data_7HDF
# 
_entry.id   7HDF 
# 
_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   7HDF         pdb_00007hdf 10.2210/pdb7hdf/pdb 
WWPDB D_1001407333 ?            ?                   
# 
_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                        7HDF 
_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 '[(2R)-4-methyl-1-(7H-pyrrolo[2,3-d]pyrimidin-4-yl)piperazin-2-yl]methanol' 247.296   2   ?                      
? ? ?                                                                                    
4 water       nat water                                                                       18.015    410 ?                      
? ? ?                                                                                    
# 
_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 '[(2R)-4-methyl-1-(7H-pyrrolo[2,3-d]pyrimidin-4-yl)piperazin-2-yl]methanol' A1A77 
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 
A1A77 non-polymer         . '[(2R)-4-methyl-1-(7H-pyrrolo[2,3-d]pyrimidin-4-yl)piperazin-2-yl]methanol' ? 'C12 H17 N5 O'   247.296 
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   401 401  DMS   DMS A . 
D 3 A1A77 1   402 201  A1A77 LA1 A . 
E 3 A1A77 1   403 301  A1A77 LA2 A . 
F 4 HOH   1   501 105  HOH   HOH A . 
F 4 HOH   2   502 93   HOH   HOH A . 
F 4 HOH   3   503 196  HOH   HOH A . 
F 4 HOH   4   504 229  HOH   HOH A . 
F 4 HOH   5   505 292  HOH   HOH A . 
F 4 HOH   6   506 281  HOH   HOH A . 
F 4 HOH   7   507 493  HOH   HOH A . 
F 4 HOH   8   508 625  HOH   HOH A . 
F 4 HOH   9   509 209  HOH   HOH A . 
F 4 HOH   10  510 85   HOH   HOH A . 
F 4 HOH   11  511 86   HOH   HOH A . 
F 4 HOH   12  512 8    HOH   HOH A . 
F 4 HOH   13  513 39   HOH   HOH A . 
F 4 HOH   14  514 109  HOH   HOH A . 
F 4 HOH   15  515 76   HOH   HOH A . 
F 4 HOH   16  516 236  HOH   HOH A . 
F 4 HOH   17  517 1094 HOH   HOH A . 
F 4 HOH   18  518 662  HOH   HOH A . 
F 4 HOH   19  519 151  HOH   HOH A . 
F 4 HOH   20  520 1295 HOH   HOH A . 
F 4 HOH   21  521 124  HOH   HOH A . 
F 4 HOH   22  522 140  HOH   HOH A . 
F 4 HOH   23  523 24   HOH   HOH A . 
F 4 HOH   24  524 225  HOH   HOH A . 
F 4 HOH   25  525 15   HOH   HOH A . 
F 4 HOH   26  526 136  HOH   HOH A . 
F 4 HOH   27  527 661  HOH   HOH A . 
F 4 HOH   28  528 153  HOH   HOH A . 
F 4 HOH   29  529 164  HOH   HOH A . 
F 4 HOH   30  530 241  HOH   HOH A . 
F 4 HOH   31  531 278  HOH   HOH A . 
F 4 HOH   32  532 393  HOH   HOH A . 
F 4 HOH   33  533 1301 HOH   HOH A . 
F 4 HOH   34  534 964  HOH   HOH A . 
F 4 HOH   35  535 192  HOH   HOH A . 
F 4 HOH   36  536 247  HOH   HOH A . 
F 4 HOH   37  537 122  HOH   HOH A . 
F 4 HOH   38  538 1300 HOH   HOH A . 
F 4 HOH   39  539 337  HOH   HOH A . 
F 4 HOH   40  540 296  HOH   HOH A . 
F 4 HOH   41  541 469  HOH   HOH A . 
F 4 HOH   42  542 320  HOH   HOH A . 
F 4 HOH   43  543 42   HOH   HOH A . 
F 4 HOH   44  544 36   HOH   HOH A . 
F 4 HOH   45  545 630  HOH   HOH A . 
F 4 HOH   46  546 139  HOH   HOH A . 
F 4 HOH   47  547 92   HOH   HOH A . 
F 4 HOH   48  548 57   HOH   HOH A . 
F 4 HOH   49  549 1283 HOH   HOH A . 
F 4 HOH   50  550 354  HOH   HOH A . 
F 4 HOH   51  551 396  HOH   HOH A . 
F 4 HOH   52  552 165  HOH   HOH A . 
F 4 HOH   53  553 17   HOH   HOH A . 
F 4 HOH   54  554 33   HOH   HOH A . 
F 4 HOH   55  555 2    HOH   HOH A . 
F 4 HOH   56  556 1290 HOH   HOH A . 
F 4 HOH   57  557 1308 HOH   HOH A . 
F 4 HOH   58  558 66   HOH   HOH A . 
F 4 HOH   59  559 21   HOH   HOH A . 
F 4 HOH   60  560 81   HOH   HOH A . 
F 4 HOH   61  561 45   HOH   HOH A . 
F 4 HOH   62  562 19   HOH   HOH A . 
F 4 HOH   63  563 102  HOH   HOH A . 
F 4 HOH   64  564 18   HOH   HOH A . 
F 4 HOH   65  565 162  HOH   HOH A . 
F 4 HOH   66  566 159  HOH   HOH A . 
F 4 HOH   67  567 939  HOH   HOH A . 
F 4 HOH   68  568 46   HOH   HOH A . 
F 4 HOH   69  569 138  HOH   HOH A . 
F 4 HOH   70  570 186  HOH   HOH A . 
F 4 HOH   71  571 5    HOH   HOH A . 
F 4 HOH   72  572 169  HOH   HOH A . 
F 4 HOH   73  573 56   HOH   HOH A . 
F 4 HOH   74  574 155  HOH   HOH A . 
F 4 HOH   75  575 6    HOH   HOH A . 
F 4 HOH   76  576 49   HOH   HOH A . 
F 4 HOH   77  577 35   HOH   HOH A . 
F 4 HOH   78  578 1310 HOH   HOH A . 
F 4 HOH   79  579 27   HOH   HOH A . 
F 4 HOH   80  580 4    HOH   HOH A . 
F 4 HOH   81  581 409  HOH   HOH A . 
F 4 HOH   82  582 134  HOH   HOH A . 
F 4 HOH   83  583 405  HOH   HOH A . 
F 4 HOH   84  584 218  HOH   HOH A . 
F 4 HOH   85  585 461  HOH   HOH A . 
F 4 HOH   86  586 154  HOH   HOH A . 
F 4 HOH   87  587 148  HOH   HOH A . 
F 4 HOH   88  588 366  HOH   HOH A . 
F 4 HOH   89  589 78   HOH   HOH A . 
F 4 HOH   90  590 1309 HOH   HOH A . 
F 4 HOH   91  591 195  HOH   HOH A . 
F 4 HOH   92  592 26   HOH   HOH A . 
F 4 HOH   93  593 83   HOH   HOH A . 
F 4 HOH   94  594 1315 HOH   HOH A . 
F 4 HOH   95  595 1    HOH   HOH A . 
F 4 HOH   96  596 12   HOH   HOH A . 
F 4 HOH   97  597 116  HOH   HOH A . 
F 4 HOH   98  598 376  HOH   HOH A . 
F 4 HOH   99  599 58   HOH   HOH A . 
F 4 HOH   100 600 333  HOH   HOH A . 
F 4 HOH   101 601 67   HOH   HOH A . 
F 4 HOH   102 602 3    HOH   HOH A . 
F 4 HOH   103 603 303  HOH   HOH A . 
F 4 HOH   104 604 1313 HOH   HOH A . 
F 4 HOH   105 605 34   HOH   HOH A . 
F 4 HOH   106 606 74   HOH   HOH A . 
F 4 HOH   107 607 1275 HOH   HOH A . 
F 4 HOH   108 608 68   HOH   HOH A . 
F 4 HOH   109 609 397  HOH   HOH A . 
F 4 HOH   110 610 121  HOH   HOH A . 
F 4 HOH   111 611 7    HOH   HOH A . 
F 4 HOH   112 612 25   HOH   HOH A . 
F 4 HOH   113 613 132  HOH   HOH A . 
F 4 HOH   114 614 1068 HOH   HOH A . 
F 4 HOH   115 615 351  HOH   HOH A . 
F 4 HOH   116 616 123  HOH   HOH A . 
F 4 HOH   117 617 199  HOH   HOH A . 
F 4 HOH   118 618 212  HOH   HOH A . 
F 4 HOH   119 619 53   HOH   HOH A . 
F 4 HOH   120 620 1279 HOH   HOH A . 
F 4 HOH   121 621 95   HOH   HOH A . 
F 4 HOH   122 622 156  HOH   HOH A . 
F 4 HOH   123 623 125  HOH   HOH A . 
F 4 HOH   124 624 115  HOH   HOH A . 
F 4 HOH   125 625 70   HOH   HOH A . 
F 4 HOH   126 626 1289 HOH   HOH A . 
F 4 HOH   127 627 96   HOH   HOH A . 
F 4 HOH   128 628 381  HOH   HOH A . 
F 4 HOH   129 629 582  HOH   HOH A . 
F 4 HOH   130 630 1222 HOH   HOH A . 
F 4 HOH   131 631 51   HOH   HOH A . 
F 4 HOH   132 632 1286 HOH   HOH A . 
F 4 HOH   133 633 73   HOH   HOH A . 
F 4 HOH   134 634 1296 HOH   HOH A . 
F 4 HOH   135 635 1189 HOH   HOH A . 
F 4 HOH   136 636 16   HOH   HOH A . 
F 4 HOH   137 637 71   HOH   HOH A . 
F 4 HOH   138 638 40   HOH   HOH A . 
F 4 HOH   139 639 952  HOH   HOH A . 
F 4 HOH   140 640 80   HOH   HOH A . 
F 4 HOH   141 641 1238 HOH   HOH A . 
F 4 HOH   142 642 94   HOH   HOH A . 
F 4 HOH   143 643 944  HOH   HOH A . 
F 4 HOH   144 644 576  HOH   HOH A . 
F 4 HOH   145 645 97   HOH   HOH A . 
F 4 HOH   146 646 188  HOH   HOH A . 
F 4 HOH   147 647 104  HOH   HOH A . 
F 4 HOH   148 648 79   HOH   HOH A . 
F 4 HOH   149 649 330  HOH   HOH A . 
F 4 HOH   150 650 2    HOH   HOH A . 
F 4 HOH   151 651 107  HOH   HOH A . 
F 4 HOH   152 652 1119 HOH   HOH A . 
F 4 HOH   153 653 1134 HOH   HOH A . 
F 4 HOH   154 654 509  HOH   HOH A . 
F 4 HOH   155 655 163  HOH   HOH A . 
F 4 HOH   156 656 726  HOH   HOH A . 
F 4 HOH   157 657 756  HOH   HOH A . 
F 4 HOH   158 658 408  HOH   HOH A . 
F 4 HOH   159 659 3    HOH   HOH A . 
F 4 HOH   160 660 63   HOH   HOH A . 
F 4 HOH   161 661 361  HOH   HOH A . 
F 4 HOH   162 662 126  HOH   HOH A . 
F 4 HOH   163 663 801  HOH   HOH A . 
F 4 HOH   164 664 319  HOH   HOH A . 
F 4 HOH   165 665 1307 HOH   HOH A . 
F 4 HOH   166 666 280  HOH   HOH A . 
F 4 HOH   167 667 556  HOH   HOH A . 
F 4 HOH   168 668 1276 HOH   HOH A . 
F 4 HOH   169 669 250  HOH   HOH A . 
F 4 HOH   170 670 326  HOH   HOH A . 
F 4 HOH   171 671 342  HOH   HOH A . 
F 4 HOH   172 672 267  HOH   HOH A . 
F 4 HOH   173 673 1306 HOH   HOH A . 
F 4 HOH   174 674 1287 HOH   HOH A . 
F 4 HOH   175 675 370  HOH   HOH A . 
F 4 HOH   176 676 1314 HOH   HOH A . 
F 4 HOH   177 677 695  HOH   HOH A . 
F 4 HOH   178 678 135  HOH   HOH A . 
F 4 HOH   179 679 674  HOH   HOH A . 
F 4 HOH   180 680 919  HOH   HOH A . 
F 4 HOH   181 681 202  HOH   HOH A . 
F 4 HOH   182 682 521  HOH   HOH A . 
F 4 HOH   183 683 224  HOH   HOH A . 
F 4 HOH   184 684 356  HOH   HOH A . 
F 4 HOH   185 685 309  HOH   HOH A . 
F 4 HOH   186 686 315  HOH   HOH A . 
F 4 HOH   187 687 318  HOH   HOH A . 
F 4 HOH   188 688 1299 HOH   HOH A . 
F 4 HOH   189 689 711  HOH   HOH A . 
F 4 HOH   190 690 805  HOH   HOH A . 
F 4 HOH   191 691 331  HOH   HOH A . 
F 4 HOH   192 692 263  HOH   HOH A . 
F 4 HOH   193 693 152  HOH   HOH A . 
F 4 HOH   194 694 941  HOH   HOH A . 
F 4 HOH   195 695 208  HOH   HOH A . 
F 4 HOH   196 696 1284 HOH   HOH A . 
F 4 HOH   197 697 1071 HOH   HOH A . 
F 4 HOH   198 698 180  HOH   HOH A . 
F 4 HOH   199 699 350  HOH   HOH A . 
F 4 HOH   200 700 363  HOH   HOH A . 
F 4 HOH   201 701 371  HOH   HOH A . 
F 4 HOH   202 702 313  HOH   HOH A . 
F 4 HOH   203 703 185  HOH   HOH A . 
F 4 HOH   204 704 429  HOH   HOH A . 
F 4 HOH   205 705 1074 HOH   HOH A . 
F 4 HOH   206 706 772  HOH   HOH A . 
F 4 HOH   207 707 346  HOH   HOH A . 
F 4 HOH   208 708 1292 HOH   HOH A . 
F 4 HOH   209 709 1078 HOH   HOH A . 
G 4 HOH   1   201 64   HOH   HOH B . 
G 4 HOH   2   202 398  HOH   HOH B . 
G 4 HOH   3   203 358  HOH   HOH B . 
G 4 HOH   4   204 900  HOH   HOH B . 
G 4 HOH   5   205 364  HOH   HOH B . 
G 4 HOH   6   206 654  HOH   HOH B . 
G 4 HOH   7   207 549  HOH   HOH B . 
G 4 HOH   8   208 240  HOH   HOH B . 
G 4 HOH   9   209 1249 HOH   HOH B . 
G 4 HOH   10  210 353  HOH   HOH B . 
G 4 HOH   11  211 758  HOH   HOH B . 
G 4 HOH   12  212 264  HOH   HOH B . 
G 4 HOH   13  213 743  HOH   HOH B . 
G 4 HOH   14  214 276  HOH   HOH B . 
G 4 HOH   15  215 343  HOH   HOH B . 
G 4 HOH   16  216 120  HOH   HOH B . 
G 4 HOH   17  217 50   HOH   HOH B . 
G 4 HOH   18  218 452  HOH   HOH B . 
G 4 HOH   19  219 232  HOH   HOH B . 
G 4 HOH   20  220 531  HOH   HOH B . 
G 4 HOH   21  221 131  HOH   HOH B . 
G 4 HOH   22  222 54   HOH   HOH B . 
G 4 HOH   23  223 282  HOH   HOH B . 
G 4 HOH   24  224 272  HOH   HOH B . 
G 4 HOH   25  225 332  HOH   HOH B . 
G 4 HOH   26  226 1278 HOH   HOH B . 
G 4 HOH   27  227 82   HOH   HOH B . 
G 4 HOH   28  228 444  HOH   HOH B . 
G 4 HOH   29  229 75   HOH   HOH B . 
G 4 HOH   30  230 1140 HOH   HOH B . 
G 4 HOH   31  231 166  HOH   HOH B . 
G 4 HOH   32  232 128  HOH   HOH B . 
G 4 HOH   33  233 1312 HOH   HOH B . 
G 4 HOH   34  234 127  HOH   HOH B . 
G 4 HOH   35  235 205  HOH   HOH B . 
G 4 HOH   36  236 325  HOH   HOH B . 
G 4 HOH   37  237 181  HOH   HOH B . 
G 4 HOH   38  238 69   HOH   HOH B . 
G 4 HOH   39  239 723  HOH   HOH B . 
G 4 HOH   40  240 110  HOH   HOH B . 
G 4 HOH   41  241 60   HOH   HOH B . 
G 4 HOH   42  242 1    HOH   HOH B . 
G 4 HOH   43  243 30   HOH   HOH B . 
G 4 HOH   44  244 129  HOH   HOH B . 
G 4 HOH   45  245 300  HOH   HOH B . 
G 4 HOH   46  246 14   HOH   HOH B . 
G 4 HOH   47  247 9    HOH   HOH B . 
G 4 HOH   48  248 252  HOH   HOH B . 
G 4 HOH   49  249 133  HOH   HOH B . 
G 4 HOH   50  250 47   HOH   HOH B . 
G 4 HOH   51  251 143  HOH   HOH B . 
G 4 HOH   52  252 31   HOH   HOH B . 
G 4 HOH   53  253 52   HOH   HOH B . 
G 4 HOH   54  254 72   HOH   HOH B . 
G 4 HOH   55  255 144  HOH   HOH B . 
G 4 HOH   56  256 347  HOH   HOH B . 
G 4 HOH   57  257 302  HOH   HOH B . 
G 4 HOH   58  258 41   HOH   HOH B . 
G 4 HOH   59  259 172  HOH   HOH B . 
G 4 HOH   60  260 20   HOH   HOH B . 
G 4 HOH   61  261 271  HOH   HOH B . 
G 4 HOH   62  262 62   HOH   HOH B . 
G 4 HOH   63  263 10   HOH   HOH B . 
G 4 HOH   64  264 61   HOH   HOH B . 
G 4 HOH   65  265 150  HOH   HOH B . 
G 4 HOH   66  266 231  HOH   HOH B . 
G 4 HOH   67  267 117  HOH   HOH B . 
G 4 HOH   68  268 243  HOH   HOH B . 
G 4 HOH   69  269 391  HOH   HOH B . 
G 4 HOH   70  270 59   HOH   HOH B . 
G 4 HOH   71  271 77   HOH   HOH B . 
G 4 HOH   72  272 103  HOH   HOH B . 
G 4 HOH   73  273 84   HOH   HOH B . 
G 4 HOH   74  274 114  HOH   HOH B . 
G 4 HOH   75  275 11   HOH   HOH B . 
G 4 HOH   76  276 1277 HOH   HOH B . 
G 4 HOH   77  277 242  HOH   HOH B . 
G 4 HOH   78  278 175  HOH   HOH B . 
G 4 HOH   79  279 1106 HOH   HOH B . 
G 4 HOH   80  280 287  HOH   HOH B . 
G 4 HOH   81  281 43   HOH   HOH B . 
G 4 HOH   82  282 1305 HOH   HOH B . 
G 4 HOH   83  283 22   HOH   HOH B . 
G 4 HOH   84  284 221  HOH   HOH B . 
G 4 HOH   85  285 106  HOH   HOH B . 
G 4 HOH   86  286 13   HOH   HOH B . 
G 4 HOH   87  287 147  HOH   HOH B . 
G 4 HOH   88  288 1066 HOH   HOH B . 
G 4 HOH   89  289 635  HOH   HOH B . 
G 4 HOH   90  290 416  HOH   HOH B . 
G 4 HOH   91  291 89   HOH   HOH B . 
G 4 HOH   92  292 141  HOH   HOH B . 
G 4 HOH   93  293 137  HOH   HOH B . 
G 4 HOH   94  294 387  HOH   HOH B . 
G 4 HOH   95  295 88   HOH   HOH B . 
G 4 HOH   96  296 297  HOH   HOH B . 
G 4 HOH   97  297 235  HOH   HOH B . 
G 4 HOH   98  298 99   HOH   HOH B . 
G 4 HOH   99  299 1291 HOH   HOH B . 
G 4 HOH   100 300 160  HOH   HOH B . 
G 4 HOH   101 301 316  HOH   HOH B . 
G 4 HOH   102 302 32   HOH   HOH B . 
G 4 HOH   103 303 299  HOH   HOH B . 
G 4 HOH   104 304 341  HOH   HOH B . 
G 4 HOH   105 305 112  HOH   HOH B . 
G 4 HOH   106 306 216  HOH   HOH B . 
G 4 HOH   107 307 38   HOH   HOH B . 
G 4 HOH   108 308 311  HOH   HOH B . 
G 4 HOH   109 309 220  HOH   HOH B . 
G 4 HOH   110 310 48   HOH   HOH B . 
G 4 HOH   111 311 101  HOH   HOH B . 
G 4 HOH   112 312 704  HOH   HOH B . 
G 4 HOH   113 313 1126 HOH   HOH B . 
G 4 HOH   114 314 142  HOH   HOH B . 
G 4 HOH   115 315 118  HOH   HOH B . 
G 4 HOH   116 316 37   HOH   HOH B . 
G 4 HOH   117 317 91   HOH   HOH B . 
G 4 HOH   118 318 215  HOH   HOH B . 
G 4 HOH   119 319 44   HOH   HOH B . 
G 4 HOH   120 320 1285 HOH   HOH B . 
G 4 HOH   121 321 23   HOH   HOH B . 
G 4 HOH   122 322 170  HOH   HOH B . 
G 4 HOH   123 323 161  HOH   HOH B . 
G 4 HOH   124 324 182  HOH   HOH B . 
G 4 HOH   125 325 28   HOH   HOH B . 
G 4 HOH   126 326 177  HOH   HOH B . 
G 4 HOH   127 327 100  HOH   HOH B . 
G 4 HOH   128 328 1294 HOH   HOH B . 
G 4 HOH   129 329 1274 HOH   HOH B . 
G 4 HOH   130 330 29   HOH   HOH B . 
G 4 HOH   131 331 339  HOH   HOH B . 
G 4 HOH   132 332 717  HOH   HOH B . 
G 4 HOH   133 333 55   HOH   HOH B . 
G 4 HOH   134 334 445  HOH   HOH B . 
G 4 HOH   135 335 98   HOH   HOH B . 
G 4 HOH   136 336 334  HOH   HOH B . 
G 4 HOH   137 337 234  HOH   HOH B . 
G 4 HOH   138 338 197  HOH   HOH B . 
G 4 HOH   139 339 207  HOH   HOH B . 
G 4 HOH   140 340 65   HOH   HOH B . 
G 4 HOH   141 341 619  HOH   HOH B . 
G 4 HOH   142 342 1293 HOH   HOH B . 
G 4 HOH   143 343 178  HOH   HOH B . 
G 4 HOH   144 344 960  HOH   HOH B . 
G 4 HOH   145 345 362  HOH   HOH B . 
G 4 HOH   146 346 90   HOH   HOH B . 
G 4 HOH   147 347 463  HOH   HOH B . 
G 4 HOH   148 348 191  HOH   HOH B . 
G 4 HOH   149 349 335  HOH   HOH B . 
G 4 HOH   150 350 304  HOH   HOH B . 
G 4 HOH   151 351 1304 HOH   HOH B . 
G 4 HOH   152 352 623  HOH   HOH B . 
G 4 HOH   153 353 1046 HOH   HOH B . 
G 4 HOH   154 354 1280 HOH   HOH B . 
G 4 HOH   155 355 87   HOH   HOH B . 
G 4 HOH   156 356 203  HOH   HOH B . 
G 4 HOH   157 357 290  HOH   HOH B . 
G 4 HOH   158 358 541  HOH   HOH B . 
G 4 HOH   159 359 1077 HOH   HOH B . 
G 4 HOH   160 360 389  HOH   HOH B . 
G 4 HOH   161 361 479  HOH   HOH B . 
G 4 HOH   162 362 718  HOH   HOH B . 
G 4 HOH   163 363 283  HOH   HOH B . 
G 4 HOH   164 364 1072 HOH   HOH B . 
G 4 HOH   165 365 1316 HOH   HOH B . 
G 4 HOH   166 366 898  HOH   HOH B . 
G 4 HOH   167 367 340  HOH   HOH B . 
G 4 HOH   168 368 667  HOH   HOH B . 
G 4 HOH   169 369 373  HOH   HOH B . 
G 4 HOH   170 370 291  HOH   HOH B . 
G 4 HOH   171 371 615  HOH   HOH B . 
G 4 HOH   172 372 1303 HOH   HOH B . 
G 4 HOH   173 373 190  HOH   HOH B . 
G 4 HOH   174 374 310  HOH   HOH B . 
G 4 HOH   175 375 149  HOH   HOH B . 
G 4 HOH   176 376 183  HOH   HOH B . 
G 4 HOH   177 377 431  HOH   HOH B . 
G 4 HOH   178 378 1173 HOH   HOH B . 
G 4 HOH   179 379 1163 HOH   HOH B . 
G 4 HOH   180 380 418  HOH   HOH B . 
G 4 HOH   181 381 1000 HOH   HOH B . 
G 4 HOH   182 382 1311 HOH   HOH B . 
G 4 HOH   183 383 176  HOH   HOH B . 
G 4 HOH   184 384 424  HOH   HOH B . 
G 4 HOH   185 385 491  HOH   HOH B . 
G 4 HOH   186 386 248  HOH   HOH B . 
G 4 HOH   187 387 470  HOH   HOH B . 
G 4 HOH   188 388 1298 HOH   HOH B . 
G 4 HOH   189 389 981  HOH   HOH B . 
G 4 HOH   190 390 265  HOH   HOH B . 
G 4 HOH   191 391 184  HOH   HOH B . 
G 4 HOH   192 392 360  HOH   HOH B . 
G 4 HOH   193 393 410  HOH   HOH B . 
G 4 HOH   194 394 355  HOH   HOH B . 
G 4 HOH   195 395 566  HOH   HOH B . 
G 4 HOH   196 396 314  HOH   HOH B . 
G 4 HOH   197 397 274  HOH   HOH B . 
G 4 HOH   198 398 157  HOH   HOH B . 
G 4 HOH   199 399 792  HOH   HOH B . 
G 4 HOH   200 400 321  HOH   HOH B . 
G 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           7HDF 
_cell.length_a           88.727 
_cell.length_b           88.727 
_cell.length_c           39.577 
_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                         7HDF 
_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          7HDF 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_Matthews      2.15 
_exptl_crystal.density_percent_sol   42.7 
_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   2023-05-20 
_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                     7HDF 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             44.360 
_reflns.d_resolution_high            1.000 
_reflns.number_obs                   165215 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         99.400 
_reflns.pdbx_Rmerge_I_obs            0.044 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        15.800 
_reflns.B_iso_Wilson_estimate        11.510 
_reflns.pdbx_redundancy              6.400 
_reflns.pdbx_Rrim_I_all              0.048 
_reflns.pdbx_Rpim_I_all              0.019 
_reflns.pdbx_CC_half                 0.999 
_reflns.pdbx_netI_over_av_sigmaI     ? 
_reflns.pdbx_number_measured_all     1053356 
_reflns.pdbx_scaling_rejects         ? 
_reflns.pdbx_chi_squared             ? 
_reflns.Rmerge_F_all                 ? 
_reflns.Rmerge_F_obs                 ? 
_reflns.observed_criterion_F_max     ? 
_reflns.observed_criterion_F_min     ? 
_reflns.observed_criterion_I_max     ? 
_reflns.observed_criterion_I_min     ? 
_reflns.pdbx_d_res_high_opt          ? 
_reflns.pdbx_d_res_low_opt           ? 
_reflns.details                      ? 
# 
loop_
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_ordinal 
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.number_measured_obs 
_reflns_shell.number_measured_all 
_reflns_shell.number_unique_obs 
_reflns_shell.pdbx_rejects 
_reflns_shell.Rmerge_I_obs 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.pdbx_Rsym_value 
_reflns_shell.pdbx_chi_squared 
_reflns_shell.pdbx_redundancy 
_reflns_shell.percent_possible_obs 
_reflns_shell.pdbx_netI_over_sigmaI_obs 
_reflns_shell.number_possible 
_reflns_shell.number_unique_all 
_reflns_shell.Rmerge_F_all 
_reflns_shell.Rmerge_F_obs 
_reflns_shell.Rmerge_I_all 
_reflns_shell.meanI_over_sigI_all 
_reflns_shell.percent_possible_all 
_reflns_shell.pdbx_Rrim_I_all 
_reflns_shell.pdbx_Rpim_I_all 
_reflns_shell.pdbx_CC_half 
1 1 1.000 1.020  ? 33493 7336 ? 0.819 ? ? ? 4.600 ? 1.200  ? ? ? ? ? ? 89.100 0.922 0.412 0.783 
1 2 5.480 44.360 ? 7552  1097 ? 0.029 ? ? ? 6.900 ? 50.600 ? ? ? ? ? ? 99.900 0.031 0.012 0.999 
# 
_refine.entry_id                                 7HDF 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_d_res_high                            1.0000 
_refine.ls_d_res_low                             44.3600 
_refine.pdbx_ls_sigma_F                          1.350 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.ls_percent_reflns_obs                    99.3500 
_refine.ls_number_reflns_obs                     165141 
_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                          0.1417 
_refine.ls_R_factor_R_work                       0.1411 
_refine.ls_wR_factor_R_work                      ? 
_refine.ls_R_factor_R_free                       0.1539 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_percent_reflns_R_free                 4.8200 
_refine.ls_number_reflns_R_free                  7961 
_refine.ls_number_reflns_R_work                  157180 
_refine.ls_R_factor_R_free_error                 ? 
_refine.B_iso_mean                               18.2134 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.overall_SU_R_free                        ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.overall_SU_ML                            0.0800 
_refine.overall_SU_B                             ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.pdbx_solvent_vdw_probe_radii             1.1000 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.B_iso_max                                66.790 
_refine.B_iso_min                                7.940 
_refine.pdbx_overall_phase_error                 15.8700 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_R_factor_R_free_error_details         ? 
# 
_refine_hist.cycle_id                         final 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.d_res_high                       1.0000 
_refine_hist.d_res_low                        44.3600 
_refine_hist.pdbx_number_atoms_ligand         10 
_refine_hist.number_atoms_solvent             410 
_refine_hist.number_atoms_total               2962 
_refine_hist.pdbx_number_residues_total       336 
_refine_hist.pdbx_B_iso_mean_ligand           22.99 
_refine_hist.pdbx_B_iso_mean_solvent          29.06 
_refine_hist.pdbx_number_atoms_protein        2542 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
# 
loop_
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.R_factor_R_free 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.pdbx_refine_id 
1.0000 1.0100  30 87.0000  4587 . 0.3434 0.3042 . 236 0.0000 4823 . 'X-RAY DIFFRACTION' 
1.0100 1.0200  30 95.0000  5020 . 0.2722 0.2889 . 223 0.0000 5243 . 'X-RAY DIFFRACTION' 
1.0200 1.0400  30 100.0000 5239 . 0.2296 0.2193 . 258 0.0000 5497 . 'X-RAY DIFFRACTION' 
1.0400 1.0500  30 100.0000 5191 . 0.2048 0.2091 . 271 0.0000 5462 . 'X-RAY DIFFRACTION' 
1.0500 1.0600  30 100.0000 5225 . 0.1869 0.1961 . 317 0.0000 5542 . 'X-RAY DIFFRACTION' 
1.0600 1.0800  30 100.0000 5222 . 0.1726 0.1904 . 252 0.0000 5474 . 'X-RAY DIFFRACTION' 
1.0800 1.0900  30 100.0000 5270 . 0.1594 0.1787 . 270 0.0000 5540 . 'X-RAY DIFFRACTION' 
1.0900 1.1100  30 100.0000 5240 . 0.1478 0.1538 . 247 0.0000 5487 . 'X-RAY DIFFRACTION' 
1.1100 1.1300  30 100.0000 5241 . 0.1405 0.1692 . 280 0.0000 5521 . 'X-RAY DIFFRACTION' 
1.1300 1.1400  30 100.0000 5258 . 0.1326 0.1468 . 243 0.0000 5501 . 'X-RAY DIFFRACTION' 
1.1400 1.1600  30 100.0000 5301 . 0.1243 0.1477 . 252 0.0000 5553 . 'X-RAY DIFFRACTION' 
1.1600 1.1900  30 100.0000 5246 . 0.1243 0.1442 . 276 0.0000 5522 . 'X-RAY DIFFRACTION' 
1.1900 1.2100  30 100.0000 5199 . 0.1185 0.1453 . 284 0.0000 5483 . 'X-RAY DIFFRACTION' 
1.2100 1.2300  30 100.0000 5304 . 0.1154 0.1330 . 240 0.0000 5544 . 'X-RAY DIFFRACTION' 
1.2300 1.2600  30 100.0000 5191 . 0.1182 0.1314 . 262 0.0000 5453 . 'X-RAY DIFFRACTION' 
1.2600 1.2900  30 100.0000 5307 . 0.1197 0.1386 . 272 0.0000 5579 . 'X-RAY DIFFRACTION' 
1.2900 1.3200  30 100.0000 5247 . 0.1209 0.1414 . 283 0.0000 5530 . 'X-RAY DIFFRACTION' 
1.3200 1.3600  30 100.0000 5208 . 0.1237 0.1358 . 280 0.0000 5488 . 'X-RAY DIFFRACTION' 
1.3600 1.4000  30 100.0000 5292 . 0.1240 0.1619 . 250 0.0000 5542 . 'X-RAY DIFFRACTION' 
1.4000 1.4400  30 100.0000 5257 . 0.1228 0.1452 . 266 0.0000 5523 . 'X-RAY DIFFRACTION' 
1.4400 1.4900  30 100.0000 5307 . 0.1202 0.1248 . 255 0.0000 5562 . 'X-RAY DIFFRACTION' 
1.4900 1.5500  30 100.0000 5216 . 0.1180 0.1271 . 276 0.0000 5492 . 'X-RAY DIFFRACTION' 
1.5500 1.6200  30 100.0000 5298 . 0.1189 0.1354 . 265 0.0000 5563 . 'X-RAY DIFFRACTION' 
1.6200 1.7100  30 100.0000 5322 . 0.1240 0.1416 . 264 0.0000 5586 . 'X-RAY DIFFRACTION' 
1.7100 1.8200  30 100.0000 5276 . 0.1343 0.1360 . 252 0.0000 5528 . 'X-RAY DIFFRACTION' 
1.8200 1.9600  30 100.0000 5281 . 0.1350 0.1278 . 281 0.0000 5562 . 'X-RAY DIFFRACTION' 
1.9600 2.1500  30 100.0000 5296 . 0.1372 0.1438 . 285 0.0000 5581 . 'X-RAY DIFFRACTION' 
2.1500 2.4700  30 100.0000 5315 . 0.1383 0.1392 . 291 0.0000 5606 . 'X-RAY DIFFRACTION' 
2.4700 3.1100  30 100.0000 5333 . 0.1515 0.1669 . 260 0.0000 5593 . 'X-RAY DIFFRACTION' 
3.1100 44.3600 30 100.0000 5491 . 0.1520 0.1770 . 270 0.0000 5761 . 'X-RAY DIFFRACTION' 
# 
_struct.entry_id                  7HDF 
_struct.title                     
'PanDDA analysis group deposition -- Crystal structure of SARS-CoV-2 NSP3 macrodomain in complex with AVI-0003721' 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_details        ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HDF 
_struct_keywords.pdbx_keywords   'VIRAL PROTEIN, Hydrolase' 
_struct_keywords.text            'Macrodomain, ADP-ribose, SARS-CoV-2, fragment-based drug discovery, VIRAL PROTEIN, Hydrolase' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 3 ? 
F N N 4 ? 
G 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 7HDF A 3 ? 169 ? P0DTD1 1025 ? 1191 ? 3 169 
2 1 7HDF 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 7HDF SER A 1 ? UNP P0DTD1 ? ? 'expression tag' 1 1 
1 7HDF MET A 2 ? UNP P0DTD1 ? ? 'expression tag' 2 2 
2 7HDF SER B 1 ? UNP P0DTD1 ? ? 'expression tag' 1 3 
2 7HDF MET B 2 ? UNP P0DTD1 ? ? 'expression tag' 2 4 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C,D,E,F 
2 1 B,G       
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 ASP A 22  ? LYS A 31  ? ASP A 22  LYS A 31  1 ? 10 
HELX_P HELX_P2  AA2 GLY A 47  ? THR A 57  ? GLY A 47  THR A 57  1 ? 11 
HELX_P HELX_P3  AA3 ASN A 59  ? GLY A 73  ? ASN A 59  GLY A 73  1 ? 15 
HELX_P HELX_P4  AA4 ASN A 99  ? GLY A 103 ? ASN A 99  GLY A 103 5 ? 5  
HELX_P HELX_P5  AA5 GLN A 107 ? ASN A 115 ? GLN A 107 ASN A 115 1 ? 9  
HELX_P HELX_P6  AA6 PHE A 116 ? HIS A 119 ? PHE A 116 HIS A 119 5 ? 4  
HELX_P HELX_P7  AA7 ALA A 129 ? GLY A 133 ? ALA A 129 GLY A 133 5 ? 5  
HELX_P HELX_P8  AA8 ASP A 135 ? VAL A 147 ? ASP A 135 VAL A 147 1 ? 13 
HELX_P HELX_P9  AA9 ASP A 157 ? SER A 167 ? ASP A 157 SER A 167 1 ? 11 
HELX_P HELX_P10 AB1 ASP B 22  ? LYS B 31  ? ASP B 22  LYS B 31  1 ? 10 
HELX_P HELX_P11 AB2 GLY B 47  ? THR B 57  ? GLY B 47  THR B 57  1 ? 11 
HELX_P HELX_P12 AB3 ASN B 59  ? GLY B 73  ? ASN B 59  GLY B 73  1 ? 15 
HELX_P HELX_P13 AB4 ASN B 99  ? GLY B 103 ? ASN B 99  GLY B 103 5 ? 5  
HELX_P HELX_P14 AB5 ASP B 105 ? GLN B 107 ? ASP B 105 GLN B 107 5 ? 3  
HELX_P HELX_P15 AB6 LEU B 108 ? ASN B 115 ? LEU B 108 ASN B 115 1 ? 8  
HELX_P HELX_P16 AB7 PHE B 116 ? HIS B 119 ? PHE B 116 HIS B 119 5 ? 4  
HELX_P HELX_P17 AB8 ALA B 129 ? GLY B 133 ? ALA B 129 GLY B 133 5 ? 5  
HELX_P HELX_P18 AB9 ASP B 135 ? VAL B 147 ? ASP B 135 VAL B 147 1 ? 13 
HELX_P HELX_P19 AC1 ASP B 157 ? LEU B 169 ? ASP B 157 LEU B 169 1 ? 13 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 4 ? 
AA2 ? 3 ? 
AA3 ? 4 ? 
AA4 ? 3 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? parallel      
AA1 3 4 ? parallel      
AA2 1 2 ? parallel      
AA2 2 3 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? parallel      
AA3 3 4 ? parallel      
AA4 1 2 ? parallel      
AA4 2 3 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 LEU A 10  ? LYS A 11  ? LEU A 10  LYS A 11  
AA1 2 VAL A 16  ? ASN A 20  ? VAL A 16  ASN A 20  
AA1 3 ASN A 150 ? VAL A 155 ? ASN A 150 VAL A 155 
AA1 4 VAL A 121 ? ALA A 124 ? VAL A 121 ALA A 124 
AA2 1 VAL A 34  ? ALA A 38  ? VAL A 34  ALA A 38  
AA2 2 HIS A 91  ? VAL A 95  ? HIS A 91  VAL A 95  
AA2 3 SER A 80  ? SER A 84  ? SER A 80  SER A 84  
AA3 1 LEU B 10  ? LYS B 11  ? LEU B 10  LYS B 11  
AA3 2 VAL B 16  ? ASN B 20  ? VAL B 16  ASN B 20  
AA3 3 ASN B 150 ? VAL B 155 ? ASN B 150 VAL B 155 
AA3 4 VAL B 121 ? ALA B 124 ? VAL B 121 ALA B 124 
AA4 1 VAL B 34  ? ALA B 38  ? VAL B 34  ALA B 38  
AA4 2 HIS B 91  ? VAL B 95  ? HIS B 91  VAL B 95  
AA4 3 SER B 80  ? SER B 84  ? SER B 80  SER B 84  
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N LEU A 10  ? N LEU A 10  O ILE A 18  ? O ILE A 18  
AA1 2 3 N TYR A 17  ? N TYR A 17  O LEU A 153 ? O LEU A 153 
AA1 3 4 O TYR A 152 ? O TYR A 152 N LEU A 122 ? N LEU A 122 
AA2 1 2 N ASN A 37  ? N ASN A 37  O VAL A 95  ? O VAL A 95  
AA2 2 3 O CYS A 92  ? O CYS A 92  N LEU A 83  ? N LEU A 83  
AA3 1 2 N LEU B 10  ? N LEU B 10  O ILE B 18  ? O ILE B 18  
AA3 2 3 N TYR B 17  ? N TYR B 17  O LEU B 153 ? O LEU B 153 
AA3 3 4 O TYR B 152 ? O TYR B 152 N LEU B 122 ? N LEU B 122 
AA4 1 2 N ASN B 37  ? N ASN B 37  O 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                   7HDF 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
_pdbx_validate_close_contact.id               1 
_pdbx_validate_close_contact.PDB_model_num    1 
_pdbx_validate_close_contact.auth_atom_id_1   O 
_pdbx_validate_close_contact.auth_asym_id_1   A 
_pdbx_validate_close_contact.auth_comp_id_1   SER 
_pdbx_validate_close_contact.auth_seq_id_1    167 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   B 
_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    501 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             2.10 
# 
_pdbx_validate_symm_contact.id                1 
_pdbx_validate_symm_contact.PDB_model_num     1 
_pdbx_validate_symm_contact.auth_atom_id_1    O 
_pdbx_validate_symm_contact.auth_asym_id_1    A 
_pdbx_validate_symm_contact.auth_comp_id_1    ASP 
_pdbx_validate_symm_contact.auth_seq_id_1     66 
_pdbx_validate_symm_contact.PDB_ins_code_1    ? 
_pdbx_validate_symm_contact.label_alt_id_1    ? 
_pdbx_validate_symm_contact.site_symmetry_1   1_555 
_pdbx_validate_symm_contact.auth_atom_id_2    HG 
_pdbx_validate_symm_contact.auth_asym_id_2    B 
_pdbx_validate_symm_contact.auth_comp_id_2    SER 
_pdbx_validate_symm_contact.auth_seq_id_2     1 
_pdbx_validate_symm_contact.PDB_ins_code_2    ? 
_pdbx_validate_symm_contact.label_alt_id_2    B 
_pdbx_validate_symm_contact.site_symmetry_2   2_655 
_pdbx_validate_symm_contact.dist              1.59 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 HIS A 86  ? ? 55.55   -133.54 
2 1 SER A 128 ? B 69.27   -3.30   
3 1 PHE A 168 ? B -134.22 -68.94  
4 1 HIS B 86  ? ? 57.40   -128.07 
# 
_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 707 ? 5.94 . 
2 1 O ? A HOH 708 ? 6.06 . 
3 1 O ? A HOH 709 ? 7.59 . 
4 1 O ? B HOH 401 ? 6.36 . 
# 
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 
A1A77 O1   O N N 1   
A1A77 C1   C N N 2   
A1A77 C2   C N N 3   
A1A77 C3   C N N 4   
A1A77 C4   C Y N 5   
A1A77 C5   C Y N 6   
A1A77 C6   C Y N 7   
A1A77 C7   C Y N 8   
A1A77 C8   C Y N 9   
A1A77 C10  C N R 10  
A1A77 C11  C N N 11  
A1A77 C12  C N N 12  
A1A77 C9   C Y N 13  
A1A77 N1   N N N 14  
A1A77 N2   N Y N 15  
A1A77 N3   N Y N 16  
A1A77 N4   N Y N 17  
A1A77 N5   N N N 18  
A1A77 H15  H N N 19  
A1A77 H2   H N N 20  
A1A77 H3   H N N 21  
A1A77 H4   H N N 22  
A1A77 H5   H N N 23  
A1A77 H6   H N N 24  
A1A77 H7   H N N 25  
A1A77 H8   H N N 26  
A1A77 H9   H N N 27  
A1A77 H10  H N N 28  
A1A77 H1   H N N 29  
A1A77 H14  H N N 30  
A1A77 H13  H N N 31  
A1A77 H17  H N N 32  
A1A77 H16  H N N 33  
A1A77 H11  H N N 34  
A1A77 H12  H N N 35  
ALA   N    N N N 36  
ALA   CA   C N S 37  
ALA   C    C N N 38  
ALA   O    O N N 39  
ALA   CB   C N N 40  
ALA   OXT  O N N 41  
ALA   H    H N N 42  
ALA   H2   H N N 43  
ALA   HA   H N N 44  
ALA   HB1  H N N 45  
ALA   HB2  H N N 46  
ALA   HB3  H N N 47  
ALA   HXT  H N N 48  
ARG   N    N N N 49  
ARG   CA   C N S 50  
ARG   C    C N N 51  
ARG   O    O N N 52  
ARG   CB   C N N 53  
ARG   CG   C N N 54  
ARG   CD   C N N 55  
ARG   NE   N N N 56  
ARG   CZ   C N N 57  
ARG   NH1  N N N 58  
ARG   NH2  N N N 59  
ARG   OXT  O N N 60  
ARG   H    H N N 61  
ARG   H2   H N N 62  
ARG   HA   H N N 63  
ARG   HB2  H N N 64  
ARG   HB3  H N N 65  
ARG   HG2  H N N 66  
ARG   HG3  H N N 67  
ARG   HD2  H N N 68  
ARG   HD3  H N N 69  
ARG   HE   H N N 70  
ARG   HH11 H N N 71  
ARG   HH12 H N N 72  
ARG   HH21 H N N 73  
ARG   HH22 H N N 74  
ARG   HXT  H N N 75  
ASN   N    N N N 76  
ASN   CA   C N S 77  
ASN   C    C N N 78  
ASN   O    O N N 79  
ASN   CB   C N N 80  
ASN   CG   C N N 81  
ASN   OD1  O N N 82  
ASN   ND2  N N N 83  
ASN   OXT  O N N 84  
ASN   H    H N N 85  
ASN   H2   H N N 86  
ASN   HA   H N N 87  
ASN   HB2  H N N 88  
ASN   HB3  H N N 89  
ASN   HD21 H N N 90  
ASN   HD22 H N N 91  
ASN   HXT  H N N 92  
ASP   N    N N N 93  
ASP   CA   C N S 94  
ASP   C    C N N 95  
ASP   O    O N N 96  
ASP   CB   C N N 97  
ASP   CG   C N N 98  
ASP   OD1  O N N 99  
ASP   OD2  O N N 100 
ASP   OXT  O N N 101 
ASP   H    H N N 102 
ASP   H2   H N N 103 
ASP   HA   H N N 104 
ASP   HB2  H N N 105 
ASP   HB3  H N N 106 
ASP   HD2  H N N 107 
ASP   HXT  H N N 108 
CYS   N    N N N 109 
CYS   CA   C N R 110 
CYS   C    C N N 111 
CYS   O    O N N 112 
CYS   CB   C N N 113 
CYS   SG   S N N 114 
CYS   OXT  O N N 115 
CYS   H    H N N 116 
CYS   H2   H N N 117 
CYS   HA   H N N 118 
CYS   HB2  H N N 119 
CYS   HB3  H N N 120 
CYS   HG   H N N 121 
CYS   HXT  H N N 122 
DMS   S    S N N 123 
DMS   O    O N N 124 
DMS   C1   C N N 125 
DMS   C2   C N N 126 
DMS   H11  H N N 127 
DMS   H12  H N N 128 
DMS   H13  H N N 129 
DMS   H21  H N N 130 
DMS   H22  H N N 131 
DMS   H23  H N N 132 
GLN   N    N N N 133 
GLN   CA   C N S 134 
GLN   C    C N N 135 
GLN   O    O N N 136 
GLN   CB   C N N 137 
GLN   CG   C N N 138 
GLN   CD   C N N 139 
GLN   OE1  O N N 140 
GLN   NE2  N N N 141 
GLN   OXT  O N N 142 
GLN   H    H N N 143 
GLN   H2   H N N 144 
GLN   HA   H N N 145 
GLN   HB2  H N N 146 
GLN   HB3  H N N 147 
GLN   HG2  H N N 148 
GLN   HG3  H N N 149 
GLN   HE21 H N N 150 
GLN   HE22 H N N 151 
GLN   HXT  H N N 152 
GLU   N    N N N 153 
GLU   CA   C N S 154 
GLU   C    C N N 155 
GLU   O    O N N 156 
GLU   CB   C N N 157 
GLU   CG   C N N 158 
GLU   CD   C N N 159 
GLU   OE1  O N N 160 
GLU   OE2  O N N 161 
GLU   OXT  O N N 162 
GLU   H    H N N 163 
GLU   H2   H N N 164 
GLU   HA   H N N 165 
GLU   HB2  H N N 166 
GLU   HB3  H N N 167 
GLU   HG2  H N N 168 
GLU   HG3  H N N 169 
GLU   HE2  H N N 170 
GLU   HXT  H N N 171 
GLY   N    N N N 172 
GLY   CA   C N N 173 
GLY   C    C N N 174 
GLY   O    O N N 175 
GLY   OXT  O N N 176 
GLY   H    H N N 177 
GLY   H2   H N N 178 
GLY   HA2  H N N 179 
GLY   HA3  H N N 180 
GLY   HXT  H N N 181 
HIS   N    N N N 182 
HIS   CA   C N S 183 
HIS   C    C N N 184 
HIS   O    O N N 185 
HIS   CB   C N N 186 
HIS   CG   C Y N 187 
HIS   ND1  N Y N 188 
HIS   CD2  C Y N 189 
HIS   CE1  C Y N 190 
HIS   NE2  N Y N 191 
HIS   OXT  O N N 192 
HIS   H    H N N 193 
HIS   H2   H N N 194 
HIS   HA   H N N 195 
HIS   HB2  H N N 196 
HIS   HB3  H N N 197 
HIS   HD1  H N N 198 
HIS   HD2  H N N 199 
HIS   HE1  H N N 200 
HIS   HE2  H N N 201 
HIS   HXT  H N N 202 
HOH   O    O N N 203 
HOH   H1   H N N 204 
HOH   H2   H N N 205 
ILE   N    N N N 206 
ILE   CA   C N S 207 
ILE   C    C N N 208 
ILE   O    O N N 209 
ILE   CB   C N S 210 
ILE   CG1  C N N 211 
ILE   CG2  C N N 212 
ILE   CD1  C N N 213 
ILE   OXT  O N N 214 
ILE   H    H N N 215 
ILE   H2   H N N 216 
ILE   HA   H N N 217 
ILE   HB   H N N 218 
ILE   HG12 H N N 219 
ILE   HG13 H N N 220 
ILE   HG21 H N N 221 
ILE   HG22 H N N 222 
ILE   HG23 H N N 223 
ILE   HD11 H N N 224 
ILE   HD12 H N N 225 
ILE   HD13 H N N 226 
ILE   HXT  H N N 227 
LEU   N    N N N 228 
LEU   CA   C N S 229 
LEU   C    C N N 230 
LEU   O    O N N 231 
LEU   CB   C N N 232 
LEU   CG   C N N 233 
LEU   CD1  C N N 234 
LEU   CD2  C N N 235 
LEU   OXT  O N N 236 
LEU   H    H N N 237 
LEU   H2   H N N 238 
LEU   HA   H N N 239 
LEU   HB2  H N N 240 
LEU   HB3  H N N 241 
LEU   HG   H N N 242 
LEU   HD11 H N N 243 
LEU   HD12 H N N 244 
LEU   HD13 H N N 245 
LEU   HD21 H N N 246 
LEU   HD22 H N N 247 
LEU   HD23 H N N 248 
LEU   HXT  H N N 249 
LYS   N    N N N 250 
LYS   CA   C N S 251 
LYS   C    C N N 252 
LYS   O    O N N 253 
LYS   CB   C N N 254 
LYS   CG   C N N 255 
LYS   CD   C N N 256 
LYS   CE   C N N 257 
LYS   NZ   N N N 258 
LYS   OXT  O N N 259 
LYS   H    H N N 260 
LYS   H2   H N N 261 
LYS   HA   H N N 262 
LYS   HB2  H N N 263 
LYS   HB3  H N N 264 
LYS   HG2  H N N 265 
LYS   HG3  H N N 266 
LYS   HD2  H N N 267 
LYS   HD3  H N N 268 
LYS   HE2  H N N 269 
LYS   HE3  H N N 270 
LYS   HZ1  H N N 271 
LYS   HZ2  H N N 272 
LYS   HZ3  H N N 273 
LYS   HXT  H N N 274 
MET   N    N N N 275 
MET   CA   C N S 276 
MET   C    C N N 277 
MET   O    O N N 278 
MET   CB   C N N 279 
MET   CG   C N N 280 
MET   SD   S N N 281 
MET   CE   C N N 282 
MET   OXT  O N N 283 
MET   H    H N N 284 
MET   H2   H N N 285 
MET   HA   H N N 286 
MET   HB2  H N N 287 
MET   HB3  H N N 288 
MET   HG2  H N N 289 
MET   HG3  H N N 290 
MET   HE1  H N N 291 
MET   HE2  H N N 292 
MET   HE3  H N N 293 
MET   HXT  H N N 294 
PHE   N    N N N 295 
PHE   CA   C N S 296 
PHE   C    C N N 297 
PHE   O    O N N 298 
PHE   CB   C N N 299 
PHE   CG   C Y N 300 
PHE   CD1  C Y N 301 
PHE   CD2  C Y N 302 
PHE   CE1  C Y N 303 
PHE   CE2  C Y N 304 
PHE   CZ   C Y N 305 
PHE   OXT  O N N 306 
PHE   H    H N N 307 
PHE   H2   H N N 308 
PHE   HA   H N N 309 
PHE   HB2  H N N 310 
PHE   HB3  H N N 311 
PHE   HD1  H N N 312 
PHE   HD2  H N N 313 
PHE   HE1  H N N 314 
PHE   HE2  H N N 315 
PHE   HZ   H N N 316 
PHE   HXT  H N N 317 
PRO   N    N N N 318 
PRO   CA   C N S 319 
PRO   C    C N N 320 
PRO   O    O N N 321 
PRO   CB   C N N 322 
PRO   CG   C N N 323 
PRO   CD   C N N 324 
PRO   OXT  O N N 325 
PRO   H    H N N 326 
PRO   HA   H N N 327 
PRO   HB2  H N N 328 
PRO   HB3  H N N 329 
PRO   HG2  H N N 330 
PRO   HG3  H N N 331 
PRO   HD2  H N N 332 
PRO   HD3  H N N 333 
PRO   HXT  H N N 334 
SER   N    N N N 335 
SER   CA   C N S 336 
SER   C    C N N 337 
SER   O    O N N 338 
SER   CB   C N N 339 
SER   OG   O N N 340 
SER   OXT  O N N 341 
SER   H    H N N 342 
SER   H2   H N N 343 
SER   HA   H N N 344 
SER   HB2  H N N 345 
SER   HB3  H N N 346 
SER   HG   H N N 347 
SER   HXT  H N N 348 
THR   N    N N N 349 
THR   CA   C N S 350 
THR   C    C N N 351 
THR   O    O N N 352 
THR   CB   C N R 353 
THR   OG1  O N N 354 
THR   CG2  C N N 355 
THR   OXT  O N N 356 
THR   H    H N N 357 
THR   H2   H N N 358 
THR   HA   H N N 359 
THR   HB   H N N 360 
THR   HG1  H N N 361 
THR   HG21 H N N 362 
THR   HG22 H N N 363 
THR   HG23 H N N 364 
THR   HXT  H N N 365 
TYR   N    N N N 366 
TYR   CA   C N S 367 
TYR   C    C N N 368 
TYR   O    O N N 369 
TYR   CB   C N N 370 
TYR   CG   C Y N 371 
TYR   CD1  C Y N 372 
TYR   CD2  C Y N 373 
TYR   CE1  C Y N 374 
TYR   CE2  C Y N 375 
TYR   CZ   C Y N 376 
TYR   OH   O N N 377 
TYR   OXT  O N N 378 
TYR   H    H N N 379 
TYR   H2   H N N 380 
TYR   HA   H N N 381 
TYR   HB2  H N N 382 
TYR   HB3  H N N 383 
TYR   HD1  H N N 384 
TYR   HD2  H N N 385 
TYR   HE1  H N N 386 
TYR   HE2  H N N 387 
TYR   HH   H N N 388 
TYR   HXT  H N N 389 
VAL   N    N N N 390 
VAL   CA   C N S 391 
VAL   C    C N N 392 
VAL   O    O N N 393 
VAL   CB   C N N 394 
VAL   CG1  C N N 395 
VAL   CG2  C N N 396 
VAL   OXT  O N N 397 
VAL   H    H N N 398 
VAL   H2   H N N 399 
VAL   HA   H N N 400 
VAL   HB   H N N 401 
VAL   HG11 H N N 402 
VAL   HG12 H N N 403 
VAL   HG13 H N N 404 
VAL   HG21 H N N 405 
VAL   HG22 H N N 406 
VAL   HG23 H N N 407 
VAL   HXT  H N N 408 
# 
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 
A1A77 C1  N5   sing N N 1   
A1A77 C2  N5   sing N N 2   
A1A77 C2  C3   sing N N 3   
A1A77 N5  C12  sing N N 4   
A1A77 C12 C10  sing N N 5   
A1A77 C3  N1   sing N N 6   
A1A77 C11 C10  sing N N 7   
A1A77 C11 O1   sing N N 8   
A1A77 C10 N1   sing N N 9   
A1A77 N1  C4   sing N N 10  
A1A77 C8  C7   sing Y N 11  
A1A77 C8  C9   doub Y N 12  
A1A77 C4  C7   doub Y N 13  
A1A77 C4  N2   sing Y N 14  
A1A77 C7  C6   sing Y N 15  
A1A77 C9  N4   sing Y N 16  
A1A77 N2  C5   doub Y N 17  
A1A77 C6  N4   sing Y N 18  
A1A77 C6  N3   doub Y N 19  
A1A77 C5  N3   sing Y N 20  
A1A77 O1  H15  sing N N 21  
A1A77 C1  H2   sing N N 22  
A1A77 C1  H3   sing N N 23  
A1A77 C1  H4   sing N N 24  
A1A77 C2  H5   sing N N 25  
A1A77 C2  H6   sing N N 26  
A1A77 C3  H7   sing N N 27  
A1A77 C3  H8   sing N N 28  
A1A77 C5  H9   sing N N 29  
A1A77 C8  H10  sing N N 30  
A1A77 C10 H1   sing N N 31  
A1A77 C11 H14  sing N N 32  
A1A77 C11 H13  sing N N 33  
A1A77 C12 H17  sing N N 34  
A1A77 C12 H16  sing N N 35  
A1A77 C9  H11  sing N N 36  
A1A77 N4  H12  sing N N 37  
ALA   N   CA   sing N N 38  
ALA   N   H    sing N N 39  
ALA   N   H2   sing N N 40  
ALA   CA  C    sing N N 41  
ALA   CA  CB   sing N N 42  
ALA   CA  HA   sing N N 43  
ALA   C   O    doub N N 44  
ALA   C   OXT  sing N N 45  
ALA   CB  HB1  sing N N 46  
ALA   CB  HB2  sing N N 47  
ALA   CB  HB3  sing N N 48  
ALA   OXT HXT  sing N N 49  
ARG   N   CA   sing N N 50  
ARG   N   H    sing N N 51  
ARG   N   H2   sing N N 52  
ARG   CA  C    sing N N 53  
ARG   CA  CB   sing N N 54  
ARG   CA  HA   sing N N 55  
ARG   C   O    doub N N 56  
ARG   C   OXT  sing N N 57  
ARG   CB  CG   sing N N 58  
ARG   CB  HB2  sing N N 59  
ARG   CB  HB3  sing N N 60  
ARG   CG  CD   sing N N 61  
ARG   CG  HG2  sing N N 62  
ARG   CG  HG3  sing N N 63  
ARG   CD  NE   sing N N 64  
ARG   CD  HD2  sing N N 65  
ARG   CD  HD3  sing N N 66  
ARG   NE  CZ   sing N N 67  
ARG   NE  HE   sing N N 68  
ARG   CZ  NH1  sing N N 69  
ARG   CZ  NH2  doub N N 70  
ARG   NH1 HH11 sing N N 71  
ARG   NH1 HH12 sing N N 72  
ARG   NH2 HH21 sing N N 73  
ARG   NH2 HH22 sing N N 74  
ARG   OXT HXT  sing N N 75  
ASN   N   CA   sing N N 76  
ASN   N   H    sing N N 77  
ASN   N   H2   sing N N 78  
ASN   CA  C    sing N N 79  
ASN   CA  CB   sing N N 80  
ASN   CA  HA   sing N N 81  
ASN   C   O    doub N N 82  
ASN   C   OXT  sing N N 83  
ASN   CB  CG   sing N N 84  
ASN   CB  HB2  sing N N 85  
ASN   CB  HB3  sing N N 86  
ASN   CG  OD1  doub N N 87  
ASN   CG  ND2  sing N N 88  
ASN   ND2 HD21 sing N N 89  
ASN   ND2 HD22 sing N N 90  
ASN   OXT HXT  sing N N 91  
ASP   N   CA   sing N N 92  
ASP   N   H    sing N N 93  
ASP   N   H2   sing N N 94  
ASP   CA  C    sing N N 95  
ASP   CA  CB   sing N N 96  
ASP   CA  HA   sing N N 97  
ASP   C   O    doub N N 98  
ASP   C   OXT  sing N N 99  
ASP   CB  CG   sing N N 100 
ASP   CB  HB2  sing N N 101 
ASP   CB  HB3  sing N N 102 
ASP   CG  OD1  doub N N 103 
ASP   CG  OD2  sing N N 104 
ASP   OD2 HD2  sing N N 105 
ASP   OXT HXT  sing N N 106 
CYS   N   CA   sing N N 107 
CYS   N   H    sing N N 108 
CYS   N   H2   sing N N 109 
CYS   CA  C    sing N N 110 
CYS   CA  CB   sing N N 111 
CYS   CA  HA   sing N N 112 
CYS   C   O    doub N N 113 
CYS   C   OXT  sing N N 114 
CYS   CB  SG   sing N N 115 
CYS   CB  HB2  sing N N 116 
CYS   CB  HB3  sing N N 117 
CYS   SG  HG   sing N N 118 
CYS   OXT HXT  sing N N 119 
DMS   S   O    doub N N 120 
DMS   S   C1   sing N N 121 
DMS   S   C2   sing N N 122 
DMS   C1  H11  sing N N 123 
DMS   C1  H12  sing N N 124 
DMS   C1  H13  sing N N 125 
DMS   C2  H21  sing N N 126 
DMS   C2  H22  sing N N 127 
DMS   C2  H23  sing N N 128 
GLN   N   CA   sing N N 129 
GLN   N   H    sing N N 130 
GLN   N   H2   sing N N 131 
GLN   CA  C    sing N N 132 
GLN   CA  CB   sing N N 133 
GLN   CA  HA   sing N N 134 
GLN   C   O    doub N N 135 
GLN   C   OXT  sing N N 136 
GLN   CB  CG   sing N N 137 
GLN   CB  HB2  sing N N 138 
GLN   CB  HB3  sing N N 139 
GLN   CG  CD   sing N N 140 
GLN   CG  HG2  sing N N 141 
GLN   CG  HG3  sing N N 142 
GLN   CD  OE1  doub N N 143 
GLN   CD  NE2  sing N N 144 
GLN   NE2 HE21 sing N N 145 
GLN   NE2 HE22 sing N N 146 
GLN   OXT HXT  sing N N 147 
GLU   N   CA   sing N N 148 
GLU   N   H    sing N N 149 
GLU   N   H2   sing N N 150 
GLU   CA  C    sing N N 151 
GLU   CA  CB   sing N N 152 
GLU   CA  HA   sing N N 153 
GLU   C   O    doub N N 154 
GLU   C   OXT  sing N N 155 
GLU   CB  CG   sing N N 156 
GLU   CB  HB2  sing N N 157 
GLU   CB  HB3  sing N N 158 
GLU   CG  CD   sing N N 159 
GLU   CG  HG2  sing N N 160 
GLU   CG  HG3  sing N N 161 
GLU   CD  OE1  doub N N 162 
GLU   CD  OE2  sing N N 163 
GLU   OE2 HE2  sing N N 164 
GLU   OXT HXT  sing N N 165 
GLY   N   CA   sing N N 166 
GLY   N   H    sing N N 167 
GLY   N   H2   sing N N 168 
GLY   CA  C    sing N N 169 
GLY   CA  HA2  sing N N 170 
GLY   CA  HA3  sing N N 171 
GLY   C   O    doub N N 172 
GLY   C   OXT  sing N N 173 
GLY   OXT HXT  sing N N 174 
HIS   N   CA   sing N N 175 
HIS   N   H    sing N N 176 
HIS   N   H2   sing N N 177 
HIS   CA  C    sing N N 178 
HIS   CA  CB   sing N N 179 
HIS   CA  HA   sing N N 180 
HIS   C   O    doub N N 181 
HIS   C   OXT  sing N N 182 
HIS   CB  CG   sing N N 183 
HIS   CB  HB2  sing N N 184 
HIS   CB  HB3  sing N N 185 
HIS   CG  ND1  sing Y N 186 
HIS   CG  CD2  doub Y N 187 
HIS   ND1 CE1  doub Y N 188 
HIS   ND1 HD1  sing N N 189 
HIS   CD2 NE2  sing Y N 190 
HIS   CD2 HD2  sing N N 191 
HIS   CE1 NE2  sing Y N 192 
HIS   CE1 HE1  sing N N 193 
HIS   NE2 HE2  sing N N 194 
HIS   OXT HXT  sing N N 195 
HOH   O   H1   sing N N 196 
HOH   O   H2   sing N N 197 
ILE   N   CA   sing N N 198 
ILE   N   H    sing N N 199 
ILE   N   H2   sing N N 200 
ILE   CA  C    sing N N 201 
ILE   CA  CB   sing N N 202 
ILE   CA  HA   sing N N 203 
ILE   C   O    doub N N 204 
ILE   C   OXT  sing N N 205 
ILE   CB  CG1  sing N N 206 
ILE   CB  CG2  sing N N 207 
ILE   CB  HB   sing N N 208 
ILE   CG1 CD1  sing N N 209 
ILE   CG1 HG12 sing N N 210 
ILE   CG1 HG13 sing N N 211 
ILE   CG2 HG21 sing N N 212 
ILE   CG2 HG22 sing N N 213 
ILE   CG2 HG23 sing N N 214 
ILE   CD1 HD11 sing N N 215 
ILE   CD1 HD12 sing N N 216 
ILE   CD1 HD13 sing N N 217 
ILE   OXT HXT  sing N N 218 
LEU   N   CA   sing N N 219 
LEU   N   H    sing N N 220 
LEU   N   H2   sing N N 221 
LEU   CA  C    sing N N 222 
LEU   CA  CB   sing N N 223 
LEU   CA  HA   sing N N 224 
LEU   C   O    doub N N 225 
LEU   C   OXT  sing N N 226 
LEU   CB  CG   sing N N 227 
LEU   CB  HB2  sing N N 228 
LEU   CB  HB3  sing N N 229 
LEU   CG  CD1  sing N N 230 
LEU   CG  CD2  sing N N 231 
LEU   CG  HG   sing N N 232 
LEU   CD1 HD11 sing N N 233 
LEU   CD1 HD12 sing N N 234 
LEU   CD1 HD13 sing N N 235 
LEU   CD2 HD21 sing N N 236 
LEU   CD2 HD22 sing N N 237 
LEU   CD2 HD23 sing N N 238 
LEU   OXT HXT  sing N N 239 
LYS   N   CA   sing N N 240 
LYS   N   H    sing N N 241 
LYS   N   H2   sing N N 242 
LYS   CA  C    sing N N 243 
LYS   CA  CB   sing N N 244 
LYS   CA  HA   sing N N 245 
LYS   C   O    doub N N 246 
LYS   C   OXT  sing N N 247 
LYS   CB  CG   sing N N 248 
LYS   CB  HB2  sing N N 249 
LYS   CB  HB3  sing N N 250 
LYS   CG  CD   sing N N 251 
LYS   CG  HG2  sing N N 252 
LYS   CG  HG3  sing N N 253 
LYS   CD  CE   sing N N 254 
LYS   CD  HD2  sing N N 255 
LYS   CD  HD3  sing N N 256 
LYS   CE  NZ   sing N N 257 
LYS   CE  HE2  sing N N 258 
LYS   CE  HE3  sing N N 259 
LYS   NZ  HZ1  sing N N 260 
LYS   NZ  HZ2  sing N N 261 
LYS   NZ  HZ3  sing N N 262 
LYS   OXT HXT  sing N N 263 
MET   N   CA   sing N N 264 
MET   N   H    sing N N 265 
MET   N   H2   sing N N 266 
MET   CA  C    sing N N 267 
MET   CA  CB   sing N N 268 
MET   CA  HA   sing N N 269 
MET   C   O    doub N N 270 
MET   C   OXT  sing N N 271 
MET   CB  CG   sing N N 272 
MET   CB  HB2  sing N N 273 
MET   CB  HB3  sing N N 274 
MET   CG  SD   sing N N 275 
MET   CG  HG2  sing N N 276 
MET   CG  HG3  sing N N 277 
MET   SD  CE   sing N N 278 
MET   CE  HE1  sing N N 279 
MET   CE  HE2  sing N N 280 
MET   CE  HE3  sing N N 281 
MET   OXT HXT  sing N N 282 
PHE   N   CA   sing N N 283 
PHE   N   H    sing N N 284 
PHE   N   H2   sing N N 285 
PHE   CA  C    sing N N 286 
PHE   CA  CB   sing N N 287 
PHE   CA  HA   sing N N 288 
PHE   C   O    doub N N 289 
PHE   C   OXT  sing N N 290 
PHE   CB  CG   sing N N 291 
PHE   CB  HB2  sing N N 292 
PHE   CB  HB3  sing N N 293 
PHE   CG  CD1  doub Y N 294 
PHE   CG  CD2  sing Y N 295 
PHE   CD1 CE1  sing Y N 296 
PHE   CD1 HD1  sing N N 297 
PHE   CD2 CE2  doub Y N 298 
PHE   CD2 HD2  sing N N 299 
PHE   CE1 CZ   doub Y N 300 
PHE   CE1 HE1  sing N N 301 
PHE   CE2 CZ   sing Y N 302 
PHE   CE2 HE2  sing N N 303 
PHE   CZ  HZ   sing N N 304 
PHE   OXT HXT  sing N N 305 
PRO   N   CA   sing N N 306 
PRO   N   CD   sing N N 307 
PRO   N   H    sing N N 308 
PRO   CA  C    sing N N 309 
PRO   CA  CB   sing N N 310 
PRO   CA  HA   sing N N 311 
PRO   C   O    doub N N 312 
PRO   C   OXT  sing N N 313 
PRO   CB  CG   sing N N 314 
PRO   CB  HB2  sing N N 315 
PRO   CB  HB3  sing N N 316 
PRO   CG  CD   sing N N 317 
PRO   CG  HG2  sing N N 318 
PRO   CG  HG3  sing N N 319 
PRO   CD  HD2  sing N N 320 
PRO   CD  HD3  sing N N 321 
PRO   OXT HXT  sing N N 322 
SER   N   CA   sing N N 323 
SER   N   H    sing N N 324 
SER   N   H2   sing N N 325 
SER   CA  C    sing N N 326 
SER   CA  CB   sing N N 327 
SER   CA  HA   sing N N 328 
SER   C   O    doub N N 329 
SER   C   OXT  sing N N 330 
SER   CB  OG   sing N N 331 
SER   CB  HB2  sing N N 332 
SER   CB  HB3  sing N N 333 
SER   OG  HG   sing N N 334 
SER   OXT HXT  sing N N 335 
THR   N   CA   sing N N 336 
THR   N   H    sing N N 337 
THR   N   H2   sing N N 338 
THR   CA  C    sing N N 339 
THR   CA  CB   sing N N 340 
THR   CA  HA   sing N N 341 
THR   C   O    doub N N 342 
THR   C   OXT  sing N N 343 
THR   CB  OG1  sing N N 344 
THR   CB  CG2  sing N N 345 
THR   CB  HB   sing N N 346 
THR   OG1 HG1  sing N N 347 
THR   CG2 HG21 sing N N 348 
THR   CG2 HG22 sing N N 349 
THR   CG2 HG23 sing N N 350 
THR   OXT HXT  sing N N 351 
TYR   N   CA   sing N N 352 
TYR   N   H    sing N N 353 
TYR   N   H2   sing N N 354 
TYR   CA  C    sing N N 355 
TYR   CA  CB   sing N N 356 
TYR   CA  HA   sing N N 357 
TYR   C   O    doub N N 358 
TYR   C   OXT  sing N N 359 
TYR   CB  CG   sing N N 360 
TYR   CB  HB2  sing N N 361 
TYR   CB  HB3  sing N N 362 
TYR   CG  CD1  doub Y N 363 
TYR   CG  CD2  sing Y N 364 
TYR   CD1 CE1  sing Y N 365 
TYR   CD1 HD1  sing N N 366 
TYR   CD2 CE2  doub Y N 367 
TYR   CD2 HD2  sing N N 368 
TYR   CE1 CZ   doub Y N 369 
TYR   CE1 HE1  sing N N 370 
TYR   CE2 CZ   sing Y N 371 
TYR   CE2 HE2  sing N N 372 
TYR   CZ  OH   sing N N 373 
TYR   OH  HH   sing N N 374 
TYR   OXT HXT  sing N N 375 
VAL   N   CA   sing N N 376 
VAL   N   H    sing N N 377 
VAL   N   H2   sing N N 378 
VAL   CA  C    sing N N 379 
VAL   CA  CB   sing N N 380 
VAL   CA  HA   sing N N 381 
VAL   C   O    doub N N 382 
VAL   C   OXT  sing N N 383 
VAL   CB  CG1  sing N N 384 
VAL   CB  CG2  sing N N 385 
VAL   CB  HB   sing N N 386 
VAL   CG1 HG11 sing N N 387 
VAL   CG1 HG12 sing N N 388 
VAL   CG1 HG13 sing N N 389 
VAL   CG2 HG21 sing N N 390 
VAL   CG2 HG22 sing N N 391 
VAL   CG2 HG23 sing N N 392 
VAL   OXT HXT  sing N N 393 
# 
_pdbx_audit_support.funding_organization   
'National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)' 
_pdbx_audit_support.country                'United States' 
_pdbx_audit_support.grant_number           U19AI171110 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_deposit_group.group_title         
'PanDDA analysis group deposition of SARS-CoV-2 NSP3 macrodomain ligand screen - FrankenROCS hits and analogues of AVI-313' 
_pdbx_deposit_group.group_description   
'SARS-CoV-2 NSP3 macrodomain in complex with ligands identified by X-ray diffraction using ALS 8.3.1,  SSRL 9-2, and SSRL 12-2' 
_pdbx_deposit_group.group_type          'changed state' 
_pdbx_deposit_group.group_id            G_1002304 
# 
_atom_sites.entry_id                    7HDF 
_atom_sites.fract_transf_matrix[1][1]   0.011271 
_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]   0.011271 
_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]   0.025267 
_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   ? 19.706 -16.323 22.294  0.88 49.35 ?  3   VAL   A N    1 
ATOM   2    N N    B VAL   A 1 3   ? 19.642 -16.305 22.355  0.12 47.87 ?  3   VAL   A N    1 
ATOM   3    C CA   A VAL   A 1 3   ? 18.743 -15.241 22.468  0.88 48.98 ?  3   VAL   A CA   1 
ATOM   4    C CA   B VAL   A 1 3   ? 18.710 -15.200 22.546  0.12 47.66 ?  3   VAL   A CA   1 
ATOM   5    C C    A VAL   A 1 3   ? 19.399 -13.898 22.175  0.88 47.53 ?  3   VAL   A C    1 
ATOM   6    C C    B VAL   A 1 3   ? 19.383 -13.877 22.210  0.12 46.81 ?  3   VAL   A C    1 
ATOM   7    O O    A VAL   A 1 3   ? 20.514 -13.630 22.624  0.88 47.85 ?  3   VAL   A O    1 
ATOM   8    O O    B VAL   A 1 3   ? 20.495 -13.603 22.663  0.12 47.12 ?  3   VAL   A O    1 
ATOM   9    C CB   A VAL   A 1 3   ? 18.116 -15.271 23.876  0.88 49.75 ?  3   VAL   A CB   1 
ATOM   10   C CB   B VAL   A 1 3   ? 18.145 -15.185 23.979  0.12 48.11 ?  3   VAL   A CB   1 
ATOM   11   C CG1  A VAL   A 1 3   ? 17.104 -14.143 24.036  0.88 50.00 ?  3   VAL   A CG1  1 
ATOM   12   C CG1  B VAL   A 1 3   ? 17.165 -14.032 24.152  0.12 48.26 ?  3   VAL   A CG1  1 
ATOM   13   C CG2  A VAL   A 1 3   ? 17.460 -16.620 24.132  0.88 49.98 ?  3   VAL   A CG2  1 
ATOM   14   C CG2  B VAL   A 1 3   ? 17.477 -16.511 24.299  0.12 48.25 ?  3   VAL   A CG2  1 
ATOM   15   H HA   A VAL   A 1 3   ? 18.025 -15.355 21.831  0.88 58.77 ?  3   VAL   A HA   1 
ATOM   16   H HA   B VAL   A 1 3   ? 17.963 -15.308 21.940  0.12 57.19 ?  3   VAL   A HA   1 
ATOM   17   H HB   A VAL   A 1 3   ? 18.812 -15.147 24.540  0.88 59.69 ?  3   VAL   A HB   1 
ATOM   18   H HB   B VAL   A 1 3   ? 18.873 -15.057 24.607  0.12 57.72 ?  3   VAL   A HB   1 
ATOM   19   H HG11 A VAL   A 1 3   ? 16.595 -14.290 24.850  0.88 59.99 ?  3   VAL   A HG11 1 
ATOM   20   H HG11 B VAL   A 1 3   ? 16.687 -14.149 24.988  0.12 57.90 ?  3   VAL   A HG11 1 
ATOM   21   H HG12 A VAL   A 1 3   ? 17.575 -13.297 24.092  0.88 59.99 ?  3   VAL   A HG12 1 
ATOM   22   H HG12 B VAL   A 1 3   ? 17.656 -13.196 24.168  0.12 57.90 ?  3   VAL   A HG12 1 
ATOM   23   H HG13 A VAL   A 1 3   ? 16.507 -14.143 23.271  0.88 59.99 ?  3   VAL   A HG13 1 
ATOM   24   H HG13 B VAL   A 1 3   ? 16.539 -14.036 23.411  0.12 57.90 ?  3   VAL   A HG13 1 
ATOM   25   H HG21 A VAL   A 1 3   ? 17.010 -16.595 24.990  0.88 59.96 ?  3   VAL   A HG21 1 
ATOM   26   H HG21 B VAL   A 1 3   ? 17.065 -16.453 25.175  0.12 57.89 ?  3   VAL   A HG21 1 
ATOM   27   H HG22 A VAL   A 1 3   ? 16.818 -16.796 23.426  0.88 59.96 ?  3   VAL   A HG22 1 
ATOM   28   H HG22 B VAL   A 1 3   ? 16.802 -16.694 23.627  0.12 57.89 ?  3   VAL   A HG22 1 
ATOM   29   H HG23 A VAL   A 1 3   ? 18.143 -17.308 24.136  0.88 59.96 ?  3   VAL   A HG23 1 
ATOM   30   H HG23 B VAL   A 1 3   ? 18.147 -17.212 24.294  0.12 57.89 ?  3   VAL   A HG23 1 
ATOM   31   N N    . ASN   A 1 4   ? 18.703 -13.059 21.410  1.00 45.40 ?  4   ASN   A N    1 
ATOM   32   C CA   . ASN   A 1 4   ? 19.168 -11.721 21.074  1.00 41.58 ?  4   ASN   A CA   1 
ATOM   33   C C    . ASN   A 1 4   ? 18.032 -10.730 21.313  1.00 38.02 ?  4   ASN   A C    1 
ATOM   34   O O    . ASN   A 1 4   ? 16.909 -11.111 21.658  1.00 37.88 ?  4   ASN   A O    1 
ATOM   35   C CB   . ASN   A 1 4   ? 19.725 -11.650 19.644  1.00 41.11 ?  4   ASN   A CB   1 
ATOM   36   C CG   . ASN   A 1 4   ? 18.700 -12.021 18.595  1.00 40.57 ?  4   ASN   A CG   1 
ATOM   37   O OD1  . ASN   A 1 4   ? 17.586 -11.498 18.586  1.00 40.33 ?  4   ASN   A OD1  1 
ATOM   38   N ND2  . ASN   A 1 4   ? 19.074 -12.930 17.700  1.00 40.43 ?  4   ASN   A ND2  1 
ATOM   39   H H    A ASN   A 1 4   ? 17.939 -13.253 21.061  0.88 54.47 ?  4   ASN   A H    1 
ATOM   40   H H    B ASN   A 1 4   ? 17.949 -13.262 21.045  0.12 54.47 ?  4   ASN   A H    1 
ATOM   41   H HA   . ASN   A 1 4   ? 19.891 -11.488 21.670  1.00 49.89 ?  4   ASN   A HA   1 
ATOM   42   H HB2  . ASN   A 1 4   ? 20.024 -10.743 19.465  1.00 49.32 ?  4   ASN   A HB2  1 
ATOM   43   H HB3  . ASN   A 1 4   ? 20.472 -12.264 19.564  1.00 49.32 ?  4   ASN   A HB3  1 
ATOM   44   H HD21 . ASN   A 1 4   ? 18.530 -13.174 17.081  1.00 48.51 ?  4   ASN   A HD21 1 
ATOM   45   H HD22 . ASN   A 1 4   ? 19.861 -13.275 17.740  1.00 48.51 ?  4   ASN   A HD22 1 
ATOM   46   N N    . SER   A 1 5   ? 18.330 -9.446  21.127  1.00 34.27 ?  5   SER   A N    1 
ATOM   47   C CA   . SER   A 1 5   ? 17.423 -8.375  21.517  1.00 30.65 ?  5   SER   A CA   1 
ATOM   48   C C    . SER   A 1 5   ? 16.510 -7.906  20.389  1.00 26.14 ?  5   SER   A C    1 
ATOM   49   O O    . SER   A 1 5   ? 15.750 -6.953  20.587  1.00 26.59 ?  5   SER   A O    1 
ATOM   50   C CB   . SER   A 1 5   ? 18.215 -7.187  22.072  1.00 31.64 ?  5   SER   A CB   1 
ATOM   51   O OG   . SER   A 1 5   ? 19.104 -6.676  21.098  1.00 32.18 ?  5   SER   A OG   1 
ATOM   52   H H    . SER   A 1 5   ? 19.059 -9.170  20.762  1.00 41.11 ?  5   SER   A H    1 
ATOM   53   H HA   . SER   A 1 5   ? 16.860 -8.699  22.233  1.00 36.77 ?  5   SER   A HA   1 
ATOM   54   H HB2  . SER   A 1 5   ? 17.596 -6.486  22.332  1.00 37.96 ?  5   SER   A HB2  1 
ATOM   55   H HB3  . SER   A 1 5   ? 18.724 -7.479  22.847  1.00 37.96 ?  5   SER   A HB3  1 
ATOM   56   H HG   . SER   A 1 5   ? 19.664 -7.263  20.880  1.00 38.60 ?  5   SER   A HG   1 
ATOM   57   N N    A PHE   A 1 6   ? 16.541 -8.550  19.224  0.88 22.92 ?  6   PHE   A N    1 
