 -0.0100 164 LEU   B O   
5348 C CB  . LEU   B 164 ? 0.1323 0.1220 0.2057 -0.0070 -0.0191 -0.0051 164 LEU   B CB  
5349 C CG  . LEU   B 164 ? 0.1402 0.1343 0.2139 -0.0098 -0.0102 -0.0012 164 LEU   B CG  
5350 C CD1 . LEU   B 164 ? 0.1454 0.1369 0.2156 -0.0086 -0.0219 -0.0093 164 LEU   B CD1 
5351 C CD2 . LEU   B 164 ? 0.1584 0.1705 0.2272 -0.0059 0.0039  -0.0220 164 LEU   B CD2 
5363 N N   . VAL   B 165 ? 0.1599 0.1335 0.2287 -0.0147 -0.0223 -0.0175 165 VAL   B N   
5364 C CA  . VAL   B 165 ? 0.1938 0.1448 0.2249 -0.0232 -0.0379 -0.0112 165 VAL   B CA  
5365 C C   . VAL   B 165 ? 0.2149 0.1535 0.2508 -0.0313 -0.0680 -0.0094 165 VAL   B C   
5366 O O   . VAL   B 165 ? 0.2282 0.1664 0.2566 -0.0396 -0.0712 -0.0050 165 VAL   B O   
5367 C CB  . VAL   B 165 ? 0.2143 0.1624 0.2265 -0.0138 -0.0142 -0.0188 165 VAL   B CB  
5368 C CG1 . VAL   B 165 ? 0.2316 0.1704 0.2510 -0.0165 -0.0063 -0.0181 165 VAL   B CG1 
5369 C CG2 . VAL   B 165 ? 0.2078 0.1712 0.2282 -0.0130 -0.0065 -0.0128 165 VAL   B CG2 
5379 N N   . SER   B 166 ? 0.2233 0.1426 0.2848 -0.0311 -0.0727 -0.0270 166 SER   B N   
5380 C CA  . SER   B 166 ? 0.2185 0.1469 0.3320 -0.0364 -0.0655 -0.0335 166 SER   B CA  
5381 C C   . SER   B 166 ? 0.2067 0.1568 0.3501 -0.0372 -0.0631 -0.0136 166 SER   B C   
5382 O O   . SER   B 166 ? 0.2114 0.1753 0.3835 -0.0454 -0.0763 -0.0324 166 SER   B O   
5383 C CB  . SER   B 166 ? 0.2219 0.1567 0.3545 -0.0255 -0.0561 -0.0385 166 SER   B CB  
5384 O OG  . SER   B 166 ? 0.2143 0.1541 0.3713 -0.0158 -0.0514 -0.0169 166 SER   B OG  
5390 N N   . SER   B 167 ? 0.1929 0.1517 0.3248 -0.0360 -0.0599 0.0185  167 SER   B N   
5391 C CA  . SER   B 167 ? 0.1845 0.1537 0.3105 -0.0337 -0.0396 0.0251  167 SER   B CA  
5392 C C   . SER   B 167 ? 0.1765 0.1643 0.3022 -0.0466 -0.0357 0.0451  167 SER   B C   
5393 O O   . SER   B 167 ? 0.1801 0.1756 0.2914 -0.0529 -0.0336 0.0479  167 SER   B O   
5394 C CB  . SER   B 167 ? 0.1780 0.1606 0.3012 -0.0275 -0.0129 0.0273  167 SER   B CB  
5395 O OG  . SER   B 167 ? 0.1744 0.1722 0.2892 -0.0181 -0.0071 0.0224  167 SER   B OG  
5401 N N   . PHE   B 168 ? 0.1733 0.1594 0.2981 -0.0417 -0.0230 0.0498  168 PHE   B N   
5402 C CA  . PHE   B 168 ? 0.1822 0.1564 0.2821 -0.0418 -0.0223 0.0293  168 PHE   B CA  
5403 C C   . PHE   B 168 ? 0.1620 0.1466 0.2413 -0.0194 -0.0062 0.0154  168 PHE   B C   
5404 O O   . PHE   B 168 ? 0.1908 0.1404 0.2453 0.0020  -0.0042 0.0048  168 PHE   B O   
5405 C CB  . PHE   B 168 ? 0.1965 0.1595 0.2828 -0.0514 -0.0392 0.0439  168 PHE   B CB  
5406 C CG  . PHE   B 168 ? 0.2234 0.1489 0.2732 -0.0526 -0.0441 0.0218  168 PHE   B CG  
5407 C CD1 . PHE   B 168 ? 0.2569 0.1514 0.2780 -0.0473 -0.0555 0.0130  168 PHE   B CD1 
5408 C CD2 . PHE   B 168 ? 0.2129 0.1433 0.2711 -0.0466 -0.0418 0.0327  168 PHE   B CD2 
5409 C CE1 . PHE   B 168 ? 0.2686 0.1644 0.2846 -0.0305 -0.0470 0.0189  168 PHE   B CE1 
5410 C CE2 . PHE   B 168 ? 0.2386 0.1546 0.2754 -0.0303 -0.0475 0.0262  168 PHE   B CE2 
5411 C CZ  . PHE   B 168 ? 0.2560 0.1519 0.2752 -0.0208 -0.0514 0.0329  168 PHE   B CZ  
5421 N N   . LEU   B 169 ? 0.1675 0.1639 0.2414 -0.0025 -0.0009 0.0000  169 LEU   B N   
5422 C CA  . LEU   B 169 ? 0.1977 0.1938 0.2816 -0.0096 -0.0050 -0.0242 169 LEU   B CA  
5423 C C   . LEU   B 169 ? 0.2222 0.2177 0.3390 0.0060  -0.0064 -0.0520 169 LEU   B C   
5424 O O   . LEU   B 169 ? 0.2424 0.2358 0.3856 0.0056  0.0001  -0.0717 169 LEU   B O   
5425 C CB  . LEU   B 169 ? 0.2194 0.2289 0.2925 -0.0149 -0.0118 0.0010  169 LEU   B CB  
5426 C CG  . LEU   B 169 ? 0.2558 0.2608 0.3302 -0.0055 -0.0136 0.0090  169 LEU   B CG  
5427 C CD1 . LEU   B 169 ? 0.2676 0.2800 0.3406 -0.0038 -0.0167 0.0230  169 LEU   B CD1 
5428 C CD2 . LEU   B 169 ? 0.2552 0.2673 0.3369 0.0060  -0.0009 0.0028  169 LEU   B CD2 
5429 O OXT . LEU   B 169 ? 0.2352 0.2315 0.3396 0.0318  -0.0061 -0.0529 169 LEU   B OXT 
5441 N N2  B A1A41 C .   ? 0.3046 0.3023 0.2696 -0.0054 0.0078  -0.0013 201 A1A41 A N2  
5442 C C3  B A1A41 C .   ? 0.3097 0.3098 0.2984 -0.0044 0.0118  -0.0022 201 A1A41 A C3  
5443 C C6  B A1A41 C .   ? 0.3214 0.3221 0.3277 0.0010  0.0083  -0.0016 201 A1A41 A C6  
5444 C C9  B A1A41 C .   ? 0.3218 0.3227 0.3230 0.0018  0.0091  -0.0024 201 A1A41 A C9  
5445 C C1  B A1A41 C .   ? 0.3048 0.3031 0.2667 -0.0061 0.0073  0.0002  201 A1A41 A C1  
5446 C C10 B A1A41 C .   ? 0.3214 0.3223 0.3238 0.0015  0.0090  -0.0025 201 A1A41 A C10 
5447 C C11 B A1A41 C .   ? 0.3205 0.3212 0.3252 0.0005  0.0088  -0.0020 201 A1A41 A C11 
5448 C C2  B A1A41 C .   ? 0.3049 0.3034 0.2768 -0.0060 0.0098  -0.0008 201 A1A41 A C2  
5449 C C4  B A1A41 C .   ? 0.3139 0.3143 0.3119 -0.0025 0.0103  -0.0022 201 A1A41 A C4  
5450 C C5  B A1A41 C .   ? 0.3200 0.3207 0.3325 -0.0005 0.0083  -0.0016 201 A1A41 A C5  
5451 C C7  B A1A41 C .   ? 0.3220 0.3227 0.3254 0.0018  0.0085  -0.0015 201 A1A41 A C7  
5452 C C8  B A1A41 C .   ? 0.3221 0.3230 0.3235 0.0021  0.0086  -0.0016 201 A1A41 A C8  
5453 N N1  B A1A41 C .   ? 0.3053 0.3042 0.2682 -0.0061 0.0063  0.0010  201 A1A41 A N1  
5454 N N3  B A1A41 C .   ? 0.3047 0.3028 0.2732 -0.0049 0.0097  -0.0011 201 A1A41 A N3  
5455 N N4  B A1A41 C .   ? 0.3183 0.3189 0.3238 -0.0010 0.0088  -0.0017 201 A1A41 A N4  
5456 O O1  B A1A41 C .   ? 0.3201 0.3211 0.3386 -0.0009 0.0080  -0.0020 201 A1A41 A O1  
