data_7HEX
# 
_entry.id   7HEX 
# 
_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   7HEX         pdb_00007hex 10.2210/pdb7hex/pdb 
WWPDB D_1001407387 ?            ?                   
# 
_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                        7HEX 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.recvd_initial_deposition_date   2024-08-15 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.pdb_format_compatible           N 
_pdbx_database_status.methods_development_category    ? 
# 
_pdbx_contact_author.id                 1 
_pdbx_contact_author.name_last          Fraser 
_pdbx_contact_author.name_first         James 
_pdbx_contact_author.name_mi            S. 
_pdbx_contact_author.email              jaimefraser@gmail.com 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-5080-2859 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Correy, G.J.' 1 ? 
'Fraser, J.S.' 2 ? 
# 
_citation.id                        primary 
_citation.title                     
;Exploration of structure-activity relationships for the SARS-CoV-2 macrodomain from shape-based fragment linking and active learning.
;
_citation.journal_abbrev            'Sci Adv' 
_citation.journal_volume            11 
_citation.page_first                eads7187 
_citation.page_last                 eads7187 
_citation.year                      2025 
_citation.pdbx_database_id_PubMed   40435250 
_citation.pdbx_database_id_DOI      10.1126/sciadv.ads7187 
_citation.journal_id_ASTM           ? 
_citation.country                   US 
_citation.journal_id_ISSN           2375-2548 
_citation.journal_id_CSD            ? 
_citation.book_publisher            ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.identifier_ORCID 
_citation_author.ordinal 
primary 'Correy, G.J.'    0000-0001-5155-7325 1  
primary 'Rachman, M.M.'   0000-0003-3671-8885 2  
primary 'Togo, T.'        0000-0003-0243-0760 3  
primary 'Gahbauer, S.'    0000-0002-3115-9757 4  
primary 'Doruk, Y.U.'     0000-0002-3388-7803 5  
primary 'Stevens, M.G.V.' 0009-0004-9732-0349 6  
primary 'Jaishankar, P.'  0009-0005-2013-8941 7  
primary 'Kelley, B.'      ?                   8  
primary 'Goldman, B.'     0009-0006-6465-6959 9  
primary 'Schmidt, M.'     ?                   10 
primary 'Kramer, T.'      0009-0002-5932-7406 11 
primary 'Radchenko, D.S.' 0000-0001-5444-7754 12 
primary 'Moroz, Y.S.'     0000-0001-6073-002X 13 
primary 'Ashworth, A.'    0000-0003-1446-7878 14 
primary 'Riley, P.'       0000-0003-0797-0272 15 
primary 'Shoichet, B.K.'  0000-0002-6098-7367 16 
primary 'Renslo, A.R.'    0000-0002-1240-2846 17 
primary 'Walters, W.P.'   0000-0003-2860-7958 18 
primary 'Fraser, J.S.'    0000-0002-5080-2859 19 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Non-structural protein 3'                                                                              
18178.766 2   '3.4.19.121, 3.4.22.-' ? ? 'HIS6 purification tag and linker (MHHHHHHSSGVDLGTENLYFQ) cleaved with TEV protease' 
2 non-polymer syn 'DIMETHYL SULFOXIDE'                                                                                    78.133 1 
?                      ? ? ?                                                                                    
3 non-polymer syn '[(2S,5R)-5-(1,3-dimethyl-1H-pyrazol-4-yl)-1-(7H-pyrrolo[2,3-d]pyrimidin-4-yl)pyrrolidin-2-yl]methanol' 312.370 
1   ?                      ? ? ?                                                                                    
4 water       nat water                                                                                                   18.015 
433 ?                      ? ? ?                                                                                    
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'nsp3, PL2-PRO, Papain-like protease, Papain-like proteinase, PL-PRO' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;SMVNSFSGYLKLTDNVYIKNADIVEEAKKVKPTVVVNAANVYLKHGGGVAGALNKATNNAMQVESDDYIATNGPLKVGGS
CVLSGHNLAKHCLHVVGPNVNKGEDIQLLKSAYENFNQHEVLLAPLLSAGIFGADPIHSLRVCVDTVRTNVYLAVFDKNL
YDKLVSSFL
;
_entity_poly.pdbx_seq_one_letter_code_can   
;SMVNSFSGYLKLTDNVYIKNADIVEEAKKVKPTVVVNAANVYLKHGGGVAGALNKATNNAMQVESDDYIATNGPLKVGGS
CVLSGHNLAKHCLHVVGPNVNKGEDIQLLKSAYENFNQHEVLLAPLLSAGIFGADPIHSLRVCVDTVRTNVYLAVFDKNL
YDKLVSSFL
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'DIMETHYL SULFOXIDE'                                                                                    DMS   
3 '[(2S,5R)-5-(1,3-dimethyl-1H-pyrazol-4-yl)-1-(7H-pyrrolo[2,3-d]pyrimidin-4-yl)pyrrolidin-2-yl]methanol' A1BAG 
4 water                                                                                                   HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   SER n 
1 2   MET n 
1 3   VAL n 
1 4   ASN n 
1 5   SER n 
1 6   PHE n 
1 7   SER n 
1 8   GLY n 
1 9   TYR n 
1 10  LEU n 
1 11  LYS n 
1 12  LEU n 
1 13  THR n 
1 14  ASP n 
1 15  ASN n 
1 16  VAL n 
1 17  TYR n 
1 18  ILE n 
1 19  LYS n 
1 20  ASN n 
1 21  ALA n 
1 22  ASP n 
1 23  ILE n 
1 24  VAL n 
1 25  GLU n 
1 26  GLU n 
1 27  ALA n 
1 28  LYS n 
1 29  LYS n 
1 30  VAL n 
1 31  LYS n 
1 32  PRO n 
1 33  THR n 
1 34  VAL n 
1 35  VAL n 
1 36  VAL n 
1 37  ASN n 
1 38  ALA n 
1 39  ALA n 
1 40  ASN n 
1 41  VAL n 
1 42  TYR n 
1 43  LEU n 
1 44  LYS n 
1 45  HIS n 
1 46  GLY n 
1 47  GLY n 
1 48  GLY n 
1 49  VAL n 
1 50  ALA n 
1 51  GLY n 
1 52  ALA n 
1 53  LEU n 
1 54  ASN n 
1 55  LYS n 
1 56  ALA n 
1 57  THR n 
1 58  ASN n 
1 59  ASN n 
1 60  ALA n 
1 61  MET n 
1 62  GLN n 
1 63  VAL n 
1 64  GLU n 
1 65  SER n 
1 66  ASP n 
1 67  ASP n 
1 68  TYR n 
1 69  ILE n 
1 70  ALA n 
1 71  THR n 
1 72  ASN n 
1 73  GLY n 
1 74  PRO n 
1 75  LEU n 
1 76  LYS n 
1 77  VAL n 
1 78  GLY n 
1 79  GLY n 
1 80  SER n 
1 81  CYS n 
1 82  VAL n 
1 83  LEU n 
1 84  SER n 
1 85  GLY n 
1 86  HIS n 
1 87  ASN n 
1 88  LEU n 
1 89  ALA n 
1 90  LYS n 
1 91  HIS n 
1 92  CYS n 
1 93  LEU n 
1 94  HIS n 
1 95  VAL n 
1 96  VAL n 
1 97  GLY n 
1 98  PRO n 
1 99  ASN n 
1 100 VAL n 
1 101 ASN n 
1 102 LYS n 
1 103 GLY n 
1 104 GLU n 
1 105 ASP n 
1 106 ILE n 
1 107 GLN n 
1 108 LEU n 
1 109 LEU n 
1 110 LYS n 
1 111 SER n 
1 112 ALA n 
1 113 TYR n 
1 114 GLU n 
1 115 ASN n 
1 116 PHE n 
1 117 ASN n 
1 118 GLN n 
1 119 HIS n 
1 120 GLU n 
1 121 VAL n 
1 122 LEU n 
1 123 LEU n 
1 124 ALA n 
1 125 PRO n 
1 126 LEU n 
1 127 LEU n 
1 128 SER n 
1 129 ALA n 
1 130 GLY n 
1 131 ILE n 
1 132 PHE n 
1 133 GLY n 
1 134 ALA n 
1 135 ASP n 
1 136 PRO n 
1 137 ILE n 
1 138 HIS n 
1 139 SER n 
1 140 LEU n 
1 141 ARG n 
1 142 VAL n 
1 143 CYS n 
1 144 VAL n 
1 145 ASP n 
1 146 THR n 
1 147 VAL n 
1 148 ARG n 
1 149 THR n 
1 150 ASN n 
1 151 VAL n 
1 152 TYR n 
1 153 LEU n 
1 154 ALA n 
1 155 VAL n 
1 156 PHE n 
1 157 ASP n 
1 158 LYS n 
1 159 ASN n 
1 160 LEU n 
1 161 TYR n 
1 162 ASP n 
1 163 LYS n 
1 164 LEU n 
1 165 VAL n 
1 166 SER n 
1 167 SER n 
1 168 PHE n 
1 169 LEU n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   169 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'rep, 1a-1b' 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Severe acute respiratory syndrome coronavirus 2' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     2697049 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          plasmid 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       'pET22b(+)' 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
A1BAG non-polymer         . 
'[(2S,5R)-5-(1,3-dimethyl-1H-pyrazol-4-yl)-1-(7H-pyrrolo[2,3-d]pyrimidin-4-yl)pyrrolidin-2-yl]methanol' ? 'C16 H20 N6 O'   312.370 
ALA   'L-peptide linking' y ALANINE ? 'C3 H7 N O2'     89.093  
ARG   'L-peptide linking' y ARGININE ? 'C6 H15 N4 O2 1' 175.209 
ASN   'L-peptide linking' y ASPARAGINE ? 'C4 H8 N2 O3'    132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4'     133.103 
CYS   'L-peptide linking' y CYSTEINE ? 'C3 H7 N O2 S'   121.158 
DMS   non-polymer         . 'DIMETHYL SULFOXIDE' ? 'C2 H6 O S'      78.133  
GLN   'L-peptide linking' y GLUTAMINE ? 'C5 H10 N2 O3'   146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4'     147.129 
GLY   'peptide linking'   y GLYCINE ? 'C2 H5 N O2'     75.067  
HIS   'L-peptide linking' y HISTIDINE ? 'C6 H10 N3 O2 1' 156.162 
HOH   non-polymer         . WATER ? 'H2 O'           18.015  
ILE   'L-peptide linking' y ISOLEUCINE ? 'C6 H13 N O2'    131.173 
LEU   'L-peptide linking' y LEUCINE ? 'C6 H13 N O2'    131.173 
LYS   'L-peptide linking' y LYSINE ? 'C6 H15 N2 O2 1' 147.195 
MET   'L-peptide linking' y METHIONINE ? 'C5 H11 N O2 S'  149.211 
PHE   'L-peptide linking' y PHENYLALANINE ? 'C9 H11 N O2'    165.189 
PRO   'L-peptide linking' y PROLINE ? 'C5 H9 N O2'     115.130 
SER   'L-peptide linking' y SERINE ? 'C3 H7 N O3'     105.093 
THR   'L-peptide linking' y THREONINE ? 'C4 H9 N O3'     119.119 
TYR   'L-peptide linking' y TYROSINE ? 'C9 H11 N O3'    181.189 
VAL   'L-peptide linking' y VALINE ? 'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   SER 1   1   ?   ?   ?   A . n 
A 1 2   MET 2   2   ?   ?   ?   A . n 
A 1 3   VAL 3   3   3   VAL VAL A . n 
A 1 4   ASN 4   4   4   ASN ASN A . n 
A 1 5   SER 5   5   5   SER SER A . n 
A 1 6   PHE 6   6   6   PHE PHE A . n 
A 1 7   SER 7   7   7   SER SER A . n 
A 1 8   GLY 8   8   8   GLY GLY A . n 
A 1 9   TYR 9   9   9   TYR TYR A . n 
A 1 10  LEU 10  10  10  LEU LEU A . n 
A 1 11  LYS 11  11  11  LYS LYS A . n 
A 1 12  LEU 12  12  12  LEU LEU A . n 
A 1 13  THR 13  13  13  THR THR A . n 
A 1 14  ASP 14  14  14  ASP ASP A . n 
A 1 15  ASN 15  15  15  ASN ASN A . n 
A 1 16  VAL 16  16  16  VAL VAL A . n 
A 1 17  TYR 17  17  17  TYR TYR A . n 
A 1 18  ILE 18  18  18  ILE ILE A . n 
A 1 19  LYS 19  19  19  LYS LYS A . n 
A 1 20  ASN 20  20  20  ASN ASN A . n 
A 1 21  ALA 21  21  21  ALA ALA A . n 
A 1 22  ASP 22  22  22  ASP ASP A . n 
A 1 23  ILE 23  23  23  ILE ILE A . n 
A 1 24  VAL 24  24  24  VAL VAL A . n 
A 1 25  GLU 25  25  25  GLU GLU A . n 
A 1 26  GLU 26  26  26  GLU GLU A . n 
A 1 27  ALA 27  27  27  ALA ALA A . n 
A 1 28  LYS 28  28  28  LYS LYS A . n 
A 1 29  LYS 29  29  29  LYS LYS A . n 
A 1 30  VAL 30  30  30  VAL VAL A . n 
A 1 31  LYS 31  31  31  LYS LYS A . n 
A 1 32  PRO 32  32  32  PRO PRO A . n 
A 1 33  THR 33  33  33  THR THR A . n 
A 1 34  VAL 34  34  34  VAL VAL A . n 
A 1 35  VAL 35  35  35  VAL VAL A . n 
A 1 36  VAL 36  36  36  VAL VAL A . n 
A 1 37  ASN 37  37  37  ASN ASN A . n 
A 1 38  ALA 38  38  38  ALA ALA A . n 
A 1 39  ALA 39  39  39  ALA ALA A . n 
A 1 40  ASN 40  40  40  ASN ASN A . n 
A 1 41  VAL 41  41  41  VAL VAL A . n 
A 1 42  TYR 42  42  42  TYR TYR A . n 
A 1 43  LEU 43  43  43  LEU LEU A . n 
A 1 44  LYS 44  44  44  LYS LYS A . n 
A 1 45  HIS 45  45  45  HIS HIS A . n 
A 1 46  GLY 46  46  46  GLY GLY A . n 
A 1 47  GLY 47  47  47  GLY GLY A . n 
A 1 48  GLY 48  48  48  GLY GLY A . n 
A 1 49  VAL 49  49  49  VAL VAL A . n 
A 1 50  ALA 50  50  50  ALA ALA A . n 
A 1 51  GLY 51  51  51  GLY GLY A . n 
A 1 52  ALA 52  52  52  ALA ALA A . n 
A 1 53  LEU 53  53  53  LEU LEU A . n 
A 1 54  ASN 54  54  54  ASN ASN A . n 
A 1 55  LYS 55  55  55  LYS LYS A . n 
A 1 56  ALA 56  56  56  ALA ALA A . n 
A 1 57  THR 57  57  57  THR THR A . n 
A 1 58  ASN 58  58  58  ASN ASN A . n 
A 1 59  ASN 59  59  59  ASN ASN A . n 
A 1 60  ALA 60  60  60  ALA ALA A . n 
A 1 61  MET 61  61  61  MET MET A . n 
A 1 62  GLN 62  62  62  GLN GLN A . n 
A 1 63  VAL 63  63  63  VAL VAL A . n 
A 1 64  GLU 64  64  64  GLU GLU A . n 
A 1 65  SER 65  65  65  SER SER A . n 
A 1 66  ASP 66  66  66  ASP ASP A . n 
A 1 67  ASP 67  67  67  ASP ASP A . n 
A 1 68  TYR 68  68  68  TYR TYR A . n 
A 1 69  ILE 69  69  69  ILE ILE A . n 
A 1 70  ALA 70  70  70  ALA ALA A . n 
A 1 71  THR 71  71  71  THR THR A . n 
A 1 72  ASN 72  72  72  ASN ASN A . n 
A 1 73  GLY 73  73  73  GLY GLY A . n 
A 1 74  PRO 74  74  74  PRO PRO A . n 
A 1 75  LEU 75  75  75  LEU LEU A . n 
A 1 76  LYS 76  76  76  LYS LYS A . n 
A 1 77  VAL 77  77  77  VAL VAL A . n 
A 1 78  GLY 78  78  78  GLY GLY A . n 
A 1 79  GLY 79  79  79  GLY GLY A . n 
A 1 80  SER 80  80  80  SER SER A . n 
A 1 81  CYS 81  81  81  CYS CYS A . n 
A 1 82  VAL 82  82  82  VAL VAL A . n 
A 1 83  LEU 83  83  83  LEU LEU A . n 
A 1 84  SER 84  84  84  SER SER A . n 
A 1 85  GLY 85  85  85  GLY GLY A . n 
A 1 86  HIS 86  86  86  HIS HIS A . n 
A 1 87  ASN 87  87  87  ASN ASN A . n 
A 1 88  LEU 88  88  88  LEU LEU A . n 
A 1 89  ALA 89  89  89  ALA ALA A . n 
A 1 90  LYS 90  90  90  LYS LYS A . n 
A 1 91  HIS 91  91  91  HIS HIS A . n 
A 1 92  CYS 92  92  92  CYS CYS A . n 
A 1 93  LEU 93  93  93  LEU LEU A . n 
A 1 94  HIS 94  94  94  HIS HIS A . n 
A 1 95  VAL 95  95  95  VAL VAL A . n 
A 1 96  VAL 96  96  96  VAL VAL A . n 
A 1 97  GLY 97  97  97  GLY GLY A . n 
A 1 98  PRO 98  98  98  PRO PRO A . n 
A 1 99  ASN 99  99  99  ASN ASN A . n 
A 1 100 VAL 100 100 100 VAL VAL A . n 
A 1 101 ASN 101 101 101 ASN ASN A . n 
A 1 102 LYS 102 102 102 LYS LYS A . n 
A 1 103 GLY 103 103 103 GLY GLY A . n 
A 1 104 GLU 104 104 104 GLU GLU A . n 
A 1 105 ASP 105 105 105 ASP ASP A . n 
A 1 106 ILE 106 106 106 ILE ILE A . n 
A 1 107 GLN 107 107 107 GLN GLN A . n 
A 1 108 LEU 108 108 108 LEU LEU A . n 
A 1 109 LEU 109 109 109 LEU LEU A . n 
A 1 110 LYS 110 110 110 LYS LYS A . n 
A 1 111 SER 111 111 111 SER SER A . n 
A 1 112 ALA 112 112 112 ALA ALA A . n 
A 1 113 TYR 113 113 113 TYR TYR A . n 
A 1 114 GLU 114 114 114 GLU GLU A . n 
A 1 115 ASN 115 115 115 ASN ASN A . n 
A 1 116 PHE 116 116 116 PHE PHE A . n 
A 1 117 ASN 117 117 117 ASN ASN A . n 
A 1 118 GLN 118 118 118 GLN GLN A . n 
A 1 119 HIS 119 119 119 HIS HIS A . n 
A 1 120 GLU 120 120 120 GLU GLU A . n 
A 1 121 VAL 121 121 121 VAL VAL A . n 
A 1 122 LEU 122 122 122 LEU LEU A . n 
A 1 123 LEU 123 123 123 LEU LEU A . n 
A 1 124 ALA 124 124 124 ALA ALA A . n 
A 1 125 PRO 125 125 125 PRO PRO A . n 
A 1 126 LEU 126 126 126 LEU LEU A . n 
A 1 127 LEU 127 127 127 LEU LEU A . n 
A 1 128 SER 128 128 128 SER SER A . n 
A 1 129 ALA 129 129 129 ALA ALA A . n 
A 1 130 GLY 130 130 130 GLY GLY A . n 
A 1 131 ILE 131 131 131 ILE ILE A . n 
A 1 132 PHE 132 132 132 PHE PHE A . n 
A 1 133 GLY 133 133 133 GLY GLY A . n 
A 1 134 ALA 134 134 134 ALA ALA A . n 
A 1 135 ASP 135 135 135 ASP ASP A . n 
A 1 136 PRO 136 136 136 PRO PRO A . n 
A 1 137 ILE 137 137 137 ILE ILE A . n 
A 1 138 HIS 138 138 138 HIS HIS A . n 
A 1 139 SER 139 139 139 SER SER A . n 
A 1 140 LEU 140 140 140 LEU LEU A . n 
A 1 141 ARG 141 141 141 ARG ARG A . n 
A 1 142 VAL 142 142 142 VAL VAL A . n 
A 1 143 CYS 143 143 143 CYS CYS A . n 
A 1 144 VAL 144 144 144 VAL VAL A . n 
A 1 145 ASP 145 145 145 ASP ASP A . n 
A 1 146 THR 146 146 146 THR THR A . n 
A 1 147 VAL 147 147 147 VAL VAL A . n 
A 1 148 ARG 148 148 148 ARG ARG A . n 
A 1 149 THR 149 149 149 THR THR A . n 
A 1 150 ASN 150 150 150 ASN ASN A . n 
A 1 151 VAL 151 151 151 VAL VAL A . n 
A 1 152 TYR 152 152 152 TYR TYR A . n 
A 1 153 LEU 153 153 153 LEU LEU A . n 
A 1 154 ALA 154 154 154 ALA ALA A . n 
A 1 155 VAL 155 155 155 VAL VAL A . n 
A 1 156 PHE 156 156 156 PHE PHE A . n 
A 1 157 ASP 157 157 157 ASP ASP A . n 
A 1 158 LYS 158 158 158 LYS LYS A . n 
A 1 159 ASN 159 159 159 ASN ASN A . n 
A 1 160 LEU 160 160 160 LEU LEU A . n 
A 1 161 TYR 161 161 161 TYR TYR A . n 
A 1 162 ASP 162 162 162 ASP ASP A . n 
A 1 163 LYS 163 163 163 LYS LYS A . n 
A 1 164 LEU 164 164 164 LEU LEU A . n 
A 1 165 VAL 165 165 165 VAL VAL A . n 
A 1 166 SER 166 166 166 SER SER A . n 
A 1 167 SER 167 167 167 SER SER A . n 
A 1 168 PHE 168 168 168 PHE PHE A . n 
A 1 169 LEU 169 169 169 LEU LEU A . n 
B 1 1   SER 1   1   1   SER SER B . n 
B 1 2   MET 2   2   2   MET MET B . n 
B 1 3   VAL 3   3   3   VAL VAL B . n 
B 1 4   ASN 4   4   4   ASN ASN B . n 
B 1 5   SER 5   5   5   SER SER B . n 
B 1 6   PHE 6   6   6   PHE PHE B . n 
B 1 7   SER 7   7   7   SER SER B . n 
B 1 8   GLY 8   8   8   GLY GLY B . n 
B 1 9   TYR 9   9   9   TYR TYR B . n 
B 1 10  LEU 10  10  10  LEU LEU B . n 
B 1 11  LYS 11  11  11  LYS LYS B . n 
B 1 12  LEU 12  12  12  LEU LEU B . n 
B 1 13  THR 13  13  13  THR THR B . n 
B 1 14  ASP 14  14  14  ASP ASP B . n 
B 1 15  ASN 15  15  15  ASN ASN B . n 
B 1 16  VAL 16  16  16  VAL VAL B . n 
B 1 17  TYR 17  17  17  TYR TYR B . n 
B 1 18  ILE 18  18  18  ILE ILE B . n 
B 1 19  LYS 19  19  19  LYS LYS B . n 
B 1 20  ASN 20  20  20  ASN ASN B . n 
B 1 21  ALA 21  21  21  ALA ALA B . n 
B 1 22  ASP 22  22  22  ASP ASP B . n 
B 1 23  ILE 23  23  23  ILE ILE B . n 
B 1 24  VAL 24  24  24  VAL VAL B . n 
B 1 25  GLU 25  25  25  GLU GLU B . n 
B 1 26  GLU 26  26  26  GLU GLU B . n 
B 1 27  ALA 27  27  27  ALA ALA B . n 
B 1 28  LYS 28  28  28  LYS LYS B . n 
B 1 29  LYS 29  29  29  LYS LYS B . n 
B 1 30  VAL 30  30  30  VAL VAL B . n 
B 1 31  LYS 31  31  31  LYS LYS B . n 
B 1 32  PRO 32  32  32  PRO PRO B . n 
B 1 33  THR 33  33  33  THR THR B . n 
B 1 34  VAL 34  34  34  VAL VAL B . n 
B 1 35  VAL 35  35  35  VAL VAL B . n 
B 1 36  VAL 36  36  36  VAL VAL B . n 
B 1 37  ASN 37  37  37  ASN ASN B . n 
B 1 38  ALA 38  38  38  ALA ALA B . n 
B 1 39  ALA 39  39  39  ALA ALA B . n 
B 1 40  ASN 40  40  40  ASN ASN B . n 
B 1 41  VAL 41  41  41  VAL VAL B . n 
B 1 42  TYR 42  42  42  TYR TYR B . n 
B 1 43  LEU 43  43  43  LEU LEU B . n 
B 1 44  LYS 44  44  44  LYS LYS B . n 
B 1 45  HIS 45  45  45  HIS HIS B . n 
B 1 46  GLY 46  46  46  GLY GLY B . n 
B 1 47  GLY 47  47  47  GLY GLY B . n 
B 1 48  GLY 48  48  48  GLY GLY B . n 
B 1 49  VAL 49  49  49  VAL VAL B . n 
B 1 50  ALA 50  50  50  ALA ALA B . n 
B 1 51  GLY 51  51  51  GLY GLY B . n 
B 1 52  ALA 52  52  52  ALA ALA B . n 
B 1 53  LEU 53  53  53  LEU LEU B . n 
B 1 54  ASN 54  54  54  ASN ASN B . n 
B 1 55  LYS 55  55  55  LYS LYS B . n 
B 1 56  ALA 56  56  56  ALA ALA B . n 
B 1 57  THR 57  57  57  THR THR B . n 
B 1 58  ASN 58  58  58  ASN ASN B . n 
B 1 59  ASN 59  59  59  ASN ASN B . n 
B 1 60  ALA 60  60  60  ALA ALA B . n 
B 1 61  MET 61  61  61  MET MET B . n 
B 1 62  GLN 62  62  62  GLN GLN B . n 
B 1 63  VAL 63  63  63  VAL VAL B . n 
B 1 64  GLU 64  64  64  GLU GLU B . n 
B 1 65  SER 65  65  65  SER SER B . n 
B 1 66  ASP 66  66  66  ASP ASP B . n 
B 1 67  ASP 67  67  67  ASP ASP B . n 
B 1 68  TYR 68  68  68  TYR TYR B . n 
B 1 69  ILE 69  69  69  ILE ILE B . n 
B 1 70  ALA 70  70  70  ALA ALA B . n 
B 1 71  THR 71  71  71  THR THR B . n 
B 1 72  ASN 72  72  72  ASN ASN B . n 
B 1 73  GLY 73  73  73  GLY GLY B . n 
B 1 74  PRO 74  74  74  PRO PRO B . n 
B 1 75  LEU 75  75  75  LEU LEU B . n 
B 1 76  LYS 76  76  76  LYS LYS B . n 
B 1 77  VAL 77  77  77  VAL VAL B . n 
B 1 78  GLY 78  78  78  GLY GLY B . n 
B 1 79  GLY 79  79  79  GLY GLY B . n 
B 1 80  SER 80  80  80  SER SER B . n 
B 1 81  CYS 81  81  81  CYS CYS B . n 
B 1 82  VAL 82  82  82  VAL VAL B . n 
B 1 83  LEU 83  83  83  LEU LEU B . n 
B 1 84  SER 84  84  84  SER SER B . n 
B 1 85  GLY 85  85  85  GLY GLY B . n 
B 1 86  HIS 86  86  86  HIS HIS B . n 
B 1 87  ASN 87  87  87  ASN ASN B . n 
B 1 88  LEU 88  88  88  LEU LEU B . n 
B 1 89  ALA 89  89  89  ALA ALA B . n 
B 1 90  LYS 90  90  90  LYS LYS B . n 
B 1 91  HIS 91  91  91  HIS HIS B . n 
B 1 92  CYS 92  92  92  CYS CYS B . n 
B 1 93  LEU 93  93  93  LEU LEU B . n 
B 1 94  HIS 94  94  94  HIS HIS B . n 
B 1 95  VAL 95  95  95  VAL VAL B . n 
B 1 96  VAL 96  96  96  VAL VAL B . n 
B 1 97  GLY 97  97  97  GLY GLY B . n 
B 1 98  PRO 98  98  98  PRO PRO B . n 
B 1 99  ASN 99  99  99  ASN ASN B . n 
B 1 100 VAL 100 100 100 VAL VAL B . n 
B 1 101 ASN 101 101 101 ASN ASN B . n 
B 1 102 LYS 102 102 102 LYS LYS B . n 
B 1 103 GLY 103 103 103 GLY GLY B . n 
B 1 104 GLU 104 104 104 GLU GLU B . n 
B 1 105 ASP 105 105 105 ASP ASP B . n 
B 1 106 ILE 106 106 106 ILE ILE B . n 
B 1 107 GLN 107 107 107 GLN GLN B . n 
B 1 108 LEU 108 108 108 LEU LEU B . n 
B 1 109 LEU 109 109 109 LEU LEU B . n 
B 1 110 LYS 110 110 110 LYS LYS B . n 
B 1 111 SER 111 111 111 SER SER B . n 
B 1 112 ALA 112 112 112 ALA ALA B . n 
B 1 113 TYR 113 113 113 TYR TYR B . n 
B 1 114 GLU 114 114 114 GLU GLU B . n 
B 1 115 ASN 115 115 115 ASN ASN B . n 
B 1 116 PHE 116 116 116 PHE PHE B . n 
B 1 117 ASN 117 117 117 ASN ASN B . n 
B 1 118 GLN 118 118 118 GLN GLN B . n 
B 1 119 HIS 119 119 119 HIS HIS B . n 
B 1 120 GLU 120 120 120 GLU GLU B . n 
B 1 121 VAL 121 121 121 VAL VAL B . n 
B 1 122 LEU 122 122 122 LEU LEU B . n 
B 1 123 LEU 123 123 123 LEU LEU B . n 
B 1 124 ALA 124 124 124 ALA ALA B . n 
B 1 125 PRO 125 125 125 PRO PRO B . n 
B 1 126 LEU 126 126 126 LEU LEU B . n 
B 1 127 LEU 127 127 127 LEU LEU B . n 
B 1 128 SER 128 128 128 SER SER B . n 
B 1 129 ALA 129 129 129 ALA ALA B . n 
B 1 130 GLY 130 130 130 GLY GLY B . n 
B 1 131 ILE 131 131 131 ILE ILE B . n 
B 1 132 PHE 132 132 132 PHE PHE B . n 
B 1 133 GLY 133 133 133 GLY GLY B . n 
B 1 134 ALA 134 134 134 ALA ALA B . n 
B 1 135 ASP 135 135 135 ASP ASP B . n 
B 1 136 PRO 136 136 136 PRO PRO B . n 
B 1 137 ILE 137 137 137 ILE ILE B . n 
B 1 138 HIS 138 138 138 HIS HIS B . n 
B 1 139 SER 139 139 139 SER SER B . n 
B 1 140 LEU 140 140 140 LEU LEU B . n 
B 1 141 ARG 141 141 141 ARG ARG B . n 
B 1 142 VAL 142 142 142 VAL VAL B . n 
B 1 143 CYS 143 143 143 CYS CYS B . n 
B 1 144 VAL 144 144 144 VAL VAL B . n 
B 1 145 ASP 145 145 145 ASP ASP B . n 
B 1 146 THR 146 146 146 THR THR B . n 
B 1 147 VAL 147 147 147 VAL VAL B . n 
B 1 148 ARG 148 148 148 ARG ARG B . n 
B 1 149 THR 149 149 149 THR THR B . n 
B 1 150 ASN 150 150 150 ASN ASN B . n 
B 1 151 VAL 151 151 151 VAL VAL B . n 
B 1 152 TYR 152 152 152 TYR TYR B . n 
B 1 153 LEU 153 153 153 LEU LEU B . n 
B 1 154 ALA 154 154 154 ALA ALA B . n 
B 1 155 VAL 155 155 155 VAL VAL B . n 
B 1 156 PHE 156 156 156 PHE PHE B . n 
B 1 157 ASP 157 157 157 ASP ASP B . n 
B 1 158 LYS 158 158 158 LYS LYS B . n 
B 1 159 ASN 159 159 159 ASN ASN B . n 
B 1 160 LEU 160 160 160 LEU LEU B . n 
B 1 161 TYR 161 161 161 TYR TYR B . n 
B 1 162 ASP 162 162 162 ASP ASP B . n 
B 1 163 LYS 163 163 163 LYS LYS B . n 
B 1 164 LEU 164 164 164 LEU LEU B . n 
B 1 165 VAL 165 165 165 VAL VAL B . n 
B 1 166 SER 166 166 166 SER SER B . n 
B 1 167 SER 167 167 167 SER SER B . n 
B 1 168 PHE 168 168 168 PHE PHE B . n 
B 1 169 LEU 169 169 169 LEU LEU B . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 DMS   1   301 301  DMS   DMS A . 
D 3 A1BAG 1   302 201  A1BAG LA1 A . 
E 4 HOH   1   401 625  HOH   HOH A . 
E 4 HOH   2   402 25   HOH   HOH A . 
E 4 HOH   3   403 196  HOH   HOH A . 
E 4 HOH   4   404 229  HOH   HOH A . 
E 4 HOH   5   405 1301 HOH   HOH A . 
E 4 HOH   6   406 109  HOH   HOH A . 
E 4 HOH   7   407 192  HOH   HOH A . 
E 4 HOH   8   408 74   HOH   HOH A . 
E 4 HOH   9   409 93   HOH   HOH A . 
E 4 HOH   10  410 292  HOH   HOH A . 
E 4 HOH   11  411 105  HOH   HOH A . 
E 4 HOH   12  412 148  HOH   HOH A . 
E 4 HOH   13  413 409  HOH   HOH A . 
E 4 HOH   14  414 493  HOH   HOH A . 
E 4 HOH   15  415 337  HOH   HOH A . 
E 4 HOH   16  416 209  HOH   HOH A . 
E 4 HOH   17  417 76   HOH   HOH A . 
E 4 HOH   18  418 124  HOH   HOH A . 
E 4 HOH   19  419 1295 HOH   HOH A . 
E 4 HOH   20  420 281  HOH   HOH A . 
E 4 HOH   21  421 153  HOH   HOH A . 
E 4 HOH   22  422 78   HOH   HOH A . 
E 4 HOH   23  423 151  HOH   HOH A . 
E 4 HOH   24  424 225  HOH   HOH A . 
E 4 HOH   25  425 1313 HOH   HOH A . 
E 4 HOH   26  426 1310 HOH   HOH A . 
E 4 HOH   27  427 964  HOH   HOH A . 
E 4 HOH   28  428 236  HOH   HOH A . 
E 4 HOH   29  429 57   HOH   HOH A . 
E 4 HOH   30  430 1309 HOH   HOH A . 
E 4 HOH   31  431 247  HOH   HOH A . 
E 4 HOH   32  432 136  HOH   HOH A . 
E 4 HOH   33  433 469  HOH   HOH A . 
E 4 HOH   34  434 164  HOH   HOH A . 
E 4 HOH   35  435 140  HOH   HOH A . 
E 4 HOH   36  436 49   HOH   HOH A . 
E 4 HOH   37  437 396  HOH   HOH A . 
E 4 HOH   38  438 241  HOH   HOH A . 
E 4 HOH   39  439 21   HOH   HOH A . 
E 4 HOH   40  440 42   HOH   HOH A . 
E 4 HOH   41  441 661  HOH   HOH A . 
E 4 HOH   42  442 320  HOH   HOH A . 
E 4 HOH   43  443 92   HOH   HOH A . 
E 4 HOH   44  444 939  HOH   HOH A . 
E 4 HOH   45  445 139  HOH   HOH A . 
E 4 HOH   46  446 630  HOH   HOH A . 
E 4 HOH   47  447 12   HOH   HOH A . 
E 4 HOH   48  448 102  HOH   HOH A . 
E 4 HOH   49  449 34   HOH   HOH A . 
E 4 HOH   50  450 461  HOH   HOH A . 
E 4 HOH   51  451 1283 HOH   HOH A . 
E 4 HOH   52  452 165  HOH   HOH A . 
E 4 HOH   53  453 1300 HOH   HOH A . 
E 4 HOH   54  454 66   HOH   HOH A . 
E 4 HOH   55  455 2    HOH   HOH A . 
E 4 HOH   56  456 18   HOH   HOH A . 
E 4 HOH   57  457 662  HOH   HOH A . 
E 4 HOH   58  458 1308 HOH   HOH A . 
E 4 HOH   59  459 2    HOH   HOH A . 
E 4 HOH   60  460 17   HOH   HOH A . 
E 4 HOH   61  461 138  HOH   HOH A . 
E 4 HOH   62  462 354  HOH   HOH A . 
E 4 HOH   63  463 162  HOH   HOH A . 
E 4 HOH   64  464 19   HOH   HOH A . 
E 4 HOH   65  465 86   HOH   HOH A . 
E 4 HOH   66  466 45   HOH   HOH A . 
E 4 HOH   67  467 81   HOH   HOH A . 
E 4 HOH   68  468 169  HOH   HOH A . 
E 4 HOH   69  469 186  HOH   HOH A . 
E 4 HOH   70  470 19   HOH   HOH A . 
E 4 HOH   71  471 5    HOH   HOH A . 
E 4 HOH   72  472 1094 HOH   HOH A . 
E 4 HOH   73  473 56   HOH   HOH A . 
E 4 HOH   74  474 21   HOH   HOH A . 
E 4 HOH   75  475 39   HOH   HOH A . 
E 4 HOH   76  476 24   HOH   HOH A . 
E 4 HOH   77  477 36   HOH   HOH A . 
E 4 HOH   78  478 159  HOH   HOH A . 
E 4 HOH   79  479 132  HOH   HOH A . 
E 4 HOH   80  480 46   HOH   HOH A . 
E 4 HOH   81  481 35   HOH   HOH A . 
E 4 HOH   82  482 1290 HOH   HOH A . 
E 4 HOH   83  483 155  HOH   HOH A . 
E 4 HOH   84  484 27   HOH   HOH A . 
E 4 HOH   85  485 12   HOH   HOH A . 
E 4 HOH   86  486 218  HOH   HOH A . 
E 4 HOH   87  487 134  HOH   HOH A . 
E 4 HOH   88  488 62   HOH   HOH A . 
E 4 HOH   89  489 26   HOH   HOH A . 
E 4 HOH   90  490 296  HOH   HOH A . 
E 4 HOH   91  491 195  HOH   HOH A . 
E 4 HOH   92  492 393  HOH   HOH A . 
E 4 HOH   93  493 15   HOH   HOH A . 
E 4 HOH   94  494 366  HOH   HOH A . 
E 4 HOH   95  495 33   HOH   HOH A . 
E 4 HOH   96  496 154  HOH   HOH A . 
E 4 HOH   97  497 3    HOH   HOH A . 
E 4 HOH   98  498 26   HOH   HOH A . 
E 4 HOH   99  499 333  HOH   HOH A . 
E 4 HOH   100 500 13   HOH   HOH A . 
E 4 HOH   101 501 6    HOH   HOH A . 
E 4 HOH   102 502 116  HOH   HOH A . 
E 4 HOH   103 503 58   HOH   HOH A . 
E 4 HOH   104 504 83   HOH   HOH A . 
E 4 HOH   105 505 67   HOH   HOH A . 
E 4 HOH   106 506 121  HOH   HOH A . 
E 4 HOH   107 507 1315 HOH   HOH A . 
E 4 HOH   108 508 5    HOH   HOH A . 
E 4 HOH   109 509 381  HOH   HOH A . 
E 4 HOH   110 510 25   HOH   HOH A . 
E 4 HOH   111 511 96   HOH   HOH A . 
E 4 HOH   112 512 1238 HOH   HOH A . 
E 4 HOH   113 513 68   HOH   HOH A . 
E 4 HOH   114 514 199  HOH   HOH A . 
E 4 HOH   115 515 1275 HOH   HOH A . 
E 4 HOH   116 516 405  HOH   HOH A . 
E 4 HOH   117 517 397  HOH   HOH A . 
E 4 HOH   118 518 11   HOH   HOH A . 
E 4 HOH   119 519 212  HOH   HOH A . 
E 4 HOH   120 520 85   HOH   HOH A . 
E 4 HOH   121 521 122  HOH   HOH A . 
E 4 HOH   122 522 1068 HOH   HOH A . 
E 4 HOH   123 523 8    HOH   HOH A . 
E 4 HOH   124 524 303  HOH   HOH A . 
E 4 HOH   125 525 4    HOH   HOH A . 
E 4 HOH   126 526 351  HOH   HOH A . 
E 4 HOH   127 527 1279 HOH   HOH A . 
E 4 HOH   128 528 123  HOH   HOH A . 
E 4 HOH   129 529 95   HOH   HOH A . 
E 4 HOH   130 530 1222 HOH   HOH A . 
E 4 HOH   131 531 582  HOH   HOH A . 
E 4 HOH   132 532 125  HOH   HOH A . 
E 4 HOH   133 533 1289 HOH   HOH A . 
E 4 HOH   134 534 278  HOH   HOH A . 
E 4 HOH   135 535 51   HOH   HOH A . 
E 4 HOH   136 536 156  HOH   HOH A . 
E 4 HOH   137 537 23   HOH   HOH A . 
E 4 HOH   138 538 53   HOH   HOH A . 
E 4 HOH   139 539 70   HOH   HOH A . 
E 4 HOH   140 540 40   HOH   HOH A . 
E 4 HOH   141 541 10   HOH   HOH A . 
E 4 HOH   142 542 115  HOH   HOH A . 
E 4 HOH   143 543 952  HOH   HOH A . 
E 4 HOH   144 544 7    HOH   HOH A . 
E 4 HOH   145 545 944  HOH   HOH A . 
E 4 HOH   146 546 4    HOH   HOH A . 
E 4 HOH   147 547 16   HOH   HOH A . 
E 4 HOH   148 548 6    HOH   HOH A . 
E 4 HOH   149 549 14   HOH   HOH A . 
E 4 HOH   150 550 71   HOH   HOH A . 
E 4 HOH   151 551 80   HOH   HOH A . 
E 4 HOH   152 552 576  HOH   HOH A . 
E 4 HOH   153 553 188  HOH   HOH A . 
E 4 HOH   154 554 97   HOH   HOH A . 
E 4 HOH   155 555 94   HOH   HOH A . 
E 4 HOH   156 556 73   HOH   HOH A . 
E 4 HOH   157 557 1189 HOH   HOH A . 
E 4 HOH   158 558 104  HOH   HOH A . 
E 4 HOH   159 559 330  HOH   HOH A . 
E 4 HOH   160 560 79   HOH   HOH A . 
E 4 HOH   161 561 1296 HOH   HOH A . 
E 4 HOH   162 562 16   HOH   HOH A . 
E 4 HOH   163 563 8    HOH   HOH A . 
E 4 HOH   164 564 107  HOH   HOH A . 
E 4 HOH   165 565 1    HOH   HOH A . 
E 4 HOH   166 566 1119 HOH   HOH A . 
E 4 HOH   167 567 509  HOH   HOH A . 
E 4 HOH   168 568 1134 HOH   HOH A . 
E 4 HOH   169 569 163  HOH   HOH A . 
E 4 HOH   170 570 1286 HOH   HOH A . 
E 4 HOH   171 571 726  HOH   HOH A . 
E 4 HOH   172 572 408  HOH   HOH A . 
E 4 HOH   173 573 756  HOH   HOH A . 
E 4 HOH   174 574 361  HOH   HOH A . 
E 4 HOH   175 575 126  HOH   HOH A . 
E 4 HOH   176 576 63   HOH   HOH A . 
E 4 HOH   177 577 280  HOH   HOH A . 
E 4 HOH   178 578 801  HOH   HOH A . 
E 4 HOH   179 579 556  HOH   HOH A . 
E 4 HOH   180 580 319  HOH   HOH A . 
E 4 HOH   181 581 1307 HOH   HOH A . 
E 4 HOH   182 582 250  HOH   HOH A . 
E 4 HOH   183 583 342  HOH   HOH A . 
E 4 HOH   184 584 1314 HOH   HOH A . 
E 4 HOH   185 585 135  HOH   HOH A . 
E 4 HOH   186 586 1306 HOH   HOH A . 
E 4 HOH   187 587 9    HOH   HOH A . 
E 4 HOH   188 588 1287 HOH   HOH A . 
E 4 HOH   189 589 202  HOH   HOH A . 
E 4 HOH   190 590 695  HOH   HOH A . 
E 4 HOH   191 591 24   HOH   HOH A . 
E 4 HOH   192 592 17   HOH   HOH A . 
E 4 HOH   193 593 919  HOH   HOH A . 
E 4 HOH   194 594 267  HOH   HOH A . 
E 4 HOH   195 595 1276 HOH   HOH A . 
E 4 HOH   196 596 370  HOH   HOH A . 
E 4 HOH   197 597 674  HOH   HOH A . 
E 4 HOH   198 598 1299 HOH   HOH A . 
E 4 HOH   199 599 224  HOH   HOH A . 
E 4 HOH   200 600 315  HOH   HOH A . 
E 4 HOH   201 601 318  HOH   HOH A . 
E 4 HOH   202 602 309  HOH   HOH A . 
E 4 HOH   203 603 521  HOH   HOH A . 
E 4 HOH   204 604 711  HOH   HOH A . 
E 4 HOH   205 605 20   HOH   HOH A . 
E 4 HOH   206 606 7    HOH   HOH A . 
E 4 HOH   207 607 805  HOH   HOH A . 
E 4 HOH   208 608 208  HOH   HOH A . 
E 4 HOH   209 609 263  HOH   HOH A . 
E 4 HOH   210 610 941  HOH   HOH A . 
E 4 HOH   211 611 3    HOH   HOH A . 
E 4 HOH   212 612 331  HOH   HOH A . 
E 4 HOH   213 613 152  HOH   HOH A . 
E 4 HOH   214 614 356  HOH   HOH A . 
E 4 HOH   215 615 1071 HOH   HOH A . 
E 4 HOH   216 616 350  HOH   HOH A . 
E 4 HOH   217 617 180  HOH   HOH A . 
E 4 HOH   218 618 363  HOH   HOH A . 
E 4 HOH   219 619 371  HOH   HOH A . 
E 4 HOH   220 620 313  HOH   HOH A . 
E 4 HOH   221 621 1284 HOH   HOH A . 
E 4 HOH   222 622 18   HOH   HOH A . 
E 4 HOH   223 623 22   HOH   HOH A . 
E 4 HOH   224 624 326  HOH   HOH A . 
E 4 HOH   225 625 185  HOH   HOH A . 
E 4 HOH   226 626 429  HOH   HOH A . 
E 4 HOH   227 627 772  HOH   HOH A . 
E 4 HOH   228 628 1292 HOH   HOH A . 
E 4 HOH   229 629 376  HOH   HOH A . 
E 4 HOH   230 630 1074 HOH   HOH A . 
E 4 HOH   231 631 346  HOH   HOH A . 
E 4 HOH   232 632 1078 HOH   HOH A . 
F 4 HOH   1   201 64   HOH   HOH B . 
F 4 HOH   2   202 549  HOH   HOH B . 
F 4 HOH   3   203 531  HOH   HOH B . 
F 4 HOH   4   204 358  HOH   HOH B . 
F 4 HOH   5   205 364  HOH   HOH B . 
F 4 HOH   6   206 398  HOH   HOH B . 
F 4 HOH   7   207 900  HOH   HOH B . 
F 4 HOH   8   208 1249 HOH   HOH B . 
F 4 HOH   9   209 758  HOH   HOH B . 
F 4 HOH   10  210 240  HOH   HOH B . 
F 4 HOH   11  211 654  HOH   HOH B . 
F 4 HOH   12  212 743  HOH   HOH B . 
F 4 HOH   13  213 232  HOH   HOH B . 
F 4 HOH   14  214 353  HOH   HOH B . 
F 4 HOH   15  215 120  HOH   HOH B . 
F 4 HOH   16  216 50   HOH   HOH B . 
F 4 HOH   17  217 15   HOH   HOH B . 
F 4 HOH   18  218 723  HOH   HOH B . 
F 4 HOH   19  219 264  HOH   HOH B . 
F 4 HOH   20  220 452  HOH   HOH B . 
F 4 HOH   21  221 276  HOH   HOH B . 
F 4 HOH   22  222 444  HOH   HOH B . 
F 4 HOH   23  223 131  HOH   HOH B . 
F 4 HOH   24  224 282  HOH   HOH B . 
F 4 HOH   25  225 54   HOH   HOH B . 
F 4 HOH   26  226 75   HOH   HOH B . 
F 4 HOH   27  227 332  HOH   HOH B . 
F 4 HOH   28  228 343  HOH   HOH B . 
F 4 HOH   29  229 1278 HOH   HOH B . 
F 4 HOH   30  230 128  HOH   HOH B . 
F 4 HOH   31  231 127  HOH   HOH B . 
F 4 HOH   32  232 272  HOH   HOH B . 
F 4 HOH   33  233 82   HOH   HOH B . 
F 4 HOH   34  234 1140 HOH   HOH B . 
F 4 HOH   35  235 205  HOH   HOH B . 
F 4 HOH   36  236 1    HOH   HOH B . 
F 4 HOH   37  237 110  HOH   HOH B . 
F 4 HOH   38  238 69   HOH   HOH B . 
F 4 HOH   39  239 60   HOH   HOH B . 
F 4 HOH   40  240 181  HOH   HOH B . 
F 4 HOH   41  241 300  HOH   HOH B . 
F 4 HOH   42  242 1312 HOH   HOH B . 
F 4 HOH   43  243 30   HOH   HOH B . 
F 4 HOH   44  244 166  HOH   HOH B . 
F 4 HOH   45  245 133  HOH   HOH B . 
F 4 HOH   46  246 143  HOH   HOH B . 
F 4 HOH   47  247 9    HOH   HOH B . 
F 4 HOH   48  248 14   HOH   HOH B . 
F 4 HOH   49  249 252  HOH   HOH B . 
F 4 HOH   50  250 31   HOH   HOH B . 
F 4 HOH   51  251 231  HOH   HOH B . 
F 4 HOH   52  252 325  HOH   HOH B . 
F 4 HOH   53  253 72   HOH   HOH B . 
F 4 HOH   54  254 172  HOH   HOH B . 
F 4 HOH   55  255 144  HOH   HOH B . 
F 4 HOH   56  256 347  HOH   HOH B . 
F 4 HOH   57  257 150  HOH   HOH B . 
F 4 HOH   58  258 52   HOH   HOH B . 
F 4 HOH   59  259 129  HOH   HOH B . 
F 4 HOH   60  260 47   HOH   HOH B . 
F 4 HOH   61  261 59   HOH   HOH B . 
F 4 HOH   62  262 10   HOH   HOH B . 
F 4 HOH   63  263 41   HOH   HOH B . 
F 4 HOH   64  264 271  HOH   HOH B . 
F 4 HOH   65  265 391  HOH   HOH B . 
F 4 HOH   66  266 11   HOH   HOH B . 
F 4 HOH   67  267 20   HOH   HOH B . 
F 4 HOH   68  268 221  HOH   HOH B . 
F 4 HOH   69  269 103  HOH   HOH B . 
F 4 HOH   70  270 117  HOH   HOH B . 
F 4 HOH   71  271 61   HOH   HOH B . 
F 4 HOH   72  272 243  HOH   HOH B . 
F 4 HOH   73  273 302  HOH   HOH B . 
F 4 HOH   74  274 1106 HOH   HOH B . 
F 4 HOH   75  275 77   HOH   HOH B . 
F 4 HOH   76  276 242  HOH   HOH B . 
F 4 HOH   77  277 84   HOH   HOH B . 
F 4 HOH   78  278 114  HOH   HOH B . 
F 4 HOH   79  279 106  HOH   HOH B . 
F 4 HOH   80  280 1277 HOH   HOH B . 
F 4 HOH   81  281 704  HOH   HOH B . 
F 4 HOH   82  282 22   HOH   HOH B . 
F 4 HOH   83  283 43   HOH   HOH B . 
F 4 HOH   84  284 175  HOH   HOH B . 
F 4 HOH   85  285 88   HOH   HOH B . 
F 4 HOH   86  286 13   HOH   HOH B . 
F 4 HOH   87  287 89   HOH   HOH B . 
F 4 HOH   88  288 287  HOH   HOH B . 
F 4 HOH   89  289 137  HOH   HOH B . 
F 4 HOH   90  290 1066 HOH   HOH B . 
F 4 HOH   91  291 635  HOH   HOH B . 
F 4 HOH   92  292 160  HOH   HOH B . 
F 4 HOH   93  293 147  HOH   HOH B . 
F 4 HOH   94  294 299  HOH   HOH B . 
F 4 HOH   95  295 1305 HOH   HOH B . 
F 4 HOH   96  296 220  HOH   HOH B . 
F 4 HOH   97  297 99   HOH   HOH B . 
F 4 HOH   98  298 235  HOH   HOH B . 
F 4 HOH   99  299 416  HOH   HOH B . 
F 4 HOH   100 300 297  HOH   HOH B . 
F 4 HOH   101 301 112  HOH   HOH B . 
F 4 HOH   102 302 387  HOH   HOH B . 
F 4 HOH   103 303 1285 HOH   HOH B . 
F 4 HOH   104 304 32   HOH   HOH B . 
F 4 HOH   105 305 38   HOH   HOH B . 
F 4 HOH   106 306 316  HOH   HOH B . 
F 4 HOH   107 307 311  HOH   HOH B . 
F 4 HOH   108 308 216  HOH   HOH B . 
F 4 HOH   109 309 142  HOH   HOH B . 
F 4 HOH   110 310 37   HOH   HOH B . 
F 4 HOH   111 311 91   HOH   HOH B . 
F 4 HOH   112 312 101  HOH   HOH B . 
F 4 HOH   113 313 48   HOH   HOH B . 
F 4 HOH   114 314 170  HOH   HOH B . 
F 4 HOH   115 315 215  HOH   HOH B . 
F 4 HOH   116 316 23   HOH   HOH B . 
F 4 HOH   117 317 207  HOH   HOH B . 
F 4 HOH   118 318 118  HOH   HOH B . 
F 4 HOH   119 319 44   HOH   HOH B . 
F 4 HOH   120 320 28   HOH   HOH B . 
F 4 HOH   121 321 1126 HOH   HOH B . 
F 4 HOH   122 322 182  HOH   HOH B . 
F 4 HOH   123 323 1291 HOH   HOH B . 
F 4 HOH   124 324 1274 HOH   HOH B . 
F 4 HOH   125 325 341  HOH   HOH B . 
F 4 HOH   126 326 100  HOH   HOH B . 
F 4 HOH   127 327 177  HOH   HOH B . 
F 4 HOH   128 328 197  HOH   HOH B . 
F 4 HOH   129 329 161  HOH   HOH B . 
F 4 HOH   130 330 29   HOH   HOH B . 
F 4 HOH   131 331 334  HOH   HOH B . 
F 4 HOH   132 332 98   HOH   HOH B . 
F 4 HOH   133 333 141  HOH   HOH B . 
F 4 HOH   134 334 234  HOH   HOH B . 
F 4 HOH   135 335 717  HOH   HOH B . 
F 4 HOH   136 336 619  HOH   HOH B . 
F 4 HOH   137 337 445  HOH   HOH B . 
F 4 HOH   138 338 55   HOH   HOH B . 
F 4 HOH   139 339 960  HOH   HOH B . 
F 4 HOH   140 340 1294 HOH   HOH B . 
F 4 HOH   141 341 65   HOH   HOH B . 
F 4 HOH   142 342 339  HOH   HOH B . 
F 4 HOH   143 343 178  HOH   HOH B . 
F 4 HOH   144 344 1293 HOH   HOH B . 
F 4 HOH   145 345 362  HOH   HOH B . 
F 4 HOH   146 346 90   HOH   HOH B . 
F 4 HOH   147 347 463  HOH   HOH B . 
F 4 HOH   148 348 623  HOH   HOH B . 
F 4 HOH   149 349 191  HOH   HOH B . 
F 4 HOH   150 350 335  HOH   HOH B . 
F 4 HOH   151 351 1304 HOH   HOH B . 
F 4 HOH   152 352 1280 HOH   HOH B . 
F 4 HOH   153 353 304  HOH   HOH B . 
F 4 HOH   154 354 203  HOH   HOH B . 
F 4 HOH   155 355 87   HOH   HOH B . 
F 4 HOH   156 356 1046 HOH   HOH B . 
F 4 HOH   157 357 541  HOH   HOH B . 
F 4 HOH   158 358 290  HOH   HOH B . 
F 4 HOH   159 359 1077 HOH   HOH B . 
F 4 HOH   160 360 479  HOH   HOH B . 
F 4 HOH   161 361 389  HOH   HOH B . 
F 4 HOH   162 362 718  HOH   HOH B . 
F 4 HOH   163 363 283  HOH   HOH B . 
F 4 HOH   164 364 1072 HOH   HOH B . 
F 4 HOH   165 365 340  HOH   HOH B . 
F 4 HOH   166 366 1316 HOH   HOH B . 
F 4 HOH   167 367 898  HOH   HOH B . 
F 4 HOH   168 368 373  HOH   HOH B . 
F 4 HOH   169 369 667  HOH   HOH B . 
F 4 HOH   170 370 615  HOH   HOH B . 
F 4 HOH   171 371 291  HOH   HOH B . 
F 4 HOH   172 372 190  HOH   HOH B . 
F 4 HOH   173 373 1303 HOH   HOH B . 
F 4 HOH   174 374 431  HOH   HOH B . 
F 4 HOH   175 375 310  HOH   HOH B . 
F 4 HOH   176 376 149  HOH   HOH B . 
F 4 HOH   177 377 1173 HOH   HOH B . 
F 4 HOH   178 378 183  HOH   HOH B . 
F 4 HOH   179 379 1163 HOH   HOH B . 
F 4 HOH   180 380 418  HOH   HOH B . 
F 4 HOH   181 381 1311 HOH   HOH B . 
F 4 HOH   182 382 176  HOH   HOH B . 
F 4 HOH   183 383 1000 HOH   HOH B . 
F 4 HOH   184 384 424  HOH   HOH B . 
F 4 HOH   185 385 491  HOH   HOH B . 
F 4 HOH   186 386 470  HOH   HOH B . 
F 4 HOH   187 387 248  HOH   HOH B . 
F 4 HOH   188 388 265  HOH   HOH B . 
F 4 HOH   189 389 1298 HOH   HOH B . 
F 4 HOH   190 390 981  HOH   HOH B . 
F 4 HOH   191 391 360  HOH   HOH B . 
F 4 HOH   192 392 184  HOH   HOH B . 
F 4 HOH   193 393 410  HOH   HOH B . 
F 4 HOH   194 394 355  HOH   HOH B . 
F 4 HOH   195 395 274  HOH   HOH B . 
F 4 HOH   196 396 314  HOH   HOH B . 
F 4 HOH   197 397 566  HOH   HOH B . 
F 4 HOH   198 398 157  HOH   HOH B . 
F 4 HOH   199 399 792  HOH   HOH B . 
F 4 HOH   200 400 321  HOH   HOH B . 
F 4 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           7HEX 
_cell.length_a           88.870 
_cell.length_b           88.870 
_cell.length_c           39.571 
_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                         7HEX 
_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          7HEX 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_Matthews      2.15 
_exptl_crystal.density_percent_sol   42.86 
_exptl_crystal.density_meas          ? 
_exptl_crystal.description           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.pH              9.5 
_exptl_crystal_grow.temp            292 
_exptl_crystal_grow.pdbx_details    '100 mM CHES, 28% PEG 3000' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp_details    ? 
# 
_diffrn.id                     1 
_diffrn.crystal_id             1 
_diffrn.ambient_temp           100 
_diffrn.ambient_temp_details   ? 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               PIXEL 
_diffrn_detector.type                   'DECTRIS PILATUS3 6M' 
_diffrn_detector.pdbx_collection_date   2023-05-28 
_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                     7HEX 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             44.440 
_reflns.d_resolution_high            0.990 
_reflns.number_obs                   170428 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         99.400 
_reflns.pdbx_Rmerge_I_obs            0.045 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        14.900 
_reflns.B_iso_Wilson_estimate        12.020 
_reflns.pdbx_redundancy              6.200 
_reflns.pdbx_Rrim_I_all              0.049 
_reflns.pdbx_Rpim_I_all              0.020 
_reflns.pdbx_CC_half                 0.999 
_reflns.pdbx_netI_over_av_sigmaI     ? 
_reflns.pdbx_number_measured_all     1060518 
_reflns.pdbx_scaling_rejects         ? 
_reflns.pdbx_chi_squared             ? 
_reflns.Rmerge_F_all                 ? 
_reflns.Rmerge_F_obs                 ? 
_reflns.observed_criterion_F_max     ? 
_reflns.observed_criterion_F_min     ? 
_reflns.observed_criterion_I_max     ? 
_reflns.observed_criterion_I_min     ? 
_reflns.pdbx_d_res_high_opt          ? 
_reflns.pdbx_d_res_low_opt           ? 
_reflns.details                      ? 
# 
loop_
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_ordinal 
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.number_measured_obs 
_reflns_shell.number_measured_all 
_reflns_shell.number_unique_obs 
_reflns_shell.pdbx_rejects 
_reflns_shell.Rmerge_I_obs 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.pdbx_Rsym_value 
_reflns_shell.pdbx_chi_squared 
_reflns_shell.pdbx_redundancy 
_reflns_shell.percent_possible_obs 
_reflns_shell.pdbx_netI_over_sigmaI_obs 
_reflns_shell.number_possible 
_reflns_shell.number_unique_all 
_reflns_shell.Rmerge_F_all 
_reflns_shell.Rmerge_F_obs 
_reflns_shell.Rmerge_I_all 
_reflns_shell.meanI_over_sigI_all 
_reflns_shell.percent_possible_all 
_reflns_shell.pdbx_Rrim_I_all 
_reflns_shell.pdbx_Rpim_I_all 
_reflns_shell.pdbx_CC_half 
1 1 0.990 1.010  ? 29262 7629 ? 1.909 ? ? ? 3.800 ? 0.500  ? ? ? ? ? ? 91.400 2.206 1.077 0.338 
1 2 5.430 44.440 ? 7774  1133 ? 0.024 ? ? ? 6.900 ? 58.100 ? ? ? ? ? ? 99.800 0.026 0.010 0.999 
# 
_refine.entry_id                                 7HEX 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_d_res_high                            0.9900 
_refine.ls_d_res_low                             44.4400 
_refine.pdbx_ls_sigma_F                          1.330 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.ls_percent_reflns_obs                    99.2400 
_refine.ls_number_reflns_obs                     170150 
_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                          0.1476 
_refine.ls_R_factor_R_work                       0.1470 
_refine.ls_wR_factor_R_work                      ? 
_refine.ls_R_factor_R_free                       0.1602 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_percent_reflns_R_free                 4.8200 
_refine.ls_number_reflns_R_free                  8207 
_refine.ls_number_reflns_R_work                  161943 
_refine.ls_R_factor_R_free_error                 ? 
_refine.B_iso_mean                               19.4944 
_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                            0.1400 
_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                                58.650 
_refine.B_iso_min                                9.120 
_refine.pdbx_overall_phase_error                 19.0700 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_R_factor_R_free_error_details         ? 
# 
_refine_hist.cycle_id                         final 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.d_res_high                       0.9900 
_refine_hist.d_res_low                        44.4400 
_refine_hist.pdbx_number_atoms_ligand         53 
_refine_hist.number_atoms_solvent             433 
_refine_hist.number_atoms_total               3028 
_refine_hist.pdbx_number_residues_total       336 
_refine_hist.pdbx_B_iso_mean_ligand           22.31 
_refine_hist.pdbx_B_iso_mean_solvent          30.74 
_refine_hist.pdbx_number_atoms_protein        2542 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
# 
loop_
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.R_factor_R_free 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.pdbx_refine_id 
0.9900 1.0000  30 87.0000  4653 . 0.4612 0.4327 . 244 0.0000 4897 . 'X-RAY DIFFRACTION' 
1.0000 1.0100  30 94.0000  5145 . 0.4160 0.3671 . 266 0.0000 5411 . 'X-RAY DIFFRACTION' 
1.0100 1.0300  30 98.0000  5244 . 0.3715 0.3552 . 228 0.0000 5472 . 'X-RAY DIFFRACTION' 
1.0300 1.0400  30 100.0000 5469 . 0.3240 0.3427 . 278 0.0000 5747 . 'X-RAY DIFFRACTION' 
1.0400 1.0500  30 100.0000 5389 . 0.2898 0.3085 . 279 0.0000 5668 . 'X-RAY DIFFRACTION' 
1.0500 1.0700  30 100.0000 5352 . 0.2569 0.2682 . 338 0.0000 5690 . 'X-RAY DIFFRACTION' 
1.0700 1.0800  30 100.0000 5421 . 0.2576 0.2701 . 260 0.0000 5681 . 'X-RAY DIFFRACTION' 
1.0800 1.1000  30 100.0000 5424 . 0.2396 0.2631 . 271 0.0000 5695 . 'X-RAY DIFFRACTION' 
1.1000 1.1200  30 100.0000 5369 . 0.2115 0.2277 . 280 0.0000 5649 . 'X-RAY DIFFRACTION' 
1.1200 1.1300  30 100.0000 5469 . 0.1860 0.1834 . 248 0.0000 5717 . 'X-RAY DIFFRACTION' 
1.1300 1.1500  30 100.0000 5430 . 0.1739 0.1922 . 253 0.0000 5683 . 'X-RAY DIFFRACTION' 
1.1500 1.1700  30 100.0000 5389 . 0.1533 0.1690 . 282 0.0000 5671 . 'X-RAY DIFFRACTION' 
1.1700 1.2000  30 100.0000 5437 . 0.1393 0.1623 . 274 0.0000 5711 . 'X-RAY DIFFRACTION' 
1.2000 1.2200  30 100.0000 5374 . 0.1242 0.1531 . 303 0.0000 5677 . 'X-RAY DIFFRACTION' 
1.2200 1.2500  30 100.0000 5444 . 0.1233 0.1421 . 254 0.0000 5698 . 'X-RAY DIFFRACTION' 
1.2500 1.2800  30 100.0000 5458 . 0.1255 0.1420 . 251 0.0000 5709 . 'X-RAY DIFFRACTION' 
1.2800 1.3100  30 100.0000 5427 . 0.1247 0.1503 . 277 0.0000 5704 . 'X-RAY DIFFRACTION' 
1.3100 1.3400  30 100.0000 5394 . 0.1311 0.1443 . 294 0.0000 5688 . 'X-RAY DIFFRACTION' 
1.3400 1.3800  30 100.0000 5422 . 0.1321 0.1544 . 286 0.0000 5708 . 'X-RAY DIFFRACTION' 
1.3800 1.4300  30 100.0000 5467 . 0.1234 0.1578 . 261 0.0000 5728 . 'X-RAY DIFFRACTION' 
1.4300 1.4800  30 100.0000 5422 . 0.1199 0.1395 . 272 0.0000 5694 . 'X-RAY DIFFRACTION' 
1.4800 1.5400  30 100.0000 5419 . 0.1138 0.1206 . 268 0.0000 5687 . 'X-RAY DIFFRACTION' 
1.5400 1.6100  30 100.0000 5447 . 0.1154 0.1323 . 293 0.0000 5740 . 'X-RAY DIFFRACTION' 
1.6100 1.6900  30 100.0000 5444 . 0.1191 0.1385 . 258 0.0000 5702 . 'X-RAY DIFFRACTION' 
1.6900 1.8000  30 100.0000 5511 . 0.1292 0.1421 . 261 0.0000 5772 . 'X-RAY DIFFRACTION' 
1.8000 1.9400  30 100.0000 5410 . 0.1307 0.1350 . 300 0.0000 5710 . 'X-RAY DIFFRACTION' 
1.9400 2.1300  30 100.0000 5489 . 0.1362 0.1446 . 275 0.0000 5764 . 'X-RAY DIFFRACTION' 
2.1300 2.4400  30 100.0000 5447 . 0.1362 0.1439 . 299 0.0000 5746 . 'X-RAY DIFFRACTION' 
2.4400 3.0800  30 100.0000 5509 . 0.1473 0.1613 . 286 0.0000 5795 . 'X-RAY DIFFRACTION' 
3.0800 44.4400 30 100.0000 5668 . 0.1501 0.1665 . 268 0.0000 5936 . 'X-RAY DIFFRACTION' 
# 
_struct.entry_id                  7HEX 
_struct.title                     
'PanDDA analysis group deposition -- Crystal structure of SARS-CoV-2 NSP3 macrodomain in complex with AVI-0003733' 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_details        ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HEX 
_struct_keywords.pdbx_keywords   'VIRAL PROTEIN, Hydrolase' 
_struct_keywords.text            'Macrodomain, ADP-ribose, SARS-CoV-2, fragment-based drug discovery, VIRAL PROTEIN, Hydrolase' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 4 ? 
F N N 4 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    R1AB_SARS2 
_struct_ref.pdbx_db_accession          P0DTD1 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;VNSFSGYLKLTDNVYIKNADIVEEAKKVKPTVVVNAANVYLKHGGGVAGALNKATNNAMQVESDDYIATNGPLKVGGSCV
LSGHNLAKHCLHVVGPNVNKGEDIQLLKSAYENFNQHEVLLAPLLSAGIFGADPIHSLRVCVDTVRTNVYLAVFDKNLYD
KLVSSFL
;
_struct_ref.pdbx_align_begin           1025 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 7HEX A 3 ? 169 ? P0DTD1 1025 ? 1191 ? 3 169 
2 1 7HEX 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 7HEX SER A 1 ? UNP P0DTD1 ? ? 'expression tag' 1 1 
1 7HEX MET A 2 ? UNP P0DTD1 ? ? 'expression tag' 2 2 
2 7HEX SER B 1 ? UNP P0DTD1 ? ? 'expression tag' 1 3 
2 7HEX MET B 2 ? UNP P0DTD1 ? ? 'expression tag' 2 4 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C,D,E 
2 1 B,F     
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 ASP A 22  ? LYS A 31  ? ASP A 22  LYS A 31  1 ? 10 
HELX_P HELX_P2  AA2 GLY A 47  ? THR A 57  ? GLY A 47  THR A 57  1 ? 11 
HELX_P HELX_P3  AA3 ASN A 59  ? GLY A 73  ? ASN A 59  GLY A 73  1 ? 15 
HELX_P HELX_P4  AA4 ASN A 99  ? GLY A 103 ? ASN A 99  GLY A 103 5 ? 5  
HELX_P HELX_P5  AA5 GLN A 107 ? ASN A 115 ? GLN A 107 ASN A 115 1 ? 9  
HELX_P HELX_P6  AA6 PHE A 116 ? HIS A 119 ? PHE A 116 HIS A 119 5 ? 4  
HELX_P HELX_P7  AA7 ALA A 129 ? GLY A 133 ? ALA A 129 GLY A 133 5 ? 5  
HELX_P HELX_P8  AA8 ASP A 135 ? VAL A 147 ? ASP A 135 VAL A 147 1 ? 13 
HELX_P HELX_P9  AA9 ASP A 157 ? SER A 167 ? ASP A 157 SER A 167 1 ? 11 
HELX_P HELX_P10 AB1 ASP B 22  ? LYS B 31  ? ASP B 22  LYS B 31  1 ? 10 
HELX_P HELX_P11 AB2 GLY B 47  ? THR B 57  ? GLY B 47  THR B 57  1 ? 11 
HELX_P HELX_P12 AB3 ASN B 59  ? GLY B 73  ? ASN B 59  GLY B 73  1 ? 15 
HELX_P HELX_P13 AB4 ASN B 99  ? GLY B 103 ? ASN B 99  GLY B 103 5 ? 5  
HELX_P HELX_P14 AB5 ASP B 105 ? GLN B 107 ? ASP B 105 GLN B 107 5 ? 3  
HELX_P HELX_P15 AB6 LEU B 108 ? ASN B 115 ? LEU B 108 ASN B 115 1 ? 8  
HELX_P HELX_P16 AB7 PHE B 116 ? HIS B 119 ? PHE B 116 HIS B 119 5 ? 4  
HELX_P HELX_P17 AB8 ALA B 129 ? GLY B 133 ? ALA B 129 GLY B 133 5 ? 5  
HELX_P HELX_P18 AB9 ASP B 135 ? VAL B 147 ? ASP B 135 VAL B 147 1 ? 13 
HELX_P HELX_P19 AC1 ASP B 157 ? LEU B 169 ? ASP B 157 LEU B 169 1 ? 13 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
_struct_mon_prot_cis.pdbx_id                1 
_struct_mon_prot_cis.label_comp_id          PHE 
_struct_mon_prot_cis.label_seq_id           156 
_struct_mon_prot_cis.label_asym_id          A 
_struct_mon_prot_cis.label_alt_id           . 
_struct_mon_prot_cis.pdbx_PDB_ins_code      ? 
_struct_mon_prot_cis.auth_comp_id           PHE 
_struct_mon_prot_cis.auth_seq_id            156 
_struct_mon_prot_cis.auth_asym_id           A 
_struct_mon_prot_cis.pdbx_label_comp_id_2   ASP 
_struct_mon_prot_cis.pdbx_label_seq_id_2    157 
_struct_mon_prot_cis.pdbx_label_asym_id_2   A 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2    ? 
_struct_mon_prot_cis.pdbx_auth_comp_id_2    ASP 
_struct_mon_prot_cis.pdbx_auth_seq_id_2     157 
_struct_mon_prot_cis.pdbx_auth_asym_id_2    A 
_struct_mon_prot_cis.pdbx_PDB_model_num     1 
_struct_mon_prot_cis.pdbx_omega_angle       6.62 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 4 ? 
AA2 ? 3 ? 
AA3 ? 4 ? 
AA4 ? 3 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? parallel      
AA1 3 4 ? parallel      
AA2 1 2 ? parallel      
AA2 2 3 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? parallel      
AA3 3 4 ? parallel      
AA4 1 2 ? parallel      
AA4 2 3 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 LEU A 10  ? LYS A 11  ? LEU A 10  LYS A 11  
AA1 2 VAL A 16  ? ASN A 20  ? VAL A 16  ASN A 20  
AA1 3 ASN A 150 ? VAL A 155 ? ASN A 150 VAL A 155 
AA1 4 VAL A 121 ? ALA A 124 ? VAL A 121 ALA A 124 
AA2 1 VAL A 34  ? ALA A 38  ? VAL A 34  ALA A 38  
AA2 2 HIS A 91  ? VAL A 95  ? HIS A 91  VAL A 95  
AA2 3 SER A 80  ? SER A 84  ? SER A 80  SER A 84  
AA3 1 LEU B 10  ? LYS B 11  ? LEU B 10  LYS B 11  
AA3 2 VAL B 16  ? ASN B 20  ? VAL B 16  ASN B 20  
AA3 3 ASN B 150 ? VAL B 155 ? ASN B 150 VAL B 155 
AA3 4 VAL B 121 ? ALA B 124 ? VAL B 121 ALA B 124 
AA4 1 VAL B 34  ? ALA B 38  ? VAL B 34  ALA B 38  
AA4 2 HIS B 91  ? VAL B 95  ? HIS B 91  VAL B 95  
AA4 3 SER B 80  ? SER B 84  ? SER B 80  SER B 84  
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N LEU A 10  ? N LEU A 10  O ILE A 18  ? O ILE A 18  
AA1 2 3 N LYS A 19  ? N LYS A 19  O VAL A 155 ? O VAL A 155 
AA1 3 4 O TYR A 152 ? O TYR A 152 N LEU A 122 ? N LEU A 122 
AA2 1 2 N ASN A 37  ? N ASN A 37  O VAL A 95  ? O VAL A 95  
AA2 2 3 O CYS A 92  ? O CYS A 92  N LEU A 83  ? N LEU A 83  
AA3 1 2 N LEU B 10  ? N LEU B 10  O ILE B 18  ? O ILE B 18  
AA3 2 3 N TYR B 17  ? N TYR B 17  O LEU B 153 ? O LEU B 153 
AA3 3 4 O TYR B 152 ? O TYR B 152 N ALA B 124 ? N ALA B 124 
AA4 1 2 N ASN B 37  ? N ASN B 37  O VAL B 95  ? O VAL B 95  
AA4 2 3 O CYS B 92  ? O CYS B 92  N LEU B 83  ? N LEU B 83  
# 
_pdbx_entry_details.entry_id                   7HEX 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
_pdbx_validate_close_contact.id               1 
_pdbx_validate_close_contact.PDB_model_num    1 
_pdbx_validate_close_contact.auth_atom_id_1   HD1 
_pdbx_validate_close_contact.auth_asym_id_1   A 
_pdbx_validate_close_contact.auth_comp_id_1   HIS 
_pdbx_validate_close_contact.auth_seq_id_1    91 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   ? 
_pdbx_validate_close_contact.auth_atom_id_2   O 
_pdbx_validate_close_contact.auth_asym_id_2   A 
_pdbx_validate_close_contact.auth_comp_id_2   HOH 
_pdbx_validate_close_contact.auth_seq_id_2    401 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             1.56 
# 
loop_
_pdbx_validate_symm_contact.id 
_pdbx_validate_symm_contact.PDB_model_num 
_pdbx_validate_symm_contact.auth_atom_id_1 
_pdbx_validate_symm_contact.auth_asym_id_1 
_pdbx_validate_symm_contact.auth_comp_id_1 
_pdbx_validate_symm_contact.auth_seq_id_1 
_pdbx_validate_symm_contact.PDB_ins_code_1 
_pdbx_validate_symm_contact.label_alt_id_1 
_pdbx_validate_symm_contact.site_symmetry_1 
_pdbx_validate_symm_contact.auth_atom_id_2 
_pdbx_validate_symm_contact.auth_asym_id_2 
_pdbx_validate_symm_contact.auth_comp_id_2 
_pdbx_validate_symm_contact.auth_seq_id_2 
_pdbx_validate_symm_contact.PDB_ins_code_2 
_pdbx_validate_symm_contact.label_alt_id_2 
_pdbx_validate_symm_contact.site_symmetry_2 
_pdbx_validate_symm_contact.dist 
1 1 O  A ASP 66 ? ? 1_555 HG  B SER 1  ? B 2_655 1.59 
2 1 HH A TYR 42 ? B 1_555 OD1 B ASP 67 ? ? 2_654 1.60 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 HIS A 86  ? ? 55.48   -133.38 
2 1 ASP A 157 ? B -134.13 -149.42 
3 1 HIS B 86  ? ? 57.45   -128.01 
# 
_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 631 ? 5.91 . 
2 1 O ? A HOH 632 ? 7.59 . 
3 1 O ? B HOH 401 ? 6.37 . 
# 
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 
A1BAG N2   N Y N 1   
A1BAG C3   C N N 2   
A1BAG C6   C N R 3   
A1BAG C9   C N S 4   
A1BAG C12  C Y N 5   
A1BAG C14  C Y N 6   
A1BAG C1   C N N 7   
A1BAG C10  C N N 8   
A1BAG C11  C Y N 9   
A1BAG C13  C Y N 10  
A1BAG C15  C Y N 11  
A1BAG C16  C Y N 12  
A1BAG C2   C Y N 13  
A1BAG C4   C Y N 14  
A1BAG C5   C Y N 15  
A1BAG C7   C N N 16  
A1BAG C8   C N N 17  
A1BAG N1   N Y N 18  
A1BAG N3   N N N 19  
A1BAG N4   N Y N 20  
A1BAG N5   N Y N 21  
A1BAG N6   N Y N 22  
A1BAG O1   O N N 23  
A1BAG H8   H N N 24  
A1BAG H6   H N N 25  
A1BAG H7   H N N 26  
A1BAG H1   H N N 27  
A1BAG H2   H N N 28  
A1BAG H17  H N N 29  
A1BAG H4   H N N 30  
A1BAG H5   H N N 31  
A1BAG H3   H N N 32  
A1BAG H15  H N N 33  
A1BAG H14  H N N 34  
A1BAG H18  H N N 35  
A1BAG H19  H N N 36  
A1BAG H9   H N N 37  
A1BAG H10  H N N 38  
A1BAG H11  H N N 39  
A1BAG H12  H N N 40  
A1BAG H13  H N N 41  
A1BAG H20  H N N 42  
A1BAG H16  H N N 43  
ALA   N    N N N 44  
ALA   CA   C N S 45  
ALA   C    C N N 46  
ALA   O    O N N 47  
ALA   CB   C N N 48  
ALA   OXT  O N N 49  
ALA   H    H N N 50  
ALA   H2   H N N 51  
ALA   HA   H N N 52  
ALA   HB1  H N N 53  
ALA   HB2  H N N 54  
ALA   HB3  H N N 55  
ALA   HXT  H N N 56  
ARG   N    N N N 57  
ARG   CA   C N S 58  
ARG   C    C N N 59  
ARG   O    O N N 60  
ARG   CB   C N N 61  
ARG   CG   C N N 62  
ARG   CD   C N N 63  
ARG   NE   N N N 64  
ARG   CZ   C N N 65  
ARG   NH1  N N N 66  
ARG   NH2  N N N 67  
ARG   OXT  O N N 68  
ARG   H    H N N 69  
ARG   H2   H N N 70  
ARG   HA   H N N 71  
ARG   HB2  H N N 72  
ARG   HB3  H N N 73  
ARG   HG2  H N N 74  
ARG   HG3  H N N 75  
ARG   HD2  H N N 76  
ARG   HD3  H N N 77  
ARG   HE   H N N 78  
ARG   HH11 H N N 79  
ARG   HH12 H N N 80  
ARG   HH21 H N N 81  
ARG   HH22 H N N 82  
ARG   HXT  H N N 83  
ASN   N    N N N 84  
ASN   CA   C N S 85  
ASN   C    C N N 86  
ASN   O    O N N 87  
ASN   CB   C N N 88  
ASN   CG   C N N 89  
ASN   OD1  O N N 90  
ASN   ND2  N N N 91  
ASN   OXT  O N N 92  
ASN   H    H N N 93  
ASN   H2   H N N 94  
ASN   HA   H N N 95  
ASN   HB2  H N N 96  
ASN   HB3  H N N 97  
ASN   HD21 H N N 98  
ASN   HD22 H N N 99  
ASN   HXT  H N N 100 
ASP   N    N N N 101 
ASP   CA   C N S 102 
ASP   C    C N N 103 
ASP   O    O N N 104 
ASP   CB   C N N 105 
ASP   CG   C N N 106 
ASP   OD1  O N N 107 
ASP   OD2  O N N 108 
ASP   OXT  O N N 109 
ASP   H    H N N 110 
ASP   H2   H N N 111 
ASP   HA   H N N 112 
ASP   HB2  H N N 113 
ASP   HB3  H N N 114 
ASP   HD2  H N N 115 
ASP   HXT  H N N 116 
CYS   N    N N N 117 
CYS   CA   C N R 118 
CYS   C    C N N 119 
CYS   O    O N N 120 
CYS   CB   C N N 121 
CYS   SG   S N N 122 
CYS   OXT  O N N 123 
CYS   H    H N N 124 
CYS   H2   H N N 125 
CYS   HA   H N N 126 
CYS   HB2  H N N 127 
CYS   HB3  H N N 128 
CYS   HG   H N N 129 
CYS   HXT  H N N 130 
DMS   S    S N N 131 
DMS   O    O N N 132 
DMS   C1   C N N 133 
DMS   C2   C N N 134 
DMS   H11  H N N 135 
DMS   H12  H N N 136 
DMS   H13  H N N 137 
DMS   H21  H N N 138 
DMS   H22  H N N 139 
DMS   H23  H N N 140 
GLN   N    N N N 141 
GLN   CA   C N S 142 
GLN   C    C N N 143 
GLN   O    O N N 144 
GLN   CB   C N N 145 
GLN   CG   C N N 146 
GLN   CD   C N N 147 
GLN   OE1  O N N 148 
GLN   NE2  N N N 149 
GLN   OXT  O N N 150 
GLN   H    H N N 151 
GLN   H2   H N N 152 
GLN   HA   H N N 153 
GLN   HB2  H N N 154 
GLN   HB3  H N N 155 
GLN   HG2  H N N 156 
GLN   HG3  H N N 157 
GLN   HE21 H N N 158 
GLN   HE22 H N N 159 
GLN   HXT  H N N 160 
GLU   N    N N N 161 
GLU   CA   C N S 162 
GLU   C    C N N 163 
GLU   O    O N N 164 
GLU   CB   C N N 165 
GLU   CG   C N N 166 
GLU   CD   C N N 167 
GLU   OE1  O N N 168 
GLU   OE2  O N N 169 
GLU   OXT  O N N 170 
GLU   H    H N N 171 
GLU   H2   H N N 172 
GLU   HA   H N N 173 
GLU   HB2  H N N 174 
GLU   HB3  H N N 175 
GLU   HG2  H N N 176 
GLU   HG3  H N N 177 
GLU   HE2  H N N 178 
GLU   HXT  H N N 179 
GLY   N    N N N 180 
GLY   CA   C N N 181 
GLY   C    C N N 182 
GLY   O    O N N 183 
GLY   OXT  O N N 184 
GLY   H    H N N 185 
GLY   H2   H N N 186 
GLY   HA2  H N N 187 
GLY   HA3  H N N 188 
GLY   HXT  H N N 189 
HIS   N    N N N 190 
HIS   CA   C N S 191 
HIS   C    C N N 192 
HIS   O    O N N 193 
HIS   CB   C N N 194 
HIS   CG   C Y N 195 
HIS   ND1  N Y N 196 
HIS   CD2  C Y N 197 
HIS   CE1  C Y N 198 
HIS   NE2  N Y N 199 
HIS   OXT  O N N 200 
HIS   H    H N N 201 
HIS   H2   H N N 202 
HIS   HA   H N N 203 
HIS   HB2  H N N 204 
HIS   HB3  H N N 205 
HIS   HD1  H N N 206 
HIS   HD2  H N N 207 
HIS   HE1  H N N 208 
HIS   HE2  H N N 209 
HIS   HXT  H N N 210 
HOH   O    O N N 211 
HOH   H1   H N N 212 
HOH   H2   H N N 213 
ILE   N    N N N 214 
ILE   CA   C N S 215 
ILE   C    C N N 216 
ILE   O    O N N 217 
ILE   CB   C N S 218 
ILE   CG1  C N N 219 
ILE   CG2  C N N 220 
ILE   CD1  C N N 221 
ILE   OXT  O N N 222 
ILE   H    H N N 223 
ILE   H2   H N N 224 
ILE   HA   H N N 225 
ILE   HB   H N N 226 
ILE   HG12 H N N 227 
ILE   HG13 H N N 228 
ILE   HG21 H N N 229 
ILE   HG22 H N N 230 
ILE   HG23 H N N 231 
ILE   HD11 H N N 232 
ILE   HD12 H N N 233 
ILE   HD13 H N N 234 
ILE   HXT  H N N 235 
LEU   N    N N N 236 
LEU   CA   C N S 237 
LEU   C    C N N 238 
LEU   O    O N N 239 
LEU   CB   C N N 240 
LEU   CG   C N N 241 
LEU   CD1  C N N 242 
LEU   CD2  C N N 243 
LEU   OXT  O N N 244 
LEU   H    H N N 245 
LEU   H2   H N N 246 
LEU   HA   H N N 247 
LEU   HB2  H N N 248 
LEU   HB3  H N N 249 
LEU   HG   H N N 250 
LEU   HD11 H N N 251 
LEU   HD12 H N N 252 
LEU   HD13 H N N 253 
LEU   HD21 H N N 254 
LEU   HD22 H N N 255 
LEU   HD23 H N N 256 
LEU   HXT  H N N 257 
LYS   N    N N N 258 
LYS   CA   C N S 259 
LYS   C    C N N 260 
LYS   O    O N N 261 
LYS   CB   C N N 262 
LYS   CG   C N N 263 
LYS   CD   C N N 264 
LYS   CE   C N N 265 
LYS   NZ   N N N 266 
LYS   OXT  O N N 267 
LYS   H    H N N 268 
LYS   H2   H N N 269 
LYS   HA   H N N 270 
LYS   HB2  H N N 271 
LYS   HB3  H N N 272 
LYS   HG2  H N N 273 
LYS   HG3  H N N 274 
LYS   HD2  H N N 275 
LYS   HD3  H N N 276 
LYS   HE2  H N N 277 
LYS   HE3  H N N 278 
LYS   HZ1  H N N 279 
LYS   HZ2  H N N 280 
LYS   HZ3  H N N 281 
LYS   HXT  H N N 282 
MET   N    N N N 283 
MET   CA   C N S 284 
MET   C    C N N 285 
MET   O    O N N 286 
MET   CB   C N N 287 
MET   CG   C N N 288 
MET   SD   S N N 289 
MET   CE   C N N 290 
MET   OXT  O N N 291 
MET   H    H N N 292 
MET   H2   H N N 293 
MET   HA   H N N 294 
MET   HB2  H N N 295 
MET   HB3  H N N 296 
MET   HG2  H N N 297 
MET   HG3  H N N 298 
MET   HE1  H N N 299 
MET   HE2  H N N 300 
MET   HE3  H N N 301 
MET   HXT  H N N 302 
PHE   N    N N N 303 
PHE   CA   C N S 304 
PHE   C    C N N 305 
PHE   O    O N N 306 
PHE   CB   C N N 307 
PHE   CG   C Y N 308 
PHE   CD1  C Y N 309 
PHE   CD2  C Y N 310 
PHE   CE1  C Y N 311 
PHE   CE2  C Y N 312 
PHE   CZ   C Y N 313 
PHE   OXT  O N N 314 
PHE   H    H N N 315 
PHE   H2   H N N 316 
PHE   HA   H N N 317 
PHE   HB2  H N N 318 
PHE   HB3  H N N 319 
PHE   HD1  H N N 320 
PHE   HD2  H N N 321 
PHE   HE1  H N N 322 
PHE   HE2  H N N 323 
PHE   HZ   H N N 324 
PHE   HXT  H N N 325 
PRO   N    N N N 326 
PRO   CA   C N S 327 
PRO   C    C N N 328 
PRO   O    O N N 329 
PRO   CB   C N N 330 
PRO   CG   C N N 331 
PRO   CD   C N N 332 
PRO   OXT  O N N 333 
PRO   H    H N N 334 
PRO   HA   H N N 335 
PRO   HB2  H N N 336 
PRO   HB3  H N N 337 
PRO   HG2  H N N 338 
PRO   HG3  H N N 339 
PRO   HD2  H N N 340 
PRO   HD3  H N N 341 
PRO   HXT  H N N 342 
SER   N    N N N 343 
SER   CA   C N S 344 
SER   C    C N N 345 
SER   O    O N N 346 
SER   CB   C N N 347 
SER   OG   O N N 348 
SER   OXT  O N N 349 
SER   H    H N N 350 
SER   H2   H N N 351 
SER   HA   H N N 352 
SER   HB2  H N N 353 
SER   HB3  H N N 354 
SER   HG   H N N 355 
SER   HXT  H N N 356 
THR   N    N N N 357 
THR   CA   C N S 358 
THR   C    C N N 359 
THR   O    O N N 360 
THR   CB   C N R 361 
THR   OG1  O N N 362 
THR   CG2  C N N 363 
THR   OXT  O N N 364 
THR   H    H N N 365 
THR   H2   H N N 366 
THR   HA   H N N 367 
THR   HB   H N N 368 
THR   HG1  H N N 369 
THR   HG21 H N N 370 
THR   HG22 H N N 371 
THR   HG23 H N N 372 
THR   HXT  H N N 373 
TYR   N    N N N 374 
TYR   CA   C N S 375 
TYR   C    C N N 376 
TYR   O    O N N 377 
TYR   CB   C N N 378 
TYR   CG   C Y N 379 
TYR   CD1  C Y N 380 
TYR   CD2  C Y N 381 
TYR   CE1  C Y N 382 
TYR   CE2  C Y N 383 
TYR   CZ   C Y N 384 
TYR   OH   O N N 385 
TYR   OXT  O N N 386 
TYR   H    H N N 387 
TYR   H2   H N N 388 
TYR   HA   H N N 389 
TYR   HB2  H N N 390 
TYR   HB3  H N N 391 
TYR   HD1  H N N 392 
TYR   HD2  H N N 393 
TYR   HE1  H N N 394 
TYR   HE2  H N N 395 
TYR   HH   H N N 396 
TYR   HXT  H N N 397 
VAL   N    N N N 398 
VAL   CA   C N S 399 
VAL   C    C N N 400 
VAL   O    O N N 401 
VAL   CB   C N N 402 
VAL   CG1  C N N 403 
VAL   CG2  C N N 404 
VAL   OXT  O N N 405 
VAL   H    H N N 406 
VAL   H2   H N N 407 
VAL   HA   H N N 408 
VAL   HB   H N N 409 
VAL   HG11 H N N 410 
VAL   HG12 H N N 411 
VAL   HG13 H N N 412 
VAL   HG21 H N N 413 
VAL   HG22 H N N 414 
VAL   HG23 H N N 415 
VAL   HXT  H N N 416 
# 
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 
A1BAG C3  N2   sing N N 1   
A1BAG N1  N2   sing Y N 2   
A1BAG N1  C2   doub Y N 3   
A1BAG N2  C4   sing Y N 4   
A1BAG C1  C2   sing N N 5   
A1BAG C2  C5   sing Y N 6   
A1BAG C4  C5   doub Y N 7   
A1BAG C7  C8   sing N N 8   
A1BAG C7  C6   sing N N 9   
A1BAG C5  C6   sing N N 10  
A1BAG C8  C9   sing N N 11  
A1BAG C6  N3   sing N N 12  
A1BAG C10 C9   sing N N 13  
A1BAG C10 O1   sing N N 14  
A1BAG C9  N3   sing N N 15  
A1BAG N3  C11  sing N N 16  
A1BAG C15 C14  sing Y N 17  
A1BAG C15 C16  doub Y N 18  
A1BAG C11 C14  doub Y N 19  
A1BAG C11 N4   sing Y N 20  
A1BAG C14 C13  sing Y N 21  
A1BAG N4  C12  doub Y N 22  
A1BAG C16 N6   sing Y N 23  
A1BAG C13 N6   sing Y N 24  
A1BAG C13 N5   doub Y N 25  
A1BAG C12 N5   sing Y N 26  
A1BAG C3  H8   sing N N 27  
A1BAG C3  H6   sing N N 28  
A1BAG C3  H7   sing N N 29  
A1BAG C6  H1   sing N N 30  
A1BAG C9  H2   sing N N 31  
A1BAG C12 H17  sing N N 32  
A1BAG C1  H4   sing N N 33  
A1BAG C1  H5   sing N N 34  
A1BAG C1  H3   sing N N 35  
A1BAG C10 H15  sing N N 36  
A1BAG C10 H14  sing N N 37  
A1BAG C15 H18  sing N N 38  
A1BAG C16 H19  sing N N 39  
A1BAG C4  H9   sing N N 40  
A1BAG C7  H10  sing N N 41  
A1BAG C7  H11  sing N N 42  
A1BAG C8  H12  sing N N 43  
A1BAG C8  H13  sing N N 44  
A1BAG N6  H20  sing N N 45  
A1BAG O1  H16  sing N N 46  
ALA   N   CA   sing N N 47  
ALA   N   H    sing N N 48  
ALA   N   H2   sing N N 49  
ALA   CA  C    sing N N 50  
ALA   CA  CB   sing N N 51  
ALA   CA  HA   sing N N 52  
ALA   C   O    doub N N 53  
ALA   C   OXT  sing N N 54  
ALA   CB  HB1  sing N N 55  
ALA   CB  HB2  sing N N 56  
ALA   CB  HB3  sing N N 57  
ALA   OXT HXT  sing N N 58  
ARG   N   CA   sing N N 59  
ARG   N   H    sing N N 60  
ARG   N   H2   sing N N 61  
ARG   CA  C    sing N N 62  
ARG   CA  CB   sing N N 63  
ARG   CA  HA   sing N N 64  
ARG   C   O    doub N N 65  
ARG   C   OXT  sing N N 66  
ARG   CB  CG   sing N N 67  
ARG   CB  HB2  sing N N 68  
ARG   CB  HB3  sing N N 69  
ARG   CG  CD   sing N N 70  
ARG   CG  HG2  sing N N 71  
ARG   CG  HG3  sing N N 72  
ARG   CD  NE   sing N N 73  
ARG   CD  HD2  sing N N 74  
ARG   CD  HD3  sing N N 75  
ARG   NE  CZ   sing N N 76  
ARG   NE  HE   sing N N 77  
ARG   CZ  NH1  sing N N 78  
ARG   CZ  NH2  doub N N 79  
ARG   NH1 HH11 sing N N 80  
ARG   NH1 HH12 sing N N 81  
ARG   NH2 HH21 sing N N 82  
ARG   NH2 HH22 sing N N 83  
ARG   OXT HXT  sing N N 84  
ASN   N   CA   sing N N 85  
ASN   N   H    sing N N 86  
ASN   N   H2   sing N N 87  
ASN   CA  C    sing N N 88  
ASN   CA  CB   sing N N 89  
ASN   CA  HA   sing N N 90  
ASN   C   O    doub N N 91  
ASN   C   OXT  sing N N 92  
ASN   CB  CG   sing N N 93  
ASN   CB  HB2  sing N N 94  
ASN   CB  HB3  sing N N 95  
ASN   CG  OD1  doub N N 96  
ASN   CG  ND2  sing N N 97  
ASN   ND2 HD21 sing N N 98  
ASN   ND2 HD22 sing N N 99  
ASN   OXT HXT  sing N N 100 
ASP   N   CA   sing N N 101 
ASP   N   H    sing N N 102 
ASP   N   H2   sing N N 103 
ASP   CA  C    sing N N 104 
ASP   CA  CB   sing N N 105 
ASP   CA  HA   sing N N 106 
ASP   C   O    doub N N 107 
ASP   C   OXT  sing N N 108 
ASP   CB  CG   sing N N 109 
ASP   CB  HB2  sing N N 110 
ASP   CB  HB3  sing N N 111 
ASP   CG  OD1  doub N N 112 
ASP   CG  OD2  sing N N 113 
ASP   OD2 HD2  sing N N 114 
ASP   OXT HXT  sing N N 115 
CYS   N   CA   sing N N 116 
CYS   N   H    sing N N 117 
CYS   N   H2   sing N N 118 
CYS   CA  C    sing N N 119 
CYS   CA  CB   sing N N 120 
CYS   CA  HA   sing N N 121 
CYS   C   O    doub N N 122 
CYS   C   OXT  sing N N 123 
CYS   CB  SG   sing N N 124 
CYS   CB  HB2  sing N N 125 
CYS   CB  HB3  sing N N 126 
CYS   SG  HG   sing N N 127 
CYS   OXT HXT  sing N N 128 
DMS   S   O    doub N N 129 
DMS   S   C1   sing N N 130 
DMS   S   C2   sing N N 131 
DMS   C1  H11  sing N N 132 
DMS   C1  H12  sing N N 133 
DMS   C1  H13  sing N N 134 
DMS   C2  H21  sing N N 135 
DMS   C2  H22  sing N N 136 
DMS   C2  H23  sing N N 137 
GLN   N   CA   sing N N 138 
GLN   N   H    sing N N 139 
GLN   N   H2   sing N N 140 
GLN   CA  C    sing N N 141 
GLN   CA  CB   sing N N 142 
GLN   CA  HA   sing N N 143 
GLN   C   O    doub N N 144 
GLN   C   OXT  sing N N 145 
GLN   CB  CG   sing N N 146 
GLN   CB  HB2  sing N N 147 
GLN   CB  HB3  sing N N 148 
GLN   CG  CD   sing N N 149 
GLN   CG  HG2  sing N N 150 
GLN   CG  HG3  sing N N 151 
GLN   CD  OE1  doub N N 152 
GLN   CD  NE2  sing N N 153 
GLN   NE2 HE21 sing N N 154 
GLN   NE2 HE22 sing N N 155 
GLN   OXT HXT  sing N N 156 
GLU   N   CA   sing N N 157 
GLU   N   H    sing N N 158 
GLU   N   H2   sing N N 159 
GLU   CA  C    sing N N 160 
GLU   CA  CB   sing N N 161 
GLU   CA  HA   sing N N 162 
GLU   C   O    doub N N 163 
GLU   C   OXT  sing N N 164 
GLU   CB  CG   sing N N 165 
GLU   CB  HB2  sing N N 166 
GLU   CB  HB3  sing N N 167 
GLU   CG  CD   sing N N 168 
GLU   CG  HG2  sing N N 169 
GLU   CG  HG3  sing N N 170 
GLU   CD  OE1  doub N N 171 
GLU   CD  OE2  sing N N 172 
GLU   OE2 HE2  sing N N 173 
GLU   OXT HXT  sing N N 174 
GLY   N   CA   sing N N 175 
GLY   N   H    sing N N 176 
GLY   N   H2   sing N N 177 
GLY   CA  C    sing N N 178 
GLY   CA  HA2  sing N N 179 
GLY   CA  HA3  sing N N 180 
GLY   C   O    doub N N 181 
GLY   C   OXT  sing N N 182 
GLY   OXT HXT  sing N N 183 
HIS   N   CA   sing N N 184 
HIS   N   H    sing N N 185 
HIS   N   H2   sing N N 186 
HIS   CA  C    sing N N 187 
HIS   CA  CB   sing N N 188 
HIS   CA  HA   sing N N 189 
HIS   C   O    doub N N 190 
HIS   C   OXT  sing N N 191 
HIS   CB  CG   sing N N 192 
HIS   CB  HB2  sing N N 193 
HIS   CB  HB3  sing N N 194 
HIS   CG  ND1  sing Y N 195 
HIS   CG  CD2  doub Y N 196 
HIS   ND1 CE1  doub Y N 197 
HIS   ND1 HD1  sing N N 198 
HIS   CD2 NE2  sing Y N 199 
HIS   CD2 HD2  sing N N 200 
HIS   CE1 NE2  sing Y N 201 
HIS   CE1 HE1  sing N N 202 
HIS   NE2 HE2  sing N N 203 
HIS   OXT HXT  sing N N 204 
HOH   O   H1   sing N N 205 
HOH   O   H2   sing N N 206 
ILE   N   CA   sing N N 207 
ILE   N   H    sing N N 208 
ILE   N   H2   sing N N 209 
ILE   CA  C    sing N N 210 
ILE   CA  CB   sing N N 211 
ILE   CA  HA   sing N N 212 
ILE   C   O    doub N N 213 
ILE   C   OXT  sing N N 214 
ILE   CB  CG1  sing N N 215 
ILE   CB  CG2  sing N N 216 
ILE   CB  HB   sing N N 217 
ILE   CG1 CD1  sing N N 218 
ILE   CG1 HG12 sing N N 219 
ILE   CG1 HG13 sing N N 220 
ILE   CG2 HG21 sing N N 221 
ILE   CG2 HG22 sing N N 222 
ILE   CG2 HG23 sing N N 223 
ILE   CD1 HD11 sing N N 224 
ILE   CD1 HD12 sing N N 225 
ILE   CD1 HD13 sing N N 226 
ILE   OXT HXT  sing N N 227 
LEU   N   CA   sing N N 228 
LEU   N   H    sing N N 229 
LEU   N   H2   sing N N 230 
LEU   CA  C    sing N N 231 
LEU   CA  CB   sing N N 232 
LEU   CA  HA   sing N N 233 
LEU   C   O    doub N N 234 
LEU   C   OXT  sing N N 235 
LEU   CB  CG   sing N N 236 
LEU   CB  HB2  sing N N 237 
LEU   CB  HB3  sing N N 238 
LEU   CG  CD1  sing N N 239 
LEU   CG  CD2  sing N N 240 
LEU   CG  HG   sing N N 241 
LEU   CD1 HD11 sing N N 242 
LEU   CD1 HD12 sing N N 243 
LEU   CD1 HD13 sing N N 244 
LEU   CD2 HD21 sing N N 245 
LEU   CD2 HD22 sing N N 246 
LEU   CD2 HD23 sing N N 247 
LEU   OXT HXT  sing N N 248 
LYS   N   CA   sing N N 249 
LYS   N   H    sing N N 250 
LYS   N   H2   sing N N 251 
LYS   CA  C    sing N N 252 
LYS   CA  CB   sing N N 253 
LYS   CA  HA   sing N N 254 
LYS   C   O    doub N N 255 
LYS   C   OXT  sing N N 256 
LYS   CB  CG   sing N N 257 
LYS   CB  HB2  sing N N 258 
LYS   CB  HB3  sing N N 259 
LYS   CG  CD   sing N N 260 
LYS   CG  HG2  sing N N 261 
LYS   CG  HG3  sing N N 262 
LYS   CD  CE   sing N N 263 
LYS   CD  HD2  sing N N 264 
LYS   CD  HD3  sing N N 265 
LYS   CE  NZ   sing N N 266 
LYS   CE  HE2  sing N N 267 
LYS   CE  HE3  sing N N 268 
LYS   NZ  HZ1  sing N N 269 
LYS   NZ  HZ2  sing N N 270 
LYS   NZ  HZ3  sing N N 271 
LYS   OXT HXT  sing N N 272 
MET   N   CA   sing N N 273 
MET   N   H    sing N N 274 
MET   N   H2   sing N N 275 
MET   CA  C    sing N N 276 
MET   CA  CB   sing N N 277 
MET   CA  HA   sing N N 278 
MET   C   O    doub N N 279 
MET   C   OXT  sing N N 280 
MET   CB  CG   sing N N 281 
MET   CB  HB2  sing N N 282 
MET   CB  HB3  sing N N 283 
MET   CG  SD   sing N N 284 
MET   CG  HG2  sing N N 285 
MET   CG  HG3  sing N N 286 
MET   SD  CE   sing N N 287 
MET   CE  HE1  sing N N 288 
MET   CE  HE2  sing N N 289 
MET   CE  HE3  sing N N 290 
MET   OXT HXT  sing N N 291 
PHE   N   CA   sing N N 292 
PHE   N   H    sing N N 293 
PHE   N   H2   sing N N 294 
PHE   CA  C    sing N N 295 
PHE   CA  CB   sing N N 296 
PHE   CA  HA   sing N N 297 
PHE   C   O    doub N N 298 
PHE   C   OXT  sing N N 299 
PHE   CB  CG   sing N N 300 
PHE   CB  HB2  sing N N 301 
PHE   CB  HB3  sing N N 302 
PHE   CG  CD1  doub Y N 303 
PHE   CG  CD2  sing Y N 304 
PHE   CD1 CE1  sing Y N 305 
PHE   CD1 HD1  sing N N 306 
PHE   CD2 CE2  doub Y N 307 
PHE   CD2 HD2  sing N N 308 
PHE   CE1 CZ   doub Y N 309 
PHE   CE1 HE1  sing N N 310 
PHE   CE2 CZ   sing Y N 311 
PHE   CE2 HE2  sing N N 312 
PHE   CZ  HZ   sing N N 313 
PHE   OXT HXT  sing N N 314 
PRO   N   CA   sing N N 315 
PRO   N   CD   sing N N 316 
PRO   N   H    sing N N 317 
PRO   CA  C    sing N N 318 
PRO   CA  CB   sing N N 319 
PRO   CA  HA   sing N N 320 
PRO   C   O    doub N N 321 
PRO   C   OXT  sing N N 322 
PRO   CB  CG   sing N N 323 
PRO   CB  HB2  sing N N 324 
PRO   CB  HB3  sing N N 325 
PRO   CG  CD   sing N N 326 
PRO   CG  HG2  sing N N 327 
PRO   CG  HG3  sing N N 328 
PRO   CD  HD2  sing N N 329 
PRO   CD  HD3  sing N N 330 
PRO   OXT HXT  sing N N 331 
SER   N   CA   sing N N 332 
SER   N   H    sing N N 333 
SER   N   H2   sing N N 334 
SER   CA  C    sing N N 335 
SER   CA  CB   sing N N 336 
SER   CA  HA   sing N N 337 
SER   C   O    doub N N 338 
SER   C   OXT  sing N N 339 
SER   CB  OG   sing N N 340 
SER   CB  HB2  sing N N 341 
SER   CB  HB3  sing N N 342 
SER   OG  HG   sing N N 343 
SER   OXT HXT  sing N N 344 
THR   N   CA   sing N N 345 
THR   N   H    sing N N 346 
THR   N   H2   sing N N 347 
THR   CA  C    sing N N 348 
THR   CA  CB   sing N N 349 
THR   CA  HA   sing N N 350 
THR   C   O    doub N N 351 
THR   C   OXT  sing N N 352 
THR   CB  OG1  sing N N 353 
THR   CB  CG2  sing N N 354 
THR   CB  HB   sing N N 355 
THR   OG1 HG1  sing N N 356 
THR   CG2 HG21 sing N N 357 
THR   CG2 HG22 sing N N 358 
THR   CG2 HG23 sing N N 359 
THR   OXT HXT  sing N N 360 
TYR   N   CA   sing N N 361 
TYR   N   H    sing N N 362 
TYR   N   H2   sing N N 363 
TYR   CA  C    sing N N 364 
TYR   CA  CB   sing N N 365 
TYR   CA  HA   sing N N 366 
TYR   C   O    doub N N 367 
TYR   C   OXT  sing N N 368 
TYR   CB  CG   sing N N 369 
TYR   CB  HB2  sing N N 370 
TYR   CB  HB3  sing N N 371 
TYR   CG  CD1  doub Y N 372 
TYR   CG  CD2  sing Y N 373 
TYR   CD1 CE1  sing Y N 374 
TYR   CD1 HD1  sing N N 375 
TYR   CD2 CE2  doub Y N 376 
TYR   CD2 HD2  sing N N 377 
TYR   CE1 CZ   doub Y N 378 
TYR   CE1 HE1  sing N N 379 
TYR   CE2 CZ   sing Y N 380 
TYR   CE2 HE2  sing N N 381 
TYR   CZ  OH   sing N N 382 
TYR   OH  HH   sing N N 383 
TYR   OXT HXT  sing N N 384 
VAL   N   CA   sing N N 385 
VAL   N   H    sing N N 386 
VAL   N   H2   sing N N 387 
VAL   CA  C    sing N N 388 
VAL   CA  CB   sing N N 389 
VAL   CA  HA   sing N N 390 
VAL   C   O    doub N N 391 
VAL   C   OXT  sing N N 392 
VAL   CB  CG1  sing N N 393 
VAL   CB  CG2  sing N N 394 
VAL   CB  HB   sing N N 395 
VAL   CG1 HG11 sing N N 396 
VAL   CG1 HG12 sing N N 397 
VAL   CG1 HG13 sing N N 398 
VAL   CG2 HG21 sing N N 399 
VAL   CG2 HG22 sing N N 400 
VAL   CG2 HG23 sing N N 401 
VAL   OXT HXT  sing N N 402 
# 
_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                    7HEX 
_atom_sites.fract_transf_matrix[1][1]   0.011252 
_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]   0.011252 
_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]   0.025271 
_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   ? 19.743 -16.351 22.248  0.60 39.56 ?  3   VAL   A N    1 
ATOM   2    N N    B VAL   A 1 3   ? 19.238 -15.336 22.988  0.40 42.75 ?  3   VAL   A N    1 
ATOM   3    C CA   A VAL   A 1 3   ? 18.788 -15.262 22.416  0.60 39.15 ?  3   VAL   A CA   1 
ATOM   4    C CA   B VAL   A 1 3   ? 18.168 -14.350 23.067  0.40 42.45 ?  3   VAL   A CA   1 
ATOM   5    C C    A VAL   A 1 3   ? 19.448 -13.923 22.108  0.60 36.83 ?  3   VAL   A C    1 
ATOM   6    C C    B VAL   A 1 3   ? 18.777 -12.951 23.127  0.40 41.29 ?  3   VAL   A C    1 
ATOM   7    O O    A VAL   A 1 3   ? 20.574 -13.663 22.534  0.60 36.92 ?  3   VAL   A O    1 
ATOM   8    O O    B VAL   A 1 3   ? 19.829 -12.751 23.734  0.40 41.54 ?  3   VAL   A O    1 
ATOM   9    C CB   A VAL   A 1 3   ? 18.163 -15.278 23.829  0.60 40.66 ?  3   VAL   A CB   1 
ATOM   10   C CB   B VAL   A 1 3   ? 17.228 -14.645 24.249  0.40 43.02 ?  3   VAL   A CB   1 
ATOM   11   C CG1  A VAL   A 1 3   ? 17.146 -14.151 23.984  0.60 41.15 ?  3   VAL   A CG1  1 
ATOM   12   C CG1  B VAL   A 1 3   ? 15.906 -13.917 24.071  0.40 43.19 ?  3   VAL   A CG1  1 
ATOM   13   C CG2  A VAL   A 1 3   ? 17.514 -16.626 24.102  0.60 41.12 ?  3   VAL   A CG2  1 
ATOM   14   C CG2  B VAL   A 1 3   ? 17.002 -16.147 24.372  0.40 43.19 ?  3   VAL   A CG2  1 
ATOM   15   H HA   A VAL   A 1 3   ? 18.068 -15.374 21.783  0.60 46.97 ?  3   VAL   A HA   1 
ATOM   16   H HA   B VAL   A 1 3   ? 17.639 -14.397 22.261  0.40 50.92 ?  3   VAL   A HA   1 
ATOM   17   H HB   A VAL   A 1 3   ? 18.860 -15.142 24.490  0.60 48.78 ?  3   VAL   A HB   1 
ATOM   18   H HB   B VAL   A 1 3   ? 17.637 -14.336 25.071  0.40 51.62 ?  3   VAL   A HB   1 
ATOM   19   H HG11 A VAL   A 1 3   ? 16.639 -14.294 24.800  0.60 49.36 ?  3   VAL   A HG11 1 
ATOM   20   H HG11 B VAL   A 1 3   ? 15.330 -14.120 24.825  0.40 51.82 ?  3   VAL   A HG11 1 
ATOM   21   H HG12 A VAL   A 1 3   ? 17.614 -13.303 24.033  0.60 49.36 ?  3   VAL   A HG12 1 
ATOM   22   H HG12 B VAL   A 1 3   ? 16.076 -12.964 24.030  0.40 51.82 ?  3   VAL   A HG12 1 
ATOM   23   H HG13 A VAL   A 1 3   ? 16.548 -14.159 23.221  0.60 49.36 ?  3   VAL   A HG13 1 
ATOM   24   H HG13 B VAL   A 1 3   ? 15.489 -14.216 23.247  0.40 51.82 ?  3   VAL   A HG13 1 
ATOM   25   H HG21 A VAL   A 1 3   ? 17.067 -16.594 24.961  0.60 49.34 ?  3   VAL   A HG21 1 
ATOM   26   H HG21 B VAL   A 1 3   ? 16.254 -16.307 24.968  0.40 51.81 ?  3   VAL   A HG21 1 
ATOM   27   H HG22 A VAL   A 1 3   ? 16.870 -16.811 23.400  0.60 49.34 ?  3   VAL   A HG22 1 
ATOM   28   H HG22 B VAL   A 1 3   ? 16.807 -16.510 23.492  0.40 51.81 ?  3   VAL   A HG22 1 
ATOM   29   H HG23 A VAL   A 1 3   ? 18.201 -17.310 24.110  0.60 49.34 ?  3   VAL   A HG23 1 
ATOM   30   H HG23 B VAL   A 1 3   ? 17.804 -16.561 24.728  0.40 51.81 ?  3   VAL   A HG23 1 
ATOM   31   N N    A ASN   A 1 4   ? 18.745 -13.083 21.350  0.60 34.00 ?  4   ASN   A N    1 
ATOM   32   N N    B ASN   A 1 4   ? 18.114 -11.985 22.489  0.40 39.73 ?  4   ASN   A N    1 
ATOM   33   C CA   A ASN   A 1 4   ? 19.185 -11.726 21.057  0.60 31.06 ?  4   ASN   A CA   1 
ATOM   34   C CA   B ASN   A 1 4   ? 18.711 -10.686 22.214  0.40 38.10 ?  4   ASN   A CA   1 
ATOM   35   C C    A ASN   A 1 4   ? 18.024 -10.766 21.297  0.60 28.76 ?  4   ASN   A C    1 
ATOM   36   C C    B ASN   A 1 4   ? 17.658 -9.593  22.355  0.40 36.90 ?  4   ASN   A C    1 
ATOM   37   O O    A ASN   A 1 4   ? 16.906 -11.176 21.626  0.60 28.48 ?  4   ASN   A O    1 
ATOM   38   O O    B ASN   A 1 4   ? 16.502 -9.852  22.705  0.40 36.81 ?  4   ASN   A O    1 
ATOM   39   C CB   A ASN   A 1 4   ? 19.749 -11.606 19.634  0.60 30.26 ?  4   ASN   A CB   1 
ATOM   40   C CB   B ASN   A 1 4   ? 19.310 -10.670 20.806  0.40 37.72 ?  4   ASN   A CB   1 
ATOM   41   C CG   A ASN   A 1 4   ? 18.747 -12.002 18.569  0.60 29.22 ?  4   ASN   A CG   1 
ATOM   42   C CG   B ASN   A 1 4   ? 18.384 -11.287 19.776  0.40 37.34 ?  4   ASN   A CG   1 
ATOM   43   O OD1  A ASN   A 1 4   ? 17.623 -11.502 18.540  0.60 28.64 ?  4   ASN   A OD1  1 
ATOM   44   O OD1  B ASN   A 1 4   ? 17.186 -11.003 19.752  0.40 37.27 ?  4   ASN   A OD1  1 
ATOM   45   N ND2  A ASN   A 1 4   ? 19.152 -12.907 17.684  0.60 28.98 ?  4   ASN   A ND2  1 
ATOM   46   N ND2  B ASN   A 1 4   ? 18.932 -12.152 18.932  0.40 37.06 ?  4   ASN   A ND2  1 
ATOM   47   H H    A ASN   A 1 4   ? 17.992 -13.282 20.982  0.60 40.79 ?  4   ASN   A H    1 
ATOM   48   H H    B ASN   A 1 4   ? 17.305 -12.065 22.204  0.40 47.67 ?  4   ASN   A H    1 
ATOM   49   H HA   A ASN   A 1 4   ? 19.896 -11.491 21.669  0.60 37.26 ?  4   ASN   A HA   1 
ATOM   50   H HA   B ASN   A 1 4   ? 19.422 -10.518 22.854  0.40 45.71 ?  4   ASN   A HA   1 
ATOM   51   H HB2  A ASN   A 1 4   ? 20.008 -10.684 19.473  0.60 36.30 ?  4   ASN   A HB2  1 
ATOM   52   H HB2  B ASN   A 1 4   ? 19.483 -9.754  20.541  0.40 45.25 ?  4   ASN   A HB2  1 
ATOM   53   H HB3  A ASN   A 1 4   ? 20.520 -12.186 19.553  0.60 36.30 ?  4   ASN   A HB3  1 
ATOM   54   H HB3  B ASN   A 1 4   ? 20.132 -11.177 20.813  0.40 45.25 ?  4   ASN   A HB3  1 
ATOM   55   H HD21 A ASN   A 1 4   ? 18.623 -13.164 17.057  0.60 34.77 ?  4   ASN   A HD21 1 
ATOM   56   H HD21 B ASN   A 1 4   ? 18.448 -12.535 18.333  0.40 44.46 ?  4   ASN   A HD21 1 
ATOM   57   H HD22 A ASN   A 1 4   ? 19.948 -13.231 17.734  0.60 34.77 ?  4   ASN   A HD22 1 
ATOM   58   H HD22 B ASN   A 1 4   ? 19.772 -12.327 18.984  0.40 44.46 ?  4   ASN   A HD22 1 
ATOM   59   N N    A SER   A 1 5   ? 18.295 -9.473  21.118  0.60 26.47 ?  5   SER   A N    1 
ATOM   60   N N    B SER   A 1 5   ? 18.069 -8.358  22.064  0.40 35.76 ?  5   SER   A N    1 
ATOM   61   C CA   A SER   A 1 5   ? 17.364 -8.417  21.494  0.60 24.51 ?  5   SER   A CA   1 
ATOM   62   C CA   B SER   A 1 5   ? 17.201 -7.191  22.157  0.40 34.53 ?  5   SER   A CA   1 
ATOM   63   C C    A SER   A 1 5   ? 16.459 -7.969  20.353  0.60 22.26 ?  5   SER   A C    1 
ATOM   64   C C    B SER   A 1 5   ? 16.475 -6.881  20.850  0.40 32.55 ?  5   SER   A C    1 
ATOM   65   O O    A SER   A 1 5   ? 15.678 -7.032  20.539  0.60 22.57 ?  5   SER   A O    1 
ATOM   66   O O    B SER   A 1 5   ? 15.838 -5.828  20.747  0.40 32.63 ?  5   SER   A O    1 
ATOM   67   C CB   A SER   A 1 5   ? 18.132 -7.213  22.053  0.60 25.23 ?  5   SER   A CB   1 
ATOM   68   C CB   B SER   A 1 5   ? 17.990 -5.968  22.643  0.40 35.25 ?  5   SER   A CB   1 
ATOM   69   O OG   A SER   A 1 5   ? 19.089 -6.744  21.121  0.60 25.67 ?  5   SER   A OG   1 
ATOM   70   O OG   B SER   A 1 5   ? 19.047 -5.642  21.756  0.40 35.72 ?  5   SER   A OG   1 
ATOM   71   H H    A SER   A 1 5   ? 19.021 -9.178  20.762  0.60 31.76 ?  5   SER   A H    1 
ATOM   72   H H    B SER   A 1 5   ? 18.866 -8.172  21.801  0.40 42.90 ?  5   SER   A H    1 
ATOM   73   H HA   A SER   A 1 5   ? 16.794 -8.741  22.202  0.60 29.40 ?  5   SER   A HA   1 
ATOM   74   H HA   B SER   A 1 5   ? 16.523 -7.370  22.821  0.40 41.42 ?  5   SER   A HA   1 
ATOM   75   H HB2  A SER   A 1 5   ? 17.508 -6.494  22.248  0.60 30.26 ?  5   SER   A HB2  1 
ATOM   76   H HB2  B SER   A 1 5   ? 17.388 -5.208  22.705  0.40 42.29 ?  5   SER   A HB2  1 
ATOM   77   H HB3  A SER   A 1 5   ? 18.590 -7.479  22.868  0.60 30.26 ?  5   SER   A HB3  1 
ATOM   78   H HB3  B SER   A 1 5   ? 18.362 -6.161  23.521  0.40 42.29 ?  5   SER   A HB3  1 
ATOM   79   H HG   A SER   A 1 5   ? 19.509 -6.085  21.442  0.60 30.79 ?  5   SER   A HG   1 
ATOM   80   H HG   B SER   A 1 5   ? 19.467 -4.972  22.044  0.40 42.85 ?  5   SER   A HG   1 
ATOM   81   N N    A PHE   A 1 6   ? 16.531 -8.607  19.189  0.60 19.24 ?  6   PHE   A N    1 
ATOM   82   N N    B PHE   A 1 6   ? 16.558 -7.762  19.855  0.40 30.57 ?  6   PHE   A N    1 
ATOM   83   C CA   A PHE   A 1 6   ? 15.639 -8.243  18.094  0.60 16.92 ?  6   PHE   A CA   1 
ATOM   84   C CA   B PHE   A 1 6   ? 15.681 -7.654  18.696  0.40 28.55 ?  6   PHE   A CA   1 
ATOM   85   C C    A PHE   A 1 6   ? 14.204 -8.618  18.450  0.60 17.31 ?  6   PHE   A C    1 
ATOM   86   C C    B PHE   A 1 6   ? 14.260 -7.997  19.125  0.40 27.61 ?  6   PHE   A C    1 
ATOM   87   O O    A PHE   A 1 6   ? 13.935 -9.744  18.876  0.60 18.26 ?  6   PHE   A O    1 
ATOM   88   O O    B PHE   A 1 6   ? 14.022 -9.050  19.724  0.40 27.69 ?  6   PHE   A O    1 
ATOM   89   C CB   A PHE   A 1 6   ? 16.063 -8.943  16.806  0.60 15.64 ?  6   PHE   A CB   1 
ATOM   90   C CB   B PHE   A 1 6   ? 16.122 -8.625  17.600  0.40 27.67 ?  6   PHE   A CB   1 
ATOM   91   C CG   A PHE   A 1 6   ? 17.329 -8.391  16.208  0.60 14.87 ?  6   PHE   A CG   1 
ATOM   92   C CG   B PHE   A 1 6   ? 17.381 -8.219  16.876  0.40 27.09 ?  6   PHE   A CG   1 
ATOM   93   C CD1  A PHE   A 1 6   ? 17.328 -7.169  15.548  0.60 14.71 ?  6   PHE   A CD1  1 
ATOM   94   C CD1  B PHE   A 1 6   ? 17.320 -7.444  15.727  0.40 26.89 ?  6   PHE   A CD1  1 
ATOM   95   C CD2  A PHE   A 1 6   ? 18.515 -9.095  16.302  0.60 15.54 ?  6   PHE   A CD2  1 
ATOM   96   C CD2  B PHE   A 1 6   ? 18.622 -8.636  17.329  0.40 27.04 ?  6   PHE   A CD2  1 
ATOM   97   C CE1  A PHE   A 1 6   ? 18.493 -6.659  14.997  0.60 14.95 ?  6   PHE   A CE1  1 
ATOM   98   C CE1  B PHE   A 1 6   ? 18.476 -7.080  15.053  0.40 26.83 ?  6   PHE   A CE1  1 
ATOM   99   C CE2  A PHE   A 1 6   ? 19.678 -8.594  15.750  0.60 15.60 ?  6   PHE   A CE2  1 
ATOM   100  C CE2  B PHE   A 1 6   ? 19.780 -8.276  16.659  0.40 26.89 ?  6   PHE   A CE2  1 
ATOM   101  C CZ   A PHE   A 1 6   ? 19.667 -7.374  15.096  0.60 15.67 ?  6   PHE   A CZ   1 
ATOM   102  C CZ   B PHE   A 1 6   ? 19.705 -7.498  15.520  0.40 26.85 ?  6   PHE   A CZ   1 
ATOM   103  H H    A PHE   A 1 6   ? 17.074 -9.249  19.014  0.60 23.08 ?  6   PHE   A H    1 
ATOM   104  H H    B PHE   A 1 6   ? 17.106 -8.425  19.830  0.40 36.67 ?  6   PHE   A H    1 
ATOM   105  H HA   A PHE   A 1 6   ? 15.673 -7.291  17.952  0.60 20.29 ?  6   PHE   A HA   1 
ATOM   106  H HA   B PHE   A 1 6   ? 15.700 -6.748  18.350  0.40 34.25 ?  6   PHE   A HA   1 
ATOM   107  H HB2  A PHE   A 1 6   ? 16.208 -9.887  16.994  0.60 18.76 ?  6   PHE   A HB2  1 
ATOM   108  H HB2  B PHE   A 1 6   ? 16.278 -9.493  18.003  0.40 33.19 ?  6   PHE   A HB2  1 
ATOM   109  H HB3  A PHE   A 1 6   ? 15.352 -8.850  16.151  0.60 18.76 ?  6   PHE   A HB3  1 
ATOM   110  H HB3  B PHE   A 1 6   ? 15.410 -8.691  16.945  0.40 33.19 ?  6   PHE   A HB3  1 
ATOM   111  H HD1  A PHE   A 1 6   ? 16.533 -6.685  15.478  0.60 17.64 ?  6   PHE   A HD1  1 
ATOM   112  H HD1  B PHE   A 1 6   ? 16.495 -7.160  15.406  0.40 32.25 ?  6   PHE   A HD1  1 
ATOM   113  H HD2  A PHE   A 1 6   ? 18.527 -9.915  16.739  0.60 18.64 ?  6   PHE   A HD2  1 
ATOM   114  H HD2  B PHE   A 1 6   ? 18.679 -9.158  18.096  0.40 32.43 ?  6   PHE   A HD2  1 
ATOM   115  H HE1  A PHE   A 1 6   ? 18.479 -5.836  14.557  0.60 17.93 ?  6   PHE   A HE1  1 
ATOM   116  H HE1  B PHE   A 1 6   ? 18.425 -6.557  14.284  0.40 32.18 ?  6   PHE   A HE1  1 
ATOM   117  H HE2  A PHE   A 1 6   ? 20.471 -9.073  15.821  0.60 18.71 ?  6   PHE   A HE2  1 
ATOM   118  H HE2  B PHE   A 1 6   ? 20.608 -8.557  16.976  0.40 32.25 ?  6   PHE   A HE2  1 
ATOM   119  H HZ   A PHE   A 1 6   ? 20.450 -7.032  14.729  0.60 18.79 ?  6   PHE   A HZ   1 
ATOM   120  H HZ   B PHE   A 1 6   ? 20.482 -7.255  15.069  0.40 32.21 ?  6   PHE   A HZ   1 
ATOM   121  N N    A SER   A 1 7   ? 13.280 -7.676  18.267  0.60 17.25 ?  7   SER   A N    1 
ATOM   122  N N    B SER   A 1 7   ? 13.312 -7.114  18.819  0.40 26.52 ?  7   SER   A N    1 
ATOM   123  C CA   A SER   A 1 7   ? 11.910 -7.823  18.741  0.60 18.45 ?  7   SER   A CA   1 
ATOM   124  C CA   B SER   A 1 7   ? 11.944 -7.259  19.295  0.40 25.68 ?  7   SER   A CA   1 
ATOM   125  C C    A SER   A 1 7   ? 10.916 -7.550  17.620  0.60 17.14 ?  7   SER   A C    1 
ATOM   126  C C    B SER   A 1 7   ? 10.967 -7.001  18.156  0.40 23.87 ?  7   SER   A C    1 
ATOM   127  O O    A SER   A 1 7   ? 11.124 -6.658  16.794  0.60 17.07 ?  7   SER   A O    1 
ATOM   128  O O    B SER   A 1 7   ? 11.178 -6.102  17.337  0.40 23.89 ?  7   SER   A O    1 
ATOM   129  C CB   A SER   A 1 7   ? 11.642 -6.857  19.901  0.60 20.60 ?  7   SER   A CB   1 
ATOM   130  C CB   B SER   A 1 7   ? 11.670 -6.279  20.450  0.40 26.52 ?  7   SER   A CB   1 
ATOM   131  O OG   A SER   A 1 7   ? 10.289 -6.914  20.310  0.60 22.11 ?  7   SER   A OG   1 
ATOM   132  O OG   B SER   A 1 7   ? 10.621 -6.743  21.281  0.40 27.20 ?  7   SER   A OG   1 
ATOM   133  H H    A SER   A 1 7   ? 13.426 -6.936  17.859  0.60 20.69 ?  7   SER   A H    1 
ATOM   134  H H    B SER   A 1 7   ? 13.438 -6.415  18.331  0.40 31.81 ?  7   SER   A H    1 
ATOM   135  H HA   A SER   A 1 7   ? 11.768 -8.728  19.058  0.60 22.12 ?  7   SER   A HA   1 
ATOM   136  H HA   B SER   A 1 7   ? 11.805 -8.160  19.623  0.40 30.80 ?  7   SER   A HA   1 
ATOM   137  H HB2  A SER   A 1 7   ? 12.212 -7.097  20.651  0.60 24.71 ?  7   SER   A HB2  1 
ATOM   138  H HB2  B SER   A 1 7   ? 12.479 -6.183  20.982  0.40 31.81 ?  7   SER   A HB2  1 
ATOM   139  H HB3  A SER   A 1 7   ? 11.838 -5.953  19.614  0.60 24.71 ?  7   SER   A HB3  1 
ATOM   140  H HB3  B SER   A 1 7   ? 11.413 -5.421  20.084  0.40 31.81 ?  7   SER   A HB3  1 
ATOM   141  H HG   A SER   A 1 7   ? 10.157 -6.390  20.956  0.60 26.51 ?  7   SER   A HG   1 
ATOM   142  H HG   B SER   A 1 7   ? 10.494 -6.205  21.915  0.40 32.63 ?  7   SER   A HG   1 
ATOM   143  N N    A GLY   A 1 8   ? 9.830  -8.324  17.599  0.60 16.62 ?  8   GLY   A N    1 
ATOM   144  N N    B GLY   A 1 8   ? 9.904  -7.801  18.104  0.40 22.28 ?  8   GLY   A N    1 
ATOM   145  C CA   A GLY   A 1 8   ? 8.747  -8.074  16.668  0.60 16.35 ?  8   GLY   A CA   1 
ATOM   146  C CA   B GLY   A 1 8   ? 8.813  -7.565  17.179  0.40 20.77 ?  8   GLY   A CA   1 
ATOM   147  C C    A GLY   A 1 8   ? 8.956  -8.583  15.262  0.60 15.56 ?  8   GLY   A C    1 
ATOM   148  C C    B GLY   A 1 8   ? 8.970  -8.141  15.790  0.40 19.27 ?  8   GLY   A C    1 
ATOM   149  O O    A GLY   A 1 8   ? 8.236  -8.158  14.353  0.60 16.39 ?  8   GLY   A O    1 
ATOM   150  O O    B GLY   A 1 8   ? 8.229  -7.737  14.887  0.40 19.46 ?  8   GLY   A O    1 
ATOM   151  H H    A GLY   A 1 8   ? 9.703  -9.003  18.113  0.60 19.93 ?  8   GLY   A H    1 
ATOM   152  H H    B GLY   A 1 8   ? 9.794  -8.488  18.608  0.40 26.73 ?  8   GLY   A H    1 
ATOM   153  H HA2  A GLY   A 1 8   ? 7.938  -8.481  17.015  0.60 19.61 ?  8   GLY   A HA2  1 
ATOM   154  H HA2  B GLY   A 1 8   ? 8.002  -7.938  17.554  0.40 24.91 ?  8   GLY   A HA2  1 
ATOM   155  H HA3  A GLY   A 1 8   ? 8.601  -7.120  16.610  0.60 19.61 ?  8   GLY   A HA3  1 
ATOM   156  H HA3  B GLY   A 1 8   ? 8.684  -6.607  17.087  0.40 24.91 ?  8   GLY   A HA3  1 
ATOM   157  N N    A TYR   A 1 9   ? 9.916  -9.483  15.046  0.60 14.04 ?  9   TYR   A N    1 
ATOM   158  N N    B TYR   A 1 9   ? 9.889  -9.079  15.585  0.40 17.92 ?  9   TYR   A N    1 
ATOM   159  C CA   A TYR   A 1 9   ? 10.181 -10.025 13.720  0.60 13.02 ?  9   TYR   A CA   1 
ATOM   160  C CA   B TYR   A 1 9   ? 10.138 -9.613  14.253  0.40 16.90 ?  9   TYR   A CA   1 
ATOM   161  C C    A TYR   A 1 9   ? 9.304  -11.239 13.440  0.60 12.72 ?  9   TYR   A C    1 
ATOM   162  C C    B TYR   A 1 9   ? 9.232  -10.803 13.956  0.40 16.25 ?  9   TYR   A C    1 
ATOM   163  O O    A TYR   A 1 9   ? 9.027  -12.049 14.331  0.60 13.77 ?  9   TYR   A O    1 
ATOM   164  O O    B TYR   A 1 9   ? 8.811  -11.533 14.856  0.40 16.76 ?  9   TYR   A O    1 
ATOM   165  C CB   A TYR   A 1 9   ? 11.657 -10.425 13.569  0.60 12.82 ?  9   TYR   A CB   1 
ATOM   166  C CB   B TYR   A 1 9   ? 11.601 -10.038 14.103  0.40 17.15 ?  9   TYR   A CB   1 
ATOM   167  C CG   A TYR   A 1 9   ? 12.566 -9.230  13.398  0.60 12.75 ?  9   TYR   A CG   1 
ATOM   168  C CG   B TYR   A 1 9   ? 12.561 -8.884  13.936  0.40 16.97 ?  9   TYR   A CG   1 
ATOM   169  C CD1  A TYR   A 1 9   ? 12.897 -8.430  14.480  0.60 13.28 ?  9   TYR   A CD1  1 
ATOM   170  C CD1  B TYR   A 1 9   ? 12.879 -8.062  15.007  0.40 17.23 ?  9   TYR   A CD1  1 
ATOM   171  C CD2  A TYR   A 1 9   ? 13.061 -8.880  12.147  0.60 12.44 ?  9   TYR   A CD2  1 
ATOM   172  C CD2  B TYR   A 1 9   ? 13.148 -8.615  12.706  0.40 16.75 ?  9   TYR   A CD2  1 
ATOM   173  C CE1  A TYR   A 1 9   ? 13.696 -7.316  14.330  0.60 13.82 ?  9   TYR   A CE1  1 
ATOM   174  C CE1  B TYR   A 1 9   ? 13.751 -7.006  14.860  0.40 17.22 ?  9   TYR   A CE1  1 
ATOM   175  C CE2  A TYR   A 1 9   ? 13.868 -7.766  11.985  0.60 13.06 ?  9   TYR   A CE2  1 
ATOM   176  C CE2  B TYR   A 1 9   ? 14.022 -7.558  12.548  0.40 17.07 ?  9   TYR   A CE2  1 
ATOM   177  C CZ   A TYR   A 1 9   ? 14.183 -6.987  13.080  0.60 13.64 ?  9   TYR   A CZ   1 
ATOM   178  C CZ   B TYR   A 1 9   ? 14.319 -6.758  13.628  0.40 17.34 ?  9   TYR   A CZ   1 
ATOM   179  O OH   A TYR   A 1 9   ? 14.979 -5.879  12.919  0.60 14.69 ?  9   TYR   A OH   1 
ATOM   180  O OH   B TYR   A 1 9   ? 15.185 -5.703  13.478  0.40 18.23 ?  9   TYR   A OH   1 
ATOM   181  H H    A TYR   A 1 9   ? 10.430 -9.801  15.656  0.60 16.84 ?  9   TYR   A H    1 
ATOM   182  H H    B TYR   A 1 9   ? 10.379 -9.427  16.204  0.40 21.50 ?  9   TYR   A H    1 
ATOM   183  H HA   A TYR   A 1 9   ? 9.982  -9.360  13.050  0.60 15.61 ?  9   TYR   A HA   1 
ATOM   184  H HA   B TYR   A 1 9   ? 9.956  -8.924  13.598  0.40 20.26 ?  9   TYR   A HA   1 
ATOM   185  H HB2  A TYR   A 1 9   ? 11.940 -10.913 14.358  0.60 15.38 ?  9   TYR   A HB2  1 
ATOM   186  H HB2  B TYR   A 1 9   ? 11.872 -10.541 14.884  0.40 20.57 ?  9   TYR   A HB2  1 
ATOM   187  H HB3  A TYR   A 1 9   ? 11.747 -10.990 12.782  0.60 15.38 ?  9   TYR   A HB3  1 
ATOM   188  H HB3  B TYR   A 1 9   ? 11.673 -10.595 13.315  0.40 20.57 ?  9   TYR   A HB3  1 
ATOM   189  H HD1  A TYR   A 1 9   ? 12.560 -8.645  15.323  0.60 15.92 ?  9   TYR   A HD1  1 
ATOM   190  H HD1  B TYR   A 1 9   ? 12.494 -8.227  15.838  0.40 20.66 ?  9   TYR   A HD1  1 
ATOM   191  H HD2  A TYR   A 1 9   ? 12.844 -9.405  11.404  0.60 14.92 ?  9   TYR   A HD2  1 
ATOM   192  H HD2  B TYR   A 1 9   ? 12.949 -9.154  11.976  0.40 20.09 ?  9   TYR   A HD2  1 
ATOM   193  H HE1  A TYR   A 1 9   ? 13.907 -6.794  15.065  0.60 16.58 ?  9   TYR   A HE1  1 
ATOM   194  H HE1  B TYR   A 1 9   ? 13.952 -6.462  15.589  0.40 20.66 ?  9   TYR   A HE1  1 
ATOM   195  H HE2  A TYR   A 1 9   ? 14.197 -7.548  11.141  0.60 15.67 ?  9   TYR   A HE2  1 
ATOM   196  H HE2  B TYR   A 1 9   ? 14.411 -7.387  11.720  0.40 20.48 ?  9   TYR   A HE2  1 
ATOM   197  H HH   A TYR   A 1 9   ? 15.097 -5.506  13.659  0.60 17.62 ?  9   TYR   A HH   1 
ATOM   198  H HH   B TYR   A 1 9   ? 15.277 -5.302  14.210  0.40 21.86 ?  9   TYR   A HH   1 
ATOM   199  N N    A LEU   A 1 10  ? 8.892  -11.368 12.185  0.60 12.52 ?  10  LEU   A N    1 
ATOM   200  N N    B LEU   A 1 10  ? 8.921  -10.971 12.672  0.40 15.94 ?  10  LEU   A N    1 
ATOM   201  C CA   A LEU   A 1 10  ? 8.294  -12.595 11.682  0.60 12.17 ?  10  LEU   A CA   1 
ATOM   202  C CA   B LEU   A 1 10  ? 8.267  -12.168 12.168  0.40 16.12 ?  10  LEU   A CA   1 
ATOM   203  C C    A LEU   A 1 10  ? 9.418  -13.517 11.220  0.60 11.74 ?  10  LEU   A C    1 
ATOM   204  C C    B LEU   A 1 10  ? 9.329  -13.143 11.688  0.40 14.56 ?  10  LEU   A C    1 
ATOM   205  O O    A LEU   A 1 10  ? 10.366 -13.073 10.562  0.60 12.29 ?  10  LEU   A O    1 
ATOM   206  O O    B LEU   A 1 10  ? 10.307 -12.752 11.043  0.40 13.93 ?  10  LEU   A O    1 
ATOM   207  C CB   A LEU   A 1 10  ? 7.379  -12.265 10.502  0.60 13.43 ?  10  LEU   A CB   1 
ATOM   208  C CB   B LEU   A 1 10  ? 7.366  -11.822 10.983  0.40 17.88 ?  10  LEU   A CB   1 
ATOM   209  C CG   A LEU   A 1 10  ? 6.657  -13.430 9.834   0.60 15.83 ?  10  LEU   A CG   1 
ATOM   210  C CG   B LEU   A 1 10  ? 5.888  -11.525 11.204  0.40 19.99 ?  10  LEU   A CG   1 
ATOM   211  C CD1  A LEU   A 1 10  ? 5.582  -13.987 10.753  0.60 17.54 ?  10  LEU   A CD1  1 
ATOM   212  C CD1  B LEU   A 1 10  ? 5.209  -11.500 9.850   0.40 20.79 ?  10  LEU   A CD1  1 
ATOM   213  C CD2  A LEU   A 1 10  ? 6.074  -13.001 8.498   0.60 17.36 ?  10  LEU   A CD2  1 
ATOM   214  C CD2  B LEU   A 1 10  ? 5.253  -12.565 12.107  0.40 20.53 ?  10  LEU   A CD2  1 
ATOM   215  H H    A LEU   A 1 10  ? 8.961  -10.756 11.583  0.60 15.01 ?  10  LEU   A H    1 
ATOM   216  H H    B LEU   A 1 10  ? 9.080  -10.386 12.064  0.40 19.12 ?  10  LEU   A H    1 
ATOM   217  H HA   A LEU   A 1 10  ? 7.781  -13.039 12.376  0.60 14.60 ?  10  LEU   A HA   1 
ATOM   218  H HA   B LEU   A 1 10  ? 7.740  -12.586 12.873  0.40 19.33 ?  10  LEU   A HA   1 
ATOM   219  H HB2  A LEU   A 1 10  ? 6.701  -11.650 10.811  0.60 16.10 ?  10  LEU   A HB2  1 
ATOM   220  H HB2  B LEU   A 1 10  ? 7.739  -11.037 10.552  0.40 21.45 ?  10  LEU   A HB2  1 
ATOM   221  H HB3  A LEU   A 1 10  ? 7.915  -11.838 9.816   0.60 16.10 ?  10  LEU   A HB3  1 
ATOM   222  H HB3  B LEU   A 1 10  ? 7.404  -12.565 10.364  0.40 21.45 ?  10  LEU   A HB3  1 
ATOM   223  H HG   A LEU   A 1 10  ? 7.293  -14.144 9.664   0.60 18.98 ?  10  LEU   A HG   1 
ATOM   224  H HG   B LEU   A 1 10  ? 5.787  -10.651 11.616  0.40 23.98 ?  10  LEU   A HG   1 
ATOM   225  H HD11 A LEU   A 1 10  ? 5.164  -14.752 10.327  0.60 21.04 ?  10  LEU   A HD11 1 
ATOM   226  H HD11 B LEU   A 1 10  ? 4.263  -11.348 9.974   0.40 24.93 ?  10  LEU   A HD11 1 
ATOM   227  H HD12 A LEU   A 1 10  ? 5.991  -14.260 11.591  0.60 21.04 ?  10  LEU   A HD12 1 
ATOM   228  H HD12 B LEU   A 1 10  ? 5.597  -10.791 9.316   0.40 24.93 ?  10  LEU   A HD12 1 
ATOM   229  H HD13 A LEU   A 1 10  ? 4.921  -13.298 10.920  0.60 21.04 ?  10  LEU   A HD13 1 
ATOM   230  H HD13 B LEU   A 1 10  ? 5.353  -12.357 9.413   0.40 24.93 ?  10  LEU   A HD13 1 
ATOM   231  H HD21 A LEU   A 1 10  ? 5.614  -13.756 8.101   0.60 20.82 ?  10  LEU   A HD21 1 
ATOM   232  H HD21 B LEU   A 1 10  ? 4.291  -12.503 12.033  0.40 24.63 ?  10  LEU   A HD21 1 
ATOM   233  H HD22 A LEU   A 1 10  ? 5.454  -12.273 8.648   0.60 20.82 ?  10  LEU   A HD22 1 
ATOM   234  H HD22 B LEU   A 1 10  ? 5.553  -13.445 11.827  0.40 24.63 ?  10  LEU   A HD22 1 
ATOM   235  H HD23 A LEU   A 1 10  ? 6.798  -12.711 7.923   0.60 20.82 ?  10  LEU   A HD23 1 
ATOM   236  H HD23 B LEU   A 1 10  ? 5.529  -12.400 13.022  0.40 24.63 ?  10  LEU   A HD23 1 
ATOM   237  N N    A LYS   A 1 11  ? 9.324  -14.796 11.584  0.60 11.96 ?  11  LYS   A N    1 
ATOM   238  N N    B LYS   A 1 11  ? 9.126  -14.416 11.986  0.40 14.46 ?  11  LYS   A N    1 
ATOM   239  C CA   A LYS   A 1 11  ? 10.326 -15.795 11.222  0.60 12.10 ?  11  LYS   A CA   1 
ATOM   240  C CA   B LYS   A 1 11  ? 10.071 -15.452 11.603  0.40 14.08 ?  11  LYS   A CA   1 
ATOM   241  C C    A LYS   A 1 11  ? 9.964  -16.388 9.866   0.60 12.18 ?  11  LYS   A C    1 
ATOM   242  C C    B LYS   A 1 11  ? 9.712  -15.960 10.213  0.40 13.55 ?  11  LYS   A C    1 
ATOM   243  O O    A LYS   A 1 11  ? 8.909  -17.015 9.729   0.60 14.05 ?  11  LYS   A O    1 
ATOM   244  O O    B LYS   A 1 11  ? 8.591  -16.433 9.991   0.40 13.92 ?  11  LYS   A O    1 
ATOM   245  C CB   A LYS   A 1 11  ? 10.372 -16.882 12.299  0.60 11.97 ?  11  LYS   A CB   1 
ATOM   246  C CB   B LYS   A 1 11  ? 10.027 -16.592 12.614  0.40 14.06 ?  11  LYS   A CB   1 
ATOM   247  C CG   A LYS   A 1 11  ? 11.416 -17.976 12.115  0.60 12.45 ?  11  LYS   A CG   1 
ATOM   248  C CG   B LYS   A 1 11  ? 11.038 -17.684 12.356  0.40 14.23 ?  11  LYS   A CG   1 
ATOM   249  C CD   A LYS   A 1 11  ? 11.498 -18.823 13.396  0.60 12.58 ?  11  LYS   A CD   1 
ATOM   250  C CD   B LYS   A 1 11  ? 10.980 -18.721 13.460  0.40 14.67 ?  11  LYS   A CD   1 
ATOM   251  C CE   A LYS   A 1 11  ? 12.501 -19.962 13.311  0.60 12.75 ?  11  LYS   A CE   1 
ATOM   252  C CE   B LYS   A 1 11  ? 12.012 -19.816 13.253  0.40 14.61 ?  11  LYS   A CE   1 
ATOM   253  N NZ   A LYS   A 1 11  ? 13.858 -19.478 12.971  0.60 12.97 ?  11  LYS   A NZ   1 
ATOM   254  N NZ   B LYS   A 1 11  ? 13.411 -19.303 13.275  0.40 14.72 ?  11  LYS   A NZ   1 
ATOM   255  H H    A LYS   A 1 11  ? 8.678  -15.126 12.051  0.60 14.34 ?  11  LYS   A H    1 
ATOM   256  H H    B LYS   A 1 11  ? 8.433  -14.707 12.403  0.40 17.34 ?  11  LYS   A H    1 
ATOM   257  H HA   A LYS   A 1 11  ? 11.201 -15.385 11.160  0.60 14.51 ?  11  LYS   A HA   1 
ATOM   258  H HA   B LYS   A 1 11  ? 10.966 -15.080 11.577  0.40 16.89 ?  11  LYS   A HA   1 
ATOM   259  H HB2  A LYS   A 1 11  ? 10.555 -16.461 13.152  0.60 14.35 ?  11  LYS   A HB2  1 
ATOM   260  H HB2  B LYS   A 1 11  ? 10.193 -16.227 13.497  0.40 16.86 ?  11  LYS   A HB2  1 
ATOM   261  H HB3  A LYS   A 1 11  ? 9.508  -17.322 12.334  0.60 14.35 ?  11  LYS   A HB3  1 
ATOM   262  H HB3  B LYS   A 1 11  ? 9.144  -16.990 12.586  0.40 16.86 ?  11  LYS   A HB3  1 
ATOM   263  H HG2  A LYS   A 1 11  ? 11.165 -18.561 11.379  0.60 14.93 ?  11  LYS   A HG2  1 
ATOM   264  H HG2  B LYS   A 1 11  ? 10.836 -18.119 11.513  0.40 17.07 ?  11  LYS   A HG2  1 
ATOM   265  H HG3  A LYS   A 1 11  ? 12.289 -17.585 11.953  0.60 14.93 ?  11  LYS   A HG3  1 
ATOM   266  H HG3  B LYS   A 1 11  ? 11.929 -17.302 12.336  0.40 17.07 ?  11  LYS   A HG3  1 
ATOM   267  H HD2  A LYS   A 1 11  ? 11.757 -18.254 14.135  0.60 15.08 ?  11  LYS   A HD2  1 
ATOM   268  H HD2  B LYS   A 1 11  ? 11.155 -18.290 14.311  0.40 17.59 ?  11  LYS   A HD2  1 
ATOM   269  H HD3  A LYS   A 1 11  ? 10.626 -19.215 13.571  0.60 15.08 ?  11  LYS   A HD3  1 
ATOM   270  H HD3  B LYS   A 1 11  ? 10.097 -19.128 13.466  0.40 17.59 ?  11  LYS   A HD3  1 
ATOM   271  H HE2  A LYS   A 1 11  ? 12.552 -20.412 14.174  0.60 15.29 ?  11  LYS   A HE2  1 
ATOM   272  H HE2  B LYS   A 1 11  ? 11.920 -20.471 13.962  0.40 17.52 ?  11  LYS   A HE2  1 
ATOM   273  H HE3  A LYS   A 1 11  ? 12.225 -20.589 12.628  0.60 15.29 ?  11  LYS   A HE3  1 
ATOM   274  H HE3  B LYS   A 1 11  ? 11.858 -20.234 12.392  0.40 17.52 ?  11  LYS   A HE3  1 
ATOM   275  H HZ1  A LYS   A 1 11  ? 14.428 -20.162 12.946  0.60 15.56 ?  11  LYS   A HZ1  1 
ATOM   276  H HZ1  B LYS   A 1 11  ? 13.983 -19.976 13.175  0.40 17.65 ?  11  LYS   A HZ1  1 
ATOM   277  H HZ2  A LYS   A 1 11  ? 13.846 -19.080 12.177  0.60 15.56 ?  11  LYS   A HZ2  1 
ATOM   278  H HZ2  B LYS   A 1 11  ? 13.532 -18.720 12.613  0.40 17.65 ?  11  LYS   A HZ2  1 
ATOM   279  H HZ3  A LYS   A 1 11  ? 14.135 -18.896 13.585  0.60 15.56 ?  11  LYS   A HZ3  1 
ATOM   280  H HZ3  B LYS   A 1 11  ? 13.574 -18.897 14.051  0.40 17.65 ?  11  LYS   A HZ3  1 
ATOM   281  N N    A LEU   A 1 12  ? 10.832 -16.205 8.866   0.60 11.29 ?  12  LEU   A N    1 
ATOM   282  N N    B LEU   A 1 12  ? 10.653 -15.849 9.277   0.40 13.55 ?  12  LEU   A N    1 
ATOM   283  C CA   A LEU   A 1 12  ? 10.571 -16.781 7.549   0.60 11.38 ?  12  LEU   A CA   1 
ATOM   284  C CA   B LEU   A 1 12  ? 10.442 -16.365 7.930   0.40 13.61 ?  12  LEU   A CA   1 
ATOM   285  C C    A LEU   A 1 12  ? 11.143 -18.183 7.395   0.60 11.82 ?  12  LEU   A C    1 
ATOM   286  C C    B LEU   A 1 12  ? 11.022 -17.759 7.735   0.40 13.03 ?  12  LEU   A C    1 
ATOM   287  O O    A LEU   A 1 12  ? 10.495 -19.057 6.809   0.60 12.61 ?  12  LEU   A O    1 
ATOM   288  O O    B LEU   A 1 12  ? 10.370 -18.620 7.135   0.40 13.25 ?  12  LEU   A O    1 
ATOM   289  C CB   A LEU   A 1 12  ? 11.128 -15.886 6.437   0.60 11.89 ?  12  LEU   A CB   1 
ATOM   290  C CB   B LEU   A 1 12  ? 11.027 -15.404 6.890   0.40 14.33 ?  12  LEU   A CB   1 
ATOM   291  C CG   A LEU   A 1 12  ? 10.477 -14.510 6.272   0.60 12.96 ?  12  LEU   A CG   1 
ATOM   292  C CG   B LEU   A 1 12  ? 10.341 -14.040 6.793   0.40 14.72 ?  12  LEU   A CG   1 
ATOM   293  C CD1  A LEU   A 1 12  ? 11.210 -13.705 5.210   0.60 13.60 ?  12  LEU   A CD1  1 
ATOM   294  C CD1  B LEU   A 1 12  ? 11.034 -13.174 5.750   0.40 15.37 ?  12  LEU   A CD1  1 
ATOM   295  C CD2  A LEU   A 1 12  ? 9.003  -14.647 5.919   0.60 13.88 ?  12  LEU   A CD2  1 
ATOM   296  C CD2  B LEU   A 1 12  ? 8.858  -14.189 6.474   0.40 15.07 ?  12  LEU   A CD2  1 
ATOM   297  H H    A LEU   A 1 12  ? 11.575 -15.762 8.922   0.60 13.54 ?  12  LEU   A H    1 
ATOM   298  H H    B LEU   A 1 12  ? 11.422 -15.470 9.396   0.40 16.24 ?  12  LEU   A H    1 
ATOM   299  H HA   A LEU   A 1 12  ? 9.617  -16.851 7.425   0.60 13.64 ?  12  LEU   A HA   1 
ATOM   300  H HA   B LEU   A 1 12  ? 9.490  -16.416 7.769   0.40 16.32 ?  12  LEU   A HA   1 
ATOM   301  H HB2  A LEU   A 1 12  ? 12.072 -15.742 6.607   0.60 14.25 ?  12  LEU   A HB2  1 
ATOM   302  H HB2  B LEU   A 1 12  ? 11.959 -15.239 7.105   0.40 17.18 ?  12  LEU   A HB2  1 
ATOM   303  H HB3  A LEU   A 1 12  ? 11.027 -16.357 5.592   0.60 14.25 ?  12  LEU   A HB3  1 
ATOM   304  H HB3  B LEU   A 1 12  ? 10.964 -15.817 6.016   0.40 17.18 ?  12  LEU   A HB3  1 
ATOM   305  H HG   A LEU   A 1 12  ? 10.544 -14.031 7.110   0.60 15.54 ?  12  LEU   A HG   1 
ATOM   306  H HG   B LEU   A 1 12  ? 10.416 -13.587 7.649   0.40 17.66 ?  12  LEU   A HG   1 
ATOM   307  H HD11 A LEU   A 1 12  ? 10.779 -12.844 5.113   0.60 16.30 ?  12  LEU   A HD11 1 
ATOM   308  H HD11 B LEU   A 1 12  ? 10.586 -12.314 5.705   0.40 18.43 ?  12  LEU   A HD11 1 
ATOM   309  H HD12 A LEU   A 1 12  ? 12.134 -13.586 5.485   0.60 16.30 ?  12  LEU   A HD12 1 
ATOM   310  H HD12 B LEU   A 1 12  ? 11.960 -13.051 6.009   0.40 18.43 ?  12  LEU   A HD12 1 
ATOM   311  H HD13 A LEU   A 1 12  ? 11.179 -14.189 4.368   0.60 16.30 ?  12  LEU   A HD13 1 
ATOM   312  H HD13 B LEU   A 1 12  ? 10.985 -13.618 4.890   0.40 18.43 ?  12  LEU   A HD13 1 
ATOM   313  H HD21 A LEU   A 1 12  ? 8.651  -13.772 5.694   0.60 16.65 ?  12  LEU   A HD21 1 
ATOM   314  H HD21 B LEU   A 1 12  ? 8.499  -13.324 6.220   0.40 18.07 ?  12  LEU   A HD21 1 
ATOM   315  H HD22 A LEU   A 1 12  ? 8.913  -15.246 5.160   0.60 16.65 ?  12  LEU   A HD22 1 
ATOM   316  H HD22 B LEU   A 1 12  ? 8.755  -14.818 5.744   0.40 18.07 ?  12  LEU   A HD22 1 
ATOM   317  H HD23 A LEU   A 1 12  ? 8.527  -15.009 6.683   0.60 16.65 ?  12  LEU   A HD23 1 
ATOM   318  H HD23 B LEU   A 1 12  ? 8.396  -14.519 7.262   0.40 18.07 ?  12  LEU   A HD23 1 
ATOM   319  N N    A THR   A 1 13  ? 12.359 -18.401 7.885   0.60 11.99 ?  13  THR   A N    1 
ATOM   320  N N    B THR   A 1 13  ? 12.236 -17.996 8.226   0.40 12.58 ?  13  THR   A N    1 
ATOM   321  C CA   A THR   A 1 13  ? 13.048 -19.681 7.781   0.60 12.10 ?  13  THR   A CA   1 
ATOM   322  C CA   B THR   A 1 13  ? 12.895 -19.292 8.126   0.40 12.74 ?  13  THR   A CA   1 
ATOM   323  C C    A THR   A 1 13  ? 13.830 -19.901 9.068   0.60 12.32 ?  13  THR   A C    1 
ATOM   324  C C    B THR   A 1 13  ? 13.649 -19.546 9.427   0.40 13.06 ?  13  THR   A C    1 
ATOM   325  O O    A THR   A 1 13  ? 13.737 -19.123 10.022  0.60 12.49 ?  13  THR   A O    1 
ATOM   326  O O    B THR   A 1 13  ? 13.537 -18.795 10.401  0.40 13.35 ?  13  THR   A O    1 
ATOM   327  C CB   A THR   A 1 13  ? 14.013 -19.737 6.585   0.60 12.99 ?  13  THR   A CB   1 
ATOM   328  C CB   B THR   A 1 13  ? 13.875 -19.334 6.945   0.40 13.08 ?  13  THR   A CB   1 
ATOM   329  O OG1  A THR   A 1 13  ? 15.096 -18.827 6.807   0.60 13.22 ?  13  THR   A OG1  1 
ATOM   330  O OG1  B THR   A 1 13  ? 14.947 -18.421 7.192   0.40 12.97 ?  13  THR   A OG1  1 
ATOM   331  C CG2  A THR   A 1 13  ? 13.323 -19.403 5.275   0.60 14.24 ?  13  THR   A CG2  1 
ATOM   332  C CG2  B THR   A 1 13  ? 13.195 -18.974 5.630   0.40 13.53 ?  13  THR   A CG2  1 
ATOM   333  H H    A THR   A 1 13  ? 12.826 -17.806 8.290   0.60 14.38 ?  13  THR   A H    1 
ATOM   334  H H    B THR   A 1 13  ? 12.712 -17.395 8.618   0.40 15.09 ?  13  THR   A H    1 
ATOM   335  H HA   A THR   A 1 13  ? 12.404 -20.400 7.686   0.60 14.50 ?  13  THR   A HA   1 
ATOM   336  H HA   B THR   A 1 13  ? 12.228 -19.987 8.004   0.40 15.28 ?  13  THR   A HA   1 
ATOM   337  H HB   A THR   A 1 13  ? 14.378 -20.634 6.512   0.60 15.58 ?  13  THR   A HB   1 
ATOM   338  H HB   B THR   A 1 13  ? 14.238 -20.229 6.863   0.40 15.68 ?  13  THR   A HB   1 
ATOM   339  H HG1  A THR   A 1 13  ? 15.629 -18.845 6.153   0.60 15.85 ?  13  THR   A HG1  1 
ATOM   340  H HG1  B THR   A 1 13  ? 15.492 -18.753 7.732   0.40 15.55 ?  13  THR   A HG1  1 
ATOM   341  H HG21 A THR   A 1 13  ? 13.908 -19.619 4.532   0.60 17.08 ?  13  THR   A HG21 1 
ATOM   342  H HG21 B THR   A 1 13  ? 13.824 -19.070 4.896   0.40 16.23 ?  13  THR   A HG21 1 
ATOM   343  H HG22 A THR   A 1 13  ? 12.509 -19.923 5.194   0.60 17.08 ?  13  THR   A HG22 1 
ATOM   344  H HG22 B THR   A 1 13  ? 12.443 -19.568 5.475   0.40 16.23 ?  13  THR   A HG22 1 
ATOM   345  H HG23 A THR   A 1 13  ? 13.104 -18.462 5.246   0.60 17.08 ?  13  THR   A HG23 1 
ATOM   346  H HG23 B THR   A 1 13  ? 12.877 -18.061 5.657   0.40 16.23 ?  13  THR   A HG23 1 
ATOM   347  N N    A ASP   A 1 14  ? 14.629 -20.970 9.083   0.60 12.68 ?  14  ASP   A N    1 
ATOM   348  N N    B ASP   A 1 14  ? 14.439 -20.619 9.417   0.40 13.75 ?  14  ASP   A N    1 
ATOM   349  C CA   A ASP   A 1 14  ? 15.461 -21.240 10.244  0.60 13.45 ?  14  ASP   A CA   1 
ATOM   350  C CA   B ASP   A 1 14  ? 15.303 -20.948 10.544  0.40 14.65 ?  14  ASP   A CA   1 
ATOM   351  C C    A ASP   A 1 14  ? 16.328 -20.043 10.619  0.60 12.52 ?  14  ASP   A C    1 
ATOM   352  C C    B ASP   A 1 14  ? 16.123 -19.744 10.998  0.40 13.43 ?  14  ASP   A C    1 
ATOM   353  O O    A ASP   A 1 14  ? 16.609 -19.833 11.804  0.60 13.35 ?  14  ASP   A O    1 
ATOM   354  O O    B ASP   A 1 14  ? 16.258 -19.496 12.202  0.40 13.70 ?  14  ASP   A O    1 
ATOM   355  C CB   A ASP   A 1 14  ? 16.355 -22.450 9.982   0.60 15.91 ?  14  ASP   A CB   1 
ATOM   356  C CB   B ASP   A 1 14  ? 16.226 -22.095 10.128  0.40 17.12 ?  14  ASP   A CB   1 
ATOM   357  C CG   A ASP   A 1 14  ? 17.255 -22.736 11.144  0.60 18.72 ?  14  ASP   A CG   1 
ATOM   358  C CG   B ASP   A 1 14  ? 17.120 -22.575 11.260  0.40 20.21 ?  14  ASP   A CG   1 
ATOM   359  O OD1  A ASP   A 1 14  ? 16.732 -23.144 12.203  0.60 18.96 ?  14  ASP   A OD1  1 
ATOM   360  O OD1  B ASP   A 1 14  ? 16.894 -22.165 12.419  0.40 21.82 ?  14  ASP   A OD1  1 
ATOM   361  O OD2  A ASP   A 1 14  ? 18.469 -22.507 11.010  0.60 20.39 -1 14  ASP   A OD2  1 
ATOM   362  O OD2  B ASP   A 1 14  ? 18.057 -23.358 10.989  0.40 21.22 -1 14  ASP   A OD2  1 
ATOM   363  H H    A ASP   A 1 14  ? 14.716 -21.544 8.441   0.60 15.21 ?  14  ASP   A H    1 
ATOM   364  H H    B ASP   A 1 14  ? 14.488 -21.165 8.764   0.40 16.49 ?  14  ASP   A H    1 
ATOM   365  H HA   A ASP   A 1 14  ? 14.901 -21.458 11.002  0.60 16.13 ?  14  ASP   A HA   1 
ATOM   366  H HA   B ASP   A 1 14  ? 14.756 -21.239 11.289  0.40 17.57 ?  14  ASP   A HA   1 
ATOM   367  H HB2  A ASP   A 1 14  ? 15.800 -23.244 9.838   0.60 19.09 ?  14  ASP   A HB2  1 
ATOM   368  H HB2  B ASP   A 1 14  ? 15.670 -22.830 9.808   0.40 20.53 ?  14  ASP   A HB2  1 
ATOM   369  H HB3  A ASP   A 1 14  ? 16.905 -22.295 9.199   0.60 19.09 ?  14  ASP   A HB3  1 
ATOM   370  H HB3  B ASP   A 1 14  ? 16.801 -21.786 9.412   0.40 20.53 ?  14  ASP   A HB3  1 
ATOM   371  N N    A ASN   A 1 15  ? 16.770 -19.252 9.630   0.60 11.57 ?  15  ASN   A N    1 
ATOM   372  N N    B ASN   A 1 15  ? 16.663 -18.971 10.053  0.40 13.02 ?  15  ASN   A N    1 
ATOM   373  C CA   A ASN   A 1 15  ? 17.763 -18.207 9.874   0.60 11.91 ?  15  ASN   A CA   1 
ATOM   374  C CA   B ASN   A 1 15  ? 17.648 -17.945 10.376  0.40 12.70 ?  15  ASN   A CA   1 
ATOM   375  C C    A ASN   A 1 15  ? 17.392 -16.812 9.373   0.60 12.14 ?  15  ASN   A C    1 
ATOM   376  C C    B ASN   A 1 15  ? 17.296 -16.539 9.909   0.40 12.45 ?  15  ASN   A C    1 
ATOM   377  O O    A ASN   A 1 15  ? 18.179 -15.880 9.582   0.60 13.34 ?  15  ASN   A O    1 
ATOM   378  O O    B ASN   A 1 15  ? 18.059 -15.613 10.203  0.40 12.36 ?  15  ASN   A O    1 
ATOM   379  C CB   A ASN   A 1 15  ? 19.132 -18.604 9.281   0.60 11.44 ?  15  ASN   A CB   1 
ATOM   380  C CB   B ASN   A 1 15  ? 19.029 -18.323 9.815   0.40 12.83 ?  15  ASN   A CB   1 
ATOM   381  C CG   A ASN   A 1 15  ? 19.110 -18.684 7.768   0.60 11.96 ?  15  ASN   A CG   1 
ATOM   382  C CG   B ASN   A 1 15  ? 19.034 -18.457 8.306   0.40 13.08 ?  15  ASN   A CG   1 
ATOM   383  O OD1  A ASN   A 1 15  ? 18.395 -19.500 7.197   0.60 12.49 ?  15  ASN   A OD1  1 
ATOM   384  O OD1  B ASN   A 1 15  ? 18.256 -19.221 7.735   0.40 13.66 ?  15  ASN   A OD1  1 
ATOM   385  N ND2  A ASN   A 1 15  ? 19.880 -17.828 7.110   0.60 12.31 ?  15  ASN   A ND2  1 
ATOM   386  N ND2  B ASN   A 1 15  ? 19.899 -17.690 7.646   0.40 13.27 ?  15  ASN   A ND2  1 
ATOM   387  H H    A ASN   A 1 15  ? 16.515 -19.318 8.814   0.60 13.87 ?  15  ASN   A H    1 
ATOM   388  H H    B ASN   A 1 15  ? 16.471 -19.016 9.219   0.40 15.61 ?  15  ASN   A H    1 
ATOM   389  H HA   A ASN   A 1 15  ? 17.899 -18.145 10.829  0.60 14.28 ?  15  ASN   A HA   1 
ATOM   390  H HA   B ASN   A 1 15  ? 17.739 -17.902 11.339  0.40 15.23 ?  15  ASN   A HA   1 
ATOM   391  H HB2  A ASN   A 1 15  ? 19.798 -17.941 9.534   0.60 13.71 ?  15  ASN   A HB2  1 
ATOM   392  H HB2  B ASN   A 1 15  ? 19.670 -17.634 10.058  0.40 15.38 ?  15  ASN   A HB2  1 
ATOM   393  H HB3  A ASN   A 1 15  ? 19.401 -19.478 9.626   0.60 13.71 ?  15  ASN   A HB3  1 
ATOM   394  H HB3  B ASN   A 1 15  ? 19.299 -19.173 10.192  0.40 15.38 ?  15  ASN   A HB3  1 
ATOM   395  H HD21 A ASN   A 1 15  ? 19.894 -17.843 6.247   0.60 14.76 ?  15  ASN   A HD21 1 
ATOM   396  H HD21 B ASN   A 1 15  ? 19.941 -17.725 6.786   0.40 15.92 ?  15  ASN   A HD21 1 
ATOM   397  H HD22 A ASN   A 1 15  ? 20.370 -17.270 7.537   0.60 14.76 ?  15  ASN   A HD22 1 
ATOM   398  H HD22 B ASN   A 1 15  ? 20.425 -17.164 8.078   0.40 15.92 ?  15  ASN   A HD22 1 
ATOM   399  N N    A VAL   A 1 16  ? 16.240 -16.633 8.723   0.60 11.72 ?  16  VAL   A N    1 
ATOM   400  N N    B VAL   A 1 16  ? 16.177 -16.339 9.214   0.40 12.56 ?  16  VAL   A N    1 
ATOM   401  C CA   A VAL   A 1 16  ? 15.847 -15.349 8.148   0.60 11.40 ?  16  VAL   A CA   1 
ATOM   402  C CA   B VAL   A 1 16  ? 15.816 -15.035 8.667   0.40 12.48 ?  16  VAL   A CA   1 
ATOM   403  C C    A VAL   A 1 16  ? 14.579 -14.840 8.836   0.60 11.02 ?  16  VAL   A C    1 
ATOM   404  C C    B VAL   A 1 16  ? 14.546 -14.538 9.348   0.40 12.81 ?  16  VAL   A C    1 
ATOM   405  O O    A VAL   A 1 16  ? 13.565 -15.550 8.907   0.60 11.31 ?  16  VAL   A O    1 
ATOM   406  O O    B VAL   A 1 16  ? 13.546 -15.264 9.426   0.40 13.20 ?  16  VAL   A O    1 
ATOM   407  C CB   A VAL   A 1 16  ? 15.656 -15.437 6.621   0.60 12.25 ?  16  VAL   A CB   1 
ATOM   408  C CB   B VAL   A 1 16  ? 15.659 -15.073 7.135   0.40 11.75 ?  16  VAL   A CB   1 
ATOM   409  C CG1  A VAL   A 1 16  ? 15.183 -14.098 6.072   0.60 12.88 ?  16  VAL   A CG1  1 
ATOM   410  C CG1  B VAL   A 1 16  ? 15.338 -13.681 6.594   0.40 11.58 ?  16  VAL   A CG1  1 
ATOM   411  C CG2  A VAL   A 1 16  ? 16.947 -15.875 5.920   0.60 12.73 ?  16  VAL   A CG2  1 
ATOM   412  C CG2  B VAL   A 1 16  ? 16.921 -15.626 6.482   0.40 12.73 ?  16  VAL   A CG2  1 
ATOM   413  H H    A VAL   A 1 16  ? 15.671 -17.267 8.601   0.60 14.05 ?  16  VAL   A H    1 
ATOM   414  H H    B VAL   A 1 16  ? 15.598 -16.951 9.050   0.40 15.06 ?  16  VAL   A H    1 
ATOM   415  H HA   A VAL   A 1 16  ? 16.564 -14.714 8.314   0.60 13.67 ?  16  VAL   A HA   1 
ATOM   416  H HA   B VAL   A 1 16  ? 16.517 -14.400 8.871   0.40 14.97 ?  16  VAL   A HA   1 
ATOM   417  H HB   A VAL   A 1 16  ? 14.981 -16.108 6.429   0.60 14.69 ?  16  VAL   A HB   1 
ATOM   418  H HB   B VAL   A 1 16  ? 14.922 -15.659 6.907   0.40 14.09 ?  16  VAL   A HB   1 
ATOM   419  H HG11 A VAL   A 1 16  ? 15.260 -14.111 5.107   0.60 15.45 ?  16  VAL   A HG11 1 
ATOM   420  H HG11 B VAL   A 1 16  ? 15.392 -13.698 5.627   0.40 13.88 ?  16  VAL   A HG11 1 
ATOM   421  H HG12 A VAL   A 1 16  ? 14.257 -13.968 6.328   0.60 15.45 ?  16  VAL   A HG12 1 
ATOM   422  H HG12 B VAL   A 1 16  ? 14.441 -13.433 6.870   0.40 13.88 ?  16  VAL   A HG12 1 
ATOM   423  H HG13 A VAL   A 1 16  ? 15.736 -13.397 6.443   0.60 15.45 ?  16  VAL   A HG13 1 
ATOM   424  H HG13 B VAL   A 1 16  ? 15.981 -13.048 6.950   0.40 13.88 ?  16  VAL   A HG13 1 
ATOM   425  H HG21 A VAL   A 1 16  ? 16.846 -15.738 4.963   0.60 15.27 ?  16  VAL   A HG21 1 
ATOM   426  H HG21 B VAL   A 1 16  ? 16.979 -15.296 5.571   0.40 15.27 ?  16  VAL   A HG21 1 
ATOM   427  H HG22 A VAL   A 1 16  ? 17.684 -15.338 6.251   0.60 15.27 ?  16  VAL   A HG22 1 
ATOM   428  H HG22 B VAL   A 1 16  ? 17.692 -15.337 6.990   0.40 15.27 ?  16  VAL   A HG22 1 
ATOM   429  H HG23 A VAL   A 1 16  ? 17.112 -16.813 6.103   0.60 15.27 ?  16  VAL   A HG23 1 
ATOM   430  H HG23 B VAL   A 1 16  ? 16.873 -16.595 6.481   0.40 15.27 ?  16  VAL   A HG23 1 
ATOM   431  N N    A TYR   A 1 17  ? 14.635 -13.582 9.292   0.60 10.98 ?  17  TYR   A N    1 
ATOM   432  N N    B TYR   A 1 17  ? 14.596 -13.293 9.831   0.40 13.27 ?  17  TYR   A N    1 
ATOM   433  C CA   A TYR   A 1 17  ? 13.562 -12.901 10.004  0.60 11.13 ?  17  TYR   A CA   1 
ATOM   434  C CA   B TYR   A 1 17  ? 13.481 -12.618 10.480  0.40 13.83 ?  17  TYR   A CA   1 
ATOM   435  C C    A TYR   A 1 17  ? 13.288 -11.574 9.305   0.60 11.63 ?  17  TYR   A C    1 
ATOM   436  C C    B TYR   A 1 17  ? 13.246 -11.288 9.786   0.40 13.26 ?  17  TYR   A C    1 
ATOM   437  O O    A TYR   A 1 17  ? 14.185 -11.008 8.677   0.60 11.57 ?  17  TYR   A O    1 
ATOM   438  O O    B TYR   A 1 17  ? 14.168 -10.716 9.200   0.40 13.45 ?  17  TYR   A O    1 
ATOM   439  C CB   A TYR   A 1 17  ? 13.986 -12.640 11.458  0.60 11.27 ?  17  TYR   A CB   1 
ATOM   440  C CB   B TYR   A 1 17  ? 13.791 -12.362 11.955  0.40 15.93 ?  17  TYR   A CB   1 
ATOM   441  C CG   A TYR   A 1 17  ? 14.168 -13.892 12.294  0.60 11.40 ?  17  TYR   A CG   1 
ATOM   442  C CG   B TYR   A 1 17  ? 13.634 -13.592 12.812  0.40 18.44 ?  17  TYR   A CG   1 
ATOM   443  C CD1  A TYR   A 1 17  ? 15.332 -14.647 12.225  0.60 12.39 ?  17  TYR   A CD1  1 
ATOM   444  C CD1  B TYR   A 1 17  ? 14.589 -14.599 12.802  0.40 19.88 ?  17  TYR   A CD1  1 
ATOM   445  C CD2  A TYR   A 1 17  ? 13.162 -14.332 13.151  0.60 11.96 ?  17  TYR   A CD2  1 
ATOM   446  C CD2  B TYR   A 1 17  ? 12.521 -13.752 13.621  0.40 19.50 ?  17  TYR   A CD2  1 
ATOM   447  C CE1  A TYR   A 1 17  ? 15.489 -15.810 12.987  0.60 12.58 ?  17  TYR   A CE1  1 
ATOM   448  C CE1  B TYR   A 1 17  ? 14.437 -15.732 13.581  0.40 20.78 ?  17  TYR   A CE1  1 
ATOM   449  C CE2  A TYR   A 1 17  ? 13.310 -15.483 13.917  0.60 12.29 ?  17  TYR   A CE2  1 
ATOM   450  C CE2  B TYR   A 1 17  ? 12.362 -14.873 14.402  0.40 20.61 ?  17  TYR   A CE2  1 
ATOM   451  C CZ   A TYR   A 1 17  ? 14.472 -16.224 13.832  0.60 12.66 ?  17  TYR   A CZ   1 
ATOM   452  C CZ   B TYR   A 1 17  ? 13.322 -15.861 14.380  0.40 21.20 ?  17  TYR   A CZ   1 
ATOM   453  O OH   A TYR   A 1 17  ? 14.626 -17.368 14.593  0.60 13.00 ?  17  TYR   A OH   1 
ATOM   454  O OH   B TYR   A 1 17  ? 13.158 -16.983 15.160  0.40 22.17 ?  17  TYR   A OH   1 
ATOM   455  H H    A TYR   A 1 17  ? 15.333 -13.093 9.181   0.60 13.16 ?  17  TYR   A H    1 
ATOM   456  H H    B TYR   A 1 17  ? 15.301 -12.795 9.788   0.40 15.91 ?  17  TYR   A H    1 
ATOM   457  H HA   A TYR   A 1 17  ? 12.764 -13.457 9.988   0.60 13.35 ?  17  TYR   A HA   1 
ATOM   458  H HA   B TYR   A 1 17  ? 12.676 -13.146 10.411  0.40 16.58 ?  17  TYR   A HA   1 
ATOM   459  H HB2  A TYR   A 1 17  ? 14.837 -12.174 11.450  0.60 13.51 ?  17  TYR   A HB2  1 
ATOM   460  H HB2  B TYR   A 1 17  ? 14.709 -12.063 12.027  0.40 19.10 ?  17  TYR   A HB2  1 
ATOM   461  H HB3  A TYR   A 1 17  ? 13.313 -12.101 11.878  0.60 13.51 ?  17  TYR   A HB3  1 
ATOM   462  H HB3  B TYR   A 1 17  ? 13.194 -11.675 12.293  0.40 19.10 ?  17  TYR   A HB3  1 
ATOM   463  H HD1  A TYR   A 1 17  ? 16.017 -14.389 11.655  0.60 14.85 ?  17  TYR   A HD1  1 
ATOM   464  H HD1  B TYR   A 1 17  ? 15.342 -14.511 12.260  0.40 23.84 ?  17  TYR   A HD1  1 
ATOM   465  H HD2  A TYR   A 1 17  ? 12.370 -13.845 13.211  0.60 14.33 ?  17  TYR   A HD2  1 
ATOM   466  H HD2  B TYR   A 1 17  ? 11.871 -13.084 13.636  0.40 23.39 ?  17  TYR   A HD2  1 
ATOM   467  H HE1  A TYR   A 1 17  ? 16.272 -16.313 12.925  0.60 15.09 ?  17  TYR   A HE1  1 
ATOM   468  H HE1  B TYR   A 1 17  ? 15.080 -16.400 13.568  0.40 24.92 ?  17  TYR   A HE1  1 
ATOM   469  H HE2  A TYR   A 1 17  ? 12.616 -15.758 14.478  0.60 14.74 ?  17  TYR   A HE2  1 
ATOM   470  H HE2  B TYR   A 1 17  ? 11.611 -14.961 14.937  0.40 24.72 ?  17  TYR   A HE2  1 
ATOM   471  H HH   A TYR   A 1 17  ? 15.395 -17.688 14.473  0.60 15.59 ?  17  TYR   A HH   1 
ATOM   472  H HH   B TYR   A 1 17  ? 12.422 -16.937 15.564  0.40 26.59 ?  17  TYR   A HH   1 
ATOM   473  N N    A ILE   A 1 18  ? 12.056 -11.062 9.414   0.60 11.86 ?  18  ILE   A N    1 
ATOM   474  N N    B ILE   A 1 18  ? 12.013 -10.784 9.853   0.40 12.72 ?  18  ILE   A N    1 
ATOM   475  C CA   A ILE   A 1 18  ? 11.662 -9.861  8.678   0.60 12.31 ?  18  ILE   A CA   1 
ATOM   476  C CA   B ILE   A 1 18  ? 11.657 -9.557  9.147   0.40 12.71 ?  18  ILE   A CA   1 
ATOM   477  C C    A ILE   A 1 18  ? 10.702 -9.008  9.503   0.60 12.70 ?  18  ILE   A C    1 
ATOM   478  C C    B ILE   A 1 18  ? 10.758 -8.695  10.023  0.40 12.57 ?  18  ILE   A C    1 
ATOM   479  O O    A ILE   A 1 18  ? 9.876  -9.526  10.261  0.60 13.17 ?  18  ILE   A O    1 
ATOM   480  O O    B ILE   A 1 18  ? 9.898  -9.204  10.751  0.40 13.03 ?  18  ILE   A O    1 
ATOM   481  C CB   A ILE   A 1 18  ? 11.085 -10.237 7.293   0.60 12.34 ?  18  ILE   A CB   1 
ATOM   482  C CB   B ILE   A 1 18  ? 11.009 -9.857  7.781   0.40 12.01 ?  18  ILE   A CB   1 
ATOM   483  C CG1  A ILE   A 1 18  ? 11.030 -9.014  6.380   0.60 12.50 ?  18  ILE   A CG1  1 
ATOM   484  C CG1  B ILE   A 1 18  ? 10.907 -8.576  6.951   0.40 12.67 ?  18  ILE   A CG1  1 
ATOM   485  C CG2  A ILE   A 1 18  ? 9.735  -10.954 7.431   0.60 12.66 ?  18  ILE   A CG2  1 
ATOM   486  C CG2  B ILE   A 1 18  ? 9.646  -10.511 7.961   0.40 12.39 ?  18  ILE   A CG2  1 
ATOM   487  C CD1  A ILE   A 1 18  ? 10.776 -9.361  4.942   0.60 13.58 ?  18  ILE   A CD1  1 
ATOM   488  C CD1  B ILE   A 1 18  ? 10.502 -8.821  5.520   0.40 13.73 ?  18  ILE   A CD1  1 
ATOM   489  H H    A ILE   A 1 18  ? 11.439 -11.412 9.902   0.60 14.22 ?  18  ILE   A H    1 
ATOM   490  H H    B ILE   A 1 18  ? 11.365 -11.138 10.299  0.40 15.26 ?  18  ILE   A H    1 
ATOM   491  H HA   A ILE   A 1 18  ? 12.458 -9.343  8.519   0.60 14.76 ?  18  ILE   A HA   1 
ATOM   492  H HA   B ILE   A 1 18  ? 12.468 -9.054  8.982   0.40 15.24 ?  18  ILE   A HA   1 
ATOM   493  H HB   A ILE   A 1 18  ? 11.696 -10.874 6.882   0.60 14.80 ?  18  ILE   A HB   1 
ATOM   494  H HB   B ILE   A 1 18  ? 11.584 -10.475 7.311   0.40 14.41 ?  18  ILE   A HB   1 
ATOM   495  H HG12 A ILE   A 1 18  ? 10.320 -8.431  6.675   0.60 14.99 ?  18  ILE   A HG12 1 
ATOM   496  H HG12 B ILE   A 1 18  ? 10.245 -7.990  7.353   0.40 15.19 ?  18  ILE   A HG12 1 
ATOM   497  H HG13 A ILE   A 1 18  ? 11.884 -8.554  6.424   0.60 14.99 ?  18  ILE   A HG13 1 
ATOM   498  H HG13 B ILE   A 1 18  ? 11.773 -8.133  6.945   0.40 15.19 ?  18  ILE   A HG13 1 
ATOM   499  H HG21 A ILE   A 1 18  ? 9.469  -11.309 6.563   0.60 15.18 ?  18  ILE   A HG21 1 
ATOM   500  H HG21 B ILE   A 1 18  ? 9.346  -10.852 7.103   0.40 14.86 ?  18  ILE   A HG21 1 
ATOM   501  H HG22 A ILE   A 1 18  ? 9.821  -11.682 8.066   0.60 15.18 ?  18  ILE   A HG22 1 
ATOM   502  H HG22 B ILE   A 1 18  ? 9.726  -11.239 8.595   0.40 14.86 ?  18  ILE   A HG22 1 
ATOM   503  H HG23 A ILE   A 1 18  ? 9.066  -10.322 7.741   0.60 15.18 ?  18  ILE   A HG23 1 
ATOM   504  H HG23 B ILE   A 1 18  ? 9.015  -9.852  8.291   0.40 14.86 ?  18  ILE   A HG23 1 
ATOM   505  H HD11 A ILE   A 1 18  ? 10.798 -8.546  4.413   0.60 16.29 ?  18  ILE   A HD11 1 
ATOM   506  H HD11 B ILE   A 1 18  ? 10.486 -7.974  5.047   0.40 16.47 ?  18  ILE   A HD11 1 
ATOM   507  H HD12 A ILE   A 1 18  ? 11.464 -9.971  4.634   0.60 16.29 ?  18  ILE   A HD12 1 
ATOM   508  H HD12 B ILE   A 1 18  ? 11.146 -9.417  5.108   0.40 16.47 ?  18  ILE   A HD12 1 
ATOM   509  H HD13 A ILE   A 1 18  ? 9.904  -9.779  4.866   0.60 16.29 ?  18  ILE   A HD13 1 
ATOM   510  H HD13 B ILE   A 1 18  ? 9.620  -9.223  5.506   0.40 16.47 ?  18  ILE   A HD13 1 
ATOM   511  N N    A LYS   A 1 19  ? 10.802 -7.684  9.327   0.60 12.77 ?  19  LYS   A N    1 
ATOM   512  N N    B LYS   A 1 19  ? 10.968 -7.378  9.946   0.40 12.70 ?  19  LYS   A N    1 
ATOM   513  C CA   A LYS   A 1 19  ? 9.994  -6.727  10.076  0.60 13.51 ?  19  LYS   A CA   1 
ATOM   514  C CA   B LYS   A 1 19  ? 10.208 -6.406  10.719  0.40 13.94 ?  19  LYS   A CA   1 
ATOM   515  C C    A LYS   A 1 19  ? 9.796  -5.455  9.258   0.60 14.13 ?  19  LYS   A C    1 
ATOM   516  C C    B LYS   A 1 19  ? 9.950  -5.180  9.854   0.40 14.88 ?  19  LYS   A C    1 
ATOM   517  O O    A LYS   A 1 19  ? 10.692 -5.041  8.517   0.60 14.30 ?  19  LYS   A O    1 
ATOM   518  O O    B LYS   A 1 19  ? 10.784 -4.798  9.030   0.40 15.14 ?  19  LYS   A O    1 
ATOM   519  C CB   A LYS   A 1 19  ? 10.694 -6.385  11.398  0.60 14.96 ?  19  LYS   A CB   1 
ATOM   520  C CB   B LYS   A 1 19  ? 10.981 -6.000  11.985  0.40 14.54 ?  19  LYS   A CB   1 
ATOM   521  C CG   A LYS   A 1 19  ? 9.959  -5.442  12.342  0.60 16.40 ?  19  LYS   A CG   1 
ATOM   522  C CG   B LYS   A 1 19  ? 10.270 -5.056  12.939  0.40 15.44 ?  19  LYS   A CG   1 
ATOM   523  C CD   A LYS   A 1 19  ? 10.853 -5.140  13.543  0.60 17.72 ?  19  LYS   A CD   1 
ATOM   524  C CD   B LYS   A 1 19  ? 11.200 -4.705  14.098  0.40 16.18 ?  19  LYS   A CD   1 
ATOM   525  C CE   A LYS   A 1 19  ? 10.184 -4.256  14.577  0.60 18.45 ?  19  LYS   A CE   1 
ATOM   526  C CE   B LYS   A 1 19  ? 10.545 -3.790  15.117  0.40 16.98 ?  19  LYS   A CE   1 
ATOM   527  N NZ   A LYS   A 1 19  ? 11.104 -3.983  15.721  0.60 18.93 ?  19  LYS   A NZ   1 
ATOM   528  N NZ   B LYS   A 1 19  ? 11.421 -3.599  16.308  0.40 17.48 ?  19  LYS   A NZ   1 
ATOM   529  H H    A LYS   A 1 19  ? 11.343 -7.327  8.765   0.60 15.31 ?  19  LYS   A H    1 
ATOM   530  H H    B LYS   A 1 19  ? 11.577 -7.012  9.449   0.40 15.23 ?  19  LYS   A H    1 
ATOM   531  H HA   A LYS   A 1 19  ? 9.127  -7.126  10.268  0.60 16.21 ?  19  LYS   A HA   1 
ATOM   532  H HA   B LYS   A 1 19  ? 9.362  -6.791  10.989  0.40 16.72 ?  19  LYS   A HA   1 
ATOM   533  H HB2  A LYS   A 1 19  ? 10.845 -7.214  11.880  0.60 17.94 ?  19  LYS   A HB2  1 
ATOM   534  H HB2  B LYS   A 1 19  ? 11.187 -6.799  12.492  0.40 17.44 ?  19  LYS   A HB2  1 
ATOM   535  H HB3  A LYS   A 1 19  ? 11.545 -5.978  11.186  0.60 17.94 ?  19  LYS   A HB3  1 
ATOM   536  H HB3  B LYS   A 1 19  ? 11.807 -5.564  11.720  0.40 17.44 ?  19  LYS   A HB3  1 
ATOM   537  H HG2  A LYS   A 1 19  ? 9.757  -4.612  11.885  0.60 19.67 ?  19  LYS   A HG2  1 
ATOM   538  H HG2  B LYS   A 1 19  ? 10.031 -4.237  12.480  0.40 18.52 ?  19  LYS   A HG2  1 
ATOM   539  H HG3  A LYS   A 1 19  ? 9.143  -5.866  12.658  0.60 19.67 ?  19  LYS   A HG3  1 
ATOM   540  H HG3  B LYS   A 1 19  ? 9.480  -5.489  13.302  0.40 18.52 ?  19  LYS   A HG3  1 
ATOM   541  H HD2  A LYS   A 1 19  ? 11.093 -5.976  13.975  0.60 21.26 ?  19  LYS   A HD2  1 
ATOM   542  H HD2  B LYS   A 1 19  ? 11.457 -5.521  14.556  0.40 19.41 ?  19  LYS   A HD2  1 
ATOM   543  H HD3  A LYS   A 1 19  ? 11.652 -4.687  13.233  0.60 21.26 ?  19  LYS   A HD3  1 
ATOM   544  H HD3  B LYS   A 1 19  ? 11.987 -4.256  13.751  0.40 19.41 ?  19  LYS   A HD3  1 
ATOM   545  H HE2  A LYS   A 1 19  ? 9.944  -3.408  14.170  0.60 22.13 ?  19  LYS   A HE2  1 
ATOM   546  H HE2  B LYS   A 1 19  ? 10.386 -2.921  14.714  0.40 20.37 ?  19  LYS   A HE2  1 
ATOM   547  H HE3  A LYS   A 1 19  ? 9.394  -4.701  14.921  0.60 22.13 ?  19  LYS   A HE3  1 
ATOM   548  H HE3  B LYS   A 1 19  ? 9.709  -4.181  15.414  0.40 20.37 ?  19  LYS   A HE3  1 
ATOM   549  H HZ1  A LYS   A 1 19  ? 10.676 -3.529  16.355  0.60 22.71 ?  19  LYS   A HZ1  1 
ATOM   550  H HZ1  B LYS   A 1 19  ? 10.969 -3.191  16.958  0.40 20.96 ?  19  LYS   A HZ1  1 
ATOM   551  H HZ2  A LYS   A 1 19  ? 11.400 -4.750  16.062  0.60 22.71 ?  19  LYS   A HZ2  1 
ATOM   552  H HZ2  B LYS   A 1 19  ? 11.706 -4.387  16.606  0.40 20.96 ?  19  LYS   A HZ2  1 
ATOM   553  H HZ3  A LYS   A 1 19  ? 11.800 -3.504  15.442  0.60 22.71 ?  19  LYS   A HZ3  1 
ATOM   554  H HZ3  B LYS   A 1 19  ? 12.126 -3.100  16.093  0.40 20.96 ?  19  LYS   A HZ3  1 
ATOM   555  N N    A ASN   A 1 20  ? 8.618  -4.838  9.388   0.60 15.37 ?  20  ASN   A N    1 
ATOM   556  N N    B ASN   A 1 20  ? 8.784  -4.565  10.048  0.40 16.57 ?  20  ASN   A N    1 
ATOM   557  C CA   A ASN   A 1 20  ? 8.403  -3.495  8.852   0.60 17.09 ?  20  ASN   A CA   1 
ATOM   558  C CA   B ASN   A 1 20  ? 8.403  -3.353  9.320   0.40 18.77 ?  20  ASN   A CA   1 
ATOM   559  C C    A ASN   A 1 20  ? 9.019  -2.506  9.834   0.60 17.49 ?  20  ASN   A C    1 
ATOM   560  C C    B ASN   A 1 20  ? 8.953  -2.163  10.094  0.40 19.70 ?  20  ASN   A C    1 
ATOM   561  O O    A ASN   A 1 20  ? 8.493  -2.297  10.932  0.60 17.99 ?  20  ASN   A O    1 
ATOM   562  O O    B ASN   A 1 20  ? 8.322  -1.653  11.020  0.40 20.58 ?  20  ASN   A O    1 
ATOM   563  C CB   A ASN   A 1 20  ? 6.918  -3.208  8.636   0.60 18.34 ?  20  ASN   A CB   1 
ATOM   564  C CB   B ASN   A 1 20  ? 6.886  -3.288  9.170   0.40 20.01 ?  20  ASN   A CB   1 
ATOM   565  C CG   A ASN   A 1 20  ? 6.639  -1.726  8.363   0.60 19.67 ?  20  ASN   A CG   1 
ATOM   566  C CG   B ASN   A 1 20  ? 6.400  -2.017  8.473   0.40 21.45 ?  20  ASN   A CG   1 
ATOM   567  O OD1  A ASN   A 1 20  ? 5.808  -1.103  9.031   0.60 21.36 ?  20  ASN   A OD1  1 
ATOM   568  O OD1  B ASN   A 1 20  ? 5.268  -1.573  8.695   0.40 22.38 ?  20  ASN   A OD1  1 
ATOM   569  N ND2  A ASN   A 1 20  ? 7.349  -1.156  7.392   0.60 20.60 ?  20  ASN   A ND2  1 
ATOM   570  N ND2  B ASN   A 1 20  ? 7.242  -1.430  7.631   0.40 22.24 ?  20  ASN   A ND2  1 
ATOM   571  H H    A ASN   A 1 20  ? 7.934  -5.186  9.779   0.60 18.44 ?  20  ASN   A H    1 
ATOM   572  H H    B ASN   A 1 20  ? 8.191  -4.833  10.604  0.40 19.87 ?  20  ASN   A H    1 
ATOM   573  H HA   A ASN   A 1 20  ? 8.860  -3.420  8.000   0.60 20.50 ?  20  ASN   A HA   1 
ATOM   574  H HA   B ASN   A 1 20  ? 8.812  -3.367  8.440   0.40 22.52 ?  20  ASN   A HA   1 
ATOM   575  H HB2  A ASN   A 1 20  ? 6.606  -3.720  7.871   0.60 22.00 ?  20  ASN   A HB2  1 
ATOM   576  H HB2  B ASN   A 1 20  ? 6.589  -4.051  8.658   0.40 23.99 ?  20  ASN   A HB2  1 
ATOM   577  H HB3  A ASN   A 1 20  ? 6.429  -3.469  9.430   0.60 22.00 ?  20  ASN   A HB3  1 
ATOM   578  H HB3  B ASN   A 1 20  ? 6.488  -3.314  10.049  0.40 23.99 ?  20  ASN   A HB3  1 
ATOM   579  H HD21 A ASN   A 1 20  ? 7.231  -0.328  7.206   0.60 24.71 ?  20  ASN   A HD21 1 
ATOM   580  H HD21 B ASN   A 1 20  ? 7.002  -0.715  7.221   0.40 26.67 ?  20  ASN   A HD21 1 
ATOM   581  H HD22 A ASN   A 1 20  ? 7.925  -1.621  6.950   0.60 24.71 ?  20  ASN   A HD22 1 
ATOM   582  H HD22 B ASN   A 1 20  ? 8.023  -1.760  7.492   0.40 26.67 ?  20  ASN   A HD22 1 
ATOM   583  N N    A ALA   A 1 21  ? 10.148 -1.911  9.459   0.60 17.49 ?  21  ALA   A N    1 
ATOM   584  N N    B ALA   A 1 21  ? 10.153 -1.721  9.720   0.40 20.00 ?  21  ALA   A N    1 
ATOM   585  C CA   A ALA   A 1 21  ? 10.836 -1.025  10.385  0.60 17.14 ?  21  ALA   A CA   1 
ATOM   586  C CA   B ALA   A 1 21  ? 10.780 -0.589  10.389  0.40 20.25 ?  21  ALA   A CA   1 
ATOM   587  C C    A ALA   A 1 21  ? 11.786 -0.112  9.629   0.60 16.99 ?  21  ALA   A C    1 
ATOM   588  C C    B ALA   A 1 21  ? 11.882 -0.023  9.507   0.40 19.52 ?  21  ALA   A C    1 
ATOM   589  O O    A ALA   A 1 21  ? 12.219 -0.415  8.513   0.60 17.20 ?  21  ALA   A O    1 
ATOM   590  O O    B ALA   A 1 21  ? 12.425 -0.709  8.637   0.40 19.38 ?  21  ALA   A O    1 
ATOM   591  C CB   A ALA   A 1 21  ? 11.597 -1.812  11.455  0.60 17.85 ?  21  ALA   A CB   1 
ATOM   592  C CB   B ALA   A 1 21  ? 11.354 -0.987  11.753  0.40 21.20 ?  21  ALA   A CB   1 
ATOM   593  H H    A ALA   A 1 21  ? 10.523 -2.003  8.690   0.60 20.98 ?  21  ALA   A H    1 
ATOM   594  H H    B ALA   A 1 21  ? 10.624 -2.062  9.086   0.40 23.99 ?  21  ALA   A H    1 
ATOM   595  H HA   A ALA   A 1 21  ? 10.174 -0.471  10.832  0.60 20.55 ?  21  ALA   A HA   1 
ATOM   596  H HA   B ALA   A 1 21  ? 10.117 0.104   10.530  0.40 24.28 ?  21  ALA   A HA   1 
ATOM   597  H HB1  A ALA   A 1 21  ? 12.026 -1.186  12.054  0.60 21.40 ?  21  ALA   A HB1  1 
ATOM   598  H HB1  B ALA   A 1 21  ? 11.764 -0.207  12.162  0.40 25.43 ?  21  ALA   A HB1  1 
ATOM   599  H HB2  A ALA   A 1 21  ? 10.965 -2.364  11.946  0.60 21.40 ?  21  ALA   A HB2  1 
ATOM   600  H HB2  B ALA   A 1 21  ? 10.635 -1.315  12.314  0.40 25.43 ?  21  ALA   A HB2  1 
ATOM   601  H HB3  A ALA   A 1 21  ? 12.257 -2.371  11.021  0.60 21.40 ?  21  ALA   A HB3  1 
ATOM   602  H HB3  B ALA   A 1 21  ? 12.020 -1.681  11.625  0.40 25.43 ?  21  ALA   A HB3  1 
ATOM   603  N N    A ASP   A 1 22  ? 12.090 1.021   10.264  0.60 16.92 ?  22  ASP   A N    1 
ATOM   604  N N    B ASP   A 1 22  ? 12.188 1.253   9.738   0.40 19.12 ?  22  ASP   A N    1 
ATOM   605  C CA   A ASP   A 1 22  ? 13.099 1.962   9.792   0.60 16.71 ?  22  ASP   A CA   1 
ATOM   606  C CA   B ASP   A 1 22  ? 13.378 1.867   9.167   0.40 18.80 ?  22  ASP   A CA   1 
ATOM   607  C C    A ASP   A 1 22  ? 14.444 1.485   10.328  0.60 15.74 ?  22  ASP   A C    1 
ATOM   608  C C    B ASP   A 1 22  ? 14.608 1.280   9.850   0.40 17.14 ?  22  ASP   A C    1 
ATOM   609  O O    A ASP   A 1 22  ? 14.666 1.467   11.543  0.60 16.28 ?  22  ASP   A O    1 
ATOM   610  O O    B ASP   A 1 22  ? 14.679 1.221   11.081  0.40 17.20 ?  22  ASP   A O    1 
ATOM   611  C CB   A ASP   A 1 22  ? 12.764 3.359   10.311  0.60 18.25 ?  22  ASP   A CB   1 
ATOM   612  C CB   B ASP   A 1 22  ? 13.322 3.380   9.394   0.40 20.31 ?  22  ASP   A CB   1 
ATOM   613  C CG   A ASP   A 1 22  ? 13.754 4.420   9.850   0.60 19.89 ?  22  ASP   A CG   1 
ATOM   614  C CG   B ASP   A 1 22  ? 14.498 4.124   8.781   0.40 21.56 ?  22  ASP   A CG   1 
ATOM   615  O OD1  A ASP   A 1 22  ? 14.830 4.081   9.323   0.60 19.83 ?  22  ASP   A OD1  1 
ATOM   616  O OD1  B ASP   A 1 22  ? 15.383 3.481   8.179   0.40 21.92 ?  22  ASP   A OD1  1 
ATOM   617  O OD2  A ASP   A 1 22  ? 13.453 5.618   10.028  0.60 21.63 -1 22  ASP   A OD2  1 
ATOM   618  O OD2  B ASP   A 1 22  ? 14.530 5.368   8.905   0.40 22.10 -1 22  ASP   A OD2  1 