ATOM   58   N N    B PHE   A 1 6   ? 16.586 -8.529  19.218  0.12 24.34 ?  6   PHE   A N    1 
ATOM   59   C CA   A PHE   A 1 6   ? 15.632 -8.172  18.147  0.88 20.10 ?  6   PHE   A CA   1 
ATOM   60   C CA   B PHE   A 1 6   ? 15.684 -8.193  18.126  0.12 22.46 ?  6   PHE   A CA   1 
ATOM   61   C C    A PHE   A 1 6   ? 14.199 -8.536  18.525  0.88 20.58 ?  6   PHE   A C    1 
ATOM   62   C C    B PHE   A 1 6   ? 14.265 -8.587  18.514  0.12 21.67 ?  6   PHE   A C    1 
ATOM   63   O O    A PHE   A 1 6   ? 13.939 -9.638  19.015  0.88 21.69 ?  6   PHE   A O    1 
ATOM   64   O O    B PHE   A 1 6   ? 13.996 -9.760  18.794  0.12 21.78 ?  6   PHE   A O    1 
ATOM   65   C CB   A PHE   A 1 6   ? 16.028 -8.875  16.851  0.88 18.14 ?  6   PHE   A CB   1 
ATOM   66   C CB   B PHE   A 1 6   ? 16.112 -8.936  16.864  0.12 21.46 ?  6   PHE   A CB   1 
ATOM   67   C CG   A PHE   A 1 6   ? 17.295 -8.344  16.234  0.88 16.84 ?  6   PHE   A CG   1 
ATOM   68   C CG   B PHE   A 1 6   ? 17.463 -8.527  16.344  0.12 20.54 ?  6   PHE   A CG   1 
ATOM   69   C CD1  A PHE   A 1 6   ? 17.300 -7.133  15.562  0.88 16.52 ?  6   PHE   A CD1  1 
ATOM   70   C CD1  B PHE   A 1 6   ? 17.583 -7.497  15.426  0.12 20.17 ?  6   PHE   A CD1  1 
ATOM   71   C CD2  A PHE   A 1 6   ? 18.473 -9.064  16.316  0.88 17.30 ?  6   PHE   A CD2  1 
ATOM   72   C CD2  B PHE   A 1 6   ? 18.612 -9.176  16.766  0.12 20.19 ?  6   PHE   A CD2  1 
ATOM   73   C CE1  A PHE   A 1 6   ? 18.463 -6.646  14.990  0.88 16.36 ?  6   PHE   A CE1  1 
ATOM   74   C CE1  B PHE   A 1 6   ? 18.822 -7.120  14.942  0.12 19.92 ?  6   PHE   A CE1  1 
ATOM   75   C CE2  A PHE   A 1 6   ? 19.635 -8.587  15.746  0.88 17.32 ?  6   PHE   A CE2  1 
ATOM   76   C CE2  B PHE   A 1 6   ? 19.856 -8.804  16.286  0.12 19.93 ?  6   PHE   A CE2  1 
ATOM   77   C CZ   A PHE   A 1 6   ? 19.631 -7.377  15.081  0.88 16.76 ?  6   PHE   A CZ   1 
ATOM   78   C CZ   B PHE   A 1 6   ? 19.961 -7.774  15.372  0.12 19.85 ?  6   PHE   A CZ   1 
ATOM   79   H H    A PHE   A 1 6   ? 17.071 -9.202  19.038  0.88 27.49 ?  6   PHE   A H    1 
ATOM   80   H H    B PHE   A 1 6   ? 17.151 -9.150  19.032  0.12 29.20 ?  6   PHE   A H    1 
ATOM   81   H HA   A PHE   A 1 6   ? 15.680 -7.218  18.010  0.88 24.11 ?  6   PHE   A HA   1 
ATOM   82   H HA   B PHE   A 1 6   ? 15.711 -7.239  17.957  0.12 26.95 ?  6   PHE   A HA   1 
ATOM   83   H HB2  A PHE   A 1 6   ? 16.160 -9.820  17.035  0.88 21.75 ?  6   PHE   A HB2  1 
ATOM   84   H HB2  B PHE   A 1 6   ? 16.145 -9.884  17.063  0.12 25.75 ?  6   PHE   A HB2  1 
ATOM   85   H HB3  A PHE   A 1 6   ? 15.311 -8.765  16.207  0.88 21.75 ?  6   PHE   A HB3  1 
ATOM   86   H HB3  B PHE   A 1 6   ? 15.460 -8.773  16.168  0.12 25.75 ?  6   PHE   A HB3  1 
ATOM   87   H HD1  A PHE   A 1 6   ? 16.511 -6.639  15.498  0.88 19.81 ?  6   PHE   A HD1  1 
ATOM   88   H HD1  B PHE   A 1 6   ? 16.821 -7.054  15.134  0.12 24.20 ?  6   PHE   A HD1  1 
ATOM   89   H HD2  A PHE   A 1 6   ? 18.480 -9.879  16.763  0.88 20.75 ?  6   PHE   A HD2  1 
ATOM   90   H HD2  B PHE   A 1 6   ? 18.547 -9.869  17.381  0.12 24.22 ?  6   PHE   A HD2  1 
ATOM   91   H HE1  A PHE   A 1 6   ? 18.456 -5.828  14.542  0.88 19.62 ?  6   PHE   A HE1  1 
ATOM   92   H HE1  B PHE   A 1 6   ? 18.889 -6.426  14.327  0.12 23.89 ?  6   PHE   A HE1  1 
ATOM   93   H HE2  A PHE   A 1 6   ? 20.424 -9.073  15.809  0.88 20.77 ?  6   PHE   A HE2  1 
ATOM   94   H HE2  B PHE   A 1 6   ? 20.621 -9.247  16.577  0.12 23.91 ?  6   PHE   A HE2  1 
ATOM   95   H HZ   A PHE   A 1 6   ? 20.413 -7.046  14.697  0.88 20.11 ?  6   PHE   A HZ   1 
ATOM   96   H HZ   B PHE   A 1 6   ? 20.796 -7.521  15.046  0.12 23.81 ?  6   PHE   A HZ   1 
ATOM   97   N N    A SER   A 1 7   ? 13.263 -7.612  18.293  0.88 20.01 ?  7   SER   A N    1 
ATOM   98   N N    B SER   A 1 7   ? 13.357 -7.613  18.533  0.12 20.78 ?  7   SER   A N    1 
ATOM   99   C CA   A SER   A 1 7   ? 11.895 -7.750  18.778  0.88 21.03 ?  7   SER   A CA   1 
ATOM   100  C CA   B SER   A 1 7   ? 11.995 -7.835  18.995  0.12 20.07 ?  7   SER   A CA   1 
ATOM   101  C C    A SER   A 1 7   ? 10.892 -7.489  17.661  0.88 19.52 ?  7   SER   A C    1 
ATOM   102  C C    B SER   A 1 7   ? 11.009 -7.318  17.958  0.12 19.03 ?  7   SER   A C    1 
ATOM   103  O O    A SER   A 1 7   ? 11.097 -6.607  16.823  0.88 19.52 ?  7   SER   A O    1 
ATOM   104  O O    B SER   A 1 7   ? 11.290 -6.361  17.231  0.12 18.97 ?  7   SER   A O    1 
ATOM   105  C CB   A SER   A 1 7   ? 11.640 -6.772  19.935  0.88 23.25 ?  7   SER   A CB   1 
ATOM   106  C CB   B SER   A 1 7   ? 11.747 -7.147  20.344  0.12 20.39 ?  7   SER   A CB   1 
ATOM   107  O OG   A SER   A 1 7   ? 10.302 -6.854  20.383  0.88 24.83 ?  7   SER   A OG   1 
ATOM   108  O OG   B SER   A 1 7   ? 10.570 -7.645  20.957  0.12 20.59 ?  7   SER   A OG   1 
ATOM   109  H H    A SER   A 1 7   ? 13.404 -6.888  17.844  0.88 24.00 ?  7   SER   A H    1 
ATOM   110  H H    B SER   A 1 7   ? 13.507 -6.805  18.270  0.12 24.93 ?  7   SER   A H    1 
ATOM   111  H HA   A SER   A 1 7   ? 11.755 -8.650  19.103  0.88 25.22 ?  7   SER   A HA   1 
ATOM   112  H HA   B SER   A 1 7   ? 11.842 -8.784  19.107  0.12 24.07 ?  7   SER   A HA   1 
ATOM   113  H HB2  A SER   A 1 7   ? 12.234 -6.994  20.672  0.88 27.89 ?  7   SER   A HB2  1 
ATOM   114  H HB2  B SER   A 1 7   ? 12.505 -7.315  20.928  0.12 24.46 ?  7   SER   A HB2  1 
ATOM   115  H HB3  A SER   A 1 7   ? 11.814 -5.867  19.634  0.88 27.89 ?  7   SER   A HB3  1 
ATOM   116  H HB3  B SER   A 1 7   ? 11.647 -6.193  20.201  0.12 24.46 ?  7   SER   A HB3  1 
ATOM   117  H HG   A SER   A 1 7   ? 10.177 -6.321  21.020  0.88 29.78 ?  7   SER   A HG   1 
ATOM   118  H HG   B SER   A 1 7   ? 10.647 -8.470  21.096  0.12 24.70 ?  7   SER   A HG   1 
ATOM   119  N N    A GLY   A 1 8   ? 9.799  -8.255  17.661  0.88 18.71 ?  8   GLY   A N    1 
ATOM   120  N N    B GLY   A 1 8   ? 9.847  -7.966  17.895  0.12 18.18 ?  8   GLY   A N    1 
ATOM   121  C CA   A GLY   A 1 8   ? 8.712  -8.012  16.736  0.88 18.26 ?  8   GLY   A CA   1 
ATOM   122  C CA   B GLY   A 1 8   ? 8.836  -7.614  16.921  0.12 17.26 ?  8   GLY   A CA   1 
ATOM   123  C C    A GLY   A 1 8   ? 8.913  -8.527  15.330  0.88 17.11 ?  8   GLY   A C    1 
ATOM   124  C C    B GLY   A 1 8   ? 9.049  -8.194  15.543  0.12 16.25 ?  8   GLY   A C    1 
ATOM   125  O O    A GLY   A 1 8   ? 8.167  -8.119  14.432  0.88 18.01 ?  8   GLY   A O    1 
ATOM   126  O O    B GLY   A 1 8   ? 8.356  -7.785  14.604  0.12 16.28 ?  8   GLY   A O    1 
ATOM   127  H H    A GLY   A 1 8   ? 9.668  -8.916  18.196  0.88 22.44 ?  8   GLY   A H    1 
ATOM   128  H H    B GLY   A 1 8   ? 9.622  -8.616  18.413  0.12 21.81 ?  8   GLY   A H    1 
ATOM   129  H HA2  A GLY   A 1 8   ? 7.907  -8.423  17.087  0.88 21.90 ?  8   GLY   A HA2  1 
ATOM   130  H HA2  B GLY   A 1 8   ? 7.972  -7.918  17.238  0.12 20.70 ?  8   GLY   A HA2  1 
ATOM   131  H HA3  A GLY   A 1 8   ? 8.557  -7.055  16.682  0.88 21.90 ?  8   GLY   A HA3  1 
ATOM   132  H HA3  B GLY   A 1 8   ? 8.802  -6.649  16.835  0.12 20.70 ?  8   GLY   A HA3  1 
ATOM   133  N N    A TYR   A 1 9   ? 9.889  -9.404  15.101  0.88 15.47 ?  9   TYR   A N    1 
ATOM   134  N N    B TYR   A 1 9   ? 9.978  -9.132  15.388  0.12 15.34 ?  9   TYR   A N    1 
ATOM   135  C CA   A TYR   A 1 9   ? 10.136 -9.942  13.771  0.88 13.82 ?  9   TYR   A CA   1 
ATOM   136  C CA   B TYR   A 1 9   ? 10.283 -9.706  14.088  0.12 14.55 ?  9   TYR   A CA   1 
ATOM   137  C C    A TYR   A 1 9   ? 9.257  -11.156 13.500  0.88 13.67 ?  9   TYR   A C    1 
ATOM   138  C C    B TYR   A 1 9   ? 9.383  -10.898 13.792  0.12 14.13 ?  9   TYR   A C    1 
ATOM   139  O O    A TYR   A 1 9   ? 8.980  -11.968 14.394  0.88 15.46 ?  9   TYR   A O    1 
ATOM   140  O O    B TYR   A 1 9   ? 8.876  -11.564 14.698  0.12 14.32 ?  9   TYR   A O    1 
ATOM   141  C CB   A TYR   A 1 9   ? 11.607 -10.347 13.598  0.88 13.87 ?  9   TYR   A CB   1 
ATOM   142  C CB   B TYR   A 1 9   ? 11.748 -10.141 14.020  0.12 14.30 ?  9   TYR   A CB   1 
ATOM   143  C CG   A TYR   A 1 9   ? 12.519 -9.154  13.430  0.88 14.05 ?  9   TYR   A CG   1 
ATOM   144  C CG   B TYR   A 1 9   ? 12.711 -8.990  13.854  0.12 13.92 ?  9   TYR   A CG   1 
ATOM   145  C CD1  A TYR   A 1 9   ? 12.846 -8.356  14.513  0.88 14.61 ?  9   TYR   A CD1  1 
ATOM   146  C CD1  B TYR   A 1 9   ? 13.043 -8.176  14.928  0.12 13.83 ?  9   TYR   A CD1  1 
ATOM   147  C CD2  A TYR   A 1 9   ? 13.029 -8.811  12.186  0.88 13.67 ?  9   TYR   A CD2  1 
ATOM   148  C CD2  B TYR   A 1 9   ? 13.285 -8.714  12.621  0.12 13.67 ?  9   TYR   A CD2  1 
ATOM   149  C CE1  A TYR   A 1 9   ? 13.653 -7.243  14.371  0.88 15.15 ?  9   TYR   A CE1  1 
ATOM   150  C CE1  B TYR   A 1 9   ? 13.918 -7.118  14.779  0.12 13.73 ?  9   TYR   A CE1  1 
ATOM   151  C CE2  A TYR   A 1 9   ? 13.837 -7.699  12.029  0.88 14.14 ?  9   TYR   A CE2  1 
ATOM   152  C CE2  B TYR   A 1 9   ? 14.158 -7.658  12.462  0.12 13.71 ?  9   TYR   A CE2  1 
ATOM   153  C CZ   A TYR   A 1 9   ? 14.146 -6.919  13.125  0.88 14.97 ?  9   TYR   A CZ   1 
ATOM   154  C CZ   B TYR   A 1 9   ? 14.476 -6.867  13.544  0.12 13.77 ?  9   TYR   A CZ   1 
ATOM   155  O OH   A TYR   A 1 9   ? 14.941 -5.813  12.970  0.88 16.01 ?  9   TYR   A OH   1 
ATOM   156  O OH   B TYR   A 1 9   ? 15.351 -5.817  13.390  0.12 14.08 ?  9   TYR   A OH   1 
ATOM   157  H H    A TYR   A 1 9   ? 10.421 -9.704  15.705  0.88 18.56 ?  9   TYR   A H    1 
ATOM   158  H H    B TYR   A 1 9   ? 10.449 -9.455  16.031  0.12 18.40 ?  9   TYR   A H    1 
ATOM   159  H HA   A TYR   A 1 9   ? 9.933  -9.262  13.109  0.88 16.57 ?  9   TYR   A HA   1 
ATOM   160  H HA   B TYR   A 1 9   ? 10.135 -9.039  13.402  0.12 17.45 ?  9   TYR   A HA   1 
ATOM   161  H HB2  A TYR   A 1 9   ? 11.895 -10.848 14.377  0.88 16.64 ?  9   TYR   A HB2  1 
ATOM   162  H HB2  B TYR   A 1 9   ? 11.982 -10.612 14.834  0.12 17.15 ?  9   TYR   A HB2  1 
ATOM   163  H HB3  A TYR   A 1 9   ? 11.679 -10.901 12.802  0.88 16.64 ?  9   TYR   A HB3  1 
ATOM   164  H HB3  B TYR   A 1 9   ? 11.860 -10.731 13.258  0.12 17.15 ?  9   TYR   A HB3  1 
ATOM   165  H HD1  A TYR   A 1 9   ? 12.496 -8.572  15.352  0.88 17.53 ?  9   TYR   A HD1  1 
ATOM   166  H HD1  B TYR   A 1 9   ? 12.667 -8.345  15.763  0.12 16.59 ?  9   TYR   A HD1  1 
ATOM   167  H HD2  A TYR   A 1 9   ? 12.818 -9.336  11.443  0.88 16.40 ?  9   TYR   A HD2  1 
ATOM   168  H HD2  B TYR   A 1 9   ? 13.077 -9.249  11.889  0.12 16.40 ?  9   TYR   A HD2  1 
ATOM   169  H HE1  A TYR   A 1 9   ? 13.851 -6.724  15.112  0.88 18.17 ?  9   TYR   A HE1  1 
ATOM   170  H HE1  B TYR   A 1 9   ? 14.134 -6.583  15.508  0.12 16.46 ?  9   TYR   A HE1  1 
ATOM   171  H HE2  A TYR   A 1 9   ? 14.179 -7.484  11.191  0.88 16.96 ?  9   TYR   A HE2  1 
ATOM   172  H HE2  B TYR   A 1 9   ? 14.544 -7.488  11.632  0.12 16.44 ?  9   TYR   A HE2  1 
ATOM   173  H HH   A TYR   A 1 9   ? 15.060 -5.443  13.714  0.88 19.20 ?  9   TYR   A HH   1 
ATOM   174  H HH   B TYR   A 1 9   ? 15.454 -5.421  14.123  0.12 16.89 ?  9   TYR   A HH   1 
ATOM   175  N N    A LEU   A 1 10  ? 8.840  -11.282 12.247  0.88 12.79 ?  10  LEU   A N    1 
ATOM   176  N N    B LEU   A 1 10  ? 9.187  -11.152 12.502  0.12 13.78 ?  10  LEU   A N    1 
ATOM   177  C CA   A LEU   A 1 10  ? 8.239  -12.507 11.746  0.88 12.81 ?  10  LEU   A CA   1 
ATOM   178  C CA   B LEU   A 1 10  ? 8.403  -12.276 12.009  0.12 13.47 ?  10  LEU   A CA   1 
ATOM   179  C C    A LEU   A 1 10  ? 9.367  -13.434 11.296  0.88 12.23 ?  10  LEU   A C    1 
ATOM   180  C C    B LEU   A 1 10  ? 9.368  -13.316 11.460  0.12 12.52 ?  10  LEU   A C    1 
ATOM   181  O O    A LEU   A 1 10  ? 10.339 -12.990 10.678  0.88 12.64 ?  10  LEU   A O    1 
ATOM   182  O O    B LEU   A 1 10  ? 10.094 -13.045 10.497  0.12 12.57 ?  10  LEU   A O    1 
ATOM   183  C CB   A LEU   A 1 10  ? 7.326  -12.165 10.567  0.88 14.04 ?  10  LEU   A CB   1 
ATOM   184  C CB   B LEU   A 1 10  ? 7.462  -11.812 10.899  0.12 14.04 ?  10  LEU   A CB   1 
ATOM   185  C CG   A LEU   A 1 10  ? 6.610  -13.342 9.906   0.88 16.34 ?  10  LEU   A CG   1 
ATOM   186  C CG   B LEU   A 1 10  ? 6.021  -12.321 10.923  0.12 14.66 ?  10  LEU   A CG   1 
ATOM   187  C CD1  A LEU   A 1 10  ? 5.538  -13.928 10.814  0.88 18.19 ?  10  LEU   A CD1  1 
ATOM   188  C CD1  B LEU   A 1 10  ? 5.294  -11.840 9.686   0.12 14.87 ?  10  LEU   A CD1  1 
ATOM   189  C CD2  A LEU   A 1 10  ? 6.034  -12.947 8.551   0.88 18.20 ?  10  LEU   A CD2  1 
ATOM   190  C CD2  B LEU   A 1 10  ? 5.966  -13.831 11.014  0.12 14.86 ?  10  LEU   A CD2  1 
ATOM   191  H H    A LEU   A 1 10  ? 8.905  -10.659 11.649  0.88 15.34 ?  10  LEU   A H    1 
ATOM   192  H H    B LEU   A 1 10  ? 9.511  -10.666 11.872  0.12 16.53 ?  10  LEU   A H    1 
ATOM   193  H HA   A LEU   A 1 10  ? 7.718  -12.936 12.446  0.88 15.36 ?  10  LEU   A HA   1 
ATOM   194  H HA   B LEU   A 1 10  ? 7.883  -12.667 12.730  0.12 16.16 ?  10  LEU   A HA   1 
ATOM   195  H HB2  A LEU   A 1 10  ? 6.643  -11.547 10.875  0.88 16.84 ?  10  LEU   A HB2  1 
ATOM   196  H HB2  B LEU   A 1 10  ? 7.422  -10.844 10.928  0.12 16.84 ?  10  LEU   A HB2  1 
ATOM   197  H HB3  A LEU   A 1 10  ? 7.862  -11.734 9.883   0.88 16.84 ?  10  LEU   A HB3  1 
ATOM   198  H HB3  B LEU   A 1 10  ? 7.845  -12.089 10.052  0.12 16.84 ?  10  LEU   A HB3  1 
ATOM   199  H HG   A LEU   A 1 10  ? 7.261  -14.042 9.748   0.88 19.60 ?  10  LEU   A HG   1 
ATOM   200  H HG   B LEU   A 1 10  ? 5.569  -11.955 11.699  0.12 17.58 ?  10  LEU   A HG   1 
ATOM   201  H HD11 A LEU   A 1 10  ? 5.149  -14.706 10.382  0.88 21.82 ?  10  LEU   A HD11 1 
ATOM   202  H HD11 B LEU   A 1 10  ? 4.360  -12.088 9.756   0.12 17.84 ?  10  LEU   A HD11 1 
ATOM   203  H HD12 A LEU   A 1 10  ? 5.944  -14.190 11.658  0.88 21.82 ?  10  LEU   A HD12 1 
ATOM   204  H HD12 B LEU   A 1 10  ? 5.381  -10.877 9.627   0.12 17.84 ?  10  LEU   A HD12 1 
ATOM   205  H HD13 A LEU   A 1 10  ? 4.854  -13.260 10.972  0.88 21.82 ?  10  LEU   A HD13 1 
ATOM   206  H HD13 B LEU   A 1 10  ? 5.694  -12.257 8.907   0.12 17.84 ?  10  LEU   A HD13 1 
ATOM   207  H HD21 A LEU   A 1 10  ? 5.587  -13.718 8.166   0.88 21.83 ?  10  LEU   A HD21 1 
ATOM   208  H HD21 B LEU   A 1 10  ? 5.093  -14.132 10.715  0.12 17.83 ?  10  LEU   A HD21 1 
ATOM   209  H HD22 A LEU   A 1 10  ? 5.402  -12.224 8.676   0.88 21.83 ?  10  LEU   A HD22 1 
ATOM   210  H HD22 B LEU   A 1 10  ? 6.658  -14.207 10.449  0.12 17.83 ?  10  LEU   A HD22 1 
ATOM   211  H HD23 A LEU   A 1 10  ? 6.759  -12.662 7.975   0.88 21.83 ?  10  LEU   A HD23 1 
ATOM   212  H HD23 B LEU   A 1 10  ? 6.109  -14.089 11.935  0.12 17.83 ?  10  LEU   A HD23 1 
ATOM   213  N N    A LYS   A 1 11  ? 9.248  -14.715 11.626  0.88 12.13 ?  11  LYS   A N    1 
ATOM   214  N N    B LYS   A 1 11  ? 9.377  -14.497 12.068  0.12 11.68 ?  11  LYS   A N    1 
ATOM   215  C CA   A LYS   A 1 11  ? 10.257 -15.709 11.277  0.88 12.00 ?  11  LYS   A CA   1 
ATOM   216  C CA   B LYS   A 1 11  ? 10.265 -15.560 11.619  0.12 11.28 ?  11  LYS   A CA   1 
ATOM   217  C C    A LYS   A 1 11  ? 9.907  -16.295 9.917   0.88 12.22 ?  11  LYS   A C    1 
ATOM   218  C C    B LYS   A 1 11  ? 9.838  -16.020 10.232  0.12 10.73 ?  11  LYS   A C    1 
ATOM   219  O O    A LYS   A 1 11  ? 8.841  -16.893 9.761   0.88 14.40 ?  11  LYS   A O    1 
ATOM   220  O O    B LYS   A 1 11  ? 8.718  -16.509 10.050  0.12 10.67 ?  11  LYS   A O    1 
ATOM   221  C CB   A LYS   A 1 11  ? 10.293 -16.792 12.355  0.88 12.28 ?  11  LYS   A CB   1 
ATOM   222  C CB   B LYS   A 1 11  ? 10.232 -16.722 12.609  0.12 11.41 ?  11  LYS   A CB   1 
ATOM   223  C CG   A LYS   A 1 11  ? 11.319 -17.896 12.154  0.88 12.33 ?  11  LYS   A CG   1 
ATOM   224  C CG   B LYS   A 1 11  ? 11.284 -17.795 12.353  0.12 11.49 ?  11  LYS   A CG   1 
ATOM   225  C CD   A LYS   A 1 11  ? 11.401 -18.748 13.422  0.88 13.03 ?  11  LYS   A CD   1 
ATOM   226  C CD   B LYS   A 1 11  ? 11.355 -18.786 13.509  0.12 11.68 ?  11  LYS   A CD   1 
ATOM   227  C CE   A LYS   A 1 11  ? 12.391 -19.901 13.311  0.88 13.35 ?  11  LYS   A CE   1 
ATOM   228  C CE   B LYS   A 1 11  ? 12.418 -19.853 13.279  0.12 11.77 ?  11  LYS   A CE   1 
ATOM   229  N NZ   A LYS   A 1 11  ? 13.767 -19.433 13.024  0.88 13.36 ?  11  LYS   A NZ   1 
ATOM   230  N NZ   B LYS   A 1 11  ? 13.786 -19.276 13.162  0.12 11.71 ?  11  LYS   A NZ   1 
ATOM   231  H H    A LYS   A 1 11  ? 8.563  -15.041 12.036  0.88 14.55 ?  11  LYS   A H    1 
ATOM   232  H H    B LYS   A 1 11  ? 8.878  -14.705 12.735  0.12 14.01 ?  11  LYS   A H    1 
ATOM   233  H HA   A LYS   A 1 11  ? 11.125 -15.279 11.220  0.88 14.39 ?  11  LYS   A HA   1 
ATOM   234  H HA   B LYS   A 1 11  ? 11.171 -15.225 11.564  0.12 13.52 ?  11  LYS   A HA   1 
ATOM   235  H HB2  A LYS   A 1 11  ? 10.488 -16.359 13.201  0.88 14.73 ?  11  LYS   A HB2  1 
ATOM   236  H HB2  B LYS   A 1 11  ? 10.378 -16.372 13.501  0.12 13.68 ?  11  LYS   A HB2  1 
ATOM   237  H HB3  A LYS   A 1 11  ? 9.418  -17.202 12.395  0.88 14.73 ?  11  LYS   A HB3  1 
ATOM   238  H HB3  B LYS   A 1 11  ? 9.361  -17.145 12.562  0.12 13.68 ?  11  LYS   A HB3  1 
ATOM   239  H HG2  A LYS   A 1 11  ? 11.044 -18.461 11.414  0.88 14.79 ?  11  LYS   A HG2  1 
ATOM   240  H HG2  B LYS   A 1 11  ? 11.055 -18.283 11.547  0.12 13.78 ?  11  LYS   A HG2  1 
ATOM   241  H HG3  A LYS   A 1 11  ? 12.189 -17.506 11.982  0.88 14.79 ?  11  LYS   A HG3  1 
ATOM   242  H HG3  B LYS   A 1 11  ? 12.153 -17.375 12.257  0.12 13.78 ?  11  LYS   A HG3  1 
ATOM   243  H HD2  A LYS   A 1 11  ? 11.673 -18.182 14.160  0.88 15.63 ?  11  LYS   A HD2  1 
ATOM   244  H HD2  B LYS   A 1 11  ? 11.576 -18.309 14.324  0.12 14.01 ?  11  LYS   A HD2  1 
ATOM   245  H HD3  A LYS   A 1 11  ? 10.522 -19.123 13.601  0.88 15.63 ?  11  LYS   A HD3  1 
ATOM   246  H HD3  B LYS   A 1 11  ? 10.497 -19.229 13.602  0.12 14.01 ?  11  LYS   A HD3  1 
ATOM   247  H HE2  A LYS   A 1 11  ? 12.410 -20.384 14.154  0.88 16.01 ?  11  LYS   A HE2  1 
ATOM   248  H HE2  B LYS   A 1 11  ? 12.416 -20.470 14.029  0.12 14.11 ?  11  LYS   A HE2  1 
ATOM   249  H HE3  A LYS   A 1 11  ? 12.118 -20.492 12.594  0.88 16.01 ?  11  LYS   A HE3  1 
ATOM   250  H HE3  B LYS   A 1 11  ? 12.221 -20.328 12.457  0.12 14.11 ?  11  LYS   A HE3  1 
ATOM   251  H HZ1  A LYS   A 1 11  ? 14.321 -20.127 12.971  0.88 16.02 ?  11  LYS   A HZ1  1 
ATOM   252  H HZ1  B LYS   A 1 11  ? 14.378 -19.924 13.013  0.12 14.04 ?  11  LYS   A HZ1  1 
ATOM   253  H HZ2  A LYS   A 1 11  ? 13.782 -18.992 12.250  0.88 16.02 ?  11  LYS   A HZ2  1 
ATOM   254  H HZ2  B LYS   A 1 11  ? 13.815 -18.697 12.487  0.12 14.04 ?  11  LYS   A HZ2  1 
ATOM   255  H HZ3  A LYS   A 1 11  ? 14.046 -18.889 13.670  0.88 16.02 ?  11  LYS   A HZ3  1 
ATOM   256  H HZ3  B LYS   A 1 11  ? 14.004 -18.854 13.914  0.12 14.04 ?  11  LYS   A HZ3  1 
ATOM   257  N N    A LEU   A 1 12  ? 10.791 -16.129 8.931   0.88 11.02 ?  12  LEU   A N    1 
ATOM   258  N N    B LEU   A 1 12  ? 10.719 -15.837 9.249   0.12 10.70 ?  12  LEU   A N    1 
ATOM   259  C CA   A LEU   A 1 12  ? 10.531 -16.708 7.616   0.88 11.52 ?  12  LEU   A CA   1 
ATOM   260  C CA   B LEU   A 1 12  ? 10.452 -16.305 7.894   0.12 10.69 ?  12  LEU   A CA   1 
ATOM   261  C C    A LEU   A 1 12  ? 11.110 -18.107 7.474   0.88 11.64 ?  12  LEU   A C    1 
ATOM   262  C C    B LEU   A 1 12  ? 10.980 -17.719 7.678   0.12 10.81 ?  12  LEU   A C    1 
ATOM   263  O O    A LEU   A 1 12  ? 10.481 -18.976 6.860   0.88 12.12 ?  12  LEU   A O    1 
ATOM   264  O O    B LEU   A 1 12  ? 10.258 -18.586 7.177   0.12 10.79 ?  12  LEU   A O    1 
ATOM   265  C CB   A LEU   A 1 12  ? 11.093 -15.818 6.503   0.88 12.05 ?  12  LEU   A CB   1 
ATOM   266  C CB   B LEU   A 1 12  ? 11.065 -15.348 6.865   0.12 10.70 ?  12  LEU   A CB   1 
ATOM   267  C CG   A LEU   A 1 12  ? 10.435 -14.449 6.338   0.88 13.36 ?  12  LEU   A CG   1 
ATOM   268  C CG   B LEU   A 1 12  ? 10.375 -13.996 6.672   0.12 10.75 ?  12  LEU   A CG   1 
ATOM   269  C CD1  A LEU   A 1 12  ? 11.180 -13.649 5.279   0.88 14.32 ?  12  LEU   A CD1  1 
ATOM   270  C CD1  B LEU   A 1 12  ? 10.990 -13.242 5.497   0.12 10.92 ?  12  LEU   A CD1  1 
ATOM   271  C CD2  A LEU   A 1 12  ? 8.968  -14.592 5.969   0.88 13.94 ?  12  LEU   A CD2  1 
ATOM   272  C CD2  B LEU   A 1 12  ? 8.880  -14.176 6.467   0.12 10.60 ?  12  LEU   A CD2  1 
ATOM   273  H H    A LEU   A 1 12  ? 11.538 -15.689 8.989   0.88 13.22 ?  12  LEU   A H    1 
ATOM   274  H H    B LEU   A 1 12  ? 11.478 -15.440 9.343   0.12 12.83 ?  12  LEU   A H    1 
ATOM   275  H HA   A LEU   A 1 12  ? 9.571  -16.770 7.487   0.88 13.81 ?  12  LEU   A HA   1 
ATOM   276  H HA   B LEU   A 1 12  ? 9.494  -16.327 7.756   0.12 12.82 ?  12  LEU   A HA   1 
ATOM   277  H HB2  A LEU   A 1 12  ? 12.032 -15.665 6.674   0.88 14.45 ?  12  LEU   A HB2  1 
ATOM   278  H HB2  B LEU   A 1 12  ? 11.980 -15.164 7.130   0.12 12.83 ?  12  LEU   A HB2  1 
ATOM   279  H HB3  A LEU   A 1 12  ? 10.991 -16.286 5.655   0.88 14.45 ?  12  LEU   A HB3  1 
ATOM   280  H HB3  B LEU   A 1 12  ? 11.065 -15.793 6.004   0.12 12.83 ?  12  LEU   A HB3  1 
ATOM   281  H HG   A LEU   A 1 12  ? 10.489 -13.962 7.174   0.88 16.02 ?  12  LEU   A HG   1 
ATOM   282  H HG   B LEU   A 1 12  ? 10.507 -13.458 7.468   0.12 12.89 ?  12  LEU   A HG   1 
ATOM   283  H HD11 A LEU   A 1 12  ? 10.759 -12.782 5.179   0.88 17.17 ?  12  LEU   A HD11 1 
ATOM   284  H HD11 B LEU   A 1 12  ? 10.542 -12.387 5.401   0.12 13.09 ?  12  LEU   A HD11 1 
ATOM   285  H HD12 A LEU   A 1 12  ? 12.103 -13.538 5.562   0.88 17.17 ?  12  LEU   A HD12 1 
ATOM   286  H HD12 B LEU   A 1 12  ? 11.935 -13.104 5.669   0.12 13.09 ?  12  LEU   A HD12 1 
ATOM   287  H HD13 A LEU   A 1 12  ? 11.150 -14.132 4.438   0.88 17.17 ?  12  LEU   A HD13 1 
ATOM   288  H HD13 B LEU   A 1 12  ? 10.874 -13.768 4.689   0.12 13.09 ?  12  LEU   A HD13 1 
ATOM   289  H HD21 A LEU   A 1 12  ? 8.612  -13.723 5.723   0.88 16.72 ?  12  LEU   A HD21 1 
ATOM   290  H HD21 B LEU   A 1 12  ? 8.509  -13.358 6.105   0.12 12.71 ?  12  LEU   A HD21 1 
ATOM   291  H HD22 A LEU   A 1 12  ? 8.887  -15.204 5.219   0.88 16.72 ?  12  LEU   A HD22 1 
ATOM   292  H HD22 B LEU   A 1 12  ? 8.734  -14.910 5.850   0.12 12.71 ?  12  LEU   A HD22 1 
ATOM   293  H HD23 A LEU   A 1 12  ? 8.481  -14.943 6.732   0.88 16.72 ?  12  LEU   A HD23 1 
ATOM   294  H HD23 B LEU   A 1 12  ? 8.468  -14.377 7.322   0.12 12.71 ?  12  LEU   A HD23 1 
ATOM   295  N N    A THR   A 1 13  ? 12.317 -18.319 7.997   0.88 11.68 ?  13  THR   A N    1 
ATOM   296  N N    B THR   A 1 13  ? 12.236 -17.960 8.045   0.12 11.04 ?  13  THR   A N    1 
ATOM   297  C CA   A THR   A 1 13  ? 13.011 -19.598 7.903   0.88 12.03 ?  13  THR   A CA   1 
ATOM   298  C CA   B THR   A 1 13  ? 12.837 -19.283 7.949   0.12 11.44 ?  13  THR   A CA   1 
ATOM   299  C C    A THR   A 1 13  ? 13.794 -19.823 9.192   0.88 11.89 ?  13  THR   A C    1 
ATOM   300  C C    B THR   A 1 13  ? 13.598 -19.556 9.242   0.12 11.90 ?  13  THR   A C    1 
ATOM   301  O O    A THR   A 1 13  ? 13.722 -19.034 10.140  0.88 11.96 ?  13  THR   A O    1 
ATOM   302  O O    B THR   A 1 13  ? 13.469 -18.831 10.233  0.12 12.11 ?  13  THR   A O    1 
ATOM   303  C CB   A THR   A 1 13  ? 13.986 -19.633 6.719   0.88 12.78 ?  13  THR   A CB   1 
ATOM   304  C CB   B THR   A 1 13  ? 13.759 -19.386 6.726   0.12 11.55 ?  13  THR   A CB   1 
ATOM   305  O OG1  A THR   A 1 13  ? 15.053 -18.723 6.984   0.88 12.91 ?  13  THR   A OG1  1 
ATOM   306  O OG1  B THR   A 1 13  ? 14.855 -18.478 6.879   0.12 11.63 ?  13  THR   A OG1  1 
ATOM   307  C CG2  A THR   A 1 13  ? 13.317 -19.270 5.401   0.88 14.17 ?  13  THR   A CG2  1 
ATOM   308  C CG2  B THR   A 1 13  ? 13.011 -19.058 5.441   0.12 11.61 ?  13  THR   A CG2  1 
ATOM   309  H H    A THR   A 1 13  ? 12.766 -17.719 8.413   0.88 14.01 ?  13  THR   A H    1 
ATOM   310  H H    B THR   A 1 13  ? 12.765 -17.358 8.354   0.12 13.23 ?  13  THR   A H    1 
ATOM   311  H HA   A THR   A 1 13  ? 12.365 -20.317 7.793   0.88 14.43 ?  13  THR   A HA   1 
ATOM   312  H HA   B THR   A 1 13  ? 12.136 -19.947 7.862   0.12 13.72 ?  13  THR   A HA   1 
ATOM   313  H HB   A THR   A 1 13  ? 14.349 -20.527 6.629   0.88 15.32 ?  13  THR   A HB   1 
ATOM   314  H HB   B THR   A 1 13  ? 14.096 -20.294 6.658   0.12 13.85 ?  13  THR   A HB   1 
ATOM   315  H HG1  A THR   A 1 13  ? 15.736 -19.142 7.232   0.88 15.49 ?  13  THR   A HG1  1 
ATOM   316  H HG1  B THR   A 1 13  ? 15.368 -18.537 6.217   0.12 13.94 ?  13  THR   A HG1  1 
ATOM   317  H HG21 A THR   A 1 13  ? 13.940 -19.406 4.666   0.88 16.99 ?  13  THR   A HG21 1 
ATOM   318  H HG21 B THR   A 1 13  ? 13.600 -19.183 4.678   0.12 13.92 ?  13  THR   A HG21 1 
ATOM   319  H HG22 A THR   A 1 13  ? 12.542 -19.836 5.259   0.88 16.99 ?  13  THR   A HG22 1 
ATOM   320  H HG22 B THR   A 1 13  ? 12.244 -19.642 5.345   0.12 13.92 ?  13  THR   A HG22 1 
ATOM   321  H HG23 A THR   A 1 13  ? 13.038 -18.345 5.411   0.88 16.99 ?  13  THR   A HG23 1 
ATOM   322  H HG23 B THR   A 1 13  ? 12.709 -18.138 5.457   0.12 13.92 ?  13  THR   A HG23 1 
ATOM   323  N N    A ASP   A 1 14  ? 14.594 -20.888 9.201   0.88 12.38 ?  14  ASP   A N    1 
ATOM   324  N N    B ASP   A 1 14  ? 14.403 -20.619 9.219   0.12 12.27 ?  14  ASP   A N    1 
ATOM   325  C CA   A ASP   A 1 14  ? 15.448 -21.163 10.349  0.88 12.91 ?  14  ASP   A CA   1 
ATOM   326  C CA   B ASP   A 1 14  ? 15.214 -20.973 10.379  0.12 12.63 ?  14  ASP   A CA   1 
ATOM   327  C C    A ASP   A 1 14  ? 16.273 -19.943 10.748  0.88 12.50 ?  14  ASP   A C    1 
ATOM   328  C C    B ASP   A 1 14  ? 16.168 -19.847 10.758  0.12 12.19 ?  14  ASP   A C    1 
ATOM   329  O O    A ASP   A 1 14  ? 16.510 -19.714 11.939  0.88 13.90 ?  14  ASP   A O    1 
ATOM   330  O O    B ASP   A 1 14  ? 16.402 -19.600 11.947  0.12 12.37 ?  14  ASP   A O    1 
ATOM   331  C CB   A ASP   A 1 14  ? 16.380 -22.328 10.032  0.88 15.60 ?  14  ASP   A CB   1 
ATOM   332  C CB   B ASP   A 1 14  ? 15.991 -22.256 10.088  0.12 13.50 ?  14  ASP   A CB   1 
ATOM   333  C CG   A ASP   A 1 14  ? 17.267 -22.686 11.197  0.88 20.29 ?  14  ASP   A CG   1 
ATOM   334  C CG   B ASP   A 1 14  ? 17.043 -22.549 11.137  0.12 14.36 ?  14  ASP   A CG   1 
ATOM   335  O OD1  A ASP   A 1 14  ? 16.721 -23.082 12.251  0.88 22.08 ?  14  ASP   A OD1  1 
ATOM   336  O OD1  B ASP   A 1 14  ? 16.682 -23.073 12.213  0.12 14.76 ?  14  ASP   A OD1  1 
ATOM   337  O OD2  A ASP   A 1 14  ? 18.498 -22.572 11.050  0.88 23.17 -1 14  ASP   A OD2  1 
ATOM   338  O OD2  B ASP   A 1 14  ? 18.229 -22.246 10.887  0.12 14.65 -1 14  ASP   A OD2  1 
ATOM   339  H H    A ASP   A 1 14  ? 14.663 -21.456 8.554   0.88 14.85 ?  14  ASP   A H    1 
ATOM   340  H H    B ASP   A 1 14  ? 14.488 -21.147 8.552   0.12 14.71 ?  14  ASP   A H    1 
ATOM   341  H HA   A ASP   A 1 14  ? 14.891 -21.411 11.101  0.88 15.48 ?  14  ASP   A HA   1 
ATOM   342  H HA   B ASP   A 1 14  ? 14.635 -21.137 11.138  0.12 15.15 ?  14  ASP   A HA   1 
ATOM   343  H HB2  A ASP   A 1 14  ? 15.835 -23.107 9.799   0.88 18.71 ?  14  ASP   A HB2  1 
ATOM   344  H HB2  B ASP   A 1 14  ? 15.368 -23.002 10.065  0.12 16.20 ?  14  ASP   A HB2  1 
ATOM   345  H HB3  A ASP   A 1 14  ? 16.945 -22.092 9.286   0.88 18.71 ?  14  ASP   A HB3  1 
ATOM   346  H HB3  B ASP   A 1 14  ? 16.433 -22.170 9.228   0.12 16.20 ?  14  ASP   A HB3  1 
ATOM   347  N N    . ASN   A 1 15  ? 16.728 -19.148 9.767   1.00 11.93 ?  15  ASN   A N    1 
ATOM   348  C CA   . ASN   A 1 15  ? 17.723 -18.112 10.025  1.00 12.17 ?  15  ASN   A CA   1 
ATOM   349  C C    . ASN   A 1 15  ? 17.353 -16.715 9.546   1.00 12.59 ?  15  ASN   A C    1 
ATOM   350  O O    . ASN   A 1 15  ? 18.128 -15.788 9.792   1.00 14.01 ?  15  ASN   A O    1 
ATOM   351  C CB   . ASN   A 1 15  ? 19.088 -18.508 9.433   1.00 12.01 ?  15  ASN   A CB   1 
ATOM   352  C CG   . ASN   A 1 15  ? 19.066 -18.595 7.928   1.00 12.46 ?  15  ASN   A CG   1 
ATOM   353  O OD1  . ASN   A 1 15  ? 18.339 -19.406 7.355   1.00 13.51 ?  15  ASN   A OD1  1 
ATOM   354  N ND2  . ASN   A 1 15  ? 19.856 -17.748 7.270   1.00 12.48 ?  15  ASN   A ND2  1 
ATOM   355  H H    A ASN   A 1 15  ? 16.472 -19.193 8.949   0.88 14.31 ?  15  ASN   A H    1 
ATOM   356  H H    B ASN   A 1 15  ? 16.540 -19.252 8.935   0.12 14.31 ?  15  ASN   A H    1 
ATOM   357  H HA   . ASN   A 1 15  ? 17.854 -18.049 10.983  1.00 14.60 ?  15  ASN   A HA   1 
ATOM   358  H HB2  . ASN   A 1 15  ? 19.752 -17.841 9.688   1.00 14.40 ?  15  ASN   A HB2  1 
ATOM   359  H HB3  . ASN   A 1 15  ? 19.350 -19.377 9.773   1.00 14.40 ?  15  ASN   A HB3  1 
ATOM   360  H HD21 . ASN   A 1 15  ? 19.875 -17.753 6.407   1.00 14.97 ?  15  ASN   A HD21 1 
ATOM   361  H HD22 . ASN   A 1 15  ? 20.355 -17.189 7.700   1.00 14.97 ?  15  ASN   A HD22 1 
ATOM   362  N N    A VAL   A 1 16  ? 16.222 -16.535 8.863   0.88 12.18 ?  16  VAL   A N    1 
ATOM   363  N N    B VAL   A 1 16  ? 16.193 -16.525 8.922   0.12 12.11 ?  16  VAL   A N    1 
ATOM   364  C CA   A VAL   A 1 16  ? 15.832 -15.249 8.295   0.88 11.96 ?  16  VAL   A CA   1 
ATOM   365  C CA   B VAL   A 1 16  ? 15.795 -15.234 8.370   0.12 11.70 ?  16  VAL   A CA   1 
ATOM   366  C C    A VAL   A 1 16  ? 14.548 -14.766 8.958   0.88 11.71 ?  16  VAL   A C    1 
ATOM   367  C C    B VAL   A 1 16  ? 14.602 -14.695 9.150   0.12 11.44 ?  16  VAL   A C    1 
ATOM   368  O O    A VAL   A 1 16  ? 13.541 -15.488 9.010   0.88 11.58 ?  16  VAL   A O    1 
ATOM   369  O O    B VAL   A 1 16  ? 13.654 -15.431 9.452   0.12 11.45 ?  16  VAL   A O    1 
ATOM   370  C CB   A VAL   A 1 16  ? 15.673 -15.311 6.767   0.88 12.84 ?  16  VAL   A CB   1 
ATOM   371  C CB   B VAL   A 1 16  ? 15.486 -15.340 6.863   0.12 11.68 ?  16  VAL   A CB   1 
ATOM   372  C CG1  A VAL   A 1 16  ? 15.234 -13.947 6.224   0.88 13.63 ?  16  VAL   A CG1  1 
ATOM   373  C CG1  B VAL   A 1 16  ? 15.071 -13.988 6.302   0.12 11.81 ?  16  VAL   A CG1  1 
ATOM   374  C CG2  A VAL   A 1 16  ? 16.966 -15.760 6.103   0.88 13.91 ?  16  VAL   A CG2  1 
ATOM   375  C CG2  B VAL   A 1 16  ? 16.697 -15.883 6.112   0.12 11.74 ?  16  VAL   A CG2  1 
ATOM   376  H H    A VAL   A 1 16  ? 15.651 -17.162 8.725   0.88 14.60 ?  16  VAL   A H    1 
ATOM   377  H H    B VAL   A 1 16  ? 15.608 -17.144 8.808   0.12 14.53 ?  16  VAL   A H    1 
ATOM   378  H HA   A VAL   A 1 16  ? 16.529 -14.602 8.491   0.88 14.34 ?  16  VAL   A HA   1 
ATOM   379  H HA   B VAL   A 1 16  ? 16.523 -14.607 8.479   0.12 14.03 ?  16  VAL   A HA   1 
ATOM   380  H HB   A VAL   A 1 16  ? 14.985 -15.958 6.550   0.88 15.40 ?  16  VAL   A HB   1 
ATOM   381  H HB   B VAL   A 1 16  ? 14.751 -15.958 6.730   0.12 14.00 ?  16  VAL   A HB   1 
ATOM   382  H HG11 A VAL   A 1 16  ? 15.342 -13.946 5.262   0.88 16.34 ?  16  VAL   A HG11 1 
ATOM   383  H HG11 B VAL   A 1 16  ? 15.053 -14.043 5.334   0.12 14.16 ?  16  VAL   A HG11 1 
ATOM   384  H HG12 A VAL   A 1 16  ? 14.301 -13.803 6.453   0.88 16.34 ?  16  VAL   A HG12 1 
ATOM   385  H HG12 B VAL   A 1 16  ? 14.189 -13.764 6.636   0.12 14.16 ?  16  VAL   A HG12 1 
ATOM   386  H HG13 A VAL   A 1 16  ? 15.785 -13.258 6.623   0.88 16.34 ?  16  VAL   A HG13 1 
ATOM   387  H HG13 B VAL   A 1 16  ? 15.714 -13.320 6.583   0.12 14.16 ?  16  VAL   A HG13 1 
ATOM   388  H HG21 A VAL   A 1 16  ? 16.859 -15.710 5.140   0.88 16.68 ?  16  VAL   A HG21 1 
ATOM   389  H HG21 B VAL   A 1 16  ? 16.507 -15.880 5.161   0.12 14.08 ?  16  VAL   A HG21 1 
ATOM   390  H HG22 A VAL   A 1 16  ? 17.686 -15.174 6.385   0.88 16.68 ?  16  VAL   A HG22 1 
ATOM   391  H HG22 B VAL   A 1 16  ? 17.463 -15.317 6.298   0.12 14.08 ?  16  VAL   A HG22 1 
ATOM   392  H HG23 A VAL   A 1 16  ? 17.159 -16.671 6.369   0.88 16.68 ?  16  VAL   A HG23 1 
ATOM   393  H HG23 B VAL   A 1 16  ? 16.876 -16.788 6.411   0.12 14.08 ?  16  VAL   A HG23 1 
ATOM   394  N N    A TYR   A 1 17  ? 14.586 -13.514 9.409   0.88 11.59 ?  17  TYR   A N    1 
ATOM   395  N N    B TYR   A 1 17  ? 14.656 -13.401 9.474   0.12 11.15 ?  17  TYR   A N    1 
ATOM   396  C CA   A TYR   A 1 17  ? 13.511 -12.836 10.110  0.88 11.60 ?  17  TYR   A CA   1 
ATOM   397  C CA   B TYR   A 1 17  ? 13.602 -12.714 10.208  0.12 10.86 ?  17  TYR   A CA   1 
ATOM   398  C C    A TYR   A 1 17  ? 13.242 -11.512 9.408   0.88 11.94 ?  17  TYR   A C    1 
ATOM   399  C C    B TYR   A 1 17  ? 13.348 -11.363 9.554   0.12 10.80 ?  17  TYR   A C    1 
ATOM   400  O O    A TYR   A 1 17  ? 14.148 -10.943 8.797   0.88 12.19 ?  17  TYR   A O    1 
ATOM   401  O O    B TYR   A 1 17  ? 14.227 -10.799 8.900   0.12 10.93 ?  17  TYR   A O    1 
ATOM   402  C CB   A TYR   A 1 17  ? 13.944 -12.570 11.553  0.88 12.14 ?  17  TYR   A CB   1 
ATOM   403  C CB   B TYR   A 1 17  ? 13.992 -12.495 11.675  0.12 10.88 ?  17  TYR   A CB   1 
ATOM   404  C CG   A TYR   A 1 17  ? 14.159 -13.835 12.358  0.88 13.05 ?  17  TYR   A CG   1 
ATOM   405  C CG   B TYR   A 1 17  ? 14.076 -13.761 12.490  0.12 10.93 ?  17  TYR   A CG   1 
ATOM   406  C CD1  A TYR   A 1 17  ? 15.334 -14.576 12.256  0.88 13.61 ?  17  TYR   A CD1  1 
ATOM   407  C CD1  B TYR   A 1 17  ? 15.203 -14.571 12.442  0.12 10.96 ?  17  TYR   A CD1  1 
ATOM   408  C CD2  A TYR   A 1 17  ? 13.168 -14.306 13.207  0.88 13.39 ?  17  TYR   A CD2  1 
ATOM   409  C CD2  B TYR   A 1 17  ? 13.028 -14.144 13.315  0.12 10.95 ?  17  TYR   A CD2  1 
ATOM   410  C CE1  A TYR   A 1 17  ? 15.512 -15.749 12.986  0.88 14.27 ?  17  TYR   A CE1  1 
ATOM   411  C CE1  B TYR   A 1 17  ? 15.279 -15.733 13.189  0.12 11.00 ?  17  TYR   A CE1  1 
ATOM   412  C CE2  A TYR   A 1 17  ? 13.339 -15.476 13.940  0.88 13.92 ?  17  TYR   A CE2  1 
ATOM   413  C CE2  B TYR   A 1 17  ? 13.094 -15.300 14.064  0.12 11.06 ?  17  TYR   A CE2  1 
ATOM   414  C CZ   A TYR   A 1 17  ? 14.512 -16.194 13.827  0.88 14.28 ?  17  TYR   A CZ   1 
ATOM   415  C CZ   B TYR   A 1 17  ? 14.221 -16.091 13.999  0.12 11.03 ?  17  TYR   A CZ   1 
ATOM   416  O OH   A TYR   A 1 17  ? 14.678 -17.352 14.560  0.88 15.02 ?  17  TYR   A OH   1 
ATOM   417  O OH   B TYR   A 1 17  ? 14.284 -17.243 14.748  0.12 11.07 ?  17  TYR   A OH   1 
ATOM   418  H H    A TYR   A 1 17  ? 15.272 -13.003 9.295   0.88 13.90 ?  17  TYR   A H    1 
ATOM   419  H H    B TYR   A 1 17  ? 15.315 -12.886 9.268   0.12 13.38 ?  17  TYR   A H    1 
ATOM   420  H HA   A TYR   A 1 17  ? 12.705 -13.380 10.097  0.88 13.92 ?  17  TYR   A HA   1 
ATOM   421  H HA   B TYR   A 1 17  ? 12.783 -13.229 10.176  0.12 13.03 ?  17  TYR   A HA   1 
ATOM   422  H HB2  A TYR   A 1 17  ? 14.779 -12.082 11.540  0.88 14.56 ?  17  TYR   A HB2  1 
ATOM   423  H HB2  B TYR   A 1 17  ? 14.862 -12.071 11.704  0.12 13.05 ?  17  TYR   A HB2  1 
ATOM   424  H HB3  A TYR   A 1 17  ? 13.259 -12.052 11.991  0.88 14.56 ?  17  TYR   A HB3  1 
ATOM   425  H HB3  B TYR   A 1 17  ? 13.331 -11.922 12.092  0.12 13.05 ?  17  TYR   A HB3  1 
ATOM   426  H HD1  A TYR   A 1 17  ? 16.010 -14.291 11.687  0.88 16.32 ?  17  TYR   A HD1  1 
ATOM   427  H HD1  B TYR   A 1 17  ? 15.915 -14.331 11.894  0.12 13.15 ?  17  TYR   A HD1  1 
ATOM   428  H HD2  A TYR   A 1 17  ? 12.371 -13.836 13.290  0.88 16.06 ?  17  TYR   A HD2  1 
ATOM   429  H HD2  B TYR   A 1 17  ? 12.265 -13.614 13.361  0.12 13.12 ?  17  TYR   A HD2  1 
ATOM   430  H HE1  A TYR   A 1 17  ? 16.304 -16.237 12.910  0.88 17.12 ?  17  TYR   A HE1  1 
ATOM   431  H HE1  B TYR   A 1 17  ? 16.041 -16.267 13.146  0.12 13.19 ?  17  TYR   A HE1  1 
ATOM   432  H HE2  A TYR   A 1 17  ? 12.663 -15.775 14.510  0.88 16.70 ?  17  TYR   A HE2  1 
ATOM   433  H HE2  B TYR   A 1 17  ? 12.384 -15.544 14.612  0.12 13.26 ?  17  TYR   A HE2  1 
ATOM   434  H HH   A TYR   A 1 17  ? 15.439 -17.678 14.421  0.88 18.02 ?  17  TYR   A HH   1 
ATOM   435  H HH   B TYR   A 1 17  ? 13.538 -17.395 15.101  0.12 13.28 ?  17  TYR   A HH   1 
ATOM   436  N N    A ILE   A 1 18  ? 12.007 -11.004 9.493   0.88 11.99 ?  18  ILE   A N    1 
ATOM   437  N N    B ILE   A 1 18  ? 12.137 -10.836 9.744   0.12 10.60 ?  18  ILE   A N    1 
ATOM   438  C CA   A ILE   A 1 18  ? 11.628 -9.796  8.761   0.88 12.31 ?  18  ILE   A CA   1 
ATOM   439  C CA   B ILE   A 1 18  ? 11.744 -9.573  9.124   0.12 10.49 ?  18  ILE   A CA   1 
ATOM   440  C C    A ILE   A 1 18  ? 10.673 -8.938  9.584   0.88 12.47 ?  18  ILE   A C    1 
ATOM   441  C C    B ILE   A 1 18  ? 10.857 -8.775  10.071  0.12 10.48 ?  18  ILE   A C    1 
ATOM   442  O O    A ILE   A 1 18  ? 9.835  -9.450  10.336  0.88 12.94 ?  18  ILE   A O    1 
ATOM   443  O O    B ILE   A 1 18  ? 10.032 -9.340  10.799  0.12 10.51 ?  18  ILE   A O    1 
ATOM   444  C CB   A ILE   A 1 18  ? 11.046 -10.163 7.373   0.88 12.50 ?  18  ILE   A CB   1 
ATOM   445  C CB   B ILE   A 1 18  ? 11.049 -9.798  7.764   0.12 10.30 ?  18  ILE   A CB   1 
ATOM   446  C CG1  A ILE   A 1 18  ? 10.980 -8.940  6.458   0.88 13.14 ?  18  ILE   A CG1  1 
ATOM   447  C CG1  B ILE   A 1 18  ? 10.806 -8.459  7.060   0.12 10.56 ?  18  ILE   A CG1  1 
ATOM   448  C CG2  A ILE   A 1 18  ? 9.691  -10.871 7.507   0.88 12.81 ?  18  ILE   A CG2  1 
ATOM   449  C CG2  B ILE   A 1 18  ? 9.745  -10.563 7.946   0.12 10.41 ?  18  ILE   A CG2  1 
ATOM   450  C CD1  A ILE   A 1 18  ? 10.741 -9.290  5.024   0.88 14.93 ?  18  ILE   A CD1  1 
ATOM   451  C CD1  B ILE   A 1 18  ? 10.314 -8.599  5.638   0.12 10.90 ?  18  ILE   A CD1  1 
ATOM   452  H H    A ILE   A 1 18  ? 11.373 -11.354 9.958   0.88 14.38 ?  18  ILE   A H    1 
ATOM   453  H H    B ILE   A 1 18  ? 11.523 -11.196 10.231  0.12 12.71 ?  18  ILE   A H    1 
ATOM   454  H HA   A ILE   A 1 18  ? 12.434 -9.278  8.603   0.88 14.77 ?  18  ILE   A HA   1 
ATOM   455  H HA   B ILE   A 1 18  ? 12.542 -9.049  8.964   0.12 12.58 ?  18  ILE   A HA   1 
ATOM   456  H HB   A ILE   A 1 18  ? 11.657 -10.791 6.958   0.88 15.00 ?  18  ILE   A HB   1 
ATOM   457  H HB   B ILE   A 1 18  ? 11.640 -10.328 7.212   0.12 12.35 ?  18  ILE   A HB   1 
ATOM   458  H HG12 A ILE   A 1 18  ? 10.260 -8.365  6.745   0.88 15.76 ?  18  ILE   A HG12 1 
ATOM   459  H HG12 B ILE   A 1 18  ? 10.139 -7.958  7.553   0.12 12.66 ?  18  ILE   A HG12 1 
ATOM   460  H HG13 A ILE   A 1 18  ? 11.826 -8.465  6.504   0.88 15.76 ?  18  ILE   A HG13 1 
ATOM   461  H HG13 B ILE   A 1 18  ? 11.638 -7.961  7.035   0.12 12.66 ?  18  ILE   A HG13 1 
ATOM   462  H HG21 A ILE   A 1 18  ? 9.427  -11.215 6.636   0.88 15.36 ?  18  ILE   A HG21 1 
ATOM   463  H HG21 B ILE   A 1 18  ? 9.411  -10.825 7.073   0.12 12.49 ?  18  ILE   A HG21 1 
ATOM   464  H HG22 A ILE   A 1 18  ? 9.780  -11.602 8.136   0.88 15.36 ?  18  ILE   A HG22 1 
ATOM   465  H HG22 B ILE   A 1 18  ? 9.914  -11.352 8.484   0.12 12.49 ?  18  ILE   A HG22 1 
ATOM   466  H HG23 A ILE   A 1 18  ? 9.031  -10.237 7.824   0.88 15.36 ?  18  ILE   A HG23 1 
ATOM   467  H HG23 B ILE   A 1 18  ? 9.099  -9.992  8.389   0.12 12.49 ?  18  ILE   A HG23 1 
ATOM   468  H HD11 A ILE   A 1 18  ? 10.768 -8.475  4.492   0.88 17.90 ?  18  ILE   A HD11 1 
ATOM   469  H HD11 B ILE   A 1 18  ? 10.263 -7.719  5.233   0.12 13.07 ?  18  ILE   A HD11 1 
ATOM   470  H HD12 A ILE   A 1 18  ? 11.432 -9.900  4.725   0.88 17.90 ?  18  ILE   A HD12 1 
ATOM   471  H HD12 B ILE   A 1 18  ? 10.935 -9.156  5.143   0.12 13.07 ?  18  ILE   A HD12 1 
ATOM   472  H HD13 A ILE   A 1 18  ? 9.870  -9.706  4.941   0.88 17.90 ?  18  ILE   A HD13 1 
ATOM   473  H HD13 B ILE   A 1 18  ? 9.436  -9.010  5.647   0.12 13.07 ?  18  ILE   A HD13 1 
ATOM   474  N N    A LYS   A 1 19  ? 10.780 -7.616  9.405   0.88 12.96 ?  19  LYS   A N    1 
ATOM   475  N N    B LYS   A 1 19  ? 11.028 -7.452  10.049  0.12 10.79 ?  19  LYS   A N    1 
ATOM   476  C CA   A LYS   A 1 19  ? 9.964  -6.664  10.149  0.88 14.34 ?  19  LYS   A CA   1 
ATOM   477  C CA   B LYS   A 1 19  ? 10.249 -6.526  10.859  0.12 11.42 ?  19  LYS   A CA   1 
ATOM   478  C C    A LYS   A 1 19  ? 9.756  -5.408  9.312   0.88 14.89 ?  19  LYS   A C    1 
ATOM   479  C C    B LYS   A 1 19  ? 9.941  -5.295  10.022  0.12 11.74 ?  19  LYS   A C    1 
ATOM   480  O O    A LYS   A 1 19  ? 10.648 -5.001  8.565   0.88 14.90 ?  19  LYS   A O    1 
ATOM   481  O O    B LYS   A 1 19  ? 10.806 -4.798  9.296   0.12 11.56 ?  19  LYS   A O    1 
ATOM   482  C CB   A LYS   A 1 19  ? 10.671 -6.288  11.457  0.88 15.21 ?  19  LYS   A CB   1 
ATOM   483  C CB   B LYS   A 1 19  ? 11.029 -6.112  12.116  0.12 11.86 ?  19  LYS   A CB   1 
ATOM   484  C CG   A LYS   A 1 19  ? 9.911  -5.369  12.404  0.88 16.60 ?  19  LYS   A CG   1 
ATOM   485  C CG   B LYS   A 1 19  ? 10.299 -5.163  13.051  0.12 12.40 ?  19  LYS   A CG   1 
ATOM   486  C CD   A LYS   A 1 19  ? 10.800 -5.065  13.606  0.88 18.03 ?  19  LYS   A CD   1 
ATOM   487  C CD   B LYS   A 1 19  ? 11.160 -4.850  14.267  0.12 12.87 ?  19  LYS   A CD   1 
ATOM   488  C CE   A LYS   A 1 19  ? 10.142 -4.144  14.614  0.88 19.24 ?  19  LYS   A CE   1 
ATOM   489  C CE   B LYS   A 1 19  ? 10.462 -3.903  15.227  0.12 13.26 ?  19  LYS   A CE   1 
ATOM   490  N NZ   A LYS   A 1 19  ? 11.037 -3.904  15.785  0.88 19.66 ?  19  LYS   A NZ   1 
ATOM   491  N NZ   B LYS   A 1 19  ? 11.290 -3.652  16.441  0.12 13.62 ?  19  LYS   A NZ   1 
ATOM   492  H H    A LYS   A 1 19  ? 11.327 -7.247  8.844   0.88 15.54 ?  19  LYS   A H    1 
ATOM   493  H H    B LYS   A 1 19  ? 11.613 -7.052  9.558   0.12 12.94 ?  19  LYS   A H    1 
ATOM   494  H HA   A LYS   A 1 19  ? 9.101  -7.063  10.349  0.88 17.20 ?  19  LYS   A HA   1 
ATOM   495  H HA   B LYS   A 1 19  ? 9.417  -6.939  11.131  0.12 13.69 ?  19  LYS   A HA   1 
ATOM   496  H HB2  A LYS   A 1 19  ? 10.859 -7.108  11.937  0.88 18.24 ?  19  LYS   A HB2  1 
ATOM   497  H HB2  B LYS   A 1 19  ? 11.237 -6.908  12.627  0.12 14.22 ?  19  LYS   A HB2  1 
ATOM   498  H HB3  A LYS   A 1 19  ? 11.503 -5.849  11.229  0.88 18.24 ?  19  LYS   A HB3  1 
ATOM   499  H HB3  B LYS   A 1 19  ? 11.851 -5.674  11.845  0.12 14.22 ?  19  LYS   A HB3  1 
ATOM   500  H HG2  A LYS   A 1 19  ? 9.695  -4.537  11.955  0.88 19.91 ?  19  LYS   A HG2  1 
ATOM   501  H HG2  B LYS   A 1 19  ? 10.110 -4.331  12.590  0.12 14.87 ?  19  LYS   A HG2  1 
ATOM   502  H HG3  A LYS   A 1 19  ? 9.103  -5.811  12.714  0.88 19.91 ?  19  LYS   A HG3  1 
ATOM   503  H HG3  B LYS   A 1 19  ? 9.478  -5.577  13.358  0.12 14.87 ?  19  LYS   A HG3  1 
ATOM   504  H HD2  A LYS   A 1 19  ? 11.015 -5.897  14.058  0.88 21.63 ?  19  LYS   A HD2  1 
ATOM   505  H HD2  B LYS   A 1 19  ? 11.354 -5.673  14.743  0.12 15.43 ?  19  LYS   A HD2  1 
ATOM   506  H HD3  A LYS   A 1 19  ? 11.615 -4.639  13.296  0.88 21.63 ?  19  LYS   A HD3  1 
ATOM   507  H HD3  B LYS   A 1 19  ? 11.985 -4.436  13.972  0.12 15.43 ?  19  LYS   A HD3  1 
ATOM   508  H HE2  A LYS   A 1 19  ? 9.956  -3.288  14.196  0.88 23.08 ?  19  LYS   A HE2  1 
ATOM   509  H HE2  B LYS   A 1 19  ? 10.305 -3.054  14.784  0.12 15.90 ?  19  LYS   A HE2  1 
ATOM   510  H HE3  A LYS   A 1 19  ? 9.322  -4.548  14.936  0.88 23.08 ?  19  LYS   A HE3  1 
ATOM   511  H HE3  B LYS   A 1 19  ? 9.620  -4.296  15.508  0.12 15.90 ?  19  LYS   A HE3  1 
ATOM   512  H HZ1  A LYS   A 1 19  ? 10.628 -3.383  16.380  0.88 23.58 ?  19  LYS   A HZ1  1 
ATOM   513  H HZ1  B LYS   A 1 19  ? 10.863 -3.097  16.990  0.12 16.34 ?  19  LYS   A HZ1  1 
ATOM   514  H HZ2  A LYS   A 1 19  ? 11.243 -4.678  16.173  0.88 23.58 ?  19  LYS   A HZ2  1 
ATOM   515  H HZ2  B LYS   A 1 19  ? 11.444 -4.418  16.867  0.12 16.34 ?  19  LYS   A HZ2  1 
ATOM   516  H HZ3  A LYS   A 1 19  ? 11.786 -3.505  15.520  0.88 23.58 ?  19  LYS   A HZ3  1 
ATOM   517  H HZ3  B LYS   A 1 19  ? 12.067 -3.288  16.208  0.12 16.34 ?  19  LYS   A HZ3  1 
ATOM   518  N N    A ASN   A 1 20  ? 8.573  -4.803  9.430   0.88 16.06 ?  20  ASN   A N    1 
ATOM   519  N N    B ASN   A 1 20  ? 8.705  -4.808  10.121  0.12 12.66 ?  20  ASN   A N    1 
ATOM   520  C CA   A ASN   A 1 20  ? 8.332  -3.474  8.875   0.88 17.77 ?  20  ASN   A CA   1 
ATOM   521  C CA   B ASN   A 1 20  ? 8.269  -3.633  9.366   0.12 13.69 ?  20  ASN   A CA   1 
ATOM   522  C C    A ASN   A 1 20  ? 8.949  -2.471  9.839   0.88 18.27 ?  20  ASN   A C    1 
ATOM   523  C C    B ASN   A 1 20  ? 8.725  -2.391  10.123  0.12 14.08 ?  20  ASN   A C    1 
ATOM   524  O O    A ASN   A 1 20  ? 8.427  -2.250  10.937  0.88 19.40 ?  20  ASN   A O    1 
ATOM   525  O O    B ASN   A 1 20  ? 8.009  -1.847  10.965  0.12 14.24 ?  20  ASN   A O    1 
ATOM   526  C CB   A ASN   A 1 20  ? 6.832  -3.243  8.693   0.88 19.07 ?  20  ASN   A CB   1 
ATOM   527  C CB   B ASN   A 1 20  ? 6.758  -3.659  9.168   0.12 14.25 ?  20  ASN   A CB   1 
ATOM   528  C CG   A ASN   A 1 20  ? 6.486  -1.802  8.312   0.88 20.85 ?  20  ASN   A CG   1 
ATOM   529  C CG   B ASN   A 1 20  ? 6.229  -2.427  8.457   0.12 14.83 ?  20  ASN   A CG   1 
ATOM   530  O OD1  A ASN   A 1 20  ? 5.521  -1.232  8.828   0.88 22.96 ?  20  ASN   A OD1  1 
ATOM   531  O OD1  B ASN   A 1 20  ? 5.163  -1.913  8.801   0.12 15.08 ?  20  ASN   A OD1  1 
ATOM   532  N ND2  A ASN   A 1 20  ? 7.257  -1.219  7.406   0.88 21.30 ?  20  ASN   A ND2  1 
ATOM   533  N ND2  B ASN   A 1 20  ? 6.969  -1.944  7.468   0.12 15.16 ?  20  ASN   A ND2  1 
ATOM   534  H H    A ASN   A 1 20  ? 7.892  -5.146  9.829   0.88 19.26 ?  20  ASN   A H    1 
ATOM   535  H H    B ASN   A 1 20  ? 8.095  -5.145  10.621  0.12 15.19 ?  20  ASN   A H    1 
ATOM   536  H HA   A ASN   A 1 20  ? 8.768  -3.394  8.015   0.88 21.32 ?  20  ASN   A HA   1 
ATOM   537  H HA   B ASN   A 1 20  ? 8.696  -3.642  8.500   0.12 16.42 ?  20  ASN   A HA   1 
ATOM   538  H HB2  A ASN   A 1 20  ? 6.509  -3.823  7.986   0.88 22.88 ?  20  ASN   A HB2  1 
ATOM   539  H HB2  B ASN   A 1 20  ? 6.517  -4.441  8.653   0.12 17.09 ?  20  ASN   A HB2  1 
ATOM   540  H HB3  A ASN   A 1 20  ? 6.379  -3.454  9.524   0.88 22.88 ?  20  ASN   A HB3  1 
ATOM   541  H HB3  B ASN   A 1 20  ? 6.330  -3.694  10.030  0.12 17.09 ?  20  ASN   A HB3  1 
ATOM   542  H HD21 A ASN   A 1 20  ? 7.093  -0.410  7.167   0.88 25.55 ?  20  ASN   A HD21 1 
ATOM   543  H HD21 B ASN   A 1 20  ? 6.707  -1.246  7.040   0.12 18.18 ?  20  ASN   A HD21 1 
ATOM   544  H HD22 A ASN   A 1 20  ? 7.918  -1.645  7.066   0.88 25.55 ?  20  ASN   A HD22 1 
ATOM   545  H HD22 B ASN   A 1 20  ? 7.709  -2.325  7.254   0.12 18.18 ?  20  ASN   A HD22 1 
ATOM   546  N N    A ALA   A 1 21  ? 10.080 -1.887  9.455   0.88 18.42 ?  21  ALA   A N    1 
ATOM   547  N N    B ALA   A 1 21  ? 9.935  -1.930  9.808   0.12 14.26 ?  21  ALA   A N    1 
ATOM   548  C CA   A ALA   A 1 21  ? 10.783 -0.998  10.367  0.88 18.13 ?  21  ALA   A CA   1 
ATOM   549  C CA   B ALA   A 1 21  ? 10.549 -0.845  10.559  0.12 14.46 ?  21  ALA   A CA   1 
ATOM   550  C C    A ALA   A 1 21  ? 11.738 -0.116  9.587   0.88 17.78 ?  21  ALA   A C    1 
ATOM   551  C C    B ALA   A 1 21  ? 11.701 -0.257  9.757   0.12 14.51 ?  21  ALA   A C    1 
ATOM   552  O O    A ALA   A 1 21  ? 12.185 -0.477  8.495   0.88 17.95 ?  21  ALA   A O    1 
ATOM   553  O O    B ALA   A 1 21  ? 12.220 -0.880  8.827   0.12 14.30 ?  21  ALA   A O    1 
ATOM   554  C CB   A ALA   A 1 21  ? 11.562 -1.783  11.424  0.88 19.09 ?  21  ALA   A CB   1 
ATOM   555  C CB   B ALA   A 1 21  ? 11.045 -1.334  11.924  0.12 14.53 ?  21  ALA   A CB   1 
ATOM   556  H H    A ALA   A 1 21  ? 10.451 -1.984  8.684   0.88 22.09 ?  21  ALA   A H    1 
ATOM   557  H H    B ALA   A 1 21  ? 10.414 -2.228  9.160   0.12 17.10 ?  21  ALA   A H    1 
ATOM   558  H HA   A ALA   A 1 21  ? 10.133 -0.430  10.820  0.88 21.75 ?  21  ALA   A HA   1 
ATOM   559  H HA   B ALA   A 1 21  ? 9.893  -0.146  10.707  0.12 17.34 ?  21  ALA   A HA   1 
ATOM   560  H HB1  A ALA   A 1 21  ? 11.969 -1.156  12.036  0.88 22.89 ?  21  ALA   A HB1  1 
ATOM   561  H HB1  B ALA   A 1 21  ? 11.529 -0.619  12.361  0.12 17.43 ?  21  ALA   A HB1  1 
ATOM   562  H HB2  A ALA   A 1 21  ? 10.943 -2.361  11.903  0.88 22.89 ?  21  ALA   A HB2  1 
ATOM   563  H HB2  B ALA   A 1 21  ? 10.282 -1.599  12.461  0.12 17.43 ?  21  ALA   A HB2  1 
ATOM   564  H HB3  A ALA   A 1 21  ? 12.237 -2.316  10.983  0.88 22.89 ?  21  ALA   A HB3  1 
ATOM   565  H HB3  B ALA   A 1 21  ? 11.635 -2.093  11.789  0.12 17.43 ?  21  ALA   A HB3  1 
ATOM   566  N N    A ASP   A 1 22  ? 12.027 1.049   10.175  0.88 17.97 ?  22  ASP   A N    1 
ATOM   567  N N    B ASP   A 1 22  ? 12.088 0.962   10.133  0.12 14.79 ?  22  ASP   A N    1 
ATOM   568  C CA   A ASP   A 1 22  ? 13.066 1.954   9.707   0.88 17.73 ?  22  ASP   A CA   1 
ATOM   569  C CA   B ASP   A 1 22  ? 13.240 1.628   9.541   0.12 14.98 ?  22  ASP   A CA   1 
ATOM   570  C C    A ASP   A 1 22  ? 14.401 1.445   10.240  0.88 16.31 ?  22  ASP   A C    1 
ATOM   571  C C    B ASP   A 1 22  ? 14.520 1.048   10.134  0.12 14.56 ?  22  ASP   A C    1 
ATOM   572  O O    A ASP   A 1 22  ? 14.610 1.407   11.456  0.88 16.93 ?  22  ASP   A O    1 
ATOM   573  O O    B ASP   A 1 22  ? 14.640 0.905   11.355  0.12 14.48 ?  22  ASP   A O    1 
ATOM   574  C CB   A ASP   A 1 22  ? 12.768 3.347   10.257  0.88 19.84 ?  22  ASP   A CB   1 
ATOM   575  C CB   B ASP   A 1 22  ? 13.168 3.128   9.834   0.12 15.61 ?  22  ASP   A CB   1 
ATOM   576  C CG   A ASP   A 1 22  ? 13.726 4.402   9.742   0.88 21.78 ?  22  ASP   A CG   1 
ATOM   577  C CG   B ASP   A 1 22  ? 14.255 3.920   9.124   0.12 15.97 ?  22  ASP   A CG   1 
ATOM   578  O OD1  A ASP   A 1 22  ? 14.848 4.056   9.327   0.88 21.87 ?  22  ASP   A OD1  1 
ATOM   579  O OD1  B ASP   A 1 22  ? 15.097 3.307   8.436   0.12 15.99 ?  22  ASP   A OD1  1 
ATOM   580  O OD2  A ASP   A 1 22  ? 13.362 5.593   9.773   0.88 23.55 -1 22  ASP   A OD2  1 
ATOM   581  O OD2  B ASP   A 1 22  ? 14.265 5.162   9.254   0.12 16.17 -1 22  ASP   A OD2  1 
ATOM   582  H H    A ASP   A 1 22  ? 11.604 1.343   10.873  0.88 21.55 ?  22  ASP   A H    1 
ATOM   583  H H    B ASP   A 1 22  ? 11.685 1.431   10.731  0.12 17.74 ?  22  ASP   A H    1 
ATOM   584  H HA   A ASP   A 1 22  ? 13.083 1.975   8.739   0.88 21.26 ?  22  ASP   A HA   1 
ATOM   585  H HA   B ASP   A 1 22  ? 13.240 1.495   8.577   0.12 17.97 ?  22  ASP   A HA   1 
ATOM   586  H HB2  A ASP   A 1 22  ? 11.864 3.598   10.009  0.88 23.80 ?  22  ASP   A HB2  1 
ATOM   587  H HB2  B ASP   A 1 22  ? 12.307 3.469   9.543   0.12 18.72 ?  22  ASP   A HB2  1 
ATOM   588  H HB3  A ASP   A 1 22  ? 12.847 3.322   11.226  0.88 23.80 ?  22  ASP   A HB3  1 
ATOM   589  H HB3  B ASP   A 1 22  ? 13.270 3.266   10.790  0.12 18.72 ?  22  ASP   A HB3  1 
ATOM   590  N N    A ILE   A 1 23  ? 15.294 1.033   9.338   0.88 15.50 ?  23  ILE   A N    1 
ATOM   591  N N    B ILE   A 1 23  ? 15.479 0.716   9.265   0.12 14.37 ?  23  ILE   A N    1 
ATOM   592  C CA   A ILE   A 1 23  ? 16.555 0.427   9.760   0.88 14.36 ?  23  ILE   A CA   1 
ATOM   593  C CA   B ILE   A 1 23  ? 16.721 0.098   9.721   0.12 14.29 ?  23  ILE   A CA   1 
ATOM   594  C C    A ILE   A 1 23  ? 17.361 1.373   10.639  0.88 14.41 ?  23  ILE   A C    1 
ATOM   595  C C    B ILE   A 1 23  ? 17.505 1.051   10.612  0.12 14.75 ?  23  ILE   A C    1 
ATOM   596  O O    A ILE   A 1 23  ? 18.089 0.925   11.533  0.88 14.68 ?  23  ILE   A O    1 
ATOM   597  O O    B ILE   A 1 23  ? 18.256 0.614   11.493  0.12 14.64 ?  23  ILE   A O    1 
ATOM   598  C CB   A ILE   A 1 23  ? 17.356 -0.078  8.540   0.88 13.90 ?  23  ILE   A CB   1 
ATOM   599  C CB   B ILE   A 1 23  ? 17.559 -0.412  8.527   0.12 13.77 ?  23  ILE   A CB   1 
ATOM   600  C CG1  A ILE   A 1 23  ? 18.512 -0.974  8.990   0.88 13.92 ?  23  ILE   A CG1  1 
ATOM   601  C CG1  B ILE   A 1 23  ? 18.616 -1.408  9.013   0.12 13.52 ?  23  ILE   A CG1  1 
ATOM   602  C CG2  A ILE   A 1 23  ? 17.842 1.085   7.681   0.88 14.07 ?  23  ILE   A CG2  1 
ATOM   603  C CG2  B ILE   A 1 23  ? 18.223 0.745   7.785   0.12 13.68 ?  23  ILE   A CG2  1 
ATOM   604  C CD1  A ILE   A 1 23  ? 19.238 -1.661  7.843   0.88 14.00 ?  23  ILE   A CD1  1 
ATOM   605  C CD1  B ILE   A 1 23  ? 19.508 -1.945  7.913   0.12 13.42 ?  23  ILE   A CD1  1 
ATOM   606  H H    A ILE   A 1 23  ? 15.184 1.086   8.494   0.88 18.59 ?  23  ILE   A H    1 
ATOM   607  H H    B ILE   A 1 23  ? 15.434 0.838   8.426   0.12 17.24 ?  23  ILE   A H    1 
ATOM   608  H HA   A ILE   A 1 23  ? 16.350 -0.348  10.303  0.88 17.23 ?  23  ILE   A HA   1 
ATOM   609  H HA   B ILE   A 1 23  ? 16.490 -0.673  10.253  0.12 17.14 ?  23  ILE   A HA   1 
ATOM   610  H HB   A ILE   A 1 23  ? 16.757 -0.615  8.001   0.88 16.67 ?  23  ILE   A HB   1 
ATOM   611  H HB   B ILE   A 1 23  ? 16.969 -0.872  7.909   0.12 16.51 ?  23  ILE   A HB   1 
ATOM   612  H HG12 A ILE   A 1 23  ? 19.161 -0.436  9.469   0.88 16.69 ?  23  ILE   A HG12 1 
ATOM   613  H HG12 B ILE   A 1 23  ? 19.183 -0.970  9.665   0.12 16.21 ?  23  ILE   A HG12 1 
ATOM   614  H HG13 A ILE   A 1 23  ? 18.164 -1.667  9.575   0.88 16.69 ?  23  ILE   A HG13 1 
ATOM   615  H HG13 B ILE   A 1 23  ? 18.166 -2.164  9.423   0.12 16.21 ?  23  ILE   A HG13 1 
ATOM   616  H HG21 A ILE   A 1 23  ? 18.193 0.734   6.847   0.88 16.87 ?  23  ILE   A HG21 1 
ATOM   617  H HG21 B ILE   A 1 23  ? 18.518 0.434   6.912   0.12 16.41 ?  23  ILE   A HG21 1 
ATOM   618  H HG22 A ILE   A 1 23  ? 17.093 1.676   7.499   0.88 16.87 ?  23  ILE   A HG22 1 
ATOM   619  H HG22 B ILE   A 1 23  ? 17.581 1.462   7.679   0.12 16.41 ?  23  ILE   A HG22 1 
ATOM   620  H HG23 A ILE   A 1 23  ? 18.534 1.565   8.158   0.88 16.87 ?  23  ILE   A HG23 1 
ATOM   621  H HG23 B ILE   A 1 23  ? 18.986 1.056   8.298   0.12 16.41 ?  23  ILE   A HG23 1 
ATOM   622  H HD11 A ILE   A 1 23  ? 19.899 -2.269  8.207   0.88 16.79 ?  23  ILE   A HD11 1 
ATOM   623  H HD11 B ILE   A 1 23  ? 20.040 -2.675  8.269   0.12 16.09 ?  23  ILE   A HD11 1 
ATOM   624  H HD12 A ILE   A 1 23  ? 18.591 -2.152  7.311   0.88 16.79 ?  23  ILE   A HD12 1 
ATOM   625  H HD12 B ILE   A 1 23  ? 18.953 -2.264  7.185   0.12 16.09 ?  23  ILE   A HD12 1 
ATOM   626  H HD13 A ILE   A 1 23  ? 19.672 -0.987  7.297   0.88 16.79 ?  23  ILE   A HD13 1 
ATOM   627  H HD13 B ILE   A 1 23  ? 20.089 -1.234  7.601   0.12 16.09 ?  23  ILE   A HD13 1 
ATOM   628  N N    A VAL   A 1 24  ? 17.236 2.685   10.419  0.88 15.46 ?  24  VAL   A N    1 
ATOM   629  N N    B VAL   A 1 24  ? 17.344 2.359   10.408  0.12 15.53 ?  24  VAL   A N    1 
ATOM   630  C CA   A VAL   A 1 24  ? 17.922 3.654   11.271  0.88 16.82 ?  24  VAL   A CA   1 
ATOM   631  C CA   B VAL   A 1 24  ? 18.021 3.332   11.259  0.12 16.26 ?  24  VAL   A CA   1 
ATOM   632  C C    A VAL   A 1 24  ? 17.417 3.549   12.703  0.88 17.56 ?  24  VAL   A C    1 
ATOM   633  C C    B VAL   A 1 24  ? 17.439 3.302   12.667  0.12 16.91 ?  24  VAL   A C    1 
ATOM   634  O O    A VAL   A 1 24  ? 18.201 3.473   13.657  0.88 17.64 ?  24  VAL   A O    1 
ATOM   635  O O    B VAL   A 1 24  ? 18.174 3.289   13.661  0.12 16.89 ?  24  VAL   A O    1 
ATOM   636  C CB   A VAL   A 1 24  ? 17.747 5.076   10.711  0.88 17.87 ?  24  VAL   A CB   1 
ATOM   637  C CB   B VAL   A 1 24  ? 17.948 4.735   10.632  0.12 16.44 ?  24  VAL   A CB   1 
ATOM   638  C CG1  A VAL   A 1 24  ? 18.280 6.114   11.696  0.88 18.84 ?  24  VAL   A CG1  1 
ATOM   639  C CG1  B VAL   A 1 24  ? 18.472 5.780   11.603  0.12 16.60 ?  24  VAL   A CG1  1 
ATOM   640  C CG2  A VAL   A 1 24  ? 18.438 5.201   9.360   0.88 18.75 ?  24  VAL   A CG2  1 
ATOM   641  C CG2  B VAL   A 1 24  ? 18.734 4.770   9.331   0.12 16.48 ?  24  VAL   A CG2  1 
ATOM   642  H H    A VAL   A 1 24  ? 16.768 3.034   9.790   0.88 18.54 ?  24  VAL   A H    1 
ATOM   643  H H    B VAL   A 1 24  ? 16.856 2.705   9.791   0.12 18.62 ?  24  VAL   A H    1 
ATOM   644  H HA   A VAL   A 1 24  ? 18.870 3.456   11.278  0.88 20.17 ?  24  VAL   A HA   1 
ATOM   645  H HA   B VAL   A 1 24  ? 18.957 3.089   11.324  0.12 19.50 ?  24  VAL   A HA   1 
ATOM   646  H HB   A VAL   A 1 24  ? 16.802 5.250   10.577  0.88 21.43 ?  24  VAL   A HB   1 
ATOM   647  H HB   B VAL   A 1 24  ? 17.023 4.946   10.430  0.12 19.72 ?  24  VAL   A HB   1 
ATOM   648  H HG11 A VAL   A 1 24  ? 18.410 6.952   11.227  0.88 22.59 ?  24  VAL   A HG11 1 
ATOM   649  H HG11 B VAL   A 1 24  ? 18.657 6.596   11.113  0.12 19.91 ?  24  VAL   A HG11 1 
ATOM   650  H HG12 A VAL   A 1 24  ? 17.635 6.232   12.410  0.88 22.59 ?  24  VAL   A HG12 1 
ATOM   651  H HG12 B VAL   A 1 24  ? 17.799 5.948   12.281  0.12 19.91 ?  24  VAL   A HG12 1 
ATOM   652  H HG13 A VAL   A 1 24  ? 19.124 5.801   12.055  0.88 22.59 ?  24  VAL   A HG13 1 
ATOM   653  H HG13 B VAL   A 1 24  ? 19.285 5.448   12.013  0.12 19.91 ?  24  VAL   A HG13 1 
ATOM   654  H HG21 A VAL   A 1 24  ? 18.267 6.083   8.996   0.88 22.49 ?  24  VAL   A HG21 1 
ATOM   655  H HG21 B VAL   A 1 24  ? 18.606 5.633   8.911   0.12 19.77 ?  24  VAL   A HG21 1 
ATOM   656  H HG22 A VAL   A 1 24  ? 19.392 5.073   9.481   0.88 22.49 ?  24  VAL   A HG22 1 
ATOM   657  H HG22 B VAL   A 1 24  ? 19.673 4.636   9.529   0.12 19.77 ?  24  VAL   A HG22 1 
ATOM   658  H HG23 A VAL   A 1 24  ? 18.087 4.523   8.760   0.88 22.49 ?  24  VAL   A HG23 1 
ATOM   659  H HG23 B VAL   A 1 24  ? 18.413 4.065   8.746   0.12 19.77 ?  24  VAL   A HG23 1 
ATOM   660  N N    A GLU   A 1 25  ? 16.094 3.542   12.872  0.88 18.71 ?  25  GLU   A N    1 
ATOM   661  N N    B GLU   A 1 25  ? 16.108 3.292   12.773  0.12 17.62 ?  25  GLU   A N    1 
ATOM   662  C CA   A GLU   A 1 25  ? 15.519 3.463   14.211  0.88 20.21 ?  25  GLU   A CA   1 
ATOM   663  C CA   B GLU   A 1 25  ? 15.478 3.193   14.086  0.12 18.40 ?  25  GLU   A CA   1 
ATOM   664  C C    A GLU   A 1 25  ? 15.776 2.099   14.843  0.88 19.35 ?  25  GLU   A C    1 
ATOM   665  C C    B GLU   A 1 25  ? 15.721 1.825   14.712  0.12 18.08 ?  25  GLU   A C    1 
ATOM   666  O O    A GLU   A 1 25  ? 16.039 2.009   16.048  0.88 19.98 ?  25  GLU   A O    1 
ATOM   667  O O    B GLU   A 1 25  ? 15.882 1.716   15.933  0.12 18.17 ?  25  GLU   A O    1 