5457 O O2  B A1A41 C .   ? 0.3208 0.3215 0.3310 0.0005  0.0080  -0.0016 201 A1A41 A O2  
5458 S S1  B A1A41 C .   ? 0.3059 0.3053 0.2840 -0.0064 0.0137  -0.0020 201 A1A41 A S1  
5459 S S2  B A1A41 C .   ? 0.3051 0.3039 0.2698 -0.0063 0.0082  -0.0001 201 A1A41 A S2  
5470 O O   . HOH   D .   ? 0.3329 0.2266 0.3484 -0.0259 -0.0344 0.0454  301 HOH   A O   
5471 O O   . HOH   D .   ? 0.3787 0.6422 0.4656 -0.0907 0.0821  0.0191  302 HOH   A O   
5472 O O   . HOH   D .   ? 0.3935 0.2518 0.3831 -0.0640 0.0458  0.0288  303 HOH   A O   
5473 O O   . HOH   D .   ? 0.7312 0.5287 0.3453 0.0201  -0.0830 0.0684  304 HOH   A O   
5474 O O   . HOH   D .   ? 0.5785 0.4355 0.3381 0.1777  -0.1082 0.0615  305 HOH   A O   
5475 O O   B HOH   D .   ? 0.3628 0.3657 0.3381 -0.0367 -0.0219 0.0278  306 HOH   A O   
5476 O O   . HOH   D .   ? 0.1790 0.3580 0.3956 -0.0267 0.0331  -0.1356 307 HOH   A O   
5477 O O   . HOH   D .   ? 0.1939 0.1722 0.3563 -0.0336 -0.0028 -0.0174 308 HOH   A O   
5478 O O   . HOH   D .   ? 0.2893 0.3117 0.1598 -0.0392 0.0419  0.0595  309 HOH   A O   
5479 O O   . HOH   D .   ? 0.7002 0.4128 0.5429 -0.0404 -0.1288 0.0010  310 HOH   A O   
5480 O O   . HOH   D .   ? 0.3984 0.3129 0.4587 -0.0022 0.1133  -0.0556 311 HOH   A O   
5481 O O   . HOH   D .   ? 0.3352 0.3424 0.3242 -0.0683 0.1300  -0.0098 312 HOH   A O   
5482 O O   . HOH   D .   ? 0.4638 0.5108 0.2584 -0.1062 0.1375  0.0791  313 HOH   A O   
5483 O O   . HOH   D .   ? 0.1675 0.2793 0.2608 0.0250  -0.0164 -0.0342 314 HOH   A O   
5484 O O   . HOH   D .   ? 0.3098 0.4351 0.2376 -0.0090 0.0634  0.0578  315 HOH   A O   
5485 O O   . HOH   D .   ? 0.2768 0.2277 0.2246 -0.0609 0.0295  0.0283  316 HOH   A O   
5486 O O   . HOH   D .   ? 0.3376 0.1935 0.3880 0.0204  -0.1241 0.0381  317 HOH   A O   
5487 O O   . HOH   D .   ? 0.3803 0.3627 0.3185 -0.0520 -0.0584 -0.0666 318 HOH   A O   
5488 O O   . HOH   D .   ? 0.1473 0.1541 0.1935 -0.0235 0.0081  -0.0014 319 HOH   A O   
5489 O O   . HOH   D .   ? 0.2531 0.2152 0.3703 -0.0196 -0.0938 0.0841  320 HOH   A O   
5490 O O   . HOH   D .   ? 0.4818 0.5524 0.4209 -0.1144 -0.1125 -0.0820 321 HOH   A O   
5491 O O   . HOH   D .   ? 0.4706 0.1864 0.4675 0.0518  0.0279  0.0124  322 HOH   A O   
5492 O O   . HOH   D .   ? 0.2279 0.4995 0.4074 -0.0013 -0.0668 0.1141  323 HOH   A O   
5493 O O   . HOH   D .   ? 0.2097 0.4094 0.4025 0.0005  -0.0609 0.1412  324 HOH   A O   
5494 O O   . HOH   D .   ? 0.5579 0.4631 0.4996 0.0777  0.1862  -0.1317 325 HOH   A O   
5495 O O   . HOH   D .   ? 0.2465 0.2141 0.2299 0.0496  0.0296  0.0322  326 HOH   A O   
5496 O O   . HOH   D .   ? 0.3210 0.3997 0.3443 -0.1292 -0.0935 -0.0306 327 HOH   A O   
5497 O O   . HOH   D .   ? 0.1391 0.3608 0.2681 -0.0109 0.0199  0.0952  328 HOH   A O   
5498 O O   . HOH   D .   ? 0.5468 0.4618 0.4059 -0.1206 0.1364  0.1298  329 HOH   A O   
5499 O O   . HOH   D .   ? 0.3638 0.4876 0.4184 -0.0469 -0.1143 -0.0439 330 HOH   A O   
5500 O O   B HOH   D .   ? 0.1223 0.1427 0.1044 -0.0485 0.0380  0.0277  331 HOH   A O   
5501 O O   . HOH   D .   ? 0.2569 0.4034 0.5329 -0.0164 0.0973  0.2132  332 HOH   A O   
5502 O O   . HOH   D .   ? 0.2385 0.2133 0.2985 -0.0203 0.0518  0.0577  333 HOH   A O   
5503 O O   . HOH   D .   ? 0.4160 0.3829 0.3836 -0.1786 -0.1023 0.1854  334 HOH   A O   
5504 O O   . HOH   D .   ? 0.1416 0.2131 0.1966 0.0064  -0.0137 0.0451  335 HOH   A O   
5505 O O   . HOH   D .   ? 0.1983 0.1619 0.2139 0.0223  -0.0293 -0.0053 336 HOH   A O   
5506 O O   . HOH   D .   ? 0.3454 0.4030 0.3919 0.1789  0.0521  0.0338  337 HOH   A O   
5507 O O   . HOH   D .   ? 0.5351 0.3809 0.2678 0.0355  0.0923  0.1301  338 HOH   A O   
5508 O O   . HOH   D .   ? 0.2375 0.3593 0.3627 0.0899  -0.0706 -0.0235 339 HOH   A O   
5509 O O   . HOH   D .   ? 0.2864 0.3655 0.2184 -0.0745 -0.0271 -0.0697 340 HOH   A O   
5510 O O   . HOH   D .   ? 0.1850 0.1978 0.3368 0.0199  0.0809  -0.0055 341 HOH   A O   
5511 O O   . HOH   D .   ? 0.2163 0.3122 0.3927 0.0386  0.0435  0.0313  342 HOH   A O   
5512 O O   . HOH   D .   ? 0.4455 0.2392 0.3787 -0.1358 0.1559  -0.0556 343 HOH   A O   
5513 O O   . HOH   D .   ? 0.2922 0.1459 0.1579 0.0289  0.0201  0.0240  344 HOH   A O   
5514 O O   . HOH   D .   ? 0.1407 0.1645 0.2423 0.0058  -0.0335 -0.0546 345 HOH   A O   
5515 O O   . HOH   D .   ? 0.1375 0.1776 0.2459 0.0085  -0.0194 0.0007  346 HOH   A O   
5516 O O   . HOH   D .   ? 0.1271 0.1204 0.1168 -0.0019 0.0116  0.0077  347 HOH   A O   
5517 O O   . HOH   D .   ? 0.2625 0.4037 0.3067 -0.0507 0.0639  -0.0188 348 HOH   A O   
5518 O O   . HOH   D .   ? 0.2963 0.2164 0.4697 -0.0554 -0.0127 0.0066  349 HOH   A O   
5519 O O   . HOH   D .   ? 0.5757 0.3952 0.5263 0.0237  -0.0844 0.0555  350 HOH   A O   
5520 O O   . HOH   D .   ? 0.1494 0.1298 0.1911 -0.0076 0.0155  -0.0121 351 HOH   A O   
5521 O O   . HOH   D .   ? 0.1940 0.1859 0.2133 -0.0380 0.0097  0.0313  352 HOH   A O   
5522 O O   . HOH   D .   ? 0.3721 0.2059 0.1906 0.1016  0.0324  0.0078  353 HOH   A O   
5523 O O   . HOH   D .   ? 0.2830 0.3231 0.5150 -0.0525 -0.1001 -0.0956 354 HOH   A O   
5524 O O   . HOH   D .   ? 0.3659 0.2065 0.3955 -0.1007 0.0859  0.0179  355 HOH   A O   
5525 O O   . HOH   D .   ? 0.2765 0.4064 0.2802 0.0610  0.0765  0.1707  356 HOH   A O   
5526 O O   . HOH   D .   ? 0.2491 0.1743 0.2264 -0.0293 -0.0047 -0.0128 357 HOH   A O   