ATOM   619  H H    A ASP   A 1 22  ? 11.701 1.273   10.991  0.60 20.29 ?  22  ASP   A H    1 
ATOM   620  H H    B ASP   A 1 22  ? 11.713 1.787   10.219  0.40 22.94 ?  22  ASP   A H    1 
ATOM   621  H HA   A ASP   A 1 22  ? 13.117 1.971   8.819   0.60 20.04 ?  22  ASP   A HA   1 
ATOM   622  H HA   B ASP   A 1 22  ? 13.422 1.688   8.211   0.40 22.55 ?  22  ASP   A HA   1 
ATOM   623  H HB2  A ASP   A 1 22  ? 11.876 3.608   10.004  0.60 21.89 ?  22  ASP   A HB2  1 
ATOM   624  H HB2  B ASP   A 1 22  ? 12.513 3.733   8.997   0.40 24.36 ?  22  ASP   A HB2  1 
ATOM   625  H HB3  A ASP   A 1 22  ? 12.782 3.343   11.282  0.60 21.89 ?  22  ASP   A HB3  1 
ATOM   626  H HB3  B ASP   A 1 22  ? 13.330 3.555   10.346  0.40 24.36 ?  22  ASP   A HB3  1 
ATOM   627  N N    A ILE   A 1 23  ? 15.341 1.092   9.420   0.60 15.06 ?  23  ILE   A N    1 
ATOM   628  N N    B ILE   A 1 23  ? 15.575 0.830   9.047   0.40 15.90 ?  23  ILE   A N    1 
ATOM   629  C CA   A ILE   A 1 23  ? 16.607 0.489   9.828   0.60 14.65 ?  23  ILE   A CA   1 
ATOM   630  C CA   B ILE   A 1 23  ? 16.770 0.198   9.598   0.40 15.07 ?  23  ILE   A CA   1 
ATOM   631  C C    A ILE   A 1 23  ? 17.430 1.441   10.687  0.60 14.61 ?  23  ILE   A C    1 
ATOM   632  C C    B ILE   A 1 23  ? 17.516 1.157   10.512  0.40 15.11 ?  23  ILE   A C    1 
ATOM   633  O O    A ILE   A 1 23  ? 18.192 0.999   11.556  0.60 15.15 ?  23  ILE   A O    1 
ATOM   634  O O    B ILE   A 1 23  ? 18.155 0.733   11.483  0.40 15.16 ?  23  ILE   A O    1 
ATOM   635  C CB   A ILE   A 1 23  ? 17.372 -0.014  8.588   0.60 14.01 ?  23  ILE   A CB   1 
ATOM   636  C CB   B ILE   A 1 23  ? 17.670 -0.358  8.475   0.40 14.38 ?  23  ILE   A CB   1 
ATOM   637  C CG1  A ILE   A 1 23  ? 18.557 -0.888  9.002   0.60 13.87 ?  23  ILE   A CG1  1 
ATOM   638  C CG1  B ILE   A 1 23  ? 18.753 -1.253  9.079   0.40 14.27 ?  23  ILE   A CG1  1 
ATOM   639  C CG2  A ILE   A 1 23  ? 17.806 1.157   7.710   0.60 13.85 ?  23  ILE   A CG2  1 
ATOM   640  C CG2  B ILE   A 1 23  ? 18.293 0.773   7.651   0.40 13.96 ?  23  ILE   A CG2  1 
ATOM   641  C CD1  A ILE   A 1 23  ? 19.207 -1.611  7.841   0.60 13.88 ?  23  ILE   A CD1  1 
ATOM   642  C CD1  B ILE   A 1 23  ? 19.646 -1.897  8.064   0.40 14.48 ?  23  ILE   A CD1  1 
ATOM   643  H H    A ILE   A 1 23  ? 15.232 1.161   8.574   0.60 18.06 ?  23  ILE   A H    1 
ATOM   644  H H    B ILE   A 1 23  ? 15.566 0.880   8.200   0.40 19.07 ?  23  ILE   A H    1 
ATOM   645  H HA   A ILE   A 1 23  ? 16.409 -0.281  10.377  0.60 17.57 ?  23  ILE   A HA   1 
ATOM   646  H HA   B ILE   A 1 23  ? 16.493 -0.554  10.138  0.40 18.07 ?  23  ILE   A HA   1 
ATOM   647  H HB   A ILE   A 1 23  ? 16.764 -0.559  8.072   0.60 16.80 ?  23  ILE   A HB   1 
ATOM   648  H HB   B ILE   A 1 23  ? 17.124 -0.900  7.884   0.40 17.25 ?  23  ILE   A HB   1 
ATOM   649  H HG12 A ILE   A 1 23  ? 19.231 -0.328  9.419   0.60 16.63 ?  23  ILE   A HG12 1 
ATOM   650  H HG12 B ILE   A 1 23  ? 19.310 -0.720  9.665   0.40 17.11 ?  23  ILE   A HG12 1 
ATOM   651  H HG13 A ILE   A 1 23  ? 18.246 -1.556  9.633   0.60 16.63 ?  23  ILE   A HG13 1 
ATOM   652  H HG13 B ILE   A 1 23  ? 18.325 -1.961  9.585   0.40 17.11 ?  23  ILE   A HG13 1 
ATOM   653  H HG21 A ILE   A 1 23  ? 18.155 0.813   6.874   0.60 16.61 ?  23  ILE   A HG21 1 
ATOM   654  H HG21 B ILE   A 1 23  ? 18.688 0.396   6.845   0.40 16.74 ?  23  ILE   A HG21 1 
ATOM   655  H HG22 A ILE   A 1 23  ? 17.034 1.724   7.534   0.60 16.61 ?  23  ILE   A HG22 1 
ATOM   656  H HG22 B ILE   A 1 23  ? 17.603 1.408   7.413   0.40 16.74 ?  23  ILE   A HG22 1 
ATOM   657  H HG23 A ILE   A 1 23  ? 18.488 1.669   8.170   0.60 16.61 ?  23  ILE   A HG23 1 
ATOM   658  H HG23 B ILE   A 1 23  ? 18.980 1.209   8.179   0.40 16.74 ?  23  ILE   A HG23 1 
ATOM   659  H HD11 A ILE   A 1 23  ? 19.897 -2.196  8.183   0.60 16.65 ?  23  ILE   A HD11 1 
ATOM   660  H HD11 B ILE   A 1 23  ? 20.215 -2.543  8.512   0.40 17.36 ?  23  ILE   A HD11 1 
ATOM   661  H HD12 A ILE   A 1 23  ? 18.529 -2.129  7.378   0.60 16.65 ?  23  ILE   A HD12 1 
ATOM   662  H HD12 B ILE   A 1 23  ? 19.095 -2.340  7.404   0.40 17.36 ?  23  ILE   A HD12 1 
ATOM   663  H HD13 A ILE   A 1 23  ? 19.591 -0.955  7.239   0.60 16.65 ?  23  ILE   A HD13 1 
ATOM   664  H HD13 B ILE   A 1 23  ? 20.190 -1.213  7.642   0.40 17.36 ?  23  ILE   A HD13 1 
ATOM   665  N N    A VAL   A 1 24  ? 17.285 2.753   10.478  0.60 15.24 ?  24  VAL   A N    1 
ATOM   666  N N    B VAL   A 1 24  ? 17.444 2.458   10.227  0.40 16.23 ?  24  VAL   A N    1 
ATOM   667  C CA   A VAL   A 1 24  ? 17.984 3.719   11.325  0.60 16.57 ?  24  VAL   A CA   1 
ATOM   668  C CA   B VAL   A 1 24  ? 18.098 3.447   11.078  0.40 17.27 ?  24  VAL   A CA   1 
ATOM   669  C C    A VAL   A 1 24  ? 17.505 3.599   12.767  0.60 17.40 ?  24  VAL   A C    1 
ATOM   670  C C    B VAL   A 1 24  ? 17.486 3.426   12.473  0.40 18.17 ?  24  VAL   A C    1 
ATOM   671  O O    A VAL   A 1 24  ? 18.308 3.523   13.706  0.60 17.32 ?  24  VAL   A O    1 
ATOM   672  O O    B VAL   A 1 24  ? 18.196 3.372   13.484  0.40 18.32 ?  24  VAL   A O    1 
ATOM   673  C CB   A VAL   A 1 24  ? 17.795 5.147   10.778  0.60 16.92 ?  24  VAL   A CB   1 
ATOM   674  C CB   B VAL   A 1 24  ? 18.010 4.841   10.432  0.40 18.01 ?  24  VAL   A CB   1 
ATOM   675  C CG1  A VAL   A 1 24  ? 18.310 6.185   11.774  0.60 17.32 ?  24  VAL   A CG1  1 
ATOM   676  C CG1  B VAL   A 1 24  ? 18.589 5.895   11.357  0.40 18.78 ?  24  VAL   A CG1  1 
ATOM   677  C CG2  A VAL   A 1 24  ? 18.490 5.295   9.432   0.60 17.80 ?  24  VAL   A CG2  1 
ATOM   678  C CG2  B VAL   A 1 24  ? 18.724 4.840   9.090   0.40 18.05 ?  24  VAL   A CG2  1 
ATOM   679  H H    A VAL   A 1 24  ? 16.798 3.106   9.864   0.60 18.27 ?  24  VAL   A H    1 
ATOM   680  H H    B VAL   A 1 24  ? 17.022 2.791   9.557   0.40 19.47 ?  24  VAL   A H    1 
ATOM   681  H HA   A VAL   A 1 24  ? 18.933 3.525   11.310  0.60 19.87 ?  24  VAL   A HA   1 
ATOM   682  H HA   B VAL   A 1 24  ? 19.036 3.221   11.163  0.40 20.71 ?  24  VAL   A HA   1 
ATOM   683  H HB   A VAL   A 1 24  ? 16.848 5.313   10.641  0.60 20.29 ?  24  VAL   A HB   1 
ATOM   684  H HB   B VAL   A 1 24  ? 17.078 5.060   10.274  0.40 21.60 ?  24  VAL   A HB   1 
ATOM   685  H HG11 A VAL   A 1 24  ? 18.450 7.025   11.308  0.60 20.77 ?  24  VAL   A HG11 1 
ATOM   686  H HG11 B VAL   A 1 24  ? 18.789 6.689   10.840  0.40 22.52 ?  24  VAL   A HG11 1 
ATOM   687  H HG12 A VAL   A 1 24  ? 17.654 6.303   12.476  0.60 20.77 ?  24  VAL   A HG12 1 
ATOM   688  H HG12 B VAL   A 1 24  ? 17.935 6.103   12.042  0.40 22.52 ?  24  VAL   A HG12 1 
ATOM   689  H HG13 A VAL   A 1 24  ? 19.150 5.873   12.146  0.60 20.77 ?  24  VAL   A HG13 1 
ATOM   690  H HG13 B VAL   A 1 24  ? 19.399 5.549   11.762  0.40 22.52 ?  24  VAL   A HG13 1 
ATOM   691  H HG21 A VAL   A 1 24  ? 18.261 6.158   9.050   0.60 21.35 ?  24  VAL   A HG21 1 
ATOM   692  H HG21 B VAL   A 1 24  ? 18.666 5.725   8.700   0.40 21.65 ?  24  VAL   A HG21 1 
ATOM   693  H HG22 A VAL   A 1 24  ? 19.449 5.238   9.564   0.60 21.35 ?  24  VAL   A HG22 1 
ATOM   694  H HG22 B VAL   A 1 24  ? 19.654 4.601   9.229   0.40 21.65 ?  24  VAL   A HG22 1 
ATOM   695  H HG23 A VAL   A 1 24  ? 18.192 4.585   8.842   0.60 21.35 ?  24  VAL   A HG23 1 
ATOM   696  H HG23 B VAL   A 1 24  ? 18.301 4.192   8.505   0.40 21.65 ?  24  VAL   A HG23 1 
ATOM   697  N N    A GLU   A 1 25  ? 16.186 3.577   12.961  0.60 18.65 ?  25  GLU   A N    1 
ATOM   698  N N    B GLU   A 1 25  ? 16.154 3.455   12.546  0.40 19.15 ?  25  GLU   A N    1 
ATOM   699  C CA   A GLU   A 1 25  ? 15.638 3.499   14.311  0.60 20.39 ?  25  GLU   A CA   1 
ATOM   700  C CA   B GLU   A 1 25  ? 15.484 3.398   13.841  0.40 20.59 ?  25  GLU   A CA   1 
ATOM   701  C C    A GLU   A 1 25  ? 15.891 2.131   14.935  0.60 19.67 ?  25  GLU   A C    1 
ATOM   702  C C    B GLU   A 1 25  ? 15.714 2.056   14.526  0.40 20.27 ?  25  GLU   A C    1 
ATOM   703  O O    A GLU   A 1 25  ? 16.163 2.035   16.138  0.60 20.08 ?  25  GLU   A O    1 
ATOM   704  O O    B GLU   A 1 25  ? 15.867 1.998   15.751  0.40 20.61 ?  25  GLU   A O    1 
ATOM   705  C CB   A GLU   A 1 25  ? 14.148 3.845   14.287  0.60 22.79 ?  25  GLU   A CB   1 
ATOM   706  C CB   B GLU   A 1 25  ? 13.991 3.678   13.668  0.40 22.63 ?  25  GLU   A CB   1 
ATOM   707  C CG   A GLU   A 1 25  ? 13.883 5.282   13.857  0.60 25.03 ?  25  GLU   A CG   1 
ATOM   708  C CG   B GLU   A 1 25  ? 13.694 5.096   13.211  0.40 24.95 ?  25  GLU   A CG   1 
ATOM   709  C CD   A GLU   A 1 25  ? 14.645 6.289   14.707  0.60 27.26 ?  25  GLU   A CD   1 
ATOM   710  C CD   B GLU   A 1 25  ? 14.202 6.137   14.181  0.40 26.95 ?  25  GLU   A CD   1 
ATOM   711  O OE1  A GLU   A 1 25  ? 14.624 6.154   15.949  0.60 28.02 ?  25  GLU   A OE1  1 
ATOM   712  O OE1  B GLU   A 1 25  ? 14.152 5.882   15.404  0.40 27.82 ?  25  GLU   A OE1  1 
ATOM   713  O OE2  A GLU   A 1 25  ? 15.283 7.197   14.134  0.60 28.22 -1 25  GLU   A OE2  1 
ATOM   714  O OE2  B GLU   A 1 25  ? 14.657 7.205   13.721  0.40 27.72 -1 25  GLU   A OE2  1 
ATOM   715  H H    A GLU   A 1 25  ? 15.598 3.616   12.336  0.60 22.37 ?  25  GLU   A H    1 
ATOM   716  H H    B GLU   A 1 25  ? 15.626 3.512   11.871  0.40 22.97 ?  25  GLU   A H    1 
ATOM   717  H HA   A GLU   A 1 25  ? 16.084 4.152   14.868  0.60 24.46 ?  25  GLU   A HA   1 
ATOM   718  H HA   B GLU   A 1 25  ? 15.854 4.085   14.413  0.40 24.70 ?  25  GLU   A HA   1 
ATOM   719  H HB2  A GLU   A 1 25  ? 13.693 3.260   13.660  0.60 27.33 ?  25  GLU   A HB2  1 
ATOM   720  H HB2  B GLU   A 1 25  ? 13.630 3.071   13.003  0.40 27.14 ?  25  GLU   A HB2  1 
ATOM   721  H HB3  A GLU   A 1 25  ? 13.778 3.731   15.176  0.60 27.33 ?  25  GLU   A HB3  1 
ATOM   722  H HB3  B GLU   A 1 25  ? 13.545 3.540   14.518  0.40 27.14 ?  25  GLU   A HB3  1 
ATOM   723  H HG2  A GLU   A 1 25  ? 14.165 5.394   12.935  0.60 30.02 ?  25  GLU   A HG2  1 
ATOM   724  H HG2  B GLU   A 1 25  ? 14.121 5.250   12.354  0.40 29.93 ?  25  GLU   A HG2  1 
ATOM   725  H HG3  A GLU   A 1 25  ? 12.929 5.464   13.934  0.60 30.02 ?  25  GLU   A HG3  1 
ATOM   726  H HG3  B GLU   A 1 25  ? 12.736 5.214   13.134  0.40 29.93 ?  25  GLU   A HG3  1 
ATOM   727  N N    A GLU   A 1 26  ? 15.838 1.065   14.133  0.60 19.04 ?  26  GLU   A N    1 
ATOM   728  N N    B GLU   A 1 26  ? 15.744 0.966   13.755  0.40 19.74 ?  26  GLU   A N    1 
ATOM   729  C CA   A GLU   A 1 26  ? 16.142 -0.266  14.652  0.60 19.15 ?  26  GLU   A CA   1 
ATOM   730  C CA   B GLU   A 1 26  ? 16.047 -0.338  14.338  0.40 19.45 ?  26  GLU   A CA   1 
ATOM   731  C C    A GLU   A 1 26  ? 17.577 -0.342  15.155  0.60 17.61 ?  26  GLU   A C    1 
ATOM   732  C C    B GLU   A 1 26  ? 17.464 -0.377  14.897  0.40 18.72 ?  26  GLU   A C    1 
ATOM   733  O O    A GLU   A 1 26  ? 17.844 -0.885  16.233  0.60 17.35 ?  26  GLU   A O    1 
ATOM   734  O O    B GLU   A 1 26  ? 17.697 -0.923  15.981  0.40 18.85 ?  26  GLU   A O    1 
ATOM   735  C CB   A GLU   A 1 26  ? 15.917 -1.317  13.567  0.60 21.25 ?  26  GLU   A CB   1 
ATOM   736  C CB   B GLU   A 1 26  ? 15.856 -1.445  13.298  0.40 19.95 ?  26  GLU   A CB   1 
ATOM   737  C CG   A GLU   A 1 26  ? 14.483 -1.702  13.343  0.60 23.79 ?  26  GLU   A CG   1 
ATOM   738  C CG   B GLU   A 1 26  ? 14.526 -2.182  13.380  0.40 20.37 ?  26  GLU   A CG   1 
ATOM   739  C CD   A GLU   A 1 26  ? 13.934 -2.541  14.465  0.60 25.32 ?  26  GLU   A CD   1 
ATOM   740  C CD   B GLU   A 1 26  ? 14.265 -2.822  14.736  0.40 19.91 ?  26  GLU   A CD   1 
ATOM   741  O OE1  A GLU   A 1 26  ? 14.555 -3.565  14.823  0.60 26.55 ?  26  GLU   A OE1  1 
ATOM   742  O OE1  B GLU   A 1 26  ? 14.595 -4.021  14.950  0.40 19.80 ?  26  GLU   A OE1  1 
ATOM   743  O OE2  A GLU   A 1 26  ? 12.889 -2.147  15.005  0.60 25.63 -1 26  GLU   A OE2  1 
ATOM   744  O OE2  B GLU   A 1 26  ? 13.709 -2.120  15.591  0.40 19.74 -1 26  GLU   A OE2  1 
ATOM   745  H H    A GLU   A 1 26  ? 15.650 1.088   13.293  0.60 22.83 ?  26  GLU   A H    1 
ATOM   746  H H    B GLU   A 1 26  ? 15.592 0.958   12.910  0.40 23.67 ?  26  GLU   A H    1 
ATOM   747  H HA   A GLU   A 1 26  ? 15.554 -0.457  15.396  0.60 22.96 ?  26  GLU   A HA   1 
ATOM   748  H HA   B GLU   A 1 26  ? 15.439 -0.493  15.073  0.40 23.32 ?  26  GLU   A HA   1 
ATOM   749  H HB2  A GLU   A 1 26  ? 16.260 -0.977  12.730  0.60 25.49 ?  26  GLU   A HB2  1 
ATOM   750  H HB2  B GLU   A 1 26  ? 15.918 -1.052  12.410  0.40 23.92 ?  26  GLU   A HB2  1 
ATOM   751  H HB3  A GLU   A 1 26  ? 16.404 -2.121  13.817  0.60 25.49 ?  26  GLU   A HB3  1 
ATOM   752  H HB3  B GLU   A 1 26  ? 16.558 -2.102  13.410  0.40 23.92 ?  26  GLU   A HB3  1 
ATOM   753  H HG2  A GLU   A 1 26  ? 13.935 -0.908  13.317  0.60 28.54 ?  26  GLU   A HG2  1 
ATOM   754  H HG2  B GLU   A 1 26  ? 13.812 -1.556  13.146  0.40 24.43 ?  26  GLU   A HG2  1 
ATOM   755  H HG3  A GLU   A 1 26  ? 14.408 -2.189  12.506  0.60 28.54 ?  26  GLU   A HG3  1 
ATOM   756  H HG3  B GLU   A 1 26  ? 14.532 -2.922  12.771  0.40 24.43 ?  26  GLU   A HG3  1 
ATOM   757  N N    A ALA   A 1 27  ? 18.522 0.188   14.377  0.60 16.38 ?  27  ALA   A N    1 
ATOM   758  N N    B ALA   A 1 27  ? 18.427 0.194   14.170  0.40 17.92 ?  27  ALA   A N    1 
ATOM   759  C CA   A ALA   A 1 27  ? 19.922 0.138   14.787  0.60 16.34 ?  27  ALA   A CA   1 
ATOM   760  C CA   B ALA   A 1 27  ? 19.806 0.187   14.649  0.40 17.93 ?  27  ALA   A CA   1 
ATOM   761  C C    A ALA   A 1 27  ? 20.140 0.937   16.064  0.60 17.54 ?  27  ALA   A C    1 
ATOM   762  C C    B ALA   A 1 27  ? 19.945 0.994   15.933  0.40 19.31 ?  27  ALA   A C    1 
ATOM   763  O O    A ALA   A 1 27  ? 20.800 0.468   16.998  0.60 17.76 ?  27  ALA   A O    1 
ATOM   764  O O    B ALA   A 1 27  ? 20.660 0.586   16.856  0.40 19.28 ?  27  ALA   A O    1 
ATOM   765  C CB   A ALA   A 1 27  ? 20.822 0.651   13.660  0.60 16.06 ?  27  ALA   A CB   1 
ATOM   766  C CB   B ALA   A 1 27  ? 20.746 0.718   13.566  0.40 17.24 ?  27  ALA   A CB   1 
ATOM   767  H H    A ALA   A 1 27  ? 18.385 0.579   13.624  0.60 19.65 ?  27  ALA   A H    1 
ATOM   768  H H    B ALA   A 1 27  ? 18.308 0.585   13.414  0.40 21.49 ?  27  ALA   A H    1 
ATOM   769  H HA   A ALA   A 1 27  ? 20.167 -0.780  14.967  0.60 19.60 ?  27  ALA   A HA   1 
ATOM   770  H HA   B ALA   A 1 27  ? 20.064 -0.724  14.845  0.40 21.50 ?  27  ALA   A HA   1 
ATOM   771  H HB1  A ALA   A 1 27  ? 21.751 0.609   13.951  0.60 19.27 ?  27  ALA   A HB1  1 
ATOM   772  H HB1  B ALA   A 1 27  ? 21.656 0.705   13.905  0.40 20.68 ?  27  ALA   A HB1  1 
ATOM   773  H HB2  A ALA   A 1 27  ? 20.701 0.089   12.878  0.60 19.27 ?  27  ALA   A HB2  1 
ATOM   774  H HB2  B ALA   A 1 27  ? 20.678 0.148   12.784  0.40 20.68 ?  27  ALA   A HB2  1 
ATOM   775  H HB3  A ALA   A 1 27  ? 20.586 1.566   13.451  0.60 19.27 ?  27  ALA   A HB3  1 
ATOM   776  H HB3  B ALA   A 1 27  ? 20.490 1.624   13.339  0.40 20.68 ?  27  ALA   A HB3  1 
ATOM   777  N N    A LYS   A 1 28  ? 19.577 2.145   16.130  0.60 19.31 ?  28  LYS   A N    1 
ATOM   778  N N    B LYS   A 1 28  ? 19.262 2.138   16.017  0.40 21.01 ?  28  LYS   A N    1 
ATOM   779  C CA   A LYS   A 1 28  ? 19.740 2.970   17.324  0.60 22.10 ?  28  LYS   A CA   1 
ATOM   780  C CA   B LYS   A 1 28  ? 19.314 2.936   17.238  0.40 23.29 ?  28  LYS   A CA   1 
ATOM   781  C C    A LYS   A 1 28  ? 19.207 2.257   18.561  0.60 22.85 ?  28  LYS   A C    1 
ATOM   782  C C    B LYS   A 1 28  ? 18.704 2.205   18.426  0.40 24.69 ?  28  LYS   A C    1 
ATOM   783  O O    A LYS   A 1 28  ? 19.798 2.348   19.643  0.60 24.14 ?  28  LYS   A O    1 
ATOM   784  O O    B LYS   A 1 28  ? 19.044 2.518   19.572  0.40 25.24 ?  28  LYS   A O    1 
ATOM   785  C CB   A LYS   A 1 28  ? 19.057 4.328   17.127  0.60 24.50 ?  28  LYS   A CB   1 
ATOM   786  C CB   B LYS   A 1 28  ? 18.610 4.278   17.029  0.40 24.38 ?  28  LYS   A CB   1 
ATOM   787  C CG   A LYS   A 1 28  ? 19.832 5.280   16.222  0.60 26.47 ?  28  LYS   A CG   1 
ATOM   788  C CG   B LYS   A 1 28  ? 19.377 5.223   16.122  0.40 25.65 ?  28  LYS   A CG   1 
ATOM   789  C CD   A LYS   A 1 28  ? 19.325 6.714   16.315  0.60 28.69 ?  28  LYS   A CD   1 
ATOM   790  C CD   B LYS   A 1 28  ? 18.821 6.637   16.159  0.40 27.41 ?  28  LYS   A CD   1 
ATOM   791  C CE   A LYS   A 1 28  ? 17.999 6.891   15.597  0.60 30.07 ?  28  LYS   A CE   1 
ATOM   792  C CE   B LYS   A 1 28  ? 17.933 6.918   14.962  0.40 28.76 ?  28  LYS   A CE   1 
ATOM   793  N NZ   A LYS   A 1 28  ? 17.581 8.320   15.559  0.60 30.99 ?  28  LYS   A NZ   1 
ATOM   794  N NZ   B LYS   A 1 28  ? 17.781 8.379   14.719  0.40 29.48 ?  28  LYS   A NZ   1 
ATOM   795  H H    A LYS   A 1 28  ? 19.102 2.499   15.512  0.60 23.16 ?  28  LYS   A H    1 
ATOM   796  H H    B LYS   A 1 28  ? 18.768 2.466   15.395  0.40 25.20 ?  28  LYS   A H    1 
ATOM   797  H HA   A LYS   A 1 28  ? 20.683 3.138   17.469  0.60 26.51 ?  28  LYS   A HA   1 
ATOM   798  H HA   B LYS   A 1 28  ? 20.240 3.122   17.448  0.40 27.93 ?  28  LYS   A HA   1 
ATOM   799  H HB2  A LYS   A 1 28  ? 18.186 4.189   16.726  0.60 29.39 ?  28  LYS   A HB2  1 
ATOM   800  H HB2  B LYS   A 1 28  ? 17.741 4.120   16.630  0.40 29.24 ?  28  LYS   A HB2  1 
ATOM   801  H HB3  A LYS   A 1 28  ? 18.957 4.762   17.989  0.60 29.39 ?  28  LYS   A HB3  1 
ATOM   802  H HB3  B LYS   A 1 28  ? 18.503 4.713   17.891  0.40 29.24 ?  28  LYS   A HB3  1 
ATOM   803  H HG2  A LYS   A 1 28  ? 20.766 5.277   16.480  0.60 31.75 ?  28  LYS   A HG2  1 
ATOM   804  H HG2  B LYS   A 1 28  ? 20.302 5.256   16.409  0.40 30.77 ?  28  LYS   A HG2  1 
ATOM   805  H HG3  A LYS   A 1 28  ? 19.739 4.991   15.301  0.60 31.75 ?  28  LYS   A HG3  1 
ATOM   806  H HG3  B LYS   A 1 28  ? 19.324 4.896   15.210  0.40 30.77 ?  28  LYS   A HG3  1 
ATOM   807  H HD2  A LYS   A 1 28  ? 19.196 6.949   17.248  0.60 34.42 ?  28  LYS   A HD2  1 
ATOM   808  H HD2  B LYS   A 1 28  ? 18.293 6.754   16.966  0.40 32.89 ?  28  LYS   A HD2  1 
ATOM   809  H HD3  A LYS   A 1 28  ? 19.972 7.310   15.906  0.60 34.42 ?  28  LYS   A HD3  1 
ATOM   810  H HD3  B LYS   A 1 28  ? 19.557 7.269   16.147  0.40 32.89 ?  28  LYS   A HD3  1 
ATOM   811  H HE2  A LYS   A 1 28  ? 18.087 6.576   14.683  0.60 36.08 ?  28  LYS   A HE2  1 
ATOM   812  H HE2  B LYS   A 1 28  ? 18.327 6.521   14.171  0.40 34.49 ?  28  LYS   A HE2  1 
ATOM   813  H HE3  A LYS   A 1 28  ? 17.313 6.387   16.061  0.60 36.08 ?  28  LYS   A HE3  1 
ATOM   814  H HE3  B LYS   A 1 28  ? 17.053 6.542   15.123  0.40 34.49 ?  28  LYS   A HE3  1 
ATOM   815  H HZ1  A LYS   A 1 28  ? 16.804 8.400   15.133  0.60 37.18 ?  28  LYS   A HZ1  1 
ATOM   816  H HZ1  B LYS   A 1 28  ? 17.258 8.517   14.013  0.40 35.37 ?  28  LYS   A HZ1  1 
ATOM   817  H HZ2  A LYS   A 1 28  ? 17.491 8.633   16.386  0.60 37.18 ?  28  LYS   A HZ2  1 
ATOM   818  H HZ2  B LYS   A 1 28  ? 17.418 8.770   15.431  0.40 35.37 ?  28  LYS   A HZ2  1 
ATOM   819  H HZ3  A LYS   A 1 28  ? 18.195 8.805   15.132  0.60 37.18 ?  28  LYS   A HZ3  1 
ATOM   820  H HZ3  B LYS   A 1 28  ? 18.578 8.745   14.564  0.40 35.37 ?  28  LYS   A HZ3  1 
ATOM   821  N N    A LYS   A 1 29  ? 18.104 1.521   18.415  0.60 23.27 ?  29  LYS   A N    1 
ATOM   822  N N    B LYS   A 1 29  ? 17.815 1.242   18.181  0.40 25.91 ?  29  LYS   A N    1 
ATOM   823  C CA   A LYS   A 1 29  ? 17.510 0.820   19.550  0.60 25.09 ?  29  LYS   A CA   1 
ATOM   824  C CA   B LYS   A 1 29  ? 17.204 0.493   19.273  0.40 27.34 ?  29  LYS   A CA   1 
ATOM   825  C C    A LYS   A 1 29  ? 18.329 -0.410  19.930  0.60 24.29 ?  29  LYS   A C    1 
ATOM   826  C C    B LYS   A 1 29  ? 18.088 -0.669  19.715  0.40 26.54 ?  29  LYS   A C    1 
ATOM   827  O O    A LYS   A 1 29  ? 18.662 -0.611  21.106  0.60 25.01 ?  29  LYS   A O    1 
ATOM   828  O O    B LYS   A 1 29  ? 18.306 -0.874  20.915  0.40 26.71 ?  29  LYS   A O    1 
ATOM   829  C CB   A LYS   A 1 29  ? 16.077 0.416   19.198  0.60 27.75 ?  29  LYS   A CB   1 
ATOM   830  C CB   B LYS   A 1 29  ? 15.826 -0.022  18.844  0.40 29.51 ?  29  LYS   A CB   1 
ATOM   831  C CG   A LYS   A 1 29  ? 15.326 -0.296  20.312  0.60 30.53 ?  29  LYS   A CG   1 
ATOM   832  C CG   B LYS   A 1 29  ? 14.720 0.210   19.867  0.40 31.71 ?  29  LYS   A CG   1 
ATOM   833  C CD   A LYS   A 1 29  ? 14.848 0.683   21.370  0.60 33.11 ?  29  LYS   A CD   1 
ATOM   834  C CD   B LYS   A 1 29  ? 15.075 -0.369  21.228  0.40 33.50 ?  29  LYS   A CD   1 
ATOM   835  C CE   A LYS   A 1 29  ? 13.943 0.002   22.385  0.60 34.87 ?  29  LYS   A CE   1 
ATOM   836  C CE   B LYS   A 1 29  ? 14.606 0.541   22.344  0.40 34.81 ?  29  LYS   A CE   1 
ATOM   837  N NZ   A LYS   A 1 29  ? 13.421 0.965   23.393  0.60 35.90 ?  29  LYS   A NZ   1 
ATOM   838  N NZ   B LYS   A 1 29  ? 15.003 0.015   23.675  0.40 35.44 ?  29  LYS   A NZ   1 
ATOM   839  H H    A LYS   A 1 29  ? 17.689 1.414   17.673  0.60 27.92 ?  29  LYS   A H    1 
ATOM   840  H H    B LYS   A 1 29  ? 17.545 1.013   17.397  0.40 31.08 ?  29  LYS   A H    1 
ATOM   841  H HA   A LYS   A 1 29  ? 17.478 1.414   20.315  0.60 30.09 ?  29  LYS   A HA   1 
ATOM   842  H HA   B LYS   A 1 29  ? 17.080 1.084   20.031  0.40 32.79 ?  29  LYS   A HA   1 
ATOM   843  H HB2  A LYS   A 1 29  ? 15.575 1.215   18.972  0.60 33.29 ?  29  LYS   A HB2  1 
ATOM   844  H HB2  B LYS   A 1 29  ? 15.564 0.427   18.025  0.40 35.41 ?  29  LYS   A HB2  1 
ATOM   845  H HB3  A LYS   A 1 29  ? 16.101 -0.180  18.433  0.60 33.29 ?  29  LYS   A HB3  1 
ATOM   846  H HB3  B LYS   A 1 29  ? 15.883 -0.978  18.688  0.40 35.41 ?  29  LYS   A HB3  1 
ATOM   847  H HG2  A LYS   A 1 29  ? 14.549 -0.739  19.938  0.60 36.63 ?  29  LYS   A HG2  1 
ATOM   848  H HG2  B LYS   A 1 29  ? 14.573 1.163   19.972  0.40 38.04 ?  29  LYS   A HG2  1 
ATOM   849  H HG3  A LYS   A 1 29  ? 15.906 -0.947  20.739  0.60 36.63 ?  29  LYS   A HG3  1 
ATOM   850  H HG3  B LYS   A 1 29  ? 13.903 -0.221  19.562  0.40 38.04 ?  29  LYS   A HG3  1 
ATOM   851  H HD2  A LYS   A 1 29  ? 15.614 1.046   21.841  0.60 39.72 ?  29  LYS   A HD2  1 
ATOM   852  H HD2  B LYS   A 1 29  ? 14.635 -1.226  21.328  0.40 40.19 ?  29  LYS   A HD2  1 
ATOM   853  H HD3  A LYS   A 1 29  ? 14.346 1.395   20.944  0.60 39.72 ?  29  LYS   A HD3  1 
ATOM   854  H HD3  B LYS   A 1 29  ? 16.033 -0.478  21.313  0.40 40.19 ?  29  LYS   A HD3  1 
ATOM   855  H HE2  A LYS   A 1 29  ? 13.187 -0.393  21.922  0.60 41.84 ?  29  LYS   A HE2  1 
ATOM   856  H HE2  B LYS   A 1 29  ? 15.007 1.419   22.230  0.40 41.76 ?  29  LYS   A HE2  1 
ATOM   857  H HE3  A LYS   A 1 29  ? 14.446 -0.684  22.851  0.60 41.84 ?  29  LYS   A HE3  1 
ATOM   858  H HE3  B LYS   A 1 29  ? 13.640 0.608   22.315  0.40 41.76 ?  29  LYS   A HE3  1 
ATOM   859  H HZ1  A LYS   A 1 29  ? 12.895 0.542   23.973  0.60 43.07 ?  29  LYS   A HZ1  1 
ATOM   860  H HZ1  B LYS   A 1 29  ? 14.718 0.563   24.314  0.40 42.52 ?  29  LYS   A HZ1  1 
ATOM   861  H HZ2  A LYS   A 1 29  ? 14.097 1.339   23.834  0.60 43.07 ?  29  LYS   A HZ2  1 
ATOM   862  H HZ2  B LYS   A 1 29  ? 14.645 -0.790  23.800  0.40 42.52 ?  29  LYS   A HZ2  1 
ATOM   863  H HZ3  A LYS   A 1 29  ? 12.951 1.604   22.989  0.60 43.07 ?  29  LYS   A HZ3  1 
ATOM   864  H HZ3  B LYS   A 1 29  ? 15.889 -0.051  23.722  0.40 42.52 ?  29  LYS   A HZ3  1 
ATOM   865  N N    A VAL   A 1 30  ? 18.649 -1.251  18.947  0.60 23.19 ?  30  VAL   A N    1 
ATOM   866  N N    B VAL   A 1 30  ? 18.602 -1.438  18.760  0.40 25.62 ?  30  VAL   A N    1 
ATOM   867  C CA   A VAL   A 1 30  ? 19.266 -2.544  19.229  0.60 22.94 ?  30  VAL   A CA   1 
ATOM   868  C CA   B VAL   A 1 30  ? 19.294 -2.682  19.078  0.40 24.73 ?  30  VAL   A CA   1 
ATOM   869  C C    A VAL   A 1 30  ? 20.774 -2.412  19.434  0.60 22.13 ?  30  VAL   A C    1 
ATOM   870  C C    B VAL   A 1 30  ? 20.787 -2.484  19.347  0.40 23.01 ?  30  VAL   A C    1 
ATOM   871  O O    A VAL   A 1 30  ? 21.360 -3.112  20.264  0.60 22.51 ?  30  VAL   A O    1 
ATOM   872  O O    B VAL   A 1 30  ? 21.366 -3.209  20.161  0.40 23.14 ?  30  VAL   A O    1 
ATOM   873  C CB   A VAL   A 1 30  ? 18.918 -3.532  18.099  0.60 23.86 ?  30  VAL   A CB   1 
ATOM   874  C CB   B VAL   A 1 30  ? 19.063 -3.697  17.943  0.40 25.46 ?  30  VAL   A CB   1 
ATOM   875  C CG1  A VAL   A 1 30  ? 19.648 -4.854  18.290  0.60 24.53 ?  30  VAL   A CG1  1 
ATOM   876  C CG1  B VAL   A 1 30  ? 19.792 -5.002  18.227  0.40 25.73 ?  30  VAL   A CG1  1 
ATOM   877  C CG2  A VAL   A 1 30  ? 17.411 -3.754  18.033  0.60 24.29 ?  30  VAL   A CG2  1 
ATOM   878  C CG2  B VAL   A 1 30  ? 17.572 -3.943  17.745  0.40 25.86 ?  30  VAL   A CG2  1 
ATOM   879  H H    A VAL   A 1 30  ? 18.510 -1.100  18.111  0.60 27.82 ?  30  VAL   A H    1 
ATOM   880  H H    B VAL   A 1 30  ? 18.554 -1.267  17.920  0.40 30.73 ?  30  VAL   A H    1 
ATOM   881  H HA   A VAL   A 1 30  ? 18.883 -2.894  20.047  0.60 27.52 ?  30  VAL   A HA   1 
ATOM   882  H HA   B VAL   A 1 30  ? 18.895 -3.055  19.880  0.40 29.67 ?  30  VAL   A HA   1 
ATOM   883  H HB   A VAL   A 1 30  ? 19.199 -3.157  17.251  0.60 28.62 ?  30  VAL   A HB   1 
ATOM   884  H HB   B VAL   A 1 30  ? 19.419 -3.333  17.117  0.40 30.54 ?  30  VAL   A HB   1 
ATOM   885  H HG11 A VAL   A 1 30  ? 19.251 -5.519  17.704  0.60 29.42 ?  30  VAL   A HG11 1 
ATOM   886  H HG11 B VAL   A 1 30  ? 19.448 -5.688  17.632  0.40 30.86 ?  30  VAL   A HG11 1 
ATOM   887  H HG12 A VAL   A 1 30  ? 20.583 -4.736  18.069  0.60 29.42 ?  30  VAL   A HG12 1 
ATOM   888  H HG12 B VAL   A 1 30  ? 20.741 -4.878  18.072  0.40 30.86 ?  30  VAL   A HG12 1 
ATOM   889  H HG13 A VAL   A 1 30  ? 19.555 -5.135  19.214  0.60 29.42 ?  30  VAL   A HG13 1 
ATOM   890  H HG13 B VAL   A 1 30  ? 19.635 -5.258  19.149  0.40 30.86 ?  30  VAL   A HG13 1 
ATOM   891  H HG21 A VAL   A 1 30  ? 17.218 -4.416  17.349  0.60 29.13 ?  30  VAL   A HG21 1 
ATOM   892  H HG21 B VAL   A 1 30  ? 17.452 -4.647  17.089  0.40 31.01 ?  30  VAL   A HG21 1 
ATOM   893  H HG22 A VAL   A 1 30  ? 17.100 -4.072  18.896  0.60 29.13 ?  30  VAL   A HG22 1 
ATOM   894  H HG22 B VAL   A 1 30  ? 17.181 -4.210  18.592  0.40 31.01 ?  30  VAL   A HG22 1 
ATOM   895  H HG23 A VAL   A 1 30  ? 16.976 -2.916  17.813  0.60 29.13 ?  30  VAL   A HG23 1 
ATOM   896  H HG23 B VAL   A 1 30  ? 17.156 -3.125  17.432  0.40 31.01 ?  30  VAL   A HG23 1 
ATOM   897  N N    . LYS   A 1 31  ? 21.422 -1.521  18.687  1.00 21.36 ?  31  LYS   A N    1 
ATOM   898  C CA   . LYS   A 1 31  ? 22.876 -1.401  18.664  1.00 22.05 ?  31  LYS   A CA   1 
ATOM   899  C C    . LYS   A 1 31  ? 23.482 -2.754  18.292  1.00 19.56 ?  31  LYS   A C    1 
ATOM   900  O O    . LYS   A 1 31  ? 24.267 -3.322  19.059  1.00 20.54 ?  31  LYS   A O    1 
ATOM   901  C CB   . LYS   A 1 31  ? 23.442 -0.885  19.983  1.00 27.47 ?  31  LYS   A CB   1 
ATOM   902  C CG   . LYS   A 1 31  ? 22.794 0.406   20.462  1.00 33.73 ?  31  LYS   A CG   1 
ATOM   903  C CD   . LYS   A 1 31  ? 23.827 1.453   20.854  1.00 38.62 ?  31  LYS   A CD   1 
ATOM   904  C CE   . LYS   A 1 31  ? 23.213 2.535   21.735  1.00 41.83 ?  31  LYS   A CE   1 
ATOM   905  N NZ   . LYS   A 1 31  ? 22.055 3.219   21.095  1.00 43.59 ?  31  LYS   A NZ   1 
ATOM   906  H H    A LYS   A 1 31  ? 21.029 -0.962  18.173  0.60 25.62 ?  31  LYS   A H    1 
ATOM   907  H H    B LYS   A 1 31  ? 21.023 -0.917  18.230  0.40 25.62 ?  31  LYS   A H    1 
ATOM   908  H HA   . LYS   A 1 31  ? 23.125 -0.770  17.980  1.00 26.45 ?  31  LYS   A HA   1 
ATOM   909  H HB2  . LYS   A 1 31  ? 23.317 -1.559  20.663  1.00 32.95 ?  31  LYS   A HB2  1 
ATOM   910  H HB3  . LYS   A 1 31  ? 24.395 -0.713  19.862  1.00 32.95 ?  31  LYS   A HB3  1 
ATOM   911  H HG2  . LYS   A 1 31  ? 22.251 0.772   19.747  1.00 40.47 ?  31  LYS   A HG2  1 
ATOM   912  H HG3  . LYS   A 1 31  ? 22.242 0.217   21.236  1.00 40.47 ?  31  LYS   A HG3  1 
ATOM   913  H HD2  . LYS   A 1 31  ? 24.545 1.029   21.349  1.00 46.33 ?  31  LYS   A HD2  1 
ATOM   914  H HD3  . LYS   A 1 31  ? 24.175 1.876   20.052  1.00 46.33 ?  31  LYS   A HD3  1 
ATOM   915  H HE2  . LYS   A 1 31  ? 22.903 2.130   22.560  1.00 50.18 ?  31  LYS   A HE2  1 
ATOM   916  H HE3  . LYS   A 1 31  ? 23.887 3.205   21.927  1.00 50.18 ?  31  LYS   A HE3  1 
ATOM   917  H HZ1  . LYS   A 1 31  ? 21.734 3.846   21.640  1.00 52.29 ?  31  LYS   A HZ1  1 
ATOM   918  H HZ2  . LYS   A 1 31  ? 22.309 3.600   20.333  1.00 52.29 ?  31  LYS   A HZ2  1 
ATOM   919  H HZ3  . LYS   A 1 31  ? 21.410 2.629   20.924  1.00 52.29 ?  31  LYS   A HZ3  1 
ATOM   920  N N    . PRO   A 1 32  ? 23.124 -3.297  17.135  1.00 17.28 ?  32  PRO   A N    1 
ATOM   921  C CA   . PRO   A 1 32  ? 23.599 -4.629  16.764  1.00 17.70 ?  32  PRO   A CA   1 
ATOM   922  C C    . PRO   A 1 32  ? 25.100 -4.641  16.550  1.00 17.69 ?  32  PRO   A C    1 
ATOM   923  O O    . PRO   A 1 32  ? 25.741 -3.609  16.336  1.00 17.52 ?  32  PRO   A O    1 
ATOM   924  C CB   . PRO   A 1 32  ? 22.864 -4.903  15.448  1.00 17.81 ?  32  PRO   A CB   1 
ATOM   925  C CG   . PRO   A 1 32  ? 22.667 -3.531  14.859  1.00 16.56 ?  32  PRO   A CG   1 
ATOM   926  C CD   . PRO   A 1 32  ? 22.384 -2.651  16.040  1.00 16.62 ?  32  PRO   A CD   1 
ATOM   927  H HA   . PRO   A 1 32  ? 23.357 -5.289  17.425  1.00 21.22 ?  32  PRO   A HA   1 
ATOM   928  H HB2  . PRO   A 1 32  ? 23.411 -5.457  14.863  1.00 21.36 ?  32  PRO   A HB2  1 
ATOM   929  H HB3  . PRO   A 1 32  ? 22.012 -5.330  15.628  1.00 21.36 ?  32  PRO   A HB3  1 
ATOM   930  H HG2  . PRO   A 1 32  ? 23.474 -3.254  14.399  1.00 19.87 ?  32  PRO   A HG2  1 
ATOM   931  H HG3  . PRO   A 1 32  ? 21.911 -3.545  14.247  1.00 19.87 ?  32  PRO   A HG3  1 
ATOM   932  H HD2  . PRO   A 1 32  ? 22.722 -1.758  15.869  1.00 19.93 ?  32  PRO   A HD2  1 
ATOM   933  H HD3  . PRO   A 1 32  ? 21.438 -2.648  16.232  1.00 19.93 ?  32  PRO   A HD3  1 
ATOM   934  N N    . THR   A 1 33  ? 25.660 -5.848  16.596  1.00 17.79 ?  33  THR   A N    1 
ATOM   935  C CA   . THR   A 1 33  ? 27.067 -6.009  16.259  1.00 17.71 ?  33  THR   A CA   1 
ATOM   936  C C    . THR   A 1 33  ? 27.345 -5.538  14.839  1.00 15.86 ?  33  THR   A C    1 
ATOM   937  O O    . THR   A 1 33  ? 28.370 -4.888  14.585  1.00 15.87 ?  33  THR   A O    1 
ATOM   938  C CB   . THR   A 1 33  ? 27.481 -7.469  16.446  1.00 19.09 ?  33  THR   A CB   1 
ATOM   939  O OG1  . THR   A 1 33  ? 27.160 -7.877  17.779  1.00 21.00 ?  33  THR   A OG1  1 
ATOM   940  C CG2  . THR   A 1 33  ? 28.978 -7.643  16.218  1.00 20.33 ?  33  THR   A CG2  1 
ATOM   941  H H    . THR   A 1 33  ? 25.259 -6.579  16.808  1.00 21.34 ?  33  THR   A H    1 
ATOM   942  H HA   . THR   A 1 33  ? 27.606 -5.475  16.860  1.00 21.25 ?  33  THR   A HA   1 
ATOM   943  H HB   . THR   A 1 33  ? 27.009 -8.036  15.810  1.00 22.89 ?  33  THR   A HB   1 
ATOM   944  H HG1  . THR   A 1 33  ? 27.579 -7.403  18.334  1.00 25.19 ?  33  THR   A HG1  1 
ATOM   945  H HG21 . THR   A 1 33  ? 29.253 -8.539  16.475  1.00 24.39 ?  33  THR   A HG21 1 
ATOM   946  H HG22 . THR   A 1 33  ? 29.193 -7.508  15.282  1.00 24.39 ?  33  THR   A HG22 1 
ATOM   947  H HG23 . THR   A 1 33  ? 29.469 -7.001  16.752  1.00 24.39 ?  33  THR   A HG23 1 
ATOM   948  N N    . VAL   A 1 34  ? 26.448 -5.851  13.904  1.00 14.44 ?  34  VAL   A N    1 
ATOM   949  C CA   . VAL   A 1 34  ? 26.616 -5.504  12.497  1.00 13.43 ?  34  VAL   A CA   1 
ATOM   950  C C    . VAL   A 1 34  ? 25.308 -4.938  11.954  1.00 12.77 ?  34  VAL   A C    1 
ATOM   951  O O    . VAL   A 1 34  ? 24.268 -5.609  12.009  1.00 13.40 ?  34  VAL   A O    1 
ATOM   952  C CB   . VAL   A 1 34  ? 27.059 -6.706  11.641  1.00 14.09 ?  34  VAL   A CB   1 
ATOM   953  C CG1  . VAL   A 1 34  ? 27.243 -6.273  10.197  1.00 14.19 ?  34  VAL   A CG1  1 
ATOM   954  C CG2  . VAL   A 1 34  ? 28.343 -7.344  12.191  1.00 15.39 ?  34  VAL   A CG2  1 
ATOM   955  H H    . VAL   A 1 34  ? 25.717 -6.280  14.064  1.00 17.31 ?  34  VAL   A H    1 
ATOM   956  H HA   . VAL   A 1 34  ? 27.297 -4.816  12.417  1.00 16.11 ?  34  VAL   A HA   1 
ATOM   957  H HB   . VAL   A 1 34  ? 26.361 -7.377  11.657  1.00 16.89 ?  34  VAL   A HB   1 
ATOM   958  H HG11 . VAL   A 1 34  ? 27.739 -6.958  9.720   1.00 17.02 ?  34  VAL   A HG11 1 
ATOM   959  H HG12 . VAL   A 1 34  ? 26.377 -6.144  9.783   1.00 17.02 ?  34  VAL   A HG12 1 
ATOM   960  H HG13 . VAL   A 1 34  ? 27.746 -5.437  10.178  1.00 17.02 ?  34  VAL   A HG13 1 
ATOM   961  H HG21 . VAL   A 1 34  ? 28.608 -8.074  11.608  1.00 18.46 ?  34  VAL   A HG21 1 
ATOM   962  H HG22 . VAL   A 1 34  ? 29.044 -6.674  12.218  1.00 18.46 ?  34  VAL   A HG22 1 
ATOM   963  H HG23 . VAL   A 1 34  ? 28.171 -7.681  13.083  1.00 18.46 ?  34  VAL   A HG23 1 
ATOM   964  N N    . VAL   A 1 35  ? 25.366 -3.722  11.398  1.00 11.86 ?  35  VAL   A N    1 
ATOM   965  C CA   . VAL   A 1 35  ? 24.321 -3.198  10.524  1.00 11.55 ?  35  VAL   A CA   1 
ATOM   966  C C    . VAL   A 1 35  ? 24.857 -3.194  9.099   1.00 11.31 ?  35  VAL   A C    1 
ATOM   967  O O    . VAL   A 1 35  ? 26.001 -2.792  8.859   1.00 11.65 ?  35  VAL   A O    1 
ATOM   968  C CB   . VAL   A 1 35  ? 23.797 -1.807  10.945  1.00 12.29 ?  35  VAL   A CB   1 
ATOM   969  C CG1  . VAL   A 1 35  ? 24.870 -0.716  10.810  1.00 12.98 ?  35  VAL   A CG1  1 
ATOM   970  C CG2  . VAL   A 1 35  ? 22.550 -1.453  10.141  1.00 13.22 ?  35  VAL   A CG2  1 
ATOM   971  H H    . VAL   A 1 35  ? 26.014 -3.169  11.515  1.00 14.22 ?  35  VAL   A H    1 
ATOM   972  H HA   . VAL   A 1 35  ? 23.564 -3.810  10.551  1.00 13.84 ?  35  VAL   A HA   1 
ATOM   973  H HB   . VAL   A 1 35  ? 23.535 -1.844  11.876  1.00 14.73 ?  35  VAL   A HB   1 
ATOM   974  H HG11 . VAL   A 1 35  ? 24.528 0.116   11.185  1.00 15.56 ?  35  VAL   A HG11 1 
ATOM   975  H HG12 . VAL   A 1 35  ? 25.665 -0.988  11.296  1.00 15.56 ?  35  VAL   A HG12 1 
ATOM   976  H HG13 . VAL   A 1 35  ? 25.085 -0.585  9.873   1.00 15.56 ?  35  VAL   A HG13 1 
ATOM   977  H HG21 . VAL   A 1 35  ? 22.198 -0.609  10.458  1.00 15.85 ?  35  VAL   A HG21 1 
ATOM   978  H HG22 . VAL   A 1 35  ? 22.792 -1.376  9.200   1.00 15.85 ?  35  VAL   A HG22 1 
ATOM   979  H HG23 . VAL   A 1 35  ? 21.892 -2.154  10.254  1.00 15.85 ?  35  VAL   A HG23 1 
ATOM   980  N N    . VAL   A 1 36  ? 24.035 -3.645  8.154   1.00 10.78 ?  36  VAL   A N    1 
ATOM   981  C CA   . VAL   A 1 36  ? 24.402 -3.654  6.744   1.00 10.14 ?  36  VAL   A CA   1 
ATOM   982  C C    . VAL   A 1 36  ? 23.949 -2.356  6.089   1.00 10.42 ?  36  VAL   A C    1 
ATOM   983  O O    . VAL   A 1 36  ? 22.793 -1.940  6.240   1.00 11.18 ?  36  VAL   A O    1 
ATOM   984  C CB   . VAL   A 1 36  ? 23.789 -4.866  6.021   1.00 10.55 ?  36  VAL   A CB   1 
ATOM   985  C CG1  . VAL   A 1 36  ? 24.040 -4.780  4.534   1.00 10.77 ?  36  VAL   A CG1  1 
ATOM   986  C CG2  . VAL   A 1 36  ? 24.346 -6.168  6.579   1.00 11.22 ?  36  VAL   A CG2  1 
ATOM   987  H H    . VAL   A 1 36  ? 23.244 -3.964  8.309   1.00 12.93 ?  36  VAL   A H    1 
ATOM   988  H HA   . VAL   A 1 36  ? 25.370 -3.719  6.669   1.00 12.15 ?  36  VAL   A HA   1 
ATOM   989  H HB   . VAL   A 1 36  ? 22.831 -4.867  6.163   1.00 12.64 ?  36  VAL   A HB   1 
ATOM   990  H HG11 . VAL   A 1 36  ? 23.904 -5.654  4.137   1.00 12.91 ?  36  VAL   A HG11 1 
ATOM   991  H HG12 . VAL   A 1 36  ? 23.427 -4.140  4.141   1.00 12.91 ?  36  VAL   A HG12 1 
ATOM   992  H HG13 . VAL   A 1 36  ? 24.958 -4.493  4.384   1.00 12.91 ?  36  VAL   A HG13 1 
ATOM   993  H HG21 . VAL   A 1 36  ? 23.945 -6.917  6.104   1.00 13.45 ?  36  VAL   A HG21 1 
ATOM   994  H HG22 . VAL   A 1 36  ? 25.310 -6.184  6.455   1.00 13.45 ?  36  VAL   A HG22 1 
ATOM   995  H HG23 . VAL   A 1 36  ? 24.135 -6.231  7.524   1.00 13.45 ?  36  VAL   A HG23 1 
ATOM   996  N N    . ASN   A 1 37  ? 24.855 -1.731  5.343   1.00 9.79  ?  37  ASN   A N    1 
ATOM   997  C CA   . ASN   A 1 37  ? 24.526 -0.604  4.488   1.00 9.82  ?  37  ASN   A CA   1 
ATOM   998  C C    . ASN   A 1 37  ? 24.381 -1.062  3.047   1.00 9.94  ?  37  ASN   A C    1 
ATOM   999  O O    . ASN   A 1 37  ? 25.157 -1.892  2.558   1.00 10.16 ?  37  ASN   A O    1 
ATOM   1000 C CB   . ASN   A 1 37  ? 25.605 0.476   4.574   1.00 10.03 ?  37  ASN   A CB   1 
ATOM   1001 C CG   . ASN   A 1 37  ? 25.285 1.684   3.722   1.00 10.21 ?  37  ASN   A CG   1 
ATOM   1002 O OD1  . ASN   A 1 37  ? 24.113 2.028   3.548   1.00 10.63 ?  37  ASN   A OD1  1 
ATOM   1003 N ND2  . ASN   A 1 37  ? 26.319 2.338   3.201   1.00 10.56 ?  37  ASN   A ND2  1 
ATOM   1004 H H    . ASN   A 1 37  ? 25.692 -1.946  5.327   1.00 11.74 ?  37  ASN   A H    1 
ATOM   1005 H HA   . ASN   A 1 37  ? 23.688 -0.218  4.778   1.00 11.77 ?  37  ASN   A HA   1 
ATOM   1006 H HB2  . ASN   A 1 37  ? 25.685 0.774   5.497   1.00 12.02 ?  37  ASN   A HB2  1 
ATOM   1007 H HB3  . ASN   A 1 37  ? 26.452 0.109   4.273   1.00 12.02 ?  37  ASN   A HB3  1 
ATOM   1008 H HD21 . ASN   A 1 37  ? 26.184 3.029   2.708   1.00 12.66 ?  37  ASN   A HD21 1 
ATOM   1009 H HD22 . ASN   A 1 37  ? 27.116 2.071   3.349   1.00 12.66 ?  37  ASN   A HD22 1 
ATOM   1010 N N    A ALA   A 1 38  ? 23.370 -0.497  2.380   0.60 10.14 ?  38  ALA   A N    1 
ATOM   1011 N N    B ALA   A 1 38  ? 23.365 -0.533  2.364   0.40 10.47 ?  38  ALA   A N    1 
ATOM   1012 C CA   A ALA   A 1 38  ? 23.150 -0.610  0.938   0.60 10.08 ?  38  ALA   A CA   1 
ATOM   1013 C CA   B ALA   A 1 38  ? 23.187 -0.782  0.932   0.40 11.12 ?  38  ALA   A CA   1 
ATOM   1014 C C    A ALA   A 1 38  ? 24.077 0.375   0.227   0.60 9.85  ?  38  ALA   A C    1 
ATOM   1015 C C    B ALA   A 1 38  ? 24.017 0.250   0.170   0.40 10.66 ?  38  ALA   A C    1 
ATOM   1016 O O    A ALA   A 1 38  ? 23.686 1.474   -0.179  0.60 9.84  ?  38  ALA   A O    1 
ATOM   1017 O O    B ALA   A 1 38  ? 23.528 1.281   -0.300  0.40 10.48 ?  38  ALA   A O    1 
ATOM   1018 C CB   A ALA   A 1 38  ? 21.687 -0.317  0.614   0.60 10.91 ?  38  ALA   A CB   1 
ATOM   1019 C CB   B ALA   A 1 38  ? 21.712 -0.737  0.557   0.40 12.24 ?  38  ALA   A CB   1 
ATOM   1020 H H    A ALA   A 1 38  ? 22.774 -0.010  2.767   0.60 12.15 ?  38  ALA   A H    1 
ATOM   1021 H H    B ALA   A 1 38  ? 22.766 -0.019  2.709   0.40 12.55 ?  38  ALA   A H    1 
ATOM   1022 H HA   A ALA   A 1 38  ? 23.359 -1.507  0.642   0.60 12.09 ?  38  ALA   A HA   1 
ATOM   1023 H HA   B ALA   A 1 38  ? 23.527 -1.667  0.718   0.40 13.33 ?  38  ALA   A HA   1 
ATOM   1024 H HB1  A ALA   A 1 38  ? 21.550 -0.396  -0.342  0.60 13.08 ?  38  ALA   A HB1  1 
ATOM   1025 H HB1  B ALA   A 1 38  ? 21.625 -0.907  -0.394  0.40 14.68 ?  38  ALA   A HB1  1 
ATOM   1026 H HB2  A ALA   A 1 38  ? 21.124 -0.956  1.082   0.60 13.08 ?  38  ALA   A HB2  1 
ATOM   1027 H HB2  B ALA   A 1 38  ? 21.236 -1.420  1.058   0.40 14.68 ?  38  ALA   A HB2  1 
ATOM   1028 H HB3  A ALA   A 1 38  ? 21.471 0.585   0.905   0.60 13.08 ?  38  ALA   A HB3  1 
ATOM   1029 H HB3  B ALA   A 1 38  ? 21.359 0.138   0.772   0.40 14.68 ?  38  ALA   A HB3  1 
ATOM   1030 N N    A ALA   A 1 39  ? 25.335 -0.034  0.081   0.60 10.00 ?  39  ALA   A N    1 
ATOM   1031 N N    B ALA   A 1 39  ? 25.307 -0.047  0.058   0.40 11.20 ?  39  ALA   A N    1 
ATOM   1032 C CA   A ALA   A 1 39  ? 26.411 0.818   -0.405  0.60 9.71  ?  39  ALA   A CA   1 
ATOM   1033 C CA   B ALA   A 1 39  ? 26.300 0.900   -0.419  0.40 11.40 ?  39  ALA   A CA   1 
ATOM   1034 C C    A ALA   A 1 39  ? 26.516 0.772   -1.926  0.60 9.95  ?  39  ALA   A C    1 
ATOM   1035 C C    B ALA   A 1 39  ? 26.480 0.800   -1.932  0.40 10.80 ?  39  ALA   A C    1 
ATOM   1036 O O    A ALA   A 1 39  ? 26.018 -0.146  -2.584  0.60 10.45 ?  39  ALA   A O    1 
ATOM   1037 O O    B ALA   A 1 39  ? 26.000 -0.127  -2.589  0.40 11.23 ?  39  ALA   A O    1 
ATOM   1038 C CB   A ALA   A 1 39  ? 27.733 0.364   0.217   0.60 9.80  ?  39  ALA   A CB   1 
ATOM   1039 C CB   B ALA   A 1 39  ? 27.633 0.645   0.286   0.40 12.26 ?  39  ALA   A CB   1 
ATOM   1040 H H    A ALA   A 1 39  ? 25.595 -0.837  0.271   0.60 11.99 ?  39  ALA   A H    1 
ATOM   1041 H H    B ALA   A 1 39  ? 25.634 -0.818  0.259   0.40 13.43 ?  39  ALA   A H    1 
ATOM   1042 H HA   A ALA   A 1 39  ? 26.240 1.732   -0.136  0.60 11.64 ?  39  ALA   A HA   1 
ATOM   1043 H HA   B ALA   A 1 39  ? 26.010 1.796   -0.200  0.40 13.67 ?  39  ALA   A HA   1 
ATOM   1044 H HB1  A ALA   A 1 39  ? 28.444 0.937   -0.109  0.60 11.75 ?  39  ALA   A HB1  1 
ATOM   1045 H HB1  B ALA   A 1 39  ? 28.286 1.282   -0.040  0.40 14.70 ?  39  ALA   A HB1  1 
ATOM   1046 H HB2  A ALA   A 1 39  ? 27.668 0.439   1.185   0.60 11.75 ?  39  ALA   A HB2  1 
ATOM   1047 H HB2  B ALA   A 1 39  ? 27.510 0.756   1.243   0.40 14.70 ?  39  ALA   A HB2  1 
ATOM   1048 H HB3  A ALA   A 1 39  ? 27.903 -0.555  -0.032  0.60 11.75 ?  39  ALA   A HB3  1 
ATOM   1049 H HB3  B ALA   A 1 39  ? 27.925 -0.259  0.093   0.40 14.70 ?  39  ALA   A HB3  1 
ATOM   1050 N N    . ASN   A 1 40  ? 27.195 1.781   -2.478  1.00 10.71 ?  40  ASN   A N    1 
ATOM   1051 C CA   . ASN   A 1 40  ? 27.711 1.741   -3.841  1.00 10.96 ?  40  ASN   A CA   1 
ATOM   1052 C C    . ASN   A 1 40  ? 29.239 1.633   -3.796  1.00 10.49 ?  40  ASN   A C    1 
ATOM   1053 O O    . ASN   A 1 40  ? 29.850 1.720   -2.727  1.00 10.61 ?  40  ASN   A O    1 
ATOM   1054 C CB   . ASN   A 1 40  ? 27.223 2.931   -4.682  1.00 11.83 ?  40  ASN   A CB   1 
ATOM   1055 C CG   . ASN   A 1 40  ? 27.606 4.275   -4.098  1.00 12.88 ?  40  ASN   A CG   1 
ATOM   1056 O OD1  . ASN   A 1 40  ? 28.784 4.538   -3.812  1.00 13.70 ?  40  ASN   A OD1  1 
ATOM   1057 N ND2  . ASN   A 1 40  ? 26.607 5.148   -3.937  1.00 13.81 ?  40  ASN   A ND2  1 
ATOM   1058 H H    A ASN   A 1 40  ? 27.376 2.511   -2.067  0.60 12.84 ?  40  ASN   A H    1 
ATOM   1059 H H    B ASN   A 1 40  ? 27.418 2.493   -2.056  0.40 12.84 ?  40  ASN   A H    1 
ATOM   1060 H HA   . ASN   A 1 40  ? 27.385 0.932   -4.270  1.00 13.14 ?  40  ASN   A HA   1 
ATOM   1061 H HB2  . ASN   A 1 40  ? 27.605 2.860   -5.572  1.00 14.18 ?  40  ASN   A HB2  1 
ATOM   1062 H HB3  . ASN   A 1 40  ? 26.256 2.886   -4.738  1.00 14.18 ?  40  ASN   A HB3  1 
ATOM   1063 H HD21 . ASN   A 1 40  ? 26.773 5.932   -3.621  1.00 16.56 ?  40  ASN   A HD21 1 
ATOM   1064 H HD22 . ASN   A 1 40  ? 25.808 4.930   -4.154  1.00 16.56 ?  40  ASN   A HD22 1 
ATOM   1065 N N    . VAL   A 1 41  ? 29.851 1.380   -4.958  1.00 11.09 ?  41  VAL   A N    1 
ATOM   1066 C CA   . VAL   A 1 41  ? 31.282 1.068   -4.994  1.00 11.91 ?  41  VAL   A CA   1 
ATOM   1067 C C    . VAL   A 1 41  ? 32.148 2.222   -4.527  1.00 11.69 ?  41  VAL   A C    1 
ATOM   1068 O O    . VAL   A 1 41  ? 33.294 1.997   -4.117  1.00 12.14 ?  41  VAL   A O    1 
ATOM   1069 C CB   . VAL   A 1 41  ? 31.767 0.586   -6.380  1.00 12.82 ?  41  VAL   A CB   1 
ATOM   1070 C CG1  . VAL   A 1 41  ? 31.077 -0.714  -6.768  1.00 13.38 ?  41  VAL   A CG1  1 
ATOM   1071 C CG2  . VAL   A 1 41  ? 31.603 1.665   -7.451  1.00 13.76 ?  41  VAL   A CG2  1 
ATOM   1072 H H    . VAL   A 1 41  ? 29.467 1.375   -5.727  1.00 13.29 ?  41  VAL   A H    1 
ATOM   1073 H HA   . VAL   A 1 41  ? 31.441 0.335   -4.374  1.00 14.28 ?  41  VAL   A HA   1 
ATOM   1074 H HB   . VAL   A 1 41  ? 32.715 0.386   -6.315  1.00 15.37 ?  41  VAL   A HB   1 
ATOM   1075 H HG11 . VAL   A 1 41  ? 31.414 -1.009  -7.627  1.00 16.04 ?  41  VAL   A HG11 1 
ATOM   1076 H HG12 . VAL   A 1 41  ? 31.266 -1.388  -6.091  1.00 16.04 ?  41  VAL   A HG12 1 
ATOM   1077 H HG13 . VAL   A 1 41  ? 30.121 -0.561  -6.820  1.00 16.04 ?  41  VAL   A HG13 1 
ATOM   1078 H HG21 . VAL   A 1 41  ? 31.823 1.283   -8.316  1.00 16.50 ?  41  VAL   A HG21 1 
ATOM   1079 H HG22 . VAL   A 1 41  ? 30.689 1.976   -7.446  1.00 16.50 ?  41  VAL   A HG22 1 
ATOM   1080 H HG23 . VAL   A 1 41  ? 32.208 2.396   -7.251  1.00 16.50 ?  41  VAL   A HG23 1 
ATOM   1081 N N    A TYR   A 1 42  ? 31.635 3.453   -4.589  0.60 11.56 ?  42  TYR   A N    1 
ATOM   1082 N N    B TYR   A 1 42  ? 31.648 3.456   -4.597  0.40 11.61 ?  42  TYR   A N    1 
ATOM   1083 C CA   A TYR   A 1 42  ? 32.366 4.648   -4.182  0.60 11.31 ?  42  TYR   A CA   1 
ATOM   1084 C CA   B TYR   A 1 42  ? 32.409 4.625   -4.168  0.40 11.50 ?  42  TYR   A CA   1 
ATOM   1085 C C    A TYR   A 1 42  ? 32.132 5.009   -2.724  0.60 11.34 ?  42  TYR   A C    1 
ATOM   1086 C C    B TYR   A 1 42  ? 32.105 5.030   -2.735  0.40 11.37 ?  42  TYR   A C    1 
ATOM   1087 O O    A TYR   A 1 42  ? 32.730 5.973   -2.229  0.60 11.98 ?  42  TYR   A O    1 
ATOM   1088 O O    B TYR   A 1 42  ? 32.636 6.044   -2.265  0.40 11.91 ?  42  TYR   A O    1 
ATOM   1089 C CB   A TYR   A 1 42  ? 31.979 5.837   -5.077  0.60 12.16 ?  42  TYR   A CB   1 
ATOM   1090 C CB   B TYR   A 1 42  ? 32.164 5.811   -5.116  0.40 12.12 ?  42  TYR   A CB   1 
ATOM   1091 C CG   A TYR   A 1 42  ? 32.109 5.547   -6.558  0.60 12.88 ?  42  TYR   A CG   1 
ATOM   1092 C CG   B TYR   A 1 42  ? 32.401 5.464   -6.568  0.40 12.45 ?  42  TYR   A CG   1 
ATOM   1093 C CD1  A TYR   A 1 42  ? 33.353 5.353   -7.141  0.60 13.54 ?  42  TYR   A CD1  1 
ATOM   1094 C CD1  B TYR   A 1 42  ? 33.685 5.263   -7.054  0.40 12.98 ?  42  TYR   A CD1  1 
ATOM   1095 C CD2  A TYR   A 1 42  ? 30.988 5.451   -7.371  0.60 14.28 ?  42  TYR   A CD2  1 
ATOM   1096 C CD2  B TYR   A 1 42  ? 31.339 5.312   -7.448  0.40 12.60 ?  42  TYR   A CD2  1 
ATOM   1097 C CE1  A TYR   A 1 42  ? 33.480 5.076   -8.495  0.60 13.84 ?  42  TYR   A CE1  1 
ATOM   1098 C CE1  B TYR   A 1 42  ? 33.904 4.930   -8.380  0.40 12.57 ?  42  TYR   A CE1  1 
ATOM   1099 C CE2  A TYR   A 1 42  ? 31.104 5.184   -8.724  0.60 14.95 ?  42  TYR   A CE2  1 
ATOM   1100 C CE2  B TYR   A 1 42  ? 31.547 4.983   -8.773  0.40 12.61 ?  42  TYR   A CE2  1 
ATOM   1101 C CZ   A TYR   A 1 42  ? 32.354 4.997   -9.281  0.60 14.67 ?  42  TYR   A CZ   1 
ATOM   1102 C CZ   B TYR   A 1 42  ? 32.831 4.797   -9.234  0.40 12.17 ?  42  TYR   A CZ   1 
ATOM   1103 O OH   A TYR   A 1 42  ? 32.480 4.729   -10.626 0.60 15.80 ?  42  TYR   A OH   1 
ATOM   1104 O OH   B TYR   A 1 42  ? 33.035 4.463   -10.552 0.40 12.60 ?  42  TYR   A OH   1 
ATOM   1105 H H    A TYR   A 1 42  ? 30.841 3.621   -4.875  0.60 13.86 ?  42  TYR   A H    1 
ATOM   1106 H H    B TYR   A 1 42  ? 30.861 3.639   -4.893  0.40 13.92 ?  42  TYR   A H    1 
ATOM   1107 H HA   A TYR   A 1 42  ? 33.312 4.491   -4.303  0.60 13.56 ?  42  TYR   A HA   1 
ATOM   1108 H HA   B TYR   A 1 42  ? 33.351 4.413   -4.212  0.40 13.78 ?  42  TYR   A HA   1 
ATOM   1109 H HB2  A TYR   A 1 42  ? 31.056 6.080   -4.904  0.60 14.58 ?  42  TYR   A HB2  1 
ATOM   1110 H HB2  B TYR   A 1 42  ? 31.246 6.107   -5.027  0.40 14.54 ?  42  TYR   A HB2  1 
ATOM   1111 H HB3  A TYR   A 1 42  ? 32.559 6.590   -4.871  0.60 14.58 ?  42  TYR   A HB3  1 
ATOM   1112 H HB3  B TYR   A 1 42  ? 32.770 6.533   -4.881  0.40 14.54 ?  42  TYR   A HB3  1 
ATOM   1113 H HD1  A TYR   A 1 42  ? 34.120 5.405   -6.617  0.60 16.23 ?  42  TYR   A HD1  1 
ATOM   1114 H HD1  B TYR   A 1 42  ? 34.413 5.353   -6.481  0.40 15.57 ?  42  TYR   A HD1  1 
ATOM   1115 H HD2  A TYR   A 1 42  ? 30.144 5.582   -7.002  0.60 17.12 ?  42  TYR   A HD2  1 
ATOM   1116 H HD2  B TYR   A 1 42  ? 30.472 5.443   -7.142  0.40 15.11 ?  42  TYR   A HD2  1 
ATOM   1117 H HE1  A TYR   A 1 42  ? 34.322 4.945   -8.873  0.60 16.59 ?  42  TYR   A HE1  1 
ATOM   1118 H HE1  B TYR   A 1 42  ? 34.773 4.801   -8.695  0.40 15.07 ?  42  TYR   A HE1  1 
ATOM   1119 H HE2  A TYR   A 1 42  ? 30.342 5.123   -9.257  0.60 17.92 ?  42  TYR   A HE2  1 
ATOM   1120 H HE2  B TYR   A 1 42  ? 30.824 4.892   -9.353  0.40 15.12 ?  42  TYR   A HE2  1 
ATOM   1121 H HH   A TYR   A 1 42  ? 31.719 4.696   -10.986 0.60 18.95 ?  42  TYR   A HH   1 
ATOM   1122 H HH   B TYR   A 1 42  ? 33.836 4.239   -10.674 0.40 15.10 ?  42  TYR   A HH   1 
ATOM   1123 N N    . LEU   A 1 43  ? 31.273 4.257   -2.035  1.00 11.07 ?  43  LEU   A N    1 
ATOM   1124 C CA   . LEU   A 1 43  ? 30.832 4.593   -0.682  1.00 10.76 ?  43  LEU   A CA   1 
ATOM   1125 C C    . LEU   A 1 43  ? 30.351 6.039   -0.582  1.00 10.86 ?  43  LEU   A C    1 
ATOM   1126 O O    . LEU   A 1 43  ? 30.623 6.739   0.395   1.00 12.02 ?  43  LEU   A O    1 
ATOM   1127 C CB   . LEU   A 1 43  ? 31.888 4.275   0.376   1.00 11.13 ?  43  LEU   A CB   1 
ATOM   1128 C CG   . LEU   A 1 43  ? 32.374 2.825   0.451   1.00 11.30 ?  43  LEU   A CG   1 
ATOM   1129 C CD1  . LEU   A 1 43  ? 33.458 2.702   1.516   1.00 12.64 ?  43  LEU   A CD1  1 
ATOM   1130 C CD2  . LEU   A 1 43  ? 31.232 1.850   0.737   1.00 12.04 ?  43  LEU   A CD2  1 
ATOM   1131 H H    A LEU   A 1 43  ? 30.918 3.530   -2.336  0.60 13.27 ?  43  LEU   A H    1 
ATOM   1132 H H    B LEU   A 1 43  ? 30.943 3.514   -2.326  0.40 13.27 ?  43  LEU   A H    1 
ATOM   1133 H HA   . LEU   A 1 43  ? 30.065 4.032   -0.477  1.00 12.90 ?  43  LEU   A HA   1 
ATOM   1134 H HB2  . LEU   A 1 43  ? 32.663 4.832   0.210   1.00 13.34 ?  43  LEU   A HB2  1 
ATOM   1135 H HB3  . LEU   A 1 43  ? 31.518 4.493   1.248   1.00 13.34 ?  43  LEU   A HB3  1 
ATOM   1136 H HG   . LEU   A 1 43  ? 32.770 2.581   -0.401  1.00 13.55 ?  43  LEU   A HG   1 
ATOM   1137 H HD11 . LEU   A 1 43  ? 33.764 1.782   1.555   1.00 15.16 ?  43  LEU   A HD11 1 
ATOM   1138 H HD12 . LEU   A 1 43  ? 34.200 3.286   1.283   1.00 15.16 ?  43  LEU   A HD12 1 
ATOM   1139 H HD13 . LEU   A 1 43  ? 33.091 2.966   2.374   1.00 15.16 ?  43  LEU   A HD13 1 
ATOM   1140 H HD21 . LEU   A 1 43  ? 31.602 0.965   0.865   1.00 14.44 ?  43  LEU   A HD21 1 
ATOM   1141 H HD22 . LEU   A 1 43  ? 30.772 2.140   1.540   1.00 14.44 ?  43  LEU   A HD22 1 
ATOM   1142 H HD23 . LEU   A 1 43  ? 30.625 1.855   -0.016  1.00 14.44 ?  43  LEU   A HD23 1 
ATOM   1143 N N    . LYS   A 1 44  ? 29.618 6.482   -1.605  1.00 10.95 ?  44  LYS   A N    1 
ATOM   1144 C CA   . LYS   A 1 44  ? 28.976 7.797   -1.605  1.00 11.77 ?  44  LYS   A CA   1 
ATOM   1145 C C    . LYS   A 1 44  ? 27.555 7.602   -1.095  1.00 10.62 ?  44  LYS   A C    1 
ATOM   1146 O O    . LYS   A 1 44  ? 26.685 7.096   -1.809  1.00 11.74 ?  44  LYS   A O    1 
ATOM   1147 C CB   . LYS   A 1 44  ? 29.013 8.413   -2.997  1.00 13.87 ?  44  LYS   A CB   1 
ATOM   1148 C CG   . LYS   A 1 44  ? 30.387 8.902   -3.422  1.00 17.89 ?  44  LYS   A CG   1 
ATOM   1149 C CD   . LYS   A 1 44  ? 31.046 9.798   -2.370  1.00 23.97 ?  44  LYS   A CD   1 
ATOM   1150 C CE   . LYS   A 1 44  ? 32.389 10.323  -2.844  1.00 27.66 ?  44  LYS   A CE   1 
ATOM   1151 N NZ   . LYS   A 1 44  ? 33.206 10.883  -1.731  1.00 29.60 ?  44  LYS   A NZ   1 
ATOM   1152 H H    . LYS   A 1 44  ? 29.469 6.025   -2.321  1.00 13.13 ?  44  LYS   A H    1 
ATOM   1153 H HA   . LYS   A 1 44  ? 29.428 8.376   -0.977  1.00 14.11 ?  44  LYS   A HA   1 
ATOM   1154 H HB2  . LYS   A 1 44  ? 28.726 7.751   -3.644  1.00 16.63 ?  44  LYS   A HB2  1 
ATOM   1155 H HB3  . LYS   A 1 44  ? 28.412 9.175   -3.018  1.00 16.63 ?  44  LYS   A HB3  1 
ATOM   1156 H HG2  . LYS   A 1 44  ? 30.966 8.142   -3.575  1.00 21.46 ?  44  LYS   A HG2  1 
ATOM   1157 H HG3  . LYS   A 1 44  ? 30.302 9.424   -4.241  1.00 21.46 ?  44  LYS   A HG3  1 
ATOM   1158 H HD2  . LYS   A 1 44  ? 30.459 10.547  -2.177  1.00 28.75 ?  44  LYS   A HD2  1 
ATOM   1159 H HD3  . LYS   A 1 44  ? 31.202 9.277   -1.564  1.00 28.75 ?  44  LYS   A HD3  1 
ATOM   1160 H HE2  . LYS   A 1 44  ? 32.889 9.593   -3.244  1.00 33.18 ?  44  LYS   A HE2  1 
ATOM   1161 H HE3  . LYS   A 1 44  ? 32.241 11.023  -3.494  1.00 33.18 ?  44  LYS   A HE3  1 
ATOM   1162 H HZ1  . LYS   A 1 44  ? 33.983 11.181  -2.045  1.00 35.51 ?  44  LYS   A HZ1  1 
ATOM   1163 H HZ2  . LYS   A 1 44  ? 32.771 11.560  -1.346  1.00 35.51 ?  44  LYS   A HZ2  1 
ATOM   1164 H HZ3  . LYS   A 1 44  ? 33.361 10.256  -1.119  1.00 35.51 ?  44  LYS   A HZ3  1 
ATOM   1165 N N    A HIS   A 1 45  ? 27.320 7.992   0.153   0.60 10.43 ?  45  HIS   A N    1 
ATOM   1166 N N    B HIS   A 1 45  ? 27.321 7.998   0.155   0.40 11.01 ?  45  HIS   A N    1 
ATOM   1167 C CA   A HIS   A 1 45  ? 26.087 7.640   0.856   0.60 10.35 ?  45  HIS   A CA   1 
ATOM   1168 C CA   B HIS   A 1 45  ? 26.070 7.702   0.852   0.40 11.32 ?  45  HIS   A CA   1 
ATOM   1169 C C    A HIS   A 1 45  ? 25.059 8.765   0.713   0.60 10.89 ?  45  HIS   A C    1 
ATOM   1170 C C    B HIS   A 1 45  ? 25.102 8.858   0.637   0.40 12.01 ?  45  HIS   A C    1 
ATOM   1171 O O    A HIS   A 1 45  ? 24.675 9.434   1.673   0.60 11.19 ?  45  HIS   A O    1 
ATOM   1172 O O    B HIS   A 1 45  ? 24.997 9.770   1.457   0.40 12.53 ?  45  HIS   A O    1 
ATOM   1173 C CB   A HIS   A 1 45  ? 26.402 7.352   2.315   0.60 10.24 ?  45  HIS   A CB   1 
ATOM   1174 C CB   B HIS   A 1 45  ? 26.344 7.483   2.332   0.40 10.94 ?  45  HIS   A CB   1 
ATOM   1175 C CG   A HIS   A 1 45  ? 27.511 6.366   2.506   0.60 9.69  ?  45  HIS   A CG   1 
ATOM   1176 C CG   B HIS   A 1 45  ? 27.468 6.534   2.599   0.40 10.48 ?  45  HIS   A CG   1 
ATOM   1177 N ND1  A HIS   A 1 45  ? 27.481 5.090   1.978   0.60 9.96  ?  45  HIS   A ND1  1 
ATOM   1178 N ND1  B HIS   A 1 45  ? 27.476 5.237   2.131   0.40 11.09 ?  45  HIS   A ND1  1 
ATOM   1179 C CD2  A HIS   A 1 45  ? 28.696 6.483   3.154   0.60 10.92 ?  45  HIS   A CD2  1 
ATOM   1180 C CD2  B HIS   A 1 45  ? 28.629 6.701   3.277   0.40 9.80  ?  45  HIS   A CD2  1 
ATOM   1181 C CE1  A HIS   A 1 45  ? 28.594 4.461   2.313   0.60 10.71 ?  45  HIS   A CE1  1 
ATOM   1182 C CE1  B HIS   A 1 45  ? 28.591 4.644   2.518   0.40 9.72  ?  45  HIS   A CE1  1 
ATOM   1183 N NE2  A HIS   A 1 45  ? 29.349 5.283   3.024   0.60 10.94 ?  45  HIS   A NE2  1 
ATOM   1184 N NE2  B HIS   A 1 45  ? 29.308 5.509   3.214   0.40 9.12  ?  45  HIS   A NE2  1 
ATOM   1185 H H    A HIS   A 1 45  ? 27.863 8.467   0.622   0.60 12.50 ?  45  HIS   A H    1 
ATOM   1186 H H    B HIS   A 1 45  ? 27.880 8.450   0.629   0.40 13.20 ?  45  HIS   A H    1 
ATOM   1187 H HA   A HIS   A 1 45  ? 25.711 6.838   0.466   0.60 12.41 ?  45  HIS   A HA   1 
ATOM   1188 H HA   B HIS   A 1 45  ? 25.672 6.901   0.486   0.40 13.58 ?  45  HIS   A HA   1 
ATOM   1189 H HB2  A HIS   A 1 45  ? 26.659 8.178   2.755   0.60 12.28 ?  45  HIS   A HB2  1 
ATOM   1190 H HB2  B HIS   A 1 45  ? 26.567 8.334   2.740   0.40 13.11 ?  45  HIS   A HB2  1 
ATOM   1191 H HB3  A HIS   A 1 45  ? 25.609 6.987   2.744   0.60 12.28 ?  45  HIS   A HB3  1 
ATOM   1192 H HB3  B HIS   A 1 45  ? 25.544 7.120   2.746   0.40 13.11 ?  45  HIS   A HB3  1 
ATOM   1193 H HD2  A HIS   A 1 45  ? 29.010 7.233   3.611   0.60 13.10 ?  45  HIS   A HD2  1 
ATOM   1194 H HD2  B HIS   A 1 45  ? 28.912 7.477   3.708   0.40 11.74 ?  45  HIS   A HD2  1 
ATOM   1195 H HE1  A HIS   A 1 45  ? 28.815 3.583   2.094   0.60 12.84 ?  45  HIS   A HE1  1 
ATOM   1196 H HE1  B HIS   A 1 45  ? 28.829 3.765   2.331   0.40 11.65 ?  45  HIS   A HE1  1 
ATOM   1197 H HE2  A HIS   A 1 45  ? 30.126 5.094   3.354   0.60 13.12 ?  45  HIS   A HE2  1 
ATOM   1198 H HE2  B HIS   A 1 45  ? 30.074 5.350   3.570   0.40 10.93 ?  45  HIS   A HE2  1 
ATOM   1199 N N    A GLY   A 1 46  ? 24.599 8.955   -0.521  0.60 12.24 ?  46  GLY   A N    1 
ATOM   1200 N N    B GLY   A 1 46  ? 24.367 8.808   -0.469  0.40 12.24 ?  46  GLY   A N    1 
ATOM   1201 C CA   A GLY   A 1 46  ? 23.806 10.129  -0.846  0.60 13.23 ?  46  GLY   A CA   1 
ATOM   1202 C CA   B GLY   A 1 46  ? 23.526 9.928   -0.843  0.40 12.17 ?  46  GLY   A CA   1 
ATOM   1203 C C    A GLY   A 1 46  ? 22.305 9.996   -0.662  0.60 13.20 ?  46  GLY   A C    1 
ATOM   1204 C C    B GLY   A 1 46  ? 22.071 9.801   -0.443  0.40 11.40 ?  46  GLY   A C    1 
ATOM   1205 O O    A GLY   A 1 46  ? 21.612 10.991  -0.420  0.60 13.48 ?  46  GLY   A O    1 
ATOM   1206 O O    B GLY   A 1 46  ? 21.467 10.762  0.046   0.40 11.83 ?  46  GLY   A O    1 
ATOM   1207 H H    A GLY   A 1 46  ? 24.721 8.414   -1.176  0.60 14.68 ?  46  GLY   A H    1 
ATOM   1208 H H    B GLY   A 1 46  ? 24.338 8.137   -1.007  0.40 14.67 ?  46  GLY   A H    1 
ATOM   1209 H HA2  A GLY   A 1 46  ? 24.114 10.871  -0.300  0.60 15.87 ?  46  GLY   A HA2  1 
ATOM   1210 H HA2  B GLY   A 1 46  ? 23.865 10.734  -0.429  0.40 14.59 ?  46  GLY   A HA2  1 
ATOM   1211 H HA3  A GLY   A 1 46  ? 23.963 10.359  -1.773  0.60 15.87 ?  46  GLY   A HA3  1 
ATOM   1212 H HA3  B GLY   A 1 46  ? 23.565 10.041  -1.802  0.40 14.59 ?  46  GLY   A HA3  1 
ATOM   1213 N N    A GLY   A 1 47  ? 21.786 8.782   -0.794  0.60 12.71 ?  47  GLY   A N    1 
ATOM   1214 N N    B GLY   A 1 47  ? 21.492 8.625   -0.649  0.40 11.15 ?  47  GLY   A N    1 
ATOM   1215 C CA   A GLY   A 1 47  ? 20.353 8.565   -0.779  0.60 12.75 ?  47  GLY   A CA   1 
ATOM   1216 C CA   B GLY   A 1 47  ? 20.073 8.451   -0.420  0.40 11.35 ?  47  GLY   A CA   1 
ATOM   1217 C C    A GLY   A 1 47  ? 20.043 7.131   -0.409  0.60 12.08 ?  47  GLY   A C    1 
ATOM   1218 C C    B GLY   A 1 47  ? 19.726 7.019   -0.096  0.40 10.36 ?  47  GLY   A C    1 
ATOM   1219 O O    A GLY   A 1 47  ? 20.936 6.321   -0.149  0.60 13.16 ?  47  GLY   A O    1 
ATOM   1220 O O    B GLY   A 1 47  ? 20.617 6.172   0.033   0.40 9.90  ?  47  GLY   A O    1 
ATOM   1221 H H    A GLY   A 1 47  ? 22.248 8.070   -0.886  0.60 15.23 ?  47  GLY   A H    1 
ATOM   1222 H H    B GLY   A 1 47  ? 21.901 7.910   -0.907  0.40 13.37 ?  47  GLY   A H    1 
ATOM   1223 H HA2  A GLY   A 1 47  ? 19.930 9.164   -0.140  0.60 15.29 ?  47  GLY   A HA2  1 
ATOM   1224 H HA2  B GLY   A 1 47  ? 19.788 9.005   0.321   0.40 13.60 ?  47  GLY   A HA2  1 
ATOM   1225 H HA3  A GLY   A 1 47  ? 19.989 8.748   -1.662  0.60 15.29 ?  47  GLY   A HA3  1 
ATOM   1226 H HA3  B GLY   A 1 47  ? 19.578 8.712   -1.211  0.40 13.60 ?  47  GLY   A HA3  1 
ATOM   1227 N N    A GLY   A 1 48  ? 18.751 6.816   -0.408  0.60 11.91 ?  48  GLY   A N    1 
ATOM   1228 N N    B GLY   A 1 48  ? 18.434 6.725   0.030   0.40 10.97 ?  48  GLY   A N    1 
ATOM   1229 C CA   A GLY   A 1 48  ? 18.320 5.493   -0.022  0.60 12.50 ?  48  GLY   A CA   1 
ATOM   1230 C CA   B GLY   A 1 48  ? 18.104 5.363   0.371   0.40 10.74 ?  48  GLY   A CA   1 
ATOM   1231 C C    A GLY   A 1 48  ? 18.695 5.178   1.413   0.60 11.80 ?  48  GLY   A C    1 
ATOM   1232 C C    B GLY   A 1 48  ? 18.614 5.020   1.759   0.40 10.37 ?  48  GLY   A C    1 
ATOM   1233 O O    A GLY   A 1 48  ? 18.842 6.066   2.259   0.60 11.93 ?  48  GLY   A O    1 
ATOM   1234 O O    B GLY   A 1 48  ? 18.697 5.867   2.656   0.40 10.09 ?  48  GLY   A O    1 
ATOM   1235 H H    A GLY   A 1 48  ? 18.118 7.348   -0.626  0.60 14.28 ?  48  GLY   A H    1 
ATOM   1236 H H    B GLY   A 1 48  ? 17.758 7.268   -0.058  0.40 13.15 ?  48  GLY   A H    1 
ATOM   1237 H HA2  A GLY   A 1 48  ? 17.362 5.422   -0.111  0.60 14.99 ?  48  GLY   A HA2  1 
ATOM   1238 H HA2  B GLY   A 1 48  ? 17.150 5.216   0.323   0.40 12.87 ?  48  GLY   A HA2  1 
ATOM   1239 H HA3  A GLY   A 1 48  ? 18.742 4.831   -0.590  0.60 14.99 ?  48  GLY   A HA3  1 
ATOM   1240 H HA3  B GLY   A 1 48  ? 18.537 4.765   -0.267  0.40 12.87 ?  48  GLY   A HA3  1 
ATOM   1241 N N    A VAL   A 1 49  ? 18.853 3.880   1.690   0.60 11.90 ?  49  VAL   A N    1 
ATOM   1242 N N    B VAL   A 1 49  ? 18.967 3.747   1.929   0.40 10.36 ?  49  VAL   A N    1 
ATOM   1243 C CA   A VAL   A 1 49  ? 19.279 3.445   3.017   0.60 11.67 ?  49  VAL   A CA   1 
ATOM   1244 C CA   B VAL   A 1 49  ? 19.537 3.282   3.189   0.40 10.60 ?  49  VAL   A CA   1 
ATOM   1245 C C    A VAL   A 1 49  ? 20.612 4.083   3.393   0.60 10.99 ?  49  VAL   A C    1 
ATOM   1246 C C    B VAL   A 1 49  ? 20.819 4.040   3.513   0.40 9.93  ?  49  VAL   A C    1 
ATOM   1247 O O    A VAL   A 1 49  ? 20.807 4.510   4.536   0.60 11.86 ?  49  VAL   A O    1 
ATOM   1248 O O    B VAL   A 1 49  ? 21.037 4.463   4.655   0.40 9.70  ?  49  VAL   A O    1 
ATOM   1249 C CB   A VAL   A 1 49  ? 19.339 1.905   3.080   0.60 12.57 ?  49  VAL   A CB   1 
ATOM   1250 C CB   B VAL   A 1 49  ? 19.783 1.765   3.126   0.40 11.11 ?  49  VAL   A CB   1 
ATOM   1251 C CG1  A VAL   A 1 49  ? 20.061 1.448   4.340   0.60 13.36 ?  49  VAL   A CG1  1 
ATOM   1252 C CG1  B VAL   A 1 49  ? 20.638 1.324   4.304   0.40 10.37 ?  49  VAL   A CG1  1 
ATOM   1253 C CG2  A VAL   A 1 49  ? 17.934 1.314   3.024   0.60 13.70 ?  49  VAL   A CG2  1 
ATOM   1254 C CG2  B VAL   A 1 49  ? 18.466 1.010   3.083   0.40 11.72 ?  49  VAL   A CG2  1 
ATOM   1255 H H    A VAL   A 1 49  ? 18.726 3.238   1.134   0.60 14.27 ?  49  VAL   A H    1 
ATOM   1256 H H    B VAL   A 1 49  ? 18.887 3.132   1.333   0.40 12.42 ?  49  VAL   A H    1 
ATOM   1257 H HA   A VAL   A 1 49  ? 18.625 3.730   3.670   0.60 14.00 ?  49  VAL   A HA   1 
ATOM   1258 H HA   B VAL   A 1 49  ? 18.909 3.452   3.905   0.40 12.71 ?  49  VAL   A HA   1 
ATOM   1259 H HB   A VAL   A 1 49  ? 19.839 1.570   2.318   0.60 15.07 ?  49  VAL   A HB   1 
ATOM   1260 H HB   B VAL   A 1 49  ? 20.269 1.560   2.311   0.40 13.32 ?  49  VAL   A HB   1 
ATOM   1261 H HG11 A VAL   A 1 49  ? 19.845 0.516   4.505   0.60 16.01 ?  49  VAL   A HG11 1 
ATOM   1262 H HG11 B VAL   A 1 49  ? 20.529 0.370   4.433   0.40 12.43 ?  49  VAL   A HG11 1 
ATOM   1263 H HG12 A VAL   A 1 49  ? 21.016 1.549   4.217   0.60 16.01 ?  49  VAL   A HG12 1 
ATOM   1264 H HG12 B VAL   A 1 49  ? 21.571 1.523   4.114   0.40 12.43 ?  49  VAL   A HG12 1 
ATOM   1265 H HG13 A VAL   A 1 49  ? 19.760 1.991   5.087   0.60 16.01 ?  49  VAL   A HG13 1 
ATOM   1266 H HG13 B VAL   A 1 49  ? 20.353 1.799   5.099   0.40 12.43 ?  49  VAL   A HG13 1 
ATOM   1267 H HG21 A VAL   A 1 49  ? 17.996 0.346   3.059   0.60 16.43 ?  49  VAL   A HG21 1 
ATOM   1268 H HG21 B VAL   A 1 49  ? 18.647 0.062   2.994   0.40 14.05 ?  49  VAL   A HG21 1 
ATOM   1269 H HG22 A VAL   A 1 49  ? 17.427 1.641   3.783   0.60 16.43 ?  49  VAL   A HG22 1 
ATOM   1270 H HG22 B VAL   A 1 49  ? 17.980 1.179   3.906   0.40 14.05 ?  49  VAL   A HG22 1 
ATOM   1271 H HG23 A VAL   A 1 49  ? 17.513 1.591   2.197   0.60 16.43 ?  49  VAL   A HG23 1 
ATOM   1272 H HG23 B VAL   A 1 49  ? 17.948 1.321   2.324   0.40 14.05 ?  49  VAL   A HG23 1 
ATOM   1273 N N    A ALA   A 1 50  ? 21.559 4.127   2.451   0.60 10.60 ?  50  ALA   A N    1 
ATOM   1274 N N    B ALA   A 1 50  ? 21.704 4.192   2.524   0.40 9.93  ?  50  ALA   A N    1 
ATOM   1275 C CA   A ALA   A 1 50  ? 22.879 4.682   2.744   0.60 10.60 ?  50  ALA   A CA   1 
ATOM   1276 C CA   B ALA   A 1 50  ? 23.018 4.765   2.796   0.40 9.80  ?  50  ALA   A CA   1 
ATOM   1277 C C    A ALA   A 1 50  ? 22.788 6.141   3.171   0.60 10.75 ?  50  ALA   A C    1 
ATOM   1278 C C    B ALA   A 1 50  ? 22.908 6.220   3.234   0.40 9.22  ?  50  ALA   A C    1 
ATOM   1279 O O    A ALA   A 1 50  ? 23.461 6.562   4.121   0.60 11.58 ?  50  ALA   A O    1 
ATOM   1280 O O    B ALA   A 1 50  ? 23.491 6.619   4.251   0.40 9.34  ?  50  ALA   A O    1 
ATOM   1281 C CB   A ALA   A 1 50  ? 23.778 4.550   1.518   0.60 10.50 ?  50  ALA   A CB   1 
ATOM   1282 C CB   B ALA   A 1 50  ? 23.919 4.632   1.567   0.40 9.49  ?  50  ALA   A CB   1 
ATOM   1283 H H    A ALA   A 1 50  ? 21.469 3.830   1.653   0.60 12.71 ?  50  ALA   A H    1 
ATOM   1284 H H    B ALA   A 1 50  ? 21.567 3.979   1.700   0.40 11.90 ?  50  ALA   A H    1 
ATOM   1285 H HA   A ALA   A 1 50  ? 23.286 4.184   3.472   0.60 12.71 ?  50  ALA   A HA   1 
ATOM   1286 H HA   B ALA   A 1 50  ? 23.432 4.274   3.519   0.40 11.75 ?  50  ALA   A HA   1 
ATOM   1287 H HB1  A ALA   A 1 50  ? 24.649 4.927   1.721   0.60 12.59 ?  50  ALA   A HB1  1 
ATOM   1288 H HB1  B ALA   A 1 50  ? 24.788 5.018   1.766   0.40 11.37 ?  50  ALA   A HB1  1 
ATOM   1289 H HB2  A ALA   A 1 50  ? 23.867 3.612   1.289   0.60 12.59 ?  50  ALA   A HB2  1 
ATOM   1290 H HB2  B ALA   A 1 50  ? 24.022 3.691   1.349   0.40 11.37 ?  50  ALA   A HB2  1 
ATOM   1291 H HB3  A ALA   A 1 50  ? 23.374 5.034   0.779   0.60 12.59 ?  50  ALA   A HB3  1 
ATOM   1292 H HB3  B ALA   A 1 50  ? 23.514 5.101   0.821   0.40 11.37 ?  50  ALA   A HB3  1 
ATOM   1293 N N    A GLY   A 1 51  ? 21.976 6.932   2.472   0.60 11.00 ?  51  GLY   A N    1 
ATOM   1294 N N    B GLY   A 1 51  ? 22.171 7.033   2.477   0.40 9.73  ?  51  GLY   A N    1 
ATOM   1295 C CA   A GLY   A 1 51  ? 21.813 8.320   2.866   0.60 11.56 ?  51  GLY   A CA   1 
ATOM   1296 C CA   B GLY   A 1 51  ? 22.015 8.424   2.862   0.40 9.66  ?  51  GLY   A CA   1 
ATOM   1297 C C    A GLY   A 1 51  ? 21.253 8.454   4.268   0.60 11.72 ?  51  GLY   A C    1 
ATOM   1298 C C    B GLY   A 1 51  ? 21.355 8.568   4.220   0.40 9.94  ?  51  GLY   A C    1 
ATOM   1299 O O    A GLY   A 1 51  ? 21.678 9.321   5.036   0.60 12.51 ?  51  GLY   A O    1 
ATOM   1300 O O    B GLY   A 1 51  ? 21.697 9.465   4.995   0.40 10.42 ?  51  GLY   A O    1 
ATOM   1301 H H    A GLY   A 1 51  ? 21.533 6.691   1.775   0.60 13.19 ?  51  GLY   A H    1 
ATOM   1302 H H    B GLY   A 1 51  ? 21.767 6.806   1.753   0.40 11.67 ?  51  GLY   A H    1 
ATOM   1303 H HA2  A GLY   A 1 51  ? 22.672 8.769   2.832   0.60 13.85 ?  51  GLY   A HA2  1 
ATOM   1304 H HA2  B GLY   A 1 51  ? 22.887 8.852   2.894   0.40 11.58 ?  51  GLY   A HA2  1 
ATOM   1305 H HA3  A GLY   A 1 51  ? 21.210 8.760   2.247   0.60 13.85 ?  51  GLY   A HA3  1 
ATOM   1306 H HA3  B GLY   A 1 51  ? 21.473 8.882   2.200   0.40 11.58 ?  51  GLY   A HA3  1 
ATOM   1307 N N    A ALA   A 1 52  ? 20.292 7.595   4.621   0.60 11.54 ?  52  ALA   A N    1 
ATOM   1308 N N    B ALA   A 1 52  ? 20.400 7.685   4.525   0.40 10.06 ?  52  ALA   A N    1 
ATOM   1309 C CA   A ALA   A 1 52  ? 19.676 7.668   5.942   0.60 11.90 ?  52  ALA   A CA   1 
ATOM   1310 C CA   B ALA   A 1 52  ? 19.721 7.731   5.816   0.40 10.90 ?  52  ALA   A CA   1 
ATOM   1311 C C    A ALA   A 1 52  ? 20.638 7.225   7.042   0.60 10.76 ?  52  ALA   A C    1 
ATOM   1312 C C    B ALA   A 1 52  ? 20.657 7.328   6.953   0.40 10.22 ?  52  ALA   A C    1 
ATOM   1313 O O    A ALA   A 1 52  ? 20.717 7.866   8.097   0.60 11.59 ?  52  ALA   A O    1 
ATOM   1314 O O    B ALA   A 1 52  ? 20.717 8.001   7.988   0.40 11.24 ?  52  ALA   A O    1 
ATOM   1315 C CB   A ALA   A 1 52  ? 18.388 6.846   5.962   0.60 13.30 ?  52  ALA   A CB   1 
ATOM   1316 C CB   B ALA   A 1 52  ? 18.479 6.839   5.781   0.40 11.91 ?  52  ALA   A CB   1 
ATOM   1317 H H    A ALA   A 1 52  ? 19.998 6.957   4.120   0.60 13.83 ?  52  ALA   A H    1 
ATOM   1318 H H    B ALA   A 1 52  ? 20.141 7.049   4.006   0.40 12.06 ?  52  ALA   A H    1 
ATOM   1319 H HA   A ALA   A 1 52  ? 19.442 8.587   6.114   0.60 14.27 ?  52  ALA   A HA   1 
ATOM   1320 H HA   B ALA   A 1 52  ? 19.426 8.640   5.977   0.40 13.06 ?  52  ALA   A HA   1 
ATOM   1321 H HB1  A ALA   A 1 52  ? 17.988 6.913   6.843   0.60 15.95 ?  52  ALA   A HB1  1 
ATOM   1322 H HB1  B ALA   A 1 52  ? 18.036 6.883   6.644   0.40 14.28 ?  52  ALA   A HB1  1 
ATOM   1323 H HB2  A ALA   A 1 52  ? 17.778 7.204   5.295   0.60 15.95 ?  52  ALA   A HB2  1 
ATOM   1324 H HB2  B ALA   A 1 52  ? 17.879 7.158   5.087   0.40 14.28 ?  52  ALA   A HB2  1 
ATOM   1325 H HB3  A ALA   A 1 52  ? 18.595 5.922   5.758   0.60 15.95 ?  52  ALA   A HB3  1 
ATOM   1326 H HB3  B ALA   A 1 52  ? 18.748 5.928   5.593   0.40 14.28 ?  52  ALA   A HB3  1 
ATOM   1327 N N    A LEU   A 1 53  ? 21.365 6.123   6.833   0.60 11.14 ?  53  LEU   A N    1 
ATOM   1328 N N    B LEU   A 1 53  ? 21.388 6.221   6.789   0.40 10.35 ?  53  LEU   A N    1 
ATOM   1329 C CA   A LEU   A 1 53  ? 22.336 5.698   7.839   0.60 11.09 ?  53  LEU   A CA   1 
ATOM   1330 C CA   B LEU   A 1 53  ? 22.367 5.827   7.802   0.40 10.38 ?  53  LEU   A CA   1 
ATOM   1331 C C    A LEU   A 1 53  ? 23.407 6.760   8.037   0.60 10.80 ?  53  LEU   A C    1 
ATOM   1332 C C    B LEU   A 1 53  ? 23.399 6.926   8.006   0.40 9.88  ?  53  LEU   A C    1 
ATOM   1333 O O    A LEU   A 1 53  ? 23.792 7.066   9.172   0.60 11.72 ?  53  LEU   A O    1 
ATOM   1334 O O    B LEU   A 1 53  ? 23.676 7.335   9.139   0.40 10.28 ?  53  LEU   A O    1 
ATOM   1335 C CB   A LEU   A 1 53  ? 22.966 4.358   7.446   0.60 11.50 ?  53  LEU   A CB   1 
ATOM   1336 C CB   B LEU   A 1 53  ? 23.068 4.522   7.405   0.40 10.68 ?  53  LEU   A CB   1 
ATOM   1337 C CG   A LEU   A 1 53  ? 22.016 3.151   7.456   0.60 11.69 ?  53  LEU   A CG   1 
ATOM   1338 C CG   B LEU   A 1 53  ? 22.350 3.171   7.540   0.40 10.88 ?  53  LEU   A CG   1 
ATOM   1339 C CD1  A LEU   A 1 53  ? 22.713 1.924   6.883   0.60 11.82 ?  53  LEU   A CD1  1 
ATOM   1340 C CD1  B LEU   A 1 53  ? 23.196 2.078   6.899   0.40 11.10 ?  53  LEU   A CD1  1 
ATOM   1341 C CD2  A LEU   A 1 53  ? 21.504 2.871   8.858   0.60 12.49 ?  53  LEU   A CD2  1 
ATOM   1342 C CD2  B LEU   A 1 53  ? 22.052 2.814   8.989   0.40 10.78 ?  53  LEU   A CD2  1 
ATOM   1343 H H    A LEU   A 1 53  ? 21.314 5.613   6.136   0.60 13.35 ?  53  LEU   A H    1 
ATOM   1344 H H    B LEU   A 1 53  ? 21.334 5.692   6.114   0.40 12.41 ?  53  LEU   A H    1 
ATOM   1345 H HA   A LEU   A 1 53  ? 21.877 5.571   8.683   0.60 13.30 ?  53  LEU   A HA   1 
ATOM   1346 H HA   B LEU   A 1 53  ? 21.909 5.684   8.644   0.40 12.44 ?  53  LEU   A HA   1 
ATOM   1347 H HB2  A LEU   A 1 53  ? 23.326 4.436   6.546   0.60 13.79 ?  53  LEU   A HB2  1 
ATOM   1348 H HB2  B LEU   A 1 53  ? 23.319 4.604   6.473   0.40 12.81 ?  53  LEU   A HB2  1 
ATOM   1349 H HB3  A LEU   A 1 53  ? 23.687 4.161   8.064   0.60 13.79 ?  53  LEU   A HB3  1 
ATOM   1350 H HB3  B LEU   A 1 53  ? 23.872 4.457   7.940   0.40 12.81 ?  53  LEU   A HB3  1 
ATOM   1351 H HG   A LEU   A 1 53  ? 21.254 3.348   6.888   0.60 14.02 ?  53  LEU   A HG   1 
ATOM   1352 H HG   B LEU   A 1 53  ? 21.510 3.209   7.061   0.40 13.05 ?  53  LEU   A HG   1 
ATOM   1353 H HD11 A LEU   A 1 53  ? 22.094 1.175   6.896   0.60 14.18 ?  53  LEU   A HD11 1 
ATOM   1354 H HD11 B LEU   A 1 53  ? 22.740 1.226   6.992   0.40 13.31 ?  53  LEU   A HD11 1 
ATOM   1355 H HD12 A LEU   A 1 53  ? 22.987 2.109   5.972   0.60 14.18 ?  53  LEU   A HD12 1 
ATOM   1356 H HD12 B LEU   A 1 53  ? 23.321 2.283   5.958   0.40 13.31 ?  53  LEU   A HD12 1 
ATOM   1357 H HD13 A LEU   A 1 53  ? 23.490 1.719   7.427   0.60 14.18 ?  53  LEU   A HD13 1 
ATOM   1358 H HD13 B LEU   A 1 53  ? 24.058 2.040   7.345   0.40 13.31 ?  53  LEU   A HD13 1 
ATOM   1359 H HD21 A LEU   A 1 53  ? 21.024 2.028   8.856   0.60 14.98 ?  53  LEU   A HD21 1 
ATOM   1360 H HD21 B LEU   A 1 53  ? 21.467 2.039   9.010   0.40 12.92 ?  53  LEU   A HD21 1 
ATOM   1361 H HD22 A LEU   A 1 53  ? 22.257 2.822   9.466   0.60 14.98 ?  53  LEU   A HD22 1 
ATOM   1362 H HD22 B LEU   A 1 53  ? 22.883 2.614   9.446   0.40 12.92 ?  53  LEU   A HD22 1 
ATOM   1363 H HD23 A LEU   A 1 53  ? 20.909 3.588   9.126   0.60 14.98 ?  53  LEU   A HD23 1 
ATOM   1364 H HD23 B LEU   A 1 53  ? 21.613 3.567   9.415   0.40 12.92 ?  53  LEU   A HD23 1 
ATOM   1365 N N    A ASN   A 1 54  ? 23.890 7.348   6.945   0.60 10.72 ?  54  ASN   A N    1 
ATOM   1366 N N    B ASN   A 1 54  ? 23.983 7.420   6.911   0.40 10.07 ?  54  ASN   A N    1 
ATOM   1367 C CA   A ASN   A 1 54  ? 24.954 8.335   7.081   0.60 10.38 ?  54  ASN   A CA   1 
ATOM   1368 C CA   B ASN   A 1 54  ? 25.026 8.428   7.044   0.40 10.03 ?  54  ASN   A CA   1 
ATOM   1369 C C    A ASN   A 1 54  ? 24.458 9.586   7.805   0.60 10.89 ?  54  ASN   A C    1 
ATOM   1370 C C    B ASN   A 1 54  ? 24.501 9.669   7.753   0.40 10.80 ?  54  ASN   A C    1 
ATOM   1371 O O    A ASN   A 1 54  ? 25.141 10.111  8.695   0.60 11.12 ?  54  ASN   A O    1 
ATOM   1372 O O    B ASN   A 1 54  ? 25.200 10.265  8.581   0.40 11.23 ?  54  ASN   A O    1 
ATOM   1373 C CB   A ASN   A 1 54  ? 25.521 8.685   5.712   0.60 10.86 ?  54  ASN   A CB   1 
ATOM   1374 C CB   B ASN   A 1 54  ? 25.595 8.804   5.680   0.40 10.40 ?  54  ASN   A CB   1 
ATOM   1375 C CG   A ASN   A 1 54  ? 26.578 9.761   5.804   0.60 10.83 ?  54  ASN   A CG   1 
ATOM   1376 C CG   B ASN   A 1 54  ? 26.551 9.967   5.775   0.40 10.28 ?  54  ASN   A CG   1 
ATOM   1377 O OD1  A ASN   A 1 54  ? 27.570 9.607   6.518   0.60 10.65 ?  54  ASN   A OD1  1 
ATOM   1378 O OD1  B ASN   A 1 54  ? 27.585 9.865   6.434   0.40 10.19 ?  54  ASN   A OD1  1 
ATOM   1379 N ND2  A ASN   A 1 54  ? 26.371 10.862  5.107   0.60 11.42 ?  54  ASN   A ND2  1 
ATOM   1380 N ND2  B ASN   A 1 54  ? 26.205 11.087  5.150   0.40 11.11 ?  54  ASN   A ND2  1 
ATOM   1381 H H    A ASN   A 1 54  ? 23.624 7.192   6.142   0.60 12.85 ?  54  ASN   A H    1 
ATOM   1382 H H    B ASN   A 1 54  ? 23.794 7.193   6.105   0.40 12.08 ?  54  ASN   A H    1 
ATOM   1383 H HA   A ASN   A 1 54  ? 25.665 7.944   7.607   0.60 12.45 ?  54  ASN   A HA   1 
ATOM   1384 H HA   B ASN   A 1 54  ? 25.745 8.067   7.580   0.40 12.02 ?  54  ASN   A HA   1 
ATOM   1385 H HB2  A ASN   A 1 54  ? 25.922 7.883   5.323   0.60 13.02 ?  54  ASN   A HB2  1 
ATOM   1386 H HB2  B ASN   A 1 54  ? 26.081 8.042   5.320   0.40 12.47 ?  54  ASN   A HB2  1 
ATOM   1387 H HB3  A ASN   A 1 54  ? 24.806 9.002   5.141   0.60 13.02 ?  54  ASN   A HB3  1 
ATOM   1388 H HB3  B ASN   A 1 54  ? 24.872 9.050   5.086   0.40 12.47 ?  54  ASN   A HB3  1 
ATOM   1389 H HD21 A ASN   A 1 54  ? 26.947 11.494  5.138   0.60 13.69 ?  54  ASN   A HD21 1 
ATOM   1390 H HD21 B ASN   A 1 54  ? 26.715 11.779  5.185   0.40 13.32 ?  54  ASN   A HD21 1 
ATOM   1391 H HD22 A ASN   A 1 54  ? 25.665 10.937  4.626   0.60 13.69 ?  54  ASN   A HD22 1 
ATOM   1392 H HD22 B ASN   A 1 54  ? 25.471 11.118  4.703   0.40 13.32 ?  54  ASN   A HD22 1 
ATOM   1393 N N    . LYS   A 1 55  ? 23.265 10.074  7.443   1.00 11.13 ?  55  LYS   A N    1 
ATOM   1394 C CA   . LYS   A 1 55  ? 22.683 11.228  8.118   1.00 11.80 ?  55  LYS   A CA   1 
ATOM   1395 C C    . LYS   A 1 55  ? 22.592 10.986  9.619   1.00 11.73 ?  55  LYS   A C    1 
ATOM   1396 O O    . LYS   A 1 55  ? 22.878 11.885  10.421  1.00 12.57 ?  55  LYS   A O    1 
ATOM   1397 C CB   . LYS   A 1 55  ? 21.314 11.542  7.504   1.00 12.36 ?  55  LYS   A CB   1 
ATOM   1398 C CG   . LYS   A 1 55  ? 20.566 12.686  8.159   1.00 14.17 ?  55  LYS   A CG   1 
ATOM   1399 C CD   . LYS   A 1 55  ? 19.246 12.946  7.432   1.00 15.53 ?  55  LYS   A CD   1 
ATOM   1400 C CE   . LYS   A 1 55  ? 18.389 14.010  8.108   1.00 17.22 ?  55  LYS   A CE   1 
ATOM   1401 N NZ   . LYS   A 1 55  ? 17.071 14.180  7.423   1.00 18.07 ?  55  LYS   A NZ   1 
ATOM   1402 H H    A LYS   A 1 55  ? 22.771 9.747   6.816   0.60 13.34 ?  55  LYS   A H    1 
ATOM   1403 H H    B LYS   A 1 55  ? 22.747 9.691   6.868   0.40 13.34 ?  55  LYS   A H    1 
ATOM   1404 H HA   . LYS   A 1 55  ? 23.258 11.994  7.977   1.00 14.15 ?  55  LYS   A HA   1 
ATOM   1405 H HB2  . LYS   A 1 55  ? 21.441 11.778  6.572   1.00 14.82 ?  55  LYS   A HB2  1 
ATOM   1406 H HB3  . LYS   A 1 55  ? 20.756 10.753  7.567   1.00 14.82 ?  55  LYS   A HB3  1 
ATOM   1407 H HG2  . LYS   A 1 55  ? 20.363 12.451  9.082   1.00 17.00 ?  55  LYS   A HG2  1 
ATOM   1408 H HG3  . LYS   A 1 55  ? 21.103 13.488  8.124   1.00 17.00 ?  55  LYS   A HG3  1 
ATOM   1409 H HD2  . LYS   A 1 55  ? 19.440 13.244  6.530   1.00 18.62 ?  55  LYS   A HD2  1 
ATOM   1410 H HD3  . LYS   A 1 55  ? 18.737 12.121  7.405   1.00 18.62 ?  55  LYS   A HD3  1 
ATOM   1411 H HE2  . LYS   A 1 55  ? 18.220 13.746  9.028   1.00 20.65 ?  55  LYS   A HE2  1 
ATOM   1412 H HE3  . LYS   A 1 55  ? 18.855 14.859  8.084   1.00 20.65 ?  55  LYS   A HE3  1 
ATOM   1413 H HZ1  . LYS   A 1 55  ? 16.588 14.804  7.840   1.00 21.68 ?  55  LYS   A HZ1  1 
ATOM   1414 H HZ2  . LYS   A 1 55  ? 17.195 14.431  6.578   1.00 21.68 ?  55  LYS   A HZ2  1 
ATOM   1415 H HZ3  . LYS   A 1 55  ? 16.618 13.413  7.433   1.00 21.68 ?  55  LYS   A HZ3  1 
ATOM   1416 N N    . ALA   A 1 56  ? 22.211 9.770   10.019  1.00 12.22 ?  56  ALA   A N    1 
ATOM   1417 C CA   . ALA   A 1 56  ? 22.097 9.441   11.434  1.00 13.37 ?  56  ALA   A CA   1 
ATOM   1418 C C    . ALA   A 1 56  ? 23.438 9.471   12.156  1.00 13.08 ?  56  ALA   A C    1 
ATOM   1419 O O    . ALA   A 1 56  ? 23.456 9.654   13.377  1.00 14.35 ?  56  ALA   A O    1 
ATOM   1420 C CB   . ALA   A 1 56  ? 21.412 8.079   11.602  1.00 14.20 ?  56  ALA   A CB   1 
ATOM   1421 H H    . ALA   A 1 56  ? 22.017 9.124   9.487   1.00 14.65 ?  56  ALA   A H    1 
ATOM   1422 H HA   . ALA   A 1 56  ? 21.529 10.095  11.856  1.00 16.04 ?  56  ALA   A HA   1 
ATOM   1423 H HB1  . ALA   A 1 56  ? 21.345 7.871   12.550  1.00 17.02 ?  56  ALA   A HB1  1 
ATOM   1424 H HB2  . ALA   A 1 56  ? 20.524 8.118   11.213  1.00 17.02 ?  56  ALA   A HB2  1 
ATOM   1425 H HB3  . ALA   A 1 56  ? 21.937 7.395   11.155  1.00 17.02 ?  56  ALA   A HB3  1 
ATOM   1426 N N    . THR   A 1 57  ? 24.553 9.291   11.439  1.00 12.09 ?  57  THR   A N    1 
ATOM   1427 C CA   . THR   A 1 57  ? 25.892 9.415   12.018  1.00 11.97 ?  57  THR   A CA   1 
ATOM   1428 C C    . THR   A 1 57  ? 26.447 10.834  11.943  1.00 12.64 ?  57  THR   A C    1 
ATOM   1429 O O    . THR   A 1 57  ? 27.633 11.042  12.240  1.00 12.96 ?  57  THR   A O    1 
ATOM   1430 C CB   . THR   A 1 57  ? 26.901 8.463   11.347  1.00 11.98 ?  57  THR   A CB   1 
ATOM   1431 O OG1  . THR   A 1 57  ? 27.286 8.966   10.054  1.00 11.62 ?  57  THR   A OG1  1 
ATOM   1432 C CG2  . THR   A 1 57  ? 26.365 7.043   11.245  1.00 11.99 ?  57  THR   A CG2  1 
ATOM   1433 H H    . THR   A 1 57  ? 24.559 9.074   10.606  1.00 14.50 ?  57  THR   A H    1 
ATOM   1434 H HA   . THR   A 1 57  ? 25.842 9.158   12.958  1.00 14.35 ?  57  THR   A HA   1 
ATOM   1435 H HB   . THR   A 1 57  ? 27.698 8.420   11.909  1.00 14.37 ?  57  THR   A HB   1 
ATOM   1436 H HG1  . THR   A 1 57  ? 26.607 9.031   9.566   1.00 13.94 ?  57  THR   A HG1  1 
ATOM   1437 H HG21 . THR   A 1 57  ? 27.042 6.454   10.873  1.00 14.38 ?  57  THR   A HG21 1 
ATOM   1438 H HG22 . THR   A 1 57  ? 26.114 6.713   12.124  1.00 14.38 ?  57  THR   A HG22 1 
ATOM   1439 H HG23 . THR   A 1 57  ? 25.585 7.022   10.671  1.00 14.38 ?  57  THR   A HG23 1 
ATOM   1440 N N    . ASN   A 1 58  ? 25.631 11.808  11.544  1.00 12.97 ?  58  ASN   A N    1 
ATOM   1441 C CA   . ASN   A 1 58  ? 26.097 13.188  11.451  1.00 13.67 ?  58  ASN   A CA   1 
ATOM   1442 C C    . ASN   A 1 58  ? 27.235 13.320  10.434  1.00 12.68 ?  58  ASN   A C    1 
ATOM   1443 O O    . ASN   A 1 58  ? 28.132 14.153  10.590  1.00 13.41 ?  58  ASN   A O    1 
ATOM   1444 C CB   . ASN   A 1 58  ? 26.490 13.717  12.846  1.00 16.15 ?  58  ASN   A CB   1 
ATOM   1445 C CG   . ASN   A 1 58  ? 26.914 15.174  12.848  1.00 19.45 ?  58  ASN   A CG   1 
ATOM   1446 O OD1  . ASN   A 1 58  ? 26.285 16.011  12.211  1.00 20.90 ?  58  ASN   A OD1  1 
ATOM   1447 N ND2  . ASN   A 1 58  ? 27.982 15.486  13.589  1.00 20.64 ?  58  ASN   A ND2  1 
ATOM   1448 H H    . ASN   A 1 58  ? 24.810 11.685  11.312  1.00 15.55 ?  58  ASN   A H    1 
ATOM   1449 H HA   . ASN   A 1 58  ? 25.360 13.726  11.138  1.00 16.39 ?  58  ASN   A HA   1 
ATOM   1450 H HB2  . ASN   A 1 58  ? 25.724 13.625  13.443  1.00 19.37 ?  58  ASN   A HB2  1 
ATOM   1451 H HB3  . ASN   A 1 58  ? 27.230 13.195  13.191  1.00 19.37 ?  58  ASN   A HB3  1 
ATOM   1452 H HD21 . ASN   A 1 58  ? 28.257 16.300  13.626  1.00 24.76 ?  58  ASN   A HD21 1 
ATOM   1453 H HD22 . ASN   A 1 58  ? 28.395 14.872  14.026  1.00 24.76 ?  58  ASN   A HD22 1 
ATOM   1454 N N    . ASN   A 1 59  ? 27.206 12.502  9.377   1.00 11.70 ?  59  ASN   A N    1 
ATOM   1455 C CA   . ASN   A 1 59  ? 28.184 12.484  8.280   1.00 11.62 ?  59  ASN   A CA   1 
ATOM   1456 C C    . ASN   A 1 59  ? 29.505 11.803  8.662   1.00 11.33 ?  59  ASN   A C    1 
ATOM   1457 O O    . ASN   A 1 59  ? 30.422 11.764  7.832   1.00 11.56 ?  59  ASN   A O    1 
ATOM   1458 C CB   . ASN   A 1 59  ? 28.465 13.872  7.674   1.00 11.90 ?  59  ASN   A CB   1 
ATOM   1459 C CG   . ASN   A 1 59  ? 28.817 13.809  6.204   1.00 12.03 ?  59  ASN   A CG   1 
ATOM   1460 O OD1  . ASN   A 1 59  ? 28.106 13.183  5.409   1.00 12.48 ?  59  ASN   A OD1  1 
ATOM   1461 N ND2  . ASN   A 1 59  ? 29.900 14.481  5.822   1.00 12.90 ?  59  ASN   A ND2  1 
ATOM   1462 H H    . ASN   A 1 59  ? 26.593 11.908  9.267   1.00 14.03 ?  59  ASN   A H    1 
ATOM   1463 H HA   . ASN   A 1 59  ? 27.803 11.954  7.569   1.00 13.93 ?  59  ASN   A HA   1 
ATOM   1464 H HB2  . ASN   A 1 59  ? 27.677 14.426  7.763   1.00 14.27 ?  59  ASN   A HB2  1 
ATOM   1465 H HB3  . ASN   A 1 59  ? 29.213 14.279  8.139   1.00 14.27 ?  59  ASN   A HB3  1 
ATOM   1466 H HD21 . ASN   A 1 59  ? 30.140 14.482  4.994   1.00 15.46 ?  59  ASN   A HD21 1 
ATOM   1467 H HD22 . ASN   A 1 59  ? 30.371 14.913  6.401   1.00 15.46 ?  59  ASN   A HD22 1 
ATOM   1468 N N    . ALA   A 1 60  ? 29.635 11.263  9.874   1.00 11.16 ?  60  ALA   A N    1 
ATOM   1469 C CA   . ALA   A 1 60  ? 30.872 10.573  10.229  1.00 11.51 ?  60  ALA   A CA   1 
ATOM   1470 C C    . ALA   A 1 60  ? 31.095 9.338   9.359   1.00 11.37 ?  60  ALA   A C    1 
ATOM   1471 O O    . ALA   A 1 60  ? 32.241 9.016   9.020   1.00 11.96 ?  60  ALA   A O    1 
ATOM   1472 C CB   . ALA   A 1 60  ? 30.862 10.204  11.712  1.00 12.05 ?  60  ALA   A CB   1 
ATOM   1473 H H    . ALA   A 1 60  ? 29.037 11.277  10.493  1.00 13.38 ?  60  ALA   A H    1 
ATOM   1474 H HA   . ALA   A 1 60  ? 31.619 11.177  10.082  1.00 13.80 ?  60  ALA   A HA   1 
ATOM   1475 H HB1  . ALA   A 1 60  ? 31.690 9.753   11.934  1.00 14.45 ?  60  ALA   A HB1  1 
ATOM   1476 H HB2  . ALA   A 1 60  ? 30.781 11.020  12.239  1.00 14.45 ?  60  ALA   A HB2  1 
ATOM   1477 H HB3  . ALA   A 1 60  ? 30.107 9.625   11.890  1.00 14.45 ?  60  ALA   A HB3  1 
ATOM   1478 N N    . MET   A 1 61  ? 30.021 8.641   8.979   1.00 11.04 ?  61  MET   A N    1 
ATOM   1479 C CA   . MET   A 1 61  ? 30.158 7.504   8.074   1.00 10.84 ?  61  MET   A CA   1 
ATOM   1480 C C    . MET   A 1 61  ? 30.791 7.932   6.750   1.00 10.64 ?  61  MET   A C    1 
ATOM   1481 O O    . MET   A 1 61  ? 31.692 7.255   6.231   1.00 11.08 ?  61  MET   A O    1 
ATOM   1482 C CB   . MET   A 1 61  ? 28.796 6.838   7.864   1.00 10.85 ?  61  MET   A CB   1 
ATOM   1483 C CG   . MET   A 1 61  ? 28.806 5.675   6.885   1.00 11.56 ?  61  MET   A CG   1 
ATOM   1484 S SD   . MET   A 1 61  ? 27.174 4.937   6.657   1.00 12.27 ?  61  MET   A SD   1 
ATOM   1485 C CE   . MET   A 1 61  ? 26.999 4.052   8.209   1.00 13.94 ?  61  MET   A CE   1 
ATOM   1486 H H    . MET   A 1 61  ? 29.215 8.804   9.232   1.00 13.23 ?  61  MET   A H    1 
ATOM   1487 H HA   . MET   A 1 61  ? 30.741 6.851   8.493   1.00 13.00 ?  61  MET   A HA   1 
ATOM   1488 H HB2  . MET   A 1 61  ? 28.487 6.499   8.719   1.00 13.01 ?  61  MET   A HB2  1 
ATOM   1489 H HB3  . MET   A 1 61  ? 28.175 7.500   7.532   1.00 13.01 ?  61  MET   A HB3  1 
ATOM   1490 H HG2  . MET   A 1 61  ? 29.103 5.987   6.018   1.00 13.85 ?  61  MET   A HG2  1 
ATOM   1491 H HG3  . MET   A 1 61  ? 29.399 4.984   7.214   1.00 13.85 ?  61  MET   A HG3  1 
ATOM   1492 H HE1  . MET   A 1 61  ? 26.148 3.581   8.212   1.00 16.72 ?  61  MET   A HE1  1 
ATOM   1493 H HE2  . MET   A 1 61  ? 27.726 3.417   8.298   1.00 16.72 ?  61  MET   A HE2  1 
ATOM   1494 H HE3  . MET   A 1 61  ? 27.024 4.687   8.944   1.00 16.72 ?  61  MET   A HE3  1 
ATOM   1495 N N    . GLN   A 1 62  ? 30.351 9.065   6.199   1.00 10.67 ?  62  GLN   A N    1 
ATOM   1496 C CA   . GLN   A 1 62  ? 30.907 9.542   4.936   1.00 11.13 ?  62  GLN   A CA   1 
ATOM   1497 C C    . GLN   A 1 62  ? 32.379 9.917   5.076   1.00 11.09 ?  62  GLN   A C    1 
ATOM   1498 O O    . GLN   A 1 62  ? 33.186 9.599   4.194   1.00 11.41 ?  62  GLN   A O    1 
ATOM   1499 C CB   . GLN   A 1 62  ? 30.102 10.731  4.408   1.00 11.02 ?  62  GLN   A CB   1 
ATOM   1500 C CG   . GLN   A 1 62  ? 30.475 11.101  2.978   1.00 10.87 ?  62  GLN   A CG   1 
ATOM   1501 C CD   . GLN   A 1 62  ? 30.150 9.976   2.024   1.00 11.19 ?  62  GLN   A CD   1 
ATOM   1502 O OE1  . GLN   A 1 62  ? 28.976 9.662   1.823   1.00 11.98 ?  62  GLN   A OE1  1 
ATOM   1503 N NE2  . GLN   A 1 62  ? 31.168 9.306   1.493   1.00 11.99 ?  62  GLN   A NE2  1 
ATOM   1504 H H    . GLN   A 1 62  ? 29.735 9.564   6.530   1.00 12.79 ?  62  GLN   A H    1 
ATOM   1505 H HA   . GLN   A 1 62  ? 30.849 8.826   4.285   1.00 13.34 ?  62  GLN   A HA   1 
ATOM   1506 H HB2  . GLN   A 1 62  ? 29.160 10.512  4.428   1.00 13.22 ?  62  GLN   A HB2  1 
ATOM   1507 H HB3  . GLN   A 1 62  ? 30.276 11.504  4.970   1.00 13.22 ?  62  GLN   A HB3  1 
ATOM   1508 H HG2  . GLN   A 1 62  ? 29.964 11.881  2.706   1.00 13.04 ?  62  GLN   A HG2  1 
ATOM   1509 H HG3  . GLN   A 1 62  ? 31.423 11.283  2.923   1.00 13.04 ?  62  GLN   A HG3  1 
ATOM   1510 H HE21 . GLN   A 1 62  ? 31.978 9.541   1.673   1.00 14.37 ?  62  GLN   A HE21 1 
ATOM   1511 H HE22 . GLN   A 1 62  ? 31.024 8.651   0.955   1.00 14.37 ?  62  GLN   A HE22 1 
ATOM   1512 N N    . VAL   A 1 63  ? 32.744 10.605  6.164   1.00 11.38 ?  63  VAL   A N    1 
ATOM   1513 C CA   . VAL   A 1 63  ? 34.138 10.991  6.380   1.00 12.44 ?  63  VAL   A CA   1 
ATOM   1514 C C    . VAL   A 1 63  ? 35.033 9.754   6.435   1.00 11.79 ?  63  VAL   A C    1 
ATOM   1515 O O    . VAL   A 1 63  ? 36.086 9.688   5.781   1.00 12.26 ?  63  VAL   A O    1 
ATOM   1516 C CB   . VAL   A 1 63  ? 34.251 11.861  7.646   1.00 13.76 ?  63  VAL   A CB   1 
ATOM   1517 C CG1  . VAL   A 1 63  ? 35.701 12.109  7.998   1.00 15.53 ?  63  VAL   A CG1  1 
ATOM   1518 C CG2  . VAL   A 1 63  ? 33.520 13.184  7.441   1.00 14.19 ?  63  VAL   A CG2  1 
ATOM   1519 H H    . VAL   A 1 63  ? 32.196 10.861  6.783   1.00 13.65 ?  63  VAL   A H    1 
ATOM   1520 H HA   . VAL   A 1 63  ? 34.419 11.531  5.627   1.00 14.91 ?  63  VAL   A HA   1 
ATOM   1521 H HB   . VAL   A 1 63  ? 33.831 11.396  8.390   1.00 16.49 ?  63  VAL   A HB   1 
ATOM   1522 H HG11 . VAL   A 1 63  ? 35.746 12.835  8.639   1.00 18.62 ?  63  VAL   A HG11 1 
ATOM   1523 H HG12 . VAL   A 1 63  ? 36.078 11.304  8.380   1.00 18.62 ?  63  VAL   A HG12 1 
ATOM   1524 H HG13 . VAL   A 1 63  ? 36.180 12.353  7.190   1.00 18.62 ?  63  VAL   A HG13 1 
ATOM   1525 H HG21 . VAL   A 1 63  ? 33.615 13.723  8.242   1.00 17.02 ?  63  VAL   A HG21 1 
ATOM   1526 H HG22 . VAL   A 1 63  ? 33.910 13.645  6.683   1.00 17.02 ?  63  VAL   A HG22 1 
ATOM   1527 H HG23 . VAL   A 1 63  ? 32.580 13.006  7.274   1.00 17.02 ?  63  VAL   A HG23 1 
ATOM   1528 N N    . GLU   A 1 64  ? 34.610 8.741   7.196   1.00 11.81 ?  64  GLU   A N    1 
ATOM   1529 C CA   . GLU   A 1 64  ? 35.373 7.503   7.289   1.00 11.76 ?  64  GLU   A CA   1 
ATOM   1530 C C    . GLU   A 1 64  ? 35.457 6.817   5.931   1.00 11.28 ?  64  GLU   A C    1 
ATOM   1531 O O    . GLU   A 1 64  ? 36.511 6.276   5.548   1.00 11.72 ?  64  GLU   A O    1 
ATOM   1532 C CB   . GLU   A 1 64  ? 34.693 6.599   8.316   1.00 12.46 ?  64  GLU   A CB   1 
ATOM   1533 C CG   . GLU   A 1 64  ? 35.351 5.254   8.477   1.00 12.76 ?  64  GLU   A CG   1 
ATOM   1534 C CD   . GLU   A 1 64  ? 34.467 4.254   9.194   1.00 13.44 ?  64  GLU   A CD   1 
ATOM   1535 O OE1  . GLU   A 1 64  ? 33.225 4.350   9.063   1.00 14.40 ?  64  GLU   A OE1  1 
ATOM   1536 O OE2  . GLU   A 1 64  ? 35.014 3.347   9.870   1.00 13.81 -1 64  GLU   A OE2  1 
ATOM   1537 H H    . GLU   A 1 64  ? 33.878 8.742   7.653   1.00 14.16 ?  64  GLU   A H    1 
ATOM   1538 H HA   . GLU   A 1 64  ? 36.274 7.710   7.596   1.00 14.10 ?  64  GLU   A HA   1 
ATOM   1539 H HB2  . GLU   A 1 64  ? 34.715 7.046   9.182   1.00 14.94 ?  64  GLU   A HB2  1 
ATOM   1540 H HB3  . GLU   A 1 64  ? 33.777 6.462   8.043   1.00 14.94 ?  64  GLU   A HB3  1 
ATOM   1541 H HG2  . GLU   A 1 64  ? 35.567 4.888   7.603   1.00 15.30 ?  64  GLU   A HG2  1 
ATOM   1542 H HG3  . GLU   A 1 64  ? 36.163 5.358   8.996   1.00 15.30 ?  64  GLU   A HG3  1 
ATOM   1543 N N    . SER   A 1 65  ? 34.337 6.817   5.199   1.00 10.87 ?  65  SER   A N    1 
ATOM   1544 C CA   . SER   A 1 65  ? 34.285 6.160   3.899   1.00 10.72 ?  65  SER   A CA   1 
ATOM   1545 C C    . SER   A 1 65  ? 35.211 6.831   2.893   1.00 11.33 ?  65  SER   A C    1 
ATOM   1546 O O    . SER   A 1 65  ? 35.851 6.156   2.083   1.00 12.07 ?  65  SER   A O    1 
ATOM   1547 C CB   . SER   A 1 65  ? 32.852 6.173   3.367   1.00 10.95 ?  65  SER   A CB   1 
ATOM   1548 O OG   . SER   A 1 65  ? 32.001 5.352   4.157   1.00 11.49 ?  65  SER   A OG   1 
ATOM   1549 H H    . SER   A 1 65  ? 33.600 7.193   5.438   1.00 13.03 ?  65  SER   A H    1 
ATOM   1550 H HA   . SER   A 1 65  ? 34.563 5.237   3.999   1.00 12.86 ?  65  SER   A HA   1 
ATOM   1551 H HB2  . SER   A 1 65  ? 32.515 7.082   3.382   1.00 13.13 ?  65  SER   A HB2  1 
ATOM   1552 H HB3  . SER   A 1 65  ? 32.854 5.837   2.456   1.00 13.13 ?  65  SER   A HB3  1 
ATOM   1553 H HG   . SER   A 1 65  ? 31.993 5.633   4.954   1.00 13.77 ?  65  SER   A HG   1 
ATOM   1554 N N    . ASP   A 1 66  ? 35.284 8.165   2.914   1.00 11.35 ?  66  ASP   A N    1 
ATOM   1555 C CA   . ASP   A 1 66  ? 36.141 8.866   1.965   1.00 12.35 ?  66  ASP   A CA   1 
ATOM   1556 C C    . ASP   A 1 66  ? 37.604 8.508   2.196   1.00 12.21 ?  66  ASP   A C    1 
ATOM   1557 O O    . ASP   A 1 66  ? 38.373 8.339   1.240   1.00 13.02 ?  66  ASP   A O    1 
ATOM   1558 C CB   . ASP   A 1 66  ? 35.925 10.375  2.076   1.00 13.69 ?  66  ASP   A CB   1 
ATOM   1559 C CG   . ASP   A 1 66  ? 34.587 10.839  1.479   1.00 15.33 ?  66  ASP   A CG   1 
ATOM   1560 O OD1  . ASP   A 1 66  ? 33.868 10.046  0.831   1.00 15.68 ?  66  ASP   A OD1  1 
ATOM   1561 O OD2  . ASP   A 1 66  ? 34.280 12.034  1.644   1.00 18.67 -1 66  ASP   A OD2  1 
ATOM   1562 H H    . ASP   A 1 66  ? 34.839 8.674   3.453   1.00 13.61 ?  66  ASP   A H    1 
ATOM   1563 H HA   . ASP   A 1 66  ? 35.901 8.593   1.067   1.00 14.81 ?  66  ASP   A HA   1 
ATOM   1564 H HB2  . ASP   A 1 66  ? 35.927 10.626  3.012   1.00 16.42 ?  66  ASP   A HB2  1 
ATOM   1565 H HB3  . ASP   A 1 66  ? 36.641 10.828  1.607   1.00 16.42 ?  66  ASP   A HB3  1 
ATOM   1566 N N    . ASP   A 1 67  ? 38.006 8.377   3.460   1.00 12.28 ?  67  ASP   A N    1 
ATOM   1567 C CA   . ASP   A 1 67  ? 39.361 7.934   3.756   1.00 13.31 ?  67  ASP   A CA   1 
ATOM   1568 C C    . ASP   A 1 67  ? 39.585 6.499   3.290   1.00 13.20 ?  67  ASP   A C    1 
ATOM   1569 O O    . ASP   A 1 67  ? 40.645 6.180   2.740   1.00 13.87 ?  67  ASP   A O    1 
ATOM   1570 C CB   . ASP   A 1 67  ? 39.637 8.074   5.250   1.00 14.54 ?  67  ASP   A CB   1 
ATOM   1571 C CG   . ASP   A 1 67  ? 40.933 7.407   5.666   1.00 15.79 ?  67  ASP   A CG   1 
ATOM   1572 O OD1  . ASP   A 1 67  ? 42.006 8.040   5.521   1.00 18.45 ?  67  ASP   A OD1  1 
ATOM   1573 O OD2  . ASP   A 1 67  ? 40.878 6.246   6.135   1.00 15.33 -1 67  ASP   A OD2  1 
ATOM   1574 H H    . ASP   A 1 67  ? 37.520 8.538   4.150   1.00 14.72 ?  67  ASP   A H    1 
ATOM   1575 H HA   . ASP   A 1 67  ? 39.987 8.495   3.280   1.00 15.96 ?  67  ASP   A HA   1 
ATOM   1576 H HB2  . ASP   A 1 67  ? 39.698 9.011   5.469   1.00 17.43 ?  67  ASP   A HB2  1 
ATOM   1577 H HB3  . ASP   A 1 67  ? 38.912 7.658   5.745   1.00 17.43 ?  67  ASP   A HB3  1 
ATOM   1578 N N    . TYR   A 1 68  ? 38.593 5.618   3.482   1.00 12.60 ?  68  TYR   A N    1 
ATOM   1579 C CA   . TYR   A 1 68  ? 38.710 4.240   3.001   1.00 12.87 ?  68  TYR   A CA   1 
ATOM   1580 C C    . TYR   A 1 68  ? 38.949 4.197   1.493   1.00 12.42 ?  68  TYR   A C    1 
ATOM   1581 O O    . TYR   A 1 68  ? 39.825 3.463   1.013   1.00 12.95 ?  68  TYR   A O    1 
ATOM   1582 C CB   . TYR   A 1 68  ? 37.460 3.416   3.381   1.00 13.13 ?  68  TYR   A CB   1 
ATOM   1583 C CG   . TYR   A 1 68  ? 37.483 2.025   2.751   1.00 14.32 ?  68  TYR   A CG   1 
ATOM   1584 C CD1  . TYR   A 1 68  ? 37.028 1.834   1.449   1.00 15.86 ?  68  TYR   A CD1  1 
ATOM   1585 C CD2  . TYR   A 1 68  ? 38.021 0.933   3.418   1.00 16.15 ?  68  TYR   A CD2  1 
ATOM   1586 C CE1  . TYR   A 1 68  ? 37.090 0.617   0.831   1.00 17.02 ?  68  TYR   A CE1  1 
ATOM   1587 C CE2  . TYR   A 1 68  ? 38.081 -0.329  2.798   1.00 16.21 ?  68  TYR   A CE2  1 
ATOM   1588 C CZ   . TYR   A 1 68  ? 37.621 -0.457  1.503   1.00 16.86 ?  68  TYR   A CZ   1 
ATOM   1589 O OH   . TYR   A 1 68  ? 37.697 -1.665  0.869   1.00 18.19 ?  68  TYR   A OH   1 
ATOM   1590 H H    . TYR   A 1 68  ? 37.847 5.788   3.884   1.00 15.10 ?  68  TYR   A H    1 
ATOM   1591 H HA   . TYR   A 1 68  ? 39.469 3.823   3.431   1.00 15.43 ?  68  TYR   A HA   1 
ATOM   1592 H HB2  . TYR   A 1 68  ? 37.428 3.304   4.345   1.00 15.74 ?  68  TYR   A HB2  1 
ATOM   1593 H HB3  . TYR   A 1 68  ? 36.663 3.873   3.070   1.00 15.74 ?  68  TYR   A HB3  1 
ATOM   1594 H HD1  . TYR   A 1 68  ? 36.683 2.565   0.982   1.00 19.02 ?  68  TYR   A HD1  1 
ATOM   1595 H HD2  . TYR   A 1 68  ? 38.349 1.035   4.281   1.00 19.37 ?  68  TYR   A HD2  1 
ATOM   1596 H HE1  . TYR   A 1 68  ? 36.778 0.521   -0.039  1.00 20.41 ?  68  TYR   A HE1  1 
ATOM   1597 H HE2  . TYR   A 1 68  ? 38.447 -1.058  3.241   1.00 19.44 ?  68  TYR   A HE2  1 
ATOM   1598 H HH   . TYR   A 1 68  ? 38.029 -2.240  1.386   1.00 21.82 ?  68  TYR   A HH   1 
ATOM   1599 N N    . ILE   A 1 69  ? 38.164 4.959   0.724   1.00 12.09 ?  69  ILE   A N    1 
ATOM   1600 C CA   . ILE   A 1 69  ? 38.296 4.936   -0.731  1.00 12.39 ?  69  ILE   A CA   1 
ATOM   1601 C C    . ILE   A 1 69  ? 39.627 5.546   -1.163  1.00 12.44 ?  69  ILE   A C    1 
ATOM   1602 O O    . ILE   A 1 69  ? 40.272 5.064   -2.102  1.00 12.63 ?  69  ILE   A O    1 
ATOM   1603 C CB   . ILE   A 1 69  ? 37.095 5.647   -1.391  1.00 13.16 ?  69  ILE   A CB   1 
ATOM   1604 C CG1  . ILE   A 1 69  ? 35.782 4.905   -1.115  1.00 13.55 ?  69  ILE   A CG1  1 
ATOM   1605 C CG2  . ILE   A 1 69  ? 37.333 5.852   -2.896  1.00 14.73 ?  69  ILE   A CG2  1 
ATOM   1606 C CD1  . ILE   A 1 69  ? 35.613 3.619   -1.892  1.00 14.29 ?  69  ILE   A CD1  1 
ATOM   1607 H H    . ILE   A 1 69  ? 37.561 5.495   1.021   1.00 14.49 ?  69  ILE   A H    1 
ATOM   1608 H HA   . ILE   A 1 69  ? 38.288 4.013   -1.026  1.00 14.86 ?  69  ILE   A HA   1 
ATOM   1609 H HB   . ILE   A 1 69  ? 37.019 6.523   -0.989  1.00 15.78 ?  69  ILE   A HB   1 
ATOM   1610 H HG12 . ILE   A 1 69  ? 35.742 4.684   -0.171  1.00 16.25 ?  69  ILE   A HG12 1 
ATOM   1611 H HG13 . ILE   A 1 69  ? 35.042 5.487   -1.346  1.00 16.25 ?  69  ILE   A HG13 1 
ATOM   1612 H HG21 . ILE   A 1 69  ? 36.486 6.065   -3.324  1.00 17.66 ?  69  ILE   A HG21 1 
ATOM   1613 H HG22 . ILE   A 1 69  ? 37.952 6.594   -3.021  1.00 17.66 ?  69  ILE   A HG22 1 
ATOM   1614 H HG23 . ILE   A 1 69  ? 37.702 5.045   -3.277  1.00 17.66 ?  69  ILE   A HG23 1 
ATOM   1615 H HD11 . ILE   A 1 69  ? 34.810 3.170   -1.585  1.00 17.13 ?  69  ILE   A HD11 1 
ATOM   1616 H HD12 . ILE   A 1 69  ? 35.533 3.827   -2.837  1.00 17.13 ?  69  ILE   A HD12 1 
ATOM   1617 H HD13 . ILE   A 1 69  ? 36.386 3.053   -1.742  1.00 17.13 ?  69  ILE   A HD13 1 
ATOM   1618 N N    . ALA   A 1 70  ? 40.048 6.628   -0.504  1.00 12.66 ?  70  ALA   A N    1 
ATOM   1619 C CA   . ALA   A 1 70  ? 41.322 7.240   -0.861  1.00 13.59 ?  70  ALA   A CA   1 
ATOM   1620 C C    . ALA   A 1 70  ? 42.473 6.255   -0.695  1.00 13.70 ?  70  ALA   A C    1 
ATOM   1621 O O    . ALA   A 1 70  ? 43.441 6.295   -1.460  1.00 15.88 ?  70  ALA   A O    1 
ATOM   1622 C CB   . ALA   A 1 70  ? 41.554 8.497   -0.018  1.00 14.14 ?  70  ALA   A CB   1 
ATOM   1623 H H    . ALA   A 1 70  ? 39.623 7.019   0.131   1.00 15.18 ?  70  ALA   A H    1 
ATOM   1624 H HA   . ALA   A 1 70  ? 41.291 7.514   -1.792  1.00 16.29 ?  70  ALA   A HA   1 
ATOM   1625 H HB1  . ALA   A 1 70  ? 42.411 8.889   -0.267  1.00 16.95 ?  70  ALA   A HB1  1 
ATOM   1626 H HB2  . ALA   A 1 70  ? 40.843 9.131   -0.185  1.00 16.95 ?  70  ALA   A HB2  1 
ATOM   1627 H HB3  . ALA   A 1 70  ? 41.570 8.250   0.920   1.00 16.95 ?  70  ALA   A HB3  1 
ATOM   1628 N N    . THR   A 1 71  ? 42.372 5.353   0.280   1.00 13.15 ?  71  THR   A N    1 
ATOM   1629 C CA   . THR   A 1 71  ? 43.427 4.380   0.531   1.00 14.74 ?  71  THR   A CA   1 
ATOM   1630 C C    . THR   A 1 71  ? 43.304 3.153   -0.362  1.00 14.87 ?  71  THR   A C    1 
ATOM   1631 O O    . THR   A 1 71  ? 44.317 2.643   -0.862  1.00 16.85 ?  71  THR   A O    1 
ATOM   1632 C CB   . THR   A 1 71  ? 43.366 3.933   1.987   1.00 16.35 ?  71  THR   A CB   1 
ATOM   1633 O OG1  . THR   A 1 71  ? 43.615 5.059   2.837   1.00 17.82 ?  71  THR   A OG1  1 
ATOM   1634 C CG2  . THR   A 1 71  ? 44.385 2.824   2.268   1.00 18.06 ?  71  THR   A CG2  1 
ATOM   1635 H H    . THR   A 1 71  ? 41.699 5.282   0.807   1.00 15.77 ?  71  THR   A H    1 
ATOM   1636 H HA   . THR   A 1 71  ? 44.292 4.787   0.367   1.00 17.67 ?  71  THR   A HA   1 
ATOM   1637 H HB   . THR   A 1 71  ? 42.482 3.570   2.167   1.00 19.60 ?  71  THR   A HB   1 
ATOM   1638 H HG1  . THR   A 1 71  ? 43.577 4.807   3.640   1.00 21.37 ?  71  THR   A HG1  1 
ATOM   1639 H HG21 . THR   A 1 71  ? 44.525 2.740   3.225   1.00 21.66 ?  71  THR   A HG21 1 
ATOM   1640 H HG22 . THR   A 1 71  ? 44.070 1.973   1.923   1.00 21.66 ?  71  THR   A HG22 1 
ATOM   1641 H HG23 . THR   A 1 71  ? 45.235 3.039   1.848   1.00 21.66 ?  71  THR   A HG23 1 
ATOM   1642 N N    . ASN   A 1 72  ? 42.079 2.650   -0.553  1.00 13.96 ?  72  ASN   A N    1 
ATOM   1643 C CA   . ASN   A 1 72  ? 41.861 1.326   -1.119  1.00 14.24 ?  72  ASN   A CA   1 
ATOM   1644 C C    . ASN   A 1 72  ? 41.235 1.315   -2.501  1.00 14.18 ?  72  ASN   A C    1 
ATOM   1645 O O    . ASN   A 1 72  ? 41.235 0.259   -3.146  1.00 15.42 ?  72  ASN   A O    1 
ATOM   1646 C CB   . ASN   A 1 72  ? 40.981 0.498   -0.174  1.00 14.92 ?  72  ASN   A CB   1 
ATOM   1647 C CG   . ASN   A 1 72  ? 41.601 0.347   1.194   1.00 15.83 ?  72  ASN   A CG   1 
ATOM   1648 O OD1  . ASN   A 1 72  ? 41.153 0.954   2.166   1.00 17.62 ?  72  ASN   A OD1  1 
ATOM   1649 N ND2  . ASN   A 1 72  ? 42.649 -0.445  1.274   1.00 16.52 ?  72  ASN   A ND2  1 
ATOM   1650 H H    . ASN   A 1 72  ? 41.351 3.068   -0.356  1.00 16.74 ?  72  ASN   A H    1 
ATOM   1651 H HA   . ASN   A 1 72  ? 42.717 0.881   -1.190  1.00 17.08 ?  72  ASN   A HA   1 
ATOM   1652 H HB2  . ASN   A 1 72  ? 40.124 0.935   -0.070  1.00 17.89 ?  72  ASN   A HB2  1 
ATOM   1653 H HB3  . ASN   A 1 72  ? 40.865 -0.389  -0.547  1.00 17.89 ?  72  ASN   A HB3  1 
ATOM   1654 H HD21 . ASN   A 1 72  ? 43.042 -0.559  2.034   1.00 19.81 ?  72  ASN   A HD21 1 
ATOM   1655 H HD22 . ASN   A 1 72  ? 42.941 -0.847  0.576   1.00 19.81 ?  72  ASN   A HD22 1 
ATOM   1656 N N    . GLY   A 1 73  ? 40.681 2.429   -2.961  1.00 13.81 ?  73  GLY   A N    1 
ATOM   1657 C CA   . GLY   A 1 73  ? 39.944 2.445   -4.199  1.00 13.50 ?  73  GLY   A CA   1 
ATOM   1658 C C    . GLY   A 1 73  ? 38.556 1.855   -4.031  1.00 12.80 ?  73  GLY   A C    1 
ATOM   1659 O O    . GLY   A 1 73  ? 38.171 1.398   -2.948  1.00 13.43 ?  73  GLY   A O    1 
ATOM   1660 H H    . GLY   A 1 73  ? 40.718 3.200   -2.569  1.00 16.56 ?  73  GLY   A H    1 
ATOM   1661 H HA2  . GLY   A 1 73  ? 39.858 3.360   -4.512  1.00 16.19 ?  73  GLY   A HA2  1 
ATOM   1662 H HA3  . GLY   A 1 73  ? 40.421 1.932   -4.868  1.00 16.19 ?  73  GLY   A HA3  1 
ATOM   1663 N N    . PRO   A 1 74  ? 37.775 1.873   -5.111  1.00 13.40 ?  74  PRO   A N    1 
ATOM   1664 C CA   . PRO   A 1 74  ? 36.375 1.446   -5.027  1.00 13.31 ?  74  PRO   A CA   1 
ATOM   1665 C C    . PRO   A 1 74  ? 36.226 -0.038  -4.720  1.00 12.73 ?  74  PRO   A C    1 
ATOM   1666 O O    . PRO   A 1 74  ? 37.099 -0.861  -5.007  1.00 13.85 ?  74  PRO   A O    1 
ATOM   1667 C CB   . PRO   A 1 74  ? 35.826 1.758   -6.425  1.00 15.20 ?  74  PRO   A CB   1 
ATOM   1668 C CG   . PRO   A 1 74  ? 36.783 2.741   -7.026  1.00 17.96 ?  74  PRO   A CG   1 
ATOM   1669 C CD   . PRO   A 1 74  ? 38.120 2.397   -6.444  1.00 15.22 ?  74  PRO   A CD   1 
ATOM   1670 H HA   . PRO   A 1 74  ? 35.894 1.968   -4.364  1.00 15.96 ?  74  PRO   A HA   1 
ATOM   1671 H HB2  . PRO   A 1 74  ? 35.792 0.944   -6.950  1.00 18.22 ?  74  PRO   A HB2  1 
ATOM   1672 H HB3  . PRO   A 1 74  ? 34.940 2.150   -6.346  1.00 18.22 ?  74  PRO   A HB3  1 
ATOM   1673 H HG2  . PRO   A 1 74  ? 36.798 2.638   -7.991  1.00 21.54 ?  74  PRO   A HG2  1 
ATOM   1674 H HG3  . PRO   A 1 74  ? 36.529 3.643   -6.782  1.00 21.54 ?  74  PRO   A HG3  1 
ATOM   1675 H HD2  . PRO   A 1 74  ? 38.561 1.712   -6.975  1.00 18.25 ?  74  PRO   A HD2  1 
ATOM   1676 H HD3  . PRO   A 1 74  ? 38.670 3.196   -6.374  1.00 18.25 ?  74  PRO   A HD3  1 
ATOM   1677 N N    . LEU   A 1 75  ? 35.081 -0.367  -4.132  1.00 12.20 ?  75  LEU   A N    1 
ATOM   1678 C CA   . LEU   A 1 75  ? 34.667 -1.756  -3.990  1.00 11.72 ?  75  LEU   A CA   1 
ATOM   1679 C C    . LEU   A 1 75  ? 34.277 -2.327  -5.351  1.00 12.29 ?  75  LEU   A C    1 
ATOM   1680 O O    . LEU   A 1 75  ? 34.164 -1.609  -6.348  1.00 13.59 ?  75  LEU   A O    1 
ATOM   1681 C CB   . LEU   A 1 75  ? 33.480 -1.868  -3.035  1.00 11.92 ?  75  LEU   A CB   1 
ATOM   1682 C CG   . LEU   A 1 75  ? 33.693 -1.460  -1.582  1.00 13.76 ?  75  LEU   A CG   1 
ATOM   1683 C CD1  . LEU   A 1 75  ? 32.413 -1.650  -0.776  1.00 15.53 ?  75  LEU   A CD1  1 
ATOM   1684 C CD2  . LEU   A 1 75  ? 34.837 -2.191  -0.942  1.00 17.39 ?  75  LEU   A CD2  1 
ATOM   1685 H H    . LEU   A 1 75  ? 34.524 0.202   -3.809  1.00 14.62 ?  75  LEU   A H    1 
ATOM   1686 H HA   . LEU   A 1 75  ? 35.403 -2.275  -3.641  1.00 14.06 ?  75  LEU   A HA   1 
ATOM   1687 H HB2  . LEU   A 1 75  ? 32.763 -1.315  -3.383  1.00 14.29 ?  75  LEU   A HB2  1 
ATOM   1688 H HB3  . LEU   A 1 75  ? 33.192 -2.795  -3.031  1.00 14.29 ?  75  LEU   A HB3  1 
ATOM   1689 H HG   . LEU   A 1 75  ? 33.916 -0.516  -1.563  1.00 16.50 ?  75  LEU   A HG   1 
ATOM   1690 H HD11 . LEU   A 1 75  ? 32.576 -1.380  0.139   1.00 18.62 ?  75  LEU   A HD11 1 
ATOM   1691 H HD12 . LEU   A 1 75  ? 31.717 -1.096  -1.167  1.00 18.62 ?  75  LEU   A HD12 1 
ATOM   1692 H HD13 . LEU   A 1 75  ? 32.155 -2.581  -0.811  1.00 18.62 ?  75  LEU   A HD13 1 
ATOM   1693 H HD21 . LEU   A 1 75  ? 34.887 -1.947  -0.006  1.00 20.86 ?  75  LEU   A HD21 1 
ATOM   1694 H HD22 . LEU   A 1 75  ? 34.693 -3.147  -1.029  1.00 20.86 ?  75  LEU   A HD22 1 
ATOM   1695 H HD23 . LEU   A 1 75  ? 35.666 -1.943  -1.389  1.00 20.86 ?  75  LEU   A HD23 1 
ATOM   1696 N N    . LYS   A 1 76  ? 34.073 -3.646  -5.375  1.00 12.93 ?  76  LYS   A N    1 
ATOM   1697 C CA   . LYS   A 1 76  ? 33.465 -4.358  -6.494  1.00 13.40 ?  76  LYS   A CA   1 
ATOM   1698 C C    . LYS   A 1 76  ? 31.955 -4.442  -6.288  1.00 12.07 ?  76  LYS   A C    1 
ATOM   1699 O O    . LYS   A 1 76  ? 31.483 -4.570  -5.162  1.00 11.83 ?  76  LYS   A O    1 
ATOM   1700 C CB   . LYS   A 1 76  ? 34.008 -5.798  -6.562  1.00 15.68 ?  76  LYS   A CB   1 
ATOM   1701 C CG   . LYS   A 1 76  ? 35.526 -5.911  -6.708  1.00 17.34 ?  76  LYS   A CG   1 
ATOM   1702 C CD   . LYS   A 1 76  ? 36.030 -7.331  -6.539  1.00 18.90 ?  76  LYS   A CD   1 
ATOM   1703 C CE   . LYS   A 1 76  ? 37.529 -7.399  -6.763  1.00 21.70 ?  76  LYS   A CE   1 
ATOM   1704 N NZ   . LYS   A 1 76  ? 38.071 -8.758  -6.563  1.00 22.77 ?  76  LYS   A NZ   1 
ATOM   1705 H H    . LYS   A 1 76  ? 34.290 -4.166  -4.726  1.00 15.50 ?  76  LYS   A H    1 
ATOM   1706 H HA   . LYS   A 1 76  ? 33.652 -3.901  -7.331  1.00 16.07 ?  76  LYS   A HA   1 
ATOM   1707 H HB2  . LYS   A 1 76  ? 33.757 -6.258  -5.747  1.00 18.80 ?  76  LYS   A HB2  1 
ATOM   1708 H HB3  . LYS   A 1 76  ? 33.607 -6.241  -7.325  1.00 18.80 ?  76  LYS   A HB3  1 
ATOM   1709 H HG2  . LYS   A 1 76  ? 35.783 -5.602  -7.592  1.00 20.79 ?  76  LYS   A HG2  1 
ATOM   1710 H HG3  . LYS   A 1 76  ? 35.952 -5.359  -6.031  1.00 20.79 ?  76  LYS   A HG3  1 
ATOM   1711 H HD2  . LYS   A 1 76  ? 35.836 -7.636  -5.639  1.00 22.67 ?  76  LYS   A HD2  1 
ATOM   1712 H HD3  . LYS   A 1 76  ? 35.594 -7.905  -7.191  1.00 22.67 ?  76  LYS   A HD3  1 
ATOM   1713 H HE2  . LYS   A 1 76  ? 37.723 -7.126  -7.672  1.00 26.02 ?  76  LYS   A HE2  1 
ATOM   1714 H HE3  . LYS   A 1 76  ? 37.965 -6.805  -6.134  1.00 26.02 ?  76  LYS   A HE3  1 
ATOM   1715 H HZ1  . LYS   A 1 76  ? 38.949 -8.760  -6.702  1.00 27.31 ?  76  LYS   A HZ1  1 
ATOM   1716 H HZ2  . LYS   A 1 76  ? 37.909 -9.034  -5.732  1.00 27.31 ?  76  LYS   A HZ2  1 
ATOM   1717 H HZ3  . LYS   A 1 76  ? 37.688 -9.328  -7.133  1.00 27.31 ?  76  LYS   A HZ3  1 
ATOM   1718 N N    . VAL   A 1 77  ? 31.194 -4.404  -7.386  1.00 12.62 ?  77  VAL   A N    1 
ATOM   1719 C CA   . VAL   A 1 77  ? 29.785 -4.785  -7.292  1.00 12.25 ?  77  VAL   A CA   1 
ATOM   1720 C C    . VAL   A 1 77  ? 29.722 -6.241  -6.855  1.00 11.86 ?  77  VAL   A C    1 
ATOM   1721 O O    . VAL   A 1 77  ? 30.378 -7.107  -7.444  1.00 12.23 ?  77  VAL   A O    1 
ATOM   1722 C CB   . VAL   A 1 77  ? 29.058 -4.555  -8.624  1.00 13.50 ?  77  VAL   A CB   1 
ATOM   1723 C CG1  . VAL   A 1 77  ? 27.603 -4.996  -8.516  1.00 14.59 ?  77  VAL   A CG1  1 
ATOM   1724 C CG2  . VAL   A 1 77  ? 29.142 -3.092  -9.029  1.00 15.21 ?  77  VAL   A CG2  1 
ATOM   1725 H H    . VAL   A 1 77  ? 31.464 -4.164  -8.163  1.00 15.13 ?  77  VAL   A H    1 
ATOM   1726 H HA   . VAL   A 1 77  ? 29.356 -4.243  -6.611  1.00 14.69 ?  77  VAL   A HA   1 
ATOM   1727 H HB   . VAL   A 1 77  ? 29.490 -5.085  -9.314  1.00 16.19 ?  77  VAL   A HB   1 
ATOM   1728 H HG11 . VAL   A 1 77  ? 27.130 -4.696  -9.305  1.00 17.49 ?  77  VAL   A HG11 1 
ATOM   1729 H HG12 . VAL   A 1 77  ? 27.569 -5.962  -8.453  1.00 17.49 ?  77  VAL   A HG12 1 
ATOM   1730 H HG13 . VAL   A 1 77  ? 27.215 -4.596  -7.723  1.00 17.49 ?  77  VAL   A HG13 1 
ATOM   1731 H HG21 . VAL   A 1 77  ? 28.631 -2.963  -9.841  1.00 18.25 ?  77  VAL   A HG21 1 
ATOM   1732 H HG22 . VAL   A 1 77  ? 28.773 -2.548  -8.314  1.00 18.25 ?  77  VAL   A HG22 1 
ATOM   1733 H HG23 . VAL   A 1 77  ? 30.070 -2.856  -9.178  1.00 18.25 ?  77  VAL   A HG23 1 
ATOM   1734 N N    . GLY   A 1 78  ? 28.940 -6.514  -5.807  1.00 11.83 ?  78  GLY   A N    1 
ATOM   1735 C CA   . GLY   A 1 78  ? 28.920 -7.807  -5.152  1.00 11.84 ?  78  GLY   A CA   1 
ATOM   1736 C C    . GLY   A 1 78  ? 29.844 -7.907  -3.959  1.00 11.29 ?  78  GLY   A C    1 
ATOM   1737 O O    . GLY   A 1 78  ? 29.787 -8.914  -3.231  1.00 12.06 ?  78  GLY   A O    1 
ATOM   1738 H H    . GLY   A 1 78  ? 28.389 -5.944  -5.464  1.00 14.19 ?  78  GLY   A H    1 
ATOM   1739 H HA2  . GLY   A 1 78  ? 28.017 -7.994  -4.853  1.00 14.19 ?  78  GLY   A HA2  1 
ATOM   1740 H HA3  . GLY   A 1 78  ? 29.175 -8.488  -5.793  1.00 14.19 ?  78  GLY   A HA3  1 
ATOM   1741 N N    . GLY   A 1 79  ? 30.701 -6.904  -3.743  1.00 11.36 ?  79  GLY   A N    1 
ATOM   1742 C CA   . GLY   A 1 79  ? 31.669 -6.924  -2.673  1.00 11.59 ?  79  GLY   A CA   1 
ATOM   1743 C C    . GLY   A 1 79  ? 31.226 -6.130  -1.454  1.00 11.03 ?  79  GLY   A C    1 
ATOM   1744 O O    . GLY   A 1 79  ? 30.106 -5.621  -1.370  1.00 11.82 ?  79  GLY   A O    1 
ATOM   1745 H H    . GLY   A 1 79  ? 30.740 -6.188  -4.222  1.00 13.61 ?  79  GLY   A H    1 
ATOM   1746 H HA2  . GLY   A 1 79  ? 31.826 -7.849  -2.402  1.00 13.90 ?  79  GLY   A HA2  1 
ATOM   1747 H HA3  . GLY   A 1 79  ? 32.510 -6.561  -2.990  1.00 13.90 ?  79  GLY   A HA3  1 
ATOM   1748 N N    . SER   A 1 80  ? 32.137 -6.040  -0.485  1.00 11.77 ?  80  SER   A N    1 
ATOM   1749 C CA   . SER   A 1 80  ? 31.826 -5.406  0.787   1.00 11.34 ?  80  SER   A CA   1 
ATOM   1750 C C    . SER   A 1 80  ? 33.103 -4.956  1.478   1.00 11.13 ?  80  SER   A C    1 
ATOM   1751 O O    . SER   A 1 80  ? 34.213 -5.393  1.145   1.00 12.67 ?  80  SER   A O    1 
ATOM   1752 C CB   . SER   A 1 80  ? 31.070 -6.365  1.713   1.00 12.43 ?  80  SER   A CB   1 
ATOM   1753 O OG   . SER   A 1 80  ? 31.902 -7.423  2.173   1.00 14.19 ?  80  SER   A OG   1 
ATOM   1754 H H    . SER   A 1 80  ? 32.946 -6.332  -0.546  1.00 14.11 ?  80  SER   A H    1 
ATOM   1755 H HA   . SER   A 1 80  ? 31.274 -4.630  0.617   1.00 13.59 ?  80  SER   A HA   1 
ATOM   1756 H HB2  . SER   A 1 80  ? 30.744 -5.869  2.478   1.00 14.90 ?  80  SER   A HB2  1 
ATOM   1757 H HB3  . SER   A 1 80  ? 30.323 -6.748  1.224   1.00 14.90 ?  80  SER   A HB3  1 
ATOM   1758 H HG   . SER   A 1 80  ? 32.196 -7.864  1.517   1.00 17.02 ?  80  SER   A HG   1 
ATOM   1759 N N    . CYS   A 1 81  ? 32.920 -4.111  2.489   1.00 10.94 ?  81  CYS   A N    1 
ATOM   1760 C CA   . CYS   A 1 81  ? 33.979 -3.832  3.448   1.00 11.40 ?  81  CYS   A CA   1 
ATOM   1761 C C    . CYS   A 1 81  ? 33.340 -3.597  4.810   1.00 11.12 ?  81  CYS   A C    1 
ATOM   1762 O O    . CYS   A 1 81  ? 32.173 -3.200  4.900   1.00 12.29 ?  81  CYS   A O    1 
ATOM   1763 C CB   . CYS   A 1 81  ? 34.850 -2.644  3.024   1.00 11.95 ?  81  CYS   A CB   1 
ATOM   1764 S SG   . CYS   A 1 81  ? 33.966 -1.062  3.060   1.00 12.05 ?  81  CYS   A SG   1 
ATOM   1765 H H    . CYS   A 1 81  ? 32.188 -3.677  2.638   1.00 13.11 ?  81  CYS   A H    1 
ATOM   1766 H HA   . CYS   A 1 81  ? 34.553 -4.611  3.512   1.00 13.67 ?  81  CYS   A HA   1 
ATOM   1767 H HB2  . CYS   A 1 81  ? 35.612 -2.579  3.625   1.00 14.32 ?  81  CYS   A HB2  1 
ATOM   1768 H HB3  . CYS   A 1 81  ? 35.170 -2.794  2.114   1.00 14.32 ?  81  CYS   A HB3  1 
ATOM   1769 H HG   . CYS   A 1 81  ? 34.715 -0.189  2.713   1.00 14.44 ?  81  CYS   A HG   1 
ATOM   1770 N N    . VAL   A 1 82  ? 34.109 -3.859  5.865   1.00 11.25 ?  82  VAL   A N    1 
ATOM   1771 C CA   . VAL   A 1 82  ? 33.690 -3.616  7.238   1.00 11.95 ?  82  VAL   A CA   1 
ATOM   1772 C C    . VAL   A 1 82  ? 34.296 -2.302  7.712   1.00 12.32 ?  82  VAL   A C    1 
ATOM   1773 O O    . VAL   A 1 82  ? 35.521 -2.131  7.693   1.00 12.89 ?  82  VAL   A O    1 
ATOM   1774 C CB   . VAL   A 1 82  ? 34.114 -4.762  8.169   1.00 13.44 ?  82  VAL   A CB   1 
ATOM   1775 C CG1  . VAL   A 1 82  ? 33.665 -4.467  9.589   1.00 14.82 ?  82  VAL   A CG1  1 
ATOM   1776 C CG2  . VAL   A 1 82  ? 33.556 -6.092  7.692   1.00 14.33 ?  82  VAL   A CG2  1 
ATOM   1777 H H    . VAL   A 1 82  ? 34.908 -4.191  5.804   1.00 13.48 ?  82  VAL   A H    1 
ATOM   1778 H HA   . VAL   A 1 82  ? 32.725 -3.536  7.264   1.00 14.33 ?  82  VAL   A HA   1 
ATOM   1779 H HB   . VAL   A 1 82  ? 35.080 -4.825  8.171   1.00 16.11 ?  82  VAL   A HB   1 
ATOM   1780 H HG11 . VAL   A 1 82  ? 33.743 -5.275  10.120  1.00 17.78 ?  82  VAL   A HG11 1 
ATOM   1781 H HG12 . VAL   A 1 82  ? 34.224 -3.770  9.967   1.00 17.78 ?  82  VAL   A HG12 1 
ATOM   1782 H HG13 . VAL   A 1 82  ? 32.737 -4.174  9.576   1.00 17.78 ?  82  VAL   A HG13 1 
ATOM   1783 H HG21 . VAL   A 1 82  ? 33.809 -6.783  8.323   1.00 17.18 ?  82  VAL   A HG21 1 
ATOM   1784 H HG22 . VAL   A 1 82  ? 32.590 -6.028  7.639   1.00 17.18 ?  82  VAL   A HG22 1 
ATOM   1785 H HG23 . VAL   A 1 82  ? 33.923 -6.291  6.817   1.00 17.18 ?  82  VAL   A HG23 1 
ATOM   1786 N N    . LEU   A 1 83  ? 33.447 -1.376  8.143   1.00 11.70 ?  83  LEU   A N    1 
ATOM   1787 C CA   . LEU   A 1 83  ? 33.878 -0.118  8.730   1.00 11.59 ?  83  LEU   A CA   1 
ATOM   1788 C C    . LEU   A 1 83  ? 33.164 0.057   10.067  1.00 11.81 ?  83  LEU   A C    1 
ATOM   1789 O O    . LEU   A 1 83  ? 32.441 -0.832  10.530  1.00 12.35 ?  83  LEU   A O    1 
ATOM   1790 C CB   . LEU   A 1 83  ? 33.634 1.046   7.760   1.00 11.90 ?  83  LEU   A CB   1 
ATOM   1791 C CG   . LEU   A 1 83  ? 34.522 1.047   6.511   1.00 12.82 ?  83  LEU   A CG   1 
ATOM   1792 C CD1  . LEU   A 1 83  ? 34.081 2.096   5.510   1.00 13.59 ?  83  LEU   A CD1  1 
ATOM   1793 C CD2  . LEU   A 1 83  ? 35.984 1.259   6.884   1.00 13.58 ?  83  LEU   A CD2  1 
ATOM   1794 H H    . LEU   A 1 83  ? 32.589 -1.456  8.095   1.00 14.03 ?  83  LEU   A H    1 
ATOM   1795 H HA   . LEU   A 1 83  ? 34.831 -0.162  8.903   1.00 13.90 ?  83  LEU   A HA   1 
ATOM   1796 H HB2  . LEU   A 1 83  ? 32.713 1.016   7.459   1.00 14.27 ?  83  LEU   A HB2  1 
ATOM   1797 H HB3  . LEU   A 1 83  ? 33.793 1.882   8.230   1.00 14.27 ?  83  LEU   A HB3  1 
ATOM   1798 H HG   . LEU   A 1 83  ? 34.456 0.181   6.086   1.00 15.38 ?  83  LEU   A HG   1 
ATOM   1799 H HD11 . LEU   A 1 83  ? 34.666 2.053   4.734   1.00 16.30 ?  83  LEU   A HD11 1 
ATOM   1800 H HD12 . LEU   A 1 83  ? 33.168 1.908   5.244   1.00 16.30 ?  83  LEU   A HD12 1 
ATOM   1801 H HD13 . LEU   A 1 83  ? 34.138 2.970   5.919   1.00 16.30 ?  83  LEU   A HD13 1 
ATOM   1802 H HD21 . LEU   A 1 83  ? 36.500 1.409   6.072   1.00 16.28 ?  83  LEU   A HD21 1 
ATOM   1803 H HD22 . LEU   A 1 83  ? 36.058 2.035   7.464   1.00 16.28 ?  83  LEU   A HD22 1 
ATOM   1804 H HD23 . LEU   A 1 83  ? 36.318 0.473   7.342   1.00 16.28 ?  83  LEU   A HD23 1 
ATOM   1805 N N    . SER   A 1 84  ? 33.375 1.205   10.704  1.00 12.31 ?  84  SER   A N    1 
ATOM   1806 C CA   . SER   A 1 84  ? 32.733 1.459   11.982  1.00 12.42 ?  84  SER   A CA   1 
ATOM   1807 C C    . SER   A 1 84  ? 31.214 1.544   11.834  1.00 12.11 ?  84  SER   A C    1 
ATOM   1808 O O    . SER   A 1 84  ? 30.688 2.011   10.822  1.00 12.58 ?  84  SER   A O    1 
ATOM   1809 C CB   . SER   A 1 84  ? 33.241 2.775   12.565  1.00 13.29 ?  84  SER   A CB   1 
ATOM   1810 O OG   . SER   A 1 84  ? 32.598 3.062   13.791  1.00 14.37 ?  84  SER   A OG   1 
ATOM   1811 H H    . SER   A 1 84  ? 33.879 1.849   10.414  1.00 14.76 ?  84  SER   A H    1 
ATOM   1812 H HA   . SER   A 1 84  ? 32.950 0.741   12.594  1.00 14.89 ?  84  SER   A HA   1 
ATOM   1813 H HB2  . SER   A 1 84  ? 34.198 2.702   12.715  1.00 15.93 ?  84  SER   A HB2  1 
ATOM   1814 H HB3  . SER   A 1 84  ? 33.061 3.489   11.933  1.00 15.93 ?  84  SER   A HB3  1 
ATOM   1815 H HG   . SER   A 1 84  ? 32.889 3.792   14.101  1.00 17.23 ?  84  SER   A HG   1 
ATOM   1816 N N    . GLY   A 1 85  ? 30.508 1.132   12.883  1.00 13.14 ?  85  GLY   A N    1 
ATOM   1817 C CA   . GLY   A 1 85  ? 29.085 1.364   12.970  1.00 13.85 ?  85  GLY   A CA   1 
ATOM   1818 C C    . GLY   A 1 85  ? 28.721 2.675   13.624  1.00 13.49 ?  85  GLY   A C    1 
ATOM   1819 O O    . GLY   A 1 85  ? 27.533 2.988   13.756  1.00 13.99 ?  85  GLY   A O    1 
ATOM   1820 H H    . GLY   A 1 85  ? 30.846 0.715   13.560  1.00 15.76 ?  85  GLY   A H    1 
ATOM   1821 H HA2  . GLY   A 1 85  ? 28.712 1.347   12.075  1.00 16.61 ?  85  GLY   A HA2  1 
ATOM   1822 H HA3  . GLY   A 1 85  ? 28.683 0.652   13.482  1.00 16.61 ?  85  GLY   A HA3  1 
ATOM   1823 N N    . HIS   A 1 86  ? 29.710 3.445   14.062  1.00 13.15 ?  86  HIS   A N    1 
ATOM   1824 C CA   . HIS   A 1 86  ? 29.482 4.778   14.640  1.00 13.85 ?  86  HIS   A CA   1 
ATOM   1825 C C    . HIS   A 1 86  ? 28.501 4.651   15.799  1.00 14.27 ?  86  HIS   A C    1 
ATOM   1826 O O    . HIS   A 1 86  ? 28.692 3.774   16.658  1.00 15.78 ?  86  HIS   A O    1 
ATOM   1827 C CB   . HIS   A 1 86  ? 29.108 5.776   13.543  1.00 13.84 ?  86  HIS   A CB   1 
ATOM   1828 C CG   . HIS   A 1 86  ? 30.156 5.874   12.495  1.00 13.89 ?  86  HIS   A CG   1 
ATOM   1829 N ND1  . HIS   A 1 86  ? 31.248 6.705   12.622  1.00 14.97 ?  86  HIS   A ND1  1 
ATOM   1830 C CD2  . HIS   A 1 86  ? 30.328 5.193   11.340  1.00 13.61 ?  86  HIS   A CD2  1 
ATOM   1831 C CE1  . HIS   A 1 86  ? 32.038 6.541   11.575  1.00 14.81 ?  86  HIS   A CE1  1 
ATOM   1832 N NE2  . HIS   A 1 86  ? 31.508 5.624   10.789  1.00 14.17 ?  86  HIS   A NE2  1 
ATOM   1833 H H    . HIS   A 1 86  ? 30.538 3.220   14.046  1.00 15.77 ?  86  HIS   A H    1 
ATOM   1834 H HA   . HIS   A 1 86  ? 30.323 5.088   15.011  1.00 16.61 ?  86  HIS   A HA   1 
ATOM   1835 H HB2  . HIS   A 1 86  ? 28.282 5.502   13.118  1.00 16.60 ?  86  HIS   A HB2  1 
ATOM   1836 H HB3  . HIS   A 1 86  ? 28.998 6.663   13.935  1.00 16.60 ?  86  HIS   A HB3  1 
ATOM   1837 H HD2  . HIS   A 1 86  ? 29.760 4.543   10.990  1.00 16.32 ?  86  HIS   A HD2  1 
ATOM   1838 H HE1  . HIS   A 1 86  ? 32.836 6.995   11.405  1.00 17.76 ?  86  HIS   A HE1  1 
ATOM   1839 H HE2  . HIS   A 1 86  ? 31.837 5.352   10.032  1.00 16.99 ?  86  HIS   A HE2  1 
ATOM   1840 N N    . ASN   A 1 87  ? 27.488 5.506   15.878  1.00 15.66 ?  87  ASN   A N    1 
ATOM   1841 C CA   . ASN   A 1 87  ? 26.507 5.487   16.947  1.00 16.61 ?  87  ASN   A CA   1 
ATOM   1842 C C    . ASN   A 1 87  ? 25.385 4.490   16.703  1.00 17.64 ?  87  ASN   A C    1 
ATOM   1843 O O    . ASN   A 1 87  ? 24.461 4.415   17.518  1.00 19.89 ?  87  ASN   A O    1 
ATOM   1844 C CB   . ASN   A 1 87  ? 25.909 6.891   17.120  1.00 17.31 ?  87  ASN   A CB   1 
ATOM   1845 C CG   . ASN   A 1 87  ? 25.379 7.475   15.814  1.00 17.99 ?  87  ASN   A CG   1 
ATOM   1846 O OD1  . ASN   A 1 87  ? 26.006 7.371   14.761  1.00 18.58 ?  87  ASN   A OD1  1 
ATOM   1847 N ND2  . ASN   A 1 87  ? 24.216 8.096   15.886  1.00 19.21 ?  87  ASN   A ND2  1 
ATOM   1848 H H    . ASN   A 1 87  ? 27.349 6.131   15.307  1.00 18.78 ?  87  ASN   A H    1 
ATOM   1849 H HA   . ASN   A 1 87  ? 26.948 5.243   17.781  1.00 19.92 ?  87  ASN   A HA   1 
ATOM   1850 H HB2  . ASN   A 1 87  ? 25.170 6.839   17.758  1.00 20.76 ?  87  ASN   A HB2  1 
ATOM   1851 H HB3  . ASN   A 1 87  ? 26.592 7.485   17.464  1.00 20.76 ?  87  ASN   A HB3  1 
ATOM   1852 H HD21 . ASN   A 1 87  ? 23.870 8.441   15.183  1.00 23.05 ?  87  ASN   A HD21 1 
ATOM   1853 H HD22 . ASN   A 1 87  ? 23.802 8.158   16.644  1.00 23.05 ?  87  ASN   A HD22 1 
ATOM   1854 N N    . LEU   A 1 88  ? 25.442 3.713   15.624  1.00 16.49 ?  88  LEU   A N    1 
ATOM   1855 C CA   . LEU   A 1 88  ? 24.333 2.846   15.241  1.00 16.48 ?  88  LEU   A CA   1 
ATOM   1856 C C    . LEU   A 1 88  ? 24.562 1.370   15.538  1.00 15.99 ?  88  LEU   A C    1 
ATOM   1857 O O    . LEU   A 1 88  ? 23.588 0.634   15.719  1.00 17.39 ?  88  LEU   A O    1 
ATOM   1858 C CB   . LEU   A 1 88  ? 24.052 3.004   13.746  1.00 17.34 ?  88  LEU   A CB   1 
ATOM   1859 C CG   . LEU   A 1 88  ? 23.780 4.431   13.261  1.00 19.03 ?  88  LEU   A CG   1 
ATOM   1860 C CD1  . LEU   A 1 88  ? 23.604 4.455   11.753  1.00 19.34 ?  88  LEU   A CD1  1 
ATOM   1861 C CD2  . LEU   A 1 88  ? 22.563 5.031   13.956  1.00 20.79 ?  88  LEU   A CD2  1 
ATOM   1862 H H    . LEU   A 1 88  ? 26.120 3.673   15.099  1.00 19.78 ?  88  LEU   A H    1 
ATOM   1863 H HA   . LEU   A 1 88  ? 23.543 3.125   15.726  1.00 19.76 ?  88  LEU   A HA   1 
ATOM   1864 H HB2  . LEU   A 1 88  ? 24.815 2.673   13.253  1.00 20.79 ?  88  LEU   A HB2  1 
ATOM   1865 H HB3  . LEU   A 1 88  ? 23.269 2.474   13.530  1.00 20.79 ?  88  LEU   A HB3  1 
ATOM   1866 H HG   . LEU   A 1 88  ? 24.547 4.983   13.474  1.00 22.83 ?  88  LEU   A HG   1 
ATOM   1867 H HD11 . LEU   A 1 88  ? 23.438 5.369   11.470  1.00 23.19 ?  88  LEU   A HD11 1 
ATOM   1868 H HD12 . LEU   A 1 88  ? 24.413 4.122   11.334  1.00 23.19 ?  88  LEU   A HD12 1 
ATOM   1869 H HD13 . LEU   A 1 88  ? 22.851 3.893   11.513  1.00 23.19 ?  88  LEU   A HD13 1 
ATOM   1870 H HD21 . LEU   A 1 88  ? 22.373 5.897   13.561  1.00 24.94 ?  88  LEU   A HD21 1 
ATOM   1871 H HD22 . LEU   A 1 88  ? 21.808 4.438   13.837  1.00 24.94 ?  88  LEU   A HD22 1 
ATOM   1872 H HD23 . LEU   A 1 88  ? 22.762 5.134   14.899  1.00 24.94 ?  88  LEU   A HD23 1 
ATOM   1873 N N    . ALA   A 1 89  ? 25.812 0.922   15.569  1.00 15.21 ?  89  ALA   A N    1 
ATOM   1874 C CA   . ALA   A 1 89  ? 26.160 -0.490  15.664  1.00 14.92 ?  89  ALA   A CA   1 
ATOM   1875 C C    . ALA   A 1 89  ? 27.644 -0.548  15.984  1.00 15.51 ?  89  ALA   A C    1 
ATOM   1876 O O    . ALA   A 1 89  ? 28.349 0.454   15.874  1.00 16.30 ?  89  ALA   A O    1 
ATOM   1877 C CB   . ALA   A 1 89  ? 25.882 -1.204  14.341  1.00 14.47 ?  89  ALA   A CB   1 
ATOM   1878 H H    . ALA   A 1 89  ? 26.499 1.435   15.529  1.00 18.24 ?  89  ALA   A H    1 
ATOM   1879 H HA   . ALA   A 1 89  ? 25.658 -0.915  16.379  1.00 17.89 ?  89  ALA   A HA   1 
ATOM   1880 H HB1  . ALA   A 1 89  ? 26.146 -2.136  14.426  1.00 17.36 ?  89  ALA   A HB1  1 
ATOM   1881 H HB2  . ALA   A 1 89  ? 24.933 -1.149  14.145  1.00 17.36 ?  89  ALA   A HB2  1 
ATOM   1882 H HB3  . ALA   A 1 89  ? 26.394 -0.779  13.639  1.00 17.36 ?  89  ALA   A HB3  1 
ATOM   1883 N N    . LYS   A 1 90  ? 28.130 -1.730  16.359  1.00 16.22 ?  90  LYS   A N    1 
ATOM   1884 C CA   . LYS   A 1 90  ? 29.575 -1.878  16.497  1.00 16.84 ?  90  LYS   A CA   1 
ATOM   1885 C C    . LYS   A 1 90  ? 30.262 -1.682  15.149  1.00 15.43 ?  90  LYS   A C    1 
ATOM   1886 O O    . LYS   A 1 90  ? 31.191 -0.870  15.019  1.00 16.56 ?  90  LYS   A O    1 
ATOM   1887 C CB   . LYS   A 1 90  ? 29.918 -3.240  17.101  1.00 19.53 ?  90  LYS   A CB   1 
ATOM   1888 C CG   . LYS   A 1 90  ? 31.386 -3.372  17.470  1.00 23.85 ?  90  LYS   A CG   1 
ATOM   1889 C CD   . LYS   A 1 90  ? 31.624 -4.589  18.347  1.00 28.35 ?  90  LYS   A CD   1 
ATOM   1890 C CE   . LYS   A 1 90  ? 33.039 -4.611  18.905  1.00 31.78 ?  90  LYS   A CE   1 
ATOM   1891 N NZ   . LYS   A 1 90  ? 34.053 -4.949  17.872  1.00 33.70 ?  90  LYS   A NZ   1 
ATOM   1892 H H    . LYS   A 1 90  ? 27.665 -2.428  16.533  1.00 19.46 ?  90  LYS   A H    1 
ATOM   1893 H HA   . LYS   A 1 90  ? 29.907 -1.195  17.096  1.00 20.19 ?  90  LYS   A HA   1 
ATOM   1894 H HB2  . LYS   A 1 90  ? 29.393 -3.367  17.908  1.00 23.42 ?  90  LYS   A HB2  1 
ATOM   1895 H HB3  . LYS   A 1 90  ? 29.707 -3.935  16.458  1.00 23.42 ?  90  LYS   A HB3  1 
ATOM   1896 H HG2  . LYS   A 1 90  ? 31.914 -3.471  16.663  1.00 28.61 ?  90  LYS   A HG2  1 
ATOM   1897 H HG3  . LYS   A 1 90  ? 31.667 -2.583  17.961  1.00 28.61 ?  90  LYS   A HG3  1 
ATOM   1898 H HD2  . LYS   A 1 90  ? 31.004 -4.573  19.094  1.00 34.01 ?  90  LYS   A HD2  1 
ATOM   1899 H HD3  . LYS   A 1 90  ? 31.494 -5.394  17.821  1.00 34.01 ?  90  LYS   A HD3  1 
ATOM   1900 H HE2  . LYS   A 1 90  ? 33.253 -3.733  19.260  1.00 38.12 ?  90  LYS   A HE2  1 
ATOM   1901 H HE3  . LYS   A 1 90  ? 33.092 -5.275  19.610  1.00 38.12 ?  90  LYS   A HE3  1 
ATOM   1902 H HZ1  . LYS   A 1 90  ? 33.885 -5.756  17.534  1.00 40.42 ?  90  LYS   A HZ1  1 
ATOM   1903 H HZ2  . LYS   A 1 90  ? 34.031 -4.350  17.215  1.00 40.42 ?  90  LYS   A HZ2  1 
ATOM   1904 H HZ3  . LYS   A 1 90  ? 34.867 -4.952  18.234  1.00 40.42 ?  90  LYS   A HZ3  1 
ATOM   1905 N N    . HIS   A 1 91  ? 29.785 -2.394  14.126  1.00 13.91 ?  91  HIS   A N    1 
ATOM   1906 C CA   . HIS   A 1 91  ? 30.353 -2.367  12.793  1.00 13.17 ?  91  HIS   A CA   1 
ATOM   1907 C C    . HIS   A 1 91  ? 29.260 -2.088  11.778  1.00 11.98 ?  91  HIS   A C    1 
ATOM   1908 O O    . HIS   A 1 91  ? 28.094 -2.451  11.975  1.00 12.83 ?  91  HIS   A O    1 
ATOM   1909 C CB   . HIS   A 1 91  ? 30.955 -3.731  12.418  1.00 15.85 ?  91  HIS   A CB   1 
ATOM   1910 C CG   . HIS   A 1 91  ? 31.955 -4.250  13.402  1.00 20.02 ?  91  HIS   A CG   1 
ATOM   1911 N ND1  . HIS   A 1 91  ? 33.233 -3.744  13.503  1.00 22.14 ?  91  HIS   A ND1  1 
ATOM   1912 C CD2  . HIS   A 1 91  ? 31.871 -5.242  14.321  1.00 21.68 ?  91  HIS   A CD2  1 
ATOM   1913 C CE1  . HIS   A 1 91  ? 33.892 -4.397  14.443  1.00 22.89 ?  91  HIS   A CE1  1 
ATOM   1914 N NE2  . HIS   A 1 91  ? 33.088 -5.314  14.954  1.00 22.95 ?  91  HIS   A NE2  1 
ATOM   1915 H H    . HIS   A 1 91  ? 29.110 -2.934  14.193  1.00 16.67 ?  91  HIS   A H    1 
ATOM   1916 H HA   . HIS   A 1 91  ? 31.041 -1.691  12.729  1.00 15.79 ?  91  HIS   A HA   1 
ATOM   1917 H HB2  . HIS   A 1 91  ? 30.239 -4.385  12.357  1.00 19.00 ?  91  HIS   A HB2  1 
ATOM   1918 H HB3  . HIS   A 1 91  ? 31.398 -3.654  11.558  1.00 19.00 ?  91  HIS   A HB3  1 
ATOM   1919 H HD1  . HIS   A 1 91  ? 33.552 -3.103  13.023  1.00 26.55 ?  91  HIS   A HD1  1 
ATOM   1920 H HD2  . HIS   A 1 91  ? 31.134 -5.775  14.493  1.00 26.01 ?  91  HIS   A HD2  1 
ATOM   1921 H HE1  . HIS   A 1 91  ? 34.775 -4.234  14.698  1.00 27.46 ?  91  HIS   A HE1  1 
ATOM   1922 N N    . CYS   A 1 92  ? 29.662 -1.490  10.663  1.00 11.79 ?  92  CYS   A N    1 
ATOM   1923 C CA   . CYS   A 1 92  ? 28.827 -1.415  9.474   1.00 11.43 ?  92  CYS   A CA   1 
ATOM   1924 C C    . CYS   A 1 92  ? 29.465 -2.238  8.366   1.00 11.14 ?  92  CYS   A C    1 
ATOM   1925 O O    . CYS   A 1 92  ? 30.618 -1.987  7.985   1.00 11.66 ?  92  CYS   A O    1 
ATOM   1926 C CB   . CYS   A 1 92  ? 28.613 0.029   9.016   1.00 12.02 ?  92  CYS   A CB   1 
ATOM   1927 S SG   . CYS   A 1 92  ? 27.582 0.141   7.521   1.00 11.34 ?  92  CYS   A SG   1 
ATOM   1928 H H    . CYS   A 1 92  ? 30.431 -1.109  10.568  1.00 14.14 ?  92  CYS   A H    1 
ATOM   1929 H HA   . CYS   A 1 92  ? 27.958 -1.793  9.673   1.00 13.71 ?  92  CYS   A HA   1 
ATOM   1930 H HB2  . CYS   A 1 92  ? 28.168 0.528   9.721   1.00 14.41 ?  92  CYS   A HB2  1 
ATOM   1931 H HB3  . CYS   A 1 92  ? 29.471 0.434   8.815   1.00 14.41 ?  92  CYS   A HB3  1 
ATOM   1932 H HG   . CYS   A 1 92  ? 27.447 1.296   7.235   1.00 13.59 ?  92  CYS   A HG   1 
ATOM   1933 N N    . LEU   A 1 93  ? 28.719 -3.215  7.858   1.00 10.86 ?  93  LEU   A N    1 
ATOM   1934 C CA   . LEU   A 1 93  ? 29.113 -3.976  6.677   1.00 10.42 ?  93  LEU   A CA   1 
ATOM   1935 C C    . LEU   A 1 93  ? 28.517 -3.273  5.463   1.00 10.44 ?  93  LEU   A C    1 
ATOM   1936 O O    . LEU   A 1 93  ? 27.302 -3.326  5.243   1.00 10.49 ?  93  LEU   A O    1 
ATOM   1937 C CB   . LEU   A 1 93  ? 28.622 -5.419  6.784   1.00 11.02 ?  93  LEU   A CB   1 
ATOM   1938 C CG   . LEU   A 1 93  ? 29.010 -6.322  5.615   1.00 11.08 ?  93  LEU   A CG   1 
ATOM   1939 C CD1  . LEU   A 1 93  ? 30.523 -6.573  5.598   1.00 12.30 ?  93  LEU   A CD1  1 
ATOM   1940 C CD2  . LEU   A 1 93  ? 28.242 -7.645  5.637   1.00 12.06 ?  93  LEU   A CD2  1 
ATOM   1941 H H    . LEU   A 1 93  ? 27.959 -3.454  8.192   1.00 13.02 ?  93  LEU   A H    1 
ATOM   1942 H HA   . LEU   A 1 93  ? 30.073 -3.971  6.601   1.00 12.49 ?  93  LEU   A HA   1 
ATOM   1943 H HB2  . LEU   A 1 93  ? 28.992 -5.807  7.594   1.00 13.22 ?  93  LEU   A HB2  1 
ATOM   1944 H HB3  . LEU   A 1 93  ? 27.656 -5.415  6.840   1.00 13.22 ?  93  LEU   A HB3  1 
ATOM   1945 H HG   . LEU   A 1 93  ? 28.792 -5.876  4.790   1.00 13.29 ?  93  LEU   A HG   1 
ATOM   1946 H HD11 . LEU   A 1 93  ? 30.743 -7.193  4.884   1.00 14.75 ?  93  LEU   A HD11 1 
ATOM   1947 H HD12 . LEU   A 1 93  ? 30.990 -5.734  5.461   1.00 14.75 ?  93  LEU   A HD12 1 
ATOM   1948 H HD13 . LEU   A 1 93  ? 30.797 -6.959  6.454   1.00 14.75 ?  93  LEU   A HD13 1 
ATOM   1949 H HD21 . LEU   A 1 93  ? 28.526 -8.188  4.880   1.00 14.46 ?  93  LEU   A HD21 1 
ATOM   1950 H HD22 . LEU   A 1 93  ? 28.434 -8.114  6.464   1.00 14.46 ?  93  LEU   A HD22 1 
ATOM   1951 H HD23 . LEU   A 1 93  ? 27.295 -7.459  5.571   1.00 14.46 ?  93  LEU   A HD23 1 
ATOM   1952 N N    . HIS   A 1 94  ? 29.365 -2.583  4.702   1.00 10.10 ?  94  HIS   A N    1 
ATOM   1953 C CA   . HIS   A 1 94  ? 28.936 -1.901  3.485   1.00 10.12 ?  94  HIS   A CA   1 
ATOM   1954 C C    . HIS   A 1 94  ? 28.928 -2.931  2.369   1.00 10.02 ?  94  HIS   A C    1 
ATOM   1955 O O    . HIS   A 1 94  ? 29.991 -3.442  2.008   1.00 11.66 ?  94  HIS   A O    1 
ATOM   1956 C CB   . HIS   A 1 94  ? 29.893 -0.758  3.153   1.00 10.28 ?  94  HIS   A CB   1 
ATOM   1957 C CG   . HIS   A 1 94  ? 29.885 0.333   4.169   1.00 10.08 ?  94  HIS   A CG   1 
ATOM   1958 N ND1  . HIS   A 1 94  ? 29.009 1.397   4.118   1.00 10.42 ?  94  HIS   A ND1  1 
ATOM   1959 C CD2  . HIS   A 1 94  ? 30.632 0.499   5.283   1.00 11.17 ?  94  HIS   A CD2  1 
ATOM   1960 C CE1  . HIS   A 1 94  ? 29.225 2.170   5.166   1.00 10.32 ?  94  HIS   A CE1  1 
ATOM   1961 N NE2  . HIS   A 1 94  ? 30.203 1.649   5.887   1.00 10.92 ?  94  HIS   A NE2  1 
ATOM   1962 H H    . HIS   A 1 94  ? 30.209 -2.498  4.874   1.00 12.10 ?  94  HIS   A H    1 
ATOM   1963 H HA   . HIS   A 1 94  ? 28.038 -1.553  3.601   1.00 12.13 ?  94  HIS   A HA   1 
ATOM   1964 H HB2  . HIS   A 1 94  ? 30.790 -1.107  3.099   1.00 12.32 ?  94  HIS   A HB2  1 
ATOM   1965 H HB3  . HIS   A 1 94  ? 29.629 -0.373  2.302   1.00 12.32 ?  94  HIS   A HB3  1 
ATOM   1966 H HD2  . HIS   A 1 94  ? 31.303 -0.061  5.587   1.00 13.39 ?  94  HIS   A HD2  1 
ATOM   1967 H HE1  . HIS   A 1 94  ? 28.766 2.961   5.362   1.00 12.37 ?  94  HIS   A HE1  1 
ATOM   1968 H HE2  . HIS   A 1 94  ? 30.522 1.992   6.611   1.00 13.09 ?  94  HIS   A HE2  1 
ATOM   1969 N N    . VAL   A 1 95  ? 27.751 -3.261  1.837   1.00 9.54  ?  95  VAL   A N    1 
ATOM   1970 C CA   . VAL   A 1 95  ? 27.607 -4.292  0.811   1.00 9.94  ?  95  VAL   A CA   1 
ATOM   1971 C C    . VAL   A 1 95  ? 27.062 -3.648  -0.452  1.00 9.67  ?  95  VAL   A C    1 
ATOM   1972 O O    . VAL   A 1 95  ? 26.062 -2.920  -0.395  1.00 10.35 ?  95  VAL   A O    1 
ATOM   1973 C CB   . VAL   A 1 95  ? 26.678 -5.435  1.261   1.00 10.64 ?  95  VAL   A CB   1 
ATOM   1974 C CG1  . VAL   A 1 95  ? 26.556 -6.471  0.150   1.00 11.43 ?  95  VAL   A CG1  1 
ATOM   1975 C CG2  . VAL   A 1 95  ? 27.194 -6.066  2.541   1.00 10.82 ?  95  VAL   A CG2  1 
ATOM   1976 H H    . VAL   A 1 95  ? 27.002 -2.894  2.061   1.00 11.44 ?  95  VAL   A H    1 
ATOM   1977 H HA   . VAL   A 1 95  ? 28.473 -4.667  0.607   1.00 11.92 ?  95  VAL   A HA   1 
ATOM   1978 H HB   . VAL   A 1 95  ? 25.797 -5.078  1.439   1.00 12.76 ?  95  VAL   A HB   1 
ATOM   1979 H HG11 . VAL   A 1 95  ? 26.161 -7.284  0.514   1.00 13.70 ?  95  VAL   A HG11 1 
ATOM   1980 H HG12 . VAL   A 1 95  ? 25.988 -6.124  -0.556  1.00 13.70 ?  95  VAL   A HG12 1 
ATOM   1981 H HG13 . VAL   A 1 95  ? 27.438 -6.672  -0.204  1.00 13.70 ?  95  VAL   A HG13 1 
ATOM   1982 H HG21 . VAL   A 1 95  ? 26.637 -6.828  2.764   1.00 12.98 ?  95  VAL   A HG21 1 
ATOM   1983 H HG22 . VAL   A 1 95  ? 28.111 -6.354  2.405   1.00 12.98 ?  95  VAL   A HG22 1 
ATOM   1984 H HG23 . VAL   A 1 95  ? 27.157 -5.409  3.253   1.00 12.98 ?  95  VAL   A HG23 1 
ATOM   1985 N N    . VAL   A 1 96  ? 27.687 -3.939  -1.593  1.00 9.75  ?  96  VAL   A N    1 
ATOM   1986 C CA   . VAL   A 1 96  ? 27.274 -3.380  -2.873  1.00 10.33 ?  96  VAL   A CA   1 
ATOM   1987 C C    . VAL   A 1 96  ? 26.468 -4.424  -3.638  1.00 10.72 ?  96  VAL   A C    1 
ATOM   1988 O O    . VAL   A 1 96  ? 27.023 -5.366  -4.215  1.00 11.58 ?  96  VAL   A O    1 
ATOM   1989 C CB   . VAL   A 1 96  ? 28.468 -2.902  -3.698  1.00 10.85 ?  96  VAL   A CB   1 
ATOM   1990 C CG1  . VAL   A 1 96  ? 27.966 -2.251  -4.970  1.00 10.83 ?  96  VAL   A CG1  1 
ATOM   1991 C CG2  . VAL   A 1 96  ? 29.341 -1.940  -2.898  1.00 11.58 ?  96  VAL   A CG2  1 
ATOM   1992 H H    . VAL   A 1 96  ? 28.377 -4.457  -1.647  1.00 11.69 ?  96  VAL   A H    1 
ATOM   1993 H HA   . VAL   A 1 96  ? 26.703 -2.616  -2.713  1.00 12.38 ?  96  VAL   A HA   1 
ATOM   1994 H HB   . VAL   A 1 96  ? 29.011 -3.660  -3.951  1.00 13.00 ?  96  VAL   A HB   1 
ATOM   1995 H HG11 . VAL   A 1 96  ? 28.701 -1.773  -5.391  1.00 12.98 ?  96  VAL   A HG11 1 
ATOM   1996 H HG12 . VAL   A 1 96  ? 27.626 -2.928  -5.566  1.00 12.98 ?  96  VAL   A HG12 1 
ATOM   1997 H HG13 . VAL   A 1 96  ? 27.260 -1.618  -4.743  1.00 12.98 ?  96  VAL   A HG13 1 
ATOM   1998 H HG21 . VAL   A 1 96  ? 30.042 -1.590  -3.469  1.00 13.88 ?  96  VAL   A HG21 1 
ATOM   1999 H HG22 . VAL   A 1 96  ? 28.791 -1.211  -2.565  1.00 13.88 ?  96  VAL   A HG22 1 
ATOM   2000 H HG23 . VAL   A 1 96  ? 29.735 -2.419  -2.149  1.00 13.88 ?  96  VAL   A HG23 1 
ATOM   2001 N N    A GLY   A 1 97  ? 25.148 -4.266  -3.647  0.60 10.91 ?  97  GLY   A N    1 
ATOM   2002 N N    B GLY   A 1 97  ? 25.150 -4.257  -3.661  0.40 10.90 ?  97  GLY   A N    1 
ATOM   2003 C CA   A GLY   A 1 97  ? 24.316 -5.001  -4.566  0.60 11.35 ?  97  GLY   A CA   1 
ATOM   2004 C CA   B GLY   A 1 97  ? 24.320 -5.020  -4.559  0.40 11.15 ?  97  GLY   A CA   1 
ATOM   2005 C C    A GLY   A 1 97  ? 24.297 -4.320  -5.921  0.60 11.25 ?  97  GLY   A C    1 
ATOM   2006 C C    B GLY   A 1 97  ? 24.336 -4.403  -5.945  0.40 11.10 ?  97  GLY   A C    1 
ATOM   2007 O O    A GLY   A 1 97  ? 24.566 -3.117  -6.035  0.60 12.48 ?  97  GLY   A O    1 
ATOM   2008 O O    B GLY   A 1 97  ? 24.661 -3.222  -6.117  0.40 11.47 ?  97  GLY   A O    1 
ATOM   2009 H H    A GLY   A 1 97  ? 24.712 -3.726  -3.127  0.60 13.08 ?  97  GLY   A H    1 
ATOM   2010 H H    B GLY   A 1 97  ? 24.715 -3.697  -3.166  0.40 13.07 ?  97  GLY   A H    1 
ATOM   2011 H HA2  A GLY   A 1 97  ? 24.663 -5.903  -4.657  0.60 13.61 ?  97  GLY   A HA2  1 
ATOM   2012 H HA2  B GLY   A 1 97  ? 24.657 -5.928  -4.611  0.40 13.37 ?  97  GLY   A HA2  1 
ATOM   2013 H HA3  A GLY   A 1 97  ? 23.408 -5.049  -4.223  0.60 13.61 ?  97  GLY   A HA3  1 
ATOM   2014 H HA3  B GLY   A 1 97  ? 23.408 -5.042  -4.226  0.40 13.37 ?  97  GLY   A HA3  1 
ATOM   2015 N N    A PRO   A 1 98  ? 23.976 -5.062  -6.979  0.60 11.13 ?  98  PRO   A N    1 
ATOM   2016 N N    B PRO   A 1 98  ? 23.994 -5.185  -6.967  0.40 11.58 ?  98  PRO   A N    1 
ATOM   2017 C CA   A PRO   A 1 98  ? 23.859 -4.431  -8.299  0.60 12.18 ?  98  PRO   A CA   1 
ATOM   2018 C CA   B PRO   A 1 98  ? 23.903 -4.618  -8.316  0.40 12.48 ?  98  PRO   A CA   1 
ATOM   2019 C C    A PRO   A 1 98  ? 22.746 -3.389  -8.320  0.60 12.18 ?  98  PRO   A C    1 
ATOM   2020 C C    B PRO   A 1 98  ? 22.782 -3.593  -8.406  0.40 12.95 ?  98  PRO   A C    1 
ATOM   2021 O O    A PRO   A 1 98  ? 21.681 -3.572  -7.727  0.60 12.11 ?  98  PRO   A O    1 
ATOM   2022 O O    B PRO   A 1 98  ? 21.684 -3.791  -7.879  0.40 13.46 ?  98  PRO   A O    1 
ATOM   2023 C CB   A PRO   A 1 98  ? 23.544 -5.610  -9.226  0.60 12.86 ?  98  PRO   A CB   1 
ATOM   2024 C CB   B PRO   A 1 98  ? 23.607 -5.841  -9.194  0.40 12.49 ?  98  PRO   A CB   1 
ATOM   2025 C CG   A PRO   A 1 98  ? 22.921 -6.640  -8.333  0.60 13.13 ?  98  PRO   A CG   1 
ATOM   2026 C CG   B PRO   A 1 98  ? 22.960 -6.819  -8.266  0.40 12.65 ?  98  PRO   A CG   1 
ATOM   2027 C CD   A PRO   A 1 98  ? 23.661 -6.503  -7.026  0.60 12.17 ?  98  PRO   A CD   1 
ATOM   2028 C CD   B PRO   A 1 98  ? 23.660 -6.621  -6.949  0.40 11.85 ?  98  PRO   A CD   1 
ATOM   2029 H HA   A PRO   A 1 98  ? 24.700 -4.022  -8.553  0.60 14.61 ?  98  PRO   A HA   1 
ATOM   2030 H HA   B PRO   A 1 98  ? 24.747 -4.213  -8.579  0.40 14.96 ?  98  PRO   A HA   1 
ATOM   2031 H HB2  A PRO   A 1 98  ? 22.922 -5.326  -9.911  0.60 15.42 ?  98  PRO   A HB2  1 
ATOM   2032 H HB2  B PRO   A 1 98  ? 23.001 -5.585  -9.908  0.40 14.98 ?  98  PRO   A HB2  1 
ATOM   2033 H HB3  A PRO   A 1 98  ? 24.365 -5.945  -9.617  0.60 15.42 ?  98  PRO   A HB3  1 
ATOM   2034 H HB3  B PRO   A 1 98  ? 24.435 -6.192  -9.551  0.40 14.98 ?  98  PRO   A HB3  1 
ATOM   2035 H HG2  A PRO   A 1 98  ? 21.979 -6.446  -8.214  0.60 15.74 ?  98  PRO   A HG2  1 
ATOM   2036 H HG2  B PRO   A 1 98  ? 22.014 -6.618  -8.187  0.40 15.17 ?  98  PRO   A HG2  1 
ATOM   2037 H HG3  A PRO   A 1 98  ? 23.050 -7.523  -8.709  0.60 15.74 ?  98  PRO   A HG3  1 
ATOM   2038 H HG3  B PRO   A 1 98  ? 23.096 -7.718  -8.598  0.40 15.17 ?  98  PRO   A HG3  1 