ATOM   668  C CB   A GLU   A 1 25  ? 14.024 3.788   14.159  0.88 22.63 ?  25  GLU   A CB   1 
ATOM   669  C CB   B GLU   A 1 25  ? 13.981 3.488   13.976  0.12 19.42 ?  25  GLU   A CB   1 
ATOM   670  C CG   A GLU   A 1 25  ? 13.737 5.230   13.755  0.88 25.57 ?  25  GLU   A CG   1 
ATOM   671  C CG   B GLU   A 1 25  ? 13.667 4.912   13.546  0.12 20.46 ?  25  GLU   A CG   1 
ATOM   672  C CD   A GLU   A 1 25  ? 14.487 6.233   14.617  0.88 28.06 ?  25  GLU   A CD   1 
ATOM   673  C CD   B GLU   A 1 25  ? 14.171 5.941   14.536  0.12 21.30 ?  25  GLU   A CD   1 
ATOM   674  O OE1  A GLU   A 1 25  ? 14.517 6.054   15.854  0.88 28.86 ?  25  GLU   A OE1  1 
ATOM   675  O OE1  B GLU   A 1 25  ? 14.219 5.629   15.745  0.12 21.55 ?  25  GLU   A OE1  1 
ATOM   676  O OE2  A GLU   A 1 25  ? 15.068 7.185   14.056  0.88 29.19 -1 25  GLU   A OE2  1 
ATOM   677  O OE2  B GLU   A 1 25  ? 14.523 7.059   14.106  0.12 21.61 -1 25  GLU   A OE2  1 
ATOM   678  H H    A GLU   A 1 25  ? 15.513 3.584   12.236  0.88 22.44 ?  25  GLU   A H    1 
ATOM   679  H H    B GLU   A 1 25  ? 15.560 3.346   12.113  0.12 21.13 ?  25  GLU   A H    1 
ATOM   680  H HA   A GLU   A 1 25  ? 15.945 4.124   14.775  0.88 24.24 ?  25  GLU   A HA   1 
ATOM   681  H HA   B GLU   A 1 25  ? 15.871 3.856   14.672  0.12 22.07 ?  25  GLU   A HA   1 
ATOM   682  H HB2  A GLU   A 1 25  ? 13.590 3.211   13.510  0.88 27.14 ?  25  GLU   A HB2  1 
ATOM   683  H HB2  B GLU   A 1 25  ? 13.590 2.890   13.321  0.12 23.29 ?  25  GLU   A HB2  1 
ATOM   684  H HB3  A GLU   A 1 25  ? 13.632 3.648   15.036  0.88 27.14 ?  25  GLU   A HB3  1 
ATOM   685  H HB3  B GLU   A 1 25  ? 13.569 3.343   14.842  0.12 23.29 ?  25  GLU   A HB3  1 
ATOM   686  H HG2  A GLU   A 1 25  ? 14.024 5.366   12.839  0.88 30.68 ?  25  GLU   A HG2  1 
ATOM   687  H HG2  B GLU   A 1 25  ? 14.084 5.084   12.687  0.12 24.55 ?  25  GLU   A HG2  1 
ATOM   688  H HG3  A GLU   A 1 25  ? 12.781 5.398   13.829  0.88 30.68 ?  25  GLU   A HG3  1 
ATOM   689  H HG3  B GLU   A 1 25  ? 12.707 5.020   13.478  0.12 24.55 ?  25  GLU   A HG3  1 
ATOM   690  N N    A GLU   A 1 26  ? 15.726 1.029   14.045  0.88 18.87 ?  26  GLU   A N    1 
ATOM   691  N N    B GLU   A 1 26  ? 15.751 0.769   13.895  0.12 17.72 ?  26  GLU   A N    1 
ATOM   692  C CA   A GLU   A 1 26  ? 16.045 -0.299  14.563  0.88 18.36 ?  26  GLU   A CA   1 
ATOM   693  C CA   B GLU   A 1 26  ? 16.092 -0.550  14.415  0.12 17.38 ?  26  GLU   A CA   1 
ATOM   694  C C    A GLU   A 1 26  ? 17.479 -0.352  15.077  0.88 16.93 ?  26  GLU   A C    1 
ATOM   695  C C    B GLU   A 1 26  ? 17.527 -0.597  14.914  0.12 16.66 ?  26  GLU   A C    1 
ATOM   696  O O    A GLU   A 1 26  ? 17.747 -0.869  16.168  0.88 16.90 ?  26  GLU   A O    1 
ATOM   697  O O    B GLU   A 1 26  ? 17.828 -1.325  15.866  0.12 16.68 ?  26  GLU   A O    1 
ATOM   698  C CB   A GLU   A 1 26  ? 15.858 -1.345  13.463  0.88 19.98 ?  26  GLU   A CB   1 
ATOM   699  C CB   B GLU   A 1 26  ? 15.884 -1.612  13.336  0.12 17.77 ?  26  GLU   A CB   1 
ATOM   700  C CG   A GLU   A 1 26  ? 14.481 -1.949  13.341  0.88 22.15 ?  26  GLU   A CG   1 
ATOM   701  C CG   B GLU   A 1 26  ? 14.430 -1.884  13.017  0.12 18.09 ?  26  GLU   A CG   1 
ATOM   702  C CD   A GLU   A 1 26  ? 14.058 -2.720  14.578  0.88 23.19 ?  26  GLU   A CD   1 
ATOM   703  C CD   B GLU   A 1 26  ? 13.685 -2.493  14.183  0.12 18.25 ?  26  GLU   A CD   1 
ATOM   704  O OE1  A GLU   A 1 26  ? 14.522 -3.866  14.824  0.88 23.49 ?  26  GLU   A OE1  1 
ATOM   705  O OE1  B GLU   A 1 26  ? 14.210 -3.446  14.796  0.12 18.73 ?  26  GLU   A OE1  1 
ATOM   706  O OE2  A GLU   A 1 26  ? 13.230 -2.167  15.309  0.88 24.02 -1 26  GLU   A OE2  1 
ATOM   707  O OE2  B GLU   A 1 26  ? 12.575 -2.014  14.492  0.12 17.86 -1 26  GLU   A OE2  1 
ATOM   708  H H    A GLU   A 1 26  ? 15.518 1.051   13.212  0.88 22.64 ?  26  GLU   A H    1 
ATOM   709  H H    B GLU   A 1 26  ? 15.583 0.790   13.052  0.12 21.26 ?  26  GLU   A H    1 
ATOM   710  H HA   A GLU   A 1 26  ? 15.449 -0.508  15.297  0.88 22.02 ?  26  GLU   A HA   1 
ATOM   711  H HA   B GLU   A 1 26  ? 15.512 -0.757  15.162  0.12 20.85 ?  26  GLU   A HA   1 
ATOM   712  H HB2  A GLU   A 1 26  ? 16.069 -0.930  12.611  0.88 23.96 ?  26  GLU   A HB2  1 
ATOM   713  H HB2  B GLU   A 1 26  ? 16.316 -1.318  12.519  0.12 21.32 ?  26  GLU   A HB2  1 
ATOM   714  H HB3  A GLU   A 1 26  ? 16.478 -2.070  13.629  0.88 23.96 ?  26  GLU   A HB3  1 
ATOM   715  H HB3  B GLU   A 1 26  ? 16.284 -2.445  13.635  0.12 21.32 ?  26  GLU   A HB3  1 
ATOM   716  H HG2  A GLU   A 1 26  ? 13.841 -1.231  13.186  0.88 26.58 ?  26  GLU   A HG2  1 
ATOM   717  H HG2  B GLU   A 1 26  ? 13.993 -1.049  12.799  0.12 21.70 ?  26  GLU   A HG2  1 
ATOM   718  H HG3  A GLU   A 1 26  ? 14.469 -2.565  12.595  0.88 26.58 ?  26  GLU   A HG3  1 
ATOM   719  H HG3  B GLU   A 1 26  ? 14.380 -2.497  12.268  0.12 21.70 ?  26  GLU   A HG3  1 
ATOM   720  N N    . ALA   A 1 27  ? 18.423 0.168   14.290  1.00 15.99 ?  27  ALA   A N    1 
ATOM   721  C CA   . ALA   A 1 27  ? 19.818 0.153   14.712  1.00 15.70 ?  27  ALA   A CA   1 
ATOM   722  C C    . ALA   A 1 27  ? 20.015 0.948   15.997  1.00 17.15 ?  27  ALA   A C    1 
ATOM   723  O O    . ALA   A 1 27  ? 20.698 0.491   16.921  1.00 17.38 ?  27  ALA   A O    1 
ATOM   724  C CB   . ALA   A 1 27  ? 20.709 0.702   13.596  1.00 14.96 ?  27  ALA   A CB   1 
ATOM   725  H H    A ALA   A 1 27  ? 18.283 0.531   13.523  0.88 19.18 ?  27  ALA   A H    1 
ATOM   726  H H    B ALA   A 1 27  ? 18.250 0.696   13.633  0.12 19.18 ?  27  ALA   A H    1 
ATOM   727  H HA   . ALA   A 1 27  ? 20.085 -0.760  14.883  1.00 18.83 ?  27  ALA   A HA   1 
ATOM   728  H HB1  . ALA   A 1 27  ? 21.636 0.686   13.893  1.00 17.95 ?  27  ALA   A HB1  1 
ATOM   729  H HB2  . ALA   A 1 27  ? 20.609 0.147   12.807  1.00 17.95 ?  27  ALA   A HB2  1 
ATOM   730  H HB3  . ALA   A 1 27  ? 20.447 1.614   13.395  1.00 17.95 ?  27  ALA   A HB3  1 
ATOM   731  N N    . LYS   A 1 28  ? 19.414 2.136   16.084  1.00 19.18 ?  28  LYS   A N    1 
ATOM   732  C CA   . LYS   A 1 28  ? 19.564 2.947   17.289  1.00 22.50 ?  28  LYS   A CA   1 
ATOM   733  C C    . LYS   A 1 28  ? 19.031 2.231   18.522  1.00 23.60 ?  28  LYS   A C    1 
ATOM   734  O O    . LYS   A 1 28  ? 19.579 2.395   19.618  1.00 25.07 ?  28  LYS   A O    1 
ATOM   735  C CB   . LYS   A 1 28  ? 18.886 4.307   17.107  1.00 24.93 ?  28  LYS   A CB   1 
ATOM   736  C CG   . LYS   A 1 28  ? 19.672 5.254   16.213  1.00 27.26 ?  28  LYS   A CG   1 
ATOM   737  C CD   . LYS   A 1 28  ? 19.172 6.683   16.311  1.00 29.88 ?  28  LYS   A CD   1 
ATOM   738  C CE   . LYS   A 1 28  ? 17.851 6.858   15.592  1.00 31.78 ?  28  LYS   A CE   1 
ATOM   739  N NZ   . LYS   A 1 28  ? 17.432 8.285   15.560  1.00 32.97 ?  28  LYS   A NZ   1 
ATOM   740  H H    . LYS   A 1 28  ? 18.930 2.488   15.471  1.00 23.00 ?  28  LYS   A H    1 
ATOM   741  H HA   . LYS   A 1 28  ? 20.505 3.111   17.442  1.00 26.99 ?  28  LYS   A HA   1 
ATOM   742  H HB2  . LYS   A 1 28  ? 18.014 4.177   16.704  1.00 29.91 ?  28  LYS   A HB2  1 
ATOM   743  H HB3  . LYS   A 1 28  ? 18.789 4.733   17.974  1.00 29.91 ?  28  LYS   A HB3  1 
ATOM   744  H HG2  . LYS   A 1 28  ? 20.605 5.243   16.479  1.00 32.70 ?  28  LYS   A HG2  1 
ATOM   745  H HG3  . LYS   A 1 28  ? 19.584 4.967   15.291  1.00 32.70 ?  28  LYS   A HG3  1 
ATOM   746  H HD2  . LYS   A 1 28  ? 19.043 6.915   17.245  1.00 35.85 ?  28  LYS   A HD2  1 
ATOM   747  H HD3  . LYS   A 1 28  ? 19.821 7.279   15.905  1.00 35.85 ?  28  LYS   A HD3  1 
ATOM   748  H HE2  . LYS   A 1 28  ? 17.943 6.547   14.678  1.00 38.13 ?  28  LYS   A HE2  1 
ATOM   749  H HE3  . LYS   A 1 28  ? 17.166 6.350   16.053  1.00 38.13 ?  28  LYS   A HE3  1 
ATOM   750  H HZ1  . LYS   A 1 28  ? 16.656 8.365   15.133  1.00 39.55 ?  28  LYS   A HZ1  1 
ATOM   751  H HZ2  . LYS   A 1 28  ? 17.340 8.594   16.390  1.00 39.55 ?  28  LYS   A HZ2  1 
ATOM   752  H HZ3  . LYS   A 1 28  ? 18.046 8.773   15.138  1.00 39.55 ?  28  LYS   A HZ3  1 
ATOM   753  N N    . LYS   A 1 29  ? 17.981 1.423   18.365  1.00 23.86 ?  29  LYS   A N    1 
ATOM   754  C CA   . LYS   A 1 29  ? 17.392 0.720   19.501  1.00 25.77 ?  29  LYS   A CA   1 
ATOM   755  C C    . LYS   A 1 29  ? 18.214 -0.505  19.892  1.00 24.40 ?  29  LYS   A C    1 
ATOM   756  O O    . LYS   A 1 29  ? 18.502 -0.719  21.076  1.00 25.38 ?  29  LYS   A O    1 
ATOM   757  C CB   . LYS   A 1 29  ? 15.961 0.299   19.158  1.00 28.87 ?  29  LYS   A CB   1 
ATOM   758  C CG   . LYS   A 1 29  ? 15.206 -0.346  20.309  1.00 32.16 ?  29  LYS   A CG   1 
ATOM   759  C CD   . LYS   A 1 29  ? 14.834 0.681   21.366  1.00 35.22 ?  29  LYS   A CD   1 
ATOM   760  C CE   . LYS   A 1 29  ? 13.969 0.070   22.456  1.00 37.42 ?  29  LYS   A CE   1 
ATOM   761  N NZ   . LYS   A 1 29  ? 13.533 1.089   23.450  1.00 38.67 ?  29  LYS   A NZ   1 
ATOM   762  H H    . LYS   A 1 29  ? 17.594 1.265   17.612  1.00 28.62 ?  29  LYS   A H    1 
ATOM   763  H HA   . LYS   A 1 29  ? 17.358 1.316   20.263  1.00 30.92 ?  29  LYS   A HA   1 
ATOM   764  H HB2  . LYS   A 1 29  ? 15.462 1.084   18.884  1.00 34.64 ?  29  LYS   A HB2  1 
ATOM   765  H HB3  . LYS   A 1 29  ? 15.989 -0.342  18.430  1.00 34.64 ?  29  LYS   A HB3  1 
ATOM   766  H HG2  . LYS   A 1 29  ? 14.388 -0.744  19.972  1.00 38.59 ?  29  LYS   A HG2  1 
ATOM   767  H HG3  . LYS   A 1 29  ? 15.759 -1.026  20.727  1.00 38.59 ?  29  LYS   A HG3  1 
ATOM   768  H HD2  . LYS   A 1 29  ? 15.642 1.027   21.776  1.00 42.26 ?  29  LYS   A HD2  1 
ATOM   769  H HD3  . LYS   A 1 29  ? 14.335 1.402   20.949  1.00 42.26 ?  29  LYS   A HD3  1 
ATOM   770  H HE2  . LYS   A 1 29  ? 13.177 -0.321  22.054  1.00 44.90 ?  29  LYS   A HE2  1 
ATOM   771  H HE3  . LYS   A 1 29  ? 14.478 -0.611  22.923  1.00 44.90 ?  29  LYS   A HE3  1 
ATOM   772  H HZ1  . LYS   A 1 29  ? 13.029 0.706   24.076  1.00 46.39 ?  29  LYS   A HZ1  1 
ATOM   773  H HZ2  . LYS   A 1 29  ? 14.242 1.460   23.837  1.00 46.39 ?  29  LYS   A HZ2  1 
ATOM   774  H HZ3  . LYS   A 1 29  ? 13.058 1.724   23.046  1.00 46.39 ?  29  LYS   A HZ3  1 
ATOM   775  N N    . VAL   A 1 30  ? 18.574 -1.331  18.910  1.00 22.96 ?  30  VAL   A N    1 
ATOM   776  C CA   . VAL   A 1 30  ? 19.218 -2.609  19.195  1.00 22.08 ?  30  VAL   A CA   1 
ATOM   777  C C    . VAL   A 1 30  ? 20.722 -2.454  19.410  1.00 20.76 ?  30  VAL   A C    1 
ATOM   778  O O    . VAL   A 1 30  ? 21.316 -3.183  20.212  1.00 21.14 ?  30  VAL   A O    1 
ATOM   779  C CB   . VAL   A 1 30  ? 18.902 -3.590  18.052  1.00 22.86 ?  30  VAL   A CB   1 
ATOM   780  C CG1  . VAL   A 1 30  ? 19.667 -4.893  18.227  1.00 23.28 ?  30  VAL   A CG1  1 
ATOM   781  C CG2  . VAL   A 1 30  ? 17.403 -3.851  17.977  1.00 23.66 ?  30  VAL   A CG2  1 
ATOM   782  H H    . VAL   A 1 30  ? 18.445 -1.183  18.072  1.00 27.54 ?  30  VAL   A H    1 
ATOM   783  H HA   . VAL   A 1 30  ? 18.832 -2.975  20.007  1.00 26.48 ?  30  VAL   A HA   1 
ATOM   784  H HB   . VAL   A 1 30  ? 19.177 -3.194  17.210  1.00 27.42 ?  30  VAL   A HB   1 
ATOM   785  H HG11 . VAL   A 1 30  ? 19.283 -5.564  17.639  1.00 27.92 ?  30  VAL   A HG11 1 
ATOM   786  H HG12 . VAL   A 1 30  ? 20.597 -4.750  18.001  1.00 27.92 ?  30  VAL   A HG12 1 
ATOM   787  H HG13 . VAL   A 1 30  ? 19.587 -5.183  19.150  1.00 27.92 ?  30  VAL   A HG13 1 
ATOM   788  H HG21 . VAL   A 1 30  ? 17.231 -4.510  17.286  1.00 28.38 ?  30  VAL   A HG21 1 
ATOM   789  H HG22 . VAL   A 1 30  ? 17.098 -4.184  18.836  1.00 28.38 ?  30  VAL   A HG22 1 
ATOM   790  H HG23 . VAL   A 1 30  ? 16.948 -3.022  17.763  1.00 28.38 ?  30  VAL   A HG23 1 
ATOM   791  N N    . LYS   A 1 31  ? 21.357 -1.511  18.724  1.00 19.61 ?  31  LYS   A N    1 
ATOM   792  C CA   . LYS   A 1 31  ? 22.811 -1.406  18.676  1.00 19.91 ?  31  LYS   A CA   1 
ATOM   793  C C    . LYS   A 1 31  ? 23.418 -2.760  18.298  1.00 17.78 ?  31  LYS   A C    1 
ATOM   794  O O    . LYS   A 1 31  ? 24.205 -3.331  19.060  1.00 18.70 ?  31  LYS   A O    1 
ATOM   795  C CB   . LYS   A 1 31  ? 23.392 -0.891  19.984  1.00 24.71 ?  31  LYS   A CB   1 
ATOM   796  C CG   . LYS   A 1 31  ? 22.712 0.365   20.507  1.00 30.39 ?  31  LYS   A CG   1 
ATOM   797  C CD   . LYS   A 1 31  ? 23.719 1.452   20.849  1.00 34.83 ?  31  LYS   A CD   1 
ATOM   798  C CE   . LYS   A 1 31  ? 23.101 2.532   21.726  1.00 37.69 ?  31  LYS   A CE   1 
ATOM   799  N NZ   . LYS   A 1 31  ? 21.902 3.159   21.105  1.00 39.08 ?  31  LYS   A NZ   1 
ATOM   800  H H    . LYS   A 1 31  ? 20.956 -0.903  18.276  1.00 23.52 ?  31  LYS   A H    1 
ATOM   801  H HA   . LYS   A 1 31  ? 23.048 -0.775  17.990  1.00 23.89 ?  31  LYS   A HA   1 
ATOM   802  H HB2  . LYS   A 1 31  ? 23.296 -1.585  20.647  1.00 29.65 ?  31  LYS   A HB2  1 
ATOM   803  H HB3  . LYS   A 1 31  ? 24.335 -0.690  19.852  1.00 29.65 ?  31  LYS   A HB3  1 
ATOM   804  H HG2  . LYS   A 1 31  ? 22.113 0.711   19.827  1.00 36.46 ?  31  LYS   A HG2  1 
ATOM   805  H HG3  . LYS   A 1 31  ? 22.215 0.148   21.312  1.00 36.46 ?  31  LYS   A HG3  1 
ATOM   806  H HD2  . LYS   A 1 31  ? 24.463 1.059   21.330  1.00 41.79 ?  31  LYS   A HD2  1 
ATOM   807  H HD3  . LYS   A 1 31  ? 24.031 1.868   20.029  1.00 41.79 ?  31  LYS   A HD3  1 
ATOM   808  H HE2  . LYS   A 1 31  ? 22.831 2.137   22.570  1.00 45.22 ?  31  LYS   A HE2  1 
ATOM   809  H HE3  . LYS   A 1 31  ? 23.758 3.229   21.880  1.00 45.22 ?  31  LYS   A HE3  1 
ATOM   810  H HZ1  . LYS   A 1 31  ? 21.578 3.792   21.641  1.00 46.89 ?  31  LYS   A HZ1  1 
ATOM   811  H HZ2  . LYS   A 1 31  ? 22.121 3.526   20.324  1.00 46.89 ?  31  LYS   A HZ2  1 
ATOM   812  H HZ3  . LYS   A 1 31  ? 21.273 2.544   20.970  1.00 46.89 ?  31  LYS   A HZ3  1 
ATOM   813  N N    . PRO   A 1 32  ? 23.058 -3.298  17.139  1.00 15.72 ?  32  PRO   A N    1 
ATOM   814  C CA   . PRO   A 1 32  ? 23.535 -4.629  16.765  1.00 15.90 ?  32  PRO   A CA   1 
ATOM   815  C C    . PRO   A 1 32  ? 25.035 -4.638  16.554  1.00 15.87 ?  32  PRO   A C    1 
ATOM   816  O O    . PRO   A 1 32  ? 25.669 -3.605  16.333  1.00 15.82 ?  32  PRO   A O    1 
ATOM   817  C CB   . PRO   A 1 32  ? 22.797 -4.904  15.450  1.00 16.20 ?  32  PRO   A CB   1 
ATOM   818  C CG   . PRO   A 1 32  ? 22.589 -3.533  14.868  1.00 15.20 ?  32  PRO   A CG   1 
ATOM   819  C CD   . PRO   A 1 32  ? 22.292 -2.665  16.053  1.00 15.13 ?  32  PRO   A CD   1 
ATOM   820  H HA   . PRO   A 1 32  ? 23.295 -5.290  17.427  1.00 19.07 ?  32  PRO   A HA   1 
ATOM   821  H HB2  . PRO   A 1 32  ? 23.347 -5.451  14.863  1.00 19.44 ?  32  PRO   A HB2  1 
ATOM   822  H HB3  . PRO   A 1 32  ? 21.949 -5.340  15.631  1.00 19.44 ?  32  PRO   A HB3  1 
ATOM   823  H HG2  . PRO   A 1 32  ? 23.392 -3.249  14.412  1.00 18.23 ?  32  PRO   A HG2  1 
ATOM   824  H HG3  . PRO   A 1 32  ? 21.833 -3.557  14.254  1.00 18.23 ?  32  PRO   A HG3  1 
ATOM   825  H HD2  . PRO   A 1 32  ? 22.608 -1.764  15.888  1.00 18.15 ?  32  PRO   A HD2  1 
ATOM   826  H HD3  . PRO   A 1 32  ? 21.345 -2.683  16.255  1.00 18.15 ?  32  PRO   A HD3  1 
ATOM   827  N N    . THR   A 1 33  ? 25.601 -5.841  16.602  1.00 15.78 ?  33  THR   A N    1 
ATOM   828  C CA   . THR   A 1 33  ? 27.008 -5.998  16.266  1.00 16.05 ?  33  THR   A CA   1 
ATOM   829  C C    . THR   A 1 33  ? 27.284 -5.530  14.844  1.00 14.61 ?  33  THR   A C    1 
ATOM   830  O O    . THR   A 1 33  ? 28.312 -4.886  14.586  1.00 14.65 ?  33  THR   A O    1 
ATOM   831  C CB   . THR   A 1 33  ? 27.416 -7.457  16.460  1.00 17.60 ?  33  THR   A CB   1 
ATOM   832  O OG1  . THR   A 1 33  ? 27.106 -7.853  17.799  1.00 19.41 ?  33  THR   A OG1  1 
ATOM   833  C CG2  . THR   A 1 33  ? 28.907 -7.647  16.217  1.00 18.54 ?  33  THR   A CG2  1 
ATOM   834  H H    . THR   A 1 33  ? 25.202 -6.570  16.812  1.00 18.92 ?  33  THR   A H    1 
ATOM   835  H HA   . THR   A 1 33  ? 27.546 -5.459  16.864  1.00 19.25 ?  33  THR   A HA   1 
ATOM   836  H HB   . THR   A 1 33  ? 26.933 -8.025  15.837  1.00 21.12 ?  33  THR   A HB   1 
ATOM   837  H HG1  . THR   A 1 33  ? 27.524 -7.372  18.350  1.00 23.29 ?  33  THR   A HG1  1 
ATOM   838  H HG21 . THR   A 1 33  ? 29.175 -8.545  16.481  1.00 22.24 ?  33  THR   A HG21 1 
ATOM   839  H HG22 . THR   A 1 33  ? 29.112 -7.523  15.279  1.00 22.24 ?  33  THR   A HG22 1 
ATOM   840  H HG23 . THR   A 1 33  ? 29.412 -7.006  16.742  1.00 22.24 ?  33  THR   A HG23 1 
ATOM   841  N N    . VAL   A 1 34  ? 26.378 -5.834  13.912  1.00 13.17 ?  34  VAL   A N    1 
ATOM   842  C CA   . VAL   A 1 34  ? 26.556 -5.496  12.504  1.00 11.95 ?  34  VAL   A CA   1 
ATOM   843  C C    . VAL   A 1 34  ? 25.251 -4.936  11.950  1.00 11.26 ?  34  VAL   A C    1 
ATOM   844  O O    . VAL   A 1 34  ? 24.211 -5.606  12.007  1.00 12.13 ?  34  VAL   A O    1 
ATOM   845  C CB   . VAL   A 1 34  ? 27.005 -6.701  11.655  1.00 12.58 ?  34  VAL   A CB   1 
ATOM   846  C CG1  . VAL   A 1 34  ? 27.184 -6.287  10.200  1.00 12.74 ?  34  VAL   A CG1  1 
ATOM   847  C CG2  . VAL   A 1 34  ? 28.295 -7.318  12.205  1.00 13.77 ?  34  VAL   A CG2  1 
ATOM   848  H H    . VAL   A 1 34  ? 25.642 -6.251  14.074  1.00 15.80 ?  34  VAL   A H    1 
ATOM   849  H HA   . VAL   A 1 34  ? 27.234 -4.803  12.425  1.00 14.33 ?  34  VAL   A HA   1 
ATOM   850  H HB   . VAL   A 1 34  ? 26.314 -7.377  11.686  1.00 15.09 ?  34  VAL   A HB   1 
ATOM   851  H HG11 . VAL   A 1 34  ? 27.671 -6.984  9.732   1.00 15.28 ?  34  VAL   A HG11 1 
ATOM   852  H HG12 . VAL   A 1 34  ? 26.317 -6.157  9.792   1.00 15.28 ?  34  VAL   A HG12 1 
ATOM   853  H HG13 . VAL   A 1 34  ? 27.694 -5.457  10.167  1.00 15.28 ?  34  VAL   A HG13 1 
ATOM   854  H HG21 . VAL   A 1 34  ? 28.567 -8.050  11.629  1.00 16.52 ?  34  VAL   A HG21 1 
ATOM   855  H HG22 . VAL   A 1 34  ? 28.990 -6.639  12.224  1.00 16.52 ?  34  VAL   A HG22 1 
ATOM   856  H HG23 . VAL   A 1 34  ? 28.133 -7.647  13.103  1.00 16.52 ?  34  VAL   A HG23 1 
ATOM   857  N N    . VAL   A 1 35  ? 25.311 -3.723  11.394  1.00 10.59 ?  35  VAL   A N    1 
ATOM   858  C CA   . VAL   A 1 35  ? 24.269 -3.211  10.514  1.00 10.22 ?  35  VAL   A CA   1 
ATOM   859  C C    . VAL   A 1 35  ? 24.816 -3.211  9.096   1.00 9.86  ?  35  VAL   A C    1 
ATOM   860  O O    . VAL   A 1 35  ? 25.957 -2.799  8.860   1.00 10.46 ?  35  VAL   A O    1 
ATOM   861  C CB   . VAL   A 1 35  ? 23.738 -1.819  10.927  1.00 11.04 ?  35  VAL   A CB   1 
ATOM   862  C CG1  . VAL   A 1 35  ? 24.807 -0.719  10.795  1.00 11.62 ?  35  VAL   A CG1  1 
ATOM   863  C CG2  . VAL   A 1 35  ? 22.492 -1.463  10.107  1.00 11.85 ?  35  VAL   A CG2  1 
ATOM   864  H H    . VAL   A 1 35  ? 25.954 -3.166  11.515  1.00 12.70 ?  35  VAL   A H    1 
ATOM   865  H HA   . VAL   A 1 35  ? 23.512 -3.823  10.539  1.00 12.25 ?  35  VAL   A HA   1 
ATOM   866  H HB   . VAL   A 1 35  ? 23.463 -1.849  11.854  1.00 13.24 ?  35  VAL   A HB   1 
ATOM   867  H HG11 . VAL   A 1 35  ? 24.459 0.114   11.160  1.00 13.93 ?  35  VAL   A HG11 1 
ATOM   868  H HG12 . VAL   A 1 35  ? 25.598 -0.986  11.289  1.00 13.93 ?  35  VAL   A HG12 1 
ATOM   869  H HG13 . VAL   A 1 35  ? 25.031 -0.595  9.858   1.00 13.93 ?  35  VAL   A HG13 1 
ATOM   870  H HG21 . VAL   A 1 35  ? 22.137 -0.614  10.412  1.00 14.21 ?  35  VAL   A HG21 1 
ATOM   871  H HG22 . VAL   A 1 35  ? 22.740 -1.391  9.165   1.00 14.21 ?  35  VAL   A HG22 1 
ATOM   872  H HG23 . VAL   A 1 35  ? 21.827 -2.159  10.215  1.00 14.21 ?  35  VAL   A HG23 1 
ATOM   873  N N    . VAL   A 1 36  ? 23.998 -3.668  8.152   1.00 9.41  ?  36  VAL   A N    1 
ATOM   874  C CA   . VAL   A 1 36  ? 24.365 -3.667  6.743   1.00 9.27  ?  36  VAL   A CA   1 
ATOM   875  C C    . VAL   A 1 36  ? 23.902 -2.373  6.090   1.00 9.28  ?  36  VAL   A C    1 
ATOM   876  O O    . VAL   A 1 36  ? 22.745 -1.959  6.246   1.00 10.16 ?  36  VAL   A O    1 
ATOM   877  C CB   . VAL   A 1 36  ? 23.756 -4.880  6.022   1.00 9.35  ?  36  VAL   A CB   1 
ATOM   878  C CG1  . VAL   A 1 36  ? 24.003 -4.802  4.535   1.00 9.89  ?  36  VAL   A CG1  1 
ATOM   879  C CG2  . VAL   A 1 36  ? 24.303 -6.177  6.596   1.00 10.12 ?  36  VAL   A CG2  1 
ATOM   880  H H    . VAL   A 1 36  ? 23.213 -3.998  8.305   1.00 11.29 ?  36  VAL   A H    1 
ATOM   881  H HA   . VAL   A 1 36  ? 25.337 -3.728  6.668   1.00 11.12 ?  36  VAL   A HA   1 
ATOM   882  H HB   . VAL   A 1 36  ? 22.802 -4.874  6.159   1.00 11.21 ?  36  VAL   A HB   1 
ATOM   883  H HG11 . VAL   A 1 36  ? 23.856 -5.676  4.143   1.00 11.86 ?  36  VAL   A HG11 1 
ATOM   884  H HG12 . VAL   A 1 36  ? 23.388 -4.159  4.143   1.00 11.86 ?  36  VAL   A HG12 1 
ATOM   885  H HG13 . VAL   A 1 36  ? 24.919 -4.520  4.378   1.00 11.86 ?  36  VAL   A HG13 1 
ATOM   886  H HG21 . VAL   A 1 36  ? 23.917 -6.928  6.113   1.00 12.14 ?  36  VAL   A HG21 1 
ATOM   887  H HG22 . VAL   A 1 36  ? 25.270 -6.190  6.497   1.00 12.14 ?  36  VAL   A HG22 1 
ATOM   888  H HG23 . VAL   A 1 36  ? 24.068 -6.237  7.535   1.00 12.14 ?  36  VAL   A HG23 1 
ATOM   889  N N    . ASN   A 1 37  ? 24.807 -1.752  5.335   1.00 8.81  ?  37  ASN   A N    1 
ATOM   890  C CA   . ASN   A 1 37  ? 24.471 -0.626  4.479   1.00 8.67  ?  37  ASN   A CA   1 
ATOM   891  C C    . ASN   A 1 37  ? 24.326 -1.088  3.039   1.00 8.74  ?  37  ASN   A C    1 
ATOM   892  O O    . ASN   A 1 37  ? 25.106 -1.915  2.553   1.00 9.12  ?  37  ASN   A O    1 
ATOM   893  C CB   . ASN   A 1 37  ? 25.554 0.448   4.555   1.00 9.24  ?  37  ASN   A CB   1 
ATOM   894  C CG   . ASN   A 1 37  ? 25.221 1.662   3.718   1.00 9.43  ?  37  ASN   A CG   1 
ATOM   895  O OD1  . ASN   A 1 37  ? 24.045 2.005   3.552   1.00 10.03 ?  37  ASN   A OD1  1 
ATOM   896  N ND2  . ASN   A 1 37  ? 26.248 2.319   3.192   1.00 9.67  ?  37  ASN   A ND2  1 
ATOM   897  H H    . ASN   A 1 37  ? 25.645 -1.966  5.313   1.00 10.57 ?  37  ASN   A H    1 
ATOM   898  H HA   . ASN   A 1 37  ? 23.637 -0.236  4.773   1.00 10.39 ?  37  ASN   A HA   1 
ATOM   899  H HB2  . ASN   A 1 37  ? 25.654 0.739   5.477   1.00 11.08 ?  37  ASN   A HB2  1 
ATOM   900  H HB3  . ASN   A 1 37  ? 26.396 0.079   4.235   1.00 11.08 ?  37  ASN   A HB3  1 
ATOM   901  H HD21 . ASN   A 1 37  ? 26.108 3.012   2.701   1.00 11.59 ?  37  ASN   A HD21 1 
ATOM   902  H HD22 . ASN   A 1 37  ? 27.049 2.053   3.327   1.00 11.59 ?  37  ASN   A HD22 1 
ATOM   903  N N    A ALA   A 1 38  ? 23.323 -0.524  2.363   0.88 9.26  ?  38  ALA   A N    1 
ATOM   904  N N    B ALA   A 1 38  ? 23.302 -0.571  2.363   0.12 9.05  ?  38  ALA   A N    1 
ATOM   905  C CA   A ALA   A 1 38  ? 23.116 -0.668  0.924   0.88 9.63  ?  38  ALA   A CA   1 
ATOM   906  C CA   B ALA   A 1 38  ? 23.082 -0.870  0.949   0.12 9.48  ?  38  ALA   A CA   1 
ATOM   907  C C    A ALA   A 1 38  ? 24.035 0.320   0.207   0.88 9.31  ?  38  ALA   A C    1 
ATOM   908  C C    B ALA   A 1 38  ? 23.844 0.171   0.134   0.12 9.60  ?  38  ALA   A C    1 
ATOM   909  O O    A ALA   A 1 38  ? 23.629 1.411   -0.206  0.88 9.46  ?  38  ALA   A O    1 
ATOM   910  O O    B ALA   A 1 38  ? 23.284 1.132   -0.398  0.12 9.71  ?  38  ALA   A O    1 
ATOM   911  C CB   A ALA   A 1 38  ? 21.652 -0.413  0.584   0.88 11.06 ?  38  ALA   A CB   1 
ATOM   912  C CB   B ALA   A 1 38  ? 21.592 -0.871  0.634   0.12 9.75  ?  38  ALA   A CB   1 
ATOM   913  H H    A ALA   A 1 38  ? 22.733 -0.026  2.741   0.88 11.10 ?  38  ALA   A H    1 
ATOM   914  H H    B ALA   A 1 38  ? 22.716 -0.040  2.706   0.12 10.85 ?  38  ALA   A H    1 
ATOM   915  H HA   A ALA   A 1 38  ? 23.347 -1.568  0.649   0.88 11.55 ?  38  ALA   A HA   1 
ATOM   916  H HA   B ALA   A 1 38  ? 23.439 -1.752  0.747   0.12 11.36 ?  38  ALA   A HA   1 
ATOM   917  H HB1  A ALA   A 1 38  ? 21.524 -0.518  -0.369  0.88 13.26 ?  38  ALA   A HB1  1 
ATOM   918  H HB1  B ALA   A 1 38  ? 21.479 -0.931  -0.325  0.12 11.69 ?  38  ALA   A HB1  1 
ATOM   919  H HB2  A ALA   A 1 38  ? 21.098 -1.056  1.064   0.88 13.26 ?  38  ALA   A HB2  1 
ATOM   920  H HB2  B ALA   A 1 38  ? 21.172 -1.631  1.068   0.12 11.69 ?  38  ALA   A HB2  1 
ATOM   921  H HB3  A ALA   A 1 38  ? 21.414 0.487   0.856   0.88 13.26 ?  38  ALA   A HB3  1 
ATOM   922  H HB3  B ALA   A 1 38  ? 21.204 -0.044  0.957   0.12 11.69 ?  38  ALA   A HB3  1 
ATOM   923  N N    A ALA   A 1 39  ? 25.300 -0.072  0.069   0.88 9.57  ?  39  ALA   A N    1 
ATOM   924  N N    B ALA   A 1 39  ? 25.153 -0.029  0.041   0.12 9.65  ?  39  ALA   A N    1 
ATOM   925  C CA   A ALA   A 1 39  ? 26.348 0.807   -0.413  0.88 9.23  ?  39  ALA   A CA   1 
ATOM   926  C CA   B ALA   A 1 39  ? 26.033 0.992   -0.503  0.12 9.53  ?  39  ALA   A CA   1 
ATOM   927  C C    A ALA   A 1 39  ? 26.468 0.760   -1.932  0.88 9.41  ?  39  ALA   A C    1 
ATOM   928  C C    B ALA   A 1 39  ? 26.285 0.777   -1.994  0.12 9.24  ?  39  ALA   A C    1 
ATOM   929  O O    A ALA   A 1 39  ? 25.976 -0.152  -2.599  0.88 10.02 ?  39  ALA   A O    1 
ATOM   930  O O    B ALA   A 1 39  ? 25.975 -0.271  -2.565  0.12 9.30  ?  39  ALA   A O    1 
ATOM   931  C CB   A ALA   A 1 39  ? 27.672 0.404   0.230   0.88 9.77  ?  39  ALA   A CB   1 
ATOM   932  C CB   B ALA   A 1 39  ? 27.359 1.001   0.253   0.12 9.67  ?  39  ALA   A CB   1 
ATOM   933  H H    A ALA   A 1 39  ? 25.571 -0.871  0.256   0.88 11.47 ?  39  ALA   A H    1 
ATOM   934  H H    B ALA   A 1 39  ? 25.552 -0.754  0.287   0.12 11.57 ?  39  ALA   A H    1 
ATOM   935  H HA   A ALA   A 1 39  ? 26.135 1.719   -0.151  0.88 11.07 ?  39  ALA   A HA   1 
ATOM   936  H HA   B ALA   A 1 39  ? 25.609 1.854   -0.378  0.12 11.43 ?  39  ALA   A HA   1 
ATOM   937  H HB1  A ALA   A 1 39  ? 28.363 0.999   -0.092  0.88 11.71 ?  39  ALA   A HB1  1 
ATOM   938  H HB1  B ALA   A 1 39  ? 27.905 1.725   -0.089  0.12 11.60 ?  39  ALA   A HB1  1 
ATOM   939  H HB2  A ALA   A 1 39  ? 27.585 0.487   1.195   0.88 11.71 ?  39  ALA   A HB2  1 
ATOM   940  H HB2  B ALA   A 1 39  ? 27.183 1.134   1.196   0.12 11.60 ?  39  ALA   A HB2  1 
ATOM   941  H HB3  A ALA   A 1 39  ? 27.869 -0.509  -0.010  0.88 11.71 ?  39  ALA   A HB3  1 
ATOM   942  H HB3  B ALA   A 1 39  ? 27.804 0.152   0.116   0.12 11.60 ?  39  ALA   A HB3  1 
ATOM   943  N N    A ASN   A 1 40  ? 27.155 1.764   -2.475  0.88 9.64  ?  40  ASN   A N    1 
ATOM   944  N N    B ASN   A 1 40  ? 26.856 1.801   -2.626  0.12 9.14  ?  40  ASN   A N    1 
ATOM   945  C CA   A ASN   A 1 40  ? 27.676 1.721   -3.834  0.88 10.04 ?  40  ASN   A CA   1 
ATOM   946  C CA   B ASN   A 1 40  ? 27.355 1.712   -3.988  0.12 9.24  ?  40  ASN   A CA   1 
ATOM   947  C C    A ASN   A 1 40  ? 29.202 1.613   -3.784  0.88 9.27  ?  40  ASN   A C    1 
ATOM   948  C C    B ASN   A 1 40  ? 28.871 1.542   -3.966  0.12 9.04  ?  40  ASN   A C    1 
ATOM   949  O O    A ASN   A 1 40  ? 29.816 1.725   -2.720  0.88 9.48  ?  40  ASN   A O    1 
ATOM   950  O O    B ASN   A 1 40  ? 29.515 1.569   -2.915  0.12 8.91  ?  40  ASN   A O    1 
ATOM   951  C CB   A ASN   A 1 40  ? 27.179 2.909   -4.680  0.88 10.89 ?  40  ASN   A CB   1 
ATOM   952  C CB   B ASN   A 1 40  ? 26.962 2.943   -4.808  0.12 9.51  ?  40  ASN   A CB   1 
ATOM   953  C CG   A ASN   A 1 40  ? 27.566 4.255   -4.106  0.88 11.79 ?  40  ASN   A CG   1 
ATOM   954  C CG   B ASN   A 1 40  ? 27.257 4.241   -4.088  0.12 9.71  ?  40  ASN   A CG   1 
ATOM   955  O OD1  A ASN   A 1 40  ? 28.746 4.509   -3.817  0.88 12.82 ?  40  ASN   A OD1  1 
ATOM   956  O OD1  B ASN   A 1 40  ? 28.414 4.633   -3.937  0.12 10.31 ?  40  ASN   A OD1  1 
ATOM   957  N ND2  A ASN   A 1 40  ? 26.573 5.137   -3.957  0.88 12.41 ?  40  ASN   A ND2  1 
ATOM   958  N ND2  B ASN   A 1 40  ? 26.207 4.919   -3.644  0.12 9.68  ?  40  ASN   A ND2  1 
ATOM   959  H H    A ASN   A 1 40  ? 27.335 2.494   -2.066  0.88 11.55 ?  40  ASN   A H    1 
ATOM   960  H H    B ASN   A 1 40  ? 26.967 2.574   -2.266  0.12 10.96 ?  40  ASN   A H    1 
ATOM   961  H HA   A ASN   A 1 40  ? 27.346 0.912   -4.262  0.88 12.04 ?  40  ASN   A HA   1 
ATOM   962  H HA   B ASN   A 1 40  ? 26.977 0.927   -4.420  0.12 11.08 ?  40  ASN   A HA   1 
ATOM   963  H HB2  A ASN   A 1 40  ? 27.551 2.835   -5.576  0.88 13.06 ?  40  ASN   A HB2  1 
ATOM   964  H HB2  B ASN   A 1 40  ? 27.467 2.942   -5.638  0.12 11.40 ?  40  ASN   A HB2  1 
ATOM   965  H HB3  A ASN   A 1 40  ? 26.206 2.869   -4.733  0.88 13.06 ?  40  ASN   A HB3  1 
ATOM   966  H HB3  B ASN   A 1 40  ? 26.015 2.905   -5.002  0.12 11.40 ?  40  ASN   A HB3  1 
ATOM   967  H HD21 A ASN   A 1 40  ? 26.738 5.921   -3.646  0.88 14.88 ?  40  ASN   A HD21 1 
ATOM   968  H HD21 B ASN   A 1 40  ? 26.323 5.658   -3.224  0.12 11.60 ?  40  ASN   A HD21 1 
ATOM   969  H HD22 A ASN   A 1 40  ? 25.765 4.923   -4.170  0.88 14.88 ?  40  ASN   A HD22 1 
ATOM   970  H HD22 B ASN   A 1 40  ? 25.413 4.615   -3.774  0.12 11.60 ?  40  ASN   A HD22 1 
ATOM   971  N N    A VAL   A 1 41  ? 29.817 1.373   -4.946  0.88 9.87  ?  41  VAL   A N    1 
ATOM   972  N N    B VAL   A 1 41  ? 29.449 1.372   -5.155  0.12 9.09  ?  41  VAL   A N    1 
ATOM   973  C CA   A VAL   A 1 41  ? 31.247 1.064   -4.973  0.88 10.51 ?  41  VAL   A CA   1 
ATOM   974  C CA   B VAL   A 1 41  ? 30.880 1.092   -5.238  0.12 9.17  ?  41  VAL   A CA   1 
ATOM   975  C C    A VAL   A 1 41  ? 32.109 2.216   -4.501  0.88 10.24 ?  41  VAL   A C    1 
ATOM   976  C C    B VAL   A 1 41  ? 31.715 2.250   -4.710  0.12 9.38  ?  41  VAL   A C    1 
ATOM   977  O O    A VAL   A 1 41  ? 33.258 1.995   -4.101  0.88 10.68 ?  41  VAL   A O    1 
ATOM   978  O O    B VAL   A 1 41  ? 32.824 2.041   -4.204  0.12 9.44  ?  41  VAL   A O    1 
ATOM   979  C CB   A VAL   A 1 41  ? 31.736 0.577   -6.355  0.88 11.21 ?  41  VAL   A CB   1 
ATOM   980  C CB   B VAL   A 1 41  ? 31.293 0.688   -6.667  0.12 9.28  ?  41  VAL   A CB   1 
ATOM   981  C CG1  A VAL   A 1 41  ? 31.046 -0.721  -6.734  0.88 11.80 ?  41  VAL   A CG1  1 
ATOM   982  C CG1  B VAL   A 1 41  ? 30.658 -0.639  -7.045  0.12 9.49  ?  41  VAL   A CG1  1 
ATOM   983  C CG2  A VAL   A 1 41  ? 31.571 1.640   -7.435  0.88 11.76 ?  41  VAL   A CG2  1 
ATOM   984  C CG2  B VAL   A 1 41  ? 30.940 1.782   -7.669  0.12 9.38  ?  41  VAL   A CG2  1 
ATOM   985  H H    A VAL   A 1 41  ? 29.435 1.372   -5.720  0.88 11.83 ?  41  VAL   A H    1 
ATOM   986  H H    B VAL   A 1 41  ? 29.029 1.400   -5.908  0.12 10.90 ?  41  VAL   A H    1 
ATOM   987  H HA   A VAL   A 1 41  ? 31.400 0.333   -4.351  0.88 12.60 ?  41  VAL   A HA   1 
ATOM   988  H HA   B VAL   A 1 41  ? 31.055 0.334   -4.666  0.12 11.00 ?  41  VAL   A HA   1 
ATOM   989  H HB   A VAL   A 1 41  ? 32.682 0.376   -6.286  0.88 13.44 ?  41  VAL   A HB   1 
ATOM   990  H HB   B VAL   A 1 41  ? 32.252 0.568   -6.684  0.12 11.12 ?  41  VAL   A HB   1 
ATOM   991  H HG11 A VAL   A 1 41  ? 31.386 -1.028  -7.587  0.88 14.15 ?  41  VAL   A HG11 1 
ATOM   992  H HG11 B VAL   A 1 41  ? 30.882 -0.844  -7.963  0.12 11.38 ?  41  VAL   A HG11 1 
ATOM   993  H HG12 A VAL   A 1 41  ? 31.221 -1.390  -6.049  0.88 14.15 ?  41  VAL   A HG12 1 
ATOM   994  H HG12 B VAL   A 1 41  ? 31.005 -1.330  -6.457  0.12 11.38 ?  41  VAL   A HG12 1 
ATOM   995  H HG13 A VAL   A 1 41  ? 30.088 -0.565  -6.797  0.88 14.15 ?  41  VAL   A HG13 1 
ATOM   996  H HG13 B VAL   A 1 41  ? 29.698 -0.575  -6.943  0.12 11.38 ?  41  VAL   A HG13 1 
ATOM   997  H HG21 A VAL   A 1 41  ? 31.809 1.253   -8.293  0.88 14.10 ?  41  VAL   A HG21 1 
ATOM   998  H HG21 B VAL   A 1 41  ? 31.225 1.499   -8.552  0.12 11.25 ?  41  VAL   A HG21 1 
ATOM   999  H HG22 A VAL   A 1 41  ? 30.650 1.934   -7.447  0.88 14.10 ?  41  VAL   A HG22 1 
ATOM   1000 H HG22 B VAL   A 1 41  ? 29.982 1.928   -7.662  0.12 11.25 ?  41  VAL   A HG22 1 
ATOM   1001 H HG23 A VAL   A 1 41  ? 32.159 2.382   -7.233  0.88 14.10 ?  41  VAL   A HG23 1 
ATOM   1002 H HG23 B VAL   A 1 41  ? 31.401 2.597   -7.418  0.12 11.25 ?  41  VAL   A HG23 1 
ATOM   1003 N N    A TYR   A 1 42  ? 31.599 3.448   -4.569  0.88 10.46 ?  42  TYR   A N    1 
ATOM   1004 N N    B TYR   A 1 42  ? 31.215 3.479   -4.816  0.12 9.52  ?  42  TYR   A N    1 
ATOM   1005 C CA   A TYR   A 1 42  ? 32.337 4.633   -4.153  0.88 10.35 ?  42  TYR   A CA   1 
ATOM   1006 C CA   B TYR   A 1 42  ? 31.976 4.655   -4.412  0.12 9.86  ?  42  TYR   A CA   1 
ATOM   1007 C C    A TYR   A 1 42  ? 32.074 5.004   -2.703  0.88 10.15 ?  42  TYR   A C    1 
ATOM   1008 C C    B TYR   A 1 42  ? 31.754 5.040   -2.954  0.12 9.84  ?  42  TYR   A C    1 
ATOM   1009 O O    A TYR   A 1 42  ? 32.639 5.988   -2.210  0.88 10.86 ?  42  TYR   A O    1 
ATOM   1010 O O    B TYR   A 1 42  ? 32.340 6.025   -2.492  0.12 9.85  ?  42  TYR   A O    1 
ATOM   1011 C CB   A TYR   A 1 42  ? 31.990 5.822   -5.071  0.88 11.25 ?  42  TYR   A CB   1 
ATOM   1012 C CB   B TYR   A 1 42  ? 31.625 5.842   -5.312  0.12 10.33 ?  42  TYR   A CB   1 
ATOM   1013 C CG   A TYR   A 1 42  ? 32.178 5.511   -6.545  0.88 12.15 ?  42  TYR   A CG   1 
ATOM   1014 C CG   B TYR   A 1 42  ? 31.752 5.542   -6.786  0.12 10.84 ?  42  TYR   A CG   1 
ATOM   1015 C CD1  A TYR   A 1 42  ? 33.440 5.311   -7.081  0.88 12.74 ?  42  TYR   A CD1  1 
ATOM   1016 C CD1  B TYR   A 1 42  ? 32.999 5.396   -7.379  0.12 10.86 ?  42  TYR   A CD1  1 
ATOM   1017 C CD2  A TYR   A 1 42  ? 31.089 5.392   -7.395  0.88 13.23 ?  42  TYR   A CD2  1 
ATOM   1018 C CD2  B TYR   A 1 42  ? 30.626 5.407   -7.587  0.12 11.36 ?  42  TYR   A CD2  1 
ATOM   1019 C CE1  A TYR   A 1 42  ? 33.610 5.009   -8.426  0.88 13.00 ?  42  TYR   A CE1  1 
ATOM   1020 C CE1  B TYR   A 1 42  ? 33.121 5.121   -8.726  0.12 11.09 ?  42  TYR   A CE1  1 
ATOM   1021 C CE2  A TYR   A 1 42  ? 31.251 5.101   -8.739  0.88 14.11 ?  42  TYR   A CE2  1 
ATOM   1022 C CE2  B TYR   A 1 42  ? 30.738 5.133   -8.936  0.12 11.52 ?  42  TYR   A CE2  1 
ATOM   1023 C CZ   A TYR   A 1 42  ? 32.516 4.907   -9.248  0.88 13.82 ?  42  TYR   A CZ   1 
ATOM   1024 C CZ   B TYR   A 1 42  ? 31.988 4.991   -9.501  0.12 11.42 ?  42  TYR   A CZ   1 
ATOM   1025 O OH   A TYR   A 1 42  ? 32.683 4.607   -10.582 0.88 15.24 ?  42  TYR   A OH   1 
ATOM   1026 O OH   B TYR   A 1 42  ? 32.104 4.721   -10.844 0.12 11.74 ?  42  TYR   A OH   1 
ATOM   1027 H H    A TYR   A 1 42  ? 30.811 3.624   -4.870  0.88 12.54 ?  42  TYR   A H    1 
ATOM   1028 H H    B TYR   A 1 42  ? 30.429 3.658   -5.119  0.12 11.41 ?  42  TYR   A H    1 
ATOM   1029 H HA   A TYR   A 1 42  ? 33.286 4.465   -4.250  0.88 12.41 ?  42  TYR   A HA   1 
ATOM   1030 H HA   B TYR   A 1 42  ? 32.919 4.466   -4.533  0.12 11.82 ?  42  TYR   A HA   1 
ATOM   1031 H HB2  A TYR   A 1 42  ? 31.060 6.071   -4.938  0.88 13.49 ?  42  TYR   A HB2  1 
ATOM   1032 H HB2  B TYR   A 1 42  ? 30.708 6.105   -5.142  0.12 12.39 ?  42  TYR   A HB2  1 
ATOM   1033 H HB3  A TYR   A 1 42  ? 32.564 6.576   -4.854  0.88 13.49 ?  42  TYR   A HB3  1 
ATOM   1034 H HB3  B TYR   A 1 42  ? 32.224 6.578   -5.107  0.12 12.39 ?  42  TYR   A HB3  1 
ATOM   1035 H HD1  A TYR   A 1 42  ? 34.188 5.378   -6.532  0.88 15.28 ?  42  TYR   A HD1  1 
ATOM   1036 H HD1  B TYR   A 1 42  ? 33.765 5.482   -6.858  0.12 13.02 ?  42  TYR   A HD1  1 
ATOM   1037 H HD2  A TYR   A 1 42  ? 30.231 5.527   -7.059  0.88 15.87 ?  42  TYR   A HD2  1 
ATOM   1038 H HD2  B TYR   A 1 42  ? 29.782 5.502   -7.208  0.12 13.63 ?  42  TYR   A HD2  1 
ATOM   1039 H HE1  A TYR   A 1 42  ? 34.466 4.880   -8.774  0.88 15.58 ?  42  TYR   A HE1  1 
ATOM   1040 H HE1  B TYR   A 1 42  ? 33.963 5.025   -9.109  0.12 13.30 ?  42  TYR   A HE1  1 
ATOM   1041 H HE2  A TYR   A 1 42  ? 30.507 5.030   -9.298  0.88 16.93 ?  42  TYR   A HE2  1 
ATOM   1042 H HE2  B TYR   A 1 42  ? 29.975 5.046   -9.461  0.12 13.82 ?  42  TYR   A HE2  1 
ATOM   1043 H HH   A TYR   A 1 42  ? 33.501 4.510   -10.759 0.88 18.27 ?  42  TYR   A HH   1 
ATOM   1044 H HH   B TYR   A 1 42  ? 31.343 4.668   -11.193 0.12 14.07 ?  42  TYR   A HH   1 
ATOM   1045 N N    A LEU   A 1 43  ? 31.223 4.243   -2.017  0.88 9.85  ?  43  LEU   A N    1 
ATOM   1046 N N    B LEU   A 1 43  ? 30.928 4.291   -2.226  0.12 10.08 ?  43  LEU   A N    1 
ATOM   1047 C CA   A LEU   A 1 43  ? 30.774 4.576   -0.667  0.88 9.67  ?  43  LEU   A CA   1 
ATOM   1048 C CA   B LEU   A 1 43  ? 30.583 4.610   -0.840  0.12 10.38 ?  43  LEU   A CA   1 
ATOM   1049 C C    A LEU   A 1 43  ? 30.293 6.023   -0.573  0.88 9.82  ?  43  LEU   A C    1 
ATOM   1050 C C    B LEU   A 1 43  ? 30.100 6.052   -0.700  0.12 10.69 ?  43  LEU   A C    1 
ATOM   1051 O O    A LEU   A 1 43  ? 30.545 6.722   0.411   0.88 10.96 ?  43  LEU   A O    1 
ATOM   1052 O O    B LEU   A 1 43  ? 30.403 6.743   0.275   0.12 10.63 ?  43  LEU   A O    1 
ATOM   1053 C CB   A LEU   A 1 43  ? 31.823 4.260   0.398   0.88 10.04 ?  43  LEU   A CB   1 
ATOM   1054 C CB   B LEU   A 1 43  ? 31.730 4.303   0.127   0.12 10.32 ?  43  LEU   A CB   1 
ATOM   1055 C CG   A LEU   A 1 43  ? 32.316 2.815   0.470   0.88 10.44 ?  43  LEU   A CG   1 
ATOM   1056 C CG   B LEU   A 1 43  ? 32.165 2.838   0.233   0.12 10.15 ?  43  LEU   A CG   1 
ATOM   1057 C CD1  A LEU   A 1 43  ? 33.384 2.703   1.545   0.88 11.30 ?  43  LEU   A CD1  1 
ATOM   1058 C CD1  B LEU   A 1 43  ? 33.197 2.676   1.339   0.12 10.20 ?  43  LEU   A CD1  1 
ATOM   1059 C CD2  A LEU   A 1 43  ? 31.178 1.837   0.728   0.88 10.79 ?  43  LEU   A CD2  1 
ATOM   1060 C CD2  B LEU   A 1 43  ? 30.970 1.919   0.465   0.12 10.02 ?  43  LEU   A CD2  1 
ATOM   1061 H H    A LEU   A 1 43  ? 30.880 3.508   -2.319  0.88 11.81 ?  43  LEU   A H    1 
ATOM   1062 H H    B LEU   A 1 43  ? 30.544 3.583   -2.519  0.12 12.08 ?  43  LEU   A H    1 
ATOM   1063 H HA   A LEU   A 1 43  ? 30.006 4.016   -0.469  0.88 11.59 ?  43  LEU   A HA   1 
ATOM   1064 H HA   B LEU   A 1 43  ? 29.841 4.046   -0.588  0.12 12.45 ?  43  LEU   A HA   1 
ATOM   1065 H HB2  A LEU   A 1 43  ? 32.597 4.823   0.240   0.88 12.04 ?  43  LEU   A HB2  1 
ATOM   1066 H HB2  B LEU   A 1 43  ? 32.507 4.813   -0.148  0.12 12.37 ?  43  LEU   A HB2  1 
ATOM   1067 H HB3  A LEU   A 1 43  ? 31.443 4.473   1.265   0.88 12.04 ?  43  LEU   A HB3  1 
ATOM   1068 H HB3  B LEU   A 1 43  ? 31.459 4.585   1.016   0.12 12.37 ?  43  LEU   A HB3  1 
ATOM   1069 H HG   A LEU   A 1 43  ? 32.726 2.581   -0.380  0.88 12.52 ?  43  LEU   A HG   1 
ATOM   1070 H HG   B LEU   A 1 43  ? 32.583 2.576   -0.601  0.12 12.17 ?  43  LEU   A HG   1 
ATOM   1071 H HD11 A LEU   A 1 43  ? 33.696 1.784   1.586   0.88 13.55 ?  43  LEU   A HD11 1 
ATOM   1072 H HD11 B LEU   A 1 43  ? 33.463 1.744   1.390   0.12 12.23 ?  43  LEU   A HD11 1 
ATOM   1073 H HD12 A LEU   A 1 43  ? 34.122 3.292   1.323   0.88 13.55 ?  43  LEU   A HD12 1 
ATOM   1074 H HD12 B LEU   A 1 43  ? 33.967 3.230   1.136   0.12 12.23 ?  43  LEU   A HD12 1 
ATOM   1075 H HD13 A LEU   A 1 43  ? 33.000 2.959   2.399   0.88 13.55 ?  43  LEU   A HD13 1 
ATOM   1076 H HD13 B LEU   A 1 43  ? 32.803 2.953   2.182   0.12 12.23 ?  43  LEU   A HD13 1 
ATOM   1077 H HD21 A LEU   A 1 43  ? 31.550 0.950   0.859   0.88 12.94 ?  43  LEU   A HD21 1 
ATOM   1078 H HD21 B LEU   A 1 43  ? 31.293 1.037   0.707   0.12 12.02 ?  43  LEU   A HD21 1 
ATOM   1079 H HD22 A LEU   A 1 43  ? 30.700 2.116   1.523   0.88 12.94 ?  43  LEU   A HD22 1 
ATOM   1080 H HD22 B LEU   A 1 43  ? 30.428 2.281   1.183   0.12 12.02 ?  43  LEU   A HD22 1 
ATOM   1081 H HD23 A LEU   A 1 43  ? 30.583 1.837   -0.037  0.88 12.94 ?  43  LEU   A HD23 1 
ATOM   1082 H HD23 B LEU   A 1 43  ? 30.447 1.868   -0.350  0.12 12.02 ?  43  LEU   A HD23 1 
ATOM   1083 N N    A LYS   A 1 44  ? 29.564 6.465   -1.601  0.88 10.00 ?  44  LYS   A N    1 
ATOM   1084 N N    B LYS   A 1 44  ? 29.331 6.507   -1.688  0.12 11.16 ?  44  LYS   A N    1 
ATOM   1085 C CA   A LYS   A 1 44  ? 28.916 7.777   -1.601  0.88 10.35 ?  44  LYS   A CA   1 
ATOM   1086 C CA   B LYS   A 1 44  ? 28.690 7.820   -1.650  0.12 11.72 ?  44  LYS   A CA   1 
ATOM   1087 C C    A LYS   A 1 44  ? 27.489 7.585   -1.102  0.88 9.78  ?  44  LYS   A C    1 
ATOM   1088 C C    B LYS   A 1 44  ? 27.286 7.632   -1.093  0.12 11.08 ?  44  LYS   A C    1 
ATOM   1089 O O    A LYS   A 1 44  ? 26.625 7.066   -1.815  0.88 10.77 ?  44  LYS   A O    1 
ATOM   1090 O O    B LYS   A 1 44  ? 26.361 7.255   -1.816  0.12 10.97 ?  44  LYS   A O    1 
ATOM   1091 C CB   A LYS   A 1 44  ? 28.965 8.415   -2.984  0.88 12.54 ?  44  LYS   A CB   1 
ATOM   1092 C CB   B LYS   A 1 44  ? 28.662 8.447   -3.040  0.12 13.16 ?  44  LYS   A CB   1 
ATOM   1093 C CG   A LYS   A 1 44  ? 30.338 8.923   -3.391  0.88 15.96 ?  44  LYS   A CG   1 
ATOM   1094 C CG   B LYS   A 1 44  ? 30.031 8.830   -3.586  0.12 14.52 ?  44  LYS   A CG   1 
ATOM   1095 C CD   A LYS   A 1 44  ? 30.972 9.847   -2.347  0.88 21.50 ?  44  LYS   A CD   1 
ATOM   1096 C CD   B LYS   A 1 44  ? 30.897 9.487   -2.522  0.12 16.00 ?  44  LYS   A CD   1 
ATOM   1097 C CE   A LYS   A 1 44  ? 32.282 10.427  -2.849  0.88 24.73 ?  44  LYS   A CE   1 
ATOM   1098 C CE   B LYS   A 1 44  ? 32.172 10.054  -3.117  0.12 16.74 ?  44  LYS   A CE   1 
ATOM   1099 N NZ   A LYS   A 1 44  ? 33.131 10.963  -1.752  0.88 26.53 ?  44  LYS   A NZ   1 
ATOM   1100 N NZ   B LYS   A 1 44  ? 33.171 10.394  -2.065  0.12 16.94 ?  44  LYS   A NZ   1 
ATOM   1101 H H    A LYS   A 1 44  ? 29.432 6.013   -2.321  0.88 12.00 ?  44  LYS   A H    1 
ATOM   1102 H H    B LYS   A 1 44  ? 29.160 6.064   -2.403  0.12 13.38 ?  44  LYS   A H    1 
ATOM   1103 H HA   A LYS   A 1 44  ? 29.370 8.354   -0.968  0.88 12.41 ?  44  LYS   A HA   1 
ATOM   1104 H HA   B LYS   A 1 44  ? 29.168 8.404   -1.041  0.12 14.06 ?  44  LYS   A HA   1 
ATOM   1105 H HB2  A LYS   A 1 44  ? 28.687 7.763   -3.642  0.88 15.03 ?  44  LYS   A HB2  1 
ATOM   1106 H HB2  B LYS   A 1 44  ? 28.268 7.813   -3.662  0.12 15.78 ?  44  LYS   A HB2  1 
ATOM   1107 H HB3  A LYS   A 1 44  ? 28.357 9.174   -2.997  0.88 15.03 ?  44  LYS   A HB3  1 
ATOM   1108 H HB3  B LYS   A 1 44  ? 28.124 9.253   -3.012  0.12 15.78 ?  44  LYS   A HB3  1 
ATOM   1109 H HG2  A LYS   A 1 44  ? 30.932 8.169   -3.523  0.88 19.14 ?  44  LYS   A HG2  1 
ATOM   1110 H HG2  B LYS   A 1 44  ? 30.486 8.034   -3.899  0.12 17.42 ?  44  LYS   A HG2  1 
ATOM   1111 H HG3  A LYS   A 1 44  ? 30.258 9.430   -4.220  0.88 19.14 ?  44  LYS   A HG3  1 
ATOM   1112 H HG3  B LYS   A 1 44  ? 29.919 9.461   -4.317  0.12 17.42 ?  44  LYS   A HG3  1 
ATOM   1113 H HD2  A LYS   A 1 44  ? 30.358 10.571  -2.148  0.88 25.79 ?  44  LYS   A HD2  1 
ATOM   1114 H HD2  B LYS   A 1 44  ? 30.398 10.210  -2.103  0.12 19.19 ?  44  LYS   A HD2  1 
ATOM   1115 H HD3  A LYS   A 1 44  ? 31.159 9.333   -1.543  0.88 25.79 ?  44  LYS   A HD3  1 
ATOM   1116 H HD3  B LYS   A 1 44  ? 31.148 8.825   -1.857  0.12 19.19 ?  44  LYS   A HD3  1 
ATOM   1117 H HE2  A LYS   A 1 44  ? 32.781 9.728   -3.301  0.88 29.66 ?  44  LYS   A HE2  1 
ATOM   1118 H HE2  B LYS   A 1 44  ? 32.566 9.395   -3.709  0.12 20.08 ?  44  LYS   A HE2  1 
ATOM   1119 H HE3  A LYS   A 1 44  ? 32.089 11.149  -3.463  0.88 29.66 ?  44  LYS   A HE3  1 
ATOM   1120 H HE3  B LYS   A 1 44  ? 31.961 10.864  -3.609  0.12 20.08 ?  44  LYS   A HE3  1 
ATOM   1121 H HZ1  A LYS   A 1 44  ? 33.887 11.293  -2.088  0.88 31.83 ?  44  LYS   A HZ1  1 
ATOM   1122 H HZ1  B LYS   A 1 44  ? 32.834 11.002  -1.509  0.12 20.32 ?  44  LYS   A HZ1  1 
ATOM   1123 H HZ2  A LYS   A 1 44  ? 32.698 11.613  -1.323  0.88 31.83 ?  44  LYS   A HZ2  1 
ATOM   1124 H HZ2  B LYS   A 1 44  ? 33.385 9.665   -1.601  0.12 20.32 ?  44  LYS   A HZ2  1 
ATOM   1125 H HZ3  A LYS   A 1 44  ? 33.329 10.317  -1.174  0.88 31.83 ?  44  LYS   A HZ3  1 
ATOM   1126 H HZ3  B LYS   A 1 44  ? 33.908 10.723  -2.441  0.12 20.32 ?  44  LYS   A HZ3  1 
ATOM   1127 N N    A HIS   A 1 45  ? 27.257 7.976   0.144   0.88 9.47  ?  45  HIS   A N    1 
ATOM   1128 N N    B HIS   A 1 45  ? 27.128 7.897   0.201   0.12 10.76 ?  45  HIS   A N    1 
ATOM   1129 C CA   A HIS   A 1 45  ? 26.025 7.624   0.845   0.88 9.76  ?  45  HIS   A CA   1 
ATOM   1130 C CA   B HIS   A 1 45  ? 25.861 7.673   0.893   0.12 10.44 ?  45  HIS   A CA   1 
ATOM   1131 C C    A HIS   A 1 45  ? 24.987 8.739   0.688   0.88 10.58 ?  45  HIS   A C    1 
ATOM   1132 C C    B HIS   A 1 45  ? 24.974 8.889   0.667   0.12 10.36 ?  45  HIS   A C    1 
ATOM   1133 O O    A HIS   A 1 45  ? 24.649 9.461   1.627   0.88 11.37 ?  45  HIS   A O    1 
ATOM   1134 O O    B HIS   A 1 45  ? 25.047 9.886   1.387   0.12 10.49 ?  45  HIS   A O    1 
ATOM   1135 C CB   A HIS   A 1 45  ? 26.327 7.357   2.307   0.88 9.60  ?  45  HIS   A CB   1 
ATOM   1136 C CB   B HIS   A 1 45  ? 26.108 7.420   2.373   0.12 10.18 ?  45  HIS   A CB   1 
ATOM   1137 C CG   A HIS   A 1 45  ? 27.436 6.382   2.527   0.88 9.14  ?  45  HIS   A CG   1 
ATOM   1138 C CG   B HIS   A 1 45  ? 27.268 6.513   2.635   0.12 9.51  ?  45  HIS   A CG   1 
ATOM   1139 N ND1  A HIS   A 1 45  ? 27.424 5.096   2.023   0.88 9.60  ?  45  HIS   A ND1  1 
ATOM   1140 N ND1  B HIS   A 1 45  ? 27.320 5.218   2.167   0.12 9.43  ?  45  HIS   A ND1  1 
ATOM   1141 C CD2  A HIS   A 1 45  ? 28.607 6.528   3.190   0.88 9.66  ?  45  HIS   A CD2  1 
ATOM   1142 C CD2  B HIS   A 1 45  ? 28.428 6.721   3.303   0.12 8.98  ?  45  HIS   A CD2  1 
ATOM   1143 C CE1  A HIS   A 1 45  ? 28.545 4.493   2.383   0.88 9.56  ?  45  HIS   A CE1  1 
ATOM   1144 C CE1  B HIS   A 1 45  ? 28.460 4.664   2.542   0.12 8.90  ?  45  HIS   A CE1  1 
ATOM   1145 N NE2  A HIS   A 1 45  ? 29.276 5.336   3.092   0.88 9.64  ?  45  HIS   A NE2  1 
ATOM   1146 N NE2  B HIS   A 1 45  ? 29.149 5.554   3.233   0.12 8.66  ?  45  HIS   A NE2  1 
ATOM   1147 H H    A HIS   A 1 45  ? 27.802 8.455   0.615   0.88 11.36 ?  45  HIS   A H    1 
ATOM   1148 H H    B HIS   A 1 45  ? 27.749 8.214   0.707   0.12 12.90 ?  45  HIS   A H    1 
ATOM   1149 H HA   A HIS   A 1 45  ? 25.657 6.818   0.455   0.88 11.70 ?  45  HIS   A HA   1 
ATOM   1150 H HA   B HIS   A 1 45  ? 25.422 6.897   0.515   0.12 12.52 ?  45  HIS   A HA   1 
ATOM   1151 H HB2  A HIS   A 1 45  ? 26.568 8.194   2.734   0.88 11.51 ?  45  HIS   A HB2  1 
ATOM   1152 H HB2  B HIS   A 1 45  ? 26.284 8.265   2.814   0.12 12.21 ?  45  HIS   A HB2  1 
ATOM   1153 H HB3  A HIS   A 1 45  ? 25.526 6.998   2.727   0.88 11.51 ?  45  HIS   A HB3  1 
ATOM   1154 H HB3  B HIS   A 1 45  ? 25.319 7.007   2.755   0.12 12.21 ?  45  HIS   A HB3  1 
ATOM   1155 H HD2  A HIS   A 1 45  ? 28.904 7.293   3.632   0.88 11.58 ?  45  HIS   A HD2  1 
ATOM   1156 H HD2  B HIS   A 1 45  ? 28.685 7.505   3.731   0.12 10.77 ?  45  HIS   A HD2  1 
ATOM   1157 H HE1  A HIS   A 1 45  ? 28.769 3.615   2.181   0.88 11.46 ?  45  HIS   A HE1  1 
ATOM   1158 H HE1  B HIS   A 1 45  ? 28.728 3.796   2.350   0.12 10.67 ?  45  HIS   A HE1  1 
ATOM   1159 H HE2  A HIS   A 1 45  ? 30.047 5.164   3.431   0.88 11.55 ?  45  HIS   A HE2  1 
ATOM   1160 H HE2  B HIS   A 1 45  ? 29.923 5.425   3.580   0.12 10.39 ?  45  HIS   A HE2  1 
ATOM   1161 N N    A GLY   A 1 46  ? 24.466 8.858   -0.529  0.88 11.32 ?  46  GLY   A N    1 
ATOM   1162 N N    B GLY   A 1 46  ? 24.125 8.804   -0.354  0.12 10.26 ?  46  GLY   A N    1 
ATOM   1163 C CA   A GLY   A 1 46  ? 23.660 10.016  -0.877  0.88 12.10 ?  46  GLY   A CA   1 
ATOM   1164 C CA   B GLY   A 1 46  ? 23.277 9.919   -0.722  0.12 10.08 ?  46  GLY   A CA   1 
ATOM   1165 C C    A GLY   A 1 46  ? 22.179 9.905   -0.589  0.88 12.00 ?  46  GLY   A C    1 
ATOM   1166 C C    B GLY   A 1 46  ? 21.831 9.768   -0.303  0.12 9.86  ?  46  GLY   A C    1 
ATOM   1167 O O    A GLY   A 1 46  ? 21.521 10.909  -0.287  0.88 12.61 ?  46  GLY   A O    1 
ATOM   1168 O O    B GLY   A 1 46  ? 21.229 10.724  0.196   0.12 9.75  ?  46  GLY   A O    1 
ATOM   1169 H H    A GLY   A 1 46  ? 24.546 8.285   -1.160  0.88 13.58 ?  46  GLY   A H    1 
ATOM   1170 H H    B GLY   A 1 46  ? 24.030 8.110   -0.853  0.12 12.31 ?  46  GLY   A H    1 
ATOM   1171 H HA2  A GLY   A 1 46  ? 23.985 10.788  -0.391  0.88 14.51 ?  46  GLY   A HA2  1 
ATOM   1172 H HA2  B GLY   A 1 46  ? 23.620 10.730  -0.317  0.12 12.09 ?  46  GLY   A HA2  1 
ATOM   1173 H HA3  A GLY   A 1 46  ? 23.751 10.195  -1.822  0.88 14.51 ?  46  GLY   A HA3  1 
ATOM   1174 H HA3  B GLY   A 1 46  ? 23.303 10.029  -1.684  0.12 12.09 ?  46  GLY   A HA3  1 
ATOM   1175 N N    A GLY   A 1 47  ? 21.635 8.702   -0.711  0.88 11.92 ?  47  GLY   A N    1 
ATOM   1176 N N    B GLY   A 1 47  ? 21.255 8.581   -0.494  0.12 9.93  ?  47  GLY   A N    1 
ATOM   1177 C CA   A GLY   A 1 47  ? 20.199 8.510   -0.647  0.88 12.03 ?  47  GLY   A CA   1 
ATOM   1178 C CA   B GLY   A 1 47  ? 19.847 8.386   -0.225  0.12 9.62  ?  47  GLY   A CA   1 
ATOM   1179 C C    A GLY   A 1 47  ? 19.877 7.069   -0.317  0.88 11.38 ?  47  GLY   A C    1 
ATOM   1180 C C    B GLY   A 1 47  ? 19.530 6.949   0.125   0.12 9.00  ?  47  GLY   A C    1 
ATOM   1181 O O    A GLY   A 1 47  ? 20.766 6.240   -0.099  0.88 11.54 ?  47  GLY   A O    1 
ATOM   1182 O O    B GLY   A 1 47  ? 20.414 6.093   0.199   0.12 8.81  ?  47  GLY   A O    1 
ATOM   1183 H H    A GLY   A 1 47  ? 22.075 7.974   -0.806  0.88 14.29 ?  47  GLY   A H    1 
ATOM   1184 H H    B GLY   A 1 47  ? 21.665 7.875   -0.773  0.12 11.91 ?  47  GLY   A H    1 
ATOM   1185 H HA2  A GLY   A 1 47  ? 19.803 9.081   0.036   0.88 14.42 ?  47  GLY   A HA2  1 
ATOM   1186 H HA2  B GLY   A 1 47  ? 19.576 8.942   0.520   0.12 11.54 ?  47  GLY   A HA2  1 
ATOM   1187 H HA3  A GLY   A 1 47  ? 19.795 8.727   -1.503  0.88 14.42 ?  47  GLY   A HA3  1 
ATOM   1188 H HA3  B GLY   A 1 47  ? 19.328 8.635   -1.004  0.12 11.54 ?  47  GLY   A HA3  1 
ATOM   1189 N N    A GLY   A 1 48  ? 18.580 6.772   -0.296  0.88 11.45 ?  48  GLY   A N    1 
ATOM   1190 N N    B GLY   A 1 48  ? 18.241 6.694   0.342   0.12 8.79  ?  48  GLY   A N    1 
ATOM   1191 C CA   A GLY   A 1 48  ? 18.153 5.445   0.079   0.88 11.54 ?  48  GLY   A CA   1 
ATOM   1192 C CA   B GLY   A 1 48  ? 17.817 5.365   0.744   0.12 8.42  ?  48  GLY   A CA   1 
ATOM   1193 C C    A GLY   A 1 48  ? 18.589 5.118   1.494   0.88 10.72 ?  48  GLY   A C    1 
ATOM   1194 C C    B GLY   A 1 48  ? 18.479 4.960   2.046   0.12 8.43  ?  48  GLY   A C    1 
ATOM   1195 O O    A GLY   A 1 48  ? 18.739 5.999   2.353   0.88 10.96 ?  48  GLY   A O    1 
ATOM   1196 O O    B GLY   A 1 48  ? 18.634 5.762   2.975   0.12 8.24  ?  48  GLY   A O    1 
ATOM   1197 H H    A GLY   A 1 48  ? 17.940 7.313   -0.489  0.88 13.73 ?  48  GLY   A H    1 
ATOM   1198 H H    B GLY   A 1 48  ? 17.600 7.267   0.267   0.12 10.53 ?  48  GLY   A H    1 
ATOM   1199 H HA2  A GLY   A 1 48  ? 17.188 5.373   0.025   0.88 13.84 ?  48  GLY   A HA2  1 
ATOM   1200 H HA2  B GLY   A 1 48  ? 16.849 5.346   0.853   0.12 10.09 ?  48  GLY   A HA2  1 
ATOM   1201 H HA3  A GLY   A 1 48  ? 18.547 4.787   -0.519  0.88 13.84 ?  48  GLY   A HA3  1 
ATOM   1202 H HA3  B GLY   A 1 48  ? 18.060 4.721   0.060   0.12 10.09 ?  48  GLY   A HA3  1 
ATOM   1203 N N    A VAL   A 1 49  ? 18.796 3.823   1.740   0.88 10.58 ?  49  VAL   A N    1 
ATOM   1204 N N    B VAL   A 1 49  ? 18.890 3.692   2.111   0.12 8.40  ?  49  VAL   A N    1 
ATOM   1205 C CA   A VAL   A 1 49  ? 19.268 3.373   3.046   0.88 10.48 ?  49  VAL   A CA   1 
ATOM   1206 C CA   B VAL   A 1 49  ? 19.544 3.174   3.309   0.12 8.59  ?  49  VAL   A CA   1 
ATOM   1207 C C    A VAL   A 1 49  ? 20.585 4.049   3.410   0.88 9.78  ?  49  VAL   A C    1 
ATOM   1208 C C    B VAL   A 1 49  ? 20.843 3.922   3.580   0.12 8.38  ?  49  VAL   A C    1 
ATOM   1209 O O    A VAL   A 1 49  ? 20.781 4.468   4.557   0.88 9.74  ?  49  VAL   A O    1 
ATOM   1210 O O    B VAL   A 1 49  ? 21.150 4.267   4.728   0.12 8.34  ?  49  VAL   A O    1 
ATOM   1211 C CB   A VAL   A 1 49  ? 19.391 1.835   3.065   0.88 11.53 ?  49  VAL   A CB   1 
ATOM   1212 C CB   B VAL   A 1 49  ? 19.782 1.659   3.167   0.12 8.77  ?  49  VAL   A CB   1 
ATOM   1213 C CG1  A VAL   A 1 49  ? 20.163 1.365   4.304   0.88 12.35 ?  49  VAL   A CG1  1 
ATOM   1214 C CG1  B VAL   A 1 49  ? 20.636 1.150   4.317   0.12 8.79  ?  49  VAL   A CG1  1 
ATOM   1215 C CG2  A VAL   A 1 49  ? 18.017 1.184   3.006   0.88 13.63 ?  49  VAL   A CG2  1 
ATOM   1216 C CG2  B VAL   A 1 49  ? 18.457 0.911   3.094   0.12 8.93  ?  49  VAL   A CG2  1 
ATOM   1217 H H    A VAL   A 1 49  ? 18.668 3.185   1.175   0.88 12.69 ?  49  VAL   A H    1 
ATOM   1218 H H    B VAL   A 1 49  ? 18.804 3.120   1.477   0.12 10.07 ?  49  VAL   A H    1 
ATOM   1219 H HA   A VAL   A 1 49  ? 18.618 3.612   3.721   0.88 12.56 ?  49  VAL   A HA   1 
ATOM   1220 H HA   B VAL   A 1 49  ? 18.960 3.310   4.070   0.12 10.30 ?  49  VAL   A HA   1 
ATOM   1221 H HB   A VAL   A 1 49  ? 19.892 1.540   2.286   0.88 13.83 ?  49  VAL   A HB   1 
ATOM   1222 H HB   B VAL   A 1 49  ? 20.264 1.492   2.342   0.12 10.51 ?  49  VAL   A HB   1 
ATOM   1223 H HG11 A VAL   A 1 49  ? 19.990 0.418   4.446   0.88 14.82 ?  49  VAL   A HG11 1 
ATOM   1224 H HG11 B VAL   A 1 49  ? 20.516 0.192   4.400   0.12 10.54 ?  49  VAL   A HG11 1 
ATOM   1225 H HG12 A VAL   A 1 49  ? 21.110 1.508   4.167   0.88 14.82 ?  49  VAL   A HG12 1 
ATOM   1226 H HG12 B VAL   A 1 49  ? 21.569 1.347   4.134   0.12 10.54 ?  49  VAL   A HG12 1 
ATOM   1227 H HG13 A VAL   A 1 49  ? 19.855 1.870   5.074   0.88 14.82 ?  49  VAL   A HG13 1 
ATOM   1228 H HG13 B VAL   A 1 49  ? 20.358 1.586   5.136   0.12 10.54 ?  49  VAL   A HG13 1 
ATOM   1229 H HG21 A VAL   A 1 49  ? 18.123 0.217   3.019   0.88 16.35 ?  49  VAL   A HG21 1 
ATOM   1230 H HG21 B VAL   A 1 49  ? 18.633 -0.041  3.043   0.12 10.70 ?  49  VAL   A HG21 1 
ATOM   1231 H HG22 A VAL   A 1 49  ? 17.504 1.468   3.777   0.88 16.35 ?  49  VAL   A HG22 1 
ATOM   1232 H HG22 B VAL   A 1 49  ? 17.938 1.110   3.889   0.12 10.70 ?  49  VAL   A HG22 1 
ATOM   1233 H HG23 A VAL   A 1 49  ? 17.578 1.458   2.190   0.88 16.35 ?  49  VAL   A HG23 1 
ATOM   1234 H HG23 B VAL   A 1 49  ? 17.976 1.201   2.303   0.12 10.70 ?  49  VAL   A HG23 1 
ATOM   1235 N N    A ALA   A 1 50  ? 21.524 4.119   2.462   0.88 9.35  ?  50  ALA   A N    1 
ATOM   1236 N N    B ALA   A 1 50  ? 21.630 4.174   2.532   0.12 8.33  ?  50  ALA   A N    1 
ATOM   1237 C CA   A ALA   A 1 50  ? 22.841 4.669   2.776   0.88 9.48  ?  50  ALA   A CA   1 
ATOM   1238 C CA   B ALA   A 1 50  ? 22.939 4.790   2.720   0.12 8.28  ?  50  ALA   A CA   1 
ATOM   1239 C C    A ALA   A 1 50  ? 22.745 6.129   3.198   0.88 9.52  ?  50  ALA   A C    1 
ATOM   1240 C C    B ALA   A 1 50  ? 22.805 6.206   3.266   0.12 8.15  ?  50  ALA   A C    1 
ATOM   1241 O O    A ALA   A 1 50  ? 23.381 6.553   4.173   0.88 10.00 ?  50  ALA   A O    1 
ATOM   1242 O O    B ALA   A 1 50  ? 23.451 6.567   4.258   0.12 7.94  ?  50  ALA   A O    1 
ATOM   1243 C CB   A ALA   A 1 50  ? 23.763 4.534   1.569   0.88 9.52  ?  50  ALA   A CB   1 
ATOM   1244 C CB   B ALA   A 1 50  ? 23.715 4.774   1.401   0.12 8.24  ?  50  ALA   A CB   1 
ATOM   1245 H H    A ALA   A 1 50  ? 21.423 3.866   1.643   0.88 11.21 ?  50  ALA   A H    1 
ATOM   1246 H H    B ALA   A 1 50  ? 21.428 4.007   1.715   0.12 9.99  ?  50  ALA   A H    1 
ATOM   1247 H HA   A ALA   A 1 50  ? 23.227 4.174   3.509   0.88 11.37 ?  50  ALA   A HA   1 
ATOM   1248 H HA   B ALA   A 1 50  ? 23.442 4.276   3.365   0.12 9.93  ?  50  ALA   A HA   1 
ATOM   1249 H HB1  A ALA   A 1 50  ? 24.631 4.906   1.792   0.88 11.41 ?  50  ALA   A HB1  1 
ATOM   1250 H HB1  B ALA   A 1 50  ? 24.609 5.117   1.554   0.12 9.88  ?  50  ALA   A HB1  1 
ATOM   1251 H HB2  A ALA   A 1 50  ? 23.852 3.597   1.342   0.88 11.41 ?  50  ALA   A HB2  1 
ATOM   1252 H HB2  B ALA   A 1 50  ? 23.767 3.858   1.078   0.12 9.88  ?  50  ALA   A HB2  1 
ATOM   1253 H HB3  A ALA   A 1 50  ? 23.379 5.021   0.821   0.88 11.41 ?  50  ALA   A HB3  1 
ATOM   1254 H HB3  B ALA   A 1 50  ? 23.252 5.324   0.750   0.12 9.88  ?  50  ALA   A HB3  1 
ATOM   1255 N N    A GLY   A 1 51  ? 21.973 6.924   2.460   0.88 9.70  ?  51  GLY   A N    1 
ATOM   1256 N N    B GLY   A 1 51  ? 21.964 7.026   2.635   0.12 8.41  ?  51  GLY   A N    1 
ATOM   1257 C CA   A GLY   A 1 51  ? 21.823 8.316   2.834   0.88 10.04 ?  51  GLY   A CA   1 
ATOM   1258 C CA   B GLY   A 1 51  ? 21.783 8.385   3.115   0.12 8.55  ?  51  GLY   A CA   1 
ATOM   1259 C C    A GLY   A 1 51  ? 21.222 8.471   4.213   0.88 9.88  ?  51  GLY   A C    1 
ATOM   1260 C C    B GLY   A 1 51  ? 21.186 8.430   4.508   0.12 8.87  ?  51  GLY   A C    1 
ATOM   1261 O O    A GLY   A 1 51  ? 21.615 9.359   4.974   0.88 10.42 ?  51  GLY   A O    1 
ATOM   1262 O O    B GLY   A 1 51  ? 21.534 9.294   5.318   0.12 9.02  ?  51  GLY   A O    1 
ATOM   1263 H H    A GLY   A 1 51  ? 21.544 6.691   1.752   0.88 11.63 ?  51  GLY   A H    1 
ATOM   1264 H H    B GLY   A 1 51  ? 21.492 6.820   1.945   0.12 10.08 ?  51  GLY   A H    1 
ATOM   1265 H HA2  A GLY   A 1 51  ? 22.688 8.753   2.830   0.88 12.04 ?  51  GLY   A HA2  1 
ATOM   1266 H HA2  B GLY   A 1 51  ? 22.641 8.840   3.132   0.12 10.25 ?  51  GLY   A HA2  1 
ATOM   1267 H HA3  A GLY   A 1 51  ? 21.245 8.767   2.200   0.88 12.04 ?  51  GLY   A HA3  1 
ATOM   1268 H HA3  B GLY   A 1 51  ? 21.196 8.867   2.509   0.12 10.25 ?  51  GLY   A HA3  1 
ATOM   1269 N N    A ALA   A 1 52  ? 20.250 7.617   4.548   0.88 10.07 ?  52  ALA   A N    1 
ATOM   1270 N N    B ALA   A 1 52  ? 20.282 7.496   4.809   0.12 8.98  ?  52  ALA   A N    1 
ATOM   1271 C CA   A ALA   A 1 52  ? 19.611 7.679   5.858   0.88 10.64 ?  52  ALA   A CA   1 
ATOM   1272 C CA   B ALA   A 1 52  ? 19.659 7.465   6.128   0.12 9.15  ?  52  ALA   A CA   1 
ATOM   1273 C C    A ALA   A 1 52  ? 20.569 7.259   6.971   0.88 9.98  ?  52  ALA   A C    1 
ATOM   1274 C C    B ALA   A 1 52  ? 20.664 7.061   7.200   0.12 9.03  ?  52  ALA   A C    1 
ATOM   1275 O O    A ALA   A 1 52  ? 20.649 7.920   8.012   0.88 10.79 ?  52  ALA   A O    1 
ATOM   1276 O O    B ALA   A 1 52  ? 20.731 7.679   8.269   0.12 9.15  ?  52  ALA   A O    1 
ATOM   1277 C CB   A ALA   A 1 52  ? 18.348 6.814   5.866   0.88 11.91 ?  52  ALA   A CB   1 
ATOM   1278 C CB   B ALA   A 1 52  ? 18.460 6.514   6.113   0.12 9.19  ?  52  ALA   A CB   1 