5527 O O   . HOH   D .   ? 0.3783 0.5970 0.4639 -0.0507 -0.1404 0.0425  358 HOH   A O   
5528 O O   . HOH   D .   ? 0.8167 0.8901 0.6539 0.0032  0.0638  -0.0686 359 HOH   A O   
5529 O O   . HOH   D .   ? 0.1906 0.1993 0.1853 -0.0226 -0.0334 0.0240  360 HOH   A O   
5530 O O   . HOH   D .   ? 0.1409 0.1438 0.1396 -0.0064 -0.0142 -0.0043 361 HOH   A O   
5531 O O   A HOH   D .   ? 0.4698 0.4086 0.4248 -0.1074 -0.0180 0.0316  362 HOH   A O   
5532 O O   . HOH   D .   ? 0.1548 0.1541 0.1933 -0.0155 0.0186  0.0194  363 HOH   A O   
5533 O O   . HOH   D .   ? 0.1854 0.2098 0.3131 0.0253  0.0748  -0.0334 364 HOH   A O   
5534 O O   . HOH   D .   ? 0.2804 0.2871 0.1940 0.0334  0.0711  0.0123  365 HOH   A O   
5535 O O   . HOH   D .   ? 0.4548 0.4189 0.4374 0.1408  0.1338  -0.0617 366 HOH   A O   
5536 O O   . HOH   D .   ? 0.3614 0.2904 0.3685 -0.1070 -0.0282 -0.0097 367 HOH   A O   
5537 O O   . HOH   D .   ? 0.2193 0.2192 0.2345 0.0148  0.0042  0.0636  368 HOH   A O   
5538 O O   . HOH   D .   ? 0.1981 0.1710 0.2484 -0.0097 -0.0427 -0.0134 369 HOH   A O   
5539 O O   . HOH   D .   ? 0.2141 0.3653 0.3550 -0.0423 -0.0282 0.0720  370 HOH   A O   
5540 O O   . HOH   D .   ? 0.2999 0.2156 0.3203 -0.0090 -0.0463 0.0701  371 HOH   A O   
5541 O O   . HOH   D .   ? 0.1639 0.1582 0.1811 0.0122  -0.0140 0.0261  372 HOH   A O   
5542 O O   . HOH   D .   ? 0.2025 0.1778 0.1620 0.0076  0.0094  0.0225  373 HOH   A O   
5543 O O   . HOH   D .   ? 0.1550 0.2411 0.2240 0.0423  0.0440  0.0738  374 HOH   A O   
5544 O O   . HOH   D .   ? 0.2596 0.1710 0.1651 -0.0506 0.0348  0.0099  375 HOH   A O   
5545 O O   . HOH   D .   ? 0.5586 0.5380 0.3801 0.1511  -0.0648 -0.0518 376 HOH   A O   
5546 O O   . HOH   D .   ? 0.5917 0.4027 0.5369 -0.0838 0.0062  0.1117  377 HOH   A O   
5547 O O   . HOH   D .   ? 0.2813 0.5257 0.6028 0.0822  0.0653  0.0758  378 HOH   A O   
5548 O O   . HOH   D .   ? 0.1655 0.2049 0.1570 -0.0032 0.0093  0.0568  379 HOH   A O   
5549 O O   . HOH   D .   ? 0.2238 0.2340 0.3558 -0.0546 0.0761  -0.0026 380 HOH   A O   
5550 O O   . HOH   D .   ? 0.2472 0.3979 0.3406 -0.0487 0.1009  -0.0917 381 HOH   A O   
5551 O O   . HOH   D .   ? 0.2736 0.5854 0.3408 0.0902  0.0433  -0.0985 382 HOH   A O   
5552 O O   . HOH   D .   ? 0.2929 0.2509 0.2209 -0.0679 -0.0971 0.0287  383 HOH   A O   
5553 O O   . HOH   D .   ? 0.4714 0.2689 0.3597 0.0843  -0.0353 -0.0356 384 HOH   A O   
5554 O O   . HOH   D .   ? 0.1455 0.1418 0.1469 0.0003  -0.0221 0.0058  385 HOH   A O   
5555 O O   . HOH   D .   ? 0.1997 0.2608 0.2545 0.0329  0.0173  0.0239  386 HOH   A O   
5556 O O   . HOH   D .   ? 0.1898 0.1761 0.3612 0.0428  0.1088  0.0962  387 HOH   A O   
5557 O O   . HOH   D .   ? 0.1575 0.2338 0.3528 -0.0085 0.0629  0.0548  388 HOH   A O   
5558 O O   . HOH   D .   ? 0.3300 0.5039 0.4225 -0.0364 -0.0342 0.1088  389 HOH   A O   
5559 O O   . HOH   D .   ? 0.2070 0.1587 0.2442 0.0057  -0.0323 -0.0049 390 HOH   A O   
5560 O O   . HOH   D .   ? 0.6028 0.5843 0.5738 -0.0095 0.0269  0.0515  391 HOH   A O   
5561 O O   . HOH   D .   ? 0.2030 0.2104 0.2476 0.0035  -0.0497 0.0316  392 HOH   A O   
5562 O O   . HOH   D .   ? 0.5883 0.6853 0.6020 0.0631  0.0160  -0.0103 393 HOH   A O   
5563 O O   . HOH   D .   ? 0.3286 0.5964 0.4085 -0.0272 0.0576  0.1466  394 HOH   A O   
5564 O O   . HOH   D .   ? 0.3403 0.3366 0.4624 0.0964  0.0950  -0.0760 395 HOH   A O   
5565 O O   . HOH   D .   ? 0.2299 0.1920 0.4275 -0.0091 0.0918  -0.0007 396 HOH   A O   
5566 O O   . HOH   D .   ? 0.1267 0.1308 0.1583 0.0023  -0.0130 0.0063  397 HOH   A O   
5567 O O   . HOH   D .   ? 0.1278 0.1627 0.1601 0.0032  -0.0191 -0.0250 398 HOH   A O   
5568 O O   . HOH   D .   ? 0.2556 0.2768 0.3260 -0.0126 0.1109  -0.0186 399 HOH   A O   
5569 O O   . HOH   D .   ? 0.5256 0.3715 0.1878 0.0412  0.0985  0.0771  400 HOH   A O   
5570 O O   . HOH   D .   ? 0.1801 0.1872 0.2179 -0.0051 -0.0007 0.0649  401 HOH   A O   
5571 O O   . HOH   D .   ? 0.1708 0.1308 0.1431 -0.0224 0.0141  0.0025  402 HOH   A O   
5572 O O   . HOH   D .   ? 0.4198 0.5961 0.3270 -0.0728 -0.0147 0.1452  403 HOH   A O   
5573 O O   . HOH   D .   ? 0.3099 0.6681 0.4855 -0.0044 -0.0696 0.1071  404 HOH   A O   
5574 O O   . HOH   D .   ? 0.2229 0.1561 0.2206 -0.0060 0.0126  0.0092  405 HOH   A O   
5575 O O   . HOH   D .   ? 0.6392 0.3643 0.4517 0.1706  -0.0388 0.1354  406 HOH   A O   
5576 O O   . HOH   D .   ? 0.4706 0.3979 0.5111 -0.1222 -0.0615 -0.1007 407 HOH   A O   
5577 O O   . HOH   D .   ? 0.2378 0.2069 0.2418 -0.0566 -0.0036 0.0511  408 HOH   A O   
5578 O O   . HOH   D .   ? 0.2890 0.3786 0.2912 0.1170  -0.0570 -0.1226 409 HOH   A O   
5579 O O   . HOH   D .   ? 0.2282 0.2728 0.2664 0.0052  -0.0079 -0.0591 410 HOH   A O   
5580 O O   . HOH   D .   ? 0.5933 0.5485 0.3830 -0.1155 0.0417  0.2130  411 HOH   A O   
5581 O O   . HOH   D .   ? 0.2989 0.3420 0.4758 -0.0150 0.1130  -0.0240 412 HOH   A O   
5582 O O   . HOH   D .   ? 0.3281 0.1228 0.2075 0.0011  -0.0555 0.0066  413 HOH   A O   
5583 O O   . HOH   D .   ? 0.2907 0.3688 0.6314 -0.0080 0.1100  -0.0469 414 HOH   A O   
5584 O O   . HOH   D .   ? 0.2725 0.5505 0.1557 -0.0545 0.0446  -0.0068 415 HOH   A O   
5585 O O   . HOH   D .   ? 0.1973 0.1587 0.1320 0.0006  0.0180  0.0118  416 HOH   A O   