ATOM   2039 H HD2  A PRO   A 1 98  ? 23.087 -6.754  -6.279  0.60 14.59 ?  98  PRO   A HD2  1 
ATOM   2040 H HD2  B PRO   A 1 98  ? 23.060 -6.823  -6.213  0.40 14.21 ?  98  PRO   A HD2  1 
ATOM   2041 H HD3  A PRO   A 1 98  ? 24.477 -7.031  -7.034  0.60 14.59 ?  98  PRO   A HD3  1 
ATOM   2042 H HD3  B PRO   A 1 98  ? 24.466 -7.160  -6.908  0.40 14.21 ?  98  PRO   A HD3  1 
ATOM   2043 N N    A ASN   A 1 99  ? 23.007 -2.281  -9.014  0.60 13.49 ?  99  ASN   A N    1 
ATOM   2044 N N    B ASN   A 1 99  ? 23.068 -2.484  -9.080  0.40 13.67 ?  99  ASN   A N    1 
ATOM   2045 C CA   A ASN   A 1 99  ? 22.033 -1.204  -9.196  0.60 14.45 ?  99  ASN   A CA   1 
ATOM   2046 C CA   B ASN   A 1 99  ? 22.082 -1.440  -9.324  0.40 14.57 ?  99  ASN   A CA   1 
ATOM   2047 C C    A ASN   A 1 99  ? 21.478 -1.332  -10.613 0.60 15.20 ?  99  ASN   A C    1 
ATOM   2048 C C    B ASN   A 1 99  ? 21.493 -1.646  -10.715 0.40 15.02 ?  99  ASN   A C    1 
ATOM   2049 O O    A ASN   A 1 99  ? 22.117 -0.920  -11.588 0.60 15.14 ?  99  ASN   A O    1 
ATOM   2050 O O    B ASN   A 1 99  ? 22.220 -1.619  -11.716 0.40 15.12 ?  99  ASN   A O    1 
ATOM   2051 C CB   A ASN   A 1 99  ? 22.679 0.158   -8.953  0.60 14.33 ?  99  ASN   A CB   1 
ATOM   2052 C CB   B ASN   A 1 99  ? 22.716 -0.052  -9.207  0.40 15.71 ?  99  ASN   A CB   1 
ATOM   2053 C CG   A ASN   A 1 99  ? 21.669 1.311   -8.974  0.60 14.59 ?  99  ASN   A CG   1 
ATOM   2054 C CG   B ASN   A 1 99  ? 21.680 1.066   -9.149  0.40 17.13 ?  99  ASN   A CG   1 
ATOM   2055 O OD1  A ASN   A 1 99  ? 20.667 1.269   -9.691  0.60 15.72 ?  99  ASN   A OD1  1 
ATOM   2056 O OD1  B ASN   A 1 99  ? 20.669 1.028   -9.852  0.40 17.67 ?  99  ASN   A OD1  1 
ATOM   2057 N ND2  A ASN   A 1 99  ? 21.947 2.351   -8.190  0.60 14.79 ?  99  ASN   A ND2  1 
ATOM   2058 N ND2  B ASN   A 1 99  ? 21.929 2.065   -8.301  0.40 17.62 ?  99  ASN   A ND2  1 
ATOM   2059 H H    A ASN   A 1 99  ? 23.760 -2.129  -9.394  0.60 16.18 ?  99  ASN   A H    1 
ATOM   2060 H H    B ASN   A 1 99  ? 23.845 -2.304  -9.401  0.40 16.39 ?  99  ASN   A H    1 
ATOM   2061 H HA   A ASN   A 1 99  ? 21.304 -1.314  -8.557  0.60 17.32 ?  99  ASN   A HA   1 
ATOM   2062 H HA   B ASN   A 1 99  ? 21.368 -1.504  -8.664  0.40 17.48 ?  99  ASN   A HA   1 
ATOM   2063 H HB2  A ASN   A 1 99  ? 23.115 0.156   -8.084  0.60 17.18 ?  99  ASN   A HB2  1 
ATOM   2064 H HB2  B ASN   A 1 99  ? 23.252 -0.009  -8.398  0.40 18.83 ?  99  ASN   A HB2  1 
ATOM   2065 H HB3  A ASN   A 1 99  ? 23.335 0.323   -9.648  0.60 17.18 ?  99  ASN   A HB3  1 
ATOM   2066 H HB3  B ASN   A 1 99  ? 23.275 0.106   -9.983  0.40 18.83 ?  99  ASN   A HB3  1 
ATOM   2067 H HD21 A ASN   A 1 99  ? 21.412 3.022   -8.162  0.60 17.73 ?  99  ASN   A HD21 1 
ATOM   2068 H HD21 B ASN   A 1 99  ? 21.374 2.718   -8.222  0.40 21.14 ?  99  ASN   A HD21 1 
ATOM   2069 H HD22 A ASN   A 1 99  ? 22.659 2.347   -7.706  0.60 17.73 ?  99  ASN   A HD22 1 
ATOM   2070 H HD22 B ASN   A 1 99  ? 22.647 2.056   -7.822  0.40 21.14 ?  99  ASN   A HD22 1 
ATOM   2071 N N    A VAL   A 1 100 ? 20.283 -1.924  -10.712 0.60 16.76 ?  100 VAL   A N    1 
ATOM   2072 N N    B VAL   A 1 100 ? 20.178 -1.863  -10.770 0.40 15.68 ?  100 VAL   A N    1 
ATOM   2073 C CA   A VAL   A 1 100 ? 19.629 -2.150  -11.999 0.60 19.31 ?  100 VAL   A CA   1 
ATOM   2074 C CA   B VAL   A 1 100 ? 19.519 -2.047  -12.057 0.40 17.46 ?  100 VAL   A CA   1 
ATOM   2075 C C    A VAL   A 1 100 ? 19.543 -0.868  -12.812 0.60 20.51 ?  100 VAL   A C    1 
ATOM   2076 C C    B VAL   A 1 100 ? 19.376 -0.715  -12.784 0.40 17.45 ?  100 VAL   A C    1 
ATOM   2077 O O    A VAL   A 1 100 ? 19.655 -0.898  -14.043 0.60 21.63 ?  100 VAL   A O    1 
ATOM   2078 O O    B VAL   A 1 100 ? 19.383 -0.672  -14.019 0.40 18.04 ?  100 VAL   A O    1 
ATOM   2079 C CB   A VAL   A 1 100 ? 18.244 -2.800  -11.777 0.60 20.72 ?  100 VAL   A CB   1 
ATOM   2080 C CB   B VAL   A 1 100 ? 18.166 -2.760  -11.875 0.40 19.32 ?  100 VAL   A CB   1 
ATOM   2081 C CG1  A VAL   A 1 100 ? 17.463 -2.891  -13.082 0.60 21.45 ?  100 VAL   A CG1  1 
ATOM   2082 C CG1  B VAL   A 1 100 ? 17.543 -3.079  -13.227 0.40 20.39 ?  100 VAL   A CG1  1 
ATOM   2083 C CG2  A VAL   A 1 100 ? 18.411 -4.177  -11.157 0.60 21.30 ?  100 VAL   A CG2  1 
ATOM   2084 C CG2  B VAL   A 1 100 ? 18.343 -4.028  -11.055 0.40 20.08 ?  100 VAL   A CG2  1 
ATOM   2085 H H    A VAL   A 1 100 ? 19.829 -2.217  -10.039 0.60 20.09 ?  100 VAL   A H    1 
ATOM   2086 H H    B VAL   A 1 100 ? 19.654 -1.901  -10.084 0.40 18.80 ?  100 VAL   A H    1 
ATOM   2087 H HA   A VAL   A 1 100 ? 20.162 -2.775  -12.509 0.60 23.16 ?  100 VAL   A HA   1 
ATOM   2088 H HA   B VAL   A 1 100 ? 20.077 -2.621  -12.602 0.40 20.94 ?  100 VAL   A HA   1 
ATOM   2089 H HB   A VAL   A 1 100 ? 17.734 -2.253  -11.161 0.60 24.85 ?  100 VAL   A HB   1 
ATOM   2090 H HB   B VAL   A 1 100 ? 17.559 -2.174  -11.396 0.40 23.17 ?  100 VAL   A HB   1 
ATOM   2091 H HG11 A VAL   A 1 100 ? 16.712 -3.493  -12.957 0.60 25.73 ?  100 VAL   A HG11 1 
ATOM   2092 H HG11 B VAL   A 1 100 ? 16.750 -3.619  -13.089 0.40 24.46 ?  100 VAL   A HG11 1 
ATOM   2093 H HG12 A VAL   A 1 100 ? 17.142 -2.009  -13.325 0.60 25.73 ?  100 VAL   A HG12 1 
ATOM   2094 H HG12 B VAL   A 1 100 ? 17.307 -2.251  -13.673 0.40 24.46 ?  100 VAL   A HG12 1 
ATOM   2095 H HG13 A VAL   A 1 100 ? 18.047 -3.236  -13.777 0.60 25.73 ?  100 VAL   A HG13 1 
ATOM   2096 H HG13 B VAL   A 1 100 ? 18.187 -3.571  -13.762 0.40 24.46 ?  100 VAL   A HG13 1 
ATOM   2097 H HG21 A VAL   A 1 100 ? 17.538 -4.589  -11.065 0.60 25.55 ?  100 VAL   A HG21 1 
ATOM   2098 H HG21 B VAL   A 1 100 ? 17.513 -4.530  -11.067 0.40 24.08 ?  100 VAL   A HG21 1 
ATOM   2099 H HG22 A VAL   A 1 100 ? 18.974 -4.717  -11.733 0.60 25.55 ?  100 VAL   A HG22 1 
ATOM   2100 H HG22 B VAL   A 1 100 ? 19.056 -4.558  -11.445 0.40 24.08 ?  100 VAL   A HG22 1 
ATOM   2101 H HG23 A VAL   A 1 100 ? 18.825 -4.083  -10.284 0.60 25.55 ?  100 VAL   A HG23 1 
ATOM   2102 H HG23 B VAL   A 1 100 ? 18.570 -3.787  -10.143 0.40 24.08 ?  100 VAL   A HG23 1 
ATOM   2103 N N    A ASN   A 1 101 ? 19.351 0.274   -12.152 0.60 21.89 ?  101 ASN   A N    1 
ATOM   2104 N N    B ASN   A 1 101 ? 19.246 0.387   -12.047 0.40 18.23 ?  101 ASN   A N    1 
ATOM   2105 C CA   A ASN   A 1 101 ? 19.324 1.545   -12.870 0.60 23.61 ?  101 ASN   A CA   1 
ATOM   2106 C CA   B ASN   A 1 101 ? 19.146 1.693   -12.686 0.40 19.49 ?  101 ASN   A CA   1 
ATOM   2107 C C    A ASN   A 1 101 ? 20.690 1.938   -13.432 0.60 24.86 ?  101 ASN   A C    1 
ATOM   2108 C C    B ASN   A 1 101 ? 20.482 2.189   -13.228 0.40 21.09 ?  101 ASN   A C    1 
ATOM   2109 O O    A ASN   A 1 101 ? 20.781 2.956   -14.130 0.60 26.40 ?  101 ASN   A O    1 
ATOM   2110 O O    B ASN   A 1 101 ? 20.497 3.184   -13.962 0.40 22.47 ?  101 ASN   A O    1 
ATOM   2111 C CB   A ASN   A 1 101 ? 18.727 2.631   -11.970 0.60 23.75 ?  101 ASN   A CB   1 
ATOM   2112 C CB   B ASN   A 1 101 ? 18.521 2.695   -11.717 0.40 19.47 ?  101 ASN   A CB   1 
ATOM   2113 C CG   A ASN   A 1 101 ? 17.363 2.239   -11.429 0.60 23.33 ?  101 ASN   A CG   1 
ATOM   2114 C CG   B ASN   A 1 101 ? 17.139 2.259   -11.249 0.40 19.23 ?  101 ASN   A CG   1 
ATOM   2115 O OD1  A ASN   A 1 101 ? 16.487 1.806   -12.182 0.60 23.70 ?  101 ASN   A OD1  1 
ATOM   2116 O OD1  B ASN   A 1 101 ? 16.392 1.615   -11.992 0.40 19.45 ?  101 ASN   A OD1  1 
ATOM   2117 N ND2  A ASN   A 1 101 ? 17.182 2.365   -10.119 0.60 23.00 ?  101 ASN   A ND2  1 
ATOM   2118 N ND2  B ASN   A 1 101 ? 16.801 2.588   -10.012 0.40 19.11 ?  101 ASN   A ND2  1 
ATOM   2119 H H    A ASN   A 1 101 ? 19.230 0.339   -11.303 0.60 26.25 ?  101 ASN   A H    1 
ATOM   2120 H H    B ASN   A 1 101 ? 19.204 0.401   -11.189 0.40 21.86 ?  101 ASN   A H    1 
ATOM   2121 H HA   A ASN   A 1 101 ? 18.736 1.454   -13.628 0.60 28.32 ?  101 ASN   A HA   1 
ATOM   2122 H HA   B ASN   A 1 101 ? 18.547 1.610   -13.441 0.40 23.37 ?  101 ASN   A HA   1 
ATOM   2123 H HB2  A ASN   A 1 101 ? 19.313 2.789   -11.216 0.60 28.49 ?  101 ASN   A HB2  1 
ATOM   2124 H HB2  B ASN   A 1 101 ? 19.093 2.786   -10.939 0.40 23.36 ?  101 ASN   A HB2  1 
ATOM   2125 H HB3  A ASN   A 1 101 ? 18.616 3.448   -12.484 0.60 28.49 ?  101 ASN   A HB3  1 
ATOM   2126 H HB3  B ASN   A 1 101 ? 18.439 3.556   -12.167 0.40 23.36 ?  101 ASN   A HB3  1 
ATOM   2127 H HD21 A ASN   A 1 101 ? 16.427 2.149   -9.766  0.60 27.59 ?  101 ASN   A HD21 1 
ATOM   2128 H HD21 B ASN   A 1 101 ? 16.029 2.367   -9.709  0.40 22.91 ?  101 ASN   A HD21 1 
ATOM   2129 H HD22 A ASN   A 1 101 ? 17.816 2.669   -9.627  0.60 27.59 ?  101 ASN   A HD22 1 
ATOM   2130 H HD22 B ASN   A 1 101 ? 17.349 3.031   -9.519  0.40 22.91 ?  101 ASN   A HD22 1 
ATOM   2131 N N    A LYS   A 1 102 ? 21.737 1.151   -13.166 0.60 26.27 ?  102 LYS   A N    1 
ATOM   2132 N N    B LYS   A 1 102 ? 21.590 1.523   -12.892 0.40 22.05 ?  102 LYS   A N    1 
ATOM   2133 C CA   A LYS   A 1 102 ? 23.033 1.292   -13.822 0.60 27.17 ?  102 LYS   A CA   1 
ATOM   2134 C CA   B LYS   A 1 102 ? 22.882 1.762   -13.523 0.40 22.99 ?  102 LYS   A CA   1 
ATOM   2135 C C    A LYS   A 1 102 ? 23.319 0.148   -14.791 0.60 27.10 ?  102 LYS   A C    1 
ATOM   2136 C C    B LYS   A 1 102 ? 23.205 0.744   -14.610 0.40 23.22 ?  102 LYS   A C    1 
ATOM   2137 O O    A LYS   A 1 102 ? 24.431 0.063   -15.320 0.60 27.35 ?  102 LYS   A O    1 
ATOM   2138 O O    B LYS   A 1 102 ? 24.222 0.895   -15.295 0.40 23.19 ?  102 LYS   A O    1 
ATOM   2139 C CB   A LYS   A 1 102 ? 24.162 1.349   -12.788 0.60 28.28 ?  102 LYS   A CB   1 
ATOM   2140 C CB   B LYS   A 1 102 ? 24.004 1.773   -12.474 0.40 23.74 ?  102 LYS   A CB   1 
ATOM   2141 C CG   A LYS   A 1 102 ? 24.072 2.486   -11.788 0.60 29.22 ?  102 LYS   A CG   1 
ATOM   2142 C CG   B LYS   A 1 102 ? 23.927 2.924   -11.483 0.40 24.52 ?  102 LYS   A CG   1 
ATOM   2143 C CD   A LYS   A 1 102 ? 25.243 2.446   -10.812 0.60 30.36 ?  102 LYS   A CD   1 
ATOM   2144 C CD   B LYS   A 1 102 ? 25.047 2.846   -10.454 0.40 25.25 ?  102 LYS   A CD   1 
ATOM   2145 C CE   A LYS   A 1 102 ? 25.165 3.573   -9.793  0.60 31.43 ?  102 LYS   A CE   1 
ATOM   2146 C CE   B LYS   A 1 102 ? 24.953 3.981   -9.442  0.40 25.93 ?  102 LYS   A CE   1 
ATOM   2147 N NZ   A LYS   A 1 102 ? 26.289 3.520   -8.813  0.60 31.91 ?  102 LYS   A NZ   1 
ATOM   2148 N NZ   B LYS   A 1 102 ? 25.965 3.863   -8.353  0.40 26.19 ?  102 LYS   A NZ   1 
ATOM   2149 H H    A LYS   A 1 102 ? 21.716 0.511   -12.591 0.60 31.52 ?  102 LYS   A H    1 
ATOM   2150 H H    B LYS   A 1 102 ? 21.618 0.914   -12.282 0.40 26.45 ?  102 LYS   A H    1 
ATOM   2151 H HA   A LYS   A 1 102 ? 23.038 2.130   -14.317 0.60 32.59 ?  102 LYS   A HA   1 
ATOM   2152 H HA   B LYS   A 1 102 ? 22.871 2.625   -13.949 0.40 27.58 ?  102 LYS   A HA   1 
ATOM   2153 H HB2  A LYS   A 1 102 ? 24.164 0.518   -12.287 0.60 33.92 ?  102 LYS   A HB2  1 
ATOM   2154 H HB2  B LYS   A 1 102 ? 23.969 0.947   -11.966 0.40 28.48 ?  102 LYS   A HB2  1 
ATOM   2155 H HB3  A LYS   A 1 102 ? 25.006 1.443   -13.261 0.60 33.92 ?  102 LYS   A HB3  1 
ATOM   2156 H HB3  B LYS   A 1 102 ? 24.858 1.839   -12.930 0.40 28.48 ?  102 LYS   A HB3  1 
ATOM   2157 H HG2  A LYS   A 1 102 ? 24.097 3.332   -12.260 0.60 35.05 ?  102 LYS   A HG2  1 
ATOM   2158 H HG2  B LYS   A 1 102 ? 24.011 3.764   -11.961 0.40 29.41 ?  102 LYS   A HG2  1 
ATOM   2159 H HG3  A LYS   A 1 102 ? 23.250 2.403   -11.282 0.60 35.05 ?  102 LYS   A HG3  1 
ATOM   2160 H HG3  B LYS   A 1 102 ? 23.079 2.887   -11.014 0.40 29.41 ?  102 LYS   A HG3  1 
ATOM   2161 H HD2  A LYS   A 1 102 ? 25.232 1.602   -10.333 0.60 36.42 ?  102 LYS   A HD2  1 
ATOM   2162 H HD2  B LYS   A 1 102 ? 24.985 2.004   -9.975  0.40 30.28 ?  102 LYS   A HD2  1 
ATOM   2163 H HD3  A LYS   A 1 102 ? 26.074 2.539   -11.305 0.60 36.42 ?  102 LYS   A HD3  1 
ATOM   2164 H HD3  B LYS   A 1 102 ? 25.904 2.911   -10.906 0.40 30.28 ?  102 LYS   A HD3  1 
ATOM   2165 H HE2  A LYS   A 1 102 ? 25.206 4.424   -10.257 0.60 37.71 ?  102 LYS   A HE2  1 
ATOM   2166 H HE2  B LYS   A 1 102 ? 25.098 4.824   -9.899  0.40 31.10 ?  102 LYS   A HE2  1 
ATOM   2167 H HE3  A LYS   A 1 102 ? 24.331 3.501   -9.303  0.60 37.71 ?  102 LYS   A HE3  1 
ATOM   2168 H HE3  B LYS   A 1 102 ? 24.071 3.969   -9.038  0.40 31.10 ?  102 LYS   A HE3  1 
ATOM   2169 H HZ1  A LYS   A 1 102 ? 26.217 4.190   -8.231  0.60 38.28 ?  102 LYS   A HZ1  1 
ATOM   2170 H HZ1  B LYS   A 1 102 ? 25.877 4.542   -7.784  0.40 31.41 ?  102 LYS   A HZ1  1 
ATOM   2171 H HZ2  A LYS   A 1 102 ? 26.270 2.748   -8.370  0.60 38.28 ?  102 LYS   A HZ2  1 
ATOM   2172 H HZ2  B LYS   A 1 102 ? 25.849 3.099   -7.912  0.40 31.41 ?  102 LYS   A HZ2  1 
ATOM   2173 H HZ3  A LYS   A 1 102 ? 27.067 3.590   -9.239  0.60 38.28 ?  102 LYS   A HZ3  1 
ATOM   2174 H HZ3  B LYS   A 1 102 ? 26.785 3.877   -8.697  0.40 31.41 ?  102 LYS   A HZ3  1 
ATOM   2175 N N    A GLY   A 1 103 ? 22.365 -0.754  -15.006 0.60 27.31 ?  103 GLY   A N    1 
ATOM   2176 N N    B GLY   A 1 103 ? 22.367 -0.273  -14.791 0.40 23.95 ?  103 GLY   A N    1 
ATOM   2177 C CA   A GLY   A 1 103 ? 22.586 -1.867  -15.910 0.60 26.96 ?  103 GLY   A CA   1 
ATOM   2178 C CA   B GLY   A 1 103 ? 22.615 -1.288  -15.798 0.40 24.66 ?  103 GLY   A CA   1 
ATOM   2179 C C    A GLY   A 1 103 ? 23.401 -3.007  -15.342 0.60 26.39 ?  103 GLY   A C    1 
ATOM   2180 C C    B GLY   A 1 103 ? 23.573 -2.380  -15.376 0.40 25.37 ?  103 GLY   A C    1 
ATOM   2181 O O    A GLY   A 1 103 ? 23.876 -3.853  -16.106 0.60 26.80 ?  103 GLY   A O    1 
ATOM   2182 O O    B GLY   A 1 103 ? 24.345 -2.873  -16.206 0.40 25.62 ?  103 GLY   A O    1 
ATOM   2183 H H    A GLY   A 1 103 ? 21.589 -0.747  -14.639 0.60 32.76 ?  103 GLY   A H    1 
ATOM   2184 H H    B GLY   A 1 103 ? 21.640 -0.399  -14.348 0.40 28.73 ?  103 GLY   A H    1 
ATOM   2185 H HA2  A GLY   A 1 103 ? 21.731 -2.226  -16.182 0.60 32.34 ?  103 GLY   A HA2  1 
ATOM   2186 H HA2  B GLY   A 1 103 ? 21.770 -1.695  -16.058 0.40 29.58 ?  103 GLY   A HA2  1 
ATOM   2187 H HA3  A GLY   A 1 103 ? 23.038 -1.533  -16.706 0.60 32.34 ?  103 GLY   A HA3  1 
ATOM   2188 H HA3  B GLY   A 1 103 ? 22.997 -0.868  -16.582 0.40 29.58 ?  103 GLY   A HA3  1 
ATOM   2189 N N    A GLU   A 1 104 ? 23.565 -3.069  -14.025 0.60 24.87 ?  104 GLU   A N    1 
ATOM   2190 N N    B GLU   A 1 104 ? 23.544 -2.781  -14.108 0.40 25.22 ?  104 GLU   A N    1 
ATOM   2191 C CA   A GLU   A 1 104 ? 24.447 -4.053  -13.413 0.60 23.35 ?  104 GLU   A CA   1 
ATOM   2192 C CA   B GLU   A 1 104 ? 24.472 -3.771  -13.580 0.40 25.13 ?  104 GLU   A CA   1 
ATOM   2193 C C    A GLU   A 1 104 ? 23.761 -5.412  -13.288 0.60 23.68 ?  104 GLU   A C    1 
ATOM   2194 C C    B GLU   A 1 104 ? 23.825 -5.153  -13.504 0.40 25.54 ?  104 GLU   A C    1 
ATOM   2195 O O    A GLU   A 1 104 ? 22.551 -5.510  -13.056 0.60 24.05 ?  104 GLU   A O    1 
ATOM   2196 O O    B GLU   A 1 104 ? 22.599 -5.296  -13.492 0.40 25.65 ?  104 GLU   A O    1 
ATOM   2197 C CB   A GLU   A 1 104 ? 24.940 -3.537  -12.058 0.60 21.36 ?  104 GLU   A CB   1 
ATOM   2198 C CB   B GLU   A 1 104 ? 24.989 -3.333  -12.207 0.40 24.35 ?  104 GLU   A CB   1 
ATOM   2199 C CG   A GLU   A 1 104 ? 25.914 -2.364  -12.225 0.60 20.68 ?  104 GLU   A CG   1 
ATOM   2200 C CG   B GLU   A 1 104 ? 25.749 -2.009  -12.272 0.40 23.88 ?  104 GLU   A CG   1 
ATOM   2201 C CD   A GLU   A 1 104 ? 26.212 -1.571  -10.963 0.60 19.54 ?  104 GLU   A CD   1 
ATOM   2202 C CD   B GLU   A 1 104 ? 26.174 -1.470  -10.914 0.40 23.29 ?  104 GLU   A CD   1 
ATOM   2203 O OE1  A GLU   A 1 104 ? 25.653 -1.867  -9.889  0.60 18.27 ?  104 GLU   A OE1  1 
ATOM   2204 O OE1  B GLU   A 1 104 ? 25.473 -1.721  -9.912  0.40 22.19 ?  104 GLU   A OE1  1 
ATOM   2205 O OE2  A GLU   A 1 104 ? 27.018 -0.616  -11.071 0.60 20.10 -1 104 GLU   A OE2  1 
ATOM   2206 O OE2  B GLU   A 1 104 ? 27.218 -0.784  -10.855 0.40 24.01 -1 104 GLU   A OE2  1 
ATOM   2207 H H    A GLU   A 1 104 ? 23.174 -2.548  -13.466 0.60 29.83 ?  104 GLU   A H    1 
ATOM   2208 H H    B GLU   A 1 104 ? 22.990 -2.484  -13.521 0.40 30.25 ?  104 GLU   A H    1 
ATOM   2209 H HA   A GLU   A 1 104 ? 25.226 -4.163  -13.984 0.60 28.00 ?  104 GLU   A HA   1 
ATOM   2210 H HA   B GLU   A 1 104 ? 25.232 -3.833  -14.178 0.40 30.15 ?  104 GLU   A HA   1 
ATOM   2211 H HB2  A GLU   A 1 104 ? 24.181 -3.235  -11.538 0.60 25.62 ?  104 GLU   A HB2  1 
ATOM   2212 H HB2  B GLU   A 1 104 ? 24.235 -3.226  -11.607 0.40 29.21 ?  104 GLU   A HB2  1 
ATOM   2213 H HB3  A GLU   A 1 104 ? 25.401 -4.255  -11.596 0.60 25.62 ?  104 GLU   A HB3  1 
ATOM   2214 H HB3  B GLU   A 1 104 ? 25.591 -4.015  -11.868 0.40 29.21 ?  104 GLU   A HB3  1 
ATOM   2215 H HG2  A GLU   A 1 104 ? 26.751 -2.707  -12.569 0.60 24.80 ?  104 GLU   A HG2  1 
ATOM   2216 H HG2  B GLU   A 1 104 ? 26.552 -2.139  -12.800 0.40 28.65 ?  104 GLU   A HG2  1 
ATOM   2217 H HG3  A GLU   A 1 104 ? 25.532 -1.733  -12.849 0.60 24.80 ?  104 GLU   A HG3  1 
ATOM   2218 H HG3  B GLU   A 1 104 ? 25.181 -1.347  -12.698 0.40 28.65 ?  104 GLU   A HG3  1 
ATOM   2219 N N    A ASP   A 1 105 ? 24.560 -6.467  -13.441 0.60 24.40 ?  105 ASP   A N    1 
ATOM   2220 N N    B ASP   A 1 105 ? 24.679 -6.176  -13.444 0.40 26.54 ?  105 ASP   A N    1 
ATOM   2221 C CA   A ASP   A 1 105 ? 24.043 -7.826  -13.564 0.60 25.34 ?  105 ASP   A CA   1 
ATOM   2222 C CA   B ASP   A 1 105 ? 24.242 -7.561  -13.584 0.40 27.54 ?  105 ASP   A CA   1 
ATOM   2223 C C    A ASP   A 1 105 ? 23.354 -8.260  -12.274 0.60 22.75 ?  105 ASP   A C    1 
ATOM   2224 C C    B ASP   A 1 105 ? 23.499 -8.006  -12.328 0.40 26.75 ?  105 ASP   A C    1 
ATOM   2225 O O    A ASP   A 1 105 ? 23.993 -8.358  -11.223 0.60 20.09 ?  105 ASP   A O    1 
ATOM   2226 O O    B ASP   A 1 105 ? 24.083 -8.069  -11.242 0.40 26.21 ?  105 ASP   A O    1 
ATOM   2227 C CB   A ASP   A 1 105 ? 25.201 -8.767  -13.886 0.60 28.95 ?  105 ASP   A CB   1 
ATOM   2228 C CB   B ASP   A 1 105 ? 25.460 -8.449  -13.832 0.40 29.02 ?  105 ASP   A CB   1 
ATOM   2229 C CG   A ASP   A 1 105 ? 24.747 -10.195 -14.116 0.60 31.90 ?  105 ASP   A CG   1 
ATOM   2230 C CG   B ASP   A 1 105 ? 25.092 -9.885  -14.128 0.40 30.23 ?  105 ASP   A CG   1 
ATOM   2231 O OD1  A ASP   A 1 105 ? 23.522 -10.421 -14.197 0.60 32.40 ?  105 ASP   A OD1  1 
ATOM   2232 O OD1  B ASP   A 1 105 ? 23.885 -10.186 -14.237 0.40 30.30 ?  105 ASP   A OD1  1 
ATOM   2233 O OD2  A ASP   A 1 105 ? 25.616 -11.089 -14.212 0.60 33.70 -1 105 ASP   A OD2  1 
ATOM   2234 O OD2  B ASP   A 1 105 ? 26.021 -10.714 -14.253 0.40 31.01 -1 105 ASP   A OD2  1 
ATOM   2235 H H    A ASP   A 1 105 ? 25.420 -6.420  -13.480 0.60 29.27 ?  105 ASP   A H    1 
ATOM   2236 H H    B ASP   A 1 105 ? 25.526 -6.096  -13.310 0.40 31.84 ?  105 ASP   A H    1 
ATOM   2237 H HA   A ASP   A 1 105 ? 23.397 -7.866  -14.284 0.60 30.39 ?  105 ASP   A HA   1 
ATOM   2238 H HA   B ASP   A 1 105 ? 23.643 -7.645  -14.343 0.40 33.03 ?  105 ASP   A HA   1 
ATOM   2239 H HB2  A ASP   A 1 105 ? 25.648 -8.450  -14.691 0.60 34.73 ?  105 ASP   A HB2  1 
ATOM   2240 H HB2  B ASP   A 1 105 ? 25.954 -8.110  -14.596 0.40 34.81 ?  105 ASP   A HB2  1 
ATOM   2241 H HB3  A ASP   A 1 105 ? 25.827 -8.764  -13.143 0.60 34.73 ?  105 ASP   A HB3  1 
ATOM   2242 H HB3  B ASP   A 1 105 ? 26.024 -8.452  -13.046 0.40 34.81 ?  105 ASP   A HB3  1 
ATOM   2243 N N    A ILE   A 1 106 ? 22.054 -8.553  -12.363 0.60 22.85 ?  106 ILE   A N    1 
ATOM   2244 N N    B ILE   A 1 106 ? 22.211 -8.327  -12.481 0.40 26.53 ?  106 ILE   A N    1 
ATOM   2245 C CA   A ILE   A 1 106 ? 21.300 -8.986  -11.192 0.60 22.60 ?  106 ILE   A CA   1 
ATOM   2246 C CA   B ILE   A 1 106 ? 21.399 -8.725  -11.336 0.40 25.92 ?  106 ILE   A CA   1 
ATOM   2247 C C    A ILE   A 1 106 ? 21.852 -10.280 -10.621 0.60 21.94 ?  106 ILE   A C    1 
ATOM   2248 C C    B ILE   A 1 106 ? 21.859 -10.052 -10.740 0.40 24.91 ?  106 ILE   A C    1 
ATOM   2249 O O    A ILE   A 1 106 ? 21.676 -10.547 -9.428  0.60 21.20 ?  106 ILE   A O    1 
ATOM   2250 O O    B ILE   A 1 106 ? 21.573 -10.330 -9.570  0.40 24.10 ?  106 ILE   A O    1 
ATOM   2251 C CB   A ILE   A 1 106 ? 19.791 -9.091  -11.512 0.60 24.06 ?  106 ILE   A CB   1 
ATOM   2252 C CB   B ILE   A 1 106 ? 19.901 -8.736  -11.708 0.40 26.64 ?  106 ILE   A CB   1 
ATOM   2253 C CG1  A ILE   A 1 106 ? 18.968 -9.191  -10.225 0.60 24.66 ?  106 ILE   A CG1  1 
ATOM   2254 C CG1  B ILE   A 1 106 ? 19.028 -8.934  -10.464 0.40 26.99 ?  106 ILE   A CG1  1 
ATOM   2255 C CG2  A ILE   A 1 106 ? 19.507 -10.296 -12.392 0.60 24.79 ?  106 ILE   A CG2  1 
ATOM   2256 C CG2  B ILE   A 1 106 ? 19.609 -9.821  -12.735 0.40 26.96 ?  106 ILE   A CG2  1 
ATOM   2257 C CD1  A ILE   A 1 106 ? 19.065 -7.973  -9.338  0.60 25.02 ?  106 ILE   A CD1  1 
ATOM   2258 C CD1  B ILE   A 1 106 ? 19.277 -7.919  -9.369  0.40 27.20 ?  106 ILE   A CD1  1 
ATOM   2259 H H    A ILE   A 1 106 ? 21.596 -8.508  -13.083 0.60 27.40 ?  106 ILE   A H    1 
ATOM   2260 H H    B ILE   A 1 106 ? 21.791 -8.315  -13.229 0.40 31.83 ?  106 ILE   A H    1 
ATOM   2261 H HA   A ILE   A 1 106 ? 21.408 -8.322  -10.503 0.60 27.10 ?  106 ILE   A HA   1 
ATOM   2262 H HA   B ILE   A 1 106 ? 21.521 -8.056  -10.652 0.40 31.09 ?  106 ILE   A HA   1 
ATOM   2263 H HB   A ILE   A 1 106 ? 19.523 -8.291  -11.988 0.60 28.85 ?  106 ILE   A HB   1 
ATOM   2264 H HB   B ILE   A 1 106 ? 19.679 -7.879  -12.101 0.40 31.95 ?  106 ILE   A HB   1 
ATOM   2265 H HG12 A ILE   A 1 106 ? 18.035 -9.309  -10.461 0.60 29.58 ?  106 ILE   A HG12 1 
ATOM   2266 H HG12 B ILE   A 1 106 ? 18.094 -8.861  -10.724 0.40 32.38 ?  106 ILE   A HG12 1 
ATOM   2267 H HG13 A ILE   A 1 106 ? 19.275 -9.956  -9.714  0.60 29.58 ?  106 ILE   A HG13 1 
ATOM   2268 H HG13 B ILE   A 1 106 ? 19.195 -9.814  -10.096 0.40 32.38 ?  106 ILE   A HG13 1 
ATOM   2269 H HG21 A ILE   A 1 106 ? 18.614 -10.211 -12.759 0.60 29.73 ?  106 ILE   A HG21 1 
ATOM   2270 H HG21 B ILE   A 1 106 ? 18.687 -9.739  -13.026 0.40 32.34 ?  106 ILE   A HG21 1 
ATOM   2271 H HG22 A ILE   A 1 106 ? 20.161 -10.321 -13.105 0.60 29.73 ?  106 ILE   A HG22 1 
ATOM   2272 H HG22 B ILE   A 1 106 ? 20.206 -9.708  -13.490 0.40 32.34 ?  106 ILE   A HG22 1 
ATOM   2273 H HG23 A ILE   A 1 106 ? 19.569 -11.100 -11.854 0.60 29.73 ?  106 ILE   A HG23 1 
ATOM   2274 H HG23 B ILE   A 1 106 ? 19.750 -10.690 -12.328 0.40 32.34 ?  106 ILE   A HG23 1 
ATOM   2275 H HD11 A ILE   A 1 106 ? 18.345 -7.998  -8.690  0.60 30.01 ?  106 ILE   A HD11 1 
ATOM   2276 H HD11 B ILE   A 1 106 ? 18.538 -7.943  -8.744  0.40 32.63 ?  106 ILE   A HD11 1 
ATOM   2277 H HD12 A ILE   A 1 106 ? 19.921 -7.981  -8.880  0.60 30.01 ?  106 ILE   A HD12 1 
ATOM   2278 H HD12 B ILE   A 1 106 ? 20.104 -8.143  -8.913  0.40 32.63 ?  106 ILE   A HD12 1 
ATOM   2279 H HD13 A ILE   A 1 106 ? 18.989 -7.176  -9.886  0.60 30.01 ?  106 ILE   A HD13 1 
ATOM   2280 H HD13 B ILE   A 1 106 ? 19.345 -7.037  -9.767  0.40 32.63 ?  106 ILE   A HD13 1 
ATOM   2281 N N    A GLN   A 1 107 ? 22.525 -11.093 -11.444 0.60 23.02 ?  107 GLN   A N    1 
ATOM   2282 N N    B GLN   A 1 107 ? 22.573 -10.878 -11.511 0.40 25.22 ?  107 GLN   A N    1 
ATOM   2283 C CA   A GLN   A 1 107 ? 23.181 -12.291 -10.934 0.60 25.31 ?  107 GLN   A CA   1 
ATOM   2284 C CA   B GLN   A 1 107 ? 23.084 -12.141 -10.986 0.40 25.94 ?  107 GLN   A CA   1 
ATOM   2285 C C    A GLN   A 1 107 ? 24.163 -11.963 -9.821  0.60 23.17 ?  107 GLN   A C    1 
ATOM   2286 C C    B GLN   A 1 107 ? 24.092 -11.926 -9.865  0.40 23.18 ?  107 GLN   A C    1 
ATOM   2287 O O    A GLN   A 1 107 ? 24.431 -12.819 -8.970  0.60 24.53 ?  107 GLN   A O    1 
ATOM   2288 O O    B GLN   A 1 107 ? 24.318 -12.839 -9.063  0.40 24.21 ?  107 GLN   A O    1 
ATOM   2289 C CB   A GLN   A 1 107 ? 23.901 -13.029 -12.070 0.60 29.53 ?  107 GLN   A CB   1 
ATOM   2290 C CB   B GLN   A 1 107 ? 23.712 -12.962 -12.118 0.40 29.45 ?  107 GLN   A CB   1 
ATOM   2291 C CG   A GLN   A 1 107 ? 23.011 -13.357 -13.262 0.60 33.86 ?  107 GLN   A CG   1 
ATOM   2292 C CG   B GLN   A 1 107 ? 22.814 -13.140 -13.339 0.40 32.97 ?  107 GLN   A CG   1 
ATOM   2293 C CD   A GLN   A 1 107 ? 21.769 -14.130 -12.869 0.60 37.38 ?  107 GLN   A CD   1 
ATOM   2294 C CD   B GLN   A 1 107 ? 21.583 -13.977 -13.048 0.40 35.81 ?  107 GLN   A CD   1 
ATOM   2295 O OE1  A GLN   A 1 107 ? 21.848 -15.144 -12.175 0.60 38.78 ?  107 GLN   A OE1  1 
ATOM   2296 O OE1  B GLN   A 1 107 ? 21.687 -15.123 -12.612 0.40 36.96 ?  107 GLN   A OE1  1 
ATOM   2297 N NE2  A GLN   A 1 107 ? 20.611 -13.647 -13.305 0.60 38.59 ?  107 GLN   A NE2  1 
ATOM   2298 N NE2  B GLN   A 1 107 ? 20.409 -13.407 -13.289 0.40 36.73 ?  107 GLN   A NE2  1 
ATOM   2299 H H    A GLN   A 1 107 ? 22.614 -10.976 -12.291 0.60 27.61 ?  107 GLN   A H    1 
ATOM   2300 H H    B GLN   A 1 107 ? 22.774 -10.729 -12.332 0.40 30.25 ?  107 GLN   A H    1 
ATOM   2301 H HA   A GLN   A 1 107 ? 22.517 -12.892 -10.568 0.60 30.36 ?  107 GLN   A HA   1 
ATOM   2302 H HA   B GLN   A 1 107 ? 22.352 -12.655 -10.621 0.40 31.11 ?  107 GLN   A HA   1 
ATOM   2303 H HB2  A GLN   A 1 107 ? 24.632 -12.480 -12.393 0.60 35.43 ?  107 GLN   A HB2  1 
ATOM   2304 H HB2  B GLN   A 1 107 ? 24.524 -12.524 -12.415 0.40 35.33 ?  107 GLN   A HB2  1 
ATOM   2305 H HB3  A GLN   A 1 107 ? 24.252 -13.870 -11.731 0.60 35.43 ?  107 GLN   A HB3  1 
ATOM   2306 H HB3  B GLN   A 1 107 ? 23.924 -13.849 -11.783 0.40 35.33 ?  107 GLN   A HB3  1 
ATOM   2307 H HG2  A GLN   A 1 107 ? 22.726 -12.532 -13.684 0.60 40.62 ?  107 GLN   A HG2  1 
ATOM   2308 H HG2  B GLN   A 1 107 ? 22.518 -12.270 -13.650 0.40 39.55 ?  107 GLN   A HG2  1 
ATOM   2309 H HG3  A GLN   A 1 107 ? 23.513 -13.895 -13.895 0.60 40.62 ?  107 GLN   A HG3  1 
ATOM   2310 H HG3  B GLN   A 1 107 ? 23.319 -13.584 -14.038 0.40 39.55 ?  107 GLN   A HG3  1 
ATOM   2311 H HE21 A GLN   A 1 107 ? 20.595 -12.933 -13.785 0.60 46.29 ?  107 GLN   A HE21 1 
ATOM   2312 H HE21 B GLN   A 1 107 ? 20.375 -12.604 -13.592 0.40 44.06 ?  107 GLN   A HE21 1 
ATOM   2313 H HE22 A GLN   A 1 107 ? 19.877 -14.049 -13.107 0.60 46.29 ?  107 GLN   A HE22 1 
ATOM   2314 H HE22 B GLN   A 1 107 ? 19.682 -13.843 -13.141 0.40 44.06 ?  107 GLN   A HE22 1 
ATOM   2315 N N    . LEU   A 1 108 ? 24.686 -10.734 -9.783  1.00 19.49 ?  108 LEU   A N    1 
ATOM   2316 C CA   . LEU   A 1 108 ? 25.621 -10.382 -8.725  1.00 16.22 ?  108 LEU   A CA   1 
ATOM   2317 C C    . LEU   A 1 108 ? 24.937 -10.242 -7.373  1.00 14.30 ?  108 LEU   A C    1 
ATOM   2318 O O    . LEU   A 1 108 ? 25.630 -10.088 -6.364  1.00 14.60 ?  108 LEU   A O    1 
ATOM   2319 C CB   . LEU   A 1 108 ? 26.365 -9.089  -9.082  1.00 15.83 ?  108 LEU   A CB   1 
ATOM   2320 C CG   . LEU   A 1 108 ? 27.367 -9.269  -10.224 1.00 17.75 ?  108 LEU   A CG   1 
ATOM   2321 C CD1  . LEU   A 1 108 ? 27.844 -7.927  -10.758 1.00 18.44 ?  108 LEU   A CD1  1 
ATOM   2322 C CD2  . LEU   A 1 108 ? 28.552 -10.115 -9.772  1.00 19.97 ?  108 LEU   A CD2  1 
ATOM   2323 H H    A LEU   A 1 108 ? 24.517 -10.105 -10.341 0.60 23.37 ?  108 LEU   A H    1 
ATOM   2324 H H    B LEU   A 1 108 ? 24.550 -10.096 -10.339 0.40 23.37 ?  108 LEU   A H    1 
ATOM   2325 H HA   . LEU   A 1 108 ? 26.276 -11.087 -8.639  1.00 19.46 ?  108 LEU   A HA   1 
ATOM   2326 H HB2  . LEU   A 1 108 ? 25.716 -8.419  -9.357  1.00 18.99 ?  108 LEU   A HB2  1 
ATOM   2327 H HB3  . LEU   A 1 108 ? 26.848 -8.777  -8.303  1.00 18.99 ?  108 LEU   A HB3  1 
ATOM   2328 H HG   . LEU   A 1 108 ? 26.929 -9.742  -10.950 1.00 21.28 ?  108 LEU   A HG   1 
ATOM   2329 H HD11 . LEU   A 1 108 ? 28.439 -8.080  -11.509 1.00 22.11 ?  108 LEU   A HD11 1 
ATOM   2330 H HD12 . LEU   A 1 108 ? 27.075 -7.410  -11.045 1.00 22.11 ?  108 LEU   A HD12 1 
ATOM   2331 H HD13 . LEU   A 1 108 ? 28.315 -7.456  -10.053 1.00 22.11 ?  108 LEU   A HD13 1 
ATOM   2332 H HD21 . LEU   A 1 108 ? 29.245 -10.066 -10.445 1.00 23.95 ?  108 LEU   A HD21 1 
ATOM   2333 H HD22 . LEU   A 1 108 ? 28.880 -9.766  -8.928  1.00 23.95 ?  108 LEU   A HD22 1 
ATOM   2334 H HD23 . LEU   A 1 108 ? 28.261 -11.033 -9.659  1.00 23.95 ?  108 LEU   A HD23 1 
ATOM   2335 N N    . LEU   A 1 109 ? 23.604 -10.297 -7.323  1.00 13.70 ?  109 LEU   A N    1 
ATOM   2336 C CA   . LEU   A 1 109 ? 22.919 -10.174 -6.044  1.00 12.54 ?  109 LEU   A CA   1 
ATOM   2337 C C    . LEU   A 1 109 ? 23.283 -11.319 -5.104  1.00 11.70 ?  109 LEU   A C    1 
ATOM   2338 O O    . LEU   A 1 109 ? 23.432 -11.112 -3.895  1.00 12.32 ?  109 LEU   A O    1 
ATOM   2339 C CB   . LEU   A 1 109 ? 21.410 -10.103 -6.282  1.00 13.47 ?  109 LEU   A CB   1 
ATOM   2340 C CG   . LEU   A 1 109 ? 20.533 -9.799  -5.070  1.00 13.66 ?  109 LEU   A CG   1 
ATOM   2341 C CD1  . LEU   A 1 109 ? 20.982 -8.517  -4.380  1.00 14.12 ?  109 LEU   A CD1  1 
ATOM   2342 C CD2  . LEU   A 1 109 ? 19.062 -9.692  -5.485  1.00 14.93 ?  109 LEU   A CD2  1 
ATOM   2343 H H    . LEU   A 1 109 ? 23.082 -10.409 -7.997  1.00 16.43 ?  109 LEU   A H    1 
ATOM   2344 H HA   . LEU   A 1 109 ? 23.194 -9.347  -5.621  1.00 15.04 ?  109 LEU   A HA   1 
ATOM   2345 H HB2  . LEU   A 1 109 ? 21.239 -9.407  -6.935  1.00 16.16 ?  109 LEU   A HB2  1 
ATOM   2346 H HB3  . LEU   A 1 109 ? 21.116 -10.954 -6.637  1.00 16.16 ?  109 LEU   A HB3  1 
ATOM   2347 H HG   . LEU   A 1 109 ? 20.604 -10.524 -4.432  1.00 16.37 ?  109 LEU   A HG   1 
ATOM   2348 H HD11 . LEU   A 1 109 ? 20.308 -8.242  -3.741  1.00 16.93 ?  109 LEU   A HD11 1 
ATOM   2349 H HD12 . LEU   A 1 109 ? 21.823 -8.681  -3.926  1.00 16.93 ?  109 LEU   A HD12 1 
ATOM   2350 H HD13 . LEU   A 1 109 ? 21.100 -7.822  -5.052  1.00 16.93 ?  109 LEU   A HD13 1 
ATOM   2351 H HD21 . LEU   A 1 109 ? 18.539 -9.370  -4.730  1.00 17.90 ?  109 LEU   A HD21 1 
ATOM   2352 H HD22 . LEU   A 1 109 ? 18.981 -9.077  -6.226  1.00 17.90 ?  109 LEU   A HD22 1 
ATOM   2353 H HD23 . LEU   A 1 109 ? 18.741 -10.573 -5.750  1.00 17.90 ?  109 LEU   A HD23 1 
ATOM   2354 N N    . LYS   A 1 110 ? 23.425 -12.539 -5.635  1.00 12.01 ?  110 LYS   A N    1 
ATOM   2355 C CA   . LYS   A 1 110 ? 23.806 -13.655 -4.774  1.00 12.21 ?  110 LYS   A CA   1 
ATOM   2356 C C    . LYS   A 1 110 ? 25.189 -13.432 -4.175  1.00 11.74 ?  110 LYS   A C    1 
ATOM   2357 O O    . LYS   A 1 110 ? 25.390 -13.625 -2.973  1.00 11.91 ?  110 LYS   A O    1 
ATOM   2358 C CB   . LYS   A 1 110 ? 23.709 -14.983 -5.532  1.00 13.35 ?  110 LYS   A CB   1 
ATOM   2359 C CG   . LYS   A 1 110 ? 23.934 -16.188 -4.627  1.00 13.30 ?  110 LYS   A CG   1 
ATOM   2360 C CD   . LYS   A 1 110 ? 23.696 -17.512 -5.339  1.00 14.29 ?  110 LYS   A CD   1 
ATOM   2361 C CE   . LYS   A 1 110 ? 23.812 -18.693 -4.389  1.00 14.70 ?  110 LYS   A CE   1 
ATOM   2362 N NZ   . LYS   A 1 110 ? 22.635 -18.830 -3.508  1.00 15.14 ?  110 LYS   A NZ   1 
ATOM   2363 H H    . LYS   A 1 110 ? 23.311 -12.740 -6.461  1.00 14.40 ?  110 LYS   A H    1 
ATOM   2364 H HA   . LYS   A 1 110 ? 23.171 -13.700 -4.036  1.00 14.64 ?  110 LYS   A HA   1 
ATOM   2365 H HB2  . LYS   A 1 110 ? 22.821 -15.063 -5.919  1.00 16.01 ?  110 LYS   A HB2  1 
ATOM   2366 H HB3  . LYS   A 1 110 ? 24.380 -15.000 -6.227  1.00 16.01 ?  110 LYS   A HB3  1 
ATOM   2367 H HG2  . LYS   A 1 110 ? 24.850 -16.180 -4.307  1.00 15.95 ?  110 LYS   A HG2  1 
ATOM   2368 H HG3  . LYS   A 1 110 ? 23.322 -16.140 -3.873  1.00 15.95 ?  110 LYS   A HG3  1 
ATOM   2369 H HD2  . LYS   A 1 110 ? 22.804 -17.520 -5.717  1.00 17.14 ?  110 LYS   A HD2  1 
ATOM   2370 H HD3  . LYS   A 1 110 ? 24.359 -17.624 -6.038  1.00 17.14 ?  110 LYS   A HD3  1 
ATOM   2371 H HE2  . LYS   A 1 110 ? 23.903 -19.511 -4.901  1.00 17.63 ?  110 LYS   A HE2  1 
ATOM   2372 H HE3  . LYS   A 1 110 ? 24.595 -18.570 -3.822  1.00 17.63 ?  110 LYS   A HE3  1 
ATOM   2373 H HZ1  . LYS   A 1 110 ? 22.734 -19.527 -2.967  1.00 18.16 ?  110 LYS   A HZ1  1 
ATOM   2374 H HZ2  . LYS   A 1 110 ? 22.531 -18.093 -3.020  1.00 18.16 ?  110 LYS   A HZ2  1 
ATOM   2375 H HZ3  . LYS   A 1 110 ? 21.901 -18.951 -4.003  1.00 18.16 ?  110 LYS   A HZ3  1 
ATOM   2376 N N    . SER   A 1 111 ? 26.148 -12.994 -4.993  1.00 11.92 ?  111 SER   A N    1 
ATOM   2377 C CA   . SER   A 1 111 ? 27.480 -12.683 -4.480  1.00 11.97 ?  111 SER   A CA   1 
ATOM   2378 C C    . SER   A 1 111 ? 27.416 -11.638 -3.372  1.00 11.63 ?  111 SER   A C    1 
ATOM   2379 O O    . SER   A 1 111 ? 28.118 -11.745 -2.361  1.00 12.19 ?  111 SER   A O    1 
ATOM   2380 C CB   . SER   A 1 111 ? 28.375 -12.197 -5.618  1.00 13.18 ?  111 SER   A CB   1 
ATOM   2381 O OG   . SER   A 1 111 ? 28.491 -13.189 -6.623  1.00 15.57 ?  111 SER   A OG   1 
ATOM   2382 H H    . SER   A 1 111 ? 26.045 -12.867 -5.834  1.00 14.30 ?  111 SER   A H    1 
ATOM   2383 H HA   . SER   A 1 111 ? 27.870 -13.491 -4.109  1.00 14.35 ?  111 SER   A HA   1 
ATOM   2384 H HB2  . SER   A 1 111 ? 27.975 -11.406 -6.012  1.00 15.80 ?  111 SER   A HB2  1 
ATOM   2385 H HB3  . SER   A 1 111 ? 29.248 -11.984 -5.258  1.00 15.80 ?  111 SER   A HB3  1 
ATOM   2386 H HG   . SER   A 1 111 ? 29.007 -12.909 -7.234  1.00 18.67 ?  111 SER   A HG   1 
ATOM   2387 N N    . ALA   A 1 112 ? 26.575 -10.614 -3.550  1.00 11.69 ?  112 ALA   A N    1 
ATOM   2388 C CA   . ALA   A 1 112 ? 26.427 -9.576  -2.533  1.00 11.28 ?  112 ALA   A CA   1 
ATOM   2389 C C    . ALA   A 1 112 ? 25.953 -10.174 -1.210  1.00 11.23 ?  112 ALA   A C    1 
ATOM   2390 O O    . ALA   A 1 112 ? 26.509 -9.882  -0.144  1.00 11.74 ?  112 ALA   A O    1 
ATOM   2391 C CB   . ALA   A 1 112 ? 25.461 -8.494  -3.027  1.00 11.54 ?  112 ALA   A CB   1 
ATOM   2392 H H    . ALA   A 1 112 ? 26.087 -10.496 -4.248  1.00 14.01 ?  112 ALA   A H    1 
ATOM   2393 H HA   . ALA   A 1 112 ? 27.285 -9.154  -2.378  1.00 13.52 ?  112 ALA   A HA   1 
ATOM   2394 H HB1  . ALA   A 1 112 ? 25.395 -7.792  -2.354  1.00 13.84 ?  112 ALA   A HB1  1 
ATOM   2395 H HB2  . ALA   A 1 112 ? 25.797 -8.119  -3.856  1.00 13.84 ?  112 ALA   A HB2  1 
ATOM   2396 H HB3  . ALA   A 1 112 ? 24.585 -8.887  -3.174  1.00 13.84 ?  112 ALA   A HB3  1 
ATOM   2397 N N    . TYR   A 1 113 ? 24.925 -11.030 -1.259  1.00 11.56 ?  113 TYR   A N    1 
ATOM   2398 C CA   . TYR   A 1 113 ? 24.418 -11.640 -0.031  1.00 11.45 ?  113 TYR   A CA   1 
ATOM   2399 C C    . TYR   A 1 113 ? 25.428 -12.587 0.617   1.00 10.75 ?  113 TYR   A C    1 
ATOM   2400 O O    . TYR   A 1 113 ? 25.394 -12.764 1.839   1.00 11.61 ?  113 TYR   A O    1 
ATOM   2401 C CB   . TYR   A 1 113 ? 23.102 -12.372 -0.298  1.00 11.97 ?  113 TYR   A CB   1 
ATOM   2402 C CG   . TYR   A 1 113 ? 21.880 -11.483 -0.203  1.00 11.70 ?  113 TYR   A CG   1 
ATOM   2403 C CD1  . TYR   A 1 113 ? 21.522 -10.894 1.002   1.00 11.84 ?  113 TYR   A CD1  1 
ATOM   2404 C CD2  . TYR   A 1 113 ? 21.077 -11.244 -1.311  1.00 12.09 ?  113 TYR   A CD2  1 
ATOM   2405 C CE1  . TYR   A 1 113 ? 20.397 -10.103 1.105   1.00 12.06 ?  113 TYR   A CE1  1 
ATOM   2406 C CE2  . TYR   A 1 113 ? 19.930 -10.441 -1.215  1.00 12.11 ?  113 TYR   A CE2  1 
ATOM   2407 C CZ   . TYR   A 1 113 ? 19.608 -9.876  -0.003  1.00 11.93 ?  113 TYR   A CZ   1 
ATOM   2408 O OH   . TYR   A 1 113 ? 18.481 -9.086  0.132   1.00 12.90 ?  113 TYR   A OH   1 
ATOM   2409 H H    . TYR   A 1 113 ? 24.513 -11.265 -1.976  1.00 13.86 ?  113 TYR   A H    1 
ATOM   2410 H HA   . TYR   A 1 113 ? 24.238 -10.936 0.608   1.00 13.73 ?  113 TYR   A HA   1 
ATOM   2411 H HB2  . TYR   A 1 113 ? 23.122 -12.743 -1.193  1.00 14.35 ?  113 TYR   A HB2  1 
ATOM   2412 H HB3  . TYR   A 1 113 ? 22.997 -13.081 0.353   1.00 14.35 ?  113 TYR   A HB3  1 
ATOM   2413 H HD1  . TYR   A 1 113 ? 22.052 -11.044 1.755   1.00 14.19 ?  113 TYR   A HD1  1 
ATOM   2414 H HD2  . TYR   A 1 113 ? 21.292 -11.637 -2.124  1.00 14.49 ?  113 TYR   A HD2  1 
ATOM   2415 H HE1  . TYR   A 1 113 ? 20.181 -9.717  1.920   1.00 14.46 ?  113 TYR   A HE1  1 
ATOM   2416 H HE2  . TYR   A 1 113 ? 19.392 -10.291 -1.960  1.00 14.52 ?  113 TYR   A HE2  1 
ATOM   2417 H HH   . TYR   A 1 113 ? 18.092 -9.028  -0.617  1.00 15.47 ?  113 TYR   A HH   1 
ATOM   2418 N N    . GLU   A 1 114 ? 26.326 -13.203 -0.168  1.00 11.31 ?  114 GLU   A N    1 
ATOM   2419 C CA   . GLU   A 1 114 ? 27.320 -14.100 0.423   1.00 11.25 ?  114 GLU   A CA   1 
ATOM   2420 C C    . GLU   A 1 114 ? 28.174 -13.392 1.468   1.00 11.22 ?  114 GLU   A C    1 
ATOM   2421 O O    . GLU   A 1 114 ? 28.658 -14.027 2.413   1.00 11.81 ?  114 GLU   A O    1 
ATOM   2422 C CB   . GLU   A 1 114 ? 28.188 -14.745 -0.668  1.00 11.52 ?  114 GLU   A CB   1 
ATOM   2423 C CG   . GLU   A 1 114 ? 27.415 -15.787 -1.457  1.00 12.28 ?  114 GLU   A CG   1 
ATOM   2424 C CD   . GLU   A 1 114 ? 28.122 -16.323 -2.692  1.00 12.68 ?  114 GLU   A CD   1 
ATOM   2425 O OE1  . GLU   A 1 114 ? 29.085 -15.703 -3.179  1.00 12.81 ?  114 GLU   A OE1  1 
ATOM   2426 O OE2  . GLU   A 1 114 ? 27.685 -17.388 -3.192  1.00 13.78 -1 114 GLU   A OE2  1 
ATOM   2427 H H    . GLU   A 1 114 ? 26.375 -13.114 -1.029  1.00 13.56 ?  114 GLU   A H    1 
ATOM   2428 H HA   . GLU   A 1 114 ? 26.849 -14.815 0.866   1.00 13.49 ?  114 GLU   A HA   1 
ATOM   2429 H HB2  . GLU   A 1 114 ? 28.488 -14.058 -1.290  1.00 13.81 ?  114 GLU   A HB2  1 
ATOM   2430 H HB3  . GLU   A 1 114 ? 28.948 -15.179 -0.258  1.00 13.81 ?  114 GLU   A HB3  1 
ATOM   2431 H HG2  . GLU   A 1 114 ? 27.234 -16.541 -0.877  1.00 14.72 ?  114 GLU   A HG2  1 
ATOM   2432 H HG3  . GLU   A 1 114 ? 26.575 -15.395 -1.751  1.00 14.72 ?  114 GLU   A HG3  1 
ATOM   2433 N N    . ASN   A 1 115 ? 28.355 -12.073 1.337   1.00 11.13 ?  115 ASN   A N    1 
ATOM   2434 C CA   . ASN   A 1 115 ? 29.118 -11.343 2.343   1.00 11.36 ?  115 ASN   A CA   1 
ATOM   2435 C C    . ASN   A 1 115 ? 28.504 -11.480 3.730   1.00 11.17 ?  115 ASN   A C    1 
ATOM   2436 O O    . ASN   A 1 115 ? 29.219 -11.409 4.737   1.00 11.71 ?  115 ASN   A O    1 
ATOM   2437 C CB   . ASN   A 1 115 ? 29.216 -9.863  1.971   1.00 11.70 ?  115 ASN   A CB   1 
ATOM   2438 C CG   . ASN   A 1 115 ? 30.014 -9.633  0.711   1.00 12.30 ?  115 ASN   A CG   1 
ATOM   2439 O OD1  . ASN   A 1 115 ? 31.238 -9.718  0.726   1.00 15.93 ?  115 ASN   A OD1  1 
ATOM   2440 N ND2  . ASN   A 1 115 ? 29.337 -9.342  -0.382  1.00 12.03 ?  115 ASN   A ND2  1 
ATOM   2441 H H    . ASN   A 1 115 ? 28.049 -11.587 0.696   1.00 13.34 ?  115 ASN   A H    1 
ATOM   2442 H HA   . ASN   A 1 115 ? 30.014 -11.705 2.382   1.00 13.62 ?  115 ASN   A HA   1 
ATOM   2443 H HB2  . ASN   A 1 115 ? 28.317 -9.516  1.842   1.00 14.03 ?  115 ASN   A HB2  1 
ATOM   2444 H HB3  . ASN   A 1 115 ? 29.646 -9.389  2.704   1.00 14.03 ?  115 ASN   A HB3  1 
ATOM   2445 H HD21 . ASN   A 1 115 ? 29.755 -9.196  -1.116  1.00 14.42 ?  115 ASN   A HD21 1 
ATOM   2446 H HD22 . ASN   A 1 115 ? 28.476 -9.308  -0.361  1.00 14.42 ?  115 ASN   A HD22 1 
ATOM   2447 N N    . PHE   A 1 116 ? 27.178 -11.650 3.813   1.00 11.35 ?  116 PHE   A N    1 
ATOM   2448 C CA   . PHE   A 1 116 ? 26.535 -11.752 5.119   1.00 11.16 ?  116 PHE   A CA   1 
ATOM   2449 C C    . PHE   A 1 116 ? 27.017 -12.986 5.885   1.00 11.43 ?  116 PHE   A C    1 
ATOM   2450 O O    . PHE   A 1 116 ? 26.943 -13.010 7.116   1.00 12.07 ?  116 PHE   A O    1 
ATOM   2451 C CB   . PHE   A 1 116 ? 25.003 -11.882 4.989   1.00 11.75 ?  116 PHE   A CB   1 
ATOM   2452 C CG   . PHE   A 1 116 ? 24.245 -10.635 4.531   1.00 11.36 ?  116 PHE   A CG   1 
ATOM   2453 C CD1  . PHE   A 1 116 ? 24.818 -9.602  3.787   1.00 11.31 ?  116 PHE   A CD1  1 
ATOM   2454 C CD2  . PHE   A 1 116 ? 22.888 -10.532 4.860   1.00 12.09 ?  116 PHE   A CD2  1 
ATOM   2455 C CE1  . PHE   A 1 116 ? 24.042 -8.520  3.378   1.00 11.77 ?  116 PHE   A CE1  1 
ATOM   2456 C CE2  . PHE   A 1 116 ? 22.119 -9.452  4.458   1.00 12.40 ?  116 PHE   A CE2  1 
ATOM   2457 C CZ   . PHE   A 1 116 ? 22.690 -8.447  3.719   1.00 11.76 ?  116 PHE   A CZ   1 
ATOM   2458 H H    . PHE   A 1 116 ? 26.641 -11.702 3.140   1.00 13.61 ?  116 PHE   A H    1 
ATOM   2459 H HA   . PHE   A 1 116 ? 26.732 -10.964 5.645   1.00 13.38 ?  116 PHE   A HA   1 
ATOM   2460 H HB2  . PHE   A 1 116 ? 24.810 -12.586 4.347   1.00 14.08 ?  116 PHE   A HB2  1 
ATOM   2461 H HB3  . PHE   A 1 116 ? 24.645 -12.137 5.855   1.00 14.08 ?  116 PHE   A HB3  1 
ATOM   2462 H HD1  . PHE   A 1 116 ? 25.708 -9.662  3.544   1.00 13.56 ?  116 PHE   A HD1  1 
ATOM   2463 H HD2  . PHE   A 1 116 ? 22.488 -11.221 5.355   1.00 14.50 ?  116 PHE   A HD2  1 
ATOM   2464 H HE1  . PHE   A 1 116 ? 24.435 -7.844  2.880   1.00 14.12 ?  116 PHE   A HE1  1 
ATOM   2465 H HE2  . PHE   A 1 116 ? 21.218 -9.413  4.696   1.00 14.86 ?  116 PHE   A HE2  1 
ATOM   2466 H HZ   . PHE   A 1 116 ? 22.185 -7.715  3.456   1.00 14.11 ?  116 PHE   A HZ   1 
ATOM   2467 N N    . ASN   A 1 117 ? 27.456 -14.034 5.178   1.00 11.49 ?  117 ASN   A N    1 
ATOM   2468 C CA   . ASN   A 1 117 ? 27.830 -15.279 5.845   1.00 11.81 ?  117 ASN   A CA   1 
ATOM   2469 C C    . ASN   A 1 117 ? 29.098 -15.161 6.671   1.00 12.31 ?  117 ASN   A C    1 
ATOM   2470 O O    . ASN   A 1 117 ? 29.404 -16.084 7.435   1.00 13.64 ?  117 ASN   A O    1 
ATOM   2471 C CB   . ASN   A 1 117 ? 27.942 -16.401 4.820   1.00 12.16 ?  117 ASN   A CB   1 
ATOM   2472 C CG   . ASN   A 1 117 ? 26.586 -16.794 4.294   1.00 12.22 ?  117 ASN   A CG   1 
ATOM   2473 O OD1  . ASN   A 1 117 ? 25.615 -16.832 5.052   1.00 12.93 ?  117 ASN   A OD1  1 
ATOM   2474 N ND2  . ASN   A 1 117 ? 26.494 -17.053 3.002   1.00 12.44 ?  117 ASN   A ND2  1 
ATOM   2475 H H    . ASN   A 1 117 ? 27.525 -14.049 4.316   1.00 13.78 ?  117 ASN   A H    1 
ATOM   2476 H HA   . ASN   A 1 117 ? 27.112 -15.516 6.450   1.00 14.16 ?  117 ASN   A HA   1 
ATOM   2477 H HB2  . ASN   A 1 117 ? 28.488 -16.102 4.073   1.00 14.58 ?  117 ASN   A HB2  1 
ATOM   2478 H HB3  . ASN   A 1 117 ? 28.337 -17.176 5.239   1.00 14.58 ?  117 ASN   A HB3  1 
ATOM   2479 H HD21 . ASN   A 1 117 ? 25.743 -17.279 2.663   1.00 14.92 ?  117 ASN   A HD21 1 
ATOM   2480 H HD22 . ASN   A 1 117 ? 27.199 -17.011 2.505   1.00 14.92 ?  117 ASN   A HD22 1 
ATOM   2481 N N    . GLN   A 1 118 ? 29.825 -14.054 6.549   1.00 12.34 ?  118 GLN   A N    1 
ATOM   2482 C CA   . GLN   A 1 118 ? 31.009 -13.813 7.362   1.00 12.80 ?  118 GLN   A CA   1 
ATOM   2483 C C    . GLN   A 1 118 ? 30.668 -13.248 8.734   1.00 12.94 ?  118 GLN   A C    1 
ATOM   2484 O O    . GLN   A 1 118 ? 31.580 -12.956 9.515   1.00 14.63 ?  118 GLN   A O    1 
ATOM   2485 C CB   . GLN   A 1 118 ? 31.992 -12.902 6.621   1.00 13.34 ?  118 GLN   A CB   1 
ATOM   2486 C CG   . GLN   A 1 118 ? 32.457 -13.488 5.296   1.00 13.08 ?  118 GLN   A CG   1 
ATOM   2487 C CD   . GLN   A 1 118 ? 33.280 -14.756 5.472   1.00 13.41 ?  118 GLN   A CD   1 
ATOM   2488 O OE1  . GLN   A 1 118 ? 34.144 -14.825 6.355   1.00 14.24 ?  118 GLN   A OE1  1 
ATOM   2489 N NE2  . GLN   A 1 118 ? 33.035 -15.755 4.625   1.00 13.54 ?  118 GLN   A NE2  1 
ATOM   2490 H H    . GLN   A 1 118 ? 29.642 -13.410 5.997   1.00 14.79 ?  118 GLN   A H    1 
ATOM   2491 H HA   . GLN   A 1 118 ? 31.446 -14.668 7.500   1.00 15.35 ?  118 GLN   A HA   1 
ATOM   2492 H HB2  . GLN   A 1 118 ? 31.561 -12.053 6.443   1.00 15.99 ?  118 GLN   A HB2  1 
ATOM   2493 H HB3  . GLN   A 1 118 ? 32.772 -12.769 7.182   1.00 15.99 ?  118 GLN   A HB3  1 
ATOM   2494 H HG2  . GLN   A 1 118 ? 31.683 -13.700 4.751   1.00 15.68 ?  118 GLN   A HG2  1 
ATOM   2495 H HG3  . GLN   A 1 118 ? 33.011 -12.833 4.839   1.00 15.68 ?  118 GLN   A HG3  1 
ATOM   2496 H HE21 . GLN   A 1 118 ? 32.422 -15.668 4.020   1.00 16.23 ?  118 GLN   A HE21 1 
ATOM   2497 H HE22 . GLN   A 1 118 ? 33.471 -16.491 4.685   1.00 16.23 ?  118 GLN   A HE22 1 
ATOM   2498 N N    . HIS   A 1 119 ? 29.380 -13.102 9.050   1.00 12.76 ?  119 HIS   A N    1 
ATOM   2499 C CA   . HIS   A 1 119 ? 28.933 -12.504 10.304  1.00 13.15 ?  119 HIS   A CA   1 
ATOM   2500 C C    . HIS   A 1 119 ? 27.797 -13.332 10.882  1.00 13.11 ?  119 HIS   A C    1 
ATOM   2501 O O    . HIS   A 1 119 ? 26.844 -13.659 10.171  1.00 14.19 ?  119 HIS   A O    1 
ATOM   2502 C CB   . HIS   A 1 119 ? 28.476 -11.065 10.052  1.00 14.05 ?  119 HIS   A CB   1 
ATOM   2503 C CG   . HIS   A 1 119 ? 29.551 -10.244 9.435   1.00 15.27 ?  119 HIS   A CG   1 
ATOM   2504 N ND1  . HIS   A 1 119 ? 30.529 -9.638  10.188  1.00 17.61 ?  119 HIS   A ND1  1 
ATOM   2505 C CD2  . HIS   A 1 119 ? 29.882 -10.041 8.140   1.00 16.07 ?  119 HIS   A CD2  1 
ATOM   2506 C CE1  . HIS   A 1 119 ? 31.388 -9.042  9.380   1.00 17.65 ?  119 HIS   A CE1  1 
ATOM   2507 N NE2  . HIS   A 1 119 ? 31.029 -9.284  8.132   1.00 17.65 ?  119 HIS   A NE2  1 
ATOM   2508 H H    . HIS   A 1 119 ? 28.728 -13.358 8.546   1.00 15.30 ?  119 HIS   A H    1 
ATOM   2509 H HA   . HIS   A 1 119 ? 29.670 -12.498 10.939  1.00 15.77 ?  119 HIS   A HA   1 
ATOM   2510 H HB2  . HIS   A 1 119 ? 27.714 -11.081 9.454   1.00 16.85 ?  119 HIS   A HB2  1 
ATOM   2511 H HB3  . HIS   A 1 119 ? 28.229 -10.666 10.902  1.00 16.85 ?  119 HIS   A HB3  1 
ATOM   2512 H HD1  . HIS   A 1 119 ? 30.559 -9.627  11.048  1.00 21.12 ?  119 HIS   A HD1  1 
ATOM   2513 H HD2  . HIS   A 1 119 ? 29.416 -10.355 7.399   1.00 19.27 ?  119 HIS   A HD2  1 
ATOM   2514 H HE1  . HIS   A 1 119 ? 32.120 -8.538  9.647   1.00 21.16 ?  119 HIS   A HE1  1 
ATOM   2515 N N    . GLU   A 1 120 ? 27.899 -13.659 12.173  1.00 14.23 ?  120 GLU   A N    1 
ATOM   2516 C CA   . GLU   A 1 120 ? 26.949 -14.594 12.770  1.00 16.68 ?  120 GLU   A CA   1 
ATOM   2517 C C    . GLU   A 1 120 ? 25.534 -14.028 12.845  1.00 14.93 ?  120 GLU   A C    1 
ATOM   2518 O O    . GLU   A 1 120 ? 24.557 -14.785 12.722  1.00 15.01 ?  120 GLU   A O    1 
ATOM   2519 C CB   . GLU   A 1 120 ? 27.430 -15.012 14.162  1.00 23.82 ?  120 GLU   A CB   1 
ATOM   2520 C CG   . GLU   A 1 120 ? 28.608 -15.974 14.156  1.00 33.69 ?  120 GLU   A CG   1 
ATOM   2521 C CD   . GLU   A 1 120 ? 28.812 -16.642 15.503  1.00 42.85 ?  120 GLU   A CD   1 
ATOM   2522 O OE1  . GLU   A 1 120 ? 28.238 -16.156 16.502  1.00 45.04 ?  120 GLU   A OE1  1 
ATOM   2523 O OE2  . GLU   A 1 120 ? 29.543 -17.652 15.564  1.00 49.90 -1 120 GLU   A OE2  1 
ATOM   2524 H H    . GLU   A 1 120 ? 28.504 -13.361 12.714  1.00 17.06 ?  120 GLU   A H    1 
ATOM   2525 H HA   . GLU   A 1 120 ? 26.924 -15.394 12.229  1.00 20.00 ?  120 GLU   A HA   1 
ATOM   2526 H HB2  . GLU   A 1 120 ? 27.708 -14.226 14.657  1.00 28.57 ?  120 GLU   A HB2  1 
ATOM   2527 H HB3  . GLU   A 1 120 ? 26.703 -15.453 14.631  1.00 28.57 ?  120 GLU   A HB3  1 
ATOM   2528 H HG2  . GLU   A 1 120 ? 28.457 -16.660 13.485  1.00 40.42 ?  120 GLU   A HG2  1 
ATOM   2529 H HG3  . GLU   A 1 120 ? 29.421 -15.487 13.956  1.00 40.42 ?  120 GLU   A HG3  1 
ATOM   2530 N N    . VAL   A 1 121 ? 25.403 -12.719 13.067  1.00 14.33 ?  121 VAL   A N    1 
ATOM   2531 C CA   . VAL   A 1 121 ? 24.113 -12.047 13.203  1.00 14.24 ?  121 VAL   A CA   1 
ATOM   2532 C C    . VAL   A 1 121 ? 24.219 -10.659 12.577  1.00 13.06 ?  121 VAL   A C    1 
ATOM   2533 O O    . VAL   A 1 121 ? 25.193 -9.940  12.817  1.00 14.18 ?  121 VAL   A O    1 
ATOM   2534 C CB   . VAL   A 1 121 ? 23.700 -11.911 14.686  1.00 17.35 ?  121 VAL   A CB   1 
ATOM   2535 C CG1  . VAL   A 1 121 ? 22.334 -11.242 14.807  1.00 18.09 ?  121 VAL   A CG1  1 
ATOM   2536 C CG2  . VAL   A 1 121 ? 23.690 -13.256 15.395  1.00 20.01 ?  121 VAL   A CG2  1 
ATOM   2537 H H    . VAL   A 1 121 ? 26.074 -12.183 13.153  1.00 17.19 ?  121 VAL   A H    1 
ATOM   2538 H HA   . VAL   A 1 121 ? 23.434 -12.556 12.737  1.00 17.07 ?  121 VAL   A HA   1 
ATOM   2539 H HB   . VAL   A 1 121 ? 24.341 -11.349 15.140  1.00 20.81 ?  121 VAL   A HB   1 
ATOM   2540 H HG11 . VAL   A 1 121 ? 22.020 -11.324 15.721  1.00 21.70 ?  121 VAL   A HG11 1 
ATOM   2541 H HG12 . VAL   A 1 121 ? 22.420 -10.303 14.573  1.00 21.70 ?  121 VAL   A HG12 1 
ATOM   2542 H HG13 . VAL   A 1 121 ? 21.711 -11.677 14.204  1.00 21.70 ?  121 VAL   A HG13 1 
ATOM   2543 H HG21 . VAL   A 1 121 ? 23.354 -13.135 16.303  1.00 24.00 ?  121 VAL   A HG21 1 
ATOM   2544 H HG22 . VAL   A 1 121 ? 23.105 -13.868 14.916  1.00 24.00 ?  121 VAL   A HG22 1 
ATOM   2545 H HG23 . VAL   A 1 121 ? 24.589 -13.611 15.424  1.00 24.00 ?  121 VAL   A HG23 1 
ATOM   2546 N N    . LEU   A 1 122 ? 23.203 -10.264 11.802  1.00 12.98 ?  122 LEU   A N    1 
ATOM   2547 C CA   . LEU   A 1 122 ? 23.203 -8.963  11.137  1.00 12.70 ?  122 LEU   A CA   1 
ATOM   2548 C C    . LEU   A 1 122 ? 21.806 -8.367  11.101  1.00 12.64 ?  122 LEU   A C    1 
ATOM   2549 O O    . LEU   A 1 122 ? 20.811 -9.084  10.979  1.00 13.70 ?  122 LEU   A O    1 
ATOM   2550 C CB   . LEU   A 1 122 ? 23.619 -9.052  9.662   1.00 14.55 ?  122 LEU   A CB   1 
ATOM   2551 C CG   . LEU   A 1 122 ? 24.828 -9.893  9.285   1.00 14.54 ?  122 LEU   A CG   1 
ATOM   2552 C CD1  . LEU   A 1 122 ? 24.423 -11.342 9.050   1.00 15.41 ?  122 LEU   A CD1  1 
ATOM   2553 C CD2  . LEU   A 1 122 ? 25.492 -9.302  8.054   1.00 13.94 ?  122 LEU   A CD2  1 
ATOM   2554 H H    . LEU   A 1 122 ? 22.503 -10.738 11.643  1.00 15.56 ?  122 LEU   A H    1 
ATOM   2555 H HA   . LEU   A 1 122 ? 23.801 -8.352  11.596  1.00 15.23 ?  122 LEU   A HA   1 
ATOM   2556 H HB2  . LEU   A 1 122 ? 22.877 -9.415  9.164   1.00 17.44 ?  122 LEU   A HB2  1 
ATOM   2557 H HB3  . LEU   A 1 122 ? 23.806 -8.155  9.351   1.00 17.44 ?  122 LEU   A HB3  1 
ATOM   2558 H HG   . LEU   A 1 122 ? 25.483 -9.874  10.004  1.00 17.43 ?  122 LEU   A HG   1 
ATOM   2559 H HD11 . LEU   A 1 122 ? 25.203 -11.854 8.778   1.00 18.48 ?  122 LEU   A HD11 1 
ATOM   2560 H HD12 . LEU   A 1 122 ? 24.063 -11.705 9.873   1.00 18.48 ?  122 LEU   A HD12 1 
ATOM   2561 H HD13 . LEU   A 1 122 ? 23.751 -11.372 8.351   1.00 18.48 ?  122 LEU   A HD13 1 
ATOM   2562 H HD21 . LEU   A 1 122 ? 26.236 -9.866  7.781   1.00 16.71 ?  122 LEU   A HD21 1 
ATOM   2563 H HD22 . LEU   A 1 122 ? 24.842 -9.247  7.336   1.00 16.71 ?  122 LEU   A HD22 1 
ATOM   2564 H HD23 . LEU   A 1 122 ? 25.823 -8.410  8.265   1.00 16.71 ?  122 LEU   A HD23 1 
ATOM   2565 N N    A LEU   A 1 123 ? 21.745 -7.039  11.190  0.60 12.05 ?  123 LEU   A N    1 
ATOM   2566 N N    B LEU   A 1 123 ? 21.762 -7.037  11.204  0.40 12.11 ?  123 LEU   A N    1 
ATOM   2567 C CA   A LEU   A 1 123 ? 20.572 -6.259  10.807  0.60 11.79 ?  123 LEU   A CA   1 
ATOM   2568 C CA   B LEU   A 1 123 ? 20.581 -6.231  10.928  0.40 11.81 ?  123 LEU   A CA   1 
ATOM   2569 C C    A LEU   A 1 123 ? 20.805 -5.752  9.390   0.60 11.53 ?  123 LEU   A C    1 
ATOM   2570 C C    B LEU   A 1 123 ? 20.791 -5.612  9.555   0.40 10.87 ?  123 LEU   A C    1 
ATOM   2571 O O    A LEU   A 1 123 ? 21.872 -5.205  9.106   0.60 11.22 ?  123 LEU   A O    1 
ATOM   2572 O O    B LEU   A 1 123 ? 21.790 -4.919  9.341   0.40 11.33 ?  123 LEU   A O    1 
ATOM   2573 C CB   A LEU   A 1 123 ? 20.425 -5.067  11.753  0.60 12.44 ?  123 LEU   A CB   1 
ATOM   2574 C CB   B LEU   A 1 123 ? 20.454 -5.123  11.974  0.40 12.70 ?  123 LEU   A CB   1 
ATOM   2575 C CG   A LEU   A 1 123 ? 19.357 -4.023  11.423  0.60 13.11 ?  123 LEU   A CG   1 
ATOM   2576 C CG   B LEU   A 1 123 ? 19.440 -4.019  11.662  0.40 12.93 ?  123 LEU   A CG   1 
ATOM   2577 C CD1  A LEU   A 1 123 ? 17.966 -4.643  11.409  0.60 13.60 ?  123 LEU   A CD1  1 
ATOM   2578 C CD1  B LEU   A 1 123 ? 18.027 -4.579  11.680  0.40 13.80 ?  123 LEU   A CD1  1 
ATOM   2579 C CD2  A LEU   A 1 123 ? 19.426 -2.861  12.413  0.60 13.76 ?  123 LEU   A CD2  1 
ATOM   2580 C CD2  B LEU   A 1 123 ? 19.581 -2.864  12.640  0.40 13.45 ?  123 LEU   A CD2  1 
ATOM   2581 H H    A LEU   A 1 123 ? 22.394 -6.554  11.484  0.60 14.45 ?  123 LEU   A H    1 
ATOM   2582 H H    B LEU   A 1 123 ? 22.444 -6.557  11.419  0.40 14.52 ?  123 LEU   A H    1 
ATOM   2583 H HA   A LEU   A 1 123 ? 19.773 -6.807  10.837  0.60 14.13 ?  123 LEU   A HA   1 
ATOM   2584 H HA   B LEU   A 1 123 ? 19.779 -6.770  10.920  0.40 14.17 ?  123 LEU   A HA   1 
ATOM   2585 H HB2  A LEU   A 1 123 ? 20.216 -5.410  12.637  0.60 14.91 ?  123 LEU   A HB2  1 
ATOM   2586 H HB2  B LEU   A 1 123 ? 20.185 -5.528  12.814  0.40 15.23 ?  123 LEU   A HB2  1 
ATOM   2587 H HB3  A LEU   A 1 123 ? 21.273 -4.603  11.785  0.60 14.91 ?  123 LEU   A HB3  1 
ATOM   2588 H HB3  B LEU   A 1 123 ? 21.319 -4.699  12.082  0.40 15.23 ?  123 LEU   A HB3  1 
ATOM   2589 H HG   A LEU   A 1 123 ? 19.529 -3.659  10.539  0.60 15.72 ?  123 LEU   A HG   1 
ATOM   2590 H HG   B LEU   A 1 123 ? 19.606 -3.660  10.775  0.40 15.50 ?  123 LEU   A HG   1 
ATOM   2591 H HD11 A LEU   A 1 123 ? 17.309 -3.947  11.251  0.60 16.30 ?  123 LEU   A HD11 1 
ATOM   2592 H HD11 B LEU   A 1 123 ? 17.400 -3.860  11.509  0.40 16.55 ?  123 LEU   A HD11 1 
ATOM   2593 H HD12 A LEU   A 1 123 ? 17.924 -5.305  10.702  0.60 16.30 ?  123 LEU   A HD12 1 
ATOM   2594 H HD12 B LEU   A 1 123 ? 17.949 -5.258  10.991  0.40 16.55 ?  123 LEU   A HD12 1 
ATOM   2595 H HD13 A LEU   A 1 123 ? 17.801 -5.064  12.268  0.60 16.30 ?  123 LEU   A HD13 1 
ATOM   2596 H HD13 B LEU   A 1 123 ? 17.856 -4.969  12.551  0.40 16.55 ?  123 LEU   A HD13 1 
ATOM   2597 H HD21 A LEU   A 1 123 ? 18.744 -2.210  12.188  0.60 16.50 ?  123 LEU   A HD21 1 
ATOM   2598 H HD21 B LEU   A 1 123 ? 18.928 -2.182  12.417  0.40 16.13 ?  123 LEU   A HD21 1 
ATOM   2599 H HD22 A LEU   A 1 123 ? 19.273 -3.203  13.310  0.60 16.50 ?  123 LEU   A HD22 1 
ATOM   2600 H HD22 B LEU   A 1 123 ? 19.423 -3.194  13.538  0.40 16.13 ?  123 LEU   A HD22 1 
ATOM   2601 H HD23 A LEU   A 1 123 ? 20.304 -2.453  12.362  0.60 16.50 ?  123 LEU   A HD23 1 
ATOM   2602 H HD23 B LEU   A 1 123 ? 20.477 -2.501  12.572  0.40 16.13 ?  123 LEU   A HD23 1 
ATOM   2603 N N    A ALA   A 1 124 ? 19.828 -5.926  8.497   0.60 11.59 ?  124 ALA   A N    1 
ATOM   2604 N N    B ALA   A 1 124 ? 19.873 -5.855  8.630   0.40 10.40 ?  124 ALA   A N    1 
ATOM   2605 C CA   A ALA   A 1 124 ? 20.101 -5.663  7.088   0.60 11.81 ?  124 ALA   A CA   1 
ATOM   2606 C CA   B ALA   A 1 124 ? 20.103 -5.493  7.243   0.40 10.31 ?  124 ALA   A CA   1 
ATOM   2607 C C    A ALA   A 1 124 ? 18.865 -5.216  6.316   0.60 10.95 ?  124 ALA   A C    1 
ATOM   2608 C C    B ALA   A 1 124 ? 18.831 -4.998  6.576   0.40 9.95  ?  124 ALA   A C    1 
ATOM   2609 O O    A ALA   A 1 124 ? 17.736 -5.588  6.666   0.60 11.45 ?  124 ALA   A O    1 
ATOM   2610 O O    B ALA   A 1 124 ? 17.719 -5.341  6.993   0.40 10.45 ?  124 ALA   A O    1 
ATOM   2611 C CB   A ALA   A 1 124 ? 20.711 -6.897  6.404   0.60 12.37 ?  124 ALA   A CB   1 
ATOM   2612 C CB   B ALA   A 1 124 ? 20.616 -6.694  6.442   0.40 10.32 ?  124 ALA   A CB   1 
ATOM   2613 H H    A ALA   A 1 124 ? 19.035 -6.200  8.678   0.60 13.90 ?  124 ALA   A H    1 
ATOM   2614 H H    B ALA   A 1 124 ? 19.115 -6.236  8.774   0.40 12.46 ?  124 ALA   A H    1 
ATOM   2615 H HA   A ALA   A 1 124 ? 20.762 -4.958  7.045   0.60 14.16 ?  124 ALA   A HA   1 
ATOM   2616 H HA   B ALA   A 1 124 ? 20.774 -4.789  7.206   0.40 12.36 ?  124 ALA   A HA   1 
ATOM   2617 H HB1  A ALA   A 1 124 ? 20.886 -6.692  5.472   0.60 14.83 ?  124 ALA   A HB1  1 
ATOM   2618 H HB1  B ALA   A 1 124 ? 20.760 -6.420  5.522   0.40 12.37 ?  124 ALA   A HB1  1 
ATOM   2619 H HB2  A ALA   A 1 124 ? 21.548 -7.130  6.848   0.60 14.83 ?  124 ALA   A HB2  1 
ATOM   2620 H HB2  B ALA   A 1 124 ? 21.447 -6.996  6.834   0.40 12.37 ?  124 ALA   A HB2  1 
ATOM   2621 H HB3  A ALA   A 1 124 ? 20.092 -7.640  6.470   0.60 14.83 ?  124 ALA   A HB3  1 
ATOM   2622 H HB3  B ALA   A 1 124 ? 19.951 -7.397  6.478   0.40 12.37 ?  124 ALA   A HB3  1 
ATOM   2623 N N    A PRO   A 1 125 ? 19.055 -4.448  5.244   0.60 10.26 ?  125 PRO   A N    1 
ATOM   2624 N N    B PRO   A 1 125 ? 18.972 -4.194  5.522   0.40 10.19 ?  125 PRO   A N    1 
ATOM   2625 C CA   A PRO   A 1 125 ? 17.988 -4.188  4.277   0.60 10.39 ?  125 PRO   A CA   1 
ATOM   2626 C CA   B PRO   A 1 125 ? 17.868 -3.959  4.591   0.40 11.11 ?  125 PRO   A CA   1 
ATOM   2627 C C    A PRO   A 1 125 ? 18.028 -5.253  3.187   0.60 10.11 ?  125 PRO   A C    1 
ATOM   2628 C C    B PRO   A 1 125 ? 17.901 -5.021  3.508   0.40 11.60 ?  125 PRO   A C    1 
ATOM   2629 O O    A PRO   A 1 125 ? 19.000 -5.996  3.048   0.60 10.37 ?  125 PRO   A O    1 
ATOM   2630 O O    B PRO   A 1 125 ? 18.820 -5.847  3.474   0.40 11.62 ?  125 PRO   A O    1 
ATOM   2631 C CB   A PRO   A 1 125 ? 18.426 -2.840  3.693   0.60 10.12 ?  125 PRO   A CB   1 
ATOM   2632 C CB   B PRO   A 1 125 ? 18.228 -2.591  4.004   0.40 11.24 ?  125 PRO   A CB   1 
ATOM   2633 C CG   A PRO   A 1 125 ? 19.939 -2.975  3.624   0.60 9.76  ?  125 PRO   A CG   1 
ATOM   2634 C CG   B PRO   A 1 125 ? 19.735 -2.662  3.906   0.40 11.66 ?  125 PRO   A CG   1 
ATOM   2635 C CD   A PRO   A 1 125 ? 20.325 -3.814  4.833   0.60 9.95  ?  125 PRO   A CD   1 
ATOM   2636 C CD   B PRO   A 1 125 ? 20.193 -3.483  5.095   0.40 11.00 ?  125 PRO   A CD   1 
ATOM   2637 H HA   A PRO   A 1 125 ? 17.116 -4.140  4.695   0.60 12.45 ?  125 PRO   A HA   1 
ATOM   2638 H HA   B PRO   A 1 125 ? 16.996 -3.945  5.024   0.40 13.32 ?  125 PRO   A HA   1 
ATOM   2639 H HB2  A PRO   A 1 125 ? 18.041 -2.724  2.810   0.60 12.14 ?  125 PRO   A HB2  1 
ATOM   2640 H HB2  B PRO   A 1 125 ? 17.827 -2.480  3.127   0.40 13.48 ?  125 PRO   A HB2  1 
ATOM   2641 H HB3  A PRO   A 1 125 ? 18.161 -2.126  4.289   0.60 12.14 ?  125 PRO   A HB3  1 
ATOM   2642 H HB3  B PRO   A 1 125 ? 17.952 -1.885  4.608   0.40 13.48 ?  125 PRO   A HB3  1 
ATOM   2643 H HG2  A PRO   A 1 125 ? 20.191 -3.419  2.798   0.60 11.69 ?  125 PRO   A HG2  1 
ATOM   2644 H HG2  B PRO   A 1 125 ? 19.987 -3.096  3.075   0.40 13.98 ?  125 PRO   A HG2  1 
ATOM   2645 H HG3  A PRO   A 1 125 ? 20.343 -2.093  3.672   0.60 11.69 ?  125 PRO   A HG3  1 
ATOM   2646 H HG3  B PRO   A 1 125 ? 20.107 -1.766  3.946   0.40 13.98 ?  125 PRO   A HG3  1 
ATOM   2647 H HD2  A PRO   A 1 125 ? 20.984 -4.485  4.580   0.60 11.93 ?  125 PRO   A HD2  1 
ATOM   2648 H HD2  B PRO   A 1 125 ? 20.873 -4.115  4.821   0.40 13.18 ?  125 PRO   A HD2  1 
ATOM   2649 H HD3  A PRO   A 1 125 ? 20.661 -3.246  5.544   0.60 11.93 ?  125 PRO   A HD3  1 
ATOM   2650 H HD3  B PRO   A 1 125 ? 20.514 -2.902  5.800   0.40 13.18 ?  125 PRO   A HD3  1 
ATOM   2651 N N    A LEU   A 1 126 ? 16.958 -5.304  2.395   0.60 10.80 ?  126 LEU   A N    1 
ATOM   2652 N N    B LEU   A 1 126 ? 16.925 -4.998  2.611   0.40 12.02 ?  126 LEU   A N    1 
ATOM   2653 C CA   A LEU   A 1 126 ? 16.985 -6.119  1.188   0.60 11.14 ?  126 LEU   A CA   1 
ATOM   2654 C CA   B LEU   A 1 126 ? 16.977 -5.837  1.423   0.40 11.80 ?  126 LEU   A CA   1 
ATOM   2655 C C    A LEU   A 1 126 ? 17.910 -5.487  0.153   0.60 11.32 ?  126 LEU   A C    1 
ATOM   2656 C C    B LEU   A 1 126 ? 17.933 -5.225  0.406   0.40 12.22 ?  126 LEU   A C    1 
ATOM   2657 O O    A LEU   A 1 126 ? 17.668 -4.369  -0.317  0.60 11.01 ?  126 LEU   A O    1 
ATOM   2658 O O    B LEU   A 1 126 ? 17.809 -4.048  0.063   0.40 13.43 ?  126 LEU   A O    1 
ATOM   2659 C CB   A LEU   A 1 126 ? 15.582 -6.282  0.624   0.60 12.01 ?  126 LEU   A CB   1 
ATOM   2660 C CB   B LEU   A 1 126 ? 15.588 -5.950  0.802   0.40 12.50 ?  126 LEU   A CB   1 
ATOM   2661 C CG   A LEU   A 1 126 ? 14.726 -7.252  1.438   0.60 13.17 ?  126 LEU   A CG   1 
ATOM   2662 C CG   B LEU   A 1 126 ? 14.557 -6.848  1.479   0.40 13.00 ?  126 LEU   A CG   1 
ATOM   2663 C CD1  A LEU   A 1 126 ? 13.262 -7.092  1.097   0.60 14.14 ?  126 LEU   A CD1  1 
ATOM   2664 C CD1  B LEU   A 1 126 ? 13.284 -6.862  0.645   0.40 13.84 ?  126 LEU   A CD1  1 
ATOM   2665 C CD2  A LEU   A 1 126 ? 15.179 -8.687  1.197   0.60 13.05 ?  126 LEU   A CD2  1 
ATOM   2666 C CD2  B LEU   A 1 126 ? 15.088 -8.260  1.655   0.40 12.85 ?  126 LEU   A CD2  1 
ATOM   2667 H H    A LEU   A 1 126 ? 16.223 -4.878  2.526   0.60 12.95 ?  126 LEU   A H    1 
ATOM   2668 H H    B LEU   A 1 126 ? 16.230 -4.497  2.678   0.40 14.41 ?  126 LEU   A H    1 
ATOM   2669 H HA   A LEU   A 1 126 ? 17.332 -6.996  1.398   0.60 13.35 ?  126 LEU   A HA   1 
ATOM   2670 H HA   B LEU   A 1 126 ? 17.296 -6.717  1.659   0.40 14.15 ?  126 LEU   A HA   1 
ATOM   2671 H HB2  A LEU   A 1 126 ? 15.131 -5.426  0.626   0.60 14.40 ?  126 LEU   A HB2  1 
ATOM   2672 H HB2  B LEU   A 1 126 ? 15.203 -5.060  0.775   0.40 14.98 ?  126 LEU   A HB2  1 
ATOM   2673 H HB3  A LEU   A 1 126 ? 15.636 -6.627  -0.284  0.60 14.40 ?  126 LEU   A HB3  1 
ATOM   2674 H HB3  B LEU   A 1 126 ? 15.692 -6.278  -0.098  0.40 14.98 ?  126 LEU   A HB3  1 
ATOM   2675 H HG   A LEU   A 1 126 ? 14.842 -7.065  2.382   0.60 15.79 ?  126 LEU   A HG   1 
ATOM   2676 H HG   B LEU   A 1 126 ? 14.339 -6.489  2.357   0.40 15.58 ?  126 LEU   A HG   1 
ATOM   2677 H HD11 A LEU   A 1 126 ? 12.744 -7.723  1.621   0.60 16.96 ?  126 LEU   A HD11 1 
ATOM   2678 H HD11 B LEU   A 1 126 ? 12.635 -7.448  1.066   0.40 16.60 ?  126 LEU   A HD11 1 
ATOM   2679 H HD12 A LEU   A 1 126 ? 12.993 -6.186  1.305   0.60 16.96 ?  126 LEU   A HD12 1 
ATOM   2680 H HD12 B LEU   A 1 126 ? 12.929 -5.963  0.587   0.40 16.60 ?  126 LEU   A HD12 1 
ATOM   2681 H HD13 A LEU   A 1 126 ? 13.139 -7.268  0.151   0.60 16.96 ?  126 LEU   A HD13 1 
ATOM   2682 H HD13 B LEU   A 1 126 ? 13.495 -7.193  -0.245  0.40 16.60 ?  126 LEU   A HD13 1 
ATOM   2683 H HD21 A LEU   A 1 126 ? 14.546 -9.295  1.606   0.60 15.64 ?  126 LEU   A HD21 1 
ATOM   2684 H HD21 B LEU   A 1 126 ? 14.363 -8.838  1.931   0.40 15.40 ?  126 LEU   A HD21 1 
ATOM   2685 H HD22 A LEU   A 1 126 ? 15.228 -8.848  0.242   0.60 15.64 ?  126 LEU   A HD22 1 
ATOM   2686 H HD22 B LEU   A 1 126 ? 15.454 -8.562  0.810   0.40 15.40 ?  126 LEU   A HD22 1 
ATOM   2687 H HD23 A LEU   A 1 126 ? 16.060 -8.814  1.595   0.60 15.64 ?  126 LEU   A HD23 1 
ATOM   2688 H HD23 B LEU   A 1 126 ? 15.783 -8.251  2.332   0.40 15.40 ?  126 LEU   A HD23 1 
ATOM   2689 N N    A LEU   A 1 127 ? 18.961 -6.216  -0.207  0.60 11.68 ?  127 LEU   A N    1 
ATOM   2690 N N    B LEU   A 1 127 ? 18.884 -6.016  -0.081  0.40 11.95 ?  127 LEU   A N    1 
ATOM   2691 C CA   A LEU   A 1 127 ? 19.944 -5.711  -1.150  0.60 11.56 ?  127 LEU   A CA   1 
ATOM   2692 C CA   B LEU   A 1 127 ? 19.858 -5.501  -1.032  0.40 12.00 ?  127 LEU   A CA   1 
ATOM   2693 C C    A LEU   A 1 127 ? 19.314 -5.463  -2.511  0.60 10.73 ?  127 LEU   A C    1 
ATOM   2694 C C    B LEU   A 1 127 ? 19.254 -5.372  -2.422  0.40 11.78 ?  127 LEU   A C    1 
ATOM   2695 O O    A LEU   A 1 127 ? 18.483 -6.236  -2.994  0.60 11.14 ?  127 LEU   A O    1 
ATOM   2696 O O    B LEU   A 1 127 ? 18.370 -6.138  -2.817  0.40 12.53 ?  127 LEU   A O    1 
ATOM   2697 C CB   A LEU   A 1 127 ? 21.097 -6.706  -1.287  0.60 11.76 ?  127 LEU   A CB   1 
ATOM   2698 C CB   B LEU   A 1 127 ? 21.088 -6.406  -1.101  0.40 12.13 ?  127 LEU   A CB   1 
ATOM   2699 C CG   A LEU   A 1 127 ? 21.904 -6.986  -0.020  0.60 11.60 ?  127 LEU   A CG   1 
ATOM   2700 C CG   B LEU   A 1 127 ? 21.887 -6.526  0.198   0.40 12.19 ?  127 LEU   A CG   1 
ATOM   2701 C CD1  A LEU   A 1 127 ? 23.001 -7.979  -0.330  0.60 11.77 ?  127 LEU   A CD1  1 
ATOM   2702 C CD1  B LEU   A 1 127 ? 23.061 -7.476  0.029   0.40 12.70 ?  127 LEU   A CD1  1 
ATOM   2703 C CD2  A LEU   A 1 127 ? 22.504 -5.707  0.545   0.60 12.47 ?  127 LEU   A CD2  1 
ATOM   2704 C CD2  B LEU   A 1 127 ? 22.369 -5.163  0.676   0.40 12.47 ?  127 LEU   A CD2  1 
ATOM   2705 H H    A LEU   A 1 127 ? 19.124 -7.006  0.090   0.60 14.01 ?  127 LEU   A H    1 
ATOM   2706 H H    B LEU   A 1 127 ? 18.986 -6.846  0.123   0.40 14.33 ?  127 LEU   A H    1 
ATOM   2707 H HA   A LEU   A 1 127 ? 20.303 -4.875  -0.822  0.60 13.86 ?  127 LEU   A HA   1 
ATOM   2708 H HA   B LEU   A 1 127 ? 20.134 -4.622  -0.749  0.40 14.39 ?  127 LEU   A HA   1 
ATOM   2709 H HB2  A LEU   A 1 127 ? 20.735 -7.555  -1.588  0.60 14.09 ?  127 LEU   A HB2  1 
ATOM   2710 H HB2  B LEU   A 1 127 ? 20.799 -7.297  -1.354  0.40 14.54 ?  127 LEU   A HB2  1 
ATOM   2711 H HB3  A LEU   A 1 127 ? 21.717 -6.367  -1.949  0.60 14.09 ?  127 LEU   A HB3  1 
ATOM   2712 H HB3  B LEU   A 1 127 ? 21.682 -6.055  -1.785  0.40 14.54 ?  127 LEU   A HB3  1 
ATOM   2713 H HG   A LEU   A 1 127 ? 21.322 -7.379  0.653   0.60 13.91 ?  127 LEU   A HG   1 
ATOM   2714 H HG   B LEU   A 1 127 ? 21.307 -6.889  0.883   0.40 14.61 ?  127 LEU   A HG   1 
ATOM   2715 H HD11 A LEU   A 1 127 ? 23.472 -8.199  0.490   0.60 14.11 ?  127 LEU   A HD11 1 
ATOM   2716 H HD11 B LEU   A 1 127 ? 23.594 -7.461  0.840   0.40 15.23 ?  127 LEU   A HD11 1 
ATOM   2717 H HD12 A LEU   A 1 127 ? 22.605 -8.784  -0.706  0.60 14.11 ?  127 LEU   A HD12 1 
ATOM   2718 H HD12 B LEU   A 1 127 ? 22.723 -8.369  -0.130  0.40 15.23 ?  127 LEU   A HD12 1 
ATOM   2719 H HD13 A LEU   A 1 127 ? 23.612 -7.585  -0.969  0.60 14.11 ?  127 LEU   A HD13 1 
ATOM   2720 H HD13 B LEU   A 1 127 ? 23.598 -7.183  -0.723  0.40 15.23 ?  127 LEU   A HD13 1 
ATOM   2721 H HD21 A LEU   A 1 127 ? 23.118 -5.935  1.259   0.60 14.95 ?  127 LEU   A HD21 1 
ATOM   2722 H HD21 B LEU   A 1 127 ? 22.988 -5.288  1.411   0.40 14.95 ?  127 LEU   A HD21 1 
ATOM   2723 H HD22 A LEU   A 1 127 ? 22.980 -5.245  -0.165  0.60 14.95 ?  127 LEU   A HD22 1 
ATOM   2724 H HD22 B LEU   A 1 127 ? 22.812 -4.708  -0.058  0.40 14.95 ?  127 LEU   A HD22 1 
ATOM   2725 H HD23 A LEU   A 1 127 ? 21.791 -5.147  0.884   0.60 14.95 ?  127 LEU   A HD23 1 
ATOM   2726 H HD23 B LEU   A 1 127 ? 21.605 -4.642  0.973   0.40 14.95 ?  127 LEU   A HD23 1 
ATOM   2727 N N    A SER   A 1 128 ? 19.734 -4.372  -3.133  0.60 11.15 ?  128 SER   A N    1 
ATOM   2728 N N    B SER   A 1 128 ? 19.746 -4.383  -3.167  0.40 11.87 ?  128 SER   A N    1 
ATOM   2729 C CA   A SER   A 1 128 ? 19.311 -3.938  -4.458  0.60 10.76 ?  128 SER   A CA   1 
ATOM   2730 C CA   B SER   A 1 128 ? 19.365 -4.100  -4.546  0.40 11.37 ?  128 SER   A CA   1 
ATOM   2731 C C    A SER   A 1 128 ? 17.853 -3.487  -4.520  0.60 10.97 ?  128 SER   A C    1 
ATOM   2732 C C    B SER   A 1 128 ? 17.921 -3.632  -4.688  0.40 11.84 ?  128 SER   A C    1 
ATOM   2733 O O    A SER   A 1 128 ? 17.367 -3.168  -5.606  0.60 12.00 ?  128 SER   A O    1 
ATOM   2734 O O    B SER   A 1 128 ? 17.475 -3.384  -5.813  0.40 13.14 ?  128 SER   A O    1 
ATOM   2735 C CB   A SER   A 1 128 ? 19.654 -4.952  -5.560  0.60 10.87 ?  128 SER   A CB   1 
ATOM   2736 C CB   B SER   A 1 128 ? 19.655 -5.278  -5.485  0.40 11.34 ?  128 SER   A CB   1 
ATOM   2737 O OG   A SER   A 1 128 ? 21.062 -5.172  -5.597  0.60 11.71 ?  128 SER   A OG   1 
ATOM   2738 O OG   B SER   A 1 128 ? 21.050 -5.400  -5.712  0.40 12.23 ?  128 SER   A OG   1 
ATOM   2739 H H    A SER   A 1 128 ? 20.315 -3.838  -2.780  0.60 13.37 ?  128 SER   A H    1 
ATOM   2740 H H    B SER   A 1 128 ? 20.347 -3.830  -2.879  0.40 14.23 ?  128 SER   A H    1 
ATOM   2741 H HA   A SER   A 1 128 ? 19.843 -3.158  -4.656  0.60 12.90 ?  128 SER   A HA   1 
ATOM   2742 H HA   B SER   A 1 128 ? 19.908 -3.360  -4.858  0.40 13.64 ?  128 SER   A HA   1 
ATOM   2743 H HB2  A SER   A 1 128 ? 19.207 -5.788  -5.381  0.60 13.04 ?  128 SER   A HB2  1 
ATOM   2744 H HB2  B SER   A 1 128 ? 19.329 -6.093  -5.068  0.40 13.60 ?  128 SER   A HB2  1 
ATOM   2745 H HB3  A SER   A 1 128 ? 19.365 -4.592  -6.416  0.60 13.04 ?  128 SER   A HB3  1 
ATOM   2746 H HB3  B SER   A 1 128 ? 19.211 -5.129  -6.327  0.40 13.60 ?  128 SER   A HB3  1 
ATOM   2747 H HG   A SER   A 1 128 ? 21.465 -4.455  -5.766  0.60 14.05 ?  128 SER   A HG   1 
ATOM   2748 H HG   B SER   A 1 128 ? 21.342 -4.688  -6.050  0.40 14.66 ?  128 SER   A HG   1 
ATOM   2749 N N    A ALA   A 1 129 ? 17.162 -3.397  -3.382  0.60 11.93 ?  129 ALA   A N    1 
ATOM   2750 N N    B ALA   A 1 129 ? 17.191 -3.469  -3.589  0.40 12.16 ?  129 ALA   A N    1 
ATOM   2751 C CA   A ALA   A 1 129 ? 15.801 -2.887  -3.338  0.60 12.19 ?  129 ALA   A CA   1 
ATOM   2752 C CA   B ALA   A 1 129 ? 15.823 -2.983  -3.618  0.40 12.49 ?  129 ALA   A CA   1 
ATOM   2753 C C    A ALA   A 1 129 ? 15.804 -1.357  -3.387  0.60 12.08 ?  129 ALA   A C    1 
ATOM   2754 C C    B ALA   A 1 129 ? 15.825 -1.450  -3.552  0.40 12.45 ?  129 ALA   A C    1 
ATOM   2755 O O    A ALA   A 1 129 ? 16.844 -0.711  -3.557  0.60 12.47 ?  129 ALA   A O    1 
ATOM   2756 O O    B ALA   A 1 129 ? 16.878 -0.805  -3.563  0.40 12.72 ?  129 ALA   A O    1 
ATOM   2757 C CB   A ALA   A 1 129 ? 15.078 -3.412  -2.095  0.60 13.09 ?  129 ALA   A CB   1 
ATOM   2758 C CB   B ALA   A 1 129 ? 15.016 -3.647  -2.499  0.40 13.20 ?  129 ALA   A CB   1 
ATOM   2759 H H    A ALA   A 1 129 ? 17.472 -3.628  -2.610  0.60 14.30 ?  129 ALA   A H    1 
ATOM   2760 H H    B ALA   A 1 129 ? 17.491 -3.630  -2.798  0.40 14.58 ?  129 ALA   A H    1 
ATOM   2761 H HA   A ALA   A 1 129 ? 15.323 -3.199  -4.117  0.60 14.61 ?  129 ALA   A HA   1 
ATOM   2762 H HA   B ALA   A 1 129 ? 15.426 -3.257  -4.454  0.40 14.98 ?  129 ALA   A HA   1 
ATOM   2763 H HB1  A ALA   A 1 129 ? 14.166 -3.079  -2.095  0.60 15.69 ?  129 ALA   A HB1  1 
ATOM   2764 H HB1  B ALA   A 1 129 ? 14.107 -3.320  -2.528  0.40 15.83 ?  129 ALA   A HB1  1 
ATOM   2765 H HB2  A ALA   A 1 129 ? 15.073 -4.383  -2.121  0.60 15.69 ?  129 ALA   A HB2  1 
ATOM   2766 H HB2  B ALA   A 1 129 ? 15.025 -4.612  -2.634  0.40 15.83 ?  129 ALA   A HB2  1 
ATOM   2767 H HB3  A ALA   A 1 129 ? 15.543 -3.105  -1.302  0.60 15.69 ?  129 ALA   A HB3  1 
ATOM   2768 H HB3  B ALA   A 1 129 ? 15.422 -3.435  -1.643  0.40 15.83 ?  129 ALA   A HB3  1 
ATOM   2769 N N    A GLY   A 1 130 ? 14.616 -0.773  -3.253  0.60 13.13 ?  130 GLY   A N    1 
ATOM   2770 N N    B GLY   A 1 130 ? 14.636 -0.849  -3.510  0.40 13.07 ?  130 GLY   A N    1 
ATOM   2771 C CA   A GLY   A 1 130 ? 14.500 0.676   -3.250  0.60 13.35 ?  130 GLY   A CA   1 
ATOM   2772 C CA   B GLY   A 1 130 ? 14.558 0.602   -3.437  0.40 13.58 ?  130 GLY   A CA   1 
ATOM   2773 C C    A GLY   A 1 130 ? 15.129 1.277   -4.483  0.60 12.75 ?  130 GLY   A C    1 
ATOM   2774 C C    B GLY   A 1 130 ? 15.120 1.239   -4.693  0.40 13.17 ?  130 GLY   A C    1 
ATOM   2775 O O    A GLY   A 1 130 ? 14.883 0.833   -5.609  0.60 13.05 ?  130 GLY   A O    1 
ATOM   2776 O O    B GLY   A 1 130 ? 14.846 0.800   -5.815  0.40 13.53 ?  130 GLY   A O    1 
ATOM   2777 H H    A GLY   A 1 130 ? 13.867 -1.196  -3.167  0.60 15.74 ?  130 GLY   A H    1 
ATOM   2778 H H    B GLY   A 1 130 ? 13.876 -1.250  -3.525  0.40 15.67 ?  130 GLY   A H    1 
ATOM   2779 H HA2  A GLY   A 1 130 ? 13.561 0.926   -3.233  0.60 16.00 ?  130 GLY   A HA2  1 
ATOM   2780 H HA2  B GLY   A 1 130 ? 13.627 0.874   -3.313  0.40 16.29 ?  130 GLY   A HA2  1 
ATOM   2781 H HA3  A GLY   A 1 130 ? 14.936 1.040   -2.469  0.60 16.00 ?  130 GLY   A HA3  1 
ATOM   2782 H HA3  B GLY   A 1 130 ? 15.070 0.917   -2.679  0.40 16.29 ?  130 GLY   A HA3  1 
ATOM   2783 N N    A ILE   A 1 131 ? 15.973 2.294   -4.278  0.60 12.83 ?  131 ILE   A N    1 
ATOM   2784 N N    B ILE   A 1 131 ? 15.935 2.284   -4.511  0.40 13.09 ?  131 ILE   A N    1 
ATOM   2785 C CA   A ILE   A 1 131 ? 16.528 3.052   -5.396  0.60 12.62 ?  131 ILE   A CA   1 
ATOM   2786 C CA   B ILE   A 1 131 ? 16.477 3.029   -5.648  0.40 13.10 ?  131 ILE   A CA   1 
ATOM   2787 C C    A ILE   A 1 131 ? 17.509 2.257   -6.244  0.60 12.00 ?  131 ILE   A C    1 
ATOM   2788 C C    B ILE   A 1 131 ? 17.583 2.273   -6.386  0.40 13.29 ?  131 ILE   A C    1 
ATOM   2789 O O    A ILE   A 1 131 ? 17.857 2.711   -7.341  0.60 12.67 ?  131 ILE   A O    1 
ATOM   2790 O O    B ILE   A 1 131 ? 18.170 2.810   -7.333  0.40 13.51 ?  131 ILE   A O    1 
ATOM   2791 C CB   A ILE   A 1 131 ? 17.126 4.411   -4.969  0.60 13.28 ?  131 ILE   A CB   1 
ATOM   2792 C CB   B ILE   A 1 131 ? 16.900 4.470   -5.282  0.40 13.66 ?  131 ILE   A CB   1 
ATOM   2793 C CG1  A ILE   A 1 131 ? 18.389 4.233   -4.119  0.60 15.09 ?  131 ILE   A CG1  1 
ATOM   2794 C CG1  B ILE   A 1 131 ? 18.088 4.488   -4.317  0.40 14.21 ?  131 ILE   A CG1  1 
ATOM   2795 C CG2  A ILE   A 1 131 ? 16.081 5.245   -4.236  0.60 13.67 ?  131 ILE   A CG2  1 
ATOM   2796 C CG2  B ILE   A 1 131 ? 15.718 5.243   -4.687  0.40 13.33 ?  131 ILE   A CG2  1 
ATOM   2797 C CD1  A ILE   A 1 131 ? 19.091 5.552   -3.783  0.60 16.41 ?  131 ILE   A CD1  1 
ATOM   2798 C CD1  B ILE   A 1 131 ? 18.564 5.894   -3.951  0.40 14.75 ?  131 ILE   A CD1  1 
ATOM   2799 H H    A ILE   A 1 131 ? 16.229 2.557   -3.501  0.60 15.38 ?  131 ILE   A H    1 
ATOM   2800 H H    B ILE   A 1 131 ? 16.167 2.590   -3.739  0.40 15.69 ?  131 ILE   A H    1 
ATOM   2801 H HA   A ILE   A 1 131 ? 15.788 3.261   -5.978  0.60 15.13 ?  131 ILE   A HA   1 
ATOM   2802 H HA   B ILE   A 1 131 ? 15.758 3.131   -6.273  0.40 15.71 ?  131 ILE   A HA   1 
ATOM   2803 H HB   A ILE   A 1 131 ? 17.370 4.892   -5.774  0.60 15.92 ?  131 ILE   A HB   1 
ATOM   2804 H HB   B ILE   A 1 131 ? 17.171 4.920   -6.104  0.40 16.38 ?  131 ILE   A HB   1 
ATOM   2805 H HG12 A ILE   A 1 131 ? 18.149 3.804   -3.285  0.60 18.10 ?  131 ILE   A HG12 1 
ATOM   2806 H HG12 B ILE   A 1 131 ? 17.832 4.040   -3.497  0.40 17.04 ?  131 ILE   A HG12 1 
ATOM   2807 H HG13 A ILE   A 1 131 ? 19.022 3.683   -4.604  0.60 18.10 ?  131 ILE   A HG13 1 
ATOM   2808 H HG13 B ILE   A 1 131 ? 18.836 4.024   -4.727  0.40 17.04 ?  131 ILE   A HG13 1 
ATOM   2809 H HG21 A ILE   A 1 131 ? 16.420 6.146   -4.115  0.60 16.39 ?  131 ILE   A HG21 1 
ATOM   2810 H HG21 B ILE   A 1 131 ? 15.963 6.177   -4.581  0.40 15.98 ?  131 ILE   A HG21 1 
ATOM   2811 H HG22 A ILE   A 1 131 ? 15.268 5.268   -4.766  0.60 16.39 ?  131 ILE   A HG22 1 
ATOM   2812 H HG22 B ILE   A 1 131 ? 14.958 5.174   -5.285  0.40 15.98 ?  131 ILE   A HG22 1 
ATOM   2813 H HG23 A ILE   A 1 131 ? 15.901 4.840   -3.374  0.60 16.39 ?  131 ILE   A HG23 1 
ATOM   2814 H HG23 B ILE   A 1 131 ? 15.493 4.861   -3.825  0.40 15.98 ?  131 ILE   A HG23 1 
ATOM   2815 H HD11 A ILE   A 1 131 ? 19.935 5.359   -3.346  0.60 19.68 ?  131 ILE   A HD11 1 
ATOM   2816 H HD11 B ILE   A 1 131 ? 19.419 5.832   -3.500  0.40 17.68 ?  131 ILE   A HD11 1 
ATOM   2817 H HD12 A ILE   A 1 131 ? 19.250 6.045   -4.604  0.60 19.68 ?  131 ILE   A HD12 1 
ATOM   2818 H HD12 B ILE   A 1 131 ? 18.653 6.417   -4.762  0.40 17.68 ?  131 ILE   A HD12 1 
ATOM   2819 H HD13 A ILE   A 1 131 ? 18.524 6.073   -3.192  0.60 19.68 ?  131 ILE   A HD13 1 
ATOM   2820 H HD13 B ILE   A 1 131 ? 17.909 6.305   -3.363  0.40 17.68 ?  131 ILE   A HD13 1 
ATOM   2821 N N    A PHE   A 1 132 ? 17.957 1.082   -5.785  0.60 11.38 ?  132 PHE   A N    1 
ATOM   2822 N N    B PHE   A 1 132 ? 17.873 1.025   -5.983  0.40 13.33 ?  132 PHE   A N    1 
ATOM   2823 C CA   A PHE   A 1 132 ? 18.774 0.222   -6.635  0.60 11.61 ?  132 PHE   A CA   1 
ATOM   2824 C CA   B PHE   A 1 132 ? 18.783 0.182   -6.759  0.40 13.84 ?  132 PHE   A CA   1 
ATOM   2825 C C    A PHE   A 1 132 ? 17.947 -0.541  -7.672  0.60 12.14 ?  132 PHE   A C    1 
ATOM   2826 C C    B PHE   A 1 132 ? 18.088 -0.552  -7.902  0.40 14.60 ?  132 PHE   A C    1 
ATOM   2827 O O    A PHE   A 1 132 ? 18.529 -1.218  -8.527  0.60 12.91 ?  132 PHE   A O    1 
ATOM   2828 O O    B PHE   A 1 132 ? 18.772 -1.111  -8.767  0.40 15.56 ?  132 PHE   A O    1 
ATOM   2829 C CB   A PHE   A 1 132 ? 19.608 -0.763  -5.804  0.60 11.05 ?  132 PHE   A CB   1 
ATOM   2830 C CB   B PHE   A 1 132 ? 19.514 -0.821  -5.859  0.40 13.51 ?  132 PHE   A CB   1 
ATOM   2831 C CG   A PHE   A 1 132 ? 20.839 -0.160  -5.144  0.60 11.32 ?  132 PHE   A CG   1 
ATOM   2832 C CG   B PHE   A 1 132 ? 20.742 -0.262  -5.187  0.40 13.60 ?  132 PHE   A CG   1 
ATOM   2833 C CD1  A PHE   A 1 132 ? 20.730 0.864   -4.217  0.60 12.58 ?  132 PHE   A CD1  1 
ATOM   2834 C CD1  B PHE   A 1 132 ? 20.655 0.823   -4.331  0.40 14.05 ?  132 PHE   A CD1  1 
ATOM   2835 C CD2  A PHE   A 1 132 ? 22.100 -0.682  -5.410  0.60 11.90 ?  132 PHE   A CD2  1 
ATOM   2836 C CD2  B PHE   A 1 132 ? 21.980 -0.850  -5.390  0.40 13.64 ?  132 PHE   A CD2  1 
ATOM   2837 C CE1  A PHE   A 1 132 ? 21.857 1.384   -3.599  0.60 12.91 ?  132 PHE   A CE1  1 
ATOM   2838 C CE1  B PHE   A 1 132 ? 21.784 1.325   -3.706  0.40 14.18 ?  132 PHE   A CE1  1 
ATOM   2839 C CE2  A PHE   A 1 132 ? 23.230 -0.164  -4.796  0.60 12.62 ?  132 PHE   A CE2  1 
ATOM   2840 C CE2  B PHE   A 1 132 ? 23.111 -0.354  -4.769  0.40 13.71 ?  132 PHE   A CE2  1 
ATOM   2841 C CZ   A PHE   A 1 132 ? 23.105 0.870   -3.889  0.60 12.65 ?  132 PHE   A CZ   1 
ATOM   2842 C CZ   B PHE   A 1 132 ? 23.012 0.735   -3.926  0.40 13.71 ?  132 PHE   A CZ   1 
ATOM   2843 H H    A PHE   A 1 132 ? 17.799 0.771   -4.999  0.60 13.65 ?  132 PHE   A H    1 
ATOM   2844 H H    B PHE   A 1 132 ? 17.574 0.645   -5.267  0.40 15.99 ?  132 PHE   A H    1 
ATOM   2845 H HA   A PHE   A 1 132 ? 19.394 0.787   -7.118  0.60 13.92 ?  132 PHE   A HA   1 
ATOM   2846 H HA   B PHE   A 1 132 ? 19.460 0.746   -7.157  0.40 16.59 ?  132 PHE   A HA   1 
ATOM   2847 H HB2  A PHE   A 1 132 ? 19.047 -1.122  -5.099  0.60 13.24 ?  132 PHE   A HB2  1 
ATOM   2848 H HB2  B PHE   A 1 132 ? 18.913 -1.118  -5.161  0.40 16.19 ?  132 PHE   A HB2  1 
ATOM   2849 H HB3  A PHE   A 1 132 ? 19.902 -1.486  -6.385  0.60 13.24 ?  132 PHE   A HB3  1 
ATOM   2850 H HB3  B PHE   A 1 132 ? 19.796 -1.585  -6.394  0.40 16.19 ?  132 PHE   A HB3  1 
ATOM   2851 H HD1  A PHE   A 1 132 ? 19.896 1.211   -4.019  0.60 15.08 ?  132 PHE   A HD1  1 
ATOM   2852 H HD1  B PHE   A 1 132 ? 19.833 1.224   -4.180  0.40 16.85 ?  132 PHE   A HD1  1 
ATOM   2853 H HD2  A PHE   A 1 132 ? 22.196 -1.380  -6.024  0.60 14.27 ?  132 PHE   A HD2  1 
ATOM   2854 H HD2  B PHE   A 1 132 ? 22.058 -1.584  -5.959  0.40 16.35 ?  132 PHE   A HD2  1 
ATOM   2855 H HE1  A PHE   A 1 132 ? 21.778 2.078   -2.989  0.60 15.48 ?  132 PHE   A HE1  1 
ATOM   2856 H HE1  B PHE   A 1 132 ? 21.720 2.058   -3.138  0.40 17.00 ?  132 PHE   A HE1  1 
ATOM   2857 H HE2  A PHE   A 1 132 ? 24.074 -0.514  -4.997  0.60 15.13 ?  132 PHE   A HE2  1 
ATOM   2858 H HE2  B PHE   A 1 132 ? 23.939 -0.755  -4.922  0.40 16.44 ?  132 PHE   A HE2  1 
ATOM   2859 H HZ   A PHE   A 1 132 ? 23.866 1.220   -3.477  0.60 15.17 ?  132 PHE   A HZ   1 
ATOM   2860 H HZ   B PHE   A 1 132 ? 23.773 1.071   -3.509  0.40 16.44 ?  132 PHE   A HZ   1 
ATOM   2861 N N    A GLY   A 1 133 ? 16.615 -0.474  -7.605  0.60 12.11 ?  133 GLY   A N    1 
ATOM   2862 N N    B GLY   A 1 133 ? 16.758 -0.588  -7.917  0.40 14.33 ?  133 GLY   A N    1 
ATOM   2863 C CA   A GLY   A 1 133 ? 15.771 -0.833  -8.729  0.60 12.76 ?  133 GLY   A CA   1 
ATOM   2864 C CA   B GLY   A 1 133 ? 16.017 -0.946  -9.107  0.40 14.26 ?  133 GLY   A CA   1 
ATOM   2865 C C    A GLY   A 1 133 ? 15.416 -2.295  -8.903  0.60 12.94 ?  133 GLY   A C    1 
ATOM   2866 C C    B GLY   A 1 133 ? 15.626 -2.400  -9.271  0.40 14.30 ?  133 GLY   A C    1 
ATOM   2867 O O    A GLY   A 1 133 ? 14.673 -2.611  -9.840  0.60 14.26 ?  133 GLY   A O    1 
ATOM   2868 O O    B GLY   A 1 133 ? 15.015 -2.734  -10.293 0.40 14.43 ?  133 GLY   A O    1 
ATOM   2869 H H    A GLY   A 1 133 ? 16.171 -0.219  -6.911  0.60 14.52 ?  133 GLY   A H    1 
ATOM   2870 H H    B GLY   A 1 133 ? 16.268 -0.404  -7.236  0.40 17.18 ?  133 GLY   A H    1 
ATOM   2871 H HA2  A GLY   A 1 133 ? 14.930 -0.356  -8.652  0.60 15.30 ?  133 GLY   A HA2  1 
ATOM   2872 H HA2  B GLY   A 1 133 ? 15.209 -0.414  -9.125  0.40 17.10 ?  133 GLY   A HA2  1 
ATOM   2873 H HA3  A GLY   A 1 133 ? 16.201 -0.539  -9.547  0.60 15.30 ?  133 GLY   A HA3  1 
ATOM   2874 H HA3  B GLY   A 1 133 ? 16.549 -0.708  -9.879  0.40 17.10 ?  133 GLY   A HA3  1 
ATOM   2875 N N    A ALA   A 1 134 ? 15.913 -3.198  -8.060  0.60 13.22 ?  134 ALA   A N    1 
ATOM   2876 N N    B ALA   A 1 134 ? 15.966 -3.279  -8.331  0.40 14.01 ?  134 ALA   A N    1 
ATOM   2877 C CA   A ALA   A 1 134 ? 15.579 -4.603  -8.228  0.60 14.06 ?  134 ALA   A CA   1 
ATOM   2878 C CA   B ALA   A 1 134 ? 15.586 -4.678  -8.460  0.40 14.38 ?  134 ALA   A CA   1 
ATOM   2879 C C    A ALA   A 1 134 ? 14.219 -4.908  -7.599  0.60 14.75 ?  134 ALA   A C    1 
ATOM   2880 C C    B ALA   A 1 134 ? 14.272 -4.949  -7.731  0.40 14.74 ?  134 ALA   A C    1 
ATOM   2881 O O    A ALA   A 1 134 ? 13.670 -4.126  -6.818  0.60 15.58 ?  134 ALA   A O    1 
ATOM   2882 O O    B ALA   A 1 134 ? 13.804 -4.147  -6.918  0.40 15.71 ?  134 ALA   A O    1 
ATOM   2883 C CB   A ALA   A 1 134 ? 16.661 -5.501  -7.623  0.60 14.86 ?  134 ALA   A CB   1 
ATOM   2884 C CB   B ALA   A 1 134 ? 16.686 -5.598  -7.930  0.40 14.67 ?  134 ALA   A CB   1 
ATOM   2885 H H    A ALA   A 1 134 ? 16.440 -3.023  -7.399  0.60 15.86 ?  134 ALA   A H    1 
ATOM   2886 H H    B ALA   A 1 134 ? 16.424 -3.093  -7.620  0.40 16.80 ?  134 ALA   A H    1 
ATOM   2887 H HA   A ALA   A 1 134 ? 15.529 -4.801  -9.177  0.60 16.86 ?  134 ALA   A HA   1 
ATOM   2888 H HA   B ALA   A 1 134 ? 15.455 -4.882  -9.397  0.40 17.25 ?  134 ALA   A HA   1 
ATOM   2889 H HB1  A ALA   A 1 134 ? 16.419 -6.427  -7.769  0.60 17.81 ?  134 ALA   A HB1  1 
ATOM   2890 H HB1  B ALA   A 1 134 ? 16.417 -6.519  -8.061  0.40 17.59 ?  134 ALA   A HB1  1 
ATOM   2891 H HB2  A ALA   A 1 134 ? 17.510 -5.309  -8.061  0.60 17.81 ?  134 ALA   A HB2  1 
ATOM   2892 H HB2  B ALA   A 1 134 ? 17.507 -5.421  -8.420  0.40 17.59 ?  134 ALA   A HB2  1 
ATOM   2893 H HB3  A ALA   A 1 134 ? 16.732 -5.317  -6.676  0.60 17.81 ?  134 ALA   A HB3  1 
ATOM   2894 H HB3  B ALA   A 1 134 ? 16.821 -5.421  -6.987  0.40 17.59 ?  134 ALA   A HB3  1 
ATOM   2895 N N    A ASP   A 1 135 ? 13.675 -6.059  -7.967  0.60 15.93 ?  135 ASP   A N    1 
ATOM   2896 N N    B ASP   A 1 135 ? 13.674 -6.098  -8.040  0.40 15.19 ?  135 ASP   A N    1 
ATOM   2897 C CA   A ASP   A 1 135 ? 12.423 -6.573  -7.416  0.60 17.12 ?  135 ASP   A CA   1 
ATOM   2898 C CA   B ASP   A 1 135 ? 12.415 -6.483  -7.409  0.40 15.99 ?  135 ASP   A CA   1 
ATOM   2899 C C    A ASP   A 1 135 ? 12.656 -7.008  -5.974  0.60 16.49 ?  135 ASP   A C    1 
ATOM   2900 C C    B ASP   A 1 135 ? 12.683 -6.958  -5.985  0.40 15.84 ?  135 ASP   A C    1 
ATOM   2901 O O    A ASP   A 1 135 ? 13.403 -7.971  -5.754  0.60 16.29 ?  135 ASP   A O    1 
ATOM   2902 O O    B ASP   A 1 135 ? 13.465 -7.896  -5.794  0.40 15.49 ?  135 ASP   A O    1 
ATOM   2903 C CB   A ASP   A 1 135 ? 12.010 -7.777  -8.270  0.60 19.27 ?  135 ASP   A CB   1 
ATOM   2904 C CB   B ASP   A 1 135 ? 11.734 -7.589  -8.208  0.40 17.33 ?  135 ASP   A CB   1 
ATOM   2905 C CG   A ASP   A 1 135 ? 10.766 -8.499  -7.745  0.60 21.35 ?  135 ASP   A CG   1 
ATOM   2906 C CG   B ASP   A 1 135 ? 10.341 -7.927  -7.686  0.40 18.68 ?  135 ASP   A CG   1 
ATOM   2907 O OD1  A ASP   A 1 135 ? 10.148 -8.049  -6.757  0.60 21.24 ?  135 ASP   A OD1  1 
ATOM   2908 O OD1  B ASP   A 1 135 ? 9.972  -7.473  -6.580  0.40 19.00 ?  135 ASP   A OD1  1 
ATOM   2909 O OD2  A ASP   A 1 135 ? 10.408 -9.538  -8.337  0.60 23.60 -1 135 ASP   A OD2  1 
ATOM   2910 O OD2  B ASP   A 1 135 ? 9.608  -8.649  -8.394  0.40 19.76 -1 135 ASP   A OD2  1 
ATOM   2911 H H    A ASP   A 1 135 ? 14.020 -6.579  -8.556  0.60 19.11 ?  135 ASP   A H    1 
ATOM   2912 H H    B ASP   A 1 135 ? 13.972 -6.669  -8.610  0.40 18.21 ?  135 ASP   A H    1 
ATOM   2913 H HA   A ASP   A 1 135 ? 11.728 -5.895  -7.458  0.60 20.53 ?  135 ASP   A HA   1 
ATOM   2914 H HA   B ASP   A 1 135 ? 11.824 -5.718  -7.393  0.40 19.17 ?  135 ASP   A HA   1 
ATOM   2915 H HB2  A ASP   A 1 135 ? 11.825 -7.474  -9.173  0.60 23.11 ?  135 ASP   A HB2  1 
ATOM   2916 H HB2  B ASP   A 1 135 ? 11.646 -7.305  -9.130  0.40 20.79 ?  135 ASP   A HB2  1 
ATOM   2917 H HB3  A ASP   A 1 135 ? 12.740 -8.417  -8.281  0.60 23.11 ?  135 ASP   A HB3  1 
ATOM   2918 H HB3  B ASP   A 1 135 ? 12.271 -8.395  -8.159  0.40 20.79 ?  135 ASP   A HB3  1 
ATOM   2919 N N    . PRO   A 1 136 ? 12.074 -6.342  -4.968  1.00 16.24 ?  136 PRO   A N    1 
ATOM   2920 C CA   . PRO   A 1 136 ? 12.332 -6.773  -3.580  1.00 16.24 ?  136 PRO   A CA   1 
ATOM   2921 C C    . PRO   A 1 136 ? 11.903 -8.200  -3.278  1.00 15.55 ?  136 PRO   A C    1 
ATOM   2922 O O    . PRO   A 1 136 ? 12.502 -8.845  -2.408  1.00 15.18 ?  136 PRO   A O    1 
ATOM   2923 C CB   . PRO   A 1 136 ? 11.559 -5.744  -2.743  1.00 17.50 ?  136 PRO   A CB   1 
ATOM   2924 C CG   . PRO   A 1 136 ? 10.533 -5.182  -3.681  1.00 19.24 ?  136 PRO   A CG   1 
ATOM   2925 C CD   . PRO   A 1 136 ? 11.173 -5.178  -5.025  1.00 17.69 ?  136 PRO   A CD   1 
ATOM   2926 H HA   . PRO   A 1 136 ? 13.281 -6.686  -3.375  1.00 19.47 ?  136 PRO   A HA   1 
ATOM   2927 H HB2  . PRO   A 1 136 ? 11.132 -6.185  -1.993  1.00 20.99 ?  136 PRO   A HB2  1 
ATOM   2928 H HB3  . PRO   A 1 136 ? 12.163 -5.048  -2.436  1.00 20.99 ?  136 PRO   A HB3  1 
ATOM   2929 H HG2  . PRO   A 1 136 ? 9.751  -5.750  -3.687  1.00 23.08 ?  136 PRO   A HG2  1 
ATOM   2930 H HG3  . PRO   A 1 136 ? 10.306 -4.280  -3.416  1.00 23.08 ?  136 PRO   A HG3  1 
ATOM   2931 H HD2  . PRO   A 1 136 ? 10.501 -5.303  -5.716  1.00 21.22 ?  136 PRO   A HD2  1 
ATOM   2932 H HD3  . PRO   A 1 136 ? 11.677 -4.358  -5.168  1.00 21.22 ?  136 PRO   A HD3  1 
ATOM   2933 N N    A ILE   A 1 137 ? 10.871 -8.711  -3.953  0.60 15.88 ?  137 ILE   A N    1 
ATOM   2934 N N    B ILE   A 1 137 ? 10.874 -8.711  -3.957  0.40 15.84 ?  137 ILE   A N    1 
ATOM   2935 C CA   A ILE   A 1 137 ? 10.487 -10.107 -3.761  0.60 16.33 ?  137 ILE   A CA   1 
ATOM   2936 C CA   B ILE   A 1 137 ? 10.481 -10.104 -3.765  0.40 16.22 ?  137 ILE   A CA   1 
ATOM   2937 C C    A ILE   A 1 137 ? 11.631 -11.023 -4.171  0.60 15.62 ?  137 ILE   A C    1 
ATOM   2938 C C    B ILE   A 1 137 ? 11.614 -11.032 -4.183  0.40 15.68 ?  137 ILE   A C    1 
ATOM   2939 O O    A ILE   A 1 137 ? 11.937 -12.011 -3.489  0.60 15.84 ?  137 ILE   A O    1 
ATOM   2940 O O    B ILE   A 1 137 ? 11.901 -12.034 -3.513  0.40 15.82 ?  137 ILE   A O    1 
ATOM   2941 C CB   A ILE   A 1 137 ? 9.194  -10.421 -4.538  0.60 17.52 ?  137 ILE   A CB   1 
ATOM   2942 C CB   B ILE   A 1 137 ? 9.178  -10.400 -4.533  0.40 17.18 ?  137 ILE   A CB   1 
ATOM   2943 C CG1  A ILE   A 1 137 ? 8.014  -9.620  -3.974  0.60 19.40 ?  137 ILE   A CG1  1 
ATOM   2944 C CG1  B ILE   A 1 137 ? 8.042  -9.497  -4.034  0.40 18.55 ?  137 ILE   A CG1  1 
ATOM   2945 C CG2  A ILE   A 1 137 ? 8.893  -11.917 -4.500  0.60 17.96 ?  137 ILE   A CG2  1 
ATOM   2946 C CG2  B ILE   A 1 137 ? 8.802  -11.870 -4.399  0.40 17.52 ?  137 ILE   A CG2  1 
ATOM   2947 C CD1  A ILE   A 1 137 ? 6.720  -9.824  -4.732  0.60 20.87 ?  137 ILE   A CD1  1 
ATOM   2948 C CD1  B ILE   A 1 137 ? 6.751  -9.632  -4.820  0.40 19.48 ?  137 ILE   A CD1  1 
ATOM   2949 H H    A ILE   A 1 137 ? 10.391 -8.276  -4.517  0.60 19.05 ?  137 ILE   A H    1 
ATOM   2950 H H    B ILE   A 1 137 ? 10.395 -8.275  -4.522  0.40 19.00 ?  137 ILE   A H    1 
ATOM   2951 H HA   A ILE   A 1 137 ? 10.314 -10.257 -2.823  0.60 19.58 ?  137 ILE   A HA   1 
ATOM   2952 H HA   B ILE   A 1 137 ? 10.313 -10.254 -2.824  0.40 19.45 ?  137 ILE   A HA   1 
ATOM   2953 H HB   A ILE   A 1 137 ? 9.317  -10.157 -5.460  0.60 21.01 ?  137 ILE   A HB   1 
ATOM   2954 H HB   B ILE   A 1 137 ? 9.327  -10.209 -5.470  0.40 20.60 ?  137 ILE   A HB   1 
ATOM   2955 H HG12 A ILE   A 1 137 ? 7.864  -9.882  -3.052  0.60 23.26 ?  137 ILE   A HG12 1 
ATOM   2956 H HG12 B ILE   A 1 137 ? 7.852  -9.717  -3.109  0.40 22.25 ?  137 ILE   A HG12 1 
ATOM   2957 H HG13 A ILE   A 1 137 ? 8.231  -8.670  -4.011  0.60 23.26 ?  137 ILE   A HG13 1 
ATOM   2958 H HG13 B ILE   A 1 137 ? 8.328  -8.571  -4.097  0.40 22.25 ?  137 ILE   A HG13 1 
ATOM   2959 H HG21 A ILE   A 1 137 ? 8.136  -12.106 -5.072  0.60 21.54 ?  137 ILE   A HG21 1 
ATOM   2960 H HG21 B ILE   A 1 137 ? 7.947  -12.020 -4.830  0.40 21.02 ?  137 ILE   A HG21 1 
ATOM   2961 H HG22 A ILE   A 1 137 ? 9.657  -12.410 -4.822  0.60 21.54 ?  137 ILE   A HG22 1 
ATOM   2962 H HG22 B ILE   A 1 137 ? 9.481  -12.413 -4.827  0.40 21.02 ?  137 ILE   A HG22 1 
ATOM   2963 H HG23 A ILE   A 1 137 ? 8.691  -12.170 -3.587  0.60 21.54 ?  137 ILE   A HG23 1 
ATOM   2964 H HG23 B ILE   A 1 137 ? 8.742  -12.094 -3.458  0.40 21.02 ?  137 ILE   A HG23 1 
ATOM   2965 H HD11 A ILE   A 1 137 ? 5.998  -9.531  -4.165  0.60 25.03 ?  137 ILE   A HD11 1 
ATOM   2966 H HD11 B ILE   A 1 137 ? 6.141  -8.933  -4.544  0.40 23.36 ?  137 ILE   A HD11 1 
ATOM   2967 H HD12 A ILE   A 1 137 ? 6.743  -9.301  -5.549  0.60 25.03 ?  137 ILE   A HD12 1 
ATOM   2968 H HD12 B ILE   A 1 137 ? 6.947  -9.549  -5.767  0.40 23.36 ?  137 ILE   A HD12 1 
ATOM   2969 H HD13 A ILE   A 1 137 ? 6.595  -10.762 -4.943  0.60 25.03 ?  137 ILE   A HD13 1 
ATOM   2970 H HD13 B ILE   A 1 137 ? 6.359  -10.502 -4.640  0.40 23.36 ?  137 ILE   A HD13 1 
ATOM   2971 N N    . HIS   A 1 138 ? 12.267 -10.717 -5.303  1.00 15.76 ?  138 HIS   A N    1 
ATOM   2972 C CA   . HIS   A 1 138 ? 13.425 -11.491 -5.737  1.00 15.05 ?  138 HIS   A CA   1 
ATOM   2973 C C    . HIS   A 1 138 ? 14.578 -11.360 -4.750  1.00 14.24 ?  138 HIS   A C    1 
ATOM   2974 O O    . HIS   A 1 138 ? 15.240 -12.353 -4.420  1.00 14.87 ?  138 HIS   A O    1 
ATOM   2975 C CB   . HIS   A 1 138 ? 13.832 -11.043 -7.140  1.00 15.90 ?  138 HIS   A CB   1 
ATOM   2976 C CG   . HIS   A 1 138 ? 15.099 -11.672 -7.622  1.00 16.86 ?  138 HIS   A CG   1 
ATOM   2977 N ND1  . HIS   A 1 138 ? 15.210 -13.022 -7.877  1.00 18.21 ?  138 HIS   A ND1  1 
ATOM   2978 C CD2  . HIS   A 1 138 ? 16.317 -11.139 -7.878  1.00 17.20 ?  138 HIS   A CD2  1 
ATOM   2979 C CE1  . HIS   A 1 138 ? 16.441 -13.292 -8.277  1.00 18.64 ?  138 HIS   A CE1  1 
ATOM   2980 N NE2  . HIS   A 1 138 ? 17.133 -12.166 -8.287  1.00 17.88 ?  138 HIS   A NE2  1 
ATOM   2981 H H    A HIS   A 1 138 ? 12.055 -10.066 -5.831  0.60 18.90 ?  138 HIS   A H    1 
ATOM   2982 H H    B HIS   A 1 138 ? 12.061 -10.062 -5.827  0.40 18.90 ?  138 HIS   A H    1 
ATOM   2983 H HA   . HIS   A 1 138 ? 13.176 -12.422 -5.788  1.00 18.05 ?  138 HIS   A HA   1 
ATOM   2984 H HB2  . HIS   A 1 138 ? 13.126 -11.283 -7.766  1.00 19.07 ?  138 HIS   A HB2  1 
ATOM   2985 H HB3  . HIS   A 1 138 ? 13.958 -10.081 -7.146  1.00 19.07 ?  138 HIS   A HB3  1 
ATOM   2986 H HD1  . HIS   A 1 138 ? 14.575 -13.599 -7.793  1.00 21.84 ?  138 HIS   A HD1  1 
ATOM   2987 H HD2  . HIS   A 1 138 ? 16.555 -10.244 -7.796  1.00 20.62 ?  138 HIS   A HD2  1 
ATOM   2988 H HE1  . HIS   A 1 138 ? 16.763 -14.132 -8.512  1.00 22.35 ?  138 HIS   A HE1  1 
ATOM   2989 N N    . SER   A 1 139 ? 14.827 -10.146 -4.257  1.00 13.91 ?  139 SER   A N    1 
ATOM   2990 C CA   . SER   A 1 139 ? 15.907 -9.958  -3.299  1.00 13.69 ?  139 SER   A CA   1 
ATOM   2991 C C    . SER   A 1 139 ? 15.698 -10.813 -2.054  1.00 13.31 ?  139 SER   A C    1 
ATOM   2992 O O    . SER   A 1 139 ? 16.651 -11.413 -1.540  1.00 13.39 ?  139 SER   A O    1 
ATOM   2993 C CB   . SER   A 1 139 ? 16.039 -8.478  -2.941  1.00 13.72 ?  139 SER   A CB   1 
ATOM   2994 O OG   . SER   A 1 139 ? 17.141 -8.322  -2.071  1.00 13.94 ?  139 SER   A OG   1 
ATOM   2995 H H    . SER   A 1 139 ? 14.391 -9.430  -4.456  1.00 16.69 ?  139 SER   A H    1 
ATOM   2996 H HA   . SER   A 1 139 ? 16.740 -10.228 -3.708  1.00 16.41 ?  139 SER   A HA   1 
ATOM   2997 H HB2  . SER   A 1 139 ? 16.186 -7.953  -3.747  1.00 16.45 ?  139 SER   A HB2  1 
ATOM   2998 H HB3  . SER   A 1 139 ? 15.230 -8.173  -2.491  1.00 16.45 ?  139 SER   A HB3  1 
ATOM   2999 H HG   . SER   A 1 139 ? 17.235 -7.511  -1.860  1.00 16.72 ?  139 SER   A HG   1 
ATOM   3000 N N    . LEU   A 1 140 ? 14.460 -10.876 -1.553  1.00 13.36 ?  140 LEU   A N    1 
ATOM   3001 C CA   . LEU   A 1 140 ? 14.187 -11.695 -0.376  1.00 13.61 ?  140 LEU   A CA   1 
ATOM   3002 C C    . LEU   A 1 140 ? 14.441 -13.171 -0.664  1.00 13.54 ?  140 LEU   A C    1 
ATOM   3003 O O    . LEU   A 1 140 ? 14.984 -13.895 0.181   1.00 14.22 ?  140 LEU   A O    1 
ATOM   3004 C CB   . LEU   A 1 140 ? 12.749 -11.462 0.093   1.00 14.27 ?  140 LEU   A CB   1 
ATOM   3005 C CG   . LEU   A 1 140 ? 12.288 -12.319 1.272   1.00 14.79 ?  140 LEU   A CG   1 
ATOM   3006 C CD1  . LEU   A 1 140 ? 13.205 -12.154 2.474   1.00 15.18 ?  140 LEU   A CD1  1 
ATOM   3007 C CD2  . LEU   A 1 140 ? 10.836 -12.001 1.642   1.00 15.65 ?  140 LEU   A CD2  1 
ATOM   3008 H H    . LEU   A 1 140 ? 13.779 -10.451 -1.863  1.00 16.02 ?  140 LEU   A H    1 
ATOM   3009 H HA   . LEU   A 1 140 ? 14.776 -11.427 0.341   1.00 16.32 ?  140 LEU   A HA   1 
ATOM   3010 H HB2  . LEU   A 1 140 ? 12.658 -10.537 0.358   1.00 17.12 ?  140 LEU   A HB2  1 
ATOM   3011 H HB3  . LEU   A 1 140 ? 12.151 -11.649 -0.648  1.00 17.12 ?  140 LEU   A HB3  1 
ATOM   3012 H HG   . LEU   A 1 140 ? 12.313 -13.254 1.009   1.00 17.73 ?  140 LEU   A HG   1 
ATOM   3013 H HD11 . LEU   A 1 140 ? 12.825 -12.631 3.229   1.00 18.21 ?  140 LEU   A HD11 1 
ATOM   3014 H HD12 . LEU   A 1 140 ? 14.076 -12.528 2.257   1.00 18.21 ?  140 LEU   A HD12 1 
ATOM   3015 H HD13 . LEU   A 1 140 ? 13.289 -11.214 2.681   1.00 18.21 ?  140 LEU   A HD13 1 
ATOM   3016 H HD21 . LEU   A 1 140 ? 10.568 -12.561 2.391   1.00 18.76 ?  140 LEU   A HD21 1 
ATOM   3017 H HD22 . LEU   A 1 140 ? 10.770 -11.066 1.892   1.00 18.76 ?  140 LEU   A HD22 1 
ATOM   3018 H HD23 . LEU   A 1 140 ? 10.265 -12.181 0.878   1.00 18.76 ?  140 LEU   A HD23 1 
ATOM   3019 N N    . ARG   A 1 141 ? 14.047 -13.632 -1.852  1.00 14.20 ?  141 ARG   A N    1 
ATOM   3020 C CA   . ARG   A 1 141 ? 14.286 -15.020 -2.234  1.00 15.56 ?  141 ARG   A CA   1 
ATOM   3021 C C    . ARG   A 1 141 ? 15.782 -15.333 -2.253  1.00 14.35 ?  141 ARG   A C    1 
ATOM   3022 O O    . ARG   A 1 141 ? 16.228 -16.349 -1.705  1.00 14.64 ?  141 ARG   A O    1 
ATOM   3023 C CB   . ARG   A 1 141 ? 13.658 -15.262 -3.608  1.00 17.34 ?  141 ARG   A CB   1 
ATOM   3024 C CG   . ARG   A 1 141 ? 13.641 -16.697 -4.060  1.00 19.97 ?  141 ARG   A CG   1 
ATOM   3025 C CD   . ARG   A 1 141 ? 12.601 -17.466 -3.300  1.00 21.79 ?  141 ARG   A CD   1 
ATOM   3026 N NE   . ARG   A 1 141 ? 13.204 -18.249 -2.236  1.00 22.37 ?  141 ARG   A NE   1 
ATOM   3027 C CZ   . ARG   A 1 141 ? 12.513 -18.822 -1.260  1.00 22.86 ?  141 ARG   A CZ   1 
ATOM   3028 N NH1  . ARG   A 1 141 ? 11.220 -18.593 -1.103  1.00 22.28 ?  141 ARG   A NH1  1 
ATOM   3029 N NH2  . ARG   A 1 141 ? 13.139 -19.632 -0.412  1.00 23.51 ?  141 ARG   A NH2  1 
ATOM   3030 H H    . ARG   A 1 141 ? 13.651 -13.162 -2.455  1.00 17.03 ?  141 ARG   A H    1 
ATOM   3031 H HA   . ARG   A 1 141 ? 13.860 -15.607 -1.593  1.00 18.66 ?  141 ARG   A HA   1 
ATOM   3032 H HB2  . ARG   A 1 141 ? 12.743 -14.940 -3.591  1.00 20.80 ?  141 ARG   A HB2  1 
ATOM   3033 H HB3  . ARG   A 1 141 ? 14.163 -14.756 -4.266  1.00 20.80 ?  141 ARG   A HB3  1 
ATOM   3034 H HG2  . ARG   A 1 141 ? 13.424 -16.739 -5.007  1.00 23.95 ?  141 ARG   A HG2  1 
ATOM   3035 H HG3  . ARG   A 1 141 ? 14.507 -17.106 -3.897  1.00 23.95 ?  141 ARG   A HG3  1 
ATOM   3036 H HD2  . ARG   A 1 141 ? 11.970 -16.848 -2.896  1.00 26.13 ?  141 ARG   A HD2  1 
ATOM   3037 H HD3  . ARG   A 1 141 ? 12.134 -18.066 -3.906  1.00 26.13 ?  141 ARG   A HD3  1 
ATOM   3038 H HE   . ARG   A 1 141 ? 14.032 -18.457 -2.312  1.00 26.83 ?  141 ARG   A HE   1 
ATOM   3039 H HH11 . ARG   A 1 141 ? 10.798 -18.083 -1.652  1.00 26.73 ?  141 ARG   A HH11 1 
ATOM   3040 H HH12 . ARG   A 1 141 ? 10.789 -18.974 -0.461  1.00 26.73 ?  141 ARG   A HH12 1 
ATOM   3041 H HH21 . ARG   A 1 141 ? 13.980 -19.784 -0.503  1.00 28.20 ?  141 ARG   A HH21 1 
ATOM   3042 H HH22 . ARG   A 1 141 ? 12.704 -20.001 0.234   1.00 28.20 ?  141 ARG   A HH22 1 
ATOM   3043 N N    . VAL   A 1 142 ? 16.576 -14.470 -2.889  1.00 13.56 ?  142 VAL   A N    1 
ATOM   3044 C CA   . VAL   A 1 142 ? 18.020 -14.687 -2.921  1.00 13.63 ?  142 VAL   A CA   1 
ATOM   3045 C C    . VAL   A 1 142 ? 18.588 -14.672 -1.510  1.00 12.78 ?  142 VAL   A C    1 
ATOM   3046 O O    . VAL   A 1 142 ? 19.458 -15.485 -1.168  1.00 13.35 ?  142 VAL   A O    1 
ATOM   3047 C CB   . VAL   A 1 142 ? 18.713 -13.664 -3.843  1.00 13.63 ?  142 VAL   A CB   1 
ATOM   3048 C CG1  . VAL   A 1 142 ? 20.224 -13.879 -3.822  1.00 13.69 ?  142 VAL   A CG1  1 
ATOM   3049 C CG2  . VAL   A 1 142 ? 18.201 -13.790 -5.272  1.00 15.17 ?  142 VAL   A CG2  1 
ATOM   3050 H H    . VAL   A 1 142 ? 16.308 -13.757 -3.303  1.00 16.26 ?  142 VAL   A H    1 
ATOM   3051 H HA   . VAL   A 1 142 ? 18.190 -15.558 -3.295  1.00 16.35 ?  142 VAL   A HA   1 
ATOM   3052 H HB   . VAL   A 1 142 ? 18.536 -12.757 -3.533  1.00 16.34 ?  142 VAL   A HB   1 
ATOM   3053 H HG11 . VAL   A 1 142 ? 20.629 -13.382 -4.550  1.00 16.42 ?  142 VAL   A HG11 1 
ATOM   3054 H HG12 . VAL   A 1 142 ? 20.582 -13.564 -2.974  1.00 16.42 ?  142 VAL   A HG12 1 
ATOM   3055 H HG13 . VAL   A 1 142 ? 20.408 -14.825 -3.926  1.00 16.42 ?  142 VAL   A HG13 1 
ATOM   3056 H HG21 . VAL   A 1 142 ? 18.679 -13.155 -5.835  1.00 18.19 ?  142 VAL   A HG21 1 
ATOM   3057 H HG22 . VAL   A 1 142 ? 18.373 -14.693 -5.582  1.00 18.19 ?  142 VAL   A HG22 1 
ATOM   3058 H HG23 . VAL   A 1 142 ? 17.257 -13.602 -5.284  1.00 18.19 ?  142 VAL   A HG23 1 
ATOM   3059 N N    . CYS   A 1 143 ? 18.126 -13.741 -0.672  1.00 12.89 ?  143 CYS   A N    1 
ATOM   3060 C CA   . CYS   A 1 143 ? 18.597 -13.690 0.708   1.00 13.06 ?  143 CYS   A CA   1 
ATOM   3061 C C    . CYS   A 1 143 ? 18.377 -15.031 1.401   1.00 13.10 ?  143 CYS   A C    1 
ATOM   3062 O O    . CYS   A 1 143 ? 19.302 -15.620 1.971   1.00 13.03 ?  143 CYS   A O    1 
ATOM   3063 C CB   . CYS   A 1 143 ? 17.859 -12.584 1.454   1.00 13.45 ?  143 CYS   A CB   1 
ATOM   3064 S SG   . CYS   A 1 143 ? 18.350 -12.412 3.176   1.00 13.66 ?  143 CYS   A SG   1 
ATOM   3065 H H    . CYS   A 1 143 ? 17.547 -13.138 -0.880  1.00 15.45 ?  143 CYS   A H    1 
ATOM   3066 H HA   . CYS   A 1 143 ? 19.543 -13.495 0.716   1.00 15.67 ?  143 CYS   A HA   1 
ATOM   3067 H HB2  . CYS   A 1 143 ? 18.025 -11.740 1.009   1.00 16.13 ?  143 CYS   A HB2  1 
ATOM   3068 H HB3  . CYS   A 1 143 ? 16.911 -12.779 1.440   1.00 16.13 ?  143 CYS   A HB3  1 
ATOM   3069 H HG   . CYS   A 1 143 ? 17.768 -11.477 3.644   1.00 16.39 ?  143 CYS   A HG   1 
ATOM   3070 N N    . VAL   A 1 144 ? 17.145 -15.535 1.355   1.00 13.64 ?  144 VAL   A N    1 
ATOM   3071 C CA   . VAL   A 1 144 ? 16.816 -16.773 2.055   1.00 15.18 ?  144 VAL   A CA   1 
ATOM   3072 C C    . VAL   A 1 144 ? 17.621 -17.945 1.513   1.00 14.53 ?  144 VAL   A C    1 
ATOM   3073 O O    . VAL   A 1 144 ? 17.988 -18.860 2.262   1.00 15.36 ?  144 VAL   A O    1 
ATOM   3074 C CB   . VAL   A 1 144 ? 15.298 -17.017 1.961   1.00 18.46 ?  144 VAL   A CB   1 
ATOM   3075 C CG1  . VAL   A 1 144 ? 14.953 -18.454 2.294   1.00 20.56 ?  144 VAL   A CG1  1 
ATOM   3076 C CG2  . VAL   A 1 144 ? 14.564 -16.024 2.859   1.00 18.30 ?  144 VAL   A CG2  1 
ATOM   3077 H H    . VAL   A 1 144 ? 16.484 -15.176 0.928   1.00 16.36 ?  144 VAL   A H    1 
ATOM   3078 H HA   . VAL   A 1 144 ? 17.038 -16.667 2.985   1.00 18.21 ?  144 VAL   A HA   1 
ATOM   3079 H HB   . VAL   A 1 144 ? 15.008 -16.848 1.047   1.00 22.14 ?  144 VAL   A HB   1 
ATOM   3080 H HG11 . VAL   A 1 144 ? 14.003 -18.511 2.490   1.00 24.66 ?  144 VAL   A HG11 1 
ATOM   3081 H HG12 . VAL   A 1 144 ? 15.164 -19.017 1.534   1.00 24.66 ?  144 VAL   A HG12 1 
ATOM   3082 H HG13 . VAL   A 1 144 ? 15.465 -18.728 3.069   1.00 24.66 ?  144 VAL   A HG13 1 
ATOM   3083 H HG21 . VAL   A 1 144 ? 13.609 -16.207 2.828   1.00 21.95 ?  144 VAL   A HG21 1 
ATOM   3084 H HG22 . VAL   A 1 144 ? 14.884 -16.117 3.769   1.00 21.95 ?  144 VAL   A HG22 1 
ATOM   3085 H HG23 . VAL   A 1 144 ? 14.730 -15.119 2.544   1.00 21.95 ?  144 VAL   A HG23 1 
ATOM   3086 N N    . ASP   A 1 145 ? 17.881 -17.958 0.207   1.00 15.05 ?  145 ASP   A N    1 
ATOM   3087 C CA   . ASP   A 1 145 ? 18.583 -19.065 -0.434  1.00 15.66 ?  145 ASP   A CA   1 
ATOM   3088 C C    . ASP   A 1 145 ? 20.105 -18.925 -0.398  1.00 15.11 ?  145 ASP   A C    1 
ATOM   3089 O O    . ASP   A 1 145 ? 20.807 -19.819 -0.884  1.00 17.17 ?  145 ASP   A O    1 
ATOM   3090 C CB   . ASP   A 1 145 ? 18.122 -19.207 -1.887  1.00 17.63 ?  145 ASP   A CB   1 
ATOM   3091 C CG   . ASP   A 1 145 ? 16.665 -19.627 -2.002  1.00 20.11 ?  145 ASP   A CG   1 
ATOM   3092 O OD1  . ASP   A 1 145 ? 16.110 -20.166 -1.021  1.00 20.63 ?  145 ASP   A OD1  1 
ATOM   3093 O OD2  . ASP   A 1 145 ? 16.077 -19.420 -3.080  1.00 21.26 -1 145 ASP   A OD2  1 
ATOM   3094 H H    . ASP   A 1 145 ? 17.642 -17.337 -0.341  1.00 18.05 ?  145 ASP   A H    1 
ATOM   3095 H HA   . ASP   A 1 145 ? 18.354 -19.885 0.026   1.00 18.78 ?  145 ASP   A HA   1 
ATOM   3096 H HB2  . ASP   A 1 145 ? 18.231 -18.357 -2.341  1.00 21.14 ?  145 ASP   A HB2  1 
ATOM   3097 H HB3  . ASP   A 1 145 ? 18.655 -19.888 -2.324  1.00 21.14 ?  145 ASP   A HB3  1 
ATOM   3098 N N    . THR   A 1 146 ? 20.636 -17.840 0.155   1.00 13.64 ?  146 THR   A N    1 
ATOM   3099 C CA   . THR   A 1 146 ? 22.076 -17.594 0.169   1.00 12.85 ?  146 THR   A CA   1 
ATOM   3100 C C    . THR   A 1 146 ? 22.638 -17.418 1.566   1.00 12.78 ?  146 THR   A C    1 
ATOM   3101 O O    . THR   A 1 146 ? 23.722 -17.942 1.864   1.00 13.83 ?  146 THR   A O    1 
ATOM   3102 C CB   . THR   A 1 146 ? 22.396 -16.336 -0.658  1.00 12.77 ?  146 THR   A CB   1 
ATOM   3103 O OG1  . THR   A 1 146 ? 21.867 -16.488 -1.976  1.00 13.55 ?  146 THR   A OG1  1 
ATOM   3104 C CG2  . THR   A 1 146 ? 23.901 -16.094 -0.744  1.00 13.40 ?  146 THR   A CG2  1 
ATOM   3105 H H    . THR   A 1 146 ? 20.176 -17.213 0.528   1.00 16.36 ?  146 THR   A H    1 
ATOM   3106 H HA   . THR   A 1 146 ? 22.532 -18.339 -0.243  1.00 15.41 ?  146 THR   A HA   1 
ATOM   3107 H HB   . THR   A 1 146 ? 21.993 -15.561 -0.237  1.00 15.31 ?  146 THR   A HB   1 
ATOM   3108 H HG1  . THR   A 1 146 ? 21.030 -16.559 -1.941  1.00 16.25 ?  146 THR   A HG1  1 
ATOM   3109 H HG21 . THR   A 1 146 ? 24.090 -15.426 -1.420  1.00 16.07 ?  146 THR   A HG21 1 
ATOM   3110 H HG22 . THR   A 1 146 ? 24.236 -15.779 0.111   1.00 16.07 ?  146 THR   A HG22 1 
ATOM   3111 H HG23 . THR   A 1 146 ? 24.355 -16.918 -0.979  1.00 16.07 ?  146 THR   A HG23 1 
ATOM   3112 N N    . VAL   A 1 147 ? 21.964 -16.644 2.408   1.00 12.49 ?  147 VAL   A N    1 
ATOM   3113 C CA   . VAL   A 1 147 ? 22.462 -16.346 3.741   1.00 12.58 ?  147 VAL   A CA   1 
ATOM   3114 C C    . VAL   A 1 147 ? 22.141 -17.515 4.661   1.00 12.95 ?  147 VAL   A C    1 
ATOM   3115 O O    . VAL   A 1 147 ? 20.995 -17.988 4.716   1.00 14.22 ?  147 VAL   A O    1 
ATOM   3116 C CB   . VAL   A 1 147 ? 21.854 -15.039 4.267   1.00 12.81 ?  147 VAL   A CB   1 
ATOM   3117 C CG1  . VAL   A 1 147 ? 22.415 -14.734 5.631   1.00 13.86 ?  147 VAL   A CG1  1 
ATOM   3118 C CG2  . VAL   A 1 147 ? 22.108 -13.881 3.293   1.00 13.17 ?  147 VAL   A CG2  1 
ATOM   3119 H H    . VAL   A 1 147 ? 21.203 -16.280 2.233   1.00 14.98 ?  147 VAL   A H    1 
ATOM   3120 H HA   . VAL   A 1 147 ? 23.428 -16.240 3.704   1.00 15.09 ?  147 VAL   A HA   1 
ATOM   3121 H HB   . VAL   A 1 147 ? 20.898 -15.152 4.359   1.00 15.36 ?  147 VAL   A HB   1 
ATOM   3122 H HG11 . VAL   A 1 147 ? 22.191 -13.825 5.868   1.00 16.62 ?  147 VAL   A HG11 1 
ATOM   3123 H HG12 . VAL   A 1 147 ? 22.029 -15.350 6.277   1.00 16.62 ?  147 VAL   A HG12 1 
ATOM   3124 H HG13 . VAL   A 1 147 ? 23.380 -14.844 5.607   1.00 16.62 ?  147 VAL   A HG13 1 
ATOM   3125 H HG21 . VAL   A 1 147 ? 21.774 -13.061 3.690   1.00 15.79 ?  147 VAL   A HG21 1 
ATOM   3126 H HG22 . VAL   A 1 147 ? 23.059 -13.808 3.130   1.00 15.79 ?  147 VAL   A HG22 1 
ATOM   3127 H HG23 . VAL   A 1 147 ? 21.640 -14.062 2.464   1.00 15.79 ?  147 VAL   A HG23 1 
ATOM   3128 N N    . ARG   A 1 148 ? 23.166 -17.993 5.370   1.00 13.55 ?  148 ARG   A N    1 
ATOM   3129 C CA   . ARG   A 1 148 ? 23.038 -19.077 6.330   1.00 13.20 ?  148 ARG   A CA   1 
ATOM   3130 C C    . ARG   A 1 148 ? 23.179 -18.609 7.766   1.00 13.77 ?  148 ARG   A C    1 
ATOM   3131 O O    . ARG   A 1 148 ? 22.777 -19.330 8.686   1.00 15.65 ?  148 ARG   A O    1 
ATOM   3132 C CB   . ARG   A 1 148 ? 24.083 -20.163 6.040   1.00 14.09 ?  148 ARG   A CB   1 
ATOM   3133 C CG   . ARG   A 1 148 ? 23.898 -20.812 4.679   1.00 15.70 ?  148 ARG   A CG   1 
ATOM   3134 C CD   . ARG   A 1 148 ? 24.986 -21.837 4.365   1.00 16.62 ?  148 ARG   A CD   1 
ATOM   3135 N NE   . ARG   A 1 148 ? 26.327 -21.261 4.393   1.00 16.21 ?  148 ARG   A NE   1 
ATOM   3136 C CZ   . ARG   A 1 148 ? 26.834 -20.509 3.425   1.00 15.45 ?  148 ARG   A CZ   1 
ATOM   3137 N NH1  . ARG   A 1 148 ? 26.161 -20.271 2.311   1.00 16.06 ?  148 ARG   A NH1  1 
ATOM   3138 N NH2  . ARG   A 1 148 ? 28.049 -19.977 3.579   1.00 15.84 ?  148 ARG   A NH2  1 
ATOM   3139 H H    . ARG   A 1 148 ? 23.976 -17.695 5.296   1.00 16.25 ?  148 ARG   A H    1 
ATOM   3140 H HA   . ARG   A 1 148 ? 22.163 -19.475 6.230   1.00 15.82 ?  148 ARG   A HA   1 
ATOM   3141 H HB2  . ARG   A 1 148 ? 24.966 -19.778 6.069   1.00 16.90 ?  148 ARG   A HB2  1 
ATOM   3142 H HB3  . ARG   A 1 148 ? 23.999 -20.865 6.710   1.00 16.90 ?  148 ARG   A HB3  1 
ATOM   3143 H HG2  . ARG   A 1 148 ? 23.039 -21.262 4.658   1.00 18.82 ?  148 ARG   A HG2  1 
ATOM   3144 H HG3  . ARG   A 1 148 ? 23.928 -20.120 4.000   1.00 18.82 ?  148 ARG   A HG3  1 
ATOM   3145 H HD2  . ARG   A 1 148 ? 24.954 -22.549 5.023   1.00 19.94 ?  148 ARG   A HD2  1 
ATOM   3146 H HD3  . ARG   A 1 148 ? 24.832 -22.202 3.477   1.00 19.94 ?  148 ARG   A HD3  1 
ATOM   3147 H HE   . ARG   A 1 148 ? 26.816 -21.411 5.080   1.00 19.44 ?  148 ARG   A HE   1 
ATOM   3148 H HH11 . ARG   A 1 148 ? 25.378 -20.601 2.198   1.00 19.26 ?  148 ARG   A HH11 1 
ATOM   3149 H HH12 . ARG   A 1 148 ? 26.510 -19.776 1.696   1.00 19.26 ?  148 ARG   A HH12 1 
ATOM   3150 H HH21 . ARG   A 1 148 ? 28.492 -20.118 4.301   1.00 18.99 ?  148 ARG   A HH21 1 
ATOM   3151 H HH22 . ARG   A 1 148 ? 28.388 -19.483 2.958   1.00 18.99 ?  148 ARG   A HH22 1 
ATOM   3152 N N    . THR   A 1 149 ? 23.724 -17.416 7.972   1.00 13.74 ?  149 THR   A N    1 
ATOM   3153 C CA   . THR   A 1 149 ? 23.808 -16.819 9.289   1.00 13.72 ?  149 THR   A CA   1 
ATOM   3154 C C    . THR   A 1 149 ? 22.485 -16.120 9.608   1.00 13.59 ?  149 THR   A C    1 
ATOM   3155 O O    . THR   A 1 149 ? 21.539 -16.119 8.811   1.00 14.39 ?  149 THR   A O    1 
ATOM   3156 C CB   . THR   A 1 149 ? 25.007 -15.879 9.345   1.00 14.21 ?  149 THR   A CB   1 
ATOM   3157 O OG1  . THR   A 1 149 ? 24.868 -14.933 8.284   1.00 14.48 ?  149 THR   A OG1  1 
ATOM   3158 C CG2  . THR   A 1 149 ? 26.319 -16.668 9.210   1.00 14.63 ?  149 THR   A CG2  1 
ATOM   3159 H H    . THR   A 1 149 ? 24.057 -16.923 7.346   1.00 16.47 ?  149 THR   A H    1 
ATOM   3160 H HA   . THR   A 1 149 ? 23.939 -17.526 9.940   1.00 16.45 ?  149 THR   A HA   1 
ATOM   3161 H HB   . THR   A 1 149 ? 25.005 -15.419 10.193  1.00 17.04 ?  149 THR   A HB   1 
ATOM   3162 H HG1  . THR   A 1 149 ? 25.523 -14.405 8.286   1.00 17.36 ?  149 THR   A HG1  1 
ATOM   3163 H HG21 . THR   A 1 149 ? 27.075 -16.063 9.263   1.00 17.54 ?  149 THR   A HG21 1 
ATOM   3164 H HG22 . THR   A 1 149 ? 26.392 -17.323 9.924   1.00 17.54 ?  149 THR   A HG22 1 
ATOM   3165 H HG23 . THR   A 1 149 ? 26.348 -17.133 8.357   1.00 17.54 ?  149 THR   A HG23 1 
ATOM   3166 N N    . ASN   A 1 150 ? 22.381 -15.577 10.811  1.00 13.58 ?  150 ASN   A N    1 
ATOM   3167 C CA   . ASN   A 1 150 ? 21.105 -15.067 11.315  1.00 14.59 ?  150 ASN   A CA   1 
ATOM   3168 C C    . ASN   A 1 150 ? 20.914 -13.626 10.863  1.00 13.76 ?  150 ASN   A C    1 
ATOM   3169 O O    . ASN   A 1 150 ? 21.647 -12.726 11.296  1.00 15.40 ?  150 ASN   A O    1 
ATOM   3170 C CB   . ASN   A 1 150 ? 21.067 -15.179 12.833  1.00 17.42 ?  150 ASN   A CB   1 
ATOM   3171 C CG   . ASN   A 1 150 ? 20.920 -16.608 13.297  1.00 21.86 ?  150 ASN   A CG   1 
ATOM   3172 O OD1  . ASN   A 1 150 ? 20.311 -17.424 12.608  1.00 23.12 ?  150 ASN   A OD1  1 
ATOM   3173 N ND2  . ASN   A 1 150 ? 21.484 -16.925 14.460  1.00 24.30 ?  150 ASN   A ND2  1 
ATOM   3174 H H    . ASN   A 1 150 ? 23.035 -15.500 11.360  1.00 16.28 ?  150 ASN   A H    1 
ATOM   3175 H HA   . ASN   A 1 150 ? 20.381 -15.607 10.952  1.00 17.49 ?  150 ASN   A HA   1 
ATOM   3176 H HB2  . ASN   A 1 150 ? 21.893 -14.830 13.200  1.00 20.89 ?  150 ASN   A HB2  1 
ATOM   3177 H HB3  . ASN   A 1 150 ? 20.310 -14.680 13.171  1.00 20.89 ?  150 ASN   A HB3  1 
ATOM   3178 H HD21 . ASN   A 1 150 ? 21.428 -17.732 14.768  1.00 29.14 ?  150 ASN   A HD21 1 
ATOM   3179 H HD22 . ASN   A 1 150 ? 21.902 -16.327 14.916  1.00 29.14 ?  150 ASN   A HD22 1 
ATOM   3180 N N    . VAL   A 1 151 ? 19.928 -13.403 10.001  1.00 13.65 ?  151 VAL   A N    1 
ATOM   3181 C CA   . VAL   A 1 151 ? 19.703 -12.092 9.411   1.00 13.52 ?  151 VAL   A CA   1 
ATOM   3182 C C    . VAL   A 1 151 ? 18.323 -11.576 9.800   1.00 13.53 ?  151 VAL   A C    1 
ATOM   3183 O O    . VAL   A 1 151 ? 17.315 -12.286 9.670   1.00 14.92 ?  151 VAL   A O    1 
ATOM   3184 C CB   . VAL   A 1 151 ? 19.974 -12.069 7.892   1.00 14.93 ?  151 VAL   A CB   1 
ATOM   3185 C CG1  . VAL   A 1 151 ? 19.160 -13.100 7.142   1.00 16.05 ?  151 VAL   A CG1  1 
ATOM   3186 C CG2  . VAL   A 1 151 ? 19.747 -10.664 7.326   1.00 15.16 ?  151 VAL   A CG2  1 
ATOM   3187 H H    . VAL   A 1 151 ? 19.372 -14.006 9.735   1.00 16.37 ?  151 VAL   A H    1 
ATOM   3188 H HA   . VAL   A 1 151 ? 20.346 -11.482 9.803   1.00 16.22 ?  151 VAL   A HA   1 
ATOM   3189 H HB   . VAL   A 1 151 ? 20.912 -12.282 7.743   1.00 17.91 ?  151 VAL   A HB   1 
ATOM   3190 H HG11 . VAL   A 1 151 ? 19.297 -12.984 6.187   1.00 19.25 ?  151 VAL   A HG11 1 
ATOM   3191 H HG12 . VAL   A 1 151 ? 19.456 -13.987 7.408   1.00 19.25 ?  151 VAL   A HG12 1 
ATOM   3192 H HG13 . VAL   A 1 151 ? 18.224 -12.984 7.359   1.00 19.25 ?  151 VAL   A HG13 1 
ATOM   3193 H HG21 . VAL   A 1 151 ? 20.070 -10.634 6.410   1.00 18.18 ?  151 VAL   A HG21 1 
ATOM   3194 H HG22 . VAL   A 1 151 ? 18.798 -10.464 7.345   1.00 18.18 ?  151 VAL   A HG22 1 
ATOM   3195 H HG23 . VAL   A 1 151 ? 20.233 -10.022 7.866   1.00 18.18 ?  151 VAL   A HG23 1 
ATOM   3196 N N    . TYR   A 1 152 ? 18.314 -10.338 10.298  1.00 13.29 ?  152 TYR   A N    1 
ATOM   3197 C CA   . TYR   A 1 152 ? 17.124 -9.598  10.689  1.00 12.99 ?  152 TYR   A CA   1 
ATOM   3198 C C    . TYR   A 1 152 ? 16.923 -8.491  9.666   1.00 12.50 ?  152 TYR   A C    1 
ATOM   3199 O O    . TYR   A 1 152 ? 17.698 -7.526  9.621   1.00 13.03 ?  152 TYR   A O    1 
ATOM   3200 C CB   . TYR   A 1 152 ? 17.314 -9.063  12.104  1.00 13.67 ?  152 TYR   A CB   1 
ATOM   3201 C CG   . TYR   A 1 152 ? 17.284 -10.199 13.092  1.00 14.39 ?  152 TYR   A CG   1 
ATOM   3202 C CD1  . TYR   A 1 152 ? 18.418 -10.955 13.350  1.00 15.63 ?  152 TYR   A CD1  1 
ATOM   3203 C CD2  . TYR   A 1 152 ? 16.105 -10.559 13.717  1.00 14.65 ?  152 TYR   A CD2  1 
ATOM   3204 C CE1  . TYR   A 1 152 ? 18.386 -12.024 14.222  1.00 17.14 ?  152 TYR   A CE1  1 
ATOM   3205 C CE2  . TYR   A 1 152 ? 16.058 -11.637 14.595  1.00 16.39 ?  152 TYR   A CE2  1 
ATOM   3206 C CZ   . TYR   A 1 152 ? 17.204 -12.363 14.844  1.00 17.14 ?  152 TYR   A CZ   1 
ATOM   3207 O OH   . TYR   A 1 152 ? 17.162 -13.435 15.715  1.00 19.62 ?  152 TYR   A OH   1 
ATOM   3208 H H    . TYR   A 1 152 ? 19.036 -9.874  10.396  1.00 15.93 ?  152 TYR   A H    1 
ATOM   3209 H HA   . TYR   A 1 152 ? 16.354 -10.189 10.668  1.00 15.57 ?  152 TYR   A HA   1 
ATOM   3210 H HB2  . TYR   A 1 152 ? 18.175 -8.624  12.165  1.00 16.39 ?  152 TYR   A HB2  1 
ATOM   3211 H HB3  . TYR   A 1 152 ? 16.599 -8.448  12.312  1.00 16.39 ?  152 TYR   A HB3  1 
ATOM   3212 H HD1  . TYR   A 1 152 ? 19.215 -10.733 12.923  1.00 18.74 ?  152 TYR   A HD1  1 
ATOM   3213 H HD2  . TYR   A 1 152 ? 15.327 -10.073 13.543  1.00 17.57 ?  152 TYR   A HD2  1 
ATOM   3214 H HE1  . TYR   A 1 152 ? 19.158 -12.511 14.390  1.00 20.56 ?  152 TYR   A HE1  1 
ATOM   3215 H HE2  . TYR   A 1 152 ? 15.259 -11.857 15.018  1.00 19.66 ?  152 TYR   A HE2  1 
ATOM   3216 H HH   . TYR   A 1 152 ? 16.384 -13.512 16.028  1.00 23.53 ?  152 TYR   A HH   1 
ATOM   3217 N N    A LEU   A 1 153 ? 15.923 -8.680  8.798   0.60 12.58 ?  153 LEU   A N    1 
ATOM   3218 N N    B LEU   A 1 153 ? 15.875 -8.601  8.863   0.40 12.65 ?  153 LEU   A N    1 
ATOM   3219 C CA   A LEU   A 1 153 ? 15.656 -7.805  7.660   0.60 12.53 ?  153 LEU   A CA   1 
ATOM   3220 C CA   B LEU   A 1 153 ? 15.605 -7.606  7.839   0.40 12.40 ?  153 LEU   A CA   1 
ATOM   3221 C C    A LEU   A 1 153 ? 14.647 -6.732  8.040   0.60 12.48 ?  153 LEU   A C    1 
ATOM   3222 C C    B LEU   A 1 153 ? 14.663 -6.532  8.368   0.40 12.93 ?  153 LEU   A C    1 
ATOM   3223 O O    A LEU   A 1 153 ? 13.554 -7.041  8.531   0.60 13.60 ?  153 LEU   A O    1 
ATOM   3224 O O    B LEU   A 1 153 ? 13.587 -6.840  8.893   0.40 13.85 ?  153 LEU   A O    1 
ATOM   3225 C CB   A LEU   A 1 153 ? 15.095 -8.618  6.486   0.60 12.42 ?  153 LEU   A CB   1 
ATOM   3226 C CB   B LEU   A 1 153 ? 14.992 -8.273  6.612   0.40 12.31 ?  153 LEU   A CB   1 
ATOM   3227 C CG   A LEU   A 1 153 ? 16.037 -9.612  5.799   0.60 12.62 ?  153 LEU   A CG   1 
ATOM   3228 C CG   B LEU   A 1 153 ? 15.871 -9.337  5.959   0.40 12.36 ?  153 LEU   A CG   1 
ATOM   3229 C CD1  A LEU   A 1 153 ? 15.270 -10.514 4.843   0.60 12.85 ?  153 LEU   A CD1  1 
ATOM   3230 C CD1  B LEU   A 1 153 ? 15.043 -10.149 4.984   0.40 12.20 ?  153 LEU   A CD1  1 
ATOM   3231 C CD2  A LEU   A 1 153 ? 17.131 -8.863  5.051   0.60 13.28 ?  153 LEU   A CD2  1 
ATOM   3232 C CD2  B LEU   A 1 153 ? 17.065 -8.695  5.263   0.40 13.43 ?  153 LEU   A CD2  1 
ATOM   3233 H H    A LEU   A 1 153 ? 15.359 -9.334  8.854   0.60 15.08 ?  153 LEU   A H    1 
ATOM   3234 H H    B LEU   A 1 153 ? 15.301 -9.246  8.890   0.40 15.17 ?  153 LEU   A H    1 
ATOM   3235 H HA   A LEU   A 1 153 ? 16.476 -7.384  7.372   0.60 15.03 ?  153 LEU   A HA   1 
ATOM   3236 H HA   B LEU   A 1 153 ? 16.437 -7.184  7.579   0.40 14.86 ?  153 LEU   A HA   1 
ATOM   3237 H HB2  A LEU   A 1 153 ? 14.334 -9.131  6.804   0.60 14.89 ?  153 LEU   A HB2  1 
ATOM   3238 H HB2  B LEU   A 1 153 ? 14.161 -8.694  6.877   0.40 14.76 ?  153 LEU   A HB2  1 
ATOM   3239 H HB3  A LEU   A 1 153 ? 14.794 -8.001  5.799   0.60 14.89 ?  153 LEU   A HB3  1 
ATOM   3240 H HB3  B LEU   A 1 153 ? 14.814 -7.585  5.950   0.40 14.76 ?  153 LEU   A HB3  1 
ATOM   3241 H HG   A LEU   A 1 153 ? 16.460 -10.171 6.472   0.60 15.13 ?  153 LEU   A HG   1 
ATOM   3242 H HG   B LEU   A 1 153 ? 16.208 -9.933  6.647   0.40 14.82 ?  153 LEU   A HG   1 
ATOM   3243 H HD11 A LEU   A 1 153 ? 15.816 -11.290 4.638   0.60 15.41 ?  153 LEU   A HD11 1 
ATOM   3244 H HD11 B LEU   A 1 153 ? 15.612 -10.814 4.569   0.40 14.62 ?  153 LEU   A HD11 1 
ATOM   3245 H HD12 A LEU   A 1 153 ? 14.448 -10.791 5.266   0.60 15.41 ?  153 LEU   A HD12 1 
ATOM   3246 H HD12 B LEU   A 1 153 ? 14.322 -10.581 5.468   0.40 14.62 ?  153 LEU   A HD12 1 
ATOM   3247 H HD13 A LEU   A 1 153 ? 15.080 -10.018 4.032   0.60 15.41 ?  153 LEU   A HD13 1 
ATOM   3248 H HD13 B LEU   A 1 153 ? 14.679 -9.554  4.309   0.40 14.62 ?  153 LEU   A HD13 1 
ATOM   3249 H HD21 A LEU   A 1 153 ? 17.725 -9.504  4.635   0.60 15.93 ?  153 LEU   A HD21 1 
ATOM   3250 H HD21 B LEU   A 1 153 ? 17.574 -9.388  4.815   0.40 16.11 ?  153 LEU   A HD21 1 
ATOM   3251 H HD22 A LEU   A 1 153 ? 16.719 -8.303  4.376   0.60 15.93 ?  153 LEU   A HD22 1 
ATOM   3252 H HD22 B LEU   A 1 153 ? 16.743 -8.049  4.617   0.40 16.11 ?  153 LEU   A HD22 1 
ATOM   3253 H HD23 A LEU   A 1 153 ? 17.624 -8.316  5.682   0.60 15.93 ?  153 LEU   A HD23 1 
ATOM   3254 H HD23 B LEU   A 1 153 ? 17.620 -8.253  5.925   0.40 16.11 ?  153 LEU   A HD23 1 
ATOM   3255 N N    A ALA   A 1 154 ? 15.000 -5.477  7.771   0.60 11.82 ?  154 ALA   A N    1 
ATOM   3256 N N    B ALA   A 1 154 ? 15.078 -5.274  8.229   0.40 13.07 ?  154 ALA   A N    1 
ATOM   3257 C CA   A ALA   A 1 154 ? 14.140 -4.332  8.031   0.60 12.89 ?  154 ALA   A CA   1 
ATOM   3258 C CA   B ALA   A 1 154 ? 14.220 -4.122  8.475   0.40 14.44 ?  154 ALA   A CA   1 
ATOM   3259 C C    A ALA   A 1 154 ? 13.634 -3.787  6.706   0.60 13.12 ?  154 ALA   A C    1 
ATOM   3260 C C    B ALA   A 1 154 ? 13.784 -3.584  7.119   0.40 15.36 ?  154 ALA   A C    1 
ATOM   3261 O O    A ALA   A 1 154 ? 14.429 -3.453  5.819   0.60 13.31 ?  154 ALA   A O    1 
ATOM   3262 O O    B ALA   A 1 154 ? 14.627 -3.190  6.306   0.40 14.84 ?  154 ALA   A O    1 
ATOM   3263 C CB   A ALA   A 1 154 ? 14.893 -3.237  8.779   0.60 13.56 ?  154 ALA   A CB   1 
ATOM   3264 C CB   B ALA   A 1 154 ? 14.969 -3.042  9.257   0.40 14.77 ?  154 ALA   A CB   1 
ATOM   3265 H H    A ALA   A 1 154 ? 15.752 -5.263  7.410   0.60 14.17 ?  154 ALA   A H    1 
ATOM   3266 H H    B ALA   A 1 154 ? 15.876 -5.053  7.984   0.40 15.67 ?  154 ALA   A H    1 
ATOM   3267 H HA   A ALA   A 1 154 ? 13.376 -4.614  8.558   0.60 15.45 ?  154 ALA   A HA   1 
ATOM   3268 H HA   B ALA   A 1 154 ? 13.437 -4.390  8.981   0.40 17.31 ?  154 ALA   A HA   1 
ATOM   3269 H HB1  A ALA   A 1 154 ? 14.290 -2.497  8.935   0.60 16.26 ?  154 ALA   A HB1  1 
ATOM   3270 H HB1  B ALA   A 1 154 ? 14.375 -2.289  9.405   0.40 17.71 ?  154 ALA   A HB1  1 
ATOM   3271 H HB2  A ALA   A 1 154 ? 15.208 -3.599  9.618   0.60 16.26 ?  154 ALA   A HB2  1 
ATOM   3272 H HB2  B ALA   A 1 154 ? 15.258 -3.408  10.108  0.40 17.71 ?  154 ALA   A HB2  1 
ATOM   3273 H HB3  A ALA   A 1 154 ? 15.642 -2.949  8.234   0.60 16.26 ?  154 ALA   A HB3  1 
ATOM   3274 H HB3  B ALA   A 1 154 ? 15.741 -2.757  8.741   0.40 17.71 ?  154 ALA   A HB3  1 
ATOM   3275 N N    A VAL   A 1 155 ? 12.315 -3.694  6.587   0.60 13.74 ?  155 VAL   A N    1 
ATOM   3276 N N    B VAL   A 1 155 ? 12.477 -3.577  6.872   0.40 17.21 ?  155 VAL   A N    1 
ATOM   3277 C CA   A VAL   A 1 155 ? 11.653 -3.174  5.403   0.60 14.53 ?  155 VAL   A CA   1 
ATOM   3278 C CA   B VAL   A 1 155 ? 11.935 -3.275  5.551   0.40 19.41 ?  155 VAL   A CA   1 
ATOM   3279 C C    A VAL   A 1 155 ? 10.934 -1.898  5.806   0.60 15.92 ?  155 VAL   A C    1 
ATOM   3280 C C    B VAL   A 1 155 ? 10.986 -2.092  5.662   0.40 21.48 ?  155 VAL   A C    1 
ATOM   3281 O O    A VAL   A 1 155 ? 10.051 -1.926  6.671   0.60 15.04 ?  155 VAL   A O    1 
ATOM   3282 O O    B VAL   A 1 155 ? 9.880  -2.215  6.203   0.40 21.54 ?  155 VAL   A O    1 
ATOM   3283 C CB   A VAL   A 1 155 ? 10.698 -4.211  4.798   0.60 14.10 ?  155 VAL   A CB   1 
ATOM   3284 C CB   B VAL   A 1 155 ? 11.242 -4.487  4.917   0.40 19.69 ?  155 VAL   A CB   1 
ATOM   3285 C CG1  A VAL   A 1 155 ? 9.983  -3.628  3.593   0.60 15.15 ?  155 VAL   A CG1  1 
ATOM   3286 C CG1  B VAL   A 1 155 ? 10.534 -4.083  3.635   0.40 19.94 ?  155 VAL   A CG1  1 
ATOM   3287 C CG2  A VAL   A 1 155 ? 11.486 -5.461  4.410   0.60 14.77 ?  155 VAL   A CG2  1 
ATOM   3288 C CG2  B VAL   A 1 155 ? 12.260 -5.576  4.636   0.40 19.62 ?  155 VAL   A CG2  1 
ATOM   3289 H H    A VAL   A 1 155 ? 11.757 -3.943  7.200   0.60 16.47 ?  155 VAL   A H    1 
ATOM   3290 H H    B VAL   A 1 155 ? 11.874 -3.740  7.465   0.40 20.64 ?  155 VAL   A H    1 
ATOM   3291 H HA   A VAL   A 1 155 ? 12.307 -2.939  4.738   0.60 17.42 ?  155 VAL   A HA   1 
ATOM   3292 H HA   B VAL   A 1 155 ? 12.659 -3.010  4.966   0.40 23.27 ?  155 VAL   A HA   1 
ATOM   3293 H HB   A VAL   A 1 155 ? 10.023 -4.455  5.458   0.60 16.91 ?  155 VAL   A HB   1 
ATOM   3294 H HB   B VAL   A 1 155 ? 10.582 -4.840  5.533   0.40 23.62 ?  155 VAL   A HB   1 
ATOM   3295 H HG11 A VAL   A 1 155 ? 9.508  -4.340  3.135   0.60 18.17 ?  155 VAL   A HG11 1 
ATOM   3296 H HG11 B VAL   A 1 155 ? 10.577 -4.821  3.010   0.40 23.92 ?  155 VAL   A HG11 1 
ATOM   3297 H HG12 A VAL   A 1 155 ? 9.346  -2.952  3.888   0.60 18.17 ?  155 VAL   A HG12 1 
ATOM   3298 H HG12 B VAL   A 1 155 ? 9.610  -3.871  3.836   0.40 23.92 ?  155 VAL   A HG12 1 
ATOM   3299 H HG13 A VAL   A 1 155 ? 10.635 -3.230  3.000   0.60 18.17 ?  155 VAL   A HG13 1 
ATOM   3300 H HG13 B VAL   A 1 155 ? 10.981 -3.313  3.255   0.40 23.92 ?  155 VAL   A HG13 1 
ATOM   3301 H HG21 A VAL   A 1 155 ? 10.892 -6.078  3.961   0.60 17.71 ?  155 VAL   A HG21 1 
ATOM   3302 H HG21 B VAL   A 1 155 ? 11.815 -6.323  4.208   0.40 23.53 ?  155 VAL   A HG21 1 
ATOM   3303 H HG22 A VAL   A 1 155 ? 12.206 -5.197  3.815   0.60 17.71 ?  155 VAL   A HG22 1 
ATOM   3304 H HG22 B VAL   A 1 155 ? 12.948 -5.220  4.050   0.40 23.53 ?  155 VAL   A HG22 1 
ATOM   3305 H HG23 A VAL   A 1 155 ? 11.847 -5.863  5.212   0.60 17.71 ?  155 VAL   A HG23 1 
ATOM   3306 H HG23 B VAL   A 1 155 ? 12.657 -5.861  5.474   0.40 23.53 ?  155 VAL   A HG23 1 
ATOM   3307 N N    A PHE   A 1 156 ? 11.325 -0.781  5.189   0.60 17.23 ?  156 PHE   A N    1 
ATOM   3308 N N    B PHE   A 1 156 ? 11.421 -0.950  5.141   0.40 23.35 ?  156 PHE   A N    1 
ATOM   3309 C CA   A PHE   A 1 156 ? 10.786 0.523   5.568   0.60 18.71 ?  156 PHE   A CA   1 
ATOM   3310 C CA   B PHE   A 1 156 ? 10.576 0.220   4.968   0.40 25.38 ?  156 PHE   A CA   1 
ATOM   3311 C C    A PHE   A 1 156 ? 9.314  0.660   5.188   0.60 19.26 ?  156 PHE   A C    1 
ATOM   3312 C C    B PHE   A 1 156 ? 9.981  0.126   3.563   0.40 26.59 ?  156 PHE   A C    1 
ATOM   3313 O O    A PHE   A 1 156 ? 8.508  1.170   5.975   0.60 20.47 ?  156 PHE   A O    1 
ATOM   3314 O O    B PHE   A 1 156 ? 10.735 0.044   2.587   0.40 26.69 ?  156 PHE   A O    1 
ATOM   3315 C CB   A PHE   A 1 156 ? 11.624 1.623   4.906   0.60 19.85 ?  156 PHE   A CB   1 
ATOM   3316 C CB   B PHE   A 1 156 ? 11.449 1.467   5.104   0.40 26.40 ?  156 PHE   A CB   1 
ATOM   3317 C CG   A PHE   A 1 156 ? 11.168 3.022   5.226   0.60 21.28 ?  156 PHE   A CG   1 
ATOM   3318 C CG   B PHE   A 1 156 ? 10.686 2.745   5.313   0.40 27.34 ?  156 PHE   A CG   1 
ATOM   3319 C CD1  A PHE   A 1 156 ? 11.190 3.488   6.530   0.60 22.57 ?  156 PHE   A CD1  1 
ATOM   3320 C CD1  B PHE   A 1 156 ? 10.263 3.497   4.232   0.40 27.78 ?  156 PHE   A CD1  1 
ATOM   3321 C CD2  A PHE   A 1 156 ? 10.747 3.880   4.220   0.60 22.32 ?  156 PHE   A CD2  1 
ATOM   3322 C CD2  B PHE   A 1 156 ? 10.425 3.212   6.592   0.40 27.72 ?  156 PHE   A CD2  1 
ATOM   3323 C CE1  A PHE   A 1 156 ? 10.782 4.776   6.830   0.60 23.70 ?  156 PHE   A CE1  1 
ATOM   3324 C CE1  B PHE   A 1 156 ? 9.574  4.682   4.418   0.40 27.94 ?  156 PHE   A CE1  1 
ATOM   3325 C CE2  A PHE   A 1 156 ? 10.336 5.170   4.512   0.60 23.30 ?  156 PHE   A CE2  1 
ATOM   3326 C CE2  B PHE   A 1 156 ? 9.737  4.398   6.786   0.40 27.95 ?  156 PHE   A CE2  1 
ATOM   3327 C CZ   A PHE   A 1 156 ? 10.359 5.620   5.819   0.60 23.81 ?  156 PHE   A CZ   1 
ATOM   3328 C CZ   B PHE   A 1 156 ? 9.311  5.132   5.696   0.40 27.96 ?  156 PHE   A CZ   1 
ATOM   3329 H H    A PHE   A 1 156 ? 11.889 -0.746  4.545   0.60 20.66 ?  156 PHE   A H    1 
ATOM   3330 H H    B PHE   A 1 156 ? 12.217 -0.824  4.866   0.40 28.00 ?  156 PHE   A H    1 
ATOM   3331 H HA   A PHE   A 1 156 ? 10.854 0.642   6.526   0.60 22.44 ?  156 PHE   A HA   1 
ATOM   3332 H HA   B PHE   A 1 156 ? 9.922  0.237   5.671   0.40 30.44 ?  156 PHE   A HA   1 
ATOM   3333 H HB2  A PHE   A 1 156 ? 12.544 1.543   5.203   0.60 23.81 ?  156 PHE   A HB2  1 
ATOM   3334 H HB2  B PHE   A 1 156 ? 12.030 1.346   5.867   0.40 31.66 ?  156 PHE   A HB2  1 
ATOM   3335 H HB3  A PHE   A 1 156 ? 11.583 1.521   3.941   0.60 23.81 ?  156 PHE   A HB3  1 
ATOM   3336 H HB3  B PHE   A 1 156 ? 11.972 1.569   4.298   0.40 31.66 ?  156 PHE   A HB3  1 
ATOM   3337 H HD1  A PHE   A 1 156 ? 11.479 2.928   7.212   0.60 27.07 ?  156 PHE   A HD1  1 
ATOM   3338 H HD1  B PHE   A 1 156 ? 10.435 3.197   3.370   0.40 33.32 ?  156 PHE   A HD1  1 
ATOM   3339 H HD2  A PHE   A 1 156 ? 10.734 3.585   3.338   0.60 26.77 ?  156 PHE   A HD2  1 
ATOM   3340 H HD2  B PHE   A 1 156 ? 10.708 2.721   7.330   0.40 33.26 ?  156 PHE   A HD2  1 
ATOM   3341 H HE1  A PHE   A 1 156 ? 10.799 5.077   7.710   0.60 28.43 ?  156 PHE   A HE1  1 
ATOM   3342 H HE1  B PHE   A 1 156 ? 9.290  5.174   3.683   0.40 33.52 ?  156 PHE   A HE1  1 
ATOM   3343 H HE2  A PHE   A 1 156 ? 10.052 5.736   3.830   0.60 27.95 ?  156 PHE   A HE2  1 
ATOM   3344 H HE2  B PHE   A 1 156 ? 9.561  4.700   7.649   0.40 33.53 ?  156 PHE   A HE2  1 
ATOM   3345 H HZ   A PHE   A 1 156 ? 10.082 6.486   6.019   0.60 28.56 ?  156 PHE   A HZ   1 
ATOM   3346 H HZ   B PHE   A 1 156 ? 8.849  5.929   5.823   0.40 33.55 ?  156 PHE   A HZ   1 
ATOM   3347 N N    A ASP   A 1 157 ? 8.950  0.228   3.985   0.60 18.85 ?  157 ASP   A N    1 
ATOM   3348 N N    B ASP   A 1 157 ? 8.649  0.120   3.437   0.40 27.78 ?  157 ASP   A N    1 
ATOM   3349 C CA   A ASP   A 1 157 ? 7.630  0.485   3.418   0.60 19.67 ?  157 ASP   A CA   1 
ATOM   3350 C CA   B ASP   A 1 157 ? 7.692  0.334   4.529   0.40 28.51 ?  157 ASP   A CA   1 
ATOM   3351 C C    A ASP   A 1 157 ? 6.646  -0.578  3.900   0.60 19.86 ?  157 ASP   A C    1 
ATOM   3352 C C    B ASP   A 1 157 ? 6.545  -0.687  4.520   0.40 27.74 ?  157 ASP   A C    1 
ATOM   3353 O O    A ASP   A 1 157 ? 6.839  -1.771  3.638   0.60 19.13 ?  157 ASP   A O    1 
ATOM   3354 O O    B ASP   A 1 157 ? 6.716  -1.827  4.089   0.40 27.72 ?  157 ASP   A O    1 
ATOM   3355 C CB   A ASP   A 1 157 ? 7.742  0.457   1.896   0.60 20.76 ?  157 ASP   A CB   1 
ATOM   3356 C CB   B ASP   A 1 157 ? 7.152  1.764   4.455   0.40 29.53 ?  157 ASP   A CB   1 
ATOM   3357 C CG   A ASP   A 1 157 ? 6.499  0.966   1.216   0.60 22.36 ?  157 ASP   A CG   1 
ATOM   3358 C CG   B ASP   A 1 157 ? 6.772  2.172   3.046   0.40 30.60 ?  157 ASP   A CG   1 
ATOM   3359 O OD1  A ASP   A 1 157 ? 6.373  2.195   1.066   0.60 23.84 ?  157 ASP   A OD1  1 
ATOM   3360 O OD1  B ASP   A 1 157 ? 6.507  1.275   2.217   0.40 30.98 ?  157 ASP   A OD1  1 
ATOM   3361 O OD2  A ASP   A 1 157 ? 5.639  0.145   0.842   0.60 22.29 -1 157 ASP   A OD2  1 
ATOM   3362 O OD2  B ASP   A 1 157 ? 6.756  3.390   2.763   0.40 31.23 -1 157 ASP   A OD2  1 
ATOM   3363 H H    A ASP   A 1 157 ? 9.473  -0.212  3.457   0.60 22.60 ?  157 ASP   A H    1 
ATOM   3364 H H    B ASP   A 1 157 ? 8.265  -0.015  2.673   0.40 33.32 ?  157 ASP   A H    1 
ATOM   3365 H HA   A ASP   A 1 157 ? 7.315  1.363   3.690   0.60 23.59 ?  157 ASP   A HA   1 
ATOM   3366 H HA   B ASP   A 1 157 ? 8.118  0.244   5.392   0.40 34.20 ?  157 ASP   A HA   1 
ATOM   3367 H HB2  A ASP   A 1 157 ? 8.495  1.014   1.620   0.60 24.91 ?  157 ASP   A HB2  1 
ATOM   3368 H HB2  B ASP   A 1 157 ? 6.386  1.876   5.034   0.40 35.43 ?  157 ASP   A HB2  1 
ATOM   3369 H HB3  A ASP   A 1 157 ? 7.890  -0.456  1.605   0.60 24.91 ?  157 ASP   A HB3  1 
ATOM   3370 H HB3  B ASP   A 1 157 ? 7.849  2.350   4.755   0.40 35.43 ?  157 ASP   A HB3  1 
ATOM   3371 N N    A LYS   A 1 158 ? 5.597  -0.147  4.607   0.60 21.60 ?  158 LYS   A N    1 
ATOM   3372 N N    B LYS   A 1 158 ? 5.374  -0.256  4.993   0.40 26.96 ?  158 LYS   A N    1 
ATOM   3373 C CA   A LYS   A 1 158 ? 4.657  -1.102  5.192   0.60 22.68 ?  158 LYS   A CA   1 
ATOM   3374 C CA   B LYS   A 1 158 ? 4.296  -1.181  5.328   0.40 26.41 ?  158 LYS   A CA   1 
ATOM   3375 C C    A LYS   A 1 158 ? 3.926  -1.895  4.113   0.60 21.90 ?  158 LYS   A C    1 
ATOM   3376 C C    B LYS   A 1 158 ? 3.787  -1.913  4.092   0.40 25.28 ?  158 LYS   A C    1 
ATOM   3377 O O    A LYS   A 1 158 ? 3.687  -3.099  4.274   0.60 21.91 ?  158 LYS   A O    1 
ATOM   3378 O O    B LYS   A 1 158 ? 3.764  -3.149  4.050   0.40 25.14 ?  158 LYS   A O    1 
ATOM   3379 C CB   A LYS   A 1 158 ? 3.680  -0.370  6.119   0.60 24.18 ?  158 LYS   A CB   1 
ATOM   3380 C CB   B LYS   A 1 158 ? 3.165  -0.411  6.012   0.40 27.22 ?  158 LYS   A CB   1 
ATOM   3381 C CG   A LYS   A 1 158 ? 2.500  -1.212  6.615   0.60 25.54 ?  158 LYS   A CG   1 
ATOM   3382 C CG   B LYS   A 1 158 ? 1.884  -1.210  6.204   0.40 27.99 ?  158 LYS   A CG   1 
ATOM   3383 C CD   A LYS   A 1 158 ? 2.941  -2.426  7.431   0.60 26.37 ?  158 LYS   A CD   1 
ATOM   3384 C CD   B LYS   A 1 158 ? 2.119  -2.448  7.051   0.40 28.54 ?  158 LYS   A CD   1 
ATOM   3385 C CE   A LYS   A 1 158 ? 1.730  -3.176  7.983   0.60 27.20 ?  158 LYS   A CE   1 
ATOM   3386 C CE   B LYS   A 1 158 ? 0.822  -3.192  7.311   0.40 28.94 ?  158 LYS   A CE   1 
ATOM   3387 N NZ   A LYS   A 1 158 ? 2.088  -4.484  8.601   0.60 27.69 ?  158 LYS   A NZ   1 
ATOM   3388 N NZ   B LYS   A 1 158 ? 1.057  -4.493  7.998   0.40 29.30 ?  158 LYS   A NZ   1 
ATOM   3389 H H    A LYS   A 1 158 ? 5.427  0.679   4.767   0.60 25.91 ?  158 LYS   A H    1 
ATOM   3390 H H    B LYS   A 1 158 ? 5.173  0.562   5.117   0.40 32.34 ?  158 LYS   A H    1 
ATOM   3391 H HA   A LYS   A 1 158 ? 5.159  -1.730  5.737   0.60 27.21 ?  158 LYS   A HA   1 
ATOM   3392 H HA   B LYS   A 1 158 ? 4.635  -1.838  5.954   0.40 31.68 ?  158 LYS   A HA   1 
ATOM   3393 H HB2  A LYS   A 1 158 ? 4.168  -0.060  6.903   0.60 29.00 ?  158 LYS   A HB2  1 
ATOM   3394 H HB2  B LYS   A 1 158 ? 3.472  -0.127  6.891   0.40 32.66 ?  158 LYS   A HB2  1 
ATOM   3395 H HB3  A LYS   A 1 158 ? 3.319  0.395   5.644   0.60 29.00 ?  158 LYS   A HB3  1 
ATOM   3396 H HB3  B LYS   A 1 158 ? 2.954  0.370   5.476   0.40 32.66 ?  158 LYS   A HB3  1 
ATOM   3397 H HG2  A LYS   A 1 158 ? 1.941  -0.659  7.183   0.60 30.63 ?  158 LYS   A HG2  1 
ATOM   3398 H HG2  B LYS   A 1 158 ? 1.233  -0.656  6.656   0.40 33.58 ?  158 LYS   A HG2  1 
ATOM   3399 H HG3  A LYS   A 1 158 ? 1.986  -1.525  5.855   0.60 30.63 ?  158 LYS   A HG3  1 
ATOM   3400 H HG3  B LYS   A 1 158 ? 1.539  -1.490  5.340   0.40 33.58 ?  158 LYS   A HG3  1 
ATOM   3401 H HD2  A LYS   A 1 158 ? 3.441  -3.030  6.862   0.60 31.63 ?  158 LYS   A HD2  1 
ATOM   3402 H HD2  B LYS   A 1 158 ? 2.726  -3.046  6.589   0.40 34.24 ?  158 LYS   A HD2  1 
ATOM   3403 H HD3  A LYS   A 1 158 ? 3.489  -2.129  8.175   0.60 31.63 ?  158 LYS   A HD3  1 
ATOM   3404 H HD3  B LYS   A 1 158 ? 2.493  -2.183  7.906   0.40 34.24 ?  158 LYS   A HD3  1 
ATOM   3405 H HE2  A LYS   A 1 158 ? 1.286  -2.628  8.648   0.60 32.62 ?  158 LYS   A HE2  1 
ATOM   3406 H HE2  B LYS   A 1 158 ? 0.256  -2.650  7.880   0.40 34.72 ?  158 LYS   A HE2  1 
ATOM   3407 H HE3  A LYS   A 1 158 ? 1.121  -3.351  7.255   0.60 32.62 ?  158 LYS   A HE3  1 
ATOM   3408 H HE3  B LYS   A 1 158 ? 0.376  -3.359  6.466   0.40 34.72 ?  158 LYS   A HE3  1 
ATOM   3409 H HZ1  A LYS   A 1 158 ? 1.357  -4.884  8.910   0.60 33.22 ?  158 LYS   A HZ1  1 
ATOM   3410 H HZ1  B LYS   A 1 158 ? 0.282  -4.909  8.136   0.40 35.15 ?  158 LYS   A HZ1  1 
ATOM   3411 H HZ2  A LYS   A 1 158 ? 2.470  -5.010  7.991   0.60 33.22 ?  158 LYS   A HZ2  1 
ATOM   3412 H HZ2  B LYS   A 1 158 ? 1.578  -5.013  7.498   0.40 35.15 ?  158 LYS   A HZ2  1 
ATOM   3413 H HZ3  A LYS   A 1 158 ? 2.658  -4.360  9.273   0.60 33.22 ?  158 LYS   A HZ3  1 
ATOM   3414 H HZ3  B LYS   A 1 158 ? 1.454  -4.355  8.782   0.40 35.15 ?  158 LYS   A HZ3  1 
ATOM   3415 N N    A ASN   A 1 159 ? 3.573  -1.248  3.000   0.60 22.55 ?  159 ASN   A N    1 
ATOM   3416 N N    B ASN   A 1 159 ? 3.349  -1.162  3.079   0.40 24.62 ?  159 ASN   A N    1 
ATOM   3417 C CA   A ASN   A 1 159 ? 2.872  -1.963  1.938   0.60 22.80 ?  159 ASN   A CA   1 
ATOM   3418 C CA   B ASN   A 1 159 ? 2.839  -1.802  1.871   0.40 24.22 ?  159 ASN   A CA   1 
ATOM   3419 C C    A ASN   A 1 159 ? 3.745  -3.069  1.334   0.60 21.21 ?  159 ASN   A C    1 
ATOM   3420 C C    B ASN   A 1 159 ? 3.867  -2.762  1.290   0.40 22.24 ?  159 ASN   A C    1 
ATOM   3421 O O    A ASN   A 1 159 ? 3.284  -4.198  1.131   0.60 20.98 ?  159 ASN   A O    1 
ATOM   3422 O O    B ASN   A 1 159 ? 3.511  -3.830  0.779   0.40 21.56 ?  159 ASN   A O    1 
ATOM   3423 C CB   A ASN   A 1 159 ? 2.382  -0.967  0.881   0.60 24.69 ?  159 ASN   A CB   1 
ATOM   3424 C CB   B ASN   A 1 159 ? 2.433  -0.750  0.841   0.40 25.86 ?  159 ASN   A CB   1 
ATOM   3425 C CG   A ASN   A 1 159 ? 1.272  -0.067  1.403   0.60 26.65 ?  159 ASN   A CG   1 
ATOM   3426 C CG   B ASN   A 1 159 ? 1.039  -0.209  1.081   0.40 27.65 ?  159 ASN   A CG   1 
ATOM   3427 O OD1  A ASN   A 1 159 ? 0.436  -0.498  2.196   0.60 27.05 ?  159 ASN   A OD1  1 
ATOM   3428 O OD1  B ASN   A 1 159 ? 0.105  -0.967  1.342   0.40 28.29 ?  159 ASN   A OD1  1 
ATOM   3429 N ND2  A ASN   A 1 159 ? 1.257  1.187   0.959   0.60 27.95 ?  159 ASN   A ND2  1 
ATOM   3430 N ND2  B ASN   A 1 159 ? 0.893  1.105   1.001   0.40 28.32 ?  159 ASN   A ND2  1 
ATOM   3431 H H    A ASN   A 1 159 ? 3.748  -0.421  2.835   0.60 27.05 ?  159 ASN   A H    1 
ATOM   3432 H H    B ASN   A 1 159 ? 3.343  -0.303  3.066   0.40 29.54 ?  159 ASN   A H    1 
ATOM   3433 H HA   A ASN   A 1 159 ? 2.090  -2.381  2.329   0.60 27.35 ?  159 ASN   A HA   1 
ATOM   3434 H HA   B ASN   A 1 159 ? 2.050  -2.316  2.103   0.40 29.05 ?  159 ASN   A HA   1 
ATOM   3435 H HB2  A ASN   A 1 159 ? 3.119  -0.402  0.609   0.60 29.62 ?  159 ASN   A HB2  1 
ATOM   3436 H HB2  B ASN   A 1 159 ? 3.055  -0.008  0.884   0.40 31.02 ?  159 ASN   A HB2  1 
ATOM   3437 H HB3  A ASN   A 1 159 ? 2.037  -1.460  0.121   0.60 29.62 ?  159 ASN   A HB3  1 
ATOM   3438 H HB3  B ASN   A 1 159 ? 2.454  -1.152  -0.042  0.40 31.02 ?  159 ASN   A HB3  1 
ATOM   3439 H HD21 A ASN   A 1 159 ? 0.647  1.731   1.224   0.60 33.53 ?  159 ASN   A HD21 1 
ATOM   3440 H HD21 B ASN   A 1 159 ? 0.123  1.458   1.131   0.40 33.97 ?  159 ASN   A HD21 1 
ATOM   3441 H HD22 A ASN   A 1 159 ? 1.857  1.455   0.411   0.60 33.53 ?  159 ASN   A HD22 1 
ATOM   3442 H HD22 B ASN   A 1 159 ? 1.572  1.601   0.819   0.40 33.97 ?  159 ASN   A HD22 1 
ATOM   3443 N N    A LEU   A 1 160 ? 5.016  -2.771  1.064   0.60 19.73 ?  160 LEU   A N    1 
ATOM   3444 N N    B LEU   A 1 160 ? 5.148  -2.401  1.360   0.40 20.57 ?  160 LEU   A N    1 
ATOM   3445 C CA   A LEU   A 1 160 ? 5.915  -3.768  0.487   0.60 18.61 ?  160 LEU   A CA   1 
ATOM   3446 C CA   B LEU   A 1 160 ? 6.188  -3.329  0.931   0.40 18.37 ?  160 LEU   A CA   1 
ATOM   3447 C C    A LEU   A 1 160 ? 6.137  -4.934  1.441   0.60 17.94 ?  160 LEU   A C    1 
ATOM   3448 C C    B LEU   A 1 160 ? 6.316  -4.497  1.902   0.40 16.49 ?  160 LEU   A C    1 
ATOM   3449 O O    A LEU   A 1 160 ? 6.185  -6.097  1.018   0.60 18.23 ?  160 LEU   A O    1 
ATOM   3450 O O    B LEU   A 1 160 ? 6.356  -5.661  1.486   0.40 16.42 ?  160 LEU   A O    1 
ATOM   3451 C CB   A LEU   A 1 160 ? 7.248  -3.106  0.149   0.60 17.63 ?  160 LEU   A CB   1 
ATOM   3452 C CB   B LEU   A 1 160 ? 7.521  -2.600  0.779   0.40 18.47 ?  160 LEU   A CB   1 
ATOM   3453 C CG   A LEU   A 1 160 ? 8.369  -4.067  -0.223  0.60 18.01 ?  160 LEU   A CG   1 
ATOM   3454 C CG   B LEU   A 1 160 ? 8.680  -3.526  0.410   0.40 18.71 ?  160 LEU   A CG   1 
ATOM   3455 C CD1  A LEU   A 1 160 ? 7.952  -4.854  -1.444  0.60 18.44 ?  160 LEU   A CD1  1 
ATOM   3456 C CD1  B LEU   A 1 160 ? 8.361  -4.334  -0.843  0.40 18.90 ?  160 LEU   A CD1  1 
ATOM   3457 C CD2  A LEU   A 1 160 ? 9.667  -3.322  -0.468  0.60 17.90 ?  160 LEU   A CD2  1 
ATOM   3458 C CD2  B LEU   A 1 160 ? 9.950  -2.727  0.221   0.40 18.68 ?  160 LEU   A CD2  1 
ATOM   3459 H H    A LEU   A 1 160 ? 5.377  -2.015  1.218   0.60 23.66 ?  160 LEU   A H    1 