ATOM   1279 H H    A ALA   A 1 52  ? 19.956 6.984   4.041   0.88 12.07 ?  52  ALA   A H    1 
ATOM   1280 H H    B ALA   A 1 52  ? 20.020 6.878   4.271   0.12 10.76 ?  52  ALA   A H    1 
ATOM   1281 H HA   A ALA   A 1 52  ? 19.346 8.588   6.033   0.88 12.76 ?  52  ALA   A HA   1 
ATOM   1282 H HA   B ALA   A 1 52  ? 19.335 8.351   6.341   0.12 10.97 ?  52  ALA   A HA   1 
ATOM   1283 H HB1  A ALA   A 1 52  ? 17.931 6.867   6.744   0.88 14.28 ?  52  ALA   A HB1  1 
ATOM   1284 H HB1  B ALA   A 1 52  ? 18.017 6.553   6.975   0.12 11.01 ?  52  ALA   A HB1  1 
ATOM   1285 H HB2  A ALA   A 1 52  ? 17.734 7.147   5.192   0.88 14.28 ?  52  ALA   A HB2  1 
ATOM   1286 H HB2  B ALA   A 1 52  ? 17.845 6.794   5.416   0.12 11.01 ?  52  ALA   A HB2  1 
ATOM   1287 H HB3  A ALA   A 1 52  ? 18.585 5.894   5.672   0.88 14.28 ?  52  ALA   A HB3  1 
ATOM   1288 H HB3  B ALA   A 1 52  ? 18.770 5.613   5.937   0.12 11.01 ?  52  ALA   A HB3  1 
ATOM   1289 N N    A LEU   A 1 53  ? 21.287 6.147   6.788   0.88 9.70  ?  53  LEU   A N    1 
ATOM   1290 N N    B LEU   A 1 53  ? 21.458 6.020   6.934   0.12 9.06  ?  53  LEU   A N    1 
ATOM   1291 C CA   A LEU   A 1 53  ? 22.253 5.726   7.805   0.88 9.89  ?  53  LEU   A CA   1 
ATOM   1292 C CA   B LEU   A 1 53  ? 22.480 5.615   7.895   0.12 8.98  ?  53  LEU   A CA   1 
ATOM   1293 C C    A LEU   A 1 53  ? 23.313 6.799   8.005   0.88 9.33  ?  53  LEU   A C    1 
ATOM   1294 C C    B LEU   A 1 53  ? 23.503 6.724   8.106   0.12 9.15  ?  53  LEU   A C    1 
ATOM   1295 O O    A LEU   A 1 53  ? 23.639 7.167   9.138   0.88 10.35 ?  53  LEU   A O    1 
ATOM   1296 O O    B LEU   A 1 53  ? 23.890 7.013   9.243   0.12 9.34  ?  53  LEU   A O    1 
ATOM   1297 C CB   A LEU   A 1 53  ? 22.910 4.392   7.425   0.88 10.19 ?  53  LEU   A CB   1 
ATOM   1298 C CB   B LEU   A 1 53  ? 23.181 4.340   7.423   0.12 8.62  ?  53  LEU   A CB   1 
ATOM   1299 C CG   A LEU   A 1 53  ? 22.030 3.136   7.480   0.88 10.81 ?  53  LEU   A CG   1 
ATOM   1300 C CG   B LEU   A 1 53  ? 22.429 3.011   7.514   0.12 8.42  ?  53  LEU   A CG   1 
ATOM   1301 C CD1  A LEU   A 1 53  ? 22.766 1.943   6.884   0.88 11.55 ?  53  LEU   A CD1  1 
ATOM   1302 C CD1  B LEU   A 1 53  ? 23.287 1.893   6.944   0.12 8.15  ?  53  LEU   A CD1  1 
ATOM   1303 C CD2  A LEU   A 1 53  ? 21.595 2.820   8.898   0.88 12.20 ?  53  LEU   A CD2  1 
ATOM   1304 C CD2  B LEU   A 1 53  ? 22.035 2.694   8.946   0.12 8.21  ?  53  LEU   A CD2  1 
ATOM   1305 H H    A LEU   A 1 53  ? 21.245 5.630   6.097   0.88 11.63 ?  53  LEU   A H    1 
ATOM   1306 H H    B LEU   A 1 53  ? 21.424 5.542   6.219   0.12 10.86 ?  53  LEU   A H    1 
ATOM   1307 H HA   A LEU   A 1 53  ? 21.795 5.598   8.645   0.88 11.85 ?  53  LEU   A HA   1 
ATOM   1308 H HA   B LEU   A 1 53  ? 22.057 5.431   8.746   0.12 10.77 ?  53  LEU   A HA   1 
ATOM   1309 H HB2  A LEU   A 1 53  ? 23.249 4.462   6.516   0.88 12.22 ?  53  LEU   A HB2  1 
ATOM   1310 H HB2  B LEU   A 1 53  ? 23.424 4.460   6.493   0.12 10.33 ?  53  LEU   A HB2  1 
ATOM   1311 H HB3  A LEU   A 1 53  ? 23.660 4.236   8.026   0.88 12.22 ?  53  LEU   A HB3  1 
ATOM   1312 H HB3  B LEU   A 1 53  ? 23.990 4.237   7.949   0.12 10.33 ?  53  LEU   A HB3  1 
ATOM   1313 H HG   A LEU   A 1 53  ? 21.237 3.286   6.945   0.88 12.96 ?  53  LEU   A HG   1 
ATOM   1314 H HG   B LEU   A 1 53  ? 21.620 3.067   6.983   0.12 10.09 ?  53  LEU   A HG   1 
ATOM   1315 H HD11 A LEU   A 1 53  ? 22.187 1.162   6.929   0.88 13.85 ?  53  LEU   A HD11 1 
ATOM   1316 H HD11 B LEU   A 1 53  ? 22.798 1.058   7.005   0.12 9.77  ?  53  LEU   A HD11 1 
ATOM   1317 H HD12 A LEU   A 1 53  ? 22.988 2.134   5.960   0.88 13.85 ?  53  LEU   A HD12 1 
ATOM   1318 H HD12 B LEU   A 1 53  ? 23.488 2.092   6.016   0.12 9.77  ?  53  LEU   A HD12 1 
ATOM   1319 H HD13 A LEU   A 1 53  ? 23.575 1.781   7.394   0.88 13.85 ?  53  LEU   A HD13 1 
ATOM   1320 H HD13 B LEU   A 1 53  ? 24.109 1.834   7.456   0.12 9.77  ?  53  LEU   A HD13 1 
ATOM   1321 H HD21 A LEU   A 1 53  ? 21.087 1.993   8.896   0.88 14.63 ?  53  LEU   A HD21 1 
ATOM   1322 H HD21 B LEU   A 1 53  ? 21.603 1.827   8.970   0.12 9.84  ?  53  LEU   A HD21 1 
ATOM   1323 H HD22 A LEU   A 1 53  ? 22.382 2.722   9.456   0.88 14.63 ?  53  LEU   A HD22 1 
ATOM   1324 H HD22 B LEU   A 1 53  ? 22.832 2.682   9.497   0.12 9.84  ?  53  LEU   A HD22 1 
ATOM   1325 H HD23 A LEU   A 1 53  ? 21.044 3.545   9.227   0.88 14.63 ?  53  LEU   A HD23 1 
ATOM   1326 H HD23 B LEU   A 1 53  ? 21.423 3.375   9.265   0.12 9.84  ?  53  LEU   A HD23 1 
ATOM   1327 N N    A ASN   A 1 54  ? 23.843 7.334   6.908   0.88 9.31  ?  54  ASN   A N    1 
ATOM   1328 N N    B ASN   A 1 54  ? 23.956 7.355   7.021   0.12 9.48  ?  54  ASN   A N    1 
ATOM   1329 C CA   A ASN   A 1 54  ? 24.900 8.327   7.043   0.88 9.26  ?  54  ASN   A CA   1 
ATOM   1330 C CA   B ASN   A 1 54  ? 24.979 8.388   7.149   0.12 9.71  ?  54  ASN   A CA   1 
ATOM   1331 C C    A ASN   A 1 54  ? 24.397 9.575   7.766   0.88 9.83  ?  54  ASN   A C    1 
ATOM   1332 C C    B ASN   A 1 54  ? 24.437 9.621   7.862   0.12 9.99  ?  54  ASN   A C    1 
ATOM   1333 O O    A ASN   A 1 54  ? 25.091 10.125  8.631   0.88 10.54 ?  54  ASN   A O    1 
ATOM   1334 O O    B ASN   A 1 54  ? 25.099 10.170  8.751   0.12 9.88  ?  54  ASN   A O    1 
ATOM   1335 C CB   A ASN   A 1 54  ? 25.464 8.695   5.682   0.88 9.59  ?  54  ASN   A CB   1 
ATOM   1336 C CB   B ASN   A 1 54  ? 25.540 8.758   5.777   0.12 9.84  ?  54  ASN   A CB   1 
ATOM   1337 C CG   A ASN   A 1 54  ? 26.482 9.796   5.794   0.88 9.87  ?  54  ASN   A CG   1 
ATOM   1338 C CG   B ASN   A 1 54  ? 26.493 9.935   5.843   0.12 9.85  ?  54  ASN   A CG   1 
ATOM   1339 O OD1  A ASN   A 1 54  ? 27.478 9.657   6.518   0.88 9.71  ?  54  ASN   A OD1  1 
ATOM   1340 O OD1  B ASN   A 1 54  ? 27.626 9.802   6.308   0.12 10.05 ?  54  ASN   A OD1  1 
ATOM   1341 N ND2  A ASN   A 1 54  ? 26.238 10.911  5.121   0.88 10.36 ?  54  ASN   A ND2  1 
ATOM   1342 N ND2  B ASN   A 1 54  ? 26.039 11.097  5.384   0.12 9.74  ?  54  ASN   A ND2  1 
ATOM   1343 H H    A ASN   A 1 54  ? 23.607 7.148   6.102   0.88 11.16 ?  54  ASN   A H    1 
ATOM   1344 H H    B ASN   A 1 54  ? 23.690 7.205   6.218   0.12 11.36 ?  54  ASN   A H    1 
ATOM   1345 H HA   A ASN   A 1 54  ? 25.614 7.946   7.570   0.88 11.10 ?  54  ASN   A HA   1 
ATOM   1346 H HA   B ASN   A 1 54  ? 25.708 8.037   7.680   0.12 11.64 ?  54  ASN   A HA   1 
ATOM   1347 H HB2  A ASN   A 1 54  ? 25.896 7.908   5.297   0.88 11.49 ?  54  ASN   A HB2  1 
ATOM   1348 H HB2  B ASN   A 1 54  ? 26.027 7.998   5.418   0.12 11.79 ?  54  ASN   A HB2  1 
ATOM   1349 H HB3  A ASN   A 1 54  ? 24.745 8.991   5.104   0.88 11.49 ?  54  ASN   A HB3  1 
ATOM   1350 H HB3  B ASN   A 1 54  ? 24.809 8.994   5.186   0.12 11.79 ?  54  ASN   A HB3  1 
ATOM   1351 H HD21 A ASN   A 1 54  ? 26.791 11.565  5.164   0.88 12.42 ?  54  ASN   A HD21 1 
ATOM   1352 H HD21 B ASN   A 1 54  ? 26.542 11.796  5.404   0.12 11.68 ?  54  ASN   A HD21 1 
ATOM   1353 H HD22 A ASN   A 1 54  ? 25.527 10.975  4.641   0.88 12.42 ?  54  ASN   A HD22 1 
ATOM   1354 H HD22 B ASN   A 1 54  ? 25.243 11.152  5.065   0.12 11.68 ?  54  ASN   A HD22 1 
ATOM   1355 N N    A LYS   A 1 55  ? 23.187 10.034  7.427   0.88 10.10 ?  55  LYS   A N    1 
ATOM   1356 N N    B LYS   A 1 55  ? 23.237 10.072  7.489   0.12 10.40 ?  55  LYS   A N    1 
ATOM   1357 C CA   A LYS   A 1 55  ? 22.602 11.186  8.107   0.88 10.39 ?  55  LYS   A CA   1 
ATOM   1358 C CA   B LYS   A 1 55  ? 22.656 11.235  8.152   0.12 10.93 ?  55  LYS   A CA   1 
ATOM   1359 C C    A LYS   A 1 55  ? 22.523 10.949  9.607   0.88 10.68 ?  55  LYS   A C    1 
ATOM   1360 C C    B LYS   A 1 55  ? 22.472 10.977  9.641   0.12 11.02 ?  55  LYS   A C    1 
ATOM   1361 O O    A LYS   A 1 55  ? 22.819 11.847  10.404  0.88 11.48 ?  55  LYS   A O    1 
ATOM   1362 O O    B LYS   A 1 55  ? 22.636 11.887  10.462  0.12 11.04 ?  55  LYS   A O    1 
ATOM   1363 C CB   A LYS   A 1 55  ? 21.222 11.482  7.510   0.88 11.49 ?  55  LYS   A CB   1 
ATOM   1364 C CB   B LYS   A 1 55  ? 21.327 11.612  7.493   0.12 11.47 ?  55  LYS   A CB   1 
ATOM   1365 C CG   A LYS   A 1 55  ? 20.467 12.629  8.161   0.88 12.67 ?  55  LYS   A CG   1 
ATOM   1366 C CG   B LYS   A 1 55  ? 20.685 12.877  8.051   0.12 11.99 ?  55  LYS   A CG   1 
ATOM   1367 C CD   A LYS   A 1 55  ? 19.151 12.886  7.423   0.88 13.91 ?  55  LYS   A CD   1 
ATOM   1368 C CD   B LYS   A 1 55  ? 19.335 13.149  7.400   0.12 12.57 ?  55  LYS   A CD   1 
ATOM   1369 C CE   A LYS   A 1 55  ? 18.324 13.982  8.075   0.88 14.87 ?  55  LYS   A CE   1 
ATOM   1370 C CE   B LYS   A 1 55  ? 18.667 14.385  7.987   0.12 13.03 ?  55  LYS   A CE   1 
ATOM   1371 N NZ   A LYS   A 1 55  ? 16.995 14.137  7.418   0.88 15.38 ?  55  LYS   A NZ   1 
ATOM   1372 N NZ   B LYS   A 1 55  ? 17.344 14.661  7.360   0.12 13.25 ?  55  LYS   A NZ   1 
ATOM   1373 H H    A LYS   A 1 55  ? 22.681 9.690   6.817   0.88 12.12 ?  55  LYS   A H    1 
ATOM   1374 H H    B LYS   A 1 55  ? 22.750 9.727   6.870   0.12 12.48 ?  55  LYS   A H    1 
ATOM   1375 H HA   A LYS   A 1 55  ? 23.165 11.958  7.956   0.88 12.46 ?  55  LYS   A HA   1 
ATOM   1376 H HA   B LYS   A 1 55  ? 23.260 11.985  8.054   0.12 13.11 ?  55  LYS   A HA   1 
ATOM   1377 H HB2  A LYS   A 1 55  ? 21.332 11.707  6.573   0.88 13.78 ?  55  LYS   A HB2  1 
ATOM   1378 H HB2  B LYS   A 1 55  ? 21.481 11.756  6.546   0.12 13.76 ?  55  LYS   A HB2  1 
ATOM   1379 H HB3  A LYS   A 1 55  ? 20.670 10.690  7.591   0.88 13.78 ?  55  LYS   A HB3  1 
ATOM   1380 H HB3  B LYS   A 1 55  ? 20.699 10.886  7.617   0.12 13.76 ?  55  LYS   A HB3  1 
ATOM   1381 H HG2  A LYS   A 1 55  ? 20.258 12.400  9.081   0.88 15.20 ?  55  LYS   A HG2  1 
ATOM   1382 H HG2  B LYS   A 1 55  ? 20.545 12.776  9.005   0.12 14.38 ?  55  LYS   A HG2  1 
ATOM   1383 H HG3  A LYS   A 1 55  ? 21.001 13.435  8.123   0.88 15.20 ?  55  LYS   A HG3  1 
ATOM   1384 H HG3  B LYS   A 1 55  ? 21.264 13.637  7.876   0.12 14.38 ?  55  LYS   A HG3  1 
ATOM   1385 H HD2  A LYS   A 1 55  ? 19.348 13.154  6.512   0.88 16.68 ?  55  LYS   A HD2  1 
ATOM   1386 H HD2  B LYS   A 1 55  ? 19.461 13.295  6.449   0.12 15.08 ?  55  LYS   A HD2  1 
ATOM   1387 H HD3  A LYS   A 1 55  ? 18.625 12.069  7.421   0.88 16.68 ?  55  LYS   A HD3  1 
ATOM   1388 H HD3  B LYS   A 1 55  ? 18.750 12.389  7.547   0.12 15.08 ?  55  LYS   A HD3  1 
ATOM   1389 H HE2  A LYS   A 1 55  ? 18.179 13.758  9.008   0.88 17.84 ?  55  LYS   A HE2  1 
ATOM   1390 H HE2  B LYS   A 1 55  ? 18.529 14.250  8.938   0.12 15.62 ?  55  LYS   A HE2  1 
ATOM   1391 H HE3  A LYS   A 1 55  ? 18.801 14.824  8.002   0.88 17.84 ?  55  LYS   A HE3  1 
ATOM   1392 H HE3  B LYS   A 1 55  ? 19.238 15.155  7.839   0.12 15.62 ?  55  LYS   A HE3  1 
ATOM   1393 H HZ1  A LYS   A 1 55  ? 16.533 14.784  7.818   0.88 18.44 ?  55  LYS   A HZ1  1 
ATOM   1394 H HZ1  B LYS   A 1 55  ? 16.918 15.294  7.818   0.12 15.89 ?  55  LYS   A HZ1  1 
ATOM   1395 H HZ2  A LYS   A 1 55  ? 17.102 14.346  6.560   0.88 18.44 ?  55  LYS   A HZ2  1 
ATOM   1396 H HZ2  B LYS   A 1 55  ? 17.456 14.938  6.522   0.12 15.89 ?  55  LYS   A HZ2  1 
ATOM   1397 H HZ3  A LYS   A 1 55  ? 16.537 13.376  7.475   0.88 18.44 ?  55  LYS   A HZ3  1 
ATOM   1398 H HZ3  B LYS   A 1 55  ? 16.848 13.922  7.358   0.12 15.89 ?  55  LYS   A HZ3  1 
ATOM   1399 N N    . ALA   A 1 56  ? 22.133 9.740   10.014  1.00 11.12 ?  56  ALA   A N    1 
ATOM   1400 C CA   . ALA   A 1 56  ? 22.014 9.412   11.427  1.00 11.93 ?  56  ALA   A CA   1 
ATOM   1401 C C    . ALA   A 1 56  ? 23.357 9.442   12.152  1.00 11.48 ?  56  ALA   A C    1 
ATOM   1402 O O    . ALA   A 1 56  ? 23.376 9.633   13.371  1.00 13.09 ?  56  ALA   A O    1 
ATOM   1403 C CB   . ALA   A 1 56  ? 21.327 8.051   11.596  1.00 13.01 ?  56  ALA   A CB   1 
ATOM   1404 H H    A ALA   A 1 56  ? 21.929 9.095   9.483   0.88 13.33 ?  56  ALA   A H    1 
ATOM   1405 H H    B ALA   A 1 56  ? 21.962 9.093   9.475   0.12 13.33 ?  56  ALA   A H    1 
ATOM   1406 H HA   . ALA   A 1 56  ? 21.449 10.069  11.850  1.00 14.31 ?  56  ALA   A HA   1 
ATOM   1407 H HB1  . ALA   A 1 56  ? 21.254 7.845   12.544  1.00 15.61 ?  56  ALA   A HB1  1 
ATOM   1408 H HB2  . ALA   A 1 56  ? 20.438 8.093   11.204  1.00 15.61 ?  56  ALA   A HB2  1 
ATOM   1409 H HB3  . ALA   A 1 56  ? 21.850 7.366   11.151  1.00 15.61 ?  56  ALA   A HB3  1 
ATOM   1410 N N    . THR   A 1 57  ? 24.472 9.263   11.434  1.00 10.69 ?  57  THR   A N    1 
ATOM   1411 C CA   . THR   A 1 57  ? 25.814 9.393   12.008  1.00 11.01 ?  57  THR   A CA   1 
ATOM   1412 C C    . THR   A 1 57  ? 26.362 10.813  11.933  1.00 11.34 ?  57  THR   A C    1 
ATOM   1413 O O    . THR   A 1 57  ? 27.545 11.024  12.226  1.00 11.89 ?  57  THR   A O    1 
ATOM   1414 C CB   . THR   A 1 57  ? 26.826 8.449   11.332  1.00 11.05 ?  57  THR   A CB   1 
ATOM   1415 O OG1  . THR   A 1 57  ? 27.204 8.949   10.037  1.00 10.59 ?  57  THR   A OG1  1 
ATOM   1416 C CG2  . THR   A 1 57  ? 26.298 7.024   11.231  1.00 11.03 ?  57  THR   A CG2  1 
ATOM   1417 H H    . THR   A 1 57  ? 24.474 9.046   10.596  1.00 12.81 ?  57  THR   A H    1 
ATOM   1418 H HA   . THR   A 1 57  ? 25.767 9.135   12.944  1.00 13.20 ?  57  THR   A HA   1 
ATOM   1419 H HB   . THR   A 1 57  ? 27.624 8.409   11.890  1.00 13.25 ?  57  THR   A HB   1 
ATOM   1420 H HG1  . THR   A 1 57  ? 26.526 9.008   9.550   1.00 12.70 ?  57  THR   A HG1  1 
ATOM   1421 H HG21 . THR   A 1 57  ? 26.786 6.535   10.546  1.00 13.23 ?  57  THR   A HG21 1 
ATOM   1422 H HG22 . THR   A 1 57  ? 26.413 6.562   12.079  1.00 13.23 ?  57  THR   A HG22 1 
ATOM   1423 H HG23 . THR   A 1 57  ? 25.358 7.019   11.003  1.00 13.23 ?  57  THR   A HG23 1 
ATOM   1424 N N    . ASN   A 1 58  ? 25.546 11.785  11.529  1.00 11.75 ?  58  ASN   A N    1 
ATOM   1425 C CA   . ASN   A 1 58  ? 26.006 13.166  11.434  1.00 12.83 ?  58  ASN   A CA   1 
ATOM   1426 C C    . ASN   A 1 58  ? 27.148 13.292  10.421  1.00 11.65 ?  58  ASN   A C    1 
ATOM   1427 O O    . ASN   A 1 58  ? 28.039 14.128  10.573  1.00 12.19 ?  58  ASN   A O    1 
ATOM   1428 C CB   . ASN   A 1 58  ? 26.396 13.688  12.832  1.00 15.18 ?  58  ASN   A CB   1 
ATOM   1429 C CG   . ASN   A 1 58  ? 26.820 15.141  12.843  1.00 18.40 ?  58  ASN   A CG   1 
ATOM   1430 O OD1  . ASN   A 1 58  ? 26.189 15.978  12.208  1.00 20.00 ?  58  ASN   A OD1  1 
ATOM   1431 N ND2  . ASN   A 1 58  ? 27.880 15.453  13.599  1.00 19.34 ?  58  ASN   A ND2  1 
ATOM   1432 H H    . ASN   A 1 58  ? 24.725 11.662  11.297  1.00 14.09 ?  58  ASN   A H    1 
ATOM   1433 H HA   . ASN   A 1 58  ? 25.269 13.704  11.115  1.00 15.39 ?  58  ASN   A HA   1 
ATOM   1434 H HB2  . ASN   A 1 58  ? 25.626 13.593  13.424  1.00 18.20 ?  58  ASN   A HB2  1 
ATOM   1435 H HB3  . ASN   A 1 58  ? 27.132 13.161  13.175  1.00 18.20 ?  58  ASN   A HB3  1 
ATOM   1436 H HD21 . ASN   A 1 58  ? 28.154 16.266  13.641  1.00 23.20 ?  58  ASN   A HD21 1 
ATOM   1437 H HD22 . ASN   A 1 58  ? 28.289 14.837  14.037  1.00 23.20 ?  58  ASN   A HD22 1 
ATOM   1438 N N    . ASN   A 1 59  ? 27.124 12.473  9.366   1.00 10.77 ?  59  ASN   A N    1 
ATOM   1439 C CA   . ASN   A 1 59  ? 28.103 12.455  8.270   1.00 10.52 ?  59  ASN   A CA   1 
ATOM   1440 C C    . ASN   A 1 59  ? 29.420 11.775  8.652   1.00 10.26 ?  59  ASN   A C    1 
ATOM   1441 O O    . ASN   A 1 59  ? 30.336 11.735  7.823   1.00 10.51 ?  59  ASN   A O    1 
ATOM   1442 C CB   . ASN   A 1 59  ? 28.386 13.845  7.670   1.00 10.77 ?  59  ASN   A CB   1 
ATOM   1443 C CG   . ASN   A 1 59  ? 28.735 13.784  6.204   1.00 10.93 ?  59  ASN   A CG   1 
ATOM   1444 O OD1  . ASN   A 1 59  ? 28.029 13.160  5.408   1.00 11.47 ?  59  ASN   A OD1  1 
ATOM   1445 N ND2  . ASN   A 1 59  ? 29.822 14.448  5.828   1.00 11.70 ?  59  ASN   A ND2  1 
ATOM   1446 H H    . ASN   A 1 59  ? 26.509 11.883  9.253   1.00 12.92 ?  59  ASN   A H    1 
ATOM   1447 H HA   . ASN   A 1 59  ? 27.721 11.928  7.555   1.00 12.62 ?  59  ASN   A HA   1 
ATOM   1448 H HB2  . ASN   A 1 59  ? 27.596 14.402  7.759   1.00 12.91 ?  59  ASN   A HB2  1 
ATOM   1449 H HB3  . ASN   A 1 59  ? 29.133 14.253  8.134   1.00 12.91 ?  59  ASN   A HB3  1 
ATOM   1450 H HD21 . ASN   A 1 59  ? 30.074 14.447  5.005   1.00 14.03 ?  59  ASN   A HD21 1 
ATOM   1451 H HD22 . ASN   A 1 59  ? 30.299 14.875  6.414   1.00 14.03 ?  59  ASN   A HD22 1 
ATOM   1452 N N    . ALA   A 1 60  ? 29.553 11.236  9.863   1.00 10.13 ?  60  ALA   A N    1 
ATOM   1453 C CA   . ALA   A 1 60  ? 30.792 10.551  10.217  1.00 10.53 ?  60  ALA   A CA   1 
ATOM   1454 C C    . ALA   A 1 60  ? 31.014 9.313   9.356   1.00 10.49 ?  60  ALA   A C    1 
ATOM   1455 O O    . ALA   A 1 60  ? 32.161 8.996   9.014   1.00 10.91 ?  60  ALA   A O    1 
ATOM   1456 C CB   . ALA   A 1 60  ? 30.791 10.186  11.698  1.00 11.21 ?  60  ALA   A CB   1 
ATOM   1457 H H    . ALA   A 1 60  ? 28.957 11.247  10.480  1.00 12.15 ?  60  ALA   A H    1 
ATOM   1458 H HA   . ALA   A 1 60  ? 31.537 11.156  10.062  1.00 12.63 ?  60  ALA   A HA   1 
ATOM   1459 H HB1  . ALA   A 1 60  ? 31.622 9.736   11.914  1.00 13.44 ?  60  ALA   A HB1  1 
ATOM   1460 H HB2  . ALA   A 1 60  ? 30.710 10.999  12.223  1.00 13.44 ?  60  ALA   A HB2  1 
ATOM   1461 H HB3  . ALA   A 1 60  ? 30.039 9.600   11.878  1.00 13.44 ?  60  ALA   A HB3  1 
ATOM   1462 N N    . MET   A 1 61  ? 29.942 8.614   8.980   1.00 10.10 ?  61  MET   A N    1 
ATOM   1463 C CA   . MET   A 1 61  ? 30.084 7.481   8.071   1.00 9.76  ?  61  MET   A CA   1 
ATOM   1464 C C    . MET   A 1 61  ? 30.713 7.911   6.748   1.00 9.53  ?  61  MET   A C    1 
ATOM   1465 O O    . MET   A 1 61  ? 31.605 7.233   6.227   1.00 10.07 ?  61  MET   A O    1 
ATOM   1466 C CB   . MET   A 1 61  ? 28.722 6.816   7.857   1.00 9.69  ?  61  MET   A CB   1 
ATOM   1467 C CG   . MET   A 1 61  ? 28.733 5.659   6.866   1.00 10.45 ?  61  MET   A CG   1 
ATOM   1468 S SD   . MET   A 1 61  ? 27.107 4.917   6.652   1.00 11.27 ?  61  MET   A SD   1 
ATOM   1469 C CE   . MET   A 1 61  ? 26.967 4.004   8.189   1.00 12.66 ?  61  MET   A CE   1 
ATOM   1470 H H    . MET   A 1 61  ? 29.138 8.773   9.235   1.00 12.11 ?  61  MET   A H    1 
ATOM   1471 H HA   . MET   A 1 61  ? 30.664 6.826   8.485   1.00 11.70 ?  61  MET   A HA   1 
ATOM   1472 H HB2  . MET   A 1 61  ? 28.412 6.466   8.707   1.00 11.62 ?  61  MET   A HB2  1 
ATOM   1473 H HB3  . MET   A 1 61  ? 28.098 7.477   7.528   1.00 11.62 ?  61  MET   A HB3  1 
ATOM   1474 H HG2  . MET   A 1 61  ? 29.021 5.979   5.997   1.00 12.53 ?  61  MET   A HG2  1 
ATOM   1475 H HG3  . MET   A 1 61  ? 29.333 4.968   7.182   1.00 12.53 ?  61  MET   A HG3  1 
ATOM   1476 H HE1  . MET   A 1 61  ? 26.148 3.484   8.179   1.00 15.18 ?  61  MET   A HE1  1 
ATOM   1477 H HE2  . MET   A 1 61  ? 27.732 3.410   8.273   1.00 15.18 ?  61  MET   A HE2  1 
ATOM   1478 H HE3  . MET   A 1 61  ? 26.954 4.628   8.932   1.00 15.18 ?  61  MET   A HE3  1 
ATOM   1479 N N    . GLN   A 1 62  ? 30.265 9.040   6.191   1.00 9.62  ?  62  GLN   A N    1 
ATOM   1480 C CA   . GLN   A 1 62  ? 30.820 9.517   4.927   1.00 10.16 ?  62  GLN   A CA   1 
ATOM   1481 C C    . GLN   A 1 62  ? 32.289 9.899   5.069   1.00 10.18 ?  62  GLN   A C    1 
ATOM   1482 O O    . GLN   A 1 62  ? 33.098 9.591   4.188   1.00 10.64 ?  62  GLN   A O    1 
ATOM   1483 C CB   . GLN   A 1 62  ? 30.017 10.705  4.399   1.00 10.11 ?  62  GLN   A CB   1 
ATOM   1484 C CG   . GLN   A 1 62  ? 30.387 11.070  2.975   1.00 10.06 ?  62  GLN   A CG   1 
ATOM   1485 C CD   . GLN   A 1 62  ? 30.056 9.944   2.024   1.00 10.41 ?  62  GLN   A CD   1 
ATOM   1486 O OE1  . GLN   A 1 62  ? 28.878 9.637   1.818   1.00 11.05 ?  62  GLN   A OE1  1 
ATOM   1487 N NE2  . GLN   A 1 62  ? 31.074 9.273   1.493   1.00 11.10 ?  62  GLN   A NE2  1 
ATOM   1488 H H    . GLN   A 1 62  ? 29.646 9.535   6.519   1.00 11.53 ?  62  GLN   A H    1 
ATOM   1489 H HA   . GLN   A 1 62  ? 30.765 8.798   4.276   1.00 12.18 ?  62  GLN   A HA   1 
ATOM   1490 H HB2  . GLN   A 1 62  ? 29.075 10.485  4.418   1.00 12.12 ?  62  GLN   A HB2  1 
ATOM   1491 H HB3  . GLN   A 1 62  ? 30.192 11.477  4.961   1.00 12.12 ?  62  GLN   A HB3  1 
ATOM   1492 H HG2  . GLN   A 1 62  ? 29.881 11.851  2.705   1.00 12.07 ?  62  GLN   A HG2  1 
ATOM   1493 H HG3  . GLN   A 1 62  ? 31.338 11.246  2.921   1.00 12.07 ?  62  GLN   A HG3  1 
ATOM   1494 H HE21 . GLN   A 1 62  ? 31.883 9.504   1.676   1.00 13.31 ?  62  GLN   A HE21 1 
ATOM   1495 H HE22 . GLN   A 1 62  ? 30.926 8.617   0.957   1.00 13.31 ?  62  GLN   A HE22 1 
ATOM   1496 N N    . VAL   A 1 63  ? 32.654 10.585  6.158   1.00 10.55 ?  63  VAL   A N    1 
ATOM   1497 C CA   . VAL   A 1 63  ? 34.046 10.978  6.367   1.00 11.31 ?  63  VAL   A CA   1 
ATOM   1498 C C    . VAL   A 1 63  ? 34.943 9.744   6.420   1.00 10.73 ?  63  VAL   A C    1 
ATOM   1499 O O    . VAL   A 1 63  ? 35.995 9.682   5.765   1.00 11.27 ?  63  VAL   A O    1 
ATOM   1500 C CB   . VAL   A 1 63  ? 34.161 11.850  7.631   1.00 13.01 ?  63  VAL   A CB   1 
ATOM   1501 C CG1  . VAL   A 1 63  ? 35.609 12.092  7.988   1.00 14.63 ?  63  VAL   A CG1  1 
ATOM   1502 C CG2  . VAL   A 1 63  ? 33.424 13.175  7.427   1.00 13.46 ?  63  VAL   A CG2  1 
ATOM   1503 H H    . VAL   A 1 63  ? 32.111 10.826  6.786   1.00 12.65 ?  63  VAL   A H    1 
ATOM   1504 H HA   . VAL   A 1 63  ? 34.323 11.515  5.614   1.00 13.56 ?  63  VAL   A HA   1 
ATOM   1505 H HB   . VAL   A 1 63  ? 33.744 11.386  8.375   1.00 15.60 ?  63  VAL   A HB   1 
ATOM   1506 H HG11 . VAL   A 1 63  ? 35.658 12.823  8.622   1.00 17.55 ?  63  VAL   A HG11 1 
ATOM   1507 H HG12 . VAL   A 1 63  ? 35.980 11.287  8.381   1.00 17.55 ?  63  VAL   A HG12 1 
ATOM   1508 H HG13 . VAL   A 1 63  ? 36.097 12.323  7.180   1.00 17.55 ?  63  VAL   A HG13 1 
ATOM   1509 H HG21 . VAL   A 1 63  ? 33.519 13.718  8.228   1.00 16.14 ?  63  VAL   A HG21 1 
ATOM   1510 H HG22 . VAL   A 1 63  ? 33.808 13.640  6.668   1.00 16.14 ?  63  VAL   A HG22 1 
ATOM   1511 H HG23 . VAL   A 1 63  ? 32.484 12.996  7.263   1.00 16.14 ?  63  VAL   A HG23 1 
ATOM   1512 N N    . GLU   A 1 64  ? 34.533 8.736   7.193   1.00 10.70 ?  64  GLU   A N    1 
ATOM   1513 C CA   . GLU   A 1 64  ? 35.298 7.499   7.286   1.00 10.74 ?  64  GLU   A CA   1 
ATOM   1514 C C    . GLU   A 1 64  ? 35.383 6.810   5.929   1.00 10.41 ?  64  GLU   A C    1 
ATOM   1515 O O    . GLU   A 1 64  ? 36.434 6.267   5.550   1.00 10.89 ?  64  GLU   A O    1 
ATOM   1516 C CB   . GLU   A 1 64  ? 34.609 6.591   8.304   1.00 11.20 ?  64  GLU   A CB   1 
ATOM   1517 C CG   . GLU   A 1 64  ? 35.262 5.237   8.448   1.00 11.73 ?  64  GLU   A CG   1 
ATOM   1518 C CD   . GLU   A 1 64  ? 34.389 4.239   9.181   1.00 12.46 ?  64  GLU   A CD   1 
ATOM   1519 O OE1  . GLU   A 1 64  ? 33.149 4.326   9.055   1.00 13.04 ?  64  GLU   A OE1  1 
ATOM   1520 O OE2  . GLU   A 1 64  ? 34.945 3.344   9.862   1.00 12.83 -1 64  GLU   A OE2  1 
ATOM   1521 H H    . GLU   A 1 64  ? 33.810 8.743   7.661   1.00 12.83 ?  64  GLU   A H    1 
ATOM   1522 H HA   . GLU   A 1 64  ? 36.195 7.698   7.600   1.00 12.88 ?  64  GLU   A HA   1 
ATOM   1523 H HB2  . GLU   A 1 64  ? 34.634 7.029   9.176   1.00 13.43 ?  64  GLU   A HB2  1 
ATOM   1524 H HB3  . GLU   A 1 64  ? 33.689 6.464   8.032   1.00 13.43 ?  64  GLU   A HB3  1 
ATOM   1525 H HG2  . GLU   A 1 64  ? 35.450 4.870   7.566   1.00 14.07 ?  64  GLU   A HG2  1 
ATOM   1526 H HG3  . GLU   A 1 64  ? 36.086 5.334   8.944   1.00 14.07 ?  64  GLU   A HG3  1 
ATOM   1527 N N    . SER   A 1 65  ? 34.263 6.801   5.200   1.00 10.18 ?  65  SER   A N    1 
ATOM   1528 C CA   . SER   A 1 65  ? 34.209 6.144   3.900   1.00 10.06 ?  65  SER   A CA   1 
ATOM   1529 C C    . SER   A 1 65  ? 35.126 6.817   2.891   1.00 10.36 ?  65  SER   A C    1 
ATOM   1530 O O    . SER   A 1 65  ? 35.763 6.140   2.078   1.00 11.19 ?  65  SER   A O    1 
ATOM   1531 C CB   . SER   A 1 65  ? 32.775 6.152   3.370   1.00 10.15 ?  65  SER   A CB   1 
ATOM   1532 O OG   . SER   A 1 65  ? 31.923 5.341   4.164   1.00 10.62 ?  65  SER   A OG   1 
ATOM   1533 H H    . SER   A 1 65  ? 33.528 7.173   5.437   1.00 12.20 ?  65  SER   A H    1 
ATOM   1534 H HA   . SER   A 1 65  ? 34.496 5.225   3.993   1.00 12.06 ?  65  SER   A HA   1 
ATOM   1535 H HB2  . SER   A 1 65  ? 32.441 7.062   3.382   1.00 12.17 ?  65  SER   A HB2  1 
ATOM   1536 H HB3  . SER   A 1 65  ? 32.779 5.814   2.462   1.00 12.17 ?  65  SER   A HB3  1 
ATOM   1537 H HG   . SER   A 1 65  ? 31.917 5.622   4.958   1.00 12.73 ?  65  SER   A HG   1 
ATOM   1538 N N    . ASP   A 1 66  ? 35.194 8.151   2.913   1.00 10.44 ?  66  ASP   A N    1 
ATOM   1539 C CA   . ASP   A 1 66  ? 36.048 8.855   1.962   1.00 11.35 ?  66  ASP   A CA   1 
ATOM   1540 C C    . ASP   A 1 66  ? 37.514 8.504   2.189   1.00 11.49 ?  66  ASP   A C    1 
ATOM   1541 O O    . ASP   A 1 66  ? 38.278 8.334   1.232   1.00 12.34 ?  66  ASP   A O    1 
ATOM   1542 C CB   . ASP   A 1 66  ? 35.827 10.361  2.074   1.00 12.55 ?  66  ASP   A CB   1 
ATOM   1543 C CG   . ASP   A 1 66  ? 34.484 10.824  1.476   1.00 13.99 ?  66  ASP   A CG   1 
ATOM   1544 O OD1  . ASP   A 1 66  ? 33.775 10.026  0.824   1.00 14.05 ?  66  ASP   A OD1  1 
ATOM   1545 O OD2  . ASP   A 1 66  ? 34.171 12.017  1.643   1.00 16.96 -1 66  ASP   A OD2  1 
ATOM   1546 H H    . ASP   A 1 66  ? 34.755 8.665   3.451   1.00 12.52 ?  66  ASP   A H    1 
ATOM   1547 H HA   . ASP   A 1 66  ? 35.809 8.585   1.061   1.00 13.61 ?  66  ASP   A HA   1 
ATOM   1548 H HB2  . ASP   A 1 66  ? 35.838 10.611  3.013   1.00 15.05 ?  66  ASP   A HB2  1 
ATOM   1549 H HB3  . ASP   A 1 66  ? 36.544 10.819  1.605   1.00 15.05 ?  66  ASP   A HB3  1 
ATOM   1550 N N    . ASP   A 1 67  ? 37.920 8.370   3.451   1.00 11.54 ?  67  ASP   A N    1 
ATOM   1551 C CA   . ASP   A 1 67  ? 39.275 7.919   3.743   1.00 12.20 ?  67  ASP   A CA   1 
ATOM   1552 C C    . ASP   A 1 67  ? 39.496 6.486   3.270   1.00 12.16 ?  67  ASP   A C    1 
ATOM   1553 O O    . ASP   A 1 67  ? 40.555 6.163   2.722   1.00 12.74 ?  67  ASP   A O    1 
ATOM   1554 C CB   . ASP   A 1 67  ? 39.544 8.043   5.238   1.00 13.77 ?  67  ASP   A CB   1 
ATOM   1555 C CG   . ASP   A 1 67  ? 40.847 7.388   5.652   1.00 14.92 ?  67  ASP   A CG   1 
ATOM   1556 O OD1  . ASP   A 1 67  ? 41.915 8.024   5.504   1.00 17.44 ?  67  ASP   A OD1  1 
ATOM   1557 O OD2  . ASP   A 1 67  ? 40.791 6.226   6.118   1.00 14.55 -1 67  ASP   A OD2  1 
ATOM   1558 H H    . ASP   A 1 67  ? 37.439 8.532   4.141   1.00 13.84 ?  67  ASP   A H    1 
ATOM   1559 H HA   . ASP   A 1 67  ? 39.905 8.485   3.270   1.00 14.64 ?  67  ASP   A HA   1 
ATOM   1560 H HB2  . ASP   A 1 67  ? 39.592 8.980   5.466   1.00 16.51 ?  67  ASP   A HB2  1 
ATOM   1561 H HB3  . ASP   A 1 67  ? 38.820 7.614   5.721   1.00 16.51 ?  67  ASP   A HB3  1 
ATOM   1562 N N    . TYR   A 1 68  ? 38.508 5.606   3.471   1.00 11.69 ?  68  TYR   A N    1 
ATOM   1563 C CA   . TYR   A 1 68  ? 38.630 4.229   2.991   1.00 11.79 ?  68  TYR   A CA   1 
ATOM   1564 C C    . TYR   A 1 68  ? 38.865 4.190   1.481   1.00 11.62 ?  68  TYR   A C    1 
ATOM   1565 O O    . TYR   A 1 68  ? 39.736 3.455   0.997   1.00 12.10 ?  68  TYR   A O    1 
ATOM   1566 C CB   . TYR   A 1 68  ? 37.381 3.404   3.377   1.00 12.25 ?  68  TYR   A CB   1 
ATOM   1567 C CG   . TYR   A 1 68  ? 37.402 2.023   2.745   1.00 13.74 ?  68  TYR   A CG   1 
ATOM   1568 C CD1  . TYR   A 1 68  ? 36.945 1.837   1.443   1.00 15.01 ?  68  TYR   A CD1  1 
ATOM   1569 C CD2  . TYR   A 1 68  ? 37.939 0.933   3.408   1.00 15.15 ?  68  TYR   A CD2  1 
ATOM   1570 C CE1  . TYR   A 1 68  ? 37.010 0.618   0.822   1.00 16.07 ?  68  TYR   A CE1  1 
ATOM   1571 C CE2  . TYR   A 1 68  ? 37.994 -0.326  2.789   1.00 15.69 ?  68  TYR   A CE2  1 
ATOM   1572 C CZ   . TYR   A 1 68  ? 37.542 -0.452  1.493   1.00 16.29 ?  68  TYR   A CZ   1 
ATOM   1573 O OH   . TYR   A 1 68  ? 37.624 -1.663  0.862   1.00 17.21 ?  68  TYR   A OH   1 
ATOM   1574 H H    . TYR   A 1 68  ? 37.769 5.775   3.880   1.00 14.02 ?  68  TYR   A H    1 
ATOM   1575 H HA   . TYR   A 1 68  ? 39.394 3.815   3.417   1.00 14.14 ?  68  TYR   A HA   1 
ATOM   1576 H HB2  . TYR   A 1 68  ? 37.356 3.290   4.340   1.00 14.69 ?  68  TYR   A HB2  1 
ATOM   1577 H HB3  . TYR   A 1 68  ? 36.583 3.862   3.072   1.00 14.69 ?  68  TYR   A HB3  1 
ATOM   1578 H HD1  . TYR   A 1 68  ? 36.602 2.566   0.977   1.00 18.01 ?  68  TYR   A HD1  1 
ATOM   1579 H HD2  . TYR   A 1 68  ? 38.266 1.029   4.270   1.00 18.16 ?  68  TYR   A HD2  1 
ATOM   1580 H HE1  . TYR   A 1 68  ? 36.694 0.524   -0.048  1.00 19.27 ?  68  TYR   A HE1  1 
ATOM   1581 H HE2  . TYR   A 1 68  ? 38.362 -1.059  3.228   1.00 18.82 ?  68  TYR   A HE2  1 
ATOM   1582 H HH   . TYR   A 1 68  ? 37.951 -2.237  1.386   1.00 20.65 ?  68  TYR   A HH   1 
ATOM   1583 N N    . ILE   A 1 69  ? 38.073 4.951   0.714   1.00 11.20 ?  69  ILE   A N    1 
ATOM   1584 C CA   . ILE   A 1 69  ? 38.205 4.936   -0.743  1.00 11.29 ?  69  ILE   A CA   1 
ATOM   1585 C C    . ILE   A 1 69  ? 39.534 5.549   -1.175  1.00 11.19 ?  69  ILE   A C    1 
ATOM   1586 O O    . ILE   A 1 69  ? 40.178 5.069   -2.115  1.00 11.68 ?  69  ILE   A O    1 
ATOM   1587 C CB   . ILE   A 1 69  ? 37.006 5.643   -1.409  1.00 12.29 ?  69  ILE   A CB   1 
ATOM   1588 C CG1  . ILE   A 1 69  ? 35.691 4.911   -1.134  1.00 12.75 ?  69  ILE   A CG1  1 
ATOM   1589 C CG2  . ILE   A 1 69  ? 37.243 5.830   -2.918  1.00 13.69 ?  69  ILE   A CG2  1 
ATOM   1590 C CD1  . ILE   A 1 69  ? 35.525 3.620   -1.902  1.00 13.48 ?  69  ILE   A CD1  1 
ATOM   1591 H H    . ILE   A 1 69  ? 37.466 5.480   1.011   1.00 13.43 ?  69  ILE   A H    1 
ATOM   1592 H HA   . ILE   A 1 69  ? 38.204 4.012   -1.040  1.00 13.54 ?  69  ILE   A HA   1 
ATOM   1593 H HB   . ILE   A 1 69  ? 36.935 6.523   -1.018  1.00 14.74 ?  69  ILE   A HB   1 
ATOM   1594 H HG12 . ILE   A 1 69  ? 35.646 4.700   -0.188  1.00 15.29 ?  69  ILE   A HG12 1 
ATOM   1595 H HG13 . ILE   A 1 69  ? 34.956 5.495   -1.375  1.00 15.29 ?  69  ILE   A HG13 1 
ATOM   1596 H HG21 . ILE   A 1 69  ? 36.396 6.040   -3.347  1.00 16.42 ?  69  ILE   A HG21 1 
ATOM   1597 H HG22 . ILE   A 1 69  ? 37.865 6.566   -3.054  1.00 16.42 ?  69  ILE   A HG22 1 
ATOM   1598 H HG23 . ILE   A 1 69  ? 37.608 5.015   -3.291  1.00 16.42 ?  69  ILE   A HG23 1 
ATOM   1599 H HD11 . ILE   A 1 69  ? 34.730 3.166   -1.585  1.00 16.16 ?  69  ILE   A HD11 1 
ATOM   1600 H HD12 . ILE   A 1 69  ? 35.434 3.821   -2.847  1.00 16.16 ?  69  ILE   A HD12 1 
ATOM   1601 H HD13 . ILE   A 1 69  ? 36.304 3.061   -1.757  1.00 16.16 ?  69  ILE   A HD13 1 
ATOM   1602 N N    . ALA   A 1 70  ? 39.951 6.630   -0.519  1.00 11.63 ?  70  ALA   A N    1 
ATOM   1603 C CA   . ALA   A 1 70  ? 41.225 7.244   -0.872  1.00 12.44 ?  70  ALA   A CA   1 
ATOM   1604 C C    . ALA   A 1 70  ? 42.375 6.258   -0.710  1.00 12.67 ?  70  ALA   A C    1 
ATOM   1605 O O    . ALA   A 1 70  ? 43.340 6.294   -1.478  1.00 14.71 ?  70  ALA   A O    1 
ATOM   1606 C CB   . ALA   A 1 70  ? 41.464 8.487   -0.014  1.00 13.05 ?  70  ALA   A CB   1 
ATOM   1607 H H    . ALA   A 1 70  ? 39.520 7.017   0.114   1.00 13.95 ?  70  ALA   A H    1 
ATOM   1608 H HA   . ALA   A 1 70  ? 41.194 7.526   -1.800  1.00 14.91 ?  70  ALA   A HA   1 
ATOM   1609 H HB1  . ALA   A 1 70  ? 42.320 8.879   -0.260  1.00 15.65 ?  70  ALA   A HB1  1 
ATOM   1610 H HB2  . ALA   A 1 70  ? 40.752 9.123   -0.165  1.00 15.65 ?  70  ALA   A HB2  1 
ATOM   1611 H HB3  . ALA   A 1 70  ? 41.484 8.224   0.922   1.00 15.65 ?  70  ALA   A HB3  1 
ATOM   1612 N N    . THR   A 1 71  ? 42.280 5.357   0.266   1.00 12.17 ?  71  THR   A N    1 
ATOM   1613 C CA   . THR   A 1 71  ? 43.336 4.381   0.510   1.00 13.70 ?  71  THR   A CA   1 
ATOM   1614 C C    . THR   A 1 71  ? 43.214 3.158   -0.387  1.00 13.74 ?  71  THR   A C    1 
ATOM   1615 O O    . THR   A 1 71  ? 44.225 2.652   -0.893  1.00 15.58 ?  71  THR   A O    1 
ATOM   1616 C CB   . THR   A 1 71  ? 43.275 3.931   1.966   1.00 15.60 ?  71  THR   A CB   1 
ATOM   1617 O OG1  . THR   A 1 71  ? 43.532 5.054   2.814   1.00 16.95 ?  71  THR   A OG1  1 
ATOM   1618 C CG2  . THR   A 1 71  ? 44.284 2.815   2.245   1.00 17.24 ?  71  THR   A CG2  1 
ATOM   1619 H H    . THR   A 1 71  ? 41.609 5.281   0.795   1.00 14.60 ?  71  THR   A H    1 
ATOM   1620 H HA   . THR   A 1 71  ? 44.200 4.786   0.345   1.00 16.43 ?  71  THR   A HA   1 
ATOM   1621 H HB   . THR   A 1 71  ? 42.388 3.580   2.149   1.00 18.71 ?  71  THR   A HB   1 
ATOM   1622 H HG1  . THR   A 1 71  ? 42.950 5.642   2.680   1.00 20.33 ?  71  THR   A HG1  1 
ATOM   1623 H HG21 . THR   A 1 71  ? 44.429 2.735   3.201   1.00 20.68 ?  71  THR   A HG21 1 
ATOM   1624 H HG22 . THR   A 1 71  ? 43.958 1.967   1.906   1.00 20.68 ?  71  THR   A HG22 1 
ATOM   1625 H HG23 . THR   A 1 71  ? 45.133 3.020   1.818   1.00 20.68 ?  71  THR   A HG23 1 
ATOM   1626 N N    . ASN   A 1 72  ? 41.992 2.651   -0.572  1.00 12.98 ?  72  ASN   A N    1 
ATOM   1627 C CA   . ASN   A 1 72  ? 41.774 1.326   -1.134  1.00 13.13 ?  72  ASN   A CA   1 
ATOM   1628 C C    . ASN   A 1 72  ? 41.145 1.317   -2.514  1.00 13.39 ?  72  ASN   A C    1 
ATOM   1629 O O    . ASN   A 1 72  ? 41.154 0.263   -3.163  1.00 14.47 ?  72  ASN   A O    1 
ATOM   1630 C CB   . ASN   A 1 72  ? 40.887 0.504   -0.191  1.00 13.90 ?  72  ASN   A CB   1 
ATOM   1631 C CG   . ASN   A 1 72  ? 41.506 0.344   1.170   1.00 14.71 ?  72  ASN   A CG   1 
ATOM   1632 O OD1  . ASN   A 1 72  ? 41.054 0.945   2.144   1.00 16.55 ?  72  ASN   A OD1  1 
ATOM   1633 N ND2  . ASN   A 1 72  ? 42.560 -0.441  1.246   1.00 15.58 ?  72  ASN   A ND2  1 
ATOM   1634 H H    . ASN   A 1 72  ? 41.259 3.068   -0.380  1.00 15.57 ?  72  ASN   A H    1 
ATOM   1635 H HA   . ASN   A 1 72  ? 42.624 0.875   -1.208  1.00 15.75 ?  72  ASN   A HA   1 
ATOM   1636 H HB2  . ASN   A 1 72  ? 40.032 0.951   -0.088  1.00 16.67 ?  72  ASN   A HB2  1 
ATOM   1637 H HB3  . ASN   A 1 72  ? 40.758 -0.381  -0.568  1.00 16.67 ?  72  ASN   A HB3  1 
ATOM   1638 H HD21 . ASN   A 1 72  ? 42.955 -0.553  2.002   1.00 18.69 ?  72  ASN   A HD21 1 
ATOM   1639 H HD22 . ASN   A 1 72  ? 42.855 -0.833  0.542   1.00 18.69 ?  72  ASN   A HD22 1 
ATOM   1640 N N    . GLY   A 1 73  ? 40.592 2.431   -2.973  1.00 12.84 ?  73  GLY   A N    1 
ATOM   1641 C CA   . GLY   A 1 73  ? 39.853 2.450   -4.209  1.00 12.58 ?  73  GLY   A CA   1 
ATOM   1642 C C    . GLY   A 1 73  ? 38.462 1.870   -4.038  1.00 12.16 ?  73  GLY   A C    1 
ATOM   1643 O O    . GLY   A 1 73  ? 38.078 1.410   -2.955  1.00 12.58 ?  73  GLY   A O    1 
ATOM   1644 H H    . GLY   A 1 73  ? 40.631 3.203   -2.584  1.00 15.39 ?  73  GLY   A H    1 
ATOM   1645 H HA2  . GLY   A 1 73  ? 39.772 3.365   -4.530  1.00 15.08 ?  73  GLY   A HA2  1 
ATOM   1646 H HA3  . GLY   A 1 73  ? 40.325 1.932   -4.882  1.00 15.08 ?  73  GLY   A HA3  1 
ATOM   1647 N N    . PRO   A 1 74  ? 37.680 1.891   -5.116  1.00 12.45 ?  74  PRO   A N    1 
ATOM   1648 C CA   . PRO   A 1 74  ? 36.285 1.449   -5.029  1.00 12.35 ?  74  PRO   A CA   1 
ATOM   1649 C C    . PRO   A 1 74  ? 36.146 -0.034  -4.714  1.00 11.58 ?  74  PRO   A C    1 
ATOM   1650 O O    . PRO   A 1 74  ? 37.016 -0.861  -5.008  1.00 12.61 ?  74  PRO   A O    1 
ATOM   1651 C CB   . PRO   A 1 74  ? 35.727 1.755   -6.425  1.00 13.83 ?  74  PRO   A CB   1 
ATOM   1652 C CG   . PRO   A 1 74  ? 36.663 2.758   -7.021  1.00 16.59 ?  74  PRO   A CG   1 
ATOM   1653 C CD   . PRO   A 1 74  ? 38.009 2.424   -6.449  1.00 14.43 ?  74  PRO   A CD   1 
ATOM   1654 H HA   . PRO   A 1 74  ? 35.801 1.972   -4.367  1.00 14.81 ?  74  PRO   A HA   1 
ATOM   1655 H HB2  . PRO   A 1 74  ? 35.704 0.945   -6.955  1.00 16.59 ?  74  PRO   A HB2  1 
ATOM   1656 H HB3  . PRO   A 1 74  ? 34.830 2.132   -6.344  1.00 16.59 ?  74  PRO   A HB3  1 
ATOM   1657 H HG2  . PRO   A 1 74  ? 36.668 2.666   -7.986  1.00 19.90 ?  74  PRO   A HG2  1 
ATOM   1658 H HG3  . PRO   A 1 74  ? 36.393 3.652   -6.762  1.00 19.90 ?  74  PRO   A HG3  1 
ATOM   1659 H HD2  . PRO   A 1 74  ? 38.450 1.748   -6.988  1.00 17.31 ?  74  PRO   A HD2  1 
ATOM   1660 H HD3  . PRO   A 1 74  ? 38.548 3.229   -6.379  1.00 17.31 ?  74  PRO   A HD3  1 
ATOM   1661 N N    . LEU   A 1 75  ? 35.008 -0.362  -4.116  1.00 11.13 ?  75  LEU   A N    1 
ATOM   1662 C CA   . LEU   A 1 75  ? 34.605 -1.749  -3.967  1.00 10.77 ?  75  LEU   A CA   1 
ATOM   1663 C C    . LEU   A 1 75  ? 34.218 -2.329  -5.326  1.00 11.42 ?  75  LEU   A C    1 
ATOM   1664 O O    . LEU   A 1 75  ? 34.092 -1.616  -6.325  1.00 13.03 ?  75  LEU   A O    1 
ATOM   1665 C CB   . LEU   A 1 75  ? 33.415 -1.864  -3.013  1.00 10.78 ?  75  LEU   A CB   1 
ATOM   1666 C CG   . LEU   A 1 75  ? 33.637 -1.451  -1.562  1.00 12.65 ?  75  LEU   A CG   1 
ATOM   1667 C CD1  . LEU   A 1 75  ? 32.346 -1.615  -0.767  1.00 14.53 ?  75  LEU   A CD1  1 
ATOM   1668 C CD2  . LEU   A 1 75  ? 34.763 -2.206  -0.909  1.00 15.69 ?  75  LEU   A CD2  1 
ATOM   1669 H H    . LEU   A 1 75  ? 34.446 0.206   -3.790  1.00 13.35 ?  75  LEU   A H    1 
ATOM   1670 H HA   . LEU   A 1 75  ? 35.343 -2.261  -3.614  1.00 12.92 ?  75  LEU   A HA   1 
ATOM   1671 H HB2  . LEU   A 1 75  ? 32.697 -1.313  -3.359  1.00 12.92 ?  75  LEU   A HB2  1 
ATOM   1672 H HB3  . LEU   A 1 75  ? 33.131 -2.792  -3.005  1.00 12.92 ?  75  LEU   A HB3  1 
ATOM   1673 H HG   . LEU   A 1 75  ? 33.878 -0.511  -1.547  1.00 15.17 ?  75  LEU   A HG   1 
ATOM   1674 H HD11 . LEU   A 1 75  ? 32.508 -1.345  0.151   1.00 17.43 ?  75  LEU   A HD11 1 
ATOM   1675 H HD12 . LEU   A 1 75  ? 31.665 -1.049  -1.163  1.00 17.43 ?  75  LEU   A HD12 1 
ATOM   1676 H HD13 . LEU   A 1 75  ? 32.073 -2.541  -0.799  1.00 17.43 ?  75  LEU   A HD13 1 
ATOM   1677 H HD21 . LEU   A 1 75  ? 34.821 -1.945  0.024   1.00 18.82 ?  75  LEU   A HD21 1 
ATOM   1678 H HD22 . LEU   A 1 75  ? 34.591 -3.157  -0.978  1.00 18.82 ?  75  LEU   A HD22 1 
ATOM   1679 H HD23 . LEU   A 1 75  ? 35.599 -1.990  -1.360  1.00 18.82 ?  75  LEU   A HD23 1 
ATOM   1680 N N    . LYS   A 1 76  ? 34.043 -3.649  -5.347  1.00 11.85 ?  76  LYS   A N    1 
ATOM   1681 C CA   . LYS   A 1 76  ? 33.444 -4.364  -6.468  1.00 12.41 ?  76  LYS   A CA   1 
ATOM   1682 C C    . LYS   A 1 76  ? 31.932 -4.443  -6.276  1.00 11.19 ?  76  LYS   A C    1 
ATOM   1683 O O    . LYS   A 1 76  ? 31.449 -4.569  -5.154  1.00 10.91 ?  76  LYS   A O    1 
ATOM   1684 C CB   . LYS   A 1 76  ? 33.984 -5.804  -6.519  1.00 13.93 ?  76  LYS   A CB   1 
ATOM   1685 C CG   . LYS   A 1 76  ? 35.492 -5.914  -6.720  1.00 15.42 ?  76  LYS   A CG   1 
ATOM   1686 C CD   . LYS   A 1 76  ? 36.009 -7.321  -6.528  1.00 16.72 ?  76  LYS   A CD   1 
ATOM   1687 C CE   . LYS   A 1 76  ? 37.510 -7.385  -6.724  1.00 19.04 ?  76  LYS   A CE   1 
ATOM   1688 N NZ   . LYS   A 1 76  ? 38.043 -8.745  -6.506  1.00 19.98 ?  76  LYS   A NZ   1 
ATOM   1689 H H    . LYS   A 1 76  ? 34.272 -4.167  -4.699  1.00 14.21 ?  76  LYS   A H    1 
ATOM   1690 H HA   . LYS   A 1 76  ? 33.643 -3.915  -7.306  1.00 14.88 ?  76  LYS   A HA   1 
ATOM   1691 H HB2  . LYS   A 1 76  ? 33.765 -6.245  -5.684  1.00 16.71 ?  76  LYS   A HB2  1 
ATOM   1692 H HB3  . LYS   A 1 76  ? 33.554 -6.267  -7.256  1.00 16.71 ?  76  LYS   A HB3  1 
ATOM   1693 H HG2  . LYS   A 1 76  ? 35.712 -5.633  -7.624  1.00 18.49 ?  76  LYS   A HG2  1 
ATOM   1694 H HG3  . LYS   A 1 76  ? 35.939 -5.340  -6.078  1.00 18.49 ?  76  LYS   A HG3  1 
ATOM   1695 H HD2  . LYS   A 1 76  ? 35.803 -7.621  -5.628  1.00 20.05 ?  76  LYS   A HD2  1 
ATOM   1696 H HD3  . LYS   A 1 76  ? 35.590 -7.910  -7.180  1.00 20.05 ?  76  LYS   A HD3  1 
ATOM   1697 H HE2  . LYS   A 1 76  ? 37.723 -7.120  -7.631  1.00 22.84 ?  76  LYS   A HE2  1 
ATOM   1698 H HE3  . LYS   A 1 76  ? 37.937 -6.791  -6.090  1.00 22.84 ?  76  LYS   A HE3  1 
ATOM   1699 H HZ1  . LYS   A 1 76  ? 38.923 -8.757  -6.628  1.00 23.97 ?  76  LYS   A HZ1  1 
ATOM   1700 H HZ2  . LYS   A 1 76  ? 37.862 -9.020  -5.677  1.00 23.97 ?  76  LYS   A HZ2  1 
ATOM   1701 H HZ3  . LYS   A 1 76  ? 37.667 -9.319  -7.082  1.00 23.97 ?  76  LYS   A HZ3  1 
ATOM   1702 N N    . VAL   A 1 77  ? 31.181 -4.411  -7.380  1.00 11.61 ?  77  VAL   A N    1 
ATOM   1703 C CA   . VAL   A 1 77  ? 29.774 -4.798  -7.294  1.00 11.55 ?  77  VAL   A CA   1 
ATOM   1704 C C    . VAL   A 1 77  ? 29.707 -6.250  -6.848  1.00 10.94 ?  77  VAL   A C    1 
ATOM   1705 O O    . VAL   A 1 77  ? 30.371 -7.118  -7.422  1.00 11.31 ?  77  VAL   A O    1 
ATOM   1706 C CB   . VAL   A 1 77  ? 29.052 -4.584  -8.632  1.00 12.76 ?  77  VAL   A CB   1 
ATOM   1707 C CG1  . VAL   A 1 77  ? 27.601 -5.022  -8.517  1.00 13.58 ?  77  VAL   A CG1  1 
ATOM   1708 C CG2  . VAL   A 1 77  ? 29.133 -3.129  -9.059  1.00 14.21 ?  77  VAL   A CG2  1 
ATOM   1709 H H    . VAL   A 1 77  ? 31.458 -4.173  -8.158  1.00 13.92 ?  77  VAL   A H    1 
ATOM   1710 H HA   . VAL   A 1 77  ? 29.339 -4.254  -6.623  1.00 13.85 ?  77  VAL   A HA   1 
ATOM   1711 H HB   . VAL   A 1 77  ? 29.483 -5.122  -9.316  1.00 15.30 ?  77  VAL   A HB   1 
ATOM   1712 H HG11 . VAL   A 1 77  ? 27.128 -4.729  -9.307  1.00 16.29 ?  77  VAL   A HG11 1 
ATOM   1713 H HG12 . VAL   A 1 77  ? 27.569 -5.988  -8.446  1.00 16.29 ?  77  VAL   A HG12 1 
ATOM   1714 H HG13 . VAL   A 1 77  ? 27.216 -4.615  -7.725  1.00 16.29 ?  77  VAL   A HG13 1 
ATOM   1715 H HG21 . VAL   A 1 77  ? 28.698 -3.033  -9.920  1.00 17.04 ?  77  VAL   A HG21 1 
ATOM   1716 H HG22 . VAL   A 1 77  ? 28.681 -2.583  -8.397  1.00 17.04 ?  77  VAL   A HG22 1 
ATOM   1717 H HG23 . VAL   A 1 77  ? 30.063 -2.867  -9.128  1.00 17.04 ?  77  VAL   A HG23 1 
ATOM   1718 N N    . GLY   A 1 78  ? 28.919 -6.521  -5.805  1.00 10.76 ?  78  GLY   A N    1 
ATOM   1719 C CA   . GLY   A 1 78  ? 28.902 -7.812  -5.150  1.00 10.93 ?  78  GLY   A CA   1 
ATOM   1720 C C    . GLY   A 1 78  ? 29.826 -7.912  -3.957  1.00 10.47 ?  78  GLY   A C    1 
ATOM   1721 O O    . GLY   A 1 78  ? 29.766 -8.917  -3.232  1.00 10.92 ?  78  GLY   A O    1 
ATOM   1722 H H    . GLY   A 1 78  ? 28.369 -5.952  -5.462  1.00 12.90 ?  78  GLY   A H    1 
ATOM   1723 H HA2  . GLY   A 1 78  ? 28.001 -8.001  -4.851  1.00 13.11 ?  78  GLY   A HA2  1 
ATOM   1724 H HA3  . GLY   A 1 78  ? 29.159 -8.493  -5.790  1.00 13.11 ?  78  GLY   A HA3  1 
ATOM   1725 N N    . GLY   A 1 79  ? 30.677 -6.908  -3.732  1.00 10.44 ?  79  GLY   A N    1 
ATOM   1726 C CA   . GLY   A 1 79  ? 31.640 -6.921  -2.654  1.00 10.89 ?  79  GLY   A CA   1 
ATOM   1727 C C    . GLY   A 1 79  ? 31.193 -6.128  -1.438  1.00 10.08 ?  79  GLY   A C    1 
ATOM   1728 O O    . GLY   A 1 79  ? 30.069 -5.624  -1.356  1.00 10.63 ?  79  GLY   A O    1 
ATOM   1729 H H    . GLY   A 1 79  ? 30.716 -6.193  -4.210  1.00 12.51 ?  79  GLY   A H    1 
ATOM   1730 H HA2  . GLY   A 1 79  ? 31.798 -7.846  -2.380  1.00 13.06 ?  79  GLY   A HA2  1 
ATOM   1731 H HA3  . GLY   A 1 79  ? 32.480 -6.556  -2.964  1.00 13.06 ?  79  GLY   A HA3  1 
ATOM   1732 N N    . SER   A 1 80  ? 32.103 -6.030  -0.471  1.00 10.86 ?  80  SER   A N    1 
ATOM   1733 C CA   . SER   A 1 80  ? 31.789 -5.405  0.802   1.00 10.33 ?  80  SER   A CA   1 
ATOM   1734 C C    . SER   A 1 80  ? 33.062 -4.955  1.497   1.00 10.37 ?  80  SER   A C    1 
ATOM   1735 O O    . SER   A 1 80  ? 34.176 -5.376  1.160   1.00 11.87 ?  80  SER   A O    1 
ATOM   1736 C CB   . SER   A 1 80  ? 31.039 -6.372  1.725   1.00 11.27 ?  80  SER   A CB   1 
ATOM   1737 O OG   . SER   A 1 80  ? 31.878 -7.420  2.197   1.00 12.89 ?  80  SER   A OG   1 
ATOM   1738 H H    . SER   A 1 80  ? 32.915 -6.301  -0.538  1.00 13.03 ?  80  SER   A H    1 
ATOM   1739 H HA   . SER   A 1 80  ? 31.230 -4.628  0.637   1.00 12.38 ?  80  SER   A HA   1 
ATOM   1740 H HB2  . SER   A 1 80  ? 30.700 -5.878  2.486   1.00 13.51 ?  80  SER   A HB2  1 
ATOM   1741 H HB3  . SER   A 1 80  ? 30.302 -6.764  1.231   1.00 13.51 ?  80  SER   A HB3  1 
ATOM   1742 H HG   . SER   A 1 80  ? 32.184 -7.853  1.543   1.00 15.46 ?  80  SER   A HG   1 
ATOM   1743 N N    . CYS   A 1 81  ? 32.870 -4.111  2.508   1.00 9.92  ?  81  CYS   A N    1 
ATOM   1744 C CA   . CYS   A 1 81  ? 33.925 -3.827  3.467   1.00 10.19 ?  81  CYS   A CA   1 
ATOM   1745 C C    . CYS   A 1 81  ? 33.289 -3.592  4.827   1.00 10.13 ?  81  CYS   A C    1 
ATOM   1746 O O    . CYS   A 1 81  ? 32.126 -3.189  4.922   1.00 11.18 ?  81  CYS   A O    1 
ATOM   1747 C CB   . CYS   A 1 81  ? 34.801 -2.640  3.044   1.00 11.10 ?  81  CYS   A CB   1 
ATOM   1748 S SG   . CYS   A 1 81  ? 33.903 -1.060  3.070   1.00 11.04 ?  81  CYS   A SG   1 
ATOM   1749 H H    . CYS   A 1 81  ? 32.132 -3.690  2.662   1.00 11.90 ?  81  CYS   A H    1 
ATOM   1750 H HA   . CYS   A 1 81  ? 34.500 -4.601  3.535   1.00 12.21 ?  81  CYS   A HA   1 
ATOM   1751 H HB2  . CYS   A 1 81  ? 35.556 -2.570  3.650   1.00 13.31 ?  81  CYS   A HB2  1 
ATOM   1752 H HB3  . CYS   A 1 81  ? 35.121 -2.789  2.137   1.00 13.31 ?  81  CYS   A HB3  1 
ATOM   1753 H HG   . CYS   A 1 81  ? 34.648 -0.180  2.730   1.00 13.24 ?  81  CYS   A HG   1 
ATOM   1754 N N    . VAL   A 1 82  ? 34.064 -3.851  5.877   1.00 10.41 ?  82  VAL   A N    1 
ATOM   1755 C CA   . VAL   A 1 82  ? 33.646 -3.615  7.251   1.00 10.91 ?  82  VAL   A CA   1 
ATOM   1756 C C    . VAL   A 1 82  ? 34.247 -2.302  7.721   1.00 11.01 ?  82  VAL   A C    1 
ATOM   1757 O O    . VAL   A 1 82  ? 35.471 -2.128  7.699   1.00 11.74 ?  82  VAL   A O    1 
ATOM   1758 C CB   . VAL   A 1 82  ? 34.071 -4.758  8.184   1.00 12.05 ?  82  VAL   A CB   1 
ATOM   1759 C CG1  . VAL   A 1 82  ? 33.614 -4.465  9.606   1.00 13.64 ?  82  VAL   A CG1  1 
ATOM   1760 C CG2  . VAL   A 1 82  ? 33.515 -6.089  7.707   1.00 13.00 ?  82  VAL   A CG2  1 
ATOM   1761 H H    . VAL   A 1 82  ? 34.861 -4.178  5.814   1.00 12.48 ?  82  VAL   A H    1 
ATOM   1762 H HA   . VAL   A 1 82  ? 32.679 -3.538  7.283   1.00 13.08 ?  82  VAL   A HA   1 
ATOM   1763 H HB   . VAL   A 1 82  ? 35.039 -4.816  8.191   1.00 14.45 ?  82  VAL   A HB   1 
ATOM   1764 H HG11 . VAL   A 1 82  ? 33.698 -5.272  10.138  1.00 16.35 ?  82  VAL   A HG11 1 
ATOM   1765 H HG12 . VAL   A 1 82  ? 34.164 -3.762  9.986   1.00 16.35 ?  82  VAL   A HG12 1 
ATOM   1766 H HG13 . VAL   A 1 82  ? 32.683 -4.182  9.589   1.00 16.35 ?  82  VAL   A HG13 1 
ATOM   1767 H HG21 . VAL   A 1 82  ? 33.770 -6.780  8.338   1.00 15.60 ?  82  VAL   A HG21 1 
ATOM   1768 H HG22 . VAL   A 1 82  ? 32.548 -6.026  7.657   1.00 15.60 ?  82  VAL   A HG22 1 
ATOM   1769 H HG23 . VAL   A 1 82  ? 33.881 -6.287  6.832   1.00 15.60 ?  82  VAL   A HG23 1 
ATOM   1770 N N    . LEU   A 1 83  ? 33.390 -1.383  8.152   1.00 10.47 ?  83  LEU   A N    1 
ATOM   1771 C CA   . LEU   A 1 83  ? 33.807 -0.117  8.731   1.00 10.50 ?  83  LEU   A CA   1 
ATOM   1772 C C    . LEU   A 1 83  ? 33.093 0.059   10.067  1.00 10.51 ?  83  LEU   A C    1 
ATOM   1773 O O    . LEU   A 1 83  ? 32.383 -0.837  10.536  1.00 11.04 ?  83  LEU   A O    1 
ATOM   1774 C CB   . LEU   A 1 83  ? 33.553 1.039   7.750   1.00 11.10 ?  83  LEU   A CB   1 
ATOM   1775 C CG   . LEU   A 1 83  ? 34.455 1.041   6.508   1.00 11.89 ?  83  LEU   A CG   1 
ATOM   1776 C CD1  . LEU   A 1 83  ? 34.013 2.083   5.504   1.00 12.35 ?  83  LEU   A CD1  1 
ATOM   1777 C CD2  . LEU   A 1 83  ? 35.922 1.255   6.884   1.00 12.67 ?  83  LEU   A CD2  1 
ATOM   1778 H H    . LEU   A 1 83  ? 32.533 -1.473  8.110   1.00 12.56 ?  83  LEU   A H    1 
ATOM   1779 H HA   . LEU   A 1 83  ? 34.759 -0.148  8.903   1.00 12.59 ?  83  LEU   A HA   1 
ATOM   1780 H HB2  . LEU   A 1 83  ? 32.634 0.989   7.438   1.00 13.31 ?  83  LEU   A HB2  1 
ATOM   1781 H HB3  . LEU   A 1 83  ? 33.691 1.879   8.213   1.00 13.31 ?  83  LEU   A HB3  1 
ATOM   1782 H HG   . LEU   A 1 83  ? 34.394 0.172   6.082   1.00 14.25 ?  83  LEU   A HG   1 
ATOM   1783 H HD11 . LEU   A 1 83  ? 34.605 2.047   4.734   1.00 14.81 ?  83  LEU   A HD11 1 
ATOM   1784 H HD12 . LEU   A 1 83  ? 33.104 1.887   5.231   1.00 14.81 ?  83  LEU   A HD12 1 
ATOM   1785 H HD13 . LEU   A 1 83  ? 34.058 2.958   5.915   1.00 14.81 ?  83  LEU   A HD13 1 
ATOM   1786 H HD21 . LEU   A 1 83  ? 36.441 1.405   6.075   1.00 15.19 ?  83  LEU   A HD21 1 
ATOM   1787 H HD22 . LEU   A 1 83  ? 35.994 2.032   7.465   1.00 15.19 ?  83  LEU   A HD22 1 
ATOM   1788 H HD23 . LEU   A 1 83  ? 36.257 0.470   7.346   1.00 15.19 ?  83  LEU   A HD23 1 
ATOM   1789 N N    . SER   A 1 84  ? 33.311 1.208   10.700  1.00 11.17 ?  84  SER   A N    1 
ATOM   1790 C CA   . SER   A 1 84  ? 32.666 1.463   11.977  1.00 11.32 ?  84  SER   A CA   1 
ATOM   1791 C C    . SER   A 1 84  ? 31.148 1.537   11.827  1.00 11.26 ?  84  SER   A C    1 
ATOM   1792 O O    . SER   A 1 84  ? 30.620 2.007   10.819  1.00 11.52 ?  84  SER   A O    1 
ATOM   1793 C CB   . SER   A 1 84  ? 33.156 2.790   12.547  1.00 12.45 ?  84  SER   A CB   1 
ATOM   1794 O OG   . SER   A 1 84  ? 32.528 3.057   13.787  1.00 13.35 ?  84  SER   A OG   1 
ATOM   1795 H H    . SER   A 1 84  ? 33.817 1.849   10.406  1.00 13.40 ?  84  SER   A H    1 
ATOM   1796 H HA   . SER   A 1 84  ? 32.890 0.756   12.592  1.00 13.58 ?  84  SER   A HA   1 
ATOM   1797 H HB2  . SER   A 1 84  ? 34.118 2.747   12.673  1.00 14.93 ?  84  SER   A HB2  1 
ATOM   1798 H HB3  . SER   A 1 84  ? 32.940 3.505   11.923  1.00 14.93 ?  84  SER   A HB3  1 
ATOM   1799 H HG   . SER   A 1 84  ? 32.807 3.785   14.098  1.00 16.01 ?  84  SER   A HG   1 
ATOM   1800 N N    . GLY   A 1 85  ? 30.443 1.112   12.871  1.00 12.12 ?  85  GLY   A N    1 
ATOM   1801 C CA   . GLY   A 1 85  ? 29.022 1.350   12.966  1.00 12.68 ?  85  GLY   A CA   1 
ATOM   1802 C C    . GLY   A 1 85  ? 28.655 2.659   13.623  1.00 12.34 ?  85  GLY   A C    1 
ATOM   1803 O O    . GLY   A 1 85  ? 27.465 2.966   13.750  1.00 12.85 ?  85  GLY   A O    1 
ATOM   1804 H H    . GLY   A 1 85  ? 30.780 0.676   13.534  1.00 14.54 ?  85  GLY   A H    1 
ATOM   1805 H HA2  . GLY   A 1 85  ? 28.643 1.338   12.072  1.00 15.21 ?  85  GLY   A HA2  1 
ATOM   1806 H HA3  . GLY   A 1 85  ? 28.619 0.636   13.474  1.00 15.21 ?  85  GLY   A HA3  1 
ATOM   1807 N N    . HIS   A 1 86  ? 29.641 3.435   14.060  1.00 11.94 ?  86  HIS   A N    1 
ATOM   1808 C CA   . HIS   A 1 86  ? 29.411 4.769   14.628  1.00 12.56 ?  86  HIS   A CA   1 
ATOM   1809 C C    . HIS   A 1 86  ? 28.428 4.642   15.785  1.00 13.31 ?  86  HIS   A C    1 
ATOM   1810 O O    . HIS   A 1 86  ? 28.614 3.763   16.642  1.00 14.51 ?  86  HIS   A O    1 
ATOM   1811 C CB   . HIS   A 1 86  ? 29.030 5.756   13.530  1.00 12.47 ?  86  HIS   A CB   1 
ATOM   1812 C CG   . HIS   A 1 86  ? 30.078 5.862   12.485  1.00 12.51 ?  86  HIS   A CG   1 
ATOM   1813 N ND1  . HIS   A 1 86  ? 31.164 6.702   12.610  1.00 13.61 ?  86  HIS   A ND1  1 
ATOM   1814 C CD2  . HIS   A 1 86  ? 30.255 5.176   11.334  1.00 12.13 ?  86  HIS   A CD2  1 
ATOM   1815 C CE1  . HIS   A 1 86  ? 31.954 6.539   11.565  1.00 13.34 ?  86  HIS   A CE1  1 
ATOM   1816 N NE2  . HIS   A 1 86  ? 31.432 5.613   10.781  1.00 12.59 ?  86  HIS   A NE2  1 
ATOM   1817 H H    . HIS   A 1 86  ? 30.470 3.214   14.048  1.00 14.32 ?  86  HIS   A H    1 
ATOM   1818 H HA   . HIS   A 1 86  ? 30.248 5.087   15.002  1.00 15.06 ?  86  HIS   A HA   1 
ATOM   1819 H HB2  . HIS   A 1 86  ? 28.207 5.468   13.104  1.00 14.96 ?  86  HIS   A HB2  1 
ATOM   1820 H HB3  . HIS   A 1 86  ? 28.906 6.643   13.916  1.00 14.96 ?  86  HIS   A HB3  1 
ATOM   1821 H HD2  . HIS   A 1 86  ? 29.694 4.515   10.986  1.00 14.55 ?  86  HIS   A HD2  1 
ATOM   1822 H HE1  . HIS   A 1 86  ? 32.744 7.001   11.392  1.00 16.00 ?  86  HIS   A HE1  1 
ATOM   1823 H HE2  . HIS   A 1 86  ? 31.763 5.339   10.027  1.00 15.10 ?  86  HIS   A HE2  1 
ATOM   1824 N N    . ASN   A 1 87  ? 27.415 5.494   15.861  1.00 13.93 ?  87  ASN   A N    1 
ATOM   1825 C CA   . ASN   A 1 87  ? 26.422 5.468   16.919  1.00 15.18 ?  87  ASN   A CA   1 
ATOM   1826 C C    . ASN   A 1 87  ? 25.305 4.466   16.665  1.00 16.52 ?  87  ASN   A C    1 
ATOM   1827 O O    . ASN   A 1 87  ? 24.377 4.389   17.475  1.00 18.74 ?  87  ASN   A O    1 
ATOM   1828 C CB   . ASN   A 1 87  ? 25.817 6.868   17.088  1.00 16.25 ?  87  ASN   A CB   1 
ATOM   1829 C CG   . ASN   A 1 87  ? 25.307 7.455   15.776  1.00 16.89 ?  87  ASN   A CG   1 
ATOM   1830 O OD1  . ASN   A 1 87  ? 25.948 7.344   14.733  1.00 17.55 ?  87  ASN   A OD1  1 
ATOM   1831 N ND2  . ASN   A 1 87  ? 24.153 8.094   15.831  1.00 17.91 ?  87  ASN   A ND2  1 
ATOM   1832 H H    . ASN   A 1 87  ? 27.280 6.119   15.293  1.00 16.71 ?  87  ASN   A H    1 
ATOM   1833 H HA   . ASN   A 1 87  ? 26.850 5.223   17.757  1.00 18.21 ?  87  ASN   A HA   1 
ATOM   1834 H HB2  . ASN   A 1 87  ? 25.068 6.814   17.709  1.00 19.49 ?  87  ASN   A HB2  1 
ATOM   1835 H HB3  . ASN   A 1 87  ? 26.495 7.462   17.444  1.00 19.49 ?  87  ASN   A HB3  1 
ATOM   1836 H HD21 . ASN   A 1 87  ? 23.825 8.446   15.121  1.00 21.49 ?  87  ASN   A HD21 1 
ATOM   1837 H HD22 . ASN   A 1 87  ? 23.733 8.162   16.580  1.00 21.49 ?  87  ASN   A HD22 1 
ATOM   1838 N N    . LEU   A 1 88  ? 25.371 3.692   15.585  1.00 15.59 ?  88  LEU   A N    1 
ATOM   1839 C CA   . LEU   A 1 88  ? 24.266 2.824   15.192  1.00 15.39 ?  88  LEU   A CA   1 
ATOM   1840 C C    . LEU   A 1 88  ? 24.489 1.349   15.503  1.00 15.13 ?  88  LEU   A C    1 
ATOM   1841 O O    . LEU   A 1 88  ? 23.515 0.615   15.690  1.00 16.34 ?  88  LEU   A O    1 
ATOM   1842 C CB   . LEU   A 1 88  ? 24.007 2.977   13.692  1.00 16.06 ?  88  LEU   A CB   1 
ATOM   1843 C CG   . LEU   A 1 88  ? 23.696 4.400   13.220  1.00 17.67 ?  88  LEU   A CG   1 
ATOM   1844 C CD1  . LEU   A 1 88  ? 23.513 4.426   11.716  1.00 17.99 ?  88  LEU   A CD1  1 
ATOM   1845 C CD2  . LEU   A 1 88  ? 22.463 4.961   13.924  1.00 19.17 ?  88  LEU   A CD2  1 
ATOM   1846 H H    . LEU   A 1 88  ? 26.057 3.649   15.062  1.00 18.70 ?  88  LEU   A H    1 
ATOM   1847 H HA   . LEU   A 1 88  ? 23.469 3.106   15.660  1.00 18.46 ?  88  LEU   A HA   1 
ATOM   1848 H HB2  . LEU   A 1 88  ? 24.791 2.683   13.207  1.00 19.27 ?  88  LEU   A HB2  1 
ATOM   1849 H HB3  . LEU   A 1 88  ? 23.247 2.427   13.452  1.00 19.27 ?  88  LEU   A HB3  1 
ATOM   1850 H HG   . LEU   A 1 88  ? 24.446 4.978   13.431  1.00 21.20 ?  88  LEU   A HG   1 
ATOM   1851 H HD11 . LEU   A 1 88  ? 23.355 5.342   11.429  1.00 21.58 ?  88  LEU   A HD11 1 
ATOM   1852 H HD12 . LEU   A 1 88  ? 24.317 4.085   11.294  1.00 21.58 ?  88  LEU   A HD12 1 
ATOM   1853 H HD13 . LEU   A 1 88  ? 22.754 3.872   11.480  1.00 21.58 ?  88  LEU   A HD13 1 
ATOM   1854 H HD21 . LEU   A 1 88  ? 22.221 5.806   13.513  1.00 23.00 ?  88  LEU   A HD21 1 
ATOM   1855 H HD22 . LEU   A 1 88  ? 21.736 4.328   13.835  1.00 23.00 ?  88  LEU   A HD22 1 
ATOM   1856 H HD23 . LEU   A 1 88  ? 22.674 5.098   14.860  1.00 23.00 ?  88  LEU   A HD23 1 
ATOM   1857 N N    . ALA   A 1 89  ? 25.741 0.907   15.548  1.00 14.06 ?  89  ALA   A N    1 
ATOM   1858 C CA   . ALA   A 1 89  ? 26.090 -0.503  15.643  1.00 13.72 ?  89  ALA   A CA   1 
ATOM   1859 C C    . ALA   A 1 89  ? 27.574 -0.561  15.963  1.00 14.01 ?  89  ALA   A C    1 
ATOM   1860 O O    . ALA   A 1 89  ? 28.280 0.442   15.856  1.00 14.84 ?  89  ALA   A O    1 
ATOM   1861 C CB   . ALA   A 1 89  ? 25.818 -1.213  14.317  1.00 13.33 ?  89  ALA   A CB   1 
ATOM   1862 H H    . ALA   A 1 89  ? 26.427 1.426   15.513  1.00 16.86 ?  89  ALA   A H    1 
ATOM   1863 H HA   . ALA   A 1 89  ? 25.584 -0.927  16.353  1.00 16.46 ?  89  ALA   A HA   1 
ATOM   1864 H HB1  . ALA   A 1 89  ? 26.075 -2.147  14.400  1.00 15.98 ?  89  ALA   A HB1  1 
ATOM   1865 H HB2  . ALA   A 1 89  ? 24.870 -1.152  14.109  1.00 15.98 ?  89  ALA   A HB2  1 
ATOM   1866 H HB3  . ALA   A 1 89  ? 26.337 -0.791  13.616  1.00 15.98 ?  89  ALA   A HB3  1 
ATOM   1867 N N    . LYS   A 1 90  ? 28.059 -1.740  16.341  1.00 14.72 ?  90  LYS   A N    1 
ATOM   1868 C CA   . LYS   A 1 90  ? 29.503 -1.884  16.487  1.00 15.32 ?  90  LYS   A CA   1 
ATOM   1869 C C    . LYS   A 1 90  ? 30.198 -1.684  15.143  1.00 14.11 ?  90  LYS   A C    1 
ATOM   1870 O O    . LYS   A 1 90  ? 31.130 -0.873  15.016  1.00 15.60 ?  90  LYS   A O    1 
ATOM   1871 C CB   . LYS   A 1 90  ? 29.844 -3.245  17.096  1.00 17.78 ?  90  LYS   A CB   1 
ATOM   1872 C CG   . LYS   A 1 90  ? 31.320 -3.385  17.434  1.00 22.00 ?  90  LYS   A CG   1 
ATOM   1873 C CD   . LYS   A 1 90  ? 31.582 -4.614  18.289  1.00 25.87 ?  90  LYS   A CD   1 
ATOM   1874 C CE   . LYS   A 1 90  ? 32.996 -4.617  18.849  1.00 28.84 ?  90  LYS   A CE   1 
ATOM   1875 N NZ   . LYS   A 1 90  ? 34.016 -4.968  17.825  1.00 30.94 ?  90  LYS   A NZ   1 
ATOM   1876 H H    . LYS   A 1 90  ? 27.590 -2.438  16.512  1.00 17.65 ?  90  LYS   A H    1 
ATOM   1877 H HA   . LYS   A 1 90  ? 29.826 -1.199  17.090  1.00 18.37 ?  90  LYS   A HA   1 
ATOM   1878 H HB2  . LYS   A 1 90  ? 29.332 -3.361  17.915  1.00 21.33 ?  90  LYS   A HB2  1 
ATOM   1879 H HB3  . LYS   A 1 90  ? 29.611 -3.943  16.463  1.00 21.33 ?  90  LYS   A HB3  1 
ATOM   1880 H HG2  . LYS   A 1 90  ? 31.827 -3.470  16.614  1.00 26.39 ?  90  LYS   A HG2  1 
ATOM   1881 H HG3  . LYS   A 1 90  ? 31.607 -2.603  17.930  1.00 26.39 ?  90  LYS   A HG3  1 
ATOM   1882 H HD2  . LYS   A 1 90  ? 30.959 -4.626  19.034  1.00 31.04 ?  90  LYS   A HD2  1 
ATOM   1883 H HD3  . LYS   A 1 90  ? 31.468 -5.411  17.746  1.00 31.04 ?  90  LYS   A HD3  1 
ATOM   1884 H HE2  . LYS   A 1 90  ? 33.203 -3.731  19.189  1.00 34.60 ?  90  LYS   A HE2  1 
ATOM   1885 H HE3  . LYS   A 1 90  ? 33.052 -5.268  19.566  1.00 34.60 ?  90  LYS   A HE3  1 
ATOM   1886 H HZ1  . LYS   A 1 90  ? 34.826 -4.980  18.195  1.00 37.12 ?  90  LYS   A HZ1  1 
ATOM   1887 H HZ2  . LYS   A 1 90  ? 33.841 -5.772  17.486  1.00 37.12 ?  90  LYS   A HZ2  1 
ATOM   1888 H HZ3  . LYS   A 1 90  ? 34.006 -4.368  17.169  1.00 37.12 ?  90  LYS   A HZ3  1 