5586 O O   . HOH   D .   ? 0.3678 0.2657 0.5174 0.0933  0.0904  0.0269  417 HOH   A O   
5587 O O   . HOH   D .   ? 0.5180 0.6205 0.3452 0.0753  0.2171  -0.0640 418 HOH   A O   
5588 O O   A HOH   D .   ? 0.1764 0.2443 0.3130 -0.0070 -0.0327 0.0176  419 HOH   A O   
5589 O O   . HOH   D .   ? 0.3327 0.2208 0.3384 0.0247  0.0862  0.1031  420 HOH   A O   
5590 O O   . HOH   D .   ? 0.2222 0.4150 0.2344 0.1545  -0.0048 0.0171  421 HOH   A O   
5591 O O   . HOH   D .   ? 0.2126 0.2357 0.3529 0.0093  -0.0478 -0.0370 422 HOH   A O   
5592 O O   . HOH   D .   ? 0.4905 0.4395 0.3184 -0.0069 -0.1295 0.0215  423 HOH   A O   
5593 O O   . HOH   D .   ? 0.1485 0.1662 0.2474 0.0035  0.0079  0.0133  424 HOH   A O   
5594 O O   B HOH   D .   ? 0.2156 0.1519 0.1596 -0.0791 -0.0941 0.0401  425 HOH   A O   
5595 O O   . HOH   D .   ? 0.2082 0.2667 0.2129 0.0084  -0.0594 0.0248  426 HOH   A O   
5596 O O   . HOH   D .   ? 0.5163 0.3114 0.3125 -0.1284 0.0519  0.0826  427 HOH   A O   
5597 O O   . HOH   D .   ? 0.1565 0.1568 0.2298 0.0140  -0.0310 0.0269  428 HOH   A O   
5598 O O   . HOH   D .   ? 0.4189 0.2231 0.4595 -0.0678 -0.2168 0.0947  429 HOH   A O   
5599 O O   . HOH   D .   ? 0.1495 0.2042 0.2674 -0.0153 -0.0046 0.0553  430 HOH   A O   
5600 O O   . HOH   D .   ? 0.2130 0.1501 0.2256 0.0203  -0.0806 -0.0318 431 HOH   A O   
5601 O O   . HOH   D .   ? 0.3915 0.3273 0.2434 0.0279  -0.1178 0.0323  432 HOH   A O   
5602 O O   A HOH   D .   ? 0.3419 0.2276 0.1619 -0.0830 0.0447  0.0329  433 HOH   A O   
5603 O O   . HOH   D .   ? 0.3343 0.2309 0.2341 0.0015  -0.0230 0.0004  434 HOH   A O   
5604 O O   . HOH   D .   ? 0.1854 0.1300 0.1410 0.0047  -0.0094 -0.0058 435 HOH   A O   
5605 O O   B HOH   D .   ? 0.4789 0.4967 0.4916 0.0230  0.0128  -0.0133 436 HOH   A O   
5606 O O   . HOH   D .   ? 0.1697 0.2014 0.5030 -0.0232 -0.0728 0.0554  437 HOH   A O   
5607 O O   . HOH   D .   ? 0.2465 0.1526 0.2339 0.0063  0.0133  0.0034  438 HOH   A O   
5608 O O   B HOH   D .   ? 0.1980 0.2267 0.2355 -0.0069 -0.0157 0.0016  439 HOH   A O   
5609 O O   . HOH   D .   ? 0.4929 0.3571 0.6055 0.0655  -0.0293 -0.0956 440 HOH   A O   
5610 O O   . HOH   D .   ? 0.3789 0.3460 0.2959 0.2103  -0.0373 -0.0535 441 HOH   A O   
5611 O O   B HOH   D .   ? 0.3351 0.3688 0.3594 0.0255  -0.0343 -0.0046 442 HOH   A O   
5612 O O   . HOH   D .   ? 0.2378 0.1943 0.2398 0.0194  0.0422  0.0210  443 HOH   A O   
5613 O O   . HOH   D .   ? 0.3809 0.3659 0.5010 -0.0858 -0.0990 -0.1062 444 HOH   A O   
5614 O O   . HOH   D .   ? 0.2840 0.2479 0.4681 0.0074  0.1066  -0.0597 445 HOH   A O   
5615 O O   A HOH   D .   ? 0.4388 0.3768 0.6421 -0.0032 -0.1282 0.0993  446 HOH   A O   
5616 O O   . HOH   D .   ? 0.4665 0.4263 0.4723 0.0216  0.0291  0.1613  447 HOH   A O   
5617 O O   . HOH   D .   ? 0.2195 0.2506 0.2122 0.0066  -0.0056 -0.0514 448 HOH   A O   
5618 O O   . HOH   D .   ? 0.6258 0.7260 0.4015 0.2014  -0.1183 0.1587  449 HOH   A O   
5619 O O   A HOH   D .   ? 0.4951 0.4987 0.6246 -0.1394 0.0885  -0.0424 450 HOH   A O   
5620 O O   . HOH   D .   ? 0.5425 0.3134 0.3747 -0.0241 0.0260  0.0863  451 HOH   A O   
5621 O O   A HOH   D .   ? 0.5480 0.5411 0.4523 0.0592  -0.1035 0.0743  452 HOH   A O   
5622 O O   . HOH   D .   ? 0.3536 0.1865 0.2989 0.0543  0.0836  0.0990  453 HOH   A O   
5623 O O   . HOH   D .   ? 0.4203 0.3731 0.4206 0.0820  -0.0206 0.1025  454 HOH   A O   
5624 O O   . HOH   D .   ? 0.2377 0.2673 0.3166 0.0455  -0.0222 0.0300  455 HOH   A O   
5625 O O   . HOH   D .   ? 0.4987 0.3298 0.4526 0.0715  0.0441  0.0223  456 HOH   A O   
5626 O O   . HOH   D .   ? 0.6552 0.5138 0.4727 -0.0527 0.1479  0.0791  457 HOH   A O   
5627 O O   . HOH   D .   ? 0.3381 0.2603 0.3098 -0.0534 0.0062  -0.0598 458 HOH   A O   
5628 O O   . HOH   D .   ? 0.3348 0.4657 0.4184 0.0876  -0.0822 0.1256  459 HOH   A O   
5629 O O   . HOH   D .   ? 0.2858 0.5268 0.4856 -0.1575 0.0859  -0.1671 460 HOH   A O   
5630 O O   . HOH   D .   ? 0.6641 0.7517 0.4674 0.0280  -0.1038 -0.0206 461 HOH   A O   
5631 O O   . HOH   D .   ? 0.2378 0.2514 0.2940 -0.0805 0.0385  -0.0339 462 HOH   A O   
5632 O O   . HOH   D .   ? 0.2433 0.3849 0.3636 -0.0286 -0.0396 0.0003  463 HOH   A O   
5633 O O   A HOH   D .   ? 0.3914 0.4828 0.3293 -0.1074 -0.0970 0.1655  464 HOH   A O   
5634 O O   . HOH   D .   ? 0.5793 0.3197 0.6832 0.0574  0.0291  0.1961  465 HOH   A O   
5635 O O   . HOH   D .   ? 0.2906 0.3755 0.4359 0.0762  0.0201  -0.1559 466 HOH   A O   
5636 O O   . HOH   D .   ? 0.2642 0.2422 0.4541 0.0605  -0.1160 -0.0303 467 HOH   A O   
5637 O O   . HOH   D .   ? 0.2913 0.1670 0.2183 0.0380  -0.0858 -0.0213 468 HOH   A O   
5638 O O   . HOH   D .   ? 0.5350 0.3776 0.4531 0.1053  0.2241  0.1480  469 HOH   A O   
5639 O O   . HOH   D .   ? 0.2638 0.2561 0.3804 0.0051  0.0539  -0.0068 470 HOH   A O   
5640 O O   . HOH   D .   ? 0.5014 0.4527 0.4410 0.0383  0.0743  0.0528  471 HOH   A O   
5641 O O   . HOH   D .   ? 0.3973 0.5285 0.3536 0.0411  -0.0591 -0.0634 472 HOH   A O   
5642 O O   . HOH   D .   ? 0.4482 0.4150 0.4874 -0.1956 -0.0377 -0.0117 473 HOH   A O   
5643 O O   . HOH   D .   ? 0.5253 0.6125 0.5488 -0.1563 -0.0928 0.0838  474 HOH   A O   
5644 O O   . HOH   D .   ? 0.6565 0.4373 0.5990 -0.1183 0.0439  -0.0228 475 HOH   A O   