ATOM   3460 H H    B LEU   A 1 160 ? 5.429  -1.634  1.635   0.40 24.67 ?  160 LEU   A H    1 
ATOM   3461 H HA   A LEU   A 1 160 ? 5.521  -4.115  -0.331  0.60 22.32 ?  160 LEU   A HA   1 
ATOM   3462 H HA   B LEU   A 1 160 ? 5.938  -3.684  0.069   0.40 22.03 ?  160 LEU   A HA   1 
ATOM   3463 H HB2  A LEU   A 1 160 ? 7.107  -2.509  -0.602  0.60 21.14 ?  160 LEU   A HB2  1 
ATOM   3464 H HB2  B LEU   A 1 160 ? 7.434  -1.934  0.079   0.40 22.15 ?  160 LEU   A HB2  1 
ATOM   3465 H HB3  A LEU   A 1 160 ? 7.537  -2.598  0.921   0.60 21.14 ?  160 LEU   A HB3  1 
ATOM   3466 H HB3  B LEU   A 1 160 ? 7.739  -2.166  1.620   0.40 22.15 ?  160 LEU   A HB3  1 
ATOM   3467 H HG   A LEU   A 1 160 ? 8.520  -4.689  0.505   0.60 21.59 ?  160 LEU   A HG   1 
ATOM   3468 H HG   B LEU   A 1 160 ? 8.830  -4.149  1.138   0.40 22.44 ?  160 LEU   A HG   1 
ATOM   3469 H HD11 A LEU   A 1 160 ? 8.686  -5.420  -1.712  0.60 22.11 ?  160 LEU   A HD11 1 
ATOM   3470 H HD11 B LEU   A 1 160 ? 9.172  -4.767  -1.151  0.40 22.66 ?  160 LEU   A HD11 1 
ATOM   3471 H HD12 A LEU   A 1 160 ? 7.179  -5.399  -1.222  0.60 22.11 ?  160 LEU   A HD12 1 
ATOM   3472 H HD12 B LEU   A 1 160 ? 7.692  -5.004  -0.627  0.40 22.66 ?  160 LEU   A HD12 1 
ATOM   3473 H HD13 A LEU   A 1 160 ? 7.726  -4.234  -2.155  0.60 22.11 ?  160 LEU   A HD13 1 
ATOM   3474 H HD13 B LEU   A 1 160 ? 8.023  -3.737  -1.527  0.40 22.66 ?  160 LEU   A HD13 1 
ATOM   3475 H HD21 A LEU   A 1 160 ? 10.357 -3.962  -0.701  0.60 21.46 ?  160 LEU   A HD21 1 
ATOM   3476 H HD21 B LEU   A 1 160 ? 10.674 -3.332  -0.004  0.40 22.40 ?  160 LEU   A HD21 1 
ATOM   3477 H HD22 A LEU   A 1 160 ? 9.538  -2.693  -1.196  0.60 21.46 ?  160 LEU   A HD22 1 
ATOM   3478 H HD22 B LEU   A 1 160 ? 9.818  -2.087  -0.496  0.40 22.40 ?  160 LEU   A HD22 1 
ATOM   3479 H HD23 A LEU   A 1 160 ? 9.916  -2.845  0.340   0.60 21.46 ?  160 LEU   A HD23 1 
ATOM   3480 H HD23 B LEU   A 1 160 ? 10.154 -2.260  1.047   0.40 22.40 ?  160 LEU   A HD23 1 
ATOM   3481 N N    A TYR   A 1 161 ? 6.309  -4.640  2.728   0.60 17.07 ?  161 TYR   A N    1 
ATOM   3482 N N    B TYR   A 1 161 ? 6.392  -4.207  3.202   0.40 15.28 ?  161 TYR   A N    1 
ATOM   3483 C CA   A TYR   A 1 161 ? 6.468  -5.692  3.724   0.60 17.05 ?  161 TYR   A CA   1 
ATOM   3484 C CA   B TYR   A 1 161 ? 6.475  -5.278  4.189   0.40 15.11 ?  161 TYR   A CA   1 
ATOM   3485 C C    A TYR   A 1 161 ? 5.322  -6.689  3.655   0.60 17.34 ?  161 TYR   A C    1 
ATOM   3486 C C    B TYR   A 1 161 ? 5.313  -6.254  4.036   0.40 15.32 ?  161 TYR   A C    1 
ATOM   3487 O O    A TYR   A 1 161 ? 5.544  -7.902  3.586   0.60 16.97 ?  161 TYR   A O    1 
ATOM   3488 O O    B TYR   A 1 161 ? 5.501  -7.474  4.107   0.40 14.80 ?  161 TYR   A O    1 
ATOM   3489 C CB   A TYR   A 1 161 ? 6.551  -5.076  5.119   0.60 16.83 ?  161 TYR   A CB   1 
ATOM   3490 C CB   B TYR   A 1 161 ? 6.513  -4.674  5.593   0.40 15.38 ?  161 TYR   A CB   1 
ATOM   3491 C CG   A TYR   A 1 161 ? 6.455  -6.092  6.229   0.60 16.55 ?  161 TYR   A CG   1 
ATOM   3492 C CG   B TYR   A 1 161 ? 6.427  -5.679  6.717   0.40 15.45 ?  161 TYR   A CG   1 
ATOM   3493 C CD1  A TYR   A 1 161 ? 7.580  -6.770  6.672   0.60 16.25 ?  161 TYR   A CD1  1 
ATOM   3494 C CD1  B TYR   A 1 161 ? 7.558  -6.345  7.177   0.40 15.62 ?  161 TYR   A CD1  1 
ATOM   3495 C CD2  A TYR   A 1 161 ? 5.236  -6.385  6.831   0.60 16.69 ?  161 TYR   A CD2  1 
ATOM   3496 C CD2  B TYR   A 1 161 ? 5.218  -5.935  7.345   0.40 15.67 ?  161 TYR   A CD2  1 
ATOM   3497 C CE1  A TYR   A 1 161 ? 7.498  -7.710  7.677   0.60 15.98 ?  161 TYR   A CE1  1 
ATOM   3498 C CE1  B TYR   A 1 161 ? 7.476  -7.254  8.216   0.40 16.49 ?  161 TYR   A CE1  1 
ATOM   3499 C CE2  A TYR   A 1 161 ? 5.145  -7.323  7.837   0.60 16.24 ?  161 TYR   A CE2  1 
ATOM   3500 C CE2  B TYR   A 1 161 ? 5.127  -6.837  8.381   0.40 16.56 ?  161 TYR   A CE2  1 
ATOM   3501 C CZ   A TYR   A 1 161 ? 6.280  -7.984  8.255   0.60 16.28 ?  161 TYR   A CZ   1 
ATOM   3502 C CZ   B TYR   A 1 161 ? 6.255  -7.492  8.815   0.40 17.37 ?  161 TYR   A CZ   1 
ATOM   3503 O OH   A TYR   A 1 161 ? 6.199  -8.923  9.258   0.60 16.70 ?  161 TYR   A OH   1 
ATOM   3504 O OH   B TYR   A 1 161 ? 6.148  -8.389  9.852   0.40 18.67 ?  161 TYR   A OH   1 
ATOM   3505 H H    A TYR   A 1 161 ? 6.330  -3.857  3.049   0.60 20.47 ?  161 TYR   A H    1 
ATOM   3506 H H    B TYR   A 1 161 ? 6.392  -3.410  3.535   0.40 18.32 ?  161 TYR   A H    1 
ATOM   3507 H HA   A TYR   A 1 161 ? 7.282  -6.186  3.554   0.60 20.45 ?  161 TYR   A HA   1 
ATOM   3508 H HA   B TYR   A 1 161 ? 7.299  -5.766  4.056   0.40 18.12 ?  161 TYR   A HA   1 
ATOM   3509 H HB2  A TYR   A 1 161 ? 7.402  -4.625  5.204   0.60 20.19 ?  161 TYR   A HB2  1 
ATOM   3510 H HB2  B TYR   A 1 161 ? 7.344  -4.186  5.703   0.40 18.44 ?  161 TYR   A HB2  1 
ATOM   3511 H HB3  A TYR   A 1 161 ? 5.823  -4.449  5.230   0.60 20.19 ?  161 TYR   A HB3  1 
ATOM   3512 H HB3  B TYR   A 1 161 ? 5.764  -4.063  5.693   0.40 18.44 ?  161 TYR   A HB3  1 
ATOM   3513 H HD1  A TYR   A 1 161 ? 8.404  -6.595  6.282   0.60 19.49 ?  161 TYR   A HD1  1 
ATOM   3514 H HD1  B TYR   A 1 161 ? 8.381  -6.180  6.777   0.40 18.73 ?  161 TYR   A HD1  1 
ATOM   3515 H HD2  A TYR   A 1 161 ? 4.467  -5.948  6.550   0.60 20.01 ?  161 TYR   A HD2  1 
ATOM   3516 H HD2  B TYR   A 1 161 ? 4.451  -5.494  7.063   0.40 18.79 ?  161 TYR   A HD2  1 
ATOM   3517 H HE1  A TYR   A 1 161 ? 8.262  -8.160  7.967   0.60 19.17 ?  161 TYR   A HE1  1 
ATOM   3518 H HE1  B TYR   A 1 161 ? 8.240  -7.696  8.514   0.40 19.78 ?  161 TYR   A HE1  1 
ATOM   3519 H HE2  A TYR   A 1 161 ? 4.319  -7.511  8.235   0.60 19.47 ?  161 TYR   A HE2  1 
ATOM   3520 H HE2  B TYR   A 1 161 ? 4.306  -7.001  8.790   0.40 19.86 ?  161 TYR   A HE2  1 
ATOM   3521 H HH   A TYR   A 1 161 ? 6.951  -9.252  9.424   0.60 20.02 ?  161 TYR   A HH   1 
ATOM   3522 H HH   B TYR   A 1 161 ? 6.896  -8.724  10.026  0.40 22.39 ?  161 TYR   A HH   1 
ATOM   3523 N N    A ASP   A 1 162 ? 4.083  -6.191  3.677   0.60 18.60 ?  162 ASP   A N    1 
ATOM   3524 N N    B ASP   A 1 162 ? 4.107  -5.730  3.799   0.40 16.30 ?  162 ASP   A N    1 
ATOM   3525 C CA   A ASP   A 1 162 ? 2.930  -7.085  3.652   0.60 19.08 ?  162 ASP   A CA   1 
ATOM   3526 C CA   B ASP   A 1 162 ? 2.936  -6.583  3.607   0.40 17.45 ?  162 ASP   A CA   1 
ATOM   3527 C C    A ASP   A 1 162 ? 2.949  -7.965  2.406   0.60 19.05 ?  162 ASP   A C    1 
ATOM   3528 C C    B ASP   A 1 162 ? 3.056  -7.412  2.338   0.40 17.54 ?  162 ASP   A C    1 
ATOM   3529 O O    A ASP   A 1 162 ? 2.574  -9.140  2.461   0.60 19.29 ?  162 ASP   A O    1 
ATOM   3530 O O    B ASP   A 1 162 ? 2.770  -8.616  2.341   0.40 18.04 ?  162 ASP   A O    1 
ATOM   3531 C CB   A ASP   A 1 162 ? 1.628  -6.276  3.743   0.60 20.08 ?  162 ASP   A CB   1 
ATOM   3532 C CB   B ASP   A 1 162 ? 1.677  -5.722  3.527   0.40 19.11 ?  162 ASP   A CB   1 
ATOM   3533 C CG   A ASP   A 1 162 ? 1.413  -5.651  5.113   0.60 21.65 ?  162 ASP   A CG   1 
ATOM   3534 C CG   B ASP   A 1 162 ? 1.076  -5.427  4.879   0.40 20.32 ?  162 ASP   A CG   1 
ATOM   3535 O OD1  A ASP   A 1 162 ? 2.072  -6.082  6.082   0.60 22.44 ?  162 ASP   A OD1  1 
ATOM   3536 O OD1  B ASP   A 1 162 ? 1.698  -5.755  5.910   0.40 20.58 ?  162 ASP   A OD1  1 
ATOM   3537 O OD2  A ASP   A 1 162 ? 0.544  -4.752  5.227   0.60 22.86 -1 162 ASP   A OD2  1 
ATOM   3538 O OD2  B ASP   A 1 162 ? -0.033 -4.856  4.907   0.40 20.65 -1 162 ASP   A OD2  1 
ATOM   3539 H H    A ASP   A 1 162 ? 3.878  -5.363  3.705   0.60 22.31 ?  162 ASP   A H    1 
ATOM   3540 H H    B ASP   A 1 162 ? 3.946  -4.888  3.743   0.40 19.55 ?  162 ASP   A H    1 
ATOM   3541 H HA   A ASP   A 1 162 ? 2.950  -7.672  4.430   0.60 22.88 ?  162 ASP   A HA   1 
ATOM   3542 H HA   B ASP   A 1 162 ? 2.852  -7.195  4.351   0.40 20.93 ?  162 ASP   A HA   1 
ATOM   3543 H HB2  A ASP   A 1 162 ? 1.641  -5.564  3.086   0.60 24.08 ?  162 ASP   A HB2  1 
ATOM   3544 H HB2  B ASP   A 1 162 ? 1.904  -4.867  3.131   0.40 22.91 ?  162 ASP   A HB2  1 
ATOM   3545 H HB3  A ASP   A 1 162 ? 0.862  -6.854  3.590   0.60 24.08 ?  162 ASP   A HB3  1 
ATOM   3546 H HB3  B ASP   A 1 162 ? 1.021  -6.180  2.974   0.40 22.91 ?  162 ASP   A HB3  1 
ATOM   3547 N N    A LYS   A 1 163 ? 3.415  -7.426  1.280   0.60 19.38 ?  163 LYS   A N    1 
ATOM   3548 N N    B LYS   A 1 163 ? 3.436  -6.773  1.229   0.40 17.79 ?  163 LYS   A N    1 
ATOM   3549 C CA   A LYS   A 1 163 ? 3.474  -8.204  0.046   0.60 19.49 ?  163 LYS   A CA   1 
ATOM   3550 C CA   B LYS   A 1 163 ? 3.624  -7.509  -0.016  0.40 18.25 ?  163 LYS   A CA   1 
ATOM   3551 C C    A LYS   A 1 163 ? 4.579  -9.259  0.098   0.60 18.68 ?  163 LYS   A C    1 
ATOM   3552 C C    B LYS   A 1 163 ? 4.658  -8.612  0.162   0.40 16.84 ?  163 LYS   A C    1 
ATOM   3553 O O    A LYS   A 1 163 ? 4.402  -10.377 -0.399  0.60 19.60 ?  163 LYS   A O    1 
ATOM   3554 O O    B LYS   A 1 163 ? 4.503  -9.712  -0.380  0.40 16.34 ?  163 LYS   A O    1 
ATOM   3555 C CB   A LYS   A 1 163 ? 3.681  -7.261  -1.134  0.60 21.60 ?  163 LYS   A CB   1 
ATOM   3556 C CB   B LYS   A 1 163 ? 4.056  -6.545  -1.125  0.40 20.87 ?  163 LYS   A CB   1 
ATOM   3557 C CG   A LYS   A 1 163 ? 3.765  -7.943  -2.477  0.60 24.29 ?  163 LYS   A CG   1 
ATOM   3558 C CG   B LYS   A 1 163 ? 4.131  -7.158  -2.523  0.40 23.73 ?  163 LYS   A CG   1 
ATOM   3559 C CD   A LYS   A 1 163 ? 4.083  -6.937  -3.566  0.60 27.16 ?  163 LYS   A CD   1 
ATOM   3560 C CD   B LYS   A 1 163 ? 4.633  -6.134  -3.547  0.40 26.28 ?  163 LYS   A CD   1 
ATOM   3561 C CE   A LYS   A 1 163 ? 3.998  -7.572  -4.940  0.60 29.45 ?  163 LYS   A CE   1 
ATOM   3562 C CE   B LYS   A 1 163 ? 3.953  -6.289  -4.908  0.40 28.26 ?  163 LYS   A CE   1 
ATOM   3563 N NZ   A LYS   A 1 163 ? 4.622  -6.727  -5.991  0.60 30.77 ?  163 LYS   A NZ   1 
ATOM   3564 N NZ   B LYS   A 1 163 ? 4.860  -6.842  -5.955  0.40 29.59 ?  163 LYS   A NZ   1 
ATOM   3565 H H    A LYS   A 1 163 ? 3.699  -6.628  1.215   0.60 23.25 ?  163 LYS   A H    1 
ATOM   3566 H H    B LYS   A 1 163 ? 3.585  -5.924  1.171   0.40 21.34 ?  163 LYS   A H    1 
ATOM   3567 H HA   A LYS   A 1 163 ? 2.624  -8.664  -0.075  0.60 23.37 ?  163 LYS   A HA   1 
ATOM   3568 H HA   B LYS   A 1 163 ? 2.783  -7.916  -0.280  0.40 21.89 ?  163 LYS   A HA   1 
ATOM   3569 H HB2  A LYS   A 1 163 ? 2.938  -6.642  -1.161  0.60 25.90 ?  163 LYS   A HB2  1 
ATOM   3570 H HB2  B LYS   A 1 163 ? 3.421  -5.811  -1.166  0.40 25.03 ?  163 LYS   A HB2  1 
ATOM   3571 H HB3  A LYS   A 1 163 ? 4.508  -6.778  -0.992  0.60 25.90 ?  163 LYS   A HB3  1 
ATOM   3572 H HB3  B LYS   A 1 163 ? 4.936  -6.200  -0.912  0.40 25.03 ?  163 LYS   A HB3  1 
ATOM   3573 H HG2  A LYS   A 1 163 ? 4.471  -8.608  -2.461  0.60 29.14 ?  163 LYS   A HG2  1 
ATOM   3574 H HG2  B LYS   A 1 163 ? 4.750  -7.904  -2.518  0.40 28.46 ?  163 LYS   A HG2  1 
ATOM   3575 H HG3  A LYS   A 1 163 ? 2.913  -8.360  -2.679  0.60 29.14 ?  163 LYS   A HG3  1 
ATOM   3576 H HG3  B LYS   A 1 163 ? 3.248  -7.456  -2.789  0.40 28.46 ?  163 LYS   A HG3  1 
ATOM   3577 H HD2  A LYS   A 1 163 ? 3.442  -6.208  -3.525  0.60 32.58 ?  163 LYS   A HD2  1 
ATOM   3578 H HD2  B LYS   A 1 163 ? 4.451  -5.239  -3.220  0.40 31.53 ?  163 LYS   A HD2  1 
ATOM   3579 H HD3  A LYS   A 1 163 ? 4.984  -6.598  -3.436  0.60 32.58 ?  163 LYS   A HD3  1 
ATOM   3580 H HD3  B LYS   A 1 163 ? 5.589  -6.252  -3.675  0.40 31.53 ?  163 LYS   A HD3  1 
ATOM   3581 H HE2  A LYS   A 1 163 ? 4.445  -8.431  -4.929  0.60 35.33 ?  163 LYS   A HE2  1 
ATOM   3582 H HE2  B LYS   A 1 163 ? 3.196  -6.889  -4.826  0.40 33.90 ?  163 LYS   A HE2  1 
ATOM   3583 H HE3  A LYS   A 1 163 ? 3.066  -7.693  -5.167  0.60 35.33 ?  163 LYS   A HE3  1 
ATOM   3584 H HE3  B LYS   A 1 163 ? 3.650  -5.418  -5.206  0.40 33.90 ?  163 LYS   A HE3  1 
ATOM   3585 H HZ1  A LYS   A 1 163 ? 4.557  -7.131  -6.781  0.60 36.91 ?  163 LYS   A HZ1  1 
ATOM   3586 H HZ1  B LYS   A 1 163 ? 4.467  -6.791  -6.753  0.40 35.50 ?  163 LYS   A HZ1  1 
ATOM   3587 H HZ2  A LYS   A 1 163 ? 4.208  -5.941  -6.031  0.60 36.91 ?  163 LYS   A HZ2  1 
ATOM   3588 H HZ2  B LYS   A 1 163 ? 5.617  -6.376  -5.977  0.40 35.50 ?  163 LYS   A HZ2  1 
ATOM   3589 H HZ3  A LYS   A 1 163 ? 5.482  -6.593  -5.804  0.60 36.91 ?  163 LYS   A HZ3  1 
ATOM   3590 H HZ3  B LYS   A 1 163 ? 5.047  -7.692  -5.779  0.40 35.50 ?  163 LYS   A HZ3  1 
ATOM   3591 N N    A LEU   A 1 164 ? 5.739  -8.915  0.663   0.60 17.48 ?  164 LEU   A N    1 
ATOM   3592 N N    B LEU   A 1 164 ? 5.715  -8.337  0.931   0.40 15.43 ?  164 LEU   A N    1 
ATOM   3593 C CA   A LEU   A 1 164 ? 6.823  -9.888  0.798   0.60 16.56 ?  164 LEU   A CA   1 
ATOM   3594 C CA   B LEU   A 1 164 ? 6.794  -9.306  1.102   0.40 14.69 ?  164 LEU   A CA   1 
ATOM   3595 C C    A LEU   A 1 164 ? 6.398  -11.064 1.665   0.60 16.62 ?  164 LEU   A C    1 
ATOM   3596 C C    B LEU   A 1 164 ? 6.343  -10.506 1.923   0.40 14.57 ?  164 LEU   A C    1 
ATOM   3597 O O    A LEU   A 1 164 ? 6.700  -12.221 1.352   0.60 17.04 ?  164 LEU   A O    1 
ATOM   3598 O O    B LEU   A 1 164 ? 6.638  -11.654 1.570   0.40 14.82 ?  164 LEU   A O    1 
ATOM   3599 C CB   A LEU   A 1 164 ? 8.051  -9.216  1.409   0.60 16.32 ?  164 LEU   A CB   1 
ATOM   3600 C CB   B LEU   A 1 164 ? 7.989  -8.625  1.767   0.40 14.29 ?  164 LEU   A CB   1 
ATOM   3601 C CG   A LEU   A 1 164 ? 8.737  -8.141  0.568   0.60 16.89 ?  164 LEU   A CG   1 
ATOM   3602 C CG   B LEU   A 1 164 ? 8.821  -7.725  0.852   0.40 15.10 ?  164 LEU   A CG   1 
ATOM   3603 C CD1  A LEU   A 1 164 ? 9.602  -7.227  1.429   0.60 16.89 ?  164 LEU   A CD1  1 
ATOM   3604 C CD1  B LEU   A 1 164 ? 9.830  -6.948  1.670   0.40 15.09 ?  164 LEU   A CD1  1 
ATOM   3605 C CD2  A LEU   A 1 164 ? 9.563  -8.802  -0.515  0.60 17.36 ?  164 LEU   A CD2  1 
ATOM   3606 C CD2  B LEU   A 1 164 ? 9.518  -8.546  -0.224  0.40 15.67 ?  164 LEU   A CD2  1 
ATOM   3607 H H    A LEU   A 1 164 ? 5.922  -8.144  0.968   0.60 20.96 ?  164 LEU   A H    1 
ATOM   3608 H H    B LEU   A 1 164 ? 5.828  -7.594  1.358   0.40 18.50 ?  164 LEU   A H    1 
ATOM   3609 H HA   A LEU   A 1 164 ? 7.059  -10.239 -0.076  0.60 19.86 ?  164 LEU   A HA   1 
ATOM   3610 H HA   B LEU   A 1 164 ? 7.075  -9.619  0.232   0.40 17.62 ?  164 LEU   A HA   1 
ATOM   3611 H HB2  A LEU   A 1 164 ? 7.783  -8.812  2.244   0.60 19.57 ?  164 LEU   A HB2  1 
ATOM   3612 H HB2  B LEU   A 1 164 ? 7.665  -8.070  2.499   0.40 17.13 ?  164 LEU   A HB2  1 
ATOM   3613 H HB3  A LEU   A 1 164 ? 8.712  -9.909  1.586   0.60 19.57 ?  164 LEU   A HB3  1 
ATOM   3614 H HB3  B LEU   A 1 164 ? 8.581  -9.306  2.118   0.40 17.13 ?  164 LEU   A HB3  1 
ATOM   3615 H HG   A LEU   A 1 164 ? 8.055  -7.599  0.142   0.60 20.26 ?  164 LEU   A HG   1 
ATOM   3616 H HG   B LEU   A 1 164 ? 8.235  -7.085  0.416   0.40 18.10 ?  164 LEU   A HG   1 
ATOM   3617 H HD11 A LEU   A 1 164 ? 10.017 -6.562  0.863   0.60 20.25 ?  164 LEU   A HD11 1 
ATOM   3618 H HD11 B LEU   A 1 164 ? 10.239 -6.268  1.112   0.40 18.10 ?  164 LEU   A HD11 1 
ATOM   3619 H HD12 A LEU   A 1 164 ? 9.038  -6.792  2.093   0.60 20.25 ?  164 LEU   A HD12 1 
ATOM   3620 H HD12 B LEU   A 1 164 ? 9.370  -6.532  2.417   0.40 18.10 ?  164 LEU   A HD12 1 
ATOM   3621 H HD13 A LEU   A 1 164 ? 10.279 -7.759  1.873   0.60 20.25 ?  164 LEU   A HD13 1 
ATOM   3622 H HD13 B LEU   A 1 164 ? 10.506 -7.559  2.001   0.40 18.10 ?  164 LEU   A HD13 1 
ATOM   3623 H HD21 A LEU   A 1 164 ? 9.980  -8.109  -1.051  0.60 20.82 ?  164 LEU   A HD21 1 
ATOM   3624 H HD21 B LEU   A 1 164 ? 10.181 -7.991  -0.665  0.40 18.79 ?  164 LEU   A HD21 1 
ATOM   3625 H HD22 A LEU   A 1 164 ? 10.242 -9.353  -0.099  0.60 20.82 ?  164 LEU   A HD22 1 
ATOM   3626 H HD22 B LEU   A 1 164 ? 9.949  -9.309  0.192   0.40 18.79 ?  164 LEU   A HD22 1 
ATOM   3627 H HD23 A LEU   A 1 164 ? 8.982  -9.345  -1.067  0.60 20.82 ?  164 LEU   A HD23 1 
ATOM   3628 H HD23 B LEU   A 1 164 ? 8.859  -8.849  -0.868  0.40 18.79 ?  164 LEU   A HD23 1 
ATOM   3629 N N    A VAL   A 1 165 ? 5.710  -10.785 2.771   0.60 16.45 ?  165 VAL   A N    1 
ATOM   3630 N N    B VAL   A 1 165 ? 5.636  -10.259 3.025   0.40 14.65 ?  165 VAL   A N    1 
ATOM   3631 C CA   A VAL   A 1 165 ? 5.229  -11.845 3.650   0.60 16.27 ?  165 VAL   A CA   1 
ATOM   3632 C CA   B VAL   A 1 165 ? 5.180  -11.355 3.872   0.40 15.00 ?  165 VAL   A CA   1 
ATOM   3633 C C    A VAL   A 1 165 ? 4.182  -12.690 2.939   0.60 16.88 ?  165 VAL   A C    1 
ATOM   3634 C C    B VAL   A 1 165 ? 4.145  -12.200 3.140   0.40 14.45 ?  165 VAL   A C    1 
ATOM   3635 O O    A VAL   A 1 165 ? 4.286  -13.920 2.878   0.60 16.58 ?  165 VAL   A O    1 
ATOM   3636 O O    B VAL   A 1 165 ? 4.227  -13.434 3.120   0.40 14.64 ?  165 VAL   A O    1 
ATOM   3637 C CB   A VAL   A 1 165 ? 4.673  -11.232 4.948   0.60 16.45 ?  165 VAL   A CB   1 
ATOM   3638 C CB   B VAL   A 1 165 ? 4.639  -10.810 5.207   0.40 16.13 ?  165 VAL   A CB   1 
ATOM   3639 C CG1  A VAL   A 1 165 ? 3.904  -12.274 5.760   0.60 16.87 ?  165 VAL   A CG1  1 
ATOM   3640 C CG1  B VAL   A 1 165 ? 3.965  -11.921 6.001   0.40 17.00 ?  165 VAL   A CG1  1 
ATOM   3641 C CG2  A VAL   A 1 165 ? 5.797  -10.603 5.764   0.60 17.06 ?  165 VAL   A CG2  1 
ATOM   3642 C CG2  B VAL   A 1 165 ? 5.764  -10.174 6.012   0.40 16.44 ?  165 VAL   A CG2  1 
ATOM   3643 H H    A VAL   A 1 165 ? 5.506  -10.001 3.034   0.60 19.72 ?  165 VAL   A H    1 
ATOM   3644 H H    B VAL   A 1 165 ? 5.414  -9.472  3.299   0.40 17.57 ?  165 VAL   A H    1 
ATOM   3645 H HA   A VAL   A 1 165 ? 5.966  -12.433 3.890   0.60 19.51 ?  165 VAL   A HA   1 
ATOM   3646 H HA   B VAL   A 1 165 ? 5.937  -11.922 4.075   0.40 17.99 ?  165 VAL   A HA   1 
ATOM   3647 H HB   A VAL   A 1 165 ? 4.050  -10.530 4.713   0.60 19.73 ?  165 VAL   A HB   1 
ATOM   3648 H HB   B VAL   A 1 165 ? 3.978  -10.121 5.028   0.40 19.34 ?  165 VAL   A HB   1 
ATOM   3649 H HG11 A VAL   A 1 165 ? 3.810  -11.951 6.670   0.60 20.24 ?  165 VAL   A HG11 1 
ATOM   3650 H HG11 B VAL   A 1 165 ? 3.879  -11.639 6.926   0.40 20.39 ?  165 VAL   A HG11 1 
ATOM   3651 H HG12 A VAL   A 1 165 ? 3.025  -12.396 5.365   0.60 20.24 ?  165 VAL   A HG12 1 
ATOM   3652 H HG12 B VAL   A 1 165 ? 3.087  -12.091 5.626   0.40 20.39 ?  165 VAL   A HG12 1 
ATOM   3653 H HG13 A VAL   A 1 165 ? 4.394  -13.107 5.751   0.60 20.24 ?  165 VAL   A HG13 1 
ATOM   3654 H HG13 B VAL   A 1 165 ? 4.511  -12.720 5.949   0.40 20.39 ?  165 VAL   A HG13 1 
ATOM   3655 H HG21 A VAL   A 1 165 ? 5.426  -10.227 6.578   0.60 20.46 ?  165 VAL   A HG21 1 
ATOM   3656 H HG21 B VAL   A 1 165 ? 5.403  -9.829  6.844   0.40 19.71 ?  165 VAL   A HG21 1 
ATOM   3657 H HG22 A VAL   A 1 165 ? 6.452  -11.284 5.982   0.60 20.46 ?  165 VAL   A HG22 1 
ATOM   3658 H HG22 B VAL   A 1 165 ? 6.438  -10.847 6.197   0.40 19.71 ?  165 VAL   A HG22 1 
ATOM   3659 H HG23 A VAL   A 1 165 ? 6.213  -9.902  5.236   0.60 20.46 ?  165 VAL   A HG23 1 
ATOM   3660 H HG23 B VAL   A 1 165 ? 6.154  -9.450  5.496   0.40 19.71 ?  165 VAL   A HG23 1 
ATOM   3661 N N    A SER   A 1 166 ? 3.156  -12.037 2.391   0.60 18.14 ?  166 SER   A N    1 
ATOM   3662 N N    B SER   A 1 166 ? 3.157  -11.550 2.525   0.40 14.31 ?  166 SER   A N    1 
ATOM   3663 C CA   A SER   A 1 166 ? 2.027  -12.767 1.824   0.60 19.05 ?  166 SER   A CA   1 
ATOM   3664 C CA   B SER   A 1 166 ? 2.039  -12.287 1.947   0.40 14.99 ?  166 SER   A CA   1 
ATOM   3665 C C    A SER   A 1 166 ? 2.449  -13.621 0.641   0.60 19.45 ?  166 SER   A C    1 
ATOM   3666 C C    B SER   A 1 166 ? 2.431  -13.086 0.712   0.40 15.51 ?  166 SER   A C    1 
ATOM   3667 O O    A SER   A 1 166 ? 1.856  -14.682 0.401   0.60 20.72 ?  166 SER   A O    1 
ATOM   3668 O O    B SER   A 1 166 ? 1.696  -14.006 0.334   0.40 16.84 ?  166 SER   A O    1 
ATOM   3669 C CB   A SER   A 1 166 ? 0.926  -11.787 1.405   0.60 20.28 ?  166 SER   A CB   1 
ATOM   3670 C CB   B SER   A 1 166 ? 0.912  -11.330 1.570   0.40 16.24 ?  166 SER   A CB   1 
ATOM   3671 O OG   A SER   A 1 166 ? 0.398  -11.080 2.520   0.60 21.44 ?  166 SER   A OG   1 
ATOM   3672 O OG   B SER   A 1 166 ? 1.175  -10.735 0.316   0.40 17.29 ?  166 SER   A OG   1 
ATOM   3673 H H    A SER   A 1 166 ? 3.088  -11.191 2.342   0.60 21.76 ?  166 SER   A H    1 
ATOM   3674 H H    B SER   A 1 166 ? 3.106  -10.695 2.442   0.40 17.16 ?  166 SER   A H    1 
ATOM   3675 H HA   A SER   A 1 166 ? 1.652  -13.362 2.493   0.60 22.85 ?  166 SER   A HA   1 
ATOM   3676 H HA   B SER   A 1 166 ? 1.692  -12.906 2.607   0.40 17.98 ?  166 SER   A HA   1 
ATOM   3677 H HB2  A SER   A 1 166 ? 1.294  -11.149 0.773   0.60 24.32 ?  166 SER   A HB2  1 
ATOM   3678 H HB2  B SER   A 1 166 ? 0.077  -11.827 1.518   0.40 19.47 ?  166 SER   A HB2  1 
ATOM   3679 H HB3  A SER   A 1 166 ? 0.200  -12.279 0.988   0.60 24.32 ?  166 SER   A HB3  1 
ATOM   3680 H HB3  B SER   A 1 166 ? 0.839  -10.636 2.245   0.40 19.47 ?  166 SER   A HB3  1 
ATOM   3681 H HG   A SER   A 1 166 ? 1.017  -10.634 2.889   0.60 25.71 ?  166 SER   A HG   1 
ATOM   3682 H HG   B SER   A 1 166 ? 0.549  -10.207 0.111   0.40 20.74 ?  166 SER   A HG   1 
ATOM   3683 N N    A SER   A 1 167 ? 3.462  -13.184 -0.105  0.60 19.33 ?  167 SER   A N    1 
ATOM   3684 N N    B SER   A 1 167 ? 3.547  -12.747 0.061   0.40 15.73 ?  167 SER   A N    1 
ATOM   3685 C CA   A SER   A 1 167 ? 3.917  -13.898 -1.286  0.60 19.79 ?  167 SER   A CA   1 
ATOM   3686 C CA   B SER   A 1 167 ? 3.985  -13.457 -1.135  0.40 16.55 ?  167 SER   A CA   1 
ATOM   3687 C C    A SER   A 1 167 ? 5.085  -14.831 -0.999  0.60 19.55 ?  167 SER   A C    1 
ATOM   3688 C C    B SER   A 1 167 ? 5.140  -14.418 -0.873  0.40 16.89 ?  167 SER   A C    1 
ATOM   3689 O O    A SER   A 1 167 ? 5.594  -15.464 -1.929  0.60 20.41 ?  167 SER   A O    1 
ATOM   3690 O O    B SER   A 1 167 ? 5.617  -15.059 -1.815  0.40 17.55 ?  167 SER   A O    1 
ATOM   3691 C CB   A SER   A 1 167 ? 4.290  -12.906 -2.396  0.60 20.36 ?  167 SER   A CB   1 
ATOM   3692 C CB   B SER   A 1 167 ? 4.385  -12.466 -2.237  0.40 17.26 ?  167 SER   A CB   1 
ATOM   3693 O OG   A SER   A 1 167 ? 5.442  -12.155 -2.051  0.60 20.32 ?  167 SER   A OG   1 
ATOM   3694 O OG   B SER   A 1 167 ? 5.454  -11.634 -1.815  0.40 17.55 ?  167 SER   A OG   1 
ATOM   3695 H H    A SER   A 1 167 ? 3.902  -12.459 0.057   0.60 23.18 ?  167 SER   A H    1 
ATOM   3696 H H    B SER   A 1 167 ? 4.065  -12.093 0.293   0.40 18.86 ?  167 SER   A H    1 
ATOM   3697 H HA   A SER   A 1 167 ? 3.190  -14.439 -1.620  0.60 23.73 ?  167 SER   A HA   1 
ATOM   3698 H HA   B SER   A 1 167 ? 3.234  -13.970 -1.471  0.40 19.85 ?  167 SER   A HA   1 
ATOM   3699 H HB2  A SER   A 1 167 ? 4.471  -13.397 -3.212  0.60 24.42 ?  167 SER   A HB2  1 
ATOM   3700 H HB2  B SER   A 1 167 ? 4.669  -12.967 -3.020  0.40 20.70 ?  167 SER   A HB2  1 
ATOM   3701 H HB3  A SER   A 1 167 ? 3.543  -12.296 -2.543  0.60 24.42 ?  167 SER   A HB3  1 
ATOM   3702 H HB3  B SER   A 1 167 ? 3.617  -11.916 -2.466  0.40 20.70 ?  167 SER   A HB3  1 
ATOM   3703 H HG   A SER   A 1 167 ? 5.291  -11.706 -1.353  0.60 24.37 ?  167 SER   A HG   1 
ATOM   3704 H HG   B SER   A 1 167 ? 5.212  -11.178 -1.152  0.40 21.05 ?  167 SER   A HG   1 
ATOM   3705 N N    A PHE   A 1 168 ? 5.509  -14.952 0.258   0.60 18.74 ?  168 PHE   A N    1 
ATOM   3706 N N    B PHE   A 1 168 ? 5.602  -14.532 0.369   0.40 16.81 ?  168 PHE   A N    1 
ATOM   3707 C CA   A PHE   A 1 168 ? 6.704  -15.733 0.547   0.60 18.86 ?  168 PHE   A CA   1 
ATOM   3708 C CA   B PHE   A 1 168 ? 6.760  -15.362 0.677   0.40 17.55 ?  168 PHE   A CA   1 
ATOM   3709 C C    A PHE   A 1 168 ? 6.414  -17.218 0.430   0.60 20.92 ?  168 PHE   A C    1 
ATOM   3710 C C    B PHE   A 1 168 ? 6.387  -16.839 0.647   0.40 18.65 ?  168 PHE   A C    1 
ATOM   3711 O O    A PHE   A 1 168 ? 5.461  -17.731 1.025   0.60 22.14 ?  168 PHE   A O    1 
ATOM   3712 O O    B PHE   A 1 168 ? 5.448  -17.267 1.330   0.40 18.91 ?  168 PHE   A O    1 
ATOM   3713 C CB   A PHE   A 1 168 ? 7.246  -15.452 1.943   0.60 17.46 ?  168 PHE   A CB   1 
ATOM   3714 C CB   B PHE   A 1 168 ? 7.299  -15.005 2.060   0.40 17.33 ?  168 PHE   A CB   1 
ATOM   3715 C CG   A PHE   A 1 168 ? 8.510  -16.212 2.241   0.60 16.32 ?  168 PHE   A CG   1 
ATOM   3716 C CG   B PHE   A 1 168 ? 8.563  -15.730 2.417   0.40 17.16 ?  168 PHE   A CG   1 
ATOM   3717 C CD1  A PHE   A 1 168 ? 9.690  -15.863 1.613   0.60 16.55 ?  168 PHE   A CD1  1 
ATOM   3718 C CD1  B PHE   A 1 168 ? 9.764  -15.352 1.848   0.40 17.62 ?  168 PHE   A CD1  1 
ATOM   3719 C CD2  A PHE   A 1 168 ? 8.516  -17.297 3.104   0.60 16.24 ?  168 PHE   A CD2  1 
ATOM   3720 C CD2  B PHE   A 1 168 ? 8.553  -16.785 3.315   0.40 17.14 ?  168 PHE   A CD2  1 
ATOM   3721 C CE1  A PHE   A 1 168 ? 10.859 -16.559 1.858   0.60 16.27 ?  168 PHE   A CE1  1 
ATOM   3722 C CE1  B PHE   A 1 168 ? 10.933 -16.011 2.165   0.40 17.66 ?  168 PHE   A CE1  1 
ATOM   3723 C CE2  A PHE   A 1 168 ? 9.687  -17.996 3.353   0.60 16.60 ?  168 PHE   A CE2  1 
ATOM   3724 C CE2  B PHE   A 1 168 ? 9.724  -17.450 3.638   0.40 17.31 ?  168 PHE   A CE2  1 
ATOM   3725 C CZ   A PHE   A 1 168 ? 10.858 -17.624 2.728   0.60 16.50 ?  168 PHE   A CZ   1 
ATOM   3726 C CZ   B PHE   A 1 168 ? 10.914 -17.062 3.061   0.40 17.52 ?  168 PHE   A CZ   1 
ATOM   3727 H H    A PHE   A 1 168 ? 5.122  -14.609 0.945   0.60 22.47 ?  168 PHE   A H    1 
ATOM   3728 H H    B PHE   A 1 168 ? 5.267  -14.123 1.051   0.40 20.15 ?  168 PHE   A H    1 
ATOM   3729 H HA   A PHE   A 1 168 ? 7.390  -15.508 -0.098  0.60 22.62 ?  168 PHE   A HA   1 
ATOM   3730 H HA   B PHE   A 1 168 ? 7.456  -15.198 0.016   0.40 21.05 ?  168 PHE   A HA   1 
ATOM   3731 H HB2  A PHE   A 1 168 ? 7.441  -14.508 2.018   0.60 20.94 ?  168 PHE   A HB2  1 
ATOM   3732 H HB2  B PHE   A 1 168 ? 7.482  -14.050 2.087   0.40 20.79 ?  168 PHE   A HB2  1 
ATOM   3733 H HB3  A PHE   A 1 168 ? 6.577  -15.710 2.596   0.60 20.94 ?  168 PHE   A HB3  1 
ATOM   3734 H HB3  B PHE   A 1 168 ? 6.627  -15.228 2.721   0.40 20.79 ?  168 PHE   A HB3  1 
ATOM   3735 H HD1  A PHE   A 1 168 ? 9.702  -15.145 1.024   0.60 19.85 ?  168 PHE   A HD1  1 
ATOM   3736 H HD1  B PHE   A 1 168 ? 9.782  -14.643 1.241   0.40 21.13 ?  168 PHE   A HD1  1 
ATOM   3737 H HD2  A PHE   A 1 168 ? 7.726  -17.555 3.526   0.60 19.47 ?  168 PHE   A HD2  1 
ATOM   3738 H HD2  B PHE   A 1 168 ? 7.747  -17.047 3.704   0.40 20.56 ?  168 PHE   A HD2  1 
ATOM   3739 H HE1  A PHE   A 1 168 ? 11.649 -16.308 1.434   0.60 19.51 ?  168 PHE   A HE1  1 
ATOM   3740 H HE1  B PHE   A 1 168 ? 11.734 -15.745 1.775   0.40 21.18 ?  168 PHE   A HE1  1 
ATOM   3741 H HE2  A PHE   A 1 168 ? 9.679  -18.722 3.938   0.60 19.91 ?  168 PHE   A HE2  1 
ATOM   3742 H HE2  B PHE   A 1 168 ? 9.703  -18.154 4.242   0.40 20.76 ?  168 PHE   A HE2  1 
ATOM   3743 H HZ   A PHE   A 1 168 ? 11.643 -18.097 2.892   0.60 19.79 ?  168 PHE   A HZ   1 
ATOM   3744 H HZ   B PHE   A 1 168 ? 11.701 -17.503 3.277   0.40 21.01 ?  168 PHE   A HZ   1 
ATOM   3745 N N    A LEU   A 1 169 ? 7.267  -17.913 -0.311  0.60 23.28 ?  169 LEU   A N    1 
ATOM   3746 N N    B LEU   A 1 169 ? 7.134  -17.621 -0.130  0.40 20.77 ?  169 LEU   A N    1 
ATOM   3747 C CA   A LEU   A 1 169 ? 7.104  -19.338 -0.487  0.60 27.23 ?  169 LEU   A CA   1 
ATOM   3748 C CA   B LEU   A 1 169 ? 6.886  -19.055 -0.225  0.40 23.07 ?  169 LEU   A CA   1 
ATOM   3749 C C    A LEU   A 1 169 ? 7.994  -20.081 0.494   0.60 28.58 ?  169 LEU   A C    1 
ATOM   3750 C C    B LEU   A 1 169 ? 7.724  -19.812 0.801   0.40 22.85 ?  169 LEU   A C    1 
ATOM   3751 O O    A LEU   A 1 169 ? 7.544  -20.488 1.566   0.60 29.11 ?  169 LEU   A O    1 
ATOM   3752 O O    B LEU   A 1 169 ? 7.182  -20.512 1.659   0.40 22.72 ?  169 LEU   A O    1 
ATOM   3753 C CB   A LEU   A 1 169 ? 7.441  -19.734 -1.923  0.60 29.06 ?  169 LEU   A CB   1 
ATOM   3754 C CB   B LEU   A 1 169 ? 7.191  -19.574 -1.634  0.40 25.18 ?  169 LEU   A CB   1 
ATOM   3755 C CG   A LEU   A 1 169 ? 7.093  -21.176 -2.284  0.60 30.63 ?  169 LEU   A CG   1 
ATOM   3756 C CG   B LEU   A 1 169 ? 6.970  -21.075 -1.859  0.40 26.82 ?  169 LEU   A CG   1 
ATOM   3757 C CD1  A LEU   A 1 169 ? 5.668  -21.499 -1.862  0.60 31.25 ?  169 LEU   A CD1  1 
ATOM   3758 C CD1  B LEU   A 1 169 ? 5.567  -21.485 -1.439  0.40 27.48 ?  169 LEU   A CD1  1 
ATOM   3759 C CD2  A LEU   A 1 169 ? 7.274  -21.403 -3.773  0.60 31.06 ?  169 LEU   A CD2  1 
ATOM   3760 C CD2  B LEU   A 1 169 ? 7.223  -21.458 -3.315  0.40 27.44 ?  169 LEU   A CD2  1 
ATOM   3761 O OXT  A LEU   A 1 169 ? 9.181  -20.279 0.240   0.60 28.79 -1 169 LEU   A OXT  1 
ATOM   3762 O OXT  B LEU   A 1 169 ? 8.957  -19.742 0.795   0.40 22.59 -1 169 LEU   A OXT  1 
ATOM   3763 H H    A LEU   A 1 169 ? 7.946  -17.578 -0.723  0.60 27.92 ?  169 LEU   A H    1 
ATOM   3764 H H    B LEU   A 1 169 ? 7.790  -17.345 -0.614  0.40 24.91 ?  169 LEU   A H    1 
ATOM   3765 H HA   A LEU   A 1 169 ? 6.182  -19.570 -0.300  0.60 32.67 ?  169 LEU   A HA   1 
ATOM   3766 H HA   B LEU   A 1 169 ? 5.946  -19.217 -0.044  0.40 27.68 ?  169 LEU   A HA   1 
ATOM   3767 H HB2  A LEU   A 1 169 ? 6.953  -19.154 -2.530  0.60 34.86 ?  169 LEU   A HB2  1 
ATOM   3768 H HB2  B LEU   A 1 169 ? 6.623  -19.103 -2.261  0.40 30.21 ?  169 LEU   A HB2  1 
ATOM   3769 H HB3  A LEU   A 1 169 ? 8.394  -19.618 -2.060  0.60 34.86 ?  169 LEU   A HB3  1 
ATOM   3770 H HB3  B LEU   A 1 169 ? 8.120  -19.388 -1.833  0.40 30.21 ?  169 LEU   A HB3  1 
ATOM   3771 H HG   A LEU   A 1 169 ? 7.691  -21.776 -1.810  0.60 36.74 ?  169 LEU   A HG   1 
ATOM   3772 H HG   B LEU   A 1 169 ? 7.598  -21.573 -1.314  0.40 32.17 ?  169 LEU   A HG   1 
ATOM   3773 H HD11 A LEU   A 1 169 ? 5.366  -22.281 -2.344  0.60 37.48 ?  169 LEU   A HD11 1 
ATOM   3774 H HD11 B LEU   A 1 169 ? 5.403  -22.395 -1.732  0.40 32.96 ?  169 LEU   A HD11 1 
ATOM   3775 H HD12 A LEU   A 1 169 ? 5.651  -21.671 -0.906  0.60 37.48 ?  169 LEU   A HD12 1 
ATOM   3776 H HD12 B LEU   A 1 169 ? 5.498  -21.432 -0.473  0.40 32.96 ?  169 LEU   A HD12 1 
ATOM   3777 H HD13 A LEU   A 1 169 ? 5.099  -20.740 -2.071  0.60 37.48 ?  169 LEU   A HD13 1 
ATOM   3778 H HD13 B LEU   A 1 169 ? 4.927  -20.885 -1.852  0.40 32.96 ?  169 LEU   A HD13 1 
ATOM   3779 H HD21 A LEU   A 1 169 ? 7.060  -22.326 -3.979  0.60 37.26 ?  169 LEU   A HD21 1 
ATOM   3780 H HD21 B LEU   A 1 169 ? 7.077  -22.412 -3.421  0.40 32.92 ?  169 LEU   A HD21 1 
ATOM   3781 H HD22 A LEU   A 1 169 ? 6.679  -20.809 -4.256  0.60 37.26 ?  169 LEU   A HD22 1 
ATOM   3782 H HD22 B LEU   A 1 169 ? 6.608  -20.966 -3.882  0.40 32.92 ?  169 LEU   A HD22 1 
ATOM   3783 H HD23 A LEU   A 1 169 ? 8.195  -21.215 -4.010  0.60 37.26 ?  169 LEU   A HD23 1 
ATOM   3784 H HD23 B LEU   A 1 169 ? 8.138  -21.236 -3.545  0.40 32.92 ?  169 LEU   A HD23 1 
ATOM   3785 N N    A SER   B 1 1   ? 50.790 -9.201  -23.712 0.60 30.99 ?  1   SER   B N    1 
ATOM   3786 N N    B SER   B 1 1   ? 50.849 -9.309  -23.779 0.40 28.90 ?  1   SER   B N    1 
ATOM   3787 C CA   A SER   B 1 1   ? 51.303 -10.269 -22.831 0.60 30.83 ?  1   SER   B CA   1 
ATOM   3788 C CA   B SER   B 1 1   ? 51.283 -10.282 -22.754 0.40 28.94 ?  1   SER   B CA   1 
ATOM   3789 C C    A SER   B 1 1   ? 50.239 -11.329 -22.592 0.60 29.58 ?  1   SER   B C    1 
ATOM   3790 C C    B SER   B 1 1   ? 50.211 -11.342 -22.530 0.40 28.21 ?  1   SER   B C    1 
ATOM   3791 O O    A SER   B 1 1   ? 49.047 -11.123 -22.853 0.60 29.21 ?  1   SER   B O    1 
ATOM   3792 O O    B SER   B 1 1   ? 49.041 -11.160 -22.886 0.40 27.83 ?  1   SER   B O    1 
ATOM   3793 C CB   A SER   B 1 1   ? 51.769 -9.694  -21.496 0.60 31.63 ?  1   SER   B CB   1 
ATOM   3794 C CB   B SER   B 1 1   ? 51.590 -9.576  -21.438 0.40 29.51 ?  1   SER   B CB   1 
ATOM   3795 O OG   A SER   B 1 1   ? 50.665 -9.378  -20.669 0.60 33.09 ?  1   SER   B OG   1 
ATOM   3796 O OG   B SER   B 1 1   ? 50.432 -9.501  -20.628 0.40 30.49 ?  1   SER   B OG   1 
ATOM   3797 H H1   A SER   B 1 1   ? 50.605 -9.547  -24.508 0.60 37.18 ?  1   SER   B H1   1 
ATOM   3798 H H1   B SER   B 1 1   ? 51.567 -8.917  -24.126 0.40 34.66 ?  1   SER   B H1   1 
ATOM   3799 H H2   A SER   B 1 1   ? 50.058 -8.856  -23.352 0.60 37.18 ?  1   SER   B H2   1 
ATOM   3800 H H2   B SER   B 1 1   ? 50.403 -9.737  -24.415 0.40 34.66 ?  1   SER   B H2   1 
ATOM   3801 H H3   A SER   B 1 1   ? 51.414 -8.574  -23.792 0.60 37.18 ?  1   SER   B H3   1 
ATOM   3802 H H3   B SER   B 1 1   ? 50.329 -8.701  -23.398 0.40 34.66 ?  1   SER   B H3   1 
ATOM   3803 H HA   A SER   B 1 1   ? 52.059 -10.685 -23.266 0.60 36.99 ?  1   SER   B HA   1 
ATOM   3804 H HA   B SER   B 1 1   ? 52.089 -10.713 -23.070 0.40 34.72 ?  1   SER   B HA   1 
ATOM   3805 H HB2  A SER   B 1 1   ? 52.322 -10.355 -21.052 0.60 37.94 ?  1   SER   B HB2  1 
ATOM   3806 H HB2  B SER   B 1 1   ? 52.278 -10.076 -20.974 0.40 35.40 ?  1   SER   B HB2  1 
ATOM   3807 H HB3  A SER   B 1 1   ? 52.279 -8.887  -21.659 0.60 37.94 ?  1   SER   B HB3  1 
ATOM   3808 H HB3  B SER   B 1 1   ? 51.901 -8.676  -21.623 0.40 35.40 ?  1   SER   B HB3  1 
ATOM   3809 H HG   A SER   B 1 1   ? 50.914 -8.875  -20.044 0.60 39.70 ?  1   SER   B HG   1 
ATOM   3810 H HG   B SER   B 1 1   ? 50.557 -8.952  -20.006 0.40 36.58 ?  1   SER   B HG   1 
ATOM   3811 N N    A MET   B 1 2   ? 50.692 -12.465 -22.080 0.60 28.57 ?  2   MET   B N    1 
ATOM   3812 N N    B MET   B 1 2   ? 50.625 -12.448 -21.921 0.40 27.72 ?  2   MET   B N    1 
ATOM   3813 C CA   A MET   B 1 2   ? 49.868 -13.653 -21.914 0.60 28.08 ?  2   MET   B CA   1 
ATOM   3814 C CA   B MET   B 1 2   ? 49.804 -13.648 -21.788 0.40 27.40 ?  2   MET   B CA   1 
ATOM   3815 C C    A MET   B 1 2   ? 49.629 -13.846 -20.424 0.60 24.88 ?  2   MET   B C    1 
ATOM   3816 C C    B MET   B 1 2   ? 49.520 -13.893 -20.311 0.40 25.49 ?  2   MET   B C    1 
ATOM   3817 O O    A MET   B 1 2   ? 50.575 -14.065 -19.662 0.60 24.45 ?  2   MET   B O    1 
ATOM   3818 O O    B MET   B 1 2   ? 50.385 -14.384 -19.578 0.40 26.00 ?  2   MET   B O    1 
ATOM   3819 C CB   A MET   B 1 2   ? 50.586 -14.851 -22.524 0.60 31.77 ?  2   MET   B CB   1 
ATOM   3820 C CB   B MET   B 1 2   ? 50.545 -14.823 -22.399 0.40 29.56 ?  2   MET   B CB   1 
ATOM   3821 C CG   A MET   B 1 2   ? 49.739 -16.101 -22.662 0.60 35.05 ?  2   MET   B CG   1 
ATOM   3822 C CG   B MET   B 1 2   ? 49.675 -16.006 -22.785 0.40 31.28 ?  2   MET   B CG   1 
ATOM   3823 S SD   A MET   B 1 2   ? 50.589 -17.360 -23.630 0.60 38.16 ?  2   MET   B SD   1 
ATOM   3824 S SD   B MET   B 1 2   ? 50.558 -17.122 -23.884 0.40 32.89 ?  2   MET   B SD   1 
ATOM   3825 C CE   A MET   B 1 2   ? 51.139 -16.365 -25.011 0.60 38.43 ?  2   MET   B CE   1 
ATOM   3826 C CE   B MET   B 1 2   ? 51.385 -15.939 -24.930 0.40 33.19 ?  2   MET   B CE   1 
ATOM   3827 H H    A MET   B 1 2   ? 51.501 -12.577 -21.807 0.60 34.27 ?  2   MET   B H    1 
ATOM   3828 H H    B MET   B 1 2   ? 51.410 -12.533 -21.581 0.40 33.26 ?  2   MET   B H    1 
ATOM   3829 H HA   A MET   B 1 2   ? 49.024 -13.542 -22.374 0.60 33.69 ?  2   MET   B HA   1 
ATOM   3830 H HA   B MET   B 1 2   ? 48.974 -13.531 -22.277 0.40 32.87 ?  2   MET   B HA   1 
ATOM   3831 H HB2  A MET   B 1 2   ? 50.886 -14.576 -23.402 0.60 38.11 ?  2   MET   B HB2  1 
ATOM   3832 H HB2  B MET   B 1 2   ? 50.992 -14.468 -23.176 0.40 35.46 ?  2   MET   B HB2  1 
ATOM   3833 H HB3  A MET   B 1 2   ? 51.351 -15.084 -21.978 0.60 38.11 ?  2   MET   B HB3  1 
ATOM   3834 H HB3  B MET   B 1 2   ? 51.204 -15.156 -21.777 0.40 35.46 ?  2   MET   B HB3  1 
ATOM   3835 H HG2  A MET   B 1 2   ? 49.556 -16.462 -21.778 0.60 42.05 ?  2   MET   B HG2  1 
ATOM   3836 H HG2  B MET   B 1 2   ? 49.423 -16.496 -21.981 0.40 37.53 ?  2   MET   B HG2  1 
ATOM   3837 H HG3  A MET   B 1 2   ? 48.911 -15.885 -23.117 0.60 42.05 ?  2   MET   B HG3  1 
ATOM   3838 H HG3  B MET   B 1 2   ? 48.887 -15.702 -23.253 0.40 37.53 ?  2   MET   B HG3  1 
ATOM   3839 H HE1  A MET   B 1 2   ? 51.313 -16.944 -25.758 0.60 46.10 ?  2   MET   B HE1  1 
ATOM   3840 H HE1  B MET   B 1 2   ? 51.613 -16.384 -25.738 0.40 39.81 ?  2   MET   B HE1  1 
ATOM   3841 H HE2  A MET   B 1 2   ? 50.435 -15.731 -25.232 0.60 46.10 ?  2   MET   B HE2  1 
ATOM   3842 H HE2  B MET   B 1 2   ? 50.775 -15.203 -25.113 0.40 39.81 ?  2   MET   B HE2  1 
ATOM   3843 H HE3  A MET   B 1 2   ? 51.948 -15.882 -24.764 0.60 46.10 ?  2   MET   B HE3  1 
ATOM   3844 H HE3  B MET   B 1 2   ? 52.188 -15.606 -24.484 0.40 39.81 ?  2   MET   B HE3  1 
ATOM   3845 N N    A VAL   B 1 3   ? 48.370 -13.724 -20.010 0.60 21.94 ?  3   VAL   B N    1 
ATOM   3846 N N    B VAL   B 1 3   ? 48.310 -13.559 -19.877 0.40 23.10 ?  3   VAL   B N    1 
ATOM   3847 C CA   A VAL   B 1 3   ? 47.960 -13.966 -18.634 0.60 20.75 ?  3   VAL   B CA   1 
ATOM   3848 C CA   B VAL   B 1 3   ? 47.872 -13.814 -18.511 0.40 21.37 ?  3   VAL   B CA   1 
ATOM   3849 C C    A VAL   B 1 3   ? 46.729 -14.863 -18.653 0.60 18.95 ?  3   VAL   B C    1 
ATOM   3850 C C    B VAL   B 1 3   ? 46.624 -14.682 -18.548 0.40 19.28 ?  3   VAL   B C    1 
ATOM   3851 O O    A VAL   B 1 3   ? 46.025 -14.976 -19.659 0.60 19.09 ?  3   VAL   B O    1 
ATOM   3852 O O    B VAL   B 1 3   ? 45.811 -14.604 -19.474 0.40 19.37 ?  3   VAL   B O    1 
ATOM   3853 C CB   A VAL   B 1 3   ? 47.668 -12.654 -17.871 0.60 22.41 ?  3   VAL   B CB   1 
ATOM   3854 C CB   B VAL   B 1 3   ? 47.608 -12.517 -17.715 0.40 22.10 ?  3   VAL   B CB   1 
ATOM   3855 C CG1  A VAL   B 1 3   ? 48.928 -11.792 -17.781 0.60 22.88 ?  3   VAL   B CG1  1 
ATOM   3856 C CG1  B VAL   B 1 3   ? 48.877 -11.683 -17.609 0.40 22.37 ?  3   VAL   B CG1  1 
ATOM   3857 C CG2  A VAL   B 1 3   ? 46.532 -11.891 -18.539 0.60 23.17 ?  3   VAL   B CG2  1 
ATOM   3858 C CG2  B VAL   B 1 3   ? 46.478 -11.723 -18.350 0.40 22.39 ?  3   VAL   B CG2  1 
ATOM   3859 H H    A VAL   B 1 3   ? 47.722 -13.491 -20.522 0.60 26.31 ?  3   VAL   B H    1 
ATOM   3860 H H    B VAL   B 1 3   ? 47.717 -13.181 -20.372 0.40 27.70 ?  3   VAL   B H    1 
ATOM   3861 H HA   A VAL   B 1 3   ? 48.669 -14.436 -18.166 0.60 24.88 ?  3   VAL   B HA   1 
ATOM   3862 H HA   B VAL   B 1 3   ? 48.565 -14.309 -18.051 0.40 25.63 ?  3   VAL   B HA   1 
ATOM   3863 H HB   A VAL   B 1 3   ? 47.393 -12.873 -16.966 0.60 26.88 ?  3   VAL   B HB   1 
ATOM   3864 H HB   B VAL   B 1 3   ? 47.335 -12.759 -16.817 0.40 26.50 ?  3   VAL   B HB   1 
ATOM   3865 H HG11 A VAL   B 1 3   ? 48.722 -10.984 -17.287 0.60 27.44 ?  3   VAL   B HG11 1 
ATOM   3866 H HG11 B VAL   B 1 3   ? 48.687 -10.887 -17.090 0.40 26.83 ?  3   VAL   B HG11 1 
ATOM   3867 H HG12 A VAL   B 1 3   ? 49.621 -12.293 -17.322 0.60 27.44 ?  3   VAL   B HG12 1 
ATOM   3868 H HG12 B VAL   B 1 3   ? 49.564 -12.209 -17.170 0.40 26.83 ?  3   VAL   B HG12 1 
ATOM   3869 H HG13 A VAL   B 1 3   ? 49.221 -11.568 -18.678 0.60 27.44 ?  3   VAL   B HG13 1 
ATOM   3870 H HG13 B VAL   B 1 3   ? 49.168 -11.437 -18.501 0.40 26.83 ?  3   VAL   B HG13 1 
ATOM   3871 H HG21 A VAL   B 1 3   ? 46.465 -11.013 -18.136 0.60 27.80 ?  3   VAL   B HG21 1 
ATOM   3872 H HG21 B VAL   B 1 3   ? 46.438 -10.850 -17.935 0.40 26.86 ?  3   VAL   B HG21 1 
ATOM   3873 H HG22 A VAL   B 1 3   ? 46.720 -11.808 -19.486 0.60 27.80 ?  3   VAL   B HG22 1 
ATOM   3874 H HG22 B VAL   B 1 3   ? 46.650 -11.633 -19.300 0.40 26.86 ?  3   VAL   B HG22 1 
ATOM   3875 H HG23 A VAL   B 1 3   ? 45.703 -12.379 -18.407 0.60 27.80 ?  3   VAL   B HG23 1 
ATOM   3876 H HG23 B VAL   B 1 3   ? 45.641 -12.196 -18.210 0.40 26.86 ?  3   VAL   B HG23 1 
ATOM   3877 N N    . ASN   B 1 4   ? 46.476 -15.512 -17.519 1.00 17.54 ?  4   ASN   B N    1 
ATOM   3878 C CA   . ASN   B 1 4   ? 45.339 -16.424 -17.398 1.00 16.47 ?  4   ASN   B CA   1 
ATOM   3879 C C    . ASN   B 1 4   ? 45.279 -17.394 -18.576 1.00 16.69 ?  4   ASN   B C    1 
ATOM   3880 O O    . ASN   B 1 4   ? 44.216 -17.648 -19.139 1.00 17.63 ?  4   ASN   B O    1 
ATOM   3881 C CB   . ASN   B 1 4   ? 44.016 -15.669 -17.238 1.00 15.84 ?  4   ASN   B CB   1 
ATOM   3882 C CG   . ASN   B 1 4   ? 43.970 -14.847 -15.968 1.00 14.80 ?  4   ASN   B CG   1 
ATOM   3883 O OD1  . ASN   B 1 4   ? 44.255 -15.350 -14.883 1.00 14.62 ?  4   ASN   B OD1  1 
ATOM   3884 N ND2  . ASN   B 1 4   ? 43.620 -13.569 -16.097 1.00 15.74 ?  4   ASN   B ND2  1 
ATOM   3885 H H    A ASN   B 1 4   ? 46.950 -15.443 -16.807 0.60 21.03 ?  4   ASN   B H    1 
ATOM   3886 H H    B ASN   B 1 4   ? 47.032 -15.565 -16.867 0.40 21.03 ?  4   ASN   B H    1 
ATOM   3887 H HA   . ASN   B 1 4   ? 45.468 -16.955 -16.597 1.00 19.75 ?  4   ASN   B HA   1 
ATOM   3888 H HB2  . ASN   B 1 4   ? 43.900 -15.068 -17.989 1.00 19.00 ?  4   ASN   B HB2  1 
ATOM   3889 H HB3  . ASN   B 1 4   ? 43.290 -16.310 -17.208 1.00 19.00 ?  4   ASN   B HB3  1 
ATOM   3890 H HD21 . ASN   B 1 4   ? 43.579 -13.060 -15.402 1.00 18.88 ?  4   ASN   B HD21 1 
ATOM   3891 H HD22 . ASN   B 1 4   ? 43.431 -13.249 -16.872 1.00 18.88 ?  4   ASN   B HD22 1 
ATOM   3892 N N    . SER   B 1 5   ? 46.437 -17.930 -18.961 1.00 17.71 ?  5   SER   B N    1 
ATOM   3893 C CA   . SER   B 1 5   ? 46.528 -18.843 -20.101 1.00 20.52 ?  5   SER   B CA   1 
ATOM   3894 C C    . SER   B 1 5   ? 46.521 -20.278 -19.585 1.00 22.15 ?  5   SER   B C    1 
ATOM   3895 O O    . SER   B 1 5   ? 47.536 -20.966 -19.548 1.00 24.45 ?  5   SER   B O    1 
ATOM   3896 C CB   . SER   B 1 5   ? 47.780 -18.545 -20.924 1.00 22.35 ?  5   SER   B CB   1 
ATOM   3897 O OG   . SER   B 1 5   ? 48.956 -18.753 -20.158 1.00 25.22 ?  5   SER   B OG   1 
ATOM   3898 H H    . SER   B 1 5   ? 47.192 -17.789 -18.570 1.00 21.24 ?  5   SER   B H    1 
ATOM   3899 H HA   . SER   B 1 5   ? 45.757 -18.724 -20.674 1.00 24.61 ?  5   SER   B HA   1 
ATOM   3900 H HB2  . SER   B 1 5   ? 47.797 -19.131 -21.702 1.00 26.80 ?  5   SER   B HB2  1 
ATOM   3901 H HB3  . SER   B 1 5   ? 47.748 -17.620 -21.215 1.00 26.80 ?  5   SER   B HB3  1 
ATOM   3902 H HG   . SER   B 1 5   ? 49.014 -19.562 -19.936 1.00 30.26 ?  5   SER   B HG   1 
ATOM   3903 N N    . PHE   B 1 6   ? 45.336 -20.711 -19.162 1.00 22.28 ?  6   PHE   B N    1 
ATOM   3904 C CA   . PHE   B 1 6   ? 45.158 -22.052 -18.626 1.00 21.60 ?  6   PHE   B CA   1 
ATOM   3905 C C    . PHE   B 1 6   ? 45.086 -23.048 -19.773 1.00 25.39 ?  6   PHE   B C    1 
ATOM   3906 O O    . PHE   B 1 6   ? 44.411 -22.806 -20.777 1.00 27.84 ?  6   PHE   B O    1 
ATOM   3907 C CB   . PHE   B 1 6   ? 43.870 -22.115 -17.804 1.00 19.47 ?  6   PHE   B CB   1 
ATOM   3908 C CG   . PHE   B 1 6   ? 43.884 -21.244 -16.578 1.00 17.44 ?  6   PHE   B CG   1 
ATOM   3909 C CD1  . PHE   B 1 6   ? 44.392 -21.725 -15.387 1.00 16.34 ?  6   PHE   B CD1  1 
ATOM   3910 C CD2  . PHE   B 1 6   ? 43.394 -19.945 -16.618 1.00 16.88 ?  6   PHE   B CD2  1 
ATOM   3911 C CE1  . PHE   B 1 6   ? 44.403 -20.932 -14.250 1.00 15.86 ?  6   PHE   B CE1  1 
ATOM   3912 C CE2  . PHE   B 1 6   ? 43.407 -19.143 -15.491 1.00 17.42 ?  6   PHE   B CE2  1 
ATOM   3913 C CZ   . PHE   B 1 6   ? 43.915 -19.631 -14.307 1.00 16.30 ?  6   PHE   B CZ   1 
ATOM   3914 H H    . PHE   B 1 6   ? 44.613 -20.248 -19.187 1.00 26.72 ?  6   PHE   B H    1 
ATOM   3915 H HA   . PHE   B 1 6   ? 45.904 -22.282 -18.050 1.00 25.91 ?  6   PHE   B HA   1 
ATOM   3916 H HB2  . PHE   B 1 6   ? 43.128 -21.830 -18.359 1.00 23.35 ?  6   PHE   B HB2  1 
ATOM   3917 H HB3  . PHE   B 1 6   ? 43.728 -23.031 -17.512 1.00 23.35 ?  6   PHE   B HB3  1 
ATOM   3918 H HD1  . PHE   B 1 6   ? 44.730 -22.588 -15.341 1.00 19.60 ?  6   PHE   B HD1  1 
ATOM   3919 H HD2  . PHE   B 1 6   ? 43.047 -19.614 -17.414 1.00 20.25 ?  6   PHE   B HD2  1 
ATOM   3920 H HE1  . PHE   B 1 6   ? 44.758 -21.257 -13.451 1.00 19.02 ?  6   PHE   B HE1  1 
ATOM   3921 H HE2  . PHE   B 1 6   ? 43.070 -18.275 -15.533 1.00 20.89 ?  6   PHE   B HE2  1 
ATOM   3922 H HZ   . PHE   B 1 6   ? 43.924 -19.094 -13.547 1.00 19.55 ?  6   PHE   B HZ   1 
ATOM   3923 N N    . SER   B 1 7   ? 45.796 -24.167 -19.626 1.00 26.44 ?  7   SER   B N    1 
ATOM   3924 C CA   . SER   B 1 7   ? 45.895 -25.159 -20.687 1.00 29.17 ?  7   SER   B CA   1 
ATOM   3925 C C    . SER   B 1 7   ? 45.846 -26.561 -20.100 1.00 28.17 ?  7   SER   B C    1 
ATOM   3926 O O    . SER   B 1 7   ? 46.445 -26.831 -19.055 1.00 29.13 ?  7   SER   B O    1 
ATOM   3927 C CB   . SER   B 1 7   ? 47.193 -24.979 -21.486 1.00 32.40 ?  7   SER   B CB   1 
ATOM   3928 O OG   . SER   B 1 7   ? 47.190 -25.784 -22.651 1.00 34.41 ?  7   SER   B OG   1 
ATOM   3929 H H    . SER   B 1 7   ? 46.235 -24.375 -18.912 1.00 31.71 ?  7   SER   B H    1 
ATOM   3930 H HA   . SER   B 1 7   ? 45.148 -25.060 -21.293 1.00 34.99 ?  7   SER   B HA   1 
ATOM   3931 H HB2  . SER   B 1 7   ? 47.276 -24.046 -21.745 1.00 38.86 ?  7   SER   B HB2  1 
ATOM   3932 H HB3  . SER   B 1 7   ? 47.946 -25.233 -20.930 1.00 38.86 ?  7   SER   B HB3  1 
ATOM   3933 H HG   . SER   B 1 7   ? 47.904 -25.671 -23.081 1.00 41.28 ?  7   SER   B HG   1 
ATOM   3934 N N    . GLY   B 1 8   ? 45.131 -27.451 -20.784 1.00 27.88 ?  8   GLY   B N    1 
ATOM   3935 C CA   . GLY   B 1 8   ? 45.095 -28.843 -20.396 1.00 26.93 ?  8   GLY   B CA   1 
ATOM   3936 C C    . GLY   B 1 8   ? 44.141 -29.169 -19.276 1.00 25.25 ?  8   GLY   B C    1 
ATOM   3937 O O    . GLY   B 1 8   ? 44.282 -30.227 -18.650 1.00 26.52 ?  8   GLY   B O    1 
ATOM   3938 H H    . GLY   B 1 8   ? 44.663 -27.263 -21.477 1.00 33.45 ?  8   GLY   B H    1 
ATOM   3939 H HA2  . GLY   B 1 8   ? 44.841 -29.375 -21.165 1.00 32.31 ?  8   GLY   B HA2  1 
ATOM   3940 H HA3  . GLY   B 1 8   ? 45.980 -29.117 -20.116 1.00 32.31 ?  8   GLY   B HA3  1 
ATOM   3941 N N    . TYR   B 1 9   ? 43.154 -28.313 -19.014 1.00 22.99 ?  9   TYR   B N    1 
ATOM   3942 C CA   . TYR   B 1 9   ? 42.188 -28.576 -17.960 1.00 21.14 ?  9   TYR   B CA   1 
ATOM   3943 C C    . TYR   B 1 9   ? 41.003 -29.369 -18.484 1.00 20.76 ?  9   TYR   B C    1 
ATOM   3944 O O    . TYR   B 1 9   ? 40.585 -29.222 -19.637 1.00 22.85 ?  9   TYR   B O    1 
ATOM   3945 C CB   . TYR   B 1 9   ? 41.678 -27.279 -17.334 1.00 20.51 ?  9   TYR   B CB   1 
ATOM   3946 C CG   . TYR   B 1 9   ? 42.695 -26.651 -16.417 1.00 19.63 ?  9   TYR   B CG   1 
ATOM   3947 C CD1  . TYR   B 1 9   ? 43.795 -25.984 -16.933 1.00 20.06 ?  9   TYR   B CD1  1 
ATOM   3948 C CD2  . TYR   B 1 9   ? 42.579 -26.749 -15.040 1.00 19.01 ?  9   TYR   B CD2  1 
ATOM   3949 C CE1  . TYR   B 1 9   ? 44.744 -25.424 -16.105 1.00 20.38 ?  9   TYR   B CE1  1 
ATOM   3950 C CE2  . TYR   B 1 9   ? 43.525 -26.190 -14.201 1.00 19.49 ?  9   TYR   B CE2  1 
ATOM   3951 C CZ   . TYR   B 1 9   ? 44.606 -25.526 -14.742 1.00 20.26 ?  9   TYR   B CZ   1 
ATOM   3952 O OH   . TYR   B 1 9   ? 45.557 -24.978 -13.917 1.00 20.80 ?  9   TYR   B OH   1 
ATOM   3953 H H    . TYR   B 1 9   ? 43.005 -27.588 -19.451 1.00 27.58 ?  9   TYR   B H    1 
ATOM   3954 H HA   . TYR   B 1 9   ? 42.610 -29.096 -17.262 1.00 25.36 ?  9   TYR   B HA   1 
ATOM   3955 H HB2  . TYR   B 1 9   ? 41.461 -26.641 -18.034 1.00 24.59 ?  9   TYR   B HB2  1 
ATOM   3956 H HB3  . TYR   B 1 9   ? 40.889 -27.481 -16.811 1.00 24.59 ?  9   TYR   B HB3  1 
ATOM   3957 H HD1  . TYR   B 1 9   ? 43.889 -25.915 -17.857 1.00 24.06 ?  9   TYR   B HD1  1 
ATOM   3958 H HD2  . TYR   B 1 9   ? 41.846 -27.199 -14.672 1.00 22.80 ?  9   TYR   B HD2  1 
ATOM   3959 H HE1  . TYR   B 1 9   ? 45.468 -24.981 -16.472 1.00 24.44 ?  9   TYR   B HE1  1 
ATOM   3960 H HE2  . TYR   B 1 9   ? 43.426 -26.264 -13.277 1.00 23.37 ?  9   TYR   B HE2  1 
ATOM   3961 H HH   . TYR   B 1 9   ? 46.148 -24.608 -14.380 1.00 24.95 ?  9   TYR   B HH   1 
ATOM   3962 N N    . LEU   B 1 10  ? 40.470 -30.218 -17.612 1.00 18.81 ?  10  LEU   B N    1 
ATOM   3963 C CA   . LEU   B 1 10  ? 39.260 -30.973 -17.888 1.00 18.65 ?  10  LEU   B CA   1 
ATOM   3964 C C    . LEU   B 1 10  ? 38.072 -30.205 -17.325 1.00 18.19 ?  10  LEU   B C    1 
ATOM   3965 O O    . LEU   B 1 10  ? 38.089 -29.781 -16.165 1.00 18.00 ?  10  LEU   B O    1 
ATOM   3966 C CB   . LEU   B 1 10  ? 39.356 -32.345 -17.226 1.00 19.69 ?  10  LEU   B CB   1 
ATOM   3967 C CG   . LEU   B 1 10  ? 38.197 -33.286 -17.533 1.00 21.83 ?  10  LEU   B CG   1 
ATOM   3968 C CD1  . LEU   B 1 10  ? 38.283 -33.788 -18.969 1.00 23.35 ?  10  LEU   B CD1  1 
ATOM   3969 C CD2  . LEU   B 1 10  ? 38.162 -34.438 -16.546 1.00 22.83 ?  10  LEU   B CD2  1 
ATOM   3970 H H    . LEU   B 1 10  ? 40.797 -30.373 -16.827 1.00 22.56 ?  10  LEU   B H    1 
ATOM   3971 H HA   . LEU   B 1 10  ? 39.146 -31.087 -18.841 1.00 22.37 ?  10  LEU   B HA   1 
ATOM   3972 H HB2  . LEU   B 1 10  ? 40.172 -32.780 -17.524 1.00 23.61 ?  10  LEU   B HB2  1 
ATOM   3973 H HB3  . LEU   B 1 10  ? 39.388 -32.228 -16.261 1.00 23.61 ?  10  LEU   B HB3  1 
ATOM   3974 H HG   . LEU   B 1 10  ? 37.364 -32.798 -17.442 1.00 26.18 ?  10  LEU   B HG   1 
ATOM   3975 H HD11 . LEU   B 1 10  ? 37.567 -34.423 -19.124 1.00 28.01 ?  10  LEU   B HD11 1 
ATOM   3976 H HD12 . LEU   B 1 10  ? 38.190 -33.033 -19.573 1.00 28.01 ?  10  LEU   B HD12 1 
ATOM   3977 H HD13 . LEU   B 1 10  ? 39.141 -34.217 -19.103 1.00 28.01 ?  10  LEU   B HD13 1 
ATOM   3978 H HD21 . LEU   B 1 10  ? 37.419 -35.019 -16.771 1.00 27.39 ?  10  LEU   B HD21 1 
ATOM   3979 H HD22 . LEU   B 1 10  ? 38.996 -34.925 -16.602 1.00 27.39 ?  10  LEU   B HD22 1 
ATOM   3980 H HD23 . LEU   B 1 10  ? 38.043 -34.079 -15.652 1.00 27.39 ?  10  LEU   B HD23 1 
ATOM   3981 N N    . LYS   B 1 11  ? 37.048 -30.024 -18.149 1.00 19.42 ?  11  LYS   B N    1 
ATOM   3982 C CA   . LYS   B 1 11  ? 35.854 -29.303 -17.737 1.00 21.58 ?  11  LYS   B CA   1 
ATOM   3983 C C    . LYS   B 1 11  ? 34.969 -30.225 -16.905 1.00 20.79 ?  11  LYS   B C    1 
ATOM   3984 O O    . LYS   B 1 11  ? 34.587 -31.308 -17.365 1.00 22.47 ?  11  LYS   B O    1 
ATOM   3985 C CB   . LYS   B 1 11  ? 35.109 -28.824 -18.981 1.00 25.03 ?  11  LYS   B CB   1 
ATOM   3986 C CG   . LYS   B 1 11  ? 33.944 -27.891 -18.713 1.00 28.36 ?  11  LYS   B CG   1 
ATOM   3987 C CD   . LYS   B 1 11  ? 33.195 -27.590 -20.007 1.00 31.12 ?  11  LYS   B CD   1 
ATOM   3988 C CE   . LYS   B 1 11  ? 32.154 -26.500 -19.818 1.00 33.22 ?  11  LYS   B CE   1 
ATOM   3989 N NZ   . LYS   B 1 11  ? 32.783 -25.176 -19.570 1.00 34.42 ?  11  LYS   B NZ   1 
ATOM   3990 H H    . LYS   B 1 11  ? 37.019 -30.319 -18.956 1.00 23.29 ?  11  LYS   B H    1 
ATOM   3991 H HA   . LYS   B 1 11  ? 36.102 -28.535 -17.200 1.00 25.88 ?  11  LYS   B HA   1 
ATOM   3992 H HB2  . LYS   B 1 11  ? 35.737 -28.352 -19.552 1.00 30.03 ?  11  LYS   B HB2  1 
ATOM   3993 H HB3  . LYS   B 1 11  ? 34.763 -29.599 -19.451 1.00 30.03 ?  11  LYS   B HB3  1 
ATOM   3994 H HG2  . LYS   B 1 11  ? 33.328 -28.313 -18.094 1.00 34.01 ?  11  LYS   B HG2  1 
ATOM   3995 H HG3  . LYS   B 1 11  ? 34.275 -27.056 -18.349 1.00 34.01 ?  11  LYS   B HG3  1 
ATOM   3996 H HD2  . LYS   B 1 11  ? 33.828 -27.293 -20.680 1.00 37.33 ?  11  LYS   B HD2  1 
ATOM   3997 H HD3  . LYS   B 1 11  ? 32.742 -28.395 -20.308 1.00 37.33 ?  11  LYS   B HD3  1 
ATOM   3998 H HE2  . LYS   B 1 11  ? 31.612 -26.434 -20.619 1.00 39.85 ?  11  LYS   B HE2  1 
ATOM   3999 H HE3  . LYS   B 1 11  ? 31.598 -26.722 -19.055 1.00 39.85 ?  11  LYS   B HE3  1 
ATOM   4000 H HZ1  . LYS   B 1 11  ? 32.155 -24.549 -19.508 1.00 41.29 ?  11  LYS   B HZ1  1 
ATOM   4001 H HZ2  . LYS   B 1 11  ? 33.249 -25.197 -18.813 1.00 41.29 ?  11  LYS   B HZ2  1 
ATOM   4002 H HZ3  . LYS   B 1 11  ? 33.330 -24.970 -20.242 1.00 41.29 ?  11  LYS   B HZ3  1 
ATOM   4003 N N    . LEU   B 1 12  ? 34.641 -29.800 -15.685 1.00 18.92 ?  12  LEU   B N    1 
ATOM   4004 C CA   . LEU   B 1 12  ? 33.686 -30.510 -14.840 1.00 18.35 ?  12  LEU   B CA   1 
ATOM   4005 C C    . LEU   B 1 12  ? 32.293 -29.904 -14.918 1.00 18.41 ?  12  LEU   B C    1 
ATOM   4006 O O    . LEU   B 1 12  ? 31.306 -30.625 -15.082 1.00 18.86 ?  12  LEU   B O    1 
ATOM   4007 C CB   . LEU   B 1 12  ? 34.159 -30.525 -13.383 1.00 17.81 ?  12  LEU   B CB   1 
ATOM   4008 C CG   . LEU   B 1 12  ? 35.492 -31.219 -13.113 1.00 17.64 ?  12  LEU   B CG   1 
ATOM   4009 C CD1  . LEU   B 1 12  ? 35.819 -31.174 -11.633 1.00 17.83 ?  12  LEU   B CD1  1 
ATOM   4010 C CD2  . LEU   B 1 12  ? 35.481 -32.655 -13.622 1.00 18.46 ?  12  LEU   B CD2  1 
ATOM   4011 H H    . LEU   B 1 12  ? 34.958 -29.088 -15.322 1.00 22.69 ?  12  LEU   B H    1 
ATOM   4012 H HA   . LEU   B 1 12  ? 33.616 -31.425 -15.145 1.00 22.01 ?  12  LEU   B HA   1 
ATOM   4013 H HB2  . LEU   B 1 12  ? 34.243 -29.610 -13.081 1.00 21.37 ?  12  LEU   B HB2  1 
ATOM   4014 H HB3  . LEU   B 1 12  ? 33.484 -30.979 -12.852 1.00 21.37 ?  12  LEU   B HB3  1 
ATOM   4015 H HG   . LEU   B 1 12  ? 36.192 -30.745 -13.586 1.00 21.16 ?  12  LEU   B HG   1 
ATOM   4016 H HD11 . LEU   B 1 12  ? 36.671 -31.618 -11.484 1.00 21.38 ?  12  LEU   B HD11 1 
ATOM   4017 H HD12 . LEU   B 1 12  ? 35.877 -30.249 -11.350 1.00 21.38 ?  12  LEU   B HD12 1 
ATOM   4018 H HD13 . LEU   B 1 12  ? 35.120 -31.630 -11.139 1.00 21.38 ?  12  LEU   B HD13 1 
ATOM   4019 H HD21 . LEU   B 1 12  ? 36.281 -33.106 -13.311 1.00 22.14 ?  12  LEU   B HD21 1 
ATOM   4020 H HD22 . LEU   B 1 12  ? 34.693 -33.105 -13.281 1.00 22.14 ?  12  LEU   B HD22 1 
ATOM   4021 H HD23 . LEU   B 1 12  ? 35.463 -32.646 -14.593 1.00 22.14 ?  12  LEU   B HD23 1 
ATOM   4022 N N    . THR   B 1 13  ? 32.202 -28.584 -14.797 1.00 18.66 ?  13  THR   B N    1 
ATOM   4023 C CA   . THR   B 1 13  ? 30.971 -27.841 -15.003 1.00 18.65 ?  13  THR   B CA   1 
ATOM   4024 C C    . THR   B 1 13  ? 31.295 -26.645 -15.889 1.00 20.22 ?  13  THR   B C    1 
ATOM   4025 O O    . THR   B 1 13  ? 32.434 -26.459 -16.330 1.00 20.94 ?  13  THR   B O    1 
ATOM   4026 C CB   . THR   B 1 13  ? 30.371 -27.361 -13.678 1.00 17.99 ?  13  THR   B CB   1 
ATOM   4027 O OG1  . THR   B 1 13  ? 31.217 -26.337 -13.132 1.00 17.45 ?  13  THR   B OG1  1 
ATOM   4028 C CG2  . THR   B 1 13  ? 30.249 -28.514 -12.687 1.00 18.68 ?  13  THR   B CG2  1 
ATOM   4029 H H    . THR   B 1 13  ? 32.866 -28.079 -14.588 1.00 22.38 ?  13  THR   B H    1 
ATOM   4030 H HA   . THR   B 1 13  ? 30.319 -28.404 -15.451 1.00 22.37 ?  13  THR   B HA   1 
ATOM   4031 H HB   . THR   B 1 13  ? 29.478 -26.999 -13.837 1.00 21.57 ?  13  THR   B HB   1 
ATOM   4032 H HG1  . THR   B 1 13  ? 30.890 -25.576 -13.306 1.00 20.93 ?  13  THR   B HG1  1 
ATOM   4033 H HG21 . THR   B 1 13  ? 29.732 -28.236 -11.912 1.00 22.40 ?  13  THR   B HG21 1 
ATOM   4034 H HG22 . THR   B 1 13  ? 29.800 -29.267 -13.105 1.00 22.40 ?  13  THR   B HG22 1 
ATOM   4035 H HG23 . THR   B 1 13  ? 31.128 -28.795 -12.394 1.00 22.40 ?  13  THR   B HG23 1 
ATOM   4036 N N    A ASP   B 1 14  ? 30.280 -25.818 -16.139 0.60 21.11 ?  14  ASP   B N    1 
ATOM   4037 N N    B ASP   B 1 14  ? 30.285 -25.807 -16.133 0.40 20.97 ?  14  ASP   B N    1 
ATOM   4038 C CA   A ASP   B 1 14  ? 30.487 -24.654 -16.992 0.60 22.65 ?  14  ASP   B CA   1 
ATOM   4039 C CA   B ASP   B 1 14  ? 30.481 -24.649 -16.999 0.40 22.01 ?  14  ASP   B CA   1 
ATOM   4040 C C    A ASP   B 1 14  ? 31.599 -23.755 -16.466 0.60 20.65 ?  14  ASP   B C    1 
ATOM   4041 C C    B ASP   B 1 14  ? 31.487 -23.652 -16.440 0.40 20.12 ?  14  ASP   B C    1 
ATOM   4042 O O    A ASP   B 1 14  ? 32.275 -23.086 -17.257 0.60 21.71 ?  14  ASP   B O    1 
ATOM   4043 O O    B ASP   B 1 14  ? 31.942 -22.775 -17.183 0.40 20.54 ?  14  ASP   B O    1 
ATOM   4044 C CB   A ASP   B 1 14  ? 29.180 -23.873 -17.140 0.60 26.10 ?  14  ASP   B CB   1 
ATOM   4045 C CB   B ASP   B 1 14  ? 29.155 -23.928 -17.241 0.40 24.81 ?  14  ASP   B CB   1 
ATOM   4046 C CG   A ASP   B 1 14  ? 28.200 -24.540 -18.080 0.60 29.34 ?  14  ASP   B CG   1 
ATOM   4047 C CG   B ASP   B 1 14  ? 28.276 -24.651 -18.244 0.40 27.34 ?  14  ASP   B CG   1 
ATOM   4048 O OD1  A ASP   B 1 14  ? 28.530 -25.605 -18.648 0.60 30.24 ?  14  ASP   B OD1  1 
ATOM   4049 O OD1  B ASP   B 1 14  ? 28.828 -25.332 -19.134 0.40 28.01 ?  14  ASP   B OD1  1 
ATOM   4050 O OD2  A ASP   B 1 14  ? 27.092 -23.993 -18.247 0.60 30.73 -1 14  ASP   B OD2  1 
ATOM   4051 O OD2  B ASP   B 1 14  ? 27.036 -24.542 -18.143 0.40 28.34 -1 14  ASP   B OD2  1 
ATOM   4052 H H    A ASP   B 1 14  ? 29.485 -25.897 -15.820 0.60 25.32 ?  14  ASP   B H    1 
ATOM   4053 H H    B ASP   B 1 14  ? 29.489 -25.883 -15.810 0.40 25.15 ?  14  ASP   B H    1 
ATOM   4054 H HA   A ASP   B 1 14  ? 30.756 -24.953 -17.869 0.60 27.17 ?  14  ASP   B HA   1 
ATOM   4055 H HA   B ASP   B 1 14  ? 30.811 -24.958 -17.855 0.40 26.40 ?  14  ASP   B HA   1 
ATOM   4056 H HB2  A ASP   B 1 14  ? 28.740 -23.810 -16.281 0.60 31.31 ?  14  ASP   B HB2  1 
ATOM   4057 H HB2  B ASP   B 1 14  ? 28.671 -23.867 -16.403 0.40 29.76 ?  14  ASP   B HB2  1 
ATOM   4058 H HB3  A ASP   B 1 14  ? 29.370 -22.989 -17.488 0.60 31.31 ?  14  ASP   B HB3  1 
ATOM   4059 H HB3  B ASP   B 1 14  ? 29.342 -23.034 -17.578 0.40 29.76 ?  14  ASP   B HB3  1 
ATOM   4060 N N    . ASN   B 1 15  ? 31.822 -23.738 -15.149 1.00 18.22 ?  15  ASN   B N    1 
ATOM   4061 C CA   . ASN   B 1 15  ? 32.783 -22.816 -14.551 1.00 15.92 ?  15  ASN   B CA   1 
ATOM   4062 C C    . ASN   B 1 15  ? 33.878 -23.466 -13.716 1.00 14.59 ?  15  ASN   B C    1 
ATOM   4063 O O    . ASN   B 1 15  ? 34.721 -22.733 -13.190 1.00 15.16 ?  15  ASN   B O    1 
ATOM   4064 C CB   . ASN   B 1 15  ? 32.070 -21.758 -13.693 1.00 16.26 ?  15  ASN   B CB   1 
ATOM   4065 C CG   . ASN   B 1 15  ? 31.446 -22.351 -12.449 1.00 15.69 ?  15  ASN   B CG   1 
ATOM   4066 O OD1  . ASN   B 1 15  ? 30.498 -23.143 -12.535 1.00 17.34 ?  15  ASN   B OD1  1 
ATOM   4067 N ND2  . ASN   B 1 15  ? 31.973 -21.997 -11.290 1.00 15.18 ?  15  ASN   B ND2  1 
ATOM   4068 H H    A ASN   B 1 15  ? 31.429 -24.258 -14.584 0.60 21.86 ?  15  ASN   B H    1 
ATOM   4069 H H    B ASN   B 1 15  ? 31.477 -24.301 -14.595 0.40 21.86 ?  15  ASN   B H    1 
ATOM   4070 H HA   . ASN   B 1 15  ? 33.228 -22.339 -15.259 1.00 19.09 ?  15  ASN   B HA   1 
ATOM   4071 H HB2  . ASN   B 1 15  ? 32.716 -21.082 -13.419 1.00 19.50 ?  15  ASN   B HB2  1 
ATOM   4072 H HB3  . ASN   B 1 15  ? 31.364 -21.341 -14.215 1.00 19.50 ?  15  ASN   B HB3  1 
ATOM   4073 H HD21 . ASN   B 1 15  ? 31.651 -22.307 -10.554 1.00 18.20 ?  15  ASN   B HD21 1 
ATOM   4074 H HD22 . ASN   B 1 15  ? 32.640 -21.448 -11.263 1.00 18.20 ?  15  ASN   B HD22 1 
ATOM   4075 N N    . VAL   B 1 16  ? 33.902 -24.791 -13.573 1.00 14.55 ?  16  VAL   B N    1 
ATOM   4076 C CA   . VAL   B 1 16  ? 34.904 -25.479 -12.762 1.00 14.07 ?  16  VAL   B CA   1 
ATOM   4077 C C    . VAL   B 1 16  ? 35.696 -26.421 -13.656 1.00 14.14 ?  16  VAL   B C    1 
ATOM   4078 O O    . VAL   B 1 16  ? 35.116 -27.295 -14.320 1.00 15.48 ?  16  VAL   B O    1 
ATOM   4079 C CB   . VAL   B 1 16  ? 34.272 -26.241 -11.583 1.00 14.72 ?  16  VAL   B CB   1 
ATOM   4080 C CG1  . VAL   B 1 16  ? 35.350 -26.977 -10.770 1.00 15.04 ?  16  VAL   B CG1  1 
ATOM   4081 C CG2  . VAL   B 1 16  ? 33.462 -25.296 -10.706 1.00 15.40 ?  16  VAL   B CG2  1 
ATOM   4082 H H    . VAL   B 1 16  ? 33.335 -25.325 -13.942 1.00 17.45 ?  16  VAL   B H    1 
ATOM   4083 H HA   . VAL   B 1 16  ? 35.519 -24.822 -12.395 1.00 16.87 ?  16  VAL   B HA   1 
ATOM   4084 H HB   . VAL   B 1 16  ? 33.666 -26.910 -11.938 1.00 17.65 ?  16  VAL   B HB   1 
ATOM   4085 H HG11 . VAL   B 1 16  ? 34.954 -27.293 -9.942  1.00 18.03 ?  16  VAL   B HG11 1 
ATOM   4086 H HG12 . VAL   B 1 16  ? 35.684 -27.724 -11.285 1.00 18.03 ?  16  VAL   B HG12 1 
ATOM   4087 H HG13 . VAL   B 1 16  ? 36.071 -26.356 -10.573 1.00 18.03 ?  16  VAL   B HG13 1 
ATOM   4088 H HG21 . VAL   B 1 16  ? 33.126 -25.787 -9.940  1.00 18.46 ?  16  VAL   B HG21 1 
ATOM   4089 H HG22 . VAL   B 1 16  ? 34.033 -24.571 -10.412 1.00 18.46 ?  16  VAL   B HG22 1 
ATOM   4090 H HG23 . VAL   B 1 16  ? 32.720 -24.944 -11.224 1.00 18.46 ?  16  VAL   B HG23 1 
ATOM   4091 N N    . TYR   B 1 17  ? 37.022 -26.257 -13.632 1.00 14.87 ?  17  TYR   B N    1 
ATOM   4092 C CA   . TYR   B 1 17  ? 37.965 -27.008 -14.443 1.00 15.22 ?  17  TYR   B CA   1 
ATOM   4093 C C    . TYR   B 1 17  ? 39.015 -27.614 -13.522 1.00 14.64 ?  17  TYR   B C    1 
ATOM   4094 O O    . TYR   B 1 17  ? 39.289 -27.082 -12.441 1.00 14.98 ?  17  TYR   B O    1 
ATOM   4095 C CB   . TYR   B 1 17  ? 38.666 -26.079 -15.444 1.00 17.83 ?  17  TYR   B CB   1 
ATOM   4096 C CG   . TYR   B 1 17  ? 37.737 -25.305 -16.348 1.00 20.92 ?  17  TYR   B CG   1 
ATOM   4097 C CD1  . TYR   B 1 17  ? 37.147 -24.116 -15.929 1.00 22.21 ?  17  TYR   B CD1  1 
ATOM   4098 C CD2  . TYR   B 1 17  ? 37.454 -25.762 -17.627 1.00 22.96 ?  17  TYR   B CD2  1 
ATOM   4099 C CE1  . TYR   B 1 17  ? 36.295 -23.408 -16.761 1.00 23.82 ?  17  TYR   B CE1  1 
ATOM   4100 C CE2  . TYR   B 1 17  ? 36.610 -25.063 -18.465 1.00 24.33 ?  17  TYR   B CE2  1 
ATOM   4101 C CZ   . TYR   B 1 17  ? 36.030 -23.890 -18.027 1.00 24.94 ?  17  TYR   B CZ   1 
ATOM   4102 O OH   . TYR   B 1 17  ? 35.190 -23.196 -18.865 1.00 26.45 ?  17  TYR   B OH   1 
ATOM   4103 H H    . TYR   B 1 17  ? 37.418 -25.686 -13.117 1.00 17.83 ?  17  TYR   B H    1 
ATOM   4104 H HA   . TYR   B 1 17  ? 37.504 -27.720 -14.922 1.00 18.25 ?  17  TYR   B HA   1 
ATOM   4105 H HB2  . TYR   B 1 17  ? 39.204 -25.442 -14.953 1.00 21.38 ?  17  TYR   B HB2  1 
ATOM   4106 H HB3  . TYR   B 1 17  ? 39.230 -26.619 -16.012 1.00 21.38 ?  17  TYR   B HB3  1 
ATOM   4107 H HD1  . TYR   B 1 17  ? 37.323 -23.793 -15.077 1.00 26.64 ?  17  TYR   B HD1  1 
ATOM   4108 H HD2  . TYR   B 1 17  ? 37.836 -26.553 -17.926 1.00 27.54 ?  17  TYR   B HD2  1 
ATOM   4109 H HE1  . TYR   B 1 17  ? 35.903 -22.613 -16.471 1.00 28.57 ?  17  TYR   B HE1  1 
ATOM   4110 H HE2  . TYR   B 1 17  ? 36.423 -25.383 -19.321 1.00 29.18 ?  17  TYR   B HE2  1 
ATOM   4111 H HH   . TYR   B 1 17  ? 35.111 -23.592 -19.602 1.00 31.73 ?  17  TYR   B HH   1 
ATOM   4112 N N    . ILE   B 1 18  ? 39.632 -28.716 -13.955 1.00 14.54 ?  18  ILE   B N    1 
ATOM   4113 C CA   . ILE   B 1 18  ? 40.562 -29.439 -13.094 1.00 14.31 ?  18  ILE   B CA   1 
ATOM   4114 C C    . ILE   B 1 18  ? 41.723 -29.988 -13.915 1.00 14.76 ?  18  ILE   B C    1 
ATOM   4115 O O    . ILE   B 1 18  ? 41.563 -30.376 -15.077 1.00 16.07 ?  18  ILE   B O    1 
ATOM   4116 C CB   . ILE   B 1 18  ? 39.814 -30.542 -12.299 1.00 15.04 ?  18  ILE   B CB   1 
ATOM   4117 C CG1  . ILE   B 1 18  ? 40.674 -31.093 -11.159 1.00 15.27 ?  18  ILE   B CG1  1 
ATOM   4118 C CG2  . ILE   B 1 18  ? 39.308 -31.656 -13.229 1.00 15.41 ?  18  ILE   B CG2  1 
ATOM   4119 C CD1  . ILE   B 1 18  ? 39.865 -31.893 -10.141 1.00 16.81 ?  18  ILE   B CD1  1 
ATOM   4120 H H    . ILE   B 1 18  ? 39.530 -29.063 -14.735 1.00 17.44 ?  18  ILE   B H    1 
ATOM   4121 H HA   . ILE   B 1 18  ? 40.925 -28.820 -12.441 1.00 17.16 ?  18  ILE   B HA   1 
ATOM   4122 H HB   . ILE   B 1 18  ? 39.032 -30.139 -11.892 1.00 18.03 ?  18  ILE   B HB   1 
ATOM   4123 H HG12 . ILE   B 1 18  ? 41.354 -31.675 -11.524 1.00 18.31 ?  18  ILE   B HG12 1 
ATOM   4124 H HG13 . ILE   B 1 18  ? 41.087 -30.349 -10.691 1.00 18.31 ?  18  ILE   B HG13 1 
ATOM   4125 H HG21 . ILE   B 1 18  ? 38.726 -32.252 -12.727 1.00 18.48 ?  18  ILE   B HG21 1 
ATOM   4126 H HG22 . ILE   B 1 18  ? 38.812 -31.252 -13.958 1.00 18.48 ?  18  ILE   B HG22 1 
ATOM   4127 H HG23 . ILE   B 1 18  ? 40.065 -32.150 -13.576 1.00 18.48 ?  18  ILE   B HG23 1 
ATOM   4128 H HD11 . ILE   B 1 18  ? 40.453 -32.173 -9.422  1.00 20.16 ?  18  ILE   B HD11 1 
ATOM   4129 H HD12 . ILE   B 1 18  ? 39.156 -31.331 -9.789  1.00 20.16 ?  18  ILE   B HD12 1 
ATOM   4130 H HD13 . ILE   B 1 18  ? 39.485 -32.669 -10.581 1.00 20.16 ?  18  ILE   B HD13 1 
ATOM   4131 N N    . LYS   B 1 19  ? 42.904 -30.022 -13.293 1.00 15.45 ?  19  LYS   B N    1 
ATOM   4132 C CA   . LYS   B 1 19  ? 44.114 -30.502 -13.946 1.00 16.10 ?  19  LYS   B CA   1 
ATOM   4133 C C    . LYS   B 1 19  ? 45.011 -31.179 -12.922 1.00 15.96 ?  19  LYS   B C    1 
ATOM   4134 O O    . LYS   B 1 19  ? 45.099 -30.738 -11.773 1.00 15.36 ?  19  LYS   B O    1 
ATOM   4135 C CB   . LYS   B 1 19  ? 44.883 -29.335 -14.584 1.00 17.73 ?  19  LYS   B CB   1 
ATOM   4136 C CG   . LYS   B 1 19  ? 46.109 -29.734 -15.392 1.00 19.57 ?  19  LYS   B CG   1 
ATOM   4137 C CD   . LYS   B 1 19  ? 46.824 -28.496 -15.924 1.00 21.33 ?  19  LYS   B CD   1 
ATOM   4138 C CE   . LYS   B 1 19  ? 47.994 -28.861 -16.820 1.00 23.26 ?  19  LYS   B CE   1 
ATOM   4139 N NZ   . LYS   B 1 19  ? 48.710 -27.659 -17.324 1.00 24.61 ?  19  LYS   B NZ   1 
ATOM   4140 H H    . LYS   B 1 19  ? 43.020 -29.775 -12.476 1.00 18.53 ?  19  LYS   B H    1 
ATOM   4141 H HA   . LYS   B 1 19  ? 43.880 -31.141 -14.636 1.00 19.31 ?  19  LYS   B HA   1 
ATOM   4142 H HB2  . LYS   B 1 19  ? 44.281 -28.861 -15.181 1.00 21.27 ?  19  LYS   B HB2  1 
ATOM   4143 H HB3  . LYS   B 1 19  ? 45.174 -28.735 -13.878 1.00 21.27 ?  19  LYS   B HB3  1 
ATOM   4144 H HG2  . LYS   B 1 19  ? 46.721 -30.226 -14.826 1.00 23.47 ?  19  LYS   B HG2  1 
ATOM   4145 H HG3  . LYS   B 1 19  ? 45.831 -30.278 -16.146 1.00 23.47 ?  19  LYS   B HG3  1 
ATOM   4146 H HD2  . LYS   B 1 19  ? 46.198 -27.962 -16.440 1.00 25.58 ?  19  LYS   B HD2  1 
ATOM   4147 H HD3  . LYS   B 1 19  ? 47.164 -27.979 -15.175 1.00 25.58 ?  19  LYS   B HD3  1 
ATOM   4148 H HE2  . LYS   B 1 19  ? 48.622 -29.402 -16.317 1.00 27.90 ?  19  LYS   B HE2  1 
ATOM   4149 H HE3  . LYS   B 1 19  ? 47.662 -29.361 -17.584 1.00 27.90 ?  19  LYS   B HE3  1 
ATOM   4150 H HZ1  . LYS   B 1 19  ? 49.345 -27.902 -17.899 1.00 29.53 ?  19  LYS   B HZ1  1 
ATOM   4151 H HZ2  . LYS   B 1 19  ? 48.139 -27.116 -17.738 1.00 29.53 ?  19  LYS   B HZ2  1 
ATOM   4152 H HZ3  . LYS   B 1 19  ? 49.086 -27.222 -16.647 1.00 29.53 ?  19  LYS   B HZ3  1 
ATOM   4153 N N    . ASN   B 1 20  ? 45.703 -32.230 -13.356 1.00 17.12 ?  20  ASN   B N    1 
ATOM   4154 C CA   . ASN   B 1 20  ? 46.734 -32.864 -12.538 1.00 18.17 ?  20  ASN   B CA   1 
ATOM   4155 C C    . ASN   B 1 20  ? 48.011 -32.049 -12.722 1.00 18.60 ?  20  ASN   B C    1 
ATOM   4156 O O    . ASN   B 1 20  ? 48.668 -32.130 -13.765 1.00 20.44 ?  20  ASN   B O    1 
ATOM   4157 C CB   . ASN   B 1 20  ? 46.897 -34.321 -12.966 1.00 19.98 ?  20  ASN   B CB   1 
ATOM   4158 C CG   . ASN   B 1 20  ? 48.062 -35.024 -12.290 1.00 21.38 ?  20  ASN   B CG   1 
ATOM   4159 O OD1  . ASN   B 1 20  ? 48.733 -35.861 -12.905 1.00 23.77 ?  20  ASN   B OD1  1 
ATOM   4160 N ND2  . ASN   B 1 20  ? 48.296 -34.714 -11.024 1.00 21.02 ?  20  ASN   B ND2  1 
ATOM   4161 H H    . ASN   B 1 20  ? 45.598 -32.587 -14.128 1.00 20.53 ?  20  ASN   B H    1 
ATOM   4162 H HA   . ASN   B 1 20  ? 46.460 -32.838 -11.605 1.00 21.79 ?  20  ASN   B HA   1 
ATOM   4163 H HB2  . ASN   B 1 20  ? 46.088 -34.806 -12.739 1.00 23.97 ?  20  ASN   B HB2  1 
ATOM   4164 H HB3  . ASN   B 1 20  ? 47.041 -34.345 -13.923 1.00 23.97 ?  20  ASN   B HB3  1 
ATOM   4165 H HD21 . ASN   B 1 20  ? 48.951 -35.079 -10.608 1.00 25.21 ?  20  ASN   B HD21 1 
ATOM   4166 H HD22 . ASN   B 1 20  ? 47.801 -34.135 -10.618 1.00 25.21 ?  20  ASN   B HD22 1 
ATOM   4167 N N    . ALA   B 1 21  ? 48.358 -31.240 -11.717 1.00 18.17 ?  21  ALA   B N    1 
ATOM   4168 C CA   . ALA   B 1 21  ? 49.465 -30.305 -11.861 1.00 18.79 ?  21  ALA   B CA   1 
ATOM   4169 C C    . ALA   B 1 21  ? 49.923 -29.821 -10.493 1.00 17.75 ?  21  ALA   B C    1 
ATOM   4170 O O    . ALA   B 1 21  ? 49.170 -29.846 -9.515  1.00 17.43 ?  21  ALA   B O    1 
ATOM   4171 C CB   . ALA   B 1 21  ? 49.063 -29.116 -12.735 1.00 20.00 ?  21  ALA   B CB   1 
ATOM   4172 H H    . ALA   B 1 21  ? 47.967 -31.219 -10.945 1.00 21.79 ?  21  ALA   B H    1 
ATOM   4173 H HA   . ALA   B 1 21  ? 50.207 -30.763 -12.282 1.00 22.54 ?  21  ALA   B HA   1 
ATOM   4174 H HB1  . ALA   B 1 21  ? 49.845 -28.569 -12.882 1.00 23.99 ?  21  ALA   B HB1  1 
ATOM   4175 H HB2  . ALA   B 1 21  ? 48.727 -29.455 -13.578 1.00 23.99 ?  21  ALA   B HB2  1 
ATOM   4176 H HB3  . ALA   B 1 21  ? 48.373 -28.611 -12.280 1.00 23.99 ?  21  ALA   B HB3  1 
ATOM   4177 N N    . ASP   B 1 22  ? 51.183 -29.388 -10.460 1.00 17.03 ?  22  ASP   B N    1 
ATOM   4178 C CA   . ASP   B 1 22  ? 51.791 -28.680 -9.338  1.00 16.38 ?  22  ASP   B CA   1 
ATOM   4179 C C    . ASP   B 1 22  ? 51.382 -27.211 -9.430  1.00 14.83 ?  22  ASP   B C    1 
ATOM   4180 O O    . ASP   B 1 22  ? 51.698 -26.542 -10.418 1.00 15.14 ?  22  ASP   B O    1 
ATOM   4181 C CB   . ASP   B 1 22  ? 53.308 -28.852 -9.490  1.00 18.15 ?  22  ASP   B CB   1 
ATOM   4182 C CG   . ASP   B 1 22  ? 54.128 -28.097 -8.455  1.00 19.67 ?  22  ASP   B CG   1 
ATOM   4183 O OD1  . ASP   B 1 22  ? 53.758 -26.985 -8.046  1.00 19.73 ?  22  ASP   B OD1  1 
ATOM   4184 O OD2  . ASP   B 1 22  ? 55.205 -28.611 -8.080  1.00 21.86 -1 22  ASP   B OD2  1 
ATOM   4185 H H    . ASP   B 1 22  ? 51.734 -29.504 -11.113 1.00 20.42 ?  22  ASP   B H    1 
ATOM   4186 H HA   . ASP   B 1 22  ? 51.501 -29.064 -8.490  1.00 19.65 ?  22  ASP   B HA   1 
ATOM   4187 H HB2  . ASP   B 1 22  ? 53.534 -29.790 -9.414  1.00 21.77 ?  22  ASP   B HB2  1 
ATOM   4188 H HB3  . ASP   B 1 22  ? 53.573 -28.516 -10.359 1.00 21.77 ?  22  ASP   B HB3  1 
ATOM   4189 N N    . ILE   B 1 23  ? 50.675 -26.712 -8.409  1.00 14.35 ?  23  ILE   B N    1 
ATOM   4190 C CA   . ILE   B 1 23  ? 50.082 -25.373 -8.485  1.00 13.60 ?  23  ILE   B CA   1 
ATOM   4191 C C    . ILE   B 1 23  ? 51.135 -24.281 -8.623  1.00 13.37 ?  23  ILE   B C    1 
ATOM   4192 O O    . ILE   B 1 23  ? 50.865 -23.234 -9.222  1.00 12.77 ?  23  ILE   B O    1 
ATOM   4193 C CB   . ILE   B 1 23  ? 49.145 -25.125 -7.288  1.00 13.96 ?  23  ILE   B CB   1 
ATOM   4194 C CG1  . ILE   B 1 23  ? 48.312 -23.861 -7.505  1.00 14.90 ?  23  ILE   B CG1  1 
ATOM   4195 C CG2  . ILE   B 1 23  ? 49.918 -25.072 -5.988  1.00 14.99 ?  23  ILE   B CG2  1 
ATOM   4196 C CD1  . ILE   B 1 23  ? 47.193 -23.692 -6.488  1.00 15.28 ?  23  ILE   B CD1  1 
ATOM   4197 H H    . ILE   B 1 23  ? 50.528 -27.129 -7.671  1.00 17.21 ?  23  ILE   B H    1 
ATOM   4198 H HA   . ILE   B 1 23  ? 49.537 -25.340 -9.285  1.00 16.31 ?  23  ILE   B HA   1 
ATOM   4199 H HB   . ILE   B 1 23  ? 48.532 -25.875 -7.238  1.00 16.74 ?  23  ILE   B HB   1 
ATOM   4200 H HG12 . ILE   B 1 23  ? 48.895 -23.086 -7.437  1.00 17.87 ?  23  ILE   B HG12 1 
ATOM   4201 H HG13 . ILE   B 1 23  ? 47.913 -23.892 -8.390  1.00 17.87 ?  23  ILE   B HG13 1 
ATOM   4202 H HG21 . ILE   B 1 23  ? 49.293 -25.072 -5.249  1.00 17.98 ?  23  ILE   B HG21 1 
ATOM   4203 H HG22 . ILE   B 1 23  ? 50.499 -25.847 -5.932  1.00 17.98 ?  23  ILE   B HG22 1 
ATOM   4204 H HG23 . ILE   B 1 23  ? 50.452 -24.260 -5.971  1.00 17.98 ?  23  ILE   B HG23 1 
ATOM   4205 H HD11 . ILE   B 1 23  ? 46.664 -22.917 -6.729  1.00 18.33 ?  23  ILE   B HD11 1 
ATOM   4206 H HD12 . ILE   B 1 23  ? 46.638 -24.489 -6.503  1.00 18.33 ?  23  ILE   B HD12 1 
ATOM   4207 H HD13 . ILE   B 1 23  ? 47.580 -23.573 -5.610  1.00 18.33 ?  23  ILE   B HD13 1 
ATOM   4208 N N    . VAL   B 1 24  ? 52.331 -24.487 -8.066  1.00 13.68 ?  24  VAL   B N    1 
ATOM   4209 C CA   . VAL   B 1 24  ? 53.408 -23.510 -8.234  1.00 14.06 ?  24  VAL   B CA   1 
ATOM   4210 C C    . VAL   B 1 24  ? 53.861 -23.464 -9.688  1.00 14.40 ?  24  VAL   B C    1 
ATOM   4211 O O    . VAL   B 1 24  ? 54.003 -22.386 -10.281 1.00 14.98 ?  24  VAL   B O    1 
ATOM   4212 C CB   . VAL   B 1 24  ? 54.583 -23.831 -7.289  1.00 15.30 ?  24  VAL   B CB   1 
ATOM   4213 C CG1  . VAL   B 1 24  ? 55.794 -22.966 -7.625  1.00 15.95 ?  24  VAL   B CG1  1 
ATOM   4214 C CG2  . VAL   B 1 24  ? 54.172 -23.627 -5.851  1.00 16.41 ?  24  VAL   B CG2  1 
ATOM   4215 H H    . VAL   B 1 24  ? 52.540 -25.171 -7.590  1.00 16.40 ?  24  VAL   B H    1 
ATOM   4216 H HA   . VAL   B 1 24  ? 53.076 -22.633 -7.997  1.00 16.85 ?  24  VAL   B HA   1 
ATOM   4217 H HB   . VAL   B 1 24  ? 54.837 -24.763 -7.394  1.00 18.35 ?  24  VAL   B HB   1 
ATOM   4218 H HG11 . VAL   B 1 24  ? 56.387 -22.941 -6.856  1.00 19.13 ?  24  VAL   B HG11 1 
ATOM   4219 H HG12 . VAL   B 1 24  ? 56.258 -23.357 -8.382  1.00 19.13 ?  24  VAL   B HG12 1 
ATOM   4220 H HG13 . VAL   B 1 24  ? 55.493 -22.071 -7.839  1.00 19.13 ?  24  VAL   B HG13 1 
ATOM   4221 H HG21 . VAL   B 1 24  ? 54.889 -23.917 -5.269  1.00 19.68 ?  24  VAL   B HG21 1 
ATOM   4222 H HG22 . VAL   B 1 24  ? 53.989 -22.684 -5.708  1.00 19.68 ?  24  VAL   B HG22 1 
ATOM   4223 H HG23 . VAL   B 1 24  ? 53.370 -24.147 -5.673  1.00 19.68 ?  24  VAL   B HG23 1 
ATOM   4224 N N    . GLU   B 1 25  ? 54.122 -24.633 -10.277 1.00 15.43 ?  25  GLU   B N    1 
ATOM   4225 C CA   . GLU   B 1 25  ? 54.517 -24.667 -11.678 1.00 16.79 ?  25  GLU   B CA   1 
ATOM   4226 C C    . GLU   B 1 25  ? 53.407 -24.126 -12.568 1.00 15.69 ?  25  GLU   B C    1 
ATOM   4227 O O    . GLU   B 1 25  ? 53.673 -23.424 -13.552 1.00 16.52 ?  25  GLU   B O    1 
ATOM   4228 C CB   . GLU   B 1 25  ? 54.910 -26.089 -12.073 1.00 21.03 ?  25  GLU   B CB   1 
ATOM   4229 C CG   . GLU   B 1 25  ? 56.205 -26.542 -11.416 1.00 26.50 ?  25  GLU   B CG   1 
ATOM   4230 C CD   . GLU   B 1 25  ? 57.319 -25.511 -11.526 1.00 31.55 ?  25  GLU   B CD   1 
ATOM   4231 O OE1  . GLU   B 1 25  ? 57.723 -25.189 -12.664 1.00 33.41 ?  25  GLU   B OE1  1 
ATOM   4232 O OE2  . GLU   B 1 25  ? 57.778 -25.002 -10.477 1.00 33.37 -1 25  GLU   B OE2  1 
ATOM   4233 H H    . GLU   B 1 25  ? 54.071 -25.404 -9.893  1.00 18.51 ?  25  GLU   B H    1 
ATOM   4234 H HA   . GLU   B 1 25  ? 55.278 -24.082 -11.799 1.00 20.14 ?  25  GLU   B HA   1 
ATOM   4235 H HB2  . GLU   B 1 25  ? 54.208 -26.701 -11.800 1.00 25.22 ?  25  GLU   B HB2  1 
ATOM   4236 H HB3  . GLU   B 1 25  ? 55.029 -26.129 -13.035 1.00 25.22 ?  25  GLU   B HB3  1 
ATOM   4237 H HG2  . GLU   B 1 25  ? 56.047 -26.693 -10.475 1.00 31.79 ?  25  GLU   B HG2  1 
ATOM   4238 H HG3  . GLU   B 1 25  ? 56.508 -27.356 -11.846 1.00 31.79 ?  25  GLU   B HG3  1 
ATOM   4239 N N    . GLU   B 1 26  ? 52.154 -24.431 -12.229 1.00 15.02 ?  26  GLU   B N    1 
ATOM   4240 C CA   . GLU   B 1 26  ? 51.031 -23.905 -12.998 1.00 15.36 ?  26  GLU   B CA   1 
ATOM   4241 C C    . GLU   B 1 26  ? 50.978 -22.388 -12.916 1.00 14.66 ?  26  GLU   B C    1 
ATOM   4242 O O    . GLU   B 1 26  ? 50.771 -21.712 -13.927 1.00 15.65 ?  26  GLU   B O    1 
ATOM   4243 C CB   . GLU   B 1 26  ? 49.717 -24.486 -12.482 1.00 17.35 ?  26  GLU   B CB   1 
ATOM   4244 C CG   . GLU   B 1 26  ? 49.290 -25.774 -13.146 1.00 21.01 ?  26  GLU   B CG   1 
ATOM   4245 C CD   . GLU   B 1 26  ? 49.053 -25.635 -14.644 1.00 22.63 ?  26  GLU   B CD   1 
ATOM   4246 O OE1  . GLU   B 1 26  ? 48.076 -24.980 -15.068 1.00 22.88 ?  26  GLU   B OE1  1 
ATOM   4247 O OE2  . GLU   B 1 26  ? 49.843 -26.214 -15.398 1.00 25.07 -1 26  GLU   B OE2  1 
ATOM   4248 H H    . GLU   B 1 26  ? 51.930 -24.940 -11.569 1.00 18.01 ?  26  GLU   B H    1 
ATOM   4249 H HA   . GLU   B 1 26  ? 51.136 -24.155 -13.926 1.00 18.42 ?  26  GLU   B HA   1 
ATOM   4250 H HB2  . GLU   B 1 26  ? 49.802 -24.662 -11.532 1.00 20.81 ?  26  GLU   B HB2  1 
ATOM   4251 H HB3  . GLU   B 1 26  ? 49.011 -23.833 -12.628 1.00 20.81 ?  26  GLU   B HB3  1 
ATOM   4252 H HG2  . GLU   B 1 26  ? 49.987 -26.428 -13.017 1.00 25.20 ?  26  GLU   B HG2  1 
ATOM   4253 H HG3  . GLU   B 1 26  ? 48.461 -26.077 -12.743 1.00 25.20 ?  26  GLU   B HG3  1 
ATOM   4254 N N    . ALA   B 1 27  ? 51.133 -21.838 -11.710 1.00 13.83 ?  27  ALA   B N    1 
ATOM   4255 C CA   . ALA   B 1 27  ? 51.090 -20.388 -11.564 1.00 14.33 ?  27  ALA   B CA   1 
ATOM   4256 C C    . ALA   B 1 27  ? 52.157 -19.725 -12.423 1.00 15.17 ?  27  ALA   B C    1 
ATOM   4257 O O    . ALA   B 1 27  ? 51.892 -18.720 -13.098 1.00 16.10 ?  27  ALA   B O    1 
ATOM   4258 C CB   . ALA   B 1 27  ? 51.250 -20.003 -10.094 1.00 14.25 ?  27  ALA   B CB   1 
ATOM   4259 H H    . ALA   B 1 27  ? 51.255 -22.274 -10.976 1.00 16.58 ?  27  ALA   B H    1 
ATOM   4260 H HA   . ALA   B 1 27  ? 50.229 -20.066 -11.861 1.00 17.18 ?  27  ALA   B HA   1 
ATOM   4261 H HB1  . ALA   B 1 27  ? 51.215 -19.036 -10.015 1.00 17.09 ?  27  ALA   B HB1  1 
ATOM   4262 H HB2  . ALA   B 1 27  ? 50.526 -20.401 -9.584  1.00 17.09 ?  27  ALA   B HB2  1 
ATOM   4263 H HB3  . ALA   B 1 27  ? 52.102 -20.331 -9.770  1.00 17.09 ?  27  ALA   B HB3  1 
ATOM   4264 N N    . LYS   B 1 28  ? 53.376 -20.272 -12.417 1.00 16.54 ?  28  LYS   B N    1 
ATOM   4265 C CA   . LYS   B 1 28  ? 54.450 -19.654 -13.186 1.00 19.02 ?  28  LYS   B CA   1 
ATOM   4266 C C    . LYS   B 1 28  ? 54.191 -19.734 -14.684 1.00 19.86 ?  28  LYS   B C    1 
ATOM   4267 O O    . LYS   B 1 28  ? 54.597 -18.833 -15.428 1.00 21.06 ?  28  LYS   B O    1 
ATOM   4268 C CB   . LYS   B 1 28  ? 55.807 -20.255 -12.804 1.00 21.79 ?  28  LYS   B CB   1 
ATOM   4269 C CG   . LYS   B 1 28  ? 56.196 -19.956 -11.359 1.00 25.17 ?  28  LYS   B CG   1 
ATOM   4270 C CD   . LYS   B 1 28  ? 57.627 -20.358 -11.028 1.00 29.63 ?  28  LYS   B CD   1 
ATOM   4271 C CE   . LYS   B 1 28  ? 57.728 -21.825 -10.678 1.00 32.85 ?  28  LYS   B CE   1 
ATOM   4272 N NZ   . LYS   B 1 28  ? 59.088 -22.176 -10.178 1.00 34.23 ?  28  LYS   B NZ   1 
ATOM   4273 H H    . LYS   B 1 28  ? 53.602 -20.982 -11.989 1.00 19.83 ?  28  LYS   B H    1 
ATOM   4274 H HA   . LYS   B 1 28  ? 54.481 -18.712 -12.964 1.00 22.81 ?  28  LYS   B HA   1 
ATOM   4275 H HB2  . LYS   B 1 28  ? 55.769 -21.216 -12.912 1.00 26.13 ?  28  LYS   B HB2  1 
ATOM   4276 H HB3  . LYS   B 1 28  ? 56.491 -19.881 -13.382 1.00 26.13 ?  28  LYS   B HB3  1 
ATOM   4277 H HG2  . LYS   B 1 28  ? 56.104 -19.001 -11.204 1.00 30.19 ?  28  LYS   B HG2  1 
ATOM   4278 H HG3  . LYS   B 1 28  ? 55.599 -20.443 -10.770 1.00 30.19 ?  28  LYS   B HG3  1 
ATOM   4279 H HD2  . LYS   B 1 28  ? 58.189 -20.184 -11.798 1.00 35.54 ?  28  LYS   B HD2  1 
ATOM   4280 H HD3  . LYS   B 1 28  ? 57.930 -19.837 -10.267 1.00 35.54 ?  28  LYS   B HD3  1 
ATOM   4281 H HE2  . LYS   B 1 28  ? 57.085 -22.032 -9.981  1.00 39.40 ?  28  LYS   B HE2  1 
ATOM   4282 H HE3  . LYS   B 1 28  ? 57.548 -22.357 -11.468 1.00 39.40 ?  28  LYS   B HE3  1 
ATOM   4283 H HZ1  . LYS   B 1 28  ? 59.124 -23.043 -9.978  1.00 41.07 ?  28  LYS   B HZ1  1 
ATOM   4284 H HZ2  . LYS   B 1 28  ? 59.697 -21.997 -10.801 1.00 41.07 ?  28  LYS   B HZ2  1 
ATOM   4285 H HZ3  . LYS   B 1 28  ? 59.275 -21.703 -9.447  1.00 41.07 ?  28  LYS   B HZ3  1 
ATOM   4286 N N    . LYS   B 1 29  ? 53.483 -20.768 -15.138 1.00 20.96 ?  29  LYS   B N    1 
ATOM   4287 C CA   . LYS   B 1 29  ? 53.203 -20.915 -16.562 1.00 23.51 ?  29  LYS   B CA   1 
ATOM   4288 C C    . LYS   B 1 29  ? 51.949 -20.164 -17.000 1.00 22.23 ?  29  LYS   B C    1 
ATOM   4289 O O    . LYS   B 1 29  ? 51.943 -19.548 -18.071 1.00 23.65 ?  29  LYS   B O    1 
ATOM   4290 C CB   . LYS   B 1 29  ? 53.081 -22.398 -16.917 1.00 28.42 ?  29  LYS   B CB   1 
ATOM   4291 C CG   . LYS   B 1 29  ? 52.940 -22.672 -18.402 1.00 32.97 ?  29  LYS   B CG   1 
ATOM   4292 C CD   . LYS   B 1 29  ? 53.199 -24.138 -18.720 1.00 36.71 ?  29  LYS   B CD   1 
ATOM   4293 C CE   . LYS   B 1 29  ? 52.147 -25.048 -18.103 1.00 39.23 ?  29  LYS   B CE   1 
ATOM   4294 N NZ   . LYS   B 1 29  ? 52.410 -26.484 -18.413 1.00 40.44 ?  29  LYS   B NZ   1 
ATOM   4295 H H    . LYS   B 1 29  ? 53.152 -21.397 -14.641 1.00 25.14 ?  29  LYS   B H    1 
ATOM   4296 H HA   . LYS   B 1 29  ? 53.949 -20.555 -17.057 1.00 28.21 ?  29  LYS   B HA   1 
ATOM   4297 H HB2  . LYS   B 1 29  ? 53.879 -22.856 -16.609 1.00 34.10 ?  29  LYS   B HB2  1 
ATOM   4298 H HB3  . LYS   B 1 29  ? 52.302 -22.762 -16.475 1.00 34.10 ?  29  LYS   B HB3  1 
ATOM   4299 H HG2  . LYS   B 1 29  ? 52.039 -22.453 -18.683 1.00 39.55 ?  29  LYS   B HG2  1 
ATOM   4300 H HG3  . LYS   B 1 29  ? 53.585 -22.135 -18.890 1.00 39.55 ?  29  LYS   B HG3  1 
ATOM   4301 H HD2  . LYS   B 1 29  ? 53.183 -24.263 -19.681 1.00 44.04 ?  29  LYS   B HD2  1 
ATOM   4302 H HD3  . LYS   B 1 29  ? 54.066 -24.393 -18.364 1.00 44.04 ?  29  LYS   B HD3  1 
ATOM   4303 H HE2  . LYS   B 1 29  ? 52.154 -24.943 -17.139 1.00 47.06 ?  29  LYS   B HE2  1 
ATOM   4304 H HE3  . LYS   B 1 29  ? 51.275 -24.815 -18.459 1.00 47.06 ?  29  LYS   B HE3  1 
ATOM   4305 H HZ1  . LYS   B 1 29  ? 51.782 -26.995 -18.043 1.00 48.52 ?  29  LYS   B HZ1  1 
ATOM   4306 H HZ2  . LYS   B 1 29  ? 52.404 -26.611 -19.294 1.00 48.52 ?  29  LYS   B HZ2  1 
ATOM   4307 H HZ3  . LYS   B 1 29  ? 53.205 -26.724 -18.092 1.00 48.52 ?  29  LYS   B HZ3  1 
ATOM   4308 N N    . VAL   B 1 30  ? 50.885 -20.212 -16.193 1.00 20.07 ?  30  VAL   B N    1 
ATOM   4309 C CA   . VAL   B 1 30  ? 49.593 -19.628 -16.561 1.00 20.45 ?  30  VAL   B CA   1 
ATOM   4310 C C    . VAL   B 1 30  ? 49.588 -18.113 -16.424 1.00 19.15 ?  30  VAL   B C    1 
ATOM   4311 O O    . VAL   B 1 30  ? 48.843 -17.418 -17.132 1.00 20.17 ?  30  VAL   B O    1 
ATOM   4312 C CB   . VAL   B 1 30  ? 48.495 -20.241 -15.671 1.00 21.64 ?  30  VAL   B CB   1 
ATOM   4313 C CG1  . VAL   B 1 30  ? 47.211 -19.425 -15.744 1.00 22.02 ?  30  VAL   B CG1  1 
ATOM   4314 C CG2  . VAL   B 1 30  ? 48.245 -21.692 -16.055 1.00 22.48 ?  30  VAL   B CG2  1 
ATOM   4315 H H    . VAL   B 1 30  ? 50.878 -20.609 -15.420 1.00 24.07 ?  30  VAL   B H    1 
ATOM   4316 H HA   . VAL   B 1 30  ? 49.393 -19.868 -17.480 1.00 24.53 ?  30  VAL   B HA   1 
ATOM   4317 H HB   . VAL   B 1 30  ? 48.795 -20.237 -14.748 1.00 25.96 ?  30  VAL   B HB   1 
ATOM   4318 H HG11 . VAL   B 1 30  ? 46.470 -19.996 -15.486 1.00 26.41 ?  30  VAL   B HG11 1 
ATOM   4319 H HG12 . VAL   B 1 30  ? 47.274 -18.677 -15.134 1.00 26.41 ?  30  VAL   B HG12 1 
ATOM   4320 H HG13 . VAL   B 1 30  ? 47.080 -19.120 -16.651 1.00 26.41 ?  30  VAL   B HG13 1 
ATOM   4321 H HG21 . VAL   B 1 30  ? 47.555 -22.062 -15.475 1.00 26.96 ?  30  VAL   B HG21 1 
ATOM   4322 H HG22 . VAL   B 1 30  ? 47.947 -21.729 -16.978 1.00 26.96 ?  30  VAL   B HG22 1 
ATOM   4323 H HG23 . VAL   B 1 30  ? 49.065 -22.196 -15.949 1.00 26.96 ?  30  VAL   B HG23 1 
ATOM   4324 N N    . LYS   B 1 31  ? 50.371 -17.592 -15.490 1.00 18.59 ?  31  LYS   B N    1 
ATOM   4325 C CA   . LYS   B 1 31  ? 50.399 -16.181 -15.138 1.00 19.16 ?  31  LYS   B CA   1 
ATOM   4326 C C    . LYS   B 1 31  ? 49.004 -15.707 -14.733 1.00 17.11 ?  31  LYS   B C    1 
ATOM   4327 O O    . LYS   B 1 31  ? 48.448 -14.795 -15.358 1.00 18.14 ?  31  LYS   B O    1 
ATOM   4328 C CB   . LYS   B 1 31  ? 51.020 -15.369 -16.282 1.00 22.09 ?  31  LYS   B CB   1 
ATOM   4329 C CG   . LYS   B 1 31  ? 52.457 -15.798 -16.601 1.00 25.78 ?  31  LYS   B CG   1 
ATOM   4330 C CD   . LYS   B 1 31  ? 53.041 -15.031 -17.769 1.00 29.49 ?  31  LYS   B CD   1 
ATOM   4331 C CE   . LYS   B 1 31  ? 54.529 -15.298 -17.912 1.00 32.10 ?  31  LYS   B CE   1 
ATOM   4332 N NZ   . LYS   B 1 31  ? 55.283 -14.862 -16.702 1.00 33.32 ?  31  LYS   B NZ   1 
ATOM   4333 H H    . LYS   B 1 31  ? 50.910 -18.068 -15.030 1.00 22.30 ?  31  LYS   B H    1 
ATOM   4334 H HA   . LYS   B 1 31  ? 50.968 -16.085 -14.370 1.00 22.97 ?  31  LYS   B HA   1 
ATOM   4335 H HB2  . LYS   B 1 31  ? 50.489 -15.486 -17.086 1.00 26.50 ?  31  LYS   B HB2  1 
ATOM   4336 H HB3  . LYS   B 1 31  ? 51.038 -14.436 -16.026 1.00 26.50 ?  31  LYS   B HB3  1 
ATOM   4337 H HG2  . LYS   B 1 31  ? 53.011 -15.641 -15.821 1.00 30.92 ?  31  LYS   B HG2  1 
ATOM   4338 H HG3  . LYS   B 1 31  ? 52.463 -16.744 -16.826 1.00 30.92 ?  31  LYS   B HG3  1 
ATOM   4339 H HD2  . LYS   B 1 31  ? 52.600 -15.312 -18.586 1.00 35.37 ?  31  LYS   B HD2  1 
ATOM   4340 H HD3  . LYS   B 1 31  ? 52.912 -14.083 -17.622 1.00 35.37 ?  31  LYS   B HD3  1 
ATOM   4341 H HE2  . LYS   B 1 31  ? 54.674 -16.250 -18.034 1.00 38.50 ?  31  LYS   B HE2  1 
ATOM   4342 H HE3  . LYS   B 1 31  ? 54.869 -14.807 -18.676 1.00 38.50 ?  31  LYS   B HE3  1 
ATOM   4343 H HZ1  . LYS   B 1 31  ? 56.158 -14.922 -16.850 1.00 39.97 ?  31  LYS   B HZ1  1 
ATOM   4344 H HZ2  . LYS   B 1 31  ? 55.080 -14.018 -16.505 1.00 39.97 ?  31  LYS   B HZ2  1 
ATOM   4345 H HZ3  . LYS   B 1 31  ? 55.072 -15.378 -16.008 1.00 39.97 ?  31  LYS   B HZ3  1 
ATOM   4346 N N    . PRO   B 1 32  ? 48.406 -16.298 -13.692 1.00 15.03 ?  32  PRO   B N    1 
ATOM   4347 C CA   . PRO   B 1 32  ? 47.025 -15.946 -13.333 1.00 13.87 ?  32  PRO   B CA   1 
ATOM   4348 C C    . PRO   B 1 32  ? 46.940 -14.599 -12.632 1.00 14.18 ?  32  PRO   B C    1 
ATOM   4349 O O    . PRO   B 1 32  ? 47.869 -14.167 -11.943 1.00 15.25 ?  32  PRO   B O    1 
ATOM   4350 C CB   . PRO   B 1 32  ? 46.635 -17.062 -12.359 1.00 14.44 ?  32  PRO   B CB   1 
ATOM   4351 C CG   . PRO   B 1 32  ? 47.939 -17.405 -11.685 1.00 14.77 ?  32  PRO   B CG   1 
ATOM   4352 C CD   . PRO   B 1 32  ? 48.997 -17.265 -12.743 1.00 14.95 ?  32  PRO   B CD   1 
ATOM   4353 H HA   . PRO   B 1 32  ? 46.440 -15.964 -14.113 1.00 16.64 ?  32  PRO   B HA   1 
ATOM   4354 H HB2  . PRO   B 1 32  ? 45.988 -16.733 -11.717 1.00 17.31 ?  32  PRO   B HB2  1 
ATOM   4355 H HB3  . PRO   B 1 32  ? 46.288 -17.826 -12.846 1.00 17.31 ?  32  PRO   B HB3  1 
ATOM   4356 H HG2  . PRO   B 1 32  ? 48.105 -16.781 -10.956 1.00 17.71 ?  32  PRO   B HG2  1 
ATOM   4357 H HG3  . PRO   B 1 32  ? 47.914 -18.314 -11.355 1.00 17.71 ?  32  PRO   B HG3  1 
ATOM   4358 H HD2  . PRO   B 1 32  ? 49.812 -16.895 -12.365 1.00 17.93 ?  32  PRO   B HD2  1 
ATOM   4359 H HD3  . PRO   B 1 32  ? 49.156 -18.109 -13.181 1.00 17.93 ?  32  PRO   B HD3  1 
ATOM   4360 N N    . THR   B 1 33  ? 45.781 -13.949 -12.790 1.00 13.52 ?  33  THR   B N    1 
ATOM   4361 C CA   . THR   B 1 33  ? 45.490 -12.768 -11.986 1.00 13.88 ?  33  THR   B CA   1 
ATOM   4362 C C    . THR   B 1 33  ? 45.442 -13.116 -10.505 1.00 13.33 ?  33  THR   B C    1 
ATOM   4363 O O    . THR   B 1 33  ? 45.914 -12.334 -9.664  1.00 14.37 ?  33  THR   B O    1 
ATOM   4364 C CB   . THR   B 1 33  ? 44.171 -12.133 -12.432 1.00 14.52 ?  33  THR   B CB   1 
ATOM   4365 O OG1  . THR   B 1 33  ? 44.222 -11.868 -13.834 1.00 14.48 ?  33  THR   B OG1  1 
ATOM   4366 C CG2  . THR   B 1 33  ? 43.915 -10.838 -11.671 1.00 15.79 ?  33  THR   B CG2  1 
ATOM   4367 H H    . THR   B 1 33  ? 45.152 -14.181 -13.336 1.00 16.21 ?  33  THR   B H    1 
ATOM   4368 H HA   . THR   B 1 33  ? 46.196 -12.121 -12.119 1.00 16.64 ?  33  THR   B HA   1 
ATOM   4369 H HB   . THR   B 1 33  ? 43.441 -12.750 -12.244 1.00 17.41 ?  33  THR   B HB   1 
ATOM   4370 H HG1  . THR   B 1 33  ? 43.499 -11.516 -14.085 1.00 17.37 ?  33  THR   B HG1  1 
ATOM   4371 H HG21 . THR   B 1 33  ? 43.170 -10.368 -12.065 1.00 18.94 ?  33  THR   B HG21 1 
ATOM   4372 H HG22 . THR   B 1 33  ? 43.715 -11.033 -10.741 1.00 18.94 ?  33  THR   B HG22 1 
ATOM   4373 H HG23 . THR   B 1 33  ? 44.705 -10.276 -11.711 1.00 18.94 ?  33  THR   B HG23 1 
ATOM   4374 N N    . VAL   B 1 34  ? 44.883 -14.283 -10.164 1.00 12.64 ?  34  VAL   B N    1 
ATOM   4375 C CA   . VAL   B 1 34  ? 44.693 -14.686 -8.774  1.00 12.45 ?  34  VAL   B CA   1 
ATOM   4376 C C    . VAL   B 1 34  ? 45.121 -16.137 -8.606  1.00 11.26 ?  34  VAL   B C    1 
ATOM   4377 O O    . VAL   B 1 34  ? 44.607 -17.026 -9.295  1.00 12.17 ?  34  VAL   B O    1 
ATOM   4378 C CB   . VAL   B 1 34  ? 43.224 -14.540 -8.327  1.00 13.44 ?  34  VAL   B CB   1 
ATOM   4379 C CG1  . VAL   B 1 34  ? 43.065 -14.991 -6.875  1.00 13.92 ?  34  VAL   B CG1  1 
ATOM   4380 C CG2  . VAL   B 1 34  ? 42.717 -13.116 -8.527  1.00 14.30 ?  34  VAL   B CG2  1 
ATOM   4381 H H    . VAL   B 1 34  ? 44.612 -14.873 -10.730 1.00 15.15 ?  34  VAL   B H    1 
ATOM   4382 H HA   . VAL   B 1 34  ? 45.247 -14.136 -8.195  1.00 14.93 ?  34  VAL   B HA   1 
ATOM   4383 H HB   . VAL   B 1 34  ? 42.679 -15.127 -8.872  1.00 16.11 ?  34  VAL   B HB   1 
ATOM   4384 H HG11 . VAL   B 1 34  ? 42.209 -14.675 -6.540  1.00 16.69 ?  34  VAL   B HG11 1 
ATOM   4385 H HG12 . VAL   B 1 34  ? 43.095 -15.960 -6.833  1.00 16.69 ?  34  VAL   B HG12 1 
ATOM   4386 H HG13 . VAL   B 1 34  ? 43.784 -14.612 -6.344  1.00 16.69 ?  34  VAL   B HG13 1 
ATOM   4387 H HG21 . VAL   B 1 34  ? 41.802 -13.061 -8.209  1.00 17.14 ?  34  VAL   B HG21 1 
ATOM   4388 H HG22 . VAL   B 1 34  ? 43.280 -12.507 -8.028  1.00 17.14 ?  34  VAL   B HG22 1 
ATOM   4389 H HG23 . VAL   B 1 34  ? 42.751 -12.902 -9.473  1.00 17.14 ?  34  VAL   B HG23 1 
ATOM   4390 N N    . VAL   B 1 35  ? 46.026 -16.386 -7.662  1.00 11.01 ?  35  VAL   B N    1 
ATOM   4391 C CA   . VAL   B 1 35  ? 46.262 -17.730 -7.148  1.00 11.05 ?  35  VAL   B CA   1 
ATOM   4392 C C    . VAL   B 1 35  ? 45.725 -17.787 -5.727  1.00 10.53 ?  35  VAL   B C    1 
ATOM   4393 O O    . VAL   B 1 35  ? 45.942 -16.865 -4.935  1.00 10.78 ?  35  VAL   B O    1 
ATOM   4394 C CB   . VAL   B 1 35  ? 47.748 -18.158 -7.232  1.00 11.67 ?  35  VAL   B CB   1 
ATOM   4395 C CG1  . VAL   B 1 35  ? 48.655 -17.312 -6.327  1.00 12.36 ?  35  VAL   B CG1  1 
ATOM   4396 C CG2  . VAL   B 1 35  ? 47.885 -19.643 -6.901  1.00 12.25 ?  35  VAL   B CG2  1 
ATOM   4397 H H    . VAL   B 1 35  ? 46.530 -15.782 -7.304  1.00 13.20 ?  35  VAL   B H    1 
ATOM   4398 H HA   . VAL   B 1 35  ? 45.744 -18.357 -7.672  1.00 13.24 ?  35  VAL   B HA   1 
ATOM   4399 H HB   . VAL   B 1 35  ? 48.046 -18.039 -8.147  1.00 13.99 ?  35  VAL   B HB   1 
ATOM   4400 H HG11 . VAL   B 1 35  ? 49.575 -17.551 -6.502  1.00 14.82 ?  35  VAL   B HG11 1 
ATOM   4401 H HG12 . VAL   B 1 35  ? 48.504 -16.378 -6.524  1.00 14.82 ?  35  VAL   B HG12 1 
ATOM   4402 H HG13 . VAL   B 1 35  ? 48.431 -17.500 -5.401  1.00 14.82 ?  35  VAL   B HG13 1 
ATOM   4403 H HG21 . VAL   B 1 35  ? 48.804 -19.914 -7.020  1.00 14.69 ?  35  VAL   B HG21 1 
ATOM   4404 H HG22 . VAL   B 1 35  ? 47.612 -19.791 -5.978  1.00 14.69 ?  35  VAL   B HG22 1 
ATOM   4405 H HG23 . VAL   B 1 35  ? 47.307 -20.159 -7.493  1.00 14.69 ?  35  VAL   B HG23 1 
ATOM   4406 N N    . VAL   B 1 36  ? 45.006 -18.863 -5.409  1.00 10.50 ?  36  VAL   B N    1 
ATOM   4407 C CA   . VAL   B 1 36  ? 44.463 -19.069 -4.075  1.00 10.34 ?  36  VAL   B CA   1 
ATOM   4408 C C    . VAL   B 1 36  ? 45.471 -19.830 -3.224  1.00 10.03 ?  36  VAL   B C    1 
ATOM   4409 O O    . VAL   B 1 36  ? 46.011 -20.863 -3.646  1.00 11.30 ?  36  VAL   B O    1 
ATOM   4410 C CB   . VAL   B 1 36  ? 43.128 -19.830 -4.152  1.00 10.97 ?  36  VAL   B CB   1 
ATOM   4411 C CG1  . VAL   B 1 36  ? 42.623 -20.199 -2.763  1.00 11.46 ?  36  VAL   B CG1  1 
ATOM   4412 C CG2  . VAL   B 1 36  ? 42.095 -19.001 -4.900  1.00 11.37 ?  36  VAL   B CG2  1 
ATOM   4413 H H    . VAL   B 1 36  ? 44.836 -19.503 -5.956  1.00 12.59 ?  36  VAL   B H    1 
ATOM   4414 H HA   . VAL   B 1 36  ? 44.300 -18.209 -3.660  1.00 12.39 ?  36  VAL   B HA   1 
ATOM   4415 H HB   . VAL   B 1 36  ? 43.263 -20.651 -4.650  1.00 13.15 ?  36  VAL   B HB   1 
ATOM   4416 H HG11 . VAL   B 1 36  ? 41.685 -20.441 -2.823  1.00 13.74 ?  36  VAL   B HG11 1 
ATOM   4417 H HG12 . VAL   B 1 36  ? 43.136 -20.947 -2.424  1.00 13.74 ?  36  VAL   B HG12 1 
ATOM   4418 H HG13 . VAL   B 1 36  ? 42.725 -19.431 -2.176  1.00 13.74 ?  36  VAL   B HG13 1 
ATOM   4419 H HG21 . VAL   B 1 36  ? 41.255 -19.482 -4.923  1.00 13.63 ?  36  VAL   B HG21 1 
ATOM   4420 H HG22 . VAL   B 1 36  ? 41.978 -18.151 -4.443  1.00 13.63 ?  36  VAL   B HG22 1 
ATOM   4421 H HG23 . VAL   B 1 36  ? 42.409 -18.842 -5.808  1.00 13.63 ?  36  VAL   B HG23 1 
ATOM   4422 N N    . ASN   B 1 37  ? 45.691 -19.337 -2.008  1.00 10.24 ?  37  ASN   B N    1 
ATOM   4423 C CA   . ASN   B 1 37  ? 46.445 -20.059 -0.999  1.00 10.84 ?  37  ASN   B CA   1 
ATOM   4424 C C    . ASN   B 1 37  ? 45.501 -20.734 -0.010  1.00 10.63 ?  37  ASN   B C    1 
ATOM   4425 O O    . ASN   B 1 37  ? 44.490 -20.161 0.408   1.00 11.26 ?  37  ASN   B O    1 
ATOM   4426 C CB   . ASN   B 1 37  ? 47.376 -19.113 -0.240  1.00 10.85 ?  37  ASN   B CB   1 
ATOM   4427 C CG   . ASN   B 1 37  ? 48.228 -19.832 0.774   1.00 10.78 ?  37  ASN   B CG   1 
ATOM   4428 O OD1  . ASN   B 1 37  ? 48.572 -21.013 0.597   1.00 11.74 ?  37  ASN   B OD1  1 
ATOM   4429 N ND2  . ASN   B 1 37  ? 48.570 -19.136 1.850   1.00 11.46 ?  37  ASN   B ND2  1 
ATOM   4430 H H    . ASN   B 1 37  ? 45.403 -18.571 -1.736  1.00 12.27 ?  37  ASN   B H    1 
ATOM   4431 H HA   . ASN   B 1 37  ? 46.981 -20.748 -1.420  1.00 12.99 ?  37  ASN   B HA   1 
ATOM   4432 H HB2  . ASN   B 1 37  ? 47.969 -18.682 -0.875  1.00 13.01 ?  37  ASN   B HB2  1 
ATOM   4433 H HB3  . ASN   B 1 37  ? 46.849 -18.451 0.228   1.00 13.01 ?  37  ASN   B HB3  1 
ATOM   4434 H HD21 . ASN   B 1 37  ? 49.054 -19.500 2.463   1.00 13.74 ?  37  ASN   B HD21 1 
ATOM   4435 H HD22 . ASN   B 1 37  ? 48.308 -18.328 1.944   1.00 13.74 ?  37  ASN   B HD22 1 
ATOM   4436 N N    . ALA   B 1 38  ? 45.853 -21.966 0.360   1.00 10.88 ?  38  ALA   B N    1 
ATOM   4437 C CA   . ALA   B 1 38  ? 45.201 -22.714 1.436   1.00 11.37 ?  38  ALA   B CA   1 
ATOM   4438 C C    . ALA   B 1 38  ? 45.787 -22.232 2.762   1.00 11.26 ?  38  ALA   B C    1 
ATOM   4439 O O    . ALA   B 1 38  ? 46.688 -22.840 3.349   1.00 12.12 ?  38  ALA   B O    1 
ATOM   4440 C CB   . ALA   B 1 38  ? 45.406 -24.210 1.235   1.00 12.62 ?  38  ALA   B CB   1 
ATOM   4441 H H    . ALA   B 1 38  ? 46.508 -22.399 0.007   1.00 13.04 ?  38  ALA   B H    1 
ATOM   4442 H HA   . ALA   B 1 38  ? 44.248 -22.525 1.431   1.00 13.63 ?  38  ALA   B HA   1 
ATOM   4443 H HB1  . ALA   B 1 38  ? 44.956 -24.689 1.958   1.00 15.13 ?  38  ALA   B HB1  1 
ATOM   4444 H HB2  . ALA   B 1 38  ? 45.014 -24.471 0.385   1.00 15.13 ?  38  ALA   B HB2  1 
ATOM   4445 H HB3  . ALA   B 1 38  ? 46.348 -24.409 1.246   1.00 15.13 ?  38  ALA   B HB3  1 
ATOM   4446 N N    . ALA   B 1 39  ? 45.267 -21.095 3.227   1.00 10.91 ?  39  ALA   B N    1 
ATOM   4447 C CA   . ALA   B 1 39  ? 45.811 -20.358 4.358   1.00 11.27 ?  39  ALA   B CA   1 
ATOM   4448 C C    . ALA   B 1 39  ? 45.195 -20.804 5.684   1.00 11.34 ?  39  ALA   B C    1 
ATOM   4449 O O    . ALA   B 1 39  ? 44.168 -21.485 5.729   1.00 12.43 ?  39  ALA   B O    1 
ATOM   4450 C CB   . ALA   B 1 39  ? 45.573 -18.860 4.159   1.00 12.04 ?  39  ALA   B CB   1 
ATOM   4451 H H    . ALA   B 1 39  ? 44.568 -20.725 2.889   1.00 13.08 ?  39  ALA   B H    1 
ATOM   4452 H HA   . ALA   B 1 39  ? 46.762 -20.510 4.408   1.00 13.51 ?  39  ALA   B HA   1 
ATOM   4453 H HB1  . ALA   B 1 39  ? 45.938 -18.379 4.917   1.00 14.43 ?  39  ALA   B HB1  1 
ATOM   4454 H HB2  . ALA   B 1 39  ? 46.018 -18.579 3.343   1.00 14.43 ?  39  ALA   B HB2  1 
ATOM   4455 H HB3  . ALA   B 1 39  ? 44.620 -18.695 4.089   1.00 14.43 ?  39  ALA   B HB3  1 
ATOM   4456 N N    . ASN   B 1 40  ? 45.830 -20.374 6.774   1.00 12.21 ?  40  ASN   B N    1 
ATOM   4457 C CA   . ASN   B 1 40  ? 45.277 -20.431 8.117   1.00 12.79 ?  40  ASN   B CA   1 
ATOM   4458 C C    . ASN   B 1 40  ? 45.087 -19.005 8.642   1.00 12.37 ?  40  ASN   B C    1 
ATOM   4459 O O    . ASN   B 1 40  ? 45.495 -18.021 8.014   1.00 12.37 ?  40  ASN   B O    1 
ATOM   4460 C CB   . ASN   B 1 40  ? 46.130 -21.305 9.055   1.00 13.98 ?  40  ASN   B CB   1 
ATOM   4461 C CG   . ASN   B 1 40  ? 47.589 -20.899 9.078   1.00 14.88 ?  40  ASN   B CG   1 
ATOM   4462 O OD1  . ASN   B 1 40  ? 47.908 -19.715 9.135   1.00 16.60 ?  40  ASN   B OD1  1 
ATOM   4463 N ND2  . ASN   B 1 40  ? 48.484 -21.879 9.030   1.00 14.82 ?  40  ASN   B ND2  1 
ATOM   4464 H H    . ASN   B 1 40  ? 46.619 -20.034 6.750   1.00 14.64 ?  40  ASN   B H    1 
ATOM   4465 H HA   . ASN   B 1 40  ? 44.397 -20.829 8.075   1.00 15.33 ?  40  ASN   B HA   1 
ATOM   4466 H HB2  . ASN   B 1 40  ? 45.785 -21.231 9.959   1.00 16.77 ?  40  ASN   B HB2  1 
ATOM   4467 H HB3  . ASN   B 1 40  ? 46.080 -22.226 8.755   1.00 16.77 ?  40  ASN   B HB3  1 
ATOM   4468 H HD21 . ASN   B 1 40  ? 49.327 -21.697 9.043   1.00 17.78 ?  40  ASN   B HD21 1 
ATOM   4469 H HD22 . ASN   B 1 40  ? 48.226 -22.698 8.990   1.00 17.78 ?  40  ASN   B HD22 1 
ATOM   4470 N N    . VAL   B 1 41  ? 44.429 -18.879 9.796   1.00 12.84 ?  41  VAL   B N    1 
ATOM   4471 C CA   . VAL   B 1 41  ? 43.975 -17.559 10.241  1.00 13.76 ?  41  VAL   B CA   1 
ATOM   4472 C C    . VAL   B 1 41  ? 45.126 -16.609 10.542  1.00 13.49 ?  41  VAL   B C    1 
ATOM   4473 O O    . VAL   B 1 41  ? 44.950 -15.389 10.468  1.00 13.51 ?  41  VAL   B O    1 
ATOM   4474 C CB   . VAL   B 1 41  ? 42.995 -17.636 11.430  1.00 15.18 ?  41  VAL   B CB   1 
ATOM   4475 C CG1  . VAL   B 1 41  ? 41.705 -18.338 11.028  1.00 15.93 ?  41  VAL   B CG1  1 
ATOM   4476 C CG2  . VAL   B 1 41  ? 43.649 -18.309 12.623  1.00 16.34 ?  41  VAL   B CG2  1 
ATOM   4477 H H    . VAL   B 1 41  ? 44.236 -19.523 10.322  1.00 15.40 ?  41  VAL   B H    1 
ATOM   4478 H HA   . VAL   B 1 41  ? 43.482 -17.158 9.512   1.00 16.51 ?  41  VAL   B HA   1 
ATOM   4479 H HB   . VAL   B 1 41  ? 42.761 -16.733 11.699  1.00 18.21 ?  41  VAL   B HB   1 
ATOM   4480 H HG11 . VAL   B 1 41  ? 41.102 -18.351 11.790  1.00 19.11 ?  41  VAL   B HG11 1 
ATOM   4481 H HG12 . VAL   B 1 41  ? 41.298 -17.854 10.294  1.00 19.11 ?  41  VAL   B HG12 1 
ATOM   4482 H HG13 . VAL   B 1 41  ? 41.912 -19.245 10.756  1.00 19.11 ?  41  VAL   B HG13 1 
ATOM   4483 H HG21 . VAL   B 1 41  ? 43.006 -18.366 13.346  1.00 19.60 ?  41  VAL   B HG21 1 
ATOM   4484 H HG22 . VAL   B 1 41  ? 43.937 -19.199 12.366  1.00 19.60 ?  41  VAL   B HG22 1 
ATOM   4485 H HG23 . VAL   B 1 41  ? 44.415 -17.783 12.903  1.00 19.60 ?  41  VAL   B HG23 1 
ATOM   4486 N N    . TYR   B 1 42  ? 46.295 -17.125 10.923  1.00 13.85 ?  42  TYR   B N    1 
ATOM   4487 C CA   . TYR   B 1 42  ? 47.451 -16.275 11.194  1.00 14.31 ?  42  TYR   B CA   1 
ATOM   4488 C C    . TYR   B 1 42  ? 48.419 -16.199 10.017  1.00 13.53 ?  42  TYR   B C    1 
ATOM   4489 O O    . TYR   B 1 42  ? 49.509 -15.628 10.155  1.00 14.78 ?  42  TYR   B O    1 
ATOM   4490 C CB   . TYR   B 1 42  ? 48.150 -16.677 12.501  1.00 16.38 ?  42  TYR   B CB   1 
ATOM   4491 C CG   . TYR   B 1 42  ? 47.561 -15.983 13.727  1.00 16.78 ?  42  TYR   B CG   1 
ATOM   4492 C CD1  . TYR   B 1 42  ? 47.780 -14.624 13.950  1.00 16.14 ?  42  TYR   B CD1  1 
ATOM   4493 C CD2  . TYR   B 1 42  ? 46.779 -16.673 14.644  1.00 19.12 ?  42  TYR   B CD2  1 
ATOM   4494 C CE1  . TYR   B 1 42  ? 47.248 -13.979 15.053  1.00 17.41 ?  42  TYR   B CE1  1 
ATOM   4495 C CE2  . TYR   B 1 42  ? 46.246 -16.036 15.753  1.00 19.26 ?  42  TYR   B CE2  1 
ATOM   4496 C CZ   . TYR   B 1 42  ? 46.481 -14.686 15.951  1.00 19.35 ?  42  TYR   B CZ   1 
ATOM   4497 O OH   . TYR   B 1 42  ? 45.957 -14.040 17.055  1.00 22.06 ?  42  TYR   B OH   1 
ATOM   4498 H H    . TYR   B 1 42  ? 46.441 -17.971 11.025  1.00 16.60 ?  42  TYR   B H    1 
ATOM   4499 H HA   . TYR   B 1 42  ? 47.121 -15.378 11.329  1.00 17.16 ?  42  TYR   B HA   1 
ATOM   4500 H HB2  . TYR   B 1 42  ? 48.061 -17.633 12.627  1.00 19.64 ?  42  TYR   B HB2  1 
ATOM   4501 H HB3  . TYR   B 1 42  ? 49.088 -16.435 12.439  1.00 19.64 ?  42  TYR   B HB3  1 
ATOM   4502 H HD1  . TYR   B 1 42  ? 48.301 -14.142 13.339  1.00 19.35 ?  42  TYR   B HD1  1 
ATOM   4503 H HD2  . TYR   B 1 42  ? 46.621 -17.581 14.511  1.00 22.93 ?  42  TYR   B HD2  1 
ATOM   4504 H HE1  . TYR   B 1 42  ? 47.412 -13.072 15.183  1.00 20.88 ?  42  TYR   B HE1  1 
ATOM   4505 H HE2  . TYR   B 1 42  ? 45.729 -16.514 16.357  1.00 23.10 ?  42  TYR   B HE2  1 
ATOM   4506 H HH   . TYR   B 1 42  ? 46.185 -13.233 17.040  1.00 26.46 ?  42  TYR   B HH   1 
ATOM   4507 N N    . LEU   B 1 43  ? 48.027 -16.719 8.855   1.00 12.53 ?  43  LEU   B N    1 
ATOM   4508 C CA   . LEU   B 1 43  ? 48.843 -16.638 7.648   1.00 12.31 ?  43  LEU   B CA   1 
ATOM   4509 C C    . LEU   B 1 43  ? 50.259 -17.146 7.903   1.00 12.81 ?  43  LEU   B C    1 
ATOM   4510 O O    . LEU   B 1 43  ? 51.238 -16.545 7.461   1.00 13.44 ?  43  LEU   B O    1 
ATOM   4511 C CB   . LEU   B 1 43  ? 48.851 -15.227 7.052   1.00 12.66 ?  43  LEU   B CB   1 
ATOM   4512 C CG   . LEU   B 1 43  ? 47.491 -14.621 6.667   1.00 12.88 ?  43  LEU   B CG   1 
ATOM   4513 C CD1  . LEU   B 1 43  ? 47.690 -13.219 6.103   1.00 14.15 ?  43  LEU   B CD1  1 
ATOM   4514 C CD2  . LEU   B 1 43  ? 46.739 -15.509 5.673   1.00 13.28 ?  43  LEU   B CD2  1 
ATOM   4515 H H    . LEU   B 1 43  ? 47.288 -17.149 8.741   1.00 15.02 ?  43  LEU   B H    1 
ATOM   4516 H HA   . LEU   B 1 43  ? 48.448 -17.223 6.979   1.00 14.76 ?  43  LEU   B HA   1 
ATOM   4517 H HB2  . LEU   B 1 43  ? 49.259 -14.630 7.698   1.00 15.18 ?  43  LEU   B HB2  1 
ATOM   4518 H HB3  . LEU   B 1 43  ? 49.391 -15.246 6.247   1.00 15.18 ?  43  LEU   B HB3  1 
ATOM   4519 H HG   . LEU   B 1 43  ? 46.949 -14.539 7.463   1.00 15.44 ?  43  LEU   B HG   1 
ATOM   4520 H HD11 . LEU   B 1 43  ? 46.826 -12.846 5.866   1.00 16.97 ?  43  LEU   B HD11 1 
ATOM   4521 H HD12 . LEU   B 1 43  ? 48.112 -12.662 6.782   1.00 16.97 ?  43  LEU   B HD12 1 
ATOM   4522 H HD13 . LEU   B 1 43  ? 48.258 -13.266 5.319   1.00 16.97 ?  43  LEU   B HD13 1 
ATOM   4523 H HD21 . LEU   B 1 43  ? 45.933 -15.050 5.386   1.00 15.92 ?  43  LEU   B HD21 1 
ATOM   4524 H HD22 . LEU   B 1 43  ? 47.309 -15.684 4.907   1.00 15.92 ?  43  LEU   B HD22 1 
ATOM   4525 H HD23 . LEU   B 1 43  ? 46.506 -16.343 6.110   1.00 15.92 ?  43  LEU   B HD23 1 
ATOM   4526 N N    . LYS   B 1 44  ? 50.364 -18.272 8.613   1.00 12.64 ?  44  LYS   B N    1 
ATOM   4527 C CA   . LYS   B 1 44  ? 51.631 -18.950 8.847   1.00 13.16 ?  44  LYS   B CA   1 
ATOM   4528 C C    . LYS   B 1 44  ? 51.746 -20.064 7.815   1.00 13.18 ?  44  LYS   B C    1 
ATOM   4529 O O    . LYS   B 1 44  ? 51.050 -21.084 7.902   1.00 14.20 ?  44  LYS   B O    1 
ATOM   4530 C CB   . LYS   B 1 44  ? 51.689 -19.474 10.280  1.00 15.20 ?  44  LYS   B CB   1 
ATOM   4531 C CG   . LYS   B 1 44  ? 51.878 -18.371 11.311  1.00 18.23 ?  44  LYS   B CG   1 
ATOM   4532 C CD   . LYS   B 1 44  ? 53.076 -17.499 10.922  1.00 21.37 ?  44  LYS   B CD   1 
ATOM   4533 C CE   . LYS   B 1 44  ? 53.545 -16.598 12.034  1.00 24.12 ?  44  LYS   B CE   1 
ATOM   4534 N NZ   . LYS   B 1 44  ? 54.725 -15.787 11.646  1.00 25.45 ?  44  LYS   B NZ   1 
ATOM   4535 H H    . LYS   B 1 44  ? 49.695 -18.660 8.981   1.00 15.16 ?  44  LYS   B H    1 
ATOM   4536 H HA   . LYS   B 1 44  ? 52.364 -18.334 8.688   1.00 15.78 ?  44  LYS   B HA   1 
ATOM   4537 H HB2  . LYS   B 1 44  ? 50.852 -19.928 10.483  1.00 18.22 ?  44  LYS   B HB2  1 
ATOM   4538 H HB3  . LYS   B 1 44  ? 52.428 -20.092 10.364  1.00 18.22 ?  44  LYS   B HB3  1 
ATOM   4539 H HG2  . LYS   B 1 44  ? 51.085 -17.818 11.346  1.00 21.86 ?  44  LYS   B HG2  1 
ATOM   4540 H HG3  . LYS   B 1 44  ? 52.056 -18.771 12.180  1.00 21.86 ?  44  LYS   B HG3  1 
ATOM   4541 H HD2  . LYS   B 1 44  ? 53.809 -18.081 10.651  1.00 25.63 ?  44  LYS   B HD2  1 
ATOM   4542 H HD3  . LYS   B 1 44  ? 52.815 -16.932 10.178  1.00 25.63 ?  44  LYS   B HD3  1 
ATOM   4543 H HE2  . LYS   B 1 44  ? 52.832 -15.985 12.242  1.00 28.94 ?  44  LYS   B HE2  1 
ATOM   4544 H HE3  . LYS   B 1 44  ? 53.776 -17.138 12.805  1.00 28.94 ?  44  LYS   B HE3  1 
ATOM   4545 H HZ1  . LYS   B 1 44  ? 54.967 -15.264 12.324  1.00 30.53 ?  44  LYS   B HZ1  1 
ATOM   4546 H HZ2  . LYS   B 1 44  ? 55.405 -16.315 11.428  1.00 30.53 ?  44  LYS   B HZ2  1 
ATOM   4547 H HZ3  . LYS   B 1 44  ? 54.523 -15.273 10.944  1.00 30.53 ?  44  LYS   B HZ3  1 
ATOM   4548 N N    . HIS   B 1 45  ? 52.594 -19.844 6.814   1.00 12.75 ?  45  HIS   B N    1 
ATOM   4549 C CA   . HIS   B 1 45  ? 52.612 -20.678 5.613   1.00 12.98 ?  45  HIS   B CA   1 
ATOM   4550 C C    . HIS   B 1 45  ? 53.632 -21.801 5.770   1.00 14.90 ?  45  HIS   B C    1 
ATOM   4551 O O    . HIS   B 1 45  ? 54.690 -21.816 5.149   1.00 17.31 ?  45  HIS   B O    1 
ATOM   4552 C CB   . HIS   B 1 45  ? 52.922 -19.827 4.396   1.00 12.88 ?  45  HIS   B CB   1 
ATOM   4553 C CG   . HIS   B 1 45  ? 52.052 -18.623 4.289   1.00 12.61 ?  45  HIS   B CG   1 
ATOM   4554 N ND1  . HIS   B 1 45  ? 50.674 -18.698 4.249   1.00 12.76 ?  45  HIS   B ND1  1 
ATOM   4555 C CD2  . HIS   B 1 45  ? 52.371 -17.310 4.234   1.00 13.48 ?  45  HIS   B CD2  1 
ATOM   4556 C CE1  . HIS   B 1 45  ? 50.188 -17.474 4.152   1.00 12.56 ?  45  HIS   B CE1  1 
ATOM   4557 N NE2  . HIS   B 1 45  ? 51.193 -16.614 4.139   1.00 13.09 ?  45  HIS   B NE2  1 
ATOM   4558 H H    . HIS   B 1 45  ? 53.170 -19.202 6.801   1.00 15.29 ?  45  HIS   B H    1 
ATOM   4559 H HA   . HIS   B 1 45  ? 51.733 -21.076 5.492   1.00 15.56 ?  45  HIS   B HA   1 
ATOM   4560 H HB2  . HIS   B 1 45  ? 53.840 -19.531 4.442   1.00 15.45 ?  45  HIS   B HB2  1 
ATOM   4561 H HB3  . HIS   B 1 45  ? 52.787 -20.367 3.596   1.00 15.45 ?  45  HIS   B HB3  1 
ATOM   4562 H HD2  . HIS   B 1 45  ? 53.226 -16.946 4.250   1.00 16.16 ?  45  HIS   B HD2  1 
ATOM   4563 H HE1  . HIS   B 1 45  ? 49.286 -17.251 4.090   1.00 15.07 ?  45  HIS   B HE1  1 
ATOM   4564 H HE2  . HIS   B 1 45  ? 51.118 -15.756 4.092   1.00 15.70 ?  45  HIS   B HE2  1 
ATOM   4565 N N    A GLY   B 1 46  ? 53.276 -22.769 6.609   0.60 15.83 ?  46  GLY   B N    1 
ATOM   4566 N N    B GLY   B 1 46  ? 53.282 -22.758 6.620   0.40 15.82 ?  46  GLY   B N    1 
ATOM   4567 C CA   A GLY   B 1 46  ? 54.205 -23.819 6.985   0.60 17.45 ?  46  GLY   B CA   1 
ATOM   4568 C CA   B GLY   B 1 46  ? 54.206 -23.819 6.961   0.40 17.12 ?  46  GLY   B CA   1 
ATOM   4569 C C    A GLY   B 1 46  ? 54.255 -25.052 6.102   0.60 19.17 ?  46  GLY   B C    1 
ATOM   4570 C C    B GLY   B 1 46  ? 54.240 -24.972 5.978   0.40 18.57 ?  46  GLY   B C    1 
ATOM   4571 O O    A GLY   B 1 46  ? 55.341 -25.508 5.731   0.60 21.85 ?  46  GLY   B O    1 
ATOM   4572 O O    B GLY   B 1 46  ? 55.283 -25.266 5.385   0.40 19.99 ?  46  GLY   B O    1 
ATOM   4573 H H    A GLY   B 1 46  ? 52.501 -22.826 6.986   0.60 18.98 ?  46  GLY   B H    1 
ATOM   4574 H H    B GLY   B 1 46  ? 52.514 -22.808 7.014   0.40 18.97 ?  46  GLY   B H    1 
ATOM   4575 H HA2  A GLY   B 1 46  ? 55.097 -23.440 7.017   0.60 20.93 ?  46  GLY   B HA2  1 
ATOM   4576 H HA2  B GLY   B 1 46  ? 55.098 -23.446 7.019   0.40 20.53 ?  46  GLY   B HA2  1 
ATOM   4577 H HA3  A GLY   B 1 46  ? 53.980 -24.124 7.875   0.60 20.93 ?  46  GLY   B HA3  1 
ATOM   4578 H HA3  B GLY   B 1 46  ? 53.969 -24.169 7.834   0.40 20.53 ?  46  GLY   B HA3  1 
ATOM   4579 N N    . GLY   B 1 47  ? 53.100 -25.633 5.783   1.00 18.77 ?  47  GLY   B N    1 
ATOM   4580 C CA   . GLY   B 1 47  ? 53.049 -26.899 5.082   1.00 16.52 ?  47  GLY   B CA   1 
ATOM   4581 C C    . GLY   B 1 47  ? 52.127 -26.877 3.879   1.00 14.38 ?  47  GLY   B C    1 
ATOM   4582 O O    . GLY   B 1 47  ? 51.467 -25.877 3.590   1.00 14.30 ?  47  GLY   B O    1 
ATOM   4583 H H    A GLY   B 1 47  ? 52.327 -25.316 5.986   0.60 22.52 ?  47  GLY   B H    1 
ATOM   4584 H H    B GLY   B 1 47  ? 52.332 -25.355 6.052   0.40 22.52 ?  47  GLY   B H    1 
ATOM   4585 H HA2  . GLY   B 1 47  ? 53.938 -27.143 4.775   1.00 19.81 ?  47  GLY   B HA2  1 
ATOM   4586 H HA3  . GLY   B 1 47  ? 52.743 -27.588 5.693   1.00 19.81 ?  47  GLY   B HA3  1 
ATOM   4587 N N    . GLY   B 1 48  ? 52.082 -28.021 3.192   1.00 13.80 ?  48  GLY   B N    1 
ATOM   4588 C CA   . GLY   B 1 48  ? 51.160 -28.181 2.085   1.00 13.47 ?  48  GLY   B CA   1 
ATOM   4589 C C    . GLY   B 1 48  ? 51.293 -27.070 1.069   1.00 12.93 ?  48  GLY   B C    1 
ATOM   4590 O O    . GLY   B 1 48  ? 52.394 -26.607 0.750   1.00 13.22 ?  48  GLY   B O    1 
ATOM   4591 H H    . GLY   B 1 48  ? 52.582 -28.701 3.344   1.00 16.55 ?  48  GLY   B H    1 
ATOM   4592 H HA2  . GLY   B 1 48  ? 51.330 -29.028 1.644   1.00 16.16 ?  48  GLY   B HA2  1 
ATOM   4593 H HA3  . GLY   B 1 48  ? 50.251 -28.183 2.420   1.00 16.16 ?  48  GLY   B HA3  1 
ATOM   4594 N N    . VAL   B 1 49  ? 50.144 -26.636 0.544   1.00 12.60 ?  49  VAL   B N    1 
ATOM   4595 C CA   . VAL   B 1 49  ? 50.120 -25.611 -0.497  1.00 12.45 ?  49  VAL   B CA   1 
ATOM   4596 C C    . VAL   B 1 49  ? 50.779 -24.326 -0.010  1.00 11.92 ?  49  VAL   B C    1 
ATOM   4597 O O    . VAL   B 1 49  ? 51.568 -23.706 -0.730  1.00 12.54 ?  49  VAL   B O    1 
ATOM   4598 C CB   . VAL   B 1 49  ? 48.675 -25.359 -0.974  1.00 14.00 ?  49  VAL   B CB   1 
ATOM   4599 C CG1  . VAL   B 1 49  ? 48.594 -24.111 -1.842  1.00 14.02 ?  49  VAL   B CG1  1 
ATOM   4600 C CG2  . VAL   B 1 49  ? 48.142 -26.571 -1.730  1.00 15.70 ?  49  VAL   B CG2  1 
ATOM   4601 H H    . VAL   B 1 49  ? 49.363 -26.918 0.775   1.00 15.11 ?  49  VAL   B H    1 
ATOM   4602 H HA   . VAL   B 1 49  ? 50.626 -25.929 -1.260  1.00 14.93 ?  49  VAL   B HA   1 
ATOM   4603 H HB   . VAL   B 1 49  ? 48.109 -25.223 -0.200  1.00 16.79 ?  49  VAL   B HB   1 
ATOM   4604 H HG11 . VAL   B 1 49  ? 47.757 -24.128 -2.336  1.00 16.82 ?  49  VAL   B HG11 1 
ATOM   4605 H HG12 . VAL   B 1 49  ? 48.620 -23.326 -1.272  1.00 16.82 ?  49  VAL   B HG12 1 
ATOM   4606 H HG13 . VAL   B 1 49  ? 49.340 -24.104 -2.458  1.00 16.82 ?  49  VAL   B HG13 1 
ATOM   4607 H HG21 . VAL   B 1 49  ? 47.234 -26.392 -2.013  1.00 18.83 ?  49  VAL   B HG21 1 
ATOM   4608 H HG22 . VAL   B 1 49  ? 48.706 -26.728 -2.507  1.00 18.83 ?  49  VAL   B HG22 1 
ATOM   4609 H HG23 . VAL   B 1 49  ? 48.165 -27.343 -1.146  1.00 18.83 ?  49  VAL   B HG23 1 
ATOM   4610 N N    . ALA   B 1 50  ? 50.432 -23.880 1.200   1.00 11.95 ?  50  ALA   B N    1 
ATOM   4611 C CA   . ALA   B 1 50  ? 50.950 -22.599 1.676   1.00 11.73 ?  50  ALA   B CA   1 
ATOM   4612 C C    . ALA   B 1 50  ? 52.469 -22.623 1.787   1.00 11.91 ?  50  ALA   B C    1 
ATOM   4613 O O    . ALA   B 1 50  ? 53.149 -21.654 1.420   1.00 12.02 ?  50  ALA   B O    1 
ATOM   4614 C CB   . ALA   B 1 50  ? 50.311 -22.243 3.016   1.00 12.17 ?  50  ALA   B CB   1 
ATOM   4615 H H    . ALA   B 1 50  ? 49.916 -24.291 1.751   1.00 14.33 ?  50  ALA   B H    1 
ATOM   4616 H HA   . ALA   B 1 50  ? 50.719 -21.909 1.044   1.00 14.06 ?  50  ALA   B HA   1 
ATOM   4617 H HB1  . ALA   B 1 50  ? 50.662 -21.389 3.321   1.00 14.60 ?  50  ALA   B HB1  1 
ATOM   4618 H HB2  . ALA   B 1 50  ? 49.348 -22.177 2.901   1.00 14.60 ?  50  ALA   B HB2  1 
ATOM   4619 H HB3  . ALA   B 1 50  ? 50.518 -22.934 3.666   1.00 14.60 ?  50  ALA   B HB3  1 
ATOM   4620 N N    . GLY   B 1 51  ? 53.021 -23.717 2.308   1.00 12.30 ?  51  GLY   B N    1 
ATOM   4621 C CA   . GLY   B 1 51  ? 54.466 -23.822 2.377   1.00 12.97 ?  51  GLY   B CA   1 
ATOM   4622 C C    . GLY   B 1 51  ? 55.114 -23.769 1.006   1.00 13.08 ?  51  GLY   B C    1 
ATOM   4623 O O    . GLY   B 1 51  ? 56.156 -23.130 0.822   1.00 13.94 ?  51  GLY   B O    1 
ATOM   4624 H H    . GLY   B 1 51  ? 52.593 -24.401 2.619   1.00 14.75 ?  51  GLY   B H    1 
ATOM   4625 H HA2  . GLY   B 1 51  ? 54.819 -23.094 2.914   1.00 15.55 ?  51  GLY   B HA2  1 
ATOM   4626 H HA3  . GLY   B 1 51  ? 54.714 -24.661 2.804   1.00 15.55 ?  51  GLY   B HA3  1 
ATOM   4627 N N    . ALA   B 1 52  ? 54.509 -24.433 0.024   1.00 12.79 ?  52  ALA   B N    1 
ATOM   4628 C CA   . ALA   B 1 52  ? 55.072 -24.440 -1.320  1.00 13.33 ?  52  ALA   B CA   1 
ATOM   4629 C C    . ALA   B 1 52  ? 54.993 -23.061 -1.970  1.00 12.45 ?  52  ALA   B C    1 
ATOM   4630 O O    . ALA   B 1 52  ? 55.957 -22.613 -2.608  1.00 13.25 ?  52  ALA   B O    1 
ATOM   4631 C CB   . ALA   B 1 52  ? 54.371 -25.483 -2.183  1.00 14.32 ?  52  ALA   B CB   1 
ATOM   4632 H H    . ALA   B 1 52  ? 53.779 -24.881 0.112   1.00 15.33 ?  52  ALA   B H    1 
ATOM   4633 H HA   . ALA   B 1 52  ? 56.008 -24.684 -1.259  1.00 15.99 ?  52  ALA   B HA   1 
ATOM   4634 H HB1  . ALA   B 1 52  ? 54.766 -25.468 -3.071  1.00 17.17 ?  52  ALA   B HB1  1 
ATOM   4635 H HB2  . ALA   B 1 52  ? 54.497 -26.358 -1.782  1.00 17.17 ?  52  ALA   B HB2  1 
ATOM   4636 H HB3  . ALA   B 1 52  ? 53.430 -25.271 -2.234  1.00 17.17 ?  52  ALA   B HB3  1 
ATOM   4637 N N    . LEU   B 1 53  ? 53.843 -22.389 -1.860  1.00 12.03 ?  53  LEU   B N    1 
ATOM   4638 C CA   . LEU   B 1 53  ? 53.730 -21.044 -2.421  1.00 12.17 ?  53  LEU   B CA   1 
ATOM   4639 C C    . LEU   B 1 53  ? 54.736 -20.104 -1.770  1.00 12.15 ?  53  LEU   B C    1 
ATOM   4640 O O    . LEU   B 1 53  ? 55.441 -19.352 -2.457  1.00 12.85 ?  53  LEU   B O    1 
ATOM   4641 C CB   . LEU   B 1 53  ? 52.302 -20.504 -2.260  1.00 12.89 ?  53  LEU   B CB   1 
ATOM   4642 C CG   . LEU   B 1 53  ? 51.172 -21.233 -2.994  1.00 13.00 ?  53  LEU   B CG   1 
ATOM   4643 C CD1  . LEU   B 1 53  ? 49.836 -20.607 -2.667  1.00 14.47 ?  53  LEU   B CD1  1 
ATOM   4644 C CD2  . LEU   B 1 53  ? 51.400 -21.244 -4.500  1.00 14.98 ?  53  LEU   B CD2  1 
ATOM   4645 H H    . LEU   B 1 53  ? 53.135 -22.678 -1.467  1.00 14.42 ?  53  LEU   B H    1 
ATOM   4646 H HA   . LEU   B 1 53  ? 53.931 -21.086 -3.372  1.00 14.59 ?  53  LEU   B HA   1 
ATOM   4647 H HB2  . LEU   B 1 53  ? 52.084 -20.524 -1.319  1.00 15.46 ?  53  LEU   B HB2  1 
ATOM   4648 H HB3  . LEU   B 1 53  ? 52.294 -19.590 -2.575  1.00 15.46 ?  53  LEU   B HB3  1 
ATOM   4649 H HG   . LEU   B 1 53  ? 51.142 -22.154 -2.691  1.00 15.59 ?  53  LEU   B HG   1 
ATOM   4650 H HD11 . LEU   B 1 53  ? 49.135 -21.086 -3.140  1.00 17.35 ?  53  LEU   B HD11 1 
ATOM   4651 H HD12 . LEU   B 1 53  ? 49.683 -20.666 -1.709  1.00 17.35 ?  53  LEU   B HD12 1 
ATOM   4652 H HD13 . LEU   B 1 53  ? 49.844 -19.678 -2.943  1.00 17.35 ?  53  LEU   B HD13 1 
ATOM   4653 H HD21 . LEU   B 1 53  ? 50.658 -21.698 -4.931  1.00 17.96 ?  53  LEU   B HD21 1 
ATOM   4654 H HD22 . LEU   B 1 53  ? 51.459 -20.332 -4.819  1.00 17.96 ?  53  LEU   B HD22 1 
ATOM   4655 H HD23 . LEU   B 1 53  ? 52.227 -21.717 -4.691  1.00 17.96 ?  53  LEU   B HD23 1 
ATOM   4656 N N    . ASN   B 1 54  ? 54.827 -20.134 -0.441  1.00 12.03 ?  54  ASN   B N    1 
ATOM   4657 C CA   . ASN   B 1 54  ? 55.740 -19.218 0.228   1.00 12.92 ?  54  ASN   B CA   1 
ATOM   4658 C C    . ASN   B 1 54  ? 57.182 -19.494 -0.173  1.00 12.97 ?  54  ASN   B C    1 
ATOM   4659 O O    . ASN   B 1 54  ? 57.958 -18.558 -0.409  1.00 13.45 ?  54  ASN   B O    1 
ATOM   4660 C CB   . ASN   B 1 54  ? 55.580 -19.286 1.739   1.00 13.49 ?  54  ASN   B CB   1 
ATOM   4661 C CG   . ASN   B 1 54  ? 56.559 -18.367 2.445   1.00 13.43 ?  54  ASN   B CG   1 
ATOM   4662 O OD1  . ASN   B 1 54  ? 56.572 -17.158 2.198   1.00 13.95 ?  54  ASN   B OD1  1 
ATOM   4663 N ND2  . ASN   B 1 54  ? 57.401 -18.934 3.298   1.00 15.15 ?  54  ASN   B ND2  1 
ATOM   4664 H H    . ASN   B 1 54  ? 54.384 -20.659 0.076   1.00 14.43 ?  54  ASN   B H    1 
ATOM   4665 H HA   . ASN   B 1 54  ? 55.527 -18.314 -0.052  1.00 15.49 ?  54  ASN   B HA   1 
ATOM   4666 H HB2  . ASN   B 1 54  ? 54.677 -19.011 1.975   1.00 16.18 ?  54  ASN   B HB2  1 
ATOM   4667 H HB3  . ASN   B 1 54  ? 55.743 -20.191 2.039   1.00 16.18 ?  54  ASN   B HB3  1 
ATOM   4668 H HD21 . ASN   B 1 54  ? 57.978 -18.450 3.715   1.00 18.17 ?  54  ASN   B HD21 1 
ATOM   4669 H HD22 . ASN   B 1 54  ? 57.372 -19.781 3.434   1.00 18.17 ?  54  ASN   B HD22 1 
ATOM   4670 N N    . LYS   B 1 55  ? 57.567 -20.771 -0.241  1.00 13.50 ?  55  LYS   B N    1 
ATOM   4671 C CA   . LYS   B 1 55  ? 58.922 -21.110 -0.659  1.00 14.64 ?  55  LYS   B CA   1 
ATOM   4672 C C    . LYS   B 1 55  ? 59.221 -20.570 -2.051  1.00 14.25 ?  55  LYS   B C    1 
ATOM   4673 O O    . LYS   B 1 55  ? 60.317 -20.055 -2.300  1.00 14.93 ?  55  LYS   B O    1 
ATOM   4674 C CB   . LYS   B 1 55  ? 59.122 -22.625 -0.605  1.00 16.28 ?  55  LYS   B CB   1 
ATOM   4675 C CG   . LYS   B 1 55  ? 60.505 -23.084 -1.015  1.00 20.31 ?  55  LYS   B CG   1 
ATOM   4676 C CD   . LYS   B 1 55  ? 60.681 -24.583 -0.829  1.00 23.63 ?  55  LYS   B CD   1 
ATOM   4677 C CE   . LYS   B 1 55  ? 60.807 -24.964 0.646   1.00 27.02 ?  55  LYS   B CE   1 
ATOM   4678 N NZ   . LYS   B 1 55  ? 61.097 -26.409 0.827   1.00 28.70 ?  55  LYS   B NZ   1 
ATOM   4679 H H    . LYS   B 1 55  ? 57.064 -21.445 -0.057  1.00 16.19 ?  55  LYS   B H    1 
ATOM   4680 H HA   . LYS   B 1 55  ? 59.550 -20.705 -0.043  1.00 17.55 ?  55  LYS   B HA   1 
ATOM   4681 H HB2  . LYS   B 1 55  ? 58.968 -22.924 0.305   1.00 19.53 ?  55  LYS   B HB2  1 
ATOM   4682 H HB3  . LYS   B 1 55  ? 58.484 -23.047 -1.200  1.00 19.53 ?  55  LYS   B HB3  1 
ATOM   4683 H HG2  . LYS   B 1 55  ? 60.649 -22.877 -1.951  1.00 24.35 ?  55  LYS   B HG2  1 
ATOM   4684 H HG3  . LYS   B 1 55  ? 61.168 -22.630 -0.467  1.00 24.35 ?  55  LYS   B HG3  1 
ATOM   4685 H HD2  . LYS   B 1 55  ? 59.910 -25.046 -1.193  1.00 28.35 ?  55  LYS   B HD2  1 
ATOM   4686 H HD3  . LYS   B 1 55  ? 61.489 -24.873 -1.283  1.00 28.35 ?  55  LYS   B HD3  1 
ATOM   4687 H HE2  . LYS   B 1 55  ? 61.532 -24.451 1.042   1.00 32.42 ?  55  LYS   B HE2  1 
ATOM   4688 H HE3  . LYS   B 1 55  ? 59.972 -24.757 1.098   1.00 32.42 ?  55  LYS   B HE3  1 
ATOM   4689 H HZ1  . LYS   B 1 55  ? 61.133 -26.602 1.694   1.00 34.43 ?  55  LYS   B HZ1  1 
ATOM   4690 H HZ2  . LYS   B 1 55  ? 60.452 -26.892 0.449   1.00 34.43 ?  55  LYS   B HZ2  1 
ATOM   4691 H HZ3  . LYS   B 1 55  ? 61.873 -26.611 0.448   1.00 34.43 ?  55  LYS   B HZ3  1 
ATOM   4692 N N    . ALA   B 1 56  ? 58.258 -20.664 -2.972  1.00 13.68 ?  56  ALA   B N    1 
ATOM   4693 C CA   . ALA   B 1 56  ? 58.479 -20.155 -4.320  1.00 14.41 ?  56  ALA   B CA   1 
ATOM   4694 C C    . ALA   B 1 56  ? 58.744 -18.655 -4.314  1.00 14.27 ?  56  ALA   B C    1 
ATOM   4695 O O    . ALA   B 1 56  ? 59.471 -18.151 -5.182  1.00 15.68 ?  56  ALA   B O    1 
ATOM   4696 C CB   . ALA   B 1 56  ? 57.288 -20.496 -5.216  1.00 15.35 ?  56  ALA   B CB   1 
ATOM   4697 H H    . ALA   B 1 56  ? 57.476 -21.000 -2.839  1.00 16.40 ?  56  ALA   B H    1 
ATOM   4698 H HA   . ALA   B 1 56  ? 59.262 -20.582 -4.688  1.00 17.28 ?  56  ALA   B HA   1 
ATOM   4699 H HB1  . ALA   B 1 56  ? 57.461 -20.153 -6.111  1.00 18.40 ?  56  ALA   B HB1  1 
ATOM   4700 H HB2  . ALA   B 1 56  ? 57.190 -21.460 -5.250  1.00 18.40 ?  56  ALA   B HB2  1 
ATOM   4701 H HB3  . ALA   B 1 56  ? 56.489 -20.090 -4.856  1.00 18.40 ?  56  ALA   B HB3  1 
ATOM   4702 N N    . THR   B 1 57  ? 58.173 -17.926 -3.350  1.00 14.01 ?  57  THR   B N    1 
ATOM   4703 C CA   . THR   B 1 57  ? 58.409 -16.490 -3.225  1.00 14.26 ?  57  THR   B CA   1 
ATOM   4704 C C    . THR   B 1 57  ? 59.661 -16.161 -2.416  1.00 15.07 ?  57  THR   B C    1 
ATOM   4705 O O    . THR   B 1 57  ? 59.895 -14.984 -2.109  1.00 15.60 ?  57  THR   B O    1 
ATOM   4706 C CB   . THR   B 1 57  ? 57.207 -15.763 -2.591  1.00 13.62 ?  57  THR   B CB   1 
ATOM   4707 O OG1  . THR   B 1 57  ? 57.189 -15.972 -1.171  1.00 13.91 ?  57  THR   B OG1  1 
ATOM   4708 C CG2  . THR   B 1 57  ? 55.884 -16.197 -3.218  1.00 13.78 ?  57  THR   B CG2  1 
ATOM   4709 H H    . THR   B 1 57  ? 57.633 -18.240 -2.756  1.00 16.80 ?  57  THR   B H    1 
ATOM   4710 H HA   . THR   B 1 57  ? 58.527 -16.122 -4.114  1.00 17.10 ?  57  THR   B HA   1 
ATOM   4711 H HB   . THR   B 1 57  ? 57.302 -14.812 -2.761  1.00 16.34 ?  57  THR   B HB   1 
ATOM   4712 H HG1  . THR   B 1 57  ? 57.126 -16.788 -1.000  1.00 16.68 ?  57  THR   B HG1  1 
ATOM   4713 H HG21 . THR   B 1 57  ? 55.159 -15.648 -2.887  1.00 16.52 ?  57  THR   B HG21 1 
ATOM   4714 H HG22 . THR   B 1 57  ? 55.929 -16.115 -4.184  1.00 16.52 ?  57  THR   B HG22 1 
ATOM   4715 H HG23 . THR   B 1 57  ? 55.700 -17.125 -2.995  1.00 16.52 ?  57  THR   B HG23 1 
ATOM   4716 N N    . ASN   B 1 58  ? 60.465 -17.161 -2.061  1.00 15.94 ?  58  ASN   B N    1 
ATOM   4717 C CA   . ASN   B 1 58  ? 61.662 -16.936 -1.255  1.00 19.02 ?  58  ASN   B CA   1 
ATOM   4718 C C    . ASN   B 1 58  ? 61.321 -16.220 0.052   1.00 16.51 ?  58  ASN   B C    1 
ATOM   4719 O O    . ASN   B 1 58  ? 62.058 -15.345 0.516   1.00 17.28 ?  58  ASN   B O    1 
ATOM   4720 C CB   . ASN   B 1 58  ? 62.743 -16.185 -2.039  1.00 27.84 ?  58  ASN   B CB   1 
ATOM   4721 C CG   . ASN   B 1 58  ? 64.115 -16.310 -1.404  1.00 36.73 ?  58  ASN   B CG   1 
ATOM   4722 O OD1  . ASN   B 1 58  ? 64.413 -17.298 -0.732  1.00 39.93 ?  58  ASN   B OD1  1 
ATOM   4723 N ND2  . ASN   B 1 58  ? 64.959 -15.306 -1.614  1.00 42.27 ?  58  ASN   B ND2  1 
ATOM   4724 H H    . ASN   B 1 58  ? 60.339 -17.989 -2.274  1.00 19.11 ?  58  ASN   B H    1 
ATOM   4725 H HA   . ASN   B 1 58  ? 62.033 -17.802 -1.021  1.00 22.81 ?  58  ASN   B HA   1 
ATOM   4726 H HB2  . ASN   B 1 58  ? 62.794 -16.546 -2.940  1.00 33.40 ?  58  ASN   B HB2  1 
ATOM   4727 H HB3  . ASN   B 1 58  ? 62.517 -15.243 -2.073  1.00 33.40 ?  58  ASN   B HB3  1 
ATOM   4728 H HD21 . ASN   B 1 58  ? 65.750 -15.330 -1.277  1.00 50.72 ?  58  ASN   B HD21 1 
ATOM   4729 H HD22 . ASN   B 1 58  ? 64.714 -14.631 -2.088  1.00 50.72 ?  58  ASN   B HD22 1 
ATOM   4730 N N    . ASN   B 1 59  ? 60.196 -16.606 0.656   1.00 15.27 ?  59  ASN   B N    1 
ATOM   4731 C CA   . ASN   B 1 59  ? 59.720 -16.143 1.961   1.00 15.30 ?  59  ASN   B CA   1 
ATOM   4732 C C    . ASN   B 1 59  ? 59.128 -14.732 1.912   1.00 14.64 ?  59  ASN   B C    1 
ATOM   4733 O O    . ASN   B 1 59  ? 58.693 -14.229 2.955   1.00 14.93 ?  59  ASN   B O    1 
ATOM   4734 C CB   . ASN   B 1 59  ? 60.792 -16.221 3.064   1.00 16.60 ?  59  ASN   B CB   1 
ATOM   4735 C CG   . ASN   B 1 59  ? 60.199 -16.385 4.446   1.00 17.82 ?  59  ASN   B CG   1 
ATOM   4736 O OD1  . ASN   B 1 59  ? 59.368 -17.268 4.679   1.00 17.89 ?  59  ASN   B OD1  1 
ATOM   4737 N ND2  . ASN   B 1 59  ? 60.616 -15.530 5.375   1.00 18.60 ?  59  ASN   B ND2  1 
ATOM   4738 H H    . ASN   B 1 59  ? 59.653 -17.179 0.305   1.00 18.31 ?  59  ASN   B H    1 
ATOM   4739 H HA   . ASN   B 1 59  ? 59.007 -16.738 2.235   1.00 18.35 ?  59  ASN   B HA   1 
ATOM   4740 H HB2  . ASN   B 1 59  ? 61.365 -16.987 2.901   1.00 19.91 ?  59  ASN   B HB2  1 
ATOM   4741 H HB3  . ASN   B 1 59  ? 61.313 -15.407 3.063   1.00 19.91 ?  59  ASN   B HB3  1 
ATOM   4742 H HD21 . ASN   B 1 59  ? 60.310 -15.580 6.179   1.00 22.31 ?  59  ASN   B HD21 1 
ATOM   4743 H HD22 . ASN   B 1 59  ? 61.196 -14.928 5.174   1.00 22.31 ?  59  ASN   B HD22 1 
ATOM   4744 N N    . ALA   B 1 60  ? 59.067 -14.083 0.745   1.00 14.51 ?  60  ALA   B N    1 
ATOM   4745 C CA   . ALA   B 1 60  ? 58.463 -12.753 0.677   1.00 14.35 ?  60  ALA   B CA   1 
ATOM   4746 C C    . ALA   B 1 60  ? 56.993 -12.786 1.079   1.00 13.62 ?  60  ALA   B C    1 
ATOM   4747 O O    . ALA   B 1 60  ? 56.485 -11.838 1.694   1.00 14.07 ?  60  ALA   B O    1 
ATOM   4748 C CB   . ALA   B 1 60  ? 58.618 -12.172 -0.727  1.00 15.44 ?  60  ALA   B CB   1 
ATOM   4749 H H    . ALA   B 1 60  ? 59.364 -14.387 0.000   1.00 17.40 ?  60  ALA   B H    1 
ATOM   4750 H HA   . ALA   B 1 60  ? 58.926 -12.169 1.296   1.00 17.21 ?  60  ALA   B HA   1 
ATOM   4751 H HB1  . ALA   B 1 60  ? 58.214 -11.292 -0.750  1.00 18.52 ?  60  ALA   B HB1  1 
ATOM   4752 H HB2  . ALA   B 1 60  ? 59.564 -12.108 -0.938  1.00 18.52 ?  60  ALA   B HB2  1 
ATOM   4753 H HB3  . ALA   B 1 60  ? 58.178 -12.758 -1.362  1.00 18.52 ?  60  ALA   B HB3  1 
ATOM   4754 N N    . MET   B 1 61  ? 56.285 -13.862 0.724   1.00 13.05 ?  61  MET   B N    1 
ATOM   4755 C CA   . MET   B 1 61  ? 54.889 -13.989 1.119   1.00 12.77 ?  61  MET   B CA   1 
ATOM   4756 C C    . MET   B 1 61  ? 54.754 -13.998 2.641   1.00 13.13 ?  61  MET   B C    1 
ATOM   4757 O O    . MET   B 1 61  ? 53.857 -13.349 3.197   1.00 12.77 ?  61  MET   B O    1 
ATOM   4758 C CB   . MET   B 1 61  ? 54.308 -15.258 0.486   1.00 12.69 ?  61  MET   B CB   1 
ATOM   4759 C CG   . MET   B 1 61  ? 52.867 -15.562 0.902   1.00 12.48 ?  61  MET   B CG   1 
ATOM   4760 S SD   . MET   B 1 61  ? 52.230 -17.066 0.139   1.00 13.13 ?  61  MET   B SD   1 
ATOM   4761 C CE   . MET   B 1 61  ? 51.976 -16.478 -1.529  1.00 14.25 ?  61  MET   B CE   1 
ATOM   4762 H H    . MET   B 1 61  ? 56.591 -14.523 0.258   1.00 15.65 ?  61  MET   B H    1 
ATOM   4763 H HA   . MET   B 1 61  ? 54.396 -13.236 0.760   1.00 15.31 ?  61  MET   B HA   1 
ATOM   4764 H HB2  . MET   B 1 61  ? 54.318 -15.160 -0.483  1.00 15.22 ?  61  MET   B HB2  1 
ATOM   4765 H HB3  . MET   B 1 61  ? 54.856 -16.016 0.740   1.00 15.22 ?  61  MET   B HB3  1 
ATOM   4766 H HG2  . MET   B 1 61  ? 52.834 -15.680 1.866   1.00 14.96 ?  61  MET   B HG2  1 
ATOM   4767 H HG3  . MET   B 1 61  ? 52.299 -14.822 0.639   1.00 14.96 ?  61  MET   B HG3  1 
ATOM   4768 H HE1  . MET   B 1 61  ? 51.589 -17.190 -2.060  1.00 17.08 ?  61  MET   B HE1  1 
ATOM   4769 H HE2  . MET   B 1 61  ? 51.376 -15.715 -1.510  1.00 17.08 ?  61  MET   B HE2  1 
ATOM   4770 H HE3  . MET   B 1 61  ? 52.832 -16.213 -1.905  1.00 17.08 ?  61  MET   B HE3  1 
ATOM   4771 N N    . GLN   B 1 62  ? 55.638 -14.715 3.339   1.00 12.64 ?  62  GLN   B N    1 
ATOM   4772 C CA   . GLN   B 1 62  ? 55.533 -14.776 4.793   1.00 13.22 ?  62  GLN   B CA   1 
ATOM   4773 C C    . GLN   B 1 62  ? 55.819 -13.421 5.431   1.00 13.54 ?  62  GLN   B C    1 
ATOM   4774 O O    . GLN   B 1 62  ? 55.142 -13.024 6.386   1.00 13.93 ?  62  GLN   B O    1 
ATOM   4775 C CB   . GLN   B 1 62  ? 56.481 -15.833 5.355   1.00 13.36 ?  62  GLN   B CB   1 
ATOM   4776 C CG   . GLN   B 1 62  ? 56.264 -16.095 6.837   1.00 13.70 ?  62  GLN   B CG   1 
ATOM   4777 C CD   . GLN   B 1 62  ? 54.893 -16.697 7.086   1.00 13.25 ?  62  GLN   B CD   1 
ATOM   4778 O OE1  . GLN   B 1 62  ? 54.640 -17.850 6.730   1.00 13.62 ?  62  GLN   B OE1  1 
ATOM   4779 N NE2  . GLN   B 1 62  ? 53.982 -15.906 7.647   1.00 13.90 ?  62  GLN   B NE2  1 
ATOM   4780 H H    . GLN   B 1 62  ? 56.289 -15.166 2.998   1.00 15.16 ?  62  GLN   B H    1 
ATOM   4781 H HA   . GLN   B 1 62  ? 54.625 -15.030 5.024   1.00 15.85 ?  62  GLN   B HA   1 
ATOM   4782 H HB2  . GLN   B 1 62  ? 56.347 -16.667 4.880   1.00 16.02 ?  62  GLN   B HB2  1 
ATOM   4783 H HB3  . GLN   B 1 62  ? 57.397 -15.529 5.236   1.00 16.02 ?  62  GLN   B HB3  1 
ATOM   4784 H HG2  . GLN   B 1 62  ? 56.935 -16.722 7.150   1.00 16.43 ?  62  GLN   B HG2  1 
ATOM   4785 H HG3  . GLN   B 1 62  ? 56.328 -15.261 7.326   1.00 16.43 ?  62  GLN   B HG3  1 
ATOM   4786 H HE21 . GLN   B 1 62  ? 54.194 -15.101 7.869   1.00 16.67 ?  62  GLN   B HE21 1 
ATOM   4787 H HE22 . GLN   B 1 62  ? 53.195 -16.203 7.801   1.00 16.67 ?  62  GLN   B HE22 1 
ATOM   4788 N N    . VAL   B 1 63  ? 56.828 -12.702 4.935   1.00 14.15 ?  63  VAL   B N    1 
ATOM   4789 C CA   . VAL   B 1 63  ? 57.131 -11.387 5.494   1.00 15.07 ?  63  VAL   B CA   1 
ATOM   4790 C C    . VAL   B 1 63  ? 55.939 -10.456 5.315   1.00 14.00 ?  63  VAL   B C    1 
ATOM   4791 O O    . VAL   B 1 63  ? 55.524 -9.753  6.247   1.00 14.94 ?  63  VAL   B O    1 
ATOM   4792 C CB   . VAL   B 1 63  ? 58.419 -10.822 4.872   1.00 16.46 ?  63  VAL   B CB   1 
ATOM   4793 C CG1  . VAL   B 1 63  ? 58.648 -9.384  5.329   1.00 17.20 ?  63  VAL   B CG1  1 
ATOM   4794 C CG2  . VAL   B 1 63  ? 59.604 -11.700 5.256   1.00 16.98 ?  63  VAL   B CG2  1 
ATOM   4795 H H    . VAL   B 1 63  ? 57.336 -12.949 4.283   1.00 16.97 ?  63  VAL   B H    1 
ATOM   4796 H HA   . VAL   B 1 63  ? 57.287 -11.489 6.443   1.00 18.07 ?  63  VAL   B HA   1 
ATOM   4797 H HB   . VAL   B 1 63  ? 58.344 -10.827 3.905   1.00 19.74 ?  63  VAL   B HB   1 
ATOM   4798 H HG11 . VAL   B 1 63  ? 59.563 -9.132  5.131   1.00 20.63 ?  63  VAL   B HG11 1 
ATOM   4799 H HG12 . VAL   B 1 63  ? 58.034 -8.800  4.860   1.00 20.63 ?  63  VAL   B HG12 1 
ATOM   4800 H HG13 . VAL   B 1 63  ? 58.493 -9.331  6.287   1.00 20.63 ?  63  VAL   B HG13 1 
ATOM   4801 H HG21 . VAL   B 1 63  ? 60.416 -11.320 4.883   1.00 20.37 ?  63  VAL   B HG21 1 
ATOM   4802 H HG22 . VAL   B 1 63  ? 59.673 -11.731 6.226   1.00 20.37 ?  63  VAL   B HG22 1 
ATOM   4803 H HG23 . VAL   B 1 63  ? 59.466 -12.593 4.908   1.00 20.37 ?  63  VAL   B HG23 1 
ATOM   4804 N N    . GLU   B 1 64  ? 55.365 -10.449 4.112   1.00 13.89 ?  64  GLU   B N    1 
ATOM   4805 C CA   . GLU   B 1 64  ? 54.199 -9.611  3.842   1.00 13.31 ?  64  GLU   B CA   1 
ATOM   4806 C C    . GLU   B 1 64  ? 53.022 -10.016 4.723   1.00 12.96 ?  64  GLU   B C    1 
ATOM   4807 O O    . GLU   B 1 64  ? 52.282 -9.159  5.232   1.00 13.59 ?  64  GLU   B O    1 
ATOM   4808 C CB   . GLU   B 1 64  ? 53.843 -9.748  2.362   1.00 13.68 ?  64  GLU   B CB   1 
ATOM   4809 C CG   . GLU   B 1 64  ? 52.580 -9.013  1.931   1.00 13.74 ?  64  GLU   B CG   1 
ATOM   4810 C CD   . GLU   B 1 64  ? 52.035 -9.511  0.599   1.00 14.57 ?  64  GLU   B CD   1 
ATOM   4811 O OE1  . GLU   B 1 64  ? 52.211 -10.718 0.279   1.00 15.42 ?  64  GLU   B OE1  1 
ATOM   4812 O OE2  . GLU   B 1 64  ? 51.414 -8.694  -0.122  1.00 15.21 -1 64  GLU   B OE2  1 
ATOM   4813 H H    . GLU   B 1 64  ? 55.630 -10.917 3.437   1.00 16.66 ?  64  GLU   B H    1 
ATOM   4814 H HA   . GLU   B 1 64  ? 54.417 -8.684  4.023   1.00 15.96 ?  64  GLU   B HA   1 
ATOM   4815 H HB2  . GLU   B 1 64  ? 54.574 -9.393  1.830   1.00 16.40 ?  64  GLU   B HB2  1 
ATOM   4816 H HB3  . GLU   B 1 64  ? 53.717 -10.685 2.158   1.00 16.40 ?  64  GLU   B HB3  1 
ATOM   4817 H HG2  . GLU   B 1 64  ? 51.882 -9.137  2.596   1.00 16.48 ?  64  GLU   B HG2  1 
ATOM   4818 H HG3  . GLU   B 1 64  ? 52.779 -8.067  1.840   1.00 16.48 ?  64  GLU   B HG3  1 
ATOM   4819 N N    . SER   B 1 65  ? 52.841 -11.324 4.913   1.00 12.77 ?  65  SER   B N    1 
ATOM   4820 C CA   . SER   B 1 65  ? 51.730 -11.829 5.713   1.00 13.15 ?  65  SER   B CA   1 
ATOM   4821 C C    . SER   B 1 65  ? 51.866 -11.433 7.177   1.00 13.05 ?  65  SER   B C    1 
ATOM   4822 O O    . SER   B 1 65  ? 50.871 -11.063 7.817   1.00 13.42 ?  65  SER   B O    1 
ATOM   4823 C CB   . SER   B 1 65  ? 51.646 -13.350 5.581   1.00 12.88 ?  65  SER   B CB   1 
ATOM   4824 O OG   . SER   B 1 65  ? 51.298 -13.745 4.259   1.00 13.38 ?  65  SER   B OG   1 
ATOM   4825 H H    . SER   B 1 65  ? 53.352 -11.944 4.596   1.00 15.32 ?  65  SER   B H    1 
ATOM   4826 H HA   . SER   B 1 65  ? 50.901 -11.453 5.378   1.00 15.77 ?  65  SER   B HA   1 
ATOM   4827 H HB2  . SER   B 1 65  ? 52.502 -13.737 5.802   1.00 15.44 ?  65  SER   B HB2  1 
ATOM   4828 H HB3  . SER   B 1 65  ? 50.964 -13.680 6.191   1.00 15.44 ?  65  SER   B HB3  1 
ATOM   4829 H HG   . SER   B 1 65  ? 51.872 -13.460 3.711   1.00 16.05 ?  65  SER   B HG   1 
ATOM   4830 N N    . ASP   B 1 66  ? 53.078 -11.528 7.737   1.00 13.30 ?  66  ASP   B N    1 
ATOM   4831 C CA   . ASP   B 1 66  ? 53.271 -11.140 9.131   1.00 13.58 ?  66  ASP   B CA   1 
ATOM   4832 C C    . ASP   B 1 66  ? 52.956 -9.661  9.336   1.00 14.07 ?  66  ASP   B C    1 
ATOM   4833 O O    . ASP   B 1 66  ? 52.384 -9.270  10.362  1.00 14.45 ?  66  ASP   B O    1 
ATOM   4834 C CB   . ASP   B 1 66  ? 54.702 -11.450 9.567   1.00 15.25 ?  66  ASP   B CB   1 
ATOM   4835 C CG   . ASP   B 1 66  ? 54.960 -12.939 9.735   1.00 17.11 ?  66  ASP   B CG   1 
ATOM   4836 O OD1  . ASP   B 1 66  ? 54.008 -13.752 9.662   1.00 17.93 ?  66  ASP   B OD1  1 
ATOM   4837 O OD2  . ASP   B 1 66  ? 56.137 -13.299 9.956   1.00 19.89 -1 66  ASP   B OD2  1 
ATOM   4838 H H    . ASP   B 1 66  ? 53.785 -11.813 7.337   1.00 15.95 ?  66  ASP   B H    1 
ATOM   4839 H HA   . ASP   B 1 66  ? 52.673 -11.651 9.692   1.00 16.28 ?  66  ASP   B HA   1 
ATOM   4840 H HB2  . ASP   B 1 66  ? 55.322 -11.121 8.896   1.00 18.29 ?  66  ASP   B HB2  1 
ATOM   4841 H HB3  . ASP   B 1 66  ? 54.878 -11.015 10.419  1.00 18.29 ?  66  ASP   B HB3  1 
ATOM   4842 N N    . ASP   B 1 67  ? 53.322 -8.820  8.370   1.00 13.85 ?  67  ASP   B N    1 
ATOM   4843 C CA   . ASP   B 1 67  ? 52.978 -7.407  8.468   1.00 14.47 ?  67  ASP   B CA   1 
ATOM   4844 C C    . ASP   B 1 67  ? 51.468 -7.195  8.385   1.00 14.41 ?  67  ASP   B C    1 
ATOM   4845 O O    . ASP   B 1 67  ? 50.907 -6.389  9.133   1.00 14.82 ?  67  ASP   B O    1 
ATOM   4846 C CB   . ASP   B 1 67  ? 53.695 -6.632  7.373   1.00 15.51 ?  67  ASP   B CB   1 
ATOM   4847 C CG   . ASP   B 1 67  ? 53.271 -5.187  7.335   1.00 17.01 ?  67  ASP   B CG   1 
ATOM   4848 O OD1  . ASP   B 1 67  ? 53.758 -4.386  8.165   1.00 18.23 ?  67  ASP   B OD1  1 
ATOM   4849 O OD2  . ASP   B 1 67  ? 52.420 -4.863  6.495   1.00 18.11 -1 67  ASP   B OD2  1 
ATOM   4850 H H    . ASP   B 1 67  ? 53.768 -9.039  7.665   1.00 16.60 ?  67  ASP   B H    1 
ATOM   4851 H HA   . ASP   B 1 67  ? 53.287 -7.066  9.322   1.00 17.35 ?  67  ASP   B HA   1 
ATOM   4852 H HB2  . ASP   B 1 67  ? 54.656 -6.659  7.536   1.00 18.60 ?  67  ASP   B HB2  1 
ATOM   4853 H HB3  . ASP   B 1 67  ? 53.502 -7.041  6.511   1.00 18.60 ?  67  ASP   B HB3  1 
ATOM   4854 N N    . TYR   B 1 68  ? 50.791 -7.927  7.494   1.00 13.80 ?  68  TYR   B N    1 
ATOM   4855 C CA   . TYR   B 1 68  ? 49.334 -7.855  7.424   1.00 14.46 ?  68  TYR   B CA   1 
ATOM   4856 C C    . TYR   B 1 68  ? 48.699 -8.201  8.768   1.00 14.12 ?  68  TYR   B C    1 
ATOM   4857 O O    . TYR   B 1 68  ? 47.766 -7.522  9.219   1.00 15.17 ?  68  TYR   B O    1 
ATOM   4858 C CB   . TYR   B 1 68  ? 48.803 -8.791  6.332   1.00 15.28 ?  68  TYR   B CB   1 
ATOM   4859 C CG   . TYR   B 1 68  ? 47.293 -8.940  6.385   1.00 16.20 ?  68  TYR   B CG   1 
ATOM   4860 C CD1  . TYR   B 1 68  ? 46.699 -9.896  7.204   1.00 17.05 ?  68  TYR   B CD1  1 
ATOM   4861 C CD2  . TYR   B 1 68  ? 46.466 -8.104  5.656   1.00 17.45 ?  68  TYR   B CD2  1 
ATOM   4862 C CE1  . TYR   B 1 68  ? 45.331 -10.021 7.289   1.00 18.42 ?  68  TYR   B CE1  1 
ATOM   4863 C CE2  . TYR   B 1 68  ? 45.082 -8.228  5.730   1.00 18.02 ?  68  TYR   B CE2  1 
ATOM   4864 C CZ   . TYR   B 1 68  ? 44.536 -9.184  6.550   1.00 18.18 ?  68  TYR   B CZ   1 
ATOM   4865 O OH   . TYR   B 1 68  ? 43.169 -9.300  6.637   1.00 19.07 ?  68  TYR   B OH   1 
ATOM   4866 H H    . TYR   B 1 68  ? 51.151 -8.479  6.933   1.00 16.55 ?  68  TYR   B H    1 
ATOM   4867 H HA   . TYR   B 1 68  ? 49.079 -6.952  7.199   1.00 17.33 ?  68  TYR   B HA   1 
ATOM   4868 H HB2  . TYR   B 1 68  ? 49.035 -8.430  5.466   1.00 18.33 ?  68  TYR   B HB2  1 
ATOM   4869 H HB3  . TYR   B 1 68  ? 49.196 -9.671  6.447   1.00 18.33 ?  68  TYR   B HB3  1 
ATOM   4870 H HD1  . TYR   B 1 68  ? 47.236 -10.467 7.709   1.00 20.45 ?  68  TYR   B HD1  1 
ATOM   4871 H HD2  . TYR   B 1 68  ? 46.842 -7.451  5.118   1.00 20.92 ?  68  TYR   B HD2  1 
ATOM   4872 H HE1  . TYR   B 1 68  ? 44.947 -10.677 7.833   1.00 22.10 ?  68  TYR   B HE1  1 
ATOM   4873 H HE2  . TYR   B 1 68  ? 44.532 -7.663  5.240   1.00 21.61 ?  68  TYR   B HE2  1 
ATOM   4874 H HH   . TYR   B 1 68  ? 42.784 -8.746  6.128   1.00 22.87 ?  68  TYR   B HH   1 
ATOM   4875 N N    . ILE   B 1 69  ? 49.184 -9.266  9.416   1.00 14.11 ?  69  ILE   B N    1 
ATOM   4876 C CA   . ILE   B 1 69  ? 48.624 -9.695  10.695  1.00 14.78 ?  69  ILE   B CA   1 
ATOM   4877 C C    . ILE   B 1 69  ? 48.877 -8.648  11.774  1.00 14.59 ?  69  ILE   B C    1 
ATOM   4878 O O    . ILE   B 1 69  ? 48.006 -8.368  12.605  1.00 14.88 ?  69  ILE   B O    1 
ATOM   4879 C CB   . ILE   B 1 69  ? 49.201 -11.071 11.080  1.00 15.79 ?  69  ILE   B CB   1 