ATOM   1889 N N    . HIS   A 1 91  ? 29.728 -2.397  14.121  1.00 12.34 ?  91  HIS   A N    1 
ATOM   1890 C CA   . HIS   A 1 91  ? 30.298 -2.381  12.790  1.00 11.83 ?  91  HIS   A CA   1 
ATOM   1891 C C    . HIS   A 1 91  ? 29.204 -2.103  11.776  1.00 10.67 ?  91  HIS   A C    1 
ATOM   1892 O O    . HIS   A 1 91  ? 28.037 -2.467  11.973  1.00 11.58 ?  91  HIS   A O    1 
ATOM   1893 C CB   . HIS   A 1 91  ? 30.891 -3.755  12.426  1.00 14.09 ?  91  HIS   A CB   1 
ATOM   1894 C CG   . HIS   A 1 91  ? 31.875 -4.279  13.424  1.00 18.32 ?  91  HIS   A CG   1 
ATOM   1895 N ND1  . HIS   A 1 91  ? 33.152 -3.777  13.542  1.00 20.45 ?  91  HIS   A ND1  1 
ATOM   1896 C CD2  . HIS   A 1 91  ? 31.775 -5.271  14.340  1.00 20.14 ?  91  HIS   A CD2  1 
ATOM   1897 C CE1  . HIS   A 1 91  ? 33.796 -4.432  14.493  1.00 21.33 ?  91  HIS   A CE1  1 
ATOM   1898 N NE2  . HIS   A 1 91  ? 32.982 -5.346  14.993  1.00 21.42 ?  91  HIS   A NE2  1 
ATOM   1899 H H    . HIS   A 1 91  ? 29.052 -2.939  14.191  1.00 14.80 ?  91  HIS   A H    1 
ATOM   1900 H HA   . HIS   A 1 91  ? 30.990 -1.716  12.724  1.00 14.18 ?  91  HIS   A HA   1 
ATOM   1901 H HB2  . HIS   A 1 91  ? 30.171 -4.407  12.361  1.00 16.90 ?  91  HIS   A HB2  1 
ATOM   1902 H HB3  . HIS   A 1 91  ? 31.346 -3.689  11.574  1.00 16.90 ?  91  HIS   A HB3  1 
ATOM   1903 H HD1  . HIS   A 1 91  ? 33.480 -3.137  13.069  1.00 24.53 ?  91  HIS   A HD1  1 
ATOM   1904 H HD2  . HIS   A 1 91  ? 31.034 -5.805  14.503  1.00 24.16 ?  91  HIS   A HD2  1 
ATOM   1905 H HE1  . HIS   A 1 91  ? 34.675 -4.273  14.764  1.00 25.58 ?  91  HIS   A HE1  1 
ATOM   1906 N N    . CYS   A 1 92  ? 29.604 -1.498  10.662  1.00 10.55 ?  92  CYS   A N    1 
ATOM   1907 C CA   . CYS   A 1 92  ? 28.764 -1.419  9.477   1.00 10.38 ?  92  CYS   A CA   1 
ATOM   1908 C C    . CYS   A 1 92  ? 29.411 -2.238  8.370   1.00 9.95  ?  92  CYS   A C    1 
ATOM   1909 O O    . CYS   A 1 92  ? 30.568 -1.989  8.000   1.00 10.68 ?  92  CYS   A O    1 
ATOM   1910 C CB   . CYS   A 1 92  ? 28.557 0.023   9.016   1.00 10.87 ?  92  CYS   A CB   1 
ATOM   1911 S SG   . CYS   A 1 92  ? 27.527 0.128   7.514   1.00 10.51 ?  92  CYS   A SG   1 
ATOM   1912 H H    . CYS   A 1 92  ? 30.373 -1.114  10.571  1.00 12.65 ?  92  CYS   A H    1 
ATOM   1913 H HA   . CYS   A 1 92  ? 27.897 -1.801  9.675   1.00 12.44 ?  92  CYS   A HA   1 
ATOM   1914 H HB2  . CYS   A 1 92  ? 28.110 0.523   9.719   1.00 13.04 ?  92  CYS   A HB2  1 
ATOM   1915 H HB3  . CYS   A 1 92  ? 29.416 0.424   8.817   1.00 13.04 ?  92  CYS   A HB3  1 
ATOM   1916 H HG   . CYS   A 1 92  ? 27.386 1.278   7.216   1.00 12.61 ?  92  CYS   A HG   1 
ATOM   1917 N N    . LEU   A 1 93  ? 28.671 -3.223  7.864   1.00 9.73  ?  93  LEU   A N    1 
ATOM   1918 C CA   . LEU   A 1 93  ? 29.064 -3.979  6.681   1.00 9.58  ?  93  LEU   A CA   1 
ATOM   1919 C C    . LEU   A 1 93  ? 28.464 -3.283  5.466   1.00 9.04  ?  93  LEU   A C    1 
ATOM   1920 O O    . LEU   A 1 93  ? 27.249 -3.349  5.239   1.00 9.30  ?  93  LEU   A O    1 
ATOM   1921 C CB   . LEU   A 1 93  ? 28.580 -5.425  6.781   1.00 10.10 ?  93  LEU   A CB   1 
ATOM   1922 C CG   . LEU   A 1 93  ? 28.970 -6.324  5.610   1.00 10.21 ?  93  LEU   A CG   1 
ATOM   1923 C CD1  . LEU   A 1 93  ? 30.477 -6.569  5.599   1.00 10.87 ?  93  LEU   A CD1  1 
ATOM   1924 C CD2  . LEU   A 1 93  ? 28.202 -7.649  5.640   1.00 11.05 ?  93  LEU   A CD2  1 
ATOM   1925 H H    . LEU   A 1 93  ? 27.914 -3.471  8.199   1.00 11.67 ?  93  LEU   A H    1 
ATOM   1926 H HA   . LEU   A 1 93  ? 30.028 -3.975  6.606   1.00 11.48 ?  93  LEU   A HA   1 
ATOM   1927 H HB2  . LEU   A 1 93  ? 28.946 -5.816  7.592   1.00 12.11 ?  93  LEU   A HB2  1 
ATOM   1928 H HB3  . LEU   A 1 93  ? 27.610 -5.421  6.836   1.00 12.11 ?  93  LEU   A HB3  1 
ATOM   1929 H HG   . LEU   A 1 93  ? 28.746 -5.878  4.789   1.00 12.24 ?  93  LEU   A HG   1 
ATOM   1930 H HD11 . LEU   A 1 93  ? 30.699 -7.193  4.892   1.00 13.04 ?  93  LEU   A HD11 1 
ATOM   1931 H HD12 . LEU   A 1 93  ? 30.941 -5.728  5.456   1.00 13.04 ?  93  LEU   A HD12 1 
ATOM   1932 H HD13 . LEU   A 1 93  ? 30.752 -6.945  6.460   1.00 13.04 ?  93  LEU   A HD13 1 
ATOM   1933 H HD21 . LEU   A 1 93  ? 28.486 -8.193  4.883   1.00 13.25 ?  93  LEU   A HD21 1 
ATOM   1934 H HD22 . LEU   A 1 93  ? 28.398 -8.117  6.467   1.00 13.25 ?  93  LEU   A HD22 1 
ATOM   1935 H HD23 . LEU   A 1 93  ? 27.254 -7.468  5.577   1.00 13.25 ?  93  LEU   A HD23 1 
ATOM   1936 N N    . HIS   A 1 94  ? 29.311 -2.589  4.710   1.00 9.01  ?  94  HIS   A N    1 
ATOM   1937 C CA   . HIS   A 1 94  ? 28.886 -1.915  3.489   1.00 9.23  ?  94  HIS   A CA   1 
ATOM   1938 C C    . HIS   A 1 94  ? 28.885 -2.944  2.374   1.00 9.10  ?  94  HIS   A C    1 
ATOM   1939 O O    . HIS   A 1 94  ? 29.948 -3.456  2.017   1.00 10.43 ?  94  HIS   A O    1 
ATOM   1940 C CB   . HIS   A 1 94  ? 29.837 -0.769  3.154   1.00 9.30  ?  94  HIS   A CB   1 
ATOM   1941 C CG   . HIS   A 1 94  ? 29.827 0.322   4.166   1.00 9.16  ?  94  HIS   A CG   1 
ATOM   1942 N ND1  . HIS   A 1 94  ? 28.946 1.381   4.112   1.00 9.56  ?  94  HIS   A ND1  1 
ATOM   1943 C CD2  . HIS   A 1 94  ? 30.568 0.491   5.285   1.00 9.85  ?  94  HIS   A CD2  1 
ATOM   1944 C CE1  . HIS   A 1 94  ? 29.163 2.162   5.154   1.00 9.54  ?  94  HIS   A CE1  1 
ATOM   1945 N NE2  . HIS   A 1 94  ? 30.139 1.645   5.881   1.00 9.86  ?  94  HIS   A NE2  1 
ATOM   1946 H H    . HIS   A 1 94  ? 30.150 -2.491  4.886   1.00 10.80 ?  94  HIS   A H    1 
ATOM   1947 H HA   . HIS   A 1 94  ? 27.983 -1.568  3.599   1.00 11.06 ?  94  HIS   A HA   1 
ATOM   1948 H HB2  . HIS   A 1 94  ? 30.734 -1.118  3.098   1.00 11.15 ?  94  HIS   A HB2  1 
ATOM   1949 H HB3  . HIS   A 1 94  ? 29.570 -0.386  2.304   1.00 11.15 ?  94  HIS   A HB3  1 
ATOM   1950 H HD2  . HIS   A 1 94  ? 31.242 -0.068  5.593   1.00 11.81 ?  94  HIS   A HD2  1 
ATOM   1951 H HE1  . HIS   A 1 94  ? 28.697 2.945   5.341   1.00 11.44 ?  94  HIS   A HE1  1 
ATOM   1952 H HE2  . HIS   A 1 94  ? 30.452 1.987   6.603   1.00 11.83 ?  94  HIS   A HE2  1 
ATOM   1953 N N    . VAL   A 1 95  ? 27.712 -3.263  1.829   1.00 8.39  ?  95  VAL   A N    1 
ATOM   1954 C CA   . VAL   A 1 95  ? 27.571 -4.298  0.808   1.00 8.91  ?  95  VAL   A CA   1 
ATOM   1955 C C    . VAL   A 1 95  ? 27.026 -3.660  -0.457  1.00 8.57  ?  95  VAL   A C    1 
ATOM   1956 O O    . VAL   A 1 95  ? 26.020 -2.942  -0.403  1.00 9.49  ?  95  VAL   A O    1 
ATOM   1957 C CB   . VAL   A 1 95  ? 26.642 -5.440  1.260   1.00 9.72  ?  95  VAL   A CB   1 
ATOM   1958 C CG1  . VAL   A 1 95  ? 26.536 -6.486  0.159   1.00 10.43 ?  95  VAL   A CG1  1 
ATOM   1959 C CG2  . VAL   A 1 95  ? 27.152 -6.056  2.543   1.00 9.86  ?  95  VAL   A CG2  1 
ATOM   1960 H H    . VAL   A 1 95  ? 26.966 -2.885  2.039   1.00 10.06 ?  95  VAL   A H    1 
ATOM   1961 H HA   . VAL   A 1 95  ? 28.439 -4.674  0.608   1.00 10.69 ?  95  VAL   A HA   1 
ATOM   1962 H HB   . VAL   A 1 95  ? 25.757 -5.089  1.428   1.00 11.65 ?  95  VAL   A HB   1 
ATOM   1963 H HG11 . VAL   A 1 95  ? 26.142 -7.298  0.525   1.00 12.51 ?  95  VAL   A HG11 1 
ATOM   1964 H HG12 . VAL   A 1 95  ? 25.979 -6.148  -0.558  1.00 12.51 ?  95  VAL   A HG12 1 
ATOM   1965 H HG13 . VAL   A 1 95  ? 27.427 -6.688  -0.181  1.00 12.51 ?  95  VAL   A HG13 1 
ATOM   1966 H HG21 . VAL   A 1 95  ? 26.598 -6.817  2.770   1.00 11.82 ?  95  VAL   A HG21 1 
ATOM   1967 H HG22 . VAL   A 1 95  ? 28.071 -6.338  2.415   1.00 11.82 ?  95  VAL   A HG22 1 
ATOM   1968 H HG23 . VAL   A 1 95  ? 27.106 -5.390  3.249   1.00 11.82 ?  95  VAL   A HG23 1 
ATOM   1969 N N    . VAL   A 1 96  ? 27.652 -3.949  -1.593  1.00 8.73  ?  96  VAL   A N    1 
ATOM   1970 C CA   . VAL   A 1 96  ? 27.238 -3.392  -2.873  1.00 9.30  ?  96  VAL   A CA   1 
ATOM   1971 C C    . VAL   A 1 96  ? 26.432 -4.431  -3.645  1.00 9.77  ?  96  VAL   A C    1 
ATOM   1972 O O    . VAL   A 1 96  ? 26.990 -5.374  -4.213  1.00 10.66 ?  96  VAL   A O    1 
ATOM   1973 C CB   . VAL   A 1 96  ? 28.433 -2.916  -3.702  1.00 9.81  ?  96  VAL   A CB   1 
ATOM   1974 C CG1  . VAL   A 1 96  ? 27.928 -2.275  -4.978  1.00 10.08 ?  96  VAL   A CG1  1 
ATOM   1975 C CG2  . VAL   A 1 96  ? 29.296 -1.947  -2.904  1.00 10.38 ?  96  VAL   A CG2  1 
ATOM   1976 H H    . VAL   A 1 96  ? 28.340 -4.469  -1.649  1.00 10.47 ?  96  VAL   A H    1 
ATOM   1977 H HA   . VAL   A 1 96  ? 26.666 -2.626  -2.716  1.00 11.15 ?  96  VAL   A HA   1 
ATOM   1978 H HB   . VAL   A 1 96  ? 28.980 -3.675  -3.946  1.00 11.76 ?  96  VAL   A HB   1 
ATOM   1979 H HG11 . VAL   A 1 96  ? 28.663 -1.786  -5.389  1.00 12.09 ?  96  VAL   A HG11 1 
ATOM   1980 H HG12 . VAL   A 1 96  ? 27.614 -2.962  -5.579  1.00 12.09 ?  96  VAL   A HG12 1 
ATOM   1981 H HG13 . VAL   A 1 96  ? 27.211 -1.659  -4.760  1.00 12.09 ?  96  VAL   A HG13 1 
ATOM   1982 H HG21 . VAL   A 1 96  ? 29.995 -1.596  -3.473  1.00 12.45 ?  96  VAL   A HG21 1 
ATOM   1983 H HG22 . VAL   A 1 96  ? 28.736 -1.217  -2.582  1.00 12.45 ?  96  VAL   A HG22 1 
ATOM   1984 H HG23 . VAL   A 1 96  ? 29.683 -2.417  -2.149  1.00 12.45 ?  96  VAL   A HG23 1 
ATOM   1985 N N    A GLY   A 1 97  ? 25.113 -4.281  -3.652  0.88 9.84  ?  97  GLY   A N    1 
ATOM   1986 N N    B GLY   A 1 97  ? 25.118 -4.238  -3.715  0.12 10.16 ?  97  GLY   A N    1 
ATOM   1987 C CA   A GLY   A 1 97  ? 24.288 -5.035  -4.560  0.88 10.37 ?  97  GLY   A CA   1 
ATOM   1988 C CA   B GLY   A 1 97  ? 24.292 -5.033  -4.592  0.12 10.58 ?  97  GLY   A CA   1 
ATOM   1989 C C    A GLY   A 1 97  ? 24.293 -4.373  -5.923  0.88 10.35 ?  97  GLY   A C    1 
ATOM   1990 C C    B GLY   A 1 97  ? 24.377 -4.537  -6.024  0.12 11.06 ?  97  GLY   A C    1 
ATOM   1991 O O    A GLY   A 1 97  ? 24.578 -3.174  -6.052  0.88 11.22 ?  97  GLY   A O    1 
ATOM   1992 O O    B GLY   A 1 97  ? 24.691 -3.370  -6.278  0.12 11.18 ?  97  GLY   A O    1 
ATOM   1993 H H    A GLY   A 1 97  ? 24.676 -3.741  -3.136  0.88 11.80 ?  97  GLY   A H    1 
ATOM   1994 H H    B GLY   A 1 97  ? 24.682 -3.653  -3.256  0.12 12.18 ?  97  GLY   A H    1 
ATOM   1995 H HA2  A GLY   A 1 97  ? 24.633 -5.937  -4.632  0.88 12.43 ?  97  GLY   A HA2  1 
ATOM   1996 H HA2  B GLY   A 1 97  ? 24.583 -5.957  -4.551  0.12 12.69 ?  97  GLY   A HA2  1 
ATOM   1997 H HA3  A GLY   A 1 97  ? 23.376 -5.073  -4.222  0.88 12.43 ?  97  GLY   A HA3  1 
ATOM   1998 H HA3  B GLY   A 1 97  ? 23.367 -4.984  -4.308  0.12 12.69 ?  97  GLY   A HA3  1 
ATOM   1999 N N    A PRO   A 1 98  ? 23.971 -5.130  -6.969  0.88 10.39 ?  98  PRO   A N    1 
ATOM   2000 N N    B PRO   A 1 98  ? 24.107 -5.414  -6.991  0.12 11.63 ?  98  PRO   A N    1 
ATOM   2001 C CA   A PRO   A 1 98  ? 23.863 -4.525  -8.299  0.88 11.54 ?  98  PRO   A CA   1 
ATOM   2002 C CA   B PRO   A 1 98  ? 24.120 -4.977  -8.392  0.12 12.16 ?  98  PRO   A CA   1 
ATOM   2003 C C    A PRO   A 1 98  ? 22.749 -3.487  -8.343  0.88 11.57 ?  98  PRO   A C    1 
ATOM   2004 C C    B PRO   A 1 98  ? 23.011 -3.977  -8.676  0.12 12.89 ?  98  PRO   A C    1 
ATOM   2005 O O    A PRO   A 1 98  ? 21.675 -3.665  -7.762  0.88 11.62 ?  98  PRO   A O    1 
ATOM   2006 O O    B PRO   A 1 98  ? 21.884 -4.114  -8.196  0.12 13.16 ?  98  PRO   A O    1 
ATOM   2007 C CB   A PRO   A 1 98  ? 23.556 -5.723  -9.206  0.88 11.68 ?  98  PRO   A CB   1 
ATOM   2008 C CB   B PRO   A 1 98  ? 23.913 -6.280  -9.175  0.12 11.86 ?  98  PRO   A CB   1 
ATOM   2009 C CG   A PRO   A 1 98  ? 22.903 -6.728  -8.299  0.88 11.85 ?  98  PRO   A CG   1 
ATOM   2010 C CG   B PRO   A 1 98  ? 23.268 -7.208  -8.205  0.12 11.82 ?  98  PRO   A CG   1 
ATOM   2011 C CD   A PRO   A 1 98  ? 23.635 -6.568  -6.985  0.88 10.94 ?  98  PRO   A CD   1 
ATOM   2012 C CD   B PRO   A 1 98  ? 23.859 -6.860  -6.872  0.12 11.69 ?  98  PRO   A CD   1 
ATOM   2013 H HA   A PRO   A 1 98  ? 24.706 -4.122  -8.556  0.88 13.84 ?  98  PRO   A HA   1 
ATOM   2014 H HA   B PRO   A 1 98  ? 24.976 -4.589  -8.623  0.12 14.58 ?  98  PRO   A HA   1 
ATOM   2015 H HB2  A PRO   A 1 98  ? 22.944 -5.449  -9.906  0.88 14.00 ?  98  PRO   A HB2  1 
ATOM   2016 H HB2  B PRO   A 1 98  ? 23.332 -6.121  -9.933  0.12 14.23 ?  98  PRO   A HB2  1 
ATOM   2017 H HB3  A PRO   A 1 98  ? 24.376 -6.075  -9.575  0.88 14.00 ?  98  PRO   A HB3  1 
ATOM   2018 H HB3  B PRO   A 1 98  ? 24.772 -6.622  -9.467  0.12 14.23 ?  98  PRO   A HB3  1 
ATOM   2019 H HG2  A PRO   A 1 98  ? 21.962 -6.517  -8.192  0.88 14.20 ?  98  PRO   A HG2  1 
ATOM   2020 H HG2  B PRO   A 1 98  ? 22.308 -7.062  -8.203  0.12 14.17 ?  98  PRO   A HG2  1 
ATOM   2021 H HG3  A PRO   A 1 98  ? 23.024 -7.620  -8.652  0.88 14.20 ?  98  PRO   A HG3  1 
ATOM   2022 H HG3  B PRO   A 1 98  ? 23.474 -8.123  -8.448  0.12 14.17 ?  98  PRO   A HG3  1 
ATOM   2023 H HD2  A PRO   A 1 98  ? 23.050 -6.794  -6.239  0.88 13.12 ?  98  PRO   A HD2  1 
ATOM   2024 H HD2  B PRO   A 1 98  ? 23.225 -7.041  -6.160  0.12 14.01 ?  98  PRO   A HD2  1 
ATOM   2025 H HD3  A PRO   A 1 98  ? 24.442 -7.108  -6.973  0.88 13.12 ?  98  PRO   A HD3  1 
ATOM   2026 H HD3  B PRO   A 1 98  ? 24.695 -7.335  -6.735  0.12 14.01 ?  98  PRO   A HD3  1 
ATOM   2027 N N    A ASN   A 1 99  ? 23.017 -2.387  -9.038  0.88 12.75 ?  99  ASN   A N    1 
ATOM   2028 N N    B ASN   A 1 99  ? 23.345 -2.964  -9.468  0.12 13.60 ?  99  ASN   A N    1 
ATOM   2029 C CA   A ASN   A 1 99  ? 22.038 -1.325  -9.251  0.88 14.09 ?  99  ASN   A CA   1 
ATOM   2030 C CA   B ASN   A 1 99  ? 22.416 -1.895  -9.814  0.12 14.48 ?  99  ASN   A CA   1 
ATOM   2031 C C    A ASN   A 1 99  ? 21.463 -1.500  -10.653 0.88 15.26 ?  99  ASN   A C    1 
ATOM   2032 C C    B ASN   A 1 99  ? 21.798 -2.199  -11.172 0.12 15.41 ?  99  ASN   A C    1 
ATOM   2033 O O    A ASN   A 1 99  ? 22.160 -1.288  -11.652 0.88 16.71 ?  99  ASN   A O    1 
ATOM   2034 O O    B ASN   A 1 99  ? 22.483 -2.155  -12.199 0.12 15.31 ?  99  ASN   A O    1 
ATOM   2035 C CB   A ASN   A 1 99  ? 22.680 0.051   -9.069  0.88 14.50 ?  99  ASN   A CB   1 
ATOM   2036 C CB   B ASN   A 1 99  ? 23.140 -0.555  -9.848  0.12 14.45 ?  99  ASN   A CB   1 
ATOM   2037 C CG   A ASN   A 1 99  ? 21.655 1.197   -9.065  0.88 15.31 ?  99  ASN   A CG   1 
ATOM   2038 C CG   B ASN   A 1 99  ? 22.188 0.613   -9.875  0.12 14.47 ?  99  ASN   A CG   1 
ATOM   2039 O OD1  A ASN   A 1 99  ? 20.652 1.150   -9.775  0.88 16.07 ?  99  ASN   A OD1  1 
ATOM   2040 O OD1  B ASN   A 1 99  ? 21.210 0.617   -10.622 0.12 13.88 ?  99  ASN   A OD1  1 
ATOM   2041 N ND2  A ASN   A 1 99  ? 21.923 2.233   -8.268  0.88 15.81 ?  99  ASN   A ND2  1 
ATOM   2042 N ND2  B ASN   A 1 99  ? 22.457 1.604   -9.042  0.12 15.07 ?  99  ASN   A ND2  1 
ATOM   2043 H H    A ASN   A 1 99  ? 23.784 -2.223  -9.389  0.88 15.29 ?  99  ASN   A H    1 
ATOM   2044 H H    B ASN   A 1 99  ? 24.125 -2.871  -9.817  0.12 16.31 ?  99  ASN   A H    1 
ATOM   2045 H HA   A ASN   A 1 99  ? 21.319 -1.416  -8.597  0.88 16.90 ?  99  ASN   A HA   1 
ATOM   2046 H HA   B ASN   A 1 99  ? 21.707 -1.854  -9.154  0.12 17.36 ?  99  ASN   A HA   1 
ATOM   2047 H HB2  A ASN   A 1 99  ? 23.160 0.072   -8.223  0.88 17.39 ?  99  ASN   A HB2  1 
ATOM   2048 H HB2  B ASN   A 1 99  ? 23.691 -0.477  -9.061  0.12 17.33 ?  99  ASN   A HB2  1 
ATOM   2049 H HB3  A ASN   A 1 99  ? 23.298 0.206   -9.800  0.88 17.39 ?  99  ASN   A HB3  1 
ATOM   2050 H HB3  B ASN   A 1 99  ? 23.689 -0.524  -10.642 0.12 17.33 ?  99  ASN   A HB3  1 
ATOM   2051 H HD21 A ASN   A 1 99  ? 21.381 2.898   -8.230  0.88 18.97 ?  99  ASN   A HD21 1 
ATOM   2052 H HD21 B ASN   A 1 99  ? 21.940 2.284   -9.014  0.12 18.07 ?  99  ASN   A HD21 1 
ATOM   2053 H HD22 A ASN   A 1 99  ? 22.637 2.231   -7.786  0.88 18.97 ?  99  ASN   A HD22 1 
ATOM   2054 H HD22 B ASN   A 1 99  ? 23.149 1.563   -8.533  0.12 18.07 ?  99  ASN   A HD22 1 
ATOM   2055 N N    A VAL   A 1 100 ? 20.194 -1.908  -10.718 0.88 16.20 ?  100 VAL   A N    1 
ATOM   2056 N N    B VAL   A 1 100 ? 20.496 -2.485  -11.175 0.12 16.52 ?  100 VAL   A N    1 
ATOM   2057 C CA   A VAL   A 1 100 ? 19.544 -2.137  -12.003 0.88 18.49 ?  100 VAL   A CA   1 
ATOM   2058 C CA   B VAL   A 1 100 ? 19.821 -2.811  -12.425 0.12 17.63 ?  100 VAL   A CA   1 
ATOM   2059 C C    A VAL   A 1 100 ? 19.452 -0.842  -12.795 0.88 19.30 ?  100 VAL   A C    1 
ATOM   2060 C C    B VAL   A 1 100 ? 19.742 -1.591  -13.332 0.12 18.21 ?  100 VAL   A C    1 
ATOM   2061 O O    A VAL   A 1 100 ? 19.521 -0.852  -14.029 0.88 20.37 ?  100 VAL   A O    1 
ATOM   2062 O O    B VAL   A 1 100 ? 19.719 -1.726  -14.562 0.12 18.14 ?  100 VAL   A O    1 
ATOM   2063 C CB   A VAL   A 1 100 ? 18.164 -2.796  -11.794 0.88 20.24 ?  100 VAL   A CB   1 
ATOM   2064 C CB   B VAL   A 1 100 ? 18.442 -3.439  -12.141 0.12 18.17 ?  100 VAL   A CB   1 
ATOM   2065 C CG1  A VAL   A 1 100 ? 17.468 -3.039  -13.130 0.88 21.04 ?  100 VAL   A CG1  1 
ATOM   2066 C CG1  B VAL   A 1 100 ? 17.316 -2.602  -12.740 0.12 18.28 ?  100 VAL   A CG1  1 
ATOM   2067 C CG2  A VAL   A 1 100 ? 18.318 -4.102  -11.031 0.88 20.84 ?  100 VAL   A CG2  1 
ATOM   2068 C CG2  B VAL   A 1 100 ? 18.401 -4.860  -12.672 0.12 18.43 ?  100 VAL   A CG2  1 
ATOM   2069 H H    A VAL   A 1 100 ? 19.688 -2.060  -10.032 0.88 19.43 ?  100 VAL   A H    1 
ATOM   2070 H H    B VAL   A 1 100 ? 19.990 -2.491  -10.480 0.12 19.81 ?  100 VAL   A H    1 
ATOM   2071 H HA   A VAL   A 1 100 ? 20.083 -2.754  -12.517 0.88 22.18 ?  100 VAL   A HA   1 
ATOM   2072 H HA   B VAL   A 1 100 ? 20.346 -3.476  -12.891 0.12 21.14 ?  100 VAL   A HA   1 
ATOM   2073 H HB   A VAL   A 1 100 ? 17.604 -2.204  -11.268 0.88 24.28 ?  100 VAL   A HB   1 
ATOM   2074 H HB   B VAL   A 1 100 ? 18.304 -3.479  -11.182 0.12 21.80 ?  100 VAL   A HB   1 
ATOM   2075 H HG11 A VAL   A 1 100 ? 16.685 -3.593  -12.980 0.88 25.24 ?  100 VAL   A HG11 1 
ATOM   2076 H HG11 B VAL   A 1 100 ? 16.472 -3.011  -12.500 0.12 21.93 ?  100 VAL   A HG11 1 
ATOM   2077 H HG12 A VAL   A 1 100 ? 17.202 -2.188  -13.511 0.88 25.24 ?  100 VAL   A HG12 1 
ATOM   2078 H HG12 B VAL   A 1 100 ? 17.354 -1.703  -12.377 0.12 21.93 ?  100 VAL   A HG12 1 
ATOM   2079 H HG13 A VAL   A 1 100 ? 18.083 -3.494  -13.727 0.88 25.24 ?  100 VAL   A HG13 1 
ATOM   2080 H HG13 B VAL   A 1 100 ? 17.404 -2.583  -13.705 0.12 21.93 ?  100 VAL   A HG13 1 
ATOM   2081 H HG21 A VAL   A 1 100 ? 17.460 -4.551  -10.999 0.88 24.99 ?  100 VAL   A HG21 1 
ATOM   2082 H HG21 B VAL   A 1 100 ? 17.501 -5.202  -12.580 0.12 22.11 ?  100 VAL   A HG21 1 
ATOM   2083 H HG22 A VAL   A 1 100 ? 18.967 -4.658  -11.488 0.88 24.99 ?  100 VAL   A HG22 1 
ATOM   2084 H HG22 B VAL   A 1 100 ? 18.660 -4.854  -13.606 0.12 22.11 ?  100 VAL   A HG22 1 
ATOM   2085 H HG23 A VAL   A 1 100 ? 18.623 -3.908  -10.131 0.88 24.99 ?  100 VAL   A HG23 1 
ATOM   2086 H HG23 B VAL   A 1 100 ? 19.020 -5.405  -12.160 0.12 22.11 ?  100 VAL   A HG23 1 
ATOM   2087 N N    A ASN   A 1 101 ? 19.301 0.289   -12.113 0.88 20.67 ?  101 ASN   A N    1 
ATOM   2088 N N    B ASN   A 1 101 ? 19.698 -0.387  -12.754 0.12 18.93 ?  101 ASN   A N    1 
ATOM   2089 C CA   A ASN   A 1 101 ? 19.253 1.568   -12.813 0.88 22.61 ?  101 ASN   A CA   1 
ATOM   2090 C CA   B ASN   A 1 101 ? 19.681 0.819   -13.575 0.12 19.70 ?  101 ASN   A CA   1 
ATOM   2091 C C    A ASN   A 1 101 ? 20.613 1.991   -13.371 0.88 24.58 ?  101 ASN   A C    1 
ATOM   2092 C C    B ASN   A 1 101 ? 21.047 1.094   -14.191 0.12 20.61 ?  101 ASN   A C    1 
ATOM   2093 O O    A ASN   A 1 101 ? 20.691 3.030   -14.040 0.88 26.12 ?  101 ASN   A O    1 
ATOM   2094 O O    B ASN   A 1 101 ? 21.128 1.705   -15.263 0.12 20.59 ?  101 ASN   A O    1 
ATOM   2095 C CB   A ASN   A 1 101 ? 18.635 2.622   -11.893 0.88 22.26 ?  101 ASN   A CB   1 
ATOM   2096 C CB   B ASN   A 1 101 ? 19.205 2.015   -12.750 0.12 19.65 ?  101 ASN   A CB   1 
ATOM   2097 C CG   A ASN   A 1 101 ? 17.275 2.187   -11.354 0.88 21.89 ?  101 ASN   A CG   1 
ATOM   2098 C CG   B ASN   A 1 101 ? 17.833 1.792   -12.144 0.12 19.76 ?  101 ASN   A CG   1 
ATOM   2099 O OD1  A ASN   A 1 101 ? 16.442 1.653   -12.094 0.88 22.46 ?  101 ASN   A OD1  1 
ATOM   2100 O OD1  B ASN   A 1 101 ? 17.107 0.882   -12.543 0.12 19.91 ?  101 ASN   A OD1  1 
ATOM   2101 N ND2  A ASN   A 1 101 ? 17.054 2.394   -10.060 0.88 21.42 ?  101 ASN   A ND2  1 
ATOM   2102 N ND2  B ASN   A 1 101 ? 17.469 2.627   -11.179 0.12 19.81 ?  101 ASN   A ND2  1 
ATOM   2103 H H    A ASN   A 1 101 ? 19.216 0.343   -11.259 0.88 24.79 ?  101 ASN   A H    1 
ATOM   2104 H H    B ASN   A 1 101 ? 19.676 -0.245  -11.905 0.12 22.71 ?  101 ASN   A H    1 
ATOM   2105 H HA   A ASN   A 1 101 ? 18.661 1.475   -13.570 0.88 27.12 ?  101 ASN   A HA   1 
ATOM   2106 H HA   B ASN   A 1 101 ? 19.052 0.695   -14.299 0.12 23.63 ?  101 ASN   A HA   1 
ATOM   2107 H HB2  A ASN   A 1 101 ? 19.223 2.778   -11.138 0.88 26.70 ?  101 ASN   A HB2  1 
ATOM   2108 H HB2  B ASN   A 1 101 ? 19.830 2.173   -12.025 0.12 23.57 ?  101 ASN   A HB2  1 
ATOM   2109 H HB3  A ASN   A 1 101 ? 18.513 3.449   -12.393 0.88 26.70 ?  101 ASN   A HB3  1 
ATOM   2110 H HB3  B ASN   A 1 101 ? 19.157 2.798   -13.322 0.12 23.57 ?  101 ASN   A HB3  1 
ATOM   2111 H HD21 A ASN   A 1 101 ? 16.301 2.168   -9.712  0.88 25.69 ?  101 ASN   A HD21 1 
ATOM   2112 H HD21 B ASN   A 1 101 ? 16.702 2.545   -10.804 0.12 23.76 ?  101 ASN   A HD21 1 
ATOM   2113 H HD22 A ASN   A 1 101 ? 17.658 2.767   -9.574  0.88 25.69 ?  101 ASN   A HD22 1 
ATOM   2114 H HD22 B ASN   A 1 101 ? 17.999 3.252   -10.928 0.12 23.76 ?  101 ASN   A HD22 1 
ATOM   2115 N N    A LYS   A 1 102 ? 21.666 1.202   -13.134 0.88 26.13 ?  102 LYS   A N    1 
ATOM   2116 N N    B LYS   A 1 102 ? 22.122 0.655   -13.537 0.12 21.61 ?  102 LYS   A N    1 
ATOM   2117 C CA   A LYS   A 1 102 ? 22.954 1.362   -13.798 0.88 27.29 ?  102 LYS   A CA   1 
ATOM   2118 C CA   B LYS   A 1 102 ? 23.461 0.761   -14.103 0.12 22.42 ?  102 LYS   A CA   1 
ATOM   2119 C C    A LYS   A 1 102 ? 23.249 0.232   -14.777 0.88 27.28 ?  102 LYS   A C    1 
ATOM   2120 C C    B LYS   A 1 102 ? 23.771 -0.356  -15.092 0.12 22.71 ?  102 LYS   A C    1 
ATOM   2121 O O    A LYS   A 1 102 ? 24.327 0.221   -15.379 0.88 27.85 ?  102 LYS   A O    1 
ATOM   2122 O O    B LYS   A 1 102 ? 24.889 -0.403  -15.616 0.12 22.82 ?  102 LYS   A O    1 
ATOM   2123 C CB   A LYS   A 1 102 ? 24.088 1.430   -12.767 0.88 28.87 ?  102 LYS   A CB   1 
ATOM   2124 C CB   B LYS   A 1 102 ? 24.518 0.738   -12.996 0.12 22.86 ?  102 LYS   A CB   1 
ATOM   2125 C CG   A LYS   A 1 102 ? 23.967 2.554   -11.754 0.88 30.30 ?  102 LYS   A CG   1 
ATOM   2126 C CG   B LYS   A 1 102 ? 24.545 1.967   -12.099 0.12 23.25 ?  102 LYS   A CG   1 
ATOM   2127 C CD   A LYS   A 1 102 ? 25.141 2.539   -10.781 0.88 31.70 ?  102 LYS   A CD   1 
ATOM   2128 C CD   B LYS   A 1 102 ? 25.573 1.796   -10.983 0.12 23.57 ?  102 LYS   A CD   1 
ATOM   2129 C CE   A LYS   A 1 102 ? 25.045 3.664   -9.761  0.88 32.84 ?  102 LYS   A CE   1 
ATOM   2130 C CE   B LYS   A 1 102 ? 25.544 2.952   -10.000 0.12 23.84 ?  102 LYS   A CE   1 
ATOM   2131 N NZ   A LYS   A 1 102 ? 26.158 3.612   -8.767  0.88 33.41 ?  102 LYS   A NZ   1 
ATOM   2132 N NZ   B LYS   A 1 102 ? 26.295 2.649   -8.752  0.12 23.99 ?  102 LYS   A NZ   1 
ATOM   2133 H H    A LYS   A 1 102 ? 21.654 0.539   -12.582 0.88 31.34 ?  102 LYS   A H    1 
ATOM   2134 H H    B LYS   A 1 102 ? 22.098 0.288   -12.760 0.12 25.92 ?  102 LYS   A H    1 
ATOM   2135 H HA   A LYS   A 1 102 ? 22.951 2.195   -14.289 0.88 32.74 ?  102 LYS   A HA   1 
ATOM   2136 H HA   B LYS   A 1 102 ? 23.539 1.608   -14.565 0.12 26.89 ?  102 LYS   A HA   1 
ATOM   2137 H HB2  A LYS   A 1 102 ? 24.111 0.594   -12.275 0.88 34.63 ?  102 LYS   A HB2  1 
ATOM   2138 H HB2  B LYS   A 1 102 ? 24.372 -0.044  -12.444 0.12 27.42 ?  102 LYS   A HB2  1 
ATOM   2139 H HB3  A LYS   A 1 102 ? 24.928 1.552   -13.239 0.88 34.63 ?  102 LYS   A HB3  1 
ATOM   2140 H HB3  B LYS   A 1 102 ? 25.389 0.672   -13.410 0.12 27.42 ?  102 LYS   A HB3  1 
ATOM   2141 H HG2  A LYS   A 1 102 ? 23.963 3.405   -12.218 0.88 36.35 ?  102 LYS   A HG2  1 
ATOM   2142 H HG2  B LYS   A 1 102 ? 24.794 2.744   -12.627 0.12 27.89 ?  102 LYS   A HG2  1 
ATOM   2143 H HG3  A LYS   A 1 102 ? 23.147 2.441   -11.248 0.88 36.35 ?  102 LYS   A HG3  1 
ATOM   2144 H HG3  B LYS   A 1 102 ? 23.673 2.098   -11.697 0.12 27.89 ?  102 LYS   A HG3  1 
ATOM   2145 H HD2  A LYS   A 1 102 ? 25.147 1.695   -10.301 0.88 38.03 ?  102 LYS   A HD2  1 
ATOM   2146 H HD2  B LYS   A 1 102 ? 25.379 0.982   -10.493 0.12 28.27 ?  102 LYS   A HD2  1 
ATOM   2147 H HD3  A LYS   A 1 102 ? 25.968 2.648   -11.276 0.88 38.03 ?  102 LYS   A HD3  1 
ATOM   2148 H HD3  B LYS   A 1 102 ? 26.460 1.751   -11.371 0.12 28.27 ?  102 LYS   A HD3  1 
ATOM   2149 H HE2  A LYS   A 1 102 ? 25.090 4.517   -10.223 0.88 39.40 ?  102 LYS   A HE2  1 
ATOM   2150 H HE2  B LYS   A 1 102 ? 25.916 3.753   -10.413 0.12 28.59 ?  102 LYS   A HE2  1 
ATOM   2151 H HE3  A LYS   A 1 102 ? 24.205 3.589   -9.282  0.88 39.40 ?  102 LYS   A HE3  1 
ATOM   2152 H HE3  B LYS   A 1 102 ? 24.629 3.099   -9.739  0.12 28.59 ?  102 LYS   A HE3  1 
ATOM   2153 H HZ1  A LYS   A 1 102 ? 26.077 4.280   -8.185  0.88 40.08 ?  102 LYS   A HZ1  1 
ATOM   2154 H HZ1  B LYS   A 1 102 ? 26.259 3.345   -8.198  0.12 28.77 ?  102 LYS   A HZ1  1 
ATOM   2155 H HZ2  A LYS   A 1 102 ? 26.135 2.839   -8.326  0.88 40.08 ?  102 LYS   A HZ2  1 
ATOM   2156 H HZ2  B LYS   A 1 102 ? 25.935 1.940   -8.349  0.12 28.77 ?  102 LYS   A HZ2  1 
ATOM   2157 H HZ3  A LYS   A 1 102 ? 26.941 3.684   -9.183  0.88 40.08 ?  102 LYS   A HZ3  1 
ATOM   2158 H HZ3  B LYS   A 1 102 ? 27.144 2.474   -8.944  0.12 28.77 ?  102 LYS   A HZ3  1 
ATOM   2159 N N    A GLY   A 1 103 ? 22.340 -0.728  -14.933 0.88 27.40 ?  103 GLY   A N    1 
ATOM   2160 N N    B GLY   A 1 103 ? 22.822 -1.252  -15.354 0.12 22.88 ?  103 GLY   A N    1 
ATOM   2161 C CA   A GLY   A 1 103 ? 22.547 -1.830  -15.854 0.88 27.02 ?  103 GLY   A CA   1 
ATOM   2162 C CA   B GLY   A 1 103 ? 23.085 -2.378  -16.226 0.12 22.94 ?  103 GLY   A CA   1 
ATOM   2163 C C    A GLY   A 1 103 ? 23.392 -2.971  -15.331 0.88 26.97 ?  103 GLY   A C    1 
ATOM   2164 C C    B GLY   A 1 103 ? 23.920 -3.472  -15.609 0.12 22.96 ?  103 GLY   A C    1 
ATOM   2165 O O    A GLY   A 1 103 ? 23.921 -3.749  -16.130 0.88 28.03 ?  103 GLY   A O    1 
ATOM   2166 O O    B GLY   A 1 103 ? 24.495 -4.285  -16.340 0.12 23.06 ?  103 GLY   A O    1 
ATOM   2167 H H    A GLY   A 1 103 ? 21.594 -0.762  -14.512 0.88 32.86 ?  103 GLY   A H    1 
ATOM   2168 H H    B GLY   A 1 103 ? 22.022 -1.224  -15.042 0.12 27.45 ?  103 GLY   A H    1 
ATOM   2169 H HA2  A GLY   A 1 103 ? 21.682 -2.190  -16.108 0.88 32.41 ?  103 GLY   A HA2  1 
ATOM   2170 H HA2  B GLY   A 1 103 ? 22.246 -2.765  -16.519 0.12 27.52 ?  103 GLY   A HA2  1 
ATOM   2171 H HA3  A GLY   A 1 103 ? 22.973 -1.490  -16.658 0.88 32.41 ?  103 GLY   A HA3  1 
ATOM   2172 H HA3  B GLY   A 1 103 ? 23.562 -2.054  -17.003 0.12 27.52 ?  103 GLY   A HA3  1 
ATOM   2173 N N    A GLU   A 1 104 ? 23.530 -3.108  -14.016 0.88 24.91 ?  104 GLU   A N    1 
ATOM   2174 N N    B GLU   A 1 104 ? 24.004 -3.525  -14.283 0.12 22.76 ?  104 GLU   A N    1 
ATOM   2175 C CA   A GLU   A 1 104 ? 24.420 -4.111  -13.447 0.88 23.06 ?  104 GLU   A CA   1 
ATOM   2176 C CA   B GLU   A 1 104 ? 24.863 -4.494  -13.621 0.12 22.60 ?  104 GLU   A CA   1 
ATOM   2177 C C    A GLU   A 1 104 ? 23.735 -5.474  -13.350 0.88 23.00 ?  104 GLU   A C    1 
ATOM   2178 C C    B GLU   A 1 104 ? 24.153 -5.834  -13.472 0.12 22.83 ?  104 GLU   A C    1 
ATOM   2179 O O    A GLU   A 1 104 ? 22.511 -5.576  -13.220 0.88 23.57 ?  104 GLU   A O    1 
ATOM   2180 O O    B GLU   A 1 104 ? 22.962 -5.897  -13.154 0.12 22.79 ?  104 GLU   A O    1 
ATOM   2181 C CB   A GLU   A 1 104 ? 24.950 -3.631  -12.092 0.88 21.24 ?  104 GLU   A CB   1 
ATOM   2182 C CB   B GLU   A 1 104 ? 25.310 -3.957  -12.261 0.12 22.35 ?  104 GLU   A CB   1 
ATOM   2183 C CG   A GLU   A 1 104 ? 25.876 -2.417  -12.260 0.88 20.65 ?  104 GLU   A CG   1 
ATOM   2184 C CG   B GLU   A 1 104 ? 26.175 -2.709  -12.377 0.12 22.25 ?  104 GLU   A CG   1 
ATOM   2185 C CD   A GLU   A 1 104 ? 26.193 -1.637  -10.990 0.88 19.77 ?  104 GLU   A CD   1 
ATOM   2186 C CD   B GLU   A 1 104 ? 26.426 -2.034  -11.041 0.12 22.22 ?  104 GLU   A CD   1 
ATOM   2187 O OE1  A GLU   A 1 104 ? 25.616 -1.911  -9.915  0.88 18.69 ?  104 GLU   A OE1  1 
ATOM   2188 O OE1  B GLU   A 1 104 ? 25.874 -2.499  -10.022 0.12 22.23 ?  104 GLU   A OE1  1 
ATOM   2189 O OE2  A GLU   A 1 104 ? 27.040 -0.717  -11.093 0.88 20.61 -1 104 GLU   A OE2  1 
ATOM   2190 O OE2  B GLU   A 1 104 ? 27.177 -1.036  -11.012 0.12 22.27 -1 104 GLU   A OE2  1 
ATOM   2191 H H    A GLU   A 1 104 ? 23.121 -2.628  -13.434 0.88 29.88 ?  104 GLU   A H    1 
ATOM   2192 H H    B GLU   A 1 104 ? 23.572 -3.007  -13.748 0.12 27.30 ?  104 GLU   A H    1 
ATOM   2193 H HA   A GLU   A 1 104 ? 25.181 -4.212  -14.038 0.88 27.66 ?  104 GLU   A HA   1 
ATOM   2194 H HA   B GLU   A 1 104 ? 25.656 -4.633  -14.160 0.12 27.11 ?  104 GLU   A HA   1 
ATOM   2195 H HB2  A GLU   A 1 104 ? 24.204 -3.376  -11.529 0.88 25.48 ?  104 GLU   A HB2  1 
ATOM   2196 H HB2  B GLU   A 1 104 ? 24.528 -3.730  -11.735 0.12 26.81 ?  104 GLU   A HB2  1 
ATOM   2197 H HB3  A GLU   A 1 104 ? 25.456 -4.349  -11.678 0.88 25.48 ?  104 GLU   A HB3  1 
ATOM   2198 H HB3  B GLU   A 1 104 ? 25.830 -4.639  -11.805 0.12 26.81 ?  104 GLU   A HB3  1 
ATOM   2199 H HG2  A GLU   A 1 104 ? 26.716 -2.727  -12.625 0.88 24.77 ?  104 GLU   A HG2  1 
ATOM   2200 H HG2  B GLU   A 1 104 ? 27.035 -2.956  -12.755 0.12 26.69 ?  104 GLU   A HG2  1 
ATOM   2201 H HG3  A GLU   A 1 104 ? 25.456 -1.800  -12.877 0.88 24.77 ?  104 GLU   A HG3  1 
ATOM   2202 H HG3  B GLU   A 1 104 ? 25.732 -2.072  -12.960 0.12 26.69 ?  104 GLU   A HG3  1 
ATOM   2203 N N    A ASP   A 1 105 ? 24.550 -6.526  -13.411 0.88 23.64 ?  105 ASP   A N    1 
ATOM   2204 N N    B ASP   A 1 105 ? 24.904 -6.906  -13.714 0.12 23.25 ?  105 ASP   A N    1 
ATOM   2205 C CA   A ASP   A 1 105 ? 24.061 -7.894  -13.551 0.88 24.70 ?  105 ASP   A CA   1 
ATOM   2206 C CA   B ASP   A 1 105 ? 24.373 -8.264  -13.716 0.12 23.71 ?  105 ASP   A CA   1 
ATOM   2207 C C    A ASP   A 1 105 ? 23.380 -8.354  -12.265 0.88 22.58 ?  105 ASP   A C    1 
ATOM   2208 C C    B ASP   A 1 105 ? 23.632 -8.563  -12.420 0.12 23.33 ?  105 ASP   A C    1 
ATOM   2209 O O    A ASP   A 1 105 ? 24.012 -8.409  -11.208 0.88 20.57 ?  105 ASP   A O    1 
ATOM   2210 O O    B ASP   A 1 105 ? 24.223 -8.551  -11.336 0.12 23.15 ?  105 ASP   A O    1 
ATOM   2211 C CB   A ASP   A 1 105 ? 25.243 -8.802  -13.880 0.88 27.97 ?  105 ASP   A CB   1 
ATOM   2212 C CB   B ASP   A 1 105 ? 25.544 -9.234  -13.893 0.12 24.55 ?  105 ASP   A CB   1 
ATOM   2213 C CG   A ASP   A 1 105 ? 24.834 -10.239 -14.101 0.88 30.75 ?  105 ASP   A CG   1 
ATOM   2214 C CG   B ASP   A 1 105 ? 25.102 -10.683 -13.958 0.12 25.26 ?  105 ASP   A CG   1 
ATOM   2215 O OD1  A ASP   A 1 105 ? 23.618 -10.500 -14.191 0.88 31.21 ?  105 ASP   A OD1  1 
ATOM   2216 O OD1  B ASP   A 1 105 ? 23.883 -10.936 -14.042 0.12 25.43 ?  105 ASP   A OD1  1 
ATOM   2217 O OD2  A ASP   A 1 105 ? 25.735 -11.104 -14.187 0.88 32.60 -1 105 ASP   A OD2  1 
ATOM   2218 O OD2  B ASP   A 1 105 ? 25.981 -11.571 -13.920 0.12 25.61 -1 105 ASP   A OD2  1 
ATOM   2219 H H    A ASP   A 1 105 ? 25.408 -6.471  -13.370 0.88 28.36 ?  105 ASP   A H    1 
ATOM   2220 H H    B ASP   A 1 105 ? 25.743 -6.869  -13.886 0.12 27.89 ?  105 ASP   A H    1 
ATOM   2221 H HA   A ASP   A 1 105 ? 23.419 -7.944  -14.272 0.88 29.63 ?  105 ASP   A HA   1 
ATOM   2222 H HA   B ASP   A 1 105 ? 23.759 -8.378  -14.458 0.12 28.45 ?  105 ASP   A HA   1 
ATOM   2223 H HB2  A ASP   A 1 105 ? 25.669 -8.483  -14.693 0.88 33.55 ?  105 ASP   A HB2  1 
ATOM   2224 H HB2  B ASP   A 1 105 ? 26.011 -9.017  -14.719 0.12 29.45 ?  105 ASP   A HB2  1 
ATOM   2225 H HB3  A ASP   A 1 105 ? 25.876 -8.782  -13.146 0.88 33.55 ?  105 ASP   A HB3  1 
ATOM   2226 H HB3  B ASP   A 1 105 ? 26.150 -9.140  -13.141 0.12 29.45 ?  105 ASP   A HB3  1 
ATOM   2227 N N    A ILE   A 1 106 ? 22.098 -8.718  -12.362 0.88 22.43 ?  106 ILE   A N    1 
ATOM   2228 N N    B ILE   A 1 106 ? 22.329 -8.838  -12.537 0.12 23.14 ?  106 ILE   A N    1 
ATOM   2229 C CA   A ILE   A 1 106 ? 21.341 -9.113  -11.180 0.88 22.10 ?  106 ILE   A CA   1 
ATOM   2230 C CA   B ILE   A 1 106 ? 21.522 -9.146  -11.361 0.12 22.95 ?  106 ILE   A CA   1 
ATOM   2231 C C    A ILE   A 1 106 ? 21.881 -10.393 -10.565 0.88 21.28 ?  106 ILE   A C    1 
ATOM   2232 C C    B ILE   A 1 106 ? 21.983 -10.422 -10.673 0.12 22.44 ?  106 ILE   A C    1 
ATOM   2233 O O    A ILE   A 1 106 ? 21.666 -10.631 -9.373  0.88 20.64 ?  106 ILE   A O    1 
ATOM   2234 O O    B ILE   A 1 106 ? 21.732 -10.601 -9.476  0.12 22.39 ?  106 ILE   A O    1 
ATOM   2235 C CB   A ILE   A 1 106 ? 19.834 -9.211  -11.501 0.88 23.78 ?  106 ILE   A CB   1 
ATOM   2236 C CB   B ILE   A 1 106 ? 20.017 -9.191  -11.712 0.12 23.35 ?  106 ILE   A CB   1 
ATOM   2237 C CG1  A ILE   A 1 106 ? 18.999 -9.298  -10.218 0.88 24.51 ?  106 ILE   A CG1  1 
ATOM   2238 C CG1  B ILE   A 1 106 ? 19.167 -9.116  -10.442 0.12 23.53 ?  106 ILE   A CG1  1 
ATOM   2239 C CG2  A ILE   A 1 106 ? 19.552 -10.409 -12.393 0.88 24.30 ?  106 ILE   A CG2  1 
ATOM   2240 C CG2  B ILE   A 1 106 ? 19.677 -10.459 -12.473 0.12 23.45 ?  106 ILE   A CG2  1 
ATOM   2241 C CD1  A ILE   A 1 106 ? 19.080 -8.061  -9.343  0.88 24.89 ?  106 ILE   A CD1  1 
ATOM   2242 C CD1  B ILE   A 1 106 ? 19.433 -7.888  -9.596  0.12 23.61 ?  106 ILE   A CD1  1 
ATOM   2243 H H    A ILE   A 1 106 ? 21.658 -8.749  -13.092 0.88 26.91 ?  106 ILE   A H    1 
ATOM   2244 H H    B ILE   A 1 106 ? 21.895 -8.833  -13.277 0.12 27.76 ?  106 ILE   A H    1 
ATOM   2245 H HA   A ILE   A 1 106 ? 21.453 -8.430  -10.511 0.88 26.50 ?  106 ILE   A HA   1 
ATOM   2246 H HA   B ILE   A 1 106 ? 21.652 -8.429  -10.728 0.12 27.53 ?  106 ILE   A HA   1 
ATOM   2247 H HB   A ILE   A 1 106 ? 19.576 -8.409  -11.978 0.88 28.52 ?  106 ILE   A HB   1 
ATOM   2248 H HB   B ILE   A 1 106 ? 19.805 -8.429  -12.271 0.12 28.01 ?  106 ILE   A HB   1 
ATOM   2249 H HG12 A ILE   A 1 106 ? 18.068 -9.424  -10.459 0.88 29.40 ?  106 ILE   A HG12 1 
ATOM   2250 H HG12 B ILE   A 1 106 ? 18.231 -9.103  -10.695 0.12 28.23 ?  106 ILE   A HG12 1 
ATOM   2251 H HG13 A ILE   A 1 106 ? 19.305 -10.052 -9.690  0.88 29.40 ?  106 ILE   A HG13 1 
ATOM   2252 H HG13 B ILE   A 1 106 ? 19.348 -9.898  -9.897  0.12 28.23 ?  106 ILE   A HG13 1 
ATOM   2253 H HG21 A ILE   A 1 106 ? 18.645 -10.340 -12.732 0.88 29.15 ?  106 ILE   A HG21 1 
ATOM   2254 H HG21 B ILE   A 1 106 ? 18.801 -10.356 -12.877 0.12 28.13 ?  106 ILE   A HG21 1 
ATOM   2255 H HG22 A ILE   A 1 106 ? 20.182 -10.407 -13.129 0.88 29.15 ?  106 ILE   A HG22 1 
ATOM   2256 H HG22 B ILE   A 1 106 ? 20.345 -10.601 -13.159 0.12 28.13 ?  106 ILE   A HG22 1 
ATOM   2257 H HG23 A ILE   A 1 106 ? 19.649 -11.222 -11.874 0.88 29.15 ?  106 ILE   A HG23 1 
ATOM   2258 H HG23 B ILE   A 1 106 ? 19.669 -11.207 -11.855 0.12 28.13 ?  106 ILE   A HG23 1 
ATOM   2259 H HD11 A ILE   A 1 106 ? 18.378 -8.101  -8.676  0.88 29.85 ?  106 ILE   A HD11 1 
ATOM   2260 H HD11 B ILE   A 1 106 ? 18.672 -7.735  -9.018  0.12 28.33 ?  106 ILE   A HD11 1 
ATOM   2261 H HD12 A ILE   A 1 106 ? 19.947 -8.036  -8.907  0.88 29.85 ?  106 ILE   A HD12 1 
ATOM   2262 H HD12 B ILE   A 1 106 ? 20.230 -8.039  -9.062  0.12 28.33 ?  106 ILE   A HD12 1 
ATOM   2263 H HD13 A ILE   A 1 106 ? 18.965 -7.274  -9.898  0.88 29.85 ?  106 ILE   A HD13 1 
ATOM   2264 H HD13 B ILE   A 1 106 ? 19.564 -7.125  -10.181 0.12 28.33 ?  106 ILE   A HD13 1 
ATOM   2265 N N    A GLN   A 1 107 ? 22.591 -11.219 -11.347 0.88 21.91 ?  107 GLN   A N    1 
ATOM   2266 N N    B GLN   A 1 107 ? 22.657 -11.320 -11.397 0.12 21.97 ?  107 GLN   A N    1 
ATOM   2267 C CA   A GLN   A 1 107 ? 23.209 -12.421 -10.795 0.88 24.02 ?  107 GLN   A CA   1 
ATOM   2268 C CA   B GLN   A 1 107 ? 23.246 -12.491 -10.760 0.12 21.67 ?  107 GLN   A CA   1 
ATOM   2269 C C    A GLN   A 1 107 ? 24.184 -12.074 -9.679  0.88 21.36 ?  107 GLN   A C    1 
ATOM   2270 C C    B GLN   A 1 107 ? 24.293 -12.117 -9.723  0.12 19.76 ?  107 GLN   A C    1 
ATOM   2271 O O    A GLN   A 1 107 ? 24.408 -12.885 -8.772  0.88 22.52 ?  107 GLN   A O    1 
ATOM   2272 O O    B GLN   A 1 107 ? 24.694 -12.978 -8.932  0.12 20.09 ?  107 GLN   A O    1 
ATOM   2273 C CB   A GLN   A 1 107 ? 23.917 -13.201 -11.909 0.88 28.64 ?  107 GLN   A CB   1 
ATOM   2274 C CB   B GLN   A 1 107 ? 23.859 -13.423 -11.809 0.12 23.20 ?  107 GLN   A CB   1 
ATOM   2275 C CG   A GLN   A 1 107 ? 23.066 -13.406 -13.160 0.88 33.44 ?  107 GLN   A CG   1 
ATOM   2276 C CG   B GLN   A 1 107 ? 22.836 -14.266 -12.552 0.12 24.59 ?  107 GLN   A CG   1 
ATOM   2277 C CD   A GLN   A 1 107 ? 21.770 -14.139 -12.875 0.88 37.23 ?  107 GLN   A CD   1 
ATOM   2278 C CD   B GLN   A 1 107 ? 22.072 -15.195 -11.629 0.12 25.77 ?  107 GLN   A CD   1 
ATOM   2279 O OE1  A GLN   A 1 107 ? 21.766 -15.195 -12.242 0.88 38.71 ?  107 GLN   A OE1  1 
ATOM   2280 O OE1  B GLN   A 1 107 ? 22.622 -15.713 -10.657 0.12 26.10 ?  107 GLN   A OE1  1 
ATOM   2281 N NE2  A GLN   A 1 107 ? 20.659 -13.576 -13.338 0.88 38.58 ?  107 GLN   A NE2  1 
ATOM   2282 N NE2  B GLN   A 1 107 ? 20.794 -15.400 -11.921 0.12 26.24 ?  107 GLN   A NE2  1 
ATOM   2283 H H    A GLN   A 1 107 ? 22.732 -11.101 -12.183 0.88 26.28 ?  107 GLN   A H    1 
ATOM   2284 H H    B GLN   A 1 107 ? 22.783 -11.272 -12.244 0.12 26.35 ?  107 GLN   A H    1 
ATOM   2285 H HA   A GLN   A 1 107 ? 22.528 -12.999 -10.423 0.88 28.82 ?  107 GLN   A HA   1 
ATOM   2286 H HA   B GLN   A 1 107 ? 22.546 -12.978 -10.301 0.12 25.99 ?  107 GLN   A HA   1 
ATOM   2287 H HB2  A GLN   A 1 107 ? 24.719 -12.722 -12.172 0.88 34.35 ?  107 GLN   A HB2  1 
ATOM   2288 H HB2  B GLN   A 1 107 ? 24.334 -12.891 -12.466 0.12 27.83 ?  107 GLN   A HB2  1 
ATOM   2289 H HB3  A GLN   A 1 107 ? 24.160 -14.083 -11.577 0.88 34.35 ?  107 GLN   A HB3  1 
ATOM   2290 H HB3  B GLN   A 1 107 ? 24.476 -14.031 -11.370 0.12 27.83 ?  107 GLN   A HB3  1 
ATOM   2291 H HG2  A GLN   A 1 107 ? 22.843 -12.543 -13.544 0.88 40.12 ?  107 GLN   A HG2  1 
ATOM   2292 H HG2  B GLN   A 1 107 ? 22.197 -13.679 -12.985 0.12 29.50 ?  107 GLN   A HG2  1 
ATOM   2293 H HG3  A GLN   A 1 107 ? 23.571 -13.927 -13.802 0.88 40.12 ?  107 GLN   A HG3  1 
ATOM   2294 H HG3  B GLN   A 1 107 ? 23.291 -14.809 -13.214 0.12 29.50 ?  107 GLN   A HG3  1 
ATOM   2295 H HE21 A GLN   A 1 107 ? 20.699 -12.837 -13.775 0.88 46.28 ?  107 GLN   A HE21 1 
ATOM   2296 H HE21 B GLN   A 1 107 ? 20.444 -15.018 -12.607 0.12 31.48 ?  107 GLN   A HE21 1 
ATOM   2297 H HE22 A GLN   A 1 107 ? 19.899 -13.954 -13.202 0.88 46.28 ?  107 GLN   A HE22 1 
ATOM   2298 H HE22 B GLN   A 1 107 ? 20.319 -15.916 -11.425 0.12 31.48 ?  107 GLN   A HE22 1 
ATOM   2299 N N    . LEU   A 1 108 ? 24.744 -10.861 -9.703  1.00 17.78 ?  108 LEU   A N    1 
ATOM   2300 C CA   . LEU   A 1 108 ? 25.657 -10.421 -8.661  1.00 14.81 ?  108 LEU   A CA   1 
ATOM   2301 C C    . LEU   A 1 108 ? 24.955 -10.249 -7.324  1.00 13.01 ?  108 LEU   A C    1 
ATOM   2302 O O    . LEU   A 1 108 ? 25.634 -10.097 -6.306  1.00 13.33 ?  108 LEU   A O    1 
ATOM   2303 C CB   . LEU   A 1 108 ? 26.368 -9.125  -9.070  1.00 14.66 ?  108 LEU   A CB   1 
ATOM   2304 C CG   . LEU   A 1 108 ? 27.379 -9.319  -10.201 1.00 16.18 ?  108 LEU   A CG   1 
ATOM   2305 C CD1  . LEU   A 1 108 ? 27.872 -7.989  -10.742 1.00 16.74 ?  108 LEU   A CD1  1 
ATOM   2306 C CD2  . LEU   A 1 108 ? 28.559 -10.160 -9.730  1.00 17.85 ?  108 LEU   A CD2  1 
ATOM   2307 H H    A LEU   A 1 108 ? 24.604 -10.279 -10.314 0.88 21.33 ?  108 LEU   A H    1 
ATOM   2308 H H    B LEU   A 1 108 ? 24.544 -10.262 -10.279 0.12 21.33 ?  108 LEU   A H    1 
ATOM   2309 H HA   . LEU   A 1 108 ? 26.334 -11.100 -8.533  1.00 17.76 ?  108 LEU   A HA   1 
ATOM   2310 H HB2  . LEU   A 1 108 ? 25.703 -8.493  -9.378  1.00 17.59 ?  108 LEU   A HB2  1 
ATOM   2311 H HB3  . LEU   A 1 108 ? 26.838 -8.764  -8.304  1.00 17.59 ?  108 LEU   A HB3  1 
ATOM   2312 H HG   . LEU   A 1 108 ? 26.950 -9.795  -10.930 1.00 19.41 ?  108 LEU   A HG   1 
ATOM   2313 H HD11 . LEU   A 1 108 ? 28.484 -8.154  -11.481 1.00 20.08 ?  108 LEU   A HD11 1 
ATOM   2314 H HD12 . LEU   A 1 108 ? 27.114 -7.472  -11.053 1.00 20.08 ?  108 LEU   A HD12 1 
ATOM   2315 H HD13 . LEU   A 1 108 ? 28.334 -7.510  -10.036 1.00 20.08 ?  108 LEU   A HD13 1 
ATOM   2316 H HD21 . LEU   A 1 108 ? 29.271 -10.098 -10.382 1.00 21.41 ?  108 LEU   A HD21 1 
ATOM   2317 H HD22 . LEU   A 1 108 ? 28.860 -9.822  -8.872  1.00 21.41 ?  108 LEU   A HD22 1 
ATOM   2318 H HD23 . LEU   A 1 108 ? 28.271 -11.082 -9.638  1.00 21.41 ?  108 LEU   A HD23 1 
ATOM   2319 N N    . LEU   A 1 109 ? 23.621 -10.302 -7.292  1.00 12.46 ?  109 LEU   A N    1 
ATOM   2320 C CA   . LEU   A 1 109 ? 22.921 -10.181 -6.021  1.00 11.68 ?  109 LEU   A CA   1 
ATOM   2321 C C    . LEU   A 1 109 ? 23.269 -11.332 -5.084  1.00 10.86 ?  109 LEU   A C    1 
ATOM   2322 O O    . LEU   A 1 109 ? 23.410 -11.133 -3.872  1.00 11.41 ?  109 LEU   A O    1 
ATOM   2323 C CB   . LEU   A 1 109 ? 21.417 -10.088 -6.272  1.00 12.34 ?  109 LEU   A CB   1 
ATOM   2324 C CG   . LEU   A 1 109 ? 20.533 -9.810  -5.059  1.00 12.71 ?  109 LEU   A CG   1 
ATOM   2325 C CD1  . LEU   A 1 109 ? 20.988 -8.544  -4.336  1.00 13.02 ?  109 LEU   A CD1  1 
ATOM   2326 C CD2  . LEU   A 1 109 ? 19.072 -9.690  -5.475  1.00 13.74 ?  109 LEU   A CD2  1 
ATOM   2327 H H    . LEU   A 1 109 ? 23.110 -10.411 -7.975  1.00 14.94 ?  109 LEU   A H    1 
ATOM   2328 H HA   . LEU   A 1 109 ? 23.203 -9.358  -5.593  1.00 14.00 ?  109 LEU   A HA   1 
ATOM   2329 H HB2  . LEU   A 1 109 ? 21.262 -9.369  -6.907  1.00 14.80 ?  109 LEU   A HB2  1 
ATOM   2330 H HB3  . LEU   A 1 109 ? 21.119 -10.923 -6.655  1.00 14.80 ?  109 LEU   A HB3  1 
ATOM   2331 H HG   . LEU   A 1 109 ? 20.606 -10.548 -4.439  1.00 15.24 ?  109 LEU   A HG   1 
ATOM   2332 H HD11 . LEU   A 1 109 ? 20.318 -8.284  -3.688  1.00 15.61 ?  109 LEU   A HD11 1 
ATOM   2333 H HD12 . LEU   A 1 109 ? 21.833 -8.718  -3.889  1.00 15.61 ?  109 LEU   A HD12 1 
ATOM   2334 H HD13 . LEU   A 1 109 ? 21.108 -7.831  -4.990  1.00 15.61 ?  109 LEU   A HD13 1 
ATOM   2335 H HD21 . LEU   A 1 109 ? 18.544 -9.401  -4.709  1.00 16.48 ?  109 LEU   A HD21 1 
ATOM   2336 H HD22 . LEU   A 1 109 ? 18.991 -9.039  -6.190  1.00 16.48 ?  109 LEU   A HD22 1 
ATOM   2337 H HD23 . LEU   A 1 109 ? 18.753 -10.555 -5.781  1.00 16.48 ?  109 LEU   A HD23 1 
ATOM   2338 N N    . LYS   A 1 110 ? 23.412 -12.546 -5.619  1.00 10.92 ?  110 LYS   A N    1 
ATOM   2339 C CA   . LYS   A 1 110 ? 23.799 -13.667 -4.766  1.00 10.74 ?  110 LYS   A CA   1 
ATOM   2340 C C    . LYS   A 1 110 ? 25.182 -13.439 -4.164  1.00 10.46 ?  110 LYS   A C    1 
ATOM   2341 O O    . LYS   A 1 110 ? 25.386 -13.638 -2.965  1.00 10.56 ?  110 LYS   A O    1 
ATOM   2342 C CB   . LYS   A 1 110 ? 23.724 -14.988 -5.534  1.00 11.64 ?  110 LYS   A CB   1 
ATOM   2343 C CG   . LYS   A 1 110 ? 23.928 -16.203 -4.629  1.00 11.70 ?  110 LYS   A CG   1 
ATOM   2344 C CD   . LYS   A 1 110 ? 23.710 -17.525 -5.343  1.00 12.20 ?  110 LYS   A CD   1 
ATOM   2345 C CE   . LYS   A 1 110 ? 23.798 -18.700 -4.384  1.00 13.48 ?  110 LYS   A CE   1 
ATOM   2346 N NZ   . LYS   A 1 110 ? 22.609 -18.834 -3.513  1.00 13.76 ?  110 LYS   A NZ   1 
ATOM   2347 H H    . LYS   A 1 110 ? 23.290 -12.746 -6.447  1.00 13.10 ?  110 LYS   A H    1 
ATOM   2348 H HA   . LYS   A 1 110 ? 23.164 -13.722 -4.028  1.00 12.88 ?  110 LYS   A HA   1 
ATOM   2349 H HB2  . LYS   A 1 110 ? 22.849 -15.066 -5.945  1.00 13.96 ?  110 LYS   A HB2  1 
ATOM   2350 H HB3  . LYS   A 1 110 ? 24.415 -14.999 -6.209  1.00 13.96 ?  110 LYS   A HB3  1 
ATOM   2351 H HG2  . LYS   A 1 110 ? 24.834 -16.192 -4.284  1.00 14.03 ?  110 LYS   A HG2  1 
ATOM   2352 H HG3  . LYS   A 1 110 ? 23.296 -16.155 -3.890  1.00 14.03 ?  110 LYS   A HG3  1 
ATOM   2353 H HD2  . LYS   A 1 110 ? 22.831 -17.528 -5.747  1.00 14.63 ?  110 LYS   A HD2  1 
ATOM   2354 H HD3  . LYS   A 1 110 ? 24.396 -17.634 -6.019  1.00 14.63 ?  110 LYS   A HD3  1 
ATOM   2355 H HE2  . LYS   A 1 110 ? 23.891 -19.517 -4.891  1.00 16.16 ?  110 LYS   A HE2  1 
ATOM   2356 H HE3  . LYS   A 1 110 ? 24.571 -18.578 -3.805  1.00 16.16 ?  110 LYS   A HE3  1 
ATOM   2357 H HZ1  . LYS   A 1 110 ? 22.700 -19.531 -2.971  1.00 16.50 ?  110 LYS   A HZ1  1 
ATOM   2358 H HZ2  . LYS   A 1 110 ? 22.499 -18.097 -3.024  1.00 16.50 ?  110 LYS   A HZ2  1 
ATOM   2359 H HZ3  . LYS   A 1 110 ? 21.878 -18.953 -4.015  1.00 16.50 ?  110 LYS   A HZ3  1 
ATOM   2360 N N    . SER   A 1 111 ? 26.139 -12.993 -4.982  1.00 10.57 ?  111 SER   A N    1 
ATOM   2361 C CA   . SER   A 1 111 ? 27.471 -12.686 -4.468  1.00 10.68 ?  111 SER   A CA   1 
ATOM   2362 C C    . SER   A 1 111 ? 27.408 -11.642 -3.356  1.00 10.54 ?  111 SER   A C    1 
ATOM   2363 O O    . SER   A 1 111 ? 28.105 -11.752 -2.340  1.00 10.91 ?  111 SER   A O    1 
ATOM   2364 C CB   . SER   A 1 111 ? 28.361 -12.194 -5.607  1.00 11.92 ?  111 SER   A CB   1 
ATOM   2365 O OG   . SER   A 1 111 ? 28.469 -13.185 -6.619  1.00 14.06 ?  111 SER   A OG   1 
ATOM   2366 H H    . SER   A 1 111 ? 26.037 -12.859 -5.823  1.00 12.67 ?  111 SER   A H    1 
ATOM   2367 H HA   . SER   A 1 111 ? 27.864 -13.494 -4.102  1.00 12.81 ?  111 SER   A HA   1 
ATOM   2368 H HB2  . SER   A 1 111 ? 27.965 -11.398 -5.995  1.00 14.30 ?  111 SER   A HB2  1 
ATOM   2369 H HB3  . SER   A 1 111 ? 29.240 -11.986 -5.252  1.00 14.30 ?  111 SER   A HB3  1 
ATOM   2370 H HG   . SER   A 1 111 ? 28.983 -12.902 -7.234  1.00 16.87 ?  111 SER   A HG   1 
ATOM   2371 N N    . ALA   A 1 112 ? 26.565 -10.622 -3.533  1.00 10.36 ?  112 ALA   A N    1 
ATOM   2372 C CA   . ALA   A 1 112 ? 26.414 -9.586  -2.513  1.00 10.19 ?  112 ALA   A CA   1 
ATOM   2373 C C    . ALA   A 1 112 ? 25.939 -10.188 -1.193  1.00 10.26 ?  112 ALA   A C    1 
ATOM   2374 O O    . ALA   A 1 112 ? 26.487 -9.889  -0.123  1.00 10.48 ?  112 ALA   A O    1 
ATOM   2375 C CB   . ALA   A 1 112 ? 25.458 -8.499  -3.010  1.00 10.62 ?  112 ALA   A CB   1 
ATOM   2376 H H    . ALA   A 1 112 ? 26.074 -10.504 -4.226  1.00 12.42 ?  112 ALA   A H    1 
ATOM   2377 H HA   . ALA   A 1 112 ? 27.274 -9.166  -2.352  1.00 12.22 ?  112 ALA   A HA   1 
ATOM   2378 H HB1  . ALA   A 1 112 ? 25.380 -7.803  -2.328  1.00 12.73 ?  112 ALA   A HB1  1 
ATOM   2379 H HB2  . ALA   A 1 112 ? 25.808 -8.111  -3.826  1.00 12.73 ?  112 ALA   A HB2  1 
ATOM   2380 H HB3  . ALA   A 1 112 ? 24.585 -8.887  -3.175  1.00 12.73 ?  112 ALA   A HB3  1 
ATOM   2381 N N    . TYR   A 1 113 ? 24.906 -11.036 -1.245  1.00 10.17 ?  113 TYR   A N    1 
ATOM   2382 C CA   . TYR   A 1 113 ? 24.397 -11.644 -0.020  1.00 10.06 ?  113 TYR   A CA   1 
ATOM   2383 C C    . TYR   A 1 113 ? 25.401 -12.595 0.625   1.00 9.61  ?  113 TYR   A C    1 
ATOM   2384 O O    . TYR   A 1 113 ? 25.369 -12.779 1.845   1.00 10.20 ?  113 TYR   A O    1 
ATOM   2385 C CB   . TYR   A 1 113 ? 23.083 -12.377 -0.295  1.00 10.45 ?  113 TYR   A CB   1 
ATOM   2386 C CG   . TYR   A 1 113 ? 21.864 -11.490 -0.204  1.00 10.38 ?  113 TYR   A CG   1 
ATOM   2387 C CD1  . TYR   A 1 113 ? 21.501 -10.897 1.002   1.00 10.36 ?  113 TYR   A CD1  1 
ATOM   2388 C CD2  . TYR   A 1 113 ? 21.060 -11.261 -1.311  1.00 10.59 ?  113 TYR   A CD2  1 
ATOM   2389 C CE1  . TYR   A 1 113 ? 20.375 -10.101 1.103   1.00 10.96 ?  113 TYR   A CE1  1 
ATOM   2390 C CE2  . TYR   A 1 113 ? 19.911 -10.464 -1.217  1.00 10.85 ?  113 TYR   A CE2  1 
ATOM   2391 C CZ   . TYR   A 1 113 ? 19.582 -9.892  -0.008  1.00 10.86 ?  113 TYR   A CZ   1 
ATOM   2392 O OH   . TYR   A 1 113 ? 18.460 -9.101  0.119   1.00 11.90 ?  113 TYR   A OH   1 
ATOM   2393 H H    . TYR   A 1 113 ? 24.494 -11.268 -1.964  1.00 12.20 ?  113 TYR   A H    1 
ATOM   2394 H HA   . TYR   A 1 113 ? 24.215 -10.939 0.619   1.00 12.06 ?  113 TYR   A HA   1 
ATOM   2395 H HB2  . TYR   A 1 113 ? 23.111 -12.743 -1.190  1.00 12.53 ?  113 TYR   A HB2  1 
ATOM   2396 H HB3  . TYR   A 1 113 ? 22.983 -13.088 0.353   1.00 12.53 ?  113 TYR   A HB3  1 
ATOM   2397 H HD1  . TYR   A 1 113 ? 22.032 -11.040 1.757   1.00 12.42 ?  113 TYR   A HD1  1 
ATOM   2398 H HD2  . TYR   A 1 113 ? 21.276 -11.658 -2.118  1.00 12.70 ?  113 TYR   A HD2  1 
ATOM   2399 H HE1  . TYR   A 1 113 ? 20.151 -9.712  1.920   1.00 13.14 ?  113 TYR   A HE1  1 
ATOM   2400 H HE2  . TYR   A 1 113 ? 19.373 -10.318 -1.962  1.00 13.01 ?  113 TYR   A HE2  1 
ATOM   2401 H HH   . TYR   A 1 113 ? 18.066 -9.053  -0.625  1.00 14.27 ?  113 TYR   A HH   1 
ATOM   2402 N N    . GLU   A 1 114 ? 26.302 -13.203 -0.160  1.00 10.12 ?  114 GLU   A N    1 
ATOM   2403 C CA   . GLU   A 1 114 ? 27.297 -14.098 0.432   1.00 10.36 ?  114 GLU   A CA   1 
ATOM   2404 C C    . GLU   A 1 114 ? 28.149 -13.390 1.479   1.00 10.11 ?  114 GLU   A C    1 
ATOM   2405 O O    . GLU   A 1 114 ? 28.630 -14.028 2.425   1.00 10.44 ?  114 GLU   A O    1 
ATOM   2406 C CB   . GLU   A 1 114 ? 28.167 -14.740 -0.658  1.00 10.34 ?  114 GLU   A CB   1 
ATOM   2407 C CG   . GLU   A 1 114 ? 27.405 -15.792 -1.440  1.00 10.73 ?  114 GLU   A CG   1 
ATOM   2408 C CD   . GLU   A 1 114 ? 28.113 -16.321 -2.683  1.00 11.30 ?  114 GLU   A CD   1 
ATOM   2409 O OE1  . GLU   A 1 114 ? 29.063 -15.688 -3.179  1.00 11.43 ?  114 GLU   A OE1  1 
ATOM   2410 O OE2  . GLU   A 1 114 ? 27.668 -17.383 -3.181  1.00 12.29 -1 114 GLU   A OE2  1 
ATOM   2411 H H    . GLU   A 1 114 ? 26.357 -13.109 -1.020  1.00 12.13 ?  114 GLU   A H    1 
ATOM   2412 H HA   . GLU   A 1 114 ? 26.826 -14.814 0.874   1.00 12.42 ?  114 GLU   A HA   1 
ATOM   2413 H HB2  . GLU   A 1 114 ? 28.460 -14.057 -1.288  1.00 12.40 ?  114 GLU   A HB2  1 
ATOM   2414 H HB3  . GLU   A 1 114 ? 28.933 -15.168 -0.251  1.00 12.40 ?  114 GLU   A HB3  1 
ATOM   2415 H HG2  . GLU   A 1 114 ? 27.236 -16.549 -0.856  1.00 12.87 ?  114 GLU   A HG2  1 
ATOM   2416 H HG3  . GLU   A 1 114 ? 26.553 -15.413 -1.724  1.00 12.87 ?  114 GLU   A HG3  1 
ATOM   2417 N N    . ASN   A 1 115 ? 28.329 -12.070 1.349   1.00 10.00 ?  115 ASN   A N    1 
ATOM   2418 C CA   . ASN   A 1 115 ? 29.095 -11.342 2.354   1.00 10.02 ?  115 ASN   A CA   1 
ATOM   2419 C C    . ASN   A 1 115 ? 28.480 -11.477 3.741   1.00 9.88  ?  115 ASN   A C    1 
ATOM   2420 O O    . ASN   A 1 115 ? 29.193 -11.407 4.749   1.00 10.38 ?  115 ASN   A O    1 
ATOM   2421 C CB   . ASN   A 1 115 ? 29.202 -9.862  1.981   1.00 10.29 ?  115 ASN   A CB   1 
ATOM   2422 C CG   . ASN   A 1 115 ? 29.995 -9.639  0.718   1.00 11.15 ?  115 ASN   A CG   1 
ATOM   2423 O OD1  . ASN   A 1 115 ? 31.212 -9.733  0.727   1.00 14.43 ?  115 ASN   A OD1  1 
ATOM   2424 N ND2  . ASN   A 1 115 ? 29.314 -9.335  -0.372  1.00 10.84 ?  115 ASN   A ND2  1 
ATOM   2425 H H    . ASN   A 1 115 ? 28.016 -11.584 0.708   1.00 11.99 ?  115 ASN   A H    1 
ATOM   2426 H HA   . ASN   A 1 115 ? 29.990 -11.710 2.389   1.00 12.01 ?  115 ASN   A HA   1 
ATOM   2427 H HB2  . ASN   A 1 115 ? 28.308 -9.506  1.853   1.00 12.34 ?  115 ASN   A HB2  1 
ATOM   2428 H HB3  . ASN   A 1 115 ? 29.643 -9.391  2.708   1.00 12.34 ?  115 ASN   A HB3  1 
ATOM   2429 H HD21 . ASN   A 1 115 ? 29.729 -9.192  -1.108  1.00 13.00 ?  115 ASN   A HD21 1 
ATOM   2430 H HD22 . ASN   A 1 115 ? 28.454 -9.297  -0.345  1.00 13.00 ?  115 ASN   A HD22 1 
ATOM   2431 N N    . PHE   A 1 116 ? 27.154 -11.647 3.821   1.00 9.90  ?  116 PHE   A N    1 
ATOM   2432 C CA   . PHE   A 1 116 ? 26.511 -11.748 5.127   1.00 9.86  ?  116 PHE   A CA   1 
ATOM   2433 C C    . PHE   A 1 116 ? 26.991 -12.980 5.893   1.00 10.07 ?  116 PHE   A C    1 
ATOM   2434 O O    . PHE   A 1 116 ? 26.916 -13.002 7.122   1.00 10.65 ?  116 PHE   A O    1 
ATOM   2435 C CB   . PHE   A 1 116 ? 24.983 -11.877 4.995   1.00 10.02 ?  116 PHE   A CB   1 
ATOM   2436 C CG   . PHE   A 1 116 ? 24.223 -10.631 4.536   1.00 9.93  ?  116 PHE   A CG   1 
ATOM   2437 C CD1  . PHE   A 1 116 ? 24.787 -9.607  3.784   1.00 10.30 ?  116 PHE   A CD1  1 
ATOM   2438 C CD2  . PHE   A 1 116 ? 22.866 -10.533 4.857   1.00 10.67 ?  116 PHE   A CD2  1 
ATOM   2439 C CE1  . PHE   A 1 116 ? 24.012 -8.524  3.370   1.00 10.54 ?  116 PHE   A CE1  1 
ATOM   2440 C CE2  . PHE   A 1 116 ? 22.095 -9.463  4.449   1.00 10.77 ?  116 PHE   A CE2  1 
ATOM   2441 C CZ   . PHE   A 1 116 ? 22.662 -8.455  3.708   1.00 10.31 ?  116 PHE   A CZ   1 
ATOM   2442 H H    . PHE   A 1 116 ? 26.616 -11.695 3.146   1.00 11.87 ?  116 PHE   A H    1 
ATOM   2443 H HA   . PHE   A 1 116 ? 26.707 -10.955 5.650   1.00 11.82 ?  116 PHE   A HA   1 
ATOM   2444 H HB2  . PHE   A 1 116 ? 24.796 -12.581 4.352   1.00 12.01 ?  116 PHE   A HB2  1 
ATOM   2445 H HB3  . PHE   A 1 116 ? 24.627 -12.133 5.859   1.00 12.01 ?  116 PHE   A HB3  1 
ATOM   2446 H HD1  . PHE   A 1 116 ? 25.683 -9.658  3.548   1.00 12.35 ?  116 PHE   A HD1  1 
ATOM   2447 H HD2  . PHE   A 1 116 ? 22.467 -11.221 5.350   1.00 12.80 ?  116 PHE   A HD2  1 
ATOM   2448 H HE1  . PHE   A 1 116 ? 24.400 -7.845  2.872   1.00 12.64 ?  116 PHE   A HE1  1 
ATOM   2449 H HE2  . PHE   A 1 116 ? 21.195 -9.430  4.683   1.00 12.92 ?  116 PHE   A HE2  1 
ATOM   2450 H HZ   . PHE   A 1 116 ? 22.150 -7.728  3.442   1.00 12.36 ?  116 PHE   A HZ   1 
ATOM   2451 N N    . ASN   A 1 117 ? 27.429 -14.026 5.185   1.00 10.34 ?  117 ASN   A N    1 
ATOM   2452 C CA   . ASN   A 1 117 ? 27.796 -15.274 5.848   1.00 10.71 ?  117 ASN   A CA   1 
ATOM   2453 C C    . ASN   A 1 117 ? 29.060 -15.159 6.680   1.00 11.14 ?  117 ASN   A C    1 
ATOM   2454 O O    . ASN   A 1 117 ? 29.369 -16.083 7.443   1.00 12.02 ?  117 ASN   A O    1 
ATOM   2455 C CB   . ASN   A 1 117 ? 27.912 -16.395 4.823   1.00 10.83 ?  117 ASN   A CB   1 
ATOM   2456 C CG   . ASN   A 1 117 ? 26.561 -16.781 4.283   1.00 10.81 ?  117 ASN   A CG   1 
ATOM   2457 O OD1  . ASN   A 1 117 ? 25.589 -16.821 5.036   1.00 11.54 ?  117 ASN   A OD1  1 
ATOM   2458 N ND2  . ASN   A 1 117 ? 26.471 -17.039 2.992   1.00 10.72 ?  117 ASN   A ND2  1 
ATOM   2459 H H    . ASN   A 1 117 ? 27.506 -14.037 4.327   1.00 12.39 ?  117 ASN   A H    1 
ATOM   2460 H HA   . ASN   A 1 117 ? 27.077 -15.510 6.452   1.00 12.84 ?  117 ASN   A HA   1 
ATOM   2461 H HB2  . ASN   A 1 117 ? 28.462 -16.097 4.080   1.00 12.99 ?  117 ASN   A HB2  1 
ATOM   2462 H HB3  . ASN   A 1 117 ? 28.306 -17.172 5.243   1.00 12.99 ?  117 ASN   A HB3  1 
ATOM   2463 H HD21 . ASN   A 1 117 ? 25.718 -17.258 2.649   1.00 12.86 ?  117 ASN   A HD21 1 
ATOM   2464 H HD22 . ASN   A 1 117 ? 27.175 -16.987 2.495   1.00 12.86 ?  117 ASN   A HD22 1 
ATOM   2465 N N    . GLN   A 1 118 ? 29.788 -14.048 6.560   1.00 11.03 ?  118 GLN   A N    1 
ATOM   2466 C CA   . GLN   A 1 118 ? 30.970 -13.812 7.378   1.00 11.47 ?  118 GLN   A CA   1 
ATOM   2467 C C    . GLN   A 1 118 ? 30.631 -13.244 8.749   1.00 11.50 ?  118 GLN   A C    1 
ATOM   2468 O O    . GLN   A 1 118 ? 31.546 -12.957 9.528   1.00 13.06 ?  118 GLN   A O    1 
ATOM   2469 C CB   . GLN   A 1 118 ? 31.957 -12.901 6.640   1.00 11.95 ?  118 GLN   A CB   1 
ATOM   2470 C CG   . GLN   A 1 118 ? 32.429 -13.483 5.316   1.00 11.96 ?  118 GLN   A CG   1 
ATOM   2471 C CD   . GLN   A 1 118 ? 33.257 -14.747 5.494   1.00 12.07 ?  118 GLN   A CD   1 
ATOM   2472 O OE1  . GLN   A 1 118 ? 34.118 -14.819 6.381   1.00 12.94 ?  118 GLN   A OE1  1 
ATOM   2473 N NE2  . GLN   A 1 118 ? 33.005 -15.748 4.650   1.00 12.47 ?  118 GLN   A NE2  1 
ATOM   2474 H H    . GLN   A 1 118 ? 29.611 -13.401 6.013   1.00 13.23 ?  118 GLN   A H    1 
ATOM   2475 H HA   . GLN   A 1 118 ? 31.407 -14.664 7.522   1.00 13.75 ?  118 GLN   A HA   1 
ATOM   2476 H HB2  . GLN   A 1 118 ? 31.527 -12.051 6.465   1.00 14.33 ?  118 GLN   A HB2  1 
ATOM   2477 H HB3  . GLN   A 1 118 ? 32.736 -12.769 7.205   1.00 14.33 ?  118 GLN   A HB3  1 
ATOM   2478 H HG2  . GLN   A 1 118 ? 31.656 -13.697 4.767   1.00 14.35 ?  118 GLN   A HG2  1 
ATOM   2479 H HG3  . GLN   A 1 118 ? 32.980 -12.822 4.860   1.00 14.35 ?  118 GLN   A HG3  1 
ATOM   2480 H HE21 . GLN   A 1 118 ? 32.394 -15.661 4.043   1.00 14.95 ?  118 GLN   A HE21 1 
ATOM   2481 H HE22 . GLN   A 1 118 ? 33.444 -16.482 4.708   1.00 14.95 ?  118 GLN   A HE22 1 
ATOM   2482 N N    . HIS   A 1 119 ? 29.344 -13.092 9.067   1.00 11.25 ?  119 HIS   A N    1 
ATOM   2483 C CA   . HIS   A 1 119 ? 28.893 -12.481 10.313  1.00 11.93 ?  119 HIS   A CA   1 
ATOM   2484 C C    . HIS   A 1 119 ? 27.761 -13.309 10.890  1.00 11.88 ?  119 HIS   A C    1 
ATOM   2485 O O    . HIS   A 1 119 ? 26.807 -13.637 10.180  1.00 12.41 ?  119 HIS   A O    1 
ATOM   2486 C CB   . HIS   A 1 119 ? 28.429 -11.050 10.039  1.00 12.53 ?  119 HIS   A CB   1 
ATOM   2487 C CG   . HIS   A 1 119 ? 29.505 -10.235 9.424   1.00 13.72 ?  119 HIS   A CG   1 
ATOM   2488 N ND1  . HIS   A 1 119 ? 30.484 -9.630  10.177  1.00 15.83 ?  119 HIS   A ND1  1 
ATOM   2489 C CD2  . HIS   A 1 119 ? 29.842 -10.041 8.129   1.00 14.80 ?  119 HIS   A CD2  1 
ATOM   2490 C CE1  . HIS   A 1 119 ? 31.347 -9.043  9.368   1.00 16.13 ?  119 HIS   A CE1  1 
ATOM   2491 N NE2  . HIS   A 1 119 ? 30.988 -9.287  8.121   1.00 16.09 ?  119 HIS   A NE2  1 
ATOM   2492 H H    . HIS   A 1 119 ? 28.693 -13.353 8.567   1.00 13.49 ?  119 HIS   A H    1 
ATOM   2493 H HA   . HIS   A 1 119 ? 29.625 -12.460 10.953  1.00 14.31 ?  119 HIS   A HA   1 
ATOM   2494 H HB2  . HIS   A 1 119 ? 27.676 -11.078 9.428   1.00 15.02 ?  119 HIS   A HB2  1 
ATOM   2495 H HB3  . HIS   A 1 119 ? 28.171 -10.638 10.875  1.00 15.02 ?  119 HIS   A HB3  1 
ATOM   2496 H HD2  . HIS   A 1 119 ? 29.381 -10.357 7.381   1.00 17.75 ?  119 HIS   A HD2  1 
ATOM   2497 H HE1  . HIS   A 1 119 ? 32.085 -8.543  9.630   1.00 19.35 ?  119 HIS   A HE1  1 
ATOM   2498 H HE2  . HIS   A 1 119 ? 31.392 -8.997  7.417   1.00 19.30 ?  119 HIS   A HE2  1 