5645 O O   . HOH   D .   ? 0.6257 0.3809 0.2971 -0.0446 -0.0839 -0.0016 476 HOH   A O   
5646 O O   . HOH   D .   ? 0.5037 0.4382 0.3576 0.0033  0.0668  -0.1308 477 HOH   A O   
5647 O O   . HOH   D .   ? 0.4611 0.5478 0.4480 0.1283  -0.0690 -0.0720 478 HOH   A O   
5648 O O   . HOH   D .   ? 0.4527 0.3594 0.3147 -0.0563 -0.0497 -0.0157 479 HOH   A O   
5649 O O   . HOH   D .   ? 0.3987 0.2389 0.3169 -0.0743 -0.1120 0.0640  480 HOH   A O   
5650 O O   . HOH   D .   ? 0.2263 0.2095 0.2359 0.0148  0.0152  -0.0032 481 HOH   A O   
5651 O O   . HOH   D .   ? 0.4191 0.4811 0.2623 -0.0138 -0.0005 0.0403  482 HOH   A O   
5652 O O   . HOH   D .   ? 0.2874 0.4998 0.3478 0.1224  0.1067  0.2263  483 HOH   A O   
5653 O O   . HOH   D .   ? 0.2672 0.4561 0.4393 0.0525  0.1133  0.1341  484 HOH   A O   
5654 O O   . HOH   D .   ? 0.5472 0.4068 0.3500 -0.0196 0.1397  0.0063  485 HOH   A O   
5655 O O   A HOH   D .   ? 0.4465 0.6049 0.4070 -0.0337 0.1332  0.0581  486 HOH   A O   
5656 O O   . HOH   D .   ? 0.5128 0.5751 0.5296 -0.0476 -0.1280 0.0634  487 HOH   A O   
5657 O O   . HOH   D .   ? 0.4511 0.3278 0.4575 -0.0301 0.2209  0.0185  488 HOH   A O   
5658 O O   . HOH   D .   ? 0.2752 0.2001 0.4736 0.0156  0.0524  0.0706  489 HOH   A O   
5659 O O   . HOH   D .   ? 0.5296 0.5331 0.4412 -0.0762 -0.0782 -0.0893 490 HOH   A O   
5660 O O   . HOH   D .   ? 0.2534 0.2623 0.6162 -0.0092 -0.1258 0.0277  491 HOH   A O   
5661 O O   . HOH   D .   ? 0.3343 0.3318 0.2316 -0.0232 0.0948  -0.0263 492 HOH   A O   
5662 O O   . HOH   D .   ? 0.6025 0.5480 0.6284 0.0901  0.1915  -0.1092 493 HOH   A O   
5663 O O   . HOH   D .   ? 0.3422 0.2673 0.4098 -0.0756 0.0489  0.0625  494 HOH   A O   
5664 O O   . HOH   D .   ? 0.3867 0.7325 0.4476 -0.0840 0.0512  0.2353  495 HOH   A O   
5665 O O   . HOH   D .   ? 0.2296 0.2911 0.4411 0.0011  0.0904  -0.0425 496 HOH   A O   
5666 O O   . HOH   D .   ? 0.5948 0.2595 0.4294 -0.0669 0.0187  0.0667  497 HOH   A O   
5667 O O   . HOH   D .   ? 0.4339 0.2351 0.4139 -0.1268 0.0238  0.0292  498 HOH   A O   
5668 O O   . HOH   D .   ? 0.2343 0.2841 0.3684 0.0373  -0.0518 0.0560  499 HOH   A O   
5669 O O   . HOH   D .   ? 0.4769 0.5658 0.5079 0.1163  -0.0608 0.0187  500 HOH   A O   
5670 O O   . HOH   D .   ? 0.2877 0.4232 0.4022 0.0737  0.0061  0.0583  501 HOH   A O   
5671 O O   . HOH   D .   ? 0.5059 0.3856 0.4331 -0.0631 -0.0108 -0.0082 502 HOH   A O   
5672 O O   . HOH   D .   ? 0.2897 0.4761 0.3088 -0.0411 -0.0125 -0.0655 503 HOH   A O   
5673 O O   . HOH   D .   ? 0.3990 0.5829 0.4238 0.2297  0.0032  0.0896  504 HOH   A O   
5674 O O   . HOH   D .   ? 0.2874 0.2404 0.3899 -0.0153 0.0207  0.0705  505 HOH   A O   
5675 O O   . HOH   D .   ? 0.4767 0.5245 0.4380 0.0674  -0.1402 0.0431  506 HOH   A O   
5676 O O   . HOH   D .   ? 0.4425 0.5344 0.4187 -0.0119 -0.0759 -0.1269 507 HOH   A O   
5677 O O   . HOH   D .   ? 0.3584 0.5968 0.3002 0.0272  0.1346  0.0378  508 HOH   A O   
5678 O O   . HOH   D .   ? 0.2486 0.6597 0.3614 0.0340  0.0408  -0.0044 509 HOH   A O   
5679 O O   . HOH   D .   ? 0.4079 0.5611 0.4985 -0.0839 -0.0693 0.0352  510 HOH   A O   
5680 O O   . HOH   D .   ? 0.3658 0.4798 0.3280 0.1102  -0.0436 0.0773  511 HOH   A O   
5681 O O   . HOH   D .   ? 0.2507 0.3615 0.5188 -0.0365 -0.0686 0.2161  512 HOH   A O   
5682 O O   . HOH   E .   ? 0.2272 0.2039 0.2673 0.0239  0.0692  0.0198  201 HOH   B O   
5683 O O   . HOH   E .   ? 0.4415 0.5081 0.2587 0.0657  -0.0774 -0.1482 202 HOH   B O   
5684 O O   . HOH   E .   ? 0.3138 0.5355 0.4594 -0.0200 0.1621  -0.1902 203 HOH   B O   
5685 O O   . HOH   E .   ? 0.5283 0.4138 0.5562 0.0626  -0.1064 0.2478  204 HOH   B O   
5686 O O   . HOH   E .   ? 0.3555 0.6063 0.3514 0.0633  0.0012  0.2012  205 HOH   B O   
5687 O O   . HOH   E .   ? 0.6489 0.3658 0.4566 0.0471  0.1416  -0.0157 206 HOH   B O   
5688 O O   . HOH   E .   ? 0.6014 0.5831 0.5489 0.2062  0.0149  0.0350  207 HOH   B O   
5689 O O   . HOH   E .   ? 0.4023 0.5447 0.3544 0.2449  -0.0907 0.0010  208 HOH   B O   
5690 O O   . HOH   E .   ? 0.4829 0.2981 0.3136 -0.0703 -0.0035 -0.1083 209 HOH   B O   
5691 O O   . HOH   E .   ? 0.3519 0.3121 0.5231 -0.0106 0.0497  0.0028  210 HOH   B O   
5692 O O   . HOH   E .   ? 0.2670 0.3097 0.6450 0.0714  -0.0935 0.0203  211 HOH   B O   
5693 O O   . HOH   E .   ? 0.4496 0.3860 0.3795 -0.0300 -0.0985 0.0643  212 HOH   B O   
5694 O O   . HOH   E .   ? 0.1862 0.2110 0.2661 0.0119  0.0183  -0.0230 213 HOH   B O   
5695 O O   . HOH   E .   ? 0.3540 0.4695 0.4107 0.1827  -0.0490 -0.0130 214 HOH   B O   
5696 O O   . HOH   E .   ? 0.1500 0.1845 0.2392 -0.0168 -0.0029 0.0015  215 HOH   B O   
5697 O O   . HOH   E .   ? 0.3875 0.3756 0.4359 -0.1562 0.0334  0.0344  216 HOH   B O   
5698 O O   . HOH   E .   ? 0.3794 0.4735 0.5187 -0.1262 -0.0060 -0.1230 217 HOH   B O   
5699 O O   . HOH   E .   ? 0.2994 0.2062 0.4704 0.0197  0.1806  0.0802  218 HOH   B O   
5700 O O   . HOH   E .   ? 0.3151 0.5170 0.3747 0.2058  0.0129  -0.0480 219 HOH   B O   
5701 O O   . HOH   E .   ? 0.4652 0.1972 0.3762 -0.0137 -0.1190 0.0172  220 HOH   B O   
5702 O O   . HOH   E .   ? 0.4870 0.3112 0.3816 -0.1479 0.0230  0.0298  221 HOH   B O   
5703 O O   . HOH   E .   ? 0.5238 0.5768 0.3068 0.1339  -0.0101 -0.0282 222 HOH   B O   
5704 O O   . HOH   E .   ? 0.3427 0.2941 0.5043 0.0321  0.0872  0.0185  223 HOH   B O   