ATOM   4880 C CG1  . ILE   B 1 69  ? 48.668 -12.168 10.148  1.00 16.00 ?  69  ILE   B CG1  1 
ATOM   4881 C CG2  . ILE   B 1 69  ? 48.919 -11.393 12.541  1.00 16.68 ?  69  ILE   B CG2  1 
ATOM   4882 C CD1  . ILE   B 1 69  ? 47.190 -12.459 10.294  1.00 16.20 ?  69  ILE   B CD1  1 
ATOM   4883 H H    . ILE   B 1 69  ? 49.834 -9.752  9.139   1.00 16.92 ?  69  ILE   B H    1 
ATOM   4884 H HA   . ILE   B 1 69  ? 47.665 -9.789  10.603  1.00 17.72 ?  69  ILE   B HA   1 
ATOM   4885 H HB   . ILE   B 1 69  ? 50.164 -11.031 10.969  1.00 18.93 ?  69  ILE   B HB   1 
ATOM   4886 H HG12 . ILE   B 1 69  ? 48.824 -11.892 9.231   1.00 19.18 ?  69  ILE   B HG12 1 
ATOM   4887 H HG13 . ILE   B 1 69  ? 49.149 -12.988 10.330  1.00 19.18 ?  69  ILE   B HG13 1 
ATOM   4888 H HG21 . ILE   B 1 69  ? 49.068 -12.344 12.683  1.00 20.01 ?  69  ILE   B HG21 1 
ATOM   4889 H HG22 . ILE   B 1 69  ? 49.520 -10.883 13.104  1.00 20.01 ?  69  ILE   B HG22 1 
ATOM   4890 H HG23 . ILE   B 1 69  ? 47.998 -11.173 12.743  1.00 20.01 ?  69  ILE   B HG23 1 
ATOM   4891 H HD11 . ILE   B 1 69  ? 46.956 -13.188 9.701   1.00 19.43 ?  69  ILE   B HD11 1 
ATOM   4892 H HD12 . ILE   B 1 69  ? 47.003 -12.709 11.213  1.00 19.43 ?  69  ILE   B HD12 1 
ATOM   4893 H HD13 . ILE   B 1 69  ? 46.682 -11.667 10.058  1.00 19.43 ?  69  ILE   B HD13 1 
ATOM   4894 N N    . ALA   B 1 70  ? 50.074 -8.063  11.796  1.00 14.73 ?  70  ALA   B N    1 
ATOM   4895 C CA   . ALA   B 1 70  ? 50.358 -7.026  12.784  1.00 14.47 ?  70  ALA   B CA   1 
ATOM   4896 C C    . ALA   B 1 70  ? 49.362 -5.879  12.676  1.00 14.79 ?  70  ALA   B C    1 
ATOM   4897 O O    . ALA   B 1 70  ? 48.923 -5.331  13.693  1.00 14.89 ?  70  ALA   B O    1 
ATOM   4898 C CB   . ALA   B 1 70  ? 51.790 -6.516  12.612  1.00 15.37 ?  70  ALA   B CB   1 
ATOM   4899 H H    . ALA   B 1 70  ? 50.719 -8.246  11.267  1.00 17.66 ?  70  ALA   B H    1 
ATOM   4900 H HA   . ALA   B 1 70  ? 50.284 -7.406  13.676  1.00 17.35 ?  70  ALA   B HA   1 
ATOM   4901 H HB1  . ALA   B 1 70  ? 51.976 -5.855  13.296  1.00 18.43 ?  70  ALA   B HB1  1 
ATOM   4902 H HB2  . ALA   B 1 70  ? 52.405 -7.263  12.701  1.00 18.43 ?  70  ALA   B HB2  1 
ATOM   4903 H HB3  . ALA   B 1 70  ? 51.881 -6.120  11.732  1.00 18.43 ?  70  ALA   B HB3  1 
ATOM   4904 N N    . THR   B 1 71  ? 48.986 -5.510  11.452  1.00 15.23 ?  71  THR   B N    1 
ATOM   4905 C CA   . THR   B 1 71  ? 48.093 -4.376  11.244  1.00 16.35 ?  71  THR   B CA   1 
ATOM   4906 C C    . THR   B 1 71  ? 46.626 -4.744  11.445  1.00 16.56 ?  71  THR   B C    1 
ATOM   4907 O O    . THR   B 1 71  ? 45.845 -3.928  11.951  1.00 18.06 ?  71  THR   B O    1 
ATOM   4908 C CB   . THR   B 1 71  ? 48.307 -3.808  9.839   1.00 18.00 ?  71  THR   B CB   1 
ATOM   4909 O OG1  . THR   B 1 71  ? 49.630 -3.266  9.744   1.00 19.83 ?  71  THR   B OG1  1 
ATOM   4910 C CG2  . THR   B 1 71  ? 47.281 -2.723  9.518   1.00 19.05 ?  71  THR   B CG2  1 
ATOM   4911 H H    . THR   B 1 71  ? 49.236 -5.903  10.729  1.00 18.27 ?  71  THR   B H    1 
ATOM   4912 H HA   . THR   B 1 71  ? 48.317 -3.680  11.882  1.00 19.61 ?  71  THR   B HA   1 
ATOM   4913 H HB   . THR   B 1 71  ? 48.212 -4.515  9.185   1.00 21.58 ?  71  THR   B HB   1 
ATOM   4914 H HG1  . THR   B 1 71  ? 49.753 -2.934  8.977   1.00 23.79 ?  71  THR   B HG1  1 
ATOM   4915 H HG21 . THR   B 1 71  ? 47.584 -2.193  8.762   1.00 22.85 ?  71  THR   B HG21 1 
ATOM   4916 H HG22 . THR   B 1 71  ? 46.427 -3.121  9.300   1.00 22.85 ?  71  THR   B HG22 1 
ATOM   4917 H HG23 . THR   B 1 71  ? 47.171 -2.133  10.284  1.00 22.85 ?  71  THR   B HG23 1 
ATOM   4918 N N    . ASN   B 1 72  ? 46.235 -5.962  11.060  1.00 16.02 ?  72  ASN   B N    1 
ATOM   4919 C CA   . ASN   B 1 72  ? 44.829 -6.319  10.930  1.00 16.43 ?  72  ASN   B CA   1 
ATOM   4920 C C    . ASN   B 1 72  ? 44.353 -7.416  11.869  1.00 16.97 ?  72  ASN   B C    1 
ATOM   4921 O O    . ASN   B 1 72  ? 43.136 -7.583  12.022  1.00 18.13 ?  72  ASN   B O    1 
ATOM   4922 C CB   . ASN   B 1 72  ? 44.523 -6.741  9.485   1.00 17.16 ?  72  ASN   B CB   1 
ATOM   4923 C CG   . ASN   B 1 72  ? 44.789 -5.635  8.500   1.00 18.20 ?  72  ASN   B CG   1 
ATOM   4924 O OD1  . ASN   B 1 72  ? 45.791 -5.640  7.780   1.00 19.52 ?  72  ASN   B OD1  1 
ATOM   4925 N ND2  . ASN   B 1 72  ? 43.915 -4.650  8.492   1.00 19.60 ?  72  ASN   B ND2  1 
ATOM   4926 H H    . ASN   B 1 72  ? 46.779 -6.606  10.863  1.00 19.22 ?  72  ASN   B H    1 
ATOM   4927 H HA   . ASN   B 1 72  ? 44.302 -5.532  11.118  1.00 19.70 ?  72  ASN   B HA   1 
ATOM   4928 H HB2  . ASN   B 1 72  ? 45.088 -7.497  9.250   1.00 20.58 ?  72  ASN   B HB2  1 
ATOM   4929 H HB3  . ASN   B 1 72  ? 43.591 -6.987  9.420   1.00 20.58 ?  72  ASN   B HB3  1 
ATOM   4930 H HD21 . ASN   B 1 72  ? 44.016 -3.987  7.952   1.00 23.50 ?  72  ASN   B HD21 1 
ATOM   4931 H HD22 . ASN   B 1 72  ? 43.229 -4.675  9.012   1.00 23.50 ?  72  ASN   B HD22 1 
ATOM   4932 N N    . GLY   B 1 73  ? 45.252 -8.170  12.488  1.00 16.42 ?  73  GLY   B N    1 
ATOM   4933 C CA   . GLY   B 1 73  ? 44.850 -9.315  13.267  1.00 15.90 ?  73  GLY   B CA   1 
ATOM   4934 C C    . GLY   B 1 73  ? 44.491 -10.496 12.390  1.00 14.39 ?  73  GLY   B C    1 
ATOM   4935 O O    . GLY   B 1 73  ? 44.476 -10.410 11.159  1.00 14.30 ?  73  GLY   B O    1 
ATOM   4936 H H    . GLY   B 1 73  ? 46.102 -8.035  12.473  1.00 19.69 ?  73  GLY   B H    1 
ATOM   4937 H HA2  . GLY   B 1 73  ? 45.573 -9.572  13.863  1.00 19.07 ?  73  GLY   B HA2  1 
ATOM   4938 H HA3  . GLY   B 1 73  ? 44.076 -9.083  13.809  1.00 19.07 ?  73  GLY   B HA3  1 
ATOM   4939 N N    . PRO   B 1 74  ? 44.192 -11.626 13.024  1.00 14.80 ?  74  PRO   B N    1 
ATOM   4940 C CA   . PRO   B 1 74  ? 43.940 -12.856 12.272  1.00 14.75 ?  74  PRO   B CA   1 
ATOM   4941 C C    . PRO   B 1 74  ? 42.639 -12.805 11.483  1.00 13.87 ?  74  PRO   B C    1 
ATOM   4942 O O    . PRO   B 1 74  ? 41.694 -12.069 11.801  1.00 15.19 ?  74  PRO   B O    1 
ATOM   4943 C CB   . PRO   B 1 74  ? 43.872 -13.927 13.367  1.00 15.81 ?  74  PRO   B CB   1 
ATOM   4944 C CG   . PRO   B 1 74  ? 43.431 -13.192 14.582  1.00 17.26 ?  74  PRO   B CG   1 
ATOM   4945 C CD   . PRO   B 1 74  ? 44.073 -11.834 14.477  1.00 16.63 ?  74  PRO   B CD   1 
ATOM   4946 H HA   . PRO   B 1 74  ? 44.684 -13.044 11.672  1.00 17.69 ?  74  PRO   B HA   1 
ATOM   4947 H HB2  . PRO   B 1 74  ? 43.224 -14.605 13.117  1.00 18.96 ?  74  PRO   B HB2  1 
ATOM   4948 H HB3  . PRO   B 1 74  ? 44.749 -14.318 13.496  1.00 18.96 ?  74  PRO   B HB3  1 
ATOM   4949 H HG2  . PRO   B 1 74  ? 42.464 -13.115 14.584  1.00 20.70 ?  74  PRO   B HG2  1 
ATOM   4950 H HG3  . PRO   B 1 74  ? 43.741 -13.657 15.373  1.00 20.70 ?  74  PRO   B HG3  1 
ATOM   4951 H HD2  . PRO   B 1 74  ? 43.498 -11.157 14.876  1.00 19.94 ?  74  PRO   B HD2  1 
ATOM   4952 H HD3  . PRO   B 1 74  ? 44.950 -11.838 14.889  1.00 19.94 ?  74  PRO   B HD3  1 
ATOM   4953 N N    . LEU   B 1 75  ? 42.610 -13.616 10.429  1.00 13.19 ?  75  LEU   B N    1 
ATOM   4954 C CA   . LEU   B 1 75  ? 41.394 -13.838 9.665   1.00 13.42 ?  75  LEU   B CA   1 
ATOM   4955 C C    . LEU   B 1 75  ? 40.423 -14.695 10.475  1.00 13.44 ?  75  LEU   B C    1 
ATOM   4956 O O    . LEU   B 1 75  ? 40.761 -15.241 11.526  1.00 14.64 ?  75  LEU   B O    1 
ATOM   4957 C CB   . LEU   B 1 75  ? 41.712 -14.549 8.349   1.00 13.52 ?  75  LEU   B CB   1 
ATOM   4958 C CG   . LEU   B 1 75  ? 42.568 -13.793 7.327   1.00 15.21 ?  75  LEU   B CG   1 
ATOM   4959 C CD1  . LEU   B 1 75  ? 42.746 -14.620 6.059   1.00 16.85 ?  75  LEU   B CD1  1 
ATOM   4960 C CD2  . LEU   B 1 75  ? 41.999 -12.440 6.991   1.00 18.44 ?  75  LEU   B CD2  1 
ATOM   4961 H H    . LEU   B 1 75  ? 43.288 -14.057 10.130  1.00 15.82 ?  75  LEU   B H    1 
ATOM   4962 H HA   . LEU   B 1 75  ? 40.968 -12.991 9.466   1.00 16.09 ?  75  LEU   B HA   1 
ATOM   4963 H HB2  . LEU   B 1 75  ? 42.178 -15.375 8.554   1.00 16.22 ?  75  LEU   B HB2  1 
ATOM   4964 H HB3  . LEU   B 1 75  ? 40.872 -14.764 7.908   1.00 16.22 ?  75  LEU   B HB3  1 
ATOM   4965 H HG   . LEU   B 1 75  ? 43.449 -13.656 7.707   1.00 18.24 ?  75  LEU   B HG   1 
ATOM   4966 H HD11 . LEU   B 1 75  ? 43.299 -14.120 5.431   1.00 20.21 ?  75  LEU   B HD11 1 
ATOM   4967 H HD12 . LEU   B 1 75  ? 43.182 -15.457 6.281   1.00 20.21 ?  75  LEU   B HD12 1 
ATOM   4968 H HD13 . LEU   B 1 75  ? 41.878 -14.792 5.665   1.00 20.21 ?  75  LEU   B HD13 1 
ATOM   4969 H HD21 . LEU   B 1 75  ? 42.522 -12.046 6.278   1.00 22.11 ?  75  LEU   B HD21 1 
ATOM   4970 H HD22 . LEU   B 1 75  ? 41.078 -12.548 6.709   1.00 22.11 ?  75  LEU   B HD22 1 
ATOM   4971 H HD23 . LEU   B 1 75  ? 42.039 -11.879 7.782   1.00 22.11 ?  75  LEU   B HD23 1 
ATOM   4972 N N    . LYS   B 1 76  ? 39.193 -14.798 9.970   1.00 14.78 ?  76  LYS   B N    1 
ATOM   4973 C CA   . LYS   B 1 76  ? 38.210 -15.764 10.446  1.00 16.31 ?  76  LYS   B CA   1 
ATOM   4974 C C    . LYS   B 1 76  ? 38.294 -17.035 9.603   1.00 14.56 ?  76  LYS   B C    1 
ATOM   4975 O O    . LYS   B 1 76  ? 38.563 -16.976 8.404   1.00 14.06 ?  76  LYS   B O    1 
ATOM   4976 C CB   . LYS   B 1 76  ? 36.792 -15.194 10.278  1.00 19.07 ?  76  LYS   B CB   1 
ATOM   4977 C CG   . LYS   B 1 76  ? 36.537 -13.787 10.855  1.00 21.33 ?  76  LYS   B CG   1 
ATOM   4978 C CD   . LYS   B 1 76  ? 35.126 -13.259 10.509  1.00 23.07 ?  76  LYS   B CD   1 
ATOM   4979 C CE   . LYS   B 1 76  ? 34.885 -11.866 11.081  1.00 25.21 ?  76  LYS   B CE   1 
ATOM   4980 N NZ   . LYS   B 1 76  ? 33.579 -11.285 10.650  1.00 26.02 ?  76  LYS   B NZ   1 
ATOM   4981 H H    . LYS   B 1 76  ? 38.898 -14.303 9.336   1.00 17.72 ?  76  LYS   B H    1 
ATOM   4982 H HA   . LYS   B 1 76  ? 38.361 -15.981 11.383  1.00 19.56 ?  76  LYS   B HA   1 
ATOM   4983 H HB2  . LYS   B 1 76  ? 36.591 -15.152 9.330   1.00 22.87 ?  76  LYS   B HB2  1 
ATOM   4984 H HB3  . LYS   B 1 76  ? 36.165 -15.794 10.712  1.00 22.87 ?  76  LYS   B HB3  1 
ATOM   4985 H HG2  . LYS   B 1 76  ? 36.619 -13.818 11.821  1.00 25.59 ?  76  LYS   B HG2  1 
ATOM   4986 H HG3  . LYS   B 1 76  ? 37.188 -13.168 10.486  1.00 25.59 ?  76  LYS   B HG3  1 
ATOM   4987 H HD2  . LYS   B 1 76  ? 35.030 -13.208 9.545   1.00 27.67 ?  76  LYS   B HD2  1 
ATOM   4988 H HD3  . LYS   B 1 76  ? 34.460 -13.855 10.882  1.00 27.67 ?  76  LYS   B HD3  1 
ATOM   4989 H HE2  . LYS   B 1 76  ? 34.887 -11.917 12.050  1.00 30.23 ?  76  LYS   B HE2  1 
ATOM   4990 H HE3  . LYS   B 1 76  ? 35.593 -11.273 10.779  1.00 30.23 ?  76  LYS   B HE3  1 
ATOM   4991 H HZ1  . LYS   B 1 76  ? 33.476 -10.473 11.003  1.00 31.21 ?  76  LYS   B HZ1  1 
ATOM   4992 H HZ2  . LYS   B 1 76  ? 33.553 -11.217 9.763   1.00 31.21 ?  76  LYS   B HZ2  1 
ATOM   4993 H HZ3  . LYS   B 1 76  ? 32.910 -11.804 10.921  1.00 31.21 ?  76  LYS   B HZ3  1 
ATOM   4994 N N    . VAL   B 1 77  ? 38.039 -18.192 10.228  1.00 15.22 ?  77  VAL   B N    1 
ATOM   4995 C CA   . VAL   B 1 77  ? 37.826 -19.403 9.438   1.00 15.26 ?  77  VAL   B CA   1 
ATOM   4996 C C    . VAL   B 1 77  ? 36.636 -19.172 8.517   1.00 14.10 ?  77  VAL   B C    1 
ATOM   4997 O O    . VAL   B 1 77  ? 35.567 -18.726 8.957   1.00 14.35 ?  77  VAL   B O    1 
ATOM   4998 C CB   . VAL   B 1 77  ? 37.625 -20.631 10.340  1.00 16.77 ?  77  VAL   B CB   1 
ATOM   4999 C CG1  . VAL   B 1 77  ? 37.355 -21.858 9.482   1.00 17.21 ?  77  VAL   B CG1  1 
ATOM   5000 C CG2  . VAL   B 1 77  ? 38.848 -20.860 11.227  1.00 18.42 ?  77  VAL   B CG2  1 
ATOM   5001 H H    . VAL   B 1 77  ? 37.988 -18.294 11.078  1.00 18.25 ?  77  VAL   B H    1 
ATOM   5002 H HA   . VAL   B 1 77  ? 38.600 -19.557 8.884   1.00 18.30 ?  77  VAL   B HA   1 
ATOM   5003 H HB   . VAL   B 1 77  ? 36.853 -20.483 10.913  1.00 20.11 ?  77  VAL   B HB   1 
ATOM   5004 H HG11 . VAL   B 1 77  ? 37.428 -22.649 10.038  1.00 20.64 ?  77  VAL   B HG11 1 
ATOM   5005 H HG12 . VAL   B 1 77  ? 36.457 -21.798 9.113   1.00 20.64 ?  77  VAL   B HG12 1 
ATOM   5006 H HG13 . VAL   B 1 77  ? 38.006 -21.892 8.768   1.00 20.64 ?  77  VAL   B HG13 1 
ATOM   5007 H HG21 . VAL   B 1 77  ? 38.703 -21.658 11.757  1.00 22.10 ?  77  VAL   B HG21 1 
ATOM   5008 H HG22 . VAL   B 1 77  ? 39.626 -20.970 10.662  1.00 22.10 ?  77  VAL   B HG22 1 
ATOM   5009 H HG23 . VAL   B 1 77  ? 38.963 -20.092 11.808  1.00 22.10 ?  77  VAL   B HG23 1 
ATOM   5010 N N    . GLY   B 1 78  ? 36.823 -19.445 7.229   1.00 13.71 ?  78  GLY   B N    1 
ATOM   5011 C CA   . GLY   B 1 78  ? 35.852 -19.119 6.209   1.00 13.17 ?  78  GLY   B CA   1 
ATOM   5012 C C    . GLY   B 1 78  ? 36.100 -17.801 5.510   1.00 12.77 ?  78  GLY   B C    1 
ATOM   5013 O O    . GLY   B 1 78  ? 35.421 -17.511 4.519   1.00 13.14 ?  78  GLY   B O    1 
ATOM   5014 H H    . GLY   B 1 78  ? 37.528 -19.827 6.921   1.00 16.44 ?  78  GLY   B H    1 
ATOM   5015 H HA2  . GLY   B 1 78  ? 35.850 -19.817 5.542   1.00 15.80 ?  78  GLY   B HA2  1 
ATOM   5016 H HA3  . GLY   B 1 78  ? 34.971 -19.078 6.613   1.00 15.80 ?  78  GLY   B HA3  1 
ATOM   5017 N N    . GLY   B 1 79  ? 37.047 -16.996 6.001   1.00 12.79 ?  79  GLY   B N    1 
ATOM   5018 C CA   . GLY   B 1 79  ? 37.347 -15.703 5.425   1.00 12.38 ?  79  GLY   B CA   1 
ATOM   5019 C C    . GLY   B 1 79  ? 38.581 -15.719 4.534   1.00 12.30 ?  79  GLY   B C    1 
ATOM   5020 O O    . GLY   B 1 79  ? 39.191 -16.755 4.277   1.00 12.70 ?  79  GLY   B O    1 
ATOM   5021 H H    . GLY   B 1 79  ? 37.544 -17.191 6.673   1.00 15.33 ?  79  GLY   B H    1 
ATOM   5022 H HA2  . GLY   B 1 79  ? 36.594 -15.401 4.890   1.00 14.85 ?  79  GLY   B HA2  1 
ATOM   5023 H HA3  . GLY   B 1 79  ? 37.493 -15.059 6.134   1.00 14.85 ?  79  GLY   B HA3  1 
ATOM   5024 N N    . SER   B 1 80  ? 38.954 -14.522 4.066   1.00 12.26 ?  80  SER   B N    1 
ATOM   5025 C CA   . SER   B 1 80  ? 40.061 -14.381 3.131   1.00 11.93 ?  80  SER   B CA   1 
ATOM   5026 C C    . SER   B 1 80  ? 40.636 -12.972 3.196   1.00 11.86 ?  80  SER   B C    1 
ATOM   5027 O O    . SER   B 1 80  ? 40.015 -12.038 3.715   1.00 13.17 ?  80  SER   B O    1 
ATOM   5028 C CB   . SER   B 1 80  ? 39.619 -14.663 1.691   1.00 12.60 ?  80  SER   B CB   1 
ATOM   5029 O OG   . SER   B 1 80  ? 38.767 -13.643 1.193   1.00 13.52 ?  80  SER   B OG   1 
ATOM   5030 H H    . SER   B 1 80  ? 38.583 -13.777 4.279   1.00 14.70 ?  80  SER   B H    1 
ATOM   5031 H HA   . SER   B 1 80  ? 40.754 -15.010 3.372   1.00 14.30 ?  80  SER   B HA   1 
ATOM   5032 H HB2  . SER   B 1 80  ? 40.403 -14.713 1.122   1.00 15.11 ?  80  SER   B HB2  1 
ATOM   5033 H HB3  . SER   B 1 80  ? 39.142 -15.508 1.668   1.00 15.11 ?  80  SER   B HB3  1 
ATOM   5034 H HG   . SER   B 1 80  ? 38.074 -13.590 1.675   1.00 16.21 ?  80  SER   B HG   1 
ATOM   5035 N N    . CYS   B 1 81  ? 41.821 -12.825 2.608   1.00 11.59 ?  81  CYS   B N    1 
ATOM   5036 C CA   . CYS   B 1 81  ? 42.363 -11.512 2.302   1.00 11.77 ?  81  CYS   B CA   1 
ATOM   5037 C C    . CYS   B 1 81  ? 43.131 -11.598 0.993   1.00 11.02 ?  81  CYS   B C    1 
ATOM   5038 O O    . CYS   B 1 81  ? 43.634 -12.661 0.610   1.00 12.32 ?  81  CYS   B O    1 
ATOM   5039 C CB   . CYS   B 1 81  ? 43.252 -10.958 3.425   1.00 12.75 ?  81  CYS   B CB   1 
ATOM   5040 S SG   . CYS   B 1 81  ? 44.777 -11.889 3.674   1.00 13.29 ?  81  CYS   B SG   1 
ATOM   5041 H H    . CYS   B 1 81  ? 42.336 -13.477 2.370   1.00 13.89 ?  81  CYS   B H    1 
ATOM   5042 H HA   . CYS   B 1 81  ? 41.625 -10.890 2.176   1.00 14.11 ?  81  CYS   B HA   1 
ATOM   5043 H HB2  . CYS   B 1 81  ? 43.496 -10.042 3.211   1.00 15.29 ?  81  CYS   B HB2  1 
ATOM   5044 H HB3  . CYS   B 1 81  ? 42.748 -10.971 4.258   1.00 15.29 ?  81  CYS   B HB3  1 
ATOM   5045 H HG   . CYS   B 1 81  ? 45.399 -11.392 4.576   1.00 15.94 ?  81  CYS   B HG   1 
ATOM   5046 N N    . VAL   B 1 82  ? 43.230 -10.455 0.319   1.00 11.48 ?  82  VAL   B N    1 
ATOM   5047 C CA   . VAL   B 1 82  ? 43.999 -10.327 -0.918  1.00 11.55 ?  82  VAL   B CA   1 
ATOM   5048 C C    . VAL   B 1 82  ? 45.343 -9.687  -0.602  1.00 12.08 ?  82  VAL   B C    1 
ATOM   5049 O O    . VAL   B 1 82  ? 45.392 -8.566  -0.075  1.00 13.12 ?  82  VAL   B O    1 
ATOM   5050 C CB   . VAL   B 1 82  ? 43.251 -9.486  -1.964  1.00 13.10 ?  82  VAL   B CB   1 
ATOM   5051 C CG1  . VAL   B 1 82  ? 44.086 -9.338  -3.229  1.00 14.28 ?  82  VAL   B CG1  1 
ATOM   5052 C CG2  . VAL   B 1 82  ? 41.888 -10.088 -2.270  1.00 14.07 ?  82  VAL   B CG2  1 
ATOM   5053 H H    . VAL   B 1 82  ? 42.854 -9.714  0.562   1.00 13.76 ?  82  VAL   B H    1 
ATOM   5054 H HA   . VAL   B 1 82  ? 44.158 -11.203 -1.289  1.00 13.85 ?  82  VAL   B HA   1 
ATOM   5055 H HB   . VAL   B 1 82  ? 43.102 -8.598  -1.606  1.00 15.71 ?  82  VAL   B HB   1 
ATOM   5056 H HG11 . VAL   B 1 82  ? 43.521 -9.013  -3.946  1.00 17.12 ?  82  VAL   B HG11 1 
ATOM   5057 H HG12 . VAL   B 1 82  ? 44.803 -8.702  -3.063  1.00 17.12 ?  82  VAL   B HG12 1 
ATOM   5058 H HG13 . VAL   B 1 82  ? 44.458 -10.201 -3.466  1.00 17.12 ?  82  VAL   B HG13 1 
ATOM   5059 H HG21 . VAL   B 1 82  ? 41.453 -9.564  -2.964  1.00 16.87 ?  82  VAL   B HG21 1 
ATOM   5060 H HG22 . VAL   B 1 82  ? 42.003 -11.003 -2.575  1.00 16.87 ?  82  VAL   B HG22 1 
ATOM   5061 H HG23 . VAL   B 1 82  ? 41.345 -10.078 -1.464  1.00 16.87 ?  82  VAL   B HG23 1 
ATOM   5062 N N    . LEU   B 1 83  ? 46.426 -10.369 -0.974  1.00 11.57 ?  83  LEU   B N    1 
ATOM   5063 C CA   . LEU   B 1 83  ? 47.782 -9.855  -0.852  1.00 11.57 ?  83  LEU   B CA   1 
ATOM   5064 C C    . LEU   B 1 83  ? 48.485 -9.995  -2.204  1.00 11.82 ?  83  LEU   B C    1 
ATOM   5065 O O    . LEU   B 1 83  ? 47.881 -10.406 -3.202  1.00 11.87 ?  83  LEU   B O    1 
ATOM   5066 C CB   . LEU   B 1 83  ? 48.532 -10.523 0.308   1.00 12.53 ?  83  LEU   B CB   1 
ATOM   5067 C CG   . LEU   B 1 83  ? 48.009 -10.171 1.709   1.00 13.60 ?  83  LEU   B CG   1 
ATOM   5068 C CD1  . LEU   B 1 83  ? 48.625 -11.053 2.774   1.00 14.39 ?  83  LEU   B CD1  1 
ATOM   5069 C CD2  . LEU   B 1 83  ? 48.224 -8.697  2.053   1.00 14.67 ?  83  LEU   B CD2  1 
ATOM   5070 H H    . LEU   B 1 83  ? 46.389 -11.161 -1.318  1.00 13.87 ?  83  LEU   B H    1 
ATOM   5071 H HA   . LEU   B 1 83  ? 47.727 -8.909  -0.659  1.00 13.87 ?  83  LEU   B HA   1 
ATOM   5072 H HB2  . LEU   B 1 83  ? 48.473 -11.482 0.204   1.00 15.03 ?  83  LEU   B HB2  1 
ATOM   5073 H HB3  . LEU   B 1 83  ? 49.462 -10.246 0.267   1.00 15.03 ?  83  LEU   B HB3  1 
ATOM   5074 H HG   . LEU   B 1 83  ? 47.052 -10.330 1.719   1.00 16.31 ?  83  LEU   B HG   1 
ATOM   5075 H HD11 . LEU   B 1 83  ? 48.259 -10.806 3.638   1.00 17.25 ?  83  LEU   B HD11 1 
ATOM   5076 H HD12 . LEU   B 1 83  ? 48.405 -11.981 2.579   1.00 17.25 ?  83  LEU   B HD12 1 
ATOM   5077 H HD13 . LEU   B 1 83  ? 49.584 -10.934 2.771   1.00 17.25 ?  83  LEU   B HD13 1 
ATOM   5078 H HD21 . LEU   B 1 83  ? 47.976 -8.553  2.980   1.00 17.59 ?  83  LEU   B HD21 1 
ATOM   5079 H HD22 . LEU   B 1 83  ? 49.158 -8.476  1.922   1.00 17.59 ?  83  LEU   B HD22 1 
ATOM   5080 H HD23 . LEU   B 1 83  ? 47.669 -8.153  1.473   1.00 17.59 ?  83  LEU   B HD23 1 
ATOM   5081 N N    . SER   B 1 84  ? 49.762 -9.615  -2.256  1.00 12.67 ?  84  SER   B N    1 
ATOM   5082 C CA   . SER   B 1 84  ? 50.497 -9.733  -3.507  1.00 12.97 ?  84  SER   B CA   1 
ATOM   5083 C C    . SER   B 1 84  ? 50.645 -11.194 -3.918  1.00 12.31 ?  84  SER   B C    1 
ATOM   5084 O O    . SER   B 1 84  ? 50.764 -12.089 -3.083  1.00 12.02 ?  84  SER   B O    1 
ATOM   5085 C CB   . SER   B 1 84  ? 51.892 -9.126  -3.361  1.00 14.96 ?  84  SER   B CB   1 
ATOM   5086 O OG   . SER   B 1 84  ? 52.638 -9.336  -4.543  1.00 16.36 ?  84  SER   B OG   1 
ATOM   5087 H H    . SER   B 1 84  ? 50.211 -9.287  -1.599  1.00 15.19 ?  84  SER   B H    1 
ATOM   5088 H HA   . SER   B 1 84  ? 50.025 -9.265  -4.210  1.00 15.55 ?  84  SER   B HA   1 
ATOM   5089 H HB2  . SER   B 1 84  ? 51.805 -8.170  -3.199  1.00 17.94 ?  84  SER   B HB2  1 
ATOM   5090 H HB3  . SER   B 1 84  ? 52.352 -9.547  -2.621  1.00 17.94 ?  84  SER   B HB3  1 
ATOM   5091 H HG   . SER   B 1 84  ? 53.404 -8.987  -4.470  1.00 19.63 ?  84  SER   B HG   1 
ATOM   5092 N N    . GLY   B 1 85  ? 50.700 -11.423 -5.225  1.00 13.18 ?  85  GLY   B N    1 
ATOM   5093 C CA   . GLY   B 1 85  ? 51.060 -12.713 -5.768  1.00 13.52 ?  85  GLY   B CA   1 
ATOM   5094 C C    . GLY   B 1 85  ? 52.531 -12.903 -6.069  1.00 12.80 ?  85  GLY   B C    1 
ATOM   5095 O O    . GLY   B 1 85  ? 52.911 -13.983 -6.526  1.00 13.24 ?  85  GLY   B O    1 
ATOM   5096 H H    . GLY   B 1 85  ? 50.537 -10.837 -5.824  1.00 15.80 ?  85  GLY   B H    1 
ATOM   5097 H HA2  . GLY   B 1 85  ? 50.794 -13.407 -5.140  1.00 16.21 ?  85  GLY   B HA2  1 
ATOM   5098 H HA3  . GLY   B 1 85  ? 50.571 -12.859 -6.590  1.00 16.21 ?  85  GLY   B HA3  1 
ATOM   5099 N N    . HIS   B 1 86  ? 53.383 -11.902 -5.845  1.00 13.09 ?  86  HIS   B N    1 
ATOM   5100 C CA   . HIS   B 1 86  ? 54.848 -12.067 -5.926  1.00 13.46 ?  86  HIS   B CA   1 
ATOM   5101 C C    . HIS   B 1 86  ? 55.219 -12.580 -7.316  1.00 13.13 ?  86  HIS   B C    1 
ATOM   5102 O O    . HIS   B 1 86  ? 54.828 -11.962 -8.320  1.00 14.07 ?  86  HIS   B O    1 
ATOM   5103 C CB   . HIS   B 1 86  ? 55.345 -12.903 -4.746  1.00 13.58 ?  86  HIS   B CB   1 
ATOM   5104 C CG   . HIS   B 1 86  ? 55.021 -12.298 -3.421  1.00 13.73 ?  86  HIS   B CG   1 
ATOM   5105 N ND1  . HIS   B 1 86  ? 55.836 -11.370 -2.807  1.00 15.29 ?  86  HIS   B ND1  1 
ATOM   5106 C CD2  . HIS   B 1 86  ? 53.952 -12.463 -2.609  1.00 13.96 ?  86  HIS   B CD2  1 
ATOM   5107 C CE1  . HIS   B 1 86  ? 55.272 -10.986 -1.674  1.00 15.16 ?  86  HIS   B CE1  1 
ATOM   5108 N NE2  . HIS   B 1 86  ? 54.128 -11.632 -1.532  1.00 14.29 ?  86  HIS   B NE2  1 
ATOM   5109 H H    . HIS   B 1 86  ? 53.140 -11.108 -5.641  1.00 15.69 ?  86  HIS   B H    1 
ATOM   5110 H HA   . HIS   B 1 86  ? 55.253 -11.190 -5.835  1.00 16.14 ?  86  HIS   B HA   1 
ATOM   5111 H HB2  . HIS   B 1 86  ? 54.943 -13.781 -4.785  1.00 16.29 ?  86  HIS   B HB2  1 
ATOM   5112 H HB3  . HIS   B 1 86  ? 56.316 -12.983 -4.803  1.00 16.29 ?  86  HIS   B HB3  1 
ATOM   5113 H HD2  . HIS   B 1 86  ? 53.220 -13.024 -2.766  1.00 16.74 ?  86  HIS   B HD2  1 
ATOM   5114 H HE1  . HIS   B 1 86  ? 55.625 -10.380 -1.065  1.00 18.18 ?  86  HIS   B HE1  1 
ATOM   5115 H HE2  . HIS   B 1 86  ? 53.586 -11.564 -0.865  1.00 17.13 ?  86  HIS   B HE2  1 
ATOM   5116 N N    . ASN   B 1 87  ? 55.989 -13.664 -7.426  1.00 13.65 ?  87  ASN   B N    1 
ATOM   5117 C CA   . ASN   B 1 87  ? 56.382 -14.241 -8.704  1.00 14.49 ?  87  ASN   B CA   1 
ATOM   5118 C C    . ASN   B 1 87  ? 55.397 -15.281 -9.207  1.00 13.77 ?  87  ASN   B C    1 
ATOM   5119 O O    . ASN   B 1 87  ? 55.715 -15.993 -10.166 1.00 15.75 ?  87  ASN   B O    1 
ATOM   5120 C CB   . ASN   B 1 87  ? 57.774 -14.874 -8.590  1.00 16.43 ?  87  ASN   B CB   1 
ATOM   5121 C CG   . ASN   B 1 87  ? 57.828 -15.990 -7.551  1.00 17.22 ?  87  ASN   B CG   1 
ATOM   5122 O OD1  . ASN   B 1 87  ? 57.195 -15.907 -6.492  1.00 16.04 ?  87  ASN   B OD1  1 
ATOM   5123 N ND2  . ASN   B 1 87  ? 58.567 -17.058 -7.866  1.00 19.34 ?  87  ASN   B ND2  1 
ATOM   5124 H H    . ASN   B 1 87  ? 56.292 -14.102 -6.753  1.00 16.37 ?  87  ASN   B H    1 
ATOM   5125 H HA   . ASN   B 1 87  ? 56.426 -13.536 -9.365  1.00 17.37 ?  87  ASN   B HA   1 
ATOM   5126 H HB2  . ASN   B 1 87  ? 58.021 -15.249 -9.453  1.00 19.71 ?  87  ASN   B HB2  1 
ATOM   5127 H HB3  . ASN   B 1 87  ? 58.409 -14.191 -8.332  1.00 19.71 ?  87  ASN   B HB3  1 
ATOM   5128 H HD21 . ASN   B 1 87  ? 58.632 -17.714 -7.316  1.00 23.20 ?  87  ASN   B HD21 1 
ATOM   5129 H HD22 . ASN   B 1 87  ? 58.990 -17.087 -8.619  1.00 23.20 ?  87  ASN   B HD22 1 
ATOM   5130 N N    . LEU   B 1 88  ? 54.217 -15.379 -8.586  1.00 13.06 ?  88  LEU   B N    1 
ATOM   5131 C CA   . LEU   B 1 88  ? 53.233 -16.409 -8.908  1.00 13.47 ?  88  LEU   B CA   1 
ATOM   5132 C C    . LEU   B 1 88  ? 52.000 -15.891 -9.628  1.00 12.92 ?  88  LEU   B C    1 
ATOM   5133 O O    . LEU   B 1 88  ? 51.400 -16.635 -10.413 1.00 14.86 ?  88  LEU   B O    1 
ATOM   5134 C CB   . LEU   B 1 88  ? 52.760 -17.099 -7.624  1.00 14.05 ?  88  LEU   B CB   1 
ATOM   5135 C CG   . LEU   B 1 88  ? 53.881 -17.749 -6.824  1.00 16.27 ?  88  LEU   B CG   1 
ATOM   5136 C CD1  . LEU   B 1 88  ? 53.385 -18.076 -5.423  1.00 17.97 ?  88  LEU   B CD1  1 
ATOM   5137 C CD2  . LEU   B 1 88  ? 54.365 -18.996 -7.534  1.00 19.22 ?  88  LEU   B CD2  1 
ATOM   5138 H H    . LEU   B 1 88  ? 53.959 -14.849 -7.954  1.00 15.65 ?  88  LEU   B H    1 
ATOM   5139 H HA   . LEU   B 1 88  ? 53.646 -17.076 -9.468  1.00 16.15 ?  88  LEU   B HA   1 
ATOM   5140 H HB2  . LEU   B 1 88  ? 52.329 -16.445 -7.050  1.00 16.84 ?  88  LEU   B HB2  1 
ATOM   5141 H HB3  . LEU   B 1 88  ? 52.124 -17.796 -7.858  1.00 16.84 ?  88  LEU   B HB3  1 
ATOM   5142 H HG   . LEU   B 1 88  ? 54.624 -17.130 -6.747  1.00 19.51 ?  88  LEU   B HG   1 
ATOM   5143 H HD11 . LEU   B 1 88  ? 54.027 -18.656 -4.990  1.00 21.55 ?  88  LEU   B HD11 1 
ATOM   5144 H HD12 . LEU   B 1 88  ? 53.292 -17.249 -4.923  1.00 21.55 ?  88  LEU   B HD12 1 
ATOM   5145 H HD13 . LEU   B 1 88  ? 52.527 -18.519 -5.493  1.00 21.55 ?  88  LEU   B HD13 1 
ATOM   5146 H HD21 . LEU   B 1 88  ? 55.034 -19.432 -6.983  1.00 23.05 ?  88  LEU   B HD21 1 
ATOM   5147 H HD22 . LEU   B 1 88  ? 53.613 -19.590 -7.676  1.00 23.05 ?  88  LEU   B HD22 1 
ATOM   5148 H HD23 . LEU   B 1 88  ? 54.754 -18.743 -8.387  1.00 23.05 ?  88  LEU   B HD23 1 
ATOM   5149 N N    . ALA   B 1 89  ? 51.586 -14.661 -9.353  1.00 12.61 ?  89  ALA   B N    1 
ATOM   5150 C CA   . ALA   B 1 89  ? 50.298 -14.158 -9.810  1.00 12.00 ?  89  ALA   B CA   1 
ATOM   5151 C C    . ALA   B 1 89  ? 50.277 -12.667 -9.533  1.00 12.24 ?  89  ALA   B C    1 
ATOM   5152 O O    . ALA   B 1 89  ? 51.114 -12.152 -8.791  1.00 13.37 ?  89  ALA   B O    1 
ATOM   5153 C CB   . ALA   B 1 89  ? 49.158 -14.829 -9.051  1.00 11.99 ?  89  ALA   B CB   1 
ATOM   5154 H H    . ALA   B 1 89  ? 52.031 -14.086 -8.886  1.00 15.12 ?  89  ALA   B H    1 
ATOM   5155 H HA   . ALA   B 1 89  ? 50.190 -14.310 -10.763 1.00 14.39 ?  89  ALA   B HA   1 
ATOM   5156 H HB1  . ALA   B 1 89  ? 48.310 -14.492 -9.394  1.00 14.38 ?  89  ALA   B HB1  1 
ATOM   5157 H HB2  . ALA   B 1 89  ? 49.206 -15.789 -9.193  1.00 14.38 ?  89  ALA   B HB2  1 
ATOM   5158 H HB3  . ALA   B 1 89  ? 49.239 -14.626 -8.111  1.00 14.38 ?  89  ALA   B HB3  1 
ATOM   5159 N N    . LYS   B 1 90  ? 49.293 -11.972 -10.098 1.00 13.27 ?  90  LYS   B N    1 
ATOM   5160 C CA   . LYS   B 1 90  ? 49.105 -10.587 -9.691  1.00 13.54 ?  90  LYS   B CA   1 
ATOM   5161 C C    . LYS   B 1 90  ? 48.784 -10.517 -8.203  1.00 13.27 ?  90  LYS   B C    1 
ATOM   5162 O O    . LYS   B 1 90  ? 49.421 -9.766  -7.450  1.00 14.63 ?  90  LYS   B O    1 
ATOM   5163 C CB   . LYS   B 1 90  ? 48.024 -9.931  -10.547 1.00 15.14 ?  90  LYS   B CB   1 
ATOM   5164 C CG   . LYS   B 1 90  ? 47.715 -8.501  -10.160 1.00 15.69 ?  90  LYS   B CG   1 
ATOM   5165 C CD   . LYS   B 1 90  ? 48.916 -7.592  -10.243 1.00 18.27 ?  90  LYS   B CD   1 
ATOM   5166 C CE   . LYS   B 1 90  ? 48.469 -6.174  -9.963  1.00 20.19 ?  90  LYS   B CE   1 
ATOM   5167 N NZ   . LYS   B 1 90  ? 49.608 -5.224  -9.919  1.00 20.08 ?  90  LYS   B NZ   1 
ATOM   5168 H H    . LYS   B 1 90  ? 48.738 -12.271 -10.683 1.00 15.91 ?  90  LYS   B H    1 
ATOM   5169 H HA   . LYS   B 1 90  ? 49.932 -10.110 -9.837  1.00 16.24 ?  90  LYS   B HA   1 
ATOM   5170 H HB2  . LYS   B 1 90  ? 48.322 -9.929  -11.472 1.00 18.15 ?  90  LYS   B HB2  1 
ATOM   5171 H HB3  . LYS   B 1 90  ? 47.206 -10.447 -10.470 1.00 18.15 ?  90  LYS   B HB3  1 
ATOM   5172 H HG2  . LYS   B 1 90  ? 47.035 -8.153  -10.760 1.00 18.81 ?  90  LYS   B HG2  1 
ATOM   5173 H HG3  . LYS   B 1 90  ? 47.381 -8.482  -9.246  1.00 18.81 ?  90  LYS   B HG3  1 
ATOM   5174 H HD2  . LYS   B 1 90  ? 49.570 -7.848  -9.573  1.00 21.91 ?  90  LYS   B HD2  1 
ATOM   5175 H HD3  . LYS   B 1 90  ? 49.298 -7.631  -11.132 1.00 21.91 ?  90  LYS   B HD3  1 
ATOM   5176 H HE2  . LYS   B 1 90  ? 47.864 -5.881  -10.666 1.00 24.22 ?  90  LYS   B HE2  1 
ATOM   5177 H HE3  . LYS   B 1 90  ? 48.018 -6.138  -9.104  1.00 24.22 ?  90  LYS   B HE3  1 
ATOM   5178 H HZ1  . LYS   B 1 90  ? 49.316 -4.398  -9.756  1.00 24.08 ?  90  LYS   B HZ1  1 
ATOM   5179 H HZ2  . LYS   B 1 90  ? 50.178 -5.460  -9.277  1.00 24.08 ?  90  LYS   B HZ2  1 
ATOM   5180 H HZ3  . LYS   B 1 90  ? 50.038 -5.226  -10.700 1.00 24.08 ?  90  LYS   B HZ3  1 
ATOM   5181 N N    . HIS   B 1 91  ? 47.821 -11.327 -7.760  1.00 11.59 ?  91  HIS   B N    1 
ATOM   5182 C CA   . HIS   B 1 91  ? 47.356 -11.355 -6.387  1.00 11.86 ?  91  HIS   B CA   1 
ATOM   5183 C C    . HIS   B 1 91  ? 47.357 -12.785 -5.871  1.00 11.15 ?  91  HIS   B C    1 
ATOM   5184 O O    . HIS   B 1 91  ? 47.123 -13.744 -6.621  1.00 11.90 ?  91  HIS   B O    1 
ATOM   5185 C CB   . HIS   B 1 91  ? 45.902 -10.877 -6.270  1.00 13.61 ?  91  HIS   B CB   1 
ATOM   5186 C CG   . HIS   B 1 91  ? 45.687 -9.471  -6.707  1.00 17.13 ?  91  HIS   B CG   1 
ATOM   5187 N ND1  . HIS   B 1 91  ? 46.274 -8.393  -6.079  1.00 19.52 ?  91  HIS   B ND1  1 
ATOM   5188 C CD2  . HIS   B 1 91  ? 44.916 -8.959  -7.690  1.00 19.40 ?  91  HIS   B CD2  1 
ATOM   5189 C CE1  . HIS   B 1 91  ? 45.893 -7.276  -6.673  1.00 20.43 ?  91  HIS   B CE1  1 
ATOM   5190 N NE2  . HIS   B 1 91  ? 45.059 -7.593  -7.649  1.00 20.59 ?  91  HIS   B NE2  1 
ATOM   5191 H H    . HIS   B 1 91  ? 47.404 -11.889 -8.260  1.00 13.89 ?  91  HIS   B H    1 
ATOM   5192 H HA   . HIS   B 1 91  ? 47.922 -10.799 -5.820  1.00 14.22 ?  91  HIS   B HA   1 
ATOM   5193 H HB2  . HIS   B 1 91  ? 45.341 -11.445 -6.822  1.00 16.32 ?  91  HIS   B HB2  1 
ATOM   5194 H HB3  . HIS   B 1 91  ? 45.620 -10.946 -5.341  1.00 16.32 ?  91  HIS   B HB3  1 
ATOM   5195 H HD1  . HIS   B 1 91  ? 46.813 -8.442  -5.407  1.00 23.41 ?  91  HIS   B HD1  1 
ATOM   5196 H HD2  . HIS   B 1 91  ? 44.393 -9.430  -8.292  1.00 23.27 ?  91  HIS   B HD2  1 
ATOM   5197 H HE1  . HIS   B 1 91  ? 46.161 -6.414  -6.432  1.00 24.50 ?  91  HIS   B HE1  1 
ATOM   5198 N N    . CYS   B 1 92  ? 47.547 -12.912 -4.566  1.00 11.08 ?  92  CYS   B N    1 
ATOM   5199 C CA   . CYS   B 1 92  ? 47.245 -14.148 -3.856  1.00 10.80 ?  92  CYS   B CA   1 
ATOM   5200 C C    . CYS   B 1 92  ? 46.027 -13.915 -2.971  1.00 10.65 ?  92  CYS   B C    1 
ATOM   5201 O O    . CYS   B 1 92  ? 46.030 -13.018 -2.117  1.00 11.43 ?  92  CYS   B O    1 
ATOM   5202 C CB   . CYS   B 1 92  ? 48.424 -14.608 -3.003  1.00 11.40 ?  92  CYS   B CB   1 
ATOM   5203 S SG   . CYS   B 1 92  ? 48.071 -16.143 -2.106  1.00 11.35 ?  92  CYS   B SG   1 
ATOM   5204 H H    . CYS   B 1 92  ? 47.863 -12.292 -4.056  1.00 13.28 ?  92  CYS   B H    1 
ATOM   5205 H HA   . CYS   B 1 92  ? 47.045 -14.847 -4.498  1.00 12.95 ?  92  CYS   B HA   1 
ATOM   5206 H HB2  . CYS   B 1 92  ? 49.190 -14.758 -3.572  1.00 13.66 ?  92  CYS   B HB2  1 
ATOM   5207 H HB3  . CYS   B 1 92  ? 48.620 -13.921 -2.346  1.00 13.66 ?  92  CYS   B HB3  1 
ATOM   5208 H HG   . CYS   B 1 92  ? 49.045 -16.457 -1.481  1.00 13.61 ?  92  CYS   B HG   1 
ATOM   5209 N N    . LEU   B 1 93  ? 44.989 -14.720 -3.185  1.00 10.43 ?  93  LEU   B N    1 
ATOM   5210 C CA   . LEU   B 1 93  ? 43.815 -14.741 -2.322  1.00 10.65 ?  93  LEU   B CA   1 
ATOM   5211 C C    . LEU   B 1 93  ? 44.039 -15.807 -1.259  1.00 10.20 ?  93  LEU   B C    1 
ATOM   5212 O O    . LEU   B 1 93  ? 43.989 -17.012 -1.552  1.00 10.84 ?  93  LEU   B O    1 
ATOM   5213 C CB   . LEU   B 1 93  ? 42.554 -15.033 -3.130  1.00 11.03 ?  93  LEU   B CB   1 
ATOM   5214 C CG   . LEU   B 1 93  ? 41.257 -15.055 -2.323  1.00 11.89 ?  93  LEU   B CG   1 
ATOM   5215 C CD1  . LEU   B 1 93  ? 40.900 -13.666 -1.824  1.00 12.11 ?  93  LEU   B CD1  1 
ATOM   5216 C CD2  . LEU   B 1 93  ? 40.132 -15.652 -3.152  1.00 12.22 ?  93  LEU   B CD2  1 
ATOM   5217 H H    . LEU   B 1 93  ? 44.941 -15.287 -3.842  1.00 12.50 ?  93  LEU   B H    1 
ATOM   5218 H HA   . LEU   B 1 93  ? 43.718 -13.877 -1.890  1.00 12.77 ?  93  LEU   B HA   1 
ATOM   5219 H HB2  . LEU   B 1 93  ? 42.459 -14.345 -3.811  1.00 13.22 ?  93  LEU   B HB2  1 
ATOM   5220 H HB3  . LEU   B 1 93  ? 42.650 -15.897 -3.551  1.00 13.22 ?  93  LEU   B HB3  1 
ATOM   5221 H HG   . LEU   B 1 93  ? 41.383 -15.619 -1.545  1.00 14.26 ?  93  LEU   B HG   1 
ATOM   5222 H HD11 . LEU   B 1 93  ? 40.048 -13.701 -1.369  1.00 14.52 ?  93  LEU   B HD11 1 
ATOM   5223 H HD12 . LEU   B 1 93  ? 41.591 -13.359 -1.214  1.00 14.52 ?  93  LEU   B HD12 1 
ATOM   5224 H HD13 . LEU   B 1 93  ? 40.846 -13.062 -2.585  1.00 14.52 ?  93  LEU   B HD13 1 
ATOM   5225 H HD21 . LEU   B 1 93  ? 39.317 -15.653 -2.623  1.00 14.65 ?  93  LEU   B HD21 1 
ATOM   5226 H HD22 . LEU   B 1 93  ? 40.005 -15.113 -3.949  1.00 14.65 ?  93  LEU   B HD22 1 
ATOM   5227 H HD23 . LEU   B 1 93  ? 40.367 -16.559 -3.399  1.00 14.65 ?  93  LEU   B HD23 1 
ATOM   5228 N N    . HIS   B 1 94  ? 44.316 -15.368 -0.036  1.00 10.08 ?  94  HIS   B N    1 
ATOM   5229 C CA   . HIS   B 1 94  ? 44.537 -16.275 1.085   1.00 10.40 ?  94  HIS   B CA   1 
ATOM   5230 C C    . HIS   B 1 94  ? 43.177 -16.636 1.663   1.00 10.89 ?  94  HIS   B C    1 
ATOM   5231 O O    . HIS   B 1 94  ? 42.498 -15.766 2.216   1.00 12.35 ?  94  HIS   B O    1 
ATOM   5232 C CB   . HIS   B 1 94  ? 45.410 -15.601 2.145   1.00 10.89 ?  94  HIS   B CB   1 
ATOM   5233 C CG   . HIS   B 1 94  ? 46.795 -15.299 1.675   1.00 10.82 ?  94  HIS   B CG   1 
ATOM   5234 N ND1  . HIS   B 1 94  ? 47.824 -16.211 1.760   1.00 11.14 ?  94  HIS   B ND1  1 
ATOM   5235 C CD2  . HIS   B 1 94  ? 47.303 -14.191 1.083   1.00 10.91 ?  94  HIS   B CD2  1 
ATOM   5236 C CE1  . HIS   B 1 94  ? 48.912 -15.663 1.251   1.00 11.12 ?  94  HIS   B CE1  1 
ATOM   5237 N NE2  . HIS   B 1 94  ? 48.625 -14.441 0.835   1.00 11.18 ?  94  HIS   B NE2  1 
ATOM   5238 H H    . HIS   B 1 94  ? 44.385 -14.531 0.176   1.00 12.08 ?  94  HIS   B H    1 
ATOM   5239 H HA   . HIS   B 1 94  ? 44.977 -17.083 0.776   1.00 12.47 ?  94  HIS   B HA   1 
ATOM   5240 H HB2  . HIS   B 1 94  ? 44.995 -14.764 2.403   1.00 13.05 ?  94  HIS   B HB2  1 
ATOM   5241 H HB3  . HIS   B 1 94  ? 45.477 -16.189 2.911   1.00 13.05 ?  94  HIS   B HB3  1 
ATOM   5242 H HD2  . HIS   B 1 94  ? 46.846 -13.408 0.888   1.00 13.08 ?  94  HIS   B HD2  1 
ATOM   5243 H HE1  . HIS   B 1 94  ? 49.747 -16.077 1.192   1.00 13.33 ?  94  HIS   B HE1  1 
ATOM   5244 H HE2  . HIS   B 1 94  ? 49.182 -13.898 0.468   1.00 13.40 ?  94  HIS   B HE2  1 
ATOM   5245 N N    . VAL   B 1 95  ? 42.748 -17.892 1.508   1.00 10.84 ?  95  VAL   B N    1 
ATOM   5246 C CA   . VAL   B 1 95  ? 41.424 -18.334 1.942   1.00 10.78 ?  95  VAL   B CA   1 
ATOM   5247 C C    . VAL   B 1 95  ? 41.594 -19.376 3.036   1.00 10.77 ?  95  VAL   B C    1 
ATOM   5248 O O    . VAL   B 1 95  ? 42.360 -20.333 2.873   1.00 11.74 ?  95  VAL   B O    1 
ATOM   5249 C CB   . VAL   B 1 95  ? 40.606 -18.942 0.786   1.00 11.03 ?  95  VAL   B CB   1 
ATOM   5250 C CG1  . VAL   B 1 95  ? 39.226 -19.372 1.271   1.00 12.54 ?  95  VAL   B CG1  1 
ATOM   5251 C CG2  . VAL   B 1 95  ? 40.482 -17.964 -0.363  1.00 11.34 ?  95  VAL   B CG2  1 
ATOM   5252 H H    . VAL   B 1 95  ? 43.212 -18.515 1.140   1.00 13.00 ?  95  VAL   B H    1 
ATOM   5253 H HA   . VAL   B 1 95  ? 40.928 -17.583 2.307   1.00 12.93 ?  95  VAL   B HA   1 
ATOM   5254 H HB   . VAL   B 1 95  ? 41.065 -19.728 0.454   1.00 13.23 ?  95  VAL   B HB   1 
ATOM   5255 H HG11 . VAL   B 1 95  ? 38.668 -19.570 0.497   1.00 15.04 ?  95  VAL   B HG11 1 
ATOM   5256 H HG12 . VAL   B 1 95  ? 39.312 -20.165 1.821   1.00 15.04 ?  95  VAL   B HG12 1 
ATOM   5257 H HG13 . VAL   B 1 95  ? 38.829 -18.651 1.782   1.00 15.04 ?  95  VAL   B HG13 1 
ATOM   5258 H HG21 . VAL   B 1 95  ? 39.913 -18.353 -1.044  1.00 13.60 ?  95  VAL   B HG21 1 
ATOM   5259 H HG22 . VAL   B 1 95  ? 40.086 -17.142 -0.030  1.00 13.60 ?  95  VAL   B HG22 1 
ATOM   5260 H HG23 . VAL   B 1 95  ? 41.362 -17.788 -0.721  1.00 13.60 ?  95  VAL   B HG23 1 
ATOM   5261 N N    . VAL   B 1 96  ? 40.857 -19.210 4.131   1.00 11.29 ?  96  VAL   B N    1 
ATOM   5262 C CA   . VAL   B 1 96  ? 40.938 -20.126 5.269   1.00 11.65 ?  96  VAL   B CA   1 
ATOM   5263 C C    . VAL   B 1 96  ? 39.751 -21.087 5.224   1.00 12.31 ?  96  VAL   B C    1 
ATOM   5264 O O    . VAL   B 1 96  ? 38.633 -20.731 5.613   1.00 12.70 ?  96  VAL   B O    1 
ATOM   5265 C CB   . VAL   B 1 96  ? 40.983 -19.379 6.603   1.00 12.21 ?  96  VAL   B CB   1 
ATOM   5266 C CG1  . VAL   B 1 96  ? 41.172 -20.369 7.747   1.00 13.27 ?  96  VAL   B CG1  1 
ATOM   5267 C CG2  . VAL   B 1 96  ? 42.081 -18.321 6.602   1.00 13.41 ?  96  VAL   B CG2  1 
ATOM   5268 H H    . VAL   B 1 96  ? 40.298 -18.568 4.244   1.00 13.54 ?  96  VAL   B H    1 
ATOM   5269 H HA   . VAL   B 1 96  ? 41.755 -20.652 5.195   1.00 13.96 ?  96  VAL   B HA   1 
ATOM   5270 H HB   . VAL   B 1 96  ? 40.136 -18.931 6.740   1.00 14.65 ?  96  VAL   B HB   1 
ATOM   5271 H HG11 . VAL   B 1 96  ? 41.356 -19.878 8.566   1.00 15.91 ?  96  VAL   B HG11 1 
ATOM   5272 H HG12 . VAL   B 1 96  ? 40.368 -20.897 7.855   1.00 15.91 ?  96  VAL   B HG12 1 
ATOM   5273 H HG13 . VAL   B 1 96  ? 41.926 -20.951 7.544   1.00 15.91 ?  96  VAL   B HG13 1 
ATOM   5274 H HG21 . VAL   B 1 96  ? 42.139 -17.920 7.485   1.00 16.08 ?  96  VAL   B HG21 1 
ATOM   5275 H HG22 . VAL   B 1 96  ? 42.925 -18.734 6.371   1.00 16.08 ?  96  VAL   B HG22 1 
ATOM   5276 H HG23 . VAL   B 1 96  ? 41.859 -17.635 5.948   1.00 16.08 ?  96  VAL   B HG23 1 
ATOM   5277 N N    . GLY   B 1 97  ? 39.985 -22.321 4.777   1.00 12.29 ?  97  GLY   B N    1 
ATOM   5278 C CA   . GLY   B 1 97  ? 39.013 -23.380 4.942   1.00 12.68 ?  97  GLY   B CA   1 
ATOM   5279 C C    . GLY   B 1 97  ? 39.133 -23.986 6.324   1.00 13.61 ?  97  GLY   B C    1 
ATOM   5280 O O    . GLY   B 1 97  ? 40.170 -23.860 6.986   1.00 14.26 ?  97  GLY   B O    1 
ATOM   5281 H H    . GLY   B 1 97  ? 40.710 -22.565 4.373   1.00 14.74 ?  97  GLY   B H    1 
ATOM   5282 H HA2  . GLY   B 1 97  ? 38.120 -23.015 4.824   1.00 15.21 ?  97  GLY   B HA2  1 
ATOM   5283 H HA3  . GLY   B 1 97  ? 39.158 -24.068 4.274   1.00 15.21 ?  97  GLY   B HA3  1 
ATOM   5284 N N    . PRO   B 1 98  ? 38.087 -24.670 6.785   1.00 14.49 ?  98  PRO   B N    1 
ATOM   5285 C CA   . PRO   B 1 98  ? 38.180 -25.368 8.070   1.00 15.25 ?  98  PRO   B CA   1 
ATOM   5286 C C    . PRO   B 1 98  ? 39.206 -26.488 8.024   1.00 14.96 ?  98  PRO   B C    1 
ATOM   5287 O O    . PRO   B 1 98  ? 39.313 -27.222 7.043   1.00 15.11 ?  98  PRO   B O    1 
ATOM   5288 C CB   . PRO   B 1 98  ? 36.762 -25.912 8.278   1.00 15.51 ?  98  PRO   B CB   1 
ATOM   5289 C CG   . PRO   B 1 98  ? 36.202 -26.048 6.903   1.00 15.28 ?  98  PRO   B CG   1 
ATOM   5290 C CD   . PRO   B 1 98  ? 36.776 -24.875 6.139   1.00 14.59 ?  98  PRO   B CD   1 
ATOM   5291 H HA   . PRO   B 1 98  ? 38.402 -24.751 8.777   1.00 18.29 ?  98  PRO   B HA   1 
ATOM   5292 H HB2  . PRO   B 1 98  ? 36.803 -26.779 8.718   1.00 18.60 ?  98  PRO   B HB2  1 
ATOM   5293 H HB3  . PRO   B 1 98  ? 36.241 -25.286 8.798   1.00 18.60 ?  98  PRO   B HB3  1 
ATOM   5294 H HG2  . PRO   B 1 98  ? 36.491 -26.893 6.513   1.00 18.32 ?  98  PRO   B HG2  1 
ATOM   5295 H HG3  . PRO   B 1 98  ? 35.235 -26.002 6.936   1.00 18.32 ?  98  PRO   B HG3  1 
ATOM   5296 H HD2  . PRO   B 1 98  ? 36.886 -25.108 5.199   1.00 17.50 ?  98  PRO   B HD2  1 
ATOM   5297 H HD3  . PRO   B 1 98  ? 36.219 -24.094 6.249   1.00 17.50 ?  98  PRO   B HD3  1 
ATOM   5298 N N    . ASN   B 1 99  ? 39.955 -26.617 9.110   1.00 15.83 ?  99  ASN   B N    1 
ATOM   5299 C CA   . ASN   B 1 99  ? 40.932 -27.690 9.274   1.00 16.82 ?  99  ASN   B CA   1 
ATOM   5300 C C    . ASN   B 1 99  ? 40.298 -28.773 10.148  1.00 19.28 ?  99  ASN   B C    1 
ATOM   5301 O O    . ASN   B 1 99  ? 40.207 -28.624 11.369  1.00 19.50 ?  99  ASN   B O    1 
ATOM   5302 C CB   . ASN   B 1 99  ? 42.205 -27.132 9.898   1.00 17.20 ?  99  ASN   B CB   1 
ATOM   5303 C CG   . ASN   B 1 99  ? 43.338 -28.139 9.910   1.00 18.38 ?  99  ASN   B CG   1 
ATOM   5304 O OD1  . ASN   B 1 99  ? 43.117 -29.333 10.079  1.00 19.08 ?  99  ASN   B OD1  1 
ATOM   5305 N ND2  . ASN   B 1 99  ? 44.556 -27.660 9.726   1.00 18.46 ?  99  ASN   B ND2  1 
ATOM   5306 H H    . ASN   B 1 99  ? 39.915 -26.083 9.778   1.00 18.98 ?  99  ASN   B H    1 
ATOM   5307 H HA   . ASN   B 1 99  ? 41.147 -28.077 8.412   1.00 20.17 ?  99  ASN   B HA   1 
ATOM   5308 H HB2  . ASN   B 1 99  ? 42.489 -26.362 9.392   1.00 20.63 ?  99  ASN   B HB2  1 
ATOM   5309 H HB3  . ASN   B 1 99  ? 42.015 -26.878 10.818  1.00 20.63 ?  99  ASN   B HB3  1 
ATOM   5310 H HD21 . ASN   B 1 99  ? 45.230 -28.191 9.723   1.00 22.14 ?  99  ASN   B HD21 1 
ATOM   5311 H HD22 . ASN   B 1 99  ? 44.668 -26.816 9.613   1.00 22.14 ?  99  ASN   B HD22 1 
ATOM   5312 N N    A VAL   B 1 100 ? 39.841 -29.858 9.515   0.60 21.19 ?  100 VAL   B N    1 
ATOM   5313 N N    B VAL   B 1 100 ? 39.846 -29.856 9.509   0.40 21.29 ?  100 VAL   B N    1 
ATOM   5314 C CA   A VAL   B 1 100 ? 39.220 -30.950 10.263  0.60 23.93 ?  100 VAL   B CA   1 
ATOM   5315 C CA   B VAL   B 1 100 ? 39.223 -30.961 10.235  0.40 23.78 ?  100 VAL   B CA   1 
ATOM   5316 C C    A VAL   B 1 100 ? 40.223 -31.603 11.203  0.60 24.37 ?  100 VAL   B C    1 
ATOM   5317 C C    B VAL   B 1 100 ? 40.216 -31.624 11.179  0.40 24.35 ?  100 VAL   B C    1 
ATOM   5318 O O    A VAL   B 1 100 ? 39.854 -32.080 12.283  0.60 25.06 ?  100 VAL   B O    1 
ATOM   5319 O O    B VAL   B 1 100 ? 39.832 -32.130 12.241  0.40 24.77 ?  100 VAL   B O    1 
ATOM   5320 C CB   A VAL   B 1 100 ? 38.579 -31.968 9.298   0.60 26.38 ?  100 VAL   B CB   1 
ATOM   5321 C CB   B VAL   B 1 100 ? 38.604 -31.965 9.240   0.40 25.70 ?  100 VAL   B CB   1 
ATOM   5322 C CG1  A VAL   B 1 100 ? 38.115 -33.208 10.052  0.60 27.30 ?  100 VAL   B CG1  1 
ATOM   5323 C CG1  B VAL   B 1 100 ? 38.121 -33.215 9.962   0.40 26.43 ?  100 VAL   B CG1  1 
ATOM   5324 C CG2  A VAL   B 1 100 ? 37.414 -31.331 8.557   0.60 26.96 ?  100 VAL   B CG2  1 
ATOM   5325 C CG2  B VAL   B 1 100 ? 37.459 -31.315 8.478   0.40 26.21 ?  100 VAL   B CG2  1 
ATOM   5326 H H    A VAL   B 1 100 ? 39.868 -29.980 8.663   0.60 25.42 ?  100 VAL   B H    1 
ATOM   5327 H H    B VAL   B 1 100 ? 39.878 -29.969 8.657   0.40 25.53 ?  100 VAL   B H    1 
ATOM   5328 H HA   A VAL   B 1 100 ? 38.504 -30.584 10.806  0.60 28.71 ?  100 VAL   B HA   1 
ATOM   5329 H HA   B VAL   B 1 100 ? 38.497 -30.609 10.774  0.40 28.52 ?  100 VAL   B HA   1 
ATOM   5330 H HB   A VAL   B 1 100 ? 39.238 -32.245 8.644   0.60 31.64 ?  100 VAL   B HB   1 
ATOM   5331 H HB   B VAL   B 1 100 ? 39.278 -32.234 8.597   0.40 30.83 ?  100 VAL   B HB   1 
ATOM   5332 H HG11 A VAL   B 1 100 ? 37.516 -33.718 9.481   0.60 32.74 ?  100 VAL   B HG11 1 
ATOM   5333 H HG11 B VAL   B 1 100 ? 37.538 -33.717 9.369   0.40 31.70 ?  100 VAL   B HG11 1 
ATOM   5334 H HG12 A VAL   B 1 100 ? 38.886 -33.751 10.282  0.60 32.74 ?  100 VAL   B HG12 1 
ATOM   5335 H HG12 B VAL   B 1 100 ? 38.886 -33.759 10.206  0.40 31.70 ?  100 VAL   B HG12 1 
ATOM   5336 H HG13 A VAL   B 1 100 ? 37.647 -32.936 10.857  0.60 32.74 ?  100 VAL   B HG13 1 
ATOM   5337 H HG13 B VAL   B 1 100 ? 37.631 -32.953 10.757  0.40 31.70 ?  100 VAL   B HG13 1 
ATOM   5338 H HG21 A VAL   B 1 100 ? 37.034 -31.985 7.948   0.60 32.34 ?  100 VAL   B HG21 1 
ATOM   5339 H HG21 B VAL   B 1 100 ? 37.080 -31.963 7.864   0.40 31.44 ?  100 VAL   B HG21 1 
ATOM   5340 H HG22 A VAL   B 1 100 ? 36.744 -31.053 9.202   0.60 32.34 ?  100 VAL   B HG22 1 
ATOM   5341 H HG22 B VAL   B 1 100 ? 36.784 -31.026 9.112   0.40 31.44 ?  100 VAL   B HG22 1 
ATOM   5342 H HG23 A VAL   B 1 100 ? 37.737 -30.565 8.062   0.60 32.34 ?  100 VAL   B HG23 1 
ATOM   5343 H HG23 B VAL   B 1 100 ? 37.801 -30.553 7.987   0.40 31.44 ?  100 VAL   B HG23 1 
ATOM   5344 N N    . ASN   B 1 101 ? 41.500 -31.648 10.812  1.00 24.77 ?  101 ASN   B N    1 
ATOM   5345 C CA   . ASN   B 1 101 ? 42.529 -32.184 11.701  1.00 27.06 ?  101 ASN   B CA   1 
ATOM   5346 C C    . ASN   B 1 101 ? 42.704 -31.342 12.959  1.00 29.66 ?  101 ASN   B C    1 
ATOM   5347 O O    . ASN   B 1 101 ? 43.321 -31.814 13.922  1.00 30.58 ?  101 ASN   B O    1 
ATOM   5348 C CB   . ASN   B 1 101 ? 43.861 -32.326 10.958  1.00 26.81 ?  101 ASN   B CB   1 
ATOM   5349 C CG   . ASN   B 1 101 ? 43.846 -33.459 9.951   1.00 26.51 ?  101 ASN   B CG   1 
ATOM   5350 O OD1  . ASN   B 1 101 ? 43.174 -34.464 10.151  1.00 27.42 ?  101 ASN   B OD1  1 
ATOM   5351 N ND2  . ASN   B 1 101 ? 44.582 -33.297 8.859   1.00 25.97 ?  101 ASN   B ND2  1 
ATOM   5352 H H    A ASN   B 1 101 ? 41.784 -31.390 10.041  0.60 29.71 ?  101 ASN   B H    1 
ATOM   5353 H H    B ASN   B 1 101 ? 41.792 -31.370 10.052  0.40 29.71 ?  101 ASN   B H    1 
ATOM   5354 H HA   . ASN   B 1 101 ? 42.258 -33.068 11.980  1.00 32.46 ?  101 ASN   B HA   1 
ATOM   5355 H HB2  . ASN   B 1 101 ? 44.056 -31.507 10.479  1.00 32.16 ?  101 ASN   B HB2  1 
ATOM   5356 H HB3  . ASN   B 1 101 ? 44.565 -32.507 11.603  1.00 32.16 ?  101 ASN   B HB3  1 
ATOM   5357 H HD21 . ASN   B 1 101 ? 44.605 -33.916 8.261   1.00 31.15 ?  101 ASN   B HD21 1 
ATOM   5358 H HD22 . ASN   B 1 101 ? 45.036 -32.577 8.749   1.00 31.15 ?  101 ASN   B HD22 1 
ATOM   5359 N N    A LYS   B 1 102 ? 42.202 -30.107 12.961  0.60 31.21 ?  102 LYS   B N    1 
ATOM   5360 N N    B LYS   B 1 102 ? 42.176 -30.117 12.975  0.40 31.24 ?  102 LYS   B N    1 
ATOM   5361 C CA   A LYS   B 1 102 ? 42.203 -29.247 14.137  0.60 33.12 ?  102 LYS   B CA   1 
ATOM   5362 C CA   B LYS   B 1 102 ? 42.124 -29.292 14.174  0.40 33.01 ?  102 LYS   B CA   1 
ATOM   5363 C C    A LYS   B 1 102 ? 40.843 -29.204 14.823  0.60 32.49 ?  102 LYS   B C    1 
ATOM   5364 C C    B LYS   B 1 102 ? 40.744 -29.279 14.821  0.40 32.54 ?  102 LYS   B C    1 
ATOM   5365 O O    A LYS   B 1 102 ? 40.650 -28.403 15.743  0.60 32.95 ?  102 LYS   B O    1 
ATOM   5366 O O    B LYS   B 1 102 ? 40.536 -28.541 15.788  0.40 32.84 ?  102 LYS   B O    1 
ATOM   5367 C CB   A LYS   B 1 102 ? 42.612 -27.822 13.758  0.60 35.81 ?  102 LYS   B CB   1 
ATOM   5368 C CB   B LYS   B 1 102 ? 42.536 -27.851 13.852  0.40 35.28 ?  102 LYS   B CB   1 
ATOM   5369 C CG   A LYS   B 1 102 ? 44.082 -27.633 13.425  0.60 38.42 ?  102 LYS   B CG   1 
ATOM   5370 C CG   B LYS   B 1 102 ? 43.991 -27.676 13.455  0.40 37.44 ?  102 LYS   B CG   1 
ATOM   5371 C CD   A LYS   B 1 102 ? 44.355 -26.178 13.064  0.60 40.71 ?  102 LYS   B CD   1 
ATOM   5372 C CD   B LYS   B 1 102 ? 44.264 -26.240 13.037  0.40 39.32 ?  102 LYS   B CD   1 
ATOM   5373 C CE   A LYS   B 1 102 ? 45.829 -25.920 12.801  0.60 42.39 ?  102 LYS   B CE   1 
ATOM   5374 C CE   B LYS   B 1 102 ? 45.740 -26.002 12.770  0.40 40.69 ?  102 LYS   B CE   1 
ATOM   5375 N NZ   A LYS   B 1 102 ? 46.079 -24.499 12.419  0.60 43.37 ?  102 LYS   B NZ   1 
ATOM   5376 N NZ   B LYS   B 1 102 ? 45.995 -24.601 12.331  0.40 41.48 ?  102 LYS   B NZ   1 
ATOM   5377 H H    A LYS   B 1 102 ? 41.842 -29.737 12.273  0.60 37.44 ?  102 LYS   B H    1 
ATOM   5378 H H    B LYS   B 1 102 ? 41.834 -29.735 12.283  0.40 37.48 ?  102 LYS   B H    1 
ATOM   5379 H HA   A LYS   B 1 102 ? 42.858 -29.584 14.770  0.60 39.74 ?  102 LYS   B HA   1 
ATOM   5380 H HA   B LYS   B 1 102 ? 42.755 -29.642 14.821  0.40 39.60 ?  102 LYS   B HA   1 
ATOM   5381 H HB2  A LYS   B 1 102 ? 42.099 -27.552 12.982  0.60 42.96 ?  102 LYS   B HB2  1 
ATOM   5382 H HB2  B LYS   B 1 102 ? 41.991 -27.528 13.118  0.40 42.33 ?  102 LYS   B HB2  1 
ATOM   5383 H HB3  A LYS   B 1 102 ? 42.406 -27.235 14.503  0.60 42.96 ?  102 LYS   B HB3  1 
ATOM   5384 H HB3  B LYS   B 1 102 ? 42.380 -27.302 14.638  0.40 42.33 ?  102 LYS   B HB3  1 
ATOM   5385 H HG2  A LYS   B 1 102 ? 44.623 -27.866 14.196  0.60 46.09 ?  102 LYS   B HG2  1 
ATOM   5386 H HG2  B LYS   B 1 102 ? 44.561 -27.888 14.211  0.40 44.92 ?  102 LYS   B HG2  1 
ATOM   5387 H HG3  A LYS   B 1 102 ? 44.316 -28.188 12.665  0.60 46.09 ?  102 LYS   B HG3  1 
ATOM   5388 H HG3  B LYS   B 1 102 ? 44.194 -28.257 12.705  0.40 44.92 ?  102 LYS   B HG3  1 
ATOM   5389 H HD2  A LYS   B 1 102 ? 43.860 -25.952 12.261  0.60 48.83 ?  102 LYS   B HD2  1 
ATOM   5390 H HD2  B LYS   B 1 102 ? 43.772 -26.045 12.223  0.40 47.17 ?  102 LYS   B HD2  1 
ATOM   5391 H HD3  A LYS   B 1 102 ? 44.074 -25.610 13.799  0.60 48.83 ?  102 LYS   B HD3  1 
ATOM   5392 H HD3  B LYS   B 1 102 ? 43.983 -25.641 13.748  0.40 47.17 ?  102 LYS   B HD3  1 
ATOM   5393 H HE2  A LYS   B 1 102 ? 46.336 -26.112 13.606  0.60 50.86 ?  102 LYS   B HE2  1 
ATOM   5394 H HE2  B LYS   B 1 102 ? 46.243 -26.162 13.584  0.40 48.82 ?  102 LYS   B HE2  1 
ATOM   5395 H HE3  A LYS   B 1 102 ? 46.128 -26.487 12.073  0.60 50.86 ?  102 LYS   B HE3  1 
ATOM   5396 H HE3  B LYS   B 1 102 ? 46.039 -26.600 12.067  0.40 48.82 ?  102 LYS   B HE3  1 
ATOM   5397 H HZ1  A LYS   B 1 102 ? 46.947 -24.372 12.270  0.60 52.03 ?  102 LYS   B HZ1  1 
ATOM   5398 H HZ1  B LYS   B 1 102 ? 46.864 -24.483 12.180  0.40 49.77 ?  102 LYS   B HZ1  1 
ATOM   5399 H HZ2  A LYS   B 1 102 ? 45.627 -24.299 11.679  0.60 52.03 ?  102 LYS   B HZ2  1 
ATOM   5400 H HZ2  B LYS   B 1 102 ? 45.546 -24.431 11.582  0.40 49.77 ?  102 LYS   B HZ2  1 
ATOM   5401 H HZ3  A LYS   B 1 102 ? 45.816 -23.957 13.074  0.60 52.03 ?  102 LYS   B HZ3  1 
ATOM   5402 H HZ3  B LYS   B 1 102 ? 45.731 -24.032 12.962  0.40 49.77 ?  102 LYS   B HZ3  1 
ATOM   5403 N N    A GLY   B 1 103 ? 39.893 -30.026 14.385  0.60 31.63 ?  103 GLY   B N    1 
ATOM   5404 N N    B GLY   B 1 103 ? 39.798 -30.063 14.308  0.40 31.82 ?  103 GLY   B N    1 
ATOM   5405 C CA   A GLY   B 1 103 ? 38.570 -30.055 14.972  0.60 31.33 ?  103 GLY   B CA   1 
ATOM   5406 C CA   B GLY   B 1 103 ? 38.469 -30.119 14.882  0.40 31.24 ?  103 GLY   B CA   1 
ATOM   5407 C C    A GLY   B 1 103 ? 37.621 -28.989 14.469  0.60 30.50 ?  103 GLY   B C    1 
ATOM   5408 C C    B GLY   B 1 103 ? 37.530 -29.018 14.445  0.40 30.31 ?  103 GLY   B C    1 
ATOM   5409 O O    A GLY   B 1 103 ? 36.490 -28.907 14.969  0.60 31.09 ?  103 GLY   B O    1 
ATOM   5410 O O    B GLY   B 1 103 ? 36.484 -28.832 15.077  0.40 30.71 ?  103 GLY   B O    1 
ATOM   5411 H H    A GLY   B 1 103 ? 39.996 -30.580 13.737  0.60 37.95 ?  103 GLY   B H    1 
ATOM   5412 H H    B GLY   B 1 103 ? 39.907 -30.574 13.625  0.40 38.17 ?  103 GLY   B H    1 
ATOM   5413 H HA2  A GLY   B 1 103 ? 38.169 -30.919 14.795  0.60 37.59 ?  103 GLY   B HA2  1 
ATOM   5414 H HA2  B GLY   B 1 103 ? 38.062 -30.967 14.647  0.40 37.48 ?  103 GLY   B HA2  1 
ATOM   5415 H HA3  A GLY   B 1 103 ? 38.653 -29.956 15.935  0.60 37.59 ?  103 GLY   B HA3  1 
ATOM   5416 H HA3  B GLY   B 1 103 ? 38.543 -30.082 15.849  0.40 37.48 ?  103 GLY   B HA3  1 
ATOM   5417 N N    A GLU   B 1 104 ? 38.032 -28.178 13.500  0.60 28.89 ?  104 GLU   B N    1 
ATOM   5418 N N    B GLU   B 1 104 ? 37.861 -28.286 13.385  0.40 28.75 ?  104 GLU   B N    1 
ATOM   5419 C CA   A GLU   B 1 104 ? 37.187 -27.094 13.025  0.60 27.18 ?  104 GLU   B CA   1 
ATOM   5420 C CA   B GLU   B 1 104 ? 37.028 -27.180 12.941  0.40 27.19 ?  104 GLU   B CA   1 
ATOM   5421 C C    A GLU   B 1 104 ? 36.009 -27.641 12.218  0.60 27.79 ?  104 GLU   B C    1 
ATOM   5422 C C    B GLU   B 1 104 ? 35.873 -27.687 12.084  0.40 27.32 ?  104 GLU   B C    1 
ATOM   5423 O O    A GLU   B 1 104 ? 36.051 -28.744 11.665  0.60 28.79 ?  104 GLU   B O    1 
ATOM   5424 O O    B GLU   B 1 104 ? 35.968 -28.723 11.420  0.40 27.68 ?  104 GLU   B O    1 
ATOM   5425 C CB   A GLU   B 1 104 ? 38.016 -26.100 12.211  0.60 25.90 ?  104 GLU   B CB   1 
ATOM   5426 C CB   B GLU   B 1 104 ? 37.872 -26.162 12.174  0.40 25.90 ?  104 GLU   B CB   1 
ATOM   5427 C CG   A GLU   B 1 104 ? 39.121 -25.460 13.041  0.60 24.79 ?  104 GLU   B CG   1 
ATOM   5428 C CG   B GLU   B 1 104 ? 38.977 -25.568 13.036  0.40 24.79 ?  104 GLU   B CG   1 
ATOM   5429 C CD   A GLU   B 1 104 ? 40.061 -24.586 12.239  0.60 23.41 ?  104 GLU   B CD   1 
ATOM   5430 C CD   B GLU   B 1 104 ? 39.931 -24.670 12.275  0.40 23.76 ?  104 GLU   B CD   1 
ATOM   5431 O OE1  A GLU   B 1 104 ? 40.043 -24.645 10.991  0.60 21.35 ?  104 GLU   B OE1  1 
ATOM   5432 O OE1  B GLU   B 1 104 ? 39.899 -24.657 11.026  0.40 22.98 ?  104 GLU   B OE1  1 
ATOM   5433 O OE2  A GLU   B 1 104 ? 40.827 -23.833 12.874  0.60 24.36 -1 104 GLU   B OE2  1 
ATOM   5434 O OE2  B GLU   B 1 104 ? 40.721 -23.971 12.942  0.40 23.72 -1 104 GLU   B OE2  1 
ATOM   5435 H H    A GLU   B 1 104 ? 38.796 -28.231 13.110  0.60 34.66 ?  104 GLU   B H    1 
ATOM   5436 H H    B GLU   B 1 104 ? 38.566 -28.409 12.910  0.40 34.49 ?  104 GLU   B H    1 
ATOM   5437 H HA   A GLU   B 1 104 ? 36.830 -26.619 13.792  0.60 32.60 ?  104 GLU   B HA   1 
ATOM   5438 H HA   B GLU   B 1 104 ? 36.656 -26.735 13.719  0.40 32.62 ?  104 GLU   B HA   1 
ATOM   5439 H HB2  A GLU   B 1 104 ? 38.430 -26.562 11.466  0.60 31.06 ?  104 GLU   B HB2  1 
ATOM   5440 H HB2  B GLU   B 1 104 ? 38.283 -26.600 11.413  0.40 31.06 ?  104 GLU   B HB2  1 
ATOM   5441 H HB3  A GLU   B 1 104 ? 37.437 -25.393 11.885  0.60 31.06 ?  104 GLU   B HB3  1 
ATOM   5442 H HB3  B GLU   B 1 104 ? 37.300 -25.438 11.874  0.40 31.06 ?  104 GLU   B HB3  1 
ATOM   5443 H HG2  A GLU   B 1 104 ? 38.719 -24.903 13.727  0.60 29.74 ?  104 GLU   B HG2  1 
ATOM   5444 H HG2  B GLU   B 1 104 ? 38.574 -25.036 13.741  0.40 29.74 ?  104 GLU   B HG2  1 
ATOM   5445 H HG3  A GLU   B 1 104 ? 39.652 -26.157 13.457  0.60 29.74 ?  104 GLU   B HG3  1 
ATOM   5446 H HG3  B GLU   B 1 104 ? 39.496 -26.289 13.426  0.40 29.74 ?  104 GLU   B HG3  1 
ATOM   5447 N N    A ASP   B 1 105 ? 34.943 -26.845 12.165  0.60 27.66 ?  105 ASP   B N    1 
ATOM   5448 N N    B ASP   B 1 105 ? 34.773 -26.937 12.106  0.40 27.20 ?  105 ASP   B N    1 
ATOM   5449 C CA   A ASP   B 1 105 ? 33.662 -27.298 11.637  0.60 28.38 ?  105 ASP   B CA   1 
ATOM   5450 C CA   B ASP   B 1 105 ? 33.521 -27.407 11.526  0.40 27.55 ?  105 ASP   B CA   1 
ATOM   5451 C C    A ASP   B 1 105 ? 33.706 -27.347 10.114  0.60 26.66 ?  105 ASP   B C    1 
ATOM   5452 C C    B ASP   B 1 105 ? 33.612 -27.422 10.005  0.40 26.44 ?  105 ASP   B C    1 
ATOM   5453 O O    A ASP   B 1 105 ? 33.873 -26.315 9.456   0.60 26.15 ?  105 ASP   B O    1 
ATOM   5454 O O    B ASP   B 1 105 ? 33.804 -26.377 9.373   0.40 25.86 ?  105 ASP   B O    1 
ATOM   5455 C CB   A ASP   B 1 105 ? 32.555 -26.358 12.109  0.60 31.25 ?  105 ASP   B CB   1 
ATOM   5456 C CB   B ASP   B 1 105 ? 32.369 -26.514 11.986  0.40 28.98 ?  105 ASP   B CB   1 
ATOM   5457 C CG   A ASP   B 1 105 ? 31.183 -26.790 11.636  0.60 33.80 ?  105 ASP   B CG   1 
ATOM   5458 C CG   B ASP   B 1 105 ? 31.010 -27.109 11.666  0.40 30.23 ?  105 ASP   B CG   1 
ATOM   5459 O OD1  A ASP   B 1 105 ? 31.051 -27.928 11.138  0.60 34.14 ?  105 ASP   B OD1  1 
ATOM   5460 O OD1  B ASP   B 1 105 ? 30.958 -28.105 10.914  0.40 30.47 ?  105 ASP   B OD1  1 
ATOM   5461 O OD2  A ASP   B 1 105 ? 30.236 -25.981 11.751  0.60 35.30 -1 105 ASP   B OD2  1 
ATOM   5462 O OD2  B ASP   B 1 105 ? 29.994 -26.590 12.175  0.40 30.50 -1 105 ASP   B OD2  1 
ATOM   5463 H H    A ASP   B 1 105 ? 34.940 -26.027 12.432  0.60 33.18 ?  105 ASP   B H    1 
ATOM   5464 H H    B ASP   B 1 105 ? 34.728 -26.151 12.449  0.40 32.63 ?  105 ASP   B H    1 
ATOM   5465 H HA   A ASP   B 1 105 ? 33.471 -28.190 11.971  0.60 34.05 ?  105 ASP   B HA   1 
ATOM   5466 H HA   B ASP   B 1 105 ? 33.341 -28.310 11.830  0.40 33.05 ?  105 ASP   B HA   1 
ATOM   5467 H HB2  A ASP   B 1 105 ? 32.571 -26.314 13.082  0.60 37.49 ?  105 ASP   B HB2  1 
ATOM   5468 H HB2  B ASP   B 1 105 ? 32.428 -26.391 12.948  0.40 34.76 ?  105 ASP   B HB2  1 
ATOM   5469 H HB3  A ASP   B 1 105 ? 32.705 -25.478 11.737  0.60 37.49 ?  105 ASP   B HB3  1 
ATOM   5470 H HB3  B ASP   B 1 105 ? 32.437 -25.654 11.539  0.40 34.76 ?  105 ASP   B HB3  1 
ATOM   5471 N N    A ILE   B 1 106 ? 33.528 -28.549 9.558   0.60 26.02 ?  106 ILE   B N    1 
ATOM   5472 N N    B ILE   B 1 106 ? 33.463 -28.614 9.419   0.40 25.97 ?  106 ILE   B N    1 
ATOM   5473 C CA   A ILE   B 1 106 ? 33.527 -28.733 8.111   0.60 25.04 ?  106 ILE   B CA   1 
ATOM   5474 C CA   B ILE   B 1 106 ? 33.473 -28.762 7.969   0.40 25.58 ?  106 ILE   B CA   1 
ATOM   5475 C C    A ILE   B 1 106 ? 32.436 -27.911 7.432   0.60 23.94 ?  106 ILE   B C    1 
ATOM   5476 C C    B ILE   B 1 106 ? 32.382 -27.928 7.310   0.40 24.96 ?  106 ILE   B C    1 
ATOM   5477 O O    A ILE   B 1 106 ? 32.546 -27.598 6.242   0.60 23.33 ?  106 ILE   B O    1 
ATOM   5478 O O    B ILE   B 1 106 ? 32.473 -27.620 6.117   0.40 24.47 ?  106 ILE   B O    1 
ATOM   5479 C CB   A ILE   B 1 106 ? 33.425 -30.242 7.783   0.60 25.72 ?  106 ILE   B CB   1 
ATOM   5480 C CB   B ILE   B 1 106 ? 33.364 -30.262 7.604   0.40 26.06 ?  106 ILE   B CB   1 
ATOM   5481 C CG1  A ILE   B 1 106 ? 33.663 -30.497 6.293   0.60 26.06 ?  106 ILE   B CG1  1 
ATOM   5482 C CG1  B ILE   B 1 106 ? 33.642 -30.487 6.116   0.40 26.28 ?  106 ILE   B CG1  1 
ATOM   5483 C CG2  A ILE   B 1 106 ? 32.072 -30.798 8.215   0.60 26.53 ?  106 ILE   B CG2  1 
ATOM   5484 C CG2  B ILE   B 1 106 ? 31.990 -30.806 7.976   0.40 26.53 ?  106 ILE   B CG2  1 
ATOM   5485 C CD1  A ILE   B 1 106 ? 35.018 -30.033 5.809   0.60 26.11 ?  106 ILE   B CD1  1 
ATOM   5486 C CD1  B ILE   B 1 106 ? 35.015 -30.033 5.680   0.40 26.38 ?  106 ILE   B CD1  1 
ATOM   5487 H H    A ILE   B 1 106 ? 33.411 -29.273 10.004  0.60 31.21 ?  106 ILE   B H    1 
ATOM   5488 H H    B ILE   B 1 106 ? 33.363 -29.351 9.846   0.40 31.15 ?  106 ILE   B H    1 
ATOM   5489 H HA   A ILE   B 1 106 ? 34.375 -28.415 7.772   0.60 30.03 ?  106 ILE   B HA   1 
ATOM   5490 H HA   B ILE   B 1 106 ? 34.321 -28.437 7.639   0.40 30.68 ?  106 ILE   B HA   1 
ATOM   5491 H HB   A ILE   B 1 106 ? 34.114 -30.707 8.282   0.60 30.85 ?  106 ILE   B HB   1 
ATOM   5492 H HB   B ILE   B 1 106 ? 34.029 -30.748 8.115   0.40 31.27 ?  106 ILE   B HB   1 
ATOM   5493 H HG12 A ILE   B 1 106 ? 33.603 -31.453 6.127   0.60 31.26 ?  106 ILE   B HG12 1 
ATOM   5494 H HG12 B ILE   B 1 106 ? 33.574 -31.438 5.927   0.40 31.53 ?  106 ILE   B HG12 1 
ATOM   5495 H HG13 A ILE   B 1 106 ? 32.987 -30.032 5.779   0.60 31.26 ?  106 ILE   B HG13 1 
ATOM   5496 H HG13 B ILE   B 1 106 ? 32.987 -30.001 5.595   0.40 31.53 ?  106 ILE   B HG13 1 
ATOM   5497 H HG21 A ILE   B 1 106 ? 32.079 -31.762 8.106   0.60 31.83 ?  106 ILE   B HG21 1 
ATOM   5498 H HG21 B ILE   B 1 106 ? 32.001 -31.772 7.888   0.40 31.83 ?  106 ILE   B HG21 1 
ATOM   5499 H HG22 A ILE   B 1 106 ? 31.922 -30.573 9.147   0.60 31.83 ?  106 ILE   B HG22 1 
ATOM   5500 H HG22 B ILE   B 1 106 ? 31.791 -30.560 8.893   0.40 31.83 ?  106 ILE   B HG22 1 
ATOM   5501 H HG23 A ILE   B 1 106 ? 31.377 -30.408 7.664   0.60 31.83 ?  106 ILE   B HG23 1 
ATOM   5502 H HG23 B ILE   B 1 106 ? 31.326 -30.427 7.380   0.40 31.83 ?  106 ILE   B HG23 1 
ATOM   5503 H HD11 A ILE   B 1 106 ? 35.200 -30.437 4.947   0.60 31.32 ?  106 ILE   B HD11 1 
ATOM   5504 H HD11 B ILE   B 1 106 ? 35.218 -30.428 4.820   0.40 31.65 ?  106 ILE   B HD11 1 
ATOM   5505 H HD12 A ILE   B 1 106 ? 35.010 -29.066 5.726   0.60 31.32 ?  106 ILE   B HD12 1 
ATOM   5506 H HD12 B ILE   B 1 106 ? 35.019 -29.065 5.610   0.40 31.65 ?  106 ILE   B HD12 1 
ATOM   5507 H HD13 A ILE   B 1 106 ? 35.693 -30.305 6.451   0.60 31.32 ?  106 ILE   B HD13 1 
ATOM   5508 H HD13 B ILE   B 1 106 ? 35.666 -30.321 6.339   0.40 31.65 ?  106 ILE   B HD13 1 
ATOM   5509 N N    A GLN   B 1 107 ? 31.384 -27.539 8.166   0.60 24.49 ?  107 GLN   B N    1 
ATOM   5510 N N    B GLN   B 1 107 ? 31.348 -27.548 8.064   0.40 25.27 ?  107 GLN   B N    1 
ATOM   5511 C CA   A GLN   B 1 107 ? 30.299 -26.755 7.583   0.60 24.81 ?  107 GLN   B CA   1 
ATOM   5512 C CA   B GLN   B 1 107 ? 30.271 -26.736 7.510   0.40 25.47 ?  107 GLN   B CA   1 
ATOM   5513 C C    A GLN   B 1 107 ? 30.777 -25.412 7.041   0.60 22.89 ?  107 GLN   B C    1 
ATOM   5514 C C    B GLN   B 1 107 ? 30.756 -25.368 7.042   0.40 23.30 ?  107 GLN   B C    1 
ATOM   5515 O O    A GLN   B 1 107 ? 30.133 -24.855 6.148   0.60 23.36 ?  107 GLN   B O    1 
ATOM   5516 O O    B GLN   B 1 107 ? 30.091 -24.744 6.210   0.40 23.76 ?  107 GLN   B O    1 
ATOM   5517 C CB   A GLN   B 1 107 ? 29.194 -26.548 8.624   0.60 28.24 ?  107 GLN   B CB   1 
ATOM   5518 C CB   B GLN   B 1 107 ? 29.154 -26.583 8.548   0.40 28.32 ?  107 GLN   B CB   1 
ATOM   5519 C CG   A GLN   B 1 107 ? 27.865 -26.054 8.060   0.60 31.82 ?  107 GLN   B CG   1 
ATOM   5520 C CG   B GLN   B 1 107 ? 27.818 -26.117 7.984   0.40 31.14 ?  107 GLN   B CG   1 
ATOM   5521 C CD   A GLN   B 1 107 ? 27.793 -24.541 7.946   0.60 34.53 ?  107 GLN   B CD   1 
ATOM   5522 C CD   B GLN   B 1 107 ? 27.686 -24.606 7.949   0.40 33.35 ?  107 GLN   B CD   1 
ATOM   5523 O OE1  A GLN   B 1 107 ? 28.641 -23.824 8.481   0.60 35.60 ?  107 GLN   B OE1  1 
ATOM   5524 O OE1  B GLN   B 1 107 ? 28.508 -23.884 8.515   0.40 34.22 ?  107 GLN   B OE1  1 
ATOM   5525 N NE2  A GLN   B 1 107 ? 26.773 -24.047 7.248   0.60 35.49 ?  107 GLN   B NE2  1 
ATOM   5526 N NE2  B GLN   B 1 107 ? 26.644 -24.120 7.283   0.40 34.14 ?  107 GLN   B NE2  1 
ATOM   5527 H H    A GLN   B 1 107 ? 31.277 -27.725 8.996   0.60 29.37 ?  107 GLN   B H    1 
ATOM   5528 H H    B GLN   B 1 107 ? 31.244 -27.750 8.891   0.40 30.32 ?  107 GLN   B H    1 
ATOM   5529 H HA   A GLN   B 1 107 ? 29.917 -27.254 6.844   0.60 29.76 ?  107 GLN   B HA   1 
ATOM   5530 H HA   B GLN   B 1 107 ? 29.895 -27.197 6.744   0.40 30.56 ?  107 GLN   B HA   1 
ATOM   5531 H HB2  A GLN   B 1 107 ? 29.026 -27.393 9.064   0.60 33.88 ?  107 GLN   B HB2  1 
ATOM   5532 H HB2  B GLN   B 1 107 ? 29.006 -27.441 8.970   0.40 33.98 ?  107 GLN   B HB2  1 
ATOM   5533 H HB3  A GLN   B 1 107 ? 29.499 -25.897 9.274   0.60 33.88 ?  107 GLN   B HB3  1 
ATOM   5534 H HB3  B GLN   B 1 107 ? 29.435 -25.937 9.215   0.40 33.98 ?  107 GLN   B HB3  1 
ATOM   5535 H HG2  A GLN   B 1 107 ? 27.737 -26.424 7.173   0.60 38.17 ?  107 GLN   B HG2  1 
ATOM   5536 H HG2  B GLN   B 1 107 ? 27.723 -26.446 7.077   0.40 37.36 ?  107 GLN   B HG2  1 
ATOM   5537 H HG3  A GLN   B 1 107 ? 27.145 -26.348 8.646   0.60 38.17 ?  107 GLN   B HG3  1 
ATOM   5538 H HG3  B GLN   B 1 107 ? 27.101 -26.471 8.539   0.40 37.36 ?  107 GLN   B HG3  1 
ATOM   5539 H HE21 A GLN   B 1 107 ? 26.200 -24.579 6.886   0.60 42.58 ?  107 GLN   B HE21 1 
ATOM   5540 H HE21 B GLN   B 1 107 ? 26.091 -24.654 6.898   0.40 40.95 ?  107 GLN   B HE21 1 
ATOM   5541 H HE22 A GLN   B 1 107 ? 26.683 -23.196 7.158   0.60 42.58 ?  107 GLN   B HE22 1 
ATOM   5542 H HE22 B GLN   B 1 107 ? 26.523 -23.270 7.237   0.40 40.95 ?  107 GLN   B HE22 1 
ATOM   5543 N N    . LEU   B 1 108 ? 31.898 -24.891 7.543   1.00 20.91 ?  108 LEU   B N    1 
ATOM   5544 C CA   . LEU   B 1 108 ? 32.434 -23.593 7.128   1.00 18.45 ?  108 LEU   B CA   1 
ATOM   5545 C C    . LEU   B 1 108 ? 33.086 -23.617 5.754   1.00 16.20 ?  108 LEU   B C    1 
ATOM   5546 O O    . LEU   B 1 108 ? 33.515 -22.559 5.267   1.00 15.98 ?  108 LEU   B O    1 
ATOM   5547 C CB   . LEU   B 1 108 ? 33.431 -23.096 8.169   1.00 18.98 ?  108 LEU   B CB   1 
ATOM   5548 C CG   . LEU   B 1 108 ? 32.778 -22.654 9.477   1.00 20.54 ?  108 LEU   B CG   1 
ATOM   5549 C CD1  . LEU   B 1 108 ? 33.782 -22.635 10.614  1.00 20.61 ?  108 LEU   B CD1  1 
ATOM   5550 C CD2  . LEU   B 1 108 ? 32.158 -21.279 9.301   1.00 21.79 ?  108 LEU   B CD2  1 
ATOM   5551 H H    A LEU   B 1 108 ? 32.371 -25.280 8.143   0.60 25.08 ?  108 LEU   B H    1 
ATOM   5552 H H    B LEU   B 1 108 ? 32.374 -25.298 8.128   0.40 25.08 ?  108 LEU   B H    1 
ATOM   5553 H HA   . LEU   B 1 108 ? 31.704 -22.960 7.092   1.00 22.12 ?  108 LEU   B HA   1 
ATOM   5554 H HB2  . LEU   B 1 108 ? 34.050 -23.811 8.380   1.00 22.76 ?  108 LEU   B HB2  1 
ATOM   5555 H HB3  . LEU   B 1 108 ? 33.909 -22.336 7.809   1.00 22.76 ?  108 LEU   B HB3  1 
ATOM   5556 H HG   . LEU   B 1 108 ? 32.066 -23.275 9.712   1.00 24.64 ?  108 LEU   B HG   1 
ATOM   5557 H HD11 . LEU   B 1 108 ? 33.333 -22.353 11.430  1.00 24.72 ?  108 LEU   B HD11 1 
ATOM   5558 H HD12 . LEU   B 1 108 ? 34.144 -23.526 10.729  1.00 24.72 ?  108 LEU   B HD12 1 
ATOM   5559 H HD13 . LEU   B 1 108 ? 34.491 -22.011 10.397  1.00 24.72 ?  108 LEU   B HD13 1 
ATOM   5560 H HD21 . LEU   B 1 108 ? 31.788 -20.986 10.149  1.00 26.14 ?  108 LEU   B HD21 1 
ATOM   5561 H HD22 . LEU   B 1 108 ? 32.845 -20.661 9.009   1.00 26.14 ?  108 LEU   B HD22 1 
ATOM   5562 H HD23 . LEU   B 1 108 ? 31.454 -21.331 8.635   1.00 26.14 ?  108 LEU   B HD23 1 
ATOM   5563 N N    . LEU   B 1 109 ? 33.157 -24.787 5.122   1.00 15.29 ?  109 LEU   B N    1 
ATOM   5564 C CA   . LEU   B 1 109 ? 33.783 -24.895 3.813   1.00 14.36 ?  109 LEU   B CA   1 
ATOM   5565 C C    . LEU   B 1 109 ? 33.018 -24.108 2.758   1.00 13.86 ?  109 LEU   B C    1 
ATOM   5566 O O    . LEU   B 1 109 ? 33.630 -23.516 1.862   1.00 13.83 ?  109 LEU   B O    1 
ATOM   5567 C CB   . LEU   B 1 109 ? 33.892 -26.370 3.432   1.00 14.63 ?  109 LEU   B CB   1 
ATOM   5568 C CG   . LEU   B 1 109 ? 34.691 -26.715 2.180   1.00 14.27 ?  109 LEU   B CG   1 
ATOM   5569 C CD1  . LEU   B 1 109 ? 36.066 -26.065 2.216   1.00 14.43 ?  109 LEU   B CD1  1 
ATOM   5570 C CD2  . LEU   B 1 109 ? 34.817 -28.221 2.043   1.00 15.34 ?  109 LEU   B CD2  1 
ATOM   5571 H H    . LEU   B 1 109 ? 32.855 -25.527 5.425   1.00 18.34 ?  109 LEU   B H    1 
ATOM   5572 H HA   . LEU   B 1 109 ? 34.677 -24.531 3.855   1.00 17.22 ?  109 LEU   B HA   1 
ATOM   5573 H HB2  . LEU   B 1 109 ? 34.308 -26.843 4.168   1.00 17.55 ?  109 LEU   B HB2  1 
ATOM   5574 H HB3  . LEU   B 1 109 ? 32.994 -26.719 3.298   1.00 17.55 ?  109 LEU   B HB3  1 
ATOM   5575 H HG   . LEU   B 1 109 ? 34.218 -26.392 1.395   1.00 17.11 ?  109 LEU   B HG   1 
ATOM   5576 H HD11 . LEU   B 1 109 ? 36.616 -26.446 1.514   1.00 17.31 ?  109 LEU   B HD11 1 
ATOM   5577 H HD12 . LEU   B 1 109 ? 35.965 -25.113 2.080   1.00 17.31 ?  109 LEU   B HD12 1 
ATOM   5578 H HD13 . LEU   B 1 109 ? 36.470 -26.240 3.081   1.00 17.31 ?  109 LEU   B HD13 1 
ATOM   5579 H HD21 . LEU   B 1 109 ? 35.391 -28.425 1.285   1.00 18.39 ?  109 LEU   B HD21 1 
ATOM   5580 H HD22 . LEU   B 1 109 ? 35.203 -28.583 2.854   1.00 18.39 ?  109 LEU   B HD22 1 
ATOM   5581 H HD23 . LEU   B 1 109 ? 33.935 -28.605 1.897   1.00 18.39 ?  109 LEU   B HD23 1 
ATOM   5582 N N    . LYS   B 1 110 ? 31.683 -24.081 2.838   1.00 13.85 ?  110 LYS   B N    1 
ATOM   5583 C CA   . LYS   B 1 110 ? 30.927 -23.318 1.850   1.00 13.75 ?  110 LYS   B CA   1 
ATOM   5584 C C    . LYS   B 1 110 ? 31.269 -21.830 1.942   1.00 13.23 ?  110 LYS   B C    1 
ATOM   5585 O O    . LYS   B 1 110 ? 31.518 -21.176 0.926   1.00 12.96 ?  110 LYS   B O    1 
ATOM   5586 C CB   . LYS   B 1 110 ? 29.421 -23.565 1.999   1.00 14.40 ?  110 LYS   B CB   1 
ATOM   5587 C CG   . LYS   B 1 110 ? 28.609 -22.930 0.867   1.00 14.56 ?  110 LYS   B CG   1 
ATOM   5588 C CD   . LYS   B 1 110 ? 27.145 -23.362 0.893   1.00 15.09 ?  110 LYS   B CD   1 
ATOM   5589 C CE   . LYS   B 1 110 ? 26.376 -22.838 -0.324  1.00 15.66 ?  110 LYS   B CE   1 
ATOM   5590 N NZ   . LYS   B 1 110 ? 26.718 -23.548 -1.582  1.00 15.93 ?  110 LYS   B NZ   1 
ATOM   5591 H H    . LYS   B 1 110 ? 31.210 -24.488 3.427   1.00 16.60 ?  110 LYS   B H    1 
ATOM   5592 H HA   . LYS   B 1 110 ? 31.182 -23.620 0.963   1.00 16.49 ?  110 LYS   B HA   1 
ATOM   5593 H HB2  . LYS   B 1 110 ? 29.255 -24.524 1.982   1.00 17.27 ?  110 LYS   B HB2  1 
ATOM   5594 H HB3  . LYS   B 1 110 ? 29.117 -23.190 2.836   1.00 17.27 ?  110 LYS   B HB3  1 
ATOM   5595 H HG2  . LYS   B 1 110 ? 28.631 -21.964 0.960   1.00 17.46 ?  110 LYS   B HG2  1 
ATOM   5596 H HG3  . LYS   B 1 110 ? 28.980 -23.193 0.012   1.00 17.46 ?  110 LYS   B HG3  1 
ATOM   5597 H HD2  . LYS   B 1 110 ? 27.097 -24.335 0.890   1.00 18.10 ?  110 LYS   B HD2  1 
ATOM   5598 H HD3  . LYS   B 1 110 ? 26.718 -23.014 1.694   1.00 18.10 ?  110 LYS   B HD3  1 
ATOM   5599 H HE2  . LYS   B 1 110 ? 25.427 -22.950 -0.171  1.00 18.78 ?  110 LYS   B HE2  1 
ATOM   5600 H HE3  . LYS   B 1 110 ? 26.589 -21.902 -0.446  1.00 18.78 ?  110 LYS   B HE3  1 
ATOM   5601 H HZ1  . LYS   B 1 110 ? 26.254 -23.210 -2.259  1.00 19.10 ?  110 LYS   B HZ1  1 
ATOM   5602 H HZ2  . LYS   B 1 110 ? 27.589 -23.460 -1.755  1.00 19.10 ?  110 LYS   B HZ2  1 
ATOM   5603 H HZ3  . LYS   B 1 110 ? 26.530 -24.416 -1.504  1.00 19.10 ?  110 LYS   B HZ3  1 
ATOM   5604 N N    . SER   B 1 111 ? 31.291 -21.281 3.161   1.00 13.51 ?  111 SER   B N    1 
ATOM   5605 C CA   . SER   B 1 111 ? 31.677 -19.881 3.338   1.00 13.57 ?  111 SER   B CA   1 
ATOM   5606 C C    . SER   B 1 111 ? 33.059 -19.615 2.756   1.00 12.99 ?  111 SER   B C    1 
ATOM   5607 O O    . SER   B 1 111 ? 33.286 -18.579 2.116   1.00 13.03 ?  111 SER   B O    1 
ATOM   5608 C CB   . SER   B 1 111 ? 31.664 -19.524 4.821   1.00 14.60 ?  111 SER   B CB   1 
ATOM   5609 O OG   . SER   B 1 111 ? 30.355 -19.540 5.341   1.00 16.49 ?  111 SER   B OG   1 
ATOM   5610 H H    . SER   B 1 111 ? 31.094 -21.696 3.887   1.00 16.21 ?  111 SER   B H    1 
ATOM   5611 H HA   . SER   B 1 111 ? 31.039 -19.313 2.880   1.00 16.27 ?  111 SER   B HA   1 
ATOM   5612 H HB2  . SER   B 1 111 ? 32.194 -20.173 5.307   1.00 17.51 ?  111 SER   B HB2  1 
ATOM   5613 H HB3  . SER   B 1 111 ? 32.033 -18.637 4.936   1.00 17.51 ?  111 SER   B HB3  1 
ATOM   5614 H HG   . SER   B 1 111 ? 30.360 -19.337 6.162   1.00 19.78 ?  111 SER   B HG   1 
ATOM   5615 N N    . ALA   B 1 112 ? 34.001 -20.533 2.981   1.00 12.95 ?  112 ALA   B N    1 
ATOM   5616 C CA   . ALA   B 1 112 ? 35.346 -20.364 2.437   1.00 12.50 ?  112 ALA   B CA   1 
ATOM   5617 C C    . ALA   B 1 112 ? 35.309 -20.266 0.916   1.00 12.07 ?  112 ALA   B C    1 
ATOM   5618 O O    . ALA   B 1 112 ? 35.936 -19.380 0.324   1.00 12.58 ?  112 ALA   B O    1 
ATOM   5619 C CB   . ALA   B 1 112 ? 36.245 -21.513 2.903   1.00 13.11 ?  112 ALA   B CB   1 
ATOM   5620 H H    . ALA   B 1 112 ? 33.889 -21.250 3.447   1.00 15.53 ?  112 ALA   B H    1 
ATOM   5621 H HA   . ALA   B 1 112 ? 35.719 -19.538 2.781   1.00 14.98 ?  112 ALA   B HA   1 
ATOM   5622 H HB1  . ALA   B 1 112 ? 37.137 -21.381 2.540   1.00 15.72 ?  112 ALA   B HB1  1 
ATOM   5623 H HB2  . ALA   B 1 112 ? 36.285 -21.510 3.875   1.00 15.72 ?  112 ALA   B HB2  1 
ATOM   5624 H HB3  . ALA   B 1 112 ? 35.880 -22.352 2.590   1.00 15.72 ?  112 ALA   B HB3  1 
ATOM   5625 N N    . TYR   B 1 113 ? 34.578 -21.171 0.259   1.00 12.00 ?  113 TYR   B N    1 
ATOM   5626 C CA   . TYR   B 1 113 ? 34.501 -21.124 -1.196  1.00 11.60 ?  113 TYR   B CA   1 
ATOM   5627 C C    . TYR   B 1 113 ? 33.790 -19.876 -1.714  1.00 11.50 ?  113 TYR   B C    1 
ATOM   5628 O O    . TYR   B 1 113 ? 34.064 -19.441 -2.840  1.00 11.69 ?  113 TYR   B O    1 
ATOM   5629 C CB   . TYR   B 1 113 ? 33.827 -22.382 -1.741  1.00 11.81 ?  113 TYR   B CB   1 
ATOM   5630 C CG   . TYR   B 1 113 ? 34.792 -23.533 -2.006  1.00 12.35 ?  113 TYR   B CG   1 
ATOM   5631 C CD1  . TYR   B 1 113 ? 35.790 -23.423 -2.969  1.00 12.88 ?  113 TYR   B CD1  1 
ATOM   5632 C CD2  . TYR   B 1 113 ? 34.694 -24.730 -1.307  1.00 12.77 ?  113 TYR   B CD2  1 
ATOM   5633 C CE1  . TYR   B 1 113 ? 36.671 -24.460 -3.221  1.00 12.78 ?  113 TYR   B CE1  1 
ATOM   5634 C CE2  . TYR   B 1 113 ? 35.563 -25.781 -1.559  1.00 13.03 ?  113 TYR   B CE2  1 
ATOM   5635 C CZ   . TYR   B 1 113 ? 36.549 -25.643 -2.518  1.00 13.00 ?  113 TYR   B CZ   1 
ATOM   5636 O OH   . TYR   B 1 113 ? 37.430 -26.662 -2.797  1.00 13.62 ?  113 TYR   B OH   1 
ATOM   5637 H H    . TYR   B 1 113 ? 34.121 -21.805 0.633   1.00 14.39 ?  113 TYR   B H    1 
ATOM   5638 H HA   . TYR   B 1 113 ? 35.401 -21.105 -1.536  1.00 13.91 ?  113 TYR   B HA   1 
ATOM   5639 H HB2  . TYR   B 1 113 ? 33.168 -22.697 -1.097  1.00 14.16 ?  113 TYR   B HB2  1 
ATOM   5640 H HB3  . TYR   B 1 113 ? 33.387 -22.167 -2.577  1.00 14.16 ?  113 TYR   B HB3  1 
ATOM   5641 H HD1  . TYR   B 1 113 ? 35.875 -22.627 -3.448  1.00 15.44 ?  113 TYR   B HD1  1 
ATOM   5642 H HD2  . TYR   B 1 113 ? 34.024 -24.831 -0.672  1.00 15.31 ?  113 TYR   B HD2  1 
ATOM   5643 H HE1  . TYR   B 1 113 ? 37.331 -24.365 -3.875  1.00 15.32 ?  113 TYR   B HE1  1 
ATOM   5644 H HE2  . TYR   B 1 113 ? 35.477 -26.577 -1.093  1.00 15.62 ?  113 TYR   B HE2  1 
ATOM   5645 H HH   . TYR   B 1 113 ? 37.250 -27.330 -2.324  1.00 16.33 ?  113 TYR   B HH   1 
ATOM   5646 N N    . GLU   B 1 114 ? 32.868 -19.294 -0.936  1.00 11.80 ?  114 GLU   B N    1 
ATOM   5647 C CA   . GLU   B 1 114 ? 32.186 -18.091 -1.398  1.00 11.72 ?  114 GLU   B CA   1 
ATOM   5648 C C    . GLU   B 1 114 ? 33.167 -16.966 -1.696  1.00 11.76 ?  114 GLU   B C    1 
ATOM   5649 O O    . GLU   B 1 114 ? 32.879 -16.104 -2.532  1.00 12.19 ?  114 GLU   B O    1 
ATOM   5650 C CB   . GLU   B 1 114 ? 31.125 -17.663 -0.381  1.00 12.52 ?  114 GLU   B CB   1 
ATOM   5651 C CG   . GLU   B 1 114 ? 29.904 -18.581 -0.440  1.00 12.60 ?  114 GLU   B CG   1 
ATOM   5652 C CD   . GLU   B 1 114 ? 28.884 -18.386 0.673   1.00 12.80 ?  114 GLU   B CD   1 
ATOM   5653 O OE1  . GLU   B 1 114 ? 29.173 -17.770 1.722   1.00 12.93 ?  114 GLU   B OE1  1 
ATOM   5654 O OE2  . GLU   B 1 114 ? 27.759 -18.912 0.508   1.00 13.81 -1 114 GLU   B OE2  1 
ATOM   5655 H H    . GLU   B 1 114 ? 32.619 -19.577 -0.158  1.00 14.14 ?  114 GLU   B H    1 
ATOM   5656 H HA   . GLU   B 1 114 ? 31.729 -18.293 -2.223  1.00 14.05 ?  114 GLU   B HA   1 
ATOM   5657 H HB2  . GLU   B 1 114 ? 31.497 -17.710 0.515   1.00 15.02 ?  114 GLU   B HB2  1 
ATOM   5658 H HB3  . GLU   B 1 114 ? 30.833 -16.762 -0.578  1.00 15.02 ?  114 GLU   B HB3  1 
ATOM   5659 H HG2  . GLU   B 1 114 ? 29.454 -18.438 -1.281  1.00 15.11 ?  114 GLU   B HG2  1 
ATOM   5660 H HG3  . GLU   B 1 114 ? 30.216 -19.503 -0.390  1.00 15.11 ?  114 GLU   B HG3  1 
ATOM   5661 N N    . ASN   B 1 115 ? 34.332 -16.955 -1.040  1.00 11.72 ?  115 ASN   B N    1 
ATOM   5662 C CA   . ASN   B 1 115 ? 35.320 -15.919 -1.333  1.00 11.49 ?  115 ASN   B CA   1 
ATOM   5663 C C    . ASN   B 1 115 ? 35.729 -15.934 -2.800  1.00 11.43 ?  115 ASN   B C    1 
ATOM   5664 O O    . ASN   B 1 115 ? 36.116 -14.891 -3.354  1.00 11.96 ?  115 ASN   B O    1 
ATOM   5665 C CB   . ASN   B 1 115 ? 36.562 -16.091 -0.451  1.00 12.08 ?  115 ASN   B CB   1 
ATOM   5666 C CG   . ASN   B 1 115 ? 36.295 -15.831 1.013   1.00 12.56 ?  115 ASN   B CG   1 
ATOM   5667 O OD1  . ASN   B 1 115 ? 36.283 -14.687 1.454   1.00 14.89 ?  115 ASN   B OD1  1 
ATOM   5668 N ND2  . ASN   B 1 115 ? 36.135 -16.898 1.788   1.00 12.59 ?  115 ASN   B ND2  1 
ATOM   5669 H H    . ASN   B 1 115 ? 34.572 -17.520 -0.429  1.00 14.05 ?  115 ASN   B H    1 
ATOM   5670 H HA   . ASN   B 1 115 ? 34.938 -15.050 -1.138  1.00 13.78 ?  115 ASN   B HA   1 
ATOM   5671 H HB2  . ASN   B 1 115 ? 36.891 -16.997 -0.538  1.00 14.49 ?  115 ASN   B HB2  1 
ATOM   5672 H HB3  . ASN   B 1 115 ? 37.244 -15.461 -0.740  1.00 14.49 ?  115 ASN   B HB3  1 
ATOM   5673 H HD21 . ASN   B 1 115 ? 35.989 -16.800 2.630   1.00 15.10 ?  115 ASN   B HD21 1 
ATOM   5674 H HD22 . ASN   B 1 115 ? 36.163 -17.686 1.446   1.00 15.10 ?  115 ASN   B HD22 1 
ATOM   5675 N N    . PHE   B 1 116 ? 35.708 -17.114 -3.435  1.00 11.18 ?  116 PHE   B N    1 
ATOM   5676 C CA   . PHE   B 1 116 ? 36.136 -17.209 -4.826  1.00 11.47 ?  116 PHE   B CA   1 
ATOM   5677 C C    . PHE   B 1 116 ? 35.234 -16.384 -5.735  1.00 11.04 ?  116 PHE   B C    1 
ATOM   5678 O O    . PHE   B 1 116 ? 35.666 -15.957 -6.812  1.00 11.70 ?  116 PHE   B O    1 
ATOM   5679 C CB   . PHE   B 1 116 ? 36.104 -18.656 -5.346  1.00 11.04 ?  116 PHE   B CB   1 
ATOM   5680 C CG   . PHE   B 1 116 ? 37.176 -19.609 -4.801  1.00 11.25 ?  116 PHE   B CG   1 
ATOM   5681 C CD1  . PHE   B 1 116 ? 37.838 -19.419 -3.599  1.00 11.85 ?  116 PHE   B CD1  1 
ATOM   5682 C CD2  . PHE   B 1 116 ? 37.474 -20.751 -5.535  1.00 11.62 ?  116 PHE   B CD2  1 
ATOM   5683 C CE1  . PHE   B 1 116 ? 38.767 -20.359 -3.145  1.00 12.14 ?  116 PHE   B CE1  1 
ATOM   5684 C CE2  . PHE   B 1 116 ? 38.399 -21.687 -5.088  1.00 11.91 ?  116 PHE   B CE2  1 
ATOM   5685 C CZ   . PHE   B 1 116 ? 39.049 -21.489 -3.901  1.00 12.09 ?  116 PHE   B CZ   1 
ATOM   5686 H H    . PHE   B 1 116 ? 35.447 -17.863 -3.090  1.00 13.40 ?  116 PHE   B H    1 
ATOM   5687 H HA   . PHE   B 1 116 ? 37.042 -16.877 -4.907  1.00 13.75 ?  116 PHE   B HA   1 
ATOM   5688 H HB2  . PHE   B 1 116 ? 35.233 -19.034 -5.123  1.00 13.24 ?  116 PHE   B HB2  1 
ATOM   5689 H HB3  . PHE   B 1 116 ? 36.196 -18.631 -6.312  1.00 13.24 ?  116 PHE   B HB3  1 
ATOM   5690 H HD1  . PHE   B 1 116 ? 37.646 -18.668 -3.083  1.00 14.21 ?  116 PHE   B HD1  1 
ATOM   5691 H HD2  . PHE   B 1 116 ? 37.026 -20.905 -6.338  1.00 13.93 ?  116 PHE   B HD2  1 
ATOM   5692 H HE1  . PHE   B 1 116 ? 39.215 -20.214 -2.343  1.00 14.55 ?  116 PHE   B HE1  1 
ATOM   5693 H HE2  . PHE   B 1 116 ? 38.586 -22.440 -5.600  1.00 14.28 ?  116 PHE   B HE2  1 
ATOM   5694 H HZ   . PHE   B 1 116 ? 39.684 -22.099 -3.602  1.00 14.50 ?  116 PHE   B HZ   1 
ATOM   5695 N N    . ASN   B 1 117 ? 33.967 -16.183 -5.345  1.00 11.48 ?  117 ASN   B N    1 
ATOM   5696 C CA   . ASN   B 1 117 ? 33.015 -15.479 -6.207  1.00 11.86 ?  117 ASN   B CA   1 
ATOM   5697 C C    . ASN   B 1 117 ? 33.329 -13.999 -6.363  1.00 12.10 ?  117 ASN   B C    1 
ATOM   5698 O O    . ASN   B 1 117 ? 32.735 -13.346 -7.224  1.00 13.28 ?  117 ASN   B O    1 
ATOM   5699 C CB   . ASN   B 1 117 ? 31.587 -15.701 -5.724  1.00 12.10 ?  117 ASN   B CB   1 
ATOM   5700 C CG   . ASN   B 1 117 ? 31.139 -17.113 -5.975  1.00 12.34 ?  117 ASN   B CG   1 
ATOM   5701 O OD1  . ASN   B 1 117 ? 31.497 -17.702 -6.999  1.00 13.07 ?  117 ASN   B OD1  1 
ATOM   5702 N ND2  . ASN   B 1 117 ? 30.399 -17.685 -5.039  1.00 12.19 ?  117 ASN   B ND2  1 
ATOM   5703 H H    . ASN   B 1 117 ? 33.644 -16.438 -4.585  1.00 13.77 ?  117 ASN   B H    1 
ATOM   5704 H HA   . ASN   B 1 117 ? 33.078 -15.876 -7.084  1.00 14.22 ?  117 ASN   B HA   1 
ATOM   5705 H HB2  . ASN   B 1 117 ? 31.537 -15.529 -4.768  1.00 14.51 ?  117 ASN   B HB2  1 
ATOM   5706 H HB3  . ASN   B 1 117 ? 30.994 -15.092 -6.199  1.00 14.51 ?  117 ASN   B HB3  1 
ATOM   5707 H HD21 . ASN   B 1 117 ? 30.120 -18.492 -5.143  1.00 14.61 ?  117 ASN   B HD21 1 
ATOM   5708 H HD22 . ASN   B 1 117 ? 30.173 -17.241 -4.336  1.00 14.61 ?  117 ASN   B HD22 1 
ATOM   5709 N N    . GLN   B 1 118 ? 34.266 -13.471 -5.588  1.00 12.04 ?  118 GLN   B N    1 
ATOM   5710 C CA   . GLN   B 1 118 ? 34.690 -12.083 -5.729  1.00 12.60 ?  118 GLN   B CA   1 
ATOM   5711 C C    . GLN   B 1 118 ? 35.760 -11.897 -6.800  1.00 12.58 ?  118 GLN   B C    1 
ATOM   5712 O O    . GLN   B 1 118 ? 36.237 -10.771 -6.980  1.00 13.91 ?  118 GLN   B O    1 
ATOM   5713 C CB   . GLN   B 1 118 ? 35.170 -11.557 -4.374  1.00 13.10 ?  118 GLN   B CB   1 
ATOM   5714 C CG   . GLN   B 1 118 ? 34.083 -11.581 -3.304  1.00 13.07 ?  118 GLN   B CG   1 
ATOM   5715 C CD   . GLN   B 1 118 ? 32.910 -10.678 -3.645  1.00 13.02 ?  118 GLN   B CD   1 
ATOM   5716 O OE1  . GLN   B 1 118 ? 33.095 -9.539  -4.090  1.00 13.80 ?  118 GLN   B OE1  1 
ATOM   5717 N NE2  . GLN   B 1 118 ? 31.693 -11.178 -3.444  1.00 13.37 ?  118 GLN   B NE2  1 
ATOM   5718 H H    . GLN   B 1 118 ? 34.687 -13.898 -4.962  1.00 14.44 ?  118 GLN   B H    1 
ATOM   5719 H HA   . GLN   B 1 118 ? 33.922 -11.556 -5.997  1.00 15.10 ?  118 GLN   B HA   1 
ATOM   5720 H HB2  . GLN   B 1 118 ? 35.908 -12.097 -4.063  1.00 15.70 ?  118 GLN   B HB2  1 
ATOM   5721 H HB3  . GLN   B 1 118 ? 35.457 -10.631 -4.478  1.00 15.70 ?  118 GLN   B HB3  1 
ATOM   5722 H HG2  . GLN   B 1 118 ? 33.751 -12.489 -3.215  1.00 15.67 ?  118 GLN   B HG2  1 
ATOM   5723 H HG3  . GLN   B 1 118 ? 34.461 -11.282 -2.462  1.00 15.67 ?  118 GLN   B HG3  1 
ATOM   5724 H HE21 . GLN   B 1 118 ? 31.603 -11.978 -3.133  1.00 16.04 ?  118 GLN   B HE21 1 
ATOM   5725 H HE22 . GLN   B 1 118 ? 31.001 -10.706 -3.623  1.00 16.04 ?  118 GLN   B HE22 1 
ATOM   5726 N N    . HIS   B 1 119 ? 36.118 -12.958 -7.529  1.00 11.77 ?  119 HIS   B N    1 
ATOM   5727 C CA   . HIS   B 1 119 ? 37.160 -12.907 -8.549  1.00 12.14 ?  119 HIS   B CA   1 
ATOM   5728 C C    . HIS   B 1 119 ? 36.685 -13.638 -9.789  1.00 12.30 ?  119 HIS   B C    1 
ATOM   5729 O O    . HIS   B 1 119 ? 36.167 -14.751 -9.688  1.00 12.79 ?  119 HIS   B O    1 
ATOM   5730 C CB   . HIS   B 1 119 ? 38.446 -13.528 -8.007  1.00 12.79 ?  119 HIS   B CB   1 
ATOM   5731 C CG   . HIS   B 1 119 ? 38.919 -12.833 -6.779  1.00 13.92 ?  119 HIS   B CG   1 
ATOM   5732 N ND1  . HIS   B 1 119 ? 39.722 -11.712 -6.824  1.00 15.58 ?  119 HIS   B ND1  1 
ATOM   5733 C CD2  . HIS   B 1 119 ? 38.622 -13.036 -5.476  1.00 15.03 ?  119 HIS   B CD2  1 
ATOM   5734 C CE1  . HIS   B 1 119 ? 39.922 -11.276 -5.595  1.00 16.96 ?  119 HIS   B CE1  1 
ATOM   5735 N NE2  . HIS   B 1 119 ? 39.261 -12.055 -4.759  1.00 16.79 ?  119 HIS   B NE2  1 
ATOM   5736 H H    . HIS   B 1 119 ? 35.755 -13.739 -7.454  1.00 14.11 ?  119 HIS   B H    1 
ATOM   5737 H HA   . HIS   B 1 119 ? 37.335 -11.980 -8.785  1.00 14.56 ?  119 HIS   B HA   1 
ATOM   5738 H HB2  . HIS   B 1 119 ? 38.283 -14.456 -7.794  1.00 15.34 ?  119 HIS   B HB2  1 
ATOM   5739 H HB3  . HIS   B 1 119 ? 39.138 -13.455 -8.687  1.00 15.34 ?  119 HIS   B HB3  1 
ATOM   5740 H HD2  . HIS   B 1 119 ? 38.082 -13.714 -5.136  1.00 18.03 ?  119 HIS   B HD2  1 
ATOM   5741 H HE1  . HIS   B 1 119 ? 40.455 -10.553 -5.353  1.00 20.34 ?  119 HIS   B HE1  1 
ATOM   5742 H HE2  . HIS   B 1 119 ? 39.260 -11.984 -3.904  1.00 20.14 ?  119 HIS   B HE2  1 
ATOM   5743 N N    . GLU   B 1 120 ? 36.846 -13.023 -10.960 1.00 13.09 ?  120 GLU   B N    1 
ATOM   5744 C CA   . GLU   B 1 120 ? 36.254 -13.604 -12.159 1.00 14.47 ?  120 GLU   B CA   1 
ATOM   5745 C C    . GLU   B 1 120 ? 36.923 -14.908 -12.573 1.00 13.16 ?  120 GLU   B C    1 
ATOM   5746 O O    . GLU   B 1 120 ? 36.254 -15.777 -13.147 1.00 13.53 ?  120 GLU   B O    1 
ATOM   5747 C CB   . GLU   B 1 120 ? 36.269 -12.598 -13.309 1.00 19.01 ?  120 GLU   B CB   1 
ATOM   5748 C CG   . GLU   B 1 120 ? 35.314 -11.437 -13.098 1.00 25.44 ?  120 GLU   B CG   1 
ATOM   5749 C CD   . GLU   B 1 120 ? 35.173 -10.560 -14.324 1.00 31.47 ?  120 GLU   B CD   1 
ATOM   5750 O OE1  . GLU   B 1 120 ? 36.174 -10.389 -15.055 1.00 33.81 ?  120 GLU   B OE1  1 
ATOM   5751 O OE2  . GLU   B 1 120 ? 34.060 -10.046 -14.557 1.00 34.24 -1 120 GLU   B OE2  1 
ATOM   5752 H H    . GLU   B 1 120 ? 37.279 -12.287 -11.086 1.00 15.69 ?  120 GLU   B H    1 
ATOM   5753 H HA   . GLU   B 1 120 ? 35.328 -13.809 -11.971 1.00 17.35 ?  120 GLU   B HA   1 
ATOM   5754 H HB2  . GLU   B 1 120 ? 37.159 -12.233 -13.404 1.00 22.80 ?  120 GLU   B HB2  1 
ATOM   5755 H HB3  . GLU   B 1 120 ? 36.005 -13.050 -14.128 1.00 22.80 ?  120 GLU   B HB3  1 
ATOM   5756 H HG2  . GLU   B 1 120 ? 34.431 -11.784 -12.885 1.00 30.51 ?  120 GLU   B HG2  1 
ATOM   5757 H HG3  . GLU   B 1 120 ? 35.637 -10.886 -12.370 1.00 30.51 ?  120 GLU   B HG3  1 
ATOM   5758 N N    . VAL   B 1 121 ? 38.225 -15.054 -12.316 1.00 12.78 ?  121 VAL   B N    1 
ATOM   5759 C CA   . VAL   B 1 121 ? 38.970 -16.263 -12.662 1.00 12.80 ?  121 VAL   B CA   1 
ATOM   5760 C C    . VAL   B 1 121 ? 40.081 -16.466 -11.640 1.00 12.11 ?  121 VAL   B C    1 
ATOM   5761 O O    . VAL   B 1 121 ? 40.758 -15.509 -11.246 1.00 12.95 ?  121 VAL   B O    1 
ATOM   5762 C CB   . VAL   B 1 121 ? 39.494 -16.221 -14.118 1.00 14.47 ?  121 VAL   B CB   1 
ATOM   5763 C CG1  . VAL   B 1 121 ? 40.365 -14.993 -14.367 1.00 16.08 ?  121 VAL   B CG1  1 
ATOM   5764 C CG2  . VAL   B 1 121 ? 40.236 -17.497 -14.466 1.00 15.59 ?  121 VAL   B CG2  1 
ATOM   5765 H H    . VAL   B 1 121 ? 38.711 -14.448 -11.937 1.00 15.32 ?  121 VAL   B H    1 
ATOM   5766 H HA   . VAL   B 1 121 ? 38.365 -17.014 -12.598 1.00 15.35 ?  121 VAL   B HA   1 
ATOM   5767 H HB   . VAL   B 1 121 ? 38.730 -16.157 -14.718 1.00 17.35 ?  121 VAL   B HB   1 
ATOM   5768 H HG11 . VAL   B 1 121 ? 40.672 -15.005 -15.288 1.00 19.28 ?  121 VAL   B HG11 1 
ATOM   5769 H HG12 . VAL   B 1 121 ? 39.839 -14.193 -14.206 1.00 19.28 ?  121 VAL   B HG12 1 
ATOM   5770 H HG13 . VAL   B 1 121 ? 41.123 -15.017 -13.765 1.00 19.28 ?  121 VAL   B HG13 1 
ATOM   5771 H HG21 . VAL   B 1 121 ? 40.433 -17.498 -15.416 1.00 18.70 ?  121 VAL   B HG21 1 
ATOM   5772 H HG22 . VAL   B 1 121 ? 41.064 -17.527 -13.959 1.00 18.70 ?  121 VAL   B HG22 1 
ATOM   5773 H HG23 . VAL   B 1 121 ? 39.680 -18.256 -14.242 1.00 18.70 ?  121 VAL   B HG23 1 
ATOM   5774 N N    . LEU   B 1 122 ? 40.265 -17.719 -11.206 1.00 11.64 ?  122 LEU   B N    1 
ATOM   5775 C CA   . LEU   B 1 122 ? 41.251 -18.067 -10.185 1.00 11.57 ?  122 LEU   B CA   1 
ATOM   5776 C C    . LEU   B 1 122 ? 41.906 -19.398 -10.507 1.00 11.42 ?  122 LEU   B C    1 
ATOM   5777 O O    . LEU   B 1 122 ? 41.246 -20.318 -11.010 1.00 12.52 ?  122 LEU   B O    1 
ATOM   5778 C CB   . LEU   B 1 122 ? 40.609 -18.292 -8.803  1.00 13.21 ?  122 LEU   B CB   1 
ATOM   5779 C CG   . LEU   B 1 122 ? 39.574 -17.276 -8.312  1.00 13.31 ?  122 LEU   B CG   1 
ATOM   5780 C CD1  . LEU   B 1 122 ? 38.172 -17.627 -8.791  1.00 14.23 ?  122 LEU   B CD1  1 
ATOM   5781 C CD2  . LEU   B 1 122 ? 39.613 -17.175 -6.800  1.00 13.00 ?  122 LEU   B CD2  1 
ATOM   5782 H H    . LEU   B 1 122 ? 39.821 -18.398 -11.492 1.00 13.95 ?  122 LEU   B H    1 
ATOM   5783 H HA   . LEU   B 1 122 ? 41.930 -17.373 -10.114 1.00 13.88 ?  122 LEU   B HA   1 
ATOM   5784 H HB2  . LEU   B 1 122 ? 40.167 -19.150 -8.817  1.00 15.84 ?  122 LEU   B HB2  1 
ATOM   5785 H HB3  . LEU   B 1 122 ? 41.318 -18.307 -8.143  1.00 15.84 ?  122 LEU   B HB3  1 
ATOM   5786 H HG   . LEU   B 1 122 ? 39.799 -16.399 -8.664  1.00 15.96 ?  122 LEU   B HG   1 
ATOM   5787 H HD11 . LEU   B 1 122 ? 37.543 -16.991 -8.415  1.00 17.07 ?  122 LEU   B HD11 1 
ATOM   5788 H HD12 . LEU   B 1 122 ? 38.152 -17.576 -9.760  1.00 17.07 ?  122 LEU   B HD12 1 
ATOM   5789 H HD13 . LEU   B 1 122 ? 37.956 -18.523 -8.499  1.00 17.07 ?  122 LEU   B HD13 1 
ATOM   5790 H HD21 . LEU   B 1 122 ? 38.932 -16.554 -6.502  1.00 15.58 ?  122 LEU   B HD21 1 
ATOM   5791 H HD22 . LEU   B 1 122 ? 39.448 -18.054 -6.421  1.00 15.58 ?  122 LEU   B HD22 1 
ATOM   5792 H HD23 . LEU   B 1 122 ? 40.491 -16.860 -6.524  1.00 15.58 ?  122 LEU   B HD23 1 
ATOM   5793 N N    . LEU   B 1 123 ? 43.192 -19.508 -10.147 1.00 11.16 ?  123 LEU   B N    1 
ATOM   5794 C CA   . LEU   B 1 123 ? 43.903 -20.780 -10.030 1.00 11.46 ?  123 LEU   B CA   1 
ATOM   5795 C C    . LEU   B 1 123 ? 43.879 -21.177 -8.560  1.00 11.21 ?  123 LEU   B C    1 
ATOM   5796 O O    . LEU   B 1 123 ? 44.236 -20.350 -7.708  1.00 11.67 ?  123 LEU   B O    1 
ATOM   5797 C CB   . LEU   B 1 123 ? 45.351 -20.606 -10.498 1.00 11.85 ?  123 LEU   B CB   1 
ATOM   5798 C CG   . LEU   B 1 123 ? 46.300 -21.783 -10.241 1.00 12.20 ?  123 LEU   B CG   1 
ATOM   5799 C CD1  . LEU   B 1 123 ? 45.869 -23.022 -11.015 1.00 13.06 ?  123 LEU   B CD1  1 
ATOM   5800 C CD2  . LEU   B 1 123 ? 47.723 -21.387 -10.604 1.00 13.18 ?  123 LEU   B CD2  1 
ATOM   5801 H H    . LEU   B 1 123 ? 43.687 -18.828 -9.948  1.00 13.37 ?  123 LEU   B H    1 
ATOM   5802 H HA   . LEU   B 1 123 ? 43.458 -21.462 -10.557 1.00 13.74 ?  123 LEU   B HA   1 
ATOM   5803 H HB2  . LEU   B 1 123 ? 45.336 -20.456 -11.459 1.00 14.21 ?  123 LEU   B HB2  1 
ATOM   5804 H HB3  . LEU   B 1 123 ? 45.723 -19.834 -10.056 1.00 14.21 ?  123 LEU   B HB3  1 
ATOM   5805 H HG   . LEU   B 1 123 ? 46.284 -22.006 -9.296  1.00 14.62 ?  123 LEU   B HG   1 
ATOM   5806 H HD11 . LEU   B 1 123 ? 46.500 -23.736 -10.840 1.00 15.65 ?  123 LEU   B HD11 1 
ATOM   5807 H HD12 . LEU   B 1 123 ? 44.982 -23.287 -10.717 1.00 15.65 ?  123 LEU   B HD12 1 
ATOM   5808 H HD13 . LEU   B 1 123 ? 45.852 -22.813 -11.959 1.00 15.65 ?  123 LEU   B HD13 1 
ATOM   5809 H HD21 . LEU   B 1 123 ? 48.312 -22.140 -10.436 1.00 15.80 ?  123 LEU   B HD21 1 
ATOM   5810 H HD22 . LEU   B 1 123 ? 47.753 -21.145 -11.542 1.00 15.80 ?  123 LEU   B HD22 1 
ATOM   5811 H HD23 . LEU   B 1 123 ? 47.986 -20.631 -10.056 1.00 15.80 ?  123 LEU   B HD23 1 
ATOM   5812 N N    . ALA   B 1 124 ? 43.448 -22.408 -8.252  1.00 11.12 ?  124 ALA   B N    1 
ATOM   5813 C CA   . ALA   B 1 124 ? 43.197 -22.725 -6.853  1.00 11.32 ?  124 ALA   B CA   1 
ATOM   5814 C C    . ALA   B 1 124 ? 43.473 -24.184 -6.528  1.00 10.67 ?  124 ALA   B C    1 
ATOM   5815 O O    . ALA   B 1 124 ? 43.340 -25.062 -7.393  1.00 11.37 ?  124 ALA   B O    1 
ATOM   5816 C CB   . ALA   B 1 124 ? 41.749 -22.416 -6.473  1.00 11.51 ?  124 ALA   B CB   1 
ATOM   5817 H H    . ALA   B 1 124 ? 43.284 -23.044 -8.816  1.00 13.33 ?  124 ALA   B H    1 
ATOM   5818 H HA   . ALA   B 1 124 ? 43.780 -22.179 -6.313  1.00 13.57 ?  124 ALA   B HA   1 
ATOM   5819 H HB1  . ALA   B 1 124 ? 41.609 -22.636 -5.541  1.00 13.80 ?  124 ALA   B HB1  1 
ATOM   5820 H HB2  . ALA   B 1 124 ? 41.587 -21.466 -6.615  1.00 13.80 ?  124 ALA   B HB2  1 
ATOM   5821 H HB3  . ALA   B 1 124 ? 41.153 -22.936 -7.032  1.00 13.80 ?  124 ALA   B HB3  1 
ATOM   5822 N N    . PRO   B 1 125 ? 43.770 -24.476 -5.264  1.00 10.95 ?  125 PRO   B N    1 
ATOM   5823 C CA   . PRO   B 1 125 ? 43.707 -25.840 -4.740  1.00 11.81 ?  125 PRO   B CA   1 
ATOM   5824 C C    . PRO   B 1 125 ? 42.304 -26.118 -4.199  1.00 11.92 ?  125 PRO   B C    1 
ATOM   5825 O O    . PRO   B 1 125 ? 41.505 -25.205 -3.992  1.00 12.48 ?  125 PRO   B O    1 
ATOM   5826 C CB   . PRO   B 1 125 ? 44.696 -25.758 -3.569  1.00 12.90 ?  125 PRO   B CB   1 
ATOM   5827 C CG   . PRO   B 1 125 ? 44.436 -24.379 -2.994  1.00 12.88 ?  125 PRO   B CG   1 
ATOM   5828 C CD   . PRO   B 1 125 ? 44.097 -23.509 -4.196  1.00 11.67 ?  125 PRO   B CD   1 
ATOM   5829 H HA   . PRO   B 1 125 ? 43.986 -26.507 -5.383  1.00 14.16 ?  125 PRO   B HA   1 
ATOM   5830 H HB2  . PRO   B 1 125 ? 44.502 -26.447 -2.910  1.00 15.46 ?  125 PRO   B HB2  1 
ATOM   5831 H HB3  . PRO   B 1 125 ? 45.609 -25.830 -3.888  1.00 15.46 ?  125 PRO   B HB3  1 
ATOM   5832 H HG2  . PRO   B 1 125 ? 43.680 -24.411 -2.379  1.00 15.44 ?  125 PRO   B HG2  1 
ATOM   5833 H HG3  . PRO   B 1 125 ? 45.227 -24.047 -2.540  1.00 15.44 ?  125 PRO   B HG3  1 
ATOM   5834 H HD2  . PRO   B 1 125 ? 43.335 -22.939 -4.005  1.00 14.00 ?  125 PRO   B HD2  1 
ATOM   5835 H HD3  . PRO   B 1 125 ? 44.875 -22.975 -4.451  1.00 14.00 ?  125 PRO   B HD3  1 
ATOM   5836 N N    . LEU   B 1 126 ? 42.035 -27.399 -3.923  1.00 12.55 ?  126 LEU   B N    1 
ATOM   5837 C CA   . LEU   B 1 126 ? 40.816 -27.770 -3.213  1.00 13.10 ?  126 LEU   B CA   1 
ATOM   5838 C C    . LEU   B 1 126 ? 40.929 -27.368 -1.749  1.00 12.88 ?  126 LEU   B C    1 
ATOM   5839 O O    . LEU   B 1 126 ? 41.824 -27.826 -1.032  1.00 14.75 ?  126 LEU   B O    1 
ATOM   5840 C CB   . LEU   B 1 126 ? 40.565 -29.268 -3.326  1.00 14.45 ?  126 LEU   B CB   1 
ATOM   5841 C CG   . LEU   B 1 126 ? 40.027 -29.765 -4.669  1.00 15.25 ?  126 LEU   B CG   1 
ATOM   5842 C CD1  . LEU   B 1 126 ? 40.075 -31.282 -4.737  1.00 17.25 ?  126 LEU   B CD1  1 
ATOM   5843 C CD2  . LEU   B 1 126 ? 38.606 -29.262 -4.914  1.00 15.43 ?  126 LEU   B CD2  1 
ATOM   5844 H H    . LEU   B 1 126 ? 42.547 -28.064 -4.124  1.00 15.05 ?  126 LEU   B H    1 
ATOM   5845 H HA   . LEU   B 1 126 ? 40.068 -27.297 -3.601  1.00 15.70 ?  126 LEU   B HA   1 
ATOM   5846 H HB2  . LEU   B 1 126 ? 41.398 -29.729 -3.157  1.00 17.32 ?  126 LEU   B HB2  1 
ATOM   5847 H HB3  . LEU   B 1 126 ? 39.916 -29.515 -2.646  1.00 17.32 ?  126 LEU   B HB3  1 
ATOM   5848 H HG   . LEU   B 1 126 ? 40.592 -29.417 -5.377  1.00 18.28 ?  126 LEU   B HG   1 
ATOM   5849 H HD11 . LEU   B 1 126 ? 39.730 -31.570 -5.596  1.00 20.69 ?  126 LEU   B HD11 1 
ATOM   5850 H HD12 . LEU   B 1 126 ? 40.993 -31.575 -4.632  1.00 20.69 ?  126 LEU   B HD12 1 
ATOM   5851 H HD13 . LEU   B 1 126 ? 39.528 -31.646 -4.022  1.00 20.69 ?  126 LEU   B HD13 1 
ATOM   5852 H HD21 . LEU   B 1 126 ? 38.260 -29.679 -5.718  1.00 18.50 ?  126 LEU   B HD21 1 
ATOM   5853 H HD22 . LEU   B 1 126 ? 38.053 -29.499 -4.153  1.00 18.50 ?  126 LEU   B HD22 1 
ATOM   5854 H HD23 . LEU   B 1 126 ? 38.624 -28.298 -5.023  1.00 18.50 ?  126 LEU   B HD23 1 
ATOM   5855 N N    . LEU   B 1 127 ? 39.999 -26.536 -1.294  1.00 12.77 ?  127 LEU   B N    1 
ATOM   5856 C CA   . LEU   B 1 127 ? 40.048 -26.040 0.070   1.00 13.30 ?  127 LEU   B CA   1 
ATOM   5857 C C    . LEU   B 1 127 ? 39.781 -27.164 1.065   1.00 13.25 ?  127 LEU   B C    1 
ATOM   5858 O O    . LEU   B 1 127 ? 38.962 -28.060 0.832   1.00 13.17 ?  127 LEU   B O    1 
ATOM   5859 C CB   . LEU   B 1 127 ? 39.025 -24.922 0.271   1.00 13.99 ?  127 LEU   B CB   1 
ATOM   5860 C CG   . LEU   B 1 127 ? 39.207 -23.651 -0.561  1.00 14.57 ?  127 LEU   B CG   1 
ATOM   5861 C CD1  . LEU   B 1 127 ? 38.098 -22.675 -0.214  1.00 14.03 ?  127 LEU   B CD1  1 
ATOM   5862 C CD2  . LEU   B 1 127 ? 40.579 -23.020 -0.337  1.00 15.19 ?  127 LEU   B CD2  1 
ATOM   5863 H H    . LEU   B 1 127 ? 39.329 -26.239 -1.755  1.00 15.31 ?  127 LEU   B H    1 
ATOM   5864 H HA   . LEU   B 1 127 ? 40.931 -25.676 0.245   1.00 15.95 ?  127 LEU   B HA   1 
ATOM   5865 H HB2  . LEU   B 1 127 ? 38.147 -25.273 0.064   1.00 16.77 ?  127 LEU   B HB2  1 
ATOM   5866 H HB3  . LEU   B 1 127 ? 39.050 -24.652 1.203   1.00 16.77 ?  127 LEU   B HB3  1 
ATOM   5867 H HG   . LEU   B 1 127 ? 39.116 -23.863 -1.501  1.00 17.48 ?  127 LEU   B HG   1 
ATOM   5868 H HD11 . LEU   B 1 127 ? 38.208 -21.864 -0.738  1.00 16.82 ?  127 LEU   B HD11 1 
ATOM   5869 H HD12 . LEU   B 1 127 ? 37.240 -23.081 -0.410  1.00 16.82 ?  127 LEU   B HD12 1 
ATOM   5870 H HD13 . LEU   B 1 127 ? 38.150 -22.459 0.734   1.00 16.82 ?  127 LEU   B HD13 1 
ATOM   5871 H HD21 . LEU   B 1 127 ? 40.616 -22.162 -0.790  1.00 18.21 ?  127 LEU   B HD21 1 
ATOM   5872 H HD22 . LEU   B 1 127 ? 40.719 -22.896 0.616   1.00 18.21 ?  127 LEU   B HD22 1 
ATOM   5873 H HD23 . LEU   B 1 127 ? 41.256 -23.613 -0.696  1.00 18.21 ?  127 LEU   B HD23 1 
ATOM   5874 N N    . SER   B 1 128 ? 40.460 -27.080 2.199   1.00 13.10 ?  128 SER   B N    1 
ATOM   5875 C CA   . SER   B 1 128 ? 40.354 -28.002 3.318   1.00 13.62 ?  128 SER   B CA   1 
ATOM   5876 C C    . SER   B 1 128 ? 40.855 -29.407 2.992   1.00 14.61 ?  128 SER   B C    1 
ATOM   5877 O O    . SER   B 1 128 ? 40.757 -30.292 3.840   1.00 15.95 ?  128 SER   B O    1 
ATOM   5878 C CB   . SER   B 1 128 ? 38.954 -28.019 3.946   1.00 13.76 ?  128 SER   B CB   1 
ATOM   5879 O OG   . SER   B 1 128 ? 38.627 -26.745 4.497   1.00 14.53 ?  128 SER   B OG   1 
ATOM   5880 H H    . SER   B 1 128 ? 41.019 -26.442 2.355   1.00 15.70 ?  128 SER   B H    1 
ATOM   5881 H HA   . SER   B 1 128 ? 40.938 -27.666 4.005   1.00 16.33 ?  128 SER   B HA   1 
ATOM   5882 H HB2  . SER   B 1 128 ? 38.298 -28.257 3.271   1.00 16.50 ?  128 SER   B HB2  1 
ATOM   5883 H HB3  . SER   B 1 128 ? 38.939 -28.690 4.660   1.00 16.50 ?  128 SER   B HB3  1 
ATOM   5884 H HG   . SER   B 1 128 ? 39.191 -26.543 5.085   1.00 17.43 ?  128 SER   B HG   1 
ATOM   5885 N N    . ALA   B 1 129 ? 41.433 -29.623 1.810   1.00 15.60 ?  129 ALA   B N    1 
ATOM   5886 C CA   . ALA   B 1 129 ? 41.978 -30.923 1.450   1.00 16.57 ?  129 ALA   B CA   1 
ATOM   5887 C C    . ALA   B 1 129 ? 43.365 -31.107 2.055   1.00 15.45 ?  129 ALA   B C    1 
ATOM   5888 O O    . ALA   B 1 129 ? 43.922 -30.209 2.703   1.00 15.50 ?  129 ALA   B O    1 
ATOM   5889 C CB   . ALA   B 1 129 ? 42.025 -31.076 -0.069  1.00 19.05 ?  129 ALA   B CB   1 
ATOM   5890 H H    . ALA   B 1 129 ? 41.519 -29.025 1.195   1.00 18.70 ?  129 ALA   B H    1 
ATOM   5891 H HA   . ALA   B 1 129 ? 41.400 -31.614 1.803   1.00 19.87 ?  129 ALA   B HA   1 
ATOM   5892 H HB1  . ALA   B 1 129 ? 42.385 -31.952 -0.285  1.00 22.85 ?  129 ALA   B HB1  1 
ATOM   5893 H HB2  . ALA   B 1 129 ? 41.128 -30.991 -0.422  1.00 22.85 ?  129 ALA   B HB2  1 
ATOM   5894 H HB3  . ALA   B 1 129 ? 42.596 -30.385 -0.438  1.00 22.85 ?  129 ALA   B HB3  1 
ATOM   5895 N N    . GLY   B 1 130 ? 43.929 -32.296 1.833   1.00 15.45 ?  130 GLY   B N    1 
ATOM   5896 C CA   . GLY   B 1 130 ? 45.317 -32.530 2.183   1.00 16.26 ?  130 GLY   B CA   1 
ATOM   5897 C C    . GLY   B 1 130 ? 45.528 -32.439 3.675   1.00 16.25 ?  130 GLY   B C    1 
ATOM   5898 O O    . GLY   B 1 130 ? 44.829 -33.083 4.472   1.00 17.13 ?  130 GLY   B O    1 
ATOM   5899 H H    . GLY   B 1 130 ? 43.529 -32.969 1.479   1.00 18.53 ?  130 GLY   B H    1 
ATOM   5900 H HA2  . GLY   B 1 130 ? 45.581 -33.417 1.886   1.00 19.50 ?  130 GLY   B HA2  1 
ATOM   5901 H HA3  . GLY   B 1 130 ? 45.880 -31.876 1.746   1.00 19.50 ?  130 GLY   B HA3  1 
ATOM   5902 N N    . ILE   B 1 131 ? 46.502 -31.611 4.065   1.00 16.60 ?  131 ILE   B N    1 
ATOM   5903 C CA   . ILE   B 1 131 ? 46.851 -31.480 5.471   1.00 17.12 ?  131 ILE   B CA   1 
ATOM   5904 C C    . ILE   B 1 131 ? 45.735 -30.875 6.303   1.00 16.60 ?  131 ILE   B C    1 
ATOM   5905 O O    . ILE   B 1 131 ? 45.810 -30.934 7.534   1.00 18.13 ?  131 ILE   B O    1 
ATOM   5906 C CB   . ILE   B 1 131 ? 48.173 -30.705 5.672   1.00 19.10 ?  131 ILE   B CB   1 
ATOM   5907 C CG1  . ILE   B 1 131 ? 48.012 -29.225 5.290   1.00 19.96 ?  131 ILE   B CG1  1 
ATOM   5908 C CG2  . ILE   B 1 131 ? 49.298 -31.361 4.870   1.00 20.07 ?  131 ILE   B CG2  1 
ATOM   5909 C CD1  . ILE   B 1 131 ? 49.221 -28.364 5.624   1.00 20.99 ?  131 ILE   B CD1  1 
ATOM   5910 H H    . ILE   B 1 131 ? 46.969 -31.118 3.537   1.00 19.91 ?  131 ILE   B H    1 
ATOM   5911 H HA   . ILE   B 1 131 ? 46.991 -32.369 5.822   1.00 20.53 ?  131 ILE   B HA   1 
ATOM   5912 H HB   . ILE   B 1 131 ? 48.402 -30.749 6.613   1.00 22.91 ?  131 ILE   B HB   1 
ATOM   5913 H HG12 . ILE   B 1 131 ? 47.858 -29.169 4.334   1.00 23.94 ?  131 ILE   B HG12 1 
ATOM   5914 H HG13 . ILE   B 1 131 ? 47.250 -28.853 5.765   1.00 23.94 ?  131 ILE   B HG13 1 
ATOM   5915 H HG21 . ILE   B 1 131 ? 50.136 -30.952 5.119   1.00 24.07 ?  131 ILE   B HG21 1 
ATOM   5916 H HG22 . ILE   B 1 131 ? 49.311 -32.308 5.072   1.00 24.07 ?  131 ILE   B HG22 1 
ATOM   5917 H HG23 . ILE   B 1 131 ? 49.125 -31.225 3.925   1.00 24.07 ?  131 ILE   B HG23 1 
ATOM   5918 H HD11 . ILE   B 1 131 ? 49.009 -27.438 5.429   1.00 25.18 ?  131 ILE   B HD11 1 
ATOM   5919 H HD12 . ILE   B 1 131 ? 49.427 -28.464 6.567   1.00 25.18 ?  131 ILE   B HD12 1 
ATOM   5920 H HD13 . ILE   B 1 131 ? 49.972 -28.653 5.087   1.00 25.18 ?  131 ILE   B HD13 1 
ATOM   5921 N N    . PHE   B 1 132 ? 44.705 -30.297 5.670   1.00 15.16 ?  132 PHE   B N    1 
ATOM   5922 C CA   . PHE   B 1 132 ? 43.544 -29.790 6.398   1.00 15.59 ?  132 PHE   B CA   1 
ATOM   5923 C C    . PHE   B 1 132 ? 42.520 -30.878 6.722   1.00 17.12 ?  132 PHE   B C    1 
ATOM   5924 O O    . PHE   B 1 132 ? 41.612 -30.630 7.522   1.00 19.01 ?  132 PHE   B O    1 
ATOM   5925 C CB   . PHE   B 1 132 ? 42.872 -28.653 5.615   1.00 14.73 ?  132 PHE   B CB   1 
ATOM   5926 C CG   . PHE   B 1 132 ? 43.572 -27.312 5.736   1.00 15.12 ?  132 PHE   B CG   1 
ATOM   5927 C CD1  . PHE   B 1 132 ? 44.869 -27.130 5.276   1.00 16.31 ?  132 PHE   B CD1  1 
ATOM   5928 C CD2  . PHE   B 1 132 ? 42.899 -26.214 6.259   1.00 14.71 ?  132 PHE   B CD2  1 
ATOM   5929 C CE1  . PHE   B 1 132 ? 45.493 -25.889 5.375   1.00 16.83 ?  132 PHE   B CE1  1 
ATOM   5930 C CE2  . PHE   B 1 132 ? 43.513 -24.970 6.354   1.00 15.24 ?  132 PHE   B CE2  1 
ATOM   5931 C CZ   . PHE   B 1 132 ? 44.808 -24.811 5.910   1.00 16.58 ?  132 PHE   B CZ   1 
ATOM   5932 H H    . PHE   B 1 132 ? 44.657 -30.181 4.815   1.00 18.18 ?  132 PHE   B H    1 
ATOM   5933 H HA   . PHE   B 1 132 ? 43.850 -29.413 7.235   1.00 18.70 ?  132 PHE   B HA   1 
ATOM   5934 H HB2  . PHE   B 1 132 ? 42.858 -28.887 4.676   1.00 17.67 ?  132 PHE   B HB2  1 
ATOM   5935 H HB3  . PHE   B 1 132 ? 41.965 -28.539 5.941   1.00 17.67 ?  132 PHE   B HB3  1 
ATOM   5936 H HD1  . PHE   B 1 132 ? 45.337 -27.853 4.917   1.00 19.56 ?  132 PHE   B HD1  1 
ATOM   5937 H HD2  . PHE   B 1 132 ? 42.026 -26.316 6.557   1.00 17.64 ?  132 PHE   B HD2  1 
ATOM   5938 H HE1  . PHE   B 1 132 ? 46.370 -25.787 5.077   1.00 20.18 ?  132 PHE   B HE1  1 
ATOM   5939 H HE2  . PHE   B 1 132 ? 43.054 -24.247 6.720   1.00 18.27 ?  132 PHE   B HE2  1 
ATOM   5940 H HZ   . PHE   B 1 132 ? 45.227 -23.980 5.981   1.00 19.89 ?  132 PHE   B HZ   1 
ATOM   5941 N N    . GLY   B 1 133 ? 42.625 -32.069 6.124   1.00 16.91 ?  133 GLY   B N    1 
ATOM   5942 C CA   . GLY   B 1 133 ? 41.909 -33.234 6.618   1.00 17.76 ?  133 GLY   B CA   1 
ATOM   5943 C C    . GLY   B 1 133 ? 40.514 -33.501 6.078   1.00 17.92 ?  133 GLY   B C    1 
ATOM   5944 O O    . GLY   B 1 133 ? 39.929 -34.525 6.443   1.00 19.88 ?  133 GLY   B O    1 
ATOM   5945 H H    . GLY   B 1 133 ? 43.118 -32.221 5.434   1.00 20.28 ?  133 GLY   B H    1 
ATOM   5946 H HA2  . GLY   B 1 133 ? 42.446 -34.017 6.431   1.00 21.30 ?  133 GLY   B HA2  1 
ATOM   5947 H HA3  . GLY   B 1 133 ? 41.835 -33.152 7.582   1.00 21.30 ?  133 GLY   B HA3  1 
ATOM   5948 N N    . ALA   B 1 134 ? 39.947 -32.632 5.247   1.00 16.92 ?  134 ALA   B N    1 
ATOM   5949 C CA   . ALA   B 1 134 ? 38.624 -32.911 4.709   1.00 17.17 ?  134 ALA   B CA   1 
ATOM   5950 C C    . ALA   B 1 134 ? 38.711 -33.907 3.556   1.00 17.38 ?  134 ALA   B C    1 
ATOM   5951 O O    . ALA   B 1 134 ? 39.763 -34.095 2.940   1.00 18.69 ?  134 ALA   B O    1 
ATOM   5952 C CB   . ALA   B 1 134 ? 37.948 -31.625 4.236   1.00 17.76 ?  134 ALA   B CB   1 
ATOM   5953 H H    . ALA   B 1 134 ? 40.297 -31.884 4.993   1.00 20.30 ?  134 ALA   B H    1 
ATOM   5954 H HA   . ALA   B 1 134 ? 38.075 -33.300 5.407   1.00 20.59 ?  134 ALA   B HA   1 
ATOM   5955 H HB1  . ALA   B 1 134 ? 37.064 -31.843 3.898   1.00 21.30 ?  134 ALA   B HB1  1 
ATOM   5956 H HB2  . ALA   B 1 134 ? 37.874 -31.013 4.984   1.00 21.30 ?  134 ALA   B HB2  1 
ATOM   5957 H HB3  . ALA   B 1 134 ? 38.483 -31.227 3.532   1.00 21.30 ?  134 ALA   B HB3  1 
ATOM   5958 N N    . ASP   B 1 135 ? 37.581 -34.535 3.265   1.00 17.44 ?  135 ASP   B N    1 
ATOM   5959 C CA   . ASP   B 1 135 ? 37.484 -35.429 2.120   1.00 18.36 ?  135 ASP   B CA   1 
ATOM   5960 C C    . ASP   B 1 135 ? 37.584 -34.593 0.852   1.00 17.23 ?  135 ASP   B C    1 
ATOM   5961 O O    . ASP   B 1 135 ? 36.733 -33.721 0.631   1.00 17.28 ?  135 ASP   B O    1 
ATOM   5962 C CB   . ASP   B 1 135 ? 36.141 -36.159 2.174   1.00 20.08 ?  135 ASP   B CB   1 
ATOM   5963 C CG   . ASP   B 1 135 ? 35.949 -37.139 1.032   1.00 22.09 ?  135 ASP   B CG   1 
ATOM   5964 O OD1  . ASP   B 1 135 ? 36.820 -37.200 0.139   1.00 22.05 ?  135 ASP   B OD1  1 
ATOM   5965 O OD2  . ASP   B 1 135 ? 34.925 -37.867 1.039   1.00 25.46 -1 135 ASP   B OD2  1 
ATOM   5966 H H    . ASP   B 1 135 ? 36.854 -34.458 3.714   1.00 20.91 ?  135 ASP   B H    1 
ATOM   5967 H HA   . ASP   B 1 135 ? 38.203 -36.080 2.151   1.00 22.02 ?  135 ASP   B HA   1 
ATOM   5968 H HB2  . ASP   B 1 135 ? 36.090 -36.654 3.003   1.00 24.09 ?  135 ASP   B HB2  1 
ATOM   5969 H HB3  . ASP   B 1 135 ? 35.431 -35.503 2.127   1.00 24.09 ?  135 ASP   B HB3  1 
ATOM   5970 N N    . PRO   B 1 136 ? 38.590 -34.804 -0.000  1.00 17.57 ?  136 PRO   B N    1 
ATOM   5971 C CA   . PRO   B 1 136 ? 38.689 -33.974 -1.212  1.00 16.79 ?  136 PRO   B CA   1 
ATOM   5972 C C    . PRO   B 1 136 ? 37.503 -34.125 -2.144  1.00 16.00 ?  136 PRO   B C    1 
ATOM   5973 O O    . PRO   B 1 136 ? 37.180 -33.178 -2.871  1.00 15.29 ?  136 PRO   B O    1 
ATOM   5974 C CB   . PRO   B 1 136 ? 40.001 -34.446 -1.858  1.00 17.72 ?  136 PRO   B CB   1 
ATOM   5975 C CG   . PRO   B 1 136 ? 40.199 -35.841 -1.327  1.00 18.91 ?  136 PRO   B CG   1 
ATOM   5976 C CD   . PRO   B 1 136 ? 39.663 -35.808 0.074   1.00 18.20 ?  136 PRO   B CD   1 
ATOM   5977 H HA   . PRO   B 1 136 ? 38.776 -33.038 -0.975  1.00 20.14 ?  136 PRO   B HA   1 
ATOM   5978 H HB2  . PRO   B 1 136 ? 39.909 -34.455 -2.826  1.00 21.25 ?  136 PRO   B HB2  1 
ATOM   5979 H HB3  . PRO   B 1 136 ? 40.726 -33.864 -1.588  1.00 21.25 ?  136 PRO   B HB3  1 
ATOM   5980 H HG2  . PRO   B 1 136 ? 39.702 -36.475 -1.866  1.00 22.68 ?  136 PRO   B HG2  1 
ATOM   5981 H HG3  . PRO   B 1 136 ? 41.144 -36.059 -1.322  1.00 22.68 ?  136 PRO   B HG3  1 
ATOM   5982 H HD2  . PRO   B 1 136 ? 39.296 -36.671 0.319   1.00 21.83 ?  136 PRO   B HD2  1 
ATOM   5983 H HD3  . PRO   B 1 136 ? 40.347 -35.520 0.699   1.00 21.83 ?  136 PRO   B HD3  1 
ATOM   5984 N N    . ILE   B 1 137 ? 36.848 -35.291 -2.152  1.00 16.05 ?  137 ILE   B N    1 
ATOM   5985 C CA   . ILE   B 1 137 ? 35.628 -35.454 -2.940  1.00 16.70 ?  137 ILE   B CA   1 
ATOM   5986 C C    . ILE   B 1 137 ? 34.557 -34.483 -2.460  1.00 16.60 ?  137 ILE   B C    1 
ATOM   5987 O O    . ILE   B 1 137 ? 33.837 -33.872 -3.261  1.00 15.77 ?  137 ILE   B O    1 
ATOM   5988 C CB   . ILE   B 1 137 ? 35.151 -36.919 -2.880  1.00 18.74 ?  137 ILE   B CB   1 
ATOM   5989 C CG1  . ILE   B 1 137 ? 36.142 -37.827 -3.611  1.00 21.34 ?  137 ILE   B CG1  1 
ATOM   5990 C CG2  . ILE   B 1 137 ? 33.751 -37.062 -3.467  1.00 19.49 ?  137 ILE   B CG2  1 
ATOM   5991 C CD1  . ILE   B 1 137 ? 35.827 -39.307 -3.497  1.00 23.92 ?  137 ILE   B CD1  1 
ATOM   5992 H H    . ILE   B 1 137 ? 37.082 -35.995 -1.718  1.00 19.25 ?  137 ILE   B H    1 
ATOM   5993 H HA   . ILE   B 1 137 ? 35.818 -35.248 -3.870  1.00 20.02 ?  137 ILE   B HA   1 
ATOM   5994 H HB   . ILE   B 1 137 ? 35.115 -37.193 -1.956  1.00 22.47 ?  137 ILE   B HB   1 
ATOM   5995 H HG12 . ILE   B 1 137 ? 36.146 -37.603 -4.554  1.00 25.59 ?  137 ILE   B HG12 1 
ATOM   5996 H HG13 . ILE   B 1 137 ? 37.026 -37.689 -3.236  1.00 25.59 ?  137 ILE   B HG13 1 
ATOM   5997 H HG21 . ILE   B 1 137 ? 33.500 -38.000 -3.495  1.00 23.38 ?  137 ILE   B HG21 1 
ATOM   5998 H HG22 . ILE   B 1 137 ? 33.118 -36.587 -2.909  1.00 23.38 ?  137 ILE   B HG22 1 
ATOM   5999 H HG23 . ILE   B 1 137 ? 33.743 -36.696 -4.365  1.00 23.38 ?  137 ILE   B HG23 1 
ATOM   6000 H HD11 . ILE   B 1 137 ? 36.484 -39.797 -4.011  1.00 28.69 ?  137 ILE   B HD11 1 
ATOM   6001 H HD12 . ILE   B 1 137 ? 35.868 -39.574 -2.564  1.00 28.69 ?  137 ILE   B HD12 1 
ATOM   6002 H HD13 . ILE   B 1 137 ? 34.943 -39.486 -3.854  1.00 28.69 ?  137 ILE   B HD13 1 
ATOM   6003 N N    . HIS   B 1 138 ? 34.432 -34.329 -1.146  1.00 16.62 ?  138 HIS   B N    1 
ATOM   6004 C CA   . HIS   B 1 138 ? 33.477 -33.368 -0.615  1.00 16.94 ?  138 HIS   B CA   1 
ATOM   6005 C C    . HIS   B 1 138 ? 33.897 -31.940 -0.931  1.00 15.72 ?  138 HIS   B C    1 
ATOM   6006 O O    . HIS   B 1 138 ? 33.052 -31.098 -1.243  1.00 16.20 ?  138 HIS   B O    1 
ATOM   6007 C CB   . HIS   B 1 138 ? 33.339 -33.545 0.889   1.00 18.18 ?  138 HIS   B CB   1 
ATOM   6008 C CG   . HIS   B 1 138 ? 32.400 -32.567 1.515   1.00 19.10 ?  138 HIS   B CG   1 
ATOM   6009 N ND1  . HIS   B 1 138 ? 31.061 -32.510 1.192   1.00 20.43 ?  138 HIS   B ND1  1 
ATOM   6010 C CD2  . HIS   B 1 138 ? 32.612 -31.580 2.417   1.00 19.72 ?  138 HIS   B CD2  1 
ATOM   6011 C CE1  . HIS   B 1 138 ? 30.485 -31.544 1.884   1.00 20.51 ?  138 HIS   B CE1  1 
ATOM   6012 N NE2  . HIS   B 1 138 ? 31.404 -30.967 2.637   1.00 20.01 ?  138 HIS   B NE2  1 
ATOM   6013 H H    . HIS   B 1 138 ? 34.882 -34.762 -0.557  1.00 19.93 ?  138 HIS   B H    1 
ATOM   6014 H HA   . HIS   B 1 138 ? 32.608 -33.530 -1.022  1.00 20.31 ?  138 HIS   B HA   1 
ATOM   6015 H HB2  . HIS   B 1 138 ? 32.999 -34.435 1.070   1.00 21.81 ?  138 HIS   B HB2  1 
ATOM   6016 H HB3  . HIS   B 1 138 ? 34.207 -33.429 1.298   1.00 21.81 ?  138 HIS   B HB3  1 
ATOM   6017 H HD1  . HIS   B 1 138 ? 30.662 -33.033 0.633   1.00 24.51 ?  138 HIS   B HD1  1 
ATOM   6018 H HD2  . HIS   B 1 138 ? 33.415 -31.361 2.822   1.00 23.66 ?  138 HIS   B HD2  1 
ATOM   6019 H HE1  . HIS   B 1 138 ? 29.578 -31.318 1.847   1.00 24.60 ?  138 HIS   B HE1  1 
ATOM   6020 N N    . SER   B 1 139 ? 35.189 -31.640 -0.849  1.00 14.84 ?  139 SER   B N    1 
ATOM   6021 C CA   . SER   B 1 139 ? 35.624 -30.289 -1.168  1.00 14.61 ?  139 SER   B CA   1 
ATOM   6022 C C    . SER   B 1 139 ? 35.281 -29.940 -2.607  1.00 13.65 ?  139 SER   B C    1 
ATOM   6023 O O    . SER   B 1 139 ? 34.834 -28.823 -2.890  1.00 14.20 ?  139 SER   B O    1 
ATOM   6024 C CB   . SER   B 1 139 ? 37.119 -30.155 -0.914  1.00 14.47 ?  139 SER   B CB   1 
ATOM   6025 O OG   . SER   B 1 139 ? 37.531 -28.826 -1.172  1.00 14.78 ?  139 SER   B OG   1 
ATOM   6026 H H    . SER   B 1 139 ? 35.809 -32.186 -0.620  1.00 17.80 ?  139 SER   B H    1 
ATOM   6027 H HA   . SER   B 1 139 ? 35.161 -29.666 -0.593  1.00 17.52 ?  139 SER   B HA   1 
ATOM   6028 H HB2  . SER   B 1 139 ? 37.305 -30.369 0.013   1.00 17.35 ?  139 SER   B HB2  1 
ATOM   6029 H HB3  . SER   B 1 139 ? 37.600 -30.762 -1.500  1.00 17.35 ?  139 SER   B HB3  1 
ATOM   6030 H HG   . SER   B 1 139 ? 38.364 -28.748 -1.037  1.00 17.72 ?  139 SER   B HG   1 
ATOM   6031 N N    . LEU   B 1 140 ? 35.472 -30.885 -3.531  1.00 13.50 ?  140 LEU   B N    1 
ATOM   6032 C CA   . LEU   B 1 140 ? 35.109 -30.636 -4.920  1.00 13.64 ?  140 LEU   B CA   1 
ATOM   6033 C C    . LEU   B 1 140 ? 33.605 -30.412 -5.052  1.00 14.08 ?  140 LEU   B C    1 
ATOM   6034 O O    . LEU   B 1 140 ? 33.163 -29.526 -5.788  1.00 14.09 ?  140 LEU   B O    1 
ATOM   6035 C CB   . LEU   B 1 140 ? 35.582 -31.801 -5.794  1.00 14.12 ?  140 LEU   B CB   1 
ATOM   6036 C CG   . LEU   B 1 140 ? 35.222 -31.696 -7.270  1.00 14.30 ?  140 LEU   B CG   1 
ATOM   6037 C CD1  . LEU   B 1 140 ? 35.788 -30.416 -7.868  1.00 15.36 ?  140 LEU   B CD1  1 
ATOM   6038 C CD2  . LEU   B 1 140 ? 35.685 -32.927 -8.034  1.00 15.69 ?  140 LEU   B CD2  1 
ATOM   6039 H H    . LEU   B 1 140 ? 35.802 -31.662 -3.380  1.00 16.19 ?  140 LEU   B H    1 
ATOM   6040 H HA   . LEU   B 1 140 ? 35.564 -29.836 -5.225  1.00 16.36 ?  140 LEU   B HA   1 
ATOM   6041 H HB2  . LEU   B 1 140 ? 36.550 -31.864 -5.736  1.00 16.94 ?  140 LEU   B HB2  1 
ATOM   6042 H HB3  . LEU   B 1 140 ? 35.186 -32.622 -5.461  1.00 16.94 ?  140 LEU   B HB3  1 
ATOM   6043 H HG   . LEU   B 1 140 ? 34.258 -31.647 -7.348  1.00 17.14 ?  140 LEU   B HG   1 
ATOM   6044 H HD11 . LEU   B 1 140 ? 35.675 -30.443 -8.829  1.00 18.42 ?  140 LEU   B HD11 1 
ATOM   6045 H HD12 . LEU   B 1 140 ? 35.306 -29.655 -7.501  1.00 18.42 ?  140 LEU   B HD12 1 
ATOM   6046 H HD13 . LEU   B 1 140 ? 36.728 -30.351 -7.644  1.00 18.42 ?  140 LEU   B HD13 1 
ATOM   6047 H HD21 . LEU   B 1 140 ? 35.435 -32.823 -8.966  1.00 18.81 ?  140 LEU   B HD21 1 
ATOM   6048 H HD22 . LEU   B 1 140 ? 36.642 -33.008 -7.949  1.00 18.81 ?  140 LEU   B HD22 1 
ATOM   6049 H HD23 . LEU   B 1 140 ? 35.244 -33.705 -7.659  1.00 18.81 ?  140 LEU   B HD23 1 
ATOM   6050 N N    . ARG   B 1 141 ? 32.809 -31.206 -4.335  1.00 13.99 ?  141 ARG   B N    1 
ATOM   6051 C CA   . ARG   B 1 141 ? 31.358 -31.035 -4.319  1.00 15.30 ?  141 ARG   B CA   1 
ATOM   6052 C C    . ARG   B 1 141 ? 30.977 -29.621 -3.896  1.00 14.74 ?  141 ARG   B C    1 
ATOM   6053 O O    . ARG   B 1 141 ? 30.173 -28.943 -4.556  1.00 15.13 ?  141 ARG   B O    1 
ATOM   6054 C CB   . ARG   B 1 141 ? 30.777 -32.060 -3.335  1.00 16.72 ?  141 ARG   B CB   1 
ATOM   6055 C CG   . ARG   B 1 141 ? 29.312 -31.945 -2.999  1.00 18.66 ?  141 ARG   B CG   1 
ATOM   6056 C CD   . ARG   B 1 141 ? 28.508 -32.579 -4.063  1.00 20.51 ?  141 ARG   B CD   1 
ATOM   6057 N NE   . ARG   B 1 141 ? 28.234 -31.670 -5.165  1.00 21.07 ?  141 ARG   B NE   1 
ATOM   6058 C CZ   . ARG   B 1 141 ? 28.217 -32.023 -6.443  1.00 20.52 ?  141 ARG   B CZ   1 
ATOM   6059 N NH1  . ARG   B 1 141 ? 28.658 -33.208 -6.841  1.00 20.17 ?  141 ARG   B NH1  1 
ATOM   6060 N NH2  . ARG   B 1 141 ? 27.745 -31.165 -7.344  1.00 21.02 ?  141 ARG   B NH2  1 
ATOM   6061 H H    . ARG   B 1 141 ? 33.092 -31.854 -3.846  1.00 16.77 ?  141 ARG   B H    1 
ATOM   6062 H HA   . ARG   B 1 141 ? 30.997 -31.207 -5.200  1.00 18.35 ?  141 ARG   B HA   1 
ATOM   6063 H HB2  . ARG   B 1 141 ? 30.930 -32.948 -3.702  1.00 20.05 ?  141 ARG   B HB2  1 
ATOM   6064 H HB3  . ARG   B 1 141 ? 31.266 -31.985 -2.501  1.00 20.05 ?  141 ARG   B HB3  1 
ATOM   6065 H HG2  . ARG   B 1 141 ? 29.143 -32.398 -2.161  1.00 22.38 ?  141 ARG   B HG2  1 
ATOM   6066 H HG3  . ARG   B 1 141 ? 29.060 -31.007 -2.931  1.00 22.38 ?  141 ARG   B HG3  1 
ATOM   6067 H HD2  . ARG   B 1 141 ? 28.988 -33.355 -4.403  1.00 24.60 ?  141 ARG   B HD2  1 
ATOM   6068 H HD3  . ARG   B 1 141 ? 27.667 -32.864 -3.683  1.00 24.60 ?  141 ARG   B HD3  1 
ATOM   6069 H HE   . ARG   B 1 141 ? 28.050 -30.853 -4.971  1.00 25.27 ?  141 ARG   B HE   1 
ATOM   6070 H HH11 . ARG   B 1 141 ? 28.960 -33.778 -6.271  1.00 24.20 ?  141 ARG   B HH11 1 
ATOM   6071 H HH12 . ARG   B 1 141 ? 28.647 -33.409 -7.675  1.00 24.20 ?  141 ARG   B HH12 1 
ATOM   6072 H HH21 . ARG   B 1 141 ? 27.457 -30.393 -7.095  1.00 25.21 ?  141 ARG   B HH21 1 
ATOM   6073 H HH22 . ARG   B 1 141 ? 27.743 -31.375 -8.178  1.00 25.21 ?  141 ARG   B HH22 1 
ATOM   6074 N N    . VAL   B 1 142 ? 31.524 -29.168 -2.772  1.00 14.22 ?  142 VAL   B N    1 
ATOM   6075 C CA   . VAL   B 1 142 ? 31.186 -27.835 -2.292  1.00 14.15 ?  142 VAL   B CA   1 
ATOM   6076 C C    . VAL   B 1 142 ? 31.663 -26.777 -3.280  1.00 14.03 ?  142 VAL   B C    1 
ATOM   6077 O O    . VAL   B 1 142 ? 30.963 -25.792 -3.537  1.00 14.64 ?  142 VAL   B O    1 
ATOM   6078 C CB   . VAL   B 1 142 ? 31.728 -27.606 -0.870  1.00 14.97 ?  142 VAL   B CB   1 
ATOM   6079 C CG1  . VAL   B 1 142 ? 31.427 -26.181 -0.402  1.00 14.91 ?  142 VAL   B CG1  1 
ATOM   6080 C CG2  . VAL   B 1 142 ? 31.144 -28.634 0.089   1.00 15.56 ?  142 VAL   B CG2  1 
ATOM   6081 H H    . VAL   B 1 142 ? 32.085 -29.603 -2.281  1.00 17.05 ?  142 VAL   B H    1 
ATOM   6082 H HA   . VAL   B 1 142 ? 30.226 -27.768 -2.245  1.00 16.97 ?  142 VAL   B HA   1 
ATOM   6083 H HB   . VAL   B 1 142 ? 32.692 -27.719 -0.878  1.00 17.95 ?  142 VAL   B HB   1 
ATOM   6084 H HG11 . VAL   B 1 142 ? 31.608 -26.116 0.545   1.00 17.87 ?  142 VAL   B HG11 1 
ATOM   6085 H HG12 . VAL   B 1 142 ? 31.992 -25.560 -0.892  1.00 17.87 ?  142 VAL   B HG12 1 
ATOM   6086 H HG13 . VAL   B 1 142 ? 30.493 -25.985 -0.577  1.00 17.87 ?  142 VAL   B HG13 1 
ATOM   6087 H HG21 . VAL   B 1 142 ? 31.456 -28.441 0.984   1.00 18.66 ?  142 VAL   B HG21 1 
ATOM   6088 H HG22 . VAL   B 1 142 ? 30.177 -28.581 0.052   1.00 18.66 ?  142 VAL   B HG22 1 
ATOM   6089 H HG23 . VAL   B 1 142 ? 31.438 -29.519 -0.182  1.00 18.66 ?  142 VAL   B HG23 1 
ATOM   6090 N N    . CYS   B 1 143 ? 32.850 -26.967 -3.860  1.00 13.73 ?  143 CYS   B N    1 
ATOM   6091 C CA   . CYS   B 1 143 ? 33.342 -26.026 -4.864  1.00 13.58 ?  143 CYS   B CA   1 
ATOM   6092 C C    . CYS   B 1 143 ? 32.338 -25.882 -6.004  1.00 13.47 ?  143 CYS   B C    1 
ATOM   6093 O O    . CYS   B 1 143 ? 31.931 -24.772 -6.366  1.00 13.54 ?  143 CYS   B O    1 
ATOM   6094 C CB   . CYS   B 1 143 ? 34.697 -26.515 -5.388  1.00 13.76 ?  143 CYS   B CB   1 
ATOM   6095 S SG   . CYS   B 1 143 ? 35.446 -25.416 -6.604  1.00 13.97 ?  143 CYS   B SG   1 
ATOM   6096 H H    . CYS   B 1 143 ? 33.383 -27.620 -3.691  1.00 16.46 ?  143 CYS   B H    1 
ATOM   6097 H HA   . CYS   B 1 143 ? 33.475 -25.157 -4.460  1.00 16.29 ?  143 CYS   B HA   1 
ATOM   6098 H HB2  . CYS   B 1 143 ? 35.317 -26.600 -4.646  1.00 16.50 ?  143 CYS   B HB2  1 
ATOM   6099 H HB3  . CYS   B 1 143 ? 34.579 -27.381 -5.808  1.00 16.50 ?  143 CYS   B HB3  1 
ATOM   6100 H HG   . CYS   B 1 143 ? 36.519 -25.859 -6.928  1.00 16.75 ?  143 CYS   B HG   1 
ATOM   6101 N N    . VAL   B 1 144 ? 31.923 -27.007 -6.584  1.00 13.88 ?  144 VAL   B N    1 
ATOM   6102 C CA   . VAL   B 1 144 ? 31.019 -26.952 -7.729  1.00 14.98 ?  144 VAL   B CA   1 
ATOM   6103 C C    . VAL   B 1 144 ? 29.680 -26.332 -7.355  1.00 14.93 ?  144 VAL   B C    1 
ATOM   6104 O O    . VAL   B 1 144 ? 29.074 -25.612 -8.159  1.00 16.19 ?  144 VAL   B O    1 
ATOM   6105 C CB   . VAL   B 1 144 ? 30.859 -28.365 -8.305  1.00 17.80 ?  144 VAL   B CB   1 
ATOM   6106 C CG1  . VAL   B 1 144 ? 29.603 -28.472 -9.162  1.00 20.60 ?  144 VAL   B CG1  1 
ATOM   6107 C CG2  . VAL   B 1 144 ? 32.116 -28.767 -9.075  1.00 17.66 ?  144 VAL   B CG2  1 
ATOM   6108 H H    . VAL   B 1 144 ? 32.145 -27.799 -6.336  1.00 16.65 ?  144 VAL   B H    1 
ATOM   6109 H HA   . VAL   B 1 144 ? 31.417 -26.401 -8.418  1.00 17.96 ?  144 VAL   B HA   1 
ATOM   6110 H HB   . VAL   B 1 144 ? 30.760 -28.993 -7.569  1.00 21.35 ?  144 VAL   B HB   1 
ATOM   6111 H HG11 . VAL   B 1 144 ? 29.682 -29.257 -9.734  1.00 24.71 ?  144 VAL   B HG11 1 
ATOM   6112 H HG12 . VAL   B 1 144 ? 28.833 -28.569 -8.582  1.00 24.71 ?  144 VAL   B HG12 1 
ATOM   6113 H HG13 . VAL   B 1 144 ? 29.523 -27.678 -9.706  1.00 24.71 ?  144 VAL   B HG13 1 
ATOM   6114 H HG21 . VAL   B 1 144 ? 31.999 -29.667 -9.426  1.00 21.18 ?  144 VAL   B HG21 1 
ATOM   6115 H HG22 . VAL   B 1 144 ? 32.250 -28.145 -9.806  1.00 21.18 ?  144 VAL   B HG22 1 
ATOM   6116 H HG23 . VAL   B 1 144 ? 32.875 -28.745 -8.474  1.00 21.18 ?  144 VAL   B HG23 1 
ATOM   6117 N N    . ASP   B 1 145 ? 29.208 -26.577 -6.138  1.00 15.00 ?  145 ASP   B N    1 
ATOM   6118 C CA   . ASP   B 1 145 ? 27.901 -26.107 -5.706  1.00 16.03 ?  145 ASP   B CA   1 
ATOM   6119 C C    . ASP   B 1 145 ? 27.935 -24.682 -5.164  1.00 15.57 ?  145 ASP   B C    1 
ATOM   6120 O O    . ASP   B 1 145 ? 26.877 -24.130 -4.844  1.00 17.47 ?  145 ASP   B O    1 
ATOM   6121 C CB   . ASP   B 1 145 ? 27.324 -27.033 -4.623  1.00 18.07 ?  145 ASP   B CB   1 
ATOM   6122 C CG   . ASP   B 1 145 ? 26.961 -28.406 -5.139  1.00 19.52 ?  145 ASP   B CG   1 
ATOM   6123 O OD1  . ASP   B 1 145 ? 26.847 -28.581 -6.367  1.00 20.00 ?  145 ASP   B OD1  1 
ATOM   6124 O OD2  . ASP   B 1 145 ? 26.781 -29.306 -4.295  1.00 21.72 -1 145 ASP   B OD2  1 
ATOM   6125 H H    . ASP   B 1 145 ? 29.641 -27.010 -5.535  1.00 17.98 ?  145 ASP   B H    1 
ATOM   6126 H HA   . ASP   B 1 145 ? 27.305 -26.105 -6.469  1.00 19.22 ?  145 ASP   B HA   1 
ATOM   6127 H HB2  . ASP   B 1 145 ? 27.976 -27.146 -3.927  1.00 21.67 ?  145 ASP   B HB2  1 
ATOM   6128 H HB3  . ASP   B 1 145 ? 26.516 -26.624 -4.271  1.00 21.67 ?  145 ASP   B HB3  1 
ATOM   6129 N N    . THR   B 1 146 ? 29.111 -24.071 -5.049  1.00 13.91 ?  146 THR   B N    1 
ATOM   6130 C CA   . THR   B 1 146 ? 29.236 -22.746 -4.447  1.00 13.72 ?  146 THR   B CA   1 
ATOM   6131 C C    . THR   B 1 146 ? 29.873 -21.717 -5.363  1.00 13.09 ?  146 THR   B C    1 
ATOM   6132 O O    . THR   B 1 146 ? 29.419 -20.559 -5.404  1.00 13.50 ?  146 THR   B O    1 
ATOM   6133 C CB   . THR   B 1 146 ? 30.063 -22.847 -3.159  1.00 14.08 ?  146 THR   B CB   1 
ATOM   6134 O OG1  . THR   B 1 146 ? 29.499 -23.847 -2.300  1.00 14.22 ?  146 THR   B OG1  1 
ATOM   6135 C CG2  . THR   B 1 146 ? 30.134 -21.496 -2.444  1.00 14.02 ?  146 THR   B CG2  1 
ATOM   6136 H H    . THR   B 1 146 ? 29.865 -24.402 -5.316  1.00 16.67 ?  146 THR   B H    1 
ATOM   6137 H HA   . THR   B 1 146 ? 28.357 -22.421 -4.214  1.00 16.45 ?  146 THR   B HA   1 
ATOM   6138 H HB   . THR   B 1 146 ? 30.971 -23.102 -3.391  1.00 16.89 ?  146 THR   B HB   1 
ATOM   6139 H HG1  . THR   B 1 146 ? 29.544 -24.603 -2.681  1.00 17.06 ?  146 THR   B HG1  1 
ATOM   6140 H HG21 . THR   B 1 146 ? 30.483 -21.613 -1.550  1.00 16.82 ?  146 THR   B HG21 1 
ATOM   6141 H HG22 . THR   B 1 146 ? 30.718 -20.890 -2.933  1.00 16.82 ?  146 THR   B HG22 1 
ATOM   6142 H HG23 . THR   B 1 146 ? 29.249 -21.103 -2.392  1.00 16.82 ?  146 THR   B HG23 1 
ATOM   6143 N N    . VAL   B 1 147 ? 30.942 -22.090 -6.061  1.00 13.15 ?  147 VAL   B N    1 
ATOM   6144 C CA   . VAL   B 1 147 ? 31.666 -21.149 -6.899  1.00 12.90 ?  147 VAL   B CA   1 
ATOM   6145 C C    . VAL   B 1 147 ? 30.931 -21.014 -8.218  1.00 13.10 ?  147 VAL   B C    1 
ATOM   6146 O O    . VAL   B 1 147 ? 30.565 -22.017 -8.848  1.00 13.92 ?  147 VAL   B O    1 
ATOM   6147 C CB   . VAL   B 1 147 ? 33.117 -21.608 -7.108  1.00 12.99 ?  147 VAL   B CB   1 
ATOM   6148 C CG1  . VAL   B 1 147 ? 33.880 -20.580 -7.927  1.00 13.39 ?  147 VAL   B CG1  1 
ATOM   6149 C CG2  . VAL   B 1 147 ? 33.798 -21.830 -5.767  1.00 13.38 ?  147 VAL   B CG2  1 
ATOM   6150 H H    . VAL   B 1 147 ? 31.273 -22.889 -6.070  1.00 15.76 ?  147 VAL   B H    1 
ATOM   6151 H HA   . VAL   B 1 147 ? 31.687 -20.281 -6.469  1.00 15.47 ?  147 VAL   B HA   1 
ATOM   6152 H HB   . VAL   B 1 147 ? 33.123 -22.452 -7.596  1.00 15.57 ?  147 VAL   B HB   1 
ATOM   6153 H HG11 . VAL   B 1 147 ? 34.824 -20.805 -7.921  1.00 16.06 ?  147 VAL   B HG11 1 
ATOM   6154 H HG12 . VAL   B 1 147 ? 33.548 -20.584 -8.839  1.00 16.06 ?  147 VAL   B HG12 1 
ATOM   6155 H HG13 . VAL   B 1 147 ? 33.749 -19.703 -7.531  1.00 16.06 ?  147 VAL   B HG13 1 
ATOM   6156 H HG21 . VAL   B 1 147 ? 34.739 -22.024 -5.918  1.00 16.04 ?  147 VAL   B HG21 1 
ATOM   6157 H HG22 . VAL   B 1 147 ? 33.712 -21.023 -5.235  1.00 16.04 ?  147 VAL   B HG22 1 
ATOM   6158 H HG23 . VAL   B 1 147 ? 33.377 -22.574 -5.313  1.00 16.04 ?  147 VAL   B HG23 1 
ATOM   6159 N N    . ARG   B 1 148 ? 30.716 -19.765 -8.635  1.00 13.02 ?  148 ARG   B N    1 
ATOM   6160 C CA   . ARG   B 1 148 ? 30.090 -19.441 -9.906  1.00 13.45 ?  148 ARG   B CA   1 
ATOM   6161 C C    . ARG   B 1 148 ? 31.047 -18.770 -10.881 1.00 13.38 ?  148 ARG   B C    1 
ATOM   6162 O O    . ARG   B 1 148 ? 30.764 -18.750 -12.081 1.00 14.66 ?  148 ARG   B O    1 
ATOM   6163 C CB   . ARG   B 1 148 ? 28.855 -18.551 -9.681  1.00 13.96 ?  148 ARG   B CB   1 
ATOM   6164 C CG   . ARG   B 1 148 ? 27.775 -19.258 -8.868  1.00 14.76 ?  148 ARG   B CG   1 
ATOM   6165 C CD   . ARG   B 1 148 ? 26.567 -18.363 -8.564  1.00 15.44 ?  148 ARG   B CD   1 
ATOM   6166 N NE   . ARG   B 1 148 ? 26.960 -17.163 -7.835  1.00 15.14 ?  148 ARG   B NE   1 
ATOM   6167 C CZ   . ARG   B 1 148 ? 27.266 -17.133 -6.543  1.00 14.26 ?  148 ARG   B CZ   1 
ATOM   6168 N NH1  . ARG   B 1 148 ? 27.192 -18.217 -5.785  1.00 14.22 ?  148 ARG   B NH1  1 
ATOM   6169 N NH2  . ARG   B 1 148 ? 27.665 -15.984 -5.998  1.00 14.49 ?  148 ARG   B NH2  1 
ATOM   6170 H H    . ARG   B 1 148 ? 30.942 -19.065 -8.178  1.00 15.61 ?  148 ARG   B H    1 
ATOM   6171 H HA   . ARG   B 1 148 ? 29.786 -20.263 -10.312 1.00 16.13 ?  148 ARG   B HA   1 
ATOM   6172 H HB2  . ARG   B 1 148 ? 29.118 -17.753 -9.196  1.00 16.74 ?  148 ARG   B HB2  1 
ATOM   6173 H HB3  . ARG   B 1 148 ? 28.475 -18.312 -10.539 1.00 16.74 ?  148 ARG   B HB3  1 
ATOM   6174 H HG2  . ARG   B 1 148 ? 27.456 -20.028 -9.367  1.00 17.70 ?  148 ARG   B HG2  1 
ATOM   6175 H HG3  . ARG   B 1 148 ? 28.151 -19.549 -8.022  1.00 17.70 ?  148 ARG   B HG3  1 
ATOM   6176 H HD2  . ARG   B 1 148 ? 26.156 -18.086 -9.397  1.00 18.52 ?  148 ARG   B HD2  1 
ATOM   6177 H HD3  . ARG   B 1 148 ? 25.930 -18.853 -8.021  1.00 18.52 ?  148 ARG   B HD3  1 
ATOM   6178 H HE   . ARG   B 1 148 ? 27.008 -16.425 -8.270  1.00 18.15 ?  148 ARG   B HE   1 
ATOM   6179 H HH11 . ARG   B 1 148 ? 26.930 -18.966 -6.121  1.00 17.05 ?  148 ARG   B HH11 1 
ATOM   6180 H HH12 . ARG   B 1 148 ? 27.388 -18.175 -4.946  1.00 17.05 ?  148 ARG   B HH12 1 
ATOM   6181 H HH21 . ARG   B 1 148 ? 27.726 -15.277 -6.482  1.00 17.38 ?  148 ARG   B HH21 1 
ATOM   6182 H HH22 . ARG   B 1 148 ? 27.869 -15.950 -5.162  1.00 17.38 ?  148 ARG   B HH22 1 
ATOM   6183 N N    . THR   B 1 149 ? 32.155 -18.219 -10.394 1.00 13.39 ?  149 THR   B N    1 
ATOM   6184 C CA   . THR   B 1 149 ? 33.197 -17.660 -11.243 1.00 13.39 ?  149 THR   B CA   1 
ATOM   6185 C C    . THR   B 1 149 ? 34.086 -18.796 -11.751 1.00 12.99 ?  149 THR   B C    1 
ATOM   6186 O O    . THR   B 1 149 ? 33.893 -19.969 -11.414 1.00 13.47 ?  149 THR   B O    1 
ATOM   6187 C CB   . THR   B 1 149 ? 33.966 -16.602 -10.461 1.00 13.55 ?  149 THR   B CB   1 
ATOM   6188 O OG1  . THR   B 1 149 ? 34.422 -17.195 -9.242  1.00 13.33 ?  149 THR   B OG1  1 
ATOM   6189 C CG2  . THR   B 1 149 ? 33.069 -15.405 -10.168 1.00 13.86 ?  149 THR   B CG2  1 
ATOM   6190 H H    . THR   B 1 149 ? 32.322 -18.151 -9.553  1.00 16.06 ?  149 THR   B H    1 
ATOM   6191 H HA   . THR   B 1 149 ? 32.782 -17.229 -12.009 1.00 16.06 ?  149 THR   B HA   1 
ATOM   6192 H HB   . THR   B 1 149 ? 34.725 -16.307 -10.979 1.00 16.24 ?  149 THR   B HB   1 
ATOM   6193 H HG1  . THR   B 1 149 ? 34.839 -16.621 -8.783  1.00 15.98 ?  149 THR   B HG1  1 
ATOM   6194 H HG21 . THR   B 1 149 ? 33.570 -14.728 -9.691  1.00 16.62 ?  149 THR   B HG21 1 
ATOM   6195 H HG22 . THR   B 1 149 ? 32.742 -15.028 -11.001 1.00 16.62 ?  149 THR   B HG22 1 
ATOM   6196 H HG23 . THR   B 1 149 ? 32.312 -15.679 -9.629  1.00 16.62 ?  149 THR   B HG23 1 
ATOM   6197 N N    . ASN   B 1 150 ? 35.053 -18.473 -12.597 1.00 13.20 ?  150 ASN   B N    1 
ATOM   6198 C CA   . ASN   B 1 150 ? 35.820 -19.497 -13.298 1.00 13.76 ?  150 ASN   B CA   1 
ATOM   6199 C C    . ASN   B 1 150 ? 36.988 -19.943 -12.427 1.00 13.31 ?  150 ASN   B C    1 
ATOM   6200 O O    . ASN   B 1 150 ? 37.915 -19.171 -12.174 1.00 14.02 ?  150 ASN   B O    1 
ATOM   6201 C CB   . ASN   B 1 150 ? 36.284 -18.963 -14.645 1.00 15.29 ?  150 ASN   B CB   1 
ATOM   6202 C CG   . ASN   B 1 150 ? 35.132 -18.747 -15.587 1.00 17.93 ?  150 ASN   B CG   1 
ATOM   6203 O OD1  . ASN   B 1 150 ? 34.243 -19.587 -15.684 1.00 19.04 ?  150 ASN   B OD1  1 
ATOM   6204 N ND2  . ASN   B 1 150 ? 35.118 -17.610 -16.261 1.00 19.69 ?  150 ASN   B ND2  1 
ATOM   6205 H H    . ASN   B 1 150 ? 35.293 -17.664 -12.779 1.00 15.83 ?  150 ASN   B H    1 
ATOM   6206 H HA   . ASN   B 1 150 ? 35.243 -20.264 -13.461 1.00 16.50 ?  150 ASN   B HA   1 
ATOM   6207 H HB2  . ASN   B 1 150 ? 36.728 -18.111 -14.513 1.00 18.33 ?  150 ASN   B HB2  1 
ATOM   6208 H HB3  . ASN   B 1 150 ? 36.888 -19.600 -15.049 1.00 18.33 ?  150 ASN   B HB3  1 
ATOM   6209 H HD21 . ASN   B 1 150 ? 34.478 -17.440 -16.814 1.00 23.62 ?  150 ASN   B HD21 1 
ATOM   6210 H HD22 . ASN   B 1 150 ? 35.755 -17.038 -16.160 1.00 23.62 ?  150 ASN   B HD22 1 
ATOM   6211 N N    . VAL   B 1 151 ? 36.947 -21.190 -11.972 1.00 12.92 ?  151 VAL   B N    1 
ATOM   6212 C CA   . VAL   B 1 151 ? 37.966 -21.726 -11.082 1.00 12.92 ?  151 VAL   B CA   1 
ATOM   6213 C C    . VAL   B 1 151 ? 38.669 -22.896 -11.757 1.00 12.76 ?  151 VAL   B C    1 
ATOM   6214 O O    . VAL   B 1 151 ? 38.025 -23.834 -12.254 1.00 13.82 ?  151 VAL   B O    1 
ATOM   6215 C CB   . VAL   B 1 151 ? 37.401 -22.072 -9.689  1.00 14.05 ?  151 VAL   B CB   1 
ATOM   6216 C CG1  . VAL   B 1 151 ? 36.241 -23.071 -9.777  1.00 14.72 ?  151 VAL   B CG1  1 
ATOM   6217 C CG2  . VAL   B 1 151 ? 38.509 -22.570 -8.775  1.00 14.25 ?  151 VAL   B CG2  1 
ATOM   6218 H H    . VAL   B 1 151 ? 36.323 -21.755 -12.168 1.00 15.50 ?  151 VAL   B H    1 
ATOM   6219 H HA   . VAL   B 1 151 ? 38.633 -21.032 -10.948 1.00 15.49 ?  151 VAL   B HA   1 
ATOM   6220 H HB   . VAL   B 1 151 ? 37.052 -21.255 -9.294  1.00 16.85 ?  151 VAL   B HB   1 
ATOM   6221 H HG11 . VAL   B 1 151 ? 35.918 -23.259 -8.881  1.00 17.65 ?  151 VAL   B HG11 1 
ATOM   6222 H HG12 . VAL   B 1 151 ? 35.528 -22.686 -10.311 1.00 17.65 ?  151 VAL   B HG12 1 
ATOM   6223 H HG13 . VAL   B 1 151 ? 36.558 -23.889 -10.191 1.00 17.65 ?  151 VAL   B HG13 1 
ATOM   6224 H HG21 . VAL   B 1 151 ? 38.159 -22.645 -7.872  1.00 17.08 ?  151 VAL   B HG21 1 
ATOM   6225 H HG22 . VAL   B 1 151 ? 38.809 -23.438 -9.085  1.00 17.08 ?  151 VAL   B HG22 1 
ATOM   6226 H HG23 . VAL   B 1 151 ? 39.245 -21.938 -8.791  1.00 17.08 ?  151 VAL   B HG23 1 
ATOM   6227 N N    . TYR   B 1 152 ? 40.000 -22.805 -11.783 1.00 12.28 ?  152 TYR   B N    1 
ATOM   6228 C CA   . TYR   B 1 152 ? 40.904 -23.790 -12.359 1.00 12.60 ?  152 TYR   B CA   1 
ATOM   6229 C C    . TYR   B 1 152 ? 41.628 -24.470 -11.201 1.00 11.99 ?  152 TYR   B C    1 
ATOM   6230 O O    . TYR   B 1 152 ? 42.464 -23.851 -10.535 1.00 12.32 ?  152 TYR   B O    1 
ATOM   6231 C CB   . TYR   B 1 152 ? 41.873 -23.075 -13.303 1.00 13.36 ?  152 TYR   B CB   1 
ATOM   6232 C CG   . TYR   B 1 152 ? 41.193 -22.618 -14.569 1.00 14.22 ?  152 TYR   B CG   1 
ATOM   6233 C CD1  . TYR   B 1 152 ? 40.525 -21.400 -14.633 1.00 14.40 ?  152 TYR   B CD1  1 
ATOM   6234 C CD2  . TYR   B 1 152 ? 41.197 -23.422 -15.694 1.00 15.21 ?  152 TYR   B CD2  1 
ATOM   6235 C CE1  . TYR   B 1 152 ? 39.883 -21.001 -15.786 1.00 15.54 ?  152 TYR   B CE1  1 
ATOM   6236 C CE2  . TYR   B 1 152 ? 40.558 -23.038 -16.851 1.00 15.95 ?  152 TYR   B CE2  1 
ATOM   6237 C CZ   . TYR   B 1 152 ? 39.904 -21.822 -16.898 1.00 16.12 ?  152 TYR   B CZ   1 
ATOM   6238 O OH   . TYR   B 1 152 ? 39.270 -21.449 -18.063 1.00 18.61 ?  152 TYR   B OH   1 
ATOM   6239 H H    . TYR   B 1 152 ? 40.429 -22.139 -11.439 1.00 14.73 ?  152 TYR   B H    1 
ATOM   6240 H HA   . TYR   B 1 152 ? 40.399 -24.454 -12.858 1.00 15.11 ?  152 TYR   B HA   1 
ATOM   6241 H HB2  . TYR   B 1 152 ? 42.232 -22.293 -12.848 1.00 16.02 ?  152 TYR   B HB2  1 
ATOM   6242 H HB3  . TYR   B 1 152 ? 42.592 -23.680 -13.538 1.00 16.02 ?  152 TYR   B HB3  1 
ATOM   6243 H HD1  . TYR   B 1 152 ? 40.504 -20.849 -13.882 1.00 17.26 ?  152 TYR   B HD1  1 
ATOM   6244 H HD2  . TYR   B 1 152 ? 41.635 -24.246 -15.663 1.00 18.24 ?  152 TYR   B HD2  1 
ATOM   6245 H HE1  . TYR   B 1 152 ? 39.441 -20.186 -15.821 1.00 18.63 ?  152 TYR   B HE1  1 
ATOM   6246 H HE2  . TYR   B 1 152 ? 40.577 -23.591 -17.597 1.00 19.13 ?  152 TYR   B HE2  1 
ATOM   6247 H HH   . TYR   B 1 152 ? 39.374 -22.047 -18.644 1.00 22.32 ?  152 TYR   B HH   1 
ATOM   6248 N N    . LEU   B 1 153 ? 41.273 -25.732 -10.941 1.00 12.31 ?  153 LEU   B N    1 
ATOM   6249 C CA   . LEU   B 1 153 ? 41.774 -26.479 -9.795  1.00 12.16 ?  153 LEU   B CA   1 
ATOM   6250 C C    . LEU   B 1 153 ? 43.006 -27.284 -10.182 1.00 12.32 ?  153 LEU   B C    1 
ATOM   6251 O O    . LEU   B 1 153 ? 42.992 -28.006 -11.182 1.00 13.49 ?  153 LEU   B O    1 
ATOM   6252 C CB   . LEU   B 1 153 ? 40.693 -27.431 -9.281  1.00 12.42 ?  153 LEU   B CB   1 
ATOM   6253 C CG   . LEU   B 1 153 ? 39.430 -26.778 -8.717  1.00 13.11 ?  153 LEU   B CG   1 
ATOM   6254 C CD1  . LEU   B 1 153 ? 38.340 -27.823 -8.572  1.00 13.87 ?  153 LEU   B CD1  1 
ATOM   6255 C CD2  . LEU   B 1 153 ? 39.719 -26.108 -7.375  1.00 13.48 ?  153 LEU   B CD2  1 
ATOM   6256 H H    . LEU   B 1 153 ? 40.713 -26.184 -11.425 1.00 14.75 ?  153 LEU   B H    1 
ATOM   6257 H HA   . LEU   B 1 153 ? 42.001 -25.859 -9.085  1.00 14.58 ?  153 LEU   B HA   1 
ATOM   6258 H HB2  . LEU   B 1 153 ? 40.415 -28.005 -10.009 1.00 14.89 ?  153 LEU   B HB2  1 
ATOM   6259 H HB3  . LEU   B 1 153 ? 41.075 -27.972 -8.570  1.00 14.89 ?  153 LEU   B HB3  1 
ATOM   6260 H HG   . LEU   B 1 153 ? 39.119 -26.089 -9.330  1.00 15.72 ?  153 LEU   B HG   1 
ATOM   6261 H HD11 . LEU   B 1 153 ? 37.535 -27.394 -8.239  1.00 16.64 ?  153 LEU   B HD11 1 
ATOM   6262 H HD12 . LEU   B 1 153 ? 38.172 -28.216 -9.439  1.00 16.64 ?  153 LEU   B HD12 1 
ATOM   6263 H HD13 . LEU   B 1 153 ? 38.638 -28.498 -7.947  1.00 16.64 ?  153 LEU   B HD13 1 
ATOM   6264 H HD21 . LEU   B 1 153 ? 38.901 -25.728 -7.023  1.00 16.16 ?  153 LEU   B HD21 1 
ATOM   6265 H HD22 . LEU   B 1 153 ? 40.068 -26.773 -6.760  1.00 16.16 ?  153 LEU   B HD22 1 
ATOM   6266 H HD23 . LEU   B 1 153 ? 40.379 -25.405 -7.506  1.00 16.16 ?  153 LEU   B HD23 1 
ATOM   6267 N N    . ALA   B 1 154 ? 44.060 -27.171 -9.378  1.00 12.37 ?  154 ALA   B N    1 
ATOM   6268 C CA   . ALA   B 1 154 ? 45.289 -27.929 -9.561  1.00 13.38 ?  154 ALA   B CA   1 
ATOM   6269 C C    . ALA   B 1 154 ? 45.353 -29.007 -8.487  1.00 13.94 ?  154 ALA   B C    1 
ATOM   6270 O O    . ALA   B 1 154 ? 45.280 -28.709 -7.287  1.00 15.38 ?  154 ALA   B O    1 
ATOM   6271 C CB   . ALA   B 1 154 ? 46.505 -27.009 -9.490  1.00 14.43 ?  154 ALA   B CB   1 
ATOM   6272 H H    . ALA   B 1 154 ? 44.079 -26.639 -8.696  1.00 14.83 ?  154 ALA   B H    1 
ATOM   6273 H HA   . ALA   B 1 154 ? 45.279 -28.354 -10.427 1.00 16.04 ?  154 ALA   B HA   1 
ATOM   6274 H HB1  . ALA   B 1 154 ? 47.310 -27.534 -9.611  1.00 17.30 ?  154 ALA   B HB1  1 
ATOM   6275 H HB2  . ALA   B 1 154 ? 46.439 -26.338 -10.190 1.00 17.30 ?  154 ALA   B HB2  1 
ATOM   6276 H HB3  . ALA   B 1 154 ? 46.526 -26.571 -8.620  1.00 17.30 ?  154 ALA   B HB3  1 
ATOM   6277 N N    . VAL   B 1 155 ? 45.478 -30.255 -8.923  1.00 13.21 ?  155 VAL   B N    1 
ATOM   6278 C CA   . VAL   B 1 155 ? 45.588 -31.408 -8.034  1.00 13.60 ?  155 VAL   B CA   1 
ATOM   6279 C C    . VAL   B 1 155 ? 46.928 -32.081 -8.314  1.00 13.46 ?  155 VAL   B C    1 
ATOM   6280 O O    . VAL   B 1 155 ? 47.161 -32.575 -9.424  1.00 15.35 ?  155 VAL   B O    1 
ATOM   6281 C CB   . VAL   B 1 155 ? 44.429 -32.403 -8.225  1.00 15.14 ?  155 VAL   B CB   1 
ATOM   6282 C CG1  . VAL   B 1 155 ? 44.617 -33.614 -7.318  1.00 15.29 ?  155 VAL   B CG1  1 
ATOM   6283 C CG2  . VAL   B 1 155 ? 43.093 -31.719 -7.956  1.00 16.33 ?  155 VAL   B CG2  1 
ATOM   6284 H H    . VAL   B 1 155 ? 45.506 -30.469 -9.757  1.00 15.84 ?  155 VAL   B H    1 
ATOM   6285 H HA   . VAL   B 1 155 ? 45.582 -31.112 -7.113  1.00 16.31 ?  155 VAL   B HA   1 
ATOM   6286 H HB   . VAL   B 1 155 ? 44.425 -32.713 -9.144  1.00 18.16 ?  155 VAL   B HB   1 
ATOM   6287 H HG11 . VAL   B 1 155 ? 43.790 -34.122 -7.287  1.00 18.34 ?  155 VAL   B HG11 1 
ATOM   6288 H HG12 . VAL   B 1 155 ? 45.330 -34.175 -7.672  1.00 18.34 ?  155 VAL   B HG12 1 
ATOM   6289 H HG13 . VAL   B 1 155 ? 44.850 -33.313 -6.425  1.00 18.34 ?  155 VAL   B HG13 1 
ATOM   6290 H HG21 . VAL   B 1 155 ? 42.382 -32.371 -8.043  1.00 19.59 ?  155 VAL   B HG21 1 
ATOM   6291 H HG22 . VAL   B 1 155 ? 43.102 -31.357 -7.055  1.00 19.59 ?  155 VAL   B HG22 1 
ATOM   6292 H HG23 . VAL   B 1 155 ? 42.969 -31.004 -8.598  1.00 19.59 ?  155 VAL   B HG23 1 
ATOM   6293 N N    . PHE   B 1 156 ? 47.800 -32.114 -7.302  1.00 14.03 ?  156 PHE   B N    1 
ATOM   6294 C CA   . PHE   B 1 156 ? 49.176 -32.578 -7.500  1.00 15.51 ?  156 PHE   B CA   1 
ATOM   6295 C C    . PHE   B 1 156 ? 49.268 -34.081 -7.778  1.00 16.18 ?  156 PHE   B C    1 
ATOM   6296 O O    . PHE   B 1 156 ? 49.990 -34.513 -8.689  1.00 18.45 ?  156 PHE   B O    1 
ATOM   6297 C CB   . PHE   B 1 156 ? 50.007 -32.205 -6.273  1.00 15.65 ?  156 PHE   B CB   1 
ATOM   6298 C CG   . PHE   B 1 156 ? 51.429 -32.669 -6.332  1.00 16.05 ?  156 PHE   B CG   1 
ATOM   6299 C CD1  . PHE   B 1 156 ? 52.308 -32.135 -7.256  1.00 17.69 ?  156 PHE   B CD1  1 