ATOM   2499 N N    . GLU   A 1 120 ? 27.860 -13.635 12.179  1.00 12.68 ?  120 GLU   A N    1 
ATOM   2500 C CA   . GLU   A 1 120 ? 26.911 -14.572 12.776  1.00 14.15 ?  120 GLU   A CA   1 
ATOM   2501 C C    . GLU   A 1 120 ? 25.494 -14.008 12.846  1.00 13.00 ?  120 GLU   A C    1 
ATOM   2502 O O    . GLU   A 1 120 ? 24.520 -14.768 12.733  1.00 13.19 ?  120 GLU   A O    1 
ATOM   2503 C CB   . GLU   A 1 120 ? 27.395 -14.980 14.168  1.00 18.77 ?  120 GLU   A CB   1 
ATOM   2504 C CG   . GLU   A 1 120 ? 28.576 -15.934 14.157  1.00 25.82 ?  120 GLU   A CG   1 
ATOM   2505 C CD   . GLU   A 1 120 ? 28.731 -16.671 15.472  1.00 31.94 ?  120 GLU   A CD   1 
ATOM   2506 O OE1  . GLU   A 1 120 ? 28.322 -16.119 16.517  1.00 33.95 ?  120 GLU   A OE1  1 
ATOM   2507 O OE2  . GLU   A 1 120 ? 29.253 -17.806 15.461  1.00 35.40 -1 120 GLU   A OE2  1 
ATOM   2508 H H    . GLU   A 1 120 ? 28.461 -13.334 12.723  1.00 15.20 ?  120 GLU   A H    1 
ATOM   2509 H HA   . GLU   A 1 120 ? 26.886 -15.373 12.235  1.00 16.97 ?  120 GLU   A HA   1 
ATOM   2510 H HB2  . GLU   A 1 120 ? 27.670 -14.188 14.658  1.00 22.52 ?  120 GLU   A HB2  1 
ATOM   2511 H HB3  . GLU   A 1 120 ? 26.671 -15.421 14.641  1.00 22.52 ?  120 GLU   A HB3  1 
ATOM   2512 H HG2  . GLU   A 1 120 ? 28.453 -16.592 13.453  1.00 30.98 ?  120 GLU   A HG2  1 
ATOM   2513 H HG3  . GLU   A 1 120 ? 29.395 -15.437 14.008  1.00 30.98 ?  120 GLU   A HG3  1 
ATOM   2514 N N    . VAL   A 1 121 ? 25.362 -12.697 13.063  1.00 12.51 ?  121 VAL   A N    1 
ATOM   2515 C CA   . VAL   A 1 121 ? 24.070 -12.030 13.204  1.00 12.65 ?  121 VAL   A CA   1 
ATOM   2516 C C    . VAL   A 1 121 ? 24.178 -10.644 12.576  1.00 11.58 ?  121 VAL   A C    1 
ATOM   2517 O O    . VAL   A 1 121 ? 25.152 -9.923  12.817  1.00 12.52 ?  121 VAL   A O    1 
ATOM   2518 C CB   . VAL   A 1 121 ? 23.657 -11.891 14.688  1.00 15.51 ?  121 VAL   A CB   1 
ATOM   2519 C CG1  . VAL   A 1 121 ? 22.271 -11.256 14.804  1.00 16.31 ?  121 VAL   A CG1  1 
ATOM   2520 C CG2  . VAL   A 1 121 ? 23.691 -13.224 15.415  1.00 17.60 ?  121 VAL   A CG2  1 
ATOM   2521 H H    . VAL   A 1 121 ? 26.029 -12.157 13.140  1.00 15.01 ?  121 VAL   A H    1 
ATOM   2522 H HA   . VAL   A 1 121 ? 23.389 -12.538 12.741  1.00 15.17 ?  121 VAL   A HA   1 
ATOM   2523 H HB   . VAL   A 1 121 ? 24.283 -11.304 15.133  1.00 18.60 ?  121 VAL   A HB   1 
ATOM   2524 H HG11 . VAL   A 1 121 ? 21.968 -11.323 15.725  1.00 19.56 ?  121 VAL   A HG11 1 
ATOM   2525 H HG12 . VAL   A 1 121 ? 22.327 -10.324 14.545  1.00 19.56 ?  121 VAL   A HG12 1 
ATOM   2526 H HG13 . VAL   A 1 121 ? 21.656 -11.728 14.222  1.00 19.56 ?  121 VAL   A HG13 1 
ATOM   2527 H HG21 . VAL   A 1 121 ? 23.349 -13.105 16.320  1.00 21.11 ?  121 VAL   A HG21 1 
ATOM   2528 H HG22 . VAL   A 1 121 ? 23.131 -13.863 14.941  1.00 21.11 ?  121 VAL   A HG22 1 
ATOM   2529 H HG23 . VAL   A 1 121 ? 24.602 -13.547 15.450  1.00 21.11 ?  121 VAL   A HG23 1 
ATOM   2530 N N    . LEU   A 1 122 ? 23.161 -10.247 11.804  1.00 11.48 ?  122 LEU   A N    1 
ATOM   2531 C CA   . LEU   A 1 122 ? 23.158 -8.948  11.135  1.00 11.32 ?  122 LEU   A CA   1 
ATOM   2532 C C    . LEU   A 1 122 ? 21.761 -8.359  11.099  1.00 11.03 ?  122 LEU   A C    1 
ATOM   2533 O O    . LEU   A 1 122 ? 20.771 -9.083  10.962  1.00 12.23 ?  122 LEU   A O    1 
ATOM   2534 C CB   . LEU   A 1 122 ? 23.571 -9.050  9.660   1.00 12.92 ?  122 LEU   A CB   1 
ATOM   2535 C CG   . LEU   A 1 122 ? 24.782 -9.892  9.283   1.00 12.82 ?  122 LEU   A CG   1 
ATOM   2536 C CD1  . LEU   A 1 122 ? 24.384 -11.344 9.057   1.00 13.62 ?  122 LEU   A CD1  1 
ATOM   2537 C CD2  . LEU   A 1 122 ? 25.450 -9.322  8.046   1.00 12.26 ?  122 LEU   A CD2  1 
ATOM   2538 H H    . LEU   A 1 122 ? 22.455 -10.717 11.647  1.00 13.77 ?  122 LEU   A H    1 
ATOM   2539 H HA   . LEU   A 1 122 ? 23.757 -8.333  11.592  1.00 13.58 ?  122 LEU   A HA   1 
ATOM   2540 H HB2  . LEU   A 1 122 ? 22.827 -9.413  9.168   1.00 15.50 ?  122 LEU   A HB2  1 
ATOM   2541 H HB3  . LEU   A 1 122 ? 23.758 -8.154  9.343   1.00 15.50 ?  122 LEU   A HB3  1 
ATOM   2542 H HG   . LEU   A 1 122 ? 25.436 -9.871  10.002  1.00 15.37 ?  122 LEU   A HG   1 
ATOM   2543 H HD11 . LEU   A 1 122 ? 25.161 -11.855 8.784   1.00 16.33 ?  122 LEU   A HD11 1 
ATOM   2544 H HD12 . LEU   A 1 122 ? 24.028 -11.705 9.886   1.00 16.33 ?  122 LEU   A HD12 1 
ATOM   2545 H HD13 . LEU   A 1 122 ? 23.705 -11.382 8.365   1.00 16.33 ?  122 LEU   A HD13 1 
ATOM   2546 H HD21 . LEU   A 1 122 ? 26.198 -9.893  7.789   1.00 14.71 ?  122 LEU   A HD21 1 
ATOM   2547 H HD22 . LEU   A 1 122 ? 24.805 -9.287  7.323   1.00 14.71 ?  122 LEU   A HD22 1 
ATOM   2548 H HD23 . LEU   A 1 122 ? 25.777 -8.429  8.242   1.00 14.71 ?  122 LEU   A HD23 1 
ATOM   2549 N N    A LEU   A 1 123 ? 21.697 -7.030  11.191  0.88 10.68 ?  123 LEU   A N    1 
ATOM   2550 N N    B LEU   A 1 123 ? 21.709 -7.030  11.225  0.12 10.88 ?  123 LEU   A N    1 
ATOM   2551 C CA   A LEU   A 1 123 ? 20.523 -6.239  10.831  0.88 10.83 ?  123 LEU   A CA   1 
ATOM   2552 C CA   B LEU   A 1 123 ? 20.525 -6.229  10.936  0.12 10.89 ?  123 LEU   A CA   1 
ATOM   2553 C C    A LEU   A 1 123 ? 20.755 -5.706  9.426   0.88 9.95  ?  123 LEU   A C    1 
ATOM   2554 C C    B LEU   A 1 123 ? 20.732 -5.642  9.546   0.12 10.61 ?  123 LEU   A C    1 
ATOM   2555 O O    A LEU   A 1 123 ? 21.821 -5.145  9.160   0.88 10.32 ?  123 LEU   A O    1 
ATOM   2556 O O    B LEU   A 1 123 ? 21.566 -4.749  9.365   0.12 10.50 ?  123 LEU   A O    1 
ATOM   2557 C CB   A LEU   A 1 123 ? 20.390 -5.058  11.795  0.88 11.23 ?  123 LEU   A CB   1 
ATOM   2558 C CB   B LEU   A 1 123 ? 20.369 -5.116  11.971  0.12 11.08 ?  123 LEU   A CB   1 
ATOM   2559 C CG   A LEU   A 1 123 ? 19.332 -4.009  11.460  0.88 11.95 ?  123 LEU   A CG   1 
ATOM   2560 C CG   B LEU   A 1 123 ? 19.403 -3.987  11.587  0.12 11.16 ?  123 LEU   A CG   1 
ATOM   2561 C CD1  A LEU   A 1 123 ? 17.942 -4.623  11.479  0.88 12.85 ?  123 LEU   A CD1  1 
ATOM   2562 C CD1  B LEU   A 1 123 ? 17.966 -4.489  11.535  0.12 11.29 ?  123 LEU   A CD1  1 
ATOM   2563 C CD2  A LEU   A 1 123 ? 19.424 -2.846  12.442  0.88 13.18 ?  123 LEU   A CD2  1 
ATOM   2564 C CD2  B LEU   A 1 123 ? 19.534 -2.795  12.526  0.12 11.37 ?  123 LEU   A CD2  1 
ATOM   2565 H H    A LEU   A 1 123 ? 22.355 -6.541  11.461  0.88 12.81 ?  123 LEU   A H    1 
ATOM   2566 H H    B LEU   A 1 123 ? 22.383 -6.550  11.474  0.12 13.05 ?  123 LEU   A H    1 
ATOM   2567 H HA   A LEU   A 1 123 ? 19.717 -6.780  10.857  0.88 12.99 ?  123 LEU   A HA   1 
ATOM   2568 H HA   B LEU   A 1 123 ? 19.732 -6.781  10.934  0.12 13.06 ?  123 LEU   A HA   1 
ATOM   2569 H HB2  A LEU   A 1 123 ? 20.173 -5.403  12.677  0.88 13.47 ?  123 LEU   A HB2  1 
ATOM   2570 H HB2  B LEU   A 1 123 ? 20.045 -5.511  12.797  0.12 13.29 ?  123 LEU   A HB2  1 
ATOM   2571 H HB3  A LEU   A 1 123 ? 21.240 -4.596  11.834  0.88 13.47 ?  123 LEU   A HB3  1 
ATOM   2572 H HB3  B LEU   A 1 123 ? 21.239 -4.714  12.127  0.12 13.29 ?  123 LEU   A HB3  1 
ATOM   2573 H HG   A LEU   A 1 123 ? 19.488 -3.656  10.569  0.88 14.33 ?  123 LEU   A HG   1 
ATOM   2574 H HG   B LEU   A 1 123 ? 19.626 -3.665  10.703  0.12 13.39 ?  123 LEU   A HG   1 
ATOM   2575 H HD11 A LEU   A 1 123 ? 17.283 -3.932  11.320  0.88 15.41 ?  123 LEU   A HD11 1 
ATOM   2576 H HD11 B LEU   A 1 123 ? 17.383 -3.749  11.301  0.12 13.53 ?  123 LEU   A HD11 1 
ATOM   2577 H HD12 A LEU   A 1 123 ? 17.887 -5.300  10.785  0.88 15.41 ?  123 LEU   A HD12 1 
ATOM   2578 H HD12 B LEU   A 1 123 ? 17.900 -5.187  10.863  0.12 13.53 ?  123 LEU   A HD12 1 
ATOM   2579 H HD13 A LEU   A 1 123 ? 17.791 -5.031  12.348  0.88 15.41 ?  123 LEU   A HD13 1 
ATOM   2580 H HD13 B LEU   A 1 123 ? 17.722 -4.842  12.404  0.12 13.53 ?  123 LEU   A HD13 1 
ATOM   2581 H HD21 A LEU   A 1 123 ? 18.747 -2.188  12.222  0.88 15.80 ?  123 LEU   A HD21 1 
ATOM   2582 H HD21 B LEU   A 1 123 ? 18.908 -2.107  12.248  0.12 13.64 ?  123 LEU   A HD21 1 
ATOM   2583 H HD22 A LEU   A 1 123 ? 19.276 -3.183  13.341  0.88 15.80 ?  123 LEU   A HD22 1 
ATOM   2584 H HD22 B LEU   A 1 123 ? 19.334 -3.080  13.429  0.12 13.64 ?  123 LEU   A HD22 1 
ATOM   2585 H HD23 A LEU   A 1 123 ? 20.306 -2.451  12.378  0.88 15.80 ?  123 LEU   A HD23 1 
ATOM   2586 H HD23 B LEU   A 1 123 ? 20.441 -2.455  12.477  0.12 13.64 ?  123 LEU   A HD23 1 
ATOM   2587 N N    A ALA   A 1 124 ? 19.778 -5.862  8.531   0.88 9.66  ?  124 ALA   A N    1 
ATOM   2588 N N    B ALA   A 1 124 ? 19.979 -6.136  8.570   0.12 10.58 ?  124 ALA   A N    1 
ATOM   2589 C CA   A ALA   A 1 124 ? 20.055 -5.576  7.130   0.88 9.93  ?  124 ALA   A CA   1 
ATOM   2590 C CA   B ALA   A 1 124 ? 20.255 -5.817  7.181   0.12 10.71 ?  124 ALA   A CA   1 
ATOM   2591 C C    A ALA   A 1 124 ? 18.808 -5.110  6.394   0.88 9.89  ?  124 ALA   A C    1 
ATOM   2592 C C    B ALA   A 1 124 ? 19.012 -5.300  6.474   0.12 10.51 ?  124 ALA   A C    1 
ATOM   2593 O O    A ALA   A 1 124 ? 17.681 -5.477  6.758   0.88 10.62 ?  124 ALA   A O    1 
ATOM   2594 O O    B ALA   A 1 124 ? 17.885 -5.625  6.857   0.12 10.43 ?  124 ALA   A O    1 
ATOM   2595 C CB   A ALA   A 1 124 ? 20.625 -6.803  6.413   0.88 10.35 ?  124 ALA   A CB   1 
ATOM   2596 C CB   B ALA   A 1 124 ? 20.769 -7.057  6.435   0.12 10.99 ?  124 ALA   A CB   1 
ATOM   2597 H H    A ALA   A 1 124 ? 18.979 -6.121  8.705   0.88 11.58 ?  124 ALA   A H    1 
ATOM   2598 H H    B ALA   A 1 124 ? 19.304 -6.655  8.686   0.12 12.68 ?  124 ALA   A H    1 
ATOM   2599 H HA   A ALA   A 1 124 ? 20.721 -4.871  7.090   0.88 11.90 ?  124 ALA   A HA   1 
ATOM   2600 H HA   B ALA   A 1 124 ? 20.939 -5.134  7.147   0.12 12.85 ?  124 ALA   A HA   1 
ATOM   2601 H HB1  A ALA   A 1 124 ? 20.804 -6.575  5.485   0.88 12.41 ?  124 ALA   A HB1  1 
ATOM   2602 H HB1  B ALA   A 1 124 ? 20.949 -6.819  5.512   0.12 13.17 ?  124 ALA   A HB1  1 
ATOM   2603 H HB2  A ALA   A 1 124 ? 21.462 -7.063  6.846   0.88 12.41 ?  124 ALA   A HB2  1 
ATOM   2604 H HB2  B ALA   A 1 124 ? 21.585 -7.366  6.862   0.12 13.17 ?  124 ALA   A HB2  1 
ATOM   2605 H HB3  A ALA   A 1 124 ? 19.991 -7.528  6.463   0.88 12.41 ?  124 ALA   A HB3  1 
ATOM   2606 H HB3  B ALA   A 1 124 ? 20.093 -7.750  6.473   0.12 13.17 ?  124 ALA   A HB3  1 
ATOM   2607 N N    A PRO   A 1 125 ? 18.988 -4.359  5.310   0.88 9.99  ?  125 PRO   A N    1 
ATOM   2608 N N    B PRO   A 1 125 ? 19.196 -4.484  5.436   0.12 10.25 ?  125 PRO   A N    1 
ATOM   2609 C CA   A PRO   A 1 125 ? 17.926 -4.130  4.332   0.88 10.34 ?  125 PRO   A CA   1 
ATOM   2610 C CA   B PRO   A 1 125 ? 18.066 -4.090  4.591   0.12 10.38 ?  125 PRO   A CA   1 
ATOM   2611 C C    A PRO   A 1 125 ? 17.987 -5.207  3.254   0.88 10.24 ?  125 PRO   A C    1 
ATOM   2612 C C    B PRO   A 1 125 ? 17.963 -5.026  3.400   0.12 10.68 ?  125 PRO   A C    1 
ATOM   2613 O O    A PRO   A 1 125 ? 18.958 -5.958  3.143   0.88 11.02 ?  125 PRO   A O    1 
ATOM   2614 O O    B PRO   A 1 125 ? 18.815 -5.905  3.238   0.12 10.75 ?  125 PRO   A O    1 
ATOM   2615 C CB   A PRO   A 1 125 ? 18.350 -2.786  3.727   0.88 10.54 ?  125 PRO   A CB   1 
ATOM   2616 C CB   B PRO   A 1 125 ? 18.469 -2.683  4.143   0.12 10.28 ?  125 PRO   A CB   1 
ATOM   2617 C CG   A PRO   A 1 125 ? 19.864 -2.939  3.631   0.88 10.74 ?  125 PRO   A CG   1 
ATOM   2618 C CG   B PRO   A 1 125 ? 19.972 -2.789  4.001   0.12 10.33 ?  125 PRO   A CG   1 
ATOM   2619 C CD   A PRO   A 1 125 ? 20.249 -3.709  4.893   0.88 10.37 ?  125 PRO   A CD   1 
ATOM   2620 C CD   B PRO   A 1 125 ? 20.440 -3.809  5.024   0.12 10.30 ?  125 PRO   A CD   1 
ATOM   2621 H HA   A PRO   A 1 125 ? 17.042 -4.083  4.742   0.88 12.40 ?  125 PRO   A HA   1 
ATOM   2622 H HA   B PRO   A 1 125 ? 17.231 -4.064  5.090   0.12 12.44 ?  125 PRO   A HA   1 
ATOM   2623 H HB2  A PRO   A 1 125 ? 17.941 -2.674  2.850   0.88 12.64 ?  125 PRO   A HB2  1 
ATOM   2624 H HB2  B PRO   A 1 125 ? 18.052 -2.472  3.293   0.12 12.32 ?  125 PRO   A HB2  1 
ATOM   2625 H HB3  A PRO   A 1 125 ? 18.097 -2.061  4.323   0.88 12.64 ?  125 PRO   A HB3  1 
ATOM   2626 H HB3  B PRO   A 1 125 ? 18.227 -2.033  4.822   0.12 12.32 ?  125 PRO   A HB3  1 
ATOM   2627 H HG2  A PRO   A 1 125 ? 20.092 -3.445  2.834   0.88 12.88 ?  125 PRO   A HG2  1 
ATOM   2628 H HG2  B PRO   A 1 125 ? 20.190 -3.085  3.104   0.12 12.38 ?  125 PRO   A HG2  1 
ATOM   2629 H HG3  A PRO   A 1 125 ? 20.280 -2.065  3.615   0.88 12.88 ?  125 PRO   A HG3  1 
ATOM   2630 H HG3  B PRO   A 1 125 ? 20.376 -1.927  4.178   0.12 12.38 ?  125 PRO   A HG3  1 
ATOM   2631 H HD2  A PRO   A 1 125 ? 20.927 -4.373  4.691   0.88 12.44 ?  125 PRO   A HD2  1 
ATOM   2632 H HD2  B PRO   A 1 125 ? 21.050 -4.445  4.616   0.12 12.35 ?  125 PRO   A HD2  1 
ATOM   2633 H HD3  A PRO   A 1 125 ? 20.551 -3.094  5.583   0.88 12.44 ?  125 PRO   A HD3  1 
ATOM   2634 H HD3  B PRO   A 1 125 ? 20.850 -3.363  5.782   0.12 12.35 ?  125 PRO   A HD3  1 
ATOM   2635 N N    A LEU   A 1 126 ? 16.935 -5.253  2.441   0.88 10.48 ?  126 LEU   A N    1 
ATOM   2636 N N    B LEU   A 1 126 ? 16.946 -4.862  2.560   0.12 11.06 ?  126 LEU   A N    1 
ATOM   2637 C CA   A LEU   A 1 126 ? 16.964 -6.067  1.234   0.88 10.72 ?  126 LEU   A CA   1 
ATOM   2638 C CA   B LEU   A 1 126 ? 16.946 -5.563  1.284   0.12 11.35 ?  126 LEU   A CA   1 
ATOM   2639 C C    A LEU   A 1 126 ? 17.895 -5.445  0.201   0.88 10.58 ?  126 LEU   A C    1 
ATOM   2640 C C    B LEU   A 1 126 ? 17.956 -4.910  0.347   0.12 11.43 ?  126 LEU   A C    1 
ATOM   2641 O O    A LEU   A 1 126 ? 17.666 -4.322  -0.269  0.88 11.51 ?  126 LEU   A O    1 
ATOM   2642 O O    B LEU   A 1 126 ? 18.062 -3.683  0.283   0.12 12.08 ?  126 LEU   A O    1 
ATOM   2643 C CB   A LEU   A 1 126 ? 15.563 -6.206  0.656   0.88 11.26 ?  126 LEU   A CB   1 
ATOM   2644 C CB   B LEU   A 1 126 ? 15.557 -5.531  0.648   0.12 11.71 ?  126 LEU   A CB   1 
ATOM   2645 C CG   A LEU   A 1 126 ? 14.641 -7.143  1.429   0.88 13.00 ?  126 LEU   A CG   1 
ATOM   2646 C CG   B LEU   A 1 126 ? 14.491 -6.497  1.171   0.12 11.87 ?  126 LEU   A CG   1 
ATOM   2647 C CD1  A LEU   A 1 126 ? 13.223 -6.999  0.926   0.88 14.25 ?  126 LEU   A CD1  1 
ATOM   2648 C CD1  B LEU   A 1 126 ? 13.281 -6.460  0.252   0.12 11.99 ?  126 LEU   A CD1  1 
ATOM   2649 C CD2  A LEU   A 1 126 ? 15.109 -8.592  1.294   0.88 13.23 ?  126 LEU   A CD2  1 
ATOM   2650 C CD2  B LEU   A 1 126 ? 15.024 -7.915  1.294   0.12 11.96 ?  126 LEU   A CD2  1 
ATOM   2651 H H    A LEU   A 1 126 ? 16.202 -4.822  2.563   0.88 12.56 ?  126 LEU   A H    1 
ATOM   2652 H H    B LEU   A 1 126 ? 16.257 -4.364  2.707   0.12 13.26 ?  126 LEU   A H    1 
ATOM   2653 H HA   A LEU   A 1 126 ? 17.298 -6.948  1.448   0.88 12.85 ?  126 LEU   A HA   1 
ATOM   2654 H HA   B LEU   A 1 126 ? 17.211 -6.483  1.425   0.12 13.61 ?  126 LEU   A HA   1 
ATOM   2655 H HB2  A LEU   A 1 126 ? 15.142 -5.331  0.647   0.88 13.51 ?  126 LEU   A HB2  1 
ATOM   2656 H HB2  B LEU   A 1 126 ? 15.200 -4.638  0.765   0.12 14.04 ?  126 LEU   A HB2  1 
ATOM   2657 H HB3  A LEU   A 1 126 ? 15.630 -6.544  -0.249  0.88 13.51 ?  126 LEU   A HB3  1 
ATOM   2658 H HB3  B LEU   A 1 126 ? 15.662 -5.710  -0.299  0.12 14.04 ?  126 LEU   A HB3  1 
ATOM   2659 H HG   A LEU   A 1 126 ? 14.653 -6.908  2.369   0.88 15.59 ?  126 LEU   A HG   1 
ATOM   2660 H HG   B LEU   A 1 126 ? 14.204 -6.206  2.051   0.12 14.23 ?  126 LEU   A HG   1 
ATOM   2661 H HD11 A LEU   A 1 126 ? 12.649 -7.605  1.419   0.88 17.09 ?  126 LEU   A HD11 1 
ATOM   2662 H HD11 B LEU   A 1 126 ? 12.629 -7.107  0.563   0.12 14.37 ?  126 LEU   A HD11 1 
ATOM   2663 H HD12 A LEU   A 1 126 ? 12.934 -6.084  1.060   0.88 17.09 ?  126 LEU   A HD12 1 
ATOM   2664 H HD12 B LEU   A 1 126 ? 12.898 -5.570  0.266   0.12 14.37 ?  126 LEU   A HD12 1 
ATOM   2665 H HD13 A LEU   A 1 126 ? 13.202 -7.219  -0.020  0.88 17.09 ?  126 LEU   A HD13 1 
ATOM   2666 H HD13 B LEU   A 1 126 ? 13.563 -6.685  -0.650  0.12 14.37 ?  126 LEU   A HD13 1 
ATOM   2667 H HD21 A LEU   A 1 126 ? 14.433 -9.181  1.660   0.88 15.87 ?  126 LEU   A HD21 1 
ATOM   2668 H HD21 B LEU   A 1 126 ? 14.280 -8.521  1.430   0.12 14.34 ?  126 LEU   A HD21 1 
ATOM   2669 H HD22 A LEU   A 1 126 ? 15.248 -8.793  0.354   0.88 15.87 ?  126 LEU   A HD22 1 
ATOM   2670 H HD22 B LEU   A 1 126 ? 15.494 -8.145  0.477   0.12 14.34 ?  126 LEU   A HD22 1 
ATOM   2671 H HD23 A LEU   A 1 126 ? 15.943 -8.703  1.780   0.88 15.87 ?  126 LEU   A HD23 1 
ATOM   2672 H HD23 B LEU   A 1 126 ? 15.631 -7.959  2.048   0.12 14.34 ?  126 LEU   A HD23 1 
ATOM   2673 N N    A LEU   A 1 127 ? 18.932 -6.187  -0.171  0.88 10.74 ?  127 LEU   A N    1 
ATOM   2674 N N    B LEU   A 1 127 ? 18.713 -5.732  -0.371  0.12 10.67 ?  127 LEU   A N    1 
ATOM   2675 C CA   A LEU   A 1 127 ? 19.914 -5.683  -1.113  0.88 10.73 ?  127 LEU   A CA   1 
ATOM   2676 C CA   B LEU   A 1 127 ? 19.744 -5.241  -1.273  0.12 10.14 ?  127 LEU   A CA   1 
ATOM   2677 C C    A LEU   A 1 127 ? 19.291 -5.485  -2.481  0.88 9.93  ?  127 LEU   A C    1 
ATOM   2678 C C    B LEU   A 1 127 ? 19.242 -5.214  -2.715  0.12 10.33 ?  127 LEU   A C    1 
ATOM   2679 O O    A LEU   A 1 127 ? 18.453 -6.271  -2.935  0.88 10.82 ?  127 LEU   A O    1 
ATOM   2680 O O    B LEU   A 1 127 ? 18.421 -6.038  -3.127  0.12 10.19 ?  127 LEU   A O    1 
ATOM   2681 C CB   A LEU   A 1 127 ? 21.093 -6.649  -1.222  0.88 11.38 ?  127 LEU   A CB   1 
ATOM   2682 C CB   B LEU   A 1 127 ? 21.008 -6.104  -1.189  0.12 9.79  ?  127 LEU   A CB   1 
ATOM   2683 C CG   A LEU   A 1 127 ? 21.902 -6.894  0.048   0.88 11.93 ?  127 LEU   A CG   1 
ATOM   2684 C CG   B LEU   A 1 127 ? 21.779 -6.103  0.137   0.12 9.19  ?  127 LEU   A CG   1 
ATOM   2685 C CD1  A LEU   A 1 127 ? 23.002 -7.894  -0.243  0.88 12.55 ?  127 LEU   A CD1  1 
ATOM   2686 C CD1  B LEU   A 1 127 ? 22.998 -7.022  0.072   0.12 8.92  ?  127 LEU   A CD1  1 
ATOM   2687 C CD2  A LEU   A 1 127 ? 22.499 -5.612  0.568   0.88 12.90 ?  127 LEU   A CD2  1 
ATOM   2688 C CD2  B LEU   A 1 127 ? 22.192 -4.689  0.520   0.12 9.10  ?  127 LEU   A CD2  1 
ATOM   2689 H H    A LEU   A 1 127 ? 19.088 -6.981  0.117   0.88 12.88 ?  127 LEU   A H    1 
ATOM   2690 H H    B LEU   A 1 127 ? 18.649 -6.587  -0.342  0.12 12.79 ?  127 LEU   A H    1 
ATOM   2691 H HA   A LEU   A 1 127 ? 20.247 -4.828  -0.802  0.88 12.87 ?  127 LEU   A HA   1 
ATOM   2692 H HA   B LEU   A 1 127 ? 19.979 -4.333  -1.015  0.12 12.16 ?  127 LEU   A HA   1 
ATOM   2693 H HB2  A LEU   A 1 127 ? 20.755 -7.505  -1.518  0.88 13.64 ?  127 LEU   A HB2  1 
ATOM   2694 H HB2  B LEU   A 1 127 ? 20.754 -7.020  -1.373  0.12 11.74 ?  127 LEU   A HB2  1 
ATOM   2695 H HB3  A LEU   A 1 127 ? 21.706 -6.297  -1.886  0.88 13.64 ?  127 LEU   A HB3  1 
ATOM   2696 H HB3  B LEU   A 1 127 ? 21.620 -5.798  -1.876  0.12 11.74 ?  127 LEU   A HB3  1 
ATOM   2697 H HG   A LEU   A 1 127 ? 21.322 -7.264  0.734   0.88 14.31 ?  127 LEU   A HG   1 
ATOM   2698 H HG   B LEU   A 1 127 ? 21.196 -6.441  0.834   0.12 11.02 ?  127 LEU   A HG   1 
ATOM   2699 H HD11 A LEU   A 1 127 ? 23.500 -8.065  0.572   0.88 15.04 ?  127 LEU   A HD11 1 
ATOM   2700 H HD11 B LEU   A 1 127 ? 23.458 -6.998  0.926   0.12 10.69 ?  127 LEU   A HD11 1 
ATOM   2701 H HD12 A LEU   A 1 127 ? 22.602 -8.722  -0.562  0.88 15.04 ?  127 LEU   A HD12 1 
ATOM   2702 H HD12 B LEU   A 1 127 ? 22.703 -7.927  -0.118  0.12 10.69 ?  127 LEU   A HD12 1 
ATOM   2703 H HD13 A LEU   A 1 127 ? 23.590 -7.531  -0.921  0.88 15.04 ?  127 LEU   A HD13 1 
ATOM   2704 H HD13 B LEU   A 1 127 ? 23.591 -6.713  -0.631  0.12 10.69 ?  127 LEU   A HD13 1 
ATOM   2705 H HD21 A LEU   A 1 127 ? 23.100 -5.821  1.305   0.88 15.48 ?  127 LEU   A HD21 1 
ATOM   2706 H HD21 B LEU   A 1 127 ? 22.793 -4.731  1.279   0.12 10.91 ?  127 LEU   A HD21 1 
ATOM   2707 H HD22 A LEU   A 1 127 ? 23.002 -5.186  -0.149  0.88 15.48 ?  127 LEU   A HD22 1 
ATOM   2708 H HD22 B LEU   A 1 127 ? 22.638 -4.275  -0.235  0.12 10.91 ?  127 LEU   A HD22 1 
ATOM   2709 H HD23 A LEU   A 1 127 ? 21.793 -5.028  0.870   0.88 15.48 ?  127 LEU   A HD23 1 
ATOM   2710 H HD23 B LEU   A 1 127 ? 21.398 -4.182  0.754   0.12 10.91 ?  127 LEU   A HD23 1 
ATOM   2711 N N    A SER   A 1 128 ? 19.727 -4.423  -3.142  0.88 10.16 ?  128 SER   A N    1 
ATOM   2712 N N    B SER   A 1 128 ? 19.750 -4.244  -3.474  0.12 10.58 ?  128 SER   A N    1 
ATOM   2713 C CA   A SER   A 1 128 ? 19.318 -4.021  -4.477  0.88 10.46 ?  128 SER   A CA   1 
ATOM   2714 C CA   B SER   A 1 128 ? 19.522 -4.045  -4.905  0.12 10.59 ?  128 SER   A CA   1 
ATOM   2715 C C    A SER   A 1 128 ? 17.866 -3.569  -4.558  0.88 10.63 ?  128 SER   A C    1 
ATOM   2716 C C    B SER   A 1 128 ? 18.105 -3.608  -5.261  0.12 10.54 ?  128 SER   A C    1 
ATOM   2717 O O    A SER   A 1 128 ? 17.405 -3.254  -5.655  0.88 11.87 ?  128 SER   A O    1 
ATOM   2718 O O    B SER   A 1 128 ? 17.840 -3.344  -6.441  0.12 10.41 ?  128 SER   A O    1 
ATOM   2719 C CB   A SER   A 1 128 ? 19.640 -5.060  -5.560  0.88 10.90 ?  128 SER   A CB   1 
ATOM   2720 C CB   B SER   A 1 128 ? 19.908 -5.261  -5.760  0.12 10.51 ?  128 SER   A CB   1 
ATOM   2721 O OG   A SER   A 1 128 ? 21.046 -5.268  -5.644  0.88 11.48 ?  128 SER   A OG   1 
ATOM   2722 O OG   B SER   A 1 128 ? 21.302 -5.504  -5.693  0.12 10.44 ?  128 SER   A OG   1 
ATOM   2723 H H    A SER   A 1 128 ? 20.320 -3.889  -2.814  0.88 12.18 ?  128 SER   A H    1 
ATOM   2724 H H    B SER   A 1 128 ? 20.278 -3.647  -3.151  0.12 12.69 ?  128 SER   A H    1 
ATOM   2725 H HA   A SER   A 1 128 ? 19.846 -3.244  -4.699  0.88 12.54 ?  128 SER   A HA   1 
ATOM   2726 H HA   B SER   A 1 128 ? 20.102 -3.323  -5.180  0.12 12.70 ?  128 SER   A HA   1 
ATOM   2727 H HB2  A SER   A 1 128 ? 19.204 -5.895  -5.346  0.88 13.07 ?  128 SER   A HB2  1 
ATOM   2728 H HB2  B SER   A 1 128 ? 19.430 -6.038  -5.438  0.12 12.61 ?  128 SER   A HB2  1 
ATOM   2729 H HB3  A SER   A 1 128 ? 19.317 -4.728  -6.420  0.88 13.07 ?  128 SER   A HB3  1 
ATOM   2730 H HB3  B SER   A 1 128 ? 19.666 -5.080  -6.684  0.12 12.61 ?  128 SER   A HB3  1 
ATOM   2731 H HG   A SER   A 1 128 ? 21.435 -4.544  -5.831  0.88 13.77 ?  128 SER   A HG   1 
ATOM   2732 H HG   B SER   A 1 128 ? 21.719 -4.825  -5.959  0.12 12.52 ?  128 SER   A HG   1 
ATOM   2733 N N    A ALA   A 1 129 ? 17.150 -3.488  -3.436  0.88 11.46 ?  129 ALA   A N    1 
ATOM   2734 N N    B ALA   A 1 129 ? 17.195 -3.508  -4.302  0.12 10.69 ?  129 ALA   A N    1 
ATOM   2735 C CA   A ALA   A 1 129 ? 15.792 -2.970  -3.427  0.88 12.04 ?  129 ALA   A CA   1 
ATOM   2736 C CA   B ALA   A 1 129 ? 15.829 -3.103  -4.578  0.12 11.29 ?  129 ALA   A CA   1 
ATOM   2737 C C    A ALA   A 1 129 ? 15.817 -1.440  -3.417  0.88 11.55 ?  129 ALA   A C    1 
ATOM   2738 C C    B ALA   A 1 129 ? 15.683 -1.605  -4.313  0.12 12.16 ?  129 ALA   A C    1 
ATOM   2739 O O    A ALA   A 1 129 ? 16.873 -0.799  -3.509  0.88 11.47 ?  129 ALA   A O    1 
ATOM   2740 O O    B ALA   A 1 129 ? 16.670 -0.883  -4.140  0.12 12.24 ?  129 ALA   A O    1 
ATOM   2741 C CB   A ALA   A 1 129 ? 15.013 -3.535  -2.239  0.88 13.52 ?  129 ALA   A CB   1 
ATOM   2742 C CB   B ALA   A 1 129 ? 14.873 -3.941  -3.731  0.12 11.43 ?  129 ALA   A CB   1 
ATOM   2743 H H    A ALA   A 1 129 ? 17.439 -3.722  -2.656  0.88 13.74 ?  129 ALA   A H    1 
ATOM   2744 H H    B ALA   A 1 129 ? 17.344 -3.657  -3.467  0.12 12.82 ?  129 ALA   A H    1 
ATOM   2745 H HA   A ALA   A 1 129 ? 15.349 -3.255  -4.235  0.88 14.44 ?  129 ALA   A HA   1 
ATOM   2746 H HA   B ALA   A 1 129 ? 15.630 -3.275  -5.516  0.12 13.54 ?  129 ALA   A HA   1 
ATOM   2747 H HB1  A ALA   A 1 129 ? 14.107 -3.186  -2.262  0.88 16.22 ?  129 ALA   A HB1  1 
ATOM   2748 H HB1  B ALA   A 1 129 ? 13.965 -3.648  -3.894  0.12 13.70 ?  129 ALA   A HB1  1 
ATOM   2749 H HB2  A ALA   A 1 129 ? 14.996 -4.502  -2.304  0.88 16.22 ?  129 ALA   A HB2  1 
ATOM   2750 H HB2  B ALA   A 1 129 ? 14.974 -4.871  -3.982  0.12 13.70 ?  129 ALA   A HB2  1 
ATOM   2751 H HB3  A ALA   A 1 129 ? 15.449 -3.266  -1.414  0.88 16.22 ?  129 ALA   A HB3  1 
ATOM   2752 H HB3  B ALA   A 1 129 ? 15.101 -3.822  -2.797  0.12 13.70 ?  129 ALA   A HB3  1 
ATOM   2753 N N    A GLY   A 1 130 ? 14.630 -0.846  -3.333  0.88 12.68 ?  130 GLY   A N    1 
ATOM   2754 N N    B GLY   A 1 130 ? 14.442 -1.127  -4.284  0.12 12.81 ?  130 GLY   A N    1 
ATOM   2755 C CA   A GLY   A 1 130 ? 14.545 0.604   -3.293  0.88 13.27 ?  130 GLY   A CA   1 
ATOM   2756 C CA   B GLY   A 1 130 ? 14.209 0.276   -3.993  0.12 13.55 ?  130 GLY   A CA   1 
ATOM   2757 C C    A GLY   A 1 130 ? 15.151 1.215   -4.537  0.88 12.86 ?  130 GLY   A C    1 
ATOM   2758 C C    B GLY   A 1 130 ? 14.797 1.145   -5.082  0.12 14.24 ?  130 GLY   A C    1 
ATOM   2759 O O    A GLY   A 1 130 ? 14.903 0.762   -5.660  0.88 13.09 ?  130 GLY   A O    1 
ATOM   2760 O O    B GLY   A 1 130 ? 14.628 0.891   -6.280  0.12 14.50 ?  130 GLY   A O    1 
ATOM   2761 H H    A GLY   A 1 130 ? 13.871 -1.253  -3.305  0.88 15.21 ?  130 GLY   A H    1 
ATOM   2762 H H    B GLY   A 1 130 ? 13.729 -1.574  -4.440  0.12 15.36 ?  130 GLY   A H    1 
ATOM   2763 H HA2  A GLY   A 1 130 ? 13.612 0.876   -3.230  0.88 15.92 ?  130 GLY   A HA2  1 
ATOM   2764 H HA2  B GLY   A 1 130 ? 13.257 0.454   -3.923  0.12 16.25 ?  130 GLY   A HA2  1 
ATOM   2765 H HA3  A GLY   A 1 130 ? 15.021 0.940   -2.523  0.88 15.92 ?  130 GLY   A HA3  1 
ATOM   2766 H HA3  B GLY   A 1 130 ? 14.631 0.512   -3.150  0.12 16.25 ?  130 GLY   A HA3  1 
ATOM   2767 N N    A ILE   A 1 131 ? 15.966 2.258   -4.340  0.88 12.69 ?  131 ILE   A N    1 
ATOM   2768 N N    B ILE   A 1 131 ? 15.512 2.186   -4.657  0.12 14.56 ?  131 ILE   A N    1 
ATOM   2769 C CA   A ILE   A 1 131 ? 16.528 3.009   -5.459  0.88 12.53 ?  131 ILE   A CA   1 
ATOM   2770 C CA   B ILE   A 1 131 ? 16.151 3.119   -5.573  0.12 14.81 ?  131 ILE   A CA   1 
ATOM   2771 C C    A ILE   A 1 131 ? 17.536 2.217   -6.277  0.88 11.88 ?  131 ILE   A C    1 
ATOM   2772 C C    B ILE   A 1 131 ? 17.223 2.458   -6.437  0.12 14.75 ?  131 ILE   A C    1 
ATOM   2773 O O    A ILE   A 1 131 ? 17.959 2.699   -7.336  0.88 12.79 ?  131 ILE   A O    1 
ATOM   2774 O O    B ILE   A 1 131 ? 17.670 3.052   -7.422  0.12 14.74 ?  131 ILE   A O    1 
ATOM   2775 C CB   A ILE   A 1 131 ? 17.105 4.376   -5.028  0.88 13.49 ?  131 ILE   A CB   1 
ATOM   2776 C CB   B ILE   A 1 131 ? 16.652 4.334   -4.748  0.12 15.28 ?  131 ILE   A CB   1 
ATOM   2777 C CG1  A ILE   A 1 131 ? 18.345 4.206   -4.140  0.88 14.59 ?  131 ILE   A CG1  1 
ATOM   2778 C CG1  B ILE   A 1 131 ? 17.503 5.297   -5.582  0.12 15.68 ?  131 ILE   A CG1  1 
ATOM   2779 C CG2  A ILE   A 1 131 ? 16.029 5.204   -4.329  0.88 14.12 ?  131 ILE   A CG2  1 
ATOM   2780 C CG2  B ILE   A 1 131 ? 17.384 3.872   -3.489  0.12 15.36 ?  131 ILE   A CG2  1 
ATOM   2781 C CD1  A ILE   A 1 131 ? 19.009 5.530   -3.754  0.88 16.04 ?  131 ILE   A CD1  1 
ATOM   2782 C CD1  B ILE   A 1 131 ? 18.920 5.480   -5.094  0.12 15.86 ?  131 ILE   A CD1  1 
ATOM   2783 H H    A ILE   A 1 131 ? 16.191 2.550   -3.566  0.88 15.22 ?  131 ILE   A H    1 
ATOM   2784 H H    B ILE   A 1 131 ? 15.631 2.369   -3.823  0.12 17.46 ?  131 ILE   A H    1 
ATOM   2785 H HA   A ILE   A 1 131 ? 15.805 3.206   -6.061  0.88 15.03 ?  131 ILE   A HA   1 
ATOM   2786 H HA   B ILE   A 1 131 ? 15.477 3.455   -6.183  0.12 17.77 ?  131 ILE   A HA   1 
ATOM   2787 H HB   A ILE   A 1 131 ? 17.374 4.849   -5.829  0.88 16.18 ?  131 ILE   A HB   1 
ATOM   2788 H HB   B ILE   A 1 131 ? 15.865 4.826   -4.473  0.12 18.33 ?  131 ILE   A HB   1 
ATOM   2789 H HG12 A ILE   A 1 131 ? 18.091 3.757   -3.322  0.88 17.49 ?  131 ILE   A HG12 1 
ATOM   2790 H HG12 B ILE   A 1 131 ? 17.535 5.005   -6.500  0.12 18.81 ?  131 ILE   A HG12 1 
ATOM   2791 H HG13 A ILE   A 1 131 ? 19.009 3.681   -4.614  0.88 17.49 ?  131 ILE   A HG13 1 
ATOM   2792 H HG13 B ILE   A 1 131 ? 17.076 6.164   -5.538  0.12 18.81 ?  131 ILE   A HG13 1 
ATOM   2793 H HG21 A ILE   A 1 131 ? 16.355 6.108   -4.205  0.88 16.93 ?  131 ILE   A HG21 1 
ATOM   2794 H HG21 B ILE   A 1 131 ? 17.748 4.637   -3.031  0.12 18.43 ?  131 ILE   A HG21 1 
ATOM   2795 H HG22 A ILE   A 1 131 ? 15.232 5.212   -4.882  0.88 16.93 ?  131 ILE   A HG22 1 
ATOM   2796 H HG22 B ILE   A 1 131 ? 16.758 3.440   -2.899  0.12 18.43 ?  131 ILE   A HG22 1 
ATOM   2797 H HG23 A ILE   A 1 131 ? 15.829 4.801   -3.469  0.88 16.93 ?  131 ILE   A HG23 1 
ATOM   2798 H HG23 B ILE   A 1 131 ? 18.085 3.255   -3.742  0.12 18.43 ?  131 ILE   A HG23 1 
ATOM   2799 H HD11 A ILE   A 1 131 ? 19.844 5.346   -3.290  0.88 19.24 ?  131 ILE   A HD11 1 
ATOM   2800 H HD11 B ILE   A 1 131 ? 19.403 6.012   -5.738  0.12 19.03 ?  131 ILE   A HD11 1 
ATOM   2801 H HD12 A ILE   A 1 131 ? 19.189 6.045   -4.558  0.88 19.24 ?  131 ILE   A HD12 1 
ATOM   2802 H HD12 B ILE   A 1 131 ? 18.903 5.941   -4.239  0.12 19.03 ?  131 ILE   A HD12 1 
ATOM   2803 H HD13 A ILE   A 1 131 ? 18.414 6.030   -3.172  0.88 19.24 ?  131 ILE   A HD13 1 
ATOM   2804 H HD13 B ILE   A 1 131 ? 19.342 4.612   -5.004  0.12 19.03 ?  131 ILE   A HD13 1 
ATOM   2805 N N    A PHE   A 1 132 ? 17.933 1.016   -5.830  0.88 11.49 ?  132 PHE   A N    1 
ATOM   2806 N N    B PHE   A 1 132 ? 17.616 1.223   -6.123  0.12 14.82 ?  132 PHE   A N    1 
ATOM   2807 C CA   A PHE   A 1 132 ? 18.781 0.161   -6.656  0.88 11.61 ?  132 PHE   A CA   1 
ATOM   2808 C CA   B PHE   A 1 132 ? 18.656 0.541   -6.884  0.12 14.79 ?  132 PHE   A CA   1 
ATOM   2809 C C    A PHE   A 1 132 ? 17.994 -0.590  -7.728  0.88 12.24 ?  132 PHE   A C    1 
ATOM   2810 C C    B PHE   A 1 132 ? 18.144 -0.191  -8.119  0.12 14.96 ?  132 PHE   A C    1 
ATOM   2811 O O    A PHE   A 1 132 ? 18.607 -1.212  -8.602  0.88 13.32 ?  132 PHE   A O    1 
ATOM   2812 O O    B PHE   A 1 132 ? 18.953 -0.536  -8.988  0.12 15.24 ?  132 PHE   A O    1 
ATOM   2813 C CB   A PHE   A 1 132 ? 19.599 -0.820  -5.804  0.88 11.25 ?  132 PHE   A CB   1 
ATOM   2814 C CB   B PHE   A 1 132 ? 19.426 -0.429  -5.984  0.12 14.58 ?  132 PHE   A CB   1 
ATOM   2815 C CG   A PHE   A 1 132 ? 20.818 -0.210  -5.138  0.88 11.13 ?  132 PHE   A CG   1 
ATOM   2816 C CG   B PHE   A 1 132 ? 20.573 0.210   -5.260  0.12 14.59 ?  132 PHE   A CG   1 
ATOM   2817 C CD1  A PHE   A 1 132 ? 20.696 0.823   -4.224  0.88 12.03 ?  132 PHE   A CD1  1 
ATOM   2818 C CD1  B PHE   A 1 132 ? 20.356 1.237   -4.356  0.12 14.74 ?  132 PHE   A CD1  1 
ATOM   2819 C CD2  A PHE   A 1 132 ? 22.082 -0.715  -5.393  0.88 11.80 ?  132 PHE   A CD2  1 
ATOM   2820 C CD2  B PHE   A 1 132 ? 21.870 -0.217  -5.485  0.12 14.61 ?  132 PHE   A CD2  1 
ATOM   2821 C CE1  A PHE   A 1 132 ? 21.815 1.360   -3.604  0.88 12.18 ?  132 PHE   A CE1  1 
ATOM   2822 C CE1  B PHE   A 1 132 ? 21.413 1.827   -3.692  0.12 14.83 ?  132 PHE   A CE1  1 
ATOM   2823 C CE2  A PHE   A 1 132 ? 23.203 -0.184  -4.770  0.88 12.03 ?  132 PHE   A CE2  1 
ATOM   2824 C CE2  B PHE   A 1 132 ? 22.930 0.367   -4.823  0.12 14.83 ?  132 PHE   A CE2  1 
ATOM   2825 C CZ   A PHE   A 1 132 ? 23.065 0.855   -3.874  0.88 11.89 ?  132 PHE   A CZ   1 
ATOM   2826 C CZ   B PHE   A 1 132 ? 22.702 1.389   -3.926  0.12 14.86 ?  132 PHE   A CZ   1 
ATOM   2827 H H    A PHE   A 1 132 ? 17.729 0.675   -5.058  0.88 13.78 ?  132 PHE   A H    1 
ATOM   2828 H H    B PHE   A 1 132 ? 17.301 0.767   -5.472  0.12 17.77 ?  132 PHE   A H    1 
ATOM   2829 H HA   A PHE   A 1 132 ? 19.417 0.726   -7.113  0.88 13.93 ?  132 PHE   A HA   1 
ATOM   2830 H HA   B PHE   A 1 132 ? 19.288 1.205   -7.192  0.12 17.74 ?  132 PHE   A HA   1 
ATOM   2831 H HB2  A PHE   A 1 132 ? 19.030 -1.175  -5.101  0.88 13.49 ?  132 PHE   A HB2  1 
ATOM   2832 H HB2  B PHE   A 1 132 ? 18.821 -0.790  -5.321  0.12 17.49 ?  132 PHE   A HB2  1 
ATOM   2833 H HB3  A PHE   A 1 132 ? 19.905 -1.553  -6.371  0.88 13.49 ?  132 PHE   A HB3  1 
ATOM   2834 H HB3  B PHE   A 1 132 ? 19.783 -1.146  -6.531  0.12 17.49 ?  132 PHE   A HB3  1 
ATOM   2835 H HD1  A PHE   A 1 132 ? 19.858 1.170   -4.032  0.88 14.43 ?  132 PHE   A HD1  1 
ATOM   2836 H HD1  B PHE   A 1 132 ? 19.488 1.537   -4.198  0.12 17.68 ?  132 PHE   A HD1  1 
ATOM   2837 H HD2  A PHE   A 1 132 ? 22.188 -1.423  -5.997  0.88 14.15 ?  132 PHE   A HD2  1 
ATOM   2838 H HD2  B PHE   A 1 132 ? 22.028 -0.904  -6.090  0.12 17.53 ?  132 PHE   A HD2  1 
ATOM   2839 H HE1  A PHE   A 1 132 ? 21.722 2.063   -3.001  0.88 14.60 ?  132 PHE   A HE1  1 
ATOM   2840 H HE1  B PHE   A 1 132 ? 21.259 2.517   -3.087  0.12 17.79 ?  132 PHE   A HE1  1 
ATOM   2841 H HE2  A PHE   A 1 132 ? 24.048 -0.527  -4.963  0.88 14.43 ?  132 PHE   A HE2  1 
ATOM   2842 H HE2  B PHE   A 1 132 ? 23.796 0.071   -4.983  0.12 17.78 ?  132 PHE   A HE2  1 
ATOM   2843 H HZ   A PHE   A 1 132 ? 23.815 1.219   -3.465  0.88 14.26 ?  132 PHE   A HZ   1 
ATOM   2844 H HZ   B PHE   A 1 132 ? 23.415 1.782   -3.480  0.12 17.82 ?  132 PHE   A HZ   1 
ATOM   2845 N N    A GLY   A 1 133 ? 16.661 -0.555  -7.687  0.88 12.53 ?  133 GLY   A N    1 
ATOM   2846 N N    B GLY   A 1 133 ? 16.840 -0.448  -8.222  0.12 14.72 ?  133 GLY   A N    1 
ATOM   2847 C CA   A GLY   A 1 133 ? 15.857 -0.918  -8.837  0.88 13.20 ?  133 GLY   A CA   1 
ATOM   2848 C CA   B GLY   A 1 133 ? 16.281 -0.951  -9.464  0.12 14.61 ?  133 GLY   A CA   1 
ATOM   2849 C C    A GLY   A 1 133 ? 15.512 -2.383  -9.014  0.88 13.62 ?  133 GLY   A C    1 
ATOM   2850 C C    B GLY   A 1 133 ? 15.530 -2.268  -9.388  0.12 14.54 ?  133 GLY   A C    1 
ATOM   2851 O O    A GLY   A 1 133 ? 14.841 -2.715  -10.001 0.88 15.10 ?  133 GLY   A O    1 
ATOM   2852 O O    B GLY   A 1 133 ? 14.440 -2.391  -9.955  0.12 14.51 ?  133 GLY   A O    1 
ATOM   2853 H H    A GLY   A 1 133 ? 16.196 -0.323  -6.997  0.88 15.03 ?  133 GLY   A H    1 
ATOM   2854 H H    B GLY   A 1 133 ? 16.267 -0.334  -7.592  0.12 17.66 ?  133 GLY   A H    1 
ATOM   2855 H HA2  A GLY   A 1 133 ? 15.018 -0.437  -8.793  0.88 15.83 ?  133 GLY   A HA2  1 
ATOM   2856 H HA2  B GLY   A 1 133 ? 15.669 -0.287  -9.813  0.12 17.52 ?  133 GLY   A HA2  1 
ATOM   2857 H HA3  A GLY   A 1 133 ? 16.321 -0.628  -9.639  0.88 15.83 ?  133 GLY   A HA3  1 
ATOM   2858 H HA3  B GLY   A 1 133 ? 16.998 -1.054  -10.112 0.12 17.52 ?  133 GLY   A HA3  1 
ATOM   2859 N N    A ALA   A 1 134 ? 15.946 -3.272  -8.123  0.88 12.83 ?  134 ALA   A N    1 
ATOM   2860 N N    B ALA   A 1 134 ? 16.094 -3.258  -8.701  0.12 14.39 ?  134 ALA   A N    1 
ATOM   2861 C CA   A ALA   A 1 134 ? 15.603 -4.678  -8.277  0.88 13.41 ?  134 ALA   A CA   1 
ATOM   2862 C CA   B ALA   A 1 134 ? 15.565 -4.613  -8.770  0.12 14.11 ?  134 ALA   A CA   1 
ATOM   2863 C C    A ALA   A 1 134 ? 14.241 -4.969  -7.652  0.88 13.70 ?  134 ALA   A C    1 
ATOM   2864 C C    B ALA   A 1 134 ? 14.270 -4.745  -7.964  0.12 14.16 ?  134 ALA   A C    1 
ATOM   2865 O O    A ALA   A 1 134 ? 13.705 -4.184  -6.865  0.88 15.02 ?  134 ALA   A O    1 
ATOM   2866 O O    B ALA   A 1 134 ? 13.865 -3.850  -7.217  0.12 14.44 ?  134 ALA   A O    1 
ATOM   2867 C CB   A ALA   A 1 134 ? 16.673 -5.577  -7.654  0.88 14.11 ?  134 ALA   A CB   1 
ATOM   2868 C CB   B ALA   A 1 134 ? 16.604 -5.615  -8.270  0.12 13.94 ?  134 ALA   A CB   1 
ATOM   2869 H H    A ALA   A 1 134 ? 16.446 -3.087  -7.440  0.88 15.38 ?  134 ALA   A H    1 
ATOM   2870 H H    B ALA   A 1 134 ? 16.779 -3.168  -8.190  0.12 17.26 ?  134 ALA   A H    1 
ATOM   2871 H HA   A ALA   A 1 134 ? 15.557 -4.886  -9.225  0.88 16.08 ?  134 ALA   A HA   1 
ATOM   2872 H HA   B ALA   A 1 134 ? 15.368 -4.825  -9.695  0.12 16.92 ?  134 ALA   A HA   1 
ATOM   2873 H HB1  A ALA   A 1 134 ? 16.425 -6.502  -7.795  0.88 16.93 ?  134 ALA   A HB1  1 
ATOM   2874 H HB1  B ALA   A 1 134 ? 16.210 -6.501  -8.267  0.12 16.71 ?  134 ALA   A HB1  1 
ATOM   2875 H HB2  A ALA   A 1 134 ? 17.529 -5.394  -8.079  0.88 16.93 ?  134 ALA   A HB2  1 
ATOM   2876 H HB2  B ALA   A 1 134 ? 17.372 -5.597  -8.862  0.12 16.71 ?  134 ALA   A HB2  1 
ATOM   2877 H HB3  A ALA   A 1 134 ? 16.731 -5.387  -6.705  0.88 16.93 ?  134 ALA   A HB3  1 
ATOM   2878 H HB3  B ALA   A 1 134 ? 16.870 -5.372  -7.371  0.12 16.71 ?  134 ALA   A HB3  1 
ATOM   2879 N N    A ASP   A 1 135 ? 13.683 -6.119  -8.024  0.88 14.83 ?  135 ASP   A N    1 
ATOM   2880 N N    B ASP   A 1 135 ? 13.618 -5.898  -8.134  0.12 14.25 ?  135 ASP   A N    1 
ATOM   2881 C CA   A ASP   A 1 135 ? 12.424 -6.598  -7.456  0.88 15.96 ?  135 ASP   A CA   1 
ATOM   2882 C CA   B ASP   A 1 135 ? 12.363 -6.194  -7.452  0.12 14.33 ?  135 ASP   A CA   1 
ATOM   2883 C C    A ASP   A 1 135 ? 12.670 -7.055  -6.022  0.88 15.35 ?  135 ASP   A C    1 
ATOM   2884 C C    B ASP   A 1 135 ? 12.649 -6.650  -6.024  0.12 14.37 ?  135 ASP   A C    1 
ATOM   2885 O O    A ASP   A 1 135 ? 13.444 -7.999  -5.813  0.88 14.77 ?  135 ASP   A O    1 
ATOM   2886 O O    B ASP   A 1 135 ? 13.411 -7.601  -5.825  0.12 14.32 ?  135 ASP   A O    1 
ATOM   2887 C CB   A ASP   A 1 135 ? 11.938 -7.775  -8.304  0.88 18.58 ?  135 ASP   A CB   1 
ATOM   2888 C CB   B ASP   A 1 135 ? 11.627 -7.308  -8.192  0.12 14.40 ?  135 ASP   A CB   1 
ATOM   2889 C CG   A ASP   A 1 135 ? 10.652 -8.408  -7.777  0.88 21.19 ?  135 ASP   A CG   1 
ATOM   2890 C CG   B ASP   A 1 135 ? 10.196 -7.490  -7.714  0.12 14.49 ?  135 ASP   A CG   1 
ATOM   2891 O OD1  A ASP   A 1 135 ? 10.105 -7.929  -6.762  0.88 21.38 ?  135 ASP   A OD1  1 
ATOM   2892 O OD1  B ASP   A 1 135 ? 9.902  -7.165  -6.544  0.12 14.59 ?  135 ASP   A OD1  1 
ATOM   2893 O OD2  A ASP   A 1 135 ? 10.183 -9.386  -8.400  0.88 24.10 -1 135 ASP   A OD2  1 
ATOM   2894 O OD2  B ASP   A 1 135 ? 9.366  -7.975  -8.512  0.12 14.52 -1 135 ASP   A OD2  1 
ATOM   2895 H H    A ASP   A 1 135 ? 14.017 -6.641  -8.619  0.88 17.79 ?  135 ASP   A H    1 
ATOM   2896 H H    B ASP   A 1 135 ? 13.882 -6.528  -8.650  0.12 17.09 ?  135 ASP   A H    1 
ATOM   2897 H HA   A ASP   A 1 135 ? 11.757 -5.890  -7.484  0.88 19.15 ?  135 ASP   A HA   1 
ATOM   2898 H HA   B ASP   A 1 135 ? 11.802 -5.402  -7.448  0.12 17.18 ?  135 ASP   A HA   1 
ATOM   2899 H HB2  A ASP   A 1 135 ? 11.769 -7.464  -9.206  0.88 22.29 ?  135 ASP   A HB2  1 
ATOM   2900 H HB2  B ASP   A 1 135 ? 11.618 -7.102  -9.139  0.12 17.27 ?  135 ASP   A HB2  1 
ATOM   2901 H HB3  A ASP   A 1 135 ? 12.631 -8.454  -8.313  0.88 22.29 ?  135 ASP   A HB3  1 
ATOM   2902 H HB3  B ASP   A 1 135 ? 12.088 -8.146  -8.038  0.12 17.27 ?  135 ASP   A HB3  1 
ATOM   2903 N N    A PRO   A 1 136 ? 12.064 -6.422  -5.013  0.88 15.36 ?  136 PRO   A N    1 
ATOM   2904 N N    B PRO   A 1 136 ? 12.057 -6.009  -5.013  0.12 14.55 ?  136 PRO   A N    1 
ATOM   2905 C CA   A PRO   A 1 136 ? 12.322 -6.847  -3.624  0.88 15.32 ?  136 PRO   A CA   1 
ATOM   2906 C CA   B PRO   A 1 136 ? 12.308 -6.436  -3.626  0.12 14.69 ?  136 PRO   A CA   1 
ATOM   2907 C C    A PRO   A 1 136 ? 11.890 -8.272  -3.315  0.88 14.32 ?  136 PRO   A C    1 
ATOM   2908 C C    B PRO   A 1 136 ? 11.864 -7.858  -3.317  0.12 14.73 ?  136 PRO   A C    1 
ATOM   2909 O O    A PRO   A 1 136 ? 12.484 -8.908  -2.435  0.88 13.79 ?  136 PRO   A O    1 
ATOM   2910 O O    B PRO   A 1 136 ? 12.414 -8.472  -2.394  0.12 14.63 ?  136 PRO   A O    1 
ATOM   2911 C CB   A PRO   A 1 136 ? 11.547 -5.814  -2.792  0.88 16.65 ?  136 PRO   A CB   1 
ATOM   2912 C CB   B PRO   A 1 136 ? 11.544 -5.397  -2.791  0.12 14.81 ?  136 PRO   A CB   1 
ATOM   2913 C CG   A PRO   A 1 136 ? 10.498 -5.283  -3.720  0.88 17.89 ?  136 PRO   A CG   1 
ATOM   2914 C CG   B PRO   A 1 136 ? 10.544 -4.800  -3.742  0.12 14.91 ?  136 PRO   A CG   1 
ATOM   2915 C CD   A PRO   A 1 136 ? 11.131 -5.283  -5.078  0.88 16.69 ?  136 PRO   A CD   1 
ATOM   2916 C CD   B PRO   A 1 136 ? 11.213 -4.805  -5.072  0.12 14.79 ?  136 PRO   A CD   1 
ATOM   2917 H HA   A PRO   A 1 136 ? 13.271 -6.757  -3.426  0.88 18.37 ?  136 PRO   A HA   1 
ATOM   2918 H HA   B PRO   A 1 136 ? 13.249 -6.363  -3.419  0.12 17.62 ?  136 PRO   A HA   1 
ATOM   2919 H HB2  A PRO   A 1 136 ? 11.144 -6.251  -2.028  0.88 19.97 ?  136 PRO   A HB2  1 
ATOM   2920 H HB2  B PRO   A 1 136 ? 11.098 -5.834  -2.052  0.12 17.77 ?  136 PRO   A HB2  1 
ATOM   2921 H HB3  A PRO   A 1 136 ? 12.149 -5.107  -2.508  0.88 19.97 ?  136 PRO   A HB3  1 
ATOM   2922 H HB3  B PRO   A 1 136 ? 12.159 -4.715  -2.469  0.12 17.77 ?  136 PRO   A HB3  1 
ATOM   2923 H HG2  A PRO   A 1 136 ? 9.727  -5.866  -3.706  0.88 21.45 ?  136 PRO   A HG2  1 
ATOM   2924 H HG2  B PRO   A 1 136 ? 9.746  -5.351  -3.766  0.12 17.88 ?  136 PRO   A HG2  1 
ATOM   2925 H HG3  A PRO   A 1 136 ? 10.259 -4.382  -3.458  0.88 21.45 ?  136 PRO   A HG3  1 
ATOM   2926 H HG3  B PRO   A 1 136 ? 10.331 -3.895  -3.475  0.12 17.88 ?  136 PRO   A HG3  1 
ATOM   2927 H HD2  A PRO   A 1 136 ? 10.456 -5.438  -5.763  0.88 20.01 ?  136 PRO   A HD2  1 
ATOM   2928 H HD2  B PRO   A 1 136 ? 10.554 -4.883  -5.780  0.12 17.74 ?  136 PRO   A HD2  1 
ATOM   2929 H HD3  A PRO   A 1 136 ? 11.608 -4.452  -5.237  0.88 20.01 ?  136 PRO   A HD3  1 
ATOM   2930 H HD3  B PRO   A 1 136 ? 11.765 -4.013  -5.184  0.12 17.74 ?  136 PRO   A HD3  1 
ATOM   2931 N N    A ILE   A 1 137 ? 10.855 -8.785  -3.986  0.88 14.59 ?  137 ILE   A N    1 
ATOM   2932 N N    B ILE   A 1 137 ? 10.895 -8.406  -4.053  0.12 14.91 ?  137 ILE   A N    1 
ATOM   2933 C CA   A ILE   A 1 137 ? 10.479 -10.185 -3.795  0.88 15.11 ?  137 ILE   A CA   1 
ATOM   2934 C CA   B ILE   A 1 137 ? 10.470 -9.782  -3.806  0.12 15.19 ?  137 ILE   A CA   1 
ATOM   2935 C C    A ILE   A 1 137 ? 11.625 -11.097 -4.214  0.88 14.33 ?  137 ILE   A C    1 
ATOM   2936 C C    B ILE   A 1 137 ? 11.590 -10.754 -4.158  0.12 14.98 ?  137 ILE   A C    1 
ATOM   2937 O O    A ILE   A 1 137 ? 11.944 -12.083 -3.536  0.88 14.36 ?  137 ILE   A O    1 
ATOM   2938 O O    B ILE   A 1 137 ? 11.871 -11.700 -3.412  0.12 15.12 ?  137 ILE   A O    1 
ATOM   2939 C CB   A ILE   A 1 137 ? 9.178  -10.501 -4.556  0.88 16.60 ?  137 ILE   A CB   1 
ATOM   2940 C CB   B ILE   A 1 137 ? 9.179  -10.095 -4.585  0.12 15.72 ?  137 ILE   A CB   1 
ATOM   2941 C CG1  A ILE   A 1 137 ? 8.011  -9.667  -4.009  0.88 18.48 ?  137 ILE   A CG1  1 
ATOM   2942 C CG1  B ILE   A 1 137 ? 8.107  -9.036  -4.313  0.12 16.03 ?  137 ILE   A CG1  1 
ATOM   2943 C CG2  A ILE   A 1 137 ? 8.861  -11.993 -4.478  0.88 17.05 ?  137 ILE   A CG2  1 
ATOM   2944 C CG2  B ILE   A 1 137 ? 8.659  -11.484 -4.222  0.12 15.93 ?  137 ILE   A CG2  1 
ATOM   2945 C CD1  A ILE   A 1 137 ? 6.724  -9.833  -4.785  0.88 20.36 ?  137 ILE   A CD1  1 
ATOM   2946 C CD1  B ILE   A 1 137 ? 6.850  -9.232  -5.127  0.12 16.21 ?  137 ILE   A CD1  1 
ATOM   2947 H H    A ILE   A 1 137 ? 10.373 -8.355  -4.550  0.88 17.49 ?  137 ILE   A H    1 
ATOM   2948 H H    B ILE   A 1 137 ? 10.480 -8.006  -4.690  0.12 17.88 ?  137 ILE   A H    1 
ATOM   2949 H HA   A ILE   A 1 137 ? 10.320 -10.341 -2.855  0.88 18.12 ?  137 ILE   A HA   1 
ATOM   2950 H HA   B ILE   A 1 137 ? 10.273 -9.884  -2.861  0.12 18.22 ?  137 ILE   A HA   1 
ATOM   2951 H HB   A ILE   A 1 137 ? 9.304  -10.267 -5.487  0.88 19.91 ?  137 ILE   A HB   1 
ATOM   2952 H HB   B ILE   A 1 137 ? 9.382  -10.084 -5.531  0.12 18.85 ?  137 ILE   A HB   1 
ATOM   2953 H HG12 A ILE   A 1 137 ? 7.843  -9.924  -3.089  0.88 22.16 ?  137 ILE   A HG12 1 
ATOM   2954 H HG12 B ILE   A 1 137 ? 7.864  -9.069  -3.375  0.12 19.23 ?  137 ILE   A HG12 1 
ATOM   2955 H HG13 A ILE   A 1 137 ? 8.257  -8.725  -4.043  0.88 22.16 ?  137 ILE   A HG13 1 
ATOM   2956 H HG13 B ILE   A 1 137 ? 8.459  -8.160  -4.532  0.12 19.23 ?  137 ILE   A HG13 1 
ATOM   2957 H HG21 A ILE   A 1 137 ? 7.959  -12.156 -4.800  0.88 20.45 ?  137 ILE   A HG21 1 
ATOM   2958 H HG21 B ILE   A 1 137 ? 7.850  -11.664 -4.725  0.12 19.11 ?  137 ILE   A HG21 1 
ATOM   2959 H HG22 A ILE   A 1 137 ? 9.491  -12.476 -5.031  0.88 20.45 ?  137 ILE   A HG22 1 
ATOM   2960 H HG22 B ILE   A 1 137 ? 9.334  -12.143 -4.444  0.12 19.11 ?  137 ILE   A HG22 1 
ATOM   2961 H HG23 A ILE   A 1 137 ? 8.934  -12.280 -3.557  0.88 20.45 ?  137 ILE   A HG23 1 
ATOM   2962 H HG23 B ILE   A 1 137 ? 8.470  -11.512 -3.271  0.12 19.11 ?  137 ILE   A HG23 1 
ATOM   2963 H HD11 A ILE   A 1 137 ? 6.024  -10.121 -4.179  0.88 24.43 ?  137 ILE   A HD11 1 
ATOM   2964 H HD11 B ILE   A 1 137 ? 6.454  -8.367  -5.307  0.12 19.45 ?  137 ILE   A HD11 1 
ATOM   2965 H HD12 A ILE   A 1 137 ? 6.498  -8.980  -5.180  0.88 24.43 ?  137 ILE   A HD12 1 
ATOM   2966 H HD12 B ILE   A 1 137 ? 7.081  -9.670  -5.962  0.12 19.45 ?  137 ILE   A HD12 1 
ATOM   2967 H HD13 A ILE   A 1 137 ? 6.851  -10.490 -5.486  0.88 24.43 ?  137 ILE   A HD13 1 
ATOM   2968 H HD13 B ILE   A 1 137 ? 6.232  -9.787  -4.625  0.12 19.45 ?  137 ILE   A HD13 1 
ATOM   2969 N N    A HIS   A 1 138 ? 12.261 -10.778 -5.341  0.88 14.39 ?  138 HIS   A N    1 
ATOM   2970 N N    B HIS   A 1 138 ? 12.242 -10.537 -5.301  0.12 14.68 ?  138 HIS   A N    1 
ATOM   2971 C CA   A HIS   A 1 138 ? 13.433 -11.530 -5.769  0.88 14.27 ?  138 HIS   A CA   1 
ATOM   2972 C CA   B HIS   A 1 138 ? 13.320 -11.422 -5.733  0.12 14.28 ?  138 HIS   A CA   1 
ATOM   2973 C C    A HIS   A 1 138 ? 14.577 -11.383 -4.772  0.88 13.42 ?  138 HIS   A C    1 
ATOM   2974 C C    B HIS   A 1 138 ? 14.500 -11.362 -4.770  0.12 13.58 ?  138 HIS   A C    1 
ATOM   2975 O O    A HIS   A 1 138 ? 15.252 -12.368 -4.441  0.88 13.92 ?  138 HIS   A O    1 
ATOM   2976 O O    B HIS   A 1 138 ? 15.122 -12.387 -4.467  0.12 13.64 ?  138 HIS   A O    1 
ATOM   2977 C CB   A HIS   A 1 138 ? 13.849 -11.085 -7.171  0.88 15.00 ?  138 HIS   A CB   1 
ATOM   2978 C CB   B HIS   A 1 138 ? 13.742 -11.029 -7.149  0.12 14.57 ?  138 HIS   A CB   1 
ATOM   2979 C CG   A HIS   A 1 138 ? 15.114 -11.725 -7.647  0.88 16.12 ?  138 HIS   A CG   1 
ATOM   2980 C CG   B HIS   A 1 138 ? 15.058 -11.600 -7.574  0.12 14.95 ?  138 HIS   A CG   1 
ATOM   2981 N ND1  A HIS   A 1 138 ? 15.218 -13.079 -7.888  0.88 17.51 ?  138 HIS   A ND1  1 
ATOM   2982 N ND1  B HIS   A 1 138 ? 15.210 -12.913 -7.962  0.12 15.31 ?  138 HIS   A ND1  1 
ATOM   2983 C CD2  A HIS   A 1 138 ? 16.334 -11.200 -7.905  0.88 16.35 ?  138 HIS   A CD2  1 
ATOM   2984 C CD2  B HIS   A 1 138 ? 16.281 -11.030 -7.683  0.12 15.02 ?  138 HIS   A CD2  1 
ATOM   2985 C CE1  A HIS   A 1 138 ? 16.447 -13.357 -8.286  0.88 17.78 ?  138 HIS   A CE1  1 
ATOM   2986 C CE1  B HIS   A 1 138 ? 16.472 -13.130 -8.287  0.12 15.38 ?  138 HIS   A CE1  1 
ATOM   2987 N NE2  A HIS   A 1 138 ? 17.143 -12.235 -8.306  0.88 16.98 ?  138 HIS   A NE2  1 
ATOM   2988 N NE2  B HIS   A 1 138 ? 17.143 -12.003 -8.127  0.12 15.23 ?  138 HIS   A NE2  1 
ATOM   2989 H H    A HIS   A 1 138 ? 12.038 -10.132 -5.872  0.88 17.26 ?  138 HIS   A H    1 
ATOM   2990 H H    B HIS   A 1 138 ? 12.082 -9.884  -5.837  0.12 17.61 ?  138 HIS   A H    1 
ATOM   2991 H HA   A HIS   A 1 138 ? 13.197 -12.466 -5.822  0.88 17.11 ?  138 HIS   A HA   1 
ATOM   2992 H HA   B HIS   A 1 138 ? 12.994 -12.333 -5.755  0.12 17.13 ?  138 HIS   A HA   1 
ATOM   2993 H HB2  A HIS   A 1 138 ? 13.141 -11.319 -7.800  0.88 17.99 ?  138 HIS   A HB2  1 
ATOM   2994 H HB2  B HIS   A 1 138 ? 13.067 -11.341 -7.773  0.12 17.48 ?  138 HIS   A HB2  1 
ATOM   2995 H HB3  A HIS   A 1 138 ? 13.980 -10.124 -7.175  0.88 17.99 ?  138 HIS   A HB3  1 
ATOM   2996 H HB3  B HIS   A 1 138 ? 13.809 -10.062 -7.199  0.12 17.48 ?  138 HIS   A HB3  1 
ATOM   2997 H HD1  A HIS   A 1 138 ? 14.580 -13.650 -7.801  0.88 21.01 ?  138 HIS   A HD1  1 
ATOM   2998 H HD2  A HIS   A 1 138 ? 16.571 -10.304 -7.831  0.88 19.62 ?  138 HIS   A HD2  1 
ATOM   2999 H HD2  B HIS   A 1 138 ? 16.497 -10.146 -7.492  0.12 18.01 ?  138 HIS   A HD2  1 
ATOM   3000 H HE1  A HIS   A 1 138 ? 16.766 -14.199 -8.512  0.88 21.32 ?  138 HIS   A HE1  1 
ATOM   3001 H HE1  B HIS   A 1 138 ? 16.827 -13.937 -8.580  0.12 18.45 ?  138 HIS   A HE1  1 
ATOM   3002 H HE2  B HIS   A 1 138 ? 17.982 -11.896 -8.276  0.12 18.26 ?  138 HIS   A HE2  1 
ATOM   3003 N N    . SER   A 1 139 ? 14.814 -10.165 -4.277  1.00 12.98 ?  139 SER   A N    1 
ATOM   3004 C CA   . SER   A 1 139 ? 15.899 -9.988  -3.323  1.00 12.64 ?  139 SER   A CA   1 
ATOM   3005 C C    . SER   A 1 139 ? 15.686 -10.828 -2.069  1.00 12.10 ?  139 SER   A C    1 
ATOM   3006 O O    . SER   A 1 139 ? 16.634 -11.431 -1.553  1.00 12.23 ?  139 SER   A O    1 
ATOM   3007 C CB   . SER   A 1 139 ? 16.038 -8.510  -2.969  1.00 12.82 ?  139 SER   A CB   1 
ATOM   3008 O OG   . SER   A 1 139 ? 17.126 -8.348  -2.080  1.00 12.95 ?  139 SER   A OG   1 
ATOM   3009 H H    A SER   A 1 139 ? 14.372 -9.450  -4.469  0.88 15.57 ?  139 SER   A H    1 
ATOM   3010 H H    B SER   A 1 139 ? 14.402 -9.435  -4.480  0.12 15.57 ?  139 SER   A H    1 
ATOM   3011 H HA   . SER   A 1 139 ? 16.729 -10.271 -3.733  1.00 15.15 ?  139 SER   A HA   1 
ATOM   3012 H HB2  . SER   A 1 139 ? 16.201 -7.993  -3.776  1.00 15.37 ?  139 SER   A HB2  1 
ATOM   3013 H HB3  . SER   A 1 139 ? 15.225 -8.201  -2.534  1.00 15.37 ?  139 SER   A HB3  1 
ATOM   3014 H HG   . SER   A 1 139 ? 17.220 -7.540  -1.876  1.00 15.53 ?  139 SER   A HG   1 
ATOM   3015 N N    A LEU   A 1 140 ? 14.447 -10.903 -1.580  0.88 12.26 ?  140 LEU   A N    1 
ATOM   3016 N N    B LEU   A 1 140 ? 14.464 -10.818 -1.524  0.12 11.58 ?  140 LEU   A N    1 
ATOM   3017 C CA   A LEU   A 1 140 ? 14.178 -11.736 -0.413  0.88 12.04 ?  140 LEU   A CA   1 
ATOM   3018 C CA   B LEU   A 1 140 ? 14.192 -11.591 -0.315  0.12 11.03 ?  140 LEU   A CA   1 
ATOM   3019 C C    A LEU   A 1 140 ? 14.451 -13.207 -0.711  0.88 11.82 ?  140 LEU   A C    1 
ATOM   3020 C C    B LEU   A 1 140 ? 14.369 -13.081 -0.564  0.12 11.25 ?  140 LEU   A C    1 
ATOM   3021 O O    A LEU   A 1 140 ? 15.017 -13.926 0.122   0.88 12.40 ?  140 LEU   A O    1 
ATOM   3022 O O    B LEU   A 1 140 ? 14.784 -13.819 0.337   0.12 11.37 ?  140 LEU   A O    1 
ATOM   3023 C CB   A LEU   A 1 140 ? 12.735 -11.526 0.039   0.88 12.61 ?  140 LEU   A CB   1 
ATOM   3024 C CB   B LEU   A 1 140 ? 12.776 -11.293 0.189   0.12 10.42 ?  140 LEU   A CB   1 
ATOM   3025 C CG   A LEU   A 1 140 ? 12.288 -12.393 1.212   0.88 13.02 ?  140 LEU   A CG   1 
ATOM   3026 C CG   B LEU   A 1 140 ? 12.265 -12.100 1.388   0.12 10.10 ?  140 LEU   A CG   1 
ATOM   3027 C CD1  A LEU   A 1 140 ? 13.195 -12.198 2.416   0.88 13.59 ?  140 LEU   A CD1  1 
ATOM   3028 C CD1  B LEU   A 1 140 ? 13.204 -11.967 2.575   0.12 9.84  ?  140 LEU   A CD1  1 
ATOM   3029 C CD2  A LEU   A 1 140 ? 10.829 -12.097 1.579   0.88 14.02 ?  140 LEU   A CD2  1 
ATOM   3030 C CD2  B LEU   A 1 140 ? 10.852 -11.670 1.776   0.12 10.18 ?  140 LEU   A CD2  1 
ATOM   3031 H H    A LEU   A 1 140 ? 13.761 -10.486 -1.893  0.88 14.71 ?  140 LEU   A H    1 
ATOM   3032 H H    B LEU   A 1 140 ? 13.791 -10.375 -1.827  0.12 13.89 ?  140 LEU   A H    1 
ATOM   3033 H HA   A LEU   A 1 140 ? 14.758 -11.463 0.313   0.88 14.44 ?  140 LEU   A HA   1 
ATOM   3034 H HA   B LEU   A 1 140 ? 14.815 -11.320 0.378   0.12 13.23 ?  140 LEU   A HA   1 
ATOM   3035 H HB2  A LEU   A 1 140 ? 12.623 -10.603 0.303   0.88 15.13 ?  140 LEU   A HB2  1 
ATOM   3036 H HB2  B LEU   A 1 140 ? 12.737 -10.359 0.443   0.12 12.49 ?  140 LEU   A HB2  1 
ATOM   3037 H HB3  A LEU   A 1 140 ? 12.147 -11.725 -0.709  0.88 15.13 ?  140 LEU   A HB3  1 
ATOM   3038 H HB3  B LEU   A 1 140 ? 12.159 -11.452 -0.540  0.12 12.49 ?  140 LEU   A HB3  1 
ATOM   3039 H HG   A LEU   A 1 140 ? 12.331 -13.329 0.951   0.88 15.61 ?  140 LEU   A HG   1 
ATOM   3040 H HG   B LEU   A 1 140 ? 12.226 -13.038 1.144   0.12 12.11 ?  140 LEU   A HG   1 
ATOM   3041 H HD11 A LEU   A 1 140 ? 12.806 -12.653 3.179   0.88 16.30 ?  140 LEU   A HD11 1 
ATOM   3042 H HD11 B LEU   A 1 140 ? 12.815 -12.426 3.336   0.12 11.80 ?  140 LEU   A HD11 1 
ATOM   3043 H HD12 A LEU   A 1 140 ? 14.065 -12.578 2.214   0.88 16.30 ?  140 LEU   A HD12 1 
ATOM   3044 H HD12 B LEU   A 1 140 ? 14.056 -12.368 2.346   0.12 11.80 ?  140 LEU   A HD12 1 
ATOM   3045 H HD13 A LEU   A 1 140 ? 13.276 -11.252 2.596   0.88 16.30 ?  140 LEU   A HD13 1 
ATOM   3046 H HD13 B LEU   A 1 140 ? 13.321 -11.027 2.779   0.12 11.80 ?  140 LEU   A HD13 1 
ATOM   3047 H HD21 A LEU   A 1 140 ? 10.568 -12.663 2.326   0.88 16.82 ?  140 LEU   A HD21 1 
ATOM   3048 H HD21 B LEU   A 1 140 ? 10.502 -12.292 2.436   0.12 12.20 ?  140 LEU   A HD21 1 
ATOM   3049 H HD22 A LEU   A 1 140 ? 10.749 -11.164 1.832   0.88 16.82 ?  140 LEU   A HD22 1 
ATOM   3050 H HD22 B LEU   A 1 140 ? 10.883 -10.777 2.151   0.12 12.20 ?  140 LEU   A HD22 1 
ATOM   3051 H HD23 A LEU   A 1 140 ? 10.261 -12.283 0.814   0.88 16.82 ?  140 LEU   A HD23 1 
ATOM   3052 H HD23 B LEU   A 1 140 ? 10.289 -11.680 0.986   0.12 12.20 ?  140 LEU   A HD23 1 
ATOM   3053 N N    A ARG   A 1 141 ? 14.044 -13.675 -1.893  0.88 12.61 ?  141 ARG   A N    1 
ATOM   3054 N N    B ARG   A 1 141 ? 14.057 -13.541 -1.777  0.12 11.46 ?  141 ARG   A N    1 
ATOM   3055 C CA   A ARG   A 1 141 ? 14.287 -15.062 -2.275  0.88 14.07 ?  141 ARG   A CA   1 
ATOM   3056 C CA   B ARG   A 1 141 ? 14.254 -14.947 -2.110  0.12 11.64 ?  141 ARG   A CA   1 
ATOM   3057 C C    A ARG   A 1 141 ? 15.782 -15.369 -2.276  0.88 13.08 ?  141 ARG   A C    1 
ATOM   3058 C C    B ARG   A 1 141 ? 15.736 -15.280 -2.250  0.12 11.67 ?  141 ARG   A C    1 
ATOM   3059 O O    A ARG   A 1 141 ? 16.228 -16.377 -1.710  0.88 13.13 ?  141 ARG   A O    1 
ATOM   3060 O O    B ARG   A 1 141 ? 16.183 -16.345 -1.808  0.12 11.80 ?  141 ARG   A O    1 
ATOM   3061 C CB   A ARG   A 1 141 ? 13.685 -15.298 -3.661  0.88 16.16 ?  141 ARG   A CB   1 
ATOM   3062 C CB   B ARG   A 1 141 ? 13.490 -15.289 -3.391  0.12 11.77 ?  141 ARG   A CB   1 
ATOM   3063 C CG   A ARG   A 1 141 ? 13.660 -16.733 -4.121  0.88 19.21 ?  141 ARG   A CG   1 
ATOM   3064 C CG   B ARG   A 1 141 ? 13.631 -16.739 -3.834  0.12 12.20 ?  141 ARG   A CG   1 
ATOM   3065 C CD   A ARG   A 1 141 ? 12.617 -17.498 -3.367  0.88 20.35 ?  141 ARG   A CD   1 
ATOM   3066 C CD   B ARG   A 1 141 ? 13.124 -17.700 -2.771  0.12 12.23 ?  141 ARG   A CD   1 
ATOM   3067 N NE   A ARG   A 1 141 ? 13.219 -18.274 -2.297  0.88 20.62 ?  141 ARG   A NE   1 
ATOM   3068 N NE   B ARG   A 1 141 ? 11.731 -17.441 -2.426  0.12 12.36 ?  141 ARG   A NE   1 
ATOM   3069 C CZ   A ARG   A 1 141 ? 12.531 -18.842 -1.316  0.88 21.27 ?  141 ARG   A CZ   1 
ATOM   3070 C CZ   B ARG   A 1 141 ? 11.045 -18.117 -1.515  0.12 12.74 ?  141 ARG   A CZ   1 
ATOM   3071 N NH1  A ARG   A 1 141 ? 11.233 -18.629 -1.169  0.88 21.57 ?  141 ARG   A NH1  1 
ATOM   3072 N NH1  B ARG   A 1 141 ? 11.591 -19.114 -0.838  0.12 13.02 ?  141 ARG   A NH1  1 
ATOM   3073 N NH2  A ARG   A 1 141 ? 13.161 -19.640 -0.461  0.88 21.81 ?  141 ARG   A NH2  1 
ATOM   3074 N NH2  B ARG   A 1 141 ? 9.779  -17.784 -1.278  0.12 12.92 ?  141 ARG   A NH2  1 
ATOM   3075 H H    A ARG   A 1 141 ? 13.631 -13.210 -2.488  0.88 15.13 ?  141 ARG   A H    1 
ATOM   3076 H H    B ARG   A 1 141 ? 13.724 -13.063 -2.408  0.12 13.74 ?  141 ARG   A H    1 
ATOM   3077 H HA   A ARG   A 1 141 ? 13.855 -15.653 -1.642  0.88 16.88 ?  141 ARG   A HA   1 
ATOM   3078 H HA   B ARG   A 1 141 ? 13.895 -15.486 -1.393  0.12 13.95 ?  141 ARG   A HA   1 
ATOM   3079 H HB2  A ARG   A 1 141 ? 12.772 -14.970 -3.659  0.88 19.38 ?  141 ARG   A HB2  1 
ATOM   3080 H HB2  B ARG   A 1 141 ? 12.545 -15.113 -3.246  0.12 14.11 ?  141 ARG   A HB2  1 
ATOM   3081 H HB3  A ARG   A 1 141 ? 14.205 -14.797 -4.308  0.88 19.38 ?  141 ARG   A HB3  1 
ATOM   3082 H HB3  B ARG   A 1 141 ? 13.817 -14.726 -4.110  0.12 14.11 ?  141 ARG   A HB3  1 
ATOM   3083 H HG2  A ARG   A 1 141 ? 13.445 -16.769 -5.067  0.88 23.05 ?  141 ARG   A HG2  1 
ATOM   3084 H HG2  B ARG   A 1 141 ? 13.109 -16.875 -4.641  0.12 14.64 ?  141 ARG   A HG2  1 
ATOM   3085 H HG3  A ARG   A 1 141 ? 14.524 -17.147 -3.957  0.88 23.05 ?  141 ARG   A HG3  1 
ATOM   3086 H HG3  B ARG   A 1 141 ? 14.566 -16.934 -4.007  0.12 14.64 ?  141 ARG   A HG3  1 
ATOM   3087 H HD2  A ARG   A 1 141 ? 11.981 -16.881 -2.973  0.88 24.41 ?  141 ARG   A HD2  1 
ATOM   3088 H HD2  B ARG   A 1 141 ? 13.184 -18.603 -3.110  0.12 14.66 ?  141 ARG   A HD2  1 
ATOM   3089 H HD3  A ARG   A 1 141 ? 12.161 -18.105 -3.974  0.88 24.41 ?  141 ARG   A HD3  1 
ATOM   3090 H HD3  B ARG   A 1 141 ? 13.663 -17.606 -1.969  0.12 14.66 ?  141 ARG   A HD3  1 
ATOM   3091 H HE   A ARG   A 1 141 ? 14.054 -18.463 -2.361  0.88 24.74 ?  141 ARG   A HE   1 
ATOM   3092 H HE   B ARG   A 1 141 ? 11.309 -16.848 -2.888  0.12 14.82 ?  141 ARG   A HE   1 
ATOM   3093 H HH11 A ARG   A 1 141 ? 10.811 -18.123 -1.723  0.88 25.88 ?  141 ARG   A HH11 1 
ATOM   3094 H HH11 B ARG   A 1 141 ? 12.409 -19.336 -0.983  0.12 15.62 ?  141 ARG   A HH11 1 
ATOM   3095 H HH12 A ARG   A 1 141 ? 10.806 -19.005 -0.524  0.88 25.88 ?  141 ARG   A HH12 1 
ATOM   3096 H HH12 B ARG   A 1 141 ? 11.127 -19.538 -0.254  0.12 15.62 ?  141 ARG   A HH12 1 
ATOM   3097 H HH21 A ARG   A 1 141 ? 14.006 -19.781 -0.547  0.88 26.16 ?  141 ARG   A HH21 1 
ATOM   3098 H HH21 B ARG   A 1 141 ? 9.417  -17.135 -1.711  0.12 15.49 ?  141 ARG   A HH21 1 
ATOM   3099 H HH22 A ARG   A 1 141 ? 12.729 -20.006 0.186   0.88 26.16 ?  141 ARG   A HH22 1 
ATOM   3100 H HH22 B ARG   A 1 141 ? 9.326  -18.215 -0.690  0.12 15.49 ?  141 ARG   A HH22 1 
ATOM   3101 N N    A VAL   A 1 142 ? 16.578 -14.501 -2.906  0.88 12.38 ?  142 VAL   A N    1 
ATOM   3102 N N    B VAL   A 1 142 ? 16.514 -14.385 -2.865  0.12 11.57 ?  142 VAL   A N    1 
ATOM   3103 C CA   A VAL   A 1 142 ? 18.023 -14.712 -2.928  0.88 12.25 ?  142 VAL   A CA   1 
ATOM   3104 C CA   B VAL   A 1 142 ? 17.957 -14.599 -2.956  0.12 11.52 ?  142 VAL   A CA   1 
ATOM   3105 C C    A VAL   A 1 142 ? 18.586 -14.685 -1.516  0.88 11.53 ?  142 VAL   A C    1 
ATOM   3106 C C    B VAL   A 1 142 ? 18.571 -14.643 -1.562  0.12 11.35 ?  142 VAL   A C    1 
ATOM   3107 O O    A VAL   A 1 142 ? 19.448 -15.501 -1.163  0.88 12.01 ?  142 VAL   A O    1 
ATOM   3108 O O    B VAL   A 1 142 ? 19.449 -15.466 -1.272  0.12 11.33 ?  142 VAL   A O    1 