5705 O O   . HOH   E .   ? 0.3993 0.3751 0.4512 0.0319  -0.0865 -0.0120 224 HOH   B O   
5706 O O   . HOH   E .   ? 0.2516 0.1716 0.2647 -0.0336 0.1095  -0.0070 225 HOH   B O   
5707 O O   . HOH   E .   ? 0.3018 0.2175 0.3800 0.0022  0.1366  0.0120  226 HOH   B O   
5708 O O   . HOH   E .   ? 0.3914 0.4841 0.3859 0.0348  0.1031  -0.1180 227 HOH   B O   
5709 O O   . HOH   E .   ? 0.2539 0.3656 0.3436 -0.0830 0.0613  -0.0605 228 HOH   B O   
5710 O O   . HOH   E .   ? 0.3583 0.5837 0.3372 0.1683  -0.0084 -0.0309 229 HOH   B O   
5711 O O   . HOH   E .   ? 0.1645 0.1904 0.2549 -0.0154 0.0033  -0.0097 230 HOH   B O   
5712 O O   . HOH   E .   ? 0.3705 0.3153 0.2106 0.0260  0.0706  0.0431  231 HOH   B O   
5713 O O   . HOH   E .   ? 0.2575 0.2330 0.2920 0.0371  0.0254  -0.0729 232 HOH   B O   
5714 O O   . HOH   E .   ? 0.5865 0.3794 0.4937 0.1069  -0.0279 -0.1116 233 HOH   B O   
5715 O O   . HOH   E .   ? 0.2156 0.1982 0.3518 -0.0252 -0.0249 -0.0463 234 HOH   B O   
5716 O O   . HOH   E .   ? 0.1951 0.2197 0.2783 -0.0464 -0.0005 -0.0253 235 HOH   B O   
5717 O O   . HOH   E .   ? 0.4298 0.4100 0.6132 0.0093  -0.1470 -0.0713 236 HOH   B O   
5718 O O   . HOH   E .   ? 0.2024 0.1281 0.3170 0.0174  -0.0572 -0.0162 237 HOH   B O   
5719 O O   . HOH   E .   ? 0.4698 0.3004 0.3816 -0.2137 0.0314  -0.0076 238 HOH   B O   
5720 O O   . HOH   E .   ? 0.1422 0.1384 0.1527 -0.0101 -0.0025 0.0011  239 HOH   B O   
5721 O O   . HOH   E .   ? 0.2052 0.3827 0.2774 -0.0325 -0.0559 -0.0692 240 HOH   B O   
5722 O O   . HOH   E .   ? 0.1488 0.1375 0.2505 -0.0043 0.0122  -0.0162 241 HOH   B O   
5723 O O   . HOH   E .   ? 0.3003 0.1649 0.5578 -0.0096 -0.1440 -0.0356 242 HOH   B O   
5724 O O   . HOH   E .   ? 0.3662 0.3249 0.4010 0.0919  -0.1177 -0.1544 243 HOH   B O   
5725 O O   . HOH   E .   ? 0.3396 0.1808 0.1888 0.0152  -0.0542 -0.0097 244 HOH   B O   
5726 O O   . HOH   E .   ? 0.2156 0.1955 0.1972 -0.0291 -0.0456 0.0019  245 HOH   B O   
5727 O O   . HOH   E .   ? 0.1919 0.3856 0.2102 -0.0417 -0.0190 0.0642  246 HOH   B O   
5728 O O   . HOH   E .   ? 0.1362 0.1280 0.1407 -0.0038 -0.0004 0.0069  247 HOH   B O   
5729 O O   . HOH   E .   ? 0.2824 0.2339 0.2733 0.0984  0.0912  0.0077  248 HOH   B O   
5730 O O   . HOH   E .   ? 0.3835 0.2560 0.3840 0.0848  -0.0339 -0.0778 249 HOH   B O   
5731 O O   . HOH   E .   ? 0.3121 0.2259 0.2711 -0.0390 0.0404  -0.0466 250 HOH   B O   
5732 O O   . HOH   E .   ? 0.2825 0.4605 0.3601 -0.1144 -0.0307 -0.0812 251 HOH   B O   
5733 O O   . HOH   E .   ? 0.2066 0.1369 0.1935 -0.0254 -0.0337 0.0183  252 HOH   B O   
5734 O O   . HOH   E .   ? 0.3322 0.4106 0.5204 0.0255  0.0625  -0.1119 253 HOH   B O   
5735 O O   . HOH   E .   ? 0.3072 0.3190 0.1855 0.0419  0.0552  0.0056  254 HOH   B O   
5736 O O   . HOH   E .   ? 0.2238 0.3164 0.2195 -0.0510 0.0275  0.0472  255 HOH   B O   
5737 O O   . HOH   E .   ? 0.1557 0.1617 0.2409 -0.0145 -0.0137 0.0057  256 HOH   B O   
5738 O O   . HOH   E .   ? 0.2303 0.2054 0.2394 0.0756  -0.0763 -0.0643 257 HOH   B O   
5739 O O   . HOH   E .   ? 0.3681 0.3771 0.4657 -0.0374 -0.0932 -0.0946 258 HOH   B O   
5740 O O   . HOH   E .   ? 0.4903 0.2824 0.2316 0.0350  0.0869  -0.0273 259 HOH   B O   
5741 O O   . HOH   E .   ? 0.2164 0.1978 0.1824 0.0039  -0.0016 0.0078  260 HOH   B O   
5742 O O   . HOH   E .   ? 0.1293 0.1536 0.1798 -0.0028 0.0068  0.0084  261 HOH   B O   
5743 O O   . HOH   E .   ? 0.2192 0.2032 0.1737 0.0134  -0.0048 0.0019  262 HOH   B O   
5744 O O   . HOH   E .   ? 0.2421 0.1915 0.2758 -0.0522 0.0135  0.0003  263 HOH   B O   
5745 O O   . HOH   E .   ? 0.1695 0.2603 0.2582 0.0471  0.0411  0.0993  264 HOH   B O   
5746 O O   . HOH   E .   ? 0.2031 0.1401 0.1972 -0.0235 -0.0206 0.0086  265 HOH   B O   
5747 O O   . HOH   E .   ? 0.2044 0.1965 0.3424 -0.0118 -0.0479 -0.0417 266 HOH   B O   
5748 O O   . HOH   E .   ? 0.2421 0.3320 0.4769 0.0779  -0.0653 -0.0651 267 HOH   B O   
5749 O O   . HOH   E .   ? 0.1953 0.3914 0.4525 -0.0598 -0.0172 -0.1689 268 HOH   B O   
5750 O O   . HOH   E .   ? 0.1734 0.1669 0.1513 -0.0340 -0.0309 0.0065  269 HOH   B O   
5751 O O   . HOH   E .   ? 0.4183 0.4927 0.4721 0.0024  -0.1291 -0.0089 270 HOH   B O   
5752 O O   . HOH   E .   ? 0.3065 0.4450 0.3630 -0.0190 -0.0975 0.1178  271 HOH   B O   
5753 O O   . HOH   E .   ? 0.1677 0.1340 0.4151 -0.0057 -0.0146 -0.0179 272 HOH   B O   
5754 O O   . HOH   E .   ? 0.2717 0.3391 0.3179 -0.0753 0.0804  -0.1274 273 HOH   B O   
5755 O O   . HOH   E .   ? 0.2387 0.2465 0.2346 -0.0405 -0.0622 -0.0444 274 HOH   B O   
5756 O O   . HOH   E .   ? 0.2397 0.3594 0.3483 0.0349  0.1081  0.0187  275 HOH   B O   
5757 O O   . HOH   E .   ? 0.3950 0.3506 0.3848 -0.0527 0.0849  -0.0911 276 HOH   B O   
5758 O O   . HOH   E .   ? 0.4149 0.3855 0.2565 0.0530  -0.0083 -0.1317 277 HOH   B O   
5759 O O   . HOH   E .   ? 0.2347 0.3398 0.2073 0.1122  -0.0216 -0.0078 278 HOH   B O   
5760 O O   . HOH   E .   ? 0.2649 0.2736 0.2242 -0.0443 -0.0880 0.0083  279 HOH   B O   
5761 O O   . HOH   E .   ? 0.1579 0.1418 0.1618 0.0039  0.0090  0.0023  280 HOH   B O   
5762 O O   . HOH   E .   ? 0.1517 0.1573 0.2864 -0.0132 0.0110  -0.0079 281 HOH   B O   
5763 O O   . HOH   E .   ? 0.2872 0.6102 0.7093 0.1075  -0.0444 -0.0716 282 HOH   B O   