ATOM   6300 C CD2  . PHE   B 1 156 ? 51.896 -33.621 -5.450  1.00 16.73 ?  156 PHE   B CD2  1 
ATOM   6301 C CE1  . PHE   B 1 156 ? 53.632 -32.544 -7.305  1.00 18.81 ?  156 PHE   B CE1  1 
ATOM   6302 C CE2  . PHE   B 1 156 ? 53.218 -34.037 -5.495  1.00 18.10 ?  156 PHE   B CE2  1 
ATOM   6303 C CZ   . PHE   B 1 156 ? 54.078 -33.499 -6.428  1.00 18.44 ?  156 PHE   B CZ   1 
ATOM   6304 H H    . PHE   B 1 156 ? 47.620 -31.875 -6.495  1.00 16.83 ?  156 PHE   B H    1 
ATOM   6305 H HA   . PHE   B 1 156 ? 49.552 -32.112 -8.260  1.00 18.60 ?  156 PHE   B HA   1 
ATOM   6306 H HB2  . PHE   B 1 156 ? 50.016 -31.236 -6.188  1.00 18.77 ?  156 PHE   B HB2  1 
ATOM   6307 H HB3  . PHE   B 1 156 ? 49.601 -32.597 -5.486  1.00 18.77 ?  156 PHE   B HB3  1 
ATOM   6308 H HD1  . PHE   B 1 156 ? 52.010 -31.481 -7.850  1.00 21.22 ?  156 PHE   B HD1  1 
ATOM   6309 H HD2  . PHE   B 1 156 ? 51.314 -33.988 -4.823  1.00 20.07 ?  156 PHE   B HD2  1 
ATOM   6310 H HE1  . PHE   B 1 156 ? 54.213 -32.176 -7.934  1.00 22.56 ?  156 PHE   B HE1  1 
ATOM   6311 H HE2  . PHE   B 1 156 ? 53.519 -34.689 -4.902  1.00 21.71 ?  156 PHE   B HE2  1 
ATOM   6312 H HZ   . PHE   B 1 156 ? 54.965 -33.781 -6.458  1.00 22.12 ?  156 PHE   B HZ   1 
ATOM   6313 N N    . ASP   B 1 157 ? 48.600 -34.897 -6.977  1.00 16.90 ?  157 ASP   B N    1 
ATOM   6314 C CA   . ASP   B 1 157 ? 48.751 -36.344 -7.073  1.00 18.13 ?  157 ASP   B CA   1 
ATOM   6315 C C    . ASP   B 1 157 ? 47.839 -36.886 -8.164  1.00 17.83 ?  157 ASP   B C    1 
ATOM   6316 O O    . ASP   B 1 157 ? 46.614 -36.761 -8.065  1.00 17.22 ?  157 ASP   B O    1 
ATOM   6317 C CB   . ASP   B 1 157 ? 48.397 -36.963 -5.728  1.00 20.03 ?  157 ASP   B CB   1 
ATOM   6318 C CG   . ASP   B 1 157 ? 48.529 -38.477 -5.719  1.00 21.59 ?  157 ASP   B CG   1 
ATOM   6319 O OD1  . ASP   B 1 157 ? 48.857 -39.079 -6.770  1.00 21.85 ?  157 ASP   B OD1  1 
ATOM   6320 O OD2  . ASP   B 1 157 ? 48.326 -39.066 -4.640  1.00 23.82 -1 157 ASP   B OD2  1 
ATOM   6321 H H    . ASP   B 1 157 ? 48.055 -34.640 -6.371  1.00 20.27 ?  157 ASP   B H    1 
ATOM   6322 H HA   . ASP   B 1 157 ? 49.672 -36.569 -7.294  1.00 21.74 ?  157 ASP   B HA   1 
ATOM   6323 H HB2  . ASP   B 1 157 ? 48.979 -36.587 -5.052  1.00 24.02 ?  157 ASP   B HB2  1 
ATOM   6324 H HB3  . ASP   B 1 157 ? 47.472 -36.746 -5.524  1.00 24.02 ?  157 ASP   B HB3  1 
ATOM   6325 N N    . LYS   B 1 158 ? 48.433 -37.512 -9.189  1.00 19.10 ?  158 LYS   B N    1 
ATOM   6326 C CA   . LYS   B 1 158 ? 47.650 -38.116 -10.270 1.00 20.36 ?  158 LYS   B CA   1 
ATOM   6327 C C    . LYS   B 1 158 ? 46.589 -39.083 -9.742  1.00 20.16 ?  158 LYS   B C    1 
ATOM   6328 O O    . LYS   B 1 158 ? 45.488 -39.180 -10.301 1.00 20.42 ?  158 LYS   B O    1 
ATOM   6329 C CB   . LYS   B 1 158 ? 48.592 -38.826 -11.252 1.00 22.35 ?  158 LYS   B CB   1 
ATOM   6330 C CG   . LYS   B 1 158 ? 47.909 -39.736 -12.264 1.00 24.97 ?  158 LYS   B CG   1 
ATOM   6331 C CD   . LYS   B 1 158 ? 47.077 -38.961 -13.263 1.00 27.27 ?  158 LYS   B CD   1 
ATOM   6332 C CE   . LYS   B 1 158 ? 46.449 -39.894 -14.288 1.00 29.04 ?  158 LYS   B CE   1 
ATOM   6333 N NZ   . LYS   B 1 158 ? 45.398 -39.211 -15.097 1.00 29.46 ?  158 LYS   B NZ   1 
ATOM   6334 H H    . LYS   B 1 158 ? 49.286 -37.604 -9.283  1.00 22.90 ?  158 LYS   B H    1 
ATOM   6335 H HA   . LYS   B 1 158 ? 47.197 -37.416 -10.762 1.00 24.42 ?  158 LYS   B HA   1 
ATOM   6336 H HB2  . LYS   B 1 158 ? 49.080 -38.154 -11.760 1.00 26.81 ?  158 LYS   B HB2  1 
ATOM   6337 H HB3  . LYS   B 1 158 ? 49.219 -39.368 -10.752 1.00 26.81 ?  158 LYS   B HB3  1 
ATOM   6338 H HG2  . LYS   B 1 158 ? 48.590 -40.219 -12.760 1.00 29.95 ?  158 LYS   B HG2  1 
ATOM   6339 H HG3  . LYS   B 1 158 ? 47.332 -40.374 -11.811 1.00 29.95 ?  158 LYS   B HG3  1 
ATOM   6340 H HD2  . LYS   B 1 158 ? 46.366 -38.493 -12.799 1.00 32.71 ?  158 LYS   B HD2  1 
ATOM   6341 H HD3  . LYS   B 1 158 ? 47.645 -38.331 -13.735 1.00 32.71 ?  158 LYS   B HD3  1 
ATOM   6342 H HE2  . LYS   B 1 158 ? 47.135 -40.213 -14.894 1.00 34.84 ?  158 LYS   B HE2  1 
ATOM   6343 H HE3  . LYS   B 1 158 ? 46.037 -40.644 -13.829 1.00 34.84 ?  158 LYS   B HE3  1 
ATOM   6344 H HZ1  . LYS   B 1 158 ? 45.048 -39.779 -15.685 1.00 35.34 ?  158 LYS   B HZ1  1 
ATOM   6345 H HZ2  . LYS   B 1 158 ? 44.751 -38.910 -14.564 1.00 35.34 ?  158 LYS   B HZ2  1 
ATOM   6346 H HZ3  . LYS   B 1 158 ? 45.754 -38.522 -15.536 1.00 35.34 ?  158 LYS   B HZ3  1 
ATOM   6347 N N    . ASN   B 1 159 ? 46.913 -39.845 -8.694  1.00 20.38 ?  159 ASN   B N    1 
ATOM   6348 C CA   . ASN   B 1 159 ? 45.959 -40.823 -8.181  1.00 21.15 ?  159 ASN   B CA   1 
ATOM   6349 C C    . ASN   B 1 159 ? 44.765 -40.148 -7.505  1.00 20.11 ?  159 ASN   B C    1 
ATOM   6350 O O    . ASN   B 1 159 ? 43.633 -40.642 -7.613  1.00 20.33 ?  159 ASN   B O    1 
ATOM   6351 C CB   . ASN   B 1 159 ? 46.673 -41.794 -7.246  1.00 23.07 ?  159 ASN   B CB   1 
ATOM   6352 C CG   . ASN   B 1 159 ? 47.695 -42.651 -7.974  1.00 25.11 ?  159 ASN   B CG   1 
ATOM   6353 O OD1  . ASN   B 1 159 ? 47.428 -43.165 -9.067  1.00 25.69 ?  159 ASN   B OD1  1 
ATOM   6354 N ND2  . ASN   B 1 159 ? 48.873 -42.807 -7.375  1.00 25.97 ?  159 ASN   B ND2  1 
ATOM   6355 H H    . ASN   B 1 159 ? 47.658 -39.798 -8.270  1.00 24.44 ?  159 ASN   B H    1 
ATOM   6356 H HA   . ASN   B 1 159 ? 45.624 -41.336 -8.933  1.00 25.37 ?  159 ASN   B HA   1 
ATOM   6357 H HB2  . ASN   B 1 159 ? 47.139 -41.297 -6.559  1.00 27.67 ?  159 ASN   B HB2  1 
ATOM   6358 H HB3  . ASN   B 1 159 ? 46.022 -42.390 -6.851  1.00 27.67 ?  159 ASN   B HB3  1 
ATOM   6359 H HD21 . ASN   B 1 159 ? 49.490 -43.281 -7.748  1.00 31.15 ?  159 ASN   B HD21 1 
ATOM   6360 H HD22 . ASN   B 1 159 ? 49.020 -42.443 -6.610  1.00 31.15 ?  159 ASN   B HD22 1 
ATOM   6361 N N    . LEU   B 1 160 ? 44.975 -39.010 -6.835  1.00 19.20 ?  160 LEU   B N    1 
ATOM   6362 C CA   . LEU   B 1 160 ? 43.841 -38.280 -6.288  1.00 18.33 ?  160 LEU   B CA   1 
ATOM   6363 C C    . LEU   B 1 160 ? 43.052 -37.610 -7.401  1.00 17.44 ?  160 LEU   B C    1 
ATOM   6364 O O    . LEU   B 1 160 ? 41.816 -37.614 -7.386  1.00 17.04 ?  160 LEU   B O    1 
ATOM   6365 C CB   . LEU   B 1 160 ? 44.303 -37.257 -5.251  1.00 17.76 ?  160 LEU   B CB   1 
ATOM   6366 C CG   . LEU   B 1 160 ? 43.176 -36.363 -4.710  1.00 17.31 ?  160 LEU   B CG   1 
ATOM   6367 C CD1  . LEU   B 1 160 ? 42.060 -37.187 -4.085  1.00 17.93 ?  160 LEU   B CD1  1 
ATOM   6368 C CD2  . LEU   B 1 160 ? 43.721 -35.357 -3.708  1.00 17.59 ?  160 LEU   B CD2  1 
ATOM   6369 H H    . LEU   B 1 160 ? 45.752 -38.652 -6.697  1.00 23.02 ?  160 LEU   B H    1 
ATOM   6370 H HA   . LEU   B 1 160 ? 43.258 -38.913 -5.849  1.00 21.98 ?  160 LEU   B HA   1 
ATOM   6371 H HB2  . LEU   B 1 160 ? 44.698 -37.735 -4.501  1.00 21.30 ?  160 LEU   B HB2  1 
ATOM   6372 H HB3  . LEU   B 1 160 ? 44.975 -36.684 -5.658  1.00 21.30 ?  160 LEU   B HB3  1 
ATOM   6373 H HG   . LEU   B 1 160 ? 42.800 -35.864 -5.447  1.00 20.76 ?  160 LEU   B HG   1 
ATOM   6374 H HD11 . LEU   B 1 160 ? 41.421 -36.587 -3.675  1.00 21.51 ?  160 LEU   B HD11 1 
ATOM   6375 H HD12 . LEU   B 1 160 ? 41.624 -37.712 -4.776  1.00 21.51 ?  160 LEU   B HD12 1 
ATOM   6376 H HD13 . LEU   B 1 160 ? 42.438 -37.778 -3.413  1.00 21.51 ?  160 LEU   B HD13 1 
ATOM   6377 H HD21 . LEU   B 1 160 ? 42.991 -34.795 -3.404  1.00 21.10 ?  160 LEU   B HD21 1 
ATOM   6378 H HD22 . LEU   B 1 160 ? 44.108 -35.832 -2.958  1.00 21.10 ?  160 LEU   B HD22 1 
ATOM   6379 H HD23 . LEU   B 1 160 ? 44.398 -34.813 -4.142  1.00 21.10 ?  160 LEU   B HD23 1 
ATOM   6380 N N    . TYR   B 1 161 ? 43.748 -37.038 -8.384  1.00 17.44 ?  161 TYR   B N    1 
ATOM   6381 C CA   . TYR   B 1 161 ? 43.073 -36.476 -9.548  1.00 17.30 ?  161 TYR   B CA   1 
ATOM   6382 C C    . TYR   B 1 161 ? 42.137 -37.501 -10.172 1.00 16.87 ?  161 TYR   B C    1 
ATOM   6383 O O    . TYR   B 1 161 ? 40.968 -37.207 -10.441 1.00 16.77 ?  161 TYR   B O    1 
ATOM   6384 C CB   . TYR   B 1 161 ? 44.118 -35.996 -10.562 1.00 18.11 ?  161 TYR   B CB   1 
ATOM   6385 C CG   . TYR   B 1 161 ? 43.541 -35.529 -11.877 1.00 18.52 ?  161 TYR   B CG   1 
ATOM   6386 C CD1  . TYR   B 1 161 ? 43.146 -34.208 -12.050 1.00 18.42 ?  161 TYR   B CD1  1 
ATOM   6387 C CD2  . TYR   B 1 161 ? 43.381 -36.408 -12.944 1.00 19.56 ?  161 TYR   B CD2  1 
ATOM   6388 C CE1  . TYR   B 1 161 ? 42.618 -33.776 -13.241 1.00 19.70 ?  161 TYR   B CE1  1 
ATOM   6389 C CE2  . TYR   B 1 161 ? 42.848 -35.981 -14.141 1.00 20.51 ?  161 TYR   B CE2  1 
ATOM   6390 C CZ   . TYR   B 1 161 ? 42.469 -34.664 -14.284 1.00 20.41 ?  161 TYR   B CZ   1 
ATOM   6391 O OH   . TYR   B 1 161 ? 41.936 -34.232 -15.474 1.00 22.48 ?  161 TYR   B OH   1 
ATOM   6392 H H    . TYR   B 1 161 ? 44.605 -36.966 -8.406  1.00 20.92 ?  161 TYR   B H    1 
ATOM   6393 H HA   . TYR   B 1 161 ? 42.545 -35.708 -9.276  1.00 20.74 ?  161 TYR   B HA   1 
ATOM   6394 H HB2  . TYR   B 1 161 ? 44.608 -35.248 -10.179 1.00 21.72 ?  161 TYR   B HB2  1 
ATOM   6395 H HB3  . TYR   B 1 161 ? 44.729 -36.722 -10.754 1.00 21.72 ?  161 TYR   B HB3  1 
ATOM   6396 H HD1  . TYR   B 1 161 ? 43.248 -33.598 -11.353 1.00 22.09 ?  161 TYR   B HD1  1 
ATOM   6397 H HD2  . TYR   B 1 161 ? 43.634 -37.296 -12.852 1.00 23.46 ?  161 TYR   B HD2  1 
ATOM   6398 H HE1  . TYR   B 1 161 ? 42.361 -32.883 -13.343 1.00 23.62 ?  161 TYR   B HE1  1 
ATOM   6399 H HE2  . TYR   B 1 161 ? 42.743 -36.576 -14.849 1.00 24.60 ?  161 TYR   B HE2  1 
ATOM   6400 H HH   . TYR   B 1 161 ? 41.894 -34.875 -16.017 1.00 26.96 ?  161 TYR   B HH   1 
ATOM   6401 N N    . ASP   B 1 162 ? 42.635 -38.723 -10.388 1.00 17.45 ?  162 ASP   B N    1 
ATOM   6402 C CA   . ASP   B 1 162 ? 41.813 -39.761 -11.004 1.00 17.92 ?  162 ASP   B CA   1 
ATOM   6403 C C    . ASP   B 1 162 ? 40.603 -40.098 -10.141 1.00 17.25 ?  162 ASP   B C    1 
ATOM   6404 O O    . ASP   B 1 162 ? 39.502 -40.316 -10.662 1.00 17.72 ?  162 ASP   B O    1 
ATOM   6405 C CB   . ASP   B 1 162 ? 42.643 -41.023 -11.253 1.00 19.57 ?  162 ASP   B CB   1 
ATOM   6406 C CG   . ASP   B 1 162 ? 43.630 -40.871 -12.394 1.00 21.08 ?  162 ASP   B CG   1 
ATOM   6407 O OD1  . ASP   B 1 162 ? 43.496 -39.931 -13.200 1.00 21.14 ?  162 ASP   B OD1  1 
ATOM   6408 O OD2  . ASP   B 1 162 ? 44.534 -41.727 -12.497 1.00 22.90 -1 162 ASP   B OD2  1 
ATOM   6409 H H    . ASP   B 1 162 ? 43.437 -38.967 -10.193 1.00 20.93 ?  162 ASP   B H    1 
ATOM   6410 H HA   . ASP   B 1 162 ? 41.490 -39.439 -11.857 1.00 21.50 ?  162 ASP   B HA   1 
ATOM   6411 H HB2  . ASP   B 1 162 ? 43.151 -41.230 -10.455 1.00 23.47 ?  162 ASP   B HB2  1 
ATOM   6412 H HB3  . ASP   B 1 162 ? 42.048 -41.752 -11.474 1.00 23.47 ?  162 ASP   B HB3  1 
ATOM   6413 N N    A LYS   B 1 163 ? 40.789 -40.172 -8.821  0.60 16.48 ?  163 LYS   B N    1 
ATOM   6414 N N    B LYS   B 1 163 ? 40.786 -40.160 -8.820  0.40 17.19 ?  163 LYS   B N    1 
ATOM   6415 C CA   A LYS   B 1 163 ? 39.660 -40.448 -7.939  0.60 16.91 ?  163 LYS   B CA   1 
ATOM   6416 C CA   B LYS   B 1 163 ? 39.660 -40.448 -7.935  0.40 17.81 ?  163 LYS   B CA   1 
ATOM   6417 C C    A LYS   B 1 163 ? 38.617 -39.338 -8.014  0.60 15.92 ?  163 LYS   B C    1 
ATOM   6418 C C    B LYS   B 1 163 ? 38.618 -39.336 -7.984  0.40 16.48 ?  163 LYS   B C    1 
ATOM   6419 O O    A LYS   B 1 163 ? 37.408 -39.606 -8.045  0.60 16.99 ?  163 LYS   B O    1 
ATOM   6420 O O    B LYS   B 1 163 ? 37.410 -39.603 -7.956  0.40 17.21 ?  163 LYS   B O    1 
ATOM   6421 C CB   A LYS   B 1 163 ? 40.140 -40.631 -6.501  0.60 19.63 ?  163 LYS   B CB   1 
ATOM   6422 C CB   B LYS   B 1 163 ? 40.153 -40.647 -6.504  0.40 20.44 ?  163 LYS   B CB   1 
ATOM   6423 C CG   A LYS   B 1 163 ? 39.052 -41.167 -5.587  0.60 24.01 ?  163 LYS   B CG   1 
ATOM   6424 C CG   B LYS   B 1 163 ? 39.080 -41.172 -5.570  0.40 23.91 ?  163 LYS   B CG   1 
ATOM   6425 C CD   A LYS   B 1 163 ? 39.465 -41.190 -4.128  0.60 27.76 ?  163 LYS   B CD   1 
ATOM   6426 C CD   B LYS   B 1 163 ? 39.570 -41.300 -4.141  0.40 27.10 ?  163 LYS   B CD   1 
ATOM   6427 C CE   A LYS   B 1 163 ? 38.391 -41.866 -3.287  0.60 30.20 ?  163 LYS   B CE   1 
ATOM   6428 C CE   B LYS   B 1 163 ? 38.514 -41.975 -3.278  0.40 29.27 ?  163 LYS   B CE   1 
ATOM   6429 N NZ   A LYS   B 1 163 ? 38.510 -41.548 -1.839  0.60 31.63 ?  163 LYS   B NZ   1 
ATOM   6430 N NZ   B LYS   B 1 163 ? 38.713 -41.721 -1.826  0.40 30.28 ?  163 LYS   B NZ   1 
ATOM   6431 H H    A LYS   B 1 163 ? 41.547 -40.068 -8.423  0.60 19.77 ?  163 LYS   B H    1 
ATOM   6432 H H    B LYS   B 1 163 ? 41.541 -40.042 -8.420  0.40 20.62 ?  163 LYS   B H    1 
ATOM   6433 H HA   A LYS   B 1 163 ? 39.242 -41.274 -8.223  0.60 20.29 ?  163 LYS   B HA   1 
ATOM   6434 H HA   B LYS   B 1 163 ? 39.237 -41.270 -8.225  0.40 21.35 ?  163 LYS   B HA   1 
ATOM   6435 H HB2  A LYS   B 1 163 ? 40.879 -41.264 -6.492  0.60 23.54 ?  163 LYS   B HB2  1 
ATOM   6436 H HB2  B LYS   B 1 163 ? 40.884 -41.286 -6.509  0.40 24.52 ?  163 LYS   B HB2  1 
ATOM   6437 H HB3  A LYS   B 1 163 ? 40.433 -39.776 -6.153  0.60 23.54 ?  163 LYS   B HB3  1 
ATOM   6438 H HB3  B LYS   B 1 163 ? 40.462 -39.796 -6.156  0.40 24.52 ?  163 LYS   B HB3  1 
ATOM   6439 H HG2  A LYS   B 1 163 ? 38.266 -40.605 -5.666  0.60 28.79 ?  163 LYS   B HG2  1 
ATOM   6440 H HG2  B LYS   B 1 163 ? 38.325 -40.563 -5.575  0.40 28.68 ?  163 LYS   B HG2  1 
ATOM   6441 H HG3  A LYS   B 1 163 ? 38.836 -42.076 -5.852  0.60 28.79 ?  163 LYS   B HG3  1 
ATOM   6442 H HG3  B LYS   B 1 163 ? 38.799 -42.051 -5.872  0.40 28.68 ?  163 LYS   B HG3  1 
ATOM   6443 H HD2  A LYS   B 1 163 ? 40.290 -41.692 -4.032  0.60 33.30 ?  163 LYS   B HD2  1 
ATOM   6444 H HD2  B LYS   B 1 163 ? 40.376 -41.841 -4.122  0.40 32.51 ?  163 LYS   B HD2  1 
ATOM   6445 H HD3  A LYS   B 1 163 ? 39.580 -40.282 -3.809  0.60 33.30 ?  163 LYS   B HD3  1 
ATOM   6446 H HD3  B LYS   B 1 163 ? 39.746 -40.417 -3.779  0.40 32.51 ?  163 LYS   B HD3  1 
ATOM   6447 H HE2  A LYS   B 1 163 ? 37.515 -41.581 -3.592  0.60 36.23 ?  163 LYS   B HE2  1 
ATOM   6448 H HE2  B LYS   B 1 163 ? 37.639 -41.639 -3.528  0.40 35.11 ?  163 LYS   B HE2  1 
ATOM   6449 H HE3  A LYS   B 1 163 ? 38.473 -42.826 -3.388  0.60 36.23 ?  163 LYS   B HE3  1 
ATOM   6450 H HE3  B LYS   B 1 163 ? 38.554 -42.933 -3.425  0.40 35.11 ?  163 LYS   B HE3  1 
ATOM   6451 H HZ1  A LYS   B 1 163 ? 37.864 -41.959 -1.384  0.60 37.94 ?  163 LYS   B HZ1  1 
ATOM   6452 H HZ1  B LYS   B 1 163 ? 38.076 -42.131 -1.357  0.40 36.33 ?  163 LYS   B HZ1  1 
ATOM   6453 H HZ2  A LYS   B 1 163 ? 39.299 -41.821 -1.533  0.60 37.94 ?  163 LYS   B HZ2  1 
ATOM   6454 H HZ2  B LYS   B 1 163 ? 39.506 -42.030 -1.569  0.40 36.33 ?  163 LYS   B HZ2  1 
ATOM   6455 H HZ3  A LYS   B 1 163 ? 38.437 -40.670 -1.713  0.60 37.94 ?  163 LYS   B HZ3  1 
ATOM   6456 H HZ3  B LYS   B 1 163 ? 38.675 -40.847 -1.662  0.40 36.33 ?  163 LYS   B HZ3  1 
ATOM   6457 N N    . LEU   B 1 164 ? 39.070 -38.082 -8.054  1.00 15.28 ?  164 LEU   B N    1 
ATOM   6458 C CA   . LEU   B 1 164 ? 38.153 -36.947 -8.108  1.00 14.95 ?  164 LEU   B CA   1 
ATOM   6459 C C    . LEU   B 1 164 ? 37.375 -36.929 -9.417  1.00 15.34 ?  164 LEU   B C    1 
ATOM   6460 O O    . LEU   B 1 164 ? 36.152 -36.735 -9.422  1.00 16.43 ?  164 LEU   B O    1 
ATOM   6461 C CB   . LEU   B 1 164 ? 38.951 -35.649 -7.942  1.00 14.39 ?  164 LEU   B CB   1 
ATOM   6462 C CG   . LEU   B 1 164 ? 39.491 -35.373 -6.541  1.00 15.23 ?  164 LEU   B CG   1 
ATOM   6463 C CD1  . LEU   B 1 164 ? 40.587 -34.310 -6.592  1.00 15.47 ?  164 LEU   B CD1  1 
ATOM   6464 C CD2  . LEU   B 1 164 ? 38.379 -34.950 -5.592  1.00 17.13 ?  164 LEU   B CD2  1 
ATOM   6465 H H    A LEU   B 1 164 ? 39.906 -37.863 -8.054  0.60 18.33 ?  164 LEU   B H    1 
ATOM   6466 H H    B LEU   B 1 164 ? 39.906 -37.865 -8.076  0.40 18.33 ?  164 LEU   B H    1 
ATOM   6467 H HA   . LEU   B 1 164 ? 37.524 -37.012 -7.383  1.00 17.93 ?  164 LEU   B HA   1 
ATOM   6468 H HB2  . LEU   B 1 164 ? 39.714 -35.676 -8.547  1.00 17.26 ?  164 LEU   B HB2  1 
ATOM   6469 H HB3  . LEU   B 1 164 ? 38.380 -34.905 -8.185  1.00 17.26 ?  164 LEU   B HB3  1 
ATOM   6470 H HG   . LEU   B 1 164 ? 39.892 -36.183 -6.196  1.00 18.26 ?  164 LEU   B HG   1 
ATOM   6471 H HD11 . LEU   B 1 164 ? 40.913 -34.144 -5.692  1.00 18.56 ?  164 LEU   B HD11 1 
ATOM   6472 H HD12 . LEU   B 1 164 ? 41.318 -34.628 -7.150  1.00 18.56 ?  164 LEU   B HD12 1 
ATOM   6473 H HD13 . LEU   B 1 164 ? 40.224 -33.491 -6.966  1.00 18.56 ?  164 LEU   B HD13 1 
ATOM   6474 H HD21 . LEU   B 1 164 ? 38.765 -34.737 -4.728  1.00 20.55 ?  164 LEU   B HD21 1 
ATOM   6475 H HD22 . LEU   B 1 164 ? 37.931 -34.171 -5.955  1.00 20.55 ?  164 LEU   B HD22 1 
ATOM   6476 H HD23 . LEU   B 1 164 ? 37.751 -35.683 -5.502  1.00 20.55 ?  164 LEU   B HD23 1 
ATOM   6477 N N    . VAL   B 1 165 ? 38.070 -37.102 -10.544 1.00 17.02 ?  165 VAL   B N    1 
ATOM   6478 C CA   . VAL   B 1 165 ? 37.413 -37.039 -11.845 1.00 18.51 ?  165 VAL   B CA   1 
ATOM   6479 C C    . VAL   B 1 165 ? 36.491 -38.236 -12.025 1.00 20.11 ?  165 VAL   B C    1 
ATOM   6480 O O    . VAL   B 1 165 ? 35.327 -38.098 -12.423 1.00 21.05 ?  165 VAL   B O    1 
ATOM   6481 C CB   . VAL   B 1 165 ? 38.460 -36.960 -12.972 1.00 19.42 ?  165 VAL   B CB   1 
ATOM   6482 C CG1  . VAL   B 1 165 ? 37.798 -37.054 -14.326 1.00 20.37 ?  165 VAL   B CG1  1 
ATOM   6483 C CG2  . VAL   B 1 165 ? 39.265 -35.678 -12.862 1.00 18.99 ?  165 VAL   B CG2  1 
ATOM   6484 H H    . VAL   B 1 165 ? 38.918 -37.248 -10.582 1.00 20.41 ?  165 VAL   B H    1 
ATOM   6485 H HA   . VAL   B 1 165 ? 36.872 -36.238 -11.892 1.00 22.20 ?  165 VAL   B HA   1 
ATOM   6486 H HB   . VAL   B 1 165 ? 39.080 -37.701 -12.886 1.00 23.29 ?  165 VAL   B HB   1 
ATOM   6487 H HG11 . VAL   B 1 165 ? 38.419 -36.754 -15.005 1.00 24.44 ?  165 VAL   B HG11 1 
ATOM   6488 H HG12 . VAL   B 1 165 ? 37.557 -37.982 -14.491 1.00 24.44 ?  165 VAL   B HG12 1 
ATOM   6489 H HG13 . VAL   B 1 165 ? 37.005 -36.501 -14.329 1.00 24.44 ?  165 VAL   B HG13 1 
ATOM   6490 H HG21 . VAL   B 1 165 ? 39.903 -35.635 -13.594 1.00 22.77 ?  165 VAL   B HG21 1 
ATOM   6491 H HG22 . VAL   B 1 165 ? 38.661 -34.917 -12.912 1.00 22.77 ?  165 VAL   B HG22 1 
ATOM   6492 H HG23 . VAL   B 1 165 ? 39.737 -35.666 -12.015 1.00 22.77 ?  165 VAL   B HG23 1 
ATOM   6493 N N    . SER   B 1 166 ? 37.001 -39.434 -11.728 1.00 20.63 ?  166 SER   B N    1 
ATOM   6494 C CA   . SER   B 1 166 ? 36.245 -40.648 -12.009 1.00 21.97 ?  166 SER   B CA   1 
ATOM   6495 C C    . SER   B 1 166 ? 34.983 -40.736 -11.162 1.00 22.08 ?  166 SER   B C    1 
ATOM   6496 O O    . SER   B 1 166 ? 34.011 -41.360 -11.586 1.00 23.86 ?  166 SER   B O    1 
ATOM   6497 C CB   . SER   B 1 166 ? 37.113 -41.900 -11.832 1.00 22.93 ?  166 SER   B CB   1 
ATOM   6498 O OG   . SER   B 1 166 ? 37.469 -42.113 -10.476 1.00 22.76 ?  166 SER   B OG   1 
ATOM   6499 H H    . SER   B 1 166 ? 37.778 -39.567 -11.374 1.00 24.74 ?  166 SER   B H    1 
ATOM   6500 H HA   . SER   B 1 166 ? 35.970 -40.629 -12.937 1.00 26.36 ?  166 SER   B HA   1 
ATOM   6501 H HB2  . SER   B 1 166 ? 36.617 -42.673 -12.149 1.00 27.51 ?  166 SER   B HB2  1 
ATOM   6502 H HB3  . SER   B 1 166 ? 37.923 -41.798 -12.360 1.00 27.51 ?  166 SER   B HB3  1 
ATOM   6503 H HG   . SER   B 1 166 ? 37.914 -41.461 -10.193 1.00 27.30 ?  166 SER   B HG   1 
ATOM   6504 N N    . SER   B 1 167 ? 34.965 -40.121 -9.981  1.00 20.30 ?  167 SER   B N    1 
ATOM   6505 C CA   . SER   B 1 167 ? 33.807 -40.182 -9.097  1.00 20.08 ?  167 SER   B CA   1 
ATOM   6506 C C    . SER   B 1 167 ? 32.889 -38.965 -9.196  1.00 19.66 ?  167 SER   B C    1 
ATOM   6507 O O    . SER   B 1 167 ? 31.812 -38.968 -8.588  1.00 19.87 ?  167 SER   B O    1 
ATOM   6508 C CB   . SER   B 1 167 ? 34.255 -40.365 -7.641  1.00 20.05 ?  167 SER   B CB   1 
ATOM   6509 O OG   . SER   B 1 167 ? 34.929 -39.204 -7.172  1.00 19.50 ?  167 SER   B OG   1 
ATOM   6510 H H    . SER   B 1 167 ? 35.618 -39.665 -9.670  1.00 24.35 ?  167 SER   B H    1 
ATOM   6511 H HA   . SER   B 1 167 ? 33.279 -40.959 -9.338  1.00 24.08 ?  167 SER   B HA   1 
ATOM   6512 H HB2  . SER   B 1 167 ? 33.474 -40.525 -7.088  1.00 24.05 ?  167 SER   B HB2  1 
ATOM   6513 H HB3  . SER   B 1 167 ? 34.853 -41.134 -7.591  1.00 24.05 ?  167 SER   B HB3  1 
ATOM   6514 H HG   . SER   B 1 167 ? 35.617 -39.073 -7.638  1.00 23.39 ?  167 SER   B HG   1 
ATOM   6515 N N    . PHE   B 1 168 ? 33.270 -37.929 -9.946  1.00 19.43 ?  168 PHE   B N    1 
ATOM   6516 C CA   . PHE   B 1 168 ? 32.436 -36.729 -10.013 1.00 18.78 ?  168 PHE   B CA   1 
ATOM   6517 C C    . PHE   B 1 168 ? 31.122 -37.000 -10.739 1.00 16.65 ?  168 PHE   B C    1 
ATOM   6518 O O    . PHE   B 1 168 ? 30.077 -36.413 -10.398 1.00 17.25 ?  168 PHE   B O    1 
ATOM   6519 C CB   . PHE   B 1 168 ? 33.189 -35.589 -10.700 1.00 19.34 ?  168 PHE   B CB   1 
ATOM   6520 C CG   . PHE   B 1 168 ? 32.382 -34.340 -10.816 1.00 19.60 ?  168 PHE   B CG   1 
ATOM   6521 C CD1  . PHE   B 1 168 ? 32.053 -33.612 -9.682  1.00 20.76 ?  168 PHE   B CD1  1 
ATOM   6522 C CD2  . PHE   B 1 168 ? 31.931 -33.904 -12.043 1.00 18.98 ?  168 PHE   B CD2  1 
ATOM   6523 C CE1  . PHE   B 1 168 ? 31.291 -32.464 -9.770  1.00 21.32 ?  168 PHE   B CE1  1 
ATOM   6524 C CE2  . PHE   B 1 168 ? 31.176 -32.739 -12.146 1.00 20.19 ?  168 PHE   B CE2  1 
ATOM   6525 C CZ   . PHE   B 1 168 ? 30.850 -32.021 -11.004 1.00 20.63 ?  168 PHE   B CZ   1 
ATOM   6526 H H    . PHE   B 1 168 ? 33.995 -37.891 -10.410 1.00 23.31 ?  168 PHE   B H    1 
ATOM   6527 H HA   . PHE   B 1 168 ? 32.221 -36.445 -9.114  1.00 22.52 ?  168 PHE   B HA   1 
ATOM   6528 H HB2  . PHE   B 1 168 ? 33.981 -35.380 -10.185 1.00 23.19 ?  168 PHE   B HB2  1 
ATOM   6529 H HB3  . PHE   B 1 168 ? 33.435 -35.865 -11.595 1.00 23.19 ?  168 PHE   B HB3  1 
ATOM   6530 H HD1  . PHE   B 1 168 ? 32.342 -33.914 -8.850  1.00 24.90 ?  168 PHE   B HD1  1 
ATOM   6531 H HD2  . PHE   B 1 168 ? 32.147 -34.379 -12.813 1.00 22.76 ?  168 PHE   B HD2  1 
ATOM   6532 H HE1  . PHE   B 1 168 ? 31.075 -31.989 -9.000  1.00 25.58 ?  168 PHE   B HE1  1 
ATOM   6533 H HE2  . PHE   B 1 168 ? 30.875 -32.448 -12.979 1.00 24.22 ?  168 PHE   B HE2  1 
ATOM   6534 H HZ   . PHE   B 1 168 ? 30.336 -31.247 -11.071 1.00 24.75 ?  168 PHE   B HZ   1 
ATOM   6535 N N    . LEU   B 1 169 ? 31.155 -37.878 -11.739 1.00 16.99 ?  169 LEU   B N    1 
ATOM   6536 C CA   . LEU   B 1 169 ? 29.975 -38.187 -12.535 1.00 19.24 ?  169 LEU   B CA   1 
ATOM   6537 C C    . LEU   B 1 169 ? 29.972 -39.626 -13.032 1.00 22.19 ?  169 LEU   B C    1 
ATOM   6538 O O    . LEU   B 1 169 ? 29.072 -40.038 -13.767 1.00 24.77 ?  169 LEU   B O    1 
ATOM   6539 C CB   . LEU   B 1 169 ? 29.889 -37.242 -13.731 1.00 21.52 ?  169 LEU   B CB   1 
ATOM   6540 C CG   . LEU   B 1 169 ? 28.615 -36.400 -13.816 1.00 24.88 ?  169 LEU   B CG   1 
ATOM   6541 C CD1  . LEU   B 1 169 ? 28.549 -35.707 -15.160 1.00 26.00 ?  169 LEU   B CD1  1 
ATOM   6542 C CD2  . LEU   B 1 169 ? 27.365 -37.234 -13.583 1.00 25.30 ?  169 LEU   B CD2  1 
ATOM   6543 O OXT  . LEU   B 1 169 ? 30.871 -40.398 -12.716 1.00 22.93 -1 169 LEU   B OXT  1 
ATOM   6544 H H    . LEU   B 1 169 ? 31.861 -38.304 -11.991 1.00 20.37 ?  169 LEU   B H    1 
ATOM   6545 H HA   . LEU   B 1 169 ? 29.193 -38.055 -11.983 1.00 23.08 ?  169 LEU   B HA   1 
ATOM   6546 H HB2  . LEU   B 1 169 ? 30.638 -36.625 -13.697 1.00 25.81 ?  169 LEU   B HB2  1 
ATOM   6547 H HB3  . LEU   B 1 169 ? 29.940 -37.765 -14.547 1.00 25.81 ?  169 LEU   B HB3  1 
ATOM   6548 H HG   . LEU   B 1 169 ? 28.646 -35.713 -13.131 1.00 29.84 ?  169 LEU   B HG   1 
ATOM   6549 H HD11 . LEU   B 1 169 ? 27.753 -35.154 -15.190 1.00 31.19 ?  169 LEU   B HD11 1 
ATOM   6550 H HD12 . LEU   B 1 169 ? 29.340 -35.157 -15.268 1.00 31.19 ?  169 LEU   B HD12 1 
ATOM   6551 H HD13 . LEU   B 1 169 ? 28.514 -36.380 -15.857 1.00 31.19 ?  169 LEU   B HD13 1 
ATOM   6552 H HD21 . LEU   B 1 169 ? 26.608 -36.796 -13.997 1.00 30.34 ?  169 LEU   B HD21 1 
ATOM   6553 H HD22 . LEU   B 1 169 ? 27.496 -38.113 -13.975 1.00 30.34 ?  169 LEU   B HD22 1 
ATOM   6554 H HD23 . LEU   B 1 169 ? 27.219 -37.318 -12.628 1.00 30.34 ?  169 LEU   B HD23 1 
HETATM 6555 S S    B DMS   C 2 .   ? 14.714 6.795   5.688   0.40 27.66 ?  301 DMS   A S    1 
HETATM 6556 O O    B DMS   C 2 .   ? 14.798 7.206   4.238   0.40 27.50 ?  301 DMS   A O    1 
HETATM 6557 C C1   B DMS   C 2 .   ? 13.131 5.915   5.891   0.40 27.78 ?  301 DMS   A C1   1 
HETATM 6558 C C2   B DMS   C 2 .   ? 14.375 8.298   6.664   0.40 28.05 ?  301 DMS   A C2   1 
HETATM 6559 H H11  B DMS   C 2 .   ? 13.109 5.622   6.884   0.40 33.32 ?  301 DMS   A H11  1 
HETATM 6560 H H12  B DMS   C 2 .   ? 12.397 6.602   5.650   0.40 33.32 ?  301 DMS   A H12  1 
HETATM 6561 H H13  B DMS   C 2 .   ? 13.142 5.097   5.238   0.40 33.32 ?  301 DMS   A H13  1 
HETATM 6562 H H21  B DMS   C 2 .   ? 13.412 8.579   6.410   0.40 33.65 ?  301 DMS   A H21  1 
HETATM 6563 H H22  B DMS   C 2 .   ? 15.084 9.016   6.389   0.40 33.65 ?  301 DMS   A H22  1 
HETATM 6564 H H23  B DMS   C 2 .   ? 14.469 8.010   7.653   0.40 33.65 ?  301 DMS   A H23  1 
HETATM 6565 N N2   B A1BAG D 3 .   ? 17.382 1.516   -0.975  0.40 19.13 ?  302 A1BAG A N2   1 
HETATM 6566 C C3   B A1BAG D 3 .   ? 18.688 1.036   -1.436  0.40 18.78 ?  302 A1BAG A C3   1 
HETATM 6567 C C6   B A1BAG D 3 .   ? 14.275 1.221   0.940   0.40 19.61 ?  302 A1BAG A C6   1 
HETATM 6568 C C9   B A1BAG D 3 .   ? 13.827 -1.058  1.730   0.40 19.49 ?  302 A1BAG A C9   1 
HETATM 6569 C C12  B A1BAG D 3 .   ? 14.831 -0.192  5.625   0.40 16.21 ?  302 A1BAG A C12  1 
HETATM 6570 C C14  B A1BAG D 3 .   ? 15.211 1.834   3.843   0.40 16.40 ?  302 A1BAG A C14  1 
HETATM 6571 C C1   B A1BAG D 3 .   ? 14.737 3.926   -0.861  0.40 19.47 ?  302 A1BAG A C1   1 
HETATM 6572 C C10  B A1BAG D 3 .   ? 14.783 -2.285  1.653   0.40 19.31 ?  302 A1BAG A C10  1 
HETATM 6573 C C11  B A1BAG D 3 .   ? 14.780 0.536   3.393   0.40 16.71 ?  302 A1BAG A C11  1 
HETATM 6574 C C13  B A1BAG D 3 .   ? 15.409 1.928   5.252   0.40 16.27 ?  302 A1BAG A C13  1 
HETATM 6575 C C15  B A1BAG D 3 .   ? 15.534 3.135   3.331   0.40 16.61 ?  302 A1BAG A C15  1 
HETATM 6576 C C16  B A1BAG D 3 .   ? 15.901 3.944   4.394   0.40 16.35 ?  302 A1BAG A C16  1 
HETATM 6577 C C2   B A1BAG D 3 .   ? 15.640 2.771   -0.708  0.40 19.40 ?  302 A1BAG A C2   1 
HETATM 6578 C C4   B A1BAG D 3 .   ? 16.560 0.812   -0.108  0.40 19.04 ?  302 A1BAG A C4   1 
HETATM 6579 C C5   B A1BAG D 3 .   ? 15.429 1.589   0.090   0.40 19.52 ?  302 A1BAG A C5   1 
HETATM 6580 C C7   B A1BAG D 3 .   ? 13.184 0.610   0.039   0.40 20.09 ?  302 A1BAG A C7   1 
HETATM 6581 C C8   B A1BAG D 3 .   ? 13.108 -0.865  0.379   0.40 20.12 ?  302 A1BAG A C8   1 
HETATM 6582 N N1   B A1BAG D 3 .   ? 16.840 2.708   -1.352  0.40 19.50 ?  302 A1BAG A N1   1 
HETATM 6583 N N3   B A1BAG D 3 .   ? 14.505 0.212   2.029   0.40 18.90 ?  302 A1BAG A N3   1 
HETATM 6584 N N4   B A1BAG D 3 .   ? 14.585 -0.467  4.308   0.40 16.33 ?  302 A1BAG A N4   1 
HETATM 6585 N N5   B A1BAG D 3 .   ? 15.235 0.955   6.165   0.40 16.13 ?  302 A1BAG A N5   1 
HETATM 6586 N N6   B A1BAG D 3 .   ? 15.836 3.229   5.601   0.40 16.38 ?  302 A1BAG A N6   1 
HETATM 6587 O O1   B A1BAG D 3 .   ? 14.806 -2.880  2.936   0.40 19.08 ?  302 A1BAG A O1   1 
HETATM 6588 H H8   B A1BAG D 3 .   ? 19.261 1.844   -1.922  0.40 22.52 ?  302 A1BAG A H8   1 
HETATM 6589 H H6   B A1BAG D 3 .   ? 18.622 0.206   -2.162  0.40 22.52 ?  302 A1BAG A H6   1 
HETATM 6590 H H7   B A1BAG D 3 .   ? 19.310 0.677   -0.596  0.40 22.52 ?  302 A1BAG A H7   1 
HETATM 6591 H H1   B A1BAG D 3 .   ? 13.867 2.148   1.419   0.40 23.52 ?  302 A1BAG A H1   1 
HETATM 6592 H H2   B A1BAG D 3 .   ? 13.063 -1.231  2.531   0.40 23.37 ?  302 A1BAG A H2   1 
HETATM 6593 H H17  B A1BAG D 3 .   ? 14.693 -0.973  6.385   0.40 19.44 ?  302 A1BAG A H17  1 
HETATM 6594 H H4   B A1BAG D 3 .   ? 15.256 4.772   -1.342  0.40 23.35 ?  302 A1BAG A H4   1 
HETATM 6595 H H5   B A1BAG D 3 .   ? 14.359 4.323   0.086   0.40 23.35 ?  302 A1BAG A H5   1 
HETATM 6596 H H3   B A1BAG D 3 .   ? 13.870 3.696   -1.492  0.40 23.35 ?  302 A1BAG A H3   1 
HETATM 6597 H H15  B A1BAG D 3 .   ? 15.811 -1.995  1.337   0.40 23.16 ?  302 A1BAG A H15  1 
HETATM 6598 H H14  B A1BAG D 3 .   ? 14.425 -3.012  0.899   0.40 23.16 ?  302 A1BAG A H14  1 
HETATM 6599 H H18  B A1BAG D 3 .   ? 15.506 3.454   2.312   0.40 19.92 ?  302 A1BAG A H18  1 
HETATM 6600 H H19  B A1BAG D 3 .   ? 16.215 4.984   4.446   0.40 19.61 ?  302 A1BAG A H19  1 
HETATM 6601 H H9   B A1BAG D 3 .   ? 16.813 -0.159  0.299   0.40 22.84 ?  302 A1BAG A H9   1 
HETATM 6602 H H10  B A1BAG D 3 .   ? 12.203 1.108   0.144   0.40 24.10 ?  302 A1BAG A H10  1 
HETATM 6603 H H11  B A1BAG D 3 .   ? 13.405 0.763   -1.036  0.40 24.10 ?  302 A1BAG A H11  1 
HETATM 6604 H H12  B A1BAG D 3 .   ? 13.511 -1.497  -0.438  0.40 24.14 ?  302 A1BAG A H12  1 
HETATM 6605 H H13  B A1BAG D 3 .   ? 12.066 -1.221  0.429   0.40 24.14 ?  302 A1BAG A H13  1 
HETATM 6606 H H20  B A1BAG D 3 .   ? 16.034 3.523   6.521   0.40 19.64 ?  302 A1BAG A H20  1 
HETATM 6607 H H16  B A1BAG D 3 .   ? 13.949 -3.299  3.072   0.40 22.88 ?  302 A1BAG A H16  1 
HETATM 6608 O O    . HOH   E 4 .   ? 34.395 -1.901  12.487  1.00 38.16 ?  401 HOH   A O    1 
HETATM 6609 O O    B HOH   E 4 .   ? 18.676 -2.059  -0.985  0.40 31.54 ?  402 HOH   A O    1 
HETATM 6610 O O    . HOH   E 4 .   ? 4.779  3.991   0.807   1.00 27.43 ?  403 HOH   A O    1 
HETATM 6611 O O    A HOH   E 4 .   ? 12.356 0.227   14.919  0.60 24.66 ?  404 HOH   A O    1 
HETATM 6612 O O    . HOH   E 4 .   ? 11.622 -10.776 -10.072 1.00 41.85 ?  405 HOH   A O    1 
HETATM 6613 O O    . HOH   E 4 .   ? 28.977 0.523   -9.663  1.00 21.59 ?  406 HOH   A O    1 
HETATM 6614 O O    . HOH   E 4 .   ? 14.174 -4.527  -11.848 1.00 31.35 ?  407 HOH   A O    1 
HETATM 6615 O O    . HOH   E 4 .   ? 15.231 -21.625 14.240  1.00 18.63 ?  408 HOH   A O    1 
HETATM 6616 O O    . HOH   E 4 .   ? 26.890 11.439  1.675   1.00 17.61 ?  409 HOH   A O    1 
HETATM 6617 O O    A HOH   E 4 .   ? 14.858 -4.635  20.461  0.60 31.84 ?  410 HOH   A O    1 
HETATM 6618 O O    . HOH   E 4 .   ? 7.986  -12.551 -0.825  1.00 21.24 ?  411 HOH   A O    1 
HETATM 6619 O O    . HOH   E 4 .   ? 14.037 -4.978  17.624  1.00 25.25 ?  412 HOH   A O    1 
HETATM 6620 O O    . HOH   E 4 .   ? -0.459 -3.060  3.135   1.00 41.56 ?  413 HOH   A O    1 
HETATM 6621 O O    . HOH   E 4 .   ? 7.685  -6.276  -6.513  1.00 42.58 ?  414 HOH   A O    1 
HETATM 6622 O O    . HOH   E 4 .   ? 18.988 -22.015 6.940   1.00 34.26 ?  415 HOH   A O    1 
HETATM 6623 O O    . HOH   E 4 .   ? 15.154 -12.287 18.724  1.00 35.21 ?  416 HOH   A O    1 
HETATM 6624 O O    . HOH   E 4 .   ? 42.498 10.563  5.140   1.00 20.35 ?  417 HOH   A O    1 
HETATM 6625 O O    . HOH   E 4 .   ? 30.248 -13.318 -8.556  1.00 24.10 ?  418 HOH   A O    1 
HETATM 6626 O O    . HOH   E 4 .   ? 28.303 -6.368  19.600  1.00 43.16 ?  419 HOH   A O    1 
HETATM 6627 O O    . HOH   E 4 .   ? 31.066 6.182   -12.297 1.00 30.38 ?  420 HOH   A O    1 
HETATM 6628 O O    . HOH   E 4 .   ? 17.093 -18.096 15.129  1.00 25.43 ?  421 HOH   A O    1 
HETATM 6629 O O    . HOH   E 4 .   ? 20.134 4.555   -7.524  1.00 17.92 ?  422 HOH   A O    1 
HETATM 6630 O O    . HOH   E 4 .   ? 19.853 -12.410 -9.032  1.00 25.49 ?  423 HOH   A O    1 
HETATM 6631 O O    . HOH   E 4 .   ? 34.056 -0.989  -8.910  1.00 29.56 ?  424 HOH   A O    1 
HETATM 6632 O O    . HOH   E 4 .   ? 16.025 2.149   24.843  1.00 51.34 ?  425 HOH   A O    1 
HETATM 6633 O O    . HOH   E 4 .   ? 28.652 -10.539 -14.002 1.00 44.92 ?  426 HOH   A O    1 
HETATM 6634 O O    . HOH   E 4 .   ? 28.322 -0.093  -13.324 1.00 35.34 ?  427 HOH   A O    1 
HETATM 6635 O O    . HOH   E 4 .   ? 36.237 -5.099  -0.554  1.00 30.72 ?  428 HOH   A O    1 
HETATM 6636 O O    . HOH   E 4 .   ? 9.856  -21.385 5.693   1.00 20.50 ?  429 HOH   A O    1 
HETATM 6637 O O    . HOH   E 4 .   ? 10.436 -22.131 -1.219  1.00 45.72 ?  430 HOH   A O    1 
HETATM 6638 O O    . HOH   E 4 .   ? 0.777  -4.560  0.280   1.00 31.80 ?  431 HOH   A O    1 
HETATM 6639 O O    . HOH   E 4 .   ? 14.764 -14.051 16.729  1.00 23.14 ?  432 HOH   A O    1 
HETATM 6640 O O    . HOH   E 4 .   ? 38.334 10.128  7.164   1.00 48.48 ?  433 HOH   A O    1 
HETATM 6641 O O    . HOH   E 4 .   ? 37.605 2.760   10.191  1.00 28.19 ?  434 HOH   A O    1 
HETATM 6642 O O    . HOH   E 4 .   ? 31.064 -18.166 7.781   1.00 21.14 ?  435 HOH   A O    1 
HETATM 6643 O O    . HOH   E 4 .   ? 17.027 -19.294 4.890   1.00 16.65 ?  436 HOH   A O    1 
HETATM 6644 O O    . HOH   E 4 .   ? 22.292 -19.373 11.336  1.00 36.58 ?  437 HOH   A O    1 
HETATM 6645 O O    . HOH   E 4 .   ? 27.357 13.804  2.894   1.00 30.92 ?  438 HOH   A O    1 
HETATM 6646 O O    A HOH   E 4 .   ? 14.678 -3.663  3.139   0.60 16.26 ?  439 HOH   A O    1 
HETATM 6647 O O    . HOH   E 4 .   ? 38.646 4.970   6.959   1.00 15.89 ?  440 HOH   A O    1 
HETATM 6648 O O    A HOH   E 4 .   ? 9.313  -10.258 19.422  0.60 32.55 ?  441 HOH   A O    1 
HETATM 6649 O O    . HOH   E 4 .   ? 20.614 -19.781 -5.052  1.00 31.51 ?  442 HOH   A O    1 
HETATM 6650 O O    . HOH   E 4 .   ? 39.806 -0.994  -5.194  1.00 20.31 ?  443 HOH   A O    1 
HETATM 6651 O O    . HOH   E 4 .   ? 37.194 -2.780  9.733   1.00 41.63 ?  444 HOH   A O    1 
HETATM 6652 O O    . HOH   E 4 .   ? 17.164 -17.874 -5.033  1.00 28.26 ?  445 HOH   A O    1 
HETATM 6653 O O    . HOH   E 4 .   ? 18.724 -19.432 13.540  1.00 41.72 ?  446 HOH   A O    1 
HETATM 6654 O O    B HOH   E 4 .   ? 24.219 3.501   -1.719  0.40 22.38 ?  447 HOH   A O    1 
HETATM 6655 O O    . HOH   E 4 .   ? 31.764 8.215   14.832  1.00 24.11 ?  448 HOH   A O    1 
HETATM 6656 O O    . HOH   E 4 .   ? 14.038 -23.076 7.456   1.00 19.26 ?  449 HOH   A O    1 
HETATM 6657 O O    . HOH   E 4 .   ? 22.634 -12.007 21.866  1.00 42.69 ?  450 HOH   A O    1 
HETATM 6658 O O    . HOH   E 4 .   ? 15.142 3.905   17.846  1.00 43.68 ?  451 HOH   A O    1 
HETATM 6659 O O    . HOH   E 4 .   ? 44.385 7.110   6.487   1.00 27.24 ?  452 HOH   A O    1 
HETATM 6660 O O    . HOH   E 4 .   ? 22.386 5.384   19.011  1.00 44.04 ?  453 HOH   A O    1 
HETATM 6661 O O    . HOH   E 4 .   ? 35.813 -12.701 6.788   1.00 16.36 ?  454 HOH   A O    1 
HETATM 6662 O O    . HOH   E 4 .   ? 24.049 -2.089  -2.051  1.00 11.01 ?  455 HOH   A O    1 
HETATM 6663 O O    . HOH   E 4 .   ? 22.792 12.539  1.658   1.00 15.67 ?  456 HOH   A O    1 
HETATM 6664 O O    . HOH   E 4 .   ? 7.832  -21.535 4.118   1.00 42.58 ?  457 HOH   A O    1 
HETATM 6665 O O    . HOH   E 4 .   ? 27.343 -5.797  -13.978 1.00 39.04 ?  458 HOH   A O    1 
HETATM 6666 O O    B HOH   E 4 .   ? 15.760 6.241   1.857   0.40 29.07 ?  459 HOH   A O    1 
HETATM 6667 O O    A HOH   E 4 .   ? 21.282 -2.400  -2.018  0.60 13.26 ?  460 HOH   A O    1 
HETATM 6668 O O    . HOH   E 4 .   ? 21.872 -21.905 8.405   1.00 28.80 ?  461 HOH   A O    1 
HETATM 6669 O O    . HOH   E 4 .   ? 42.670 4.307   5.387   1.00 33.34 ?  462 HOH   A O    1 
HETATM 6670 O O    . HOH   E 4 .   ? 37.432 11.935  4.956   1.00 30.71 ?  463 HOH   A O    1 
HETATM 6671 O O    . HOH   E 4 .   ? 31.090 -13.949 -2.505  1.00 13.99 ?  464 HOH   A O    1 
HETATM 6672 O O    A HOH   E 4 .   ? 7.004  -8.180  11.895  0.60 18.73 ?  465 HOH   A O    1 
HETATM 6673 O O    . HOH   E 4 .   ? 33.694 -7.179  4.254   1.00 16.85 ?  466 HOH   A O    1 
HETATM 6674 O O    . HOH   E 4 .   ? 31.783 -9.357  -6.687  1.00 22.08 ?  467 HOH   A O    1 
HETATM 6675 O O    . HOH   E 4 .   ? 14.330 -21.218 -4.231  1.00 32.43 ?  468 HOH   A O    1 
HETATM 6676 O O    . HOH   E 4 .   ? 16.489 -22.043 0.966   1.00 29.17 ?  469 HOH   A O    1 
HETATM 6677 O O    B HOH   E 4 .   ? 12.230 6.783   9.489   0.40 34.26 ?  470 HOH   A O    1 
HETATM 6678 O O    . HOH   E 4 .   ? 30.871 3.076   8.278   1.00 12.44 ?  471 HOH   A O    1 
HETATM 6679 O O    . HOH   E 4 .   ? -1.613 -5.172  7.753   1.00 48.57 ?  472 HOH   A O    1 
HETATM 6680 O O    A HOH   E 4 .   ? 18.605 9.435   8.957   0.60 17.71 ?  473 HOH   A O    1 
HETATM 6681 O O    B HOH   E 4 .   ? 10.955 2.489   11.888  0.40 32.06 ?  474 HOH   A O    1 
HETATM 6682 O O    . HOH   E 4 .   ? 13.293 -1.391  -6.594  1.00 17.42 ?  475 HOH   A O    1 
HETATM 6683 O O    . HOH   E 4 .   ? 6.543  -5.649  11.265  1.00 23.11 ?  476 HOH   A O    1 
HETATM 6684 O O    A HOH   E 4 .   ? 17.536 -1.719  0.482   0.60 16.25 ?  477 HOH   A O    1 
HETATM 6685 O O    . HOH   E 4 .   ? 43.966 8.473   -3.100  1.00 28.56 ?  478 HOH   A O    1 
HETATM 6686 O O    A HOH   E 4 .   ? 11.096 1.530   12.807  0.60 21.25 ?  479 HOH   A O    1 
HETATM 6687 O O    . HOH   E 4 .   ? 27.588 -10.666 14.034  1.00 17.88 ?  480 HOH   A O    1 
HETATM 6688 O O    . HOH   E 4 .   ? 24.374 -7.858  14.473  1.00 17.98 ?  481 HOH   A O    1 
HETATM 6689 O O    . HOH   E 4 .   ? -0.542 -8.472  2.259   1.00 48.91 ?  482 HOH   A O    1 
HETATM 6690 O O    . HOH   E 4 .   ? 13.539 -15.225 -7.497  1.00 27.39 ?  483 HOH   A O    1 
HETATM 6691 O O    A HOH   E 4 .   ? 24.465 3.598   -1.817  0.60 12.47 ?  484 HOH   A O    1 
HETATM 6692 O O    . HOH   E 4 .   ? 23.532 11.393  4.124   1.00 12.95 ?  485 HOH   A O    1 
HETATM 6693 O O    . HOH   E 4 .   ? 43.451 7.853   2.718   1.00 28.72 ?  486 HOH   A O    1 
HETATM 6694 O O    . HOH   E 4 .   ? 31.736 -7.254  -9.890  1.00 21.66 ?  487 HOH   A O    1 
HETATM 6695 O O    . HOH   E 4 .   ? 33.537 -16.979 8.044   1.00 19.88 ?  488 HOH   A O    1 
HETATM 6696 O O    . HOH   E 4 .   ? 25.700 -0.745  -7.292  1.00 14.82 ?  489 HOH   A O    1 
HETATM 6697 O O    A HOH   E 4 .   ? 15.592 11.899  8.117   0.60 25.18 ?  490 HOH   A O    1 
HETATM 6698 O O    . HOH   E 4 .   ? 14.475 -0.434  -12.034 1.00 26.23 ?  491 HOH   A O    1 
HETATM 6699 O O    . HOH   E 4 .   ? 3.423  -9.016  10.119  1.00 44.54 ?  492 HOH   A O    1 
HETATM 6700 O O    B HOH   E 4 .   ? 18.385 9.293   8.884   0.40 25.54 ?  493 HOH   A O    1 
HETATM 6701 O O    . HOH   E 4 .   ? 21.294 10.288  15.061  1.00 37.12 ?  494 HOH   A O    1 
HETATM 6702 O O    A HOH   E 4 .   ? 14.326 0.559   6.849   0.60 21.36 ?  495 HOH   A O    1 
HETATM 6703 O O    . HOH   E 4 .   ? 24.782 -17.594 12.689  1.00 24.98 ?  496 HOH   A O    1 
HETATM 6704 O O    . HOH   E 4 .   ? 26.964 4.176   -0.649  1.00 12.84 ?  497 HOH   A O    1 
HETATM 6705 O O    B HOH   E 4 .   ? 21.351 -2.128  -2.565  0.40 16.79 ?  498 HOH   A O    1 
HETATM 6706 O O    . HOH   E 4 .   ? 21.834 -13.784 -8.083  1.00 34.01 ?  499 HOH   A O    1 
HETATM 6707 O O    B HOH   E 4 .   ? 21.091 2.695   0.065   0.40 22.77 ?  500 HOH   A O    1 
HETATM 6708 O O    A HOH   E 4 .   ? 21.389 3.149   -0.307  0.60 11.08 ?  501 HOH   A O    1 
HETATM 6709 O O    . HOH   E 4 .   ? 37.604 -2.052  5.752   1.00 28.03 ?  502 HOH   A O    1 
HETATM 6710 O O    . HOH   E 4 .   ? 32.829 -9.265  5.920   1.00 20.63 ?  503 HOH   A O    1 
HETATM 6711 O O    . HOH   E 4 .   ? 30.808 1.846   16.701  1.00 21.13 ?  504 HOH   A O    1 
HETATM 6712 O O    . HOH   E 4 .   ? 20.592 -20.036 2.752   1.00 18.57 ?  505 HOH   A O    1 
HETATM 6713 O O    . HOH   E 4 .   ? 30.156 -10.152 12.983  1.00 22.13 ?  506 HOH   A O    1 
HETATM 6714 O O    . HOH   E 4 .   ? 27.369 2.263   18.708  1.00 30.19 ?  507 HOH   A O    1 
HETATM 6715 O O    B HOH   E 4 .   ? 24.424 1.888   -6.884  0.40 24.76 ?  508 HOH   A O    1 
HETATM 6716 O O    A HOH   E 4 .   ? 5.352  2.629   5.338   0.60 28.26 ?  509 HOH   A O    1 
HETATM 6717 O O    . HOH   E 4 .   ? 23.948 -20.302 -1.406  1.00 17.25 ?  510 HOH   A O    1 
HETATM 6718 O O    . HOH   E 4 .   ? 15.132 -8.035  -9.602  1.00 23.04 ?  511 HOH   A O    1 
HETATM 6719 O O    . HOH   E 4 .   ? 18.493 4.919   -15.101 1.00 47.92 ?  512 HOH   A O    1 
HETATM 6720 O O    . HOH   E 4 .   ? 38.163 -1.372  -1.964  1.00 19.34 ?  513 HOH   A O    1 
HETATM 6721 O O    . HOH   E 4 .   ? 23.976 -15.704 -9.181  1.00 36.70 ?  514 HOH   A O    1 
HETATM 6722 O O    . HOH   E 4 .   ? 14.412 -24.748 11.562  1.00 40.79 ?  515 HOH   A O    1 
HETATM 6723 O O    A HOH   E 4 .   ? 9.069  -12.149 17.226  0.60 38.45 ?  516 HOH   A O    1 
HETATM 6724 O O    . HOH   E 4 .   ? 41.658 1.559   4.960   1.00 37.47 ?  517 HOH   A O    1 
HETATM 6725 O O    B HOH   E 4 .   ? 20.917 4.394   -2.245  0.40 23.38 ?  518 HOH   A O    1 
HETATM 6726 O O    . HOH   E 4 .   ? 27.160 -3.290  19.333  1.00 36.05 ?  519 HOH   A O    1 
HETATM 6727 O O    A HOH   E 4 .   ? 24.613 2.043   -6.952  0.60 15.85 ?  520 HOH   A O    1 
HETATM 6728 O O    A HOH   E 4 .   ? 24.125 3.958   -4.877  0.60 19.29 ?  521 HOH   A O    1 
HETATM 6729 O O    . HOH   E 4 .   ? 40.944 -8.308  -6.648  1.00 37.03 ?  522 HOH   A O    1 
HETATM 6730 O O    . HOH   E 4 .   ? 27.974 0.841   -7.119  1.00 14.05 ?  523 HOH   A O    1 
HETATM 6731 O O    A HOH   E 4 .   ? 15.848 -0.957  5.314   0.60 21.67 ?  524 HOH   A O    1 
HETATM 6732 O O    A HOH   E 4 .   ? 18.996 -0.672  -1.586  0.60 11.54 ?  525 HOH   A O    1 
HETATM 6733 O O    . HOH   E 4 .   ? 6.807  -3.368  13.060  1.00 33.25 ?  526 HOH   A O    1 
HETATM 6734 O O    . HOH   E 4 .   ? 45.035 -0.669  2.949   1.00 42.12 ?  527 HOH   A O    1 
HETATM 6735 O O    . HOH   E 4 .   ? 30.442 -13.004 13.471  1.00 20.56 ?  528 HOH   A O    1 
HETATM 6736 O O    . HOH   E 4 .   ? 36.772 -4.968  5.355   1.00 24.19 ?  529 HOH   A O    1 
HETATM 6737 O O    . HOH   E 4 .   ? 22.763 8.101   18.434  1.00 43.01 ?  530 HOH   A O    1 
HETATM 6738 O O    . HOH   E 4 .   ? 16.265 -14.270 20.320  1.00 48.43 ?  531 HOH   A O    1 
HETATM 6739 O O    . HOH   E 4 .   ? 32.664 -4.229  -9.927  1.00 29.04 ?  532 HOH   A O    1 
HETATM 6740 O O    . HOH   E 4 .   ? 18.695 -2.385  -16.398 1.00 51.69 ?  533 HOH   A O    1 
HETATM 6741 O O    . HOH   E 4 .   ? 16.275 16.708  8.712   1.00 30.88 ?  534 HOH   A O    1 
HETATM 6742 O O    . HOH   E 4 .   ? 10.392 -13.716 -1.620  1.00 18.00 ?  535 HOH   A O    1 
HETATM 6743 O O    . HOH   E 4 .   ? 32.564 -10.637 3.194   1.00 32.13 ?  536 HOH   A O    1 
HETATM 6744 O O    B HOH   E 4 .   ? 11.867 -1.745  -3.027  0.40 15.50 ?  537 HOH   A O    1 
HETATM 6745 O O    . HOH   E 4 .   ? 35.073 -5.226  -3.092  1.00 18.46 ?  538 HOH   A O    1 
HETATM 6746 O O    . HOH   E 4 .   ? 11.733 -10.792 17.180  1.00 26.63 ?  539 HOH   A O    1 
HETATM 6747 O O    A HOH   E 4 .   ? 16.297 2.945   -1.391  0.60 15.64 ?  540 HOH   A O    1 
HETATM 6748 O O    B HOH   E 4 .   ? 23.333 6.457   -1.990  0.40 19.35 ?  541 HOH   A O    1 
HETATM 6749 O O    A HOH   E 4 .   ? 11.110 -0.385  1.986   0.60 24.13 ?  542 HOH   A O    1 
HETATM 6750 O O    . HOH   E 4 .   ? 9.484  -16.248 -1.840  1.00 34.32 ?  543 HOH   A O    1 
HETATM 6751 O O    A HOH   E 4 .   ? 16.065 6.946   3.046   0.60 13.53 ?  544 HOH   A O    1 
HETATM 6752 O O    A HOH   E 4 .   ? 18.403 -16.088 16.448  0.60 29.51 ?  545 HOH   A O    1 
HETATM 6753 O O    B HOH   E 4 .   ? 24.077 3.689   -4.724  0.40 26.80 ?  546 HOH   A O    1 
HETATM 6754 O O    A HOH   E 4 .   ? 18.903 2.029   -0.707  0.60 11.63 ?  547 HOH   A O    1 
HETATM 6755 O O    B HOH   E 4 .   ? 25.147 6.402   -6.905  0.40 23.63 ?  548 HOH   A O    1 
HETATM 6756 O O    B HOH   E 4 .   ? 16.305 7.787   9.375   0.40 27.15 ?  549 HOH   A O    1 
HETATM 6757 O O    . HOH   E 4 .   ? 23.646 -8.089  17.071  1.00 22.35 ?  550 HOH   A O    1 
HETATM 6758 O O    . HOH   E 4 .   ? 23.368 -20.966 1.295   1.00 19.17 ?  551 HOH   A O    1 
HETATM 6759 O O    . HOH   E 4 .   ? 21.609 -14.724 17.983  1.00 51.78 ?  552 HOH   A O    1 
HETATM 6760 O O    A HOH   E 4 .   ? 23.238 7.510   -3.190  0.60 24.41 ?  553 HOH   A O    1 
HETATM 6761 O O    . HOH   E 4 .   ? 30.644 14.775  2.842   1.00 19.66 ?  554 HOH   A O    1 
HETATM 6762 O O    . HOH   E 4 .   ? 34.434 -8.110  -0.559  1.00 27.88 ?  555 HOH   A O    1 
HETATM 6763 O O    . HOH   E 4 .   ? 37.729 -8.832  -3.471  1.00 26.10 ?  556 HOH   A O    1 
HETATM 6764 O O    . HOH   E 4 .   ? 20.653 -17.821 24.842  1.00 47.00 ?  557 HOH   A O    1 
HETATM 6765 O O    . HOH   E 4 .   ? 31.360 -12.782 -0.011  1.00 19.75 ?  558 HOH   A O    1 
HETATM 6766 O O    . HOH   E 4 .   ? 29.879 -16.066 10.608  1.00 38.38 ?  559 HOH   A O    1 
HETATM 6767 O O    A HOH   E 4 .   ? 14.073 -0.347  3.510   0.60 20.65 ?  560 HOH   A O    1 
HETATM 6768 O O    A HOH   E 4 .   ? 19.385 -11.081 24.176  0.60 48.84 ?  561 HOH   A O    1 
HETATM 6769 O O    B HOH   E 4 .   ? 16.786 10.894  6.945   0.40 27.55 ?  562 HOH   A O    1 
HETATM 6770 O O    B HOH   E 4 .   ? 24.192 7.402   -4.593  0.40 26.95 ?  563 HOH   A O    1 
HETATM 6771 O O    A HOH   E 4 .   ? 25.452 8.202   -4.768  0.60 19.68 ?  564 HOH   A O    1 
HETATM 6772 O O    B HOH   E 4 .   ? 7.601  1.915   7.346   0.40 31.66 ?  565 HOH   A O    1 
HETATM 6773 O O    . HOH   E 4 .   ? 27.825 7.020   -6.495  1.00 41.51 ?  566 HOH   A O    1 
HETATM 6774 O O    . HOH   E 4 .   ? 32.487 -15.979 10.826  1.00 36.52 ?  567 HOH   A O    1 
HETATM 6775 O O    . HOH   E 4 .   ? 29.906 -1.931  -12.705 1.00 42.97 ?  568 HOH   A O    1 
HETATM 6776 O O    . HOH   E 4 .   ? 19.886 -17.350 -5.062  1.00 24.52 ?  569 HOH   A O    1 
HETATM 6777 O O    . HOH   E 4 .   ? 21.831 -8.900  21.329  1.00 58.65 ?  570 HOH   A O    1 
HETATM 6778 O O    . HOH   E 4 .   ? 24.892 5.715   20.797  1.00 49.63 ?  571 HOH   A O    1 
HETATM 6779 O O    . HOH   E 4 .   ? 23.247 -22.369 -3.344  1.00 35.14 ?  572 HOH   A O    1 
HETATM 6780 O O    . HOH   E 4 .   ? 24.670 14.601  7.863   1.00 37.84 ?  573 HOH   A O    1 
HETATM 6781 O O    . HOH   E 4 .   ? 26.961 11.656  -1.343  1.00 32.35 ?  574 HOH   A O    1 
HETATM 6782 O O    . HOH   E 4 .   ? 15.728 -21.505 3.671   1.00 24.23 ?  575 HOH   A O    1 
HETATM 6783 O O    . HOH   E 4 .   ? 23.543 13.734  5.564   1.00 19.35 ?  576 HOH   A O    1 
HETATM 6784 O O    A HOH   E 4 .   ? 21.998 5.269   -5.792  0.60 23.96 ?  577 HOH   A O    1 
HETATM 6785 O O    . HOH   E 4 .   ? 27.576 -11.415 16.504  1.00 36.45 ?  578 HOH   A O    1 
HETATM 6786 O O    . HOH   E 4 .   ? 39.657 -7.046  -3.577  1.00 47.73 ?  579 HOH   A O    1 
HETATM 6787 O O    . HOH   E 4 .   ? 18.774 10.786  11.351  1.00 32.19 ?  580 HOH   A O    1 
HETATM 6788 O O    . HOH   E 4 .   ? 12.371 1.566   17.408  1.00 44.15 ?  581 HOH   A O    1 
HETATM 6789 O O    A HOH   E 4 .   ? 25.867 10.800  -3.748  0.60 21.87 ?  582 HOH   A O    1 
HETATM 6790 O O    . HOH   E 4 .   ? 11.021 -14.915 -6.117  1.00 34.16 ?  583 HOH   A O    1 
HETATM 6791 O O    . HOH   E 4 .   ? 28.646 -7.892  -15.265 1.00 48.02 ?  584 HOH   A O    1 
HETATM 6792 O O    . HOH   E 4 .   ? 23.129 11.782  -4.021  1.00 19.99 ?  585 HOH   A O    1 
HETATM 6793 O O    . HOH   E 4 .   ? 35.258 7.383   12.236  1.00 48.80 ?  586 HOH   A O    1 
HETATM 6794 O O    B HOH   E 4 .   ? 25.111 10.350  -4.181  0.40 35.30 ?  587 HOH   A O    1 
HETATM 6795 O O    . HOH   E 4 .   ? 28.945 8.929   17.574  1.00 38.87 ?  588 HOH   A O    1 
HETATM 6796 O O    . HOH   E 4 .   ? 16.779 -20.617 16.208  1.00 28.59 ?  589 HOH   A O    1 
HETATM 6797 O O    . HOH   E 4 .   ? 17.395 -18.766 19.830  1.00 47.11 ?  590 HOH   A O    1 
HETATM 6798 O O    B HOH   E 4 .   ? 10.798 -1.581  -5.657  0.40 19.39 ?  591 HOH   A O    1 
HETATM 6799 O O    B HOH   E 4 .   ? 14.622 11.151  8.884   0.40 35.58 ?  592 HOH   A O    1 
HETATM 6800 O O    . HOH   E 4 .   ? 30.850 0.743   19.199  1.00 39.87 ?  593 HOH   A O    1 
HETATM 6801 O O    . HOH   E 4 .   ? 13.999 -10.314 -10.824 1.00 33.19 ?  594 HOH   A O    1 
HETATM 6802 O O    . HOH   E 4 .   ? 12.142 -13.164 16.908  1.00 48.84 ?  595 HOH   A O    1 
HETATM 6803 O O    . HOH   E 4 .   ? 18.057 -16.231 -8.748  1.00 39.47 ?  596 HOH   A O    1 
HETATM 6804 O O    . HOH   E 4 .   ? 40.983 -3.984  -0.379  1.00 38.54 ?  597 HOH   A O    1 
HETATM 6805 O O    . HOH   E 4 .   ? 23.269 -12.903 19.352  1.00 48.40 ?  598 HOH   A O    1 
HETATM 6806 O O    . HOH   E 4 .   ? 15.722 -17.124 -6.940  1.00 31.05 ?  599 HOH   A O    1 
HETATM 6807 O O    . HOH   E 4 .   ? 31.444 -0.539  -10.598 1.00 28.67 ?  600 HOH   A O    1 
HETATM 6808 O O    . HOH   E 4 .   ? 44.588 10.446  -1.616  1.00 32.44 ?  601 HOH   A O    1 
HETATM 6809 O O    . HOH   E 4 .   ? 41.791 9.348   -4.036  1.00 32.34 ?  602 HOH   A O    1 
HETATM 6810 O O    . HOH   E 4 .   ? 28.614 -4.620  -12.300 1.00 36.78 ?  603 HOH   A O    1 
HETATM 6811 O O    . HOH   E 4 .   ? 15.942 -6.703  -11.791 1.00 38.87 ?  604 HOH   A O    1 
HETATM 6812 O O    B HOH   E 4 .   ? 10.695 5.323   10.965  0.40 38.06 ?  605 HOH   A O    1 
HETATM 6813 O O    B HOH   E 4 .   ? 23.400 7.378   -8.577  0.40 23.26 ?  606 HOH   A O    1 
HETATM 6814 O O    . HOH   E 4 .   ? 18.463 -23.185 1.822   1.00 41.81 ?  607 HOH   A O    1 
HETATM 6815 O O    . HOH   E 4 .   ? 16.189 -23.393 5.780   1.00 30.51 ?  608 HOH   A O    1 
HETATM 6816 O O    . HOH   E 4 .   ? 40.507 -0.239  -7.835  1.00 34.50 ?  609 HOH   A O    1 
HETATM 6817 O O    . HOH   E 4 .   ? 14.056 -25.331 8.889   1.00 30.78 ?  610 HOH   A O    1 
HETATM 6818 O O    B HOH   E 4 .   ? 21.574 4.945   -4.972  0.40 22.63 ?  611 HOH   A O    1 
HETATM 6819 O O    . HOH   E 4 .   ? 39.222 2.363   7.570   1.00 32.21 ?  612 HOH   A O    1 
HETATM 6820 O O    . HOH   E 4 .   ? 20.047 -22.376 4.163   1.00 31.48 ?  613 HOH   A O    1 
HETATM 6821 O O    . HOH   E 4 .   ? 30.878 5.780   -14.724 1.00 35.79 ?  614 HOH   A O    1 
HETATM 6822 O O    . HOH   E 4 .   ? 30.794 -5.775  -11.829 1.00 47.93 ?  615 HOH   A O    1 
HETATM 6823 O O    . HOH   E 4 .   ? 23.173 -23.792 1.684   1.00 31.07 ?  616 HOH   A O    1 
HETATM 6824 O O    . HOH   E 4 .   ? 37.437 -6.680  7.517   1.00 24.21 ?  617 HOH   A O    1 
HETATM 6825 O O    . HOH   E 4 .   ? 39.572 0.000   6.561   1.00 32.30 ?  618 HOH   A O    1 
HETATM 6826 O O    . HOH   E 4 .   ? 29.083 14.401  0.876   1.00 49.83 ?  619 HOH   A O    1 
HETATM 6827 O O    . HOH   E 4 .   ? 38.100 13.945  6.719   1.00 44.66 ?  620 HOH   A O    1 
HETATM 6828 O O    . HOH   E 4 .   ? 8.164  -3.088  -5.664  1.00 43.82 ?  621 HOH   A O    1 
HETATM 6829 O O    B HOH   E 4 .   ? 10.863 8.374   7.896   0.40 34.96 ?  622 HOH   A O    1 
HETATM 6830 O O    B HOH   E 4 .   ? 10.640 1.476   14.351  0.40 33.47 ?  623 HOH   A O    1 
HETATM 6831 O O    . HOH   E 4 .   ? 20.503 -16.133 -7.366  1.00 29.25 ?  624 HOH   A O    1 
HETATM 6832 O O    . HOH   E 4 .   ? 22.047 -24.073 4.466   1.00 27.87 ?  625 HOH   A O    1 
HETATM 6833 O O    . HOH   E 4 .   ? 36.499 -6.514  10.174  1.00 45.69 ?  626 HOH   A O    1 
HETATM 6834 O O    . HOH   E 4 .   ? 17.303 -6.790  -13.832 1.00 37.59 ?  627 HOH   A O    1 
HETATM 6835 O O    . HOH   E 4 .   ? 15.954 -12.284 27.421  1.00 44.16 ?  628 HOH   A O    1 
HETATM 6836 O O    A HOH   E 4 .   ? 14.902 8.640   4.949   0.60 28.55 ?  629 HOH   A O    1 
HETATM 6837 O O    . HOH   E 4 .   ? 24.082 8.981   -7.190  1.00 40.44 ?  630 HOH   A O    1 
HETATM 6838 O O    . HOH   E 4 .   ? 16.377 -21.154 18.773  1.00 37.95 ?  631 HOH   A O    1 
HETATM 6839 O O    . HOH   E 4 .   ? 14.663 -22.868 19.853  1.00 36.08 ?  632 HOH   A O    1 
HETATM 6840 O O    . HOH   F 4 .   ? 29.856 -22.457 5.438   1.00 21.98 ?  201 HOH   B O    1 
HETATM 6841 O O    . HOH   F 4 .   ? 41.817 -36.017 -17.237 1.00 32.49 ?  202 HOH   B O    1 
HETATM 6842 O O    . HOH   F 4 .   ? 52.910 -13.438 -20.413 1.00 38.42 ?  203 HOH   B O    1 
HETATM 6843 O O    . HOH   F 4 .   ? 48.173 -6.902  15.551  1.00 38.97 ?  204 HOH   B O    1 
HETATM 6844 O O    . HOH   F 4 .   ? 59.218 -18.718 6.775   1.00 37.87 ?  205 HOH   B O    1 
HETATM 6845 O O    . HOH   F 4 .   ? 27.861 -41.825 -15.152 1.00 36.97 ?  206 HOH   B O    1 
HETATM 6846 O O    . HOH   F 4 .   ? 49.420 -22.712 -19.760 1.00 47.63 ?  207 HOH   B O    1 
HETATM 6847 O O    . HOH   F 4 .   ? 37.971 -39.495 -0.229  1.00 42.63 ?  208 HOH   B O    1 
HETATM 6848 O O    . HOH   F 4 .   ? 41.412 -7.767  5.494   1.00 37.17 ?  209 HOH   B O    1 
HETATM 6849 O O    . HOH   F 4 .   ? 27.739 -29.243 -1.878  1.00 39.14 ?  210 HOH   B O    1 
HETATM 6850 O O    . HOH   F 4 .   ? 47.439 -7.438  -3.953  1.00 41.72 ?  211 HOH   B O    1 
HETATM 6851 O O    . HOH   F 4 .   ? 56.384 -19.715 7.292   1.00 33.43 ?  212 HOH   B O    1 
HETATM 6852 O O    . HOH   F 4 .   ? 29.940 -26.328 3.983   1.00 28.70 ?  213 HOH   B O    1 
HETATM 6853 O O    . HOH   F 4 .   ? 50.289 -3.363  7.184   1.00 38.95 ?  214 HOH   B O    1 
HETATM 6854 O O    . HOH   F 4 .   ? 54.502 -9.371  -8.783  1.00 19.14 ?  215 HOH   B O    1 
HETATM 6855 O O    . HOH   F 4 .   ? 30.253 -41.083 -8.153  1.00 17.03 ?  216 HOH   B O    1 
HETATM 6856 O O    . HOH   F 4 .   ? 26.502 -19.351 -1.799  1.00 14.74 ?  217 HOH   B O    1 
HETATM 6857 O O    . HOH   F 4 .   ? 45.159 -34.955 6.846   1.00 42.15 ?  218 HOH   B O    1 
HETATM 6858 O O    . HOH   F 4 .   ? 58.256 -12.891 8.374   1.00 36.13 ?  219 HOH   B O    1 
HETATM 6859 O O    . HOH   F 4 .   ? 57.813 -24.463 5.021   1.00 38.45 ?  220 HOH   B O    1 
HETATM 6860 O O    . HOH   F 4 .   ? 29.825 -34.229 -0.450  1.00 36.42 ?  221 HOH   B O    1 
HETATM 6861 O O    . HOH   F 4 .   ? 44.487 -7.266  2.087   1.00 34.72 ?  222 HOH   B O    1 
HETATM 6862 O O    . HOH   F 4 .   ? 50.721 -6.121  0.233   1.00 27.48 ?  223 HOH   B O    1 
HETATM 6863 O O    . HOH   F 4 .   ? 35.995 -43.296 -8.548  1.00 31.43 ?  224 HOH   B O    1 
HETATM 6864 O O    . HOH   F 4 .   ? 57.433 -16.273 -12.231 1.00 19.50 ?  225 HOH   B O    1 
HETATM 6865 O O    . HOH   F 4 .   ? 34.581 -36.423 -7.247  1.00 18.36 ?  226 HOH   B O    1 
HETATM 6866 O O    . HOH   F 4 .   ? 56.750 -30.808 -7.776  1.00 30.50 ?  227 HOH   B O    1 
HETATM 6867 O O    . HOH   F 4 .   ? 55.412 -16.500 -14.315 1.00 33.71 ?  228 HOH   B O    1 
HETATM 6868 O O    . HOH   F 4 .   ? 37.135 -19.780 -18.155 1.00 41.41 ?  229 HOH   B O    1 
HETATM 6869 O O    . HOH   F 4 .   ? 40.692 -16.048 14.117  1.00 25.26 ?  230 HOH   B O    1 
HETATM 6870 O O    . HOH   F 4 .   ? 41.392 -9.672  13.041  1.00 23.30 ?  231 HOH   B O    1 
HETATM 6871 O O    . HOH   F 4 .   ? 39.357 -10.886 6.085   1.00 26.86 ?  232 HOH   B O    1 
HETATM 6872 O O    . HOH   F 4 .   ? 41.532 -39.227 -14.940 1.00 22.72 ?  233 HOH   B O    1 
HETATM 6873 O O    . HOH   F 4 .   ? 57.272 -26.887 -7.696  1.00 40.73 ?  234 HOH   B O    1 
HETATM 6874 O O    . HOH   F 4 .   ? 30.891 -28.814 4.255   1.00 27.34 ?  235 HOH   B O    1 
HETATM 6875 O O    . HOH   F 4 .   ? 50.766 -12.984 -0.499  1.00 12.57 ?  236 HOH   B O    1 
HETATM 6876 O O    . HOH   F 4 .   ? 35.136 -8.016  -3.086  1.00 19.03 ?  237 HOH   B O    1 
HETATM 6877 O O    . HOH   F 4 .   ? 32.862 -43.841 -11.359 1.00 20.37 ?  238 HOH   B O    1 
HETATM 6878 O O    . HOH   F 4 .   ? 51.720 -6.502  4.408   1.00 20.40 ?  239 HOH   B O    1 
HETATM 6879 O O    . HOH   F 4 .   ? 28.422 -19.717 -13.139 1.00 24.67 ?  240 HOH   B O    1 
HETATM 6880 O O    . HOH   F 4 .   ? 25.438 -25.974 -1.400  1.00 33.90 ?  241 HOH   B O    1 
HETATM 6881 O O    . HOH   F 4 .   ? 48.562 -36.514 -15.574 1.00 44.03 ?  242 HOH   B O    1 
HETATM 6882 O O    . HOH   F 4 .   ? 39.527 -11.152 0.298   1.00 17.50 ?  243 HOH   B O    1 
HETATM 6883 O O    . HOH   F 4 .   ? 45.001 -43.593 -10.523 1.00 28.58 ?  244 HOH   B O    1 
HETATM 6884 O O    . HOH   F 4 .   ? 44.564 -27.752 -0.733  1.00 23.13 ?  245 HOH   B O    1 
HETATM 6885 O O    . HOH   F 4 .   ? 43.224 -32.416 -17.103 1.00 24.45 ?  246 HOH   B O    1 
HETATM 6886 O O    . HOH   F 4 .   ? 42.670 -22.909 3.820   1.00 12.23 ?  247 HOH   B O    1 
HETATM 6887 O O    . HOH   F 4 .   ? 42.615 -25.400 2.605   1.00 15.90 ?  248 HOH   B O    1 
HETATM 6888 O O    . HOH   F 4 .   ? 48.110 -24.524 -17.797 1.00 30.86 ?  249 HOH   B O    1 
HETATM 6889 O O    . HOH   F 4 .   ? 40.372 -12.786 -11.551 1.00 15.72 ?  250 HOH   B O    1 
HETATM 6890 O O    . HOH   F 4 .   ? 51.580 -13.904 10.982  1.00 29.12 ?  251 HOH   B O    1 
HETATM 6891 O O    . HOH   F 4 .   ? 46.422 -1.581  13.300  1.00 27.64 ?  252 HOH   B O    1 
HETATM 6892 O O    . HOH   F 4 .   ? 41.907 -23.538 9.269   1.00 17.13 ?  253 HOH   B O    1 
HETATM 6893 O O    . HOH   F 4 .   ? 34.879 -24.649 13.852  1.00 30.92 ?  254 HOH   B O    1 
HETATM 6894 O O    . HOH   F 4 .   ? 34.242 -18.608 11.395  1.00 24.09 ?  255 HOH   B O    1 
HETATM 6895 O O    . HOH   F 4 .   ? 38.952 -12.009 12.303  1.00 35.55 ?  256 HOH   B O    1 
HETATM 6896 O O    . HOH   F 4 .   ? 58.212 -10.630 -4.065  1.00 22.60 ?  257 HOH   B O    1 
HETATM 6897 O O    . HOH   F 4 .   ? 57.669 -24.418 -3.868  1.00 21.95 ?  258 HOH   B O    1 
HETATM 6898 O O    . HOH   F 4 .   ? 43.128 -43.300 -8.298  1.00 29.86 ?  259 HOH   B O    1 
HETATM 6899 O O    . HOH   F 4 .   ? 29.742 -25.251 -10.851 1.00 17.04 ?  260 HOH   B O    1 
HETATM 6900 O O    . HOH   F 4 .   ? 48.025 -22.788 5.807   1.00 18.00 ?  261 HOH   B O    1 
HETATM 6901 O O    . HOH   F 4 .   ? 30.889 -15.747 2.621   1.00 14.10 ?  262 HOH   B O    1 
HETATM 6902 O O    . HOH   F 4 .   ? 38.485 -11.072 -2.251  1.00 19.59 ?  263 HOH   B O    1 
HETATM 6903 O O    . HOH   F 4 .   ? 31.817 -17.944 -14.556 1.00 31.93 ?  264 HOH   B O    1 
HETATM 6904 O O    . HOH   F 4 .   ? 51.023 -40.022 -8.290  1.00 32.05 ?  265 HOH   B O    1 
HETATM 6905 O O    . HOH   F 4 .   ? 43.390 -15.798 -12.188 1.00 14.77 ?  266 HOH   B O    1 
HETATM 6906 O O    . HOH   F 4 .   ? 49.379 -28.730 -6.939  1.00 16.31 ?  267 HOH   B O    1 
HETATM 6907 O O    . HOH   F 4 .   ? 30.691 -42.291 -10.639 1.00 29.28 ?  268 HOH   B O    1 
HETATM 6908 O O    . HOH   F 4 .   ? 27.166 -31.876 -10.007 1.00 20.91 ?  269 HOH   B O    1 
HETATM 6909 O O    . HOH   F 4 .   ? 42.357 -9.898  9.374   1.00 21.64 ?  270 HOH   B O    1 
HETATM 6910 O O    . HOH   F 4 .   ? 57.516 -9.228  1.413   1.00 20.42 ?  271 HOH   B O    1 
HETATM 6911 O O    . HOH   F 4 .   ? 28.503 -30.836 -14.766 1.00 30.34 ?  272 HOH   B O    1 
HETATM 6912 O O    . HOH   F 4 .   ? 49.770 -0.477  10.257  1.00 31.99 ?  273 HOH   B O    1 
HETATM 6913 O O    . HOH   F 4 .   ? 57.239 -12.090 12.278  1.00 39.41 ?  274 HOH   B O    1 
HETATM 6914 O O    . HOH   F 4 .   ? 28.298 -34.401 -9.466  1.00 20.44 ?  275 HOH   B O    1 
HETATM 6915 O O    . HOH   F 4 .   ? 56.225 -23.514 -14.803 1.00 27.29 ?  276 HOH   B O    1 
HETATM 6916 O O    . HOH   F 4 .   ? 56.985 -8.653  8.428   1.00 20.25 ?  277 HOH   B O    1 
HETATM 6917 O O    . HOH   F 4 .   ? 46.650 -31.292 -4.820  1.00 21.52 ?  278 HOH   B O    1 
HETATM 6918 O O    . HOH   F 4 .   ? 33.569 -15.330 -14.013 1.00 21.81 ?  279 HOH   B O    1 
HETATM 6919 O O    . HOH   F 4 .   ? 34.969 -33.438 -19.234 1.00 30.61 ?  280 HOH   B O    1 
HETATM 6920 O O    . HOH   F 4 .   ? 62.804 -20.252 -0.898  1.00 38.33 ?  281 HOH   B O    1 
HETATM 6921 O O    . HOH   F 4 .   ? 48.452 -25.084 3.081   1.00 13.56 ?  282 HOH   B O    1 
HETATM 6922 O O    . HOH   F 4 .   ? 27.965 -22.919 -8.038  1.00 17.79 ?  283 HOH   B O    1 
HETATM 6923 O O    . HOH   F 4 .   ? 34.478 -12.761 2.593   1.00 26.93 ?  284 HOH   B O    1 
HETATM 6924 O O    . HOH   F 4 .   ? 52.547 -10.423 12.994  1.00 22.70 ?  285 HOH   B O    1 
HETATM 6925 O O    . HOH   F 4 .   ? 48.762 -20.057 5.917   1.00 14.50 ?  286 HOH   B O    1 
HETATM 6926 O O    . HOH   F 4 .   ? 47.125 -34.044 -4.654  1.00 17.75 ?  287 HOH   B O    1 
HETATM 6927 O O    . HOH   F 4 .   ? 46.900 -29.610 9.851   1.00 31.91 ?  288 HOH   B O    1 
HETATM 6928 O O    . HOH   F 4 .   ? 51.287 -37.651 -9.576  1.00 26.01 ?  289 HOH   B O    1 
HETATM 6929 O O    . HOH   F 4 .   ? 36.815 -12.780 -1.512  1.00 28.27 ?  290 HOH   B O    1 
HETATM 6930 O O    . HOH   F 4 .   ? 37.397 -35.694 7.203   1.00 33.72 ?  291 HOH   B O    1 
HETATM 6931 O O    . HOH   F 4 .   ? 42.707 -12.307 -18.537 1.00 29.68 ?  292 HOH   B O    1 
HETATM 6932 O O    . HOH   F 4 .   ? 42.467 -34.751 3.749   1.00 26.19 ?  293 HOH   B O    1 
HETATM 6933 O O    . HOH   F 4 .   ? 45.973 -40.449 -3.664  1.00 31.88 ?  294 HOH   B O    1 
HETATM 6934 O O    . HOH   F 4 .   ? 41.236 -5.453  11.510  1.00 43.62 ?  295 HOH   B O    1 
HETATM 6935 O O    . HOH   F 4 .   ? 49.980 -24.704 5.786   1.00 35.51 ?  296 HOH   B O    1 
HETATM 6936 O O    . HOH   F 4 .   ? 45.386 -33.436 -15.975 1.00 24.16 ?  297 HOH   B O    1 
HETATM 6937 O O    . HOH   F 4 .   ? 27.575 -26.787 -15.719 1.00 33.76 ?  298 HOH   B O    1 
HETATM 6938 O O    . HOH   F 4 .   ? 42.926 -20.309 -20.778 1.00 36.13 ?  299 HOH   B O    1 
HETATM 6939 O O    . HOH   F 4 .   ? 35.133 -33.590 4.513   1.00 29.58 ?  300 HOH   B O    1 
HETATM 6940 O O    . HOH   F 4 .   ? 44.662 -27.497 1.966   1.00 16.05 ?  301 HOH   B O    1 
HETATM 6941 O O    . HOH   F 4 .   ? 42.308 -9.994  -14.969 1.00 34.97 ?  302 HOH   B O    1 
HETATM 6942 O O    . HOH   F 4 .   ? 51.660 -5.998  -7.992  1.00 46.88 ?  303 HOH   B O    1 
HETATM 6943 O O    . HOH   F 4 .   ? 40.280 -10.856 -9.562  1.00 17.23 ?  304 HOH   B O    1 
HETATM 6944 O O    . HOH   F 4 .   ? 25.982 -21.502 -3.542  1.00 17.08 ?  305 HOH   B O    1 
HETATM 6945 O O    . HOH   F 4 .   ? 52.667 -35.695 -8.598  1.00 29.07 ?  306 HOH   B O    1 
HETATM 6946 O O    . HOH   F 4 .   ? 37.545 -18.186 13.116  1.00 32.01 ?  307 HOH   B O    1 
HETATM 6947 O O    . HOH   F 4 .   ? 59.806 -15.347 8.185   1.00 35.09 ?  308 HOH   B O    1 
HETATM 6948 O O    . HOH   F 4 .   ? 44.117 -29.372 -4.670  1.00 23.90 ?  309 HOH   B O    1 
HETATM 6949 O O    . HOH   F 4 .   ? 37.855 -10.266 -10.782 1.00 17.72 ?  310 HOH   B O    1 
HETATM 6950 O O    . HOH   F 4 .   ? 41.749 -8.112  1.333   1.00 25.19 ?  311 HOH   B O    1 
HETATM 6951 O O    . HOH   F 4 .   ? 53.494 -30.252 4.515   1.00 19.76 ?  312 HOH   B O    1 
HETATM 6952 O O    . HOH   F 4 .   ? 32.841 -34.629 -5.938  1.00 17.25 ?  313 HOH   B O    1 
HETATM 6953 O O    . HOH   F 4 .   ? 62.754 -13.582 4.730   1.00 28.56 ?  314 HOH   B O    1 
HETATM 6954 O O    . HOH   F 4 .   ? 53.071 -16.008 -12.784 1.00 29.15 ?  315 HOH   B O    1 
HETATM 6955 O O    . HOH   F 4 .   ? 43.234 -21.464 10.646  1.00 16.48 ?  316 HOH   B O    1 
HETATM 6956 O O    . HOH   F 4 .   ? 48.627 -12.046 -14.240 1.00 27.80 ?  317 HOH   B O    1 
HETATM 6957 O O    . HOH   F 4 .   ? 52.603 -29.255 -13.081 1.00 25.46 ?  318 HOH   B O    1 
HETATM 6958 O O    . HOH   F 4 .   ? 38.388 -12.804 7.897   1.00 19.21 ?  319 HOH   B O    1 
HETATM 6959 O O    . HOH   F 4 .   ? 26.357 -21.044 -6.268  1.00 17.28 ?  320 HOH   B O    1 
HETATM 6960 O O    . HOH   F 4 .   ? 41.314 -24.621 15.800  1.00 43.24 ?  321 HOH   B O    1 
HETATM 6961 O O    . HOH   F 4 .   ? 38.364 -9.369  -13.289 1.00 30.65 ?  322 HOH   B O    1 
HETATM 6962 O O    . HOH   F 4 .   ? 48.155 -32.610 -16.686 1.00 43.79 ?  323 HOH   B O    1 
HETATM 6963 O O    . HOH   F 4 .   ? 51.461 -33.014 -10.850 1.00 42.22 ?  324 HOH   B O    1 
HETATM 6964 O O    . HOH   F 4 .   ? 43.561 -15.446 18.225  1.00 33.59 ?  325 HOH   B O    1 
HETATM 6965 O O    . HOH   F 4 .   ? 44.643 -24.652 9.543   1.00 20.56 ?  326 HOH   B O    1 
HETATM 6966 O O    . HOH   F 4 .   ? 37.164 -30.636 -21.103 1.00 32.41 ?  327 HOH   B O    1 
HETATM 6967 O O    . HOH   F 4 .   ? 53.701 -12.540 -22.315 1.00 36.36 ?  328 HOH   B O    1 
HETATM 6968 O O    . HOH   F 4 .   ? 60.009 -17.203 -10.527 1.00 35.31 ?  329 HOH   B O    1 
HETATM 6969 O O    . HOH   F 4 .   ? 36.752 -12.443 4.265   1.00 19.00 ?  330 HOH   B O    1 
HETATM 6970 O O    . HOH   F 4 .   ? 27.992 -14.799 -9.450  1.00 35.14 ?  331 HOH   B O    1 
HETATM 6971 O O    . HOH   F 4 .   ? 47.213 -24.510 8.151   1.00 27.09 ?  332 HOH   B O    1 
HETATM 6972 O O    . HOH   F 4 .   ? 57.646 -21.980 3.280   1.00 29.69 ?  333 HOH   B O    1 
HETATM 6973 O O    . HOH   F 4 .   ? 42.921 -43.526 -14.409 1.00 43.62 ?  334 HOH   B O    1 
HETATM 6974 O O    . HOH   F 4 .   ? 33.718 -31.235 11.069  1.00 36.42 ?  335 HOH   B O    1 
HETATM 6975 O O    . HOH   F 4 .   ? 46.918 -19.860 12.214  1.00 30.59 ?  336 HOH   B O    1 
HETATM 6976 O O    . HOH   F 4 .   ? 45.762 -36.325 -16.157 1.00 36.57 ?  337 HOH   B O    1 
HETATM 6977 O O    . HOH   F 4 .   ? 43.148 -34.729 0.081   1.00 21.25 ?  338 HOH   B O    1 
HETATM 6978 O O    . HOH   F 4 .   ? 38.372 -12.251 -16.226 1.00 41.53 ?  339 HOH   B O    1 
HETATM 6979 O O    . HOH   F 4 .   ? 44.222 -1.699  7.536   1.00 45.73 ?  340 HOH   B O    1 
HETATM 6980 O O    . HOH   F 4 .   ? 47.513 -27.475 1.998   1.00 15.32 ?  341 HOH   B O    1 
HETATM 6981 O O    . HOH   F 4 .   ? 39.483 -23.595 -20.339 1.00 37.30 ?  342 HOH   B O    1 
HETATM 6982 O O    . HOH   F 4 .   ? 37.098 -45.260 -9.817  1.00 39.95 ?  343 HOH   B O    1 
HETATM 6983 O O    . HOH   F 4 .   ? 37.060 -15.021 -16.499 1.00 39.14 ?  344 HOH   B O    1 
HETATM 6984 O O    . HOH   F 4 .   ? 28.921 -42.995 -12.373 1.00 40.84 ?  345 HOH   B O    1 
HETATM 6985 O O    . HOH   F 4 .   ? 33.019 -14.703 0.989   1.00 20.22 ?  346 HOH   B O    1 
HETATM 6986 O O    . HOH   F 4 .   ? 39.824 -44.332 -11.228 1.00 36.64 ?  347 HOH   B O    1 
HETATM 6987 O O    . HOH   F 4 .   ? 33.770 -9.427  -8.843  1.00 33.58 ?  348 HOH   B O    1 
HETATM 6988 O O    . HOH   F 4 .   ? 40.452 -43.528 -9.148  1.00 27.73 ?  349 HOH   B O    1 
HETATM 6989 O O    . HOH   F 4 .   ? 27.832 -26.605 -0.572  1.00 30.83 ?  350 HOH   B O    1 
HETATM 6990 O O    . HOH   F 4 .   ? 38.603 -22.330 15.090  1.00 43.67 ?  351 HOH   B O    1 
HETATM 6991 O O    . HOH   F 4 .   ? 44.213 -37.391 -17.771 1.00 35.52 ?  352 HOH   B O    1 
HETATM 6992 O O    . HOH   F 4 .   ? 55.672 -8.271  10.875  1.00 25.60 ?  353 HOH   B O    1 
HETATM 6993 O O    . HOH   F 4 .   ? 23.195 -23.702 6.759   1.00 37.02 ?  354 HOH   B O    1 
HETATM 6994 O O    . HOH   F 4 .   ? 34.704 -10.314 7.451   1.00 24.96 ?  355 HOH   B O    1 
HETATM 6995 O O    . HOH   F 4 .   ? 62.635 -20.125 -4.965  1.00 44.16 ?  356 HOH   B O    1 
HETATM 6996 O O    . HOH   F 4 .   ? 36.142 -8.504  -9.701  1.00 36.46 ?  357 HOH   B O    1 
HETATM 6997 O O    . HOH   F 4 .   ? 56.569 -7.276  3.033   1.00 28.58 ?  358 HOH   B O    1 
HETATM 6998 O O    . HOH   F 4 .   ? 34.185 -7.783  11.389  1.00 42.79 ?  359 HOH   B O    1 
HETATM 6999 O O    . HOH   F 4 .   ? 43.250 -12.642 -21.215 1.00 37.88 ?  360 HOH   B O    1 
HETATM 7000 O O    . HOH   F 4 .   ? 61.580 -19.945 1.609   1.00 35.58 ?  361 HOH   B O    1 
HETATM 7001 O O    . HOH   F 4 .   ? 56.948 -21.611 -16.406 1.00 39.91 ?  362 HOH   B O    1 
HETATM 7002 O O    . HOH   F 4 .   ? 40.240 -8.836  9.933   1.00 38.07 ?  363 HOH   B O    1 
HETATM 7003 O O    . HOH   F 4 .   ? 27.146 -25.992 -11.486 1.00 33.41 ?  364 HOH   B O    1 
HETATM 7004 O O    . HOH   F 4 .   ? 36.230 -8.716  9.045   1.00 38.93 ?  365 HOH   B O    1 
HETATM 7005 O O    . HOH   F 4 .   ? 54.224 -5.748  2.993   1.00 38.31 ?  366 HOH   B O    1 
HETATM 7006 O O    . HOH   F 4 .   ? 32.618 -23.684 14.100  1.00 41.32 ?  367 HOH   B O    1 
HETATM 7007 O O    . HOH   F 4 .   ? 59.002 -10.472 9.181   1.00 36.85 ?  368 HOH   B O    1 
HETATM 7008 O O    . HOH   F 4 .   ? 39.924 -7.081  7.851   1.00 45.86 ?  369 HOH   B O    1 
HETATM 7009 O O    . HOH   F 4 .   ? 48.428 -26.568 8.773   1.00 39.34 ?  370 HOH   B O    1 
HETATM 7010 O O    . HOH   F 4 .   ? 40.119 -11.362 -13.980 1.00 34.21 ?  371 HOH   B O    1 
HETATM 7011 O O    . HOH   F 4 .   ? 56.129 -7.817  -0.567  1.00 36.86 ?  372 HOH   B O    1 
HETATM 7012 O O    . HOH   F 4 .   ? 41.866 -9.985  -17.443 1.00 56.07 ?  373 HOH   B O    1 
HETATM 7013 O O    . HOH   F 4 .   ? 63.103 -12.454 6.923   1.00 39.23 ?  374 HOH   B O    1 
HETATM 7014 O O    . HOH   F 4 .   ? 52.072 -12.938 13.393  1.00 31.90 ?  375 HOH   B O    1 
HETATM 7015 O O    . HOH   F 4 .   ? 38.061 -10.621 10.058  1.00 31.39 ?  376 HOH   B O    1 
HETATM 7016 O O    . HOH   F 4 .   ? 41.863 -6.773  -4.889  1.00 46.64 ?  377 HOH   B O    1 
HETATM 7017 O O    . HOH   F 4 .   ? 36.561 -22.847 13.295  1.00 26.39 ?  378 HOH   B O    1 
HETATM 7018 O O    . HOH   F 4 .   ? 44.162 -5.591  -3.502  1.00 43.49 ?  379 HOH   B O    1 
HETATM 7019 O O    . HOH   F 4 .   ? 40.156 -7.644  3.199   1.00 35.67 ?  380 HOH   B O    1 
HETATM 7020 O O    . HOH   F 4 .   ? 39.758 -14.095 15.698  1.00 51.02 ?  381 HOH   B O    1 
HETATM 7021 O O    . HOH   F 4 .   ? 52.902 -29.899 7.154   1.00 25.07 ?  382 HOH   B O    1 
HETATM 7022 O O    . HOH   F 4 .   ? 42.621 -16.993 -23.265 1.00 42.78 ?  383 HOH   B O    1 
HETATM 7023 O O    . HOH   F 4 .   ? 60.537 -22.355 2.772   1.00 49.89 ?  384 HOH   B O    1 
HETATM 7024 O O    . HOH   F 4 .   ? 46.750 -5.392  2.870   1.00 42.93 ?  385 HOH   B O    1 
HETATM 7025 O O    . HOH   F 4 .   ? 35.415 -33.729 7.234   1.00 42.64 ?  386 HOH   B O    1 
HETATM 7026 O O    . HOH   F 4 .   ? 23.888 -20.815 -7.690  1.00 29.14 ?  387 HOH   B O    1 
HETATM 7027 O O    . HOH   F 4 .   ? 35.357 -20.369 13.293  1.00 30.99 ?  388 HOH   B O    1 
HETATM 7028 O O    . HOH   F 4 .   ? 40.942 -9.864  15.825  1.00 49.35 ?  389 HOH   B O    1 
HETATM 7029 O O    . HOH   F 4 .   ? 25.813 -18.913 -12.012 1.00 37.16 ?  390 HOH   B O    1 
HETATM 7030 O O    . HOH   F 4 .   ? 44.159 -31.755 -3.867  1.00 33.89 ?  391 HOH   B O    1 
HETATM 7031 O O    . HOH   F 4 .   ? 40.743 -6.614  -0.847  1.00 24.55 ?  392 HOH   B O    1 
HETATM 7032 O O    . HOH   F 4 .   ? 27.963 -27.125 2.222   1.00 31.60 ?  393 HOH   B O    1 
HETATM 7033 O O    . HOH   F 4 .   ? 26.635 -28.011 -13.604 1.00 36.77 ?  394 HOH   B O    1 
HETATM 7034 O O    . HOH   F 4 .   ? 24.632 -20.711 -10.453 1.00 40.85 ?  395 HOH   B O    1 
HETATM 7035 O O    . HOH   F 4 .   ? 50.688 -30.817 8.633   1.00 28.61 ?  396 HOH   B O    1 
HETATM 7036 O O    . HOH   F 4 .   ? 34.441 -33.521 9.604   1.00 36.50 ?  397 HOH   B O    1 
HETATM 7037 O O    . HOH   F 4 .   ? 26.882 -30.735 -12.648 1.00 29.45 ?  398 HOH   B O    1 
HETATM 7038 O O    . HOH   F 4 .   ? 45.735 -20.245 15.195  1.00 49.43 ?  399 HOH   B O    1 
HETATM 7039 O O    . HOH   F 4 .   ? 57.644 -6.438  -2.321  1.00 35.35 ?  400 HOH   B O    1 
HETATM 7040 O O    . HOH   F 4 .   ? 40.893 -11.781 -22.367 1.00 43.18 ?  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   ? 0.4758 0.4750 0.5522 0.0296  -0.0119 0.0764  3   VAL   A N   
2    N N   B VAL   A 3   ? 0.5346 0.5108 0.5788 0.0014  0.0130  0.0135  3   VAL   A N   
3    C CA  A VAL   A 3   ? 0.4729 0.4725 0.5423 0.0277  -0.0118 0.0749  3   VAL   A CA  
4    C CA  B VAL   A 3   ? 0.5329 0.5093 0.5705 0.0011  0.0125  0.0131  3   VAL   A CA  
5    C C   A VAL   A 3   ? 0.4541 0.4589 0.4863 0.0199  -0.0177 0.0733  3   VAL   A C   
6    C C   B VAL   A 3   ? 0.5255 0.5019 0.5417 0.0009  0.0094  0.0048  3   VAL   A C   
7    O O   A VAL   A 3   ? 0.4564 0.4603 0.4860 0.0246  -0.0189 0.0761  3   VAL   A O   
8    O O   B VAL   A 3   ? 0.5278 0.5038 0.5468 0.0012  0.0104  0.0036  3   VAL   A O   
9    C CB  A VAL   A 3   ? 0.4860 0.4820 0.5768 0.0310  -0.0050 0.0758  3   VAL   A CB  
10   C CB  B VAL   A 3   ? 0.5372 0.5134 0.5841 0.0009  0.0148  0.0182  3   VAL   A CB  
11   C CG1 A VAL   A 3   ? 0.4907 0.4853 0.5873 0.0322  -0.0027 0.0761  3   VAL   A CG1 
12   C CG1 B VAL   A 3   ? 0.5387 0.5147 0.5876 0.0004  0.0157  0.0197  3   VAL   A CG1 
13   C CG2 A VAL   A 3   ? 0.4901 0.4858 0.5867 0.0320  -0.0026 0.0764  3   VAL   A CG2 
14   C CG2 B VAL   A 3   ? 0.5381 0.5144 0.5884 0.0012  0.0161  0.0196  3   VAL   A CG2 
31   N N   A ASN   A 4   ? 0.4297 0.4412 0.4211 0.0084  -0.0236 0.0682  4   ASN   A N   
32   N N   B ASN   A 4   ? 0.5144 0.4912 0.5042 -0.0001 0.0068  -0.0013 4   ASN   A N   
33   C CA  A ASN   A 4   ? 0.4049 0.4224 0.3529 -0.0047 -0.0265 0.0599  4   ASN   A CA  
34   C CA  B ASN   A 4   ? 0.5022 0.4795 0.4661 -0.0020 0.0047  -0.0068 4   ASN   A CA  
35   C C   A ASN   A 4   ? 0.3773 0.4035 0.3120 -0.0198 -0.0202 0.0363  4   ASN   A C   
36   C C   B ASN   A 4   ? 0.4839 0.4653 0.4528 -0.0092 0.0146  -0.0021 4   ASN   A C   
37   O O   A ASN   A 4   ? 0.3800 0.4000 0.3024 -0.0191 -0.0239 0.0450  4   ASN   A O   
38   O O   B ASN   A 4   ? 0.4848 0.4657 0.4479 -0.0100 0.0160  0.0005  4   ASN   A O   
39   C CB  A ASN   A 4   ? 0.4055 0.4222 0.3222 -0.0033 -0.0350 0.0716  4   ASN   A CB  
40   C CB  B ASN   A 4   ? 0.5067 0.4816 0.4449 0.0020  -0.0064 -0.0173 4   ASN   A CB  
41   C CG  A ASN   A 4   ? 0.4049 0.4191 0.2861 -0.0033 -0.0430 0.0868  4   ASN   A CG  
42   C CG  B ASN   A 4   ? 0.5104 0.4835 0.4249 0.0052  -0.0162 -0.0261 4   ASN   A CG  
43   O OD1 A ASN   A 4   ? 0.4058 0.4158 0.2668 -0.0033 -0.0450 0.0924  4   ASN   A OD1 
44   O OD1 B ASN   A 4   ? 0.5124 0.4845 0.4191 0.0061  -0.0195 -0.0279 4   ASN   A OD1 
45   N ND2 A ASN   A 4   ? 0.4030 0.4182 0.2801 -0.0019 -0.0489 0.0957  4   ASN   A ND2 
46   N ND2 B ASN   A 4   ? 0.5107 0.4828 0.4147 0.0060  -0.0184 -0.0301 4   ASN   A ND2 
59   N N   A SER   A 5   ? 0.3461 0.3829 0.2769 -0.0363 -0.0129 0.0048  5   SER   A N   
60   N N   B SER   A 5   ? 0.4637 0.4502 0.4448 -0.0167 0.0236  -0.0002 5   SER   A N   
61   C CA  A SER   A 5   ? 0.3167 0.3653 0.2494 -0.0474 -0.0048 -0.0264 5   SER   A CA  
62   C CA  B SER   A 5   ? 0.4417 0.4342 0.4361 -0.0253 0.0321  0.0009  5   SER   A CA  
63   C C   A SER   A 5   ? 0.2858 0.3412 0.2188 -0.0486 0.0109  -0.0400 5   SER   A C   
64   C C   B SER   A 5   ? 0.4157 0.4162 0.4051 -0.0347 0.0382  0.0030  5   SER   A C   
65   O O   A SER   A 5   ? 0.2896 0.3468 0.2211 -0.0376 0.0124  -0.0642 5   SER   A O   
66   O O   B SER   A 5   ? 0.4172 0.4147 0.4077 -0.0365 0.0373  0.0035  5   SER   A O   
67   C CB  A SER   A 5   ? 0.3229 0.3722 0.2633 -0.0537 -0.0060 -0.0384 5   SER   A CB  
68   C CB  B SER   A 5   ? 0.4451 0.4357 0.4586 -0.0243 0.0350  -0.0006 5   SER   A CB  
69   O OG  A SER   A 5   ? 0.3293 0.3765 0.2694 -0.0547 0.0016  -0.0377 5   SER   A OG  
70   O OG  B SER   A 5   ? 0.4476 0.4367 0.4728 -0.0231 0.0363  -0.0017 5   SER   A OG  
81   N N   A PHE   A 6   ? 0.2480 0.3063 0.1768 -0.0577 0.0309  -0.0279 6   PHE   A N   
82   N N   B PHE   A 6   ? 0.3890 0.3997 0.3728 -0.0427 0.0452  0.0064  6   PHE   A N   
83   C CA  A PHE   A 6   ? 0.2191 0.2758 0.1479 -0.0620 0.0363  -0.0076 6   PHE   A CA  
84   C CA  B PHE   A 6   ? 0.3621 0.3820 0.3406 -0.0498 0.0505  0.0111  6   PHE   A CA  
85   C C   A PHE   A 6   ? 0.2194 0.2733 0.1652 -0.0723 0.0557  -0.0067 6   PHE   A C   
86   C C   B PHE   A 6   ? 0.3475 0.3678 0.3337 -0.0525 0.0578  0.0009  6   PHE   A C   
87   O O   A PHE   A 6   ? 0.2244 0.2792 0.1904 -0.0785 0.0531  0.0051  6   PHE   A O   
88   O O   B PHE   A 6   ? 0.3474 0.3678 0.3367 -0.0524 0.0601  0.0013  6   PHE   A O   
89   C CB  A PHE   A 6   ? 0.2026 0.2528 0.1389 -0.0500 0.0316  0.0176  6   PHE   A CB  
90   C CB  B PHE   A 6   ? 0.3526 0.3798 0.3190 -0.0537 0.0468  0.0252  6   PHE   A CB  
91   C CG  A PHE   A 6   ? 0.1922 0.2356 0.1372 -0.0435 0.0297  0.0327  6   PHE   A CG  
92   C CG  B PHE   A 6   ? 0.3461 0.3791 0.3040 -0.0551 0.0424  0.0340  6   PHE   A CG  
93   C CD1 A PHE   A 6   ? 0.1875 0.2268 0.1445 -0.0385 0.0265  0.0398  6   PHE   A CD1 
94   C CD1 B PHE   A 6   ? 0.3433 0.3775 0.3008 -0.0546 0.0369  0.0372  6   PHE   A CD1 
95   C CD2 A PHE   A 6   ? 0.1996 0.2330 0.1580 -0.0308 0.0243  0.0278  6   PHE   A CD2 
96   C CD2 B PHE   A 6   ? 0.3453 0.3806 0.3014 -0.0556 0.0417  0.0393  6   PHE   A CD2 
97   C CE1 A PHE   A 6   ? 0.1890 0.2229 0.1561 -0.0396 0.0265  0.0345  6   PHE   A CE1 
98   C CE1 B PHE   A 6   ? 0.3427 0.3772 0.2995 -0.0547 0.0362  0.0403  6   PHE   A CE1 
99   C CE2 A PHE   A 6   ? 0.1975 0.2326 0.1627 -0.0295 0.0230  0.0196  6   PHE   A CE2 
100  C CE2 B PHE   A 6   ? 0.3442 0.3801 0.2973 -0.0555 0.0395  0.0402  6   PHE   A CE2 
101  C CZ  A PHE   A 6   ? 0.1965 0.2288 0.1702 -0.0361 0.0182  0.0218  6   PHE   A CZ  
102  C CZ  B PHE   A 6   ? 0.3427 0.3781 0.2994 -0.0561 0.0368  0.0407  6   PHE   A CZ  
121  N N   A SER   A 7   ? 0.2151 0.2674 0.1730 -0.0734 0.0639  -0.0142 7   SER   A N   
122  N N   B SER   A 7   ? 0.3324 0.3520 0.3232 -0.0527 0.0619  -0.0104 7   SER   A N   
123  C CA  A SER   A 7   ? 0.2249 0.2744 0.2015 -0.0640 0.0651  -0.0277 7   SER   A CA  
124  C CA  B SER   A 7   ? 0.3204 0.3383 0.3170 -0.0488 0.0570  -0.0241 7   SER   A CA  
125  C C   A SER   A 7   ? 0.2094 0.2441 0.1976 -0.0614 0.0790  -0.0266 7   SER   A C   
126  C C   B SER   A 7   ? 0.3022 0.3197 0.2850 -0.0433 0.0634  -0.0207 7   SER   A C   
127  O O   A SER   A 7   ? 0.2144 0.2293 0.2051 -0.0638 0.0810  -0.0309 7   SER   A O   
128  O O   B SER   A 7   ? 0.3070 0.3228 0.2779 -0.0418 0.0631  -0.0163 7   SER   A O   
129  C CB  A SER   A 7   ? 0.2477 0.3073 0.2278 -0.0503 0.0577  -0.0328 7   SER   A CB  
130  C CB  B SER   A 7   ? 0.3252 0.3428 0.3396 -0.0510 0.0446  -0.0381 7   SER   A CB  
131  O OG  A SER   A 7   ? 0.2665 0.3267 0.2467 -0.0411 0.0562  -0.0315 7   SER   A OG  
132  O OG  B SER   A 7   ? 0.3292 0.3467 0.3576 -0.0519 0.0333  -0.0481 7   SER   A OG  
143  N N   A GLY   A 8   ? 0.1973 0.2276 0.2065 -0.0592 0.0714  -0.0344 8   GLY   A N   
144  N N   B GLY   A 8   ? 0.2834 0.3017 0.2615 -0.0364 0.0687  -0.0186 8   GLY   A N   
145  C CA  A GLY   A 8   ? 0.1908 0.2142 0.2162 -0.0453 0.0618  -0.0276 8   GLY   A CA  
146  C CA  B GLY   A 8   ? 0.2656 0.2816 0.2420 -0.0299 0.0680  -0.0149 8   GLY   A CA  
147  C C   A GLY   A 8   ? 0.1786 0.2005 0.2122 -0.0332 0.0529  -0.0221 8   GLY   A C   
148  C C   B GLY   A 8   ? 0.2459 0.2616 0.2247 -0.0253 0.0657  -0.0068 8   GLY   A C   
149  O O   A GLY   A 8   ? 0.1809 0.2062 0.2357 -0.0144 0.0530  -0.0398 8   GLY   A O   
150  O O   B GLY   A 8   ? 0.2480 0.2633 0.2283 -0.0255 0.0652  -0.0173 8   GLY   A O   
157  N N   A TYR   A 9   ? 0.1616 0.1887 0.1833 -0.0254 0.0491  -0.0122 9   TYR   A N   
158  N N   B TYR   A 9   ? 0.2242 0.2404 0.2164 -0.0207 0.0550  0.0079  9   TYR   A N   
159  C CA  A TYR   A 9   ? 0.1553 0.1750 0.1642 -0.0257 0.0378  -0.0017 9   TYR   A CA  
160  C CA  B TYR   A 9   ? 0.2088 0.2212 0.2119 -0.0186 0.0521  0.0119  9   TYR   A CA  
161  C C   A TYR   A 9   ? 0.1626 0.1592 0.1616 -0.0217 0.0370  0.0177  9   TYR   A C   
162  C C   B TYR   A 9   ? 0.2038 0.2028 0.2107 -0.0140 0.0604  0.0168  9   TYR   A C   
163  O O   A TYR   A 9   ? 0.1890 0.1673 0.1668 -0.0207 0.0413  0.0048  9   TYR   A O   
164  O O   B TYR   A 9   ? 0.2080 0.2069 0.2219 -0.0135 0.0660  0.0185  9   TYR   A O   
165  C CB  A TYR   A 9   ? 0.1441 0.1807 0.1625 -0.0138 0.0271  -0.0061 9   TYR   A CB  
166  C CB  B TYR   A 9   ? 0.2048 0.2284 0.2183 -0.0208 0.0351  0.0020  9   TYR   A CB  
167  C CG  A TYR   A 9   ? 0.1384 0.1860 0.1600 -0.0043 0.0342  -0.0137 9   TYR   A CG  
168  C CG  B TYR   A 9   ? 0.2018 0.2328 0.2101 -0.0229 0.0264  -0.0067 9   TYR   A CG  
169  C CD1 A TYR   A 9   ? 0.1361 0.1918 0.1766 -0.0159 0.0420  -0.0178 9   TYR   A CD1 
170  C CD1 B TYR   A 9   ? 0.2017 0.2383 0.2145 -0.0264 0.0244  -0.0149 9   TYR   A CD1 
171  C CD2 A TYR   A 9   ? 0.1329 0.1771 0.1627 -0.0001 0.0272  0.0043  9   TYR   A CD2 
172  C CD2 B TYR   A 9   ? 0.1957 0.2311 0.2097 -0.0242 0.0166  -0.0090 9   TYR   A CD2 
173  C CE1 A TYR   A 9   ? 0.1442 0.1963 0.1847 -0.0182 0.0389  -0.0223 9   TYR   A CE1 
174  C CE1 B TYR   A 9   ? 0.2002 0.2386 0.2157 -0.0277 0.0264  -0.0210 9   TYR   A CE1 
175  C CE2 A TYR   A 9   ? 0.1397 0.1872 0.1695 -0.0037 0.0311  -0.0094 9   TYR   A CE2 
176  C CE2 B TYR   A 9   ? 0.1966 0.2351 0.2170 -0.0240 0.0228  -0.0178 9   TYR   A CE2 
177  C CZ  A TYR   A 9   ? 0.1378 0.1969 0.1835 -0.0246 0.0410  -0.0132 9   TYR   A CZ  
178  C CZ  B TYR   A 9   ? 0.1980 0.2395 0.2213 -0.0275 0.0244  -0.0216 9   TYR   A CZ  
179  O OH  A TYR   A 9   ? 0.1459 0.2094 0.2029 -0.0399 0.0350  -0.0163 9   TYR   A OH  
180  O OH  B TYR   A 9   ? 0.2100 0.2468 0.2358 -0.0316 0.0196  -0.0247 9   TYR   A OH  
199  N N   A LEU   A 10  ? 0.1560 0.1497 0.1699 -0.0219 0.0189  0.0300  10  LEU   A N   
200  N N   B LEU   A 10  ? 0.2042 0.1901 0.2116 -0.0127 0.0504  0.0163  10  LEU   A N   
201  C CA  A LEU   A 10  ? 0.1398 0.1436 0.1791 -0.0223 0.0091  0.0346  10  LEU   A CA  
202  C CA  B LEU   A 10  ? 0.2055 0.1933 0.2136 -0.0105 0.0377  0.0196  10  LEU   A CA  
203  C C   A LEU   A 10  ? 0.1293 0.1420 0.1748 -0.0202 0.0104  0.0402  10  LEU   A C   
204  C C   B LEU   A 10  ? 0.1950 0.1684 0.1898 -0.0144 0.0305  0.0260  10  LEU   A C   
205  O O   A LEU   A 10  ? 0.1431 0.1403 0.1837 -0.0230 0.0332  0.0317  10  LEU   A O   
206  O O   B LEU   A 10  ? 0.2021 0.1588 0.1684 -0.0222 0.0427  0.0132  10  LEU   A O   
207  C CB  A LEU   A 10  ? 0.1492 0.1593 0.2017 -0.0189 -0.0042 0.0485  10  LEU   A CB  
208  C CB  B LEU   A 10  ? 0.2212 0.2108 0.2475 -0.0136 0.0205  0.0181  10  LEU   A CB  
209  C CG  A LEU   A 10  ? 0.1713 0.1834 0.2467 -0.0104 -0.0312 0.0601  10  LEU   A CG  
210  C CG  B LEU   A 10  ? 0.2397 0.2316 0.2883 -0.0118 0.0049  0.0084  10  LEU   A CG  
211  C CD1 A LEU   A 10  ? 0.1868 0.1986 0.2812 -0.0204 -0.0186 0.0644  10  LEU   A CD1 
212  C CD1 B LEU   A 10  ? 0.2473 0.2420 0.3006 -0.0079 -0.0066 0.0114  10  LEU   A CD1 
213  C CD2 A LEU   A 10  ? 0.1936 0.2052 0.2608 -0.0061 -0.0093 0.0479  10  LEU   A CD2 
214  C CD2 B LEU   A 10  ? 0.2428 0.2358 0.3016 -0.0089 0.0070  0.0060  10  LEU   A CD2 
237  N N   A LYS   A 11  ? 0.1314 0.1475 0.1757 -0.0165 0.0232  0.0339  11  LYS   A N   
238  N N   B LYS   A 11  ? 0.1908 0.1608 0.1979 -0.0198 0.0249  0.0306  11  LYS   A N   
239  C CA  A LYS   A 11  ? 0.1317 0.1473 0.1807 -0.0181 0.0183  0.0288  11  LYS   A CA  
240  C CA  B LYS   A 11  ? 0.1839 0.1558 0.1954 -0.0259 0.0198  0.0343  11  LYS   A CA  
241  C C   A LYS   A 11  ? 0.1301 0.1467 0.1860 -0.0155 0.0231  0.0166  11  LYS   A C   
242  C C   B LYS   A 11  ? 0.1730 0.1461 0.1958 -0.0352 0.0145  0.0327  11  LYS   A C   
243  O O   A LYS   A 11  ? 0.1415 0.1620 0.2305 -0.0404 0.0343  0.0043  11  LYS   A O   
244  O O   B LYS   A 11  ? 0.1708 0.1430 0.2152 -0.0329 0.0067  0.0195  11  LYS   A O   
245  C CB  A LYS   A 11  ? 0.1330 0.1428 0.1790 -0.0130 0.0124  0.0308  11  LYS   A CB  
246  C CB  B LYS   A 11  ? 0.1914 0.1523 0.1904 -0.0237 0.0233  0.0321  11  LYS   A CB  
247  C CG  A LYS   A 11  ? 0.1431 0.1436 0.1863 -0.0137 0.0166  0.0280  11  LYS   A CG  
248  C CG  B LYS   A 11  ? 0.1946 0.1535 0.1926 -0.0192 0.0235  0.0306  11  LYS   A CG  
249  C CD  A LYS   A 11  ? 0.1426 0.1510 0.1843 -0.0118 0.0073  0.0352  11  LYS   A CD  
250  C CD  B LYS   A 11  ? 0.2013 0.1614 0.1946 -0.0125 0.0226  0.0359  11  LYS   A CD  
251  C CE  A LYS   A 11  ? 0.1421 0.1496 0.1928 -0.0070 0.0099  0.0422  11  LYS   A CE  
252  C CE  B LYS   A 11  ? 0.1999 0.1625 0.1927 -0.0115 0.0151  0.0443  11  LYS   A CE  
253  N NZ  A LYS   A 11  ? 0.1436 0.1480 0.2013 0.0104  0.0162  0.0296  11  LYS   A NZ  
254  N NZ  B LYS   A 11  ? 0.1986 0.1641 0.1965 -0.0073 0.0121  0.0406  11  LYS   A NZ  
281  N N   A LEU   A 12  ? 0.1263 0.1434 0.1593 -0.0214 0.0219  0.0166  12  LEU   A N   
282  N N   B LEU   A 12  ? 0.1667 0.1523 0.1957 -0.0271 0.0146  0.0258  12  LEU   A N   
283  C CA  A LEU   A 12  ? 0.1338 0.1524 0.1463 -0.0126 0.0059  0.0284  12  LEU   A CA  
284  C CA  B LEU   A 12  ? 0.1682 0.1560 0.1930 -0.0272 0.0182  0.0291  12  LEU   A CA  
285  C C   A LEU   A 12  ? 0.1392 0.1465 0.1634 -0.0243 0.0062  0.0194  12  LEU   A C   
286  C C   B LEU   A 12  ? 0.1683 0.1468 0.1800 -0.0267 0.0234  0.0306  12  LEU   A C   
287  O O   A LEU   A 12  ? 0.1508 0.1501 0.1783 -0.0193 0.0088  0.0051  12  LEU   A O   
288  O O   B LEU   A 12  ? 0.1784 0.1453 0.1798 -0.0194 0.0167  0.0339  12  LEU   A O   
289  C CB  A LEU   A 12  ? 0.1430 0.1516 0.1571 -0.0073 0.0002  0.0340  12  LEU   A CB  
290  C CB  B LEU   A 12  ? 0.1708 0.1639 0.2097 -0.0279 0.0199  0.0308  12  LEU   A CB  
291  C CG  A LEU   A 12  ? 0.1539 0.1610 0.1774 -0.0048 0.0132  0.0375  12  LEU   A CG  
292  C CG  B LEU   A 12  ? 0.1692 0.1662 0.2241 -0.0280 0.0285  0.0270  12  LEU   A CG  
293  C CD1 A LEU   A 12  ? 0.1679 0.1624 0.1863 0.0051  0.0249  0.0443  12  LEU   A CD1 
294  C CD1 B LEU   A 12  ? 0.1727 0.1707 0.2404 -0.0238 0.0269  0.0296  12  LEU   A CD1 
295  C CD2 A LEU   A 12  ? 0.1546 0.1684 0.2045 0.0006  0.0051  0.0277  12  LEU   A CD2 
296  C CD2 B LEU   A 12  ? 0.1669 0.1754 0.2302 -0.0287 0.0277  0.0124  12  LEU   A CD2 
319  N N   A THR   A 13  ? 0.1345 0.1405 0.1807 -0.0157 0.0095  0.0098  13  THR   A N   
320  N N   B THR   A 13  ? 0.1641 0.1433 0.1708 -0.0189 0.0188  0.0208  13  THR   A N   
321  C CA  A THR   A 13  ? 0.1361 0.1384 0.1851 -0.0111 0.0175  0.0044  13  THR   A CA  
322  C CA  B THR   A 13  ? 0.1682 0.1469 0.1691 -0.0239 0.0202  0.0230  13  THR   A CA  
323  C C   A THR   A 13  ? 0.1420 0.1403 0.1857 -0.0126 0.0181  0.0136  13  THR   A C   
324  C C   B THR   A 13  ? 0.1717 0.1531 0.1716 -0.0283 0.0197  0.0256  13  THR   A C   
325  O O   A THR   A 13  ? 0.1380 0.1482 0.1881 -0.0034 0.0219  0.0139  13  THR   A O   
326  O O   B THR   A 13  ? 0.1693 0.1620 0.1759 -0.0306 0.0190  0.0236  13  THR   A O   
327  C CB  A THR   A 13  ? 0.1418 0.1544 0.1974 -0.0100 0.0175  0.0051  13  THR   A CB  
328  C CB  B THR   A 13  ? 0.1659 0.1522 0.1788 -0.0201 0.0267  0.0193  13  THR   A CB  
329  O OG1 A THR   A 13  ? 0.1498 0.1466 0.2058 -0.0082 0.0075  -0.0033 13  THR   A OG1 
330  O OG1 B THR   A 13  ? 0.1586 0.1571 0.1770 -0.0275 0.0295  0.0275  13  THR   A OG1 
331  C CG2 A THR   A 13  ? 0.1544 0.1612 0.2256 -0.0127 0.0149  -0.0050 13  THR   A CG2 
332  C CG2 B THR   A 13  ? 0.1670 0.1588 0.1884 -0.0179 0.0291  0.0089  13  THR   A CG2 
347  N N   A ASP   A 14  ? 0.1499 0.1366 0.1954 -0.0195 0.0129  0.0131  14  ASP   A N   
348  N N   B ASP   A 14  ? 0.1757 0.1595 0.1873 -0.0287 0.0197  0.0312  14  ASP   A N   
349  C CA  A ASP   A 14  ? 0.1480 0.1519 0.2111 -0.0152 0.0061  0.0216  14  ASP   A CA  
350  C CA  B ASP   A 14  ? 0.1847 0.1646 0.2074 -0.0250 0.0137  0.0342  14  ASP   A CA  
351  C C   A ASP   A 14  ? 0.1459 0.1535 0.1765 -0.0099 0.0064  0.0226  14  ASP   A C   
352  C C   B ASP   A 14  ? 0.1695 0.1625 0.1785 -0.0250 0.0031  0.0422  14  ASP   A C   
353  O O   A ASP   A 14  ? 0.1559 0.1650 0.1863 -0.0068 0.0147  0.0195  14  ASP   A O   
354  O O   B ASP   A 14  ? 0.1676 0.1670 0.1861 -0.0330 0.0031  0.0469  14  ASP   A O   
355  C CB  A ASP   A 14  ? 0.1644 0.1734 0.2669 -0.0192 -0.0021 0.0437  14  ASP   A CB  
356  C CB  B ASP   A 14  ? 0.2145 0.1750 0.2609 -0.0245 0.0144  0.0330  14  ASP   A CB  
357  C CG  A ASP   A 14  ? 0.1782 0.2021 0.3310 -0.0164 -0.0065 0.0476  14  ASP   A CG  
358  C CG  B ASP   A 14  ? 0.2415 0.2047 0.3217 -0.0161 0.0134  0.0108  14  ASP   A CG  
359  O OD1 A ASP   A 14  ? 0.1877 0.1997 0.3328 -0.0151 -0.0228 0.0711  14  ASP   A OD1 
360  O OD1 B ASP   A 14  ? 0.2574 0.2218 0.3498 -0.0119 0.0040  -0.0023 14  ASP   A OD1 
361  O OD2 A ASP   A 14  ? 0.1886 0.2251 0.3612 -0.0256 -0.0104 0.0406  14  ASP   A OD2 
362  O OD2 B ASP   A 14  ? 0.2513 0.2094 0.3455 -0.0165 0.0107  0.0160  14  ASP   A OD2 
371  N N   A ASN   A 15  ? 0.1371 0.1435 0.1590 -0.0160 0.0182  0.0177  15  ASN   A N   
372  N N   B ASN   A 15  ? 0.1652 0.1559 0.1735 -0.0220 0.0068  0.0445  15  ASN   A N   
373  C CA  A ASN   A 15  ? 0.1333 0.1512 0.1680 -0.0128 0.0095  0.0098  15  ASN   A CA  
374  C CA  B ASN   A 15  ? 0.1641 0.1504 0.1680 -0.0189 0.0082  0.0311  15  ASN   A CA  
375  C C   A ASN   A 15  ? 0.1337 0.1472 0.1802 -0.0135 0.0151  0.0088  15  ASN   A C   
376  C C   B ASN   A 15  ? 0.1627 0.1434 0.1667 -0.0166 0.0095  0.0270  15  ASN   A C   
377  O O   A ASN   A 15  ? 0.1423 0.1475 0.2172 -0.0106 0.0029  0.0005  15  ASN   A O   
378  O O   B ASN   A 15  ? 0.1625 0.1397 0.1676 -0.0186 0.0028  0.0202  15  ASN   A O   
379  C CB  A ASN   A 15  ? 0.1275 0.1494 0.1577 -0.0118 0.0101  0.0109  15  ASN   A CB  
380  C CB  B ASN   A 15  ? 0.1660 0.1494 0.1719 -0.0178 0.0088  0.0279  15  ASN   A CB  
381  C CG  A ASN   A 15  ? 0.1315 0.1565 0.1666 -0.0083 0.0118  -0.0006 15  ASN   A CG  
382  C CG  B ASN   A 15  ? 0.1707 0.1535 0.1728 -0.0171 0.0052  0.0279  15  ASN   A CG  
383  O OD1 A ASN   A 15  ? 0.1396 0.1598 0.1754 -0.0208 0.0151  -0.0110 15  ASN   A OD1 
384  O OD1 B ASN   A 15  ? 0.1759 0.1547 0.1885 -0.0181 0.0159  0.0305  15  ASN   A OD1 
385  N ND2 A ASN   A 15  ? 0.1381 0.1729 0.1568 -0.0161 0.0122  0.0023  15  ASN   A ND2 
386  N ND2 B ASN   A 15  ? 0.1717 0.1585 0.1742 -0.0185 0.0064  0.0307  15  ASN   A ND2 
399  N N   A VAL   A 16  ? 0.1339 0.1373 0.1742 -0.0094 0.0126  0.0167  16  VAL   A N   
400  N N   B VAL   A 16  ? 0.1679 0.1425 0.1669 -0.0144 0.0025  0.0235  16  VAL   A N   
401  C CA  A VAL   A 16  ? 0.1309 0.1385 0.1637 -0.0116 0.0074  0.0110  16  VAL   A CA  
402  C CA  B VAL   A 16  ? 0.1690 0.1504 0.1549 -0.0087 0.0102  0.0282  16  VAL   A CA  
403  C C   A VAL   A 16  ? 0.1224 0.1360 0.1603 -0.0173 0.0030  0.0223  16  VAL   A C   
404  C C   B VAL   A 16  ? 0.1726 0.1540 0.1600 -0.0147 0.0155  0.0383  16  VAL   A C   
405  O O   A VAL   A 16  ? 0.1231 0.1368 0.1699 -0.0265 0.0103  0.0077  16  VAL   A O   
406  O O   B VAL   A 16  ? 0.1754 0.1569 0.1693 -0.0194 0.0170  0.0332  16  VAL   A O   
407  C CB  A VAL   A 16  ? 0.1467 0.1523 0.1664 -0.0013 0.0205  0.0090  16  VAL   A CB  
408  C CB  B VAL   A 16  ? 0.1653 0.1517 0.1295 -0.0007 0.0110  0.0280  16  VAL   A CB  
409  C CG1 A VAL   A 16  ? 0.1602 0.1576 0.1716 0.0003  0.0074  0.0017  16  VAL   A CG1 
410  C CG1 B VAL   A 16  ? 0.1667 0.1427 0.1305 -0.0016 0.0040  0.0295  16  VAL   A CG1 
411  C CG2 A VAL   A 16  ? 0.1569 0.1610 0.1660 -0.0010 0.0394  0.0065  16  VAL   A CG2 
412  C CG2 B VAL   A 16  ? 0.1703 0.1686 0.1450 0.0046  0.0245  0.0256  16  VAL   A CG2 
431  N N   A TYR   A 17  ? 0.1261 0.1368 0.1542 -0.0141 0.0188  0.0178  17  TYR   A N   
432  N N   B TYR   A 17  ? 0.1801 0.1496 0.1743 -0.0154 0.0195  0.0344  17  TYR   A N   
433  C CA  A TYR   A 17  ? 0.1308 0.1360 0.1562 -0.0192 0.0139  0.0246  17  TYR   A CA  
434  C CA  B TYR   A 17  ? 0.1896 0.1603 0.1755 -0.0190 0.0201  0.0363  17  TYR   A CA  
435  C C   A TYR   A 17  ? 0.1334 0.1318 0.1767 -0.0106 0.0078  0.0178  17  TYR   A C   
436  C C   B TYR   A 17  ? 0.1705 0.1609 0.1726 -0.0195 0.0273  0.0419  17  TYR   A C   
437  O O   A TYR   A 17  ? 0.1272 0.1313 0.1810 -0.0079 0.0136  0.0161  17  TYR   A O   
438  O O   B TYR   A 17  ? 0.1621 0.1659 0.1831 -0.0280 0.0268  0.0420  17  TYR   A O   
439  C CB  A TYR   A 17  ? 0.1332 0.1378 0.1572 -0.0149 0.0110  0.0350  17  TYR   A CB  
440  C CB  B TYR   A 17  ? 0.2286 0.1778 0.1989 -0.0227 0.0064  0.0324  17  TYR   A CB  
441  C CG  A TYR   A 17  ? 0.1397 0.1383 0.1552 -0.0154 0.0046  0.0415  17  TYR   A CG  
442  C CG  B TYR   A 17  ? 0.2719 0.1985 0.2301 -0.0271 -0.0113 0.0281  17  TYR   A CG  
443  C CD1 A TYR   A 17  ? 0.1512 0.1512 0.1683 -0.0077 0.0020  0.0367  17  TYR   A CD1 
444  C CD1 B TYR   A 17  ? 0.2930 0.2106 0.2516 -0.0271 -0.0162 0.0277  17  TYR   A CD1 
445  C CD2 A TYR   A 17  ? 0.1550 0.1395 0.1598 -0.0247 -0.0056 0.0396  17  TYR   A CD2 
446  C CD2 B TYR   A 17  ? 0.2879 0.2063 0.2467 -0.0337 -0.0158 0.0290  17  TYR   A CD2 
447  C CE1 A TYR   A 17  ? 0.1595 0.1403 0.1783 -0.0182 -0.0158 0.0259  17  TYR   A CE1 
448  C CE1 B TYR   A 17  ? 0.3058 0.2158 0.2679 -0.0286 -0.0213 0.0312  17  TYR   A CE1 
449  C CE2 A TYR   A 17  ? 0.1657 0.1373 0.1641 -0.0274 -0.0088 0.0270  17  TYR   A CE2 
450  C CE2 B TYR   A 17  ? 0.3022 0.2139 0.2669 -0.0341 -0.0192 0.0282  17  TYR   A CE2 
451  C CZ  A TYR   A 17  ? 0.1700 0.1408 0.1701 -0.0236 -0.0243 0.0403  17  TYR   A CZ  
452  C CZ  B TYR   A 17  ? 0.3118 0.2187 0.2749 -0.0326 -0.0223 0.0331  17  TYR   A CZ  
453  O OH  A TYR   A 17  ? 0.1889 0.1386 0.1666 -0.0253 -0.0264 0.0386  17  TYR   A OH  
454  O OH  B TYR   A 17  ? 0.3221 0.2274 0.2929 -0.0381 -0.0252 0.0363  17  TYR   A OH  
473  N N   A ILE   A 18  ? 0.1395 0.1390 0.1722 -0.0093 0.0149  0.0342  18  ILE   A N   
474  N N   B ILE   A 18  ? 0.1615 0.1559 0.1661 -0.0190 0.0340  0.0368  18  ILE   A N   
475  C CA  A ILE   A 18  ? 0.1512 0.1419 0.1748 -0.0067 0.0205  0.0167  18  ILE   A CA  
476  C CA  B ILE   A 18  ? 0.1631 0.1574 0.1625 -0.0117 0.0378  0.0307  18  ILE   A CA  
477  C C   A ILE   A 18  ? 0.1485 0.1434 0.1906 -0.0176 0.0163  0.0210  18  ILE   A C   
478  C C   B ILE   A 18  ? 0.1564 0.1696 0.1516 -0.0129 0.0316  0.0308  18  ILE   A C   
479  O O   A ILE   A 18  ? 0.1447 0.1553 0.2003 -0.0218 0.0324  0.0274  18  ILE   A O   
480  O O   B ILE   A 18  ? 0.1538 0.1768 0.1645 -0.0165 0.0425  0.0313  18  ILE   A O   
481  C CB  A ILE   A 18  ? 0.1556 0.1423 0.1711 0.0007  0.0192  0.0282  18  ILE   A CB  
482  C CB  B ILE   A 18  ? 0.1629 0.1516 0.1420 -0.0048 0.0391  0.0343  18  ILE   A CB  
483  C CG1 A ILE   A 18  ? 0.1553 0.1489 0.1707 0.0177  0.0105  0.0299  18  ILE   A CG1 
484  C CG1 B ILE   A 18  ? 0.1726 0.1583 0.1504 -0.0096 0.0493  0.0307  18  ILE   A CG1 
485  C CG2 A ILE   A 18  ? 0.1559 0.1467 0.1784 -0.0032 0.0132  0.0186  18  ILE   A CG2 
486  C CG2 B ILE   A 18  ? 0.1669 0.1651 0.1388 -0.0104 0.0223  0.0331  18  ILE   A CG2 
487  C CD1 A ILE   A 18  ? 0.1730 0.1614 0.1817 0.0245  0.0069  0.0256  18  ILE   A CD1 
488  C CD1 B ILE   A 18  ? 0.1819 0.1673 0.1727 -0.0111 0.0507  0.0159  18  ILE   A CD1 
511  N N   A LYS   A 19  ? 0.1512 0.1469 0.1870 -0.0170 0.0332  0.0248  19  LYS   A N   
512  N N   B LYS   A 19  ? 0.1559 0.1743 0.1523 -0.0091 0.0373  0.0229  19  LYS   A N   
513  C CA  A LYS   A 19  ? 0.1546 0.1528 0.2061 -0.0117 0.0356  0.0269  19  LYS   A CA  
514  C CA  B LYS   A 19  ? 0.1714 0.1905 0.1678 0.0005  0.0327  0.0186  19  LYS   A CA  
515  C C   A LYS   A 19  ? 0.1484 0.1535 0.2349 -0.0011 0.0342  0.0385  19  LYS   A C   
516  C C   B LYS   A 19  ? 0.1826 0.1989 0.1840 0.0125  0.0279  0.0178  19  LYS   A C   
517  O O   A LYS   A 19  ? 0.1476 0.1525 0.2431 0.0059  0.0294  0.0409  19  LYS   A O   
518  O O   B LYS   A 19  ? 0.1881 0.1925 0.1946 0.0017  0.0279  0.0277  19  LYS   A O   
519  C CB  A LYS   A 19  ? 0.1737 0.1688 0.2260 -0.0207 0.0334  0.0219  19  LYS   A CB  
520  C CB  B LYS   A 19  ? 0.1796 0.2029 0.1701 -0.0036 0.0322  -0.0006 19  LYS   A CB  
521  C CG  A LYS   A 19  ? 0.2050 0.1841 0.2340 -0.0260 0.0301  0.0021  19  LYS   A CG  
522  C CG  B LYS   A 19  ? 0.1934 0.2195 0.1737 -0.0078 0.0308  -0.0037 19  LYS   A CG  
523  C CD  A LYS   A 19  ? 0.2287 0.2000 0.2447 -0.0250 0.0313  -0.0046 19  LYS   A CD  
524  C CD  B LYS   A 19  ? 0.2055 0.2314 0.1779 -0.0171 0.0311  -0.0068 19  LYS   A CD  
525  C CE  A LYS   A 19  ? 0.2442 0.2078 0.2493 -0.0281 0.0332  -0.0114 19  LYS   A CE  
526  C CE  B LYS   A 19  ? 0.2131 0.2431 0.1890 -0.0223 0.0226  -0.0103 19  LYS   A CE  
527  N NZ  A LYS   A 19  ? 0.2558 0.2163 0.2472 -0.0313 0.0400  -0.0143 19  LYS   A NZ  
528  N NZ  B LYS   A 19  ? 0.2210 0.2494 0.1937 -0.0308 0.0287  -0.0180 19  LYS   A NZ  
555  N N   A ASN   A 20  ? 0.1605 0.1605 0.2631 0.0013  0.0340  0.0483  20  ASN   A N   
556  N N   B ASN   A 20  ? 0.1998 0.2168 0.2128 0.0268  0.0355  0.0062  20  ASN   A N   
557  C CA  A ASN   A 20  ? 0.1750 0.1791 0.2953 0.0273  0.0462  0.0472  20  ASN   A CA  
558  C CA  B ASN   A 20  ? 0.2150 0.2410 0.2573 0.0382  0.0348  -0.0013 20  ASN   A CA  
559  C C   A ASN   A 20  ? 0.1881 0.1808 0.2958 0.0235  0.0516  0.0343  20  ASN   A C   
560  C C   B ASN   A 20  ? 0.2357 0.2459 0.2670 0.0336  0.0385  -0.0088 20  ASN   A C   
561  O O   A ASN   A 20  ? 0.2030 0.1785 0.3019 0.0157  0.0595  0.0233  20  ASN   A O   
562  O O   B ASN   A 20  ? 0.2490 0.2485 0.2843 0.0307  0.0441  -0.0120 20  ASN   A O   
563  C CB  A ASN   A 20  ? 0.1820 0.1944 0.3205 0.0410  0.0461  0.0708  20  ASN   A CB  
564  C CB  B ASN   A 20  ? 0.2127 0.2579 0.2895 0.0502  0.0344  0.0019  20  ASN   A CB  
565  C CG  A ASN   A 20  ? 0.1910 0.2020 0.3545 0.0460  0.0543  0.0807  20  ASN   A CG  
566  C CG  B ASN   A 20  ? 0.2150 0.2704 0.3298 0.0577  0.0329  0.0025  20  ASN   A CG  
567  O OD1 A ASN   A 20  ? 0.2126 0.2116 0.3875 0.0383  0.0518  0.0629  20  ASN   A OD1 
568  O OD1 B ASN   A 20  ? 0.2145 0.2764 0.3597 0.0557  0.0369  -0.0021 20  ASN   A OD1 
569  N ND2 A ASN   A 20  ? 0.2028 0.2079 0.3721 0.0468  0.0409  0.0951  20  ASN   A ND2 
570  N ND2 B ASN   A 20  ? 0.2276 0.2756 0.3417 0.0566  0.0258  0.0102  20  ASN   A ND2 
583  N N   A ALA   A 21  ? 0.1877 0.1826 0.2943 0.0230  0.0274  0.0255  21  ALA   A N   
584  N N   B ALA   A 21  ? 0.2421 0.2499 0.2679 0.0314  0.0220  -0.0074 21  ALA   A N   
585  C CA  A ALA   A 21  ? 0.1851 0.1811 0.2848 0.0169  0.0241  0.0274  21  ALA   A CA  
586  C CA  B ALA   A 21  ? 0.2452 0.2528 0.2713 0.0242  0.0194  0.0029  21  ALA   A CA  
587  C C   A ALA   A 21  ? 0.1852 0.1858 0.2746 0.0127  0.0262  0.0328  21  ALA   A C   
588  C C   B ALA   A 21  ? 0.2373 0.2462 0.2580 0.0258  0.0283  0.0011  21  ALA   A C   
589  O O   A ALA   A 21  ? 0.1865 0.1894 0.2777 0.0139  0.0160  0.0387  21  ALA   A O   
590  O O   B ALA   A 21  ? 0.2346 0.2420 0.2597 0.0284  0.0303  -0.0053 21  ALA   A O   
591  C CB  A ALA   A 21  ? 0.1967 0.1861 0.2953 0.0163  0.0199  0.0260  21  ALA   A CB  
592  C CB  B ALA   A 21  ? 0.2536 0.2576 0.2944 0.0205  0.0135  0.0071  21  ALA   A CB  
603  N N   A ASP   A 22  ? 0.1887 0.1872 0.2669 0.0004  0.0345  0.0332  22  ASP   A N   
604  N N   B ASP   A 22  ? 0.2343 0.2415 0.2508 0.0189  0.0308  0.0091  22  ASP   A N   
605  C CA  A ASP   A 22  ? 0.1942 0.1916 0.2490 -0.0010 0.0394  0.0192  22  ASP   A CA  
606  C CA  B ASP   A 22  ? 0.2330 0.2377 0.2437 0.0150  0.0271  0.0132  22  ASP   A CA  
607  C C   A ASP   A 22  ? 0.1888 0.1932 0.2161 -0.0077 0.0355  0.0155  22  ASP   A C   
608  C C   B ASP   A 22  ? 0.2127 0.2295 0.2090 0.0032  0.0386  0.0132  22  ASP   A C   
609  O O   A ASP   A 22  ? 0.1873 0.2066 0.2246 -0.0130 0.0354  0.0100  22  ASP   A O   
610  O O   B ASP   A 22  ? 0.2084 0.2355 0.2098 -0.0014 0.0441  0.0054  22  ASP   A O   
611  C CB  A ASP   A 22  ? 0.2089 0.1922 0.2923 -0.0028 0.0322  0.0102  22  ASP   A CB  
612  C CB  B ASP   A 22  ? 0.2503 0.2436 0.2779 0.0196  0.0173  0.0083  22  ASP   A CB  
613  C CG  A ASP   A 22  ? 0.2256 0.1907 0.3394 -0.0101 0.0113  0.0101  22  ASP   A CG  
614  C CG  B ASP   A 22  ? 0.2626 0.2481 0.3082 0.0196  0.0088  0.0107  22  ASP   A CG  
615  O OD1 A ASP   A 22  ? 0.2197 0.1808 0.3530 -0.0238 -0.0040 0.0219  22  ASP   A OD1 
616  O OD1 B ASP   A 22  ? 0.2681 0.2471 0.3175 0.0218  0.0083  0.0111  22  ASP   A OD1 
617  O OD2 A ASP   A 22  ? 0.2482 0.2018 0.3718 -0.0018 0.0114  -0.0027 22  ASP   A OD2 
618  O OD2 B ASP   A 22  ? 0.2661 0.2550 0.3185 0.0163  0.0060  0.0100  22  ASP   A OD2 
627  N N   A ILE   A 23  ? 0.1883 0.1881 0.1958 -0.0077 0.0338  0.0097  23  ILE   A N   
628  N N   B ILE   A 23  ? 0.2004 0.2160 0.1878 -0.0015 0.0376  0.0211  23  ILE   A N   
629  C CA  A ILE   A 23  ? 0.1870 0.1801 0.1894 -0.0072 0.0299  0.0125  23  ILE   A CA  
630  C CA  B ILE   A 23  ? 0.1913 0.2098 0.1714 -0.0061 0.0208  0.0309  23  ILE   A CA  
631  C C   A ILE   A 23  ? 0.1803 0.1886 0.1862 -0.0030 0.0446  0.0070  23  ILE   A C   
632  C C   B ILE   A 23  ? 0.1911 0.2130 0.1700 -0.0173 0.0263  0.0269  23  ILE   A C   
633  O O   A ILE   A 23  ? 0.1892 0.1942 0.1924 0.0007  0.0505  0.0013  23  ILE   A O   
634  O O   B ILE   A 23  ? 0.1888 0.2094 0.1776 -0.0263 0.0281  0.0245  23  ILE   A O   
635  C CB  A ILE   A 23  ? 0.1929 0.1674 0.1721 -0.0044 0.0188  0.0195  23  ILE   A CB  
636  C CB  B ILE   A 23  ? 0.1867 0.2030 0.1569 -0.0021 0.0065  0.0379  23  ILE   A CB  
637  C CG1 A ILE   A 23  ? 0.1966 0.1702 0.1602 -0.0023 0.0162  0.0182  23  ILE   A CG1 
638  C CG1 B ILE   A 23  ? 0.1883 0.2061 0.1478 0.0001  -0.0030 0.0322  23  ILE   A CG1 
639  C CG2 A ILE   A 23  ? 0.1942 0.1636 0.1684 -0.0087 0.0131  0.0227  23  ILE   A CG2 
640  C CG2 B ILE   A 23  ? 0.1815 0.1971 0.1519 0.0048  0.0033  0.0381  23  ILE   A CG2 
641  C CD1 A ILE   A 23  ? 0.1919 0.1729 0.1627 -0.0024 -0.0055 0.0108  23  ILE   A CD1 
642  C CD1 B ILE   A 23  ? 0.1849 0.2070 0.1583 -0.0002 -0.0165 0.0252  23  ILE   A CD1 
665  N N   A VAL   A 24  ? 0.1855 0.1974 0.1960 -0.0081 0.0438  -0.0064 24  VAL   A N   
666  N N   B VAL   A 24  ? 0.2044 0.2233 0.1890 -0.0197 0.0201  0.0194  24  VAL   A N   
667  C CA  A VAL   A 24  ? 0.1994 0.2103 0.2197 -0.0189 0.0387  -0.0153 24  VAL   A CA  
668  C CA  B VAL   A 24  ? 0.2179 0.2307 0.2076 -0.0185 0.0235  0.0133  24  VAL   A CA  
669  C C   A VAL   A 24  ? 0.2047 0.2350 0.2214 -0.0301 0.0353  -0.0224 24  VAL   A C   
670  C C   B VAL   A 24  ? 0.2257 0.2471 0.2174 -0.0187 0.0262  0.0055  24  VAL   A C   
671  O O   A VAL   A 24  ? 0.2093 0.2355 0.2133 -0.0209 0.0372  -0.0215 24  VAL   A O   
672  O O   B VAL   A 24  ? 0.2293 0.2470 0.2198 -0.0150 0.0278  0.0050  24  VAL   A O   
673  C CB  A VAL   A 24  ? 0.2014 0.2077 0.2337 -0.0163 0.0543  -0.0173 24  VAL   A CB  
674  C CB  B VAL   A 24  ? 0.2233 0.2319 0.2290 -0.0180 0.0234  0.0146  24  VAL   A CB  
675  C CG1 A VAL   A 24  ? 0.2067 0.2117 0.2397 -0.0127 0.0555  -0.0258 24  VAL   A CG1 
676  C CG1 B VAL   A 24  ? 0.2325 0.2364 0.2447 -0.0185 0.0204  0.0152  24  VAL   A CG1 
677  C CG2 A VAL   A 24  ? 0.2099 0.2150 0.2515 -0.0077 0.0685  -0.0076 24  VAL   A CG2 
678  C CG2 B VAL   A 24  ? 0.2256 0.2315 0.2289 -0.0168 0.0279  0.0113  24  VAL   A CG2 
697  N N   A GLU   A 25  ? 0.2132 0.2696 0.2258 -0.0383 0.0504  -0.0293 25  GLU   A N   
698  N N   B GLU   A 25  ? 0.2334 0.2673 0.2269 -0.0174 0.0344  -0.0033 25  GLU   A N   
699  C CA  A GLU   A 25  ? 0.2279 0.3054 0.2415 -0.0374 0.0673  -0.0362 25  GLU   A CA  
700  C CA  B GLU   A 25  ? 0.2461 0.2891 0.2473 -0.0160 0.0344  -0.0084 25  GLU   A CA  
701  C C   A GLU   A 25  ? 0.2179 0.3137 0.2156 -0.0531 0.0830  -0.0342 25  GLU   A C   
702  C C   B GLU   A 25  ? 0.2406 0.2913 0.2384 -0.0184 0.0408  -0.0074 25  GLU   A C   
703  O O   A GLU   A 25  ? 0.2213 0.3232 0.2182 -0.0581 0.0862  -0.0330 25  GLU   A O   
704  O O   B GLU   A 25  ? 0.2428 0.2993 0.2410 -0.0175 0.0405  -0.0097 25  GLU   A O   
705  C CB  A GLU   A 25  ? 0.2511 0.3301 0.2847 -0.0262 0.0643  -0.0386 25  GLU   A CB  
706  C CB  B GLU   A 25  ? 0.2658 0.3073 0.2867 -0.0122 0.0326  -0.0120 25  GLU   A CB  
707  C CG  A GLU   A 25  ? 0.2714 0.3508 0.3288 -0.0225 0.0486  -0.0403 25  GLU   A CG  
708  C CG  B GLU   A 25  ? 0.2856 0.3244 0.3379 -0.0134 0.0283  -0.0096 25  GLU   A CG  
709  C CD  A GLU   A 25  ? 0.2893 0.3716 0.3748 -0.0184 0.0341  -0.0387 25  GLU   A CD  
710  C CD  B GLU   A 25  ? 0.2990 0.3396 0.3853 -0.0164 0.0197  -0.0084 25  GLU   A CD  
711  O OE1 A GLU   A 25  ? 0.3000 0.3806 0.3839 -0.0168 0.0155  -0.0470 25  GLU   A OE1 
712  O OE1 B GLU   A 25  ? 0.3038 0.3463 0.4069 -0.0177 0.0166  -0.0082 25  GLU   A OE1 
713  O OE2 A GLU   A 25  ? 0.2902 0.3794 0.4027 -0.0142 0.0331  -0.0385 25  GLU   A OE2 
714  O OE2 B GLU   A 25  ? 0.3061 0.3444 0.4029 -0.0178 0.0160  -0.0094 25  GLU   A OE2 
727  N N   A GLU   A 26  ? 0.2084 0.3074 0.2076 -0.0682 0.0846  -0.0366 26  GLU   A N   
728  N N   B GLU   A 26  ? 0.2346 0.2825 0.2328 -0.0219 0.0533  -0.0075 26  GLU   A N   
729  C CA  A GLU   A 26  ? 0.2267 0.3044 0.1964 -0.0802 0.0770  -0.0216 26  GLU   A CA  
730  C CA  B GLU   A 26  ? 0.2373 0.2732 0.2283 -0.0256 0.0524  0.0056  26  GLU   A CA  
731  C C   A GLU   A 26  ? 0.2218 0.2863 0.1609 -0.0835 0.0644  -0.0095 26  GLU   A C   
732  C C   B GLU   A 26  ? 0.2342 0.2679 0.2091 -0.0210 0.0485  0.0070  26  GLU   A C   
733  O O   A GLU   A 26  ? 0.2268 0.2862 0.1462 -0.0938 0.0595  -0.0053 26  GLU   A O   
734  O O   B GLU   A 26  ? 0.2367 0.2688 0.2106 -0.0266 0.0442  0.0046  26  GLU   A O   
735  C CB  A GLU   A 26  ? 0.2519 0.3114 0.2442 -0.0893 0.0693  -0.0116 26  GLU   A CB  
736  C CB  B GLU   A 26  ? 0.2438 0.2634 0.2507 -0.0358 0.0499  0.0221  26  GLU   A CB  
737  C CG  A GLU   A 26  ? 0.2743 0.3230 0.3067 -0.0955 0.0658  -0.0065 26  GLU   A CG  
738  C CG  B GLU   A 26  ? 0.2486 0.2541 0.2711 -0.0428 0.0638  0.0333  26  GLU   A CG  
739  C CD  A GLU   A 26  ? 0.2846 0.3320 0.3454 -0.1016 0.0707  -0.0060 26  GLU   A CD  
740  C CD  B GLU   A 26  ? 0.2429 0.2419 0.2717 -0.0556 0.0954  0.0422  26  GLU   A CD  
741  O OE1 A GLU   A 26  ? 0.2901 0.3558 0.3628 -0.0818 0.0851  -0.0218 26  GLU   A OE1 
742  O OE1 B GLU   A 26  ? 0.2377 0.2436 0.2711 -0.0524 0.1150  0.0058  26  GLU   A OE1 
743  O OE2 A GLU   A 26  ? 0.2880 0.3263 0.3596 -0.1149 0.0622  -0.0077 26  GLU   A OE2 
744  O OE2 B GLU   A 26  ? 0.2352 0.2479 0.2671 -0.0475 0.1111  0.0538  26  GLU   A OE2 
757  N N   A ALA   A 27  ? 0.2029 0.2659 0.1537 -0.0823 0.0526  -0.0092 27  ALA   A N   
758  N N   B ALA   A 27  ? 0.2264 0.2612 0.1933 -0.0114 0.0466  0.0102  27  ALA   A N   
759  C CA  A ALA   A 27  ? 0.2063 0.2657 0.1489 -0.0736 0.0537  -0.0090 27  ALA   A CA  
760  C CA  B ALA   A 27  ? 0.2343 0.2639 0.1830 -0.0030 0.0398  0.0107  27  ALA   A CA  
761  C C   A ALA   A 27  ? 0.2285 0.2805 0.1575 -0.0761 0.0595  -0.0254 27  ALA   A C   
762  C C   B ALA   A 27  ? 0.2566 0.2806 0.1965 -0.0007 0.0375  -0.0034 27  ALA   A C   
763  O O   A ALA   A 27  ? 0.2386 0.2753 0.1610 -0.0763 0.0417  -0.0194 27  ALA   A O   
764  O O   B ALA   A 27  ? 0.2589 0.2775 0.1963 -0.0029 0.0329  -0.0015 27  ALA   A O   
765  C CB  A ALA   A 27  ? 0.1971 0.2534 0.1599 -0.0675 0.0449  -0.0094 27  ALA   A CB  
766  C CB  B ALA   A 27  ? 0.2260 0.2546 0.1745 -0.0019 0.0332  0.0135  27  ALA   A CB  
777  N N   A LYS   A 28  ? 0.2563 0.3037 0.1736 -0.0684 0.0648  -0.0534 28  LYS   A N   
778  N N   B LYS   A 28  ? 0.2819 0.2997 0.2168 0.0043  0.0314  -0.0221 28  LYS   A N   
779  C CA  A LYS   A 28  ? 0.2932 0.3344 0.2122 -0.0597 0.0658  -0.0688 28  LYS   A CA  
780  C CA  B LYS   A 28  ? 0.3107 0.3247 0.2494 0.0090  0.0290  -0.0353 28  LYS   A CA  
781  C C   A LYS   A 28  ? 0.3065 0.3603 0.2014 -0.0618 0.0845  -0.0546 28  LYS   A C   
782  C C   B LYS   A 28  ? 0.3311 0.3478 0.2593 0.0026  0.0413  -0.0285 28  LYS   A C   
783  O O   A LYS   A 28  ? 0.3106 0.3674 0.2391 -0.0604 0.0684  -0.0435 28  LYS   A O   
784  O O   B LYS   A 28  ? 0.3332 0.3520 0.2739 0.0042  0.0399  -0.0267 28  LYS   A O   
785  C CB  A LYS   A 28  ? 0.3163 0.3453 0.2694 -0.0455 0.0522  -0.0814 28  LYS   A CB  
786  C CB  B LYS   A 28  ? 0.3218 0.3297 0.2748 0.0183  0.0164  -0.0472 28  LYS   A CB  
787  C CG  A LYS   A 28  ? 0.3340 0.3546 0.3172 -0.0345 0.0428  -0.0879 28  LYS   A CG  
788  C CG  B LYS   A 28  ? 0.3332 0.3363 0.3051 0.0262  0.0065  -0.0528 28  LYS   A CG  
789  C CD  A LYS   A 28  ? 0.3481 0.3680 0.3740 -0.0254 0.0296  -0.0859 28  LYS   A CD  
790  C CD  B LYS   A 28  ? 0.3462 0.3467 0.3487 0.0315  -0.0035 -0.0545 28  LYS   A CD  
791  C CE  A LYS   A 28  ? 0.3597 0.3767 0.4064 -0.0201 0.0198  -0.0892 28  LYS   A CE  
792  C CE  B LYS   A 28  ? 0.3569 0.3543 0.3814 0.0339  -0.0094 -0.0582 28  LYS   A CE  
793  N NZ  A LYS   A 28  ? 0.3683 0.3820 0.4271 -0.0164 0.0182  -0.0905 28  LYS   A NZ  
794  N NZ  B LYS   A 28  ? 0.3635 0.3587 0.3981 0.0349  -0.0121 -0.0604 28  LYS   A NZ  
821  N N   A LYS   A 29  ? 0.3172 0.3805 0.1866 -0.0668 0.1030  -0.0398 29  LYS   A N   
822  N N   B LYS   A 29  ? 0.3478 0.3661 0.2706 -0.0080 0.0523  -0.0197 29  LYS   A N   
823  C CA  A LYS   A 29  ? 0.3365 0.4052 0.2114 -0.0678 0.1112  -0.0223 29  LYS   A CA  
824  C CA  B LYS   A 29  ? 0.3645 0.3836 0.2905 -0.0198 0.0542  -0.0149 29  LYS   A CA  
825  C C   A LYS   A 29  ? 0.3353 0.4002 0.1874 -0.0789 0.1037  -0.0189 29  LYS   A C   
826  C C   B LYS   A 29  ? 0.3637 0.3787 0.2660 -0.0399 0.0563  -0.0071 29  LYS   A C   
827  O O   A LYS   A 29  ? 0.3431 0.4073 0.1999 -0.0741 0.0909  -0.0238 29  LYS   A O   
828  O O   B LYS   A 29  ? 0.3669 0.3794 0.2685 -0.0425 0.0596  -0.0060 29  LYS   A O   
829  C CB  A LYS   A 29  ? 0.3517 0.4331 0.2697 -0.0588 0.1249  -0.0075 29  LYS   A CB  
830  C CB  B LYS   A 29  ? 0.3807 0.4039 0.3368 -0.0110 0.0482  -0.0203 29  LYS   A CB  
831  C CG  A LYS   A 29  ? 0.3672 0.4564 0.3365 -0.0506 0.1265  0.0030  29  LYS   A CG  
832  C CG  B LYS   A 29  ? 0.3969 0.4226 0.3852 -0.0027 0.0412  -0.0235 29  LYS   A CG  
833  C CD  A LYS   A 29  ? 0.3807 0.4762 0.4011 -0.0434 0.1253  0.0062  29  LYS   A CD  
834  C CD  B LYS   A 29  ? 0.4093 0.4372 0.4262 0.0040  0.0348  -0.0271 29  LYS   A CD  
835  C CE  A LYS   A 29  ? 0.3892 0.4897 0.4461 -0.0394 0.1242  0.0082  29  LYS   A CE  
836  C CE  B LYS   A 29  ? 0.4184 0.4487 0.4554 0.0085  0.0288  -0.0286 29  LYS   A CE  
837  N NZ  A LYS   A 29  ? 0.3946 0.4973 0.4722 -0.0369 0.1217  0.0073  29  LYS   A NZ  
838  N NZ  B LYS   A 29  ? 0.4232 0.4547 0.4688 0.0116  0.0255  -0.0303 29  LYS   A NZ  
865  N N   A VAL   A 30  ? 0.3226 0.3856 0.1730 -0.0935 0.1003  -0.0124 30  VAL   A N   
866  N N   B VAL   A 30  ? 0.3567 0.3707 0.2461 -0.0566 0.0556  0.0005  30  VAL   A N   
867  C CA  A VAL   A 30  ? 0.3199 0.3714 0.1805 -0.1040 0.0762  0.0091  30  VAL   A CA  
868  C CA  B VAL   A 30  ? 0.3506 0.3631 0.2260 -0.0719 0.0486  0.0108  30  VAL   A CA  
869  C C   A VAL   A 30  ? 0.3289 0.3593 0.1528 -0.0981 0.0615  0.0202  30  VAL   A C   
870  C C   B VAL   A 30  ? 0.3433 0.3556 0.1756 -0.0816 0.0465  0.0167  30  VAL   A C   
871  O O   A VAL   A 30  ? 0.3381 0.3625 0.1549 -0.0971 0.0573  0.0284  30  VAL   A O   
872  O O   B VAL   A 30  ? 0.3495 0.3581 0.1717 -0.0806 0.0422  0.0187  30  VAL   A O   
873  C CB  A VAL   A 30  ? 0.3093 0.3681 0.2291 -0.1167 0.0542  0.0153  30  VAL   A CB  
874  C CB  B VAL   A 30  ? 0.3491 0.3624 0.2558 -0.0781 0.0391  0.0120  30  VAL   A CB  
875  C CG1 A VAL   A 30  ? 0.3116 0.3672 0.2533 -0.1187 0.0391  0.0207  30  VAL   A CG1 
876  C CG1 B VAL   A 30  ? 0.3498 0.3617 0.2661 -0.0798 0.0344  0.0138  30  VAL   A CG1 
877  C CG2 A VAL   A 30  ? 0.3035 0.3697 0.2495 -0.1210 0.0595  0.0186  30  VAL   A CG2 
878  C CG2 B VAL   A 30  ? 0.3483 0.3630 0.2710 -0.0793 0.0405  0.0131  30  VAL   A CG2 
897  N N   . LYS   A 31  ? 0.3285 0.3440 0.1392 -0.0922 0.0435  0.0178  31  LYS   A N   
898  C CA  . LYS   A 31  ? 0.3480 0.3425 0.1474 -0.0838 0.0120  0.0178  31  LYS   A CA  
899  C C   . LYS   A 31  ? 0.3164 0.3143 0.1126 -0.0709 0.0078  0.0498  31  LYS   A C   
900  O O   . LYS   A 31  ? 0.3230 0.3226 0.1348 -0.0638 -0.0164 0.0626  31  LYS   A O   
901  C CB  . LYS   A 31  ? 0.4033 0.3727 0.2677 -0.0800 -0.0076 0.0026  31  LYS   A CB  
902  C CG  . LYS   A 31  ? 0.4521 0.4106 0.4190 -0.0704 -0.0244 -0.0059 31  LYS   A CG  
903  C CD  . LYS   A 31  ? 0.4926 0.4386 0.5363 -0.0628 -0.0392 -0.0132 31  LYS   A CD  
904  C CE  . LYS   A 31  ? 0.5226 0.4561 0.6106 -0.0572 -0.0528 -0.0207 31  LYS   A CE  
905  N NZ  . LYS   A 31  ? 0.5391 0.4683 0.6487 -0.0553 -0.0607 -0.0256 31  LYS   A NZ  
920  N N   . PRO   A 32  ? 0.2770 0.2785 0.1011 -0.0652 0.0071  0.0346  32  PRO   A N   
921  C CA  . PRO   A 32  ? 0.2701 0.2592 0.1431 -0.0641 0.0015  0.0406  32  PRO   A CA  
922  C C   . PRO   A 32  ? 0.2649 0.2539 0.1535 -0.0535 -0.0112 0.0452  32  PRO   A C   
923  O O   . PRO   A 32  ? 0.2580 0.2476 0.1601 -0.0564 -0.0299 0.0521  32  PRO   A O   
924  C CB  . PRO   A 32  ? 0.2625 0.2649 0.1493 -0.0609 -0.0039 0.0321  32  PRO   A CB  
925  C CG  . PRO   A 32  ? 0.2580 0.2665 0.1049 -0.0554 -0.0120 0.0258  32  PRO   A CG  
926  C CD  . PRO   A 32  ? 0.2612 0.2653 0.1050 -0.0607 -0.0046 0.0350  32  PRO   A CD  
934  N N   . THR   A 33  ? 0.2735 0.2481 0.1543 -0.0462 -0.0122 0.0511  33  THR   A N   
935  C CA  . THR   A 33  ? 0.2690 0.2463 0.1578 -0.0304 -0.0243 0.0513  33  THR   A CA  
936  C C   . THR   A 33  ? 0.2357 0.2236 0.1431 -0.0303 -0.0260 0.0425  33  THR   A C   
937  O O   . THR   A 33  ? 0.2263 0.2218 0.1549 -0.0288 -0.0362 0.0402  33  THR   A O   
938  C CB  . THR   A 33  ? 0.2926 0.2655 0.1672 -0.0183 -0.0343 0.0778  33  THR   A CB  
939  O OG1 . THR   A 33  ? 0.3114 0.2795 0.2072 -0.0078 -0.0224 0.0861  33  THR   A OG1 
940  C CG2 . THR   A 33  ? 0.2967 0.2753 0.2005 -0.0113 -0.0399 0.0763  33  THR   A CG2 
948  N N   . VAL   A 34  ? 0.2074 0.2094 0.1316 -0.0314 -0.0166 0.0412  34  VAL   A N   
949  C CA  . VAL   A 34  ? 0.1892 0.1933 0.1279 -0.0278 -0.0040 0.0394  34  VAL   A CA  
950  C C   . VAL   A 34  ? 0.1731 0.1818 0.1302 -0.0232 0.0035  0.0276  34  VAL   A C   
951  O O   . VAL   A 34  ? 0.1763 0.1830 0.1496 -0.0297 0.0066  0.0367  34  VAL   A O   
952  C CB  . VAL   A 34  ? 0.1958 0.1874 0.1520 -0.0228 -0.0061 0.0336  34  VAL   A CB  
953  C CG1 . VAL   A 34  ? 0.2009 0.1879 0.1505 -0.0260 0.0019  0.0239  34  VAL   A CG1 
954  C CG2 . VAL   A 34  ? 0.1963 0.1984 0.1901 -0.0114 -0.0219 0.0329  34  VAL   A CG2 
964  N N   . VAL   A 35  ? 0.1596 0.1679 0.1232 -0.0232 -0.0053 0.0242  35  VAL   A N   
965  C CA  . VAL   A 35  ? 0.1525 0.1610 0.1253 -0.0215 0.0025  0.0208  35  VAL   A CA  
966  C C   . VAL   A 35  ? 0.1456 0.1557 0.1283 -0.0158 0.0065  0.0225  35  VAL   A C   
967  O O   . VAL   A 35  ? 0.1406 0.1627 0.1393 -0.0195 0.0103  0.0165  35  VAL   A O   
968  C CB  . VAL   A 35  ? 0.1570 0.1717 0.1380 -0.0122 0.0091  0.0049  35  VAL   A CB  
969  C CG1 . VAL   A 35  ? 0.1724 0.1773 0.1434 -0.0050 0.0029  -0.0009 35  VAL   A CG1 
970  C CG2 . VAL   A 35  ? 0.1582 0.1790 0.1650 -0.0034 0.0126  0.0046  35  VAL   A CG2 
980  N N   . VAL   A 36  ? 0.1313 0.1509 0.1276 -0.0192 0.0050  0.0243  36  VAL   A N   
981  C CA  . VAL   A 36  ? 0.1236 0.1440 0.1176 -0.0090 0.0015  0.0202  36  VAL   A CA  
982  C C   . VAL   A 36  ? 0.1203 0.1419 0.1338 -0.0141 0.0081  0.0152  36  VAL   A C   
983  O O   . VAL   A 36  ? 0.1341 0.1423 0.1485 -0.0051 0.0180  0.0185  36  VAL   A O   
984  C CB  . VAL   A 36  ? 0.1350 0.1291 0.1366 -0.0101 0.0056  0.0130  36  VAL   A CB  
985  C CG1 . VAL   A 36  ? 0.1418 0.1303 0.1370 -0.0177 0.0028  0.0060  36  VAL   A CG1 
986  C CG2 . VAL   A 36  ? 0.1432 0.1368 0.1461 -0.0081 0.0054  0.0218  36  VAL   A CG2 
996  N N   . ASN   A 37  ? 0.1238 0.1319 0.1163 -0.0011 0.0020  0.0165  37  ASN   A N   
997  C CA  . ASN   A 37  ? 0.1244 0.1287 0.1200 0.0043  0.0059  0.0132  37  ASN   A CA  
998  C C   . ASN   A 37  ? 0.1293 0.1182 0.1302 0.0005  0.0145  0.0222  37  ASN   A C   
999  O O   . ASN   A 37  ? 0.1416 0.1327 0.1116 0.0061  0.0121  0.0101  37  ASN   A O   
1000 C CB  . ASN   A 37  ? 0.1267 0.1282 0.1261 0.0003  0.0048  0.0069  37  ASN   A CB  
1001 C CG  . ASN   A 37  ? 0.1275 0.1278 0.1328 0.0020  0.0087  0.0088  37  ASN   A CG  
1002 O OD1 . ASN   A 37  ? 0.1296 0.1307 0.1438 0.0006  0.0078  0.0181  37  ASN   A OD1 
1003 N ND2 . ASN   A 37  ? 0.1266 0.1310 0.1437 0.0003  -0.0034 0.0245  37  ASN   A ND2 
1010 N N   A ALA   A 38  ? 0.1288 0.1308 0.1256 0.0004  0.0153  0.0119  38  ALA   A N   
1011 N N   B ALA   A 38  ? 0.1315 0.1264 0.1398 0.0011  0.0110  0.0142  38  ALA   A N   
1012 C CA  A ALA   A 38  ? 0.1312 0.1315 0.1204 -0.0056 0.0055  0.0032  38  ALA   A CA  
1013 C CA  B ALA   A 38  ? 0.1382 0.1314 0.1530 -0.0016 -0.0007 0.0087  38  ALA   A CA  
1014 C C   A ALA   A 38  ? 0.1243 0.1338 0.1163 -0.0017 -0.0023 -0.0023 38  ALA   A C   
1015 C C   B ALA   A 38  ? 0.1331 0.1341 0.1380 0.0065  -0.0084 0.0046  38  ALA   A C   
1016 O O   A ALA   A 38  ? 0.1284 0.1239 0.1214 -0.0050 -0.0052 -0.0023 38  ALA   A O   
1017 O O   B ALA   A 38  ? 0.1299 0.1297 0.1387 0.0070  -0.0211 0.0081  38  ALA   A O   
1018 C CB  A ALA   A 38  ? 0.1340 0.1481 0.1324 -0.0125 0.0042  0.0031  38  ALA   A CB  
1019 C CB  B ALA   A 38  ? 0.1470 0.1373 0.1810 -0.0082 -0.0086 -0.0024 38  ALA   A CB  
1030 N N   A ALA   A 39  ? 0.1236 0.1337 0.1227 -0.0005 0.0008  0.0040  39  ALA   A N   
1031 N N   B ALA   A 39  ? 0.1395 0.1405 0.1456 0.0041  -0.0026 0.0177  39  ALA   A N   
1032 C CA  A ALA   A 39  ? 0.1187 0.1274 0.1228 0.0031  0.0098  0.0052  39  ALA   A CA  
1033 C CA  B ALA   A 39  ? 0.1447 0.1422 0.1464 -0.0013 0.0043  0.0231  39  ALA   A CA  
1034 C C   A ALA   A 39  ? 0.1275 0.1267 0.1237 -0.0027 0.0045  0.0054  39  ALA   A C   
1035 C C   B ALA   A 39  ? 0.1401 0.1345 0.1356 -0.0039 0.0073  0.0141  39  ALA   A C   
1036 O O   A ALA   A 39  ? 0.1448 0.1288 0.1236 -0.0065 0.0110  0.0008  39  ALA   A O   
1037 O O   B ALA   A 39  ? 0.1511 0.1363 0.1395 -0.0042 0.0129  0.0111  39  ALA   A O   
1038 C CB  A ALA   A 39  ? 0.1127 0.1280 0.1317 0.0067  -0.0037 -0.0121 39  ALA   A CB  
1039 C CB  B ALA   A 39  ? 0.1540 0.1509 0.1608 0.0031  0.0010  0.0157  39  ALA   A CB  
1050 N N   . ASN   A 40  ? 0.1425 0.1339 0.1307 -0.0109 0.0201  0.0065  40  ASN   A N   
1051 C CA  . ASN   A 40  ? 0.1508 0.1295 0.1362 0.0013  0.0126  0.0046  40  ASN   A CA  
1052 C C   . ASN   A 40  ? 0.1554 0.1229 0.1201 -0.0019 0.0240  0.0132  40  ASN   A C   
1053 O O   . ASN   A 40  ? 0.1480 0.1259 0.1293 -0.0038 0.0202  0.0180  40  ASN   A O   
1054 C CB  . ASN   A 40  ? 0.1611 0.1330 0.1553 0.0012  -0.0018 0.0039  40  ASN   A CB  
1055 C CG  . ASN   A 40  ? 0.1722 0.1335 0.1839 -0.0005 -0.0062 0.0038  40  ASN   A CG  
1056 O OD1 . ASN   A 40  ? 0.1770 0.1428 0.2005 0.0008  -0.0059 0.0036  40  ASN   A OD1 
1057 N ND2 . ASN   A 40  ? 0.1744 0.1416 0.2087 0.0056  -0.0008 -0.0058 40  ASN   A ND2 
1065 N N   . VAL   A 41  ? 0.1644 0.1337 0.1232 -0.0028 0.0292  0.0140  41  VAL   A N   
1066 C CA  . VAL   A 41  ? 0.1658 0.1389 0.1480 -0.0039 0.0336  0.0117  41  VAL   A CA  
1067 C C   . VAL   A 41  ? 0.1608 0.1349 0.1482 -0.0032 0.0378  0.0150  41  VAL   A C   
1068 O O   . VAL   A 41  ? 0.1621 0.1255 0.1737 0.0001  0.0335  -0.0003 41  VAL   A O   
1069 C CB  . VAL   A 41  ? 0.1857 0.1449 0.1565 -0.0164 0.0492  -0.0025 41  VAL   A CB  
1070 C CG1 . VAL   A 41  ? 0.1919 0.1526 0.1639 -0.0116 0.0489  -0.0130 41  VAL   A CG1 
1071 C CG2 . VAL   A 41  ? 0.2114 0.1557 0.1555 -0.0196 0.0572  0.0033  41  VAL   A CG2 
1081 N N   A TYR   A 42  ? 0.1452 0.1291 0.1652 -0.0041 0.0355  0.0186  42  TYR   A N   
1082 N N   B TYR   A 42  ? 0.1504 0.1332 0.1574 -0.0058 0.0318  0.0194  42  TYR   A N   
1083 C CA  A TYR   A 42  ? 0.1460 0.1225 0.1612 -0.0073 0.0354  0.0228  42  TYR   A CA  
1084 C CA  B TYR   A 42  ? 0.1503 0.1310 0.1555 -0.0091 0.0293  0.0241  42  TYR   A CA  
1085 C C   A TYR   A 42  ? 0.1416 0.1221 0.1671 -0.0059 0.0241  0.0237  42  TYR   A C   
1086 C C   B TYR   A 42  ? 0.1458 0.1283 0.1579 -0.0065 0.0194  0.0243  42  TYR   A C   
1087 O O   A TYR   A 42  ? 0.1369 0.1190 0.1993 -0.0142 0.0250  0.0008  42  TYR   A O   
1088 O O   B TYR   A 42  ? 0.1437 0.1302 0.1787 -0.0099 0.0153  0.0132  42  TYR   A O   
1089 C CB  A TYR   A 42  ? 0.1628 0.1330 0.1661 -0.0034 0.0243  0.0196  42  TYR   A CB  
1090 C CB  B TYR   A 42  ? 0.1597 0.1426 0.1583 -0.0074 0.0262  0.0208  42  TYR   A CB  
1091 C CG  A TYR   A 42  ? 0.1710 0.1525 0.1660 0.0041  0.0109  0.0274  42  TYR   A CG  
1092 C CG  B TYR   A 42  ? 0.1608 0.1541 0.1582 -0.0054 0.0224  0.0248  42  TYR   A CG  
1093 C CD1 A TYR   A 42  ? 0.1741 0.1605 0.1798 -0.0036 0.0122  0.0312  42  TYR   A CD1 
1094 C CD1 B TYR   A 42  ? 0.1628 0.1648 0.1657 -0.0043 0.0221  0.0214  42  TYR   A CD1 
1095 C CD2 A TYR   A 42  ? 0.1795 0.1752 0.1878 0.0112  0.0086  0.0173  42  TYR   A CD2 
1096 C CD2 B TYR   A 42  ? 0.1523 0.1618 0.1648 0.0001  0.0208  0.0220  42  TYR   A CD2 
1097 C CE1 A TYR   A 42  ? 0.1740 0.1714 0.1803 -0.0046 0.0189  0.0282  42  TYR   A CE1 
1098 C CE1 B TYR   A 42  ? 0.1537 0.1679 0.1560 -0.0019 0.0304  0.0208  42  TYR   A CE1 
1099 C CE2 A TYR   A 42  ? 0.1846 0.1866 0.1967 0.0094  0.0080  0.0174  42  TYR   A CE2 
1100 C CE2 B TYR   A 42  ? 0.1458 0.1655 0.1679 -0.0043 0.0205  0.0266  42  TYR   A CE2 
1101 C CZ  A TYR   A 42  ? 0.1798 0.1889 0.1886 0.0028  0.0180  0.0234  42  TYR   A CZ  
1102 C CZ  B TYR   A 42  ? 0.1480 0.1675 0.1471 -0.0017 0.0298  0.0300  42  TYR   A CZ  
1103 O OH  A TYR   A 42  ? 0.1739 0.2097 0.2167 -0.0048 0.0187  0.0090  42  TYR   A OH  
1104 O OH  B TYR   A 42  ? 0.1502 0.1728 0.1556 0.0060  0.0261  0.0240  42  TYR   A OH  
1123 N N   . LEU   A 43  ? 0.1439 0.1236 0.1529 -0.0076 0.0132  0.0106  43  LEU   A N   
1124 C CA  . LEU   A 43  ? 0.1345 0.1228 0.1514 -0.0084 0.0152  0.0054  43  LEU   A CA  
1125 C C   . LEU   A 43  ? 0.1336 0.1280 0.1511 -0.0000 0.0106  0.0072  43  LEU   A C   
1126 O O   . LEU   A 43  ? 0.1514 0.1341 0.1711 0.0032  -0.0005 0.0053  43  LEU   A O   
1127 C CB  . LEU   A 43  ? 0.1415 0.1251 0.1561 -0.0113 0.0184  0.0051  43  LEU   A CB  
1128 C CG  . LEU   A 43  ? 0.1445 0.1240 0.1609 -0.0023 0.0041  0.0063  43  LEU   A CG  
1129 C CD1 . LEU   A 43  ? 0.1546 0.1409 0.1849 -0.0014 -0.0005 0.0100  43  LEU   A CD1 
1130 C CD2 . LEU   A 43  ? 0.1584 0.1368 0.1624 -0.0050 0.0052  0.0192  43  LEU   A CD2 
1143 N N   . LYS   A 44  ? 0.1357 0.1312 0.1493 -0.0036 0.0094  0.0080  44  LYS   A N   
1144 C CA  . LYS   A 44  ? 0.1570 0.1391 0.1511 -0.0008 0.0194  0.0199  44  LYS   A CA  
1145 C C   . LYS   A 44  ? 0.1410 0.1276 0.1349 0.0015  0.0024  0.0138  44  LYS   A C   
1146 O O   . LYS   A 44  ? 0.1490 0.1476 0.1494 0.0026  0.0049  -0.0045 44  LYS   A O   
1147 C CB  . LYS   A 44  ? 0.1900 0.1515 0.1856 -0.0047 0.0328  0.0257  44  LYS   A CB  
1148 C CG  . LYS   A 44  ? 0.2293 0.1917 0.2588 -0.0172 0.0569  0.0369  44  LYS   A CG  
1149 C CD  . LYS   A 44  ? 0.2720 0.2562 0.3823 -0.0226 0.0401  0.0339  44  LYS   A CD  
1150 C CE  . LYS   A 44  ? 0.2907 0.2922 0.4681 -0.0256 0.0288  0.0343  44  LYS   A CE  
1151 N NZ  . LYS   A 44  ? 0.3031 0.3134 0.5081 -0.0296 0.0305  0.0387  44  LYS   A NZ  
1165 N N   A HIS   A 45  ? 0.1302 0.1279 0.1382 0.0038  0.0057  0.0183  45  HIS   A N   
1166 N N   B HIS   A 45  ? 0.1370 0.1341 0.1471 0.0003  -0.0033 0.0143  45  HIS   A N   
1167 C CA  A HIS   A 45  ? 0.1277 0.1281 0.1373 0.0047  0.0063  0.0087  45  HIS   A CA  
1168 C CA  B HIS   A 45  ? 0.1377 0.1382 0.1544 -0.0013 -0.0105 0.0072  45  HIS   A CA  
1169 C C   A HIS   A 45  ? 0.1323 0.1399 0.1414 0.0063  0.0136  0.0221  45  HIS   A C   
1170 C C   B HIS   A 45  ? 0.1441 0.1484 0.1637 0.0012  -0.0097 0.0107  45  HIS   A C   
1171 O O   A HIS   A 45  ? 0.1366 0.1294 0.1589 0.0034  0.0082  0.0096  45  HIS   A O   
1172 O O   B HIS   A 45  ? 0.1447 0.1493 0.1819 0.0126  0.0009  0.0112  45  HIS   A O   
1173 C CB  A HIS   A 45  ? 0.1288 0.1256 0.1347 0.0053  0.0035  -0.0001 45  HIS   A CB  
1174 C CB  B HIS   A 45  ? 0.1325 0.1351 0.1480 -0.0005 -0.0099 0.0027  45  HIS   A CB  
1175 C CG  A HIS   A 45  ? 0.1319 0.1148 0.1213 -0.0011 0.0080  0.0031  45  HIS   A CG  
1176 C CG  B HIS   A 45  ? 0.1268 0.1333 0.1381 -0.0021 0.0024  0.0031  45  HIS   A CG  
1177 N ND1 A HIS   A 45  ? 0.1304 0.1226 0.1252 0.0002  0.0047  0.0059  45  HIS   A ND1 
1178 N ND1 B HIS   A 45  ? 0.1254 0.1379 0.1580 -0.0003 0.0030  0.0095  45  HIS   A ND1 
1179 C CD2 A HIS   A 45  ? 0.1379 0.1270 0.1501 -0.0060 0.0103  0.0121  45  HIS   A CD2 
1180 C CD2 B HIS   A 45  ? 0.1208 0.1292 0.1222 -0.0048 0.0009  -0.0020 45  HIS   A CD2 
1181 C CE1 A HIS   A 45  ? 0.1343 0.1354 0.1373 -0.0040 -0.0007 0.0178  45  HIS   A CE1 
1182 C CE1 B HIS   A 45  ? 0.1187 0.1257 0.1249 -0.0024 -0.0004 -0.0132 45  HIS   A CE1 
1183 N NE2 A HIS   A 45  ? 0.1377 0.1318 0.1461 0.0011  0.0104  0.0198  45  HIS   A NE2 
1184 N NE2 B HIS   A 45  ? 0.1159 0.1261 0.1043 -0.0058 -0.0028 -0.0101 45  HIS   A NE2 
1199 N N   A GLY   A 46  ? 0.1360 0.1547 0.1745 0.0161  0.0012  0.0321  46  GLY   A N   
1200 N N   B GLY   A 46  ? 0.1513 0.1523 0.1614 -0.0051 -0.0216 0.0112  46  GLY   A N   
1201 C CA  A GLY   A 46  ? 0.1410 0.1598 0.2019 0.0143  -0.0020 0.0453  46  GLY   A CA  
1202 C CA  B GLY   A 46  ? 0.1472 0.1557 0.1595 -0.0030 -0.0169 0.0127  46  GLY   A CA  
1203 C C   A GLY   A 46  ? 0.1512 0.1514 0.1990 0.0176  -0.0040 0.0558  46  GLY   A C   
1204 C C   B GLY   A 46  ? 0.1444 0.1451 0.1436 0.0088  -0.0024 0.0220  46  GLY   A C   
1205 O O   A GLY   A 46  ? 0.1600 0.1516 0.2006 0.0207  -0.0112 0.0602  46  GLY   A O   
1206 O O   B GLY   A 46  ? 0.1520 0.1465 0.1508 0.0070  -0.0027 0.0134  46  GLY   A O   
1213 N N   A GLY   A 47  ? 0.1434 0.1539 0.1854 0.0074  -0.0056 0.0399  47  GLY   A N   
1214 N N   B GLY   A 47  ? 0.1425 0.1443 0.1370 0.0169  -0.0045 0.0145  47  GLY   A N   
1215 C CA  A GLY   A 47  ? 0.1468 0.1588 0.1790 0.0099  -0.0070 0.0303  47  GLY   A CA  
1216 C CA  B GLY   A 47  ? 0.1406 0.1476 0.1429 0.0127  -0.0122 0.0168  47  GLY   A CA  
1217 C C   A GLY   A 47  ? 0.1408 0.1503 0.1679 0.0111  -0.0147 0.0181  47  GLY   A C   
1218 C C   B GLY   A 47  ? 0.1328 0.1427 0.1180 0.0138  -0.0197 0.0062  47  GLY   A C   
1219 O O   A GLY   A 47  ? 0.1477 0.1492 0.2031 0.0185  -0.0109 0.0164  47  GLY   A O   
1220 O O   B GLY   A 47  ? 0.1276 0.1399 0.1086 0.0152  -0.0169 0.0204  47  GLY   A O   
1227 N N   A GLY   A 48  ? 0.1385 0.1552 0.1587 0.0142  -0.0148 0.0095  48  GLY   A N   
1228 N N   B GLY   A 48  ? 0.1342 0.1448 0.1378 0.0113  -0.0084 0.0054  48  GLY   A N   
1229 C CA  A GLY   A 48  ? 0.1453 0.1497 0.1800 0.0068  -0.0114 0.0084  48  GLY   A CA  
1230 C CA  B GLY   A 48  ? 0.1392 0.1414 0.1273 0.0064  -0.0018 -0.0120 48  GLY   A CA  
1231 C C   A GLY   A 48  ? 0.1401 0.1432 0.1649 0.0028  0.0023  0.0082  48  GLY   A C   
1232 C C   B GLY   A 48  ? 0.1419 0.1402 0.1119 0.0032  0.0059  -0.0082 48  GLY   A C   
1233 O O   A GLY   A 48  ? 0.1458 0.1385 0.1691 0.0019  0.0027  0.0039  48  GLY   A O   
1234 O O   B GLY   A 48  ? 0.1486 0.1390 0.0957 -0.0064 0.0164  -0.0065 48  GLY   A O   
1241 N N   A VAL   A 49  ? 0.1366 0.1328 0.1828 -0.0005 -0.0147 0.0058  49  VAL   A N   
1242 N N   B VAL   A 49  ? 0.1370 0.1340 0.1226 0.0012  -0.0084 -0.0102 49  VAL   A N   
1243 C CA  A VAL   A 49  ? 0.1453 0.1279 0.1704 -0.0063 -0.0011 0.0073  49  VAL   A CA  
1244 C CA  B VAL   A 49  ? 0.1300 0.1402 0.1328 0.0030  0.0050  -0.0046 49  VAL   A CA  
1245 C C   A VAL   A 49  ? 0.1421 0.1218 0.1538 -0.0058 -0.0026 0.0150  49  VAL   A C   
1246 C C   B VAL   A 49  ? 0.1300 0.1347 0.1126 0.0109  0.0144  -0.0202 49  VAL   A C   
1247 O O   A VAL   A 49  ? 0.1450 0.1297 0.1758 -0.0216 0.0022  0.0087  49  VAL   A O   
1248 O O   B VAL   A 49  ? 0.1328 0.1427 0.0928 0.0126  0.0140  -0.0130 49  VAL   A O   
1249 C CB  A VAL   A 49  ? 0.1556 0.1267 0.1952 -0.0099 -0.0043 0.0011  49  VAL   A CB  
1250 C CB  B VAL   A 49  ? 0.1249 0.1368 0.1604 0.0084  0.0051  0.0069  49  VAL   A CB  
1251 C CG1 A VAL   A 49  ? 0.1673 0.1268 0.2133 -0.0095 0.0037  0.0122  49  VAL   A CG1 
1252 C CG1 B VAL   A 49  ? 0.1098 0.1308 0.1533 0.0190  0.0076  0.0176  49  VAL   A CG1 
1253 C CG2 A VAL   A 49  ? 0.1596 0.1338 0.2272 -0.0189 -0.0050 -0.0037 49  VAL   A CG2 
1254 C CG2 B VAL   A 49  ? 0.1315 0.1312 0.1826 0.0065  0.0004  0.0132  49  VAL   A CG2 
1273 N N   A ALA   A 50  ? 0.1379 0.1218 0.1430 -0.0132 -0.0162 0.0245  50  ALA   A N   
1274 N N   B ALA   A 50  ? 0.1313 0.1260 0.1198 0.0092  0.0092  -0.0160 50  ALA   A N   
1275 C CA  A ALA   A 50  ? 0.1312 0.1314 0.1401 -0.0167 -0.0137 0.0249  50  ALA   A CA  
1276 C CA  B ALA   A 50  ? 0.1301 0.1273 0.1150 0.0103  0.0034  -0.0123 50  ALA   A CA  
1277 C C   A ALA   A 50  ? 0.1274 0.1334 0.1477 -0.0135 -0.0132 0.0163  50  ALA   A C   
1278 C C   B ALA   A 50  ? 0.1247 0.1247 0.1009 0.0142  0.0025  -0.0191 50  ALA   A C   
1279 O O   A ALA   A 50  ? 0.1336 0.1403 0.1662 -0.0071 -0.0145 0.0142  50  ALA   A O   
1280 O O   B ALA   A 50  ? 0.1267 0.1269 0.1012 0.0197  0.0013  -0.0127 50  ALA   A O   
1281 C CB  A ALA   A 50  ? 0.1284 0.1330 0.1375 -0.0225 -0.0117 0.0168  50  ALA   A CB  
1282 C CB  B ALA   A 50  ? 0.1316 0.1224 0.1065 0.0107  0.0119  -0.0174 50  ALA   A CB  
1293 N N   A GLY   A 51  ? 0.1304 0.1226 0.1650 -0.0045 -0.0118 0.0212  51  GLY   A N   
1294 N N   B GLY   A 51  ? 0.1236 0.1227 0.1234 0.0205  -0.0014 -0.0216 51  GLY   A N   
1295 C CA  A GLY   A 51  ? 0.1422 0.1227 0.1742 -0.0040 -0.0187 0.0157  51  GLY   A CA  
1296 C CA  B GLY   A 51  ? 0.1237 0.1190 0.1244 0.0140  -0.0115 -0.0169 51  GLY   A CA  
1297 C C   A GLY   A 51  ? 0.1410 0.1321 0.1722 -0.0024 -0.0111 0.0013  51  GLY   A C   
1298 C C   B GLY   A 51  ? 0.1243 0.1280 0.1253 0.0134  -0.0022 -0.0111 51  GLY   A C   
1299 O O   A GLY   A 51  ? 0.1485 0.1403 0.1866 -0.0003 -0.0111 -0.0087 51  GLY   A O   
1300 O O   B GLY   A 51  ? 0.1256 0.1333 0.1369 0.0113  -0.0017 -0.0098 51  GLY   A O   
1307 N N   A ALA   A 52  ? 0.1386 0.1461 0.1536 -0.0044 -0.0085 -0.0012 52  ALA   A N   
1308 N N   B ALA   A 52  ? 0.1279 0.1356 0.1188 0.0122  0.0048  -0.0137 52  ALA   A N   
1309 C CA  A ALA   A 52  ? 0.1342 0.1594 0.1586 -0.0084 -0.0068 -0.0016 52  ALA   A CA  
1310 C CA  B ALA   A 52  ? 0.1240 0.1484 0.1416 0.0104  0.0071  -0.0097 52  ALA   A CA  
1311 C C   A ALA   A 52  ? 0.1277 0.1557 0.1255 -0.0162 -0.0030 -0.0080 52  ALA   A C   
1312 C C   B ALA   A 52  ? 0.1207 0.1493 0.1181 0.0045  0.0107  -0.0058 52  ALA   A C   
1313 O O   A ALA   A 52  ? 0.1409 0.1575 0.1418 -0.0128 0.0049  -0.0184 52  ALA   A O   
1314 O O   B ALA   A 52  ? 0.1337 0.1589 0.1345 0.0026  0.0055  -0.0051 52  ALA   A O   
1315 C CB  A ALA   A 52  ? 0.1413 0.1855 0.1786 -0.0168 -0.0082 -0.0063 52  ALA   A CB  
1316 C CB  B ALA   A 52  ? 0.1284 0.1660 0.1582 0.0021  0.0120  -0.0116 52  ALA   A CB  
1327 N N   A LEU   A 53  ? 0.1287 0.1545 0.1399 -0.0072 -0.0021 -0.0034 53  LEU   A N   
1328 N N   B LEU   A 53  ? 0.1194 0.1422 0.1316 0.0036  0.0104  -0.0093 53  LEU   A N   
1329 C CA  A LEU   A 53  ? 0.1371 0.1548 0.1295 -0.0061 0.0048  0.0077  53  LEU   A CA  
1330 C CA  B LEU   A 53  ? 0.1262 0.1441 0.1239 0.0005  0.0097  -0.0046 53  LEU   A CA  
1331 C C   A LEU   A 53  ? 0.1398 0.1522 0.1183 0.0037  0.0088  0.0017  53  LEU   A C   
1332 C C   B LEU   A 53  ? 0.1302 0.1429 0.1021 0.0066  0.0126  -0.0033 53  LEU   A C   
1333 O O   A LEU   A 53  ? 0.1536 0.1520 0.1397 -0.0070 0.0033  0.0037  53  LEU   A O   
1334 O O   B LEU   A 53  ? 0.1469 0.1399 0.1039 0.0042  0.0032  -0.0013 53  LEU   A O   
1335 C CB  A LEU   A 53  ? 0.1482 0.1576 0.1311 -0.0017 0.0029  0.0111  53  LEU   A CB  
1336 C CB  B LEU   A 53  ? 0.1276 0.1469 0.1315 -0.0026 0.0015  -0.0010 53  LEU   A CB  
1337 C CG  A LEU   A 53  ? 0.1471 0.1523 0.1448 -0.0149 0.0009  0.0127  53  LEU   A CG  
1338 C CG  B LEU   A 53  ? 0.1257 0.1493 0.1385 -0.0063 0.0021  -0.0003 53  LEU   A CG  
1339 C CD1 A LEU   A 53  ? 0.1394 0.1575 0.1523 -0.0098 -0.0029 0.0174  53  LEU   A CD1 
1340 C CD1 B LEU   A 53  ? 0.1274 0.1502 0.1441 -0.0102 0.0132  -0.0012 53  LEU   A CD1 
1341 C CD2 A LEU   A 53  ? 0.1527 0.1701 0.1518 -0.0184 0.0008  0.0117  53  LEU   A CD2 
1342 C CD2 B LEU   A 53  ? 0.1208 0.1529 0.1358 -0.0150 -0.0041 -0.0024 53  LEU   A CD2 
1365 N N   A ASN   A 54  ? 0.1337 0.1457 0.1277 -0.0012 -0.0010 0.0026  54  ASN   A N   
1366 N N   B ASN   A 54  ? 0.1230 0.1467 0.1131 0.0054  0.0060  -0.0039 54  ASN   A N   
1367 C CA  A ASN   A 54  ? 0.1251 0.1348 0.1346 -0.0062 -0.0051 0.0011  54  ASN   A CA  
1368 C CA  B ASN   A 54  ? 0.1175 0.1448 0.1187 0.0036  0.0023  -0.0084 54  ASN   A CA  
1369 C C   A ASN   A 54  ? 0.1374 0.1433 0.1329 -0.0092 0.0010  -0.0010 54  ASN   A C   
1370 C C   B ASN   A 54  ? 0.1308 0.1472 0.1325 -0.0010 0.0002  -0.0038 54  ASN   A C   
1371 O O   A ASN   A 54  ? 0.1388 0.1460 0.1376 -0.0083 0.0004  -0.0113 54  ASN   A O   
1372 O O   B ASN   A 54  ? 0.1312 0.1449 0.1506 0.0031  -0.0096 -0.0041 54  ASN   A O   
1373 C CB  A ASN   A 54  ? 0.1234 0.1304 0.1590 -0.0126 -0.0142 0.0013  54  ASN   A CB  
1374 C CB  B ASN   A 54  ? 0.1197 0.1477 0.1279 0.0112  0.0040  -0.0103 54  ASN   A CB  
1375 C CG  A ASN   A 54  ? 0.1271 0.1279 0.1564 -0.0035 -0.0119 0.0102  54  ASN   A CG  
1376 C CG  B ASN   A 54  ? 0.1228 0.1434 0.1242 0.0179  0.0063  -0.0109 54  ASN   A CG  
1377 O OD1 A ASN   A 54  ? 0.1281 0.1188 0.1576 -0.0059 -0.0136 0.0226  54  ASN   A OD1 
1378 O OD1 B ASN   A 54  ? 0.1222 0.1363 0.1287 0.0121  0.0072  -0.0156 54  ASN   A OD1 
1379 N ND2 A ASN   A 54  ? 0.1253 0.1352 0.1732 -0.0060 -0.0237 0.0132  54  ASN   A ND2 
1380 N ND2 B ASN   A 54  ? 0.1314 0.1472 0.1435 0.0159  -0.0042 -0.0066 54  ASN   A ND2 
1393 N N   . LYS   A 55  ? 0.1345 0.1474 0.1409 -0.0004 -0.0013 -0.0113 55  LYS   A N   
1394 C CA  . LYS   A 55  ? 0.1459 0.1582 0.1443 0.0064  -0.0080 -0.0156 55  LYS   A CA  
1395 C C   . LYS   A 55  ? 0.1415 0.1648 0.1392 0.0029  0.0005  -0.0229 55  LYS   A C   
1396 O O   . LYS   A 55  ? 0.1522 0.1723 0.1531 0.0063  -0.0013 -0.0306 55  LYS   A O   
1397 C CB  . LYS   A 55  ? 0.1468 0.1602 0.1628 0.0218  -0.0025 -0.0136 55  LYS   A CB  
1398 C CG  . LYS   A 55  ? 0.1663 0.1895 0.1827 0.0272  -0.0130 -0.0210 55  LYS   A CG  
1399 C CD  . LYS   A 55  ? 0.1771 0.2163 0.1966 0.0440  -0.0098 -0.0254 55  LYS   A CD  
1400 C CE  . LYS   A 55  ? 0.2003 0.2461 0.2079 0.0504  -0.0228 -0.0312 55  LYS   A CE  
1401 N NZ  . LYS   A 55  ? 0.2024 0.2612 0.2231 0.0534  -0.0243 -0.0265 55  LYS   A NZ  
1416 N N   . ALA   A 56  ? 0.1431 0.1741 0.1470 -0.0024 0.0104  -0.0230 56  ALA   A N   
1417 C CA  . ALA   A 56  ? 0.1599 0.1937 0.1547 -0.0110 0.0051  -0.0250 56  ALA   A CA  
1418 C C   . ALA   A 56  ? 0.1596 0.2010 0.1363 -0.0114 0.0052  -0.0324 56  ALA   A C   
1419 O O   . ALA   A 56  ? 0.1629 0.2354 0.1470 0.0049  0.0092  -0.0243 56  ALA   A O   
1420 C CB  . ALA   A 56  ? 0.1624 0.2115 0.1654 -0.0183 0.0049  -0.0136 56  ALA   A CB  
1426 N N   . THR   A 57  ? 0.1445 0.1762 0.1388 -0.0055 0.0095  -0.0203 57  THR   A N   
1427 C CA  . THR   A 57  ? 0.1466 0.1705 0.1377 -0.0072 0.0021  -0.0153 57  THR   A CA  
1428 C C   . THR   A 57  ? 0.1495 0.1772 0.1535 -0.0023 -0.0004 -0.0246 57  THR   A C   
1429 O O   . THR   A 57  ? 0.1418 0.1836 0.1668 -0.0098 -0.0064 -0.0319 57  THR   A O   
1430 C CB  . THR   A 57  ? 0.1486 0.1712 0.1355 -0.0035 0.0037  -0.0092 57  THR   A CB  
1431 O OG1 . THR   A 57  ? 0.1357 0.1664 0.1395 -0.0036 0.0030  -0.0132 57  THR   A OG1 
1432 C CG2 . THR   A 57  ? 0.1452 0.1769 0.1336 -0.0065 -0.0017 -0.0033 57  THR   A CG2 
1440 N N   . ASN   A 58  ? 0.1501 0.1777 0.1649 -0.0033 0.0078  -0.0336 58  ASN   A N   
1441 C CA  . ASN   A 58  ? 0.1715 0.1695 0.1784 -0.0085 0.0105  -0.0406 58  ASN   A CA  
1442 C C   . ASN   A 58  ? 0.1539 0.1593 0.1684 -0.0011 0.0031  -0.0229 58  ASN   A C   
1443 O O   . ASN   A 58  ? 0.1540 0.1721 0.1835 -0.0124 -0.0016 -0.0318 58  ASN   A O   
1444 C CB  . ASN   A 58  ? 0.2150 0.1881 0.2105 -0.0178 0.0351  -0.0518 58  ASN   A CB  
1445 C CG  . ASN   A 58  ? 0.2528 0.2146 0.2716 -0.0125 0.0282  -0.0481 58  ASN   A CG  