ATOM   3109 C CB   A VAL   A 1 142 ? 18.724 -13.699 -3.853  0.88 12.43 ?  142 VAL   A CB   1 
ATOM   3110 C CB   B VAL   A 1 142 ? 18.603 -13.511 -3.835  0.12 11.57 ?  142 VAL   A CB   1 
ATOM   3111 C CG1  A VAL   A 1 142 ? 20.234 -13.924 -3.820  0.88 12.15 ?  142 VAL   A CG1  1 
ATOM   3112 C CG1  B VAL   A 1 142 ? 20.114 -13.672 -3.859  0.12 11.60 ?  142 VAL   A CG1  1 
ATOM   3113 C CG2  A VAL   A 1 142 ? 18.215 -13.830 -5.278  0.88 13.64 ?  142 VAL   A CG2  1 
ATOM   3114 C CG2  B VAL   A 1 142 ? 18.045 -13.564 -5.247  0.12 11.70 ?  142 VAL   A CG2  1 
ATOM   3115 H H    A VAL   A 1 142 ? 16.313 -13.792 -3.322  0.88 14.85 ?  142 VAL   A H    1 
ATOM   3116 H H    B VAL   A 1 142 ? 16.234 -13.654 -3.229  0.12 13.87 ?  142 VAL   A H    1 
ATOM   3117 H HA   A VAL   A 1 142 ? 18.196 -15.589 -3.294  0.88 14.69 ?  142 VAL   A HA   1 
ATOM   3118 H HA   B VAL   A 1 142 ? 18.117 -15.453 -3.383  0.12 13.82 ?  142 VAL   A HA   1 
ATOM   3119 H HB   A VAL   A 1 142 ? 18.547 -12.792 -3.544  0.88 14.90 ?  142 VAL   A HB   1 
ATOM   3120 H HB   B VAL   A 1 142 ? 18.399 -12.636 -3.465  0.12 13.88 ?  142 VAL   A HB   1 
ATOM   3121 H HG11 A VAL   A 1 142 ? 20.644 -13.441 -4.554  0.88 14.57 ?  142 VAL   A HG11 1 
ATOM   3122 H HG11 B VAL   A 1 142 ? 20.481 -13.093 -4.546  0.12 13.91 ?  142 VAL   A HG11 1 
ATOM   3123 H HG12 A VAL   A 1 142 ? 20.589 -13.597 -2.975  0.88 14.57 ?  142 VAL   A HG12 1 
ATOM   3124 H HG12 B VAL   A 1 142 ? 20.474 -13.425 -2.994  0.12 13.91 ?  142 VAL   A HG12 1 
ATOM   3125 H HG13 A VAL   A 1 142 ? 20.412 -14.873 -3.908  0.88 14.57 ?  142 VAL   A HG13 1 
ATOM   3126 H HG13 B VAL   A 1 142 ? 20.327 -14.596 -4.058  0.12 13.91 ?  142 VAL   A HG13 1 
ATOM   3127 H HG21 A VAL   A 1 142 ? 18.696 -13.205 -5.845  0.88 16.36 ?  142 VAL   A HG21 1 
ATOM   3128 H HG21 B VAL   A 1 142 ? 18.407 -12.822 -5.757  0.12 14.04 ?  142 VAL   A HG21 1 
ATOM   3129 H HG22 A VAL   A 1 142 ? 18.371 -14.737 -5.581  0.88 16.36 ?  142 VAL   A HG22 1 
ATOM   3130 H HG22 B VAL   A 1 142 ? 18.306 -14.403 -5.654  0.12 14.04 ?  142 VAL   A HG22 1 
ATOM   3131 H HG23 A VAL   A 1 142 ? 17.269 -13.630 -5.293  0.88 16.36 ?  142 VAL   A HG23 1 
ATOM   3132 H HG23 B VAL   A 1 142 ? 17.079 -13.500 -5.211  0.12 14.04 ?  142 VAL   A HG23 1 
ATOM   3133 N N    . CYS   A 1 143 ? 18.116 -13.751 -0.683  1.00 11.44 ?  143 CYS   A N    1 
ATOM   3134 C CA   . CYS   A 1 143 ? 18.584 -13.712 0.698   1.00 11.40 ?  143 CYS   A CA   1 
ATOM   3135 C C    . CYS   A 1 143 ? 18.363 -15.055 1.385   1.00 11.21 ?  143 CYS   A C    1 
ATOM   3136 O O    . CYS   A 1 143 ? 19.285 -15.641 1.959   1.00 11.31 ?  143 CYS   A O    1 
ATOM   3137 C CB   . CYS   A 1 143 ? 17.843 -12.606 1.447   1.00 12.13 ?  143 CYS   A CB   1 
ATOM   3138 S SG   . CYS   A 1 143 ? 18.338 -12.419 3.166   1.00 12.31 ?  143 CYS   A SG   1 
ATOM   3139 H H    A CYS   A 1 143 ? 17.541 -13.149 -0.890  0.88 13.72 ?  143 CYS   A H    1 
ATOM   3140 H H    B CYS   A 1 143 ? 17.530 -13.152 -0.868  0.12 13.72 ?  143 CYS   A H    1 
ATOM   3141 H HA   . CYS   A 1 143 ? 19.533 -13.518 0.713   1.00 13.67 ?  143 CYS   A HA   1 
ATOM   3142 H HB2  . CYS   A 1 143 ? 18.004 -11.764 0.996   1.00 14.54 ?  143 CYS   A HB2  1 
ATOM   3143 H HB3  . CYS   A 1 143 ? 16.896 -12.806 1.433   1.00 14.54 ?  143 CYS   A HB3  1 
ATOM   3144 H HG   . CYS   A 1 143 ? 17.757 -11.481 3.636   1.00 14.76 ?  143 CYS   A HG   1 
ATOM   3145 N N    . VAL   A 1 144 ? 17.132 -15.558 1.333   1.00 11.88 ?  144 VAL   A N    1 
ATOM   3146 C CA   . VAL   A 1 144 ? 16.797 -16.791 2.035   1.00 13.24 ?  144 VAL   A CA   1 
ATOM   3147 C C    . VAL   A 1 144 ? 17.609 -17.963 1.502   1.00 12.80 ?  144 VAL   A C    1 
ATOM   3148 O O    . VAL   A 1 144 ? 17.982 -18.873 2.255   1.00 13.38 ?  144 VAL   A O    1 
ATOM   3149 C CB   . VAL   A 1 144 ? 15.282 -17.037 1.918   1.00 15.99 ?  144 VAL   A CB   1 
ATOM   3150 C CG1  . VAL   A 1 144 ? 14.930 -18.470 2.258   1.00 17.72 ?  144 VAL   A CG1  1 
ATOM   3151 C CG2  . VAL   A 1 144 ? 14.532 -16.043 2.801   1.00 15.90 ?  144 VAL   A CG2  1 
ATOM   3152 H H    . VAL   A 1 144 ? 16.472 -15.199 0.901   1.00 14.25 ?  144 VAL   A H    1 
ATOM   3153 H HA   . VAL   A 1 144 ? 17.001 -16.680 2.973   1.00 15.87 ?  144 VAL   A HA   1 
ATOM   3154 H HB   . VAL   A 1 144 ? 15.004 -16.873 1.000   1.00 19.18 ?  144 VAL   A HB   1 
ATOM   3155 H HG11 . VAL   A 1 144 ? 13.976 -18.524 2.448   1.00 21.25 ?  144 VAL   A HG11 1 
ATOM   3156 H HG12 . VAL   A 1 144 ? 15.143 -19.039 1.503   1.00 21.25 ?  144 VAL   A HG12 1 
ATOM   3157 H HG13 . VAL   A 1 144 ? 15.434 -18.742 3.038   1.00 21.25 ?  144 VAL   A HG13 1 
ATOM   3158 H HG21 . VAL   A 1 144 ? 13.580 -16.098 2.609   1.00 19.07 ?  144 VAL   A HG21 1 
ATOM   3159 H HG22 . VAL   A 1 144 ? 14.692 -16.257 3.732   1.00 19.07 ?  144 VAL   A HG22 1 
ATOM   3160 H HG23 . VAL   A 1 144 ? 14.847 -15.142 2.609   1.00 19.07 ?  144 VAL   A HG23 1 
ATOM   3161 N N    . ASP   A 1 145 ? 17.878 -17.975 0.199   1.00 12.97 ?  145 ASP   A N    1 
ATOM   3162 C CA   . ASP   A 1 145 ? 18.584 -19.083 -0.434  1.00 13.56 ?  145 ASP   A CA   1 
ATOM   3163 C C    . ASP   A 1 145 ? 20.103 -18.938 -0.395  1.00 13.09 ?  145 ASP   A C    1 
ATOM   3164 O O    . ASP   A 1 145 ? 20.807 -19.829 -0.882  1.00 15.34 ?  145 ASP   A O    1 
ATOM   3165 C CB   . ASP   A 1 145 ? 18.134 -19.225 -1.889  1.00 15.22 ?  145 ASP   A CB   1 
ATOM   3166 C CG   . ASP   A 1 145 ? 16.687 -19.656 -2.015  1.00 17.41 ?  145 ASP   A CG   1 
ATOM   3167 O OD1  . ASP   A 1 145 ? 16.122 -20.197 -1.039  1.00 18.04 ?  145 ASP   A OD1  1 
ATOM   3168 O OD2  . ASP   A 1 145 ? 16.110 -19.452 -3.101  1.00 18.63 -1 145 ASP   A OD2  1 
ATOM   3169 H H    . ASP   A 1 145 ? 17.639 -17.352 -0.349  1.00 15.55 ?  145 ASP   A H    1 
ATOM   3170 H HA   . ASP   A 1 145 ? 18.349 -19.902 0.027   1.00 16.27 ?  145 ASP   A HA   1 
ATOM   3171 H HB2  . ASP   A 1 145 ? 18.239 -18.371 -2.338  1.00 18.26 ?  145 ASP   A HB2  1 
ATOM   3172 H HB3  . ASP   A 1 145 ? 18.681 -19.897 -2.322  1.00 18.26 ?  145 ASP   A HB3  1 
ATOM   3173 N N    . THR   A 1 146 ? 20.625 -17.843 0.156   1.00 11.74 ?  146 THR   A N    1 
ATOM   3174 C CA   . THR   A 1 146 ? 22.065 -17.587 0.172   1.00 11.16 ?  146 THR   A CA   1 
ATOM   3175 C C    . THR   A 1 146 ? 22.624 -17.406 1.572   1.00 11.11 ?  146 THR   A C    1 
ATOM   3176 O O    . THR   A 1 146 ? 23.705 -17.931 1.881   1.00 12.16 ?  146 THR   A O    1 
ATOM   3177 C CB   . THR   A 1 146 ? 22.387 -16.333 -0.664  1.00 11.10 ?  146 THR   A CB   1 
ATOM   3178 O OG1  . THR   A 1 146 ? 21.858 -16.492 -1.979  1.00 11.83 ?  146 THR   A OG1  1 
ATOM   3179 C CG2  . THR   A 1 146 ? 23.892 -16.100 -0.757  1.00 11.71 ?  146 THR   A CG2  1 
ATOM   3180 H H    . THR   A 1 146 ? 20.157 -17.218 0.526   1.00 14.08 ?  146 THR   A H    1 
ATOM   3181 H HA   . THR   A 1 146 ? 22.522 -18.337 -0.229  1.00 13.38 ?  146 THR   A HA   1 
ATOM   3182 H HB   . THR   A 1 146 ? 21.991 -15.554 -0.247  1.00 13.31 ?  146 THR   A HB   1 
ATOM   3183 H HG1  . THR   A 1 146 ? 21.022 -16.564 -1.943  1.00 14.19 ?  146 THR   A HG1  1 
ATOM   3184 H HG21 . THR   A 1 146 ? 24.080 -15.430 -1.431  1.00 14.05 ?  146 THR   A HG21 1 
ATOM   3185 H HG22 . THR   A 1 146 ? 24.235 -15.794 0.097   1.00 14.05 ?  146 THR   A HG22 1 
ATOM   3186 H HG23 . THR   A 1 146 ? 24.339 -16.926 -1.000  1.00 14.05 ?  146 THR   A HG23 1 
ATOM   3187 N N    . VAL   A 1 147 ? 21.948 -16.626 2.407   1.00 10.98 ?  147 VAL   A N    1 
ATOM   3188 C CA   . VAL   A 1 147 ? 22.438 -16.330 3.744   1.00 11.12 ?  147 VAL   A CA   1 
ATOM   3189 C C    . VAL   A 1 147 ? 22.121 -17.504 4.658   1.00 11.39 ?  147 VAL   A C    1 
ATOM   3190 O O    . VAL   A 1 147 ? 20.978 -17.980 4.711   1.00 11.85 ?  147 VAL   A O    1 
ATOM   3191 C CB   . VAL   A 1 147 ? 21.818 -15.024 4.268   1.00 11.20 ?  147 VAL   A CB   1 
ATOM   3192 C CG1  . VAL   A 1 147 ? 22.361 -14.717 5.643   1.00 12.28 ?  147 VAL   A CG1  1 
ATOM   3193 C CG2  . VAL   A 1 147 ? 22.074 -13.876 3.300   1.00 11.67 ?  147 VAL   A CG2  1 
ATOM   3194 H H    . VAL   A 1 147 ? 21.186 -16.262 2.228   1.00 13.17 ?  147 VAL   A H    1 
ATOM   3195 H HA   . VAL   A 1 147 ? 23.400 -16.216 3.712   1.00 13.33 ?  147 VAL   A HA   1 
ATOM   3196 H HB   . VAL   A 1 147 ? 20.860 -15.140 4.349   1.00 13.44 ?  147 VAL   A HB   1 
ATOM   3197 H HG11 . VAL   A 1 147 ? 22.123 -13.811 5.883   1.00 14.73 ?  147 VAL   A HG11 1 
ATOM   3198 H HG12 . VAL   A 1 147 ? 21.974 -15.341 6.283   1.00 14.73 ?  147 VAL   A HG12 1 
ATOM   3199 H HG13 . VAL   A 1 147 ? 23.326 -14.816 5.632   1.00 14.73 ?  147 VAL   A HG13 1 
ATOM   3200 H HG21 . VAL   A 1 147 ? 21.746 -13.052 3.697   1.00 13.99 ?  147 VAL   A HG21 1 
ATOM   3201 H HG22 . VAL   A 1 147 ? 23.026 -13.807 3.137   1.00 13.99 ?  147 VAL   A HG22 1 
ATOM   3202 H HG23 . VAL   A 1 147 ? 21.605 -14.053 2.471   1.00 13.99 ?  147 VAL   A HG23 1 
ATOM   3203 N N    . ARG   A 1 148 ? 23.147 -17.975 5.368   1.00 11.56 ?  148 ARG   A N    1 
ATOM   3204 C CA   . ARG   A 1 148 ? 23.019 -19.054 6.334   1.00 11.77 ?  148 ARG   A CA   1 
ATOM   3205 C C    . ARG   A 1 148 ? 23.155 -18.582 7.768   1.00 12.08 ?  148 ARG   A C    1 
ATOM   3206 O O    . ARG   A 1 148 ? 22.750 -19.306 8.688   1.00 13.52 ?  148 ARG   A O    1 
ATOM   3207 C CB   . ARG   A 1 148 ? 24.057 -20.151 6.052   1.00 12.39 ?  148 ARG   A CB   1 
ATOM   3208 C CG   . ARG   A 1 148 ? 23.881 -20.790 4.689   1.00 13.49 ?  148 ARG   A CG   1 
ATOM   3209 C CD   . ARG   A 1 148 ? 24.965 -21.821 4.382   1.00 14.46 ?  148 ARG   A CD   1 
ATOM   3210 N NE   . ARG   A 1 148 ? 26.301 -21.237 4.400   1.00 14.31 ?  148 ARG   A NE   1 
ATOM   3211 C CZ   . ARG   A 1 148 ? 26.807 -20.497 3.424   1.00 13.67 ?  148 ARG   A CZ   1 
ATOM   3212 N NH1  . ARG   A 1 148 ? 26.126 -20.254 2.317   1.00 14.27 ?  148 ARG   A NH1  1 
ATOM   3213 N NH2  . ARG   A 1 148 ? 28.023 -19.974 3.568   1.00 14.07 ?  148 ARG   A NH2  1 
ATOM   3214 H H    . ARG   A 1 148 ? 23.956 -17.673 5.295   1.00 13.86 ?  148 ARG   A H    1 
ATOM   3215 H HA   . ARG   A 1 148 ? 22.144 -19.448 6.238   1.00 14.11 ?  148 ARG   A HA   1 
ATOM   3216 H HB2  . ARG   A 1 148 ? 24.946 -19.776 6.094   1.00 14.86 ?  148 ARG   A HB2  1 
ATOM   3217 H HB3  . ARG   A 1 148 ? 23.960 -20.854 6.720   1.00 14.86 ?  148 ARG   A HB3  1 
ATOM   3218 H HG2  . ARG   A 1 148 ? 23.017 -21.232 4.657   1.00 16.18 ?  148 ARG   A HG2  1 
ATOM   3219 H HG3  . ARG   A 1 148 ? 23.921 -20.094 4.013   1.00 16.18 ?  148 ARG   A HG3  1 
ATOM   3220 H HD2  . ARG   A 1 148 ? 24.933 -22.523 5.050   1.00 17.34 ?  148 ARG   A HD2  1 
ATOM   3221 H HD3  . ARG   A 1 148 ? 24.806 -22.195 3.500   1.00 17.34 ?  148 ARG   A HD3  1 
ATOM   3222 H HE   . ARG   A 1 148 ? 26.792 -21.385 5.086   1.00 17.16 ?  148 ARG   A HE   1 
ATOM   3223 H HH11 . ARG   A 1 148 ? 25.338 -20.578 2.212   1.00 17.12 ?  148 ARG   A HH11 1 
ATOM   3224 H HH12 . ARG   A 1 148 ? 26.474 -19.765 1.698   1.00 17.12 ?  148 ARG   A HH12 1 
ATOM   3225 H HH21 . ARG   A 1 148 ? 28.470 -20.122 4.285   1.00 16.88 ?  148 ARG   A HH21 1 
ATOM   3226 H HH22 . ARG   A 1 148 ? 28.359 -19.488 2.942   1.00 16.88 ?  148 ARG   A HH22 1 
ATOM   3227 N N    . THR   A 1 149 ? 23.704 -17.391 7.976   1.00 11.82 ?  149 THR   A N    1 
ATOM   3228 C CA   . THR   A 1 149 ? 23.785 -16.798 9.294   1.00 11.94 ?  149 THR   A CA   1 
ATOM   3229 C C    . THR   A 1 149 ? 22.460 -16.102 9.611   1.00 11.67 ?  149 THR   A C    1 
ATOM   3230 O O    . THR   A 1 149 ? 21.511 -16.104 8.813   1.00 12.40 ?  149 THR   A O    1 
ATOM   3231 C CB   . THR   A 1 149 ? 24.986 -15.860 9.348   1.00 12.65 ?  149 THR   A CB   1 
ATOM   3232 O OG1  . THR   A 1 149 ? 24.847 -14.920 8.282   1.00 12.58 ?  149 THR   A OG1  1 
ATOM   3233 C CG2  . THR   A 1 149 ? 26.296 -16.648 9.197   1.00 13.12 ?  149 THR   A CG2  1 
ATOM   3234 H H    . THR   A 1 149 ? 24.051 -16.901 7.355   1.00 14.18 ?  149 THR   A H    1 
ATOM   3235 H HA   . THR   A 1 149 ? 23.917 -17.499 9.948   1.00 14.32 ?  149 THR   A HA   1 
ATOM   3236 H HB   . THR   A 1 149 ? 24.994 -15.397 10.196  1.00 15.17 ?  149 THR   A HB   1 
ATOM   3237 H HG1  . THR   A 1 149 ? 25.497 -14.386 8.282   1.00 15.08 ?  149 THR   A HG1  1 
ATOM   3238 H HG21 . THR   A 1 149 ? 27.054 -16.047 9.254   1.00 15.74 ?  149 THR   A HG21 1 
ATOM   3239 H HG22 . THR   A 1 149 ? 26.369 -17.316 9.899   1.00 15.74 ?  149 THR   A HG22 1 
ATOM   3240 H HG23 . THR   A 1 149 ? 26.320 -17.100 8.335   1.00 15.74 ?  149 THR   A HG23 1 
ATOM   3241 N N    . ASN   A 1 150 ? 22.350 -15.560 10.816  1.00 11.94 ?  150 ASN   A N    1 
ATOM   3242 C CA   . ASN   A 1 150 ? 21.071 -15.054 11.313  1.00 12.62 ?  150 ASN   A CA   1 
ATOM   3243 C C    . ASN   A 1 150 ? 20.880 -13.613 10.862  1.00 11.93 ?  150 ASN   A C    1 
ATOM   3244 O O    . ASN   A 1 150 ? 21.618 -12.717 11.289  1.00 13.54 ?  150 ASN   A O    1 
ATOM   3245 C CB   . ASN   A 1 150 ? 21.025 -15.176 12.830  1.00 15.17 ?  150 ASN   A CB   1 
ATOM   3246 C CG   . ASN   A 1 150 ? 20.892 -16.610 13.283  1.00 19.23 ?  150 ASN   A CG   1 
ATOM   3247 O OD1  . ASN   A 1 150 ? 20.281 -17.427 12.597  1.00 20.70 ?  150 ASN   A OD1  1 
ATOM   3248 N ND2  . ASN   A 1 150 ? 21.482 -16.932 14.427  1.00 21.51 ?  150 ASN   A ND2  1 
ATOM   3249 H H    . ASN   A 1 150 ? 23.005 -15.467 11.368  1.00 14.32 ?  150 ASN   A H    1 
ATOM   3250 H HA   . ASN   A 1 150 ? 20.351 -15.588 10.944  1.00 15.14 ?  150 ASN   A HA   1 
ATOM   3251 H HB2  . ASN   A 1 150 ? 21.846 -14.818 13.206  1.00 18.20 ?  150 ASN   A HB2  1 
ATOM   3252 H HB3  . ASN   A 1 150 ? 20.261 -14.685 13.169  1.00 18.20 ?  150 ASN   A HB3  1 
ATOM   3253 H HD21 . ASN   A 1 150 ? 21.437 -17.741 14.724  1.00 25.80 ?  150 ASN   A HD21 1 
ATOM   3254 H HD22 . ASN   A 1 150 ? 21.904 -16.336 14.880  1.00 25.80 ?  150 ASN   A HD22 1 
ATOM   3255 N N    . VAL   A 1 151 ? 19.893 -13.382 10.002  1.00 11.65 ?  151 VAL   A N    1 
ATOM   3256 C CA   . VAL   A 1 151 ? 19.675 -12.069 9.412   1.00 11.54 ?  151 VAL   A CA   1 
ATOM   3257 C C    . VAL   A 1 151 ? 18.288 -11.561 9.781   1.00 11.50 ?  151 VAL   A C    1 
ATOM   3258 O O    . VAL   A 1 151 ? 17.282 -12.274 9.639   1.00 12.64 ?  151 VAL   A O    1 
ATOM   3259 C CB   . VAL   A 1 151 ? 19.961 -12.051 7.894   1.00 12.82 ?  151 VAL   A CB   1 
ATOM   3260 C CG1  . VAL   A 1 151 ? 19.134 -13.070 7.138   1.00 13.80 ?  151 VAL   A CG1  1 
ATOM   3261 C CG2  . VAL   A 1 151 ? 19.766 -10.647 7.323   1.00 13.31 ?  151 VAL   A CG2  1 
ATOM   3262 H H    . VAL   A 1 151 ? 19.337 -13.981 9.738   1.00 13.97 ?  151 VAL   A H    1 
ATOM   3263 H HA   . VAL   A 1 151 ? 20.314 -11.457 9.806   1.00 13.83 ?  151 VAL   A HA   1 
ATOM   3264 H HB   . VAL   A 1 151 ? 20.895 -12.287 7.752   1.00 15.38 ?  151 VAL   A HB   1 
ATOM   3265 H HG11 . VAL   A 1 151 ? 19.333 -13.011 6.189   1.00 16.55 ?  151 VAL   A HG11 1 
ATOM   3266 H HG12 . VAL   A 1 151 ? 19.354 -13.962 7.461   1.00 16.55 ?  151 VAL   A HG12 1 
ATOM   3267 H HG13 . VAL   A 1 151 ? 18.192 -12.892 7.289   1.00 16.55 ?  151 VAL   A HG13 1 
ATOM   3268 H HG21 . VAL   A 1 151 ? 20.083 -10.632 6.404   1.00 15.96 ?  151 VAL   A HG21 1 
ATOM   3269 H HG22 . VAL   A 1 151 ? 18.825 -10.421 7.350   1.00 15.96 ?  151 VAL   A HG22 1 
ATOM   3270 H HG23 . VAL   A 1 151 ? 20.277 -10.018 7.855   1.00 15.96 ?  151 VAL   A HG23 1 
ATOM   3271 N N    . TYR   A 1 152 ? 18.270 -10.318 10.269  1.00 11.50 ?  152 TYR   A N    1 
ATOM   3272 C CA   . TYR   A 1 152 ? 17.080 -9.585  10.665  1.00 11.42 ?  152 TYR   A CA   1 
ATOM   3273 C C    . TYR   A 1 152 ? 16.882 -8.478  9.641   1.00 11.16 ?  152 TYR   A C    1 
ATOM   3274 O O    . TYR   A 1 152 ? 17.655 -7.514  9.597   1.00 11.54 ?  152 TYR   A O    1 
ATOM   3275 C CB   . TYR   A 1 152 ? 17.275 -9.044  12.080  1.00 12.01 ?  152 TYR   A CB   1 
ATOM   3276 C CG   . TYR   A 1 152 ? 17.238 -10.174 13.076  1.00 12.65 ?  152 TYR   A CG   1 
ATOM   3277 C CD1  . TYR   A 1 152 ? 18.373 -10.926 13.352  1.00 14.21 ?  152 TYR   A CD1  1 
ATOM   3278 C CD2  . TYR   A 1 152 ? 16.054 -10.538 13.697  1.00 12.97 ?  152 TYR   A CD2  1 
ATOM   3279 C CE1  . TYR   A 1 152 ? 18.340 -11.993 14.231  1.00 15.27 ?  152 TYR   A CE1  1 
ATOM   3280 C CE2  . TYR   A 1 152 ? 16.009 -11.610 14.581  1.00 14.17 ?  152 TYR   A CE2  1 
ATOM   3281 C CZ   . TYR   A 1 152 ? 17.156 -12.332 14.841  1.00 15.10 ?  152 TYR   A CZ   1 
ATOM   3282 O OH   . TYR   A 1 152 ? 17.122 -13.402 15.714  1.00 17.19 ?  152 TYR   A OH   1 
ATOM   3283 H H    . TYR   A 1 152 ? 18.989 -9.846  10.366  1.00 13.79 ?  152 TYR   A H    1 
ATOM   3284 H HA   . TYR   A 1 152 ? 16.310 -10.174 10.652  1.00 13.69 ?  152 TYR   A HA   1 
ATOM   3285 H HB2  . TYR   A 1 152 ? 18.139 -8.620  12.142  1.00 14.40 ?  152 TYR   A HB2  1 
ATOM   3286 H HB3  . TYR   A 1 152 ? 16.575 -8.415  12.294  1.00 14.40 ?  152 TYR   A HB3  1 
ATOM   3287 H HD1  . TYR   A 1 152 ? 19.173 -10.702 12.932  1.00 17.04 ?  152 TYR   A HD1  1 
ATOM   3288 H HD2  . TYR   A 1 152 ? 15.273 -10.063 13.519  1.00 15.56 ?  152 TYR   A HD2  1 
ATOM   3289 H HE1  . TYR   A 1 152 ? 19.115 -12.474 14.409  1.00 18.32 ?  152 TYR   A HE1  1 
ATOM   3290 H HE2  . TYR   A 1 152 ? 15.207 -11.836 14.998  1.00 16.99 ?  152 TYR   A HE2  1 
ATOM   3291 H HH   . TYR   A 1 152 ? 16.343 -13.486 16.025  1.00 20.61 ?  152 TYR   A HH   1 
ATOM   3292 N N    A LEU   A 1 153 ? 15.876 -8.651  8.785   0.88 11.47 ?  153 LEU   A N    1 
ATOM   3293 N N    B LEU   A 1 153 ? 15.840 -8.603  8.831   0.12 10.94 ?  153 LEU   A N    1 
ATOM   3294 C CA   A LEU   A 1 153 ? 15.611 -7.747  7.674   0.88 11.57 ?  153 LEU   A CA   1 
ATOM   3295 C CA   B LEU   A 1 153 ? 15.558 -7.608  7.812   0.12 10.79 ?  153 LEU   A CA   1 
ATOM   3296 C C    A LEU   A 1 153 ? 14.606 -6.679  8.078   0.88 12.28 ?  153 LEU   A C    1 
ATOM   3297 C C    B LEU   A 1 153 ? 14.609 -6.545  8.346   0.12 10.74 ?  153 LEU   A C    1 
ATOM   3298 O O    A LEU   A 1 153 ? 13.509 -6.994  8.556   0.88 13.04 ?  153 LEU   A O    1 
ATOM   3299 O O    B LEU   A 1 153 ? 13.615 -6.854  9.010   0.12 10.58 ?  153 LEU   A O    1 
ATOM   3300 C CB   A LEU   A 1 153 ? 15.040 -8.529  6.492   0.88 11.81 ?  153 LEU   A CB   1 
ATOM   3301 C CB   B LEU   A 1 153 ? 14.958 -8.272  6.576   0.12 10.93 ?  153 LEU   A CB   1 
ATOM   3302 C CG   A LEU   A 1 153 ? 15.970 -9.535  5.819   0.88 11.81 ?  153 LEU   A CG   1 
ATOM   3303 C CG   B LEU   A 1 153 ? 15.887 -9.299  5.929   0.12 10.88 ?  153 LEU   A CG   1 
ATOM   3304 C CD1  A LEU   A 1 153 ? 15.172 -10.428 4.884   0.88 12.09 ?  153 LEU   A CD1  1 
ATOM   3305 C CD1  B LEU   A 1 153 ? 15.182 -10.006 4.791   0.12 11.01 ?  153 LEU   A CD1  1 
ATOM   3306 C CD2  A LEU   A 1 153 ? 17.072 -8.815  5.056   0.88 12.16 ?  153 LEU   A CD2  1 
ATOM   3307 C CD2  B LEU   A 1 153 ? 17.177 -8.641  5.445   0.12 10.95 ?  153 LEU   A CD2  1 
ATOM   3308 H H    A LEU   A 1 153 ? 15.314 -9.306  8.835   0.88 13.76 ?  153 LEU   A H    1 
ATOM   3309 H H    B LEU   A 1 153 ? 15.284 -9.262  8.849   0.12 13.12 ?  153 LEU   A H    1 
ATOM   3310 H HA   A LEU   A 1 153 ? 16.437 -7.320  7.405   0.88 13.88 ?  153 LEU   A HA   1 
ATOM   3311 H HA   B LEU   A 1 153 ? 16.386 -7.178  7.562   0.12 12.94 ?  153 LEU   A HA   1 
ATOM   3312 H HB2  A LEU   A 1 153 ? 14.262 -9.014  6.798   0.88 14.16 ?  153 LEU   A HB2  1 
ATOM   3313 H HB2  B LEU   A 1 153 ? 14.140 -8.725  6.833   0.12 13.11 ?  153 LEU   A HB2  1 
ATOM   3314 H HB3  A LEU   A 1 153 ? 14.772 -7.887  5.813   0.88 14.16 ?  153 LEU   A HB3  1 
ATOM   3315 H HB3  B LEU   A 1 153 ? 14.764 -7.584  5.921   0.12 13.11 ?  153 LEU   A HB3  1 
ATOM   3316 H HG   A LEU   A 1 153 ? 16.387 -10.089 6.500   0.88 14.16 ?  153 LEU   A HG   1 
ATOM   3317 H HG   B LEU   A 1 153 ? 16.126 -9.964  6.593   0.12 13.04 ?  153 LEU   A HG   1 
ATOM   3318 H HD11 A LEU   A 1 153 ? 15.755 -11.126 4.543   0.88 14.50 ?  153 LEU   A HD11 1 
ATOM   3319 H HD11 B LEU   A 1 153 ? 15.776 -10.678 4.425   0.12 13.20 ?  153 LEU   A HD11 1 
ATOM   3320 H HD12 A LEU   A 1 153 ? 14.439 -10.823 5.378   0.88 14.50 ?  153 LEU   A HD12 1 
ATOM   3321 H HD12 B LEU   A 1 153 ? 14.377 -10.424 5.134   0.12 13.20 ?  153 LEU   A HD12 1 
ATOM   3322 H HD13 A LEU   A 1 153 ? 14.832 -9.892  4.153   0.88 14.50 ?  153 LEU   A HD13 1 
ATOM   3323 H HD13 B LEU   A 1 153 ? 14.955 -9.355  4.110   0.12 13.20 ?  153 LEU   A HD13 1 
ATOM   3324 H HD21 A LEU   A 1 153 ? 17.652 -9.476  4.649   0.88 14.58 ?  153 LEU   A HD21 1 
ATOM   3325 H HD21 B LEU   A 1 153 ? 17.658 -9.269  4.884   0.12 13.13 ?  153 LEU   A HD21 1 
ATOM   3326 H HD22 A LEU   A 1 153 ? 16.666 -8.262  4.372   0.88 14.58 ?  153 LEU   A HD22 1 
ATOM   3327 H HD22 B LEU   A 1 153 ? 16.955 -7.845  4.938   0.12 13.13 ?  153 LEU   A HD22 1 
ATOM   3328 H HD23 A LEU   A 1 153 ? 17.577 -8.266  5.673   0.88 14.58 ?  153 LEU   A HD23 1 
ATOM   3329 H HD23 B LEU   A 1 153 ? 17.721 -8.402  6.214   0.12 13.13 ?  153 LEU   A HD23 1 
ATOM   3330 N N    A ALA   A 1 154 ? 14.974 -5.420  7.851   0.88 12.23 ?  154 ALA   A N    1 
ATOM   3331 N N    B ALA   A 1 154 ? 14.930 -5.288  8.052   0.12 10.87 ?  154 ALA   A N    1 
ATOM   3332 C CA   A ALA   A 1 154 ? 14.106 -4.274  8.079   0.88 12.95 ?  154 ALA   A CA   1 
ATOM   3333 C CA   B ALA   A 1 154 ? 14.121 -4.142  8.442   0.12 11.38 ?  154 ALA   A CA   1 
ATOM   3334 C C    A ALA   A 1 154 ? 13.608 -3.764  6.734   0.88 12.83 ?  154 ALA   A C    1 
ATOM   3335 C C    B ALA   A 1 154 ? 13.619 -3.468  7.174   0.12 11.65 ?  154 ALA   A C    1 
ATOM   3336 O O    A ALA   A 1 154 ? 14.410 -3.415  5.860   0.88 13.24 ?  154 ALA   A O    1 
ATOM   3337 O O    B ALA   A 1 154 ? 14.419 -2.975  6.372   0.12 11.51 ?  154 ALA   A O    1 
ATOM   3338 C CB   A ALA   A 1 154 ? 14.864 -3.161  8.802   0.88 13.48 ?  154 ALA   A CB   1 
ATOM   3339 C CB   B ALA   A 1 154 ? 14.939 -3.157  9.281   0.12 11.32 ?  154 ALA   A CB   1 
ATOM   3340 H H    A ALA   A 1 154 ? 15.750 -5.201  7.549   0.88 14.66 ?  154 ALA   A H    1 
ATOM   3341 H H    B ALA   A 1 154 ? 15.634 -5.070  7.607   0.12 13.03 ?  154 ALA   A H    1 
ATOM   3342 H HA   A ALA   A 1 154 ? 13.346 -4.533  8.622   0.88 15.53 ?  154 ALA   A HA   1 
ATOM   3343 H HA   B ALA   A 1 154 ? 13.360 -4.436  8.966   0.12 13.65 ?  154 ALA   A HA   1 
ATOM   3344 H HB1  A ALA   A 1 154 ? 14.269 -2.406  8.942   0.88 16.16 ?  154 ALA   A HB1  1 
ATOM   3345 H HB1  B ALA   A 1 154 ? 14.376 -2.405  9.525   0.12 13.58 ?  154 ALA   A HB1  1 
ATOM   3346 H HB2  A ALA   A 1 154 ? 15.186 -3.490  9.654   0.88 16.16 ?  154 ALA   A HB2  1 
ATOM   3347 H HB2  B ALA   A 1 154 ? 15.255 -3.607  10.081  0.12 13.58 ?  154 ALA   A HB2  1 
ATOM   3348 H HB3  A ALA   A 1 154 ? 15.619 -2.881  8.252   0.88 16.16 ?  154 ALA   A HB3  1 
ATOM   3349 H HB3  B ALA   A 1 154 ? 15.695 -2.847  8.757   0.12 13.58 ?  154 ALA   A HB3  1 
ATOM   3350 N N    A VAL   A 1 155 ? 12.288 -3.707  6.581   0.88 13.70 ?  155 VAL   A N    1 
ATOM   3351 N N    B VAL   A 1 155 ? 12.301 -3.453  6.993   0.12 12.09 ?  155 VAL   A N    1 
ATOM   3352 C CA   A VAL   A 1 155 ? 11.634 -3.223  5.372   0.88 14.80 ?  155 VAL   A CA   1 
ATOM   3353 C CA   B VAL   A 1 155 ? 11.663 -2.852  5.828   0.12 12.54 ?  155 VAL   A CA   1 
ATOM   3354 C C    A VAL   A 1 155 ? 10.885 -1.949  5.734   0.88 16.40 ?  155 VAL   A C    1 
ATOM   3355 C C    B VAL   A 1 155 ? 10.621 -1.868  6.337   0.12 13.47 ?  155 VAL   A C    1 
ATOM   3356 O O    A VAL   A 1 155 ? 9.940  -1.988  6.530   0.88 16.78 ?  155 VAL   A O    1 
ATOM   3357 O O    B VAL   A 1 155 ? 9.672  -2.266  7.022   0.12 13.48 ?  155 VAL   A O    1 
ATOM   3358 C CB   A VAL   A 1 155 ? 10.687 -4.281  4.787   0.88 14.63 ?  155 VAL   A CB   1 
ATOM   3359 C CB   B VAL   A 1 155 ? 11.009 -3.907  4.919   0.12 12.14 ?  155 VAL   A CB   1 
ATOM   3360 C CG1  A VAL   A 1 155 ? 9.953  -3.728  3.576   0.88 15.55 ?  155 VAL   A CG1  1 
ATOM   3361 C CG1  B VAL   A 1 155 ? 10.395 -3.243  3.697   0.12 12.09 ?  155 VAL   A CG1  1 
ATOM   3362 C CG2  A VAL   A 1 155 ? 11.466 -5.537  4.413   0.88 15.40 ?  155 VAL   A CG2  1 
ATOM   3363 C CG2  B VAL   A 1 155 ? 12.025 -4.965  4.507   0.12 11.86 ?  155 VAL   A CG2  1 
ATOM   3364 H H    A VAL   A 1 155 ? 11.733 -3.968  7.187   0.88 16.44 ?  155 VAL   A H    1 
ATOM   3365 H H    B VAL   A 1 155 ? 11.741 -3.789  7.553   0.12 14.50 ?  155 VAL   A H    1 
ATOM   3366 H HA   A VAL   A 1 155 ? 12.304 -3.009  4.707   0.88 17.75 ?  155 VAL   A HA   1 
ATOM   3367 H HA   B VAL   A 1 155 ? 12.321 -2.363  5.310   0.12 15.04 ?  155 VAL   A HA   1 
ATOM   3368 H HB   A VAL   A 1 155 ? 10.026 -4.524  5.460   0.88 17.54 ?  155 VAL   A HB   1 
ATOM   3369 H HB   B VAL   A 1 155 ? 10.300 -4.349  5.409   0.12 14.56 ?  155 VAL   A HB   1 
ATOM   3370 H HG11 A VAL   A 1 155 ? 9.511  -4.457  3.113   0.88 18.65 ?  155 VAL   A HG11 1 
ATOM   3371 H HG11 B VAL   A 1 155 ? 10.171 -3.930  3.053   0.12 14.49 ?  155 VAL   A HG11 1 
ATOM   3372 H HG12 A VAL   A 1 155 ? 9.290  -3.080  3.871   0.88 18.65 ?  155 VAL   A HG12 1 
ATOM   3373 H HG12 B VAL   A 1 155 ? 9.596  -2.762  3.963   0.12 14.49 ?  155 VAL   A HG12 1 
ATOM   3374 H HG13 A VAL   A 1 155 ? 10.592 -3.301  2.986   0.88 18.65 ?  155 VAL   A HG13 1 
ATOM   3375 H HG13 B VAL   A 1 155 ? 11.041 -2.628  3.313   0.12 14.49 ?  155 VAL   A HG13 1 
ATOM   3376 H HG21 A VAL   A 1 155 ? 10.861 -6.174  4.003   0.88 18.46 ?  155 VAL   A HG21 1 
ATOM   3377 H HG21 B VAL   A 1 155 ? 11.601 -5.586  3.894   0.12 14.22 ?  155 VAL   A HG21 1 
ATOM   3378 H HG22 A VAL   A 1 155 ? 12.167 -5.296  3.786   0.88 18.46 ?  155 VAL   A HG22 1 
ATOM   3379 H HG22 B VAL   A 1 155 ? 12.775 -4.530  4.072   0.12 14.22 ?  155 VAL   A HG22 1 
ATOM   3380 H HG23 A VAL   A 1 155 ? 11.857 -5.919  5.214   0.88 18.46 ?  155 VAL   A HG23 1 
ATOM   3381 H HG23 B VAL   A 1 155 ? 12.329 -5.437  5.298   0.12 14.22 ?  155 VAL   A HG23 1 
ATOM   3382 N N    A PHE   A 1 156 ? 11.301 -0.822  5.143   0.88 18.20 ?  156 PHE   A N    1 
ATOM   3383 N N    B PHE   A 1 156 ? 10.792 -0.588  6.002   0.12 14.45 ?  156 PHE   A N    1 
ATOM   3384 C CA   A PHE   A 1 156 ? 10.746 0.481   5.513   0.88 20.09 ?  156 PHE   A CA   1 
ATOM   3385 C CA   B PHE   A 1 156 ? 9.911  0.436   6.556   0.12 15.37 ?  156 PHE   A CA   1 
ATOM   3386 C C    A PHE   A 1 156 ? 9.277  0.615   5.123   0.88 20.47 ?  156 PHE   A C    1 
ATOM   3387 C C    B PHE   A 1 156 ? 8.569  0.489   5.834   0.12 16.21 ?  156 PHE   A C    1 
ATOM   3388 O O    A PHE   A 1 156 ? 8.467  1.146   5.896   0.88 21.82 ?  156 PHE   A O    1 
ATOM   3389 O O    B PHE   A 1 156 ? 7.520  0.602   6.479   0.12 16.19 ?  156 PHE   A O    1 
ATOM   3390 C CB   A PHE   A 1 156 ? 11.572 1.584   4.849   0.88 21.51 ?  156 PHE   A CB   1 
ATOM   3391 C CB   B PHE   A 1 156 ? 10.594 1.802   6.506   0.12 15.57 ?  156 PHE   A CB   1 
ATOM   3392 C CG   A PHE   A 1 156 ? 11.095 2.974   5.163   0.88 23.32 ?  156 PHE   A CG   1 
ATOM   3393 C CG   B PHE   A 1 156 ? 9.748  2.916   7.050   0.12 15.73 ?  156 PHE   A CG   1 
ATOM   3394 C CD1  A PHE   A 1 156 ? 11.063 3.418   6.474   0.88 24.40 ?  156 PHE   A CD1  1 
ATOM   3395 C CD1  B PHE   A 1 156 ? 9.717  3.177   8.409   0.12 15.84 ?  156 PHE   A CD1  1 
ATOM   3396 C CD2  A PHE   A 1 156 ? 10.690 3.835   4.154   0.88 24.21 ?  156 PHE   A CD2  1 
ATOM   3397 C CD2  B PHE   A 1 156 ? 8.980  3.698   6.203   0.12 15.81 ?  156 PHE   A CD2  1 
ATOM   3398 C CE1  A PHE   A 1 156 ? 10.629 4.693   6.777   0.88 25.39 ?  156 PHE   A CE1  1 
ATOM   3399 C CE1  B PHE   A 1 156 ? 8.937  4.199   8.915   0.12 15.83 ?  156 PHE   A CE1  1 
ATOM   3400 C CE2  A PHE   A 1 156 ? 10.254 5.117   4.449   0.88 25.32 ?  156 PHE   A CE2  1 
ATOM   3401 C CE2  B PHE   A 1 156 ? 8.195  4.720   6.703   0.12 15.93 ?  156 PHE   A CE2  1 
ATOM   3402 C CZ   A PHE   A 1 156 ? 10.228 5.547   5.764   0.88 25.69 ?  156 PHE   A CZ   1 
ATOM   3403 C CZ   B PHE   A 1 156 ? 8.177  4.973   8.059   0.12 15.86 ?  156 PHE   A CZ   1 
ATOM   3404 H H    A PHE   A 1 156 ? 11.909 -0.789  4.535   0.88 21.83 ?  156 PHE   A H    1 
ATOM   3405 H H    B PHE   A 1 156 ? 11.401 -0.292  5.470   0.12 17.33 ?  156 PHE   A H    1 
ATOM   3406 H HA   A PHE   A 1 156 ? 10.820 0.593   6.473   0.88 24.10 ?  156 PHE   A HA   1 
ATOM   3407 H HA   B PHE   A 1 156 ? 9.740  0.227   7.484   0.12 18.43 ?  156 PHE   A HA   1 
ATOM   3408 H HB2  A PHE   A 1 156 ? 12.493 1.512   5.148   0.88 25.81 ?  156 PHE   A HB2  1 
ATOM   3409 H HB2  B PHE   A 1 156 ? 11.409 1.764   7.032   0.12 18.67 ?  156 PHE   A HB2  1 
ATOM   3410 H HB3  A PHE   A 1 156 ? 11.531 1.468   3.886   0.88 25.81 ?  156 PHE   A HB3  1 
ATOM   3411 H HB3  B PHE   A 1 156 ? 10.808 2.015   5.584   0.12 18.67 ?  156 PHE   A HB3  1 
ATOM   3412 H HD1  A PHE   A 1 156 ? 11.335 2.846   7.159   0.88 29.27 ?  156 PHE   A HD1  1 
ATOM   3413 H HD1  B PHE   A 1 156 ? 10.228 2.659   8.988   0.12 19.00 ?  156 PHE   A HD1  1 
ATOM   3414 H HD2  A PHE   A 1 156 ? 10.707 3.545   3.269   0.88 29.04 ?  156 PHE   A HD2  1 
ATOM   3415 H HD2  B PHE   A 1 156 ? 8.992  3.534   5.288   0.12 18.97 ?  156 PHE   A HD2  1 
ATOM   3416 H HE1  A PHE   A 1 156 ? 10.611 4.979   7.662   0.88 30.46 ?  156 PHE   A HE1  1 
ATOM   3417 H HE1  B PHE   A 1 156 ? 8.924  4.367   9.830   0.12 18.98 ?  156 PHE   A HE1  1 
ATOM   3418 H HE2  A PHE   A 1 156 ? 9.981  5.683   3.767   0.88 30.38 ?  156 PHE   A HE2  1 
ATOM   3419 H HE2  B PHE   A 1 156 ? 7.687  5.243   6.124   0.12 19.11 ?  156 PHE   A HE2  1 
ATOM   3420 H HZ   A PHE   A 1 156 ? 9.932  6.404   5.968   0.88 30.82 ?  156 PHE   A HZ   1 
ATOM   3421 H HZ   B PHE   A 1 156 ? 7.651  5.662   8.397   0.12 19.02 ?  156 PHE   A HZ   1 
ATOM   3422 N N    A ASP   A 1 157 ? 8.921  0.162   3.928   0.88 20.44 ?  157 ASP   A N    1 
ATOM   3423 N N    B ASP   A 1 157 ? 8.583  0.424   4.506   0.12 17.01 ?  157 ASP   A N    1 
ATOM   3424 C CA   A ASP   A 1 157 ? 7.598  0.400   3.367   0.88 21.38 ?  157 ASP   A CA   1 
ATOM   3425 C CA   B ASP   A 1 157 ? 7.354  0.534   3.731   0.12 17.88 ?  157 ASP   A CA   1 
ATOM   3426 C C    A ASP   A 1 157 ? 6.617  -0.660  3.863   0.88 21.18 ?  157 ASP   A C    1 
ATOM   3427 C C    B ASP   A 1 157 ? 6.370  -0.559  4.133   0.12 18.63 ?  157 ASP   A C    1 
ATOM   3428 O O    A ASP   A 1 157 ? 6.802  -1.853  3.597   0.88 20.30 ?  157 ASP   A O    1 
ATOM   3429 O O    B ASP   A 1 157 ? 6.719  -1.742  4.186   0.12 18.60 ?  157 ASP   A O    1 
ATOM   3430 C CB   A ASP   A 1 157 ? 7.682  0.364   1.846   0.88 23.00 ?  157 ASP   A CB   1 
ATOM   3431 C CB   B ASP   A 1 157 ? 7.691  0.428   2.245   0.12 17.90 ?  157 ASP   A CB   1 
ATOM   3432 C CG   A ASP   A 1 157 ? 6.413  0.860   1.192   0.88 24.82 ?  157 ASP   A CG   1 
ATOM   3433 C CG   B ASP   A 1 157 ? 6.509  0.730   1.348   0.12 17.86 ?  157 ASP   A CG   1 
ATOM   3434 O OD1  A ASP   A 1 157 ? 6.160  2.080   1.234   0.88 26.66 ?  157 ASP   A OD1  1 
ATOM   3435 O OD1  B ASP   A 1 157 ? 5.389  0.267   1.648   0.12 17.58 ?  157 ASP   A OD1  1 
ATOM   3436 O OD2  A ASP   A 1 157 ? 5.648  0.030   0.660   0.88 24.79 -1 157 ASP   A OD2  1 
ATOM   3437 O OD2  B ASP   A 1 157 ? 6.704  1.441   0.338   0.12 17.92 -1 157 ASP   A OD2  1 
ATOM   3438 H H    A ASP   A 1 157 ? 9.442  -0.291  3.415   0.88 24.51 ?  157 ASP   A H    1 
ATOM   3439 H H    B ASP   A 1 157 ? 9.289  0.321   4.031   0.12 20.40 ?  157 ASP   A H    1 
ATOM   3440 H HA   A ASP   A 1 157 ? 7.279  1.272   3.642   0.88 25.65 ?  157 ASP   A HA   1 
ATOM   3441 H HA   B ASP   A 1 157 ? 6.939  1.396   3.888   0.12 21.44 ?  157 ASP   A HA   1 
ATOM   3442 H HB2  A ASP   A 1 157 ? 8.441  0.907   1.562   0.88 27.59 ?  157 ASP   A HB2  1 
ATOM   3443 H HB2  B ASP   A 1 157 ? 8.374  1.071   2.034   0.12 21.47 ?  157 ASP   A HB2  1 
ATOM   3444 H HB3  A ASP   A 1 157 ? 7.819  -0.553  1.558   0.88 27.59 ?  157 ASP   A HB3  1 
ATOM   3445 H HB3  B ASP   A 1 157 ? 8.023  -0.458  2.059   0.12 21.47 ?  157 ASP   A HB3  1 
ATOM   3446 N N    A LYS   A 1 158 ? 5.570  -0.223  4.576   0.88 22.38 ?  158 LYS   A N    1 
ATOM   3447 N N    B LYS   A 1 158 ? 5.130  -0.151  4.415   0.12 19.35 ?  158 LYS   A N    1 
ATOM   3448 C CA   A LYS   A 1 158 ? 4.606  -1.165  5.144   0.88 23.24 ?  158 LYS   A CA   1 
ATOM   3449 C CA   B LYS   A 1 158 ? 4.104  -1.103  4.828   0.12 20.06 ?  158 LYS   A CA   1 
ATOM   3450 C C    A LYS   A 1 158 ? 3.887  -1.947  4.050   0.88 22.80 ?  158 LYS   A C    1 
ATOM   3451 C C    B LYS   A 1 158 ? 3.660  -1.975  3.658   0.12 20.30 ?  158 LYS   A C    1 
ATOM   3452 O O    A LYS   A 1 158 ? 3.705  -3.166  4.161   0.88 22.63 ?  158 LYS   A O    1 
ATOM   3453 O O    B LYS   A 1 158 ? 3.661  -3.208  3.752   0.12 20.23 ?  158 LYS   A O    1 
ATOM   3454 C CB   A LYS   A 1 158 ? 3.608  -0.418  6.037   0.88 24.63 ?  158 LYS   A CB   1 
ATOM   3455 C CB   B LYS   A 1 158 ? 2.916  -0.345  5.426   0.12 20.56 ?  158 LYS   A CB   1 
ATOM   3456 C CG   A LYS   A 1 158 ? 2.406  -1.249  6.505   0.88 26.23 ?  158 LYS   A CG   1 
ATOM   3457 C CG   B LYS   A 1 158 ? 1.679  -1.193  5.676   0.12 21.06 ?  158 LYS   A CG   1 
ATOM   3458 C CD   A LYS   A 1 158 ? 2.810  -2.481  7.318   0.88 27.51 ?  158 LYS   A CD   1 
ATOM   3459 C CD   B LYS   A 1 158 ? 1.956  -2.316  6.657   0.12 21.43 ?  158 LYS   A CD   1 
ATOM   3460 C CE   A LYS   A 1 158 ? 1.575  -3.215  7.839   0.88 28.49 ?  158 LYS   A CE   1 
ATOM   3461 C CE   B LYS   A 1 158 ? 0.670  -3.017  7.054   0.12 21.69 ?  158 LYS   A CE   1 
ATOM   3462 N NZ   A LYS   A 1 158 ? 1.894  -4.542  8.439   0.88 29.03 ?  158 LYS   A NZ   1 
ATOM   3463 N NZ   B LYS   A 1 158 ? 0.919  -4.257  7.837   0.12 21.88 ?  158 LYS   A NZ   1 
ATOM   3464 H H    A LYS   A 1 158 ? 5.408  0.602   4.747   0.88 26.84 ?  158 LYS   A H    1 
ATOM   3465 H H    B LYS   A 1 158 ? 4.862  0.664   4.375   0.12 23.21 ?  158 LYS   A H    1 
ATOM   3466 H HA   A LYS   A 1 158 ? 5.081  -1.798  5.709   0.88 27.88 ?  158 LYS   A HA   1 
ATOM   3467 H HA   B LYS   A 1 158 ? 4.465  -1.682  5.517   0.12 24.06 ?  158 LYS   A HA   1 
ATOM   3468 H HB2  A LYS   A 1 158 ? 4.071  -0.106  6.833   0.88 29.55 ?  158 LYS   A HB2  1 
ATOM   3469 H HB2  B LYS   A 1 158 ? 3.185  0.034   6.279   0.12 24.67 ?  158 LYS   A HB2  1 
ATOM   3470 H HB3  A LYS   A 1 158 ? 3.263  0.345   5.546   0.88 29.55 ?  158 LYS   A HB3  1 
ATOM   3471 H HB3  B LYS   A 1 158 ? 2.664  0.369   4.820   0.12 24.67 ?  158 LYS   A HB3  1 
ATOM   3472 H HG2  A LYS   A 1 158 ? 1.844  -0.693  7.067   0.88 31.47 ?  158 LYS   A HG2  1 
ATOM   3473 H HG2  B LYS   A 1 158 ? 0.984  -0.632  6.052   0.12 25.26 ?  158 LYS   A HG2  1 
ATOM   3474 H HG3  A LYS   A 1 158 ? 1.901  -1.546  5.732   0.88 31.47 ?  158 LYS   A HG3  1 
ATOM   3475 H HG3  B LYS   A 1 158 ? 1.372  -1.582  4.841   0.12 25.26 ?  158 LYS   A HG3  1 
ATOM   3476 H HD2  A LYS   A 1 158 ? 3.314  -3.087  6.754   0.88 33.00 ?  158 LYS   A HD2  1 
ATOM   3477 H HD2  B LYS   A 1 158 ? 2.546  -2.967  6.245   0.12 25.70 ?  158 LYS   A HD2  1 
ATOM   3478 H HD3  A LYS   A 1 158 ? 3.346  -2.200  8.077   0.88 33.00 ?  158 LYS   A HD3  1 
ATOM   3479 H HD3  B LYS   A 1 158 ? 2.364  -1.950  7.458   0.12 25.70 ?  158 LYS   A HD3  1 
ATOM   3480 H HE2  A LYS   A 1 158 ? 1.149  -2.671  8.520   0.88 34.18 ?  158 LYS   A HE2  1 
ATOM   3481 H HE2  B LYS   A 1 158 ? 0.147  -2.416  7.604   0.12 26.02 ?  158 LYS   A HE2  1 
ATOM   3482 H HE3  A LYS   A 1 158 ? 0.962  -3.358  7.102   0.88 34.18 ?  158 LYS   A HE3  1 
ATOM   3483 H HE3  B LYS   A 1 158 ? 0.171  -3.249  6.257   0.12 26.02 ?  158 LYS   A HE3  1 
ATOM   3484 H HZ1  A LYS   A 1 158 ? 1.148  -4.933  8.728   0.88 34.83 ?  158 LYS   A HZ1  1 
ATOM   3485 H HZ1  B LYS   A 1 158 ? 0.145  -4.640  8.051   0.12 26.25 ?  158 LYS   A HZ1  1 
ATOM   3486 H HZ2  A LYS   A 1 158 ? 2.277  -5.067  7.830   0.88 34.83 ?  158 LYS   A HZ2  1 
ATOM   3487 H HZ2  B LYS   A 1 158 ? 1.402  -4.830  7.355   0.12 26.25 ?  158 LYS   A HZ2  1 
ATOM   3488 H HZ3  A LYS   A 1 158 ? 2.452  -4.441  9.125   0.88 34.83 ?  158 LYS   A HZ3  1 
ATOM   3489 H HZ3  B LYS   A 1 158 ? 1.362  -4.061  8.583   0.12 26.25 ?  158 LYS   A HZ3  1 
ATOM   3490 N N    A ASN   A 1 159 ? 3.471  -1.265  2.984   0.88 23.48 ?  159 ASN   A N    1 
ATOM   3491 N N    B ASN   A 1 159 ? 3.270  -1.347  2.546   0.12 20.69 ?  159 ASN   A N    1 
ATOM   3492 C CA   A ASN   A 1 159 ? 2.817  -1.969  1.888   0.88 23.98 ?  159 ASN   A CA   1 
ATOM   3493 C CA   B ASN   A 1 159 ? 2.829  -2.108  1.382   0.12 21.06 ?  159 ASN   A CA   1 
ATOM   3494 C C    A ASN   A 1 159 ? 3.730  -3.045  1.299   0.88 22.41 ?  159 ASN   A C    1 
ATOM   3495 C C    B ASN   A 1 159 ? 3.926  -3.042  0.893   0.12 20.35 ?  159 ASN   A C    1 
ATOM   3496 O O    A ASN   A 1 159 ? 3.290  -4.172  1.039   0.88 22.15 ?  159 ASN   A O    1 
ATOM   3497 O O    B ASN   A 1 159 ? 3.656  -4.188  0.515   0.12 20.41 ?  159 ASN   A O    1 
ATOM   3498 C CB   A ASN   A 1 159 ? 2.351  -0.962  0.836   0.88 26.29 ?  159 ASN   A CB   1 
ATOM   3499 C CB   B ASN   A 1 159 ? 2.406  -1.151  0.269   0.12 22.08 ?  159 ASN   A CB   1 
ATOM   3500 C CG   A ASN   A 1 159 ? 1.160  -0.144  1.309   0.88 28.88 ?  159 ASN   A CG   1 
ATOM   3501 C CG   B ASN   A 1 159 ? 1.316  -0.195  0.707   0.12 22.94 ?  159 ASN   A CG   1 
ATOM   3502 O OD1  A ASN   A 1 159 ? 0.288  -0.658  2.008   0.88 29.81 ?  159 ASN   A OD1  1 
ATOM   3503 O OD1  B ASN   A 1 159 ? 0.314  -0.603  1.293   0.12 23.25 ?  159 ASN   A OD1  1 
ATOM   3504 N ND2  A ASN   A 1 159 ? 1.118  1.132   0.932   0.88 30.08 ?  159 ASN   A ND2  1 
ATOM   3505 N ND2  B ASN   A 1 159 ? 1.512  1.089   0.433   0.12 23.28 ?  159 ASN   A ND2  1 
ATOM   3506 H H    A ASN   A 1 159 ? 3.565  -0.419  2.878   0.88 28.16 ?  159 ASN   A H    1 
ATOM   3507 H H    B ASN   A 1 159 ? 3.257  -0.496  2.444   0.12 24.82 ?  159 ASN   A H    1 
ATOM   3508 H HA   A ASN   A 1 159 ? 2.030  -2.411  2.240   0.88 28.76 ?  159 ASN   A HA   1 
ATOM   3509 H HA   B ASN   A 1 159 ? 2.062  -2.649  1.624   0.12 25.26 ?  159 ASN   A HA   1 
ATOM   3510 H HB2  A ASN   A 1 159 ? 3.072  -0.347  0.638   0.88 31.54 ?  159 ASN   A HB2  1 
ATOM   3511 H HB2  B ASN   A 1 159 ? 3.174  -0.627  -0.006  0.12 26.48 ?  159 ASN   A HB2  1 
ATOM   3512 H HB3  A ASN   A 1 159 ? 2.085  -1.439  0.037   0.88 31.54 ?  159 ASN   A HB3  1 
ATOM   3513 H HB3  B ASN   A 1 159 ? 2.070  -1.667  -0.481  0.12 26.48 ?  159 ASN   A HB3  1 
ATOM   3514 H HD21 A ASN   A 1 159 ? 0.465  1.636   1.177   0.88 36.09 ?  159 ASN   A HD21 1 
ATOM   3515 H HD21 B ASN   A 1 159 ? 0.923  1.671   0.664   0.12 27.92 ?  159 ASN   A HD21 1 
ATOM   3516 H HD22 A ASN   A 1 159 ? 1.752  1.457   0.449   0.88 36.09 ?  159 ASN   A HD22 1 
ATOM   3517 H HD22 B ASN   A 1 159 ? 2.226  1.337   0.024   0.12 27.92 ?  159 ASN   A HD22 1 
ATOM   3518 N N    A LEU   A 1 160 ? 5.013  -2.732  1.117   0.88 20.90 ?  160 LEU   A N    1 
ATOM   3519 N N    B LEU   A 1 160 ? 5.173  -2.567  0.887   0.12 19.54 ?  160 LEU   A N    1 
ATOM   3520 C CA   A LEU   A 1 160 ? 5.941  -3.723  0.579   0.88 19.89 ?  160 LEU   A CA   1 
ATOM   3521 C CA   B LEU   A 1 160 ? 6.290  -3.429  0.517   0.12 18.71 ?  160 LEU   A CA   1 
ATOM   3522 C C    A LEU   A 1 160 ? 6.152  -4.871  1.555   0.88 19.08 ?  160 LEU   A C    1 
ATOM   3523 C C    B LEU   A 1 160 ? 6.449  -4.571  1.516   0.12 18.16 ?  160 LEU   A C    1 
ATOM   3524 O O    A LEU   A 1 160 ? 6.198  -6.040  1.150   0.88 19.71 ?  160 LEU   A O    1 
ATOM   3525 O O    B LEU   A 1 160 ? 6.502  -5.744  1.131   0.12 18.19 ?  160 LEU   A O    1 
ATOM   3526 C CB   A LEU   A 1 160 ? 7.276  -3.064  0.243   0.88 19.56 ?  160 LEU   A CB   1 
ATOM   3527 C CB   B LEU   A 1 160 ? 7.570  -2.601  0.420   0.12 18.49 ?  160 LEU   A CB   1 
ATOM   3528 C CG   A LEU   A 1 160 ? 8.363  -4.045  -0.187  0.88 19.75 ?  160 LEU   A CG   1 
ATOM   3529 C CG   B LEU   A 1 160 ? 8.902  -3.343  0.314   0.12 18.33 ?  160 LEU   A CG   1 
ATOM   3530 C CD1  A LEU   A 1 160 ? 7.908  -4.800  -1.416  0.88 20.41 ?  160 LEU   A CD1  1 
ATOM   3531 C CD1  B LEU   A 1 160 ? 8.844  -4.434  -0.730  0.12 18.28 ?  160 LEU   A CD1  1 
ATOM   3532 C CD2  A LEU   A 1 160 ? 9.677  -3.333  -0.443  0.88 19.62 ?  160 LEU   A CD2  1 
ATOM   3533 C CD2  B LEU   A 1 160 ? 10.025 -2.368  -0.002  0.12 18.29 ?  160 LEU   A CD2  1 
ATOM   3534 H H    A LEU   A 1 160 ? 5.363  -1.968  1.306   0.88 25.07 ?  160 LEU   A H    1 
ATOM   3535 H H    B LEU   A 1 160 ? 5.392  -1.759  1.089   0.12 23.44 ?  160 LEU   A H    1 
ATOM   3536 H HA   A LEU   A 1 160 ? 5.564  -4.084  -0.234  0.88 23.86 ?  160 LEU   A HA   1 
ATOM   3537 H HA   B LEU   A 1 160 ? 6.120  -3.810  -0.354  0.12 22.44 ?  160 LEU   A HA   1 
ATOM   3538 H HB2  A LEU   A 1 160 ? 7.136  -2.428  -0.481  0.88 23.46 ?  160 LEU   A HB2  1 
ATOM   3539 H HB2  B LEU   A 1 160 ? 7.502  -1.995  -0.341  0.12 22.18 ?  160 LEU   A HB2  1 
ATOM   3540 H HB3  A LEU   A 1 160 ? 7.594  -2.599  1.030   0.88 23.46 ?  160 LEU   A HB3  1 
ATOM   3541 H HB3  B LEU   A 1 160 ? 7.618  -2.092  1.232   0.12 22.18 ?  160 LEU   A HB3  1 
ATOM   3542 H HG   A LEU   A 1 160 ? 8.511  -4.688  0.522   0.88 23.69 ?  160 LEU   A HG   1 
ATOM   3543 H HG   B LEU   A 1 160 ? 9.105  -3.750  1.173   0.12 21.99 ?  160 LEU   A HG   1 
ATOM   3544 H HD11 A LEU   A 1 160 ? 8.645  -5.334  -1.741  0.88 24.49 ?  160 LEU   A HD11 1 
ATOM   3545 H HD11 B LEU   A 1 160 ? 9.694  -4.896  -0.736  0.12 21.92 ?  160 LEU   A HD11 1 
ATOM   3546 H HD12 A LEU   A 1 160 ? 7.162  -5.374  -1.181  0.88 24.49 ?  160 LEU   A HD12 1 
ATOM   3547 H HD12 B LEU   A 1 160 ? 8.136  -5.053  -0.506  0.12 21.92 ?  160 LEU   A HD12 1 
ATOM   3548 H HD13 A LEU   A 1 160 ? 7.634  -4.161  -2.094  0.88 24.49 ?  160 LEU   A HD13 1 
ATOM   3549 H HD13 B LEU   A 1 160 ? 8.676  -4.030  -1.594  0.12 21.92 ?  160 LEU   A HD13 1 
ATOM   3550 H HD21 A LEU   A 1 160 ? 10.340 -3.987  -0.711  0.88 23.53 ?  160 LEU   A HD21 1 
ATOM   3551 H HD21 B LEU   A 1 160 ? 10.572 -2.723  -0.721  0.12 21.94 ?  160 LEU   A HD21 1 
ATOM   3552 H HD22 A LEU   A 1 160 ? 9.550  -2.681  -1.150  0.88 23.53 ?  160 LEU   A HD22 1 
ATOM   3553 H HD22 B LEU   A 1 160 ? 9.654  -1.507  -0.259  0.12 21.94 ?  160 LEU   A HD22 1 
ATOM   3554 H HD23 A LEU   A 1 160 ? 9.958  -2.888  0.371   0.88 23.53 ?  160 LEU   A HD23 1 
ATOM   3555 H HD23 B LEU   A 1 160 ? 10.558 -2.267  0.798   0.12 21.94 ?  160 LEU   A HD23 1 
ATOM   3556 N N    A TYR   A 1 161 ? 6.295  -4.556  2.842   0.88 18.30 ?  161 TYR   A N    1 
ATOM   3557 N N    B TYR   A 1 161 ? 6.524  -4.245  2.809   0.12 17.62 ?  161 TYR   A N    1 
ATOM   3558 C CA   A TYR   A 1 161 ? 6.436  -5.601  3.848   0.88 17.84 ?  161 TYR   A CA   1 
ATOM   3559 C CA   B TYR   A 1 161 ? 6.615  -5.289  3.826   0.12 17.24 ?  161 TYR   A CA   1 
ATOM   3560 C C    A TYR   A 1 161 ? 5.293  -6.607  3.759   0.88 18.39 ?  161 TYR   A C    1 
ATOM   3561 C C    B TYR   A 1 161 ? 5.437  -6.250  3.729   0.12 17.58 ?  161 TYR   A C    1 
ATOM   3562 O O    A TYR   A 1 161 ? 5.515  -7.822  3.742   0.88 18.30 ?  161 TYR   A O    1 
ATOM   3563 O O    B TYR   A 1 161 ? 5.600  -7.464  3.899   0.12 17.49 ?  161 TYR   A O    1 
ATOM   3564 C CB   A TYR   A 1 161 ? 6.500  -4.975  5.242   0.88 17.97 ?  161 TYR   A CB   1 
ATOM   3565 C CB   B TYR   A 1 161 ? 6.687  -4.658  5.216   0.12 16.66 ?  161 TYR   A CB   1 
ATOM   3566 C CG   A TYR   A 1 161 ? 6.411  -5.994  6.341   0.88 17.50 ?  161 TYR   A CG   1 
ATOM   3567 C CG   B TYR   A 1 161 ? 6.504  -5.634  6.358   0.12 16.13 ?  161 TYR   A CG   1 
ATOM   3568 C CD1  A TYR   A 1 161 ? 7.539  -6.677  6.769   0.88 17.32 ?  161 TYR   A CD1  1 
ATOM   3569 C CD1  B TYR   A 1 161 ? 7.594  -6.281  6.929   0.12 16.03 ?  161 TYR   A CD1  1 
ATOM   3570 C CD2  A TYR   A 1 161 ? 5.196  -6.292  6.943   0.88 17.70 ?  161 TYR   A CD2  1 
ATOM   3571 C CD2  B TYR   A 1 161 ? 5.242  -5.895  6.879   0.12 15.87 ?  161 TYR   A CD2  1 
ATOM   3572 C CE1  A TYR   A 1 161 ? 7.462  -7.630  7.764   0.88 17.49 ?  161 TYR   A CE1  1 
ATOM   3573 C CE1  B TYR   A 1 161 ? 7.429  -7.166  7.979   0.12 16.00 ?  161 TYR   A CE1  1 
ATOM   3574 C CE2  A TYR   A 1 161 ? 5.109  -7.240  7.941   0.88 17.43 ?  161 TYR   A CE2  1 
ATOM   3575 C CE2  B TYR   A 1 161 ? 5.069  -6.777  7.928   0.12 15.83 ?  161 TYR   A CE2  1 
ATOM   3576 C CZ   A TYR   A 1 161 ? 6.245  -7.908  8.345   0.88 17.69 ?  161 TYR   A CZ   1 
ATOM   3577 C CZ   B TYR   A 1 161 ? 6.165  -7.409  8.474   0.12 16.02 ?  161 TYR   A CZ   1 
ATOM   3578 O OH   A TYR   A 1 161 ? 6.174  -8.859  9.339   0.88 18.56 ?  161 TYR   A OH   1 
ATOM   3579 O OH   B TYR   A 1 161 ? 5.991  -8.289  9.517   0.12 16.34 ?  161 TYR   A OH   1 
ATOM   3580 H H    A TYR   A 1 161 ? 6.295  -3.759  3.157   0.88 21.95 ?  161 TYR   A H    1 
ATOM   3581 H H    B TYR   A 1 161 ? 6.524  -3.442  3.118   0.12 21.13 ?  161 TYR   A H    1 
ATOM   3582 H HA   A TYR   A 1 161 ? 7.259  -6.080  3.697   0.88 21.40 ?  161 TYR   A HA   1 
ATOM   3583 H HA   B TYR   A 1 161 ? 7.430  -5.795  3.686   0.12 20.68 ?  161 TYR   A HA   1 
ATOM   3584 H HB2  A TYR   A 1 161 ? 7.342  -4.509  5.338   0.88 21.55 ?  161 TYR   A HB2  1 
ATOM   3585 H HB2  B TYR   A 1 161 ? 7.556  -4.241  5.325   0.12 19.99 ?  161 TYR   A HB2  1 
ATOM   3586 H HB3  A TYR   A 1 161 ? 5.760  -4.357  5.350   0.88 21.55 ?  161 TYR   A HB3  1 
ATOM   3587 H HB3  B TYR   A 1 161 ? 5.991  -3.988  5.292   0.12 19.99 ?  161 TYR   A HB3  1 
ATOM   3588 H HD1  A TYR   A 1 161 ? 8.358  -6.498  6.377   0.88 20.78 ?  161 TYR   A HD1  1 
ATOM   3589 H HD1  B TYR   A 1 161 ? 8.448  -6.117  6.600   0.12 19.22 ?  161 TYR   A HD1  1 
ATOM   3590 H HD2  A TYR   A 1 161 ? 4.422  -5.854  6.673   0.88 21.23 ?  161 TYR   A HD2  1 
ATOM   3591 H HD2  B TYR   A 1 161 ? 4.500  -5.469  6.517   0.12 19.03 ?  161 TYR   A HD2  1 
ATOM   3592 H HE1  A TYR   A 1 161 ? 8.227  -8.083  8.044   0.88 20.98 ?  161 TYR   A HE1  1 
ATOM   3593 H HE1  B TYR   A 1 161 ? 8.168  -7.594  8.350   0.12 19.19 ?  161 TYR   A HE1  1 
ATOM   3594 H HE2  A TYR   A 1 161 ? 4.282  -7.438  8.341   0.88 20.91 ?  161 TYR   A HE2  1 
ATOM   3595 H HE2  B TYR   A 1 161 ? 4.218  -6.944  8.264   0.12 18.99 ?  161 TYR   A HE2  1 
ATOM   3596 H HH   A TYR   A 1 161 ? 6.926  -9.191  9.494   0.88 22.26 ?  161 TYR   A HH   1 
ATOM   3597 H HH   B TYR   A 1 161 ? 6.732  -8.604  9.755   0.12 19.60 ?  161 TYR   A HH   1 
ATOM   3598 N N    A ASP   A 1 162 ? 4.056  -6.113  3.702   0.88 19.10 ?  162 ASP   A N    1 
ATOM   3599 N N    B ASP   A 1 162 ? 4.241  -5.725  3.459   0.12 18.03 ?  162 ASP   A N    1 
ATOM   3600 C CA   A ASP   A 1 162 ? 2.906  -7.014  3.644   0.88 19.82 ?  162 ASP   A CA   1 
ATOM   3601 C CA   B ASP   A 1 162 ? 3.076  -6.588  3.286   0.12 18.57 ?  162 ASP   A CA   1 
ATOM   3602 C C    A ASP   A 1 162 ? 2.944  -7.875  2.386   0.88 20.00 ?  162 ASP   A C    1 
ATOM   3603 C C    B ASP   A 1 162 ? 3.259  -7.519  2.094   0.12 19.13 ?  162 ASP   A C    1 
ATOM   3604 O O    A ASP   A 1 162 ? 2.591  -9.061  2.422   0.88 20.53 ?  162 ASP   A O    1 
ATOM   3605 O O    B ASP   A 1 162 ? 3.000  -8.725  2.188   0.12 19.27 ?  162 ASP   A O    1 
ATOM   3606 C CB   A ASP   A 1 162 ? 1.602  -6.211  3.711   0.88 20.52 ?  162 ASP   A CB   1 
ATOM   3607 C CB   B ASP   A 1 162 ? 1.815  -5.742  3.114   0.12 18.64 ?  162 ASP   A CB   1 
ATOM   3608 C CG   A ASP   A 1 162 ? 1.315  -5.655  5.093   0.88 21.86 ?  162 ASP   A CG   1 
ATOM   3609 C CG   B ASP   A 1 162 ? 1.316  -5.155  4.418   0.12 18.63 ?  162 ASP   A CG   1 
ATOM   3610 O OD1  A ASP   A 1 162 ? 1.966  -6.071  6.068   0.88 22.64 ?  162 ASP   A OD1  1 
ATOM   3611 O OD1  B ASP   A 1 162 ? 1.820  -5.548  5.491   0.12 18.67 ?  162 ASP   A OD1  1 
ATOM   3612 O OD2  A ASP   A 1 162 ? 0.408  -4.801  5.202   0.88 23.05 -1 162 ASP   A OD2  1 
ATOM   3613 O OD2  B ASP   A 1 162 ? 0.412  -4.297  4.363   0.12 18.61 -1 162 ASP   A OD2  1 
ATOM   3614 H H    A ASP   A 1 162 ? 3.854  -5.283  3.705   0.88 22.91 ?  162 ASP   A H    1 
ATOM   3615 H H    B ASP   A 1 162 ? 4.083  -4.884  3.378   0.12 21.63 ?  162 ASP   A H    1 
ATOM   3616 H HA   A ASP   A 1 162 ? 2.919  -7.612  4.410   0.88 23.78 ?  162 ASP   A HA   1 
ATOM   3617 H HA   B ASP   A 1 162 ? 2.972  -7.138  4.074   0.12 22.27 ?  162 ASP   A HA   1 
ATOM   3618 H HB2  A ASP   A 1 162 ? 1.656  -5.463  3.101   0.88 24.62 ?  162 ASP   A HB2  1 
ATOM   3619 H HB2  B ASP   A 1 162 ? 2.009  -5.004  2.519   0.12 22.36 ?  162 ASP   A HB2  1 
ATOM   3620 H HB3  A ASP   A 1 162 ? 0.856  -6.784  3.477   0.88 24.62 ?  162 ASP   A HB3  1 
ATOM   3621 H HB3  B ASP   A 1 162 ? 1.113  -6.298  2.745   0.12 22.36 ?  162 ASP   A HB3  1 
ATOM   3622 N N    A LYS   A 1 163 ? 3.381  -7.301  1.264   0.88 21.06 ?  163 LYS   A N    1 
ATOM   3623 N N    B LYS   A 1 163 ? 3.694  -6.975  0.955   0.12 19.63 ?  163 LYS   A N    1 
ATOM   3624 C CA   A LYS   A 1 163 ? 3.469  -8.076  0.030   0.88 21.35 ?  163 LYS   A CA   1 
ATOM   3625 C CA   B LYS   A 1 163 ? 3.931  -7.816  -0.214  0.12 20.01 ?  163 LYS   A CA   1 
ATOM   3626 C C    A LYS   A 1 163 ? 4.566  -9.131  0.110   0.88 20.51 ?  163 LYS   A C    1 
ATOM   3627 C C    B LYS   A 1 163 ? 5.034  -8.831  0.056   0.12 19.33 ?  163 LYS   A C    1 
ATOM   3628 O O    A LYS   A 1 163 ? 4.405  -10.241 -0.407  0.88 21.48 ?  163 LYS   A O    1 
ATOM   3629 O O    B LYS   A 1 163 ? 4.965  -9.973  -0.414  0.12 19.44 ?  163 LYS   A O    1 
ATOM   3630 C CB   A LYS   A 1 163 ? 3.708  -7.143  -1.154  0.88 23.73 ?  163 LYS   A CB   1 
ATOM   3631 C CB   B LYS   A 1 163 ? 4.274  -6.949  -1.426  0.12 21.04 ?  163 LYS   A CB   1 
ATOM   3632 C CG   A LYS   A 1 163 ? 3.779  -7.850  -2.492  0.88 26.54 ?  163 LYS   A CG   1 
ATOM   3633 C CG   B LYS   A 1 163 ? 4.393  -7.729  -2.727  0.12 21.99 ?  163 LYS   A CG   1 
ATOM   3634 C CD   A LYS   A 1 163 ? 4.129  -6.878  -3.603  0.88 29.36 ?  163 LYS   A CD   1 
ATOM   3635 C CD   B LYS   A 1 163 ? 4.498  -6.804  -3.931  0.12 22.81 ?  163 LYS   A CD   1 
ATOM   3636 C CE   A LYS   A 1 163 ? 4.022  -7.538  -4.966  0.88 31.33 ?  163 LYS   A CE   1 
ATOM   3637 C CE   B LYS   A 1 163 ? 3.248  -5.956  -4.093  0.12 23.36 ?  163 LYS   A CE   1 
ATOM   3638 N NZ   A LYS   A 1 163 ? 4.602  -6.690  -6.045  0.88 32.37 ?  163 LYS   A NZ   1 
ATOM   3639 N NZ   B LYS   A 1 163 ? 2.987  -5.625  -5.520  0.12 23.67 ?  163 LYS   A NZ   1 
ATOM   3640 H H    A LYS   A 1 163 ? 3.627  -6.479  1.195   0.88 25.27 ?  163 LYS   A H    1 
ATOM   3641 H H    B LYS   A 1 163 ? 3.849  -6.138  0.833   0.12 23.55 ?  163 LYS   A H    1 
ATOM   3642 H HA   A LYS   A 1 163 ? 2.623  -8.530  -0.114  0.88 25.61 ?  163 LYS   A HA   1 
ATOM   3643 H HA   B LYS   A 1 163 ? 3.122  -8.305  -0.420  0.12 24.01 ?  163 LYS   A HA   1 
ATOM   3644 H HB2  A LYS   A 1 163 ? 2.980  -6.502  -1.199  0.88 28.46 ?  163 LYS   A HB2  1 
ATOM   3645 H HB2  B LYS   A 1 163 ? 3.578  -6.284  -1.535  0.12 25.23 ?  163 LYS   A HB2  1 
ATOM   3646 H HB3  A LYS   A 1 163 ? 4.546  -6.678  -1.020  0.88 28.46 ?  163 LYS   A HB3  1 
ATOM   3647 H HB3  B LYS   A 1 163 ? 5.125  -6.512  -1.271  0.12 25.23 ?  163 LYS   A HB3  1 
ATOM   3648 H HG2  A LYS   A 1 163 ? 4.466  -8.534  -2.461  0.88 31.84 ?  163 LYS   A HG2  1 
ATOM   3649 H HG2  B LYS   A 1 163 ? 5.191  -8.281  -2.700  0.12 26.38 ?  163 LYS   A HG2  1 
ATOM   3650 H HG3  A LYS   A 1 163 ? 2.917  -8.248  -2.690  0.88 31.84 ?  163 LYS   A HG3  1 
ATOM   3651 H HG3  B LYS   A 1 163 ? 3.606  -8.285  -2.841  0.12 26.38 ?  163 LYS   A HG3  1 
ATOM   3652 H HD2  A LYS   A 1 163 ? 3.513  -6.129  -3.578  0.88 35.23 ?  163 LYS   A HD2  1 
ATOM   3653 H HD2  B LYS   A 1 163 ? 5.258  -6.211  -3.815  0.12 27.36 ?  163 LYS   A HD2  1 
ATOM   3654 H HD3  A LYS   A 1 163 ? 5.040  -6.568  -3.481  0.88 35.23 ?  163 LYS   A HD3  1 
ATOM   3655 H HD3  B LYS   A 1 163 ? 4.605  -7.335  -4.735  0.12 27.36 ?  163 LYS   A HD3  1 
ATOM   3656 H HE2  A LYS   A 1 163 ? 4.490  -8.387  -4.950  0.88 37.58 ?  163 LYS   A HE2  1 
ATOM   3657 H HE2  B LYS   A 1 163 ? 2.485  -6.445  -3.746  0.12 28.02 ?  163 LYS   A HE2  1 
ATOM   3658 H HE3  A LYS   A 1 163 ? 3.088  -7.683  -5.171  0.88 37.58 ?  163 LYS   A HE3  1 
ATOM   3659 H HE3  B LYS   A 1 163 ? 3.362  -5.125  -3.603  0.12 28.02 ?  163 LYS   A HE3  1 
ATOM   3660 H HZ1  A LYS   A 1 163 ? 4.526  -7.103  -6.830  0.88 38.83 ?  163 LYS   A HZ1  1 
ATOM   3661 H HZ1  B LYS   A 1 163 ? 2.251  -5.130  -5.588  0.12 28.40 ?  163 LYS   A HZ1  1 
ATOM   3662 H HZ2  A LYS   A 1 163 ? 4.170  -5.913  -6.084  0.88 38.83 ?  163 LYS   A HZ2  1 
ATOM   3663 H HZ2  B LYS   A 1 163 ? 3.674  -5.172  -5.858  0.12 28.40 ?  163 LYS   A HZ2  1 
ATOM   3664 H HZ3  A LYS   A 1 163 ? 5.463  -6.534  -5.882  0.88 38.83 ?  163 LYS   A HZ3  1 
ATOM   3665 H HZ3  B LYS   A 1 163 ? 2.875  -6.374  -5.989  0.12 28.40 ?  163 LYS   A HZ3  1 
ATOM   3666 N N    A LEU   A 1 164 ? 5.695  -8.796  0.738   0.88 18.69 ?  164 LEU   A N    1 
ATOM   3667 N N    B LEU   A 1 164 ? 6.058  -8.437  0.816   0.12 18.55 ?  164 LEU   A N    1 
ATOM   3668 C CA   A LEU   A 1 164 ? 6.787  -9.757  0.878   0.88 17.57 ?  164 LEU   A CA   1 
ATOM   3669 C CA   B LEU   A 1 164 ? 7.113  -9.378  1.177   0.12 17.83 ?  164 LEU   A CA   1 
ATOM   3670 C C    A LEU   A 1 164 ? 6.361  -10.946 1.725   0.88 17.46 ?  164 LEU   A C    1 
ATOM   3671 C C    B LEU   A 1 164 ? 6.577  -10.484 2.076   0.12 17.63 ?  164 LEU   A C    1 
ATOM   3672 O O    A LEU   A 1 164 ? 6.658  -12.099 1.393   0.88 18.02 ?  164 LEU   A O    1 
ATOM   3673 O O    B LEU   A 1 164 ? 6.913  -11.660 1.891   0.12 17.61 ?  164 LEU   A O    1 
ATOM   3674 C CB   A LEU   A 1 164 ? 7.990  -9.070  1.519   0.88 16.72 ?  164 LEU   A CB   1 
ATOM   3675 C CB   B LEU   A 1 164 ? 8.259  -8.641  1.872   0.12 17.39 ?  164 LEU   A CB   1 
ATOM   3676 C CG   A LEU   A 1 164 ? 8.737  -8.067  0.638   0.88 17.08 ?  164 LEU   A CG   1 
ATOM   3677 C CG   B LEU   A 1 164 ? 9.165  -7.760  1.010   0.12 17.09 ?  164 LEU   A CG   1 
ATOM   3678 C CD1  A LEU   A 1 164 ? 9.646  -7.166  1.473   0.88 16.77 ?  164 LEU   A CD1  1 
ATOM   3679 C CD1  B LEU   A 1 164 ? 10.090 -6.940  1.895   0.12 16.99 ?  164 LEU   A CD1  1 
ATOM   3680 C CD2  A LEU   A 1 164 ? 9.536  -8.781  -0.440  0.88 17.66 ?  164 LEU   A CD2  1 
ATOM   3681 C CD2  B LEU   A 1 164 ? 9.970  -8.598  0.027   0.12 16.98 ?  164 LEU   A CD2  1 
ATOM   3682 H H    A LEU   A 1 164 ? 5.854  -8.023  1.084   0.88 22.42 ?  164 LEU   A H    1 
ATOM   3683 H H    B LEU   A 1 164 ? 6.162  -7.644  1.129   0.12 22.25 ?  164 LEU   A H    1 
ATOM   3684 H HA   A LEU   A 1 164 ? 7.048  -10.081 0.005   0.88 21.08 ?  164 LEU   A HA   1 
ATOM   3685 H HA   B LEU   A 1 164 ? 7.460  -9.792  0.374   0.12 21.38 ?  164 LEU   A HA   1 
ATOM   3686 H HB2  A LEU   A 1 164 ? 7.689  -8.588  2.305   0.88 20.05 ?  164 LEU   A HB2  1 
ATOM   3687 H HB2  B LEU   A 1 164 ? 7.876  -8.068  2.554   0.12 20.86 ?  164 LEU   A HB2  1 
ATOM   3688 H HB3  A LEU   A 1 164 ? 8.629  -9.750  1.783   0.88 20.05 ?  164 LEU   A HB3  1 
ATOM   3689 H HB3  B LEU   A 1 164 ? 8.828  -9.302  2.295   0.12 20.86 ?  164 LEU   A HB3  1 
ATOM   3690 H HG   A LEU   A 1 164 ? 8.092  -7.498  0.195   0.88 20.49 ?  164 LEU   A HG   1 
ATOM   3691 H HG   B LEU   A 1 164 ? 8.618  -7.144  0.500   0.12 20.50 ?  164 LEU   A HG   1 
ATOM   3692 H HD11 A LEU   A 1 164 ? 10.107 -6.545  0.886   0.88 20.11 ?  164 LEU   A HD11 1 
ATOM   3693 H HD11 B LEU   A 1 164 ? 10.608 -6.338  1.339   0.12 20.38 ?  164 LEU   A HD11 1 
ATOM   3694 H HD12 A LEU   A 1 164 ? 9.103  -6.673  2.111   0.88 20.11 ?  164 LEU   A HD12 1 
ATOM   3695 H HD12 B LEU   A 1 164 ? 9.554  -6.431  2.523   0.12 20.38 ?  164 LEU   A HD12 1 
ATOM   3696 H HD13 A LEU   A 1 164 ? 10.292 -7.714  1.946   0.88 20.11 ?  164 LEU   A HD13 1 
ATOM   3697 H HD13 B LEU   A 1 164 ? 10.682 -7.540  2.375   0.12 20.38 ?  164 LEU   A HD13 1 
ATOM   3698 H HD21 A LEU   A 1 164 ? 10.036 -8.123  -0.953  0.88 21.19 ?  164 LEU   A HD21 1 
ATOM   3699 H HD21 B LEU   A 1 164 ? 10.552 -8.013  -0.483  0.12 20.36 ?  164 LEU   A HD21 1 
ATOM   3700 H HD22 A LEU   A 1 164 ? 10.149 -9.405  -0.022  0.88 21.19 ?  164 LEU   A HD22 1 
ATOM   3701 H HD22 B LEU   A 1 164 ? 10.501 -9.241  0.521   0.12 20.36 ?  164 LEU   A HD22 1 
ATOM   3702 H HD23 A LEU   A 1 164 ? 8.925  -9.256  -1.024  0.88 21.19 ?  164 LEU   A HD23 1 
ATOM   3703 H HD23 B LEU   A 1 164 ? 9.360  -9.059  -0.569  0.12 20.36 ?  164 LEU   A HD23 1 
ATOM   3704 N N    A VAL   A 1 165 ? 5.672  -10.679 2.834   0.88 17.16 ?  165 VAL   A N    1 
ATOM   3705 N N    B VAL   A 1 165 ? 5.741  -10.130 3.051   0.12 17.56 ?  165 VAL   A N    1 
ATOM   3706 C CA   A VAL   A 1 165 ? 5.201  -11.752 3.701   0.88 17.01 ?  165 VAL   A CA   1 
ATOM   3707 C CA   B VAL   A 1 165 ? 5.252  -11.122 4.003   0.12 17.66 ?  165 VAL   A CA   1 
ATOM   3708 C C    A VAL   A 1 165 ? 4.157  -12.594 2.982   0.88 16.95 ?  165 VAL   A C    1 
ATOM   3709 C C    B VAL   A 1 165 ? 4.077  -11.905 3.428   0.12 17.90 ?  165 VAL   A C    1 
ATOM   3710 O O    A VAL   A 1 165 ? 4.248  -13.826 2.935   0.88 16.80 ?  165 VAL   A O    1 
ATOM   3711 O O    B VAL   A 1 165 ? 4.022  -13.134 3.543   0.12 17.93 ?  165 VAL   A O    1 
ATOM   3712 C CB   A VAL   A 1 165 ? 4.645  -11.155 5.007   0.88 17.35 ?  165 VAL   A CB   1 
ATOM   3713 C CB   B VAL   A 1 165 ? 4.909  -10.448 5.344   0.12 17.60 ?  165 VAL   A CB   1 
ATOM   3714 C CG1  A VAL   A 1 165 ? 3.880  -12.209 5.799   0.88 17.57 ?  165 VAL   A CG1  1 
ATOM   3715 C CG1  B VAL   A 1 165 ? 4.198  -11.424 6.265   0.12 17.59 ?  165 VAL   A CG1  1 
ATOM   3716 C CG2  A VAL   A 1 165 ? 5.767  -10.540 5.835   0.88 17.75 ?  165 VAL   A CG2  1 
ATOM   3717 C CG2  B VAL   A 1 165 ? 6.174  -9.916  6.002   0.12 17.55 ?  165 VAL   A CG2  1 
ATOM   3718 H H    A VAL   A 1 165 ? 5.472  -9.890  3.108   0.88 20.58 ?  165 VAL   A H    1 