5764 O O   . HOH   E .   ? 0.2670 0.2778 0.4690 -0.0349 0.0371  -0.1262 283 HOH   B O   
5765 O O   . HOH   E .   ? 0.2353 0.2554 0.2527 0.0257  -0.0616 0.0216  284 HOH   B O   
5766 O O   . HOH   E .   ? 0.3690 0.3582 0.4227 0.1474  -0.0822 -0.0900 285 HOH   B O   
5767 O O   . HOH   E .   ? 0.1539 0.2015 0.1412 -0.0160 -0.0167 0.0040  286 HOH   B O   
5768 O O   . HOH   E .   ? 0.4367 0.6054 0.2440 -0.0588 -0.0498 0.1105  287 HOH   B O   
5769 O O   . HOH   E .   ? 0.2521 0.2096 0.4434 0.0123  0.0447  0.0327  288 HOH   B O   
5770 O O   . HOH   E .   ? 0.3713 0.1987 0.3865 -0.0666 -0.2022 0.0600  289 HOH   B O   
5771 O O   . HOH   E .   ? 0.3507 0.5780 0.3051 0.1769  -0.0943 0.0101  290 HOH   B O   
5772 O O   . HOH   E .   ? 0.1663 0.2878 0.4488 0.0082  -0.0064 -0.1231 291 HOH   B O   
5773 O O   . HOH   E .   ? 0.4365 0.3094 0.4644 -0.0741 0.0262  0.1268  292 HOH   B O   
5774 O O   . HOH   E .   ? 0.2874 0.3165 0.4021 -0.0963 0.1284  -0.0726 293 HOH   B O   
5775 O O   . HOH   E .   ? 0.2886 0.2668 0.2485 -0.0082 0.0229  -0.1093 294 HOH   B O   
5776 O O   . HOH   E .   ? 0.4088 0.3662 0.2390 0.1083  -0.0703 0.0608  295 HOH   B O   
5777 O O   . HOH   E .   ? 0.1903 0.2587 0.5639 0.0386  -0.0501 -0.1170 296 HOH   B O   
5778 O O   . HOH   E .   ? 0.2900 0.2554 0.4609 -0.0120 -0.0564 0.0903  297 HOH   B O   
5779 O O   . HOH   E .   ? 0.1661 0.1794 0.2445 0.0148  -0.0140 0.0072  298 HOH   B O   
5780 O O   . HOH   E .   ? 0.3447 0.2543 0.2030 0.0402  -0.0687 -0.0218 299 HOH   B O   
5781 O O   . HOH   E .   ? 0.2023 0.1525 0.2435 -0.0169 -0.0254 -0.0082 300 HOH   B O   
5782 O O   . HOH   E .   ? 0.2550 0.4520 0.4832 -0.0927 -0.0942 0.0991  301 HOH   B O   
5783 O O   . HOH   E .   ? 0.2342 0.6357 0.2456 0.0381  -0.0055 -0.0338 302 HOH   B O   
5784 O O   . HOH   E .   ? 0.1722 0.1489 0.2245 0.0094  -0.0026 0.0136  303 HOH   B O   
5785 O O   . HOH   E .   ? 0.2359 0.3356 0.3922 -0.0510 -0.1099 0.0978  304 HOH   B O   
5786 O O   . HOH   E .   ? 0.4757 0.3894 0.5508 0.0906  0.0190  0.0678  305 HOH   B O   
5787 O O   . HOH   E .   ? 0.2799 0.2872 0.3030 -0.0399 0.1001  -0.0746 306 HOH   B O   
5788 O O   . HOH   E .   ? 0.5604 0.3619 0.2976 0.2502  0.1007  0.0774  307 HOH   B O   
5789 O O   . HOH   E .   ? 0.4422 0.4168 0.2323 0.1284  -0.0736 -0.0336 308 HOH   B O   
5790 O O   . HOH   E .   ? 0.3348 0.1819 0.3107 0.0744  0.1133  0.0439  309 HOH   B O   
5791 O O   . HOH   E .   ? 0.2268 0.1425 0.2368 -0.0111 -0.0022 0.0255  310 HOH   B O   
5792 O O   . HOH   E .   ? 0.4907 0.2724 0.2432 -0.1722 0.0773  -0.0259 311 HOH   B O   
5793 O O   . HOH   E .   ? 0.1557 0.1836 0.2327 -0.0245 -0.0059 0.0060  312 HOH   B O   
5794 O O   . HOH   E .   ? 0.2104 0.1495 0.3195 0.0287  -0.1065 -0.0034 313 HOH   B O   
5795 O O   . HOH   E .   ? 0.6857 0.4953 0.4540 0.2171  0.1225  0.0567  314 HOH   B O   
5796 O O   . HOH   E .   ? 0.2191 0.3293 0.4719 -0.0171 -0.0429 -0.0219 315 HOH   B O   
5797 O O   . HOH   E .   ? 0.4040 0.2326 0.2658 0.1556  0.1034  0.0315  316 HOH   B O   
5798 O O   . HOH   E .   ? 0.3987 0.4441 0.1706 -0.0202 0.0510  0.0269  317 HOH   B O   
5799 O O   . HOH   E .   ? 0.4296 0.2499 0.2845 0.0403  0.0658  0.0980  318 HOH   B O   
5800 O O   . HOH   E .   ? 0.4226 0.3135 0.4893 0.0980  0.2145  0.1601  319 HOH   B O   
5801 O O   . HOH   E .   ? 0.2033 0.1856 0.1556 -0.0108 0.0177  0.0152  320 HOH   B O   
5802 O O   . HOH   E .   ? 0.1568 0.1470 0.2580 0.0092  -0.0011 -0.0127 321 HOH   B O   
5803 O O   . HOH   E .   ? 0.1554 0.2711 0.2195 -0.0122 -0.0203 0.0616  322 HOH   B O   
5804 O O   . HOH   E .   ? 0.3046 0.3825 0.6591 -0.0318 -0.0735 0.2031  323 HOH   B O   
5805 O O   . HOH   E .   ? 0.4685 0.5019 0.3055 -0.0203 -0.0920 0.0582  324 HOH   B O   
5806 O O   . HOH   E .   ? 0.1524 0.1565 0.2660 -0.0110 -0.0062 -0.0194 325 HOH   B O   
5807 O O   . HOH   E .   ? 0.6200 0.4724 0.4913 -0.1044 -0.0137 0.1066  326 HOH   B O   
5808 O O   . HOH   E .   ? 0.4416 0.4282 0.2419 0.0504  -0.0232 -0.0551 327 HOH   B O   
5809 O O   . HOH   E .   ? 0.2652 0.2020 0.2294 0.0179  -0.0222 0.0299  328 HOH   B O   
5810 O O   . HOH   E .   ? 0.6457 0.3328 0.3230 -0.0108 0.1139  0.0998  329 HOH   B O   
5811 O O   . HOH   E .   ? 0.1716 0.2885 0.2858 0.0257  -0.0099 -0.0703 330 HOH   B O   
5812 O O   . HOH   E .   ? 0.1955 0.2037 0.2979 0.0400  0.0562  0.0274  331 HOH   B O   
5813 O O   . HOH   E .   ? 0.4927 0.3412 0.3724 0.0304  0.0790  -0.1503 332 HOH   B O   
5814 O O   . HOH   E .   ? 0.5676 0.5512 0.4971 0.2364  0.0543  0.0435  333 HOH   B O   
5815 O O   . HOH   E .   ? 0.7857 0.2008 0.2560 0.0254  -0.0372 0.0099  334 HOH   B O   
5816 O O   . HOH   E .   ? 0.2528 0.1862 0.4769 0.0085  0.0043  0.0139  335 HOH   B O   
5817 O O   . HOH   E .   ? 0.1975 0.5088 0.5127 -0.0236 0.0238  -0.0253 336 HOH   B O   
5818 O O   . HOH   E .   ? 0.5534 0.4994 0.5398 -0.0684 -0.0527 -0.0994 337 HOH   B O   
5819 O O   . HOH   E .   ? 0.2198 0.2233 0.5452 -0.0409 0.0265  0.1279  338 HOH   B O   
5820 O O   . HOH   E .   ? 0.1683 0.1361 0.2254 0.0052  -0.0208 0.0031  339 HOH   B O   
5821 O O   . HOH   E .   ? 0.5196 0.4710 0.5923 0.0376  -0.0777 0.2241  340 HOH   B O   
5822 O O   . HOH   E .   ? 0.4858 0.3463 0.2916 0.0722  -0.1231 -0.0701 341 HOH   B O   
5823 O O   . HOH   E .   ? 0.4032 0.5558 0.3637 -0.0400 -0.1181 -0.0605 342 HOH   B O   