1446 O OD1 . ASN   A 58  ? 0.2772 0.2095 0.3073 0.0263  0.0526  -0.0460 58  ASN   A OD1 
1447 N ND2 . ASN   A 58  ? 0.2619 0.2217 0.3008 -0.0181 0.0116  -0.0539 58  ASN   A ND2 
1454 N N   . ASN   A 59  ? 0.1372 0.1489 0.1583 -0.0026 -0.0048 -0.0148 59  ASN   A N   
1455 C CA  . ASN   A 59  ? 0.1424 0.1383 0.1607 -0.0062 -0.0036 -0.0125 59  ASN   A CA  
1456 C C   . ASN   A 59  ? 0.1365 0.1408 0.1532 -0.0040 -0.0099 -0.0065 59  ASN   A C   
1457 O O   . ASN   A 59  ? 0.1331 0.1466 0.1595 -0.0050 -0.0025 0.0012  59  ASN   A O   
1458 C CB  . ASN   A 59  ? 0.1502 0.1364 0.1657 0.0000  -0.0151 -0.0196 59  ASN   A CB  
1459 C CG  . ASN   A 59  ? 0.1509 0.1401 0.1658 -0.0028 -0.0248 -0.0013 59  ASN   A CG  
1460 O OD1 . ASN   A 59  ? 0.1616 0.1481 0.1644 -0.0116 -0.0231 0.0014  59  ASN   A OD1 
1461 N ND2 . ASN   A 59  ? 0.1557 0.1485 0.1858 -0.0092 -0.0146 0.0018  59  ASN   A ND2 
1468 N N   . ALA   A 60  ? 0.1309 0.1481 0.1449 -0.0024 -0.0056 -0.0063 60  ALA   A N   
1469 C CA  . ALA   A 60  ? 0.1344 0.1509 0.1519 -0.0014 -0.0100 -0.0095 60  ALA   A CA  
1470 C C   . ALA   A 60  ? 0.1321 0.1457 0.1541 0.0033  -0.0067 -0.0064 60  ALA   A C   
1471 O O   . ALA   A 60  ? 0.1292 0.1463 0.1789 0.0011  -0.0112 -0.0128 60  ALA   A O   
1472 C CB  . ALA   A 60  ? 0.1465 0.1610 0.1504 0.0009  -0.0149 -0.0266 60  ALA   A CB  
1478 N N   . MET   A 61  ? 0.1272 0.1399 0.1523 -0.0061 -0.0064 -0.0074 61  MET   A N   
1479 C CA  . MET   A 61  ? 0.1338 0.1309 0.1473 -0.0088 -0.0024 0.0018  61  MET   A CA  
1480 C C   . MET   A 61  ? 0.1261 0.1268 0.1514 -0.0062 -0.0051 -0.0054 61  MET   A C   
1481 O O   . MET   A 61  ? 0.1318 0.1273 0.1619 -0.0033 0.0049  0.0041  61  MET   A O   
1482 C CB  . MET   A 61  ? 0.1323 0.1361 0.1438 -0.0055 0.0002  -0.0026 61  MET   A CB  
1483 C CG  . MET   A 61  ? 0.1328 0.1474 0.1588 -0.0013 -0.0052 0.0015  61  MET   A CG  
1484 S SD  . MET   A 61  ? 0.1374 0.1428 0.1859 -0.0091 0.0014  -0.0166 61  MET   A SD  
1485 C CE  . MET   A 61  ? 0.1586 0.1617 0.2096 -0.0097 0.0138  -0.0158 61  MET   A CE  
1495 N N   . GLN   A 62  ? 0.1284 0.1286 0.1484 -0.0045 0.0034  -0.0014 62  GLN   A N   
1496 C CA  . GLN   A 62  ? 0.1333 0.1280 0.1614 -0.0022 0.0024  -0.0005 62  GLN   A CA  
1497 C C   . GLN   A 62  ? 0.1318 0.1156 0.1740 0.0020  0.0085  0.0032  62  GLN   A C   
1498 O O   . GLN   A 62  ? 0.1357 0.1321 0.1657 -0.0035 0.0070  -0.0008 62  GLN   A O   
1499 C CB  . GLN   A 62  ? 0.1333 0.1193 0.1662 -0.0017 -0.0026 0.0001  62  GLN   A CB  
1500 C CG  . GLN   A 62  ? 0.1362 0.1171 0.1599 -0.0033 -0.0075 0.0102  62  GLN   A CG  
1501 C CD  . GLN   A 62  ? 0.1464 0.1271 0.1516 -0.0042 0.0025  0.0086  62  GLN   A CD  
1502 O OE1 . GLN   A 62  ? 0.1503 0.1383 0.1666 -0.0069 -0.0070 0.0033  62  GLN   A OE1 
1503 N NE2 . GLN   A 62  ? 0.1524 0.1343 0.1688 0.0005  -0.0062 -0.0059 62  GLN   A NE2 
1512 N N   . VAL   A 63  ? 0.1267 0.1240 0.1818 -0.0038 0.0050  -0.0151 63  VAL   A N   
1513 C CA  . VAL   A 63  ? 0.1337 0.1380 0.2008 -0.0111 -0.0051 -0.0145 63  VAL   A CA  
1514 C C   . VAL   A 63  ? 0.1247 0.1390 0.1842 -0.0136 -0.0087 -0.0180 63  VAL   A C   
1515 O O   . VAL   A 63  ? 0.1244 0.1367 0.2048 -0.0114 -0.0005 -0.0092 63  VAL   A O   
1516 C CB  . VAL   A 63  ? 0.1481 0.1512 0.2234 -0.0100 -0.0088 -0.0379 63  VAL   A CB  
1517 C CG1 . VAL   A 63  ? 0.1594 0.1717 0.2589 -0.0103 -0.0108 -0.0615 63  VAL   A CG1 
1518 C CG2 . VAL   A 63  ? 0.1579 0.1484 0.2329 -0.0074 0.0102  -0.0345 63  VAL   A CG2 
1528 N N   . GLU   A 64  ? 0.1272 0.1429 0.1786 0.0003  -0.0009 -0.0126 64  GLU   A N   
1529 C CA  . GLU   A 64  ? 0.1280 0.1416 0.1773 -0.0046 -0.0011 -0.0040 64  GLU   A CA  
1530 C C   . GLU   A 64  ? 0.1225 0.1358 0.1703 -0.0063 0.0083  -0.0029 64  GLU   A C   
1531 O O   . GLU   A 64  ? 0.1310 0.1409 0.1734 0.0019  0.0017  -0.0010 64  GLU   A O   
1532 C CB  . GLU   A 64  ? 0.1393 0.1540 0.1801 -0.0011 0.0025  -0.0041 64  GLU   A CB  
1533 C CG  . GLU   A 64  ? 0.1439 0.1577 0.1832 -0.0041 0.0014  0.0057  64  GLU   A CG  
1534 C CD  . GLU   A 64  ? 0.1596 0.1682 0.1828 -0.0122 0.0096  0.0030  64  GLU   A CD  
1535 O OE1 . GLU   A 64  ? 0.1546 0.1807 0.2118 -0.0185 0.0178  -0.0027 64  GLU   A OE1 
1536 O OE2 . GLU   A 64  ? 0.1748 0.1673 0.1828 -0.0273 0.0019  0.0076  64  GLU   A OE2 
1543 N N   . SER   A 65  ? 0.1184 0.1356 0.1591 0.0026  0.0032  -0.0085 65  SER   A N   
1544 C CA  . SER   A 65  ? 0.1300 0.1261 0.1513 -0.0048 0.0003  -0.0035 65  SER   A CA  
1545 C C   . SER   A 65  ? 0.1318 0.1405 0.1583 -0.0002 0.0016  -0.0076 65  SER   A C   
1546 O O   . SER   A 65  ? 0.1370 0.1440 0.1777 0.0007  0.0133  -0.0096 65  SER   A O   
1547 C CB  . SER   A 65  ? 0.1294 0.1303 0.1564 -0.0082 0.0024  0.0044  65  SER   A CB  
1548 O OG  . SER   A 65  ? 0.1232 0.1423 0.1709 -0.0050 -0.0021 0.0139  65  SER   A OG  
1554 N N   . ASP   A 66  ? 0.1316 0.1355 0.1643 -0.0036 0.0148  0.0039  66  ASP   A N   
1555 C CA  . ASP   A 66  ? 0.1411 0.1454 0.1829 -0.0013 0.0071  0.0152  66  ASP   A CA  
1556 C C   . ASP   A 66  ? 0.1379 0.1467 0.1792 -0.0085 0.0128  0.0138  66  ASP   A C   
1557 O O   . ASP   A 66  ? 0.1474 0.1489 0.1984 -0.0011 0.0299  0.0238  66  ASP   A O   
1558 C CB  . ASP   A 66  ? 0.1579 0.1502 0.2120 0.0069  0.0162  0.0316  66  ASP   A CB  
1559 C CG  . ASP   A 66  ? 0.1769 0.1706 0.2350 0.0082  -0.0013 0.0446  66  ASP   A CG  
1560 O OD1 . ASP   A 66  ? 0.1735 0.2038 0.2187 0.0006  -0.0054 0.0558  66  ASP   A OD1 
1561 O OD2 . ASP   A 66  ? 0.1951 0.1876 0.3267 0.0286  -0.0221 0.0179  66  ASP   A OD2 
1566 N N   . ASP   A 67  ? 0.1264 0.1467 0.1934 -0.0009 0.0109  0.0139  67  ASP   A N   
1567 C CA  . ASP   A 67  ? 0.1352 0.1615 0.2089 0.0004  0.0053  0.0285  67  ASP   A CA  
1568 C C   . ASP   A 67  ? 0.1356 0.1605 0.2053 0.0046  0.0130  0.0219  67  ASP   A C   
1569 O O   . ASP   A 67  ? 0.1363 0.1682 0.2223 0.0039  0.0284  0.0355  67  ASP   A O   
1570 C CB  . ASP   A 67  ? 0.1444 0.1702 0.2378 -0.0047 -0.0143 0.0303  67  ASP   A CB  
1571 C CG  . ASP   A 67  ? 0.1414 0.1848 0.2738 -0.0114 -0.0281 0.0349  67  ASP   A CG  
1572 O OD1 . ASP   A 67  ? 0.1471 0.2057 0.3482 -0.0146 -0.0418 0.0453  67  ASP   A OD1 
1573 O OD2 . ASP   A 67  ? 0.1399 0.1857 0.2570 -0.0021 -0.0115 0.0237  67  ASP   A OD2 
1578 N N   . TYR   A 68  ? 0.1353 0.1497 0.1936 0.0015  0.0136  0.0252  68  TYR   A N   
1579 C CA  . TYR   A 68  ? 0.1458 0.1501 0.1931 0.0022  0.0237  0.0222  68  TYR   A CA  
1580 C C   . TYR   A 68  ? 0.1374 0.1456 0.1889 0.0021  0.0280  0.0183  68  TYR   A C   
1581 O O   . TYR   A 68  ? 0.1465 0.1512 0.1944 0.0106  0.0300  0.0214  68  TYR   A O   
1582 C CB  . TYR   A 68  ? 0.1470 0.1392 0.2128 0.0099  0.0397  0.0305  68  TYR   A CB  
1583 C CG  . TYR   A 68  ? 0.1510 0.1583 0.2348 0.0051  0.0516  0.0316  68  TYR   A CG  
1584 C CD1 . TYR   A 68  ? 0.1696 0.1710 0.2620 -0.0159 0.0488  -0.0031 68  TYR   A CD1 
1585 C CD2 . TYR   A 68  ? 0.1788 0.1644 0.2703 0.0165  0.0581  0.0337  68  TYR   A CD2 
1586 C CE1 . TYR   A 68  ? 0.1764 0.1765 0.2938 -0.0199 0.0559  -0.0063 68  TYR   A CE1 
1587 C CE2 . TYR   A 68  ? 0.1719 0.1655 0.2784 0.0084  0.0645  0.0097  68  TYR   A CE2 
1588 C CZ  . TYR   A 68  ? 0.1750 0.1699 0.2956 -0.0197 0.0557  -0.0074 68  TYR   A CZ  
1589 O OH  . TYR   A 68  ? 0.2004 0.1719 0.3190 -0.0129 0.0225  -0.0344 68  TYR   A OH  
1599 N N   . ILE   A 69  ? 0.1307 0.1376 0.1910 0.0021  0.0217  0.0110  69  ILE   A N   
1600 C CA  . ILE   A 69  ? 0.1447 0.1397 0.1865 0.0052  0.0163  0.0012  69  ILE   A CA  
1601 C C   . ILE   A 69  ? 0.1465 0.1427 0.1836 0.0090  0.0209  0.0124  69  ILE   A C   
1602 O O   . ILE   A 69  ? 0.1526 0.1489 0.1782 -0.0020 0.0224  0.0159  69  ILE   A O   
1603 C CB  . ILE   A 69  ? 0.1542 0.1620 0.1840 0.0060  0.0147  -0.0049 69  ILE   A CB  
1604 C CG1 . ILE   A 69  ? 0.1517 0.1772 0.1860 0.0058  0.0198  -0.0159 69  ILE   A CG1 
1605 C CG2 . ILE   A 69  ? 0.1752 0.1829 0.2015 0.0080  0.0087  -0.0077 69  ILE   A CG2 
1606 C CD1 . ILE   A 69  ? 0.1509 0.1895 0.2024 -0.0034 0.0211  -0.0228 69  ILE   A CD1 
1618 N N   . ALA   A 70  ? 0.1507 0.1420 0.1883 -0.0021 0.0215  0.0158  70  ALA   A N   
1619 C CA  . ALA   A 70  ? 0.1564 0.1570 0.2029 -0.0152 0.0294  0.0235  70  ALA   A CA  
1620 C C   . ALA   A 70  ? 0.1488 0.1693 0.2024 -0.0135 0.0318  0.0227  70  ALA   A C   
1621 O O   . ALA   A 70  ? 0.1677 0.2082 0.2273 0.0040  0.0473  0.0384  70  ALA   A O   
1622 C CB  . ALA   A 70  ? 0.1613 0.1525 0.2234 -0.0152 0.0257  0.0136  70  ALA   A CB  
1628 N N   . THR   A 71  ? 0.1460 0.1631 0.1906 -0.0036 0.0230  0.0267  71  THR   A N   
1629 C CA  . THR   A 71  ? 0.1600 0.1782 0.2217 0.0060  0.0228  0.0291  71  THR   A CA  
1630 C C   . THR   A 71  ? 0.1466 0.1754 0.2431 0.0149  0.0380  0.0152  71  THR   A C   
1631 O O   . THR   A 71  ? 0.1491 0.2035 0.2875 0.0105  0.0439  -0.0048 71  THR   A O   
1632 C CB  . THR   A 71  ? 0.1785 0.2011 0.2415 0.0125  -0.0106 0.0342  71  THR   A CB  
1633 O OG1 . THR   A 71  ? 0.2038 0.2241 0.2492 0.0078  -0.0355 0.0215  71  THR   A OG1 
1634 C CG2 . THR   A 71  ? 0.1952 0.2212 0.2698 0.0175  -0.0200 0.0487  71  THR   A CG2 
1642 N N   . ASN   A 72  ? 0.1486 0.1584 0.2236 0.0104  0.0248  0.0122  72  ASN   A N   
1643 C CA  . ASN   A 72  ? 0.1548 0.1643 0.2221 0.0130  0.0441  0.0170  72  ASN   A CA  
1644 C C   . ASN   A 72  ? 0.1669 0.1612 0.2106 0.0107  0.0532  0.0054  72  ASN   A C   
1645 O O   . ASN   A 72  ? 0.1849 0.1588 0.2422 0.0141  0.0450  0.0031  72  ASN   A O   
1646 C CB  . ASN   A 72  ? 0.1733 0.1716 0.2220 0.0151  0.0383  0.0216  72  ASN   A CB  
1647 C CG  . ASN   A 72  ? 0.1920 0.1815 0.2279 0.0251  0.0272  0.0192  72  ASN   A CG  
1648 O OD1 . ASN   A 72  ? 0.2090 0.2114 0.2491 0.0240  0.0407  0.0219  72  ASN   A OD1 
1649 N ND2 . ASN   A 72  ? 0.2137 0.1829 0.2310 0.0480  0.0045  0.0096  72  ASN   A ND2 
1656 N N   . GLY   A 73  ? 0.1703 0.1603 0.1942 0.0044  0.0427  0.0037  73  GLY   A N   
1657 C CA  . GLY   A 73  ? 0.1747 0.1569 0.1813 -0.0113 0.0449  -0.0001 73  GLY   A CA  
1658 C C   . GLY   A 73  ? 0.1733 0.1484 0.1647 0.0033  0.0542  0.0209  73  GLY   A C   
1659 O O   . GLY   A 73  ? 0.1730 0.1519 0.1853 0.0127  0.0396  0.0246  73  GLY   A O   
1663 N N   . PRO   A 74  ? 0.1812 0.1517 0.1760 -0.0115 0.0463  0.0120  74  PRO   A N   
1664 C CA  . PRO   A 74  ? 0.1729 0.1480 0.1849 -0.0012 0.0464  0.0111  74  PRO   A CA  
1665 C C   . PRO   A 74  ? 0.1650 0.1333 0.1852 0.0004  0.0286  0.0035  74  PRO   A C   
1666 O O   . PRO   A 74  ? 0.1764 0.1370 0.2127 0.0026  0.0379  -0.0046 74  PRO   A O   
1667 C CB  . PRO   A 74  ? 0.1876 0.1772 0.2126 0.0021  0.0487  0.0252  74  PRO   A CB  
1668 C CG  . PRO   A 74  ? 0.2180 0.2108 0.2535 -0.0192 0.0315  0.0170  74  PRO   A CG  
1669 C CD  . PRO   A 74  ? 0.1981 0.1875 0.1927 -0.0227 0.0372  0.0035  74  PRO   A CD  
1677 N N   . LEU   A 75  ? 0.1599 0.1291 0.1744 -0.0004 0.0299  0.0069  75  LEU   A N   
1678 C CA  . LEU   A 75  ? 0.1637 0.1297 0.1521 0.0006  0.0111  0.0085  75  LEU   A CA  
1679 C C   . LEU   A 75  ? 0.1764 0.1445 0.1461 0.0063  0.0150  0.0110  75  LEU   A C   
1680 O O   . LEU   A 75  ? 0.2060 0.1570 0.1533 0.0101  0.0081  0.0058  75  LEU   A O   
1681 C CB  . LEU   A 75  ? 0.1716 0.1358 0.1454 -0.0097 0.0141  0.0164  75  LEU   A CB  
1682 C CG  . LEU   A 75  ? 0.1904 0.1639 0.1685 -0.0444 0.0134  0.0104  75  LEU   A CG  
1683 C CD1 . LEU   A 75  ? 0.2014 0.2142 0.1744 -0.0454 0.0122  -0.0053 75  LEU   A CD1 
1684 C CD2 . LEU   A 75  ? 0.2201 0.2109 0.2298 -0.0212 0.0126  0.0191  75  LEU   A CD2 
1696 N N   . LYS   A 76  ? 0.1805 0.1433 0.1674 -0.0073 0.0133  -0.0042 76  LYS   A N   
1697 C CA  . LYS   A 76  ? 0.1793 0.1619 0.1679 -0.0134 0.0214  -0.0185 76  LYS   A CA  
1698 C C   . LYS   A 76  ? 0.1722 0.1423 0.1440 -0.0030 0.0209  -0.0032 76  LYS   A C   
1699 O O   . LYS   A 76  ? 0.1762 0.1298 0.1437 -0.0028 0.0229  0.0040  76  LYS   A O   
1700 C CB  . LYS   A 76  ? 0.1811 0.1887 0.2258 -0.0001 0.0216  -0.0416 76  LYS   A CB  
1701 C CG  . LYS   A 76  ? 0.1916 0.1834 0.2837 0.0069  0.0215  -0.0333 76  LYS   A CG  
1702 C CD  . LYS   A 76  ? 0.1995 0.1818 0.3369 0.0121  0.0082  -0.0398 76  LYS   A CD  
1703 C CE  . LYS   A 76  ? 0.2190 0.2053 0.4001 -0.0007 0.0072  -0.0495 76  LYS   A CE  
1704 N NZ  . LYS   A 76  ? 0.2234 0.2031 0.4386 -0.0113 0.0021  -0.0606 76  LYS   A NZ  
1718 N N   . VAL   A 77  ? 0.1852 0.1431 0.1512 0.0003  0.0208  0.0085  77  VAL   A N   
1719 C CA  . VAL   A 77  ? 0.1767 0.1446 0.1441 0.0080  0.0243  0.0104  77  VAL   A CA  
1720 C C   . VAL   A 77  ? 0.1694 0.1422 0.1392 0.0122  0.0214  0.0017  77  VAL   A C   
1721 O O   . VAL   A 77  ? 0.1753 0.1517 0.1379 0.0115  0.0302  -0.0071 77  VAL   A O   
1722 C CB  . VAL   A 77  ? 0.1998 0.1626 0.1505 0.0022  0.0132  0.0186  77  VAL   A CB  
1723 C CG1 . VAL   A 77  ? 0.2035 0.1802 0.1705 0.0116  0.0026  0.0040  77  VAL   A CG1 
1724 C CG2 . VAL   A 77  ? 0.2261 0.1687 0.1833 0.0023  -0.0023 0.0195  77  VAL   A CG2 
1734 N N   . GLY   A 78  ? 0.1661 0.1381 0.1453 0.0112  0.0251  0.0067  78  GLY   A N   
1735 C CA  . GLY   A 78  ? 0.1585 0.1410 0.1502 0.0041  0.0234  0.0060  78  GLY   A CA  
1736 C C   . GLY   A 78  ? 0.1458 0.1358 0.1473 0.0067  0.0193  0.0039  78  GLY   A C   
1737 O O   . GLY   A 78  ? 0.1450 0.1378 0.1756 0.0016  0.0188  0.0244  78  GLY   A O   
1741 N N   . GLY   A 79  ? 0.1471 0.1338 0.1506 -0.0012 0.0102  0.0120  79  GLY   A N   
1742 C CA  . GLY   A 79  ? 0.1492 0.1320 0.1593 0.0002  0.0202  0.0144  79  GLY   A CA  
1743 C C   . GLY   A 79  ? 0.1366 0.1310 0.1516 -0.0018 0.0169  0.0034  79  GLY   A C   
1744 O O   . GLY   A 79  ? 0.1448 0.1436 0.1608 0.0197  0.0157  0.0034  79  GLY   A O   
1748 N N   . SER   A 80  ? 0.1344 0.1403 0.1724 0.0049  0.0159  0.0006  80  SER   A N   
1749 C CA  . SER   A 80  ? 0.1323 0.1363 0.1623 0.0016  0.0087  -0.0016 80  SER   A CA  
1750 C C   . SER   A 80  ? 0.1332 0.1385 0.1513 -0.0007 0.0150  0.0128  80  SER   A C   
1751 O O   . SER   A 80  ? 0.1341 0.1603 0.1870 0.0098  0.0169  -0.0007 80  SER   A O   
1752 C CB  . SER   A 80  ? 0.1443 0.1374 0.1905 -0.0053 0.0137  0.0057  80  SER   A CB  
1753 O OG  . SER   A 80  ? 0.1664 0.1427 0.2302 0.0079  -0.0041 0.0181  80  SER   A OG  
1759 N N   . CYS   A 81  ? 0.1278 0.1336 0.1542 0.0028  -0.0044 0.0123  81  CYS   A N   
1760 C CA  . CYS   A 81  ? 0.1346 0.1494 0.1490 -0.0055 -0.0069 0.0226  81  CYS   A CA  
1761 C C   . CYS   A 81  ? 0.1318 0.1383 0.1523 -0.0095 -0.0030 0.0303  81  CYS   A C   
1762 O O   . CYS   A 81  ? 0.1293 0.1669 0.1707 -0.0012 0.0036  0.0347  81  CYS   A O   
1763 C CB  . CYS   A 81  ? 0.1338 0.1507 0.1694 -0.0115 0.0002  0.0304  81  CYS   A CB  
1764 S SG  . CYS   A 81  ? 0.1510 0.1402 0.1666 -0.0144 0.0010  0.0140  81  CYS   A SG  
1770 N N   . VAL   A 82  ? 0.1320 0.1402 0.1551 -0.0030 -0.0050 0.0157  82  VAL   A N   
1771 C CA  . VAL   A 82  ? 0.1424 0.1521 0.1595 0.0027  -0.0055 0.0284  82  VAL   A CA  
1772 C C   . VAL   A 82  ? 0.1391 0.1590 0.1700 -0.0044 -0.0098 0.0234  82  VAL   A C   
1773 O O   . VAL   A 82  ? 0.1328 0.1688 0.1882 -0.0017 -0.0080 -0.0036 82  VAL   A O   
1774 C CB  . VAL   A 82  ? 0.1767 0.1669 0.1668 0.0037  -0.0057 0.0302  82  VAL   A CB  
1775 C CG1 . VAL   A 82  ? 0.2022 0.1795 0.1816 0.0067  0.0059  0.0326  82  VAL   A CG1 
1776 C CG2 . VAL   A 82  ? 0.1815 0.1673 0.1955 -0.0002 -0.0100 0.0326  82  VAL   A CG2 
1786 N N   . LEU   A 83  ? 0.1352 0.1525 0.1569 -0.0057 -0.0091 0.0144  83  LEU   A N   
1787 C CA  . LEU   A 83  ? 0.1367 0.1555 0.1483 -0.0074 -0.0114 0.0125  83  LEU   A CA  
1788 C C   . LEU   A 83  ? 0.1449 0.1587 0.1452 -0.0128 -0.0140 0.0091  83  LEU   A C   
1789 O O   . LEU   A 83  ? 0.1516 0.1640 0.1536 -0.0117 -0.0039 0.0219  83  LEU   A O   
1790 C CB  . LEU   A 83  ? 0.1444 0.1595 0.1483 -0.0077 -0.0082 0.0141  83  LEU   A CB  
1791 C CG  . LEU   A 83  ? 0.1590 0.1703 0.1579 -0.0098 0.0064  0.0091  83  LEU   A CG  
1792 C CD1 . LEU   A 83  ? 0.1727 0.1795 0.1644 -0.0232 0.0006  0.0240  83  LEU   A CD1 
1793 C CD2 . LEU   A 83  ? 0.1598 0.1888 0.1672 -0.0130 0.0184  0.0222  83  LEU   A CD2 
1805 N N   . SER   A 84  ? 0.1587 0.1613 0.1476 -0.0136 -0.0066 0.0163  84  SER   A N   
1806 C CA  . SER   A 84  ? 0.1664 0.1681 0.1374 -0.0122 -0.0061 0.0122  84  SER   A CA  
1807 C C   . SER   A 84  ? 0.1663 0.1690 0.1248 -0.0141 0.0007  0.0123  84  SER   A C   
1808 O O   . SER   A 84  ? 0.1581 0.1867 0.1331 -0.0084 -0.0057 0.0072  84  SER   A O   
1809 C CB  . SER   A 84  ? 0.1677 0.1946 0.1426 -0.0118 -0.0034 0.0015  84  SER   A CB  
1810 O OG  . SER   A 84  ? 0.1755 0.2186 0.1519 -0.0103 -0.0130 -0.0097 84  SER   A OG  
1816 N N   . GLY   A 85  ? 0.1784 0.1894 0.1317 -0.0189 0.0132  0.0110  85  GLY   A N   
1817 C CA  . GLY   A 85  ? 0.1810 0.1967 0.1486 -0.0179 0.0198  0.0051  85  GLY   A CA  
1818 C C   . GLY   A 85  ? 0.1742 0.2046 0.1337 -0.0158 0.0098  0.0074  85  GLY   A C   
1819 O O   . GLY   A 85  ? 0.1771 0.2155 0.1389 -0.0219 0.0163  -0.0084 85  GLY   A O   
1823 N N   . HIS   A 86  ? 0.1763 0.1953 0.1281 -0.0131 0.0026  -0.0012 86  HIS   A N   
1824 C CA  . HIS   A 86  ? 0.2012 0.2068 0.1184 -0.0131 0.0018  0.0025  86  HIS   A CA  
1825 C C   . HIS   A 86  ? 0.2171 0.2143 0.1107 -0.0092 -0.0089 0.0033  86  HIS   A C   
1826 O O   . HIS   A 86  ? 0.2264 0.2376 0.1358 -0.0090 0.0059  0.0049  86  HIS   A O   
1827 C CB  . HIS   A 86  ? 0.1968 0.1954 0.1336 -0.0023 0.0057  0.0015  86  HIS   A CB  
1828 C CG  . HIS   A 86  ? 0.1902 0.1896 0.1478 -0.0036 0.0185  0.0078  86  HIS   A CG  
1829 N ND1 . HIS   A 86  ? 0.1940 0.1856 0.1894 -0.0139 0.0091  0.0117  86  HIS   A ND1 
1830 C CD2 . HIS   A 86  ? 0.1985 0.1828 0.1359 0.0043  0.0262  0.0148  86  HIS   A CD2 
1831 C CE1 . HIS   A 86  ? 0.1910 0.1880 0.1835 -0.0075 0.0283  0.0175  86  HIS   A CE1 
1832 N NE2 . HIS   A 86  ? 0.1979 0.1752 0.1653 0.0039  0.0209  0.0309  86  HIS   A NE2 
1840 N N   . ASN   A 87  ? 0.2278 0.2246 0.1425 -0.0050 0.0150  -0.0131 87  ASN   A N   
1841 C CA  . ASN   A 87  ? 0.2465 0.2394 0.1452 -0.0051 0.0429  -0.0225 87  ASN   A CA  
1842 C C   . ASN   A 87  ? 0.2412 0.2525 0.1765 -0.0076 0.0631  -0.0083 87  ASN   A C   
1843 O O   . ASN   A 87  ? 0.2667 0.2659 0.2230 -0.0223 0.0906  -0.0141 87  ASN   A O   
1844 C CB  . ASN   A 87  ? 0.2663 0.2466 0.1449 0.0004  0.0442  -0.0205 87  ASN   A CB  
1845 C CG  . ASN   A 87  ? 0.2819 0.2532 0.1483 0.0078  0.0526  -0.0055 87  ASN   A CG  
1846 O OD1 . ASN   A 87  ? 0.2961 0.2479 0.1620 0.0273  0.0412  0.0059  87  ASN   A OD1 
1847 N ND2 . ASN   A 87  ? 0.2853 0.2727 0.1721 0.0106  0.0497  -0.0009 87  ASN   A ND2 
1854 N N   . LEU   A 88  ? 0.2168 0.2426 0.1674 -0.0180 0.0376  0.0163  88  LEU   A N   
1855 C CA  . LEU   A 88  ? 0.1998 0.2430 0.1833 -0.0235 0.0334  0.0300  88  LEU   A CA  
1856 C C   . LEU   A 88  ? 0.1946 0.2433 0.1699 -0.0243 0.0275  0.0360  88  LEU   A C   
1857 O O   . LEU   A 88  ? 0.2001 0.2490 0.2114 -0.0264 0.0279  0.0472  88  LEU   A O   
1858 C CB  . LEU   A 88  ? 0.2063 0.2530 0.1994 -0.0299 -0.0049 0.0504  88  LEU   A CB  
1859 C CG  . LEU   A 88  ? 0.2246 0.2655 0.2329 -0.0280 -0.0218 0.0426  88  LEU   A CG  
1860 C CD1 . LEU   A 88  ? 0.2352 0.2739 0.2255 -0.0232 -0.0339 0.0266  88  LEU   A CD1 
1861 C CD2 . LEU   A 88  ? 0.2372 0.2728 0.2799 -0.0236 -0.0211 0.0326  88  LEU   A CD2 
1873 N N   . ALA   A 89  ? 0.1957 0.2317 0.1505 -0.0246 0.0245  0.0106  89  ALA   A N   
1874 C CA  . ALA   A 89  ? 0.2073 0.2299 0.1295 -0.0216 0.0088  0.0262  89  ALA   A CA  
1875 C C   . ALA   A 89  ? 0.2104 0.2348 0.1441 -0.0154 -0.0037 0.0196  89  ALA   A C   
1876 O O   . ALA   A 89  ? 0.2060 0.2319 0.1814 -0.0261 -0.0132 -0.0057 89  ALA   A O   
1877 C CB  . ALA   A 89  ? 0.2050 0.2276 0.1173 -0.0213 0.0110  0.0307  89  ALA   A CB  
1883 N N   . LYS   A 90  ? 0.2224 0.2450 0.1491 -0.0249 -0.0178 0.0256  90  LYS   A N   
1884 C CA  . LYS   A 90  ? 0.2311 0.2598 0.1489 -0.0164 -0.0256 0.0272  90  LYS   A CA  
1885 C C   . LYS   A 90  ? 0.2016 0.2415 0.1433 -0.0200 -0.0243 0.0126  90  LYS   A C   
1886 O O   . LYS   A 90  ? 0.2022 0.2541 0.1730 -0.0253 -0.0327 0.0072  90  LYS   A O   
1887 C CB  . LYS   A 90  ? 0.2572 0.2901 0.1947 -0.0092 -0.0347 0.0557  90  LYS   A CB  
1888 C CG  . LYS   A 90  ? 0.2904 0.3216 0.2941 -0.0051 -0.0304 0.0623  90  LYS   A CG  
1889 C CD  . LYS   A 90  ? 0.3309 0.3540 0.3922 -0.0062 -0.0223 0.0677  90  LYS   A CD  
1890 C CE  . LYS   A 90  ? 0.3615 0.3794 0.4665 -0.0063 -0.0154 0.0666  90  LYS   A CE  
1891 N NZ  . LYS   A 90  ? 0.3703 0.3937 0.5164 -0.0072 -0.0106 0.0607  90  LYS   A NZ  
1905 N N   . HIS   A 91  ? 0.1941 0.2153 0.1189 -0.0142 -0.0318 0.0165  91  HIS   A N   
1906 C CA  . HIS   A 91  ? 0.1832 0.1935 0.1238 -0.0147 -0.0265 0.0203  91  HIS   A CA  
1907 C C   . HIS   A 91  ? 0.1612 0.1781 0.1158 -0.0118 -0.0109 0.0234  91  HIS   A C   
1908 O O   . HIS   A 91  ? 0.1593 0.1942 0.1340 -0.0196 -0.0002 0.0233  91  HIS   A O   
1909 C CB  . HIS   A 91  ? 0.2018 0.2197 0.1807 0.0057  -0.0378 0.0241  91  HIS   A CB  
1910 C CG  . HIS   A 91  ? 0.2408 0.2679 0.2520 0.0153  -0.0676 0.0166  91  HIS   A CG  
1911 N ND1 . HIS   A 91  ? 0.2504 0.2968 0.2939 0.0216  -0.0757 -0.0099 91  HIS   A ND1 
1912 C CD2 . HIS   A 91  ? 0.2635 0.2868 0.2735 0.0220  -0.0829 0.0277  91  HIS   A CD2 
1913 C CE1 . HIS   A 91  ? 0.2615 0.3026 0.3056 0.0254  -0.0777 0.0037  91  HIS   A CE1 
1914 N NE2 . HIS   A 91  ? 0.2731 0.3007 0.2982 0.0296  -0.0849 0.0141  91  HIS   A NE2 
1922 N N   . CYS   A 92  ? 0.1543 0.1732 0.1205 -0.0193 -0.0142 0.0210  92  CYS   A N   
1923 C CA  . CYS   A 92  ? 0.1426 0.1605 0.1312 -0.0104 -0.0012 0.0207  92  CYS   A CA  
1924 C C   . CYS   A 92  ? 0.1388 0.1590 0.1255 -0.0139 -0.0012 0.0149  92  CYS   A C   
1925 O O   . CYS   A 92  ? 0.1388 0.1578 0.1465 -0.0164 -0.0052 0.0108  92  CYS   A O   
1926 C CB  . CYS   A 92  ? 0.1468 0.1610 0.1488 -0.0047 -0.0043 0.0121  92  CYS   A CB  
1927 S SG  . CYS   A 92  ? 0.1446 0.1473 0.1388 -0.0100 -0.0013 0.0107  92  CYS   A SG  
1933 N N   . LEU   A 93  ? 0.1321 0.1466 0.1338 -0.0069 0.0092  0.0176  93  LEU   A N   
1934 C CA  . LEU   A 93  ? 0.1287 0.1344 0.1327 -0.0039 0.0069  0.0176  93  LEU   A CA  
1935 C C   . LEU   A 93  ? 0.1252 0.1301 0.1414 -0.0026 0.0060  0.0110  93  LEU   A C   
1936 O O   . LEU   A 93  ? 0.1243 0.1349 0.1394 -0.0017 -0.0028 0.0143  93  LEU   A O   
1937 C CB  . LEU   A 93  ? 0.1369 0.1416 0.1403 -0.0019 -0.0035 0.0216  93  LEU   A CB  
1938 C CG  . LEU   A 93  ? 0.1450 0.1371 0.1391 -0.0080 0.0031  0.0240  93  LEU   A CG  
1939 C CD1 . LEU   A 93  ? 0.1452 0.1415 0.1808 -0.0012 0.0117  0.0166  93  LEU   A CD1 
1940 C CD2 . LEU   A 93  ? 0.1545 0.1462 0.1575 -0.0069 -0.0024 0.0192  93  LEU   A CD2 
1952 N N   . HIS   A 94  ? 0.1207 0.1258 0.1370 -0.0005 0.0103  0.0178  94  HIS   A N   
1953 C CA  . HIS   A 94  ? 0.1240 0.1230 0.1376 -0.0043 0.0026  0.0188  94  HIS   A CA  
1954 C C   . HIS   A 94  ? 0.1207 0.1215 0.1385 -0.0026 0.0077  0.0065  94  HIS   A C   
1955 O O   . HIS   A 94  ? 0.1274 0.1459 0.1696 0.0004  0.0031  -0.0139 94  HIS   A O   
1956 C CB  . HIS   A 94  ? 0.1201 0.1247 0.1457 0.0013  0.0017  0.0195  94  HIS   A CB  
1957 C CG  . HIS   A 94  ? 0.1244 0.1234 0.1354 -0.0055 0.0010  0.0149  94  HIS   A CG  
1958 N ND1 . HIS   A 94  ? 0.1256 0.1270 0.1432 -0.0027 0.0013  0.0102  94  HIS   A ND1 
1959 C CD2 . HIS   A 94  ? 0.1357 0.1389 0.1497 -0.0029 -0.0057 0.0072  94  HIS   A CD2 
1960 C CE1 . HIS   A 94  ? 0.1315 0.1285 0.1321 -0.0050 -0.0065 0.0045  94  HIS   A CE1 
1961 N NE2 . HIS   A 94  ? 0.1337 0.1334 0.1478 -0.0049 -0.0073 0.0031  94  HIS   A NE2 
1969 N N   . VAL   A 95  ? 0.1206 0.1229 0.1190 -0.0021 0.0083  0.0026  95  VAL   A N   
1970 C CA  . VAL   A 95  ? 0.1282 0.1275 0.1221 -0.0033 0.0156  0.0125  95  VAL   A CA  
1971 C C   . VAL   A 95  ? 0.1302 0.1217 0.1155 -0.0121 0.0062  0.0106  95  VAL   A C   
1972 O O   . VAL   A 95  ? 0.1353 0.1342 0.1239 0.0069  0.0103  0.0099  95  VAL   A O   
1973 C CB  . VAL   A 95  ? 0.1313 0.1237 0.1493 -0.0095 0.0096  0.0135  95  VAL   A CB  
1974 C CG1 . VAL   A 95  ? 0.1449 0.1243 0.1650 -0.0174 0.0120  -0.0006 95  VAL   A CG1 
1975 C CG2 . VAL   A 95  ? 0.1362 0.1289 0.1461 -0.0163 0.0074  0.0229  95  VAL   A CG2 
1985 N N   . VAL   A 96  ? 0.1326 0.1226 0.1153 -0.0038 0.0045  0.0144  96  VAL   A N   
1986 C CA  . VAL   A 96  ? 0.1375 0.1237 0.1313 -0.0022 0.0119  0.0166  96  VAL   A CA  
1987 C C   . VAL   A 96  ? 0.1389 0.1305 0.1381 -0.0048 0.0126  0.0168  96  VAL   A C   
1988 O O   . VAL   A 96  ? 0.1542 0.1332 0.1526 -0.0028 0.0217  -0.0010 96  VAL   A O   
1989 C CB  . VAL   A 96  ? 0.1382 0.1298 0.1441 -0.0050 0.0218  0.0126  96  VAL   A CB  
1990 C CG1 . VAL   A 96  ? 0.1460 0.1377 0.1276 -0.0037 0.0169  0.0126  96  VAL   A CG1 
1991 C CG2 . VAL   A 96  ? 0.1419 0.1390 0.1590 -0.0128 0.0128  0.0165  96  VAL   A CG2 
2001 N N   A GLY   A 97  ? 0.1404 0.1390 0.1350 -0.0085 0.0094  0.0096  97  GLY   A N   
2002 N N   B GLY   A 97  ? 0.1447 0.1382 0.1314 -0.0030 0.0104  0.0129  97  GLY   A N   
2003 C CA  A GLY   A 97  ? 0.1534 0.1519 0.1261 -0.0048 0.0001  0.0032  97  GLY   A CA  
2004 C CA  B GLY   A 97  ? 0.1580 0.1464 0.1193 0.0023  0.0073  0.0136  97  GLY   A CA  
2005 C C   A GLY   A 97  ? 0.1498 0.1628 0.1149 -0.0091 -0.0023 -0.0013 97  GLY   A C   
2006 C C   B GLY   A 97  ? 0.1606 0.1542 0.1069 0.0012  0.0103  0.0137  97  GLY   A C   
2007 O O   A GLY   A 97  ? 0.1578 0.1600 0.1565 -0.0040 -0.0076 0.0059  97  GLY   A O   
2008 O O   B GLY   A 97  ? 0.1690 0.1566 0.1103 -0.0021 0.0144  0.0182  97  GLY   A O   
2015 N N   A PRO   A 98  ? 0.1563 0.1645 0.1023 -0.0081 -0.0026 0.0064  98  PRO   A N   
2016 N N   B PRO   A 98  ? 0.1673 0.1545 0.1183 0.0065  0.0042  0.0226  98  PRO   A N   
2017 C CA  A PRO   A 98  ? 0.1678 0.1833 0.1118 -0.0140 0.0017  -0.0026 98  PRO   A CA  
2018 C CA  B PRO   A 98  ? 0.1780 0.1673 0.1287 0.0014  -0.0003 0.0137  98  PRO   A CA  
2019 C C   A PRO   A 98  ? 0.1692 0.1845 0.1089 -0.0205 0.0124  0.0020  98  PRO   A C   
2020 C C   B PRO   A 98  ? 0.1889 0.1716 0.1317 -0.0045 -0.0052 0.0354  98  PRO   A C   
2021 O O   A PRO   A 98  ? 0.1612 0.1660 0.1329 -0.0169 0.0075  0.0072  98  PRO   A O   
2022 O O   B PRO   A 98  ? 0.1840 0.1653 0.1622 0.0017  -0.0127 0.0279  98  PRO   A O   
2023 C CB  A PRO   A 98  ? 0.1823 0.1933 0.1129 -0.0059 -0.0076 -0.0125 98  PRO   A CB  
2024 C CB  B PRO   A 98  ? 0.1829 0.1703 0.1215 0.0092  -0.0044 0.0102  98  PRO   A CB  
2025 C CG  A PRO   A 98  ? 0.1836 0.1841 0.1310 -0.0038 -0.0094 -0.0206 98  PRO   A CG  
2026 C CG  B PRO   A 98  ? 0.1847 0.1657 0.1304 0.0090  -0.0010 0.0083  98  PRO   A CG  
2027 C CD  A PRO   A 98  ? 0.1676 0.1694 0.1255 -0.0034 -0.0045 -0.0082 98  PRO   A CD  
2028 C CD  B PRO   A 98  ? 0.1740 0.1531 0.1233 0.0115  0.0022  0.0201  98  PRO   A CD  
2043 N N   A ASN   A 99  ? 0.1786 0.2066 0.1275 -0.0162 0.0137  0.0175  99  ASN   A N   
2044 N N   B ASN   A 99  ? 0.2030 0.1840 0.1322 -0.0061 -0.0101 0.0606  99  ASN   A N   
2045 C CA  A ASN   A 99  ? 0.1988 0.2161 0.1340 -0.0208 0.0088  0.0259  99  ASN   A CA  
2046 C CA  B ASN   A 99  ? 0.2213 0.1938 0.1387 -0.0077 -0.0137 0.0677  99  ASN   A CA  
2047 C C   A ASN   A 99  ? 0.2168 0.2390 0.1217 -0.0286 0.0127  0.0330  99  ASN   A C   
2048 C C   B ASN   A 99  ? 0.2317 0.2102 0.1288 -0.0142 -0.0121 0.0603  99  ASN   A C   
2049 O O   A ASN   A 99  ? 0.2192 0.2343 0.1216 -0.0186 -0.0019 0.0272  99  ASN   A O   
2050 O O   B ASN   A 99  ? 0.2354 0.2061 0.1331 -0.0039 -0.0195 0.0589  99  ASN   A O   
2051 C CB  A ASN   A 99  ? 0.1970 0.2022 0.1451 -0.0261 -0.0145 0.0256  99  ASN   A CB  
2052 C CB  B ASN   A 99  ? 0.2262 0.1964 0.1741 -0.0071 -0.0287 0.0717  99  ASN   A CB  
2053 C CG  A ASN   A 99  ? 0.1983 0.1902 0.1657 -0.0224 -0.0252 0.0185  99  ASN   A CG  
2054 C CG  B ASN   A 99  ? 0.2322 0.2058 0.2126 -0.0037 -0.0343 0.0637  99  ASN   A CG  
2055 O OD1 A ASN   A 99  ? 0.2125 0.2062 0.1788 -0.0121 -0.0215 0.0105  99  ASN   A OD1 
2056 O OD1 B ASN   A 99  ? 0.2426 0.2101 0.2188 -0.0025 -0.0399 0.0643  99  ASN   A OD1 
2057 N ND2 A ASN   A 99  ? 0.1995 0.1725 0.1899 -0.0187 -0.0327 0.0296  99  ASN   A ND2 
2058 N ND2 B ASN   A 99  ? 0.2328 0.2077 0.2292 0.0035  -0.0291 0.0620  99  ASN   A ND2 
2071 N N   A VAL   A 100 ? 0.2396 0.2625 0.1346 -0.0431 -0.0122 0.0317  100 VAL   A N   
2072 N N   B VAL   A 100 ? 0.2409 0.2270 0.1278 -0.0279 -0.0274 0.0445  100 VAL   A N   
2073 C CA  A VAL   A 100 ? 0.2745 0.2928 0.1664 -0.0471 -0.0258 0.0420  100 VAL   A CA  
2074 C CA  B VAL   A 100 ? 0.2578 0.2460 0.1597 -0.0393 -0.0333 0.0338  100 VAL   A CA  
2075 C C   A VAL   A 100 ? 0.2898 0.3195 0.1700 -0.0488 -0.0395 0.0775  100 VAL   A C   
2076 C C   B VAL   A 100 ? 0.2617 0.2559 0.1454 -0.0485 -0.0364 0.0462  100 VAL   A C   
2077 O O   A VAL   A 100 ? 0.2978 0.3343 0.1899 -0.0437 -0.0283 0.0774  100 VAL   A O   
2078 O O   B VAL   A 100 ? 0.2694 0.2619 0.1542 -0.0418 -0.0193 0.0474  100 VAL   A O   
2079 C CB  A VAL   A 100 ? 0.2941 0.2928 0.2004 -0.0502 -0.0343 0.0281  100 VAL   A CB  
2080 C CB  B VAL   A 100 ? 0.2726 0.2527 0.2087 -0.0445 -0.0399 0.0231  100 VAL   A CB  
2081 C CG1 A VAL   A 100 ? 0.2998 0.2990 0.2162 -0.0508 -0.0283 0.0283  100 VAL   A CG1 
2082 C CG1 B VAL   A 100 ? 0.2781 0.2637 0.2331 -0.0463 -0.0384 0.0245  100 VAL   A CG1 
2083 C CG2 A VAL   A 100 ? 0.3021 0.2931 0.2141 -0.0542 -0.0353 0.0175  100 VAL   A CG2 
2084 C CG2 B VAL   A 100 ? 0.2797 0.2541 0.2291 -0.0468 -0.0358 0.0183  100 VAL   A CG2 
2103 N N   A ASN   A 101 ? 0.3023 0.3298 0.1995 -0.0468 -0.0486 0.1158  101 ASN   A N   
2104 N N   B ASN   A 101 ? 0.2624 0.2634 0.1667 -0.0581 -0.0425 0.0658  101 ASN   A N   
2105 C CA  A ASN   A 101 ? 0.3265 0.3437 0.2268 -0.0477 -0.0465 0.1293  101 ASN   A CA  
2106 C CA  B ASN   A 101 ? 0.2761 0.2772 0.1871 -0.0641 -0.0482 0.0690  101 ASN   A CA  
2107 C C   A ASN   A 101 ? 0.3491 0.3636 0.2317 -0.0548 -0.0141 0.1597  101 ASN   A C   
2108 C C   B ASN   A 101 ? 0.2932 0.3016 0.2064 -0.0703 -0.0343 0.0762  101 ASN   A C   
2109 O O   A ASN   A 101 ? 0.3646 0.3699 0.2684 -0.0505 -0.0116 0.1619  101 ASN   A O   
2110 O O   B ASN   A 101 ? 0.3037 0.3074 0.2425 -0.0658 -0.0345 0.0662  101 ASN   A O   
2111 C CB  A ASN   A 101 ? 0.3289 0.3346 0.2390 -0.0398 -0.0689 0.1071  101 ASN   A CB  
2112 C CB  B ASN   A 101 ? 0.2757 0.2692 0.1950 -0.0651 -0.0634 0.0621  101 ASN   A CB  
2113 C CG  A ASN   A 101 ? 0.3307 0.3252 0.2307 -0.0377 -0.0765 0.0791  101 ASN   A CG  
2114 C CG  B ASN   A 101 ? 0.2747 0.2606 0.1954 -0.0704 -0.0690 0.0488  101 ASN   A CG  
2115 O OD1 A ASN   A 101 ? 0.3279 0.3355 0.2372 -0.0320 -0.0710 0.0452  101 ASN   A OD1 
2116 O OD1 B ASN   A 101 ? 0.2728 0.2616 0.2044 -0.0709 -0.0665 0.0329  101 ASN   A OD1 
2117 N ND2 A ASN   A 101 ? 0.3355 0.3118 0.2267 -0.0402 -0.0800 0.0813  101 ASN   A ND2 
2118 N ND2 B ASN   A 101 ? 0.2736 0.2566 0.1958 -0.0728 -0.0666 0.0496  101 ASN   A ND2 
2131 N N   A LYS   A 102 ? 0.3546 0.3862 0.2575 -0.0685 0.0020  0.1524  102 LYS   A N   
2132 N N   B LYS   A 102 ? 0.2964 0.3235 0.2179 -0.0810 -0.0293 0.0711  102 LYS   A N   
2133 C CA  A LYS   A 102 ? 0.3646 0.4064 0.2613 -0.0732 0.0078  0.1384  102 LYS   A CA  
2134 C CA  B LYS   A 102 ? 0.3066 0.3455 0.2214 -0.0832 -0.0257 0.0646  102 LYS   A CA  
2135 C C   A LYS   A 102 ? 0.3706 0.4200 0.2390 -0.0655 0.0104  0.1344  102 LYS   A C   
2136 C C   B LYS   A 102 ? 0.3139 0.3605 0.2080 -0.0757 -0.0164 0.0579  102 LYS   A C   
2137 O O   A LYS   A 102 ? 0.3737 0.4253 0.2402 -0.0627 0.0161  0.1393  102 LYS   A O   
2138 O O   B LYS   A 102 ? 0.3152 0.3628 0.2030 -0.0698 -0.0115 0.0587  102 LYS   A O   
2139 C CB  A LYS   A 102 ? 0.3713 0.4123 0.2908 -0.0816 0.0006  0.1205  102 LYS   A CB  
2140 C CB  B LYS   A 102 ? 0.3128 0.3490 0.2402 -0.0896 -0.0312 0.0564  102 LYS   A CB  
2141 C CG  A LYS   A 102 ? 0.3777 0.4158 0.3167 -0.0872 -0.0076 0.0991  102 LYS   A CG  
2142 C CG  B LYS   A 102 ? 0.3201 0.3520 0.2596 -0.0940 -0.0378 0.0465  102 LYS   A CG  
2143 C CD  A LYS   A 102 ? 0.3861 0.4213 0.3461 -0.0898 -0.0176 0.0760  102 LYS   A CD  
2144 C CD  B LYS   A 102 ? 0.3286 0.3548 0.2758 -0.0947 -0.0437 0.0373  102 LYS   A CD  
2145 C CE  A LYS   A 102 ? 0.3944 0.4273 0.3726 -0.0890 -0.0252 0.0591  102 LYS   A CE  
2146 C CE  B LYS   A 102 ? 0.3377 0.3574 0.2900 -0.0926 -0.0465 0.0316  102 LYS   A CE  
2147 N NZ  A LYS   A 102 ? 0.3981 0.4290 0.3855 -0.0924 -0.0253 0.0487  102 LYS   A NZ  
2148 N NZ  B LYS   A 102 ? 0.3426 0.3568 0.2955 -0.0955 -0.0461 0.0289  102 LYS   A NZ  
2175 N N   A GLY   A 103 ? 0.3708 0.4306 0.2362 -0.0556 -0.0016 0.1064  103 GLY   A N   
2176 N N   B GLY   A 103 ? 0.3199 0.3741 0.2161 -0.0711 -0.0139 0.0388  103 GLY   A N   
2177 C CA  A GLY   A 103 ? 0.3681 0.4332 0.2231 -0.0486 -0.0060 0.0875  103 GLY   A CA  
2178 C CA  B GLY   A 103 ? 0.3257 0.3858 0.2256 -0.0639 -0.0065 0.0218  103 GLY   A CA  
2179 C C   A GLY   A 103 ? 0.3592 0.4352 0.2084 -0.0462 -0.0010 0.0671  103 GLY   A C   
2180 C C   B GLY   A 103 ? 0.3292 0.3964 0.2382 -0.0574 0.0065  0.0147  103 GLY   A C   
2181 O O   A GLY   A 103 ? 0.3655 0.4412 0.2116 -0.0443 0.0016  0.0575  103 GLY   A O   
2182 O O   B GLY   A 103 ? 0.3352 0.3972 0.2409 -0.0562 0.0162  0.0146  103 GLY   A O   
2189 N N   A GLU   A 104 ? 0.3395 0.4284 0.1771 -0.0461 0.0007  0.0565  104 GLU   A N   
2190 N N   B GLU   A 104 ? 0.3254 0.4051 0.2276 -0.0520 0.0127  0.0062  104 GLU   A N   
2191 C CA  A GLU   A 104 ? 0.3151 0.4191 0.1529 -0.0557 0.0004  0.0478  104 GLU   A CA  
2192 C CA  B GLU   A 104 ? 0.3196 0.4098 0.2256 -0.0512 0.0157  -0.0041 104 GLU   A CA  
2193 C C   A GLU   A 104 ? 0.3128 0.4246 0.1625 -0.0582 0.0081  0.0211  104 GLU   A C   
2194 C C   B GLU   A 104 ? 0.3254 0.4212 0.2238 -0.0514 0.0145  -0.0151 104 GLU   A C   
2195 O O   A GLU   A 104 ? 0.3083 0.4246 0.1810 -0.0565 0.0089  0.0182  104 GLU   A O   
2196 O O   B GLU   A 104 ? 0.3259 0.4270 0.2217 -0.0494 0.0054  -0.0169 104 GLU   A O   
2197 C CB  A GLU   A 104 ? 0.2853 0.3977 0.1287 -0.0609 0.0004  0.0704  104 GLU   A CB  
2198 C CB  B GLU   A 104 ? 0.3055 0.4008 0.2190 -0.0495 0.0236  0.0001  104 GLU   A CB  
2199 C CG  A GLU   A 104 ? 0.2625 0.3824 0.1408 -0.0631 -0.0085 0.0804  104 GLU   A CG  
2200 C CG  B GLU   A 104 ? 0.2936 0.3916 0.2222 -0.0462 0.0285  0.0015  104 GLU   A CG  
2201 C CD  A GLU   A 104 ? 0.2396 0.3653 0.1374 -0.0668 -0.0120 0.0891  104 GLU   A CD  
2202 C CD  B GLU   A 104 ? 0.2819 0.3821 0.2208 -0.0447 0.0368  0.0048  104 GLU   A CD  
2203 O OE1 A GLU   A 104 ? 0.2213 0.3490 0.1237 -0.0658 -0.0172 0.0764  104 GLU   A OE1 
2204 O OE1 B GLU   A 104 ? 0.2741 0.3767 0.1925 -0.0406 0.0479  0.0051  104 GLU   A OE1 
2205 O OE2 A GLU   A 104 ? 0.2487 0.3637 0.1511 -0.0684 -0.0097 0.1019  104 GLU   A OE2 
2206 O OE2 B GLU   A 104 ? 0.2851 0.3805 0.2467 -0.0461 0.0314  0.0060  104 GLU   A OE2 
2219 N N   A ASP   A 105 ? 0.3171 0.4320 0.1780 -0.0620 0.0177  -0.0090 105 ASP   A N   
2220 N N   B ASP   A 105 ? 0.3333 0.4268 0.2484 -0.0512 0.0180  -0.0284 105 ASP   A N   
2221 C CA  A ASP   A 105 ? 0.3160 0.4321 0.2145 -0.0580 0.0240  -0.0413 105 ASP   A CA  
2222 C CA  B ASP   A 105 ? 0.3363 0.4304 0.2796 -0.0516 0.0207  -0.0427 105 ASP   A CA  
2223 C C   A ASP   A 105 ? 0.2776 0.4134 0.1736 -0.0707 0.0126  -0.0588 105 ASP   A C   
2224 C C   B ASP   A 105 ? 0.3239 0.4214 0.2709 -0.0547 0.0163  -0.0449 105 ASP   A C   
2225 O O   A ASP   A 105 ? 0.2499 0.3798 0.1336 -0.0669 0.0120  -0.0824 105 ASP   A O   
2226 O O   B ASP   A 105 ? 0.3203 0.4209 0.2547 -0.0522 0.0218  -0.0518 105 ASP   A O   
2227 C CB  A ASP   A 105 ? 0.3480 0.4565 0.2956 -0.0502 0.0335  -0.0559 105 ASP   A CB  
2228 C CB  B ASP   A 105 ? 0.3471 0.4395 0.3160 -0.0513 0.0255  -0.0592 105 ASP   A CB  
2229 C CG  A ASP   A 105 ? 0.3752 0.4729 0.3637 -0.0399 0.0369  -0.0689 105 ASP   A CG  
2230 C CG  B ASP   A 105 ? 0.3544 0.4458 0.3486 -0.0526 0.0286  -0.0744 105 ASP   A CG  
2231 O OD1 A ASP   A 105 ? 0.3830 0.4791 0.3690 -0.0391 0.0383  -0.0824 105 ASP   A OD1 
2232 O OD1 B ASP   A 105 ? 0.3558 0.4486 0.3467 -0.0575 0.0314  -0.0843 105 ASP   A OD1 
2233 O OD2 A ASP   A 105 ? 0.3921 0.4783 0.4101 -0.0366 0.0385  -0.0636 105 ASP   A OD2 
2234 O OD2 B ASP   A 105 ? 0.3574 0.4490 0.3717 -0.0534 0.0317  -0.0750 105 ASP   A OD2 
2243 N N   A ILE   A 106 ? 0.2634 0.4063 0.1984 -0.0742 -0.0090 -0.0540 106 ILE   A N   
2244 N N   B ILE   A 106 ? 0.3144 0.4113 0.2825 -0.0595 0.0008  -0.0443 106 ILE   A N   
2245 C CA  A ILE   A 106 ? 0.2398 0.3959 0.2228 -0.0862 -0.0307 -0.0612 106 ILE   A CA  
2246 C CA  B ILE   A 106 ? 0.2997 0.3954 0.2896 -0.0656 -0.0102 -0.0501 106 ILE   A CA  
2247 C C   A ILE   A 106 ? 0.2254 0.3744 0.2339 -0.0970 -0.0244 -0.0852 106 ILE   A C   
2248 C C   B ILE   A 106 ? 0.2855 0.3737 0.2874 -0.0712 -0.0018 -0.0754 106 ILE   A C   
2249 O O   A ILE   A 106 ? 0.2066 0.3642 0.2348 -0.0987 -0.0124 -0.0828 106 ILE   A O   
2250 O O   B ILE   A 106 ? 0.2751 0.3648 0.2757 -0.0737 0.0015  -0.0814 106 ILE   A O   
2251 C CB  A ILE   A 106 ? 0.2425 0.4036 0.2679 -0.0735 -0.0427 -0.0281 106 ILE   A CB  
2252 C CB  B ILE   A 106 ? 0.3035 0.3996 0.3090 -0.0612 -0.0243 -0.0261 106 ILE   A CB  
2253 C CG1 A ILE   A 106 ? 0.2368 0.4032 0.2971 -0.0581 -0.0429 -0.0043 106 ILE   A CG1 
2254 C CG1 B ILE   A 106 ? 0.3030 0.3978 0.3249 -0.0563 -0.0278 -0.0131 106 ILE   A CG1 
2255 C CG2 A ILE   A 106 ? 0.2487 0.4077 0.2853 -0.0718 -0.0514 -0.0217 106 ILE   A CG2 
2256 C CG2 B ILE   A 106 ? 0.3073 0.4033 0.3138 -0.0605 -0.0299 -0.0195 106 ILE   A CG2 
2257 C CD1 A ILE   A 106 ? 0.2376 0.3999 0.3132 -0.0458 -0.0350 0.0057  106 ILE   A CD1 
2258 C CD1 B ILE   A 106 ? 0.3049 0.3948 0.3339 -0.0511 -0.0251 -0.0066 106 ILE   A CD1 
2281 N N   A GLN   A 107 ? 0.2434 0.3640 0.2674 -0.0900 -0.0089 -0.0982 107 GLN   A N   
2282 N N   B GLN   A 107 ? 0.2854 0.3619 0.3108 -0.0695 0.0114  -0.0875 107 GLN   A N   
2283 C CA  A GLN   A 107 ? 0.2690 0.3510 0.3416 -0.0746 0.0168  -0.0957 107 GLN   A CA  
2284 C CA  B GLN   A 107 ? 0.2876 0.3458 0.3521 -0.0619 0.0262  -0.0882 107 GLN   A CA  
2285 C C   A GLN   A 107 ? 0.2482 0.3024 0.3299 -0.0677 0.0403  -0.0811 107 GLN   A C   
2286 C C   B GLN   A 107 ? 0.2547 0.3015 0.3246 -0.0616 0.0437  -0.0802 107 GLN   A C   
2287 O O   A GLN   A 107 ? 0.2530 0.2937 0.3852 -0.0626 0.0492  -0.0758 107 GLN   A O   
2288 O O   B GLN   A 107 ? 0.2567 0.2980 0.3652 -0.0559 0.0536  -0.0755 107 GLN   A O   
2289 C CB  A GLN   A 107 ? 0.3079 0.3802 0.4340 -0.0727 0.0088  -0.0922 107 GLN   A CB  
2290 C CB  B GLN   A 107 ? 0.3185 0.3696 0.4309 -0.0583 0.0146  -0.0839 107 GLN   A CB  
2291 C CG  A GLN   A 107 ? 0.3452 0.4085 0.5328 -0.0689 0.0016  -0.0808 107 GLN   A CG  
2292 C CG  B GLN   A 107 ? 0.3473 0.3920 0.5135 -0.0543 0.0046  -0.0737 107 GLN   A CG  
2293 C CD  A GLN   A 107 ? 0.3746 0.4300 0.6159 -0.0666 -0.0024 -0.0665 107 GLN   A CD  
2294 C CD  B GLN   A 107 ? 0.3702 0.4082 0.5824 -0.0516 -0.0026 -0.0615 107 GLN   A CD  
2295 O OE1 A GLN   A 107 ? 0.3870 0.4369 0.6497 -0.0666 -0.0038 -0.0640 107 GLN   A OE1 
2296 O OE1 B GLN   A 107 ? 0.3795 0.4145 0.6104 -0.0514 -0.0054 -0.0596 107 GLN   A OE1 
2297 N NE2 A GLN   A 107 ? 0.3830 0.4392 0.6438 -0.0668 -0.0042 -0.0627 107 GLN   A NE2 
2298 N NE2 B GLN   A 107 ? 0.3775 0.4129 0.6052 -0.0514 -0.0041 -0.0574 107 GLN   A NE2 
2315 N N   . LEU   A 108 ? 0.2185 0.2564 0.2656 -0.0636 0.0498  -0.0835 108 LEU   A N   
2316 C CA  . LEU   A 108 ? 0.1946 0.1994 0.2224 -0.0234 0.0383  -0.0273 108 LEU   A CA  
2317 C C   . LEU   A 108 ? 0.1738 0.1562 0.2135 -0.0097 0.0229  -0.0029 108 LEU   A C   
2318 O O   . LEU   A 108 ? 0.1631 0.1537 0.2381 -0.0033 0.0304  0.0034  108 LEU   A O   
2319 C CB  . LEU   A 108 ? 0.1999 0.2057 0.1960 -0.0245 0.0427  -0.0129 108 LEU   A CB  
2320 C CG  . LEU   A 108 ? 0.2207 0.2348 0.2188 -0.0253 0.0510  -0.0186 108 LEU   A CG  
2321 C CD1 . LEU   A 108 ? 0.2402 0.2448 0.2155 -0.0338 0.0616  -0.0136 108 LEU   A CD1 
2322 C CD2 . LEU   A 108 ? 0.2274 0.2598 0.2716 -0.0210 0.0460  -0.0096 108 LEU   A CD2 
2335 N N   . LEU   A 109 ? 0.1578 0.1545 0.2083 0.0012  0.0178  0.0157  109 LEU   A N   
2336 C CA  . LEU   A 109 ? 0.1489 0.1456 0.1820 0.0013  0.0026  0.0192  109 LEU   A CA  
2337 C C   . LEU   A 109 ? 0.1416 0.1367 0.1664 -0.0097 0.0073  0.0048  109 LEU   A C   
2338 O O   . LEU   A 109 ? 0.1523 0.1273 0.1885 -0.0018 0.0027  0.0037  109 LEU   A O   
2339 C CB  . LEU   A 109 ? 0.1630 0.1585 0.1905 0.0062  -0.0050 0.0298  109 LEU   A CB  
2340 C CG  . LEU   A 109 ? 0.1509 0.1677 0.2003 0.0029  0.0031  0.0370  109 LEU   A CG  
2341 C CD1 . LEU   A 109 ? 0.1550 0.1631 0.2185 0.0045  0.0040  0.0113  109 LEU   A CD1 
2342 C CD2 . LEU   A 109 ? 0.1522 0.1894 0.2257 0.0009  -0.0003 0.0386  109 LEU   A CD2 
2354 N N   . LYS   A 110 ? 0.1381 0.1400 0.1783 -0.0073 -0.0007 0.0012  110 LYS   A N   
2355 C CA  . LYS   A 110 ? 0.1421 0.1341 0.1878 -0.0055 -0.0043 0.0121  110 LYS   A CA  
2356 C C   . LYS   A 110 ? 0.1416 0.1283 0.1764 -0.0083 -0.0029 -0.0006 110 LYS   A C   
2357 O O   . LYS   A 110 ? 0.1355 0.1329 0.1843 -0.0102 0.0016  -0.0045 110 LYS   A O   
2358 C CB  . LYS   A 110 ? 0.1522 0.1400 0.2150 -0.0038 -0.0115 -0.0023 110 LYS   A CB  
2359 C CG  . LYS   A 110 ? 0.1550 0.1342 0.2162 -0.0020 -0.0159 -0.0028 110 LYS   A CG  
2360 C CD  . LYS   A 110 ? 0.1597 0.1482 0.2352 -0.0102 -0.0145 -0.0001 110 LYS   A CD  
2361 C CE  . LYS   A 110 ? 0.1635 0.1514 0.2435 -0.0062 0.0044  -0.0005 110 LYS   A CE  
2362 N NZ  . LYS   A 110 ? 0.1656 0.1478 0.2618 -0.0087 0.0186  0.0027  110 LYS   A NZ  
2376 N N   . SER   A 111 ? 0.1435 0.1344 0.1751 -0.0062 -0.0030 0.0094  111 SER   A N   
2377 C CA  . SER   A 111 ? 0.1382 0.1398 0.1769 -0.0015 0.0083  0.0027  111 SER   A CA  
2378 C C   . SER   A 111 ? 0.1338 0.1338 0.1745 -0.0080 0.0132  0.0077  111 SER   A C   
2379 O O   . SER   A 111 ? 0.1445 0.1232 0.1955 -0.0040 0.0048  0.0089  111 SER   A O   
2380 C CB  . SER   A 111 ? 0.1563 0.1561 0.1884 -0.0002 0.0179  -0.0146 111 SER   A CB  
2381 O OG  . SER   A 111 ? 0.2079 0.1770 0.2066 -0.0031 0.0342  -0.0156 111 SER   A OG  
2387 N N   . ALA   A 112 ? 0.1365 0.1234 0.1841 -0.0021 0.0154  0.0093  112 ALA   A N   
2388 C CA  . ALA   A 112 ? 0.1354 0.1255 0.1676 -0.0024 0.0194  0.0014  112 ALA   A CA  
2389 C C   . ALA   A 112 ? 0.1334 0.1197 0.1737 -0.0024 0.0061  0.0031  112 ALA   A C   
2390 O O   . ALA   A 112 ? 0.1402 0.1227 0.1830 -0.0073 0.0144  0.0112  112 ALA   A O   
2391 C CB  . ALA   A 112 ? 0.1481 0.1238 0.1667 -0.0040 0.0143  0.0007  112 ALA   A CB  
2397 N N   . TYR   A 113 ? 0.1257 0.1267 0.1869 -0.0020 0.0057  0.0161  113 TYR   A N   
2398 C CA  . TYR   A 113 ? 0.1222 0.1251 0.1879 -0.0028 0.0111  0.0171  113 TYR   A CA  
2399 C C   . TYR   A 113 ? 0.1210 0.1231 0.1645 -0.0068 0.0070  0.0096  113 TYR   A C   
2400 O O   . TYR   A 113 ? 0.1272 0.1293 0.1847 -0.0012 0.0124  0.0101  113 TYR   A O   
2401 C CB  . TYR   A 113 ? 0.1219 0.1380 0.1946 0.0004  -0.0008 0.0261  113 TYR   A CB  
2402 C CG  . TYR   A 113 ? 0.1246 0.1410 0.1791 -0.0124 0.0136  0.0239  113 TYR   A CG  
2403 C CD1 . TYR   A 113 ? 0.1294 0.1510 0.1693 0.0007  0.0124  0.0294  113 TYR   A CD1 
2404 C CD2 . TYR   A 113 ? 0.1345 0.1406 0.1841 -0.0102 0.0067  0.0235  113 TYR   A CD2 
2405 C CE1 . TYR   A 113 ? 0.1380 0.1515 0.1686 -0.0016 0.0135  0.0356  113 TYR   A CE1 
2406 C CE2 . TYR   A 113 ? 0.1359 0.1449 0.1792 -0.0096 0.0029  0.0236  113 TYR   A CE2 
2407 C CZ  . TYR   A 113 ? 0.1349 0.1528 0.1657 0.0075  0.0085  0.0341  113 TYR   A CZ  
2408 O OH  . TYR   A 113 ? 0.1322 0.1627 0.1955 0.0127  0.0150  0.0372  113 TYR   A OH  
2418 N N   . GLU   A 114 ? 0.1252 0.1264 0.1781 -0.0044 0.0090  0.0108  114 GLU   A N   
2419 C CA  . GLU   A 114 ? 0.1290 0.1153 0.1833 0.0011  -0.0010 0.0092  114 GLU   A CA  
2420 C C   . GLU   A 114 ? 0.1260 0.1260 0.1742 0.0000  0.0106  0.0141  114 GLU   A C   
2421 O O   . GLU   A 114 ? 0.1333 0.1268 0.1886 -0.0021 0.0012  0.0177  114 GLU   A O   
2422 C CB  . GLU   A 114 ? 0.1303 0.1197 0.1876 -0.0053 0.0037  0.0068  114 GLU   A CB  
2423 C CG  . GLU   A 114 ? 0.1364 0.1245 0.2055 0.0003  0.0065  0.0042  114 GLU   A CG  
2424 C CD  . GLU   A 114 ? 0.1440 0.1323 0.2056 -0.0110 0.0053  0.0052  114 GLU   A CD  
2425 O OE1 . GLU   A 114 ? 0.1480 0.1288 0.2097 -0.0069 0.0155  -0.0038 114 GLU   A OE1 
2426 O OE2 . GLU   A 114 ? 0.1608 0.1330 0.2298 -0.0138 0.0073  -0.0112 114 GLU   A OE2 
2433 N N   . ASN   A 115 ? 0.1298 0.1256 0.1674 0.0001  0.0106  0.0070  115 ASN   A N   
2434 C CA  . ASN   A 115 ? 0.1292 0.1351 0.1673 -0.0054 0.0093  0.0119  115 ASN   A CA  
2435 C C   . ASN   A 115 ? 0.1336 0.1271 0.1637 -0.0103 0.0017  0.0083  115 ASN   A C   
2436 O O   . ASN   A 115 ? 0.1348 0.1399 0.1703 -0.0092 0.0133  0.0173  115 ASN   A O   
2437 C CB  . ASN   A 115 ? 0.1417 0.1392 0.1637 -0.0139 0.0071  0.0102  115 ASN   A CB  
2438 C CG  . ASN   A 115 ? 0.1418 0.1527 0.1728 -0.0169 0.0179  0.0100  115 ASN   A CG  
2439 O OD1 . ASN   A 115 ? 0.1431 0.2513 0.2107 -0.0152 0.0210  0.0208  115 ASN   A OD1 
2440 N ND2 . ASN   A 115 ? 0.1441 0.1393 0.1737 -0.0130 0.0254  0.0151  115 ASN   A ND2 
2447 N N   . PHE   A 116 ? 0.1281 0.1303 0.1729 -0.0010 0.0124  0.0230  116 PHE   A N   
2448 C CA  . PHE   A 116 ? 0.1266 0.1356 0.1619 -0.0010 0.0103  0.0236  116 PHE   A CA  
2449 C C   . PHE   A 116 ? 0.1245 0.1403 0.1696 -0.0046 0.0121  0.0333  116 PHE   A C   
2450 O O   . PHE   A 116 ? 0.1338 0.1476 0.1773 0.0022  0.0103  0.0358  116 PHE   A O   
2451 C CB  . PHE   A 116 ? 0.1262 0.1326 0.1875 0.0004  0.0213  0.0221  116 PHE   A CB  
2452 C CG  . PHE   A 116 ? 0.1307 0.1275 0.1734 -0.0060 0.0105  0.0142  116 PHE   A CG  
2453 C CD1 . PHE   A 116 ? 0.1351 0.1269 0.1677 -0.0076 0.0137  0.0157  116 PHE   A CD1 
2454 C CD2 . PHE   A 116 ? 0.1355 0.1370 0.1869 -0.0043 0.0124  0.0210  116 PHE   A CD2 
2455 C CE1 . PHE   A 116 ? 0.1341 0.1267 0.1865 -0.0148 0.0117  0.0117  116 PHE   A CE1 
2456 C CE2 . PHE   A 116 ? 0.1376 0.1362 0.1971 -0.0034 0.0141  0.0208  116 PHE   A CE2 
2457 C CZ  . PHE   A 116 ? 0.1390 0.1257 0.1823 -0.0020 0.0088  0.0251  116 PHE   A CZ  
2467 N N   . ASN   A 117 ? 0.1234 0.1337 0.1795 -0.0016 0.0066  0.0314  117 ASN   A N   
2468 C CA  . ASN   A 117 ? 0.1303 0.1367 0.1817 -0.0014 0.0098  0.0285  117 ASN   A CA  
2469 C C   . ASN   A 117 ? 0.1279 0.1460 0.1939 -0.0018 0.0103  0.0337  117 ASN   A C   
2470 O O   . ASN   A 117 ? 0.1432 0.1505 0.2245 -0.0061 -0.0078 0.0459  117 ASN   A O   
2471 C CB  . ASN   A 117 ? 0.1325 0.1402 0.1894 0.0007  0.0075  0.0320  117 ASN   A CB  
2472 C CG  . ASN   A 117 ? 0.1317 0.1413 0.1915 -0.0049 0.0095  0.0342  117 ASN   A CG  
2473 O OD1 . ASN   A 117 ? 0.1341 0.1576 0.1994 -0.0097 0.0145  0.0233  117 ASN   A OD1 
2474 N ND2 . ASN   A 117 ? 0.1317 0.1424 0.1987 -0.0000 0.0081  0.0334  117 ASN   A ND2 
2481 N N   . GLN   A 118 ? 0.1266 0.1458 0.1965 -0.0057 0.0014  0.0328  118 GLN   A N   
2482 C CA  . GLN   A 118 ? 0.1348 0.1548 0.1969 -0.0097 -0.0035 0.0210  118 GLN   A CA  
2483 C C   . GLN   A 118 ? 0.1394 0.1612 0.1911 -0.0130 -0.0049 0.0320  118 GLN   A C   
2484 O O   . GLN   A 118 ? 0.1399 0.1937 0.2224 -0.0021 -0.0116 0.0131  118 GLN   A O   
2485 C CB  . GLN   A 118 ? 0.1352 0.1536 0.2179 -0.0060 0.0066  0.0248  118 GLN   A CB  
2486 C CG  . GLN   A 118 ? 0.1331 0.1580 0.2057 -0.0015 0.0081  0.0287  118 GLN   A CG  
2487 C CD  . GLN   A 118 ? 0.1311 0.1604 0.2180 0.0060  0.0104  0.0187  118 GLN   A CD  
2488 O OE1 . GLN   A 118 ? 0.1352 0.1740 0.2319 0.0089  0.0046  0.0150  118 GLN   A OE1 
2489 N NE2 . GLN   A 118 ? 0.1446 0.1580 0.2117 0.0097  0.0049  0.0235  118 GLN   A NE2 
2498 N N   . HIS   A 119 ? 0.1419 0.1645 0.1785 -0.0070 0.0043  0.0324  119 HIS   A N   
2499 C CA  . HIS   A 119 ? 0.1475 0.1692 0.1829 -0.0051 0.0016  0.0415  119 HIS   A CA  
2500 C C   . HIS   A 119 ? 0.1579 0.1724 0.1676 -0.0052 0.0114  0.0418  119 HIS   A C   
2501 O O   . HIS   A 119 ? 0.1654 0.1838 0.1900 -0.0223 0.0012  0.0430  119 HIS   A O   
2502 C CB  . HIS   A 119 ? 0.1573 0.1674 0.2093 -0.0038 0.0169  0.0395  119 HIS   A CB  
2503 C CG  . HIS   A 119 ? 0.1592 0.1704 0.2508 0.0011  0.0245  0.0481  119 HIS   A CG  
2504 N ND1 . HIS   A 119 ? 0.1753 0.1904 0.3035 -0.0121 0.0236  0.0291  119 HIS   A ND1 
2505 C CD2 . HIS   A 119 ? 0.1720 0.1701 0.2684 0.0129  0.0391  0.0639  119 HIS   A CD2 
2506 C CE1 . HIS   A 119 ? 0.1734 0.1841 0.3130 -0.0138 0.0428  0.0462  119 HIS   A CE1 
2507 N NE2 . HIS   A 119 ? 0.1854 0.1739 0.3115 0.0018  0.0564  0.0559  119 HIS   A NE2 
2515 N N   . GLU   A 120 ? 0.1695 0.1983 0.1729 -0.0051 0.0027  0.0565  120 GLU   A N   
2516 C CA  . GLU   A 120 ? 0.1997 0.2366 0.1973 0.0086  0.0037  0.1001  120 GLU   A CA  
2517 C C   . GLU   A 120 ? 0.1732 0.2148 0.1795 -0.0043 -0.0011 0.0749  120 GLU   A C   
2518 O O   . GLU   A 120 ? 0.1713 0.2041 0.1950 -0.0077 -0.0024 0.0739  120 GLU   A O   
2519 C CB  . GLU   A 120 ? 0.2963 0.3327 0.2761 0.0330  0.0075  0.1484  120 GLU   A CB  
2520 C CG  . GLU   A 120 ? 0.4190 0.4385 0.4227 0.0420  0.0076  0.1481  120 GLU   A CG  
2521 C CD  . GLU   A 120 ? 0.5250 0.5289 0.5741 0.0454  0.0149  0.1309  120 GLU   A CD  
2522 O OE1 . GLU   A 120 ? 0.5574 0.5546 0.5994 0.0463  0.0156  0.1253  120 GLU   A OE1 
2523 O OE2 . GLU   A 120 ? 0.6213 0.6213 0.6534 0.0462  0.0198  0.1222  120 GLU   A OE2 
2530 N N   . VAL   A 121 ? 0.1665 0.2128 0.1654 -0.0076 0.0114  0.0584  121 VAL   A N   
2531 C CA  . VAL   A 121 ? 0.1731 0.2160 0.1518 -0.0115 0.0238  0.0648  121 VAL   A CA  
2532 C C   . VAL   A 121 ? 0.1605 0.1990 0.1367 -0.0130 0.0136  0.0501  121 VAL   A C   
2533 O O   . VAL   A 121 ? 0.1610 0.2067 0.1711 -0.0206 -0.0035 0.0436  121 VAL   A O   
2534 C CB  . VAL   A 121 ? 0.2119 0.2519 0.1955 0.0057  0.0393  0.0746  121 VAL   A CB  
2535 C CG1 . VAL   A 121 ? 0.2197 0.2685 0.1992 0.0160  0.0422  0.0735  121 VAL   A CG1 
2536 C CG2 . VAL   A 121 ? 0.2401 0.2715 0.2487 -0.0032 0.0346  0.0529  121 VAL   A CG2 
2546 N N   . LEU   A 122 ? 0.1566 0.1796 0.1570 -0.0152 0.0099  0.0466  122 LEU   A N   
2547 C CA  . LEU   A 122 ? 0.1642 0.1632 0.1551 -0.0162 0.0236  0.0465  122 LEU   A CA  
2548 C C   . LEU   A 122 ? 0.1587 0.1643 0.1574 -0.0186 0.0140  0.0349  122 LEU   A C   
2549 O O   . LEU   A 122 ? 0.1576 0.1729 0.1902 -0.0250 0.0059  0.0392  122 LEU   A O   
2550 C CB  . LEU   A 122 ? 0.1870 0.1663 0.1994 -0.0084 0.0161  0.0546  122 LEU   A CB  
2551 C CG  . LEU   A 122 ? 0.1881 0.1776 0.1867 -0.0100 0.0272  0.0320  122 LEU   A CG  
2552 C CD1 . LEU   A 122 ? 0.2074 0.1832 0.1949 -0.0175 0.0297  0.0362  122 LEU   A CD1 
2553 C CD2 . LEU   A 122 ? 0.1784 0.1693 0.1818 -0.0036 0.0354  0.0266  122 LEU   A CD2 
2565 N N   A LEU   A 123 ? 0.1507 0.1557 0.1515 -0.0222 0.0087  0.0376  123 LEU   A N   
2566 N N   B LEU   A 123 ? 0.1518 0.1589 0.1493 -0.0160 0.0031  0.0269  123 LEU   A N   
2567 C CA  A LEU   A 123 ? 0.1537 0.1585 0.1356 -0.0257 0.0182  0.0393  123 LEU   A CA  
2568 C CA  B LEU   A 123 ? 0.1515 0.1613 0.1360 -0.0128 0.0044  0.0180  123 LEU   A CA  
2569 C C   A LEU   A 123 ? 0.1465 0.1527 0.1389 -0.0228 0.0118  0.0337  123 LEU   A C   
2570 C C   B LEU   A 123 ? 0.1511 0.1538 0.1082 -0.0020 0.0011  0.0114  123 LEU   A C   
2571 O O   A LEU   A 123 ? 0.1329 0.1517 0.1415 -0.0259 0.0166  0.0288  123 LEU   A O   
2572 O O   B LEU   A 123 ? 0.1509 0.1552 0.1244 -0.0015 0.0054  0.0093  123 LEU   A O   
2573 C CB  A LEU   A 123 ? 0.1628 0.1723 0.1375 -0.0277 0.0314  0.0415  123 LEU   A CB  
2574 C CB  B LEU   A 123 ? 0.1521 0.1742 0.1563 -0.0151 0.0054  0.0171  123 LEU   A CB  
2575 C CG  A LEU   A 123 ? 0.1688 0.1910 0.1382 -0.0153 0.0238  0.0250  123 LEU   A CG  
2576 C CG  B LEU   A 123 ? 0.1500 0.1851 0.1561 -0.0139 0.0060  0.0107  123 LEU   A CG  
2577 C CD1 A LEU   A 123 ? 0.1748 0.1954 0.1464 -0.0054 0.0223  0.0167  123 LEU   A CD1 
2578 C CD1 B LEU   A 123 ? 0.1571 0.1860 0.1814 -0.0066 0.0086  0.0028  123 LEU   A CD1 
2579 C CD2 A LEU   A 123 ? 0.1837 0.2024 0.1367 -0.0141 0.0132  0.0170  123 LEU   A CD2 
2580 C CD2 B LEU   A 123 ? 0.1542 0.1933 0.1635 -0.0168 -0.0037 0.0040  123 LEU   A CD2 
2603 N N   A ALA   A 124 ? 0.1486 0.1454 0.1464 -0.0283 0.0154  0.0392  124 ALA   A N   
2604 N N   B ALA   A 124 ? 0.1492 0.1449 0.1010 0.0024  0.0015  0.0059  124 ALA   A N   
2605 C CA  A ALA   A 124 ? 0.1396 0.1406 0.1683 -0.0294 0.0076  0.0355  124 ALA   A CA  
2606 C CA  B ALA   A 124 ? 0.1421 0.1393 0.1105 0.0089  0.0006  0.0094  124 ALA   A CA  
2607 C C   A ALA   A 124 ? 0.1296 0.1302 0.1563 -0.0217 0.0082  0.0221  124 ALA   A C   
2608 C C   B ALA   A 124 ? 0.1404 0.1315 0.1060 0.0032  0.0150  0.0073  124 ALA   A C   
2609 O O   A ALA   A 124 ? 0.1280 0.1377 0.1694 -0.0154 0.0175  0.0122  124 ALA   A O   
2610 O O   B ALA   A 124 ? 0.1445 0.1345 0.1179 -0.0044 0.0230  0.0197  124 ALA   A O   
2611 C CB  A ALA   A 124 ? 0.1449 0.1418 0.1833 -0.0317 0.0074  0.0350  124 ALA   A CB  
2612 C CB  B ALA   A 124 ? 0.1296 0.1358 0.1266 0.0165  -0.0034 0.0095  124 ALA   A CB  
2623 N N   A PRO   A 125 ? 0.1183 0.1255 0.1461 -0.0141 0.0022  0.0211  125 PRO   A N   
2624 N N   B PRO   A 125 ? 0.1449 0.1318 0.1105 0.0050  0.0182  0.0098  125 PRO   A N   
2625 C CA  A PRO   A 125 ? 0.1223 0.1346 0.1377 -0.0091 0.0132  0.0146  125 PRO   A CA  
2626 C CA  B PRO   A 125 ? 0.1526 0.1414 0.1280 0.0022  0.0208  -0.0000 125 PRO   A CA  
2627 C C   A PRO   A 125 ? 0.1187 0.1374 0.1281 -0.0084 0.0107  0.0170  125 PRO   A C   
2628 C C   B PRO   A 125 ? 0.1574 0.1461 0.1374 -0.0062 0.0196  -0.0043 125 PRO   A C   
2629 O O   A PRO   A 125 ? 0.1240 0.1388 0.1311 0.0065  0.0160  0.0213  125 PRO   A O   
2630 O O   B PRO   A 125 ? 0.1595 0.1436 0.1386 -0.0078 0.0262  -0.0071 125 PRO   A O   
2631 C CB  A PRO   A 125 ? 0.1300 0.1233 0.1314 -0.0122 0.0175  0.0135  125 PRO   A CB  
2632 C CB  B PRO   A 125 ? 0.1586 0.1406 0.1279 0.0040  0.0242  0.0024  125 PRO   A CB  
2633 C CG  A PRO   A 125 ? 0.1237 0.1110 0.1360 -0.0067 0.0187  0.0110  125 PRO   A CG  
2634 C CG  B PRO   A 125 ? 0.1652 0.1417 0.1362 0.0065  0.0155  0.0078  125 PRO   A CG  
2635 C CD  A PRO   A 125 ? 0.1173 0.1177 0.1430 -0.0100 0.0143  0.0149  125 PRO   A CD  
2636 C CD  B PRO   A 125 ? 0.1546 0.1390 0.1242 0.0047  0.0202  0.0004  125 PRO   A CD  
2651 N N   A LEU   A 126 ? 0.1191 0.1466 0.1448 -0.0031 0.0046  0.0185  126 LEU   A N   
2652 N N   B LEU   A 126 ? 0.1659 0.1499 0.1411 -0.0059 0.0042  -0.0018 126 LEU   A N   
2653 C CA  A LEU   A 126 ? 0.1208 0.1479 0.1544 -0.0078 0.0072  0.0222  126 LEU   A CA  
2654 C CA  B LEU   A 126 ? 0.1621 0.1421 0.1441 -0.0102 0.0049  0.0009  126 LEU   A CA  
2655 C C   A LEU   A 126 ? 0.1321 0.1420 0.1561 -0.0035 -0.0026 0.0165  126 LEU   A C   
2656 C C   B LEU   A 126 ? 0.1661 0.1318 0.1665 0.0005  0.0196  0.0047  126 LEU   A C   
2657 O O   A LEU   A 126 ? 0.1483 0.1288 0.1412 -0.0050 0.0008  0.0078  126 LEU   A O   
2658 O O   B LEU   A 126 ? 0.1815 0.1173 0.2114 0.0007  0.0377  0.0035  126 LEU   A O   
2659 C CB  A LEU   A 126 ? 0.1275 0.1545 0.1745 -0.0087 0.0087  0.0206  126 LEU   A CB  
2660 C CB  B LEU   A 126 ? 0.1640 0.1508 0.1601 -0.0212 0.0028  0.0040  126 LEU   A CB  
2661 C CG  A LEU   A 126 ? 0.1244 0.1730 0.2029 -0.0039 0.0115  0.0251  126 LEU   A CG  
2662 C CG  B LEU   A 126 ? 0.1610 0.1610 0.1718 -0.0160 0.0076  0.0174  126 LEU   A CG  
2663 C CD1 A LEU   A 126 ? 0.1330 0.1942 0.2102 -0.0166 0.0105  0.0369  126 LEU   A CD1 
2664 C CD1 B LEU   A 126 ? 0.1612 0.1775 0.1872 -0.0141 -0.0048 0.0301  126 LEU   A CD1 
2665 C CD2 A LEU   A 126 ? 0.1334 0.1620 0.2003 -0.0156 0.0201  0.0112  126 LEU   A CD2 
2666 C CD2 B LEU   A 126 ? 0.1672 0.1578 0.1630 -0.0246 0.0113  0.0208  126 LEU   A CD2 
2689 N N   A LEU   A 127 ? 0.1311 0.1501 0.1627 0.0043  0.0032  0.0305  127 LEU   A N   
2690 N N   B LEU   A 127 ? 0.1606 0.1401 0.1533 0.0111  0.0148  0.0222  127 LEU   A N   
2691 C CA  A LEU   A 127 ? 0.1346 0.1492 0.1556 -0.0067 0.0033  0.0209  127 LEU   A CA  
2692 C CA  B LEU   A 127 ? 0.1585 0.1480 0.1495 0.0155  0.0050  0.0222  127 LEU   A CA  
2693 C C   A LEU   A 127 ? 0.1254 0.1423 0.1399 -0.0122 0.0043  0.0225  127 LEU   A C   
2694 C C   B LEU   A 127 ? 0.1561 0.1465 0.1450 0.0154  0.0016  0.0130  127 LEU   A C   
2695 O O   A LEU   A 127 ? 0.1387 0.1405 0.1441 -0.0206 0.0117  0.0304  127 LEU   A O   
2696 O O   B LEU   A 127 ? 0.1661 0.1497 0.1603 0.0102  0.0078  0.0141  127 LEU   A O   
2697 C CB  A LEU   A 127 ? 0.1425 0.1490 0.1552 0.0040  0.0041  0.0181  127 LEU   A CB  
2698 C CB  B LEU   A 127 ? 0.1587 0.1525 0.1496 0.0152  -0.0022 0.0206  127 LEU   A CB  
2699 C CG  A LEU   A 127 ? 0.1467 0.1424 0.1519 0.0098  0.0047  0.0182  127 LEU   A CG  
2700 C CG  B LEU   A 127 ? 0.1572 0.1606 0.1454 0.0170  -0.0051 0.0245  127 LEU   A CG  
2701 C CD1 A LEU   A 127 ? 0.1477 0.1335 0.1660 0.0026  -0.0015 0.0062  127 LEU   A CD1 
2702 C CD1 B LEU   A 127 ? 0.1558 0.1613 0.1655 0.0180  0.0070  0.0277  127 LEU   A CD1 
2703 C CD2 A LEU   A 127 ? 0.1561 0.1411 0.1766 0.0214  0.0003  0.0132  127 LEU   A CD2 
2704 C CD2 B LEU   A 127 ? 0.1664 0.1708 0.1365 0.0179  -0.0201 0.0103  127 LEU   A CD2 
2727 N N   A SER   A 128 ? 0.1376 0.1477 0.1383 -0.0182 -0.0057 0.0213  128 SER   A N   
2728 N N   B SER   A 128 ? 0.1612 0.1489 0.1408 0.0110  -0.0068 0.0134  128 SER   A N   
2729 C CA  A SER   A 128 ? 0.1429 0.1368 0.1291 -0.0165 -0.0060 0.0161  128 SER   A CA  
2730 C CA  B SER   A 128 ? 0.1607 0.1409 0.1306 0.0160  -0.0061 0.0089  128 SER   A CA  
2731 C C   A SER   A 128 ? 0.1535 0.1414 0.1220 -0.0072 -0.0020 0.0155  128 SER   A C   
2732 C C   B SER   A 128 ? 0.1634 0.1439 0.1427 0.0238  -0.0173 0.0152  128 SER   A C   
2733 O O   A SER   A 128 ? 0.1668 0.1522 0.1372 -0.0062 -0.0097 -0.0005 128 SER   A O   
2734 O O   B SER   A 128 ? 0.1734 0.1531 0.1726 0.0332  -0.0167 0.0031  128 SER   A O   
2735 C CB  A SER   A 128 ? 0.1407 0.1355 0.1370 -0.0179 -0.0091 0.0244  128 SER   A CB  
2736 C CB  B SER   A 128 ? 0.1630 0.1426 0.1253 0.0128  0.0041  0.0065  128 SER   A CB  
2737 O OG  A SER   A 128 ? 0.1428 0.1430 0.1593 -0.0129 -0.0013 0.0153  128 SER   A OG  
2738 O OG  B SER   A 128 ? 0.1646 0.1556 0.1443 0.0089  0.0145  0.0132  128 SER   A OG  
2749 N N   A ALA   A 129 ? 0.1451 0.1505 0.1576 -0.0041 -0.0035 0.0215  129 ALA   A N   
2750 N N   B ALA   A 129 ? 0.1552 0.1538 0.1531 0.0162  -0.0219 0.0215  129 ALA   A N   
2751 C CA  A ALA   A 129 ? 0.1454 0.1496 0.1679 -0.0044 -0.0022 0.0178  129 ALA   A CA  
2752 C CA  B ALA   A 129 ? 0.1546 0.1585 0.1614 0.0120  -0.0128 0.0211  129 ALA   A CA  
2753 C C   A ALA   A 129 ? 0.1470 0.1477 0.1644 -0.0058 -0.0112 0.0059  129 ALA   A C   
2754 C C   B ALA   A 129 ? 0.1599 0.1614 0.1518 0.0124  -0.0172 0.0131  129 ALA   A C   
2755 O O   A ALA   A 129 ? 0.1575 0.1456 0.1705 -0.0165 -0.0081 0.0127  129 ALA   A O   
2756 O O   B ALA   A 129 ? 0.1653 0.1630 0.1549 0.0036  -0.0059 0.0193  129 ALA   A O   
2757 C CB  A ALA   A 129 ? 0.1539 0.1580 0.1853 0.0033  0.0046  0.0144  129 ALA   A CB  
2758 C CB  B ALA   A 129 ? 0.1558 0.1673 0.1785 0.0082  -0.0024 0.0246  129 ALA   A CB  
2769 N N   A GLY   A 130 ? 0.1584 0.1484 0.1918 -0.0060 0.0020  -0.0053 130 GLY   A N   
2770 N N   B GLY   A 130 ? 0.1706 0.1633 0.1627 0.0159  -0.0194 0.0135  130 GLY   A N   
2771 C CA  A GLY   A 130 ? 0.1723 0.1464 0.1884 -0.0020 0.0051  -0.0049 130 GLY   A CA  
2772 C CA  B GLY   A 130 ? 0.1869 0.1600 0.1692 0.0142  -0.0186 0.0071  130 GLY   A CA  
2773 C C   A GLY   A 130 ? 0.1727 0.1433 0.1683 -0.0019 -0.0100 0.0024  130 GLY   A C   
2774 C C   B GLY   A 130 ? 0.1933 0.1506 0.1564 0.0108  -0.0326 0.0079  130 GLY   A C   
2775 O O   A GLY   A 130 ? 0.1767 0.1423 0.1771 -0.0071 -0.0200 0.0019  130 GLY   A O   
2776 O O   B GLY   A 130 ? 0.2002 0.1496 0.1641 0.0086  -0.0367 0.0081  130 GLY   A O   
2783 N N   A ILE   A 131 ? 0.1838 0.1489 0.1548 -0.0067 -0.0163 0.0055  131 ILE   A N   
2784 N N   B ILE   A 131 ? 0.2006 0.1467 0.1499 0.0025  -0.0268 0.0214  131 ILE   A N   
2785 C CA  A ILE   A 131 ? 0.1927 0.1485 0.1384 -0.0082 -0.0330 0.0073  131 ILE   A CA  
2786 C CA  B ILE   A 131 ? 0.2063 0.1434 0.1482 0.0002  -0.0335 0.0132  131 ILE   A CA  
2787 C C   A ILE   A 131 ? 0.1754 0.1507 0.1298 -0.0082 -0.0310 0.0183  131 ILE   A C   
2788 C C   B ILE   A 131 ? 0.2079 0.1438 0.1532 -0.0042 -0.0278 0.0171  131 ILE   A C   
2789 O O   A ILE   A 131 ? 0.1708 0.1599 0.1508 -0.0093 -0.0277 0.0295  131 ILE   A O   
2790 O O   B ILE   A 131 ? 0.2132 0.1379 0.1620 -0.0175 -0.0213 0.0141  131 ILE   A O   
2791 C CB  A ILE   A 131 ? 0.2133 0.1618 0.1294 -0.0175 -0.0583 0.0034  131 ILE   A CB  
2792 C CB  B ILE   A 131 ? 0.2064 0.1522 0.1606 0.0012  -0.0368 0.0038  131 ILE   A CB  
2793 C CG1 A ILE   A 131 ? 0.2276 0.1931 0.1527 -0.0236 -0.0603 0.0089  131 ILE   A CG1 
2794 C CG1 B ILE   A 131 ? 0.2007 0.1653 0.1738 0.0008  -0.0332 0.0078  131 ILE   A CG1 
2795 C CG2 A ILE   A 131 ? 0.2245 0.1487 0.1461 -0.0211 -0.0623 -0.0104 131 ILE   A CG2 
2796 C CG2 B ILE   A 131 ? 0.2086 0.1410 0.1569 0.0080  -0.0451 -0.0002 131 ILE   A CG2 
2797 C CD1 A ILE   A 131 ? 0.2303 0.2016 0.1918 -0.0276 -0.0656 0.0036  131 ILE   A CD1 
2798 C CD1 B ILE   A 131 ? 0.1946 0.1668 0.1989 -0.0002 -0.0398 0.0130  131 ILE   A CD1 
2821 N N   A PHE   A 132 ? 0.1697 0.1422 0.1207 -0.0052 -0.0197 0.0106  132 PHE   A N   
2822 N N   B PHE   A 132 ? 0.2051 0.1457 0.1558 0.0057  -0.0245 0.0162  132 PHE   A N   
2823 C CA  A PHE   A 132 ? 0.1722 0.1531 0.1158 -0.0143 0.0018  0.0102  132 PHE   A CA  
2824 C CA  B PHE   A 132 ? 0.2061 0.1619 0.1578 0.0069  -0.0169 0.0149  132 PHE   A CA  
2825 C C   A PHE   A 132 ? 0.1798 0.1675 0.1141 -0.0145 0.0006  0.0110  132 PHE   A C   
2826 C C   B PHE   A 132 ? 0.2097 0.1738 0.1711 0.0008  -0.0171 0.0128  132 PHE   A C   
2827 O O   A PHE   A 132 ? 0.1836 0.1770 0.1298 -0.0198 -0.0033 0.0122  132 PHE   A O   
2828 O O   B PHE   A 132 ? 0.2159 0.1855 0.1899 -0.0081 -0.0154 0.0209  132 PHE   A O   
2829 C CB  A PHE   A 132 ? 0.1642 0.1426 0.1129 -0.0189 0.0025  0.0181  132 PHE   A CB  
2830 C CB  B PHE   A 132 ? 0.2019 0.1625 0.1487 0.0168  -0.0141 0.0202  132 PHE   A CB  
2831 C CG  A PHE   A 132 ? 0.1650 0.1463 0.1189 -0.0120 -0.0107 0.0133  132 PHE   A CG  
2832 C CG  B PHE   A 132 ? 0.1979 0.1668 0.1520 0.0271  -0.0109 0.0268  132 PHE   A CG  
2833 C CD1 A PHE   A 132 ? 0.1696 0.1632 0.1451 -0.0005 -0.0150 -0.0104 132 PHE   A CD1 
2834 C CD1 B PHE   A 132 ? 0.1967 0.1763 0.1609 0.0299  -0.0126 0.0180  132 PHE   A CD1 
2835 C CD2 A PHE   A 132 ? 0.1695 0.1499 0.1327 -0.0051 -0.0188 -0.0022 132 PHE   A CD2 
2836 C CD2 B PHE   A 132 ? 0.1962 0.1661 0.1559 0.0289  -0.0065 0.0274  132 PHE   A CD2 
2837 C CE1 A PHE   A 132 ? 0.1739 0.1646 0.1519 0.0003  -0.0226 -0.0209 132 PHE   A CE1 
2838 C CE1 B PHE   A 132 ? 0.1979 0.1766 0.1642 0.0283  -0.0119 0.0112  132 PHE   A CE1 
2839 C CE2 A PHE   A 132 ? 0.1677 0.1604 0.1513 -0.0004 -0.0214 -0.0109 132 PHE   A CE2 
2840 C CE2 B PHE   A 132 ? 0.1947 0.1691 0.1569 0.0274  -0.0049 0.0185  132 PHE   A CE2 
2841 C CZ  A PHE   A 132 ? 0.1641 0.1639 0.1526 -0.0070 -0.0323 -0.0074 132 PHE   A CZ  
2842 C CZ  B PHE   A 132 ? 0.1928 0.1730 0.1550 0.0259  -0.0121 0.0188  132 PHE   A CZ  
2861 N N   A GLY   A 133 ? 0.1822 0.1737 0.1043 -0.0113 -0.0177 0.0117  133 GLY   A N   
2862 N N   B GLY   A 133 ? 0.2067 0.1751 0.1626 -0.0021 -0.0233 0.0088  133 GLY   A N   
2863 C CA  A GLY   A 133 ? 0.1845 0.1830 0.1172 -0.0049 -0.0236 0.0068  133 GLY   A CA  
2864 C CA  B GLY   A 133 ? 0.2039 0.1806 0.1574 -0.0076 -0.0186 0.0012  133 GLY   A CA  
2865 C C   A GLY   A 133 ? 0.1860 0.1921 0.1134 -0.0074 -0.0357 -0.0008 133 GLY   A C   
2866 C C   B GLY   A 133 ? 0.2019 0.1875 0.1539 -0.0121 -0.0198 -0.0084 133 GLY   A C   
2867 O O   A GLY   A 133 ? 0.2030 0.2068 0.1321 -0.0097 -0.0294 -0.0270 133 GLY   A O   
2868 O O   B GLY   A 133 ? 0.2108 0.2012 0.1364 -0.0120 -0.0036 -0.0161 133 GLY   A O   
2875 N N   A ALA   A 134 ? 0.1859 0.1818 0.1347 -0.0108 -0.0282 0.0025  134 ALA   A N   
2876 N N   B ALA   A 134 ? 0.1977 0.1774 0.1574 -0.0188 -0.0281 -0.0157 134 ALA   A N   
2877 C CA  A ALA   A 134 ? 0.1858 0.1821 0.1663 -0.0065 -0.0290 -0.0039 134 ALA   A CA  
2878 C CA  B ALA   A 134 ? 0.1939 0.1796 0.1730 -0.0214 -0.0288 -0.0115 134 ALA   A CA  
2879 C C   A ALA   A 134 ? 0.1896 0.1940 0.1767 -0.0061 -0.0243 0.0024  134 ALA   A C   
2880 C C   B ALA   A 134 ? 0.1930 0.1919 0.1752 -0.0192 -0.0260 0.0113  134 ALA   A C   
2881 O O   A ALA   A 134 ? 0.1967 0.2000 0.1953 0.0034  0.0017  0.0058  134 ALA   A O   
2882 O O   B ALA   A 134 ? 0.2006 0.1968 0.1994 -0.0158 -0.0123 0.0210  134 ALA   A O   
2883 C CB  A ALA   A 134 ? 0.1926 0.1765 0.1953 -0.0050 -0.0308 0.0043  134 ALA   A CB  
2884 C CB  B ALA   A 134 ? 0.1979 0.1732 0.1862 -0.0224 -0.0313 -0.0190 134 ALA   A CB  
2895 N N   A ASP   A 135 ? 0.1947 0.2047 0.2059 -0.0141 -0.0337 0.0228  135 ASP   A N   
2896 N N   B ASP   A 135 ? 0.1913 0.1988 0.1868 -0.0192 -0.0285 0.0261  135 ASP   A N   
2897 C CA  A ASP   A 135 ? 0.1922 0.2158 0.2423 -0.0254 -0.0454 0.0397  135 ASP   A CA  
2898 C CA  B ASP   A 135 ? 0.1860 0.2056 0.2158 -0.0229 -0.0369 0.0364  135 ASP   A CA  
2899 C C   A ASP   A 135 ? 0.1777 0.2076 0.2411 -0.0167 -0.0348 0.0496  135 ASP   A C   
2900 C C   B ASP   A 135 ? 0.1741 0.2035 0.2243 -0.0156 -0.0293 0.0474  135 ASP   A C   
2901 O O   A ASP   A 135 ? 0.1760 0.1927 0.2502 -0.0188 -0.0345 0.0456  135 ASP   A O   
2902 O O   B ASP   A 135 ? 0.1711 0.1899 0.2273 -0.0203 -0.0285 0.0457  135 ASP   A O   
2903 C CB  A ASP   A 135 ? 0.2128 0.2384 0.2810 -0.0444 -0.0618 0.0326  135 ASP   A CB  
2904 C CB  B ASP   A 135 ? 0.1972 0.2201 0.2413 -0.0315 -0.0494 0.0240  135 ASP   A CB  
2905 C CG  A ASP   A 135 ? 0.2264 0.2576 0.3273 -0.0538 -0.0628 0.0332  135 ASP   A CG  
2906 C CG  B ASP   A 135 ? 0.2040 0.2361 0.2698 -0.0322 -0.0526 0.0218  135 ASP   A CG  
2907 O OD1 A ASP   A 135 ? 0.2201 0.2634 0.3236 -0.0696 -0.0760 0.0481  135 ASP   A OD1 
2908 O OD1 B ASP   A 135 ? 0.2028 0.2354 0.2839 -0.0229 -0.0493 0.0312  135 ASP   A OD1 
2909 O OD2 A ASP   A 135 ? 0.2512 0.2726 0.3730 -0.0476 -0.0359 0.0279  135 ASP   A OD2 
2910 O OD2 B ASP   A 135 ? 0.2095 0.2507 0.2905 -0.0378 -0.0598 0.0169  135 ASP   A OD2 
2919 N N   . PRO   A 136 ? 0.1646 0.2126 0.2397 -0.0042 -0.0169 0.0649  136 PRO   A N   
2920 C CA  . PRO   A 136 ? 0.1540 0.2162 0.2468 -0.0030 0.0011  0.0566  136 PRO   A CA  
2921 C C   . PRO   A 136 ? 0.1341 0.2111 0.2457 0.0011  -0.0038 0.0493  136 PRO   A C   
2922 O O   . PRO   A 136 ? 0.1374 0.2047 0.2348 -0.0027 -0.0062 0.0475  136 PRO   A O   
2923 C CB  . PRO   A 136 ? 0.1778 0.2130 0.2741 0.0041  -0.0011 0.0585  136 PRO   A CB  
2924 C CG  . PRO   A 136 ? 0.1993 0.2299 0.3019 0.0128  -0.0068 0.0571  136 PRO   A CG  
2925 C CD  . PRO   A 136 ? 0.1803 0.2211 0.2707 0.0129  -0.0001 0.0816  136 PRO   A CD  
2933 N N   A ILE   A 137 ? 0.1386 0.2120 0.2529 -0.0073 -0.0125 0.0561  137 ILE   A N   
2934 N N   B ILE   A 137 ? 0.1415 0.2131 0.2473 -0.0053 -0.0116 0.0516  137 ILE   A N   
2935 C CA  A ILE   A 137 ? 0.1422 0.2200 0.2581 -0.0165 -0.0243 0.0445  137 ILE   A CA  
2936 C CA  B ILE   A 137 ? 0.1479 0.2200 0.2484 -0.0109 -0.0220 0.0423  137 ILE   A CA  
2937 C C   A ILE   A 137 ? 0.1419 0.2125 0.2391 -0.0194 -0.0245 0.0470  137 ILE   A C   
2938 C C   B ILE   A 137 ? 0.1472 0.2146 0.2342 -0.0157 -0.0194 0.0445  137 ILE   A C   
2939 O O   A ILE   A 137 ? 0.1502 0.2140 0.2378 -0.0238 -0.0146 0.0457  137 ILE   A O   
2940 O O   B ILE   A 137 ? 0.1531 0.2153 0.2327 -0.0191 -0.0113 0.0438  137 ILE   A O   
2941 C CB  A ILE   A 137 ? 0.1529 0.2345 0.2781 -0.0225 -0.0361 0.0422  137 ILE   A CB  
2942 C CB  B ILE   A 137 ? 0.1590 0.2314 0.2624 -0.0118 -0.0350 0.0386  137 ILE   A CB  
2943 C CG1 A ILE   A 137 ? 0.1691 0.2572 0.3106 -0.0214 -0.0342 0.0432  137 ILE   A CG1 
2944 C CG1 B ILE   A 137 ? 0.1701 0.2483 0.2866 -0.0058 -0.0415 0.0378  137 ILE   A CG1 
2945 C CG2 A ILE   A 137 ? 0.1621 0.2327 0.2878 -0.0271 -0.0467 0.0314  137 ILE   A CG2 
2946 C CG2 B ILE   A 137 ? 0.1672 0.2301 0.2685 -0.0172 -0.0389 0.0308  137 ILE   A CG2 
2947 C CD1 A ILE   A 137 ? 0.1860 0.2732 0.3338 -0.0153 -0.0261 0.0469  137 ILE   A CD1 
2948 C CD1 B ILE   A 137 ? 0.1788 0.2591 0.3022 -0.0013 -0.0401 0.0403  137 ILE   A CD1 
2971 N N   . HIS   A 138 ? 0.1488 0.2167 0.2333 -0.0156 -0.0114 0.0387  138 HIS   A N   
2972 C CA  . HIS   A 138 ? 0.1567 0.2125 0.2027 -0.0156 -0.0037 0.0336  138 HIS   A CA  
2973 C C   . HIS   A 138 ? 0.1481 0.1954 0.1977 -0.0082 -0.0075 0.0415  138 HIS   A C   
2974 O O   . HIS   A 138 ? 0.1607 0.1930 0.2112 -0.0136 -0.0061 0.0333  138 HIS   A O   
2975 C CB  . HIS   A 138 ? 0.1759 0.2266 0.2017 -0.0171 -0.0150 0.0148  138 HIS   A CB  
2976 C CG  . HIS   A 138 ? 0.1912 0.2378 0.2115 -0.0222 -0.0138 0.0029  138 HIS   A CG  
2977 N ND1 . HIS   A 138 ? 0.2020 0.2502 0.2396 -0.0219 -0.0104 -0.0078 138 HIS   A ND1 
2978 C CD2 . HIS   A 138 ? 0.1902 0.2460 0.2171 -0.0163 -0.0151 0.0106  138 HIS   A CD2 
2979 C CE1 . HIS   A 138 ? 0.2039 0.2589 0.2454 -0.0136 -0.0178 -0.0103 138 HIS   A CE1 
2980 N NE2 . HIS   A 138 ? 0.1992 0.2568 0.2233 -0.0142 -0.0079 -0.0022 138 HIS   A NE2 
2989 N N   . SER   A 139 ? 0.1409 0.1836 0.2043 -0.0114 -0.0089 0.0548  139 SER   A N   
2990 C CA  . SER   A 139 ? 0.1370 0.1842 0.1989 -0.0079 -0.0066 0.0518  139 SER   A CA  
2991 C C   . SER   A 139 ? 0.1329 0.1745 0.1985 -0.0098 0.0033  0.0430  139 SER   A C   
2992 O O   . SER   A 139 ? 0.1278 0.1684 0.2127 -0.0116 -0.0043 0.0461  139 SER   A O   
2993 C CB  . SER   A 139 ? 0.1367 0.1784 0.2061 -0.0067 -0.0053 0.0528  139 SER   A CB  
2994 O OG  . SER   A 139 ? 0.1430 0.1759 0.2108 -0.0137 -0.0144 0.0579  139 SER   A OG  
3000 N N   . LEU   A 140 ? 0.1304 0.1800 0.1973 -0.0048 -0.0025 0.0524  140 LEU   A N   
3001 C CA  . LEU   A 140 ? 0.1275 0.1763 0.2132 -0.0016 0.0031  0.0575  140 LEU   A CA  
3002 C C   . LEU   A 140 ? 0.1246 0.1854 0.2044 -0.0101 -0.0038 0.0542  140 LEU   A C   
3003 O O   . LEU   A 140 ? 0.1287 0.1839 0.2276 -0.0080 -0.0077 0.0537  140 LEU   A O   
3004 C CB  . LEU   A 140 ? 0.1344 0.1873 0.2206 -0.0027 0.0031  0.0551  140 LEU   A CB  
3005 C CG  . LEU   A 140 ? 0.1322 0.2008 0.2289 -0.0171 0.0081  0.0636  140 LEU   A CG  
3006 C CD1 . LEU   A 140 ? 0.1395 0.2056 0.2318 -0.0138 -0.0001 0.0638  140 LEU   A CD1 
3007 C CD2 . LEU   A 140 ? 0.1393 0.2208 0.2343 -0.0134 0.0203  0.0712  140 LEU   A CD2 
3019 N N   . ARG   A 141 ? 0.1316 0.1895 0.2184 -0.0094 -0.0109 0.0528  141 ARG   A N   
3020 C CA  . ARG   A 141 ? 0.1518 0.2027 0.2368 -0.0267 -0.0171 0.0265  141 ARG   A CA  
3021 C C   . ARG   A 141 ? 0.1483 0.1780 0.2188 -0.0154 -0.0146 0.0288  141 ARG   A C   
3022 O O   . ARG   A 141 ? 0.1410 0.1722 0.2431 -0.0219 0.0029  0.0245  141 ARG   A O   
3023 C CB  . ARG   A 141 ? 0.1651 0.2219 0.2720 -0.0359 -0.0289 0.0109  141 ARG   A CB  
3024 C CG  . ARG   A 141 ? 0.1958 0.2502 0.3128 -0.0337 -0.0197 0.0127  141 ARG   A CG  
3025 C CD  . ARG   A 141 ? 0.2175 0.2636 0.3468 -0.0389 -0.0149 0.0133  141 ARG   A CD  
3026 N NE  . ARG   A 141 ? 0.2056 0.2777 0.3665 -0.0398 -0.0261 0.0149  141 ARG   A NE  
3027 C CZ  . ARG   A 141 ? 0.2071 0.2907 0.3706 -0.0497 -0.0240 0.0219  141 ARG   A CZ  
3028 N NH1 . ARG   A 141 ? 0.1936 0.2944 0.3587 -0.0518 -0.0113 0.0062  141 ARG   A NH1 
3029 N NH2 . ARG   A 141 ? 0.2115 0.2938 0.3879 -0.0470 -0.0354 0.0336  141 ARG   A NH2 
3043 N N   . VAL   A 142 ? 0.1381 0.1742 0.2029 -0.0139 -0.0062 0.0225  142 VAL   A N   
3044 C CA  . VAL   A 142 ? 0.1408 0.1667 0.2105 -0.0183 0.0075  0.0113  142 VAL   A CA  
3045 C C   . VAL   A 142 ? 0.1267 0.1575 0.2015 -0.0201 0.0078  0.0176  142 VAL   A C   
3046 O O   . VAL   A 142 ? 0.1365 0.1572 0.2136 -0.0046 0.0036  0.0229  142 VAL   A O   
3047 C CB  . VAL   A 142 ? 0.1537 0.1726 0.1917 -0.0133 0.0024  0.0194  142 VAL   A CB  
3048 C CG1 . VAL   A 142 ? 0.1558 0.1695 0.1950 -0.0195 0.0051  0.0071  142 VAL   A CG1 
3049 C CG2 . VAL   A 142 ? 0.1677 0.1955 0.2132 -0.0053 0.0015  0.0329  142 VAL   A CG2 
3059 N N   . CYS   A 143 ? 0.1326 0.1623 0.1947 -0.0156 0.0006  0.0313  143 CYS   A N   
3060 C CA  . CYS   A 143 ? 0.1345 0.1581 0.2038 -0.0112 0.0033  0.0314  143 CYS   A CA  
3061 C C   . CYS   A 143 ? 0.1307 0.1563 0.2106 -0.0111 -0.0005 0.0389  143 CYS   A C   
3062 O O   . CYS   A 143 ? 0.1293 0.1529 0.2129 -0.0071 -0.0013 0.0417  143 CYS   A O   
3063 C CB  . CYS   A 143 ? 0.1451 0.1633 0.2027 -0.0053 0.0201  0.0396  143 CYS   A CB  
3064 S SG  . CYS   A 143 ? 0.1587 0.1687 0.1918 0.0030  0.0130  0.0305  143 CYS   A SG  
3070 N N   . VAL   A 144 ? 0.1273 0.1623 0.2287 -0.0112 0.0045  0.0486  144 VAL   A N   
3071 C CA  . VAL   A 144 ? 0.1359 0.1702 0.2708 -0.0137 0.0131  0.0507  144 VAL   A CA  
3072 C C   . VAL   A 144 ? 0.1383 0.1623 0.2514 -0.0208 -0.0215 0.0411  144 VAL   A C   
3073 O O   . VAL   A 144 ? 0.1562 0.1670 0.2605 -0.0106 -0.0201 0.0451  144 VAL   A O   
3074 C CB  . VAL   A 144 ? 0.1657 0.1975 0.3381 -0.0007 0.0356  0.0621  144 VAL   A CB  
3075 C CG1 . VAL   A 144 ? 0.1802 0.2233 0.3776 -0.0048 0.0214  0.0592  144 VAL   A CG1 
3076 C CG2 . VAL   A 144 ? 0.1501 0.2053 0.3400 -0.0024 0.0481  0.0750  144 VAL   A CG2 
3086 N N   . ASP   A 145 ? 0.1447 0.1622 0.2649 -0.0207 -0.0141 0.0346  145 ASP   A N   
3087 C CA  . ASP   A 145 ? 0.1583 0.1628 0.2738 -0.0306 -0.0189 0.0285  145 ASP   A CA  
3088 C C   . ASP   A 145 ? 0.1592 0.1505 0.2643 -0.0151 -0.0067 0.0121  145 ASP   A C   
3089 O O   . ASP   A 145 ? 0.1797 0.1565 0.3161 -0.0188 -0.0157 -0.0246 145 ASP   A O   
3090 C CB  . ASP   A 145 ? 0.1783 0.1920 0.2995 -0.0370 -0.0333 0.0244  145 ASP   A CB  
3091 C CG  . ASP   A 145 ? 0.1964 0.2332 0.3344 -0.0557 -0.0456 0.0365  145 ASP   A CG  
3092 O OD1 . ASP   A 145 ? 0.1896 0.2418 0.3523 -0.0683 -0.0399 0.0404  145 ASP   A OD1 
3093 O OD2 . ASP   A 145 ? 0.2189 0.2571 0.3316 -0.0675 -0.0567 0.0400  145 ASP   A OD2 
3098 N N   . THR   A 146 ? 0.1404 0.1458 0.2322 -0.0125 0.0010  0.0164  146 THR   A N   
3099 C CA  . THR   A 146 ? 0.1355 0.1422 0.2105 -0.0060 0.0030  0.0133  146 THR   A CA  
3100 C C   . THR   A 146 ? 0.1312 0.1431 0.2113 -0.0026 0.0080  0.0193  146 THR   A C   
3101 O O   . THR   A 146 ? 0.1425 0.1538 0.2293 0.0041  0.0022  0.0173  146 THR   A O   
3102 C CB  . THR   A 146 ? 0.1390 0.1470 0.1992 -0.0011 0.0006  0.0193  146 THR   A CB  
3103 O OG1 . THR   A 146 ? 0.1395 0.1672 0.2083 -0.0028 0.0014  0.0155  146 THR   A OG1 
3104 C CG2 . THR   A 146 ? 0.1366 0.1515 0.2210 -0.0097 0.0064  0.0146  146 THR   A CG2 
3112 N N   . VAL   A 147 ? 0.1248 0.1439 0.2060 -0.0027 0.0088  0.0210  147 VAL   A N   
3113 C CA  . VAL   A 147 ? 0.1279 0.1483 0.2020 -0.0090 0.0136  0.0283  147 VAL   A CA  
3114 C C   . VAL   A 147 ? 0.1296 0.1396 0.2228 -0.0112 0.0085  0.0374  147 VAL   A C   
3115 O O   . VAL   A 147 ? 0.1352 0.1533 0.2518 -0.0134 0.0039  0.0298  147 VAL   A O   
3116 C CB  . VAL   A 147 ? 0.1491 0.1435 0.1941 -0.0101 0.0233  0.0258  147 VAL   A CB  
3117 C CG1 . VAL   A 147 ? 0.1845 0.1490 0.1933 -0.0029 0.0244  0.0325  147 VAL   A CG1 
3118 C CG2 . VAL   A 147 ? 0.1550 0.1455 0.1998 -0.0146 0.0103  0.0197  147 VAL   A CG2 
3128 N N   . ARG   A 148 ? 0.1340 0.1473 0.2337 -0.0118 0.0138  0.0460  148 ARG   A N   
3129 C CA  . ARG   A 148 ? 0.1394 0.1445 0.2175 -0.0077 0.0042  0.0533  148 ARG   A CA  
3130 C C   . ARG   A 148 ? 0.1538 0.1546 0.2150 -0.0150 0.0113  0.0633  148 ARG   A C   
3131 O O   . ARG   A 148 ? 0.1843 0.1696 0.2408 -0.0205 0.0182  0.0571  148 ARG   A O   
3132 C CB  . ARG   A 148 ? 0.1476 0.1457 0.2422 -0.0038 0.0119  0.0533  148 ARG   A CB  
3133 C CG  . ARG   A 148 ? 0.1631 0.1530 0.2803 -0.0058 0.0274  0.0308  148 ARG   A CG  
3134 C CD  . ARG   A 148 ? 0.1799 0.1518 0.2999 -0.0045 0.0380  0.0504  148 ARG   A CD  
3135 N NE  . ARG   A 148 ? 0.1696 0.1573 0.2889 0.0119  0.0425  0.0564  148 ARG   A NE  
3136 C CZ  . ARG   A 148 ? 0.1746 0.1430 0.2696 0.0021  0.0438  0.0493  148 ARG   A CZ  
3137 N NH1 . ARG   A 148 ? 0.1870 0.1475 0.2757 -0.0091 0.0432  0.0204  148 ARG   A NH1 
3138 N NH2 . ARG   A 148 ? 0.1658 0.1632 0.2728 0.0099  0.0403  0.0510  148 ARG   A NH2 
3152 N N   . THR   A 149 ? 0.1537 0.1673 0.2009 -0.0221 -0.0026 0.0503  149 THR   A N   
3153 C CA  . THR   A 149 ? 0.1545 0.1644 0.2024 -0.0125 0.0042  0.0470  149 THR   A CA  
3154 C C   . THR   A 149 ? 0.1491 0.1643 0.2031 -0.0224 0.0090  0.0502  149 THR   A C   
3155 O O   . THR   A 149 ? 0.1460 0.1737 0.2271 -0.0199 0.0092  0.0490  149 THR   A O   
3156 C CB  . THR   A 149 ? 0.1552 0.1760 0.2087 -0.0126 0.0053  0.0406  149 THR   A CB  
3157 O OG1 . THR   A 149 ? 0.1587 0.1697 0.2217 -0.0225 0.0073  0.0414  149 THR   A OG1 
3158 C CG2 . THR   A 149 ? 0.1507 0.1902 0.2149 -0.0084 -0.0008 0.0427  149 THR   A CG2 
3166 N N   . ASN   A 150 ? 0.1488 0.1708 0.1962 -0.0059 0.0007  0.0629  150 ASN   A N   
3167 C CA  . ASN   A 150 ? 0.1671 0.1859 0.2011 -0.0061 0.0107  0.0567  150 ASN   A CA  
3168 C C   . ASN   A 150 ? 0.1491 0.1681 0.2056 -0.0113 0.0052  0.0546  150 ASN   A C   
3169 O O   . ASN   A 150 ? 0.1609 0.1820 0.2424 -0.0108 -0.0117 0.0449  150 ASN   A O   
3170 C CB  . ASN   A 150 ? 0.2134 0.2198 0.2285 -0.0039 0.0340  0.0766  150 ASN   A CB  
3171 C CG  . ASN   A 150 ? 0.2684 0.2517 0.3103 -0.0041 0.0100  0.0830  150 ASN   A CG  
3172 O OD1 . ASN   A 150 ? 0.2882 0.2572 0.3330 -0.0186 0.0154  0.1050  150 ASN   A OD1 
3173 N ND2 . ASN   A 150 ? 0.2984 0.2785 0.3462 -0.0002 -0.0001 0.0748  150 ASN   A ND2 
3180 N N   . VAL   A 151 ? 0.1519 0.1581 0.2087 -0.0125 0.0097  0.0476  151 VAL   A N   
3181 C CA  . VAL   A 151 ? 0.1549 0.1600 0.1990 -0.0148 0.0139  0.0466  151 VAL   A CA  
3182 C C   . VAL   A 151 ? 0.1527 0.1508 0.2104 -0.0248 0.0175  0.0481  151 VAL   A C   
3183 O O   . VAL   A 151 ? 0.1568 0.1592 0.2508 -0.0202 0.0164  0.0463  151 VAL   A O   
3184 C CB  . VAL   A 151 ? 0.1845 0.1830 0.1998 -0.0046 0.0133  0.0468  151 VAL   A CB  
3185 C CG1 . VAL   A 151 ? 0.1760 0.2073 0.2265 -0.0086 0.0060  0.0388  151 VAL   A CG1 
3186 C CG2 . VAL   A 151 ? 0.2022 0.1775 0.1963 -0.0042 0.0280  0.0488  151 VAL   A CG2 
3196 N N   . TYR   A 152 ? 0.1492 0.1545 0.2011 -0.0176 0.0171  0.0479  152 TYR   A N   
3197 C CA  . TYR   A 152 ? 0.1517 0.1641 0.1777 -0.0173 0.0186  0.0451  152 TYR   A CA  
3198 C C   . TYR   A 152 ? 0.1476 0.1586 0.1686 -0.0146 0.0250  0.0440  152 TYR   A C   
3199 O O   . TYR   A 152 ? 0.1520 0.1559 0.1873 -0.0238 0.0216  0.0388  152 TYR   A O   
3200 C CB  . TYR   A 152 ? 0.1622 0.1708 0.1862 -0.0047 0.0275  0.0497  152 TYR   A CB  
3201 C CG  . TYR   A 152 ? 0.1725 0.1914 0.1828 -0.0117 0.0303  0.0526  152 TYR   A CG  
3202 C CD1 . TYR   A 152 ? 0.1803 0.2134 0.2000 0.0004  0.0301  0.0599  152 TYR   A CD1 
3203 C CD2 . TYR   A 152 ? 0.1759 0.2004 0.1806 -0.0351 0.0207  0.0488  152 TYR   A CD2 
3204 C CE1 . TYR   A 152 ? 0.2058 0.2274 0.2182 0.0024  0.0204  0.0730  152 TYR   A CE1 
3205 C CE2 . TYR   A 152 ? 0.1997 0.2209 0.2022 -0.0258 0.0299  0.0534  152 TYR   A CE2 
3206 C CZ  . TYR   A 152 ? 0.2203 0.2256 0.2055 -0.0115 0.0243  0.0786  152 TYR   A CZ  
3207 O OH  . TYR   A 152 ? 0.2485 0.2505 0.2463 -0.0007 0.0281  0.0941  152 TYR   A OH  
3217 N N   A LEU   A 153 ? 0.1323 0.1550 0.1906 -0.0184 0.0227  0.0479  153 LEU   A N   
3218 N N   B LEU   A 153 ? 0.1497 0.1590 0.1720 -0.0130 0.0196  0.0430  153 LEU   A N   
3219 C CA  A LEU   A 153 ? 0.1250 0.1464 0.2048 -0.0109 0.0147  0.0495  153 LEU   A CA  
3220 C CA  B LEU   A 153 ? 0.1552 0.1513 0.1645 -0.0017 0.0199  0.0350  153 LEU   A CA  
3221 C C   A LEU   A 153 ? 0.1288 0.1461 0.1992 -0.0111 0.0281  0.0445  153 LEU   A C   
3222 C C   B LEU   A 153 ? 0.1653 0.1586 0.1673 0.0001  0.0262  0.0303  153 LEU   A C   
3223 O O   A LEU   A 153 ? 0.1361 0.1576 0.2229 -0.0116 0.0358  0.0313  153 LEU   A O   
3224 O O   B LEU   A 153 ? 0.1669 0.1695 0.1897 -0.0028 0.0361  0.0396  153 LEU   A O   
3225 C CB  A LEU   A 153 ? 0.1202 0.1407 0.2110 -0.0115 0.0056  0.0416  153 LEU   A CB  
3226 C CB  B LEU   A 153 ? 0.1558 0.1450 0.1670 0.0114  0.0086  0.0387  153 LEU   A CB  
3227 C CG  A LEU   A 153 ? 0.1219 0.1443 0.2134 -0.0122 0.0216  0.0292  153 LEU   A CG  
3228 C CG  B LEU   A 153 ? 0.1637 0.1465 0.1594 0.0190  0.0138  0.0389  153 LEU   A CG  
3229 C CD1 A LEU   A 153 ? 0.1293 0.1409 0.2182 -0.0080 0.0023  0.0295  153 LEU   A CD1 
3230 C CD1 B LEU   A 153 ? 0.1642 0.1447 0.1545 0.0260  0.0177  0.0352  153 LEU   A CD1 
3231 C CD2 A LEU   A 153 ? 0.1348 0.1564 0.2135 -0.0183 0.0370  0.0044  153 LEU   A CD2 
3232 C CD2 B LEU   A 153 ? 0.1732 0.1556 0.1815 0.0182  0.0161  0.0256  153 LEU   A CD2 
3255 N N   A ALA   A 154 ? 0.1269 0.1406 0.1814 -0.0081 0.0325  0.0366  154 ALA   A N   
3256 N N   B ALA   A 154 ? 0.1804 0.1616 0.1545 0.0002  0.0257  0.0170  154 ALA   A N   
3257 C CA  A ALA   A 154 ? 0.1382 0.1478 0.2037 -0.0048 0.0287  0.0255  154 ALA   A CA  
3258 C CA  B ALA   A 154 ? 0.1973 0.1699 0.1813 0.0022  0.0272  0.0133  154 ALA   A CA  
3259 C C   A ALA   A 154 ? 0.1454 0.1413 0.2116 -0.0064 0.0253  0.0374  154 ALA   A C   
3260 C C   B ALA   A 154 ? 0.2109 0.1844 0.1885 -0.0029 0.0320  0.0292  154 ALA   A C   
3261 O O   A ALA   A 154 ? 0.1565 0.1499 0.1994 -0.0021 0.0186  0.0245  154 ALA   A O   
3262 O O   B ALA   A 154 ? 0.2065 0.1855 0.1717 -0.0081 0.0363  0.0427  154 ALA   A O   
3263 C CB  A ALA   A 154 ? 0.1508 0.1570 0.2075 0.0050  0.0229  0.0122  154 ALA   A CB  
3264 C CB  B ALA   A 154 ? 0.2011 0.1651 0.1951 0.0035  0.0217  -0.0031 154 ALA   A CB  
3275 N N   A VAL   A 155 ? 0.1513 0.1477 0.2230 0.0015  0.0263  0.0605  155 VAL   A N   
3276 N N   B VAL   A 155 ? 0.2314 0.2010 0.2213 0.0009  0.0266  0.0331  155 VAL   A N   
3277 C CA  A VAL   A 155 ? 0.1654 0.1567 0.2300 0.0056  0.0153  0.0793  155 VAL   A CA  
3278 C CA  B VAL   A 155 ? 0.2542 0.2213 0.2619 0.0046  0.0139  0.0353  155 VAL   A CA  
3279 C C   A VAL   A 155 ? 0.1773 0.1677 0.2597 0.0101  0.0127  0.0803  155 VAL   A C   
3280 C C   B VAL   A 155 ? 0.2750 0.2407 0.3003 0.0127  0.0151  0.0399  155 VAL   A C   
3281 O O   A VAL   A 155 ? 0.1665 0.1612 0.2439 0.0197  0.0093  0.0502  155 VAL   A O   
3282 O O   B VAL   A 155 ? 0.2714 0.2379 0.3093 0.0147  0.0187  0.0363  155 VAL   A O   
3283 C CB  A VAL   A 155 ? 0.1654 0.1610 0.2095 0.0169  0.0012  0.0731  155 VAL   A CB  
3284 C CB  B VAL   A 155 ? 0.2560 0.2222 0.2700 0.0062  0.0025  0.0268  155 VAL   A CB  
3285 C CG1 A VAL   A 155 ? 0.1735 0.1686 0.2335 0.0253  -0.0009 0.0702  155 VAL   A CG1 
3286 C CG1 B VAL   A 155 ? 0.2584 0.2288 0.2703 0.0089  0.0007  0.0178  155 VAL   A CG1 
3287 C CG2 A VAL   A 155 ? 0.1701 0.1714 0.2197 0.0294  -0.0048 0.0452  155 VAL   A CG2 
3288 C CG2 B VAL   A 155 ? 0.2548 0.2218 0.2688 0.0064  0.0020  0.0206  155 VAL   A CG2 
3307 N N   A PHE   A 156 ? 0.1909 0.1755 0.2883 0.0132  0.0186  0.0961  156 PHE   A N   
3308 N N   B PHE   A 156 ? 0.2991 0.2621 0.3258 0.0189  0.0099  0.0451  156 PHE   A N   
3309 C CA  A PHE   A 156 ? 0.2043 0.1793 0.3271 0.0162  0.0060  0.1041  156 PHE   A CA  
3310 C CA  B PHE   A 156 ? 0.3266 0.2843 0.3533 0.0217  0.0068  0.0405  156 PHE   A CA  
3311 C C   A PHE   A 156 ? 0.2052 0.1878 0.3387 0.0252  0.0105  0.1126  156 PHE   A C   
3312 C C   B PHE   A 156 ? 0.3372 0.2999 0.3732 0.0173  0.0131  0.0433  156 PHE   A C   
3313 O O   A PHE   A 156 ? 0.2076 0.2016 0.3687 0.0202  0.0203  0.0818  156 PHE   A O   
3314 O O   B PHE   A 156 ? 0.3398 0.3035 0.3708 0.0178  0.0133  0.0370  156 PHE   A O   
3315 C CB  A PHE   A 156 ? 0.2265 0.1787 0.3491 0.0115  -0.0075 0.1114  156 PHE   A CB  
3316 C CB  B PHE   A 156 ? 0.3446 0.2932 0.3652 0.0301  -0.0053 0.0312  156 PHE   A CB  
3317 C CG  A PHE   A 156 ? 0.2506 0.1887 0.3692 0.0212  -0.0309 0.1023  156 PHE   A CG  
3318 C CG  B PHE   A 156 ? 0.3610 0.3031 0.3748 0.0387  -0.0159 0.0176  156 PHE   A CG  
3319 C CD1 A PHE   A 156 ? 0.2668 0.2061 0.3847 0.0254  -0.0343 0.0840  156 PHE   A CD1 
3320 C CD1 B PHE   A 156 ? 0.3678 0.3078 0.3799 0.0427  -0.0199 0.0121  156 PHE   A CD1 
3321 C CD2 A PHE   A 156 ? 0.2657 0.2004 0.3819 0.0272  -0.0371 0.1005  156 PHE   A CD2 
3322 C CD2 B PHE   A 156 ? 0.3687 0.3079 0.3768 0.0420  -0.0205 0.0124  156 PHE   A CD2 
3323 C CE1 A PHE   A 156 ? 0.2814 0.2181 0.4010 0.0273  -0.0323 0.0699  156 PHE   A CE1 
3324 C CE1 B PHE   A 156 ? 0.3708 0.3103 0.3805 0.0446  -0.0221 0.0074  156 PHE   A CE1 
3325 C CE2 A PHE   A 156 ? 0.2804 0.2115 0.3933 0.0325  -0.0357 0.0813  156 PHE   A CE2 
3326 C CE2 B PHE   A 156 ? 0.3716 0.3109 0.3794 0.0445  -0.0233 0.0081  156 PHE   A CE2 
3327 C CZ  A PHE   A 156 ? 0.2840 0.2201 0.4004 0.0345  -0.0326 0.0671  156 PHE   A CZ  
3328 C CZ  B PHE   A 156 ? 0.3721 0.3103 0.3801 0.0455  -0.0235 0.0046  156 PHE   A CZ  
3347 N N   A ASP   A 157 ? 0.2010 0.1980 0.3170 0.0189  0.0062  0.1299  157 ASP   A N   
3348 N N   B ASP   A 157 ? 0.3453 0.3119 0.3982 0.0126  0.0221  0.0481  157 ASP   A N   
3349 C CA  A ASP   A 157 ? 0.2051 0.2194 0.3230 0.0255  0.0034  0.1302  157 ASP   A CA  
3350 C CA  B ASP   A 157 ? 0.3519 0.3214 0.4098 0.0075  0.0281  0.0530  157 ASP   A CA  
3351 C C   A ASP   A 157 ? 0.1852 0.2329 0.3365 0.0355  0.0256  0.1433  157 ASP   A C   
3352 C C   B ASP   A 157 ? 0.3336 0.3186 0.4016 0.0039  0.0451  0.0589  157 ASP   A C   
3353 O O   A ASP   A 157 ? 0.1704 0.2300 0.3263 0.0368  0.0354  0.1485  157 ASP   A O   
3354 O O   B ASP   A 157 ? 0.3331 0.3197 0.4005 0.0057  0.0463  0.0564  157 ASP   A O   
3355 C CB  A ASP   A 157 ? 0.2322 0.2289 0.3279 0.0260  -0.0136 0.1132  157 ASP   A CB  
3356 C CB  B ASP   A 157 ? 0.3698 0.3295 0.4229 0.0073  0.0126  0.0551  157 ASP   A CB  
3357 C CG  A ASP   A 157 ? 0.2594 0.2370 0.3531 0.0293  -0.0384 0.1046  157 ASP   A CG  
3358 C CG  B ASP   A 157 ? 0.3865 0.3362 0.4400 0.0082  -0.0018 0.0557  157 ASP   A CG  
3359 O OD1 A ASP   A 157 ? 0.2841 0.2494 0.3724 0.0196  -0.0682 0.0961  157 ASP   A OD1 
3360 O OD1 B ASP   A 157 ? 0.3923 0.3408 0.4440 0.0094  -0.0082 0.0537  157 ASP   A OD1 
3361 O OD2 A ASP   A 157 ? 0.2525 0.2232 0.3712 0.0310  -0.0343 0.1225  157 ASP   A OD2 
3362 O OD2 B ASP   A 157 ? 0.3944 0.3405 0.4515 0.0073  -0.0077 0.0581  157 ASP   A OD2 
3371 N N   A LYS   A 158 ? 0.1930 0.2518 0.3759 0.0431  0.0319  0.1345  158 LYS   A N   
3372 N N   B LYS   A 158 ? 0.3161 0.3134 0.3948 -0.0008 0.0553  0.0676  158 LYS   A N   
3373 C CA  A LYS   A 158 ? 0.1885 0.2744 0.3990 0.0529  0.0443  0.1307  158 LYS   A CA  
3374 C CA  B LYS   A 158 ? 0.3015 0.3136 0.3885 -0.0011 0.0576  0.0731  158 LYS   A CA  
3375 C C   A LYS   A 158 ? 0.1671 0.2802 0.3848 0.0539  0.0463  0.1566  158 LYS   A C   
3376 C C   B LYS   A 158 ? 0.2805 0.3079 0.3722 0.0073  0.0487  0.0891  158 LYS   A C   
3377 O O   A LYS   A 158 ? 0.1676 0.2790 0.3859 0.0484  0.0521  0.1593  158 LYS   A O   
3378 O O   B LYS   A 158 ? 0.2784 0.3105 0.3666 0.0084  0.0505  0.0930  158 LYS   A O   
3379 C CB  A LYS   A 158 ? 0.1991 0.2912 0.4284 0.0573  0.0582  0.1168  158 LYS   A CB  
3380 C CB  B LYS   A 158 ? 0.3087 0.3223 0.4034 -0.0058 0.0621  0.0624  158 LYS   A CB  
3381 C CG  A LYS   A 158 ? 0.2118 0.3078 0.4507 0.0620  0.0671  0.1110  158 LYS   A CG  
3382 C CG  B LYS   A 158 ? 0.3143 0.3308 0.4185 -0.0110 0.0646  0.0550  158 LYS   A CG  
3383 C CD  A LYS   A 158 ? 0.2160 0.3235 0.4623 0.0622  0.0878  0.1130  158 LYS   A CD  
3384 C CD  B LYS   A 158 ? 0.3180 0.3363 0.4301 -0.0154 0.0656  0.0514  158 LYS   A CD  
3385 C CE  A LYS   A 158 ? 0.2239 0.3347 0.4748 0.0566  0.1048  0.1179  158 LYS   A CE  
3386 C CE  B LYS   A 158 ? 0.3209 0.3399 0.4390 -0.0161 0.0620  0.0465  158 LYS   A CE  
3387 N NZ  A LYS   A 158 ? 0.2305 0.3405 0.4812 0.0524  0.1140  0.1238  158 LYS   A NZ  
3388 N NZ  B LYS   A 158 ? 0.3240 0.3427 0.4466 -0.0153 0.0606  0.0409  158 LYS   A NZ  
3415 N N   A ASN   A 159 ? 0.1680 0.2947 0.3943 0.0551  0.0414  0.1460  159 ASN   A N   
3416 N N   B ASN   A 159 ? 0.2641 0.2990 0.3724 0.0165  0.0368  0.0917  159 ASN   A N   
3417 C CA  A ASN   A 159 ? 0.1739 0.3021 0.3903 0.0574  0.0257  0.1563  159 ASN   A CA  
3418 C CA  B ASN   A 159 ? 0.2551 0.2925 0.3727 0.0167  0.0256  0.0927  159 ASN   A CA  
3419 C C   A ASN   A 159 ? 0.1606 0.2941 0.3513 0.0412  0.0273  0.1582  159 ASN   A C   
3420 C C   B ASN   A 159 ? 0.2330 0.2744 0.3377 0.0145  0.0278  0.0845  159 ASN   A C   
3421 O O   A ASN   A 159 ? 0.1517 0.2994 0.3460 0.0383  0.0138  0.1635  159 ASN   A O   
3422 O O   B ASN   A 159 ? 0.2225 0.2700 0.3268 0.0116  0.0252  0.0857  159 ASN   A O   
3423 C CB  A ASN   A 159 ? 0.2002 0.3148 0.4231 0.0603  0.0220  0.1630  159 ASN   A CB  
3424 C CB  B ASN   A 159 ? 0.2685 0.3047 0.4095 0.0139  0.0161  0.0953  159 ASN   A CB  
3425 C CG  A ASN   A 159 ? 0.2261 0.3284 0.4581 0.0510  0.0249  0.1558  159 ASN   A CG  
3426 C CG  B ASN   A 159 ? 0.2808 0.3195 0.4501 0.0115  0.0117  0.0890  159 ASN   A CG  
3427 O OD1 A ASN   A 159 ? 0.2278 0.3348 0.4651 0.0450  0.0330  0.1494  159 ASN   A OD1 
3428 O OD1 B ASN   A 159 ? 0.2846 0.3248 0.4654 0.0090  0.0088  0.0825  159 ASN   A OD1 
3429 N ND2 A ASN   A 159 ? 0.2423 0.3361 0.4836 0.0466  0.0252  0.1484  159 ASN   A ND2 
3430 N ND2 B ASN   A 159 ? 0.2830 0.3259 0.4670 0.0128  0.0077  0.0846  159 ASN   A ND2 
3443 N N   A LEU   A 160 ? 0.1503 0.2758 0.3234 0.0259  0.0106  0.1435  160 LEU   A N   
3444 N N   B LEU   A 160 ? 0.2177 0.2573 0.3065 0.0154  0.0213  0.0726  160 LEU   A N   
3445 C CA  A LEU   A 160 ? 0.1577 0.2606 0.2889 0.0070  0.0086  0.1177  160 LEU   A CA  
3446 C CA  B LEU   A 160 ? 0.2027 0.2362 0.2590 0.0121  0.0167  0.0647  160 LEU   A CA  
3447 C C   A LEU   A 160 ? 0.1454 0.2564 0.2798 0.0025  0.0091  0.1058  160 LEU   A C   
3448 C C   B LEU   A 160 ? 0.1899 0.2127 0.2238 0.0099  0.0279  0.0607  160 LEU   A C   
3449 O O   A LEU   A 160 ? 0.1369 0.2618 0.2938 -0.0063 0.0023  0.1017  160 LEU   A O   
3450 O O   B LEU   A 160 ? 0.1899 0.2134 0.2208 0.0119  0.0185  0.0548  160 LEU   A O   
3451 C CB  A LEU   A 160 ? 0.1650 0.2509 0.2540 -0.0089 0.0119  0.1033  160 LEU   A CB  
3452 C CB  B LEU   A 160 ? 0.2060 0.2436 0.2521 0.0067  0.0163  0.0592  160 LEU   A CB  
3453 C CG  A LEU   A 160 ? 0.1788 0.2514 0.2539 -0.0253 0.0200  0.0711  160 LEU   A CG  
3454 C CG  B LEU   A 160 ? 0.2110 0.2533 0.2466 0.0003  0.0116  0.0461  160 LEU   A CG  
3455 C CD1 A LEU   A 160 ? 0.1918 0.2553 0.2535 -0.0235 0.0087  0.0582  160 LEU   A CD1 
3456 C CD1 B LEU   A 160 ? 0.2140 0.2568 0.2472 -0.0053 0.0095  0.0433  160 LEU   A CD1 
3457 C CD2 A LEU   A 160 ? 0.1774 0.2500 0.2526 -0.0284 0.0324  0.0571  160 LEU   A CD2 
3458 C CD2 B LEU   A 160 ? 0.2103 0.2569 0.2425 -0.0020 0.0149  0.0420  160 LEU   A CD2 
3481 N N   A TYR   A 161 ? 0.1400 0.2443 0.2642 0.0039  0.0131  0.0974  161 TYR   A N   
3482 N N   B TYR   A 161 ? 0.1831 0.1937 0.2038 0.0126  0.0339  0.0593  161 TYR   A N   
3483 C CA  A TYR   A 161 ? 0.1443 0.2336 0.2700 0.0071  0.0209  0.0956  161 TYR   A CA  
3484 C CA  B TYR   A 161 ? 0.1840 0.1911 0.1989 0.0197  0.0414  0.0411  161 TYR   A CA  
3485 C C   A TYR   A 161 ? 0.1370 0.2352 0.2867 0.0101  0.0195  0.1051  161 TYR   A C   
3486 C C   B TYR   A 161 ? 0.1806 0.1938 0.2078 0.0184  0.0400  0.0462  161 TYR   A C   
3487 O O   A TYR   A 161 ? 0.1306 0.2364 0.2776 0.0131  0.0267  0.0930  161 TYR   A O   
3488 O O   B TYR   A 161 ? 0.1745 0.1891 0.1989 0.0133  0.0450  0.0365  161 TYR   A O   
3489 C CB  A TYR   A 161 ? 0.1520 0.2275 0.2601 0.0089  0.0330  0.0736  161 TYR   A CB  
3490 C CB  B TYR   A 161 ? 0.1909 0.1919 0.2016 0.0218  0.0491  0.0169  161 TYR   A CB  
3491 C CG  A TYR   A 161 ? 0.1596 0.2187 0.2505 0.0065  0.0247  0.0548  161 TYR   A CG  
3492 C CG  B TYR   A 161 ? 0.1950 0.1909 0.2011 0.0230  0.0428  0.0123  161 TYR   A CG  
3493 C CD1 A TYR   A 161 ? 0.1585 0.2145 0.2445 0.0102  0.0185  0.0438  161 TYR   A CD1 
3494 C CD1 B TYR   A 161 ? 0.1974 0.1897 0.2064 0.0202  0.0369  0.0116  161 TYR   A CD1 
3495 C CD2 A TYR   A 161 ? 0.1623 0.2204 0.2512 0.0069  0.0183  0.0418  161 TYR   A CD2 
3496 C CD2 B TYR   A 161 ? 0.2001 0.1943 0.2009 0.0227  0.0411  0.0166  161 TYR   A CD2 
3497 C CE1 A TYR   A 161 ? 0.1602 0.2070 0.2400 0.0111  0.0183  0.0429  161 TYR   A CE1 
3498 C CE1 B TYR   A 161 ? 0.2047 0.1998 0.2221 0.0152  0.0314  0.0111  161 TYR   A CE1 
3499 C CE2 A TYR   A 161 ? 0.1626 0.2115 0.2428 0.0096  0.0184  0.0421  161 TYR   A CE2 
3500 C CE2 B TYR   A 161 ? 0.2081 0.2043 0.2169 0.0164  0.0346  0.0213  161 TYR   A CE2 
3501 C CZ  A TYR   A 161 ? 0.1711 0.2046 0.2430 0.0056  0.0083  0.0491  161 TYR   A CZ  
3502 C CZ  B TYR   A 161 ? 0.2164 0.2095 0.2340 0.0145  0.0291  0.0171  161 TYR   A CZ  
3503 O OH  A TYR   A 161 ? 0.1841 0.2019 0.2484 0.0002  0.0012  0.0504  161 TYR   A OH  
3504 O OH  B TYR   A 161 ? 0.2332 0.2194 0.2568 0.0099  0.0200  0.0250  161 TYR   A OH  
3523 N N   A ASP   A 162 ? 0.1396 0.2444 0.3228 0.0045  0.0250  0.1203  162 ASP   A N   
3524 N N   B ASP   A 162 ? 0.1802 0.2081 0.2311 0.0213  0.0423  0.0656  162 ASP   A N   
3525 C CA  A ASP   A 162 ? 0.1379 0.2623 0.3247 -0.0039 0.0340  0.1318  162 ASP   A CA  
3526 C CA  B ASP   A 162 ? 0.1844 0.2288 0.2499 0.0226  0.0442  0.0623  162 ASP   A CA  
3527 C C   A ASP   A 162 ? 0.1329 0.2729 0.3181 -0.0064 0.0292  0.1335  162 ASP   A C   
3528 C C   B ASP   A 162 ? 0.1876 0.2251 0.2538 0.0182  0.0401  0.0699  162 ASP   A C   
3529 O O   A ASP   A 162 ? 0.1358 0.2714 0.3259 -0.0245 0.0236  0.1394  162 ASP   A O   
3530 O O   B ASP   A 162 ? 0.1836 0.2291 0.2728 0.0115  0.0439  0.0709  162 ASP   A O   
3531 C CB  A ASP   A 162 ? 0.1429 0.2792 0.3409 0.0035  0.0397  0.1268  162 ASP   A CB  
3532 C CB  B ASP   A 162 ? 0.1840 0.2538 0.2882 0.0300  0.0371  0.0430  162 ASP   A CB  
3533 C CG  A ASP   A 162 ? 0.1431 0.3038 0.3757 0.0182  0.0394  0.1005  162 ASP   A CG  
3534 C CG  B ASP   A 162 ? 0.1789 0.2760 0.3172 0.0358  0.0285  0.0292  162 ASP   A CG  
3535 O OD1 A ASP   A 162 ? 0.1582 0.3108 0.3837 0.0139  0.0415  0.0924  162 ASP   A OD1 
3536 O OD1 B ASP   A 162 ? 0.1695 0.2840 0.3284 0.0379  0.0331  0.0321  162 ASP   A OD1 
3537 O OD2 A ASP   A 162 ? 0.1410 0.3193 0.4083 0.0262  0.0468  0.0777  162 ASP   A OD2 
3538 O OD2 B ASP   A 162 ? 0.1750 0.2839 0.3256 0.0354  0.0194  0.0174  162 ASP   A OD2 
3547 N N   A LYS   A 163 ? 0.1415 0.2816 0.3135 -0.0057 0.0005  0.1304  163 LYS   A N   
3548 N N   B LYS   A 163 ? 0.2058 0.2272 0.2431 0.0167  0.0253  0.0718  163 LYS   A N   
3549 C CA  A LYS   A 163 ? 0.1493 0.2923 0.2988 -0.0153 -0.0107 0.1260  163 LYS   A CA  
3550 C CA  B LYS   A 163 ? 0.2193 0.2324 0.2418 0.0147  0.0172  0.0625  163 LYS   A CA  
3551 C C   A LYS   A 163 ? 0.1390 0.2768 0.2940 -0.0203 0.0100  0.1101  163 LYS   A C   
3552 C C   B LYS   A 163 ? 0.2018 0.2104 0.2276 0.0026  0.0158  0.0451  163 LYS   A C   
3553 O O   A LYS   A 163 ? 0.1380 0.2862 0.3204 -0.0294 0.0014  0.1055  163 LYS   A O   
3554 O O   B LYS   A 163 ? 0.1908 0.2010 0.2290 -0.0068 0.0103  0.0338  163 LYS   A O   
3555 C CB  A LYS   A 163 ? 0.1816 0.3197 0.3192 -0.0120 -0.0306 0.1213  163 LYS   A CB  
3556 C CB  B LYS   A 163 ? 0.2556 0.2584 0.2789 0.0233  0.0134  0.0627  163 LYS   A CB  
3557 C CG  A LYS   A 163 ? 0.2188 0.3443 0.3599 -0.0127 -0.0268 0.1117  163 LYS   A CG  
3558 C CG  B LYS   A 163 ? 0.2885 0.2843 0.3287 0.0264  0.0172  0.0543  163 LYS   A CG  
3559 C CD  A LYS   A 163 ? 0.2549 0.3657 0.4114 -0.0092 -0.0282 0.0972  163 LYS   A CD  
3560 C CD  B LYS   A 163 ? 0.3147 0.3062 0.3777 0.0308  0.0204  0.0475  163 LYS   A CD  
3561 C CE  A LYS   A 163 ? 0.2828 0.3822 0.4540 -0.0065 -0.0255 0.0844  163 LYS   A CE  
3562 C CE  B LYS   A 163 ? 0.3336 0.3231 0.4169 0.0339  0.0237  0.0396  163 LYS   A CE  
3563 N NZ  A LYS   A 163 ? 0.2925 0.3946 0.4820 -0.0060 -0.0237 0.0776  163 LYS   A NZ  
3564 N NZ  B LYS   A 163 ? 0.3460 0.3343 0.4442 0.0347  0.0221  0.0329  163 LYS   A NZ  
3591 N N   A LEU   A 164 ? 0.1285 0.2526 0.2830 -0.0208 0.0030  0.0901  164 LEU   A N   
3592 N N   B LEU   A 164 ? 0.1839 0.1923 0.2099 0.0044  0.0132  0.0385  164 LEU   A N   
3593 C CA  A LEU   A 164 ? 0.1330 0.2335 0.2627 -0.0213 0.0185  0.0755  164 LEU   A CA  
3594 C CA  B LEU   A 164 ? 0.1789 0.1807 0.1986 -0.0046 0.0232  0.0297  164 LEU   A CA  
3595 C C   A LEU   A 164 ? 0.1434 0.2239 0.2643 -0.0138 0.0254  0.0670  164 LEU   A C   
3596 C C   B LEU   A 164 ? 0.1751 0.1811 0.1974 -0.0063 0.0278  0.0356  164 LEU   A C   
3597 O O   A LEU   A 164 ? 0.1562 0.2244 0.2669 -0.0125 0.0440  0.0464  164 LEU   A O   
3598 O O   B LEU   A 164 ? 0.1770 0.1834 0.2027 -0.0101 0.0511  0.0294  164 LEU   A O   
3599 C CB  A LEU   A 164 ? 0.1309 0.2322 0.2569 -0.0270 0.0229  0.0760  164 LEU   A CB  
3600 C CB  B LEU   A 164 ? 0.1771 0.1708 0.1949 -0.0053 0.0239  0.0145  164 LEU   A CB  
3601 C CG  A LEU   A 164 ? 0.1365 0.2360 0.2694 -0.0194 0.0152  0.0683  164 LEU   A CG  
3602 C CG  B LEU   A 164 ? 0.1858 0.1735 0.2143 -0.0098 0.0162  -0.0002 164 LEU   A CG  
3603 C CD1 A LEU   A 164 ? 0.1326 0.2336 0.2754 -0.0210 0.0067  0.0680  164 LEU   A CD1 
3604 C CD1 B LEU   A 164 ? 0.1790 0.1701 0.2243 -0.0107 0.0202  -0.0046 164 LEU   A CD1 
3605 C CD2 A LEU   A 164 ? 0.1496 0.2409 0.2692 -0.0134 0.0214  0.0676  164 LEU   A CD2 
3606 C CD2 B LEU   A 164 ? 0.1983 0.1825 0.2144 -0.0118 0.0236  0.0014  164 LEU   A CD2 
3629 N N   A VAL   A 165 ? 0.1479 0.2183 0.2587 -0.0084 0.0230  0.0636  165 VAL   A N   
3630 N N   B VAL   A 165 ? 0.1699 0.1876 0.1991 -0.0093 0.0253  0.0411  165 VAL   A N   
3631 C CA  A VAL   A 165 ? 0.1537 0.2183 0.2460 -0.0108 0.0349  0.0699  165 VAL   A CA  
3632 C CA  B VAL   A 165 ? 0.1707 0.1959 0.2033 -0.0063 0.0316  0.0480  165 VAL   A CA  
3633 C C   A VAL   A 165 ? 0.1482 0.2353 0.2576 -0.0067 0.0260  0.0720  165 VAL   A C   
3634 C C   B VAL   A 165 ? 0.1551 0.1975 0.1964 -0.0010 0.0356  0.0512  165 VAL   A C   
3635 O O   A VAL   A 165 ? 0.1419 0.2337 0.2544 -0.0051 0.0215  0.0736  165 VAL   A O   
3636 O O   B VAL   A 165 ? 0.1552 0.1978 0.2032 0.0005  0.0329  0.0373  165 VAL   A O   
3637 C CB  A VAL   A 165 ? 0.1675 0.2105 0.2470 -0.0081 0.0375  0.0537  165 VAL   A CB  
3638 C CB  B VAL   A 165 ? 0.1903 0.2063 0.2163 -0.0056 0.0279  0.0482  165 VAL   A CB  
3639 C CG1 A VAL   A 165 ? 0.1756 0.2146 0.2509 -0.0095 0.0480  0.0432  165 VAL   A CG1 
3640 C CG1 B VAL   A 165 ? 0.2002 0.2158 0.2301 -0.0066 0.0275  0.0386  165 VAL   A CG1 
3641 C CG2 A VAL   A 165 ? 0.1835 0.2080 0.2566 -0.0102 0.0290  0.0568  165 VAL   A CG2 
3642 C CG2 B VAL   A 165 ? 0.1996 0.2069 0.2180 -0.0044 0.0210  0.0460  165 VAL   A CG2 
3661 N N   A SER   A 166 ? 0.1479 0.2552 0.2862 -0.0104 0.0162  0.0673  166 SER   A N   
3662 N N   B SER   A 166 ? 0.1364 0.2032 0.2039 -0.0016 0.0368  0.0587  166 SER   A N   
3663 C CA  A SER   A 166 ? 0.1486 0.2796 0.2958 -0.0115 0.0177  0.0577  166 SER   A CA  
3664 C CA  B SER   A 166 ? 0.1370 0.2193 0.2133 -0.0026 0.0227  0.0526  166 SER   A CA  
3665 C C   A SER   A 166 ? 0.1459 0.2955 0.2977 -0.0122 0.0042  0.0533  166 SER   A C   
3666 C C   B SER   A 166 ? 0.1456 0.2235 0.2203 0.0028  -0.0019 0.0456  166 SER   A C   
3667 O O   A SER   A 166 ? 0.1583 0.2975 0.3314 -0.0124 0.0110  0.0422  166 SER   A O   
3668 O O   B SER   A 166 ? 0.1646 0.2290 0.2462 0.0044  -0.0053 0.0316  166 SER   A O   
3669 C CB  A SER   A 166 ? 0.1680 0.2898 0.3126 -0.0047 0.0246  0.0499  166 SER   A CB  
3670 C CB  B SER   A 166 ? 0.1392 0.2365 0.2413 0.0049  0.0167  0.0394  166 SER   A CB  
3671 O OG  A SER   A 166 ? 0.1914 0.3023 0.3209 -0.0049 0.0331  0.0570  166 SER   A OG  
3672 O OG  B SER   A 166 ? 0.1399 0.2481 0.2690 0.0028  0.0105  0.0437  166 SER   A OG  
3683 N N   A SER   A 167 ? 0.1589 0.3061 0.2695 -0.0031 0.0035  0.0487  167 SER   A N   
3684 N N   B SER   A 167 ? 0.1535 0.2328 0.2114 0.0134  -0.0078 0.0529  167 SER   A N   
3685 C CA  A SER   A 167 ? 0.1794 0.3146 0.2578 0.0056  0.0019  0.0329  167 SER   A CA  
3686 C CA  B SER   A 167 ? 0.1739 0.2387 0.2163 0.0136  -0.0141 0.0523  167 SER   A CA  
3687 C C   A SER   A 167 ? 0.1808 0.3153 0.2465 0.0100  0.0128  0.0243  167 SER   A C   
3688 C C   B SER   A 167 ? 0.1836 0.2449 0.2134 0.0172  -0.0014 0.0582  167 SER   A C   
3689 O O   A SER   A 167 ? 0.1982 0.3170 0.2603 0.0106  0.0008  0.0204  167 SER   A O   
3690 O O   B SER   A 167 ? 0.1937 0.2479 0.2251 0.0215  -0.0069 0.0540  167 SER   A O   
3691 C CB  A SER   A 167 ? 0.1920 0.3210 0.2606 0.0138  0.0127  0.0323  167 SER   A CB  
3692 C CB  B SER   A 167 ? 0.1867 0.2407 0.2284 0.0121  -0.0115 0.0578  167 SER   A CB  
3693 O OG  A SER   A 167 ? 0.1938 0.3233 0.2549 0.0177  0.0372  0.0402  167 SER   A OG  
3694 O OG  B SER   A 167 ? 0.1938 0.2410 0.2321 0.0099  -0.0028 0.0588  167 SER   A OG  
3705 N N   A PHE   A 168 ? 0.1651 0.3129 0.2339 0.0164  0.0195  0.0152  168 PHE   A N   
3706 N N   B PHE   A 168 ? 0.1805 0.2483 0.2097 0.0191  0.0080  0.0625  168 PHE   A N   
3707 C CA  A PHE   A 168 ? 0.1657 0.3085 0.2423 0.0115  0.0314  0.0118  168 PHE   A CA  
3708 C CA  B PHE   A 168 ? 0.1854 0.2602 0.2213 0.0166  0.0182  0.0624  168 PHE   A CA  
3709 C C   A PHE   A 168 ? 0.1832 0.3326 0.2791 0.0069  0.0637  -0.0058 168 PHE   A C   
3710 C C   B PHE   A 168 ? 0.1987 0.2777 0.2320 0.0146  0.0364  0.0395  168 PHE   A C   
3711 O O   A PHE   A 168 ? 0.1890 0.3330 0.3193 -0.0069 0.0625  -0.0044 168 PHE   A O   
3712 O O   B PHE   A 168 ? 0.1999 0.2812 0.2375 0.0045  0.0485  0.0350  168 PHE   A O   
3713 C CB  A PHE   A 168 ? 0.1604 0.2800 0.2231 0.0009  0.0067  0.0215  168 PHE   A CB  
3714 C CB  B PHE   A 168 ? 0.1818 0.2545 0.2224 0.0172  0.0163  0.0722  168 PHE   A CB  
3715 C CG  A PHE   A 168 ? 0.1538 0.2578 0.2086 -0.0072 -0.0099 0.0296  168 PHE   A CG  
3716 C CG  B PHE   A 168 ? 0.1747 0.2508 0.2266 0.0122  0.0186  0.0791  168 PHE   A CG  
3717 C CD1 A PHE   A 168 ? 0.1537 0.2554 0.2197 -0.0172 -0.0129 0.0405  168 PHE   A CD1 
3718 C CD1 B PHE   A 168 ? 0.1790 0.2512 0.2392 0.0057  0.0266  0.0797  168 PHE   A CD1 
3719 C CD2 A PHE   A 168 ? 0.1576 0.2452 0.2142 -0.0087 -0.0091 0.0230  168 PHE   A CD2 
3720 C CD2 B PHE   A 168 ? 0.1708 0.2502 0.2304 0.0059  0.0240  0.0839  168 PHE   A CD2 
3721 C CE1 A PHE   A 168 ? 0.1459 0.2507 0.2216 -0.0198 -0.0190 0.0290  168 PHE   A CE1 
3722 C CE1 B PHE   A 168 ? 0.1734 0.2501 0.2474 0.0024  0.0313  0.0798  168 PHE   A CE1 
3723 C CE2 A PHE   A 168 ? 0.1632 0.2420 0.2257 -0.0123 -0.0042 0.0230  168 PHE   A CE2 
3724 C CE2 B PHE   A 168 ? 0.1741 0.2462 0.2372 0.0025  0.0274  0.0885  168 PHE   A CE2 
3725 C CZ  A PHE   A 168 ? 0.1559 0.2454 0.2255 -0.0144 -0.0101 0.0304  168 PHE   A CZ  
3726 C CZ  B PHE   A 168 ? 0.1713 0.2472 0.2470 -0.0002 0.0284  0.0812  168 PHE   A CZ  
3745 N N   A LEU   A 169 ? 0.2209 0.3542 0.3094 0.0064  0.0732  -0.0221 169 LEU   A N   
3746 N N   B LEU   A 169 ? 0.2291 0.2920 0.2680 0.0150  0.0279  0.0220  169 LEU   A N   
3747 C CA  A LEU   A 169 ? 0.2776 0.3769 0.3802 0.0117  0.0408  -0.0325 169 LEU   A CA  
3748 C CA  B LEU   A 169 ? 0.2574 0.3073 0.3120 0.0219  0.0141  0.0080  169 LEU   A CA  
3749 C C   A LEU   A 169 ? 0.2904 0.3824 0.4132 0.0147  0.0259  -0.0254 169 LEU   A C   
3750 C C   B LEU   A 169 ? 0.2468 0.3018 0.3196 0.0245  0.0133  0.0279  169 LEU   A C   
3751 O O   A LEU   A 169 ? 0.2978 0.3853 0.4230 0.0181  0.0215  -0.0256 169 LEU   A O   
3752 O O   B LEU   A 169 ? 0.2388 0.3023 0.3223 0.0257  0.0172  0.0337  169 LEU   A O   
3753 C CB  A LEU   A 169 ? 0.3080 0.3902 0.4061 0.0120  0.0291  -0.0483 169 LEU   A CB  
3754 C CB  B LEU   A 169 ? 0.2867 0.3265 0.3437 0.0208  0.0062  -0.0191 169 LEU   A CB  
3755 C CG  A LEU   A 169 ? 0.3374 0.4007 0.4256 0.0075  0.0161  -0.0660 169 LEU   A CG  
3756 C CG  B LEU   A 169 ? 0.3079 0.3420 0.3692 0.0160  -0.0018 -0.0432 169 LEU   A CG  
3757 C CD1 A LEU   A 169 ? 0.3478 0.4034 0.4361 0.0065  0.0114  -0.0700 169 LEU   A CD1 
3758 C CD1 B LEU   A 169 ? 0.3154 0.3458 0.3828 0.0136  -0.0073 -0.0482 169 LEU   A CD1 
3759 C CD2 A LEU   A 169 ? 0.3468 0.4050 0.4283 0.0050  0.0147  -0.0720 169 LEU   A CD2 
3760 C CD2 B LEU   A 169 ? 0.3155 0.3500 0.3772 0.0139  -0.0037 -0.0503 169 LEU   A CD2 
3761 O OXT A LEU   A 169 ? 0.2844 0.3843 0.4251 0.0183  0.0233  -0.0259 169 LEU   A OXT 
3762 O OXT B LEU   A 169 ? 0.2446 0.2980 0.3156 0.0241  0.0118  0.0363  169 LEU   A OXT 
3785 N N   A SER   B 1   ? 0.3951 0.3805 0.4018 -0.0973 -0.0921 0.0418  1   SER   B N   
3786 N N   B SER   B 1   ? 0.3676 0.3589 0.3714 -0.0827 -0.0681 0.0285  1   SER   B N   
3787 C CA  A SER   B 1   ? 0.3880 0.3812 0.4023 -0.1007 -0.0936 0.0419  1   SER   B CA  
3788 C CA  B SER   B 1   ? 0.3631 0.3621 0.3745 -0.0843 -0.0691 0.0278  1   SER   B CA  
3789 C C   A SER   B 1   ? 0.3637 0.3756 0.3847 -0.1011 -0.0981 0.0581  1   SER   B C   
3790 C C   B SER   B 1   ? 0.3467 0.3615 0.3638 -0.0815 -0.0755 0.0405  1   SER   B C   
3791 O O   A SER   B 1   ? 0.3694 0.3742 0.3665 -0.0952 -0.0955 0.0563  1   SER   B O   
3792 O O   B SER   B 1   ? 0.3487 0.3595 0.3493 -0.0798 -0.0773 0.0382  1   SER   B O   
3793 C CB  A SER   B 1   ? 0.4005 0.3839 0.4173 -0.1009 -0.0880 0.0258  1   SER   B CB  
3794 C CB  B SER   B 1   ? 0.3717 0.3628 0.3868 -0.0859 -0.0623 0.0135  1   SER   B CB  
3795 O OG  A SER   B 1   ? 0.4130 0.3928 0.4514 -0.0995 -0.0781 0.0198  1   SER   B OG  
3796 O OG  B SER   B 1   ? 0.3801 0.3681 0.4104 -0.0866 -0.0566 0.0066  1   SER   B OG  
3811 N N   A MET   B 2   ? 0.3376 0.3684 0.3795 -0.1036 -0.0969 0.0897  2   MET   B N   
3812 N N   B MET   B 2   ? 0.3310 0.3606 0.3618 -0.0773 -0.0740 0.0649  2   MET   B N   
3813 C CA  A MET   B 2   ? 0.3175 0.3635 0.3861 -0.0907 -0.0957 0.1096  2   MET   B CA  
3814 C CA  B MET   B 2   ? 0.3177 0.3597 0.3637 -0.0640 -0.0713 0.0830  2   MET   B CA  
3815 C C   A MET   B 2   ? 0.2756 0.3307 0.3389 -0.0855 -0.1068 0.1402  2   MET   B C   
3816 C C   B MET   B 2   ? 0.2936 0.3406 0.3343 -0.0576 -0.0658 0.0959  2   MET   B C   
3817 O O   A MET   B 2   ? 0.2660 0.3353 0.3278 -0.0803 -0.1215 0.1504  2   MET   B O   
3818 O O   B MET   B 2   ? 0.2960 0.3506 0.3413 -0.0521 -0.0607 0.0941  2   MET   B O   
3819 C CB  A MET   B 2   ? 0.3481 0.3960 0.4631 -0.0711 -0.0734 0.0847  2   MET   B CB  
3820 C CB  B MET   B 2   ? 0.3337 0.3799 0.4096 -0.0510 -0.0675 0.0819  2   MET   B CB  
3821 C CG  A MET   B 2   ? 0.3743 0.4244 0.5332 -0.0513 -0.0536 0.0693  2   MET   B CG  
3822 C CG  B MET   B 2   ? 0.3458 0.3966 0.4461 -0.0375 -0.0642 0.0888  2   MET   B CG  
3823 S SD  A MET   B 2   ? 0.3985 0.4509 0.6004 -0.0336 -0.0380 0.0568  2   MET   B SD  
3824 S SD  B MET   B 2   ? 0.3576 0.4133 0.4788 -0.0247 -0.0630 0.0950  2   MET   B SD  
3825 C CE  A MET   B 2   ? 0.4021 0.4574 0.6006 -0.0307 -0.0321 0.0559  2   MET   B CE  
3826 C CE  B MET   B 2   ? 0.3589 0.4160 0.4861 -0.0242 -0.0595 0.0899  2   MET   B CE  
3845 N N   A VAL   B 3   ? 0.2416 0.2854 0.3064 -0.0939 -0.0971 0.1537  3   VAL   B N   
3846 N N   B VAL   B 3   ? 0.2659 0.3081 0.3036 -0.0598 -0.0641 0.1055  3   VAL   B N   
3847 C CA  A VAL   B 3   ? 0.2289 0.2526 0.3067 -0.0827 -0.0835 0.1344  3   VAL   B CA  
3848 C CA  B VAL   B 3   ? 0.2446 0.2778 0.2896 -0.0549 -0.0598 0.0976  3   VAL   B CA  
3849 C C   A VAL   B 3   ? 0.2096 0.2423 0.2682 -0.0682 -0.0744 0.1169  3   VAL   B C   
3850 C C   B VAL   B 3   ? 0.2185 0.2569 0.2570 -0.0516 -0.0601 0.0953  3   VAL   B C   
3851 O O   A VAL   B 3   ? 0.2059 0.2448 0.2748 -0.0681 -0.0766 0.1200  3   VAL   B O   
3852 O O   B VAL   B 3   ? 0.2150 0.2647 0.2562 -0.0424 -0.0615 0.0945  3   VAL   B O   
3853 C CB  A VAL   B 3   ? 0.2465 0.2463 0.3587 -0.0812 -0.0786 0.1097  3   VAL   B CB  
3854 C CB  B VAL   B 3   ? 0.2536 0.2722 0.3137 -0.0538 -0.0537 0.0879  3   VAL   B CB  
3855 C CG1 A VAL   B 3   ? 0.2530 0.2375 0.3788 -0.0811 -0.0802 0.1048  3   VAL   B CG1 
3856 C CG1 B VAL   B 3   ? 0.2567 0.2676 0.3257 -0.0541 -0.0539 0.0836  3   VAL   B CG1 
3857 C CG2 A VAL   B 3   ? 0.2560 0.2496 0.3749 -0.0774 -0.0679 0.1094  3   VAL   B CG2 
3858 C CG2 B VAL   B 3   ? 0.2591 0.2726 0.3192 -0.0514 -0.0491 0.0906  3   VAL   B CG2 
3877 N N   . ASN   B 4   ? 0.1989 0.2269 0.2405 -0.0582 -0.0620 0.0931  4   ASN   B N   
3878 C CA  . ASN   B 4   ? 0.1977 0.2206 0.2075 -0.0618 -0.0534 0.0450  4   ASN   B CA  
3879 C C   . ASN   B 4   ? 0.2113 0.2300 0.1929 -0.0590 -0.0452 0.0295  4   ASN   B C   
3880 O O   . ASN   B 4   ? 0.2151 0.2359 0.2188 -0.0533 -0.0324 0.0173  4   ASN   B O   
3881 C CB  . ASN   B 4   ? 0.1913 0.2177 0.1929 -0.0480 -0.0582 0.0372  4   ASN   B CB  
3882 C CG  . ASN   B 4   ? 0.1867 0.1977 0.1778 -0.0452 -0.0565 0.0317  4   ASN   B CG  
3883 O OD1 . ASN   B 4   ? 0.1949 0.1801 0.1804 -0.0481 -0.0502 0.0268  4   ASN   B OD1 
3884 N ND2 . ASN   B 4   ? 0.2045 0.2029 0.1907 -0.0238 -0.0409 0.0203  4   ASN   B ND2 
3892 N N   . SER   B 5   ? 0.2255 0.2482 0.1993 -0.0613 -0.0308 0.0262  5   SER   B N   
3893 C CA  . SER   B 5   ? 0.2535 0.2873 0.2388 -0.0549 -0.0075 0.0320  5   SER   B CA  
3894 C C   . SER   B 5   ? 0.2747 0.2922 0.2748 -0.0708 0.0223  0.0310  5   SER   B C   
3895 O O   . SER   B 5   ? 0.2893 0.2923 0.3473 -0.0638 0.0564  0.0284  5   SER   B O   
3896 C CB  . SER   B 5   ? 0.2655 0.3146 0.2690 -0.0447 -0.0047 0.0497  5   SER   B CB  
3897 O OG  . SER   B 5   ? 0.2943 0.3346 0.3294 -0.0302 -0.0080 0.0559  5   SER   B OG  
3903 N N   . PHE   B 6   ? 0.2935 0.3091 0.2440 -0.0746 0.0426  0.0369  6   PHE   B N   
3904 C CA  . PHE   B 6   ? 0.3016 0.3150 0.2043 -0.0910 0.0504  0.0147  6   PHE   B CA  
3905 C C   . PHE   B 6   ? 0.3550 0.3523 0.2574 -0.0966 0.0710  -0.0188 6   PHE   B C   
3906 O O   . PHE   B 6   ? 0.3717 0.3847 0.3013 -0.0846 0.0581  -0.0300 6   PHE   B O   
3907 C CB  . PHE   B 6   ? 0.2674 0.2878 0.1847 -0.0816 0.0214  0.0132  6   PHE   B CB  
3908 C CG  . PHE   B 6   ? 0.2334 0.2518 0.1774 -0.0733 0.0027  0.0061  6   PHE   B CG  
3909 C CD1 . PHE   B 6   ? 0.2306 0.2250 0.1654 -0.0671 -0.0131 0.0083  6   PHE   B CD1 
3910 C CD2 . PHE   B 6   ? 0.2127 0.2479 0.1808 -0.0604 0.0037  0.0332  6   PHE   B CD2 
3911 C CE1 . PHE   B 6   ? 0.2262 0.2059 0.1705 -0.0528 -0.0171 0.0066  6   PHE   B CE1 
3912 C CE2 . PHE   B 6   ? 0.2147 0.2335 0.2138 -0.0454 0.0030  0.0320  6   PHE   B CE2 
3913 C CZ  . PHE   B 6   ? 0.2194 0.2096 0.1903 -0.0484 -0.0027 0.0104  6   PHE   B CZ  
3923 N N   . SER   B 7   ? 0.3894 0.3430 0.2720 -0.1199 0.0994  -0.0485 7   SER   B N   
3924 C CA  . SER   B 7   ? 0.4236 0.3634 0.3214 -0.1201 0.1284  -0.0543 7   SER   B CA  
3925 C C   . SER   B 7   ? 0.4227 0.3388 0.3090 -0.1246 0.1424  -0.0617 7   SER   B C   
3926 O O   . SER   B 7   ? 0.4324 0.3361 0.3381 -0.1305 0.1406  -0.0568 7   SER   B O   
3927 C CB  . SER   B 7   ? 0.4497 0.3934 0.3878 -0.1143 0.1512  -0.0498 7   SER   B CB  
3928 O OG  . SER   B 7   ? 0.4651 0.3968 0.4454 -0.1131 0.1535  -0.0399 7   SER   B OG  
3934 N N   . GLY   B 8   ? 0.4203 0.3247 0.3145 -0.1075 0.1413  -0.0715 8   GLY   B N   
3935 C CA  . GLY   B 8   ? 0.4043 0.3049 0.3142 -0.1000 0.1419  -0.0749 8   GLY   B CA  
3936 C C   . GLY   B 8   ? 0.3820 0.2727 0.3046 -0.0991 0.1374  -0.0699 8   GLY   B C   
3937 O O   . GLY   B 8   ? 0.3912 0.2768 0.3397 -0.0884 0.1419  -0.0750 8   GLY   B O   
3941 N N   . TYR   B 9   ? 0.3598 0.2463 0.2675 -0.0918 0.1121  -0.0771 9   TYR   B N   
3942 C CA  . TYR   B 9   ? 0.3364 0.2232 0.2438 -0.0740 0.0839  -0.0582 9   TYR   B CA  
3943 C C   . TYR   B 9   ? 0.3328 0.2247 0.2312 -0.0652 0.0493  -0.0503 9   TYR   B C   
3944 O O   . TYR   B 9   ? 0.3474 0.2508 0.2699 -0.0604 0.0491  -0.0387 9   TYR   B O   
3945 C CB  . TYR   B 9   ? 0.3264 0.2031 0.2495 -0.0635 0.0773  -0.0476 9   TYR   B CB  
3946 C CG  . TYR   B 9   ? 0.3142 0.1856 0.2461 -0.0677 0.0747  -0.0491 9   TYR   B CG  
3947 C CD1 . TYR   B 9   ? 0.3171 0.1856 0.2596 -0.0817 0.0760  -0.0438 9   TYR   B CD1 
3948 C CD2 . TYR   B 9   ? 0.3000 0.1802 0.2419 -0.0585 0.0738  -0.0528 9   TYR   B CD2 
3949 C CE1 . TYR   B 9   ? 0.3109 0.1944 0.2690 -0.0859 0.0798  -0.0536 9   TYR   B CE1 
3950 C CE2 . TYR   B 9   ? 0.2992 0.1833 0.2580 -0.0590 0.0692  -0.0545 9   TYR   B CE2 
3951 C CZ  . TYR   B 9   ? 0.3012 0.1962 0.2724 -0.0720 0.0753  -0.0673 9   TYR   B CZ  
3952 O OH  . TYR   B 9   ? 0.2921 0.2070 0.2911 -0.0829 0.0777  -0.0792 9   TYR   B OH  
3962 N N   . LEU   B 10  ? 0.3155 0.1962 0.2029 -0.0624 0.0257  -0.0446 10  LEU   B N   
3963 C CA  . LEU   B 10  ? 0.3120 0.1943 0.2023 -0.0723 -0.0119 -0.0330 10  LEU   B CA  
3964 C C   . LEU   B 10  ? 0.2898 0.1982 0.2033 -0.0710 -0.0233 -0.0307 10  LEU   B C   
3965 O O   . LEU   B 10  ? 0.2736 0.2015 0.2086 -0.0531 -0.0197 -0.0219 10  LEU   B O   
3966 C CB  . LEU   B 10  ? 0.3315 0.1989 0.2177 -0.0761 -0.0351 -0.0180 10  LEU   B CB  
3967 C CG  . LEU   B 10  ? 0.3534 0.2135 0.2625 -0.0717 -0.0628 -0.0034 10  LEU   B CG  
3968 C CD1 . LEU   B 10  ? 0.3674 0.2256 0.2942 -0.0667 -0.0650 -0.0088 10  LEU   B CD1 
3969 C CD2 . LEU   B 10  ? 0.3614 0.2179 0.2882 -0.0743 -0.0600 0.0137  10  LEU   B CD2 
3981 N N   . LYS   B 11  ? 0.3007 0.2267 0.2103 -0.0651 -0.0308 -0.0259 11  LYS   B N   
3982 C CA  . LYS   B 11  ? 0.3193 0.2573 0.2433 -0.0472 -0.0439 -0.0286 11  LYS   B CA  
3983 C C   . LYS   B 11  ? 0.3005 0.2353 0.2541 -0.0663 -0.0465 -0.0458 11  LYS   B C   
3984 O O   . LYS   B 11  ? 0.3155 0.2539 0.2842 -0.0798 -0.0454 -0.0788 11  LYS   B O   
3985 C CB  . LYS   B 11  ? 0.3507 0.3066 0.2937 -0.0180 -0.0488 -0.0178 11  LYS   B CB  
3986 C CG  . LYS   B 11  ? 0.3794 0.3413 0.3566 -0.0003 -0.0496 -0.0166 11  LYS   B CG  
3987 C CD  . LYS   B 11  ? 0.4017 0.3648 0.4160 0.0108  -0.0472 -0.0187 11  LYS   B CD  
3988 C CE  . LYS   B 11  ? 0.4192 0.3810 0.4620 0.0137  -0.0445 -0.0216 11  LYS   B CE  
3989 N NZ  . LYS   B 11  ? 0.4288 0.3912 0.4877 0.0139  -0.0446 -0.0210 11  LYS   B NZ  
4003 N N   . LEU   B 12  ? 0.2626 0.2023 0.2540 -0.0616 -0.0382 -0.0359 12  LEU   B N   
4004 C CA  . LEU   B 12  ? 0.2405 0.1848 0.2719 -0.0564 -0.0319 -0.0296 12  LEU   B CA  
4005 C C   . LEU   B 12  ? 0.2269 0.1923 0.2804 -0.0585 -0.0476 -0.0301 12  LEU   B C   
4006 O O   . LEU   B 12  ? 0.2223 0.1978 0.2964 -0.0667 -0.0603 -0.0234 12  LEU   B O   
4007 C CB  . LEU   B 12  ? 0.2382 0.1690 0.2696 -0.0398 -0.0200 -0.0278 12  LEU   B CB  
4008 C CG  . LEU   B 12  ? 0.2314 0.1641 0.2747 -0.0389 -0.0170 -0.0232 12  LEU   B CG  
4009 C CD1 . LEU   B 12  ? 0.2400 0.1672 0.2703 -0.0205 -0.0179 -0.0003 12  LEU   B CD1 
4010 C CD2 . LEU   B 12  ? 0.2371 0.1710 0.2933 -0.0384 -0.0124 -0.0343 12  LEU   B CD2 
4022 N N   . THR   B 13  ? 0.2228 0.1962 0.2899 -0.0547 -0.0448 -0.0394 13  THR   B N   
4023 C CA  . THR   B 13  ? 0.2241 0.2010 0.2833 -0.0613 -0.0560 -0.0282 13  THR   B CA  
4024 C C   . THR   B 13  ? 0.2595 0.2182 0.2907 -0.0675 -0.0706 -0.0243 13  THR   B C   
4025 O O   . THR   B 13  ? 0.2788 0.2199 0.2970 -0.0600 -0.0374 -0.0269 13  THR   B O   
4026 C CB  . THR   B 13  ? 0.2041 0.1978 0.2815 -0.0537 -0.0539 -0.0137 13  THR   B CB  
4027 O OG1 . THR   B 13  ? 0.1944 0.1905 0.2782 -0.0447 -0.0402 -0.0116 13  THR   B OG1 
4028 C CG2 . THR   B 13  ? 0.2154 0.2051 0.2891 -0.0497 -0.0424 -0.0104 13  THR   B CG2 
4036 N N   A ASP   B 14  ? 0.2690 0.2319 0.3012 -0.0764 -0.1009 -0.0136 14  ASP   B N   
4037 N N   B ASP   B 14  ? 0.2682 0.2302 0.2985 -0.0701 -0.0871 -0.0089 14  ASP   B N   
4038 C CA  A ASP   B 14  ? 0.2815 0.2501 0.3290 -0.0763 -0.1056 0.0091  14  ASP   B CA  
4039 C CA  B ASP   B 14  ? 0.2773 0.2447 0.3143 -0.0679 -0.0907 0.0117  14  ASP   B CA  
4040 C C   A ASP   B 14  ? 0.2675 0.2314 0.2855 -0.0785 -0.0915 0.0158  14  ASP   B C   
4041 C C   B ASP   B 14  ? 0.2614 0.2262 0.2769 -0.0703 -0.0875 0.0159  14  ASP   B C   
4042 O O   A ASP   B 14  ? 0.2876 0.2453 0.2918 -0.0815 -0.0903 0.0272  14  ASP   B O   
4043 O O   B ASP   B 14  ? 0.2738 0.2306 0.2763 -0.0694 -0.0907 0.0222  14  ASP   B O   
4044 C CB  A ASP   B 14  ? 0.3050 0.2826 0.4042 -0.0737 -0.1156 0.0093  14  ASP   B CB  
4045 C CB  B ASP   B 14  ? 0.2993 0.2737 0.3697 -0.0625 -0.0913 0.0173  14  ASP   B CB  
4046 C CG  A ASP   B 14  ? 0.3305 0.3077 0.4767 -0.0719 -0.1096 -0.0011 14  ASP   B CG  
4047 C CG  B ASP   B 14  ? 0.3211 0.2968 0.4208 -0.0579 -0.0848 0.0141  14  ASP   B CG  
4048 O OD1 A ASP   B 14  ? 0.3435 0.3151 0.4904 -0.0772 -0.1109 -0.0146 14  ASP   B OD1 
4049 O OD1 B ASP   B 14  ? 0.3287 0.3068 0.4289 -0.0592 -0.0798 0.0073  14  ASP   B OD1 
4050 O OD2 A ASP   B 14  ? 0.3367 0.3179 0.5129 -0.0702 -0.1014 0.0009  14  ASP   B OD2 
4051 O OD2 B ASP   B 14  ? 0.3288 0.3033 0.4448 -0.0577 -0.0843 0.0168  14  ASP   B OD2 
4060 N N   . ASN   B 15  ? 0.2352 0.2043 0.2530 -0.0656 -0.0867 0.0106  15  ASN   B N   
4061 C CA  . ASN   B 15  ? 0.1920 0.1749 0.2379 -0.0440 -0.0598 0.0030  15  ASN   B CA  
4062 C C   . ASN   B 15  ? 0.1732 0.1611 0.2202 -0.0237 -0.0501 0.0023  15  ASN   B C   
4063 O O   . ASN   B 15  ? 0.1753 0.1542 0.2465 -0.0264 -0.0513 -0.0138 15  ASN   B O   
4064 C CB  . ASN   B 15  ? 0.1859 0.1708 0.2611 -0.0223 -0.0574 0.0061  15  ASN   B CB  
4065 C CG  . ASN   B 15  ? 0.1753 0.1645 0.2562 -0.0293 -0.0390 0.0053  15  ASN   B CG  
4066 O OD1 . ASN   B 15  ? 0.1825 0.1906 0.2857 -0.0418 -0.0371 0.0120  15  ASN   B OD1 
4067 N ND2 . ASN   B 15  ? 0.1806 0.1450 0.2511 -0.0140 -0.0110 -0.0067 15  ASN   B ND2 
4075 N N   . VAL   B 16  ? 0.1789 0.1553 0.2186 -0.0297 -0.0505 0.0048  16  VAL   B N   
4076 C CA  . VAL   B 16  ? 0.1778 0.1533 0.2032 -0.0270 -0.0428 -0.0188 16  VAL   B CA  
4077 C C   . VAL   B 16  ? 0.1782 0.1607 0.1985 -0.0374 -0.0435 -0.0169 16  VAL   B C   
4078 O O   . VAL   B 16  ? 0.1839 0.1737 0.2305 -0.0329 -0.0305 -0.0295 16  VAL   B O   
4079 C CB  . VAL   B 16  ? 0.1877 0.1501 0.2216 -0.0132 -0.0308 -0.0153 16  VAL   B CB  
4080 C CG1 . VAL   B 16  ? 0.1937 0.1515 0.2261 -0.0037 -0.0345 -0.0078 16  VAL   B CG1 
4081 C CG2 . VAL   B 16  ? 0.1882 0.1622 0.2346 -0.0087 -0.0192 -0.0155 16  VAL   B CG2 
4091 N N   . TYR   B 17  ? 0.1833 0.1751 0.2065 -0.0339 -0.0304 -0.0227 17  TYR   B N   
4092 C CA  . TYR   B 17  ? 0.1947 0.1884 0.1951 -0.0403 -0.0284 -0.0015 17  TYR   B CA  
4093 C C   . TYR   B 17  ? 0.1899 0.1625 0.2040 -0.0377 -0.0215 -0.0062 17  TYR   B C   
4094 O O   . TYR   B 17  ? 0.1887 0.1657 0.2148 -0.0310 -0.0318 -0.0303 17  TYR   B O   
4095 C CB  . TYR   B 17  ? 0.2249 0.2322 0.2202 -0.0248 -0.0296 0.0283  17  TYR   B CB  
4096 C CG  . TYR   B 17  ? 0.2567 0.2775 0.2609 -0.0182 -0.0450 0.0408  17  TYR   B CG  
4097 C CD1 . TYR   B 17  ? 0.2738 0.2897 0.2803 -0.0175 -0.0500 0.0522  17  TYR   B CD1 
4098 C CD2 . TYR   B 17  ? 0.2809 0.3049 0.2867 -0.0074 -0.0555 0.0372  17  TYR   B CD2 
4099 C CE1 . TYR   B 17  ? 0.2946 0.3126 0.2979 -0.0085 -0.0654 0.0457  17  TYR   B CE1 
4100 C CE2 . TYR   B 17  ? 0.2965 0.3215 0.3063 0.0028  -0.0747 0.0416  17  TYR   B CE2 
4101 C CZ  . TYR   B 17  ? 0.3070 0.3291 0.3112 0.0041  -0.0813 0.0460  17  TYR   B CZ  
4102 O OH  . TYR   B 17  ? 0.3236 0.3489 0.3325 0.0115  -0.0915 0.0461  17  TYR   B OH  
4112 N N   . ILE   B 18  ? 0.2017 0.1635 0.1872 -0.0332 -0.0093 -0.0143 18  ILE   B N   
4113 C CA  . ILE   B 18  ? 0.2018 0.1587 0.1833 -0.0399 -0.0089 -0.0233 18  ILE   B CA  
4114 C C   . ILE   B 18  ? 0.2161 0.1603 0.1843 -0.0495 -0.0045 -0.0359 18  ILE   B C   
4115 O O   . ILE   B 18  ? 0.2379 0.1751 0.1977 -0.0395 0.0063  -0.0388 18  ILE   B O   
4116 C CB  . ILE   B 18  ? 0.2076 0.1637 0.2000 -0.0465 -0.0073 -0.0181 18  ILE   B CB  
4117 C CG1 . ILE   B 18  ? 0.2103 0.1668 0.2030 -0.0464 0.0005  -0.0079 18  ILE   B CG1 
4118 C CG2 . ILE   B 18  ? 0.2053 0.1705 0.2097 -0.0463 -0.0107 -0.0183 18  ILE   B CG2 
4119 C CD1 . ILE   B 18  ? 0.2151 0.1934 0.2300 -0.0464 -0.0137 0.0062  18  ILE   B CD1 
4131 N N   . LYS   B 19  ? 0.2117 0.1627 0.2127 -0.0330 0.0362  -0.0329 19  LYS   B N   
4132 C CA  . LYS   B 19  ? 0.2197 0.1643 0.2278 -0.0315 0.0292  -0.0348 19  LYS   B CA  
4133 C C   . LYS   B 19  ? 0.2029 0.1646 0.2389 -0.0284 0.0298  -0.0473 19  LYS   B C   
4134 O O   . LYS   B 19  ? 0.1964 0.1677 0.2195 -0.0153 0.0203  -0.0441 19  LYS   B O   
4135 C CB  . LYS   B 19  ? 0.2443 0.1885 0.2409 -0.0358 0.0408  -0.0277 19  LYS   B CB  
4136 C CG  . LYS   B 19  ? 0.2646 0.2103 0.2687 -0.0450 0.0533  -0.0245 19  LYS   B CG  
4137 C CD  . LYS   B 19  ? 0.2910 0.2426 0.2769 -0.0519 0.0557  -0.0160 19  LYS   B CD  
4138 C CE  . LYS   B 19  ? 0.3189 0.2678 0.2972 -0.0521 0.0526  -0.0189 19  LYS   B CE  
4139 N NZ  . LYS   B 19  ? 0.3382 0.2861 0.3109 -0.0554 0.0609  -0.0189 19  LYS   B NZ  
4153 N N   . ASN   B 20  ? 0.2069 0.1728 0.2707 -0.0288 0.0404  -0.0577 20  ASN   B N   
4154 C CA  . ASN   B 20  ? 0.2077 0.1866 0.2962 -0.0152 0.0441  -0.0761 20  ASN   B CA  
4155 C C   . ASN   B 20  ? 0.1986 0.2069 0.3014 -0.0257 0.0573  -0.0767 20  ASN   B C   
4156 O O   . ASN   B 20  ? 0.2199 0.2410 0.3156 -0.0376 0.0557  -0.0761 20  ASN   B O   
4157 C CB  . ASN   B 20  ? 0.2383 0.1907 0.3303 0.0088  0.0279  -0.0811 20  ASN   B CB  
4158 C CG  . ASN   B 20  ? 0.2617 0.1937 0.3570 0.0399  0.0260  -0.0836 20  ASN   B CG  
4159 O OD1 . ASN   B 20  ? 0.2892 0.2305 0.3834 0.0554  0.0205  -0.0877 20  ASN   B OD1 
4160 N ND2 . ASN   B 20  ? 0.2511 0.1956 0.3521 0.0366  0.0159  -0.0761 20  ASN   B ND2 
4167 N N   . ALA   B 21  ? 0.1974 0.1880 0.3048 -0.0285 0.0524  -0.0622 21  ALA   B N   
4168 C CA  . ALA   B 21  ? 0.2069 0.1928 0.3143 -0.0299 0.0393  -0.0548 21  ALA   B CA  
4169 C C   . ALA   B 21  ? 0.2071 0.1689 0.2986 -0.0213 0.0437  -0.0398 21  ALA   B C   
4170 O O   . ALA   B 21  ? 0.2105 0.1602 0.2917 -0.0280 0.0406  -0.0307 21  ALA   B O   
4171 C CB  . ALA   B 21  ? 0.2230 0.2157 0.3214 -0.0428 0.0315  -0.0362 21  ALA   B CB  
4177 N N   . ASP   B 22  ? 0.1983 0.1640 0.2846 -0.0230 0.0416  -0.0342 22  ASP   B N   
4178 C CA  . ASP   B 22  ? 0.1953 0.1590 0.2682 -0.0134 0.0301  -0.0295 22  ASP   B CA  
4179 C C   . ASP   B 22  ? 0.1892 0.1500 0.2244 -0.0160 0.0169  -0.0094 22  ASP   B C   
4180 O O   . ASP   B 22  ? 0.1882 0.1542 0.2328 -0.0087 0.0077  -0.0039 22  ASP   B O   
4181 C CB  . ASP   B 22  ? 0.2085 0.1744 0.3069 -0.0108 0.0327  -0.0085 22  ASP   B CB  
4182 C CG  . ASP   B 22  ? 0.2059 0.1892 0.3522 -0.0009 0.0079  -0.0029 22  ASP   B CG  
4183 O OD1 . ASP   B 22  ? 0.2182 0.1839 0.3475 0.0004  -0.0131 -0.0075 22  ASP   B OD1 
4184 O OD2 . ASP   B 22  ? 0.2150 0.2149 0.4006 0.0092  -0.0091 -0.0205 22  ASP   B OD2 
4189 N N   . ILE   B 23  ? 0.1865 0.1450 0.2138 -0.0126 0.0001  0.0093  23  ILE   B N   
4190 C CA  . ILE   B 23  ? 0.1777 0.1496 0.1894 -0.0112 -0.0078 0.0119  23  ILE   B CA  
4191 C C   . ILE   B 23  ? 0.1703 0.1515 0.1863 -0.0099 -0.0113 0.0055  23  ILE   B C   
4192 O O   . ILE   B 23  ? 0.1592 0.1502 0.1759 -0.0110 -0.0058 0.0026  23  ILE   B O   
4193 C CB  . ILE   B 23  ? 0.1708 0.1550 0.2047 -0.0174 -0.0025 0.0155  23  ILE   B CB  
4194 C CG1 . ILE   B 23  ? 0.1783 0.1692 0.2187 -0.0138 0.0088  0.0218  23  ILE   B CG1 
4195 C CG2 . ILE   B 23  ? 0.1784 0.1792 0.2122 -0.0124 0.0001  0.0049  23  ILE   B CG2 
4196 C CD1 . ILE   B 23  ? 0.1808 0.1730 0.2269 -0.0099 0.0041  0.0183  23  ILE   B CD1 
4208 N N   . VAL   B 24  ? 0.1725 0.1500 0.1972 -0.0074 -0.0102 -0.0022 24  VAL   B N   
4209 C CA  . VAL   B 24  ? 0.1637 0.1492 0.2211 -0.0031 -0.0154 -0.0039 24  VAL   B CA  
4210 C C   . VAL   B 24  ? 0.1617 0.1595 0.2260 -0.0107 -0.0036 0.0031  24  VAL   B C   
4211 O O   . VAL   B 24  ? 0.1613 0.1704 0.2375 -0.0133 -0.0077 0.0065  24  VAL   B O   
4212 C CB  . VAL   B 24  ? 0.1755 0.1725 0.2334 0.0029  -0.0239 0.0050  24  VAL   B CB  
4213 C CG1 . VAL   B 24  ? 0.1734 0.1726 0.2600 -0.0051 -0.0222 0.0017  24  VAL   B CG1 
4214 C CG2 . VAL   B 24  ? 0.1857 0.1999 0.2380 0.0038  -0.0226 -0.0076 24  VAL   B CG2 
4224 N N   . GLU   B 25  ? 0.1846 0.1741 0.2276 -0.0095 0.0013  0.0069  25  GLU   B N   
4225 C CA  . GLU   B 25  ? 0.1982 0.1983 0.2416 0.0008  0.0127  -0.0021 25  GLU   B CA  
4226 C C   . GLU   B 25  ? 0.1958 0.1902 0.2100 -0.0032 0.0168  0.0038  25  GLU   B C   
4227 O O   . GLU   B 25  ? 0.2039 0.1980 0.2256 -0.0086 0.0253  0.0138  25  GLU   B O   
4228 C CB  . GLU   B 25  ? 0.2412 0.2468 0.3110 0.0235  0.0256  -0.0029 25  GLU   B CB  
4229 C CG  . GLU   B 25  ? 0.2787 0.3117 0.4166 0.0294  0.0222  -0.0059 25  GLU   B CG  
4230 C CD  . GLU   B 25  ? 0.3242 0.3691 0.5054 0.0252  0.0204  -0.0107 25  GLU   B CD  
4231 O OE1 . GLU   B 25  ? 0.3418 0.3918 0.5358 0.0274  0.0256  -0.0104 25  GLU   B OE1 
4232 O OE2 . GLU   B 25  ? 0.3398 0.3864 0.5418 0.0254  0.0180  -0.0164 25  GLU   B OE2 
4239 N N   . GLU   B 26  ? 0.1925 0.1782 0.2000 -0.0254 0.0102  -0.0001 26  GLU   B N   
4240 C CA  . GLU   B 26  ? 0.1887 0.1941 0.2007 -0.0300 -0.0025 0.0022  26  GLU   B CA  
4241 C C   . GLU   B 26  ? 0.1706 0.1910 0.1952 -0.0209 0.0073  0.0159  26  GLU   B C   
4242 O O   . GLU   B 26  ? 0.1869 0.2125 0.1954 -0.0241 -0.0019 0.0278  26  GLU   B O   
4243 C CB  . GLU   B 26  ? 0.2177 0.2137 0.2277 -0.0453 -0.0027 0.0082  26  GLU   B CB  
4244 C CG  . GLU   B 26  ? 0.2617 0.2518 0.2848 -0.0495 0.0088  -0.0152 26  GLU   B CG  
4245 C CD  . GLU   B 26  ? 0.2895 0.2711 0.2993 -0.0729 0.0234  -0.0463 26  GLU   B CD  
4246 O OE1 . GLU   B 26  ? 0.3130 0.2549 0.3016 -0.0818 0.0667  -0.0385 26  GLU   B OE1 
4247 O OE2 . GLU   B 26  ? 0.2917 0.3140 0.3469 -0.0654 0.0226  -0.0358 26  GLU   B OE2 
4254 N N   . ALA   B 27  ? 0.1503 0.1708 0.2043 -0.0194 0.0054  0.0210  27  ALA   B N   
4255 C CA  . ALA   B 27  ? 0.1625 0.1710 0.2110 -0.0124 -0.0050 0.0311  27  ALA   B CA  
4256 C C   . ALA   B 27  ? 0.1718 0.1772 0.2272 -0.0147 0.0113  0.0405  27  ALA   B C   
4257 O O   . ALA   B 27  ? 0.1821 0.1853 0.2442 -0.0045 0.0111  0.0487  27  ALA   B O   
4258 C CB  . ALA   B 27  ? 0.1763 0.1572 0.2081 -0.0138 -0.0063 0.0260  27  ALA   B CB  
4264 N N   . LYS   B 28  ? 0.1654 0.1953 0.2676 -0.0216 0.0227  0.0605  28  LYS   B N   
4265 C CA  . LYS   B 28  ? 0.1827 0.2374 0.3026 -0.0055 0.0541  0.0901  28  LYS   B CA  
4266 C C   . LYS   B 28  ? 0.2049 0.2588 0.2908 0.0041  0.0661  0.0827  28  LYS   B C   
4267 O O   . LYS   B 28  ? 0.2256 0.2663 0.3082 0.0019  0.0652  0.0778  28  LYS   B O   
4268 C CB  . LYS   B 28  ? 0.2038 0.2707 0.3533 0.0125  0.0828  0.1086  28  LYS   B CB  
4269 C CG  . LYS   B 28  ? 0.2364 0.3219 0.3979 0.0301  0.0845  0.1116  28  LYS   B CG  
4270 C CD  . LYS   B 28  ? 0.2889 0.3868 0.4501 0.0380  0.0984  0.1114  28  LYS   B CD  
4271 C CE  . LYS   B 28  ? 0.3251 0.4303 0.4926 0.0476  0.1017  0.1143  28  LYS   B CE  
4272 N NZ  . LYS   B 28  ? 0.3477 0.4416 0.5113 0.0555  0.1026  0.1196  28  LYS   B NZ  
4286 N N   . LYS   B 29  ? 0.2260 0.2829 0.2874 0.0249  0.0665  0.0704  29  LYS   B N   
4287 C CA  . LYS   B 29  ? 0.2687 0.3146 0.3101 0.0300  0.0633  0.0658  29  LYS   B CA  
4288 C C   . LYS   B 29  ? 0.2612 0.3086 0.2748 0.0232  0.0519  0.0721  29  LYS   B C   
4289 O O   . LYS   B 29  ? 0.2814 0.3322 0.2849 0.0240  0.0523  0.0764  29  LYS   B O   
4290 C CB  . LYS   B 29  ? 0.3287 0.3593 0.3920 0.0298  0.0603  0.0582  29  LYS   B CB  
4291 C CG  . LYS   B 29  ? 0.3805 0.3950 0.4771 0.0268  0.0621  0.0562  29  LYS   B CG  
4292 C CD  . LYS   B 29  ? 0.4242 0.4249 0.5458 0.0220  0.0696  0.0520  29  LYS   B CD  
4293 C CE  . LYS   B 29  ? 0.4523 0.4460 0.5923 0.0180  0.0767  0.0497  29  LYS   B CE  
4294 N NZ  . LYS   B 29  ? 0.4632 0.4510 0.6225 0.0167  0.0785  0.0478  29  LYS   B NZ  
4308 N N   . VAL   B 30  ? 0.2278 0.2823 0.2525 0.0056  0.0408  0.0669  30  VAL   B N   
4309 C CA  . VAL   B 30  ? 0.2167 0.2694 0.2908 -0.0108 0.0035  0.0650  30  VAL   B CA  
4310 C C   . VAL   B 30  ? 0.1946 0.2605 0.2726 -0.0157 0.0065  0.0808  30  VAL   B C   
4311 O O   . VAL   B 30  ? 0.2104 0.2772 0.2785 -0.0042 0.0046  0.0943  30  VAL   B O   
4312 C CB  . VAL   B 30  ? 0.2262 0.2615 0.3346 -0.0260 -0.0238 0.0634  30  VAL   B CB  
4313 C CG1 . VAL   B 30  ? 0.2314 0.2654 0.3397 -0.0287 -0.0248 0.0624  30  VAL   B CG1 
4314 C CG2 . VAL   B 30  ? 0.2413 0.2615 0.3512 -0.0329 -0.0340 0.0518  30  VAL   B CG2 
4324 N N   . LYS   B 31  ? 0.1846 0.2269 0.2948 -0.0313 0.0060  0.0840  31  LYS   B N   
4325 C CA  . LYS   B 31  ? 0.1765 0.2276 0.3238 -0.0426 -0.0042 0.0848  31  LYS   B CA  
4326 C C   . LYS   B 31  ? 0.1731 0.1917 0.2851 -0.0384 -0.0228 0.0743  31  LYS   B C   
4327 O O   . LYS   B 31  ? 0.1853 0.2014 0.3025 -0.0331 -0.0205 0.0917  31  LYS   B O   
4328 C CB  . LYS   B 31  ? 0.1924 0.2752 0.3717 -0.0365 0.0182  0.1046  31  LYS   B CB  
4329 C CG  . LYS   B 31  ? 0.2341 0.3247 0.4206 -0.0338 0.0295  0.1038  31  LYS   B CG  
4330 C CD  . LYS   B 31  ? 0.2746 0.3732 0.4726 -0.0275 0.0170  0.0896  31  LYS   B CD  
4331 C CE  . LYS   B 31  ? 0.3025 0.4003 0.5166 -0.0251 0.0037  0.0785  31  LYS   B CE  
4332 N NZ  . LYS   B 31  ? 0.3154 0.4147 0.5357 -0.0200 -0.0102 0.0667  31  LYS   B NZ  
4346 N N   . PRO   B 32  ? 0.1783 0.1607 0.2321 -0.0334 -0.0381 0.0461  32  PRO   B N   
4347 C CA  . PRO   B 32  ? 0.1851 0.1603 0.1817 -0.0370 -0.0453 0.0294  32  PRO   B CA  
4348 C C   . PRO   B 32  ? 0.1939 0.1507 0.1944 -0.0335 -0.0500 0.0317  32  PRO   B C   
4349 O O   . PRO   B 32  ? 0.2036 0.1513 0.2247 -0.0415 -0.0694 0.0292  32  PRO   B O   
4350 C CB  . PRO   B 32  ? 0.2009 0.1570 0.1906 -0.0397 -0.0452 0.0178  32  PRO   B CB  
4351 C CG  . PRO   B 32  ? 0.2152 0.1452 0.2008 -0.0281 -0.0549 0.0217  32  PRO   B CG  
4352 C CD  . PRO   B 32  ? 0.1998 0.1502 0.2181 -0.0249 -0.0540 0.0272  32  PRO   B CD  
4360 N N   . THR   B 33  ? 0.1939 0.1404 0.1793 -0.0288 -0.0493 0.0236  33  THR   B N   
4361 C CA  . THR   B 33  ? 0.2011 0.1505 0.1756 -0.0284 -0.0457 0.0255  33  THR   B CA  
4362 C C   . THR   B 33  ? 0.2035 0.1366 0.1663 -0.0279 -0.0433 0.0234  33  THR   B C   
4363 O O   . THR   B 33  ? 0.2235 0.1430 0.1794 -0.0397 -0.0547 0.0182  33  THR   B O   
4364 C CB  . THR   B 33  ? 0.2104 0.1580 0.1831 -0.0156 -0.0519 0.0284  33  THR   B CB  
4365 O OG1 . THR   B 33  ? 0.1983 0.1647 0.1873 -0.0183 -0.0453 0.0282  33  THR   B OG1 
4366 C CG2 . THR   B 33  ? 0.2312 0.1625 0.2063 -0.0107 -0.0454 0.0184  33  THR   B CG2 
4374 N N   . VAL   B 34  ? 0.1855 0.1378 0.1569 -0.0317 -0.0374 0.0184  34  VAL   B N   
4375 C CA  . VAL   B 34  ? 0.1737 0.1402 0.1592 -0.0232 -0.0350 0.0141  34  VAL   B CA  
4376 C C   . VAL   B 34  ? 0.1542 0.1337 0.1399 -0.0302 -0.0230 0.0083  34  VAL   B C   
4377 O O   . VAL   B 34  ? 0.1777 0.1368 0.1479 -0.0258 -0.0338 0.0102  34  VAL   B O   
4378 C CB  . VAL   B 34  ? 0.1786 0.1452 0.1868 -0.0087 -0.0306 0.0008  34  VAL   B CB  
4379 C CG1 . VAL   B 34  ? 0.1790 0.1564 0.1936 -0.0103 -0.0098 -0.0096 34  VAL   B CG1 
4380 C CG2 . VAL   B 34  ? 0.1859 0.1451 0.2122 -0.0114 -0.0222 0.0021  34  VAL   B CG2 
4390 N N   . VAL   B 35  ? 0.1503 0.1294 0.1387 -0.0246 -0.0135 0.0072  35  VAL   B N   
4391 C CA  . VAL   B 35  ? 0.1443 0.1318 0.1436 -0.0198 -0.0102 0.0077  35  VAL   B CA  
4392 C C   . VAL   B 35  ? 0.1342 0.1268 0.1391 -0.0136 -0.0174 0.0027  35  VAL   B C   
4393 O O   . VAL   B 35  ? 0.1395 0.1322 0.1379 -0.0210 -0.0011 -0.0039 35  VAL   B O   
4394 C CB  . VAL   B 35  ? 0.1448 0.1471 0.1513 -0.0139 -0.0028 0.0070  35  VAL   B CB  
4395 C CG1 . VAL   B 35  ? 0.1426 0.1588 0.1684 -0.0223 -0.0017 0.0021  35  VAL   B CG1 
4396 C CG2 . VAL   B 35  ? 0.1466 0.1470 0.1718 -0.0053 -0.0012 -0.0023 35  VAL   B CG2 
4406 N N   . VAL   B 36  ? 0.1384 0.1259 0.1348 -0.0153 -0.0173 0.0095  36  VAL   B N   
4407 C CA  . VAL   B 36  ? 0.1320 0.1215 0.1393 -0.0120 -0.0101 -0.0002 36  VAL   B CA  
4408 C C   . VAL   B 36  ? 0.1270 0.1208 0.1334 -0.0114 -0.0086 0.0064  36  VAL   B C   
4409 O O   . VAL   B 36  ? 0.1373 0.1368 0.1552 -0.0138 -0.0038 -0.0086 36  VAL   B O   
4410 C CB  . VAL   B 36  ? 0.1316 0.1307 0.1544 -0.0145 -0.0045 0.0054  36  VAL   B CB  
4411 C CG1 . VAL   B 36  ? 0.1251 0.1434 0.1670 -0.0166 -0.0077 0.0045  36  VAL   B CG1 
4412 C CG2 . VAL   B 36  ? 0.1423 0.1345 0.1553 -0.0143 -0.0122 0.0117  36  VAL   B CG2 
4422 N N   . ASN   B 37  ? 0.1300 0.1285 0.1306 -0.0003 -0.0071 0.0066  37  ASN   B N   
4423 C CA  . ASN   B 37  ? 0.1370 0.1297 0.1450 -0.0010 -0.0150 0.0066  37  ASN   B CA  
4424 C C   . ASN   B 37  ? 0.1325 0.1294 0.1422 0.0018  -0.0064 0.0035  37  ASN   B C   
4425 O O   . ASN   B 37  ? 0.1453 0.1377 0.1448 0.0005  -0.0043 0.0077  37  ASN   B O   
4426 C CB  . ASN   B 37  ? 0.1403 0.1393 0.1327 -0.0019 -0.0117 0.0073  37  ASN   B CB  
4427 C CG  . ASN   B 37  ? 0.1428 0.1318 0.1350 -0.0004 -0.0084 0.0038  37  ASN   B CG  
4428 O OD1 . ASN   B 37  ? 0.1474 0.1400 0.1587 0.0073  -0.0164 0.0026  37  ASN   B OD1 
4429 N ND2 . ASN   B 37  ? 0.1508 0.1338 0.1508 0.0019  -0.0170 0.0086  37  ASN   B ND2 
4436 N N   . ALA   B 38  ? 0.1379 0.1319 0.1435 0.0069  -0.0017 0.0047  38  ALA   B N   
4437 C CA  . ALA   B 38  ? 0.1479 0.1353 0.1489 -0.0019 0.0024  0.0119  38  ALA   B CA  
4438 C C   . ALA   B 38  ? 0.1515 0.1333 0.1432 0.0016  0.0024  0.0109  38  ALA   B C   
4439 O O   . ALA   B 38  ? 0.1583 0.1430 0.1594 0.0056  -0.0046 0.0121  38  ALA   B O   
4440 C CB  . ALA   B 38  ? 0.1725 0.1505 0.1563 -0.0125 0.0153  0.0092  38  ALA   B CB  
4446 N N   . ALA   B 39  ? 0.1454 0.1332 0.1359 0.0087  -0.0045 0.0047  39  ALA   B N   
4447 C CA  . ALA   B 39  ? 0.1582 0.1395 0.1305 0.0107  -0.0040 0.0042  39  ALA   B CA  
4448 C C   . ALA   B 39  ? 0.1592 0.1497 0.1219 0.0082  -0.0057 -0.0011 39  ALA   B C   
4449 O O   . ALA   B 39  ? 0.1622 0.1517 0.1584 -0.0009 -0.0017 0.0128  39  ALA   B O   
4450 C CB  . ALA   B 39  ? 0.1578 0.1470 0.1526 -0.0059 0.0032  0.0025  39  ALA   B CB  
4456 N N   . ASN   B 40  ? 0.1660 0.1690 0.1288 -0.0054 0.0056  -0.0082 40  ASN   B N   
4457 C CA  . ASN   B 40  ? 0.1685 0.1734 0.1440 -0.0014 -0.0053 -0.0072 40  ASN   B CA  
4458 C C   . ASN   B 40  ? 0.1728 0.1694 0.1280 0.0042  -0.0064 -0.0031 40  ASN   B C   
4459 O O   . ASN   B 40  ? 0.1708 0.1598 0.1395 0.0081  -0.0111 0.0012  40  ASN   B O   
4460 C CB  . ASN   B 40  ? 0.1871 0.1712 0.1729 0.0155  -0.0167 0.0109  40  ASN   B CB  
4461 C CG  . ASN   B 40  ? 0.1923 0.1756 0.1975 0.0084  -0.0277 0.0141  40  ASN   B CG  
4462 O OD1 . ASN   B 40  ? 0.1911 0.1696 0.2700 0.0073  -0.0326 0.0154  40  ASN   B OD1 
4463 N ND2 . ASN   B 40  ? 0.1875 0.1760 0.1997 0.0058  -0.0212 0.0135  40  ASN   B ND2 
4470 N N   . VAL   B 41  ? 0.1811 0.1696 0.1373 0.0104  0.0070  -0.0005 41  VAL   B N   
4471 C CA  . VAL   B 41  ? 0.1906 0.1856 0.1467 0.0059  0.0004  -0.0088 41  VAL   B CA  
4472 C C   . VAL   B 41  ? 0.1878 0.1847 0.1402 0.0144  -0.0050 -0.0108 41  VAL   B C   
4473 O O   . VAL   B 41  ? 0.1834 0.1818 0.1479 0.0108  -0.0112 -0.0150 41  VAL   B O   
4474 C CB  . VAL   B 41  ? 0.2068 0.2025 0.1676 -0.0038 0.0140  -0.0194 41  VAL   B CB  
4475 C CG1 . VAL   B 41  ? 0.2037 0.2155 0.1862 -0.0082 0.0244  -0.0187 41  VAL   B CG1 
4476 C CG2 . VAL   B 41  ? 0.2195 0.2176 0.1839 -0.0125 0.0145  -0.0149 41  VAL   B CG2 
4486 N N   . TYR   B 42  ? 0.1947 0.1877 0.1437 0.0131  -0.0216 0.0035  42  TYR   B N   
4487 C CA  . TYR   B 42  ? 0.1997 0.1983 0.1459 0.0143  -0.0286 -0.0069 42  TYR   B CA  
4488 C C   . TYR   B 42  ? 0.1836 0.1743 0.1561 0.0170  -0.0248 -0.0143 42  TYR   B C   
4489 O O   . TYR   B 42  ? 0.1890 0.1841 0.1885 0.0086  -0.0323 -0.0203 42  TYR   B O   
4490 C CB  . TYR   B 42  ? 0.2192 0.2299 0.1732 0.0120  -0.0249 0.0053  42  TYR   B CB  
4491 C CG  . TYR   B 42  ? 0.2229 0.2473 0.1672 0.0063  -0.0297 0.0082  42  TYR   B CG  
4492 C CD1 . TYR   B 42  ? 0.2132 0.2442 0.1558 0.0043  -0.0231 -0.0048 42  TYR   B CD1 
4493 C CD2 . TYR   B 42  ? 0.2446 0.2609 0.2210 0.0099  -0.0113 0.0147  42  TYR   B CD2 
4494 C CE1 . TYR   B 42  ? 0.2335 0.2614 0.1667 0.0073  -0.0183 0.0016  42  TYR   B CE1 
4495 C CE2 . TYR   B 42  ? 0.2470 0.2684 0.2165 0.0113  0.0030  0.0324  42  TYR   B CE2 
4496 C CZ  . TYR   B 42  ? 0.2546 0.2764 0.2044 0.0231  0.0063  0.0221  42  TYR   B CZ  
4497 O OH  . TYR   B 42  ? 0.2856 0.3017 0.2510 0.0379  0.0153  0.0378  42  TYR   B OH  
4507 N N   . LEU   B 43  ? 0.1690 0.1563 0.1507 0.0127  -0.0190 -0.0087 43  LEU   B N   
4508 C CA  . LEU   B 43  ? 0.1666 0.1557 0.1454 0.0043  -0.0141 0.0013  43  LEU   B CA  
4509 C C   . LEU   B 43  ? 0.1752 0.1600 0.1517 0.0018  -0.0160 0.0012  43  LEU   B C   
4510 O O   . LEU   B 43  ? 0.1625 0.1665 0.1817 0.0067  -0.0206 0.0112  43  LEU   B O   
4511 C CB  . LEU   B 43  ? 0.1698 0.1527 0.1584 -0.0050 -0.0279 -0.0027 43  LEU   B CB  
4512 C CG  . LEU   B 43  ? 0.1686 0.1492 0.1715 0.0011  -0.0300 -0.0003 43  LEU   B CG  
4513 C CD1 . LEU   B 43  ? 0.1750 0.1601 0.2024 -0.0023 -0.0411 0.0011  43  LEU   B CD1 
4514 C CD2 . LEU   B 43  ? 0.1696 0.1502 0.1846 -0.0028 -0.0317 0.0004  43  LEU   B CD2 
4526 N N   . LYS   B 44  ? 0.1713 0.1543 0.1547 0.0074  -0.0151 -0.0080 44  LYS   B N   
4527 C CA  . LYS   B 44  ? 0.1808 0.1682 0.1510 0.0062  -0.0172 0.0099  44  LYS   B CA  
4528 C C   . LYS   B 44  ? 0.1740 0.1672 0.1597 0.0123  -0.0111 0.0053  44  LYS   B C   
4529 O O   . LYS   B 44  ? 0.1930 0.1678 0.1787 0.0057  -0.0082 0.0043  44  LYS   B O   
4530 C CB  . LYS   B 44  ? 0.2105 0.1917 0.1752 0.0197  -0.0319 0.0032  44  LYS   B CB  
4531 C CG  . LYS   B 44  ? 0.2508 0.2238 0.2180 0.0121  -0.0538 0.0092  44  LYS   B CG  
4532 C CD  . LYS   B 44  ? 0.2910 0.2450 0.2760 -0.0042 -0.0648 0.0125  44  LYS   B CD  
4533 C CE  . LYS   B 44  ? 0.3247 0.2728 0.3191 -0.0115 -0.0657 0.0215  44  LYS   B CE  
4534 N NZ  . LYS   B 44  ? 0.3376 0.2836 0.3459 -0.0115 -0.0700 0.0328  44  LYS   B NZ  
4548 N N   . HIS   B 45  ? 0.1668 0.1679 0.1499 0.0084  -0.0116 0.0126  45  HIS   B N   
4549 C CA  . HIS   B 45  ? 0.1704 0.1658 0.1569 0.0091  -0.0037 -0.0008 45  HIS   B CA  
4550 C C   . HIS   B 45  ? 0.1934 0.1811 0.1917 0.0171  -0.0189 -0.0047 45  HIS   B C   
4551 O O   . HIS   B 45  ? 0.2042 0.2138 0.2397 0.0415  0.0034  0.0011  45  HIS   B O   
4552 C CB  . HIS   B 45  ? 0.1656 0.1656 0.1583 0.0032  -0.0087 -0.0061 45  HIS   B CB  
4553 C CG  . HIS   B 45  ? 0.1614 0.1591 0.1584 -0.0092 -0.0110 0.0017  45  HIS   B CG  
4554 N ND1 . HIS   B 45  ? 0.1639 0.1569 0.1639 0.0023  -0.0182 -0.0050 45  HIS   B ND1 
4555 C CD2 . HIS   B 45  ? 0.1702 0.1675 0.1744 -0.0157 -0.0191 0.0053  45  HIS   B CD2 
4556 C CE1 . HIS   B 45  ? 0.1713 0.1507 0.1555 -0.0017 -0.0227 -0.0010 45  HIS   B CE1 
4557 N NE2 . HIS   B 45  ? 0.1756 0.1605 0.1614 -0.0049 -0.0198 0.0014  45  HIS   B NE2 
4565 N N   A GLY   B 46  ? 0.2035 0.1725 0.2253 0.0162  -0.0409 0.0029  46  GLY   B N   
4566 N N   B GLY   B 46  ? 0.2032 0.1829 0.2150 0.0160  -0.0337 0.0058  46  GLY   B N   
4567 C CA  A GLY   B 46  ? 0.2165 0.1828 0.2638 0.0152  -0.0499 0.0057  46  GLY   B CA  
4568 C CA  B GLY   B 46  ? 0.2143 0.1950 0.2411 0.0139  -0.0406 0.0138  46  GLY   B CA  
4569 C C   A GLY   B 46  ? 0.2173 0.1981 0.3130 0.0239  -0.0426 0.0075  46  GLY   B C   
4570 C C   B GLY   B 46  ? 0.2179 0.2090 0.2786 0.0176  -0.0348 0.0210  46  GLY   B C   
4571 O O   A GLY   B 46  ? 0.2255 0.2090 0.3957 0.0324  -0.0288 -0.0122 46  GLY   B O   
4572 O O   B GLY   B 46  ? 0.2249 0.2254 0.3092 0.0203  -0.0289 0.0304  46  GLY   B O   
4579 N N   . GLY   B 47  ? 0.2172 0.2126 0.2835 0.0090  -0.0244 0.0116  47  GLY   B N   
4580 C CA  . GLY   B 47  ? 0.1991 0.1872 0.2414 0.0044  -0.0197 0.0058  47  GLY   B CA  
4581 C C   . GLY   B 47  ? 0.1755 0.1650 0.2060 0.0032  -0.0044 0.0134  47  GLY   B C   
4582 O O   . GLY   B 47  ? 0.1846 0.1495 0.2092 0.0025  -0.0105 0.0172  47  GLY   B O   
4587 N N   . GLY   B 48  ? 0.1578 0.1594 0.2073 0.0006  -0.0095 0.0296  48  GLY   B N   
4588 C CA  . GLY   B 48  ? 0.1538 0.1527 0.2054 0.0009  -0.0016 0.0127  48  GLY   B CA  
4589 C C   . GLY   B 48  ? 0.1503 0.1487 0.1921 -0.0006 0.0044  0.0045  48  GLY   B C   
4590 O O   . GLY   B 48  ? 0.1470 0.1511 0.2041 0.0009  -0.0076 0.0073  48  GLY   B O   
4594 N N   . VAL   B 49  ? 0.1535 0.1492 0.1760 0.0099  0.0033  0.0077  49  VAL   B N   
4595 C CA  . VAL   B 49  ? 0.1560 0.1579 0.1591 0.0121  -0.0143 -0.0006 49  VAL   B CA  
4596 C C   . VAL   B 49  ? 0.1483 0.1527 0.1520 0.0112  -0.0076 0.0138  49  VAL   B C   
4597 O O   . VAL   B 49  ? 0.1562 0.1567 0.1635 0.0066  -0.0030 0.0131  49  VAL   B O   
4598 C CB  . VAL   B 49  ? 0.1609 0.1723 0.1988 0.0006  -0.0263 0.0040  49  VAL   B CB  
4599 C CG1 . VAL   B 49  ? 0.1572 0.1875 0.1882 0.0082  -0.0280 0.0042  49  VAL   B CG1 
4600 C CG2 . VAL   B 49  ? 0.1787 0.1840 0.2340 -0.0023 -0.0391 0.0044  49  VAL   B CG2 
4610 N N   . ALA   B 50  ? 0.1435 0.1486 0.1620 0.0041  -0.0030 0.0110  50  ALA   B N   
4611 C CA  . ALA   B 50  ? 0.1412 0.1475 0.1569 0.0102  -0.0080 0.0108  50  ALA   B CA  
4612 C C   . ALA   B 50  ? 0.1508 0.1454 0.1561 0.0071  -0.0044 0.0110  50  ALA   B C   
4613 O O   . ALA   B 50  ? 0.1535 0.1448 0.1583 0.0063  -0.0009 0.0038  50  ALA   B O   
4614 C CB  . ALA   B 50  ? 0.1498 0.1467 0.1660 -0.0000 -0.0062 0.0175  50  ALA   B CB  
4620 N N   . GLY   B 51  ? 0.1480 0.1563 0.1633 0.0147  -0.0142 0.0088  51  GLY   B N   
4621 C CA  . GLY   B 51  ? 0.1513 0.1584 0.1829 0.0173  -0.0183 0.0103  51  GLY   B CA  
4622 C C   . GLY   B 51  ? 0.1518 0.1557 0.1897 0.0197  -0.0071 0.0141  51  GLY   B C   
4623 O O   . GLY   B 51  ? 0.1541 0.1666 0.2089 0.0117  -0.0152 0.0111  51  GLY   B O   
4627 N N   . ALA   B 52  ? 0.1512 0.1476 0.1871 0.0130  -0.0027 0.0156  52  ALA   B N   
4628 C CA  . ALA   B 52  ? 0.1554 0.1585 0.1926 0.0182  0.0094  0.0023  52  ALA   B CA  
4629 C C   . ALA   B 52  ? 0.1443 0.1571 0.1718 0.0100  0.0034  0.0032  52  ALA   B C   
4630 O O   . ALA   B 52  ? 0.1524 0.1609 0.1902 0.0112  0.0050  0.0084  52  ALA   B O   
4631 C CB  . ALA   B 52  ? 0.1753 0.1661 0.2026 0.0049  0.0114  0.0029  52  ALA   B CB  
4637 N N   . LEU   B 53  ? 0.1387 0.1500 0.1682 0.0113  -0.0015 0.0076  53  LEU   B N   
4638 C CA  . LEU   B 53  ? 0.1410 0.1603 0.1611 0.0129  -0.0099 0.0079  53  LEU   B CA  
4639 C C   . LEU   B 53  ? 0.1455 0.1511 0.1651 0.0110  0.0056  0.0094  53  LEU   B C   
4640 O O   . LEU   B 53  ? 0.1483 0.1603 0.1798 0.0008  -0.0039 0.0180  53  LEU   B O   
4641 C CB  . LEU   B 53  ? 0.1437 0.1712 0.1749 0.0108  0.0043  0.0129  53  LEU   B CB  
4642 C CG  . LEU   B 53  ? 0.1433 0.1801 0.1707 -0.0010 -0.0032 0.0190  53  LEU   B CG  
4643 C CD1 . LEU   B 53  ? 0.1416 0.2042 0.2039 0.0052  -0.0034 0.0020  53  LEU   B CD1 
4644 C CD2 . LEU   B 53  ? 0.1647 0.2088 0.1955 -0.0093 -0.0133 -0.0086 53  LEU   B CD2 
4656 N N   . ASN   B 54  ? 0.1456 0.1414 0.1702 0.0048  -0.0027 0.0153  54  ASN   B N   
4657 C CA  . ASN   B 54  ? 0.1521 0.1601 0.1787 0.0007  -0.0047 0.0045  54  ASN   B CA  
4658 C C   . ASN   B 54  ? 0.1461 0.1575 0.1893 -0.0006 -0.0050 0.0034  54  ASN   B C   
4659 O O   . ASN   B 54  ? 0.1481 0.1623 0.2005 -0.0016 0.0016  0.0056  54  ASN   B O   
4660 C CB  . ASN   B 54  ? 0.1543 0.1740 0.1843 0.0058  -0.0002 0.0111  54  ASN   B CB  
4661 C CG  . ASN   B 54  ? 0.1507 0.1790 0.1806 0.0014  -0.0059 0.0068  54  ASN   B CG  
4662 O OD1 . ASN   B 54  ? 0.1490 0.1792 0.2020 0.0038  -0.0142 -0.0047 54  ASN   B OD1 
4663 N ND2 . ASN   B 54  ? 0.1676 0.2003 0.2077 -0.0057 -0.0342 0.0169  54  ASN   B ND2 
4670 N N   . LYS   B 55  ? 0.1437 0.1670 0.2023 0.0118  0.0031  0.0075  55  LYS   B N   
4671 C CA  . LYS   B 55  ? 0.1545 0.1804 0.2212 0.0176  0.0004  0.0106  55  LYS   B CA  
4672 C C   . LYS   B 55  ? 0.1466 0.1759 0.2188 0.0121  0.0022  0.0024  55  LYS   B C   
4673 O O   . LYS   B 55  ? 0.1376 0.1953 0.2343 0.0121  0.0010  -0.0019 55  LYS   B O   
4674 C CB  . LYS   B 55  ? 0.1616 0.1906 0.2665 0.0281  0.0144  0.0180  55  LYS   B CB  
4675 C CG  . LYS   B 55  ? 0.2104 0.2195 0.3417 0.0300  0.0242  0.0321  55  LYS   B CG  
4676 C CD  . LYS   B 55  ? 0.2444 0.2452 0.4085 0.0441  0.0384  0.0463  55  LYS   B CD  
4677 C CE  . LYS   B 55  ? 0.2755 0.2716 0.4796 0.0427  0.0490  0.0455  55  LYS   B CE  
4678 N NZ  . LYS   B 55  ? 0.2845 0.2879 0.5183 0.0426  0.0373  0.0550  55  LYS   B NZ  
4692 N N   . ALA   B 56  ? 0.1409 0.1814 0.1974 0.0091  0.0034  0.0011  56  ALA   B N   
4693 C CA  . ALA   B 56  ? 0.1548 0.1971 0.1956 0.0030  0.0061  0.0037  56  ALA   B CA  
4694 C C   . ALA   B 56  ? 0.1578 0.1902 0.1941 0.0023  0.0147  0.0080  56  ALA   B C   
4695 O O   . ALA   B 56  ? 0.1751 0.2032 0.2175 0.0070  0.0295  0.0132  56  ALA   B O   
4696 C CB  . ALA   B 56  ? 0.1693 0.2136 0.2002 -0.0099 0.0033  0.0002  56  ALA   B CB  
4702 N N   . THR   B 57  ? 0.1491 0.1843 0.1991 0.0033  0.0133  0.0104  57  THR   B N   
4703 C CA  . THR   B 57  ? 0.1551 0.1852 0.2014 -0.0010 0.0162  0.0194  57  THR   B CA  
4704 C C   . THR   B 57  ? 0.1604 0.1928 0.2194 -0.0037 0.0148  0.0201  57  THR   B C   
4705 O O   . THR   B 57  ? 0.1695 0.1946 0.2287 -0.0190 0.0054  0.0200  57  THR   B O   
4706 C CB  . THR   B 57  ? 0.1634 0.1766 0.1776 0.0016  0.0161  0.0234  57  THR   B CB  
4707 O OG1 . THR   B 57  ? 0.1656 0.1657 0.1973 -0.0022 0.0188  0.0113  57  THR   B OG1 
4708 C CG2 . THR   B 57  ? 0.1604 0.1805 0.1825 0.0004  0.0143  0.0078  57  THR   B CG2 
4716 N N   . ASN   B 58  ? 0.1485 0.2159 0.2411 -0.0176 0.0040  0.0079  58  ASN   B N   
4717 C CA  . ASN   B 58  ? 0.1717 0.2644 0.2865 -0.0323 0.0315  0.0150  58  ASN   B CA  
4718 C C   . ASN   B 58  ? 0.1451 0.2380 0.2444 -0.0219 -0.0050 0.0082  58  ASN   B C   
4719 O O   . ASN   B 58  ? 0.1563 0.2494 0.2509 -0.0290 0.0009  0.0024  58  ASN   B O   
4720 C CB  . ASN   B 58  ? 0.2813 0.3559 0.4206 -0.0505 0.0639  0.0276  58  ASN   B CB  
4721 C CG  . ASN   B 58  ? 0.3936 0.4306 0.5715 -0.0547 0.0824  0.0438  58  ASN   B CG  
4722 O OD1 . ASN   B 58  ? 0.4400 0.4524 0.6249 -0.0564 0.0877  0.0486  58  ASN   B OD1 
4723 N ND2 . ASN   B 58  ? 0.4915 0.4915 0.6233 -0.0561 0.0890  0.0476  58  ASN   B ND2 
4730 N N   . ASN   B 59  ? 0.1498 0.2160 0.2142 -0.0136 -0.0089 0.0165  59  ASN   B N   
4731 C CA  . ASN   B 59  ? 0.1519 0.2181 0.2115 -0.0179 -0.0148 0.0224  59  ASN   B CA  
4732 C C   . ASN   B 59  ? 0.1473 0.2059 0.2031 -0.0183 -0.0139 0.0150  59  ASN   B C   
4733 O O   . ASN   B 59  ? 0.1512 0.2047 0.2114 -0.0121 -0.0101 0.0101  59  ASN   B O   
4734 C CB  . ASN   B 59  ? 0.1643 0.2380 0.2285 -0.0168 -0.0326 0.0245  59  ASN   B CB  
4735 C CG  . ASN   B 59  ? 0.1761 0.2556 0.2455 -0.0037 -0.0441 0.0199  59  ASN   B CG  
4736 O OD1 . ASN   B 59  ? 0.1832 0.2584 0.2381 -0.0021 -0.0218 0.0289  59  ASN   B OD1 
4737 N ND2 . ASN   B 59  ? 0.1835 0.2595 0.2638 -0.0098 -0.0409 0.0180  59  ASN   B ND2 
4744 N N   . ALA   B 60  ? 0.1558 0.1921 0.2035 -0.0129 -0.0110 0.0076  60  ALA   B N   
4745 C CA  . ALA   B 60  ? 0.1582 0.1808 0.2062 -0.0244 -0.0071 0.0147  60  ALA   B CA  
4746 C C   . ALA   B 60  ? 0.1556 0.1733 0.1884 -0.0147 -0.0108 0.0124  60  ALA   B C   
4747 O O   . ALA   B 60  ? 0.1619 0.1763 0.1965 -0.0169 -0.0054 0.0046  60  ALA   B O   
4748 C CB  . ALA   B 60  ? 0.1713 0.1859 0.2295 -0.0171 -0.0042 0.0220  60  ALA   B CB  
4754 N N   . MET   B 61  ? 0.1473 0.1646 0.1841 -0.0080 -0.0040 0.0074  61  MET   B N   
4755 C CA  . MET   B 61  ? 0.1462 0.1583 0.1806 -0.0107 -0.0126 0.0013  61  MET   B CA  
4756 C C   . MET   B 61  ? 0.1600 0.1557 0.1833 -0.0115 -0.0114 0.0088  61  MET   B C   
4757 O O   . MET   B 61  ? 0.1619 0.1518 0.1714 -0.0063 -0.0108 -0.0007 61  MET   B O   
4758 C CB  . MET   B 61  ? 0.1428 0.1636 0.1760 -0.0025 -0.0119 0.0083  61  MET   B CB  
4759 C CG  . MET   B 61  ? 0.1463 0.1586 0.1692 -0.0041 -0.0109 0.0017  61  MET   B CG  
4760 S SD  . MET   B 61  ? 0.1465 0.1580 0.1945 -0.0022 -0.0080 -0.0048 61  MET   B SD  
4761 C CE  . MET   B 61  ? 0.1580 0.1782 0.2051 0.0027  0.0056  -0.0222 61  MET   B CE  
4771 N N   . GLN   B 62  ? 0.1522 0.1581 0.1700 -0.0064 -0.0152 0.0093  62  GLN   B N   
4772 C CA  . GLN   B 62  ? 0.1548 0.1674 0.1801 -0.0000 -0.0233 -0.0011 62  GLN   B CA  
4773 C C   . GLN   B 62  ? 0.1620 0.1698 0.1827 -0.0035 -0.0300 0.0029  62  GLN   B C   
4774 O O   . GLN   B 62  ? 0.1741 0.1656 0.1896 -0.0057 -0.0370 -0.0103 62  GLN   B O   
4775 C CB  . GLN   B 62  ? 0.1625 0.1701 0.1751 0.0016  -0.0215 0.0052  62  GLN   B CB  
4776 C CG  . GLN   B 62  ? 0.1654 0.1790 0.1763 -0.0000 -0.0313 -0.0048 62  GLN   B CG  
4777 C CD  . GLN   B 62  ? 0.1655 0.1705 0.1675 0.0010  -0.0268 0.0095  62  GLN   B CD  
4778 O OE1 . GLN   B 62  ? 0.1622 0.1683 0.1870 -0.0003 -0.0251 -0.0032 62  GLN   B OE1 
4779 N NE2 . GLN   B 62  ? 0.1722 0.1733 0.1827 -0.0037 -0.0242 -0.0038 62  GLN   B NE2 
4788 N N   . VAL   B 63  ? 0.1581 0.1786 0.2010 -0.0107 -0.0299 -0.0117 63  VAL   B N   
4789 C CA  . VAL   B 63  ? 0.1750 0.1772 0.2202 -0.0164 -0.0357 -0.0042 63  VAL   B CA  
4790 C C   . VAL   B 63  ? 0.1733 0.1625 0.1962 -0.0218 -0.0356 -0.0071 63  VAL   B C   
4791 O O   . VAL   B 63  ? 0.1824 0.1697 0.2154 -0.0181 -0.0497 -0.0067 63  VAL   B O   
4792 C CB  . VAL   B 63  ? 0.1785 0.1923 0.2546 -0.0210 -0.0388 -0.0001 63  VAL   B CB  
4793 C CG1 . VAL   B 63  ? 0.1896 0.1958 0.2683 -0.0329 -0.0326 -0.0043 63  VAL   B CG1 
4794 C CG2 . VAL   B 63  ? 0.1725 0.2061 0.2668 -0.0209 -0.0344 0.0012  63  VAL   B CG2 
4804 N N   . GLU   B 64  ? 0.1670 0.1600 0.2007 -0.0137 -0.0329 -0.0039 64  GLU   B N   
4805 C CA  . GLU   B 64  ? 0.1681 0.1505 0.1871 -0.0132 -0.0400 -0.0069 64  GLU   B CA  
4806 C C   . GLU   B 64  ? 0.1645 0.1506 0.1771 -0.0067 -0.0300 -0.0170 64  GLU   B C   
4807 O O   . GLU   B 64  ? 0.1774 0.1579 0.1810 -0.0127 -0.0318 -0.0084 64  GLU   B O   
4808 C CB  . GLU   B 64  ? 0.1663 0.1620 0.1913 -0.0183 -0.0318 0.0000  64  GLU   B CB  
4809 C CG  . GLU   B 64  ? 0.1755 0.1604 0.1863 -0.0277 -0.0371 -0.0047 64  GLU   B CG  
4810 C CD  . GLU   B 64  ? 0.1770 0.1751 0.2015 -0.0283 -0.0326 -0.0038 64  GLU   B CD  
4811 O OE1 . GLU   B 64  ? 0.1862 0.1951 0.2045 -0.0339 -0.0237 -0.0283 64  GLU   B OE1 
4812 O OE2 . GLU   B 64  ? 0.1920 0.1805 0.2053 -0.0288 -0.0465 -0.0051 64  GLU   B OE2 
4819 N N   . SER   B 65  ? 0.1658 0.1455 0.1741 -0.0085 -0.0186 -0.0130 65  SER   B N   
4820 C CA  . SER   B 65  ? 0.1665 0.1518 0.1813 -0.0031 -0.0157 -0.0093 65  SER   B CA  
4821 C C   . SER   B 65  ? 0.1660 0.1561 0.1737 0.0006  -0.0290 -0.0137 65  SER   B C   
4822 O O   . SER   B 65  ? 0.1675 0.1597 0.1826 -0.0017 -0.0280 -0.0203 65  SER   B O   
4823 C CB  . SER   B 65  ? 0.1660 0.1588 0.1647 -0.0093 -0.0168 -0.0149 65  SER   B CB  
4824 O OG  . SER   B 65  ? 0.1691 0.1513 0.1881 -0.0120 -0.0160 -0.0140 65  SER   B OG  
4830 N N   . ASP   B 66  ? 0.1701 0.1587 0.1768 -0.0003 -0.0286 -0.0130 66  ASP   B N   
4831 C CA  . ASP   B 66  ? 0.1799 0.1663 0.1699 0.0023  -0.0341 -0.0161 66  ASP   B CA  
4832 C C   . ASP   B 66  ? 0.1847 0.1770 0.1730 -0.0030 -0.0328 -0.0166 66  ASP   B C   
4833 O O   . ASP   B 66  ? 0.1867 0.1813 0.1810 0.0077  -0.0383 -0.0176 66  ASP   B O   
4834 C CB  . ASP   B 66  ? 0.1958 0.1821 0.2014 0.0115  -0.0443 -0.0119 66  ASP   B CB  
4835 C CG  . ASP   B 66  ? 0.2288 0.1997 0.2217 0.0169  -0.0595 -0.0003 66  ASP   B CG  
4836 O OD1 . ASP   B 66  ? 0.2570 0.1929 0.2315 0.0081  -0.0629 0.0029  66  ASP   B OD1 
4837 O OD2 . ASP   B 66  ? 0.2426 0.2261 0.2872 0.0348  -0.0583 -0.0025 66  ASP   B OD2 
4842 N N   . ASP   B 67  ? 0.1798 0.1650 0.1814 -0.0082 -0.0344 -0.0189 67  ASP   B N   
4843 C CA  . ASP   B 67  ? 0.1943 0.1670 0.1886 -0.0100 -0.0286 -0.0101 67  ASP   B CA  
4844 C C   . ASP   B 67  ? 0.1889 0.1640 0.1948 -0.0014 -0.0318 -0.0159 67  ASP   B C   
4845 O O   . ASP   B 67  ? 0.1931 0.1677 0.2024 -0.0051 -0.0269 -0.0250 67  ASP   B O   
4846 C CB  . ASP   B 67  ? 0.2163 0.1733 0.1998 -0.0121 -0.0363 -0.0008 67  ASP   B CB  
4847 C CG  . ASP   B 67  ? 0.2509 0.1880 0.2073 -0.0137 -0.0696 -0.0126 67  ASP   B CG  
4848 O OD1 . ASP   B 67  ? 0.2694 0.1953 0.2279 -0.0171 -0.0709 -0.0028 67  ASP   B OD1 
4849 O OD2 . ASP   B 67  ? 0.2683 0.1938 0.2261 -0.0002 -0.0773 -0.0123 67  ASP   B OD2 
4854 N N   . TYR   B 68  ? 0.1826 0.1618 0.1800 -0.0051 -0.0381 -0.0222 68  TYR   B N   
4855 C CA  . TYR   B 68  ? 0.1773 0.1794 0.1926 0.0047  -0.0429 -0.0303 68  TYR   B CA  
4856 C C   . TYR   B 68  ? 0.1731 0.1774 0.1859 -0.0012 -0.0357 -0.0434 68  TYR   B C   
4857 O O   . TYR   B 68  ? 0.1810 0.1856 0.2096 0.0065  -0.0357 -0.0567 68  TYR   B O   
4858 C CB  . TYR   B 68  ? 0.1830 0.2008 0.1969 0.0113  -0.0453 -0.0409 68  TYR   B CB  
4859 C CG  . TYR   B 68  ? 0.1954 0.2142 0.2058 0.0159  -0.0373 -0.0570 68  TYR   B CG  
4860 C CD1 . TYR   B 68  ? 0.1984 0.2183 0.2312 -0.0100 -0.0287 -0.0684 68  TYR   B CD1 
4861 C CD2 . TYR   B 68  ? 0.2018 0.2305 0.2305 0.0225  -0.0444 -0.0555 68  TYR   B CD2 
4862 C CE1 . TYR   B 68  ? 0.2027 0.2365 0.2608 -0.0004 -0.0251 -0.0615 68  TYR   B CE1 
4863 C CE2 . TYR   B 68  ? 0.2044 0.2378 0.2425 0.0141  -0.0339 -0.0685 68  TYR   B CE2 
4864 C CZ  . TYR   B 68  ? 0.1974 0.2368 0.2565 0.0045  -0.0346 -0.0689 68  TYR   B CZ  
4865 O OH  . TYR   B 68  ? 0.1905 0.2545 0.2795 0.0011  -0.0318 -0.0521 68  TYR   B OH  
4875 N N   . ILE   B 69  ? 0.1775 0.1687 0.1898 -0.0029 -0.0324 -0.0337 69  ILE   B N   
4876 C CA  . ILE   B 69  ? 0.1868 0.1751 0.1996 -0.0062 -0.0193 -0.0354 69  ILE   B CA  
4877 C C   . ILE   B 69  ? 0.1872 0.1727 0.1945 0.0056  -0.0326 -0.0301 69  ILE   B C   
4878 O O   . ILE   B 69  ? 0.1939 0.1852 0.1861 0.0030  -0.0225 -0.0309 69  ILE   B O   
4879 C CB  . ILE   B 69  ? 0.1959 0.1787 0.2252 -0.0093 0.0007  -0.0289 69  ILE   B CB  
4880 C CG1 . ILE   B 69  ? 0.1922 0.1808 0.2348 -0.0070 0.0138  -0.0346 69  ILE   B CG1 
4881 C CG2 . ILE   B 69  ? 0.2117 0.1836 0.2385 -0.0074 0.0019  -0.0210 69  ILE   B CG2 
4882 C CD1 . ILE   B 69  ? 0.1869 0.1865 0.2421 -0.0194 0.0113  -0.0446 69  ILE   B CD1 
4894 N N   . ALA   B 70  ? 0.1879 0.1700 0.2017 0.0063  -0.0399 -0.0291 70  ALA   B N   
4895 C CA  . ALA   B 70  ? 0.1902 0.1708 0.1886 -0.0002 -0.0458 -0.0240 70  ALA   B CA  
4896 C C   . ALA   B 70  ? 0.1963 0.1683 0.1973 -0.0005 -0.0513 -0.0304 70  ALA   B C   
4897 O O   . ALA   B 70  ? 0.2010 0.1693 0.1954 -0.0000 -0.0462 -0.0291 70  ALA   B O   
4898 C CB  . ALA   B 70  ? 0.1964 0.1890 0.1985 -0.0039 -0.0499 -0.0200 70  ALA   B CB  
4904 N N   . THR   B 71  ? 0.2041 0.1707 0.2040 0.0044  -0.0585 -0.0343 71  THR   B N   
4905 C CA  . THR   B 71  ? 0.2154 0.1775 0.2283 0.0074  -0.0704 -0.0310 71  THR   B CA  
4906 C C   . THR   B 71  ? 0.2065 0.1761 0.2468 0.0251  -0.0662 -0.0491 71  THR   B C   
4907 O O   . THR   B 71  ? 0.2187 0.1847 0.2830 0.0233  -0.0603 -0.0685 71  THR   B O   
4908 C CB  . THR   B 71  ? 0.2411 0.2003 0.2424 -0.0023 -0.0740 -0.0169 71  THR   B CB  
4909 O OG1 . THR   B 71  ? 0.2561 0.2220 0.2755 -0.0219 -0.0706 0.0076  71  THR   B OG1 
4910 C CG2 . THR   B 71  ? 0.2559 0.1980 0.2701 0.0002  -0.0644 -0.0044 71  THR   B CG2 
4918 N N   . ASN   B 72  ? 0.1922 0.1782 0.2385 0.0124  -0.0588 -0.0642 72  ASN   B N   
4919 C CA  . ASN   B 72  ? 0.1969 0.1978 0.2295 0.0102  -0.0480 -0.0676 72  ASN   B CA  
4920 C C   . ASN   B 72  ? 0.1975 0.2097 0.2376 -0.0007 -0.0264 -0.0675 72  ASN   B C   
4921 O O   . ASN   B 72  ? 0.1951 0.2302 0.2636 0.0118  -0.0126 -0.0683 72  ASN   B O   
4922 C CB  . ASN   B 72  ? 0.2015 0.2134 0.2371 0.0107  -0.0601 -0.0555 72  ASN   B CB  
4923 C CG  . ASN   B 72  ? 0.2178 0.2290 0.2446 0.0337  -0.0600 -0.0322 72  ASN   B CG  
4924 O OD1 . ASN   B 72  ? 0.2395 0.2492 0.2530 0.0215  -0.0448 -0.0427 72  ASN   B OD1 
4925 N ND2 . ASN   B 72  ? 0.2324 0.2344 0.2777 0.0465  -0.0497 0.0000  72  ASN   B ND2 
4932 N N   . GLY   B 73  ? 0.2001 0.2060 0.2178 -0.0040 -0.0300 -0.0594 73  GLY   B N   
4933 C CA  . GLY   B 73  ? 0.1964 0.2094 0.1984 -0.0057 -0.0232 -0.0510 73  GLY   B CA  
4934 C C   . GLY   B 73  ? 0.1887 0.2106 0.1474 0.0019  -0.0208 -0.0442 73  GLY   B C   
4935 O O   . GLY   B 73  ? 0.1801 0.1973 0.1658 0.0031  -0.0180 -0.0332 73  GLY   B O   
4939 N N   . PRO   B 74  ? 0.1889 0.2229 0.1505 0.0031  -0.0288 -0.0340 74  PRO   B N   
4940 C CA  . PRO   B 74  ? 0.1816 0.2240 0.1548 0.0089  -0.0261 -0.0218 74  PRO   B CA  
4941 C C   . PRO   B 74  ? 0.1666 0.2100 0.1505 0.0047  -0.0149 -0.0219 74  PRO   B C   
4942 O O   . PRO   B 74  ? 0.1718 0.2104 0.1950 0.0066  -0.0132 -0.0369 74  PRO   B O   
4943 C CB  . PRO   B 74  ? 0.1962 0.2441 0.1604 0.0041  -0.0265 -0.0197 74  PRO   B CB  
4944 C CG  . PRO   B 74  ? 0.2148 0.2531 0.1880 0.0017  -0.0198 -0.0158 74  PRO   B CG  
4945 C CD  . PRO   B 74  ? 0.2125 0.2426 0.1767 0.0040  -0.0155 -0.0273 74  PRO   B CD  
4953 N N   . LEU   B 75  ? 0.1639 0.2014 0.1360 0.0055  -0.0187 -0.0236 75  LEU   B N   
4954 C CA  . LEU   B 75  ? 0.1689 0.2003 0.1406 0.0024  -0.0120 -0.0058 75  LEU   B CA  
4955 C C   . LEU   B 75  ? 0.1726 0.2047 0.1335 0.0029  -0.0056 -0.0084 75  LEU   B C   
4956 O O   . LEU   B 75  ? 0.1956 0.2121 0.1486 -0.0032 -0.0071 -0.0023 75  LEU   B O   
4957 C CB  . LEU   B 75  ? 0.1762 0.2011 0.1366 -0.0114 -0.0233 0.0087  75  LEU   B CB  
4958 C CG  . LEU   B 75  ? 0.2066 0.2152 0.1563 -0.0345 -0.0113 0.0017  75  LEU   B CG  
4959 C CD1 . LEU   B 75  ? 0.2397 0.2337 0.1669 -0.0481 0.0074  -0.0011 75  LEU   B CD1 
4960 C CD2 . LEU   B 75  ? 0.2424 0.2334 0.2247 -0.0257 -0.0066 0.0084  75  LEU   B CD2 
4972 N N   . LYS   B 76  ? 0.1684 0.2265 0.1665 0.0041  0.0000  -0.0023 76  LYS   B N   
4973 C CA  . LYS   B 76  ? 0.1805 0.2350 0.2042 -0.0055 0.0212  -0.0007 76  LYS   B CA  
4974 C C   . LYS   B 76  ? 0.1721 0.2163 0.1649 0.0047  0.0023  0.0177  76  LYS   B C   
4975 O O   . LYS   B 76  ? 0.1712 0.1986 0.1642 0.0031  0.0039  0.0237  76  LYS   B O   
4976 C CB  . LYS   B 76  ? 0.1999 0.2477 0.2769 -0.0120 0.0438  -0.0364 76  LYS   B CB  
4977 C CG  . LYS   B 76  ? 0.2126 0.2687 0.3291 0.0015  0.0349  -0.0461 76  LYS   B CG  
4978 C CD  . LYS   B 76  ? 0.2128 0.2807 0.3830 0.0108  0.0179  -0.0596 76  LYS   B CD  
4979 C CE  . LYS   B 76  ? 0.2207 0.2980 0.4390 0.0153  0.0011  -0.0689 76  LYS   B CE  
4980 N NZ  . LYS   B 76  ? 0.2230 0.3032 0.4623 0.0141  -0.0244 -0.0873 76  LYS   B NZ  
4994 N N   . VAL   B 77  ? 0.1846 0.2298 0.1638 0.0123  0.0094  0.0125  77  VAL   B N   
4995 C CA  . VAL   B 77  ? 0.1889 0.2171 0.1738 0.0178  0.0166  0.0464  77  VAL   B CA  
4996 C C   . VAL   B 77  ? 0.1728 0.1953 0.1677 0.0162  0.0236  0.0405  77  VAL   B C   
4997 O O   . VAL   B 77  ? 0.1789 0.1928 0.1736 0.0262  0.0372  0.0274  77  VAL   B O   
4998 C CB  . VAL   B 77  ? 0.1987 0.2261 0.2122 0.0204  0.0277  0.0596  77  VAL   B CB  
4999 C CG1 . VAL   B 77  ? 0.2026 0.2094 0.2419 0.0178  0.0290  0.0776  77  VAL   B CG1 
5000 C CG2 . VAL   B 77  ? 0.2132 0.2514 0.2354 0.0138  0.0164  0.0701  77  VAL   B CG2 
5010 N N   . GLY   B 78  ? 0.1653 0.1815 0.1740 0.0147  0.0174  0.0294  78  GLY   B N   
5011 C CA  . GLY   B 78  ? 0.1656 0.1734 0.1615 0.0168  0.0189  0.0170  78  GLY   B CA  
5012 C C   . GLY   B 78  ? 0.1549 0.1654 0.1647 0.0131  0.0170  0.0176  78  GLY   B C   
5013 O O   . GLY   B 78  ? 0.1584 0.1645 0.1766 0.0198  0.0162  0.0237  78  GLY   B O   
5017 N N   . GLY   B 79  ? 0.1514 0.1689 0.1656 0.0088  0.0192  0.0108  79  GLY   B N   
5018 C CA  . GLY   B 79  ? 0.1529 0.1660 0.1516 0.0107  0.0066  0.0071  79  GLY   B CA  
5019 C C   . GLY   B 79  ? 0.1480 0.1559 0.1635 0.0102  0.0091  0.0068  79  GLY   B C   
5020 O O   . GLY   B 79  ? 0.1555 0.1528 0.1741 0.0119  0.0163  0.0214  79  GLY   B O   
5024 N N   . SER   B 80  ? 0.1503 0.1444 0.1711 0.0076  0.0142  0.0021  80  SER   B N   
5025 C CA  . SER   B 80  ? 0.1424 0.1472 0.1636 0.0050  0.0022  0.0038  80  SER   B CA  
5026 C C   . SER   B 80  ? 0.1427 0.1407 0.1671 0.0118  -0.0058 0.0020  80  SER   B C   
5027 O O   . SER   B 80  ? 0.1579 0.1471 0.1955 0.0140  0.0037  -0.0044 80  SER   B O   
5028 C CB  . SER   B 80  ? 0.1502 0.1501 0.1786 -0.0042 0.0018  0.0059  80  SER   B CB  
5029 O OG  . SER   B 80  ? 0.1522 0.1626 0.1989 -0.0042 -0.0156 0.0103  80  SER   B OG  
5035 N N   . CYS   B 81  ? 0.1382 0.1327 0.1693 0.0008  -0.0009 -0.0031 81  CYS   B N   
5036 C CA  . CYS   B 81  ? 0.1502 0.1274 0.1695 0.0021  -0.0113 0.0019  81  CYS   B CA  
5037 C C   . CYS   B 81  ? 0.1473 0.1250 0.1464 0.0002  -0.0170 -0.0029 81  CYS   B C   
5038 O O   . CYS   B 81  ? 0.1715 0.1330 0.1636 0.0073  -0.0029 -0.0059 81  CYS   B O   
5039 C CB  . CYS   B 81  ? 0.1646 0.1446 0.1754 -0.0016 -0.0216 -0.0033 81  CYS   B CB  
5040 S SG  . CYS   B 81  ? 0.1672 0.1623 0.1755 -0.0039 -0.0298 -0.0129 81  CYS   B SG  
5046 N N   . VAL   B 82  ? 0.1516 0.1288 0.1557 -0.0007 -0.0138 -0.0061 82  VAL   B N   
5047 C CA  . VAL   B 82  ? 0.1571 0.1295 0.1523 -0.0081 -0.0128 0.0054  82  VAL   B CA  
5048 C C   . VAL   B 82  ? 0.1634 0.1244 0.1711 -0.0049 -0.0110 -0.0028 82  VAL   B C   
5049 O O   . VAL   B 82  ? 0.1713 0.1256 0.2015 -0.0045 -0.0106 -0.0116 82  VAL   B O   
5050 C CB  . VAL   B 82  ? 0.1681 0.1527 0.1769 -0.0032 -0.0111 0.0057  82  VAL   B CB  
5051 C CG1 . VAL   B 82  ? 0.1803 0.1742 0.1880 -0.0007 -0.0228 0.0235  82  VAL   B CG1 
5052 C CG2 . VAL   B 82  ? 0.1767 0.1671 0.1907 -0.0051 -0.0266 0.0056  82  VAL   B CG2 
5062 N N   . LEU   B 83  ? 0.1480 0.1237 0.1678 -0.0121 -0.0203 -0.0022 83  LEU   B N   
5063 C CA  . LEU   B 83  ? 0.1520 0.1307 0.1568 -0.0136 -0.0185 0.0006  83  LEU   B CA  
5064 C C   . LEU   B 83  ? 0.1548 0.1287 0.1657 -0.0181 -0.0209 0.0045  83  LEU   B C   
5065 O O   . LEU   B 83  ? 0.1534 0.1435 0.1540 -0.0193 -0.0165 0.0062  83  LEU   B O   
5066 C CB  . LEU   B 83  ? 0.1610 0.1427 0.1724 -0.0139 -0.0270 -0.0148 83  LEU   B CB  
5067 C CG  . LEU   B 83  ? 0.1821 0.1644 0.1702 -0.0154 -0.0164 -0.0168 83  LEU   B CG  
5068 C CD1 . LEU   B 83  ? 0.1920 0.1750 0.1795 -0.0076 -0.0198 -0.0059 83  LEU   B CD1 
5069 C CD2 . LEU   B 83  ? 0.2007 0.1712 0.1856 -0.0052 -0.0131 -0.0285 83  LEU   B CD2 
5081 N N   . SER   B 84  ? 0.1555 0.1395 0.1863 -0.0248 -0.0196 0.0123  84  SER   B N   
5082 C CA  . SER   B 84  ? 0.1599 0.1607 0.1720 -0.0261 -0.0221 0.0214  84  SER   B CA  
5083 C C   . SER   B 84  ? 0.1523 0.1772 0.1382 -0.0231 -0.0308 0.0267  84  SER   B C   
5084 O O   . SER   B 84  ? 0.1593 0.1596 0.1377 -0.0188 -0.0136 0.0023  84  SER   B O   
5085 C CB  . SER   B 84  ? 0.1739 0.1656 0.2290 -0.0305 0.0065  0.0156  84  SER   B CB  
5086 O OG  . SER   B 84  ? 0.1711 0.1803 0.2704 -0.0356 0.0079  0.0291  84  SER   B OG  
5092 N N   . GLY   B 85  ? 0.1562 0.1979 0.1467 -0.0288 -0.0217 0.0272  85  GLY   B N   
5093 C CA  . GLY   B 85  ? 0.1521 0.2039 0.1576 -0.0400 -0.0036 -0.0017 85  GLY   B CA  
5094 C C   . GLY   B 85  ? 0.1519 0.1893 0.1453 -0.0396 -0.0055 0.0129  85  GLY   B C   
5095 O O   . GLY   B 85  ? 0.1587 0.1884 0.1562 -0.0485 0.0104  -0.0059 85  GLY   B O   
5099 N N   . HIS   B 86  ? 0.1515 0.1779 0.1680 -0.0315 -0.0175 0.0140  86  HIS   B N   
5100 C CA  . HIS   B 86  ? 0.1543 0.1752 0.1820 -0.0280 -0.0160 0.0205  86  HIS   B CA  
5101 C C   . HIS   B 86  ? 0.1505 0.1863 0.1621 -0.0376 -0.0061 0.0375  86  HIS   B C   
5102 O O   . HIS   B 86  ? 0.1699 0.1956 0.1690 -0.0338 0.0053  0.0338  86  HIS   B O   
5103 C CB  . HIS   B 86  ? 0.1590 0.1765 0.1807 -0.0171 -0.0240 0.0069  86  HIS   B CB  
5104 C CG  . HIS   B 86  ? 0.1650 0.1850 0.1718 -0.0135 -0.0286 0.0153  86  HIS   B CG  
5105 N ND1 . HIS   B 86  ? 0.1790 0.2076 0.1946 -0.0281 -0.0271 0.0060  86  HIS   B ND1 
5106 C CD2 . HIS   B 86  ? 0.1676 0.1863 0.1766 -0.0097 -0.0275 0.0114  86  HIS   B CD2 
5107 C CE1 . HIS   B 86  ? 0.1876 0.2043 0.1841 -0.0174 -0.0082 -0.0081 86  HIS   B CE1 
5108 N NE2 . HIS   B 86  ? 0.1776 0.1943 0.1709 -0.0080 -0.0164 0.0015  86  HIS   B NE2 
5116 N N   . ASN   B 87  ? 0.1572 0.1866 0.1747 -0.0328 -0.0008 0.0247  87  ASN   B N   
5117 C CA  . ASN   B 87  ? 0.1658 0.2050 0.1797 -0.0275 0.0203  0.0169  87  ASN   B CA  
5118 C C   . ASN   B 87  ? 0.1813 0.1836 0.1585 -0.0254 0.0315  0.0158  87  ASN   B C   
5119 O O   . ASN   B 87  ? 0.2066 0.1941 0.1978 -0.0208 0.0497  0.0067  87  ASN   B O   
5120 C CB  . ASN   B 87  ? 0.1675 0.2400 0.2169 -0.0229 0.0222  0.0140  87  ASN   B CB  
5121 C CG  . ASN   B 87  ? 0.1750 0.2584 0.2208 0.0065  0.0270  0.0244  87  ASN   B CG  
5122 O OD1 . ASN   B 87  ? 0.1700 0.2444 0.1952 0.0111  0.0348  0.0444  87  ASN   B OD1 
5123 N ND2 . ASN   B 87  ? 0.2073 0.2701 0.2577 0.0090  0.0340  0.0137  87  ASN   B ND2 
5130 N N   . LEU   B 88  ? 0.1692 0.1753 0.1515 -0.0300 0.0118  0.0153  88  LEU   B N   
5131 C CA  . LEU   B 88  ? 0.1806 0.1724 0.1587 -0.0311 0.0022  0.0066  88  LEU   B CA  
5132 C C   . LEU   B 88  ? 0.1789 0.1695 0.1426 -0.0313 0.0014  0.0056  88  LEU   B C   
5133 O O   . LEU   B 88  ? 0.2035 0.1788 0.1824 -0.0172 -0.0283 -0.0050 88  LEU   B O   
5134 C CB  . LEU   B 88  ? 0.1815 0.1800 0.1721 -0.0397 -0.0057 0.0209  88  LEU   B CB  
5135 C CG  . LEU   B 88  ? 0.2243 0.2089 0.1851 -0.0302 -0.0236 0.0340  88  LEU   B CG  
5136 C CD1 . LEU   B 88  ? 0.2365 0.2406 0.2055 -0.0432 -0.0168 0.0411  88  LEU   B CD1 
5137 C CD2 . LEU   B 88  ? 0.2614 0.2341 0.2346 0.0099  -0.0504 0.0080  88  LEU   B CD2 
5149 N N   . ALA   B 89  ? 0.1665 0.1621 0.1504 -0.0329 0.0187  0.0069  89  ALA   B N   
5150 C CA  . ALA   B 89  ? 0.1647 0.1555 0.1357 -0.0320 0.0007  0.0141  89  ALA   B CA  
5151 C C   . ALA   B 89  ? 0.1710 0.1585 0.1354 -0.0356 0.0078  0.0040  89  ALA   B C   
5152 O O   . ALA   B 89  ? 0.1549 0.1724 0.1806 -0.0407 0.0113  -0.0233 89  ALA   B O   
5153 C CB  . ALA   B 89  ? 0.1555 0.1458 0.1544 -0.0400 0.0026  0.0161  89  ALA   B CB  
5159 N N   . LYS   B 90  ? 0.2061 0.1492 0.1488 -0.0405 -0.0118 0.0151  90  LYS   B N   
5160 C CA  . LYS   B 90  ? 0.2193 0.1411 0.1541 -0.0407 -0.0114 0.0132  90  LYS   B CA  
5161 C C   . LYS   B 90  ? 0.2025 0.1363 0.1656 -0.0426 -0.0088 0.0010  90  LYS   B C   
5162 O O   . LYS   B 90  ? 0.2178 0.1559 0.1821 -0.0581 -0.0043 0.0035  90  LYS   B O   
5163 C CB  . LYS   B 90  ? 0.2402 0.1463 0.1886 -0.0334 -0.0029 0.0207  90  LYS   B CB  
5164 C CG  . LYS   B 90  ? 0.2445 0.1696 0.1819 -0.0226 0.0304  0.0207  90  LYS   B CG  
5165 C CD  . LYS   B 90  ? 0.2755 0.1908 0.2278 -0.0100 0.0491  -0.0060 90  LYS   B CD  
5166 C CE  . LYS   B 90  ? 0.2846 0.2052 0.2775 -0.0186 0.0593  -0.0152 90  LYS   B CE  
5167 N NZ  . LYS   B 90  ? 0.2921 0.1950 0.2759 -0.0316 0.0755  -0.0232 90  LYS   B NZ  
5181 N N   . HIS   B 91  ? 0.1715 0.1313 0.1374 -0.0287 -0.0203 0.0108  91  HIS   B N   
5182 C CA  . HIS   B 91  ? 0.1620 0.1352 0.1534 -0.0182 -0.0139 0.0102  91  HIS   B CA  
5183 C C   . HIS   B 91  ? 0.1528 0.1383 0.1324 -0.0244 -0.0056 0.0086  91  HIS   B C   
5184 O O   . HIS   B 91  ? 0.1711 0.1410 0.1400 -0.0234 -0.0227 0.0005  91  HIS   B O   
5185 C CB  . HIS   B 91  ? 0.1825 0.1395 0.1950 -0.0059 -0.0059 0.0131  91  HIS   B CB  
5186 C CG  . HIS   B 91  ? 0.2245 0.1552 0.2711 0.0055  0.0237  0.0176  91  HIS   B CG  
5187 N ND1 . HIS   B 91  ? 0.2561 0.1616 0.3238 0.0026  0.0306  0.0070  91  HIS   B ND1 
5188 C CD2 . HIS   B 91  ? 0.2366 0.1822 0.3185 0.0140  0.0099  0.0479  91  HIS   B CD2 
5189 C CE1 . HIS   B 91  ? 0.2604 0.1711 0.3446 0.0177  0.0285  0.0143  91  HIS   B CE1 
5190 N NE2 . HIS   B 91  ? 0.2490 0.1869 0.3465 0.0276  0.0261  0.0588  91  HIS   B NE2 
5198 N N   . CYS   B 92  ? 0.1488 0.1351 0.1369 -0.0252 -0.0174 0.0064  92  CYS   B N   
5199 C CA  . CYS   B 92  ? 0.1463 0.1331 0.1312 -0.0209 -0.0099 0.0034  92  CYS   B CA  
5200 C C   . CYS   B 92  ? 0.1440 0.1293 0.1312 -0.0127 -0.0088 0.0023  92  CYS   B C   
5201 O O   . CYS   B 92  ? 0.1512 0.1324 0.1509 -0.0178 -0.0030 0.0027  92  CYS   B O   
5202 C CB  . CYS   B 92  ? 0.1457 0.1489 0.1384 -0.0061 -0.0067 -0.0024 92  CYS   B CB  
5203 S SG  . CYS   B 92  ? 0.1451 0.1400 0.1462 -0.0117 -0.0107 0.0077  92  CYS   B SG  
5209 N N   . LEU   B 93  ? 0.1378 0.1294 0.1290 -0.0140 -0.0127 -0.0020 93  LEU   B N   
5210 C CA  . LEU   B 93  ? 0.1355 0.1320 0.1371 -0.0061 -0.0144 0.0081  93  LEU   B CA  
5211 C C   . LEU   B 93  ? 0.1289 0.1290 0.1296 -0.0010 -0.0135 0.0068  93  LEU   B C   
5212 O O   . LEU   B 93  ? 0.1364 0.1258 0.1498 -0.0048 -0.0059 -0.0010 93  LEU   B O   
5213 C CB  . LEU   B 93  ? 0.1381 0.1278 0.1531 -0.0041 -0.0124 0.0061  93  LEU   B CB  
5214 C CG  . LEU   B 93  ? 0.1356 0.1426 0.1737 -0.0055 -0.0071 0.0192  93  LEU   B CG  
5215 C CD1 . LEU   B 93  ? 0.1427 0.1493 0.1683 0.0067  -0.0033 0.0020  93  LEU   B CD1 
5216 C CD2 . LEU   B 93  ? 0.1335 0.1449 0.1858 -0.0015 -0.0114 0.0082  93  LEU   B CD2 
5228 N N   . HIS   B 94  ? 0.1353 0.1210 0.1265 -0.0057 -0.0129 0.0046  94  HIS   B N   
5229 C CA  . HIS   B 94  ? 0.1374 0.1237 0.1342 -0.0043 -0.0101 0.0048  94  HIS   B CA  
5230 C C   . HIS   B 94  ? 0.1353 0.1286 0.1499 -0.0012 -0.0055 0.0123  94  HIS   B C   
5231 O O   . HIS   B 94  ? 0.1390 0.1355 0.1948 -0.0043 0.0101  -0.0080 94  HIS   B O   
5232 C CB  . HIS   B 94  ? 0.1376 0.1350 0.1409 -0.0008 -0.0059 0.0049  94  HIS   B CB  
5233 C CG  . HIS   B 94  ? 0.1423 0.1291 0.1396 -0.0053 -0.0247 0.0040  94  HIS   B CG  
5234 N ND1 . HIS   B 94  ? 0.1424 0.1359 0.1451 -0.0076 -0.0231 0.0023  94  HIS   B ND1 
5235 C CD2 . HIS   B 94  ? 0.1435 0.1316 0.1393 -0.0032 -0.0196 0.0042  94  HIS   B CD2 
5236 C CE1 . HIS   B 94  ? 0.1436 0.1349 0.1441 -0.0091 -0.0202 0.0012  94  HIS   B CE1 
5237 N NE2 . HIS   B 94  ? 0.1377 0.1413 0.1458 -0.0168 -0.0138 0.0020  94  HIS   B NE2 
5245 N N   . VAL   B 95  ? 0.1244 0.1265 0.1610 -0.0028 -0.0002 0.0067  95  VAL   B N   
5246 C CA  . VAL   B 95  ? 0.1315 0.1307 0.1474 -0.0003 0.0010  0.0153  95  VAL   B CA  
5247 C C   . VAL   B 95  ? 0.1391 0.1309 0.1391 -0.0031 0.0100  0.0082  95  VAL   B C   
5248 O O   . VAL   B 95  ? 0.1442 0.1304 0.1714 0.0055  0.0062  0.0170  95  VAL   B O   
5249 C CB  . VAL   B 95  ? 0.1386 0.1265 0.1542 -0.0062 -0.0000 0.0033  95  VAL   B CB  
5250 C CG1 . VAL   B 95  ? 0.1583 0.1395 0.1788 -0.0113 -0.0024 0.0153  95  VAL   B CG1 
5251 C CG2 . VAL   B 95  ? 0.1487 0.1272 0.1550 0.0049  -0.0097 0.0024  95  VAL   B CG2 
5261 N N   . VAL   B 96  ? 0.1468 0.1404 0.1419 0.0140  0.0056  0.0137  96  VAL   B N   
5262 C CA  . VAL   B 96  ? 0.1531 0.1528 0.1366 0.0108  0.0056  0.0167  96  VAL   B CA  
5263 C C   . VAL   B 96  ? 0.1579 0.1558 0.1541 0.0100  0.0075  0.0130  96  VAL   B C   
5264 O O   . VAL   B 96  ? 0.1564 0.1570 0.1692 0.0042  0.0176  0.0057  96  VAL   B O   
5265 C CB  . VAL   B 96  ? 0.1599 0.1686 0.1355 0.0084  0.0069  0.0118  96  VAL   B CB  
5266 C CG1 . VAL   B 96  ? 0.1586 0.1844 0.1611 0.0175  0.0113  0.0101  96  VAL   B CG1 
5267 C CG2 . VAL   B 96  ? 0.1700 0.1751 0.1643 0.0074  0.0123  0.0043  96  VAL   B CG2 
5277 N N   . GLY   B 97  ? 0.1576 0.1533 0.1560 0.0074  0.0079  0.0199  97  GLY   B N   
5278 C CA  . GLY   B 97  ? 0.1648 0.1560 0.1611 0.0014  0.0162  0.0244  97  GLY   B CA  
5279 C C   . GLY   B 97  ? 0.1864 0.1636 0.1671 0.0074  0.0081  0.0207  97  GLY   B C   
5280 O O   . GLY   B 97  ? 0.1979 0.1744 0.1693 0.0073  0.0087  0.0104  97  GLY   B O   
5284 N N   . PRO   B 98  ? 0.2027 0.1688 0.1789 0.0057  0.0294  0.0305  98  PRO   B N   
5285 C CA  . PRO   B 98  ? 0.2119 0.1826 0.1849 0.0194  0.0394  0.0296  98  PRO   B CA  
5286 C C   . PRO   B 98  ? 0.2218 0.1832 0.1636 0.0297  0.0350  0.0436  98  PRO   B C   
5287 O O   . PRO   B 98  ? 0.2139 0.1744 0.1857 0.0214  0.0329  0.0391  98  PRO   B O   
5288 C CB  . PRO   B 98  ? 0.2050 0.1855 0.1986 0.0129  0.0507  0.0281  98  PRO   B CB  
5289 C CG  . PRO   B 98  ? 0.1996 0.1798 0.2011 0.0076  0.0406  0.0389  98  PRO   B CG  
5290 C CD  . PRO   B 98  ? 0.1847 0.1713 0.1985 0.0118  0.0366  0.0319  98  PRO   B CD  
5298 N N   . ASN   B 99  ? 0.2317 0.1982 0.1715 0.0445  0.0339  0.0233  99  ASN   B N   
5299 C CA  . ASN   B 99  ? 0.2492 0.2062 0.1836 0.0485  0.0302  0.0421  99  ASN   B CA  
5300 C C   . ASN   B 99  ? 0.2816 0.2405 0.2104 0.0446  0.0523  0.0683  99  ASN   B C   
5301 O O   . ASN   B 99  ? 0.2957 0.2378 0.2072 0.0427  0.0364  0.0620  99  ASN   B O   
5302 C CB  . ASN   B 99  ? 0.2569 0.2040 0.1927 0.0478  0.0237  0.0403  99  ASN   B CB  
5303 C CG  . ASN   B 99  ? 0.2632 0.2161 0.2191 0.0458  0.0099  0.0413  99  ASN   B CG  
5304 O OD1 . ASN   B 99  ? 0.2688 0.2176 0.2387 0.0540  0.0074  0.0457  99  ASN   B OD1 
5305 N ND2 . ASN   B 99  ? 0.2590 0.2150 0.2272 0.0487  -0.0211 0.0336  99  ASN   B ND2 
5312 N N   A VAL   B 100 ? 0.3010 0.2571 0.2471 0.0354  0.0565  0.0939  100 VAL   B N   
5313 N N   B VAL   B 100 ? 0.3030 0.2572 0.2487 0.0368  0.0498  0.0885  100 VAL   B N   
5314 C CA  A VAL   B 100 ? 0.3304 0.2770 0.3020 0.0259  0.0601  0.1072  100 VAL   B CA  
5315 C CA  B VAL   B 100 ? 0.3309 0.2757 0.2969 0.0283  0.0479  0.0998  100 VAL   B CA  
5316 C C   A VAL   B 100 ? 0.3530 0.2839 0.2891 0.0335  0.0595  0.1299  100 VAL   B C   
5317 C C   B VAL   B 100 ? 0.3523 0.2830 0.2898 0.0343  0.0476  0.1209  100 VAL   B C   
5318 O O   A VAL   B 100 ? 0.3603 0.2964 0.2955 0.0320  0.0733  0.1245  100 VAL   B O   
5319 O O   B VAL   B 100 ? 0.3570 0.2912 0.2931 0.0318  0.0545  0.1151  100 VAL   B O   
5320 C CB  A VAL   B 100 ? 0.3400 0.2936 0.3685 0.0044  0.0575  0.1083  100 VAL   B CB  
5321 C CB  B VAL   B 100 ? 0.3386 0.2892 0.3487 0.0113  0.0434  0.0971  100 VAL   B CB  
5322 C CG1 A VAL   B 100 ? 0.3433 0.2987 0.3951 0.0013  0.0585  0.1070  100 VAL   B CG1 
5323 C CG1 B VAL   B 100 ? 0.3415 0.2933 0.3694 0.0089  0.0436  0.0963  100 VAL   B CG1 
5324 C CG2 A VAL   B 100 ? 0.3429 0.2979 0.3836 -0.0037 0.0602  0.1139  100 VAL   B CG2 
5325 C CG2 B VAL   B 100 ? 0.3408 0.2929 0.3620 0.0049  0.0442  0.0992  100 VAL   B CG2 
5344 N N   . ASN   B 101 ? 0.3681 0.2876 0.2855 0.0436  0.0381  0.1328  101 ASN   B N   
5345 C CA  . ASN   B 101 ? 0.4083 0.3117 0.3081 0.0502  0.0114  0.1291  101 ASN   B CA  
5346 C C   . ASN   B 101 ? 0.4530 0.3621 0.3118 0.0451  -0.0011 0.1214  101 ASN   B C   
5347 O O   . ASN   B 101 ? 0.4576 0.3742 0.3303 0.0525  -0.0002 0.0988  101 ASN   B O   
5348 C CB  . ASN   B 101 ? 0.4049 0.2941 0.3198 0.0466  0.0145  0.1194  101 ASN   B CB  
5349 C CG  . ASN   B 101 ? 0.3997 0.2793 0.3281 0.0481  0.0167  0.1147  101 ASN   B CG  
5350 O OD1 . ASN   B 101 ? 0.4044 0.2784 0.3588 0.0422  0.0320  0.1078  101 ASN   B OD1 
5351 N ND2 . ASN   B 101 ? 0.3922 0.2723 0.3221 0.0493  0.0135  0.1008  101 ASN   B ND2 
5359 N N   A LYS   B 102 ? 0.4766 0.3860 0.3233 0.0360  0.0023  0.1157  102 LYS   B N   
5360 N N   B LYS   B 102 ? 0.4679 0.3842 0.3349 0.0342  0.0007  0.1035  102 LYS   B N   
5361 C CA  A LYS   B 102 ? 0.4986 0.4144 0.3455 0.0240  0.0125  0.0991  102 LYS   B CA  
5362 C CA  B LYS   B 102 ? 0.4812 0.4081 0.3648 0.0216  0.0079  0.0797  102 LYS   B CA  
5363 C C   A LYS   B 102 ? 0.4983 0.4161 0.3200 0.0264  0.0245  0.1122  102 LYS   B C   
5364 C C   B LYS   B 102 ? 0.4768 0.4071 0.3526 0.0200  0.0144  0.0805  102 LYS   B C   
5365 O O   A LYS   B 102 ? 0.5065 0.4196 0.3257 0.0280  0.0163  0.1091  102 LYS   B O   
5366 O O   B LYS   B 102 ? 0.4819 0.4098 0.3561 0.0206  0.0113  0.0771  102 LYS   B O   
5367 C CB  A LYS   B 102 ? 0.5181 0.4394 0.4031 0.0110  0.0183  0.0624  102 LYS   B CB  
5368 C CB  B LYS   B 102 ? 0.4965 0.4309 0.4131 0.0116  0.0124  0.0506  102 LYS   B CB  
5369 C CG  A LYS   B 102 ? 0.5345 0.4609 0.4642 0.0007  0.0250  0.0282  102 LYS   B CG  
5370 C CG  B LYS   B 102 ? 0.5094 0.4505 0.4627 0.0038  0.0176  0.0236  102 LYS   B CG  
5371 C CD  A LYS   B 102 ? 0.5484 0.4780 0.5203 -0.0072 0.0323  0.0013  102 LYS   B CD  
5372 C CD  B LYS   B 102 ? 0.5204 0.4658 0.5077 -0.0023 0.0229  0.0025  102 LYS   B CD  
5373 C CE  A LYS   B 102 ? 0.5580 0.4895 0.5632 -0.0135 0.0379  -0.0179 102 LYS   B CE  
5374 C CE  B LYS   B 102 ? 0.5280 0.4761 0.5420 -0.0070 0.0271  -0.0127 102 LYS   B CE  
5375 N NZ  A LYS   B 102 ? 0.5631 0.4963 0.5884 -0.0165 0.0403  -0.0287 102 LYS   B NZ  
5376 N NZ  B LYS   B 102 ? 0.5320 0.4822 0.5619 -0.0091 0.0291  -0.0208 102 LYS   B NZ  
5403 N N   A GLY   B 103 ? 0.4862 0.4114 0.3043 0.0264  0.0478  0.1208  103 GLY   B N   
5404 N N   B GLY   B 103 ? 0.4646 0.4002 0.3441 0.0171  0.0258  0.0817  103 GLY   B N   
5405 C CA  A GLY   B 103 ? 0.4728 0.4060 0.3117 0.0280  0.0709  0.1128  103 GLY   B CA  
5406 C CA  B GLY   B 103 ? 0.4514 0.3916 0.3440 0.0143  0.0366  0.0740  103 GLY   B CA  
5407 C C   A GLY   B 103 ? 0.4555 0.3966 0.3069 0.0272  0.0925  0.1007  103 GLY   B C   
5408 C C   B GLY   B 103 ? 0.4357 0.3799 0.3359 0.0090  0.0457  0.0623  103 GLY   B C   
5409 O O   A GLY   B 103 ? 0.4598 0.4038 0.3178 0.0240  0.0925  0.1028  103 GLY   B O   
5410 O O   B GLY   B 103 ? 0.4383 0.3844 0.3440 0.0092  0.0475  0.0625  103 GLY   B O   
5417 N N   A GLU   B 104 ? 0.4310 0.3769 0.2899 0.0304  0.1118  0.0788  104 GLU   B N   
5418 N N   B GLU   B 104 ? 0.4157 0.3609 0.3160 0.0024  0.0499  0.0457  104 GLU   B N   
5419 C CA  A GLU   B 104 ? 0.4067 0.3578 0.2682 0.0367  0.1201  0.0572  104 GLU   B CA  
5420 C CA  B GLU   B 104 ? 0.3959 0.3429 0.2943 -0.0040 0.0488  0.0310  104 GLU   B CA  
5421 C C   A GLU   B 104 ? 0.4113 0.3584 0.2861 0.0221  0.1483  0.0525  104 GLU   B C   
5422 C C   B GLU   B 104 ? 0.3941 0.3417 0.3022 -0.0097 0.0682  0.0270  104 GLU   B C   
5423 O O   A GLU   B 104 ? 0.4143 0.3622 0.3174 0.0171  0.1430  0.0455  104 GLU   B O   
5424 O O   B GLU   B 104 ? 0.3955 0.3430 0.3133 -0.0115 0.0682  0.0222  104 GLU   B O   
5425 C CB  A GLU   B 104 ? 0.3851 0.3372 0.2618 0.0586  0.0818  0.0276  104 GLU   B CB  
5426 C CB  B GLU   B 104 ? 0.3818 0.3245 0.2776 -0.0064 0.0236  0.0145  104 GLU   B CB  
5427 C CG  A GLU   B 104 ? 0.3669 0.3231 0.2520 0.0769  0.0381  -0.0036 104 GLU   B CG  
5428 C CG  B GLU   B 104 ? 0.3708 0.3098 0.2613 -0.0099 -0.0041 -0.0034 104 GLU   B CG  
5429 C CD  A GLU   B 104 ? 0.3495 0.3079 0.2322 0.0942  0.0084  -0.0196 104 GLU   B CD  
5430 C CD  B GLU   B 104 ? 0.3618 0.2951 0.2457 -0.0160 -0.0227 -0.0104 104 GLU   B CD  
5431 O OE1 A GLU   B 104 ? 0.3299 0.2930 0.1885 0.1074  0.0217  -0.0210 104 GLU   B OE1 
5432 O OE1 B GLU   B 104 ? 0.3530 0.2851 0.2351 -0.0228 -0.0198 -0.0081 104 GLU   B OE1 
5433 O OE2 A GLU   B 104 ? 0.3549 0.3164 0.2544 0.0913  -0.0218 -0.0280 104 GLU   B OE2 
5434 O OE2 B GLU   B 104 ? 0.3625 0.2958 0.2432 -0.0181 -0.0399 -0.0166 104 GLU   B OE2 
5447 N N   A ASP   B 105 ? 0.4089 0.3575 0.2847 0.0113  0.1751  0.0562  105 ASP   B N   
5448 N N   B ASP   B 105 ? 0.3894 0.3408 0.3032 -0.0151 0.0861  0.0284  105 ASP   B N   
5449 C CA  A ASP   B 105 ? 0.4092 0.3556 0.3136 0.0014  0.1918  0.0439  105 ASP   B CA  
5450 C CA  B ASP   B 105 ? 0.3873 0.3392 0.3203 -0.0201 0.0998  0.0221  105 ASP   B CA  
5451 C C   A ASP   B 105 ? 0.3912 0.3251 0.2965 -0.0088 0.1907  0.0398  105 ASP   B C   
5452 C C   B ASP   B 105 ? 0.3778 0.3246 0.3022 -0.0243 0.1019  0.0163  105 ASP   B C   
5453 O O   A ASP   B 105 ? 0.3789 0.3186 0.2959 -0.0075 0.1921  0.0383  105 ASP   B O   
5454 O O   B ASP   B 105 ? 0.3721 0.3208 0.2896 -0.0254 0.1070  0.0159  105 ASP   B O   
5455 C CB  A ASP   B 105 ? 0.4256 0.3787 0.3831 0.0072  0.1939  0.0256  105 ASP   B CB  
5456 C CB  B ASP   B 105 ? 0.3917 0.3491 0.3602 -0.0188 0.1088  0.0175  105 ASP   B CB  
5457 C CG  A ASP   B 105 ? 0.4371 0.3950 0.4523 0.0086  0.1976  0.0153  105 ASP   B CG  
5458 C CG  B ASP   B 105 ? 0.3949 0.3544 0.3994 -0.0212 0.1174  0.0188  105 ASP   B CG  
5459 O OD1 A ASP   B 105 ? 0.4373 0.4008 0.4589 0.0024  0.2105  0.0214  105 ASP   B OD1 
5460 O OD1 B ASP   B 105 ? 0.3945 0.3572 0.4061 -0.0265 0.1217  0.0216  105 ASP   B OD1 
5461 O OD2 A ASP   B 105 ? 0.4434 0.4012 0.4965 0.0149  0.1855  0.0032  105 ASP   B OD2 
5462 O OD2 B ASP   B 105 ? 0.3928 0.3559 0.4103 -0.0231 0.1263  0.0218  105 ASP   B OD2 
5471 N N   A ILE   B 106 ? 0.3807 0.2989 0.3091 -0.0150 0.1725  0.0421  106 ILE   B N   
5472 N N   B ILE   B 106 ? 0.3717 0.3131 0.3020 -0.0238 0.0935  0.0123  106 ILE   B N   
5473 C CA  A ILE   B 106 ? 0.3592 0.2725 0.3196 -0.0265 0.1730  0.0404  106 ILE   B CA  
5474 C CA  B ILE   B 106 ? 0.3601 0.3030 0.3086 -0.0254 0.0928  0.0068  106 ILE   B CA  
5475 C C   A ILE   B 106 ? 0.3253 0.2646 0.3198 -0.0208 0.1697  0.0155  106 ILE   B C   
5476 C C   B ILE   B 106 ? 0.3385 0.2999 0.3098 -0.0231 0.0909  -0.0080 106 ILE   B C   
5477 O O   A ILE   B 106 ? 0.3164 0.2420 0.3281 -0.0224 0.1630  0.0096  106 ILE   B O   
5478 O O   B ILE   B 106 ? 0.3341 0.2899 0.3057 -0.0286 0.0827  -0.0163 106 ILE   B O   
5479 C CB  A ILE   B 106 ? 0.3760 0.2644 0.3369 -0.0350 0.1623  0.0537  106 ILE   B CB  
5480 C CB  B ILE   B 106 ? 0.3715 0.3017 0.3171 -0.0268 0.0902  0.0136  106 ILE   B CB  
5481 C CG1 A ILE   B 106 ? 0.3834 0.2642 0.3425 -0.0253 0.1484  0.0466  106 ILE   B CG1 
5482 C CG1 B ILE   B 106 ? 0.3760 0.3015 0.3210 -0.0210 0.0846  0.0150  106 ILE   B CG1 
5483 C CG2 A ILE   B 106 ? 0.3811 0.2678 0.3593 -0.0438 0.1646  0.0600  106 ILE   B CG2 
5484 C CG2 B ILE   B 106 ? 0.3756 0.3051 0.3274 -0.0295 0.0920  0.0138  106 ILE   B CG2 
5485 C CD1 A ILE   B 106 ? 0.3872 0.2660 0.3388 -0.0177 0.1443  0.0510  106 ILE   B CD1 
5486 C CD1 B ILE   B 106 ? 0.3784 0.3025 0.3215 -0.0163 0.0834  0.0193  106 ILE   B CD1 
5509 N N   A GLN   B 107 ? 0.3102 0.2841 0.3361 -0.0181 0.1532  0.0053  107 GLN   B N   
5510 N N   B GLN   B 107 ? 0.3246 0.3086 0.3271 -0.0182 0.0886  -0.0122 107 GLN   B N   
5511 C CA  A GLN   B 107 ? 0.2928 0.2997 0.3501 -0.0201 0.1368  0.0054  107 GLN   B CA  
5512 C CA  B GLN   B 107 ? 0.3098 0.3143 0.3438 -0.0146 0.0858  -0.0087 107 GLN   B CA  
5513 C C   A GLN   B 107 ? 0.2649 0.2796 0.3254 -0.0102 0.1022  -0.0026 107 GLN   B C   
5514 C C   B GLN   B 107 ? 0.2770 0.2908 0.3175 -0.0071 0.0804  -0.0114 107 GLN   B C   
5515 O O   A GLN   B 107 ? 0.2575 0.2754 0.3546 -0.0022 0.0727  -0.0117 107 GLN   B O   
5516 O O   B GLN   B 107 ? 0.2751 0.2937 0.3337 -0.0044 0.0635  -0.0210 107 GLN   B O   
5517 C CB  A GLN   B 107 ? 0.3209 0.3379 0.4144 -0.0233 0.1191  0.0103  107 GLN   B CB  
5518 C CB  B GLN   B 107 ? 0.3342 0.3435 0.3985 -0.0148 0.0745  -0.0029 107 GLN   B CB  
5519 C CG  A GLN   B 107 ? 0.3530 0.3716 0.4844 -0.0214 0.0844  0.0132  107 GLN   B CG  
5520 C CG  B GLN   B 107 ? 0.3586 0.3688 0.4559 -0.0127 0.0551  0.0026  107 GLN   B CG  
5521 C CD  A GLN   B 107 ? 0.3758 0.3963 0.5398 -0.0221 0.0618  0.0175  107 GLN   B CD  
5522 C CD  B GLN   B 107 ? 0.3767 0.3877 0.5026 -0.0124 0.0412  0.0079  107 GLN   B CD  
5523 O OE1 A GLN   B 107 ? 0.3838 0.4068 0.5621 -0.0188 0.0599  0.0156  107 GLN   B OE1 
5524 O OE1 B GLN   B 107 ? 0.3838 0.3955 0.5208 -0.0108 0.0411  0.0084  107 GLN   B OE1 
5525 N NE2 A GLN   B 107 ? 0.3860 0.4038 0.5586 -0.0219 0.0514  0.0243  107 GLN   B NE2 
5526 N NE2 B GLN   B 107 ? 0.3844 0.3939 0.5188 -0.0118 0.0348  0.0125  107 GLN   B NE2 
5543 N N   . LEU   B 108 ? 0.2457 0.2626 0.2862 0.0044  0.0848  -0.0084 108 LEU   B N   
5544 C CA  . LEU   B 108 ? 0.2280 0.2356 0.2374 0.0202  0.0621  0.0054  108 LEU   B CA  
5545 C C   . LEU   B 108 ? 0.1925 0.1943 0.2287 0.0237  0.0376  0.0201  108 LEU   B C   
5546 O O   . LEU   B 108 ? 0.1924 0.1839 0.2310 0.0251  0.0245  0.0195  108 LEU   B O   
5547 C CB  . LEU   B 108 ? 0.2472 0.2542 0.2198 0.0185  0.0559  0.0103  108 LEU   B CB  
5548 C CG  . LEU   B 108 ? 0.2715 0.2797 0.2293 0.0175  0.0436  -0.0110 108 LEU   B CG  
5549 C CD1 . LEU   B 108 ? 0.2779 0.2902 0.2148 0.0041  0.0464  -0.0037 108 LEU   B CD1 
5550 C CD2 . LEU   B 108 ? 0.2907 0.2930 0.2443 0.0284  0.0343  -0.0249 108 LEU   B CD2 
5563 N N   . LEU   B 109 ? 0.1786 0.1762 0.2261 0.0148  0.0323  0.0252  109 LEU   B N   
5564 C CA  . LEU   B 109 ? 0.1603 0.1500 0.2355 0.0072  0.0303  0.0346  109 LEU   B CA  
5565 C C   . LEU   B 109 ? 0.1485 0.1374 0.2407 0.0063  0.0303  0.0222  109 LEU   B C   
5566 O O   . LEU   B 109 ? 0.1517 0.1359 0.2379 0.0076  0.0289  0.0347  109 LEU   B O   
5567 C CB  . LEU   B 109 ? 0.1666 0.1507 0.2387 0.0036  0.0185  0.0414  109 LEU   B CB  
5568 C CG  . LEU   B 109 ? 0.1619 0.1429 0.2372 0.0043  0.0179  0.0318  109 LEU   B CG  
5569 C CD1 . LEU   B 109 ? 0.1638 0.1595 0.2251 0.0158  0.0300  0.0281  109 LEU   B CD1 
5570 C CD2 . LEU   B 109 ? 0.1805 0.1455 0.2568 0.0048  0.0072  0.0254  109 LEU   B CD2 
5582 N N   . LYS   B 110 ? 0.1519 0.1406 0.2336 -0.0036 0.0293  0.0284  110 LYS   B N   
5583 C CA  . LYS   B 110 ? 0.1498 0.1382 0.2345 -0.0002 0.0185  0.0249  110 LYS   B CA  
5584 C C   . LYS   B 110 ? 0.1423 0.1446 0.2158 0.0002  0.0280  0.0146  110 LYS   B C   
5585 O O   . LYS   B 110 ? 0.1396 0.1431 0.2097 -0.0050 0.0181  0.0076  110 LYS   B O   
5586 C CB  . LYS   B 110 ? 0.1527 0.1326 0.2620 -0.0026 0.0232  0.0151  110 LYS   B CB  
5587 C CG  . LYS   B 110 ? 0.1524 0.1348 0.2661 -0.0077 0.0152  0.0213  110 LYS   B CG  
5588 C CD  . LYS   B 110 ? 0.1570 0.1433 0.2731 -0.0061 0.0105  0.0180  110 LYS   B CD  
5589 C CE  . LYS   B 110 ? 0.1558 0.1498 0.2895 -0.0032 0.0073  0.0127  110 LYS   B CE  
5590 N NZ  . LYS   B 110 ? 0.1564 0.1629 0.2860 0.0004  -0.0069 0.0037  110 LYS   B NZ  
5604 N N   . SER   B 111 ? 0.1488 0.1406 0.2241 -0.0037 0.0266  0.0215  111 SER   B N   
5605 C CA  . SER   B 111 ? 0.1530 0.1468 0.2158 0.0014  0.0185  0.0207  111 SER   B CA  
5606 C C   . SER   B 111 ? 0.1464 0.1395 0.2075 -0.0006 0.0097  0.0110  111 SER   B C   
5607 O O   . SER   B 111 ? 0.1404 0.1431 0.2116 0.0000  0.0061  0.0114  111 SER   B O   
5608 C CB  . SER   B 111 ? 0.1662 0.1705 0.2181 0.0055  0.0361  0.0293  111 SER   B CB  
5609 O OG  . SER   B 111 ? 0.1849 0.2061 0.2356 0.0113  0.0433  0.0325  111 SER   B OG  
5615 N N   . ALA   B 112 ? 0.1394 0.1377 0.2149 0.0071  0.0200  0.0167  112 ALA   B N   
5616 C CA  . ALA   B 112 ? 0.1369 0.1412 0.1967 0.0023  0.0088  0.0025  112 ALA   B CA  
5617 C C   . ALA   B 112 ? 0.1276 0.1414 0.1897 0.0024  0.0047  0.0010  112 ALA   B C   
5618 O O   . ALA   B 112 ? 0.1319 0.1379 0.2081 -0.0016 0.0081  0.0005  112 ALA   B O   
5619 C CB  . ALA   B 112 ? 0.1480 0.1510 0.1992 0.0034  0.0039  0.0136  112 ALA   B CB  
5625 N N   . TYR   B 113 ? 0.1296 0.1290 0.1973 -0.0017 0.0101  0.0056  113 TYR   B N   
5626 C CA  . TYR   B 113 ? 0.1271 0.1286 0.1852 -0.0031 0.0095  0.0072  113 TYR   B CA  
5627 C C   . TYR   B 113 ? 0.1261 0.1219 0.1889 -0.0086 0.0036  0.0064  113 TYR   B C   
5628 O O   . TYR   B 113 ? 0.1300 0.1231 0.1910 -0.0038 0.0024  -0.0041 113 TYR   B O   
5629 C CB  . TYR   B 113 ? 0.1329 0.1187 0.1971 -0.0044 0.0174  0.0094  113 TYR   B CB  
5630 C CG  . TYR   B 113 ? 0.1374 0.1276 0.2042 -0.0040 0.0096  0.0112  113 TYR   B CG  
5631 C CD1 . TYR   B 113 ? 0.1445 0.1317 0.2130 -0.0032 0.0056  0.0154  113 TYR   B CD1 
5632 C CD2 . TYR   B 113 ? 0.1425 0.1269 0.2158 -0.0002 0.0020  0.0129  113 TYR   B CD2 
5633 C CE1 . TYR   B 113 ? 0.1400 0.1314 0.2141 -0.0016 0.0161  0.0108  113 TYR   B CE1 
5634 C CE2 . TYR   B 113 ? 0.1505 0.1244 0.2200 0.0055  0.0060  0.0191  113 TYR   B CE2 
5635 C CZ  . TYR   B 113 ? 0.1384 0.1259 0.2296 0.0039  0.0050  0.0115  113 TYR   B CZ  
5636 O OH  . TYR   B 113 ? 0.1445 0.1269 0.2460 0.0114  0.0144  0.0071  113 TYR   B OH  
5646 N N   . GLU   B 114 ? 0.1245 0.1200 0.2036 0.0013  0.0085  0.0014  114 GLU   B N   
5647 C CA  . GLU   B 114 ? 0.1289 0.1145 0.2019 0.0027  0.0024  -0.0003 114 GLU   B CA  
5648 C C   . GLU   B 114 ? 0.1248 0.1210 0.2011 0.0025  0.0041  -0.0024 114 GLU   B C   
5649 O O   . GLU   B 114 ? 0.1252 0.1254 0.2126 0.0049  0.0025  0.0042  114 GLU   B O   
5650 C CB  . GLU   B 114 ? 0.1279 0.1266 0.2214 -0.0014 0.0075  0.0078  114 GLU   B CB  
5651 C CG  . GLU   B 114 ? 0.1375 0.1239 0.2174 -0.0053 0.0057  0.0108  114 GLU   B CG  
5652 C CD  . GLU   B 114 ? 0.1332 0.1308 0.2224 -0.0086 0.0019  0.0081  114 GLU   B CD  
5653 O OE1 . GLU   B 114 ? 0.1277 0.1472 0.2164 -0.0101 0.0138  0.0127  114 GLU   B OE1 
5654 O OE2 . GLU   B 114 ? 0.1328 0.1510 0.2410 -0.0184 0.0118  0.0106  114 GLU   B OE2 
5661 N N   . ASN   B 115 ? 0.1313 0.1172 0.1968 -0.0038 -0.0057 0.0036  115 ASN   B N   
5662 C CA  . ASN   B 115 ? 0.1276 0.1258 0.1834 -0.0021 -0.0024 0.0043  115 ASN   B CA  
5663 C C   . ASN   B 115 ? 0.1282 0.1220 0.1842 -0.0094 -0.0037 -0.0026 115 ASN   B C   
5664 O O   . ASN   B 115 ? 0.1437 0.1252 0.1855 -0.0144 -0.0033 0.0010  115 ASN   B O   
5665 C CB  . ASN   B 115 ? 0.1396 0.1362 0.1833 -0.0047 0.0045  0.0049  115 ASN   B CB  
5666 C CG  . ASN   B 115 ? 0.1504 0.1419 0.1850 0.0029  0.0018  0.0031  115 ASN   B CG  
5667 O OD1 . ASN   B 115 ? 0.1994 0.1542 0.2120 0.0057  0.0153  -0.0142 115 ASN   B OD1 
5668 N ND2 . ASN   B 115 ? 0.1526 0.1509 0.1748 -0.0094 0.0067  0.0049  115 ASN   B ND2 
5675 N N   . PHE   B 116 ? 0.1260 0.1255 0.1732 -0.0036 -0.0003 0.0029  116 PHE   B N   
5676 C CA  . PHE   B 116 ? 0.1304 0.1280 0.1773 -0.0068 -0.0045 0.0046  116 PHE   B CA  
5677 C C   . PHE   B 116 ? 0.1282 0.1157 0.1755 -0.0078 -0.0025 0.0012  116 PHE   B C   
5678 O O   . PHE   B 116 ? 0.1343 0.1266 0.1837 -0.0007 -0.0035 0.0012  116 PHE   B O   
5679 C CB  . PHE   B 116 ? 0.1279 0.1180 0.1736 -0.0062 -0.0149 0.0060  116 PHE   B CB  
5680 C CG  . PHE   B 116 ? 0.1246 0.1194 0.1833 -0.0043 -0.0069 0.0051  116 PHE   B CG  
5681 C CD1 . PHE   B 116 ? 0.1330 0.1246 0.1927 -0.0007 -0.0013 0.0060  116 PHE   B CD1 
5682 C CD2 . PHE   B 116 ? 0.1303 0.1341 0.1771 0.0005  -0.0014 -0.0003 116 PHE   B CD2 
5683 C CE1 . PHE   B 116 ? 0.1351 0.1287 0.1974 -0.0050 -0.0054 0.0008  116 PHE   B CE1 
5684 C CE2 . PHE   B 116 ? 0.1362 0.1356 0.1808 -0.0037 0.0020  0.0047  116 PHE   B CE2 
5685 C CZ  . PHE   B 116 ? 0.1296 0.1352 0.1946 -0.0028 -0.0111 0.0077  116 PHE   B CZ  
5695 N N   . ASN   B 117 ? 0.1279 0.1199 0.1884 -0.0011 -0.0069 0.0056  117 ASN   B N   
5696 C CA  . ASN   B 117 ? 0.1371 0.1284 0.1851 0.0009  -0.0061 -0.0028 117 ASN   B CA  
5697 C C   . ASN   B 117 ? 0.1406 0.1191 0.2001 0.0009  -0.0073 -0.0022 117 ASN   B C   
5698 O O   . ASN   B 117 ? 0.1479 0.1271 0.2297 -0.0040 -0.0328 0.0071  117 ASN   B O   
5699 C CB  . ASN   B 117 ? 0.1388 0.1311 0.1899 0.0016  -0.0048 -0.0041 117 ASN   B CB  
5700 C CG  . ASN   B 117 ? 0.1354 0.1334 0.1999 0.0024  -0.0006 -0.0074 117 ASN   B CG  
5701 O OD1 . ASN   B 117 ? 0.1526 0.1316 0.2123 -0.0128 -0.0031 -0.0004 117 ASN   B OD1 
5702 N ND2 . ASN   B 117 ? 0.1345 0.1340 0.1945 0.0012  -0.0033 -0.0063 117 ASN   B ND2 
5709 N N   . GLN   B 118 ? 0.1434 0.1176 0.1965 -0.0063 -0.0194 -0.0028 118 GLN   B N   
5710 C CA  . GLN   B 118 ? 0.1555 0.1227 0.2005 0.0021  -0.0115 0.0009  118 GLN   B CA  
5711 C C   . GLN   B 118 ? 0.1521 0.1253 0.2006 -0.0005 -0.0033 0.0032  118 GLN   B C   
5712 O O   . GLN   B 118 ? 0.1669 0.1233 0.2382 -0.0103 0.0002  0.0054  118 GLN   B O   
5713 C CB  . GLN   B 118 ? 0.1614 0.1268 0.2094 -0.0014 -0.0169 -0.0003 118 GLN   B CB  
5714 C CG  . GLN   B 118 ? 0.1667 0.1250 0.2048 0.0005  -0.0107 -0.0129 118 GLN   B CG  
5715 C CD  . GLN   B 118 ? 0.1663 0.1219 0.2066 -0.0014 -0.0123 -0.0125 118 GLN   B CD  
5716 O OE1 . GLN   B 118 ? 0.1729 0.1222 0.2292 -0.0020 0.0023  -0.0009 118 GLN   B OE1 
5717 N NE2 . GLN   B 118 ? 0.1764 0.1224 0.2094 0.0013  -0.0174 -0.0038 118 GLN   B NE2 
5726 N N   . HIS   B 119 ? 0.1500 0.1314 0.1659 -0.0064 -0.0068 0.0083  119 HIS   B N   
5727 C CA  . HIS   B 119 ? 0.1559 0.1396 0.1657 -0.0005 -0.0149 0.0103  119 HIS   B CA  
5728 C C   . HIS   B 119 ? 0.1604 0.1399 0.1668 -0.0047 -0.0279 0.0101  119 HIS   B C   
5729 O O   . HIS   B 119 ? 0.1635 0.1414 0.1812 -0.0248 -0.0155 0.0100  119 HIS   B O   
5730 C CB  . HIS   B 119 ? 0.1586 0.1578 0.1698 0.0014  -0.0196 0.0042  119 HIS   B CB  
5731 C CG  . HIS   B 119 ? 0.1634 0.1756 0.1900 0.0103  -0.0348 -0.0166 119 HIS   B CG  
5732 N ND1 . HIS   B 119 ? 0.1756 0.1899 0.2263 0.0026  -0.0411 -0.0350 119 HIS   B ND1 
5733 C CD2 . HIS   B 119 ? 0.1828 0.1894 0.1989 0.0364  -0.0431 -0.0258 119 HIS   B CD2 
5734 C CE1 . HIS   B 119 ? 0.2001 0.2073 0.2370 0.0198  -0.0510 -0.0526 119 HIS   B CE1 
5735 N NE2 . HIS   B 119 ? 0.2039 0.2169 0.2173 0.0333  -0.0511 -0.0400 119 HIS   B NE2 
5743 N N   . GLU   B 120 ? 0.1842 0.1392 0.1738 -0.0107 -0.0431 0.0175  120 GLU   B N   
5744 C CA  . GLU   B 120 ? 0.2086 0.1572 0.1839 -0.0023 -0.0514 0.0241  120 GLU   B CA  
5745 C C   . GLU   B 120 ? 0.1854 0.1480 0.1667 -0.0094 -0.0442 0.0275  120 GLU   B C   
5746 O O   . GLU   B 120 ? 0.1792 0.1609 0.1740 -0.0121 -0.0311 0.0130  120 GLU   B O   
5747 C CB  . GLU   B 120 ? 0.2761 0.1929 0.2531 0.0184  -0.0838 0.0438  120 GLU   B CB  
5748 C CG  . GLU   B 120 ? 0.3396 0.2704 0.3565 0.0257  -0.1054 0.0677  120 GLU   B CG  
5749 C CD  . GLU   B 120 ? 0.3866 0.3399 0.4691 0.0240  -0.1108 0.0783  120 GLU   B CD  
5750 O OE1 . GLU   B 120 ? 0.4090 0.3667 0.5088 0.0166  -0.1043 0.0902  120 GLU   B OE1 
5751 O OE2 . GLU   B 120 ? 0.4075 0.3671 0.5263 0.0234  -0.1097 0.0724  120 GLU   B OE2 
5758 N N   . VAL   B 121 ? 0.1782 0.1404 0.1669 -0.0125 -0.0225 0.0137  121 VAL   B N   
5759 C CA  . VAL   B 121 ? 0.1708 0.1599 0.1558 -0.0136 -0.0246 0.0124  121 VAL   B CA  
5760 C C   . VAL   B 121 ? 0.1596 0.1506 0.1499 -0.0210 -0.0179 0.0134  121 VAL   B C   
5761 O O   . VAL   B 121 ? 0.1660 0.1435 0.1827 -0.0267 -0.0279 0.0037  121 VAL   B O   
5762 C CB  . VAL   B 121 ? 0.1917 0.1934 0.1647 -0.0021 -0.0358 0.0222  121 VAL   B CB  
5763 C CG1 . VAL   B 121 ? 0.1948 0.2050 0.2112 -0.0141 -0.0176 0.0140  121 VAL   B CG1 
5764 C CG2 . VAL   B 121 ? 0.2102 0.2158 0.1664 0.0018  -0.0291 0.0068  121 VAL   B CG2 
5774 N N   . LEU   B 122 ? 0.1521 0.1390 0.1511 -0.0134 -0.0219 0.0081  122 LEU   B N   
5775 C CA  . LEU   B 122 ? 0.1459 0.1449 0.1490 -0.0186 -0.0210 0.0128  122 LEU   B CA  
5776 C C   . LEU   B 122 ? 0.1461 0.1310 0.1568 -0.0260 -0.0177 0.0031  122 LEU   B C   
5777 O O   . LEU   B 122 ? 0.1619 0.1352 0.1785 -0.0282 -0.0235 0.0022  122 LEU   B O   
5778 C CB  . LEU   B 122 ? 0.1705 0.1522 0.1791 -0.0033 -0.0332 0.0132  122 LEU   B CB  
5779 C CG  . LEU   B 122 ? 0.1592 0.1642 0.1822 -0.0153 -0.0157 0.0108  122 LEU   B CG  
5780 C CD1 . LEU   B 122 ? 0.1661 0.1812 0.1935 -0.0167 -0.0200 0.0029  122 LEU   B CD1 
5781 C CD2 . LEU   B 122 ? 0.1618 0.1610 0.1710 -0.0102 -0.0041 -0.0013 122 LEU   B CD2 
5793 N N   . LEU   B 123 ? 0.1511 0.1236 0.1492 -0.0235 -0.0126 0.0077  123 LEU   B N   
5794 C CA  . LEU   B 123 ? 0.1515 0.1336 0.1502 -0.0203 -0.0174 -0.0006 123 LEU   B CA  
5795 C C   . LEU   B 123 ? 0.1430 0.1318 0.1513 -0.0249 -0.0170 0.0043  123 LEU   B C   
5796 O O   . LEU   B 123 ? 0.1585 0.1314 0.1534 -0.0317 -0.0133 0.0070  123 LEU   B O   
5797 C CB  . LEU   B 123 ? 0.1611 0.1305 0.1586 -0.0203 -0.0134 -0.0067 123 LEU   B CB  
5798 C CG  . LEU   B 123 ? 0.1590 0.1351 0.1693 -0.0162 -0.0042 0.0061  123 LEU   B CG  
5799 C CD1 . LEU   B 123 ? 0.1728 0.1426 0.1806 -0.0151 0.0068  -0.0169 123 LEU   B CD1 
5800 C CD2 . LEU   B 123 ? 0.1652 0.1451 0.1904 -0.0157 0.0025  0.0173  123 LEU   B CD2 
5812 N N   . ALA   B 124 ? 0.1438 0.1307 0.1480 -0.0212 -0.0096 -0.0012 124 ALA   B N   
5813 C CA  . ALA   B 124 ? 0.1362 0.1331 0.1609 -0.0115 -0.0070 -0.0124 124 ALA   B CA  
5814 C C   . ALA   B 124 ? 0.1317 0.1282 0.1454 -0.0150 -0.0144 -0.0038 124 ALA   B C   
5815 O O   . ALA   B 124 ? 0.1444 0.1284 0.1593 -0.0115 -0.0124 0.0029  124 ALA   B O   
5816 C CB  . ALA   B 124 ? 0.1407 0.1331 0.1636 0.0036  0.0012  -0.0050 124 ALA   B CB  
5822 N N   . PRO   B 125 ? 0.1438 0.1260 0.1464 -0.0149 -0.0164 0.0093  125 PRO   B N   
5823 C CA  . PRO   B 125 ? 0.1505 0.1317 0.1666 -0.0138 -0.0158 0.0214  125 PRO   B CA  
5824 C C   . PRO   B 125 ? 0.1453 0.1231 0.1846 -0.0158 -0.0107 0.0076  125 PRO   B C   
5825 O O   . PRO   B 125 ? 0.1486 0.1198 0.2058 -0.0123 -0.0038 0.0207  125 PRO   B O   
5826 C CB  . PRO   B 125 ? 0.1536 0.1583 0.1780 -0.0151 -0.0176 0.0287  125 PRO   B CB  
5827 C CG  . PRO   B 125 ? 0.1611 0.1583 0.1698 -0.0272 -0.0193 0.0172  125 PRO   B CG  
5828 C CD  . PRO   B 125 ? 0.1522 0.1398 0.1515 -0.0309 -0.0126 0.0096  125 PRO   B CD  
5836 N N   . LEU   B 126 ? 0.1480 0.1234 0.2056 -0.0151 0.0083  0.0177  126 LEU   B N   
5837 C CA  . LEU   B 126 ? 0.1553 0.1297 0.2126 -0.0108 0.0177  0.0199  126 LEU   B CA  
5838 C C   . LEU   B 126 ? 0.1454 0.1364 0.2077 0.0011  0.0210  0.0195  126 LEU   B C   
5839 O O   . LEU   B 126 ? 0.1673 0.1727 0.2205 0.0242  -0.0045 -0.0035 126 LEU   B O   
5840 C CB  . LEU   B 126 ? 0.1722 0.1356 0.2412 -0.0112 0.0190  0.0101  126 LEU   B CB  
5841 C CG  . LEU   B 126 ? 0.1907 0.1449 0.2437 -0.0198 0.0234  -0.0093 126 LEU   B CG  
5842 C CD1 . LEU   B 126 ? 0.2043 0.1514 0.2998 -0.0220 0.0143  -0.0174 126 LEU   B CD1 
5843 C CD2 . LEU   B 126 ? 0.1934 0.1552 0.2377 -0.0284 0.0169  -0.0121 126 LEU   B CD2 
5855 N N   . LEU   B 127 ? 0.1449 0.1286 0.2115 -0.0010 0.0211  0.0089  127 LEU   B N   
5856 C CA  . LEU   B 127 ? 0.1426 0.1394 0.2233 -0.0022 0.0296  0.0219  127 LEU   B CA  
5857 C C   . LEU   B 127 ? 0.1356 0.1400 0.2280 0.0001  0.0180  0.0155  127 LEU   B C   
5858 O O   . LEU   B 127 ? 0.1462 0.1386 0.2158 -0.0117 0.0096  0.0199  127 LEU   B O   
5859 C CB  . LEU   B 127 ? 0.1572 0.1383 0.2360 -0.0013 0.0232  0.0274  127 LEU   B CB  
5860 C CG  . LEU   B 127 ? 0.1728 0.1384 0.2425 0.0029  0.0183  0.0205  127 LEU   B CG  
5861 C CD1 . LEU   B 127 ? 0.1689 0.1356 0.2285 0.0075  0.0055  0.0129  127 LEU   B CD1 
5862 C CD2 . LEU   B 127 ? 0.1754 0.1465 0.2551 -0.0078 0.0184  0.0284  127 LEU   B CD2 
5874 N N   . SER   B 128 ? 0.1416 0.1376 0.2183 0.0003  0.0030  0.0206  128 SER   B N   
5875 C CA  . SER   B 128 ? 0.1618 0.1477 0.2080 0.0078  -0.0019 0.0239  128 SER   B CA  
5876 C C   . SER   B 128 ? 0.1741 0.1484 0.2326 0.0093  -0.0256 0.0236  128 SER   B C   
5877 O O   . SER   B 128 ? 0.1878 0.1477 0.2706 0.0043  -0.0183 0.0305  128 SER   B O   
5878 C CB  . SER   B 128 ? 0.1706 0.1490 0.2032 0.0055  0.0001  0.0242  128 SER   B CB  
5879 O OG  . SER   B 128 ? 0.1800 0.1613 0.2110 0.0109  0.0103  0.0337  128 SER   B OG  
5885 N N   . ALA   B 129 ? 0.1855 0.1548 0.2523 0.0247  -0.0175 0.0097  129 ALA   B N   
5886 C CA  . ALA   B 129 ? 0.1987 0.1622 0.2686 0.0314  -0.0150 -0.0028 129 ALA   B CA  
5887 C C   . ALA   B 129 ? 0.1831 0.1517 0.2521 0.0210  0.0003  0.0078  129 ALA   B C   
5888 O O   . ALA   B 129 ? 0.1789 0.1566 0.2534 0.0205  -0.0014 0.0113  129 ALA   B O   
5889 C CB  . ALA   B 129 ? 0.2203 0.1917 0.3119 0.0359  -0.0062 -0.0153 129 ALA   B CB  
5895 N N   . GLY   B 130 ? 0.1792 0.1513 0.2566 0.0314  0.0154  -0.0012 130 GLY   B N   
5896 C CA  . GLY   B 130 ? 0.1837 0.1605 0.2737 0.0246  0.0350  -0.0015 130 GLY   B CA  
5897 C C   . GLY   B 130 ? 0.1918 0.1642 0.2614 0.0167  0.0181  0.0127  130 GLY   B C   
5898 O O   . GLY   B 130 ? 0.2125 0.1736 0.2646 0.0205  0.0101  0.0210  130 GLY   B O   
5902 N N   . ILE   B 131 ? 0.1853 0.1766 0.2688 0.0313  0.0130  0.0106  131 ILE   B N   
5903 C CA  . ILE   B 131 ? 0.2019 0.1910 0.2576 0.0289  0.0011  0.0245  131 ILE   B CA  
5904 C C   . ILE   B 131 ? 0.2167 0.1822 0.2319 0.0201  0.0000  0.0284  131 ILE   B C   
5905 O O   . ILE   B 131 ? 0.2431 0.1974 0.2484 0.0262  -0.0191 0.0271  131 ILE   B O   
5906 C CB  . ILE   B 131 ? 0.2042 0.2270 0.2945 0.0252  -0.0061 0.0318  131 ILE   B CB  
5907 C CG1 . ILE   B 131 ? 0.2087 0.2479 0.3019 0.0010  0.0025  0.0300  131 ILE   B CG1 
5908 C CG2 . ILE   B 131 ? 0.2009 0.2414 0.3203 0.0270  -0.0019 0.0226  131 ILE   B CG2 
5909 C CD1 . ILE   B 131 ? 0.2213 0.2695 0.3068 -0.0155 -0.0008 0.0374  131 ILE   B CD1 
5921 N N   . PHE   B 132 ? 0.1977 0.1648 0.2136 0.0154  0.0126  0.0275  132 PHE   B N   
5922 C CA  . PHE   B 132 ? 0.2082 0.1640 0.2203 0.0081  0.0308  0.0155  132 PHE   B CA  
5923 C C   . PHE   B 132 ? 0.2260 0.1800 0.2445 0.0078  0.0358  0.0168  132 PHE   B C   
5924 O O   . PHE   B 132 ? 0.2450 0.2041 0.2734 0.0045  0.0502  0.0230  132 PHE   B O   
5925 C CB  . PHE   B 132 ? 0.1924 0.1597 0.2076 0.0098  0.0363  0.0182  132 PHE   B CB  
5926 C CG  . PHE   B 132 ? 0.1921 0.1704 0.2122 0.0159  0.0326  0.0180  132 PHE   B CG  
5927 C CD1 . PHE   B 132 ? 0.1998 0.1710 0.2487 0.0061  0.0338  0.0221  132 PHE   B CD1 
5928 C CD2 . PHE   B 132 ? 0.1923 0.1722 0.1945 0.0244  0.0237  0.0300  132 PHE   B CD2 
5929 C CE1 . PHE   B 132 ? 0.2031 0.1770 0.2594 0.0035  0.0200  0.0259  132 PHE   B CE1 
5930 C CE2 . PHE   B 132 ? 0.2016 0.1790 0.1983 0.0215  0.0124  0.0276  132 PHE   B CE2 
5931 C CZ  . PHE   B 132 ? 0.2062 0.1782 0.2456 0.0104  -0.0015 0.0342  132 PHE   B CZ  
5941 N N   . GLY   B 133 ? 0.2249 0.1678 0.2498 0.0057  0.0211  0.0343  133 GLY   B N   
5942 C CA  . GLY   B 133 ? 0.2354 0.1801 0.2593 -0.0155 0.0205  0.0375  133 GLY   B CA  
5943 C C   . GLY   B 133 ? 0.2395 0.1864 0.2548 -0.0268 0.0294  0.0401  133 GLY   B C   
5944 O O   . GLY   B 133 ? 0.2601 0.2001 0.2952 -0.0402 0.0237  0.0573  133 GLY   B O   
5948 N N   . ALA   B 134 ? 0.2152 0.1884 0.2394 -0.0258 0.0314  0.0200  134 ALA   B N   
5949 C CA  . ALA   B 134 ? 0.2078 0.1889 0.2556 -0.0142 0.0372  0.0087  134 ALA   B CA  
5950 C C   . ALA   B 134 ? 0.2181 0.1812 0.2612 -0.0135 0.0346  0.0243  134 ALA   B C   
5951 O O   . ALA   B 134 ? 0.2251 0.2041 0.2808 -0.0037 0.0290  0.0137  134 ALA   B O   
5952 C CB  . ALA   B 134 ? 0.2089 0.1845 0.2814 -0.0006 0.0275  0.0051  134 ALA   B CB  
5958 N N   . ASP   B 135 ? 0.2325 0.1680 0.2619 -0.0119 0.0162  0.0329  135 ASP   B N   
5959 C CA  . ASP   B 135 ? 0.2503 0.1600 0.2874 -0.0111 -0.0043 0.0345  135 ASP   B CA  
5960 C C   . ASP   B 135 ? 0.2320 0.1524 0.2702 -0.0057 -0.0103 0.0310  135 ASP   B C   
5961 O O   . ASP   B 135 ? 0.2246 0.1485 0.2833 -0.0093 -0.0139 0.0316  135 ASP   B O   
5962 C CB  . ASP   B 135 ? 0.2823 0.1755 0.3053 -0.0300 -0.0013 0.0338  135 ASP   B CB  
5963 C CG  . ASP   B 135 ? 0.3137 0.1777 0.3481 -0.0498 0.0007  0.0272  135 ASP   B CG  
5964 O OD1 . ASP   B 135 ? 0.3290 0.1636 0.3454 -0.0307 -0.0094 0.0220  135 ASP   B OD1 
5965 O OD2 . ASP   B 135 ? 0.3389 0.2169 0.4115 -0.0604 -0.0030 0.0077  135 ASP   B OD2 
5970 N N   . PRO   B 136 ? 0.2246 0.1621 0.2810 0.0176  -0.0181 0.0256  136 PRO   B N   
5971 C CA  . PRO   B 136 ? 0.2057 0.1538 0.2786 0.0149  -0.0168 0.0095  136 PRO   B CA  
5972 C C   . PRO   B 136 ? 0.1842 0.1396 0.2840 0.0102  -0.0079 0.0052  136 PRO   B C   
5973 O O   . PRO   B 136 ? 0.1634 0.1377 0.2800 0.0074  -0.0008 0.0117  136 PRO   B O   
5974 C CB  . PRO   B 136 ? 0.2137 0.1746 0.2850 0.0263  -0.0172 -0.0008 136 PRO   B CB  
5975 C CG  . PRO   B 136 ? 0.2293 0.1834 0.3059 0.0306  -0.0107 0.0022  136 PRO   B CG  
5976 C CD  . PRO   B 136 ? 0.2282 0.1733 0.2901 0.0382  -0.0087 0.0181  136 PRO   B CD  
5984 N N   . ILE   B 137 ? 0.1907 0.1308 0.2882 0.0125  -0.0101 0.0021  137 ILE   B N   
5985 C CA  . ILE   B 137 ? 0.1979 0.1285 0.3080 -0.0040 0.0031  0.0094  137 ILE   B CA  
5986 C C   . ILE   B 137 ? 0.1934 0.1418 0.2954 -0.0089 0.0116  0.0138  137 ILE   B C   
5987 O O   . ILE   B 137 ? 0.1771 0.1450 0.2770 -0.0123 0.0075  0.0065  137 ILE   B O   
5988 C CB  . ILE   B 137 ? 0.2261 0.1385 0.3474 -0.0086 0.0022  0.0088  137 ILE   B CB  
5989 C CG1 . ILE   B 137 ? 0.2601 0.1494 0.4012 0.0028  0.0118  -0.0026 137 ILE   B CG1 
5990 C CG2 . ILE   B 137 ? 0.2320 0.1449 0.3637 -0.0307 -0.0081 0.0120  137 ILE   B CG2 
5991 C CD1 . ILE   B 137 ? 0.2854 0.1817 0.4417 0.0175  0.0087  0.0048  137 ILE   B CD1 
6003 N N   . HIS   B 138 ? 0.2030 0.1329 0.2955 -0.0054 0.0169  0.0180  138 HIS   B N   
6004 C CA  . HIS   B 138 ? 0.2087 0.1435 0.2914 -0.0004 0.0313  0.0184  138 HIS   B CA  
6005 C C   . HIS   B 138 ? 0.1898 0.1383 0.2691 -0.0034 0.0283  0.0248  138 HIS   B C   
6006 O O   . HIS   B 138 ? 0.1850 0.1448 0.2859 -0.0005 0.0343  0.0373  138 HIS   B O   
6007 C CB  . HIS   B 138 ? 0.2307 0.1556 0.3045 -0.0023 0.0527  0.0233  138 HIS   B CB  
6008 C CG  . HIS   B 138 ? 0.2464 0.1712 0.3082 -0.0085 0.0696  0.0381  138 HIS   B CG  
6009 N ND1 . HIS   B 138 ? 0.2562 0.1926 0.3275 -0.0048 0.0795  0.0262  138 HIS   B ND1 
6010 C CD2 . HIS   B 138 ? 0.2605 0.1852 0.3037 -0.0097 0.0802  0.0246  138 HIS   B CD2 
6011 C CE1 . HIS   B 138 ? 0.2603 0.1953 0.3237 -0.0033 0.0823  0.0246  138 HIS   B CE1 
6012 N NE2 . HIS   B 138 ? 0.2689 0.1807 0.3107 0.0039  0.0835  0.0204  138 HIS   B NE2 
6020 N N   . SER   B 139 ? 0.1842 0.1216 0.2581 0.0007  0.0204  0.0163  139 SER   B N   
6021 C CA  . SER   B 139 ? 0.1779 0.1327 0.2446 -0.0009 0.0221  0.0055  139 SER   B CA  
6022 C C   . SER   B 139 ? 0.1526 0.1228 0.2434 0.0023  0.0143  0.0067  139 SER   B C   
6023 O O   . SER   B 139 ? 0.1551 0.1261 0.2582 0.0067  0.0060  0.0165  139 SER   B O   
6024 C CB  . SER   B 139 ? 0.1834 0.1297 0.2366 -0.0041 0.0046  0.0036  139 SER   B CB  
6025 O OG  . SER   B 139 ? 0.1824 0.1298 0.2494 -0.0021 -0.0065 0.0190  139 SER   B OG  
6031 N N   . LEU   B 140 ? 0.1516 0.1186 0.2428 -0.0054 0.0175  0.0029  140 LEU   B N   
6032 C CA  . LEU   B 140 ? 0.1505 0.1216 0.2463 -0.0030 0.0135  0.0088  140 LEU   B CA  
6033 C C   . LEU   B 140 ? 0.1473 0.1237 0.2639 -0.0018 0.0009  -0.0025 140 LEU   B C   
6034 O O   . LEU   B 140 ? 0.1429 0.1290 0.2633 -0.0079 -0.0049 0.0112  140 LEU   B O   
6035 C CB  . LEU   B 140 ? 0.1483 0.1191 0.2692 -0.0103 0.0146  0.0000  140 LEU   B CB  
6036 C CG  . LEU   B 140 ? 0.1554 0.1275 0.2602 -0.0053 0.0029  0.0059  140 LEU   B CG  
6037 C CD1 . LEU   B 140 ? 0.1681 0.1378 0.2777 -0.0093 -0.0025 0.0082  140 LEU   B CD1 
6038 C CD2 . LEU   B 140 ? 0.1796 0.1455 0.2709 -0.0083 0.0057  -0.0082 140 LEU   B CD2 
6050 N N   . ARG   B 141 ? 0.1408 0.1262 0.2644 -0.0055 0.0096  0.0050  141 ARG   B N   
6051 C CA  . ARG   B 141 ? 0.1517 0.1271 0.3026 -0.0108 0.0198  -0.0047 141 ARG   B CA  
6052 C C   . ARG   B 141 ? 0.1404 0.1310 0.2886 -0.0110 0.0049  0.0011  141 ARG   B C   
6053 O O   . ARG   B 141 ? 0.1471 0.1285 0.2993 -0.0138 -0.0036 -0.0105 141 ARG   B O   
6054 C CB  . ARG   B 141 ? 0.1656 0.1328 0.3367 -0.0156 0.0318  0.0040  141 ARG   B CB  
6055 C CG  . ARG   B 141 ? 0.1972 0.1541 0.3575 -0.0239 0.0277  0.0080  141 ARG   B CG  
6056 C CD  . ARG   B 141 ? 0.2423 0.1758 0.3613 -0.0168 0.0060  -0.0035 141 ARG   B CD  
6057 N NE  . ARG   B 141 ? 0.2667 0.1797 0.3540 -0.0372 0.0095  -0.0147 141 ARG   B NE  
6058 C CZ  . ARG   B 141 ? 0.2834 0.1678 0.3286 -0.0295 0.0151  -0.0212 141 ARG   B CZ  
6059 N NH1 . ARG   B 141 ? 0.2933 0.1585 0.3148 -0.0337 0.0159  -0.0186 141 ARG   B NH1 
6060 N NH2 . ARG   B 141 ? 0.2864 0.1759 0.3364 -0.0186 0.0050  -0.0183 141 ARG   B NH2 
6074 N N   . VAL   B 142 ? 0.1470 0.1239 0.2693 -0.0085 0.0128  -0.0009 142 VAL   B N   
6075 C CA  . VAL   B 142 ? 0.1403 0.1251 0.2721 -0.0017 0.0146  0.0025  142 VAL   B CA  
6076 C C   . VAL   B 142 ? 0.1421 0.1229 0.2683 -0.0047 0.0053  -0.0072 142 VAL   B C   
6077 O O   . VAL   B 142 ? 0.1459 0.1184 0.2919 0.0011  0.0095  0.0026  142 VAL   B O   
6078 C CB  . VAL   B 142 ? 0.1521 0.1388 0.2777 0.0041  0.0211  0.0088  142 VAL   B CB  
6079 C CG1 . VAL   B 142 ? 0.1492 0.1317 0.2854 0.0063  0.0227  0.0067  142 VAL   B CG1 
6080 C CG2 . VAL   B 142 ? 0.1741 0.1437 0.2733 0.0032  0.0213  0.0093  142 VAL   B CG2 
6090 N N   . CYS   B 143 ? 0.1431 0.1249 0.2536 -0.0004 0.0076  0.0040  143 CYS   B N   
6091 C CA  . CYS   B 143 ? 0.1411 0.1277 0.2473 -0.0058 0.0036  0.0012  143 CYS   B CA  
6092 C C   . CYS   B 143 ? 0.1352 0.1340 0.2426 -0.0010 0.0042  -0.0067 143 CYS   B C   
6093 O O   . CYS   B 143 ? 0.1357 0.1337 0.2449 -0.0045 -0.0099 0.0005  143 CYS   B O   
6094 C CB  . CYS   B 143 ? 0.1469 0.1333 0.2427 -0.0084 0.0001  -0.0021 143 CYS   B CB  
6095 S SG  . CYS   B 143 ? 0.1463 0.1489 0.2357 -0.0045 0.0017  0.0043  143 CYS   B SG  
6101 N N   . VAL   B 144 ? 0.1478 0.1291 0.2506 -0.0079 -0.0017 -0.0197 144 VAL   B N   
6102 C CA  . VAL   B 144 ? 0.1533 0.1353 0.2806 -0.0147 -0.0187 -0.0205 144 VAL   B CA  
6103 C C   . VAL   B 144 ? 0.1450 0.1362 0.2860 -0.0082 -0.0128 -0.0022 144 VAL   B C   
6104 O O   . VAL   B 144 ? 0.1546 0.1580 0.3026 0.0007  -0.0088 0.0191  144 VAL   B O   
6105 C CB  . VAL   B 144 ? 0.1770 0.1550 0.3443 -0.0133 -0.0230 -0.0255 144 VAL   B CB  
6106 C CG1 . VAL   B 144 ? 0.2025 0.2010 0.3792 -0.0063 -0.0287 -0.0251 144 VAL   B CG1 
6107 C CG2 . VAL   B 144 ? 0.1876 0.1543 0.3292 -0.0029 -0.0331 -0.0311 144 VAL   B CG2 
6117 N N   . ASP   B 145 ? 0.1413 0.1291 0.2994 -0.0059 -0.0117 -0.0164 145 ASP   B N   
6118 C CA  . ASP   B 145 ? 0.1491 0.1359 0.3240 -0.0066 0.0043  -0.0106 145 ASP   B CA  
6119 C C   . ASP   B 145 ? 0.1433 0.1401 0.3083 -0.0070 0.0055  -0.0095 145 ASP   B C   
6120 O O   . ASP   B 145 ? 0.1455 0.1559 0.3625 -0.0086 0.0057  -0.0266 145 ASP   B O   
6121 C CB  . ASP   B 145 ? 0.1640 0.1471 0.3756 -0.0161 0.0123  -0.0046 145 ASP   B CB  
6122 C CG  . ASP   B 145 ? 0.1718 0.1463 0.4236 -0.0218 0.0192  -0.0062 145 ASP   B CG  
6123 O OD1 . ASP   B 145 ? 0.1753 0.1504 0.4341 -0.0264 -0.0180 -0.0247 145 ASP   B OD1 
6124 O OD2 . ASP   B 145 ? 0.2029 0.1539 0.4686 -0.0267 0.0460  0.0012  145 ASP   B OD2 
6129 N N   . THR   B 146 ? 0.1367 0.1271 0.2646 -0.0128 0.0041  0.0065  146 THR   B N   
6130 C CA  . THR   B 146 ? 0.1429 0.1280 0.2504 -0.0060 0.0085  0.0009  146 THR   B CA  
6131 C C   . THR   B 146 ? 0.1387 0.1237 0.2351 -0.0039 -0.0027 -0.0042 146 THR   B C   
6132 O O   . THR   B 146 ? 0.1452 0.1235 0.2444 -0.0033 -0.0087 0.0025  146 THR   B O   
6133 C CB  . THR   B 146 ? 0.1426 0.1377 0.2548 -0.0021 0.0192  0.0069  146 THR   B CB  
6134 O OG1 . THR   B 146 ? 0.1434 0.1350 0.2621 -0.0054 0.0173  0.0157  146 THR   B OG1 
6135 C CG2 . THR   B 146 ? 0.1529 0.1338 0.2462 -0.0033 0.0190  0.0036  146 THR   B CG2 
6143 N N   . VAL   B 147 ? 0.1436 0.1297 0.2261 -0.0046 0.0054  0.0023  147 VAL   B N   
6144 C CA  . VAL   B 147 ? 0.1449 0.1303 0.2151 -0.0076 0.0007  -0.0015 147 VAL   B CA  
6145 C C   . VAL   B 147 ? 0.1375 0.1342 0.2261 -0.0145 -0.0153 -0.0040 147 VAL   B C   
6146 O O   . VAL   B 147 ? 0.1498 0.1434 0.2357 -0.0194 -0.0327 -0.0126 147 VAL   B O   
6147 C CB  . VAL   B 147 ? 0.1497 0.1399 0.2038 -0.0019 -0.0110 0.0081  147 VAL   B CB  
6148 C CG1 . VAL   B 147 ? 0.1502 0.1521 0.2064 -0.0105 -0.0081 0.0132  147 VAL   B CG1 
6149 C CG2 . VAL   B 147 ? 0.1606 0.1439 0.2038 -0.0088 -0.0060 0.0121  147 VAL   B CG2 
6159 N N   . ARG   B 148 ? 0.1434 0.1323 0.2191 -0.0074 -0.0246 -0.0110 148 ARG   B N   
6160 C CA  . ARG   B 148 ? 0.1509 0.1433 0.2168 -0.0092 -0.0300 -0.0105 148 ARG   B CA  
6161 C C   . ARG   B 148 ? 0.1532 0.1560 0.1993 -0.0109 -0.0292 -0.0055 148 ARG   B C   
6162 O O   . ARG   B 148 ? 0.1722 0.1795 0.2051 -0.0219 -0.0429 -0.0015 148 ARG   B O   
6163 C CB  . ARG   B 148 ? 0.1587 0.1440 0.2279 -0.0100 -0.0351 -0.0195 148 ARG   B CB  
6164 C CG  . ARG   B 148 ? 0.1563 0.1628 0.2418 -0.0053 -0.0306 -0.0300 148 ARG   B CG  
6165 C CD  . ARG   B 148 ? 0.1613 0.1786 0.2469 0.0056  -0.0378 -0.0333 148 ARG   B CD  
6166 N NE  . ARG   B 148 ? 0.1654 0.1713 0.2383 0.0229  -0.0348 -0.0347 148 ARG   B NE  
6167 C CZ  . ARG   B 148 ? 0.1585 0.1659 0.2174 0.0116  -0.0230 -0.0252 148 ARG   B CZ  
6168 N NH1 . ARG   B 148 ? 0.1490 0.1714 0.2200 -0.0038 -0.0032 -0.0192 148 ARG   B NH1 
6169 N NH2 . ARG   B 148 ? 0.1774 0.1556 0.2176 0.0091  -0.0158 -0.0108 148 ARG   B NH2 
6183 N N   . THR   B 149 ? 0.1564 0.1434 0.2091 -0.0132 -0.0288 -0.0017 149 THR   B N   
6184 C CA  . THR   B 149 ? 0.1608 0.1464 0.2016 -0.0186 -0.0262 0.0099  149 THR   B CA  
6185 C C   . THR   B 149 ? 0.1584 0.1482 0.1869 -0.0143 -0.0282 0.0020  149 THR   B C   
6186 O O   . THR   B 149 ? 0.1607 0.1476 0.2035 -0.0154 -0.0160 0.0019  149 THR   B O   
6187 C CB  . THR   B 149 ? 0.1647 0.1436 0.2064 -0.0164 -0.0291 0.0030  149 THR   B CB  
6188 O OG1 . THR   B 149 ? 0.1695 0.1408 0.1961 -0.0257 -0.0340 -0.0000 149 THR   B OG1 
6189 C CG2 . THR   B 149 ? 0.1665 0.1429 0.2174 -0.0047 -0.0197 0.0068  149 THR   B CG2 
6197 N N   . ASN   B 150 ? 0.1668 0.1407 0.1940 -0.0170 -0.0315 0.0014  150 ASN   B N   
6198 C CA  . ASN   B 150 ? 0.1759 0.1551 0.1917 -0.0204 -0.0272 -0.0053 150 ASN   B CA  
6199 C C   . ASN   B 150 ? 0.1683 0.1427 0.1946 -0.0123 -0.0283 -0.0011 150 ASN   B C   
6200 O O   . ASN   B 150 ? 0.1727 0.1462 0.2139 -0.0241 -0.0466 -0.0079 150 ASN   B O   
6201 C CB  . ASN   B 150 ? 0.1956 0.1933 0.1919 -0.0181 -0.0383 0.0092  150 ASN   B CB  
6202 C CG  . ASN   B 150 ? 0.2188 0.2356 0.2270 -0.0198 -0.0371 0.0249  150 ASN   B CG  
6203 O OD1 . ASN   B 150 ? 0.2291 0.2545 0.2396 -0.0300 -0.0557 0.0156  150 ASN   B OD1 
6204 N ND2 . ASN   B 150 ? 0.2277 0.2579 0.2626 -0.0117 -0.0462 0.0651  150 ASN   B ND2 
6211 N N   . VAL   B 151 ? 0.1594 0.1477 0.1840 -0.0211 -0.0247 -0.0008 151 VAL   B N   
6212 C CA  . VAL   B 151 ? 0.1602 0.1482 0.1825 -0.0243 -0.0279 -0.0038 151 VAL   B CA  
6213 C C   . VAL   B 151 ? 0.1596 0.1472 0.1782 -0.0297 -0.0352 -0.0094 151 VAL   B C   
6214 O O   . VAL   B 151 ? 0.1669 0.1527 0.2054 -0.0254 -0.0229 -0.0105 151 VAL   B O   
6215 C CB  . VAL   B 151 ? 0.1789 0.1621 0.1928 -0.0083 -0.0235 -0.0024 151 VAL   B CB  
6216 C CG1 . VAL   B 151 ? 0.1831 0.1566 0.2197 -0.0140 -0.0044 -0.0141 151 VAL   B CG1 
6217 C CG2 . VAL   B 151 ? 0.1917 0.1729 0.1767 0.0044  -0.0209 0.0078  151 VAL   B CG2 
6227 N N   . TYR   B 152 ? 0.1555 0.1327 0.1785 -0.0211 -0.0267 -0.0071 152 TYR   B N   
6228 C CA  . TYR   B 152 ? 0.1629 0.1474 0.1686 -0.0238 -0.0124 -0.0099 152 TYR   B CA  
6229 C C   . TYR   B 152 ? 0.1582 0.1363 0.1610 -0.0235 -0.0103 -0.0165 152 TYR   B C   
6230 O O   . TYR   B 152 ? 0.1608 0.1385 0.1688 -0.0223 -0.0112 -0.0023 152 TYR   B O   
6231 C CB  . TYR   B 152 ? 0.1740 0.1613 0.1723 -0.0221 -0.0171 0.0046  152 TYR   B CB  
6232 C CG  . TYR   B 152 ? 0.1915 0.1773 0.1714 -0.0342 -0.0195 0.0015  152 TYR   B CG  
6233 C CD1 . TYR   B 152 ? 0.2060 0.1893 0.1517 -0.0290 -0.0262 0.0045  152 TYR   B CD1 
6234 C CD2 . TYR   B 152 ? 0.2110 0.1942 0.1728 -0.0328 -0.0105 -0.0062 152 TYR   B CD2 
6235 C CE1 . TYR   B 152 ? 0.2170 0.2058 0.1675 -0.0277 -0.0342 0.0270  152 TYR   B CE1 
6236 C CE2 . TYR   B 152 ? 0.2197 0.2152 0.1712 -0.0367 -0.0167 -0.0059 152 TYR   B CE2 
6237 C CZ  . TYR   B 152 ? 0.2251 0.2291 0.1584 -0.0328 -0.0459 0.0206  152 TYR   B CZ  
6238 O OH  . TYR   B 152 ? 0.2459 0.2659 0.1954 -0.0262 -0.0427 0.0172  152 TYR   B OH  
6248 N N   . LEU   B 153 ? 0.1598 0.1353 0.1724 -0.0275 -0.0142 -0.0089 153 LEU   B N   
6249 C CA  . LEU   B 153 ? 0.1638 0.1296 0.1687 -0.0210 -0.0019 -0.0071 153 LEU   B CA  
6250 C C   . LEU   B 153 ? 0.1629 0.1312 0.1740 -0.0245 -0.0050 -0.0172 153 LEU   B C   
6251 O O   . LEU   B 153 ? 0.1783 0.1493 0.1850 -0.0164 -0.0087 -0.0284 153 LEU   B O   
6252 C CB  . LEU   B 153 ? 0.1630 0.1302 0.1787 -0.0178 -0.0042 0.0009  153 LEU   B CB  
6253 C CG  . LEU   B 153 ? 0.1567 0.1346 0.2068 -0.0189 -0.0069 0.0015  153 LEU   B CG  
6254 C CD1 . LEU   B 153 ? 0.1642 0.1483 0.2146 -0.0252 -0.0011 0.0095  153 LEU   B CD1 
6255 C CD2 . LEU   B 153 ? 0.1521 0.1525 0.2074 -0.0207 0.0114  -0.0005 153 LEU   B CD2 
6267 N N   . ALA   B 154 ? 0.1544 0.1300 0.1855 -0.0087 -0.0148 -0.0101 154 ALA   B N   
6268 C CA  . ALA   B 154 ? 0.1670 0.1386 0.2027 -0.0006 -0.0108 -0.0198 154 ALA   B CA  
6269 C C   . ALA   B 154 ? 0.1815 0.1407 0.2075 0.0042  -0.0245 -0.0320 154 ALA   B C   
6270 O O   . ALA   B 154 ? 0.2119 0.1420 0.2305 0.0094  -0.0135 -0.0151 154 ALA   B O   
6271 C CB  . ALA   B 154 ? 0.1640 0.1593 0.2249 -0.0038 -0.0071 -0.0269 154 ALA   B CB  
6277 N N   . VAL   B 155 ? 0.1510 0.1327 0.2182 0.0002  -0.0014 -0.0159 155 VAL   B N   
6278 C CA  . VAL   B 155 ? 0.1462 0.1349 0.2358 0.0009  -0.0117 -0.0142 155 VAL   B CA  
6279 C C   . VAL   B 155 ? 0.1447 0.1384 0.2284 -0.0044 -0.0076 -0.0141 155 VAL   B C   
6280 O O   . VAL   B 155 ? 0.1608 0.1580 0.2646 0.0039  -0.0056 -0.0342 155 VAL   B O   
6281 C CB  . VAL   B 155 ? 0.1466 0.1509 0.2780 -0.0053 -0.0202 -0.0031 155 VAL   B CB  
6282 C CG1 . VAL   B 155 ? 0.1530 0.1457 0.2823 -0.0137 -0.0186 -0.0041 155 VAL   B CG1 
6283 C CG2 . VAL   B 155 ? 0.1417 0.1623 0.3165 -0.0126 -0.0143 0.0315  155 VAL   B CG2 
6293 N N   . PHE   B 156 ? 0.1363 0.1509 0.2460 0.0031  -0.0033 -0.0110 156 PHE   B N   
6294 C CA  . PHE   B 156 ? 0.1426 0.1567 0.2902 0.0074  -0.0089 -0.0099 156 PHE   B CA  
6295 C C   . PHE   B 156 ? 0.1369 0.1600 0.3178 0.0119  -0.0175 -0.0411 156 PHE   B C   
6296 O O   . PHE   B 156 ? 0.1677 0.1805 0.3527 0.0242  -0.0013 -0.0409 156 PHE   B O   
6297 C CB  . PHE   B 156 ? 0.1513 0.1526 0.2907 0.0015  -0.0149 -0.0024 156 PHE   B CB  
6298 C CG  . PHE   B 156 ? 0.1498 0.1570 0.3030 0.0028  -0.0169 0.0077  156 PHE   B CG  
6299 C CD1 . PHE   B 156 ? 0.1513 0.1817 0.3393 0.0081  -0.0008 0.0395  156 PHE   B CD1 
6300 C CD2 . PHE   B 156 ? 0.1623 0.1754 0.2982 0.0088  -0.0249 0.0060  156 PHE   B CD2 
6301 C CE1 . PHE   B 156 ? 0.1582 0.2001 0.3565 0.0040  0.0013  0.0397  156 PHE   B CE1 
6302 C CE2 . PHE   B 156 ? 0.1673 0.1966 0.3240 0.0106  -0.0229 0.0095  156 PHE   B CE2 
6303 C CZ  . PHE   B 156 ? 0.1520 0.1995 0.3493 0.0108  -0.0211 0.0219  156 PHE   B CZ  
6313 N N   . ASP   B 157 ? 0.1447 0.1462 0.3513 0.0078  -0.0214 -0.0235 157 ASP   B N   
6314 C CA  . ASP   B 157 ? 0.1521 0.1578 0.3789 0.0042  -0.0188 -0.0311 157 ASP   B CA  
6315 C C   . ASP   B 157 ? 0.1551 0.1482 0.3743 0.0052  -0.0181 -0.0448 157 ASP   B C   
6316 O O   . ASP   B 157 ? 0.1480 0.1555 0.3509 0.0049  -0.0164 -0.0346 157 ASP   B O   
6317 C CB  . ASP   B 157 ? 0.1837 0.1805 0.3968 0.0000  -0.0327 -0.0160 157 ASP   B CB  
6318 C CG  . ASP   B 157 ? 0.2152 0.1891 0.4159 -0.0024 -0.0261 -0.0211 157 ASP   B CG  
6319 O OD1 . ASP   B 157 ? 0.2268 0.1751 0.4284 0.0092  -0.0306 -0.0132 157 ASP   B OD1 
6320 O OD2 . ASP   B 157 ? 0.2438 0.2166 0.4446 -0.0028 -0.0028 -0.0199 157 ASP   B OD2 
6325 N N   . LYS   B 158 ? 0.1599 0.1763 0.3894 0.0036  -0.0090 -0.0605 158 LYS   B N   
6326 C CA  . LYS   B 158 ? 0.1759 0.1934 0.4043 0.0034  -0.0013 -0.0829 158 LYS   B CA  
6327 C C   . LYS   B 158 ? 0.1751 0.1808 0.4102 0.0100  -0.0063 -0.0824 158 LYS   B C   
6328 O O   . LYS   B 158 ? 0.1796 0.1799 0.4161 0.0002  -0.0075 -0.0858 158 LYS   B O   
6329 C CB  . LYS   B 158 ? 0.2019 0.2390 0.4082 0.0035  0.0107  -0.1033 158 LYS   B CB  
6330 C CG  . LYS   B 158 ? 0.2476 0.2861 0.4151 0.0084  0.0231  -0.1076 158 LYS   B CG  
6331 C CD  . LYS   B 158 ? 0.2743 0.3322 0.4295 0.0066  0.0307  -0.1069 158 LYS   B CD  
6332 C CE  . LYS   B 158 ? 0.2916 0.3646 0.4473 0.0075  0.0325  -0.1039 158 LYS   B CE  
6333 N NZ  . LYS   B 158 ? 0.2946 0.3763 0.4486 0.0048  0.0354  -0.1030 158 LYS   B NZ  
6347 N N   . ASN   B 159 ? 0.1726 0.1712 0.4306 0.0106  -0.0158 -0.0661 159 ASN   B N   
6348 C CA  . ASN   B 159 ? 0.1866 0.1666 0.4504 0.0160  -0.0360 -0.0512 159 ASN   B CA  
6349 C C   . ASN   B 159 ? 0.1691 0.1525 0.4423 0.0126  -0.0510 -0.0397 159 ASN   B C   
6350 O O   . ASN   B 159 ? 0.1750 0.1456 0.4520 -0.0011 -0.0613 -0.0250 159 ASN   B O   
6351 C CB  . ASN   B 159 ? 0.2149 0.1806 0.4809 0.0262  -0.0411 -0.0418 159 ASN   B CB  
6352 C CG  . ASN   B 159 ? 0.2449 0.2027 0.5064 0.0300  -0.0497 -0.0577 159 ASN   B CG  
6353 O OD1 . ASN   B 159 ? 0.2566 0.2125 0.5070 0.0358  -0.0500 -0.0732 159 ASN   B OD1 
6354 N ND2 . ASN   B 159 ? 0.2515 0.2116 0.5236 0.0390  -0.0532 -0.0491 159 ASN   B ND2 
6361 N N   . LEU   B 160 ? 0.1620 0.1494 0.4180 0.0025  -0.0389 -0.0381 160 LEU   B N   
6362 C CA  . LEU   B 160 ? 0.1600 0.1570 0.3793 0.0044  -0.0305 -0.0207 160 LEU   B CA  
6363 C C   . LEU   B 160 ? 0.1588 0.1428 0.3611 -0.0022 -0.0234 -0.0292 160 LEU   B C   
6364 O O   . LEU   B 160 ? 0.1495 0.1502 0.3478 -0.0024 -0.0245 -0.0258 160 LEU   B O   
6365 C CB  . LEU   B 160 ? 0.1524 0.1653 0.3571 0.0009  -0.0341 -0.0111 160 LEU   B CB  
6366 C CG  . LEU   B 160 ? 0.1591 0.1738 0.3250 0.0065  -0.0317 -0.0075 160 LEU   B CG  
6367 C CD1 . LEU   B 160 ? 0.1746 0.1918 0.3150 -0.0036 -0.0110 -0.0077 160 LEU   B CD1 
6368 C CD2 . LEU   B 160 ? 0.1692 0.1755 0.3237 0.0196  -0.0393 -0.0131 160 LEU   B CD2 
6380 N N   . TYR   B 161 ? 0.1545 0.1480 0.3603 -0.0065 -0.0009 -0.0356 161 TYR   B N   
6381 C CA  . TYR   B 161 ? 0.1663 0.1442 0.3467 -0.0134 0.0178  -0.0494 161 TYR   B CA  
6382 C C   . TYR   B 161 ? 0.1670 0.1471 0.3268 -0.0086 0.0137  -0.0448 161 TYR   B C   
6383 O O   . TYR   B 161 ? 0.1718 0.1488 0.3165 -0.0126 0.0050  -0.0425 161 TYR   B O   
6384 C CB  . TYR   B 161 ? 0.1807 0.1601 0.3474 -0.0202 0.0347  -0.0492 161 TYR   B CB  
6385 C CG  . TYR   B 161 ? 0.2028 0.1648 0.3363 -0.0291 0.0487  -0.0560 161 TYR   B CG  
6386 C CD1 . TYR   B 161 ? 0.2091 0.1617 0.3291 -0.0391 0.0494  -0.0545 161 TYR   B CD1 
6387 C CD2 . TYR   B 161 ? 0.2288 0.1792 0.3352 -0.0313 0.0360  -0.0548 161 TYR   B CD2 
6388 C CE1 . TYR   B 161 ? 0.2307 0.1833 0.3343 -0.0486 0.0442  -0.0547 161 TYR   B CE1 
6389 C CE2 . TYR   B 161 ? 0.2444 0.1957 0.3393 -0.0356 0.0327  -0.0552 161 TYR   B CE2 
6390 C CZ  . TYR   B 161 ? 0.2436 0.1965 0.3353 -0.0515 0.0322  -0.0476 161 TYR   B CZ  
6391 O OH  . TYR   B 161 ? 0.2715 0.2239 0.3588 -0.0527 0.0313  -0.0456 161 TYR   B OH  
6401 N N   . ASP   B 162 ? 0.1697 0.1506 0.3428 -0.0071 -0.0010 -0.0540 162 ASP   B N   
6402 C CA  . ASP   B 162 ? 0.1831 0.1539 0.3440 -0.0066 0.0003  -0.0558 162 ASP   B CA  
6403 C C   . ASP   B 162 ? 0.1799 0.1403 0.3354 -0.0142 -0.0098 -0.0479 162 ASP   B C   
6404 O O   . ASP   B 162 ? 0.1876 0.1522 0.3335 -0.0173 -0.0193 -0.0381 162 ASP   B O   
6405 C CB  . ASP   B 162 ? 0.2014 0.1765 0.3658 0.0053  -0.0075 -0.0690 162 ASP   B CB  
6406 C CG  . ASP   B 162 ? 0.2040 0.2070 0.3900 0.0124  -0.0075 -0.0795 162 ASP   B CG  
6407 O OD1 . ASP   B 162 ? 0.2029 0.2273 0.3731 0.0061  0.0067  -0.0833 162 ASP   B OD1 
6408 O OD2 . ASP   B 162 ? 0.2184 0.2262 0.4257 0.0245  -0.0005 -0.0807 162 ASP   B OD2 
6413 N N   A LYS   B 163 ? 0.1763 0.1286 0.3214 -0.0106 -0.0256 -0.0314 163 LYS   B N   
6414 N N   B LYS   B 163 ? 0.1831 0.1440 0.3260 -0.0128 -0.0195 -0.0308 163 LYS   B N   
6415 C CA  A LYS   B 163 ? 0.1837 0.1385 0.3205 -0.0157 -0.0274 -0.0102 163 LYS   B CA  
6416 C CA  B LYS   B 163 ? 0.1914 0.1592 0.3260 -0.0162 -0.0200 -0.0120 163 LYS   B CA  
6417 C C   A LYS   B 163 ? 0.1577 0.1351 0.3121 -0.0143 -0.0283 -0.0033 163 LYS   B C   
6418 C C   B LYS   B 163 ? 0.1658 0.1460 0.3145 -0.0153 -0.0219 -0.0041 163 LYS   B C   
6419 O O   A LYS   B 163 ? 0.1569 0.1476 0.3411 -0.0220 -0.0281 -0.0050 163 LYS   B O   
6420 O O   B LYS   B 163 ? 0.1658 0.1528 0.3354 -0.0202 -0.0231 -0.0009 163 LYS   B O   
6421 C CB  A LYS   B 163 ? 0.2188 0.1719 0.3550 -0.0178 -0.0295 0.0052  163 LYS   B CB  
6422 C CB  B LYS   B 163 ? 0.2239 0.1967 0.3560 -0.0182 -0.0209 -0.0014 163 LYS   B CB  
6423 C CG  A LYS   B 163 ? 0.2797 0.2339 0.3985 -0.0223 -0.0199 0.0099  163 LYS   B CG  
6424 C CG  B LYS   B 163 ? 0.2710 0.2452 0.3924 -0.0207 -0.0151 0.0038  163 LYS   B CG  
6425 C CD  A LYS   B 163 ? 0.3278 0.2830 0.4439 -0.0300 -0.0187 0.0032  163 LYS   B CD  
6426 C CD  B LYS   B 163 ? 0.3096 0.2891 0.4311 -0.0253 -0.0142 0.0016  163 LYS   B CD  
6427 C CE  A LYS   B 163 ? 0.3591 0.3153 0.4731 -0.0349 -0.0138 0.0046  163 LYS   B CE  
6428 C CE  B LYS   B 163 ? 0.3341 0.3191 0.4589 -0.0292 -0.0106 0.0041  163 LYS   B CE  
6429 N NZ  A LYS   B 163 ? 0.3797 0.3279 0.4942 -0.0375 -0.0111 0.0036  163 LYS   B NZ  
6430 N NZ  B LYS   B 163 ? 0.3483 0.3244 0.4780 -0.0313 -0.0090 0.0046  163 LYS   B NZ  
6457 N N   . LEU   B 164 ? 0.1504 0.1343 0.2960 -0.0162 -0.0155 -0.0058 164 LEU   B N   
6458 C CA  . LEU   B 164 ? 0.1556 0.1369 0.2756 -0.0110 -0.0246 -0.0047 164 LEU   B CA  
6459 C C   . LEU   B 164 ? 0.1593 0.1391 0.2844 -0.0179 -0.0363 -0.0053 164 LEU   B C   
6460 O O   . LEU   B 164 ? 0.1593 0.1596 0.3054 -0.0182 -0.0311 -0.0039 164 LEU   B O   
6461 C CB  . LEU   B 164 ? 0.1484 0.1411 0.2572 -0.0122 -0.0176 0.0004  164 LEU   B CB  
6462 C CG  . LEU   B 164 ? 0.1528 0.1550 0.2708 -0.0076 -0.0120 0.0011  164 LEU   B CG  
6463 C CD1 . LEU   B 164 ? 0.1629 0.1577 0.2673 -0.0162 -0.0213 -0.0043 164 LEU   B CD1 
6464 C CD2 . LEU   B 164 ? 0.1704 0.1909 0.2897 -0.0020 0.0003  -0.0093 164 LEU   B CD2 
6477 N N   . VAL   B 165 ? 0.1915 0.1454 0.3098 -0.0219 -0.0447 -0.0090 165 VAL   B N   
6478 C CA  . VAL   B 165 ? 0.2273 0.1565 0.3195 -0.0292 -0.0552 -0.0100 165 VAL   B CA  
6479 C C   . VAL   B 165 ? 0.2543 0.1684 0.3413 -0.0334 -0.0808 -0.0085 165 VAL   B C   
6480 O O   . VAL   B 165 ? 0.2743 0.1775 0.3480 -0.0420 -0.0873 -0.0004 165 VAL   B O   
6481 C CB  . VAL   B 165 ? 0.2488 0.1762 0.3129 -0.0131 -0.0220 -0.0216 165 VAL   B CB  
6482 C CG1 . VAL   B 165 ? 0.2650 0.1796 0.3295 -0.0208 -0.0039 -0.0151 165 VAL   B CG1 
6483 C CG2 . VAL   B 165 ? 0.2420 0.1847 0.2947 -0.0108 -0.0155 -0.0164 165 VAL   B CG2 
6493 N N   . SER   B 166 ? 0.2569 0.1574 0.3695 -0.0360 -0.0884 -0.0319 166 SER   B N   
6494 C CA  . SER   B 166 ? 0.2486 0.1636 0.4227 -0.0364 -0.0768 -0.0403 166 SER   B CA  
6495 C C   . SER   B 166 ? 0.2320 0.1660 0.4411 -0.0402 -0.0807 -0.0160 166 SER   B C   
6496 O O   . SER   B 166 ? 0.2384 0.1911 0.4771 -0.0480 -0.0956 -0.0378 166 SER   B O   
6497 C CB  . SER   B 166 ? 0.2473 0.1734 0.4507 -0.0261 -0.0653 -0.0437 166 SER   B CB  
6498 O OG  . SER   B 166 ? 0.2376 0.1659 0.4612 -0.0201 -0.0677 -0.0276 166 SER   B OG  
6504 N N   . SER   B 167 ? 0.2091 0.1606 0.4018 -0.0388 -0.0878 0.0267  167 SER   B N   
6505 C CA  . SER   B 167 ? 0.2057 0.1690 0.3882 -0.0333 -0.0603 0.0298  167 SER   B CA  
6506 C C   . SER   B 167 ? 0.1994 0.1776 0.3699 -0.0431 -0.0626 0.0454  167 SER   B C   
6507 O O   . SER   B 167 ? 0.2075 0.1877 0.3596 -0.0495 -0.0549 0.0434  167 SER   B O   
6508 C CB  . SER   B 167 ? 0.1960 0.1767 0.3891 -0.0259 -0.0303 0.0238  167 SER   B CB  
6509 O OG  . SER   B 167 ? 0.1815 0.1846 0.3749 -0.0185 -0.0142 0.0234  167 SER   B OG  
6515 N N   . PHE   B 168 ? 0.1997 0.1747 0.3639 -0.0425 -0.0409 0.0522  168 PHE   B N   
6516 C CA  . PHE   B 168 ? 0.2064 0.1717 0.3352 -0.0465 -0.0383 0.0321  168 PHE   B CA  
6517 C C   . PHE   B 168 ? 0.1826 0.1655 0.2843 -0.0292 -0.0131 0.0141  168 PHE   B C   
6518 O O   . PHE   B 168 ? 0.2103 0.1532 0.2920 -0.0073 -0.0190 -0.0077 168 PHE   B O   
6519 C CB  . PHE   B 168 ? 0.2216 0.1747 0.3385 -0.0588 -0.0570 0.0537  168 PHE   B CB  
6520 C CG  . PHE   B 168 ? 0.2546 0.1629 0.3272 -0.0612 -0.0563 0.0310  168 PHE   B CG  
6521 C CD1 . PHE   B 168 ? 0.2849 0.1673 0.3366 -0.0580 -0.0619 0.0291  168 PHE   B CD1 
6522 C CD2 . PHE   B 168 ? 0.2412 0.1623 0.3176 -0.0531 -0.0620 0.0319  168 PHE   B CD2 
6523 C CE1 . PHE   B 168 ? 0.2979 0.1803 0.3319 -0.0417 -0.0564 0.0306  168 PHE   B CE1 
6524 C CE2 . PHE   B 168 ? 0.2708 0.1717 0.3246 -0.0380 -0.0642 0.0210  168 PHE   B CE2 
6525 C CZ  . PHE   B 168 ? 0.2869 0.1691 0.3279 -0.0305 -0.0637 0.0302  168 PHE   B CZ  
6535 N N   . LEU   B 169 ? 0.1859 0.1831 0.2764 -0.0058 -0.0010 0.0034  169 LEU   B N   
6536 C CA  . LEU   B 169 ? 0.2140 0.2074 0.3097 -0.0102 -0.0001 -0.0310 169 LEU   B CA  
6537 C C   . LEU   B 169 ? 0.2451 0.2306 0.3673 0.0054  -0.0060 -0.0540 169 LEU   B C   
6538 O O   . LEU   B 169 ? 0.2743 0.2458 0.4211 0.0002  -0.0100 -0.0755 169 LEU   B O   
6539 C CB  . LEU   B 169 ? 0.2438 0.2507 0.3231 -0.0134 -0.0116 -0.0023 169 LEU   B CB  
6540 C CG  . LEU   B 169 ? 0.2895 0.2860 0.3697 -0.0077 -0.0130 0.0077  169 LEU   B CG  
6541 C CD1 . LEU   B 169 ? 0.3073 0.3060 0.3745 -0.0045 -0.0200 0.0220  169 LEU   B CD1 
6542 C CD2 . LEU   B 169 ? 0.2886 0.2935 0.3789 0.0003  -0.0053 -0.0028 169 LEU   B CD2 
6543 O OXT . LEU   B 169 ? 0.2648 0.2438 0.3626 0.0371  -0.0008 -0.0534 169 LEU   B OXT 
6555 S S   B DMS   C .   ? 0.3208 0.3462 0.3838 0.0713  0.0987  0.0293  301 DMS   A S   
6556 O O   B DMS   C .   ? 0.3220 0.3470 0.3758 0.0707  0.1041  0.0224  301 DMS   A O   
6557 C C1  B DMS   C .   ? 0.3239 0.3465 0.3852 0.0742  0.1066  0.0217  301 DMS   A C1  
6558 C C2  B DMS   C .   ? 0.3247 0.3497 0.3914 0.0716  0.1014  0.0274  301 DMS   A C2  
6565 N N2  B A1BAG D .   ? 0.2645 0.2614 0.2010 0.0222  -0.0190 -0.0377 302 A1BAG A N2  
6566 C C3  B A1BAG D .   ? 0.2624 0.2574 0.1936 0.0275  -0.0162 -0.0418 302 A1BAG A C3  
6567 C C6  B A1BAG D .   ? 0.2572 0.2632 0.2247 0.0062  -0.0204 -0.0111 302 A1BAG A C6  
6568 C C9  B A1BAG D .   ? 0.2510 0.2566 0.2328 0.0024  -0.0128 -0.0064 302 A1BAG A C9  
6569 C C12 B A1BAG D .   ? 0.2242 0.2145 0.1771 -0.0226 0.0484  0.0495  302 A1BAG A C12 
6570 C C14 B A1BAG D .   ? 0.2157 0.2190 0.1882 -0.0006 0.0165  0.0385  302 A1BAG A C14 
6571 C C1  B A1BAG D .   ? 0.2723 0.2588 0.2085 0.0130  -0.0173 -0.0177 302 A1BAG A C1  
6572 C C10 B A1BAG D .   ? 0.2513 0.2513 0.2311 0.0080  -0.0150 -0.0119 302 A1BAG A C10 
6573 C C11 B A1BAG D .   ? 0.2273 0.2260 0.1817 -0.0071 0.0216  0.0271  302 A1BAG A C11 
6574 C C13 B A1BAG D .   ? 0.2108 0.2166 0.1906 -0.0057 0.0223  0.0462  302 A1BAG A C13 
6575 C C15 B A1BAG D .   ? 0.2104 0.2200 0.2006 0.0068  0.0106  0.0344  302 A1BAG A C15 
6576 C C16 B A1BAG D .   ? 0.1988 0.2209 0.2015 0.0035  0.0073  0.0364  302 A1BAG A C16 
6577 C C2  B A1BAG D .   ? 0.2668 0.2600 0.2102 0.0114  -0.0166 -0.0242 302 A1BAG A C2  
6578 C C4  B A1BAG D .   ? 0.2608 0.2604 0.2023 0.0196  -0.0243 -0.0343 302 A1BAG A C4  
6579 C C5  B A1BAG D .   ? 0.2639 0.2630 0.2146 0.0091  -0.0217 -0.0215 302 A1BAG A C5  
6580 C C7  B A1BAG D .   ? 0.2593 0.2679 0.2363 0.0050  -0.0239 -0.0056 302 A1BAG A C7  
6581 C C8  B A1BAG D .   ? 0.2603 0.2657 0.2387 0.0040  -0.0173 -0.0043 302 A1BAG A C8  
6582 N N1  B A1BAG D .   ? 0.2680 0.2621 0.2108 0.0149  -0.0117 -0.0324 302 A1BAG A N1  
6583 N N3  B A1BAG D .   ? 0.2487 0.2513 0.2180 0.0001  -0.0050 -0.0000 302 A1BAG A N3  
6584 N N4  B A1BAG D .   ? 0.2295 0.2193 0.1715 -0.0205 0.0501  0.0323  302 A1BAG A N4  
6585 N N5  B A1BAG D .   ? 0.2171 0.2166 0.1793 -0.0179 0.0403  0.0480  302 A1BAG A N5  
6586 N N6  B A1BAG D .   ? 0.2048 0.2153 0.2021 0.0062  0.0037  0.0408  302 A1BAG A N6  
6587 O O1  B A1BAG D .   ? 0.2501 0.2504 0.2244 0.0130  -0.0221 -0.0124 302 A1BAG A O1  
6608 O O   . HOH   E .   ? 0.6438 0.4321 0.3739 0.1748  -0.1546 0.0372  401 HOH   A O   
6609 O O   B HOH   E .   ? 0.3733 0.3664 0.4587 -0.0462 -0.1008 -0.0782 402 HOH   A O   
6610 O O   . HOH   E .   ? 0.3872 0.2557 0.3994 -0.0079 -0.0605 0.0340  403 HOH   A O   
6611 O O   A HOH   E .   ? 0.3253 0.2808 0.3307 0.0114  0.1074  -0.0310 404 HOH   A O   
6612 O O   . HOH   E .   ? 0.5153 0.6347 0.4401 -0.1448 -0.0984 -0.0660 405 HOH   A O   
6613 O O   . HOH   E .   ? 0.3145 0.3425 0.1634 -0.0591 0.0467  0.0323  406 HOH   A O   
6614 O O   . HOH   E .   ? 0.5354 0.3480 0.3077 -0.1438 -0.1136 0.0171  407 HOH   A O   
6615 O O   . HOH   E .   ? 0.2102 0.2332 0.2644 -0.0228 -0.0197 0.0788  408 HOH   A O   
6616 O O   . HOH   E .   ? 0.2395 0.1934 0.2362 0.0366  -0.0317 -0.0067 409 HOH   A O   
6617 O O   A HOH   E .   ? 0.3095 0.5318 0.3686 -0.0415 0.0352  0.0462  410 HOH   A O   
6618 O O   . HOH   E .   ? 0.1573 0.3697 0.2800 0.0035  0.0263  0.0946  411 HOH   A O   
6619 O O   . HOH   E .   ? 0.2657 0.2913 0.4023 -0.0574 0.1008  0.0132  412 HOH   A O   
6620 O O   . HOH   E .   ? 0.3133 0.5639 0.7018 0.1189  0.0916  0.1248  413 HOH   A O   
6621 O O   . HOH   E .   ? 0.3021 0.7816 0.5343 0.0078  -0.0571 0.2296  414 HOH   A O   
6622 O O   . HOH   E .   ? 0.5433 0.2139 0.5445 0.0723  -0.0362 -0.0107 415 HOH   A O   
6623 O O   . HOH   E .   ? 0.5053 0.3639 0.4688 -0.0014 0.1518  0.0861  416 HOH   A O   
6624 O O   . HOH   E .   ? 0.2159 0.1887 0.3685 -0.0338 0.0042  -0.0253 417 HOH   A O   
6625 O O   . HOH   E .   ? 0.1852 0.3946 0.3356 0.0507  -0.0211 0.0546  418 HOH   A O   
6626 O O   . HOH   E .   ? 0.7457 0.5284 0.3657 -0.0318 -0.0578 0.1012  419 HOH   A O   
6627 O O   . HOH   E .   ? 0.5161 0.3121 0.3263 -0.1429 0.0776  0.0180  420 HOH   A O   
6628 O O   . HOH   E .   ? 0.2819 0.2663 0.4181 -0.0176 -0.0714 0.1129  421 HOH   A O   
6629 O O   . HOH   E .   ? 0.2367 0.2189 0.2253 0.0084  -0.0173 0.0566  422 HOH   A O   
6630 O O   . HOH   E .   ? 0.1988 0.3404 0.4295 -0.0309 0.0327  -0.0921 423 HOH   A O   
6631 O O   . HOH   E .   ? 0.3319 0.4493 0.3420 0.0045  0.0398  0.0902  424 HOH   A O   
6632 O O   . HOH   E .   ? 0.6728 0.6670 0.6109 0.0818  0.0974  -0.0411 425 HOH   A O   
6633 O O   . HOH   E .   ? 0.6778 0.6102 0.4187 0.2344  -0.0758 -0.0779 426 HOH   A O   
6634 O O   . HOH   E .   ? 0.4949 0.5576 0.2904 -0.1376 0.1384  0.0731  427 HOH   A O   
6635 O O   . HOH   E .   ? 0.4341 0.3280 0.4052 -0.0623 0.2069  -0.0089 428 HOH   A O   
6636 O O   . HOH   E .   ? 0.2725 0.2406 0.2658 -0.0306 0.0105  0.0015  429 HOH   A O   
6637 O O   . HOH   E .   ? 0.5653 0.6380 0.5341 -0.0442 0.0765  0.0851  430 HOH   A O   
6638 O O   . HOH   E .   ? 0.2859 0.5082 0.4142 -0.0059 -0.0530 0.1085  431 HOH   A O   
6639 O O   . HOH   E .   ? 0.3034 0.2804 0.2954 -0.0673 0.0312  0.0592  432 HOH   A O   
6640 O O   . HOH   E .   ? 0.7315 0.5748 0.5357 -0.0341 -0.0779 -0.0224 433 HOH   A O   
6641 O O   . HOH   E .   ? 0.2285 0.4797 0.3628 -0.0020 -0.0309 0.1715  434 HOH   A O   
6642 O O   . HOH   E .   ? 0.2540 0.2450 0.3045 0.0401  0.0286  0.0518  435 HOH   A O   
6643 O O   . HOH   E .   ? 0.1774 0.1888 0.2665 -0.0265 0.0046  0.0470  436 HOH   A O   
6644 O O   . HOH   E .   ? 0.6431 0.4072 0.3395 0.0076  0.0856  0.1408  437 HOH   A O   
6645 O O   . HOH   E .   ? 0.4561 0.2293 0.4895 0.0501  -0.1337 0.0654  438 HOH   A O   
6646 O O   A HOH   E .   ? 0.1530 0.2504 0.2144 0.0550  0.0417  0.0822  439 HOH   A O   
6647 O O   . HOH   E .   ? 0.1595 0.2280 0.2163 0.0034  -0.0007 0.0430  440 HOH   A O   
6648 O O   A HOH   E .   ? 0.4601 0.4266 0.3501 -0.0714 0.1225  0.1316  441 HOH   A O   
6649 O O   . HOH   E .   ? 0.3377 0.4430 0.4166 -0.1297 -0.1343 -0.0026 442 HOH   A O   
6650 O O   . HOH   E .   ? 0.1909 0.2045 0.3762 0.0232  0.0725  -0.0096 443 HOH   A O   
6651 O O   . HOH   E .   ? 0.4088 0.6889 0.4840 -0.0524 -0.1099 0.0211  444 HOH   A O   
6652 O O   . HOH   E .   ? 0.2850 0.4412 0.3477 -0.0557 0.0618  0.0070  445 HOH   A O   
6653 O O   . HOH   E .   ? 0.6400 0.4688 0.4765 -0.1460 -0.0730 0.2535  446 HOH   A O   
6654 O O   B HOH   E .   ? 0.2773 0.3172 0.2559 -0.0623 0.0629  -0.0744 447 HOH   A O   
6655 O O   . HOH   E .   ? 0.3113 0.3755 0.2292 -0.0937 -0.0131 -0.0696 448 HOH   A O   
6656 O O   . HOH   E .   ? 0.2495 0.1998 0.2826 -0.0197 0.0175  0.0277  449 HOH   A O   
6657 O O   . HOH   E .   ? 0.5648 0.5207 0.5364 -0.1109 -0.0744 0.1166  450 HOH   A O   
6658 O O   . HOH   E .   ? 0.4749 0.5686 0.6162 0.1882  0.1513  -0.1243 451 HOH   A O   
6659 O O   . HOH   E .   ? 0.2599 0.3943 0.3807 0.1020  -0.0940 -0.0236 452 HOH   A O   
6660 O O   . HOH   E .   ? 0.6044 0.5323 0.5367 0.1356  0.2346  -0.1160 453 HOH   A O   
6661 O O   . HOH   E .   ? 0.1527 0.2026 0.2661 0.0117  -0.0082 0.0124  454 HOH   A O   
6662 O O   . HOH   E .   ? 0.1402 0.1319 0.1463 0.0011  0.0096  0.0085  455 HOH   A O   
6663 O O   . HOH   E .   ? 0.1893 0.1801 0.2260 0.0182  -0.0201 0.0255  456 HOH   A O   
6664 O O   . HOH   E .   ? 0.6604 0.4526 0.5049 -0.0100 -0.0294 -0.0024 457 HOH   A O   
6665 O O   . HOH   E .   ? 0.3726 0.6646 0.4463 -0.0701 0.0074  0.1588  458 HOH   A O   
6666 O O   B HOH   E .   ? 0.2428 0.4319 0.4297 -0.0341 0.0030  0.1288  459 HOH   A O   
6667 O O   A HOH   E .   ? 0.1197 0.1708 0.2135 0.0160  -0.0241 -0.0321 460 HOH   A O   
6668 O O   . HOH   E .   ? 0.3755 0.2696 0.4492 -0.1287 0.0453  0.0501  461 HOH   A O   
6669 O O   . HOH   E .   ? 0.3741 0.5055 0.3871 0.2124  0.0911  0.0728  462 HOH   A O   
6670 O O   . HOH   E .   ? 0.4932 0.2631 0.4104 -0.1442 0.1819  -0.0676 463 HOH   A O   
6671 O O   . HOH   E .   ? 0.1559 0.1347 0.2410 -0.0057 0.0091  -0.0115 464 HOH   A O   
6672 O O   A HOH   E .   ? 0.1983 0.2232 0.2902 -0.0136 0.0362  0.0803  465 HOH   A O   
6673 O O   . HOH   E .   ? 0.1960 0.2020 0.2423 -0.0329 0.0045  0.0310  466 HOH   A O   
6674 O O   . HOH   E .   ? 0.3825 0.2141 0.2423 0.1008  0.0491  0.0127  467 HOH   A O   
6675 O O   . HOH   E .   ? 0.3112 0.3581 0.5630 -0.0923 -0.1150 -0.0757 468 HOH   A O   
6676 O O   . HOH   E .   ? 0.3517 0.2478 0.5088 -0.0679 -0.0314 0.0438  469 HOH   A O   
6677 O O   B HOH   E .   ? 0.5062 0.3464 0.4490 0.0927  -0.0693 -0.0314 470 HOH   A O   
6678 O O   . HOH   E .   ? 0.1521 0.1559 0.1646 -0.0031 -0.0095 -0.0055 471 HOH   A O   
6679 O O   . HOH   E .   ? 0.6786 0.5461 0.6207 0.0881  0.1800  0.2856  472 HOH   A O   
6680 O O   A HOH   E .   ? 0.1534 0.2081 0.3116 0.0268  0.0651  -0.0475 473 HOH   A O   
6681 O O   B HOH   E .   ? 0.3707 0.6000 0.2476 -0.0972 -0.0281 0.0284  474 HOH   A O   
6682 O O   . HOH   E .   ? 0.2159 0.1869 0.2590 -0.0039 -0.0611 -0.0042 475 HOH   A O   
6683 O O   . HOH   E .   ? 0.1825 0.3167 0.3791 -0.0069 0.0746  0.1024  476 HOH   A O   
6684 O O   A HOH   E .   ? 0.3211 0.1435 0.1527 0.0253  0.0275  0.0197  477 HOH   A O   
6685 O O   . HOH   E .   ? 0.2899 0.4739 0.3214 0.0398  0.0800  0.1960  478 HOH   A O   
6686 O O   A HOH   E .   ? 0.2564 0.2680 0.2831 0.0044  0.0843  -0.0002 479 HOH   A O   
6687 O O   . HOH   E .   ? 0.2135 0.2355 0.2302 -0.0210 -0.0311 0.0266  480 HOH   A O   
6688 O O   . HOH   E .   ? 0.2783 0.2180 0.1868 -0.0519 0.0259  0.0376  481 HOH   A O   
6689 O O   . HOH   E .   ? 0.6393 0.5901 0.6291 -0.1093 -0.1227 -0.0143 482 HOH   A O   
6690 O O   . HOH   E .   ? 0.3557 0.3100 0.3749 -0.0951 -0.0072 -0.0071 483 HOH   A O   
6691 O O   A HOH   E .   ? 0.1540 0.1602 0.1596 0.0144  0.0053  0.0327  484 HOH   A O   
6692 O O   . HOH   E .   ? 0.1448 0.1550 0.1924 0.0053  -0.0218 -0.0004 485 HOH   A O   
6693 O O   . HOH   E .   ? 0.2937 0.4435 0.3541 0.0610  -0.0095 0.0226  486 HOH   A O   
6694 O O   . HOH   E .   ? 0.2926 0.3123 0.2181 0.0246  0.0621  0.0022  487 HOH   A O   
6695 O O   . HOH   E .   ? 0.1911 0.2798 0.2843 0.0471  0.0438  0.1012  488 HOH   A O   
6696 O O   . HOH   E .   ? 0.1789 0.2011 0.1829 -0.0105 0.0079  0.0495  489 HOH   A O   
6697 O O   A HOH   E .   ? 0.2026 0.3769 0.3774 0.0465  0.0145  0.0958  490 HOH   A O   
6698 O O   . HOH   E .   ? 0.3674 0.3713 0.2581 -0.0072 -0.1107 0.0287  491 HOH   A O   
6699 O O   . HOH   E .   ? 0.4644 0.5899 0.6379 -0.0721 0.1901  0.2474  492 HOH   A O   
6700 O O   B HOH   E .   ? 0.3380 0.3387 0.2936 0.0184  0.0737  -0.0062 493 HOH   A O   
6701 O O   . HOH   E .   ? 0.3571 0.6631 0.3900 0.1231  0.0979  -0.1129 494 HOH   A O   
6702 O O   A HOH   E .   ? 0.2252 0.3955 0.1909 0.0964  0.0121  0.0163  495 HOH   A O   
6703 O O   . HOH   E .   ? 0.3378 0.2613 0.3501 -0.0028 -0.0346 0.0965  496 HOH   A O   
6704 O O   . HOH   E .   ? 0.1815 0.1424 0.1639 -0.0170 0.0126  0.0003  497 HOH   A O   
6705 O O   B HOH   E .   ? 0.2187 0.1931 0.2262 0.0001  -0.0518 -0.0067 498 HOH   A O   
6706 O O   . HOH   E .   ? 0.2589 0.5667 0.4667 0.0602  -0.0344 0.0984  499 HOH   A O   
6707 O O   B HOH   E .   ? 0.2523 0.3036 0.3092 -0.0928 -0.0011 -0.1108 500 HOH   A O   
6708 O O   A HOH   E .   ? 0.1146 0.1483 0.1579 0.0133  -0.0263 -0.0357 501 HOH   A O   
6709 O O   . HOH   E .   ? 0.2578 0.4001 0.4072 -0.0321 0.1101  -0.0820 502 HOH   A O   
6710 O O   . HOH   E .   ? 0.1923 0.2014 0.3901 0.0380  0.1002  0.1076  503 HOH   A O   
6711 O O   . HOH   E .   ? 0.2994 0.2929 0.2105 -0.0533 -0.0764 0.0329  504 HOH   A O   
6712 O O   . HOH   E .   ? 0.2254 0.1841 0.2962 -0.0001 -0.0418 0.0058  505 HOH   A O   
6713 O O   . HOH   E .   ? 0.2073 0.2848 0.3488 -0.0173 -0.0149 0.0284  506 HOH   A O   
6714 O O   . HOH   E .   ? 0.5154 0.4230 0.2087 -0.0192 0.0979  0.0581  507 HOH   A O   
6715 O O   B HOH   E .   ? 0.2797 0.3746 0.2864 0.0749  -0.1297 -0.0477 508 HOH   A O   
6716 O O   A HOH   E .   ? 0.3675 0.2431 0.4632 0.0695  0.0759  0.0194  509 HOH   A O   
6717 O O   . HOH   E .   ? 0.1618 0.1712 0.3223 0.0005  -0.0055 0.0251  510 HOH   A O   
6718 O O   . HOH   E .   ? 0.2616 0.2792 0.3348 -0.0040 -0.0256 -0.0447 511 HOH   A O   
6719 O O   . HOH   E .   ? 0.6438 0.7366 0.4405 0.2243  -0.0852 0.2022  512 HOH   A O   
6720 O O   . HOH   E .   ? 0.2682 0.2115 0.2552 -0.0655 -0.0072 0.0529  513 HOH   A O   
6721 O O   . HOH   E .   ? 0.5984 0.2730 0.5232 0.0731  -0.0319 -0.0668 514 HOH   A O   
6722 O O   . HOH   E .   ? 0.6576 0.3921 0.5002 0.1171  0.2296  -0.0816 515 HOH   A O   
6723 O O   A HOH   E .   ? 0.5937 0.3473 0.5201 -0.0906 0.0994  0.0234  516 HOH   A O   
6724 O O   . HOH   E .   ? 0.4294 0.6758 0.3185 -0.1108 -0.0502 0.1237  517 HOH   A O   
6725 O O   B HOH   E .   ? 0.4439 0.2084 0.2362 0.1262  -0.0167 -0.0022 518 HOH   A O   
6726 O O   . HOH   E .   ? 0.5470 0.4860 0.3367 -0.0033 -0.1341 0.0215  519 HOH   A O   
6727 O O   A HOH   E .   ? 0.1854 0.1475 0.2693 -0.0177 -0.0220 0.0414  520 HOH   A O   
6728 O O   A HOH   E .   ? 0.1838 0.1773 0.3718 0.0369  -0.0784 -0.0681 521 HOH   A O   
6729 O O   . HOH   E .   ? 0.3149 0.3813 0.7107 -0.0220 0.1006  -0.0151 522 HOH   A O   
6730 O O   . HOH   E .   ? 0.2052 0.1748 0.1536 -0.0049 0.0164  0.0159  523 HOH   A O   
6731 O O   A HOH   E .   ? 0.2412 0.2078 0.3743 -0.0239 0.0884  -0.0019 524 HOH   A O   
6732 O O   A HOH   E .   ? 0.1484 0.1286 0.1617 -0.0074 -0.0310 0.0133  525 HOH   A O   
6733 O O   . HOH   E .   ? 0.3363 0.3905 0.5366 -0.0011 0.1171  -0.0196 526 HOH   A O   
6734 O O   . HOH   E .   ? 0.6862 0.3810 0.5330 0.2064  -0.0642 0.1291  527 HOH   A O   
6735 O O   . HOH   E .   ? 0.2155 0.2919 0.2738 -0.0083 -0.0576 0.0491  528 HOH   A O   
6736 O O   . HOH   E .   ? 0.2347 0.4369 0.2475 0.1575  -0.0074 0.0150  529 HOH   A O   
6737 O O   . HOH   E .   ? 0.5560 0.6189 0.4591 0.0797  0.2763  -0.0779 530 HOH   A O   
6738 O O   . HOH   E .   ? 0.5794 0.6087 0.6521 0.0165  -0.1326 -0.0992 531 HOH   A O   
6739 O O   . HOH   E .   ? 0.3046 0.6195 0.1793 -0.0684 0.0372  -0.0144 532 HOH   A O   
6740 O O   . HOH   E .   ? 0.8053 0.7426 0.4160 -0.0639 -0.0581 0.2626  533 HOH   A O   
6741 O O   . HOH   E .   ? 0.3522 0.4551 0.3661 0.1208  -0.0558 -0.1501 534 HOH   A O   
6742 O O   . HOH   E .   ? 0.1662 0.2144 0.3031 -0.0120 0.0047  0.0559  535 HOH   A O   
6743 O O   . HOH   E .   ? 0.4296 0.2325 0.5588 -0.0846 -0.2412 0.1138  536 HOH   A O   
6744 O O   B HOH   E .   ? 0.1307 0.1968 0.2612 -0.0086 0.0250  0.0825  537 HOH   A O   
6745 O O   . HOH   E .   ? 0.3408 0.1410 0.2197 0.0048  -0.0375 0.0076  538 HOH   A O   
6746 O O   . HOH   E .   ? 0.4009 0.2909 0.3202 -0.0195 0.0102  0.0410  539 HOH   A O   
6747 O O   A HOH   E .   ? 0.2087 0.1562 0.2292 0.0323  -0.0725 -0.0467 540 HOH   A O   
6748 O O   B HOH   E .   ? 0.3182 0.2574 0.1595 0.1427  -0.0387 -0.0295 541 HOH   A O   
6749 O O   A HOH   E .   ? 0.3664 0.2013 0.3492 0.0790  0.1465  0.1045  542 HOH   A O   
6750 O O   . HOH   E .   ? 0.4625 0.2667 0.5749 0.0191  -0.0342 -0.0168 543 HOH   A O   
6751 O O   A HOH   E .   ? 0.1448 0.1489 0.2203 0.0218  -0.0251 0.0321  544 HOH   A O   
6752 O O   A HOH   E .   ? 0.3340 0.3879 0.3993 -0.0963 -0.0543 -0.1065 545 HOH   A O   
6753 O O   B HOH   E .   ? 0.2831 0.4078 0.3274 -0.1305 0.0706  -0.0291 546 HOH   A O   
6754 O O   A HOH   E .   ? 0.1792 0.1330 0.1297 -0.0048 -0.0088 -0.0081 547 HOH   A O   
6755 O O   B HOH   E .   ? 0.2968 0.2166 0.3845 0.0065  0.0921  0.0547  548 HOH   A O   
6756 O O   B HOH   E .   ? 0.2348 0.3234 0.4735 0.0154  -0.0028 -0.0673 549 HOH   A O   
6757 O O   . HOH   E .   ? 0.3562 0.2977 0.1953 -0.0864 0.0353  0.0535  550 HOH   A O   
6758 O O   . HOH   E .   ? 0.2610 0.1799 0.2875 0.0066  0.0162  0.0196  551 HOH   A O   
6759 O O   . HOH   E .   ? 0.6664 0.5244 0.7766 0.0264  -0.1347 0.1941  552 HOH   A O   
6760 O O   A HOH   E .   ? 0.2798 0.2253 0.4222 0.0059  0.1175  -0.0349 553 HOH   A O   
6761 O O   . HOH   E .   ? 0.2635 0.2169 0.2665 0.0172  0.0311  0.0252  554 HOH   A O   
6762 O O   . HOH   E .   ? 0.3822 0.3223 0.3548 0.1856  -0.0465 -0.0487 555 HOH   A O   
6763 O O   . HOH   E .   ? 0.1880 0.2448 0.5588 -0.0214 -0.0774 0.0983  556 HOH   A O   
6764 O O   . HOH   E .   ? 0.6156 0.6137 0.5565 0.0438  -0.1006 0.0133  557 HOH   A O   
6765 O O   . HOH   E .   ? 0.2251 0.2735 0.2518 0.0054  -0.0222 -0.0406 558 HOH   A O   
6766 O O   . HOH   E .   ? 0.6027 0.2851 0.5706 -0.0257 -0.0234 0.1407  559 HOH   A O   
6767 O O   A HOH   E .   ? 0.3319 0.1715 0.2812 -0.0137 0.0813  0.0637  560 HOH   A O   
6768 O O   A HOH   E .   ? 0.7249 0.6224 0.5085 -0.0025 -0.0808 -0.0196 561 HOH   A O   
6769 O O   B HOH   E .   ? 0.3419 0.4529 0.2520 0.0151  -0.0211 0.1275  562 HOH   A O   
6770 O O   B HOH   E .   ? 0.3739 0.3336 0.3163 -0.0734 -0.0953 0.0899  563 HOH   A O   
6771 O O   A HOH   E .   ? 0.2336 0.2108 0.3032 0.0518  -0.0296 0.0025  564 HOH   A O   
6772 O O   B HOH   E .   ? 0.6079 0.2795 0.3156 0.0286  -0.0049 0.0551  565 HOH   A O   
6773 O O   . HOH   E .   ? 0.4921 0.5455 0.5395 0.0231  -0.0088 0.1565  566 HOH   A O   
6774 O O   . HOH   E .   ? 0.5312 0.3456 0.5109 0.0621  0.1234  0.0154  567 HOH   A O   
6775 O O   . HOH   E .   ? 0.6393 0.5301 0.4631 -0.0623 0.0945  0.0384  568 HOH   A O   
6776 O O   . HOH   E .   ? 0.2819 0.2716 0.3783 -0.0563 0.0104  -0.0636 569 HOH   A O   
6777 O O   . HOH   E .   ? 0.8233 0.6757 0.7295 -0.0087 0.0827  -0.1293 570 HOH   A O   
6778 O O   . HOH   E .   ? 0.6248 0.7843 0.4766 0.1124  -0.0411 -0.0713 571 HOH   A O   
6779 O O   . HOH   E .   ? 0.3076 0.4966 0.5310 -0.1225 0.0595  -0.1521 572 HOH   A O   
6780 O O   . HOH   E .   ? 0.3078 0.5675 0.5626 0.0735  -0.0762 0.2245  573 HOH   A O   
6781 O O   . HOH   E .   ? 0.3176 0.3837 0.5278 -0.0276 0.0152  -0.0384 574 HOH   A O   
6782 O O   . HOH   E .   ? 0.2562 0.3032 0.3612 -0.0994 0.0372  -0.0132 575 HOH   A O   
6783 O O   . HOH   E .   ? 0.2956 0.1834 0.2561 0.0367  -0.0803 -0.0211 576 HOH   A O   
6784 O O   A HOH   E .   ? 0.2624 0.2250 0.4232 0.0611  -0.1498 -0.0515 577 HOH   A O   
6785 O O   . HOH   E .   ? 0.4189 0.5768 0.3892 -0.0953 -0.0843 0.1892  578 HOH   A O   
6786 O O   . HOH   E .   ? 0.6643 0.3554 0.7938 0.1104  0.0788  0.2400  579 HOH   A O   
6787 O O   . HOH   E .   ? 0.2996 0.3888 0.5346 0.0711  0.0049  -0.1811 580 HOH   A O   
6788 O O   . HOH   E .   ? 0.5880 0.5617 0.5278 0.0490  0.1625  0.1178  581 HOH   A O   
6789 O O   A HOH   E .   ? 0.2674 0.2556 0.3081 -0.0182 0.0027  0.0009  582 HOH   A O   
6790 O O   . HOH   E .   ? 0.3569 0.5823 0.3587 0.0193  -0.0064 -0.0328 583 HOH   A O   
6791 O O   . HOH   E .   ? 0.6151 0.6164 0.5929 0.1816  0.1172  -0.1129 584 HOH   A O   
6792 O O   . HOH   E .   ? 0.2454 0.2348 0.2794 0.0241  -0.0112 -0.0151 585 HOH   A O   
6793 O O   . HOH   E .   ? 0.5533 0.6354 0.6654 -0.1590 -0.1100 0.0512  586 HOH   A O   
6794 O O   B HOH   E .   ? 0.4421 0.4559 0.4434 -0.0901 -0.0230 -0.0418 587 HOH   A O   
6795 O O   . HOH   E .   ? 0.4618 0.4723 0.5430 -0.2007 -0.0746 -0.0123 588 HOH   A O   
6796 O O   . HOH   E .   ? 0.4446 0.2592 0.3825 -0.0648 -0.1200 0.0599  589 HOH   A O   
6797 O O   . HOH   E .   ? 0.6541 0.4896 0.6463 -0.0856 0.0627  -0.0415 590 HOH   A O   
6798 O O   B HOH   E .   ? 0.1922 0.1966 0.3479 0.0481  0.0020  0.0819  591 HOH   A O   
6799 O O   B HOH   E .   ? 0.4505 0.4895 0.4120 0.1583  -0.0371 0.0216  592 HOH   A O   
6800 O O   . HOH   E .   ? 0.7795 0.4004 0.3350 -0.0302 -0.1166 0.0036  593 HOH   A O   
6801 O O   . HOH   E .   ? 0.4502 0.4551 0.3557 -0.0441 -0.0553 -0.0345 594 HOH   A O   
6802 O O   . HOH   E .   ? 0.6659 0.5583 0.6316 0.1158  0.1180  0.1602  595 HOH   A O   
6803 O O   . HOH   E .   ? 0.4704 0.5659 0.4635 0.0681  -0.0584 -0.0851 596 HOH   A O   
6804 O O   . HOH   E .   ? 0.5644 0.4217 0.4781 0.0107  0.0155  -0.1204 597 HOH   A O   
6805 O O   . HOH   E .   ? 0.6081 0.7167 0.5142 -0.0987 0.1587  0.1004  598 HOH   A O   
6806 O O   . HOH   E .   ? 0.4426 0.4435 0.2937 -0.0299 -0.0128 -0.0071 599 HOH   A O   
6807 O O   . HOH   E .   ? 0.4573 0.3560 0.2762 -0.0850 0.1382  -0.0363 600 HOH   A O   
6808 O O   . HOH   E .   ? 0.3444 0.4278 0.4604 0.0065  0.1462  0.1003  601 HOH   A O   
6809 O O   . HOH   E .   ? 0.2952 0.5319 0.4016 0.1238  0.1144  0.2563  602 HOH   A O   
6810 O O   . HOH   E .   ? 0.5814 0.4365 0.3797 -0.0364 0.1615  -0.0184 603 HOH   A O   
6811 O O   . HOH   E .   ? 0.5220 0.5641 0.3908 -0.0229 -0.0424 -0.0619 604 HOH   A O   
6812 O O   B HOH   E .   ? 0.4210 0.5611 0.4639 0.2044  0.0742  -0.0695 605 HOH   A O   
6813 O O   B HOH   E .   ? 0.2598 0.3822 0.2418 -0.0850 -0.0537 -0.0068 606 HOH   A O   
6814 O O   . HOH   E .   ? 0.4911 0.4724 0.6249 -0.0261 -0.0977 0.0652  607 HOH   A O   
6815 O O   . HOH   E .   ? 0.2536 0.3639 0.5419 -0.0396 0.0759  -0.0866 608 HOH   A O   
6816 O O   . HOH   E .   ? 0.5130 0.3428 0.4550 -0.0249 0.2168  0.0192  609 HOH   A O   
6817 O O   . HOH   E .   ? 0.4087 0.3244 0.4365 -0.1065 0.0512  0.0693  610 HOH   A O   
6818 O O   B HOH   E .   ? 0.3387 0.2379 0.2832 -0.0763 -0.0599 0.0835  611 HOH   A O   
6819 O O   . HOH   E .   ? 0.2715 0.2749 0.6774 -0.0010 -0.1018 0.0067  612 HOH   A O   
6820 O O   . HOH   E .   ? 0.3112 0.2257 0.6591 0.0234  0.1008  0.0920  613 HOH   A O   
6821 O O   . HOH   E .   ? 0.6473 0.2744 0.4381 -0.0707 0.0352  0.0338  614 HOH   A O   
6822 O O   . HOH   E .   ? 0.3561 0.8625 0.6026 -0.1151 -0.0399 0.2648  615 HOH   A O   
6823 O O   . HOH   E .   ? 0.5001 0.2468 0.4336 -0.1373 -0.0059 0.0539  616 HOH   A O   
6824 O O   . HOH   E .   ? 0.2450 0.2946 0.3802 0.0178  -0.0476 0.0613  617 HOH   A O   
6825 O O   . HOH   E .   ? 0.3458 0.3976 0.4841 0.0916  0.0682  0.0731  618 HOH   A O   
6826 O O   . HOH   E .   ? 0.5432 0.7835 0.5665 0.0956  -0.1015 0.1379  619 HOH   A O   
6827 O O   . HOH   E .   ? 0.6960 0.4616 0.5394 0.0752  0.0004  0.0564  620 HOH   A O   
6828 O O   . HOH   E .   ? 0.6860 0.5085 0.4705 0.1715  -0.1520 -0.0101 621 HOH   A O   
6829 O O   B HOH   E .   ? 0.4971 0.3955 0.4359 -0.0062 -0.1024 0.0595  622 HOH   A O   
6830 O O   B HOH   E .   ? 0.4007 0.3880 0.4830 0.0003  0.0219  0.0608  623 HOH   A O   
6831 O O   . HOH   E .   ? 0.3354 0.4489 0.3273 -0.0230 -0.0359 -0.0813 624 HOH   A O   
6832 O O   . HOH   E .   ? 0.2949 0.2602 0.5040 0.0313  0.0507  0.0781  625 HOH   A O   
6833 O O   . HOH   E .   ? 0.5843 0.6868 0.4651 0.3134  0.0355  0.1080  626 HOH   A O   
6834 O O   . HOH   E .   ? 0.4548 0.5157 0.4577 0.0579  -0.1142 -0.1316 627 HOH   A O   
6835 O O   . HOH   E .   ? 0.5009 0.6281 0.5490 -0.0704 -0.0622 0.0456  628 HOH   A O   
6836 O O   A HOH   E .   ? 0.3362 0.5131 0.2355 0.1198  0.1113  0.0462  629 HOH   A O   
6837 O O   . HOH   E .   ? 0.3009 0.8122 0.4232 0.0340  0.0576  -0.0529 630 HOH   A O   
6838 O O   . HOH   E .   ? 0.4286 0.5336 0.4799 0.1156  -0.0749 0.1526  631 HOH   A O   
6839 O O   . HOH   E .   ? 0.3477 0.4498 0.5736 -0.0478 -0.1009 0.2239  632 HOH   A O   
6840 O O   . HOH   F .   ? 0.2501 0.2367 0.3482 0.0290  0.0879  0.0506  201 HOH   B O   
6841 O O   . HOH   F .   ? 0.5220 0.3305 0.3821 -0.0278 0.0214  -0.1145 202 HOH   B O   
6842 O O   . HOH   F .   ? 0.4350 0.4366 0.5881 -0.1134 0.0267  -0.1286 203 HOH   B O   
6843 O O   . HOH   F .   ? 0.5703 0.6512 0.2591 0.2076  -0.0743 -0.1368 204 HOH   B O   
6844 O O   . HOH   F .   ? 0.3243 0.7009 0.4138 0.1320  0.0267  0.2265  205 HOH   B O   
6845 O O   . HOH   F .   ? 0.2933 0.5902 0.5213 -0.0203 0.1566  -0.1976 206 HOH   B O   
6846 O O   . HOH   F .   ? 0.6064 0.6465 0.5568 0.1861  0.0776  0.0339  207 HOH   B O   
6847 O O   . HOH   F .   ? 0.7347 0.3655 0.5197 0.1179  0.0897  -0.0065 208 HOH   B O   
6848 O O   . HOH   F .   ? 0.4419 0.5945 0.3759 0.2691  -0.1157 -0.0346 209 HOH   B O   
6849 O O   . HOH   F .   ? 0.3650 0.4131 0.7088 -0.0626 0.0667  -0.0584 210 HOH   B O   
6850 O O   . HOH   F .   ? 0.5306 0.4250 0.6294 0.0528  -0.1243 0.2598  211 HOH   B O   
6851 O O   . HOH   F .   ? 0.3001 0.3031 0.6672 0.0757  -0.1101 0.0501  212 HOH   B O   
6852 O O   . HOH   F .   ? 0.3066 0.2071 0.5770 0.0250  0.1954  0.0926  213 HOH   B O   
6853 O O   . HOH   F .   ? 0.4884 0.6128 0.3787 0.3051  -0.0424 0.0451  214 HOH   B O   
6854 O O   . HOH   F .   ? 0.2068 0.2418 0.2786 0.0029  0.0202  -0.0246 215 HOH   B O   
6855 O O   . HOH   F .   ? 0.1726 0.1861 0.2885 -0.0137 -0.0037 0.0097  216 HOH   B O   
6856 O O   . HOH   F .   ? 0.1548 0.1558 0.2493 -0.0235 0.0019  0.0120  217 HOH   B O   
6857 O O   . HOH   F .   ? 0.6088 0.6670 0.3257 0.0180  0.0048  0.0313  218 HOH   B O   
6858 O O   . HOH   F .   ? 0.5443 0.4118 0.4166 -0.0184 -0.1407 0.0916  219 HOH   B O   
6859 O O   . HOH   F .   ? 0.3464 0.6039 0.5105 0.2410  0.0364  -0.0639 220 HOH   B O   
6860 O O   . HOH   F .   ? 0.3915 0.4654 0.5270 -0.1724 0.0234  0.0806  221 HOH   B O   
6861 O O   . HOH   F .   ? 0.4465 0.4548 0.4179 0.0217  0.0756  -0.1510 222 HOH   B O   
6862 O O   . HOH   F .   ? 0.4722 0.2215 0.3505 -0.0201 -0.0934 0.0238  223 HOH   B O   
6863 O O   . HOH   F .   ? 0.3149 0.2554 0.6240 -0.0227 0.0515  -0.0016 224 HOH   B O   
6864 O O   . HOH   F .   ? 0.2534 0.1892 0.2981 -0.0303 0.0920  -0.0065 225 HOH   B O   
6865 O O   . HOH   F .   ? 0.1738 0.2196 0.3043 -0.0116 -0.0021 -0.0025 226 HOH   B O   
6866 O O   . HOH   F .   ? 0.3353 0.3437 0.4800 0.0771  -0.0756 0.0079  227 HOH   B O   
6867 O O   . HOH   F .   ? 0.5460 0.3279 0.4069 -0.1816 0.0292  -0.0115 228 HOH   B O   
6868 O O   . HOH   F .   ? 0.4519 0.7205 0.4009 0.2470  0.0341  -0.0008 229 HOH   B O   
6869 O O   . HOH   F .   ? 0.3901 0.3632 0.2063 0.0460  0.0711  0.0489  230 HOH   B O   
6870 O O   . HOH   F .   ? 0.2959 0.2561 0.3332 0.0321  0.0282  -0.0887 231 HOH   B O   
6871 O O   . HOH   F .   ? 0.2795 0.3658 0.3754 -0.0988 0.0449  -0.0504 232 HOH   B O   
6872 O O   . HOH   F .   ? 0.2387 0.2257 0.3990 -0.0310 -0.0166 -0.0600 233 HOH   B O   
6873 O O   . HOH   F .   ? 0.4648 0.4526 0.6301 -0.0541 -0.1685 -0.0950 234 HOH   B O   
6874 O O   . HOH   F .   ? 0.3273 0.2304 0.4812 0.0127  0.1637  0.0271  235 HOH   B O   
6875 O O   . HOH   F .   ? 0.1544 0.1489 0.1743 -0.0152 -0.0102 -0.0033 236 HOH   B O   
6876 O O   . HOH   F .   ? 0.2254 0.1342 0.3635 0.0123  -0.0680 -0.0214 237 HOH   B O   
6877 O O   . HOH   F .   ? 0.2143 0.2304 0.3294 -0.0474 0.0074  -0.0278 238 HOH   B O   
6878 O O   . HOH   F .   ? 0.3590 0.1923 0.2239 0.0065  -0.0678 -0.0131 239 HOH   B O   
6879 O O   . HOH   F .   ? 0.2429 0.3761 0.3182 -0.0483 -0.0692 -0.0449 240 HOH   B O   
6880 O O   . HOH   F .   ? 0.5733 0.3043 0.4104 -0.2243 0.0315  -0.0009 241 HOH   B O   
6881 O O   . HOH   F .   ? 0.6825 0.5004 0.4898 0.1895  0.0062  -0.1291 242 HOH   B O   
6882 O O   . HOH   F .   ? 0.2248 0.2108 0.2292 -0.0232 -0.0476 0.0116  243 HOH   B O   
6883 O O   . HOH   F .   ? 0.3988 0.2592 0.4278 0.0847  -0.0519 -0.0697 244 HOH   B O   
6884 O O   . HOH   F .   ? 0.2083 0.4236 0.2469 -0.0488 -0.0220 0.0662  245 HOH   B O   
6885 O O   . HOH   F .   ? 0.3493 0.2467 0.3331 -0.0363 0.0361  -0.0663 246 HOH   B O   
6886 O O   . HOH   F .   ? 0.1511 0.1409 0.1726 -0.0036 -0.0073 0.0081  247 HOH   B O   
6887 O O   . HOH   F .   ? 0.1562 0.1608 0.2870 -0.0025 0.0015  -0.0110 248 HOH   B O   
6888 O O   . HOH   F .   ? 0.4717 0.3463 0.3546 -0.0922 0.0820  -0.0471 249 HOH   B O   
6889 O O   . HOH   F .   ? 0.2246 0.1515 0.2213 -0.0293 -0.0473 0.0245  250 HOH   B O   
6890 O O   . HOH   F .   ? 0.3076 0.4733 0.3254 -0.1121 -0.0501 -0.0759 251 HOH   B O   
6891 O O   . HOH   F .   ? 0.3704 0.2826 0.3973 0.0436  -0.1058 -0.1183 252 HOH   B O   
6892 O O   . HOH   F .   ? 0.2359 0.2210 0.1940 0.0185  -0.0015 0.0065  253 HOH   B O   
6893 O O   . HOH   F .   ? 0.5620 0.3566 0.2563 -0.0153 0.0915  -0.0214 254 HOH   B O   
6894 O O   . HOH   F .   ? 0.3269 0.3538 0.2347 0.0610  0.0689  0.0243  255 HOH   B O   
6895 O O   . HOH   F .   ? 0.2904 0.4783 0.5821 0.0119  0.0499  -0.0929 256 HOH   B O   
6896 O O   . HOH   F .   ? 0.2404 0.3718 0.2466 -0.0805 0.0144  0.0867  257 HOH   B O   
6897 O O   . HOH   F .   ? 0.2820 0.2404 0.3118 0.0878  0.0752  0.0097  258 HOH   B O   
6898 O O   . HOH   F .   ? 0.3437 0.1797 0.6113 -0.0142 -0.1326 -0.0380 259 HOH   B O   
6899 O O   . HOH   F .   ? 0.1662 0.1828 0.2986 -0.0204 -0.0270 0.0199  260 HOH   B O   
6900 O O   . HOH   F .   ? 0.2486 0.2215 0.2140 0.0222  0.0064  -0.0027 261 HOH   B O   
6901 O O   . HOH   F .   ? 0.1449 0.1737 0.2170 -0.0079 0.0082  0.0129  262 HOH   B O   
6902 O O   . HOH   F .   ? 0.2424 0.2325 0.2694 0.0824  -0.0852 -0.0667 263 HOH   B O   
6903 O O   . HOH   F .   ? 0.3291 0.5138 0.3702 -0.0383 -0.0978 0.1431  264 HOH   B O   
6904 O O   . HOH   F .   ? 0.2681 0.3933 0.5565 0.1199  -0.0486 -0.0831 265 HOH   B O   
6905 O O   . HOH   F .   ? 0.1954 0.1852 0.1804 -0.0405 -0.0473 0.0076  266 HOH   B O   
6906 O O   . HOH   F .   ? 0.2101 0.1524 0.2570 -0.0225 -0.0153 0.0170  267 HOH   B O   
6907 O O   . HOH   F .   ? 0.4431 0.3708 0.2986 0.0636  -0.0166 -0.0997 268 HOH   B O   
6908 O O   . HOH   F .   ? 0.2316 0.2021 0.3610 -0.0058 -0.0510 -0.0259 269 HOH   B O   
6909 O O   . HOH   F .   ? 0.2740 0.2905 0.2576 -0.0446 -0.0895 0.0192  270 HOH   B O   
6910 O O   . HOH   F .   ? 0.2684 0.2034 0.3039 -0.0554 0.0120  0.0013  271 HOH   B O   
6911 O O   . HOH   F .   ? 0.2276 0.3925 0.5326 -0.0322 -0.0526 -0.1752 272 HOH   B O   
6912 O O   . HOH   F .   ? 0.4382 0.3292 0.4480 -0.0279 -0.1361 -0.0744 273 HOH   B O   
6913 O O   . HOH   F .   ? 0.4659 0.5845 0.4469 0.0770  -0.1250 -0.0236 274 HOH   B O   
6914 O O   . HOH   F .   ? 0.1794 0.1489 0.4484 -0.0099 -0.0315 -0.0086 275 HOH   B O   
6915 O O   . HOH   F .   ? 0.2607 0.4083 0.3681 0.0432  0.0957  0.0063  276 HOH   B O   
6916 O O   . HOH   F .   ? 0.2476 0.2670 0.2548 -0.0438 -0.0727 -0.0388 277 HOH   B O   
6917 O O   . HOH   F .   ? 0.2261 0.3561 0.2355 0.0927  -0.0163 -0.0263 278 HOH   B O   
6918 O O   . HOH   F .   ? 0.2585 0.2741 0.2960 0.0170  -0.0728 0.0208  279 HOH   B O   
6919 O O   . HOH   F .   ? 0.3134 0.3156 0.5339 -0.0485 0.0205  -0.1264 280 HOH   B O   
6920 O O   . HOH   F .   ? 0.3490 0.4119 0.6956 0.0516  -0.0797 0.0535  281 HOH   B O   
6921 O O   . HOH   F .   ? 0.1656 0.1639 0.1859 -0.0029 -0.0008 -0.0038 282 HOH   B O   
6922 O O   . HOH   F .   ? 0.1624 0.1598 0.3538 -0.0115 0.0087  0.0007  283 HOH   B O   
6923 O O   . HOH   F .   ? 0.2563 0.3875 0.3796 -0.0840 0.0754  -0.1683 284 HOH   B O   
6924 O O   . HOH   F .   ? 0.3422 0.2849 0.2355 0.0311  -0.0760 -0.0188 285 HOH   B O   
6925 O O   . HOH   F .   ? 0.1663 0.2123 0.1723 -0.0127 -0.0200 0.0070  286 HOH   B O   
6926 O O   . HOH   F .   ? 0.1821 0.2011 0.2911 0.0204  -0.0086 -0.0068 287 HOH   B O   
6927 O O   . HOH   F .   ? 0.3814 0.3973 0.4338 0.1285  -0.0824 -0.0986 288 HOH   B O   
6928 O O   . HOH   F .   ? 0.1779 0.3026 0.5077 0.0082  -0.0008 -0.1258 289 HOH   B O   
6929 O O   . HOH   F .   ? 0.3947 0.2232 0.4561 -0.0949 -0.2220 0.0812  290 HOH   B O   
6930 O O   . HOH   F .   ? 0.4771 0.3114 0.4926 -0.0838 0.0097  0.0915  291 HOH   B O   
6931 O O   . HOH   F .   ? 0.4837 0.3748 0.2694 0.1499  -0.0951 0.0285  292 HOH   B O   
6932 O O   . HOH   F .   ? 0.2718 0.2168 0.5065 0.0201  0.0452  0.0394  293 HOH   B O   
6933 O O   . HOH   F .   ? 0.2977 0.3109 0.6026 -0.0205 -0.0992 0.1476  294 HOH   B O   
6934 O O   . HOH   F .   ? 0.2576 0.6426 0.7574 0.1370  -0.0726 -0.0933 295 HOH   B O   
6935 O O   . HOH   F .   ? 0.6077 0.3855 0.3562 0.2649  0.1302  0.0873  296 HOH   B O   
6936 O O   . HOH   F .   ? 0.3341 0.2978 0.2859 -0.0266 0.0268  -0.1254 297 HOH   B O   
6937 O O   . HOH   F .   ? 0.2928 0.4890 0.5009 -0.0905 -0.1290 0.1259  298 HOH   B O   
6938 O O   . HOH   F .   ? 0.5234 0.6087 0.2406 -0.0099 -0.0674 0.1050  299 HOH   B O   
6939 O O   . HOH   F .   ? 0.3212 0.3913 0.4114 -0.1322 0.1294  -0.0547 300 HOH   B O   
6940 O O   . HOH   F .   ? 0.1823 0.1660 0.2616 0.0123  -0.0024 0.0171  301 HOH   B O   
6941 O O   . HOH   F .   ? 0.3382 0.6747 0.3160 0.1631  -0.0456 0.0582  302 HOH   B O   
6942 O O   . HOH   F .   ? 0.6304 0.6284 0.5222 0.2901  -0.0355 0.0126  303 HOH   B O   
6943 O O   . HOH   F .   ? 0.2181 0.1655 0.2711 -0.0225 -0.0285 -0.0020 304 HOH   B O   
6944 O O   . HOH   F .   ? 0.1621 0.1555 0.3315 0.0091  -0.0126 0.0042  305 HOH   B O   
6945 O O   . HOH   F .   ? 0.2073 0.2810 0.6161 0.0525  -0.0330 -0.1051 306 HOH   B O   
6946 O O   . HOH   F .   ? 0.4279 0.5568 0.2316 0.0331  0.0690  0.0760  307 HOH   B O   
6947 O O   . HOH   F .   ? 0.2731 0.7905 0.2696 0.0642  -0.0451 -0.0570 308 HOH   B O   
6948 O O   . HOH   F .   ? 0.3558 0.1919 0.3604 0.0777  0.1062  0.0476  309 HOH   B O   
6949 O O   . HOH   F .   ? 0.2544 0.1569 0.2619 -0.0150 -0.0199 0.0312  310 HOH   B O   
6950 O O   . HOH   F .   ? 0.4210 0.2465 0.2898 0.1614  0.1223  0.0522  311 HOH   B O   
6951 O O   . HOH   F .   ? 0.2116 0.1668 0.3725 0.0354  -0.0987 -0.0007 312 HOH   B O   
6952 O O   . HOH   F .   ? 0.1643 0.1954 0.2955 -0.0278 -0.0123 0.0176  313 HOH   B O   
6953 O O   . HOH   F .   ? 0.2463 0.3162 0.5228 -0.0444 -0.0625 -0.0003 314 HOH   B O   
6954 O O   . HOH   F .   ? 0.5146 0.3359 0.2571 -0.2026 0.0737  -0.0352 315 HOH   B O   
6955 O O   . HOH   F .   ? 0.2183 0.2047 0.2030 -0.0097 0.0245  0.0151  316 HOH   B O   
6956 O O   . HOH   F .   ? 0.2355 0.2350 0.5858 -0.0385 0.0203  0.1427  317 HOH   B O   
6957 O O   . HOH   F .   ? 0.2827 0.3038 0.3810 -0.0327 0.0896  -0.0852 318 HOH   B O   
6958 O O   . HOH   F .   ? 0.1752 0.2956 0.2588 -0.0106 -0.0288 0.0788  319 HOH   B O   
6959 O O   . HOH   F .   ? 0.1655 0.1729 0.3182 -0.0160 -0.0224 -0.0102 320 HOH   B O   
6960 O O   . HOH   F .   ? 0.6077 0.5105 0.5247 -0.1116 -0.0192 0.0706  321 HOH   B O   
6961 O O   . HOH   F .   ? 0.5520 0.2567 0.3558 0.0399  -0.0309 0.0930  322 HOH   B O   
6962 O O   . HOH   F .   ? 0.6193 0.5102 0.5342 0.1339  0.1679  0.0051  323 HOH   B O   
6963 O O   . HOH   F .   ? 0.3320 0.4646 0.8074 -0.0426 -0.1065 0.2639  324 HOH   B O   
6964 O O   . HOH   F .   ? 0.5300 0.4988 0.2476 0.1272  -0.0555 -0.0396 325 HOH   B O   
6965 O O   . HOH   F .   ? 0.2872 0.2303 0.2638 0.0222  -0.0341 0.0221  326 HOH   B O   
6966 O O   . HOH   F .   ? 0.5142 0.4477 0.2695 0.0231  -0.0550 -0.0653 327 HOH   B O   
6967 O O   . HOH   F .   ? 0.2461 0.5920 0.5436 -0.0766 0.0251  -0.0296 328 HOH   B O   
6968 O O   . HOH   F .   ? 0.4383 0.3235 0.5799 0.1050  0.2183  0.1886  329 HOH   B O   
6969 O O   . HOH   F .   ? 0.1996 0.2157 0.3068 0.0368  0.0375  0.0200  330 HOH   B O   
6970 O O   . HOH   F .   ? 0.7973 0.2042 0.3336 -0.0066 -0.0711 -0.0131 331 HOH   B O   
6971 O O   . HOH   F .   ? 0.2663 0.2075 0.5554 0.0075  0.0179  0.0250  332 HOH   B O   
6972 O O   . HOH   F .   ? 0.2786 0.3627 0.4867 -0.0635 -0.1541 0.1408  333 HOH   B O   
6973 O O   . HOH   F .   ? 0.5544 0.4934 0.6096 -0.0384 -0.0424 -0.1240 334 HOH   B O   
6974 O O   . HOH   F .   ? 0.6436 0.3601 0.3800 0.0029  0.1235  0.0961  335 HOH   B O   
6975 O O   . HOH   F .   ? 0.5094 0.3221 0.3308 0.0362  -0.1444 -0.0340 336 HOH   B O   
6976 O O   . HOH   F .   ? 0.6097 0.3315 0.4484 0.0064  0.0717  -0.1483 337 HOH   B O   
6977 O O   . HOH   F .   ? 0.1758 0.2922 0.3394 0.0184  -0.0131 -0.0604 338 HOH   B O   
6978 O O   . HOH   F .   ? 0.6341 0.6674 0.2764 -0.0295 -0.0342 0.0670  339 HOH   B O   
6979 O O   . HOH   F .   ? 0.5013 0.5494 0.6868 0.0900  -0.0942 0.2339  340 HOH   B O   
6980 O O   . HOH   F .   ? 0.1837 0.1604 0.2379 0.0079  -0.0198 0.0064  341 HOH   B O   
6981 O O   . HOH   F .   ? 0.4806 0.5875 0.3491 0.0225  -0.1009 0.0054  342 HOH   B O   
6982 O O   . HOH   F .   ? 0.4361 0.7046 0.3773 -0.0921 -0.0918 -0.0783 343 HOH   B O   
6983 O O   . HOH   F .   ? 0.4645 0.6256 0.3970 -0.0146 -0.0535 0.1393  344 HOH   B O   
6984 O O   . HOH   F .   ? 0.2554 0.5845 0.7119 0.0073  -0.0438 0.0472  345 HOH   B O   
6985 O O   . HOH   F .   ? 0.2175 0.1925 0.3582 -0.0073 0.0751  -0.0009 346 HOH   B O   
6986 O O   . HOH   F .   ? 0.4319 0.4594 0.5009 0.0214  -0.0772 0.0479  347 HOH   B O   
6987 O O   . HOH   F .   ? 0.2632 0.6446 0.3681 0.1752  -0.0654 -0.1462 348 HOH   B O   
6988 O O   . HOH   F .   ? 0.2754 0.2573 0.5211 -0.0191 -0.1038 -0.0582 349 HOH   B O   
6989 O O   . HOH   F .   ? 0.2272 0.3627 0.5816 0.0107  0.0170  0.0483  350 HOH   B O   
6990 O O   . HOH   F .   ? 0.5258 0.6288 0.5045 -0.1183 0.0649  0.1107  351 HOH   B O   
6991 O O   . HOH   F .   ? 0.3508 0.4982 0.5004 -0.1661 0.0301  -0.0195 352 HOH   B O   
6992 O O   . HOH   F .   ? 0.3954 0.2305 0.3469 -0.0611 -0.0012 -0.0768 353 HOH   B O   
6993 O O   . HOH   F .   ? 0.4590 0.3676 0.5800 -0.1077 0.1678  0.0636  354 HOH   B O   
6994 O O   . HOH   F .   ? 0.3250 0.2051 0.4182 0.0527  -0.1445 -0.0551 355 HOH   B O   
6995 O O   . HOH   F .   ? 0.4484 0.5929 0.6366 0.0066  0.0145  -0.0552 356 HOH   B O   
6996 O O   . HOH   F .   ? 0.5488 0.3650 0.4714 0.0570  0.1778  -0.0368 357 HOH   B O   
6997 O O   . HOH   F .   ? 0.4000 0.2872 0.3987 -0.0902 -0.0212 -0.0569 358 HOH   B O   
6998 O O   . HOH   F .   ? 0.4706 0.5688 0.5862 0.1842  -0.1336 0.1572  359 HOH   B O   
6999 O O   . HOH   F .   ? 0.4305 0.5377 0.4710 -0.0372 -0.1247 0.0152  360 HOH   B O   
7000 O O   . HOH   F .   ? 0.5288 0.3429 0.4801 -0.0237 -0.1704 -0.0153 361 HOH   B O   
7001 O O   . HOH   F .   ? 0.4838 0.4412 0.5915 0.0374  0.0496  0.1415  362 HOH   B O   
7002 O O   . HOH   F .   ? 0.4489 0.6673 0.3305 0.2214  -0.0401 0.0447  363 HOH   B O   
7003 O O   . HOH   F .   ? 0.2289 0.3756 0.6648 -0.0807 -0.0656 -0.0888 364 HOH   B O   
7004 O O   . HOH   F .   ? 0.6081 0.4095 0.4615 -0.0255 -0.1677 0.0491  365 HOH   B O   
7005 O O   . HOH   F .   ? 0.5947 0.3081 0.5526 -0.1428 -0.0032 0.0045  366 HOH   B O   
7006 O O   . HOH   F .   ? 0.6367 0.4968 0.4366 0.1730  0.0847  0.1022  367 HOH   B O   
7007 O O   . HOH   F .   ? 0.5091 0.5479 0.3431 0.0935  -0.1588 0.0422  368 HOH   B O   
7008 O O   . HOH   F .   ? 0.4678 0.6396 0.6351 0.2868  0.0591  0.1166  369 HOH   B O   
7009 O O   . HOH   F .   ? 0.5214 0.5378 0.4355 -0.0582 -0.0635 -0.1025 370 HOH   B O   
7010 O O   . HOH   F .   ? 0.7125 0.2199 0.3676 -0.0151 0.0692  0.0330  371 HOH   B O   
7011 O O   . HOH   F .   ? 0.6763 0.4057 0.3186 -0.1164 -0.1094 -0.0730 372 HOH   B O   
7012 O O   . HOH   F .   ? 0.8166 0.7681 0.5457 0.1943  -0.1389 0.1176  373 HOH   B O   
7013 O O   . HOH   F .   ? 0.4907 0.4848 0.5151 -0.0748 -0.0783 0.0468  374 HOH   B O   
7014 O O   . HOH   F .   ? 0.3904 0.3390 0.4826 0.0504  -0.1255 -0.0399 375 HOH   B O   
7015 O O   . HOH   F .   ? 0.2431 0.4584 0.4913 0.0688  -0.0759 -0.0652 376 HOH   B O   
7016 O O   . HOH   F .   ? 0.4657 0.7218 0.5848 0.1328  0.0133  0.3007  377 HOH   B O   
7017 O O   . HOH   F .   ? 0.3325 0.4432 0.2270 0.0409  0.0229  0.0240  378 HOH   B O   
7018 O O   . HOH   F .   ? 0.7283 0.3664 0.5577 -0.1155 0.0071  -0.0332 379 HOH   B O   
7019 O O   . HOH   F .   ? 0.3461 0.5103 0.4988 0.1151  -0.0100 0.0933  380 HOH   B O   
7020 O O   . HOH   F .   ? 0.5422 0.7477 0.6488 0.0355  0.1497  0.1715  381 HOH   B O   
7021 O O   . HOH   F .   ? 0.3219 0.2651 0.3654 0.0025  0.0155  0.0354  382 HOH   B O   
7022 O O   . HOH   F .   ? 0.5421 0.6926 0.3907 -0.1175 0.0336  -0.1482 383 HOH   B O   
7023 O O   . HOH   F .   ? 0.3948 0.9049 0.5958 0.0155  0.2082  0.1210  384 HOH   B O   
7024 O O   . HOH   F .   ? 0.6761 0.4397 0.5155 0.1404  0.0508  -0.1045 385 HOH   B O   
7025 O O   . HOH   F .   ? 0.6034 0.4578 0.5588 -0.0792 0.0573  -0.0013 386 HOH   B O   
7026 O O   . HOH   F .   ? 0.2544 0.4321 0.4208 -0.0764 -0.1048 -0.0223 387 HOH   B O   
7027 O O   . HOH   F .   ? 0.4752 0.3313 0.3710 0.0221  0.0525  -0.0297 388 HOH   B O   
7028 O O   . HOH   F .   ? 0.8061 0.6293 0.4395 0.2079  -0.0044 0.0954  389 HOH   B O   
7029 O O   . HOH   F .   ? 0.5594 0.4657 0.3869 0.0020  -0.0954 -0.0517 390 HOH   B O   
7030 O O   . HOH   F .   ? 0.4716 0.4260 0.3899 -0.0043 0.0004  0.0653  391 HOH   B O   
7031 O O   . HOH   F .   ? 0.3732 0.2391 0.3206 0.0759  0.0023  0.0270  392 HOH   B O   
7032 O O   . HOH   F .   ? 0.3996 0.2337 0.5674 -0.0271 0.0457  0.0528  393 HOH   B O   
7033 O O   . HOH   F .   ? 0.2634 0.4516 0.6821 -0.1475 -0.0603 -0.0052 394 HOH   B O   
7034 O O   . HOH   F .   ? 0.5319 0.6391 0.3811 0.2171  -0.0137 -0.0651 395 HOH   B O   
7035 O O   . HOH   F .   ? 0.3153 0.3906 0.3811 0.0632  0.0178  -0.0509 396 HOH   B O   
7036 O O   . HOH   F .   ? 0.4146 0.4843 0.4880 0.0063  0.1021  0.0947  397 HOH   B O   
7037 O O   . HOH   F .   ? 0.2196 0.2873 0.6121 -0.0558 -0.1051 0.0262  398 HOH   B O   
7038 O O   . HOH   F .   ? 0.5987 0.6179 0.6614 0.1021  -0.0686 0.2807  399 HOH   B O   
7039 O O   . HOH   F .   ? 0.5805 0.4427 0.3200 -0.2301 -0.0493 0.1238  400 HOH   B O   
7040 O O   . HOH   F .   ? 0.6637 0.5694 0.4075 0.1805  -0.0411 -0.0222 401 HOH   B O   
# 