5824 O O   . HOH   E .   ? 0.4253 0.6761 0.3269 -0.0756 0.0011  0.1185  343 HOH   B O   
5825 O O   . HOH   E .   ? 0.2170 0.5710 0.6220 0.0159  -0.0622 0.0123  344 HOH   B O   
5826 O O   . HOH   E .   ? 0.2114 0.1844 0.2935 -0.0018 0.0551  -0.0029 345 HOH   B O   
5827 O O   . HOH   E .   ? 0.4597 0.4640 0.4972 0.0261  -0.1040 0.0246  346 HOH   B O   
5828 O O   . HOH   E .   ? 0.5769 0.5882 0.2906 -0.0066 -0.0637 0.1283  347 HOH   B O   
5829 O O   . HOH   E .   ? 0.2593 0.2346 0.4743 -0.0205 -0.0898 -0.0643 348 HOH   B O   
5830 O O   . HOH   E .   ? 0.4545 0.5431 0.4434 -0.1171 0.0232  0.1015  349 HOH   B O   
5831 O O   . HOH   E .   ? 0.2091 0.3580 0.4843 0.0321  0.0388  0.0447  350 HOH   B O   
5832 O O   . HOH   E .   ? 0.2263 0.5071 0.3712 0.1291  -0.0436 -0.1345 351 HOH   B O   
5833 O O   . HOH   E .   ? 0.3537 0.2179 0.3257 -0.0649 -0.0100 -0.0686 352 HOH   B O   
5834 O O   . HOH   E .   ? 0.4431 0.6005 0.5433 0.0872  0.0168  -0.0952 353 HOH   B O   
5835 O O   . HOH   E .   ? 0.3526 0.4222 0.4908 -0.1706 -0.0323 0.0342  354 HOH   B O   
5836 O O   . HOH   E .   ? 0.4936 0.3587 0.4229 0.0633  0.1279  -0.0350 355 HOH   B O   
5837 O O   . HOH   E .   ? 0.3680 0.3004 0.4579 -0.1030 -0.0409 -0.0522 356 HOH   B O   
5838 O O   . HOH   E .   ? 0.4241 0.2702 0.4864 -0.0856 0.1526  0.0083  357 HOH   B O   
5839 O O   . HOH   E .   ? 0.3090 0.1847 0.3995 0.0527  -0.1247 -0.0611 358 HOH   B O   
5840 O O   . HOH   E .   ? 0.4337 0.3326 0.4536 0.0358  -0.1538 -0.0126 359 HOH   B O   
5841 O O   . HOH   E .   ? 0.4369 0.5591 0.5343 0.1916  -0.1294 0.1372  360 HOH   B O   
5842 O O   . HOH   E .   ? 0.4399 0.5101 0.4719 -0.0901 -0.0471 -0.0108 361 HOH   B O   
5843 O O   . HOH   E .   ? 0.3933 0.6771 0.2798 0.2071  0.0109  0.0475  362 HOH   B O   
5844 O O   . HOH   E .   ? 0.4770 0.3832 0.5566 -0.0317 0.0676  0.0665  363 HOH   B O   
5845 O O   . HOH   E .   ? 0.2036 0.3644 0.6090 -0.0819 -0.0354 -0.0832 364 HOH   B O   
5846 O O   . HOH   E .   ? 0.4811 0.3083 0.5657 -0.1106 -0.0629 0.0306  365 HOH   B O   
5847 O O   . HOH   E .   ? 0.5820 0.4039 0.4243 0.0753  0.1222  0.0409  366 HOH   B O   
5848 O O   . HOH   E .   ? 0.4293 0.4670 0.5631 0.1999  0.0740  0.0696  367 HOH   B O   
5849 O O   . HOH   E .   ? 0.5452 0.3531 0.4789 0.0866  -0.1529 0.0057  368 HOH   B O   
5850 O O   . HOH   E .   ? 0.5209 0.5129 0.3002 0.0935  -0.1401 0.0410  369 HOH   B O   
5851 O O   . HOH   E .   ? 0.6177 0.2050 0.3272 0.0366  0.0463  0.0721  370 HOH   B O   
5852 O O   . HOH   E .   ? 0.4675 0.5421 0.4276 -0.0577 -0.0496 -0.1213 371 HOH   B O   
5853 O O   . HOH   E .   ? 0.6396 0.4456 0.3259 -0.1333 -0.1100 -0.0879 372 HOH   B O   
5854 O O   . HOH   E .   ? 0.7236 0.7238 0.5217 0.2065  -0.1395 0.0637  373 HOH   B O   
5855 O O   . HOH   E .   ? 0.3972 0.3374 0.4511 0.0638  -0.1505 -0.0362 374 HOH   B O   
5856 O O   . HOH   E .   ? 0.2338 0.3968 0.4076 0.0426  -0.0722 -0.0505 375 HOH   B O   
5857 O O   . HOH   E .   ? 0.4154 0.4468 0.4654 -0.0817 -0.0599 0.0333  376 HOH   B O   
5858 O O   . HOH   E .   ? 0.6266 0.3282 0.5196 -0.0699 -0.0112 -0.0038 377 HOH   B O   
5859 O O   . HOH   E .   ? 0.4845 0.6702 0.5419 0.1694  0.0577  0.2367  378 HOH   B O   
5860 O O   . HOH   E .   ? 0.2981 0.3940 0.2021 0.0551  0.0198  0.0188  379 HOH   B O   
5861 O O   . HOH   E .   ? 0.4724 0.6750 0.3926 -0.1036 0.0037  -0.1508 380 HOH   B O   
5862 O O   . HOH   E .   ? 0.3488 0.4186 0.4871 0.1370  -0.0187 -0.0089 381 HOH   B O   
5863 O O   . HOH   E .   ? 0.5116 0.6837 0.5999 -0.0342 0.1460  0.1038  382 HOH   B O   
5864 O O   . HOH   E .   ? 0.2869 0.2391 0.3203 -0.0001 0.0102  0.0462  383 HOH   B O   
5865 O O   . HOH   E .   ? 0.3583 0.7183 0.5332 0.1140  0.1795  0.0963  384 HOH   B O   
5866 O O   . HOH   E .   ? 0.6623 0.5852 0.4028 0.1597  0.0215  0.0493  385 HOH   B O   
5867 O O   . HOH   E .   ? 0.5448 0.4279 0.4808 -0.0619 0.0333  0.0067  386 HOH   B O   
5868 O O   . HOH   E .   ? 0.2308 0.3963 0.3420 -0.0573 -0.0816 -0.0330 387 HOH   B O   
5869 O O   . HOH   E .   ? 0.6161 0.4100 0.4309 0.0916  0.0925  -0.0963 388 HOH   B O   
5870 O O   . HOH   E .   ? 0.4369 0.3669 0.2681 -0.0009 0.0387  -0.0173 389 HOH   B O   
5871 O O   . HOH   E .   ? 0.5119 0.3936 0.4283 -0.0444 -0.0548 -0.0534 390 HOH   B O   
5872 O O   . HOH   E .   ? 0.3754 0.2020 0.3140 0.0712  -0.0290 0.0162  391 HOH   B O   
5873 O O   . HOH   E .   ? 0.4977 0.3706 0.3590 0.0058  0.0263  0.0603  392 HOH   B O   
5874 O O   . HOH   E .   ? 0.4709 0.2304 0.4434 -0.0687 0.0469  0.0394  393 HOH   B O   
5875 O O   . HOH   E .   ? 0.2434 0.4888 0.5663 -0.1678 -0.0342 -0.0255 394 HOH   B O   
5876 O O   . HOH   E .   ? 0.2907 0.4070 0.3279 0.0553  0.0109  -0.0609 395 HOH   B O   
5877 O O   . HOH   E .   ? 0.4626 0.5311 0.3489 0.1327  -0.0052 -0.0644 396 HOH   B O   
5878 O O   . HOH   E .   ? 0.4306 0.3881 0.3909 0.0324  0.1084  0.0681  397 HOH   B O   
5879 O O   . HOH   E .   ? 0.2135 0.3093 0.4711 -0.0660 -0.0733 -0.0267 398 HOH   B O   
5880 O O   . HOH   E .   ? 0.5242 0.5774 0.6344 0.1702  -0.0408 0.1835  399 HOH   B O   
5881 O O   . HOH   E .   ? 0.5806 0.4220 0.3173 -0.1983 0.0228  0.1222  400 HOH   B O   
5882 O O   . HOH   E .   ? 0.6255 0.5912 0.3825 0.2039  -0.0410 0.0309  401 HOH   B O   
# 