ATOM   3719 H H    B VAL   A 1 165 ? 5.449  -9.329  3.183   0.12 21.07 ?  165 VAL   A H    1 
ATOM   3720 H HA   A VAL   A 1 165 ? 5.945  -12.330 3.933   0.88 20.40 ?  165 VAL   A HA   1 
ATOM   3721 H HA   B VAL   A 1 165 ? 5.965  -11.754 4.176   0.12 21.18 ?  165 VAL   A HA   1 
ATOM   3722 H HB   A VAL   A 1 165 ? 4.023  -10.444 4.785   0.88 20.81 ?  165 VAL   A HB   1 
ATOM   3723 H HB   B VAL   A 1 165 ? 4.315  -9.697  5.184   0.12 21.11 ?  165 VAL   A HB   1 
ATOM   3724 H HG11 A VAL   A 1 165 ? 3.791  -11.905 6.716   0.88 21.08 ?  165 VAL   A HG11 1 
ATOM   3725 H HG11 B VAL   A 1 165 ? 4.211  -11.070 7.168   0.12 21.10 ?  165 VAL   A HG11 1 
ATOM   3726 H HG12 A VAL   A 1 165 ? 3.000  -12.321 5.405   0.88 21.08 ?  165 VAL   A HG12 1 
ATOM   3727 H HG12 B VAL   A 1 165 ? 3.282  -11.532 5.967   0.12 21.10 ?  165 VAL   A HG12 1 
ATOM   3728 H HG13 A VAL   A 1 165 ? 4.371  -13.041 5.770   0.88 21.08 ?  165 VAL   A HG13 1 
ATOM   3729 H HG13 B VAL   A 1 165 ? 4.662  -12.275 6.238   0.12 21.10 ?  165 VAL   A HG13 1 
ATOM   3730 H HG21 A VAL   A 1 165 ? 5.396  -10.172 6.653   0.88 21.29 ?  165 VAL   A HG21 1 
ATOM   3731 H HG21 B VAL   A 1 165 ? 5.967  -9.636  6.906   0.12 21.06 ?  165 VAL   A HG21 1 
ATOM   3732 H HG22 A VAL   A 1 165 ? 6.419  -11.226 6.046   0.88 21.29 ?  165 VAL   A HG22 1 
ATOM   3733 H HG22 B VAL   A 1 165 ? 6.840  -10.622 6.020   0.12 21.06 ?  165 VAL   A HG22 1 
ATOM   3734 H HG23 A VAL   A 1 165 ? 6.190  -9.833  5.319   0.88 21.29 ?  165 VAL   A HG23 1 
ATOM   3735 H HG23 B VAL   A 1 165 ? 6.506  -9.163  5.488   0.12 21.06 ?  165 VAL   A HG23 1 
ATOM   3736 N N    A SER   A 1 166 ? 3.149  -11.936 2.408   0.88 17.89 ?  166 SER   A N    1 
ATOM   3737 N N    B SER   A 1 166 ? 3.124  -11.215 2.796   0.12 18.15 ?  166 SER   A N    1 
ATOM   3738 C CA   A SER   A 1 166 ? 2.017  -12.663 1.846   0.88 19.15 ?  166 SER   A CA   1 
ATOM   3739 C CA   B SER   A 1 166 ? 1.920  -11.881 2.313   0.12 18.44 ?  166 SER   A CA   1 
ATOM   3740 C C    A SER   A 1 166 ? 2.419  -13.506 0.648   0.88 19.78 ?  166 SER   A C    1 
ATOM   3741 C C    B SER   A 1 166 ? 2.197  -12.844 1.166   0.12 18.40 ?  166 SER   A C    1 
ATOM   3742 O O    A SER   A 1 166 ? 1.766  -14.519 0.359   0.88 21.51 ?  166 SER   A O    1 
ATOM   3743 O O    B SER   A 1 166 ? 1.388  -13.746 0.925   0.12 18.37 ?  166 SER   A O    1 
ATOM   3744 C CB   A SER   A 1 166 ? 0.911  -11.685 1.442   0.88 21.03 ?  166 SER   A CB   1 
ATOM   3745 C CB   B SER   A 1 166 ? 0.876  -10.848 1.881   0.12 18.79 ?  166 SER   A CB   1 
ATOM   3746 O OG   A SER   A 1 166 ? 0.292  -11.099 2.575   0.88 23.04 ?  166 SER   A OG   1 
ATOM   3747 O OG   B SER   A 1 166 ? 0.610  -9.925  2.923   0.12 19.05 ?  166 SER   A OG   1 
ATOM   3748 H H    A SER   A 1 166 ? 3.094  -11.084 2.338   0.88 21.46 ?  166 SER   A H    1 
ATOM   3749 H H    B SER   A 1 166 ? 3.153  -10.371 2.641   0.12 21.77 ?  166 SER   A H    1 
ATOM   3750 H HA   A SER   A 1 166 ? 1.648  -13.259 2.517   0.88 22.97 ?  166 SER   A HA   1 
ATOM   3751 H HA   B SER   A 1 166 ? 1.541  -12.393 3.038   0.12 22.12 ?  166 SER   A HA   1 
ATOM   3752 H HB2  A SER   A 1 166 ? 1.290  -10.989 0.881   0.88 25.23 ?  166 SER   A HB2  1 
ATOM   3753 H HB2  B SER   A 1 166 ? 1.207  -10.363 1.111   0.12 22.54 ?  166 SER   A HB2  1 
ATOM   3754 H HB3  A SER   A 1 166 ? 0.221  -12.161 0.953   0.88 25.23 ?  166 SER   A HB3  1 
ATOM   3755 H HB3  B SER   A 1 166 ? 0.053  -11.311 1.651   0.12 22.54 ?  166 SER   A HB3  1 
ATOM   3756 H HG   A SER   A 1 166 ? -0.286 -10.538 2.335   0.88 27.63 ?  166 SER   A HG   1 
ATOM   3757 H HG   B SER   A 1 166 ? 0.030  -9.370  2.675   0.12 22.85 ?  166 SER   A HG   1 
ATOM   3758 N N    A SER   A 1 167 ? 3.476  -13.108 -0.060  0.88 19.53 ?  167 SER   A N    1 
ATOM   3759 N N    B SER   A 1 167 ? 3.313  -12.679 0.457   0.12 18.65 ?  167 SER   A N    1 
ATOM   3760 C CA   A SER   A 1 167 ? 3.931  -13.824 -1.239  0.88 20.22 ?  167 SER   A CA   1 
ATOM   3761 C CA   B SER   A 1 167 ? 3.665  -13.526 -0.683  0.12 18.96 ?  167 SER   A CA   1 
ATOM   3762 C C    A SER   A 1 167 ? 5.095  -14.759 -0.948  0.88 20.01 ?  167 SER   A C    1 
ATOM   3763 C C    B SER   A 1 167 ? 5.073  -14.061 -0.442  0.12 19.42 ?  167 SER   A C    1 
ATOM   3764 O O    A SER   A 1 167 ? 5.597  -15.403 -1.874  0.88 20.72 ?  167 SER   A O    1 
ATOM   3765 O O    B SER   A 1 167 ? 6.056  -13.444 -0.860  0.12 19.51 ?  167 SER   A O    1 
ATOM   3766 C CB   A SER   A 1 167 ? 4.322  -12.833 -2.345  0.88 20.91 ?  167 SER   A CB   1 
ATOM   3767 C CB   B SER   A 1 167 ? 3.576  -12.741 -1.987  0.12 19.01 ?  167 SER   A CB   1 
ATOM   3768 O OG   A SER   A 1 167 ? 5.397  -12.001 -1.933  0.88 21.25 ?  167 SER   A OG   1 
ATOM   3769 O OG   B SER   A 1 167 ? 4.217  -13.439 -3.041  0.12 19.05 ?  167 SER   A OG   1 
ATOM   3770 H H    A SER   A 1 167 ? 3.944  -12.408 0.128   0.88 23.42 ?  167 SER   A H    1 
ATOM   3771 H H    B SER   A 1 167 ? 3.899  -12.069 0.621   0.12 22.37 ?  167 SER   A H    1 
ATOM   3772 H HA   A SER   A 1 167 ? 3.198  -14.358 -1.576  0.88 24.25 ?  167 SER   A HA   1 
ATOM   3773 H HA   B SER   A 1 167 ? 3.052  -14.275 -0.734  0.12 22.75 ?  167 SER   A HA   1 
ATOM   3774 H HB2  A SER   A 1 167 ? 4.596  -13.333 -3.131  0.88 25.08 ?  167 SER   A HB2  1 
ATOM   3775 H HB2  B SER   A 1 167 ? 2.642  -12.619 -2.219  0.12 22.80 ?  167 SER   A HB2  1 
ATOM   3776 H HB3  A SER   A 1 167 ? 3.547  -12.283 -2.566  0.88 25.08 ?  167 SER   A HB3  1 
ATOM   3777 H HB3  B SER   A 1 167 ? 4.002  -11.877 -1.865  0.12 22.80 ?  167 SER   A HB3  1 
ATOM   3778 H HG   A SER   A 1 167 ? 5.160  -11.549 -1.262  0.88 25.49 ?  167 SER   A HG   1 
ATOM   3779 H HG   B SER   A 1 167 ? 4.173  -12.992 -3.750  0.12 22.85 ?  167 SER   A HG   1 
ATOM   3780 N N    A PHE   A 1 168 ? 5.535  -14.855 0.306   0.88 19.51 ?  168 PHE   A N    1 
ATOM   3781 N N    B PHE   A 1 168 ? 5.168  -15.206 0.236   0.12 19.88 ?  168 PHE   A N    1 
ATOM   3782 C CA   A PHE   A 1 168 ? 6.715  -15.657 0.607   0.88 19.81 ?  168 PHE   A CA   1 
ATOM   3783 C CA   B PHE   A 1 168 ? 6.469  -15.809 0.503   0.12 20.39 ?  168 PHE   A CA   1 
ATOM   3784 C C    A PHE   A 1 168 ? 6.398  -17.140 0.502   0.88 22.02 ?  168 PHE   A C    1 
ATOM   3785 C C    B PHE   A 1 168 ? 6.471  -17.308 0.214   0.12 21.53 ?  168 PHE   A C    1 
ATOM   3786 O O    A PHE   A 1 168 ? 5.424  -17.627 1.087   0.88 23.10 ?  168 PHE   A O    1 
ATOM   3787 O O    B PHE   A 1 168 ? 7.115  -17.753 -0.742  0.12 21.51 ?  168 PHE   A O    1 
ATOM   3788 C CB   A PHE   A 1 168 ? 7.244  -15.364 2.007   0.88 18.42 ?  168 PHE   A CB   1 
ATOM   3789 C CB   B PHE   A 1 168 ? 6.907  -15.514 1.940   0.12 19.81 ?  168 PHE   A CB   1 
ATOM   3790 C CG   A PHE   A 1 168 ? 8.505  -16.120 2.323   0.88 17.18 ?  168 PHE   A CG   1 
ATOM   3791 C CG   B PHE   A 1 168 ? 8.308  -15.965 2.253   0.12 19.32 ?  168 PHE   A CG   1 
ATOM   3792 C CD1  A PHE   A 1 168 ? 9.686  -15.771 1.705   0.88 17.25 ?  168 PHE   A CD1  1 
ATOM   3793 C CD1  B PHE   A 1 168 ? 9.396  -15.341 1.665   0.12 19.19 ?  168 PHE   A CD1  1 
ATOM   3794 C CD2  A PHE   A 1 168 ? 8.512  -17.195 3.201   0.88 16.63 ?  168 PHE   A CD2  1 
ATOM   3795 C CD2  B PHE   A 1 168 ? 8.537  -17.002 3.141   0.12 19.12 ?  168 PHE   A CD2  1 
ATOM   3796 C CE1  A PHE   A 1 168 ? 10.852 -16.455 1.963   0.88 16.72 ?  168 PHE   A CE1  1 
ATOM   3797 C CE1  B PHE   A 1 168 ? 10.684 -15.751 1.952   0.12 19.09 ?  168 PHE   A CE1  1 
ATOM   3798 C CE2  A PHE   A 1 168 ? 9.688  -17.882 3.465   0.88 16.53 ?  168 PHE   A CE2  1 
ATOM   3799 C CE2  B PHE   A 1 168 ? 9.819  -17.414 3.433   0.12 19.04 ?  168 PHE   A CE2  1 
ATOM   3800 C CZ   A PHE   A 1 168 ? 10.854 -17.508 2.843   0.88 16.72 ?  168 PHE   A CZ   1 
ATOM   3801 C CZ   B PHE   A 1 168 ? 10.894 -16.790 2.839   0.12 19.06 ?  168 PHE   A CZ   1 
ATOM   3802 H H    A PHE   A 1 168 ? 5.181  -14.462 0.985   0.88 23.40 ?  168 PHE   A H    1 
ATOM   3803 H H    B PHE   A 1 168 ? 4.497  -15.641 0.557   0.12 23.84 ?  168 PHE   A H    1 
ATOM   3804 H HA   A PHE   A 1 168 ? 7.415  -15.443 -0.034  0.88 23.76 ?  168 PHE   A HA   1 
ATOM   3805 H HA   B PHE   A 1 168 ? 7.120  -15.402 -0.083  0.12 24.46 ?  168 PHE   A HA   1 
ATOM   3806 H HB2  A PHE   A 1 168 ? 7.439  -14.416 2.080   0.88 22.09 ?  168 PHE   A HB2  1 
ATOM   3807 H HB2  B PHE   A 1 168 ? 6.867  -14.556 2.090   0.12 23.76 ?  168 PHE   A HB2  1 
ATOM   3808 H HB3  A PHE   A 1 168 ? 6.571  -15.616 2.656   0.88 22.09 ?  168 PHE   A HB3  1 
ATOM   3809 H HB3  B PHE   A 1 168 ? 6.301  -15.958 2.547   0.12 23.76 ?  168 PHE   A HB3  1 
ATOM   3810 H HD1  A PHE   A 1 168 ? 9.701  -15.058 1.109   0.88 20.69 ?  168 PHE   A HD1  1 
ATOM   3811 H HD1  B PHE   A 1 168 ? 9.258  -14.642 1.066   0.12 23.02 ?  168 PHE   A HD1  1 
ATOM   3812 H HD2  A PHE   A 1 168 ? 7.721  -17.451 3.622   0.88 19.94 ?  168 PHE   A HD2  1 
ATOM   3813 H HD2  B PHE   A 1 168 ? 7.818  -17.428 3.546   0.12 22.93 ?  168 PHE   A HD2  1 
ATOM   3814 H HE1  A PHE   A 1 168 ? 11.646 -16.203 1.545   0.88 20.05 ?  168 PHE   A HE1  1 
ATOM   3815 H HE1  B PHE   A 1 168 ? 11.409 -15.328 1.550   0.12 22.90 ?  168 PHE   A HE1  1 
ATOM   3816 H HE2  A PHE   A 1 168 ? 9.681  -18.601 4.060   0.88 19.83 ?  168 PHE   A HE2  1 
ATOM   3817 H HE2  B PHE   A 1 168 ? 9.955  -18.112 4.032   0.12 22.84 ?  168 PHE   A HE2  1 
ATOM   3818 H HZ   A PHE   A 1 168 ? 11.643 -17.971 3.018   0.88 20.06 ?  168 PHE   A HZ   1 
ATOM   3819 H HZ   B PHE   A 1 168 ? 11.759 -17.067 3.036   0.12 22.87 ?  168 PHE   A HZ   1 
ATOM   3820 N N    A LEU   A 1 169 ? 7.253  -17.864 -0.215  0.88 24.99 ?  169 LEU   A N    1 
ATOM   3821 N N    B LEU   A 1 169 ? 5.758  -18.090 1.021   0.12 22.68 ?  169 LEU   A N    1 
ATOM   3822 C CA   A LEU   A 1 169 ? 7.068  -19.291 -0.392  0.88 29.35 ?  169 LEU   A CA   1 
ATOM   3823 C CA   B LEU   A 1 169 ? 5.703  -19.542 0.844   0.12 23.70 ?  169 LEU   A CA   1 
ATOM   3824 C C    A LEU   A 1 169 ? 7.958  -20.046 0.583   0.88 30.95 ?  169 LEU   A C    1 
ATOM   3825 C C    B LEU   A 1 169 ? 7.126  -20.095 0.780   0.12 24.18 ?  169 LEU   A C    1 
ATOM   3826 O O    A LEU   A 1 169 ? 7.494  -20.494 1.632   0.88 31.48 ?  169 LEU   A O    1 
ATOM   3827 O O    B LEU   A 1 169 ? 7.390  -21.191 0.290   0.12 24.37 ?  169 LEU   A O    1 
ATOM   3828 C CB   A LEU   A 1 169 ? 7.385  -19.697 -1.834  0.88 31.45 ?  169 LEU   A CB   1 
ATOM   3829 C CB   B LEU   A 1 169 ? 4.918  -19.878 -0.430  0.12 24.12 ?  169 LEU   A CB   1 
ATOM   3830 C CG   A LEU   A 1 169 ? 7.053  -21.143 -2.211  0.88 33.07 ?  169 LEU   A CG   1 
ATOM   3831 C CG   B LEU   A 1 169 ? 4.533  -21.292 -0.886  0.12 24.40 ?  169 LEU   A CG   1 
ATOM   3832 C CD1  A LEU   A 1 169 ? 5.642  -21.503 -1.774  0.88 33.77 ?  169 LEU   A CD1  1 
ATOM   3833 C CD1  B LEU   A 1 169 ? 5.343  -21.683 -2.117  0.12 24.53 ?  169 LEU   A CD1  1 
ATOM   3834 C CD2  A LEU   A 1 169 ? 7.217  -21.357 -3.708  0.88 33.50 ?  169 LEU   A CD2  1 
ATOM   3835 C CD2  B LEU   A 1 169 ? 4.669  -22.345 0.203   0.12 24.48 ?  169 LEU   A CD2  1 
ATOM   3836 O OXT  A LEU   A 1 169 ? 9.157  -20.208 0.354   0.88 31.14 -1 169 LEU   A OXT  1 
ATOM   3837 O OXT  B LEU   A 1 169 ? 8.068  -19.433 1.215   0.12 24.34 -1 169 LEU   A OXT  1 
ATOM   3838 H H    A LEU   A 1 169 ? 7.951  -17.547 -0.609  0.88 29.98 ?  169 LEU   A H    1 
ATOM   3839 H H    B LEU   A 1 169 ? 5.290  -17.799 1.677   0.12 27.21 ?  169 LEU   A H    1 
ATOM   3840 H HA   A LEU   A 1 169 ? 6.144  -19.511 -0.200  0.88 35.22 ?  169 LEU   A HA   1 
ATOM   3841 H HA   B LEU   A 1 169 ? 5.236  -19.932 1.604   0.12 28.43 ?  169 LEU   A HA   1 
ATOM   3842 H HB2  A LEU   A 1 169 ? 6.884  -19.121 -2.431  0.88 37.73 ?  169 LEU   A HB2  1 
ATOM   3843 H HB2  B LEU   A 1 169 ? 4.073  -19.436 -0.323  0.12 28.93 ?  169 LEU   A HB2  1 
ATOM   3844 H HB3  A LEU   A 1 169 ? 8.335  -19.571 -1.985  0.88 37.73 ?  169 LEU   A HB3  1 
ATOM   3845 H HB3  B LEU   A 1 169 ? 5.393  -19.476 -1.173  0.12 28.93 ?  169 LEU   A HB3  1 
ATOM   3846 H HG   A LEU   A 1 169 ? 7.669  -21.739 -1.756  0.88 39.68 ?  169 LEU   A HG   1 
ATOM   3847 H HG   B LEU   A 1 169 ? 3.597  -21.276 -1.156  0.12 29.27 ?  169 LEU   A HG   1 
ATOM   3848 H HD11 A LEU   A 1 169 ? 5.373  -22.320 -2.219  0.88 40.51 ?  169 LEU   A HD11 1 
ATOM   3849 H HD11 B LEU   A 1 169 ? 5.109  -22.589 -2.374  0.12 29.43 ?  169 LEU   A HD11 1 
ATOM   3850 H HD12 A LEU   A 1 169 ? 5.632  -21.631 -0.812  0.88 40.51 ?  169 LEU   A HD12 1 
ATOM   3851 H HD12 B LEU   A 1 169 ? 5.133  -21.071 -2.841  0.12 29.43 ?  169 LEU   A HD12 1 
ATOM   3852 H HD13 A LEU   A 1 169 ? 5.042  -20.780 -2.019  0.88 40.51 ?  169 LEU   A HD13 1 
ATOM   3853 H HD13 B LEU   A 1 169 ? 6.285  -21.632 -1.901  0.12 29.43 ?  169 LEU   A HD13 1 
ATOM   3854 H HD21 A LEU   A 1 169 ? 7.010  -22.281 -3.921  0.88 40.19 ?  169 LEU   A HD21 1 
ATOM   3855 H HD21 B LEU   A 1 169 ? 4.324  -23.176 -0.149  0.12 29.37 ?  169 LEU   A HD21 1 
ATOM   3856 H HD22 A LEU   A 1 169 ? 6.610  -20.765 -4.180  0.88 40.19 ?  169 LEU   A HD22 1 
ATOM   3857 H HD22 B LEU   A 1 169 ? 5.595  -22.463 0.430   0.12 29.37 ?  169 LEU   A HD22 1 
ATOM   3858 H HD23 A LEU   A 1 169 ? 8.133  -21.158 -3.957  0.88 40.19 ?  169 LEU   A HD23 1 
ATOM   3859 H HD23 B LEU   A 1 169 ? 4.168  -22.076 0.990   0.12 29.37 ?  169 LEU   A HD23 1 
ATOM   3860 N N    A SER   B 1 1   ? 50.724 -9.234  -23.777 0.88 29.27 ?  1   SER   B N    1 
ATOM   3861 N N    B SER   B 1 1   ? 50.682 -9.192  -23.717 0.12 27.88 ?  1   SER   B N    1 
ATOM   3862 C CA   A SER   B 1 1   ? 51.204 -10.273 -22.844 0.88 28.78 ?  1   SER   B CA   1 
ATOM   3863 C CA   B SER   B 1 1   ? 51.203 -10.214 -22.785 0.12 27.78 ?  1   SER   B CA   1 
ATOM   3864 C C    A SER   B 1 1   ? 50.123 -11.310 -22.577 0.88 27.09 ?  1   SER   B C    1 
ATOM   3865 C C    B SER   B 1 1   ? 50.161 -11.301 -22.567 0.12 27.47 ?  1   SER   B C    1 
ATOM   3866 O O    A SER   B 1 1   ? 48.931 -11.110 -22.865 0.88 26.23 ?  1   SER   B O    1 
ATOM   3867 O O    B SER   B 1 1   ? 49.007 -11.163 -22.974 0.12 27.37 ?  1   SER   B O    1 
ATOM   3868 C CB   A SER   B 1 1   ? 51.656 -9.655  -21.524 0.88 29.88 ?  1   SER   B CB   1 
ATOM   3869 C CB   B SER   B 1 1   ? 51.580 -9.576  -21.452 0.12 27.94 ?  1   SER   B CB   1 
ATOM   3870 O OG   A SER   B 1 1   ? 50.548 -9.424  -20.674 0.88 31.54 ?  1   SER   B OG   1 
ATOM   3871 O OG   B SER   B 1 1   ? 50.435 -9.401  -20.637 0.12 28.20 ?  1   SER   B OG   1 
ATOM   3872 H H1   A SER   B 1 1   ? 50.608 -9.597  -24.579 0.88 35.12 ?  1   SER   B H1   1 
ATOM   3873 H H1   B SER   B 1 1   ? 51.364 -8.718  -24.032 0.12 33.45 ?  1   SER   B H1   1 
ATOM   3874 H H2   A SER   B 1 1   ? 49.958 -8.908  -23.477 0.88 35.12 ?  1   SER   B H2   1 
ATOM   3875 H H2   B SER   B 1 1   ? 50.263 -9.597  -24.386 0.12 33.45 ?  1   SER   B H2   1 
ATOM   3876 H H3   A SER   B 1 1   ? 51.334 -8.590  -23.823 0.88 35.12 ?  1   SER   B H3   1 
ATOM   3877 H H3   B SER   B 1 1   ? 50.120 -8.663  -23.282 0.12 33.45 ?  1   SER   B H3   1 
ATOM   3878 H HA   A SER   B 1 1   ? 51.961 -10.716 -23.250 0.88 34.53 ?  1   SER   B HA   1 
ATOM   3879 H HA   B SER   B 1 1   ? 51.990 -10.613 -23.175 0.12 33.32 ?  1   SER   B HA   1 
ATOM   3880 H HB2  A SER   B 1 1   ? 52.266 -10.269 -21.089 0.88 35.85 ?  1   SER   B HB2  1 
ATOM   3881 H HB2  B SER   B 1 1   ? 52.217 -10.153 -21.004 0.12 33.52 ?  1   SER   B HB2  1 
ATOM   3882 H HB3  A SER   B 1 1   ? 52.099 -8.812  -21.702 0.88 35.85 ?  1   SER   B HB3  1 
ATOM   3883 H HB3  B SER   B 1 1   ? 51.978 -8.707  -21.618 0.12 33.52 ?  1   SER   B HB3  1 
ATOM   3884 H HG   A SER   B 1 1   ? 50.778 -8.926  -20.038 0.88 37.84 ?  1   SER   B HG   1 
ATOM   3885 H HG   B SER   B 1 1   ? 50.579 -8.800  -20.071 0.12 33.84 ?  1   SER   B HG   1 
ATOM   3886 N N    A MET   B 1 2   ? 50.565 -12.418 -22.001 0.88 26.55 ?  2   MET   B N    1 
ATOM   3887 N N    B MET   B 1 2   ? 50.578 -12.379 -21.911 0.12 27.22 ?  2   MET   B N    1 
ATOM   3888 C CA   A MET   B 1 2   ? 49.757 -13.617 -21.833 0.88 26.50 ?  2   MET   B CA   1 
ATOM   3889 C CA   B MET   B 1 2   ? 49.760 -13.575 -21.745 0.12 26.89 ?  2   MET   B CA   1 
ATOM   3890 C C    A MET   B 1 2   ? 49.522 -13.821 -20.344 0.88 23.96 ?  2   MET   B C    1 
ATOM   3891 C C    B MET   B 1 2   ? 49.500 -13.783 -20.260 0.12 24.89 ?  2   MET   B C    1 
ATOM   3892 O O    A MET   B 1 2   ? 50.454 -14.146 -19.603 0.88 24.11 ?  2   MET   B O    1 
ATOM   3893 O O    B MET   B 1 2   ? 50.406 -14.169 -19.514 0.12 25.00 ?  2   MET   B O    1 
ATOM   3894 C CB   A MET   B 1 2   ? 50.507 -14.800 -22.433 0.88 30.35 ?  2   MET   B CB   1 
ATOM   3895 C CB   B MET   B 1 2   ? 50.484 -14.775 -22.340 0.12 28.56 ?  2   MET   B CB   1 
ATOM   3896 C CG   A MET   B 1 2   ? 49.669 -16.041 -22.679 0.88 33.87 ?  2   MET   B CG   1 
ATOM   3897 C CG   B MET   B 1 2   ? 49.587 -15.938 -22.719 0.12 30.02 ?  2   MET   B CG   1 
ATOM   3898 S SD   A MET   B 1 2   ? 50.541 -17.219 -23.730 0.88 37.02 ?  2   MET   B SD   1 
ATOM   3899 S SD   B MET   B 1 2   ? 50.463 -17.127 -23.744 0.12 31.21 ?  2   MET   B SD   1 
ATOM   3900 C CE   A MET   B 1 2   ? 51.093 -16.126 -25.030 0.88 37.34 ?  2   MET   B CE   1 
ATOM   3901 C CE   B MET   B 1 2   ? 51.313 -16.011 -24.855 0.12 31.56 ?  2   MET   B CE   1 
ATOM   3902 H H    A MET   B 1 2   ? 51.360 -12.506 -21.685 0.88 31.85 ?  2   MET   B H    1 
ATOM   3903 H H    B MET   B 1 2   ? 51.357 -12.446 -21.553 0.12 32.65 ?  2   MET   B H    1 
ATOM   3904 H HA   A MET   B 1 2   ? 48.911 -13.523 -22.294 0.88 31.80 ?  2   MET   B HA   1 
ATOM   3905 H HA   B MET   B 1 2   ? 48.921 -13.467 -22.218 0.12 32.25 ?  2   MET   B HA   1 
ATOM   3906 H HB2  A MET   B 1 2   ? 50.878 -14.497 -23.272 0.88 36.41 ?  2   MET   B HB2  1 
ATOM   3907 H HB2  B MET   B 1 2   ? 50.943 -14.446 -23.124 0.12 34.26 ?  2   MET   B HB2  1 
ATOM   3908 H HB3  A MET   B 1 2   ? 51.225 -15.061 -21.839 0.88 36.41 ?  2   MET   B HB3  1 
ATOM   3909 H HB3  B MET   B 1 2   ? 51.130 -15.116 -21.707 0.12 34.26 ?  2   MET   B HB3  1 
ATOM   3910 H HG2  A MET   B 1 2   ? 49.476 -16.469 -21.826 0.88 40.64 ?  2   MET   B HG2  1 
ATOM   3911 H HG2  B MET   B 1 2   ? 49.294 -16.391 -21.912 0.12 36.02 ?  2   MET   B HG2  1 
ATOM   3912 H HG3  A MET   B 1 2   ? 48.846 -15.798 -23.127 0.88 40.64 ?  2   MET   B HG3  1 
ATOM   3913 H HG3  B MET   B 1 2   ? 48.822 -15.617 -23.217 0.12 36.02 ?  2   MET   B HG3  1 
ATOM   3914 H HE1  A MET   B 1 2   ? 51.232 -16.647 -25.824 0.88 44.80 ?  2   MET   B HE1  1 
ATOM   3915 H HE1  B MET   B 1 2   ? 51.545 -16.494 -25.647 0.12 37.86 ?  2   MET   B HE1  1 
ATOM   3916 H HE2  A MET   B 1 2   ? 50.404 -15.457 -25.181 0.88 44.80 ?  2   MET   B HE2  1 
ATOM   3917 H HE2  B MET   B 1 2   ? 50.723 -15.267 -25.077 0.12 37.86 ?  2   MET   B HE2  1 
ATOM   3918 H HE3  A MET   B 1 2   ? 51.920 -15.689 -24.760 0.88 44.80 ?  2   MET   B HE3  1 
ATOM   3919 H HE3  B MET   B 1 2   ? 52.116 -15.675 -24.415 0.12 37.86 ?  2   MET   B HE3  1 
ATOM   3920 N N    A VAL   B 1 3   ? 48.284 -13.603 -19.906 0.88 21.30 ?  3   VAL   B N    1 
ATOM   3921 N N    B VAL   B 1 3   ? 48.268 -13.521 -19.836 0.12 22.73 ?  3   VAL   B N    1 
ATOM   3922 C CA   A VAL   B 1 3   ? 47.871 -13.862 -18.535 0.88 20.06 ?  3   VAL   B CA   1 
ATOM   3923 C CA   B VAL   B 1 3   ? 47.836 -13.788 -18.471 0.12 20.63 ?  3   VAL   B CA   1 
ATOM   3924 C C    A VAL   B 1 3   ? 46.639 -14.757 -18.571 0.88 18.25 ?  3   VAL   B C    1 
ATOM   3925 C C    B VAL   B 1 3   ? 46.592 -14.663 -18.515 0.12 18.44 ?  3   VAL   B C    1 
ATOM   3926 O O    A VAL   B 1 3   ? 45.911 -14.818 -19.563 0.88 18.85 ?  3   VAL   B O    1 
ATOM   3927 O O    B VAL   B 1 3   ? 45.801 -14.609 -19.462 0.12 18.34 ?  3   VAL   B O    1 
ATOM   3928 C CB   A VAL   B 1 3   ? 47.589 -12.563 -17.741 0.88 21.70 ?  3   VAL   B CB   1 
ATOM   3929 C CB   B VAL   B 1 3   ? 47.565 -12.492 -17.674 0.12 20.85 ?  3   VAL   B CB   1 
ATOM   3930 C CG1  A VAL   B 1 3   ? 48.855 -11.707 -17.643 0.88 22.21 ?  3   VAL   B CG1  1 
ATOM   3931 C CG1  B VAL   B 1 3   ? 48.827 -11.645 -17.587 0.12 20.94 ?  3   VAL   B CG1  1 
ATOM   3932 C CG2  A VAL   B 1 3   ? 46.449 -11.780 -18.374 0.88 22.43 ?  3   VAL   B CG2  1 
ATOM   3933 C CG2  B VAL   B 1 3   ? 46.426 -11.708 -18.304 0.12 20.95 ?  3   VAL   B CG2  1 
ATOM   3934 H H    A VAL   B 1 3   ? 47.649 -13.305 -20.401 0.88 25.55 ?  3   VAL   B H    1 
ATOM   3935 H H    B VAL   B 1 3   ? 47.657 -13.177 -20.335 0.12 27.26 ?  3   VAL   B H    1 
ATOM   3936 H HA   A VAL   B 1 3   ? 48.573 -14.343 -18.070 0.88 24.06 ?  3   VAL   B HA   1 
ATOM   3937 H HA   B VAL   B 1 3   ? 48.533 -14.280 -18.013 0.12 24.75 ?  3   VAL   B HA   1 
ATOM   3938 H HB   A VAL   B 1 3   ? 47.326 -12.795 -16.836 0.88 26.03 ?  3   VAL   B HB   1 
ATOM   3939 H HB   B VAL   B 1 3   ? 47.303 -12.731 -16.771 0.12 25.01 ?  3   VAL   B HB   1 
ATOM   3940 H HG11 A VAL   B 1 3   ? 48.657 -10.906 -17.132 0.88 26.64 ?  3   VAL   B HG11 1 
ATOM   3941 H HG11 B VAL   B 1 3   ? 48.637 -10.852 -17.061 0.12 25.12 ?  3   VAL   B HG11 1 
ATOM   3942 H HG12 A VAL   B 1 3   ? 49.548 -12.219 -17.197 0.88 26.64 ?  3   VAL   B HG12 1 
ATOM   3943 H HG12 B VAL   B 1 3   ? 49.527 -12.164 -17.161 0.12 25.12 ?  3   VAL   B HG12 1 
ATOM   3944 H HG13 A VAL   B 1 3   ? 49.143 -11.467 -18.537 0.88 26.64 ?  3   VAL   B HG13 1 
ATOM   3945 H HG13 B VAL   B 1 3   ? 49.100 -11.391 -18.482 0.12 25.12 ?  3   VAL   B HG13 1 
ATOM   3946 H HG21 A VAL   B 1 3   ? 46.401 -10.904 -17.964 0.88 26.90 ?  3   VAL   B HG21 1 
ATOM   3947 H HG21 B VAL   B 1 3   ? 46.380 -10.835 -17.888 0.12 25.13 ?  3   VAL   B HG21 1 
ATOM   3948 H HG22 A VAL   B 1 3   ? 46.616 -11.694 -19.324 0.88 26.90 ?  3   VAL   B HG22 1 
ATOM   3949 H HG22 B VAL   B 1 3   ? 46.595 -11.615 -19.254 0.12 25.13 ?  3   VAL   B HG22 1 
ATOM   3950 H HG23 A VAL   B 1 3   ? 45.618 -12.260 -18.225 0.88 26.90 ?  3   VAL   B HG23 1 
ATOM   3951 H HG23 B VAL   B 1 3   ? 45.595 -12.188 -18.162 0.12 25.13 ?  3   VAL   B HG23 1 
ATOM   3952 N N    . ASN   B 1 4   ? 46.422 -15.472 -17.471 1.00 16.49 ?  4   ASN   B N    1 
ATOM   3953 C CA   . ASN   B 1 4   ? 45.288 -16.391 -17.366 1.00 15.32 ?  4   ASN   B CA   1 
ATOM   3954 C C    . ASN   B 1 4   ? 45.238 -17.353 -18.553 1.00 15.64 ?  4   ASN   B C    1 
ATOM   3955 O O    . ASN   B 1 4   ? 44.178 -17.616 -19.118 1.00 16.53 ?  4   ASN   B O    1 
ATOM   3956 C CB   . ASN   B 1 4   ? 43.963 -15.638 -17.208 1.00 14.58 ?  4   ASN   B CB   1 
ATOM   3957 C CG   . ASN   B 1 4   ? 43.914 -14.822 -15.935 1.00 13.89 ?  4   ASN   B CG   1 
ATOM   3958 O OD1  . ASN   B 1 4   ? 44.211 -15.328 -14.855 1.00 13.54 ?  4   ASN   B OD1  1 
ATOM   3959 N ND2  . ASN   B 1 4   ? 43.566 -13.545 -16.056 1.00 14.59 ?  4   ASN   B ND2  1 
ATOM   3960 H H    A ASN   B 1 4   ? 46.923 -15.453 -16.773 0.88 19.78 ?  4   ASN   B H    1 
ATOM   3961 H H    B ASN   B 1 4   ? 46.953 -15.501 -16.796 0.12 19.78 ?  4   ASN   B H    1 
ATOM   3962 H HA   . ASN   B 1 4   ? 45.411 -16.927 -16.567 1.00 18.37 ?  4   ASN   B HA   1 
ATOM   3963 H HB2  . ASN   B 1 4   ? 43.847 -15.036 -17.957 1.00 17.49 ?  4   ASN   B HB2  1 
ATOM   3964 H HB3  . ASN   B 1 4   ? 43.235 -16.282 -17.182 1.00 17.49 ?  4   ASN   B HB3  1 
ATOM   3965 H HD21 . ASN   B 1 4   ? 43.526 -13.038 -15.358 1.00 17.50 ?  4   ASN   B HD21 1 
ATOM   3966 H HD22 . ASN   B 1 4   ? 43.367 -13.221 -16.828 1.00 17.50 ?  4   ASN   B HD22 1 
ATOM   3967 N N    . SER   B 1 5   ? 46.399 -17.879 -18.938 1.00 16.49 ?  5   SER   B N    1 
ATOM   3968 C CA   . SER   B 1 5   ? 46.493 -18.797 -20.074 1.00 18.95 ?  5   SER   B CA   1 
ATOM   3969 C C    . SER   B 1 5   ? 46.490 -20.233 -19.561 1.00 20.32 ?  5   SER   B C    1 
ATOM   3970 O O    . SER   B 1 5   ? 47.497 -20.936 -19.561 1.00 22.46 ?  5   SER   B O    1 
ATOM   3971 C CB   . SER   B 1 5   ? 47.737 -18.496 -20.903 1.00 20.35 ?  5   SER   B CB   1 
ATOM   3972 O OG   . SER   B 1 5   ? 48.922 -18.736 -20.161 1.00 22.76 ?  5   SER   B OG   1 
ATOM   3973 H H    . SER   B 1 5   ? 47.155 -17.717 -18.557 1.00 19.78 ?  5   SER   B H    1 
ATOM   3974 H HA   . SER   B 1 5   ? 45.717 -18.682 -20.641 1.00 22.73 ?  5   SER   B HA   1 
ATOM   3975 H HB2  . SER   B 1 5   ? 47.730 -19.061 -21.692 1.00 24.41 ?  5   SER   B HB2  1 
ATOM   3976 H HB3  . SER   B 1 5   ? 47.702 -17.565 -21.163 1.00 24.41 ?  5   SER   B HB3  1 
ATOM   3977 H HG   . SER   B 1 5   ? 48.977 -19.552 -19.966 1.00 27.31 ?  5   SER   B HG   1 
ATOM   3978 N N    . PHE   B 1 6   ? 45.314 -20.650 -19.106 1.00 20.47 ?  6   PHE   B N    1 
ATOM   3979 C CA   . PHE   B 1 6   ? 45.121 -21.999 -18.599 1.00 19.91 ?  6   PHE   B CA   1 
ATOM   3980 C C    . PHE   B 1 6   ? 45.049 -22.977 -19.761 1.00 22.90 ?  6   PHE   B C    1 
ATOM   3981 O O    . PHE   B 1 6   ? 44.392 -22.710 -20.770 1.00 24.85 ?  6   PHE   B O    1 
ATOM   3982 C CB   . PHE   B 1 6   ? 43.829 -22.061 -17.785 1.00 18.07 ?  6   PHE   B CB   1 
ATOM   3983 C CG   . PHE   B 1 6   ? 43.847 -21.197 -16.550 1.00 16.10 ?  6   PHE   B CG   1 
ATOM   3984 C CD1  . PHE   B 1 6   ? 44.361 -21.683 -15.365 1.00 14.84 ?  6   PHE   B CD1  1 
ATOM   3985 C CD2  . PHE   B 1 6   ? 43.353 -19.898 -16.577 1.00 15.43 ?  6   PHE   B CD2  1 
ATOM   3986 C CE1  . PHE   B 1 6   ? 44.374 -20.898 -14.222 1.00 14.38 ?  6   PHE   B CE1  1 
ATOM   3987 C CE2  . PHE   B 1 6   ? 43.370 -19.105 -15.441 1.00 15.69 ?  6   PHE   B CE2  1 
ATOM   3988 C CZ   . PHE   B 1 6   ? 43.889 -19.597 -14.265 1.00 14.59 ?  6   PHE   B CZ   1 
ATOM   3989 H H    . PHE   B 1 6   ? 44.604 -20.170 -19.084 1.00 24.55 ?  6   PHE   B H    1 
ATOM   3990 H HA   . PHE   B 1 6   ? 45.861 -22.253 -18.028 1.00 23.88 ?  6   PHE   B HA   1 
ATOM   3991 H HB2  . PHE   B 1 6   ? 43.092 -21.765 -18.343 1.00 21.68 ?  6   PHE   B HB2  1 
ATOM   3992 H HB3  . PHE   B 1 6   ? 43.676 -22.978 -17.501 1.00 21.68 ?  6   PHE   B HB3  1 
ATOM   3993 H HD1  . PHE   B 1 6   ? 44.699 -22.549 -15.330 1.00 17.80 ?  6   PHE   B HD1  1 
ATOM   3994 H HD2  . PHE   B 1 6   ? 43.000 -19.560 -17.369 1.00 18.50 ?  6   PHE   B HD2  1 
ATOM   3995 H HE1  . PHE   B 1 6   ? 44.734 -21.231 -13.428 1.00 17.25 ?  6   PHE   B HE1  1 
ATOM   3996 H HE2  . PHE   B 1 6   ? 43.032 -18.237 -15.472 1.00 18.82 ?  6   PHE   B HE2  1 
ATOM   3997 H HZ   . PHE   B 1 6   ? 43.899 -19.070 -13.496 1.00 17.50 ?  6   PHE   B HZ   1 
ATOM   3998 N N    . SER   B 1 7   ? 45.740 -24.109 -19.618 1.00 23.69 ?  7   SER   B N    1 
ATOM   3999 C CA   . SER   B 1 7   ? 45.834 -25.100 -20.681 1.00 26.05 ?  7   SER   B CA   1 
ATOM   4000 C C    . SER   B 1 7   ? 45.781 -26.502 -20.093 1.00 25.24 ?  7   SER   B C    1 
ATOM   4001 O O    . SER   B 1 7   ? 46.358 -26.766 -19.034 1.00 26.19 ?  7   SER   B O    1 
ATOM   4002 C CB   . SER   B 1 7   ? 47.134 -24.924 -21.477 1.00 28.78 ?  7   SER   B CB   1 
ATOM   4003 O OG   . SER   B 1 7   ? 47.181 -25.809 -22.581 1.00 30.76 ?  7   SER   B OG   1 
ATOM   4004 H H    . SER   B 1 7   ? 46.170 -24.328 -18.901 1.00 28.42 ?  7   SER   B H    1 
ATOM   4005 H HA   . SER   B 1 7   ? 45.086 -24.999 -21.285 1.00 31.26 ?  7   SER   B HA   1 
ATOM   4006 H HB2  . SER   B 1 7   ? 47.180 -24.011 -21.802 1.00 34.52 ?  7   SER   B HB2  1 
ATOM   4007 H HB3  . SER   B 1 7   ? 47.888 -25.104 -20.894 1.00 34.52 ?  7   SER   B HB3  1 
ATOM   4008 H HG   . SER   B 1 7   ? 47.898 -25.700 -23.007 1.00 36.90 ?  7   SER   B HG   1 
ATOM   4009 N N    . GLY   B 1 8   ? 45.087 -27.398 -20.791 1.00 25.00 ?  8   GLY   B N    1 
ATOM   4010 C CA   . GLY   B 1 8   ? 45.056 -28.790 -20.401 1.00 24.27 ?  8   GLY   B CA   1 
ATOM   4011 C C    . GLY   B 1 8   ? 44.102 -29.119 -19.281 1.00 22.91 ?  8   GLY   B C    1 
ATOM   4012 O O    . GLY   B 1 8   ? 44.234 -30.185 -18.667 1.00 24.22 ?  8   GLY   B O    1 
ATOM   4013 H H    . GLY   B 1 8   ? 44.626 -27.216 -21.491 1.00 29.99 ?  8   GLY   B H    1 
ATOM   4014 H HA2  . GLY   B 1 8   ? 44.808 -29.327 -21.170 1.00 29.11 ?  8   GLY   B HA2  1 
ATOM   4015 H HA3  . GLY   B 1 8   ? 45.941 -29.061 -20.118 1.00 29.11 ?  8   GLY   B HA3  1 
ATOM   4016 N N    . TYR   B 1 9   ? 43.128 -28.255 -19.005 1.00 21.05 ?  9   TYR   B N    1 
ATOM   4017 C CA   . TYR   B 1 9   ? 42.164 -28.527 -17.951 1.00 19.02 ?  9   TYR   B CA   1 
ATOM   4018 C C    . TYR   B 1 9   ? 40.978 -29.314 -18.477 1.00 18.50 ?  9   TYR   B C    1 
ATOM   4019 O O    . TYR   B 1 9   ? 40.562 -29.168 -19.630 1.00 20.41 ?  9   TYR   B O    1 
ATOM   4020 C CB   . TYR   B 1 9   ? 41.658 -27.239 -17.306 1.00 18.32 ?  9   TYR   B CB   1 
ATOM   4021 C CG   . TYR   B 1 9   ? 42.677 -26.614 -16.388 1.00 17.78 ?  9   TYR   B CG   1 
ATOM   4022 C CD1  . TYR   B 1 9   ? 43.782 -25.954 -16.903 1.00 18.37 ?  9   TYR   B CD1  1 
ATOM   4023 C CD2  . TYR   B 1 9   ? 42.549 -26.701 -15.011 1.00 17.14 ?  9   TYR   B CD2  1 
ATOM   4024 C CE1  . TYR   B 1 9   ? 44.732 -25.398 -16.073 1.00 18.70 ?  9   TYR   B CE1  1 
ATOM   4025 C CE2  . TYR   B 1 9   ? 43.492 -26.142 -14.170 1.00 17.47 ?  9   TYR   B CE2  1 
ATOM   4026 C CZ   . TYR   B 1 9   ? 44.583 -25.489 -14.710 1.00 18.39 ?  9   TYR   B CZ   1 
ATOM   4027 O OH   . TYR   B 1 9   ? 45.530 -24.941 -13.884 1.00 19.07 ?  9   TYR   B OH   1 
ATOM   4028 H H    . TYR   B 1 9   ? 42.988 -27.521 -19.429 1.00 25.26 ?  9   TYR   B H    1 
ATOM   4029 H HA   . TYR   B 1 9   ? 42.586 -29.057 -17.264 1.00 22.81 ?  9   TYR   B HA   1 
ATOM   4030 H HB2  . TYR   B 1 9   ? 41.432 -26.595 -17.997 1.00 21.97 ?  9   TYR   B HB2  1 
ATOM   4031 H HB3  . TYR   B 1 9   ? 40.873 -27.452 -16.780 1.00 21.97 ?  9   TYR   B HB3  1 
ATOM   4032 H HD1  . TYR   B 1 9   ? 43.885 -25.895 -17.825 1.00 22.04 ?  9   TYR   B HD1  1 
ATOM   4033 H HD2  . TYR   B 1 9   ? 41.810 -27.145 -14.646 1.00 20.56 ?  9   TYR   B HD2  1 
ATOM   4034 H HE1  . TYR   B 1 9   ? 45.460 -24.959 -16.434 1.00 22.43 ?  9   TYR   B HE1  1 
ATOM   4035 H HE2  . TYR   B 1 9   ? 43.381 -26.210 -13.247 1.00 20.96 ?  9   TYR   B HE2  1 
ATOM   4036 H HH   . TYR   B 1 9   ? 46.122 -24.574 -14.345 1.00 22.88 ?  9   TYR   B HH   1 
ATOM   4037 N N    . LEU   B 1 10  ? 40.443 -30.160 -17.606 1.00 16.63 ?  10  LEU   B N    1 
ATOM   4038 C CA   . LEU   B 1 10  ? 39.237 -30.917 -17.880 1.00 16.52 ?  10  LEU   B CA   1 
ATOM   4039 C C    . LEU   B 1 10  ? 38.046 -30.153 -17.315 1.00 15.96 ?  10  LEU   B C    1 
ATOM   4040 O O    . LEU   B 1 10  ? 38.056 -29.744 -16.152 1.00 15.55 ?  10  LEU   B O    1 
ATOM   4041 C CB   . LEU   B 1 10  ? 39.348 -32.293 -17.222 1.00 17.30 ?  10  LEU   B CB   1 
ATOM   4042 C CG   . LEU   B 1 10  ? 38.210 -33.251 -17.556 1.00 19.00 ?  10  LEU   B CG   1 
ATOM   4043 C CD1  . LEU   B 1 10  ? 38.351 -33.768 -18.982 1.00 20.26 ?  10  LEU   B CD1  1 
ATOM   4044 C CD2  . LEU   B 1 10  ? 38.144 -34.390 -16.553 1.00 20.21 ?  10  LEU   B CD2  1 
ATOM   4045 H H    . LEU   B 1 10  ? 40.770 -30.315 -16.822 1.00 19.94 ?  10  LEU   B H    1 
ATOM   4046 H HA   . LEU   B 1 10  ? 39.117 -31.032 -18.833 1.00 19.81 ?  10  LEU   B HA   1 
ATOM   4047 H HB2  . LEU   B 1 10  ? 40.178 -32.711 -17.510 1.00 20.75 ?  10  LEU   B HB2  1 
ATOM   4048 H HB3  . LEU   B 1 10  ? 39.363 -32.181 -16.257 1.00 20.75 ?  10  LEU   B HB3  1 
ATOM   4049 H HG   . LEU   B 1 10  ? 37.372 -32.769 -17.502 1.00 22.79 ?  10  LEU   B HG   1 
ATOM   4050 H HD11 . LEU   B 1 10  ? 37.644 -34.408 -19.155 1.00 24.30 ?  10  LEU   B HD11 1 
ATOM   4051 H HD12 . LEU   B 1 10  ? 38.276 -33.019 -19.595 1.00 24.30 ?  10  LEU   B HD12 1 
ATOM   4052 H HD13 . LEU   B 1 10  ? 39.216 -34.192 -19.080 1.00 24.30 ?  10  LEU   B HD13 1 
ATOM   4053 H HD21 . LEU   B 1 10  ? 37.416 -34.979 -16.798 1.00 24.24 ?  10  LEU   B HD21 1 
ATOM   4054 H HD22 . LEU   B 1 10  ? 38.984 -34.869 -16.567 1.00 24.24 ?  10  LEU   B HD22 1 
ATOM   4055 H HD23 . LEU   B 1 10  ? 37.987 -34.016 -15.671 1.00 24.24 ?  10  LEU   B HD23 1 
ATOM   4056 N N    . LYS   B 1 11  ? 37.020 -29.970 -18.136 1.00 17.03 ?  11  LYS   B N    1 
ATOM   4057 C CA   . LYS   B 1 11  ? 35.829 -29.248 -17.717 1.00 18.81 ?  11  LYS   B CA   1 
ATOM   4058 C C    . LYS   B 1 11  ? 34.940 -30.173 -16.893 1.00 18.00 ?  11  LYS   B C    1 
ATOM   4059 O O    . LYS   B 1 11  ? 34.553 -31.249 -17.361 1.00 19.83 ?  11  LYS   B O    1 
ATOM   4060 C CB   . LYS   B 1 11  ? 35.092 -28.753 -18.961 1.00 22.41 ?  11  LYS   B CB   1 
ATOM   4061 C CG   . LYS   B 1 11  ? 33.926 -27.819 -18.699 1.00 25.75 ?  11  LYS   B CG   1 
ATOM   4062 C CD   . LYS   B 1 11  ? 33.191 -27.510 -20.001 1.00 28.55 ?  11  LYS   B CD   1 
ATOM   4063 C CE   . LYS   B 1 11  ? 32.151 -26.419 -19.821 1.00 30.67 ?  11  LYS   B CE   1 
ATOM   4064 N NZ   . LYS   B 1 11  ? 32.778 -25.096 -19.565 1.00 31.92 ?  11  LYS   B NZ   1 
ATOM   4065 H H    . LYS   B 1 11  ? 36.984 -30.267 -18.940 1.00 20.42 ?  11  LYS   B H    1 
ATOM   4066 H HA   . LYS   B 1 11  ? 36.078 -28.487 -17.172 1.00 22.56 ?  11  LYS   B HA   1 
ATOM   4067 H HB2  . LYS   B 1 11  ? 35.726 -28.276 -19.520 1.00 26.88 ?  11  LYS   B HB2  1 
ATOM   4068 H HB3  . LYS   B 1 11  ? 34.749 -29.521 -19.441 1.00 26.88 ?  11  LYS   B HB3  1 
ATOM   4069 H HG2  . LYS   B 1 11  ? 33.301 -28.242 -18.089 1.00 30.89 ?  11  LYS   B HG2  1 
ATOM   4070 H HG3  . LYS   B 1 11  ? 34.253 -26.986 -18.327 1.00 30.89 ?  11  LYS   B HG3  1 
ATOM   4071 H HD2  . LYS   B 1 11  ? 33.833 -27.211 -20.665 1.00 34.25 ?  11  LYS   B HD2  1 
ATOM   4072 H HD3  . LYS   B 1 11  ? 32.741 -28.312 -20.311 1.00 34.25 ?  11  LYS   B HD3  1 
ATOM   4073 H HE2  . LYS   B 1 11  ? 31.616 -26.351 -20.628 1.00 36.79 ?  11  LYS   B HE2  1 
ATOM   4074 H HE3  . LYS   B 1 11  ? 31.586 -26.641 -19.064 1.00 36.79 ?  11  LYS   B HE3  1 
ATOM   4075 H HZ1  . LYS   B 1 11  ? 32.149 -24.470 -19.496 1.00 38.29 ?  11  LYS   B HZ1  1 
ATOM   4076 H HZ2  . LYS   B 1 11  ? 33.245 -25.122 -18.808 1.00 38.29 ?  11  LYS   B HZ2  1 
ATOM   4077 H HZ3  . LYS   B 1 11  ? 33.325 -24.884 -20.235 1.00 38.29 ?  11  LYS   B HZ3  1 
ATOM   4078 N N    . LEU   B 1 12  ? 34.617 -29.761 -15.668 1.00 16.41 ?  12  LEU   B N    1 
ATOM   4079 C CA   . LEU   B 1 12  ? 33.650 -30.466 -14.832 1.00 16.10 ?  12  LEU   B CA   1 
ATOM   4080 C C    . LEU   B 1 12  ? 32.260 -29.855 -14.924 1.00 16.10 ?  12  LEU   B C    1 
ATOM   4081 O O    . LEU   B 1 12  ? 31.272 -30.572 -15.091 1.00 16.61 ?  12  LEU   B O    1 
ATOM   4082 C CB   . LEU   B 1 12  ? 34.105 -30.479 -13.369 1.00 15.62 ?  12  LEU   B CB   1 
ATOM   4083 C CG   . LEU   B 1 12  ? 35.443 -31.157 -13.099 1.00 15.91 ?  12  LEU   B CG   1 
ATOM   4084 C CD1  . LEU   B 1 12  ? 35.771 -31.109 -11.623 1.00 15.96 ?  12  LEU   B CD1  1 
ATOM   4085 C CD2  . LEU   B 1 12  ? 35.435 -32.590 -13.606 1.00 16.75 ?  12  LEU   B CD2  1 
ATOM   4086 H H    . LEU   B 1 12  ? 34.953 -29.066 -15.291 1.00 19.68 ?  12  LEU   B H    1 
ATOM   4087 H HA   . LEU   B 1 12  ? 33.581 -31.384 -15.134 1.00 19.32 ?  12  LEU   B HA   1 
ATOM   4088 H HB2  . LEU   B 1 12  ? 34.172 -29.562 -13.062 1.00 18.73 ?  12  LEU   B HB2  1 
ATOM   4089 H HB3  . LEU   B 1 12  ? 33.431 -30.944 -12.844 1.00 18.73 ?  12  LEU   B HB3  1 
ATOM   4090 H HG   . LEU   B 1 12  ? 36.137 -30.674 -13.575 1.00 19.08 ?  12  LEU   B HG   1 
ATOM   4091 H HD11 . LEU   B 1 12  ? 36.628 -31.540 -11.476 1.00 19.14 ?  12  LEU   B HD11 1 
ATOM   4092 H HD12 . LEU   B 1 12  ? 35.816 -30.182 -11.338 1.00 19.14 ?  12  LEU   B HD12 1 
ATOM   4093 H HD13 . LEU   B 1 12  ? 35.078 -31.573 -11.129 1.00 19.14 ?  12  LEU   B HD13 1 
ATOM   4094 H HD21 . LEU   B 1 12  ? 36.225 -33.044 -13.278 1.00 20.09 ?  12  LEU   B HD21 1 
ATOM   4095 H HD22 . LEU   B 1 12  ? 34.636 -33.034 -13.281 1.00 20.09 ?  12  LEU   B HD22 1 
ATOM   4096 H HD23 . LEU   B 1 12  ? 35.436 -32.582 -14.577 1.00 20.09 ?  12  LEU   B HD23 1 
ATOM   4097 N N    . THR   B 1 13  ? 32.174 -28.536 -14.809 1.00 16.12 ?  13  THR   B N    1 
ATOM   4098 C CA   . THR   B 1 13  ? 30.944 -27.788 -15.005 1.00 16.13 ?  13  THR   B CA   1 
ATOM   4099 C C    . THR   B 1 13  ? 31.272 -26.586 -15.883 1.00 17.73 ?  13  THR   B C    1 
ATOM   4100 O O    . THR   B 1 13  ? 32.418 -26.381 -16.296 1.00 18.71 ?  13  THR   B O    1 
ATOM   4101 C CB   . THR   B 1 13  ? 30.351 -27.325 -13.669 1.00 15.77 ?  13  THR   B CB   1 
ATOM   4102 O OG1  . THR   B 1 13  ? 31.192 -26.301 -13.120 1.00 15.67 ?  13  THR   B OG1  1 
ATOM   4103 C CG2  . THR   B 1 13  ? 30.252 -28.486 -12.682 1.00 16.47 ?  13  THR   B CG2  1 
ATOM   4104 H H    . THR   B 1 13  ? 32.843 -28.035 -14.615 1.00 19.34 ?  13  THR   B H    1 
ATOM   4105 H HA   . THR   B 1 13  ? 30.291 -28.340 -15.456 1.00 19.35 ?  13  THR   B HA   1 
ATOM   4106 H HB   . THR   B 1 13  ? 29.455 -26.973 -13.813 1.00 18.92 ?  13  THR   B HB   1 
ATOM   4107 H HG1  . THR   B 1 13  ? 30.938 -25.547 -13.396 1.00 18.80 ?  13  THR   B HG1  1 
ATOM   4108 H HG21 . THR   B 1 13  ? 29.751 -28.218 -11.896 1.00 19.75 ?  13  THR   B HG21 1 
ATOM   4109 H HG22 . THR   B 1 13  ? 29.804 -29.240 -13.098 1.00 19.75 ?  13  THR   B HG22 1 
ATOM   4110 H HG23 . THR   B 1 13  ? 31.142 -28.765 -12.406 1.00 19.75 ?  13  THR   B HG23 1 
ATOM   4111 N N    . ASP   B 1 14  ? 30.257 -25.767 -16.156 1.00 19.09 ?  14  ASP   B N    1 
ATOM   4112 C CA   . ASP   B 1 14  ? 30.476 -24.602 -17.002 1.00 20.80 ?  14  ASP   B CA   1 
ATOM   4113 C C    . ASP   B 1 14  ? 31.539 -23.662 -16.448 1.00 19.04 ?  14  ASP   B C    1 
ATOM   4114 O O    . ASP   B 1 14  ? 32.133 -22.906 -17.224 1.00 20.48 ?  14  ASP   B O    1 
ATOM   4115 C CB   . ASP   B 1 14  ? 29.167 -23.842 -17.217 1.00 24.86 ?  14  ASP   B CB   1 
ATOM   4116 C CG   . ASP   B 1 14  ? 28.245 -24.540 -18.190 1.00 28.77 ?  14  ASP   B CG   1 
ATOM   4117 O OD1  . ASP   B 1 14  ? 28.724 -25.390 -18.973 1.00 30.28 ?  14  ASP   B OD1  1 
ATOM   4118 O OD2  . ASP   B 1 14  ? 27.036 -24.238 -18.171 1.00 30.38 -1 14  ASP   B OD2  1 
ATOM   4119 H H    . ASP   B 1 14  ? 29.450 -25.863 -15.869 1.00 22.90 ?  14  ASP   B H    1 
ATOM   4120 H HA   . ASP   B 1 14  ? 30.782 -24.902 -17.868 1.00 24.96 ?  14  ASP   B HA   1 
ATOM   4121 H HB2  . ASP   B 1 14  ? 28.691 -23.770 -16.376 1.00 29.82 ?  14  ASP   B HB2  1 
ATOM   4122 H HB3  . ASP   B 1 14  ? 29.361 -22.959 -17.568 1.00 29.82 ?  14  ASP   B HB3  1 
ATOM   4123 N N    . ASN   B 1 15  ? 31.796 -23.689 -15.134 1.00 16.18 ?  15  ASN   B N    1 
ATOM   4124 C CA   . ASN   B 1 15  ? 32.751 -22.763 -14.535 1.00 14.33 ?  15  ASN   B CA   1 
ATOM   4125 C C    . ASN   B 1 15  ? 33.847 -23.417 -13.701 1.00 13.26 ?  15  ASN   B C    1 
ATOM   4126 O O    . ASN   B 1 15  ? 34.687 -22.688 -13.163 1.00 13.61 ?  15  ASN   B O    1 
ATOM   4127 C CB   . ASN   B 1 15  ? 32.034 -21.713 -13.670 1.00 14.30 ?  15  ASN   B CB   1 
ATOM   4128 C CG   . ASN   B 1 15  ? 31.414 -22.317 -12.429 1.00 14.25 ?  15  ASN   B CG   1 
ATOM   4129 O OD1  . ASN   B 1 15  ? 30.471 -23.114 -12.514 1.00 15.70 ?  15  ASN   B OD1  1 
ATOM   4130 N ND2  . ASN   B 1 15  ? 31.942 -21.966 -11.270 1.00 13.42 ?  15  ASN   B ND2  1 
ATOM   4131 H H    . ASN   B 1 15  ? 31.417 -24.224 -14.573 1.00 19.41 ?  15  ASN   B H    1 
ATOM   4132 H HA   . ASN   B 1 15  ? 33.187 -22.283 -15.248 1.00 17.18 ?  15  ASN   B HA   1 
ATOM   4133 H HB2  . ASN   B 1 15  ? 32.679 -21.037 -13.391 1.00 17.15 ?  15  ASN   B HB2  1 
ATOM   4134 H HB3  . ASN   B 1 15  ? 31.326 -21.294 -14.186 1.00 17.15 ?  15  ASN   B HB3  1 
ATOM   4135 H HD21 . ASN   B 1 15  ? 31.624 -22.281 -10.534 1.00 16.10 ?  15  ASN   B HD21 1 
ATOM   4136 H HD22 . ASN   B 1 15  ? 32.604 -21.410 -11.241 1.00 16.10 ?  15  ASN   B HD22 1 
ATOM   4137 N N    . VAL   B 1 16  ? 33.867 -24.742 -13.564 1.00 13.14 ?  16  VAL   B N    1 
ATOM   4138 C CA   . VAL   B 1 16  ? 34.862 -25.436 -12.750 1.00 12.65 ?  16  VAL   B CA   1 
ATOM   4139 C C    . VAL   B 1 16  ? 35.658 -26.374 -13.645 1.00 12.78 ?  16  VAL   B C    1 
ATOM   4140 O O    . VAL   B 1 16  ? 35.081 -27.246 -14.314 1.00 13.76 ?  16  VAL   B O    1 
ATOM   4141 C CB   . VAL   B 1 16  ? 34.230 -26.201 -11.577 1.00 13.19 ?  16  VAL   B CB   1 
ATOM   4142 C CG1  . VAL   B 1 16  ? 35.306 -26.931 -10.785 1.00 13.39 ?  16  VAL   B CG1  1 
ATOM   4143 C CG2  . VAL   B 1 16  ? 33.433 -25.259 -10.681 1.00 14.19 ?  16  VAL   B CG2  1 
ATOM   4144 H H    . VAL   B 1 16  ? 33.297 -25.272 -13.936 1.00 15.76 ?  16  VAL   B H    1 
ATOM   4145 H HA   . VAL   B 1 16  ? 35.477 -24.784 -12.378 1.00 15.17 ?  16  VAL   B HA   1 
ATOM   4146 H HB   . VAL   B 1 16  ? 33.617 -26.867 -11.928 1.00 15.82 ?  16  VAL   B HB   1 
ATOM   4147 H HG11 . VAL   B 1 16  ? 34.929 -27.221 -9.939  1.00 16.05 ?  16  VAL   B HG11 1 
ATOM   4148 H HG12 . VAL   B 1 16  ? 35.610 -27.697 -11.291 1.00 16.05 ?  16  VAL   B HG12 1 
ATOM   4149 H HG13 . VAL   B 1 16  ? 36.043 -26.321 -10.624 1.00 16.05 ?  16  VAL   B HG13 1 
ATOM   4150 H HG21 . VAL   B 1 16  ? 33.082 -25.758 -9.927  1.00 17.02 ?  16  VAL   B HG21 1 
ATOM   4151 H HG22 . VAL   B 1 16  ? 34.016 -24.551 -10.367 1.00 17.02 ?  16  VAL   B HG22 1 
ATOM   4152 H HG23 . VAL   B 1 16  ? 32.700 -24.879 -11.194 1.00 17.02 ?  16  VAL   B HG23 1 
ATOM   4153 N N    . TYR   B 1 17  ? 36.983 -26.210 -13.624 1.00 13.21 ?  17  TYR   B N    1 
ATOM   4154 C CA   . TYR   B 1 17  ? 37.926 -26.965 -14.435 1.00 13.62 ?  17  TYR   B CA   1 
ATOM   4155 C C    . TYR   B 1 17  ? 38.975 -27.577 -13.520 1.00 12.76 ?  17  TYR   B C    1 
ATOM   4156 O O    . TYR   B 1 17  ? 39.255 -27.044 -12.443 1.00 13.03 ?  17  TYR   B O    1 
ATOM   4157 C CB   . TYR   B 1 17  ? 38.639 -26.042 -15.430 1.00 15.90 ?  17  TYR   B CB   1 
ATOM   4158 C CG   . TYR   B 1 17  ? 37.714 -25.272 -16.335 1.00 18.74 ?  17  TYR   B CG   1 
ATOM   4159 C CD1  . TYR   B 1 17  ? 37.130 -24.080 -15.922 1.00 20.02 ?  17  TYR   B CD1  1 
ATOM   4160 C CD2  . TYR   B 1 17  ? 37.423 -25.738 -17.608 1.00 20.54 ?  17  TYR   B CD2  1 
ATOM   4161 C CE1  . TYR   B 1 17  ? 36.279 -23.374 -16.755 1.00 21.58 ?  17  TYR   B CE1  1 
ATOM   4162 C CE2  . TYR   B 1 17  ? 36.580 -25.039 -18.449 1.00 22.09 ?  17  TYR   B CE2  1 
ATOM   4163 C CZ   . TYR   B 1 17  ? 36.008 -23.862 -18.016 1.00 22.60 ?  17  TYR   B CZ   1 
ATOM   4164 O OH   . TYR   B 1 17  ? 35.168 -23.166 -18.853 1.00 24.01 ?  17  TYR   B OH   1 
ATOM   4165 H H    . TYR   B 1 17  ? 37.380 -25.632 -13.119 1.00 15.85 ?  17  TYR   B H    1 
ATOM   4166 H HA   . TYR   B 1 17  ? 37.468 -27.672 -14.919 1.00 16.33 ?  17  TYR   B HA   1 
ATOM   4167 H HB2  . TYR   B 1 17  ? 39.178 -25.405 -14.938 1.00 19.08 ?  17  TYR   B HB2  1 
ATOM   4168 H HB3  . TYR   B 1 17  ? 39.206 -26.584 -15.996 1.00 19.08 ?  17  TYR   B HB3  1 
ATOM   4169 H HD1  . TYR   B 1 17  ? 37.314 -23.752 -15.072 1.00 24.02 ?  17  TYR   B HD1  1 
ATOM   4170 H HD2  . TYR   B 1 17  ? 37.802 -26.534 -17.903 1.00 24.64 ?  17  TYR   B HD2  1 
ATOM   4171 H HE1  . TYR   B 1 17  ? 35.894 -22.576 -16.468 1.00 25.89 ?  17  TYR   B HE1  1 
ATOM   4172 H HE2  . TYR   B 1 17  ? 36.388 -25.366 -19.300 1.00 26.49 ?  17  TYR   B HE2  1 
ATOM   4173 H HH   . TYR   B 1 17  ? 35.083 -23.570 -19.585 1.00 28.80 ?  17  TYR   B HH   1 
ATOM   4174 N N    . ILE   B 1 18  ? 39.593 -28.676 -13.958 1.00 12.89 ?  18  ILE   B N    1 
ATOM   4175 C CA   . ILE   B 1 18  ? 40.523 -29.400 -13.098 1.00 12.79 ?  18  ILE   B CA   1 
ATOM   4176 C C    . ILE   B 1 18  ? 41.686 -29.948 -13.917 1.00 13.10 ?  18  ILE   B C    1 
ATOM   4177 O O    . ILE   B 1 18  ? 41.526 -30.344 -15.076 1.00 14.41 ?  18  ILE   B O    1 
ATOM   4178 C CB   . ILE   B 1 18  ? 39.775 -30.498 -12.301 1.00 13.48 ?  18  ILE   B CB   1 
ATOM   4179 C CG1  . ILE   B 1 18  ? 40.627 -31.034 -11.147 1.00 13.70 ?  18  ILE   B CG1  1 
ATOM   4180 C CG2  . ILE   B 1 18  ? 39.280 -31.616 -13.229 1.00 13.87 ?  18  ILE   B CG2  1 
ATOM   4181 C CD1  . ILE   B 1 18  ? 39.810 -31.817 -10.127 1.00 15.29 ?  18  ILE   B CD1  1 
ATOM   4182 H H    . ILE   B 1 18  ? 39.499 -29.018 -14.741 1.00 15.46 ?  18  ILE   B H    1 
ATOM   4183 H HA   . ILE   B 1 18  ? 40.891 -28.783 -12.447 1.00 15.34 ?  18  ILE   B HA   1 
ATOM   4184 H HB   . ILE   B 1 18  ? 38.989 -30.092 -11.904 1.00 16.17 ?  18  ILE   B HB   1 
ATOM   4185 H HG12 . ILE   B 1 18  ? 41.308 -31.623 -11.501 1.00 16.43 ?  18  ILE   B HG12 1 
ATOM   4186 H HG13 . ILE   B 1 18  ? 41.038 -30.285 -10.687 1.00 16.43 ?  18  ILE   B HG13 1 
ATOM   4187 H HG21 . ILE   B 1 18  ? 38.690 -32.203 -12.730 1.00 16.64 ?  18  ILE   B HG21 1 
ATOM   4188 H HG22 . ILE   B 1 18  ? 38.802 -31.215 -13.968 1.00 16.64 ?  18  ILE   B HG22 1 
ATOM   4189 H HG23 . ILE   B 1 18  ? 40.044 -32.115 -13.556 1.00 16.64 ?  18  ILE   B HG23 1 
ATOM   4190 H HD11 . ILE   B 1 18  ? 40.392 -32.097 -9.404  1.00 18.33 ?  18  ILE   B HD11 1 
ATOM   4191 H HD12 . ILE   B 1 18  ? 39.105 -31.247 -9.780  1.00 18.33 ?  18  ILE   B HD12 1 
ATOM   4192 H HD13 . ILE   B 1 18  ? 39.423 -32.594 -10.560 1.00 18.33 ?  18  ILE   B HD13 1 
ATOM   4193 N N    . LYS   B 1 19  ? 42.865 -29.983 -13.292 1.00 13.66 ?  19  LYS   B N    1 
ATOM   4194 C CA   . LYS   B 1 19  ? 44.077 -30.459 -13.942 1.00 14.32 ?  19  LYS   B CA   1 
ATOM   4195 C C    . LYS   B 1 19  ? 44.971 -31.138 -12.916 1.00 14.07 ?  19  LYS   B C    1 
ATOM   4196 O O    . LYS   B 1 19  ? 45.055 -30.698 -11.767 1.00 13.82 ?  19  LYS   B O    1 
ATOM   4197 C CB   . LYS   B 1 19  ? 44.849 -29.293 -14.576 1.00 15.68 ?  19  LYS   B CB   1 
ATOM   4198 C CG   . LYS   B 1 19  ? 46.062 -29.699 -15.394 1.00 17.48 ?  19  LYS   B CG   1 
ATOM   4199 C CD   . LYS   B 1 19  ? 46.790 -28.465 -15.914 1.00 19.39 ?  19  LYS   B CD   1 
ATOM   4200 C CE   . LYS   B 1 19  ? 47.951 -28.834 -16.817 1.00 21.29 ?  19  LYS   B CE   1 
ATOM   4201 N NZ   . LYS   B 1 19  ? 48.720 -27.641 -17.259 1.00 22.34 ?  19  LYS   B NZ   1 
ATOM   4202 H H    . LYS   B 1 19  ? 42.982 -29.728 -12.475 1.00 16.38 ?  19  LYS   B H    1 
ATOM   4203 H HA   . LYS   B 1 19  ? 43.844 -31.100 -14.633 1.00 17.18 ?  19  LYS   B HA   1 
ATOM   4204 H HB2  . LYS   B 1 19  ? 44.244 -28.812 -15.162 1.00 18.81 ?  19  LYS   B HB2  1 
ATOM   4205 H HB3  . LYS   B 1 19  ? 45.149 -28.704 -13.864 1.00 18.81 ?  19  LYS   B HB3  1 
ATOM   4206 H HG2  . LYS   B 1 19  ? 46.670 -30.207 -14.837 1.00 20.96 ?  19  LYS   B HG2  1 
ATOM   4207 H HG3  . LYS   B 1 19  ? 45.770 -30.231 -16.152 1.00 20.96 ?  19  LYS   B HG3  1 
ATOM   4208 H HD2  . LYS   B 1 19  ? 46.168 -27.918 -16.422 1.00 23.26 ?  19  LYS   B HD2  1 
ATOM   4209 H HD3  . LYS   B 1 19  ? 47.137 -27.959 -15.161 1.00 23.26 ?  19  LYS   B HD3  1 
ATOM   4210 H HE2  . LYS   B 1 19  ? 48.551 -29.424 -16.335 1.00 25.54 ?  19  LYS   B HE2  1 
ATOM   4211 H HE3  . LYS   B 1 19  ? 47.605 -29.283 -17.606 1.00 25.54 ?  19  LYS   B HE3  1 
ATOM   4212 H HZ1  . LYS   B 1 19  ? 49.346 -27.884 -17.844 1.00 26.80 ?  19  LYS   B HZ1  1 
ATOM   4213 H HZ2  . LYS   B 1 19  ? 48.175 -27.054 -17.645 1.00 26.80 ?  19  LYS   B HZ2  1 
ATOM   4214 H HZ3  . LYS   B 1 19  ? 49.111 -27.257 -16.559 1.00 26.80 ?  19  LYS   B HZ3  1 
ATOM   4215 N N    . ASN   B 1 20  ? 45.657 -32.193 -13.346 1.00 15.14 ?  20  ASN   B N    1 
ATOM   4216 C CA   . ASN   B 1 20  ? 46.696 -32.820 -12.534 1.00 16.06 ?  20  ASN   B CA   1 
ATOM   4217 C C    . ASN   B 1 20  ? 47.962 -31.992 -12.725 1.00 16.64 ?  20  ASN   B C    1 
ATOM   4218 O O    . ASN   B 1 20  ? 48.605 -32.058 -13.776 1.00 18.49 ?  20  ASN   B O    1 
ATOM   4219 C CB   . ASN   B 1 20  ? 46.882 -34.270 -12.976 1.00 17.61 ?  20  ASN   B CB   1 
ATOM   4220 C CG   . ASN   B 1 20  ? 48.042 -34.971 -12.287 1.00 18.89 ?  20  ASN   B CG   1 
ATOM   4221 O OD1  . ASN   B 1 20  ? 48.725 -35.803 -12.898 1.00 20.96 ?  20  ASN   B OD1  1 
ATOM   4222 N ND2  . ASN   B 1 20  ? 48.261 -34.665 -11.018 1.00 18.36 ?  20  ASN   B ND2  1 
ATOM   4223 H H    . ASN   B 1 20  ? 45.540 -32.566 -14.112 1.00 18.16 ?  20  ASN   B H    1 
ATOM   4224 H HA   . ASN   B 1 20  ? 46.431 -32.803 -11.600 1.00 19.26 ?  20  ASN   B HA   1 
ATOM   4225 H HB2  . ASN   B 1 20  ? 46.074 -34.765 -12.769 1.00 21.12 ?  20  ASN   B HB2  1 
ATOM   4226 H HB3  . ASN   B 1 20  ? 47.044 -34.284 -13.930 1.00 21.12 ?  20  ASN   B HB3  1 
ATOM   4227 H HD21 . ASN   B 1 20  ? 48.910 -35.033 -10.593 1.00 22.02 ?  20  ASN   B HD21 1 
ATOM   4228 H HD22 . ASN   B 1 20  ? 47.758 -34.091 -10.615 1.00 22.02 ?  20  ASN   B HD22 1 
ATOM   4229 N N    . ALA   B 1 21  ? 48.314 -31.190 -11.718 1.00 16.29 ?  21  ALA   B N    1 
ATOM   4230 C CA   . ALA   B 1 21  ? 49.412 -30.245 -11.865 1.00 16.96 ?  21  ALA   B CA   1 
ATOM   4231 C C    . ALA   B 1 21  ? 49.876 -29.763 -10.499 1.00 16.26 ?  21  ALA   B C    1 
ATOM   4232 O O    . ALA   B 1 21  ? 49.132 -29.796 -9.514  1.00 16.05 ?  21  ALA   B O    1 
ATOM   4233 C CB   . ALA   B 1 21  ? 48.999 -29.056 -12.733 1.00 18.31 ?  21  ALA   B CB   1 
ATOM   4234 H H    . ALA   B 1 21  ? 47.933 -31.178 -10.942 1.00 19.53 ?  21  ALA   B H    1 
ATOM   4235 H HA   . ALA   B 1 21  ? 50.155 -30.694 -12.294 1.00 20.34 ?  21  ALA   B HA   1 
ATOM   4236 H HB1  . ALA   B 1 21  ? 49.779 -28.511 -12.895 1.00 21.96 ?  21  ALA   B HB1  1 
ATOM   4237 H HB2  . ALA   B 1 21  ? 48.646 -29.393 -13.570 1.00 21.96 ?  21  ALA   B HB2  1 
ATOM   4238 H HB3  . ALA   B 1 21  ? 48.317 -28.548 -12.267 1.00 21.96 ?  21  ALA   B HB3  1 
ATOM   4239 N N    . ASP   B 1 22  ? 51.134 -29.322 -10.472 1.00 15.55 ?  22  ASP   B N    1 
ATOM   4240 C CA   . ASP   B 1 22  ? 51.744 -28.629 -9.342  1.00 14.84 ?  22  ASP   B CA   1 
ATOM   4241 C C    . ASP   B 1 22  ? 51.338 -27.160 -9.431  1.00 13.57 ?  22  ASP   B C    1 
ATOM   4242 O O    . ASP   B 1 22  ? 51.648 -26.491 -10.420 1.00 13.86 ?  22  ASP   B O    1 
ATOM   4243 C CB   . ASP   B 1 22  ? 53.259 -28.805 -9.499  1.00 16.62 ?  22  ASP   B CB   1 
ATOM   4244 C CG   . ASP   B 1 22  ? 54.088 -28.045 -8.470  1.00 18.15 ?  22  ASP   B CG   1 
ATOM   4245 O OD1  . ASP   B 1 22  ? 53.712 -26.935 -8.056  1.00 18.20 ?  22  ASP   B OD1  1 
ATOM   4246 O OD2  . ASP   B 1 22  ? 55.166 -28.564 -8.103  1.00 20.23 -1 22  ASP   B OD2  1 
ATOM   4247 H H    . ASP   B 1 22  ? 51.680 -29.425 -11.131 1.00 18.65 ?  22  ASP   B H    1 
ATOM   4248 H HA   . ASP   B 1 22  ? 51.451 -29.017 -8.497  1.00 17.80 ?  22  ASP   B HA   1 
ATOM   4249 H HB2  . ASP   B 1 22  ? 53.481 -29.743 -9.417  1.00 19.94 ?  22  ASP   B HB2  1 
ATOM   4250 H HB3  . ASP   B 1 22  ? 53.519 -28.478 -10.374 1.00 19.94 ?  22  ASP   B HB3  1 
ATOM   4251 N N    . ILE   B 1 23  ? 50.626 -26.666 -8.412  1.00 12.85 ?  23  ILE   B N    1 
ATOM   4252 C CA   . ILE   B 1 23  ? 50.031 -25.329 -8.486  1.00 12.25 ?  23  ILE   B CA   1 
ATOM   4253 C C    . ILE   B 1 23  ? 51.085 -24.238 -8.621  1.00 12.05 ?  23  ILE   B C    1 
ATOM   4254 O O    . ILE   B 1 23  ? 50.818 -23.193 -9.224  1.00 11.78 ?  23  ILE   B O    1 
ATOM   4255 C CB   . ILE   B 1 23  ? 49.090 -25.091 -7.290  1.00 12.81 ?  23  ILE   B CB   1 
ATOM   4256 C CG1  . ILE   B 1 23  ? 48.266 -23.817 -7.488  1.00 13.22 ?  23  ILE   B CG1  1 
ATOM   4257 C CG2  . ILE   B 1 23  ? 49.857 -25.056 -5.986  1.00 13.76 ?  23  ILE   B CG2  1 
ATOM   4258 C CD1  . ILE   B 1 23  ? 47.137 -23.660 -6.478  1.00 14.24 ?  23  ILE   B CD1  1 
ATOM   4259 H H    . ILE   B 1 23  ? 50.475 -27.084 -7.674  1.00 15.40 ?  23  ILE   B H    1 
ATOM   4260 H HA   . ILE   B 1 23  ? 49.483 -25.294 -9.286  1.00 14.69 ?  23  ILE   B HA   1 
ATOM   4261 H HB   . ILE   B 1 23  ? 48.468 -25.836 -7.251  1.00 15.37 ?  23  ILE   B HB   1 
ATOM   4262 H HG12 . ILE   B 1 23  ? 48.856 -23.047 -7.402  1.00 15.86 ?  23  ILE   B HG12 1 
ATOM   4263 H HG13 . ILE   B 1 23  ? 47.876 -23.827 -8.379  1.00 15.86 ?  23  ILE   B HG13 1 
ATOM   4264 H HG21 . ILE   B 1 23  ? 49.226 -25.054 -5.251  1.00 16.50 ?  23  ILE   B HG21 1 
ATOM   4265 H HG22 . ILE   B 1 23  ? 50.424 -25.841 -5.934  1.00 16.50 ?  23  ILE   B HG22 1 
ATOM   4266 H HG23 . ILE   B 1 23  ? 50.399 -24.253 -5.962  1.00 16.50 ?  23  ILE   B HG23 1 
ATOM   4267 H HD11 . ILE   B 1 23  ? 46.613 -22.878 -6.712  1.00 17.08 ?  23  ILE   B HD11 1 
ATOM   4268 H HD12 . ILE   B 1 23  ? 46.580 -24.453 -6.509  1.00 17.08 ?  23  ILE   B HD12 1 
ATOM   4269 H HD13 . ILE   B 1 23  ? 47.518 -23.554 -5.595  1.00 17.08 ?  23  ILE   B HD13 1 
ATOM   4270 N N    . VAL   B 1 24  ? 52.280 -24.444 -8.062  1.00 12.44 ?  24  VAL   B N    1 
ATOM   4271 C CA   . VAL   B 1 24  ? 53.356 -23.465 -8.228  1.00 12.95 ?  24  VAL   B CA   1 
ATOM   4272 C C    . VAL   B 1 24  ? 53.810 -23.417 -9.679  1.00 13.29 ?  24  VAL   B C    1 
ATOM   4273 O O    . VAL   B 1 24  ? 53.952 -22.339 -10.273 1.00 13.77 ?  24  VAL   B O    1 
ATOM   4274 C CB   . VAL   B 1 24  ? 54.534 -23.785 -7.284  1.00 14.03 ?  24  VAL   B CB   1 
ATOM   4275 C CG1  . VAL   B 1 24  ? 55.740 -22.900 -7.605  1.00 14.71 ?  24  VAL   B CG1  1 
ATOM   4276 C CG2  . VAL   B 1 24  ? 54.117 -23.609 -5.849  1.00 14.97 ?  24  VAL   B CG2  1 
ATOM   4277 H H    . VAL   B 1 24  ? 52.488 -25.130 -7.591  1.00 14.92 ?  24  VAL   B H    1 
ATOM   4278 H HA   . VAL   B 1 24  ? 53.021 -22.589 -7.995  1.00 15.53 ?  24  VAL   B HA   1 
ATOM   4279 H HB   . VAL   B 1 24  ? 54.799 -24.711 -7.404  1.00 16.83 ?  24  VAL   B HB   1 
ATOM   4280 H HG11 . VAL   B 1 24  ? 56.335 -22.890 -6.838  1.00 17.64 ?  24  VAL   B HG11 1 
ATOM   4281 H HG12 . VAL   B 1 24  ? 56.202 -23.267 -8.374  1.00 17.64 ?  24  VAL   B HG12 1 
ATOM   4282 H HG13 . VAL   B 1 24  ? 55.431 -22.002 -7.795  1.00 17.64 ?  24  VAL   B HG13 1 
ATOM   4283 H HG21 . VAL   B 1 24  ? 54.843 -23.885 -5.271  1.00 17.95 ?  24  VAL   B HG21 1 
ATOM   4284 H HG22 . VAL   B 1 24  ? 53.909 -22.673 -5.696  1.00 17.95 ?  24  VAL   B HG22 1 
ATOM   4285 H HG23 . VAL   B 1 24  ? 53.332 -24.154 -5.678  1.00 17.95 ?  24  VAL   B HG23 1 
ATOM   4286 N N    . GLU   B 1 25  ? 54.069 -24.590 -10.268 1.00 14.21 ?  25  GLU   B N    1 
ATOM   4287 C CA   . GLU   B 1 25  ? 54.467 -24.627 -11.669 1.00 15.81 ?  25  GLU   B CA   1 
ATOM   4288 C C    . GLU   B 1 25  ? 53.362 -24.080 -12.559 1.00 14.69 ?  25  GLU   B C    1 
ATOM   4289 O O    . GLU   B 1 25  ? 53.632 -23.367 -13.534 1.00 15.51 ?  25  GLU   B O    1 
ATOM   4290 C CB   . GLU   B 1 25  ? 54.855 -26.053 -12.060 1.00 19.24 ?  25  GLU   B CB   1 
ATOM   4291 C CG   . GLU   B 1 25  ? 56.154 -26.505 -11.407 1.00 24.26 ?  25  GLU   B CG   1 
ATOM   4292 C CD   . GLU   B 1 25  ? 57.269 -25.473 -11.516 1.00 28.78 ?  25  GLU   B CD   1 
ATOM   4293 O OE1  . GLU   B 1 25  ? 57.647 -25.114 -12.652 1.00 30.32 ?  25  GLU   B OE1  1 
ATOM   4294 O OE2  . GLU   B 1 25  ? 57.755 -25.001 -10.461 1.00 30.37 -1 25  GLU   B OE2  1 
ATOM   4295 H H    . GLU   B 1 25  ? 54.017 -25.361 -9.885  1.00 17.04 ?  25  GLU   B H    1 
ATOM   4296 H HA   . GLU   B 1 25  ? 55.228 -24.048 -11.792 1.00 18.96 ?  25  GLU   B HA   1 
ATOM   4297 H HB2  . GLU   B 1 25  ? 54.154 -26.666 -11.779 1.00 23.07 ?  25  GLU   B HB2  1 
ATOM   4298 H HB3  . GLU   B 1 25  ? 54.968 -26.102 -13.022 1.00 23.07 ?  25  GLU   B HB3  1 
ATOM   4299 H HG2  . GLU   B 1 25  ? 56.001 -26.653 -10.466 1.00 29.10 ?  25  GLU   B HG2  1 
ATOM   4300 H HG3  . GLU   B 1 25  ? 56.457 -27.320 -11.836 1.00 29.10 ?  25  GLU   B HG3  1 
ATOM   4301 N N    . GLU   B 1 26  ? 52.110 -24.390 -12.225 1.00 13.68 ?  26  GLU   B N    1 
ATOM   4302 C CA   . GLU   B 1 26  ? 50.982 -23.860 -12.984 1.00 14.23 ?  26  GLU   B CA   1 
ATOM   4303 C C    . GLU   B 1 26  ? 50.932 -22.343 -12.899 1.00 13.40 ?  26  GLU   B C    1 
ATOM   4304 O O    . GLU   B 1 26  ? 50.730 -21.664 -13.909 1.00 14.63 ?  26  GLU   B O    1 
ATOM   4305 C CB   . GLU   B 1 26  ? 49.670 -24.448 -12.462 1.00 16.39 ?  26  GLU   B CB   1 
ATOM   4306 C CG   . GLU   B 1 26  ? 49.233 -25.728 -13.134 1.00 19.64 ?  26  GLU   B CG   1 
ATOM   4307 C CD   . GLU   B 1 26  ? 48.979 -25.573 -14.630 1.00 21.24 ?  26  GLU   B CD   1 
ATOM   4308 O OE1  . GLU   B 1 26  ? 48.008 -24.903 -15.044 1.00 21.33 ?  26  GLU   B OE1  1 
ATOM   4309 O OE2  . GLU   B 1 26  ? 49.754 -26.153 -15.397 1.00 23.08 -1 26  GLU   B OE2  1 
ATOM   4310 H H    . GLU   B 1 26  ? 51.884 -24.906 -11.569 1.00 16.41 ?  26  GLU   B H    1 
ATOM   4311 H HA   . GLU   B 1 26  ? 51.080 -24.107 -13.915 1.00 17.06 ?  26  GLU   B HA   1 
ATOM   4312 H HB2  . GLU   B 1 26  ? 49.764 -24.634 -11.515 1.00 19.66 ?  26  GLU   B HB2  1 
ATOM   4313 H HB3  . GLU   B 1 26  ? 48.963 -23.795 -12.595 1.00 19.66 ?  26  GLU   B HB3  1 
ATOM   4314 H HG2  . GLU   B 1 26  ? 49.933 -26.384 -13.016 1.00 23.56 ?  26  GLU   B HG2  1 
ATOM   4315 H HG3  . GLU   B 1 26  ? 48.410 -26.036 -12.723 1.00 23.56 ?  26  GLU   B HG3  1 
ATOM   4316 N N    . ALA   B 1 27  ? 51.081 -21.796 -11.691 1.00 12.57 ?  27  ALA   B N    1 
ATOM   4317 C CA   . ALA   B 1 27  ? 51.043 -20.345 -11.539 1.00 13.20 ?  27  ALA   B CA   1 
ATOM   4318 C C    . ALA   B 1 27  ? 52.112 -19.680 -12.395 1.00 13.93 ?  27  ALA   B C    1 
ATOM   4319 O O    . ALA   B 1 27  ? 51.847 -18.679 -13.076 1.00 14.53 ?  27  ALA   B O    1 
ATOM   4320 C CB   . ALA   B 1 27  ? 51.199 -19.967 -10.067 1.00 13.38 ?  27  ALA   B CB   1 
ATOM   4321 H H    . ALA   B 1 27  ? 51.199 -22.236 -10.956 1.00 15.08 ?  27  ALA   B H    1 
ATOM   4322 H HA   . ALA   B 1 27  ? 50.184 -20.021 -11.835 1.00 15.84 ?  27  ALA   B HA   1 
ATOM   4323 H HB1  . ALA   B 1 27  ? 51.168 -19.003 -9.981  1.00 16.05 ?  27  ALA   B HB1  1 
ATOM   4324 H HB2  . ALA   B 1 27  ? 50.469 -20.367 -9.561  1.00 16.05 ?  27  ALA   B HB2  1 
ATOM   4325 H HB3  . ALA   B 1 27  ? 52.047 -20.304 -9.738  1.00 16.05 ?  27  ALA   B HB3  1 
ATOM   4326 N N    . LYS   B 1 28  ? 53.327 -20.225 -12.385 1.00 15.36 ?  28  LYS   B N    1 
ATOM   4327 C CA   . LYS   B 1 28  ? 54.404 -19.605 -13.147 1.00 17.61 ?  28  LYS   B CA   1 
ATOM   4328 C C    . LYS   B 1 28  ? 54.152 -19.682 -14.648 1.00 18.21 ?  28  LYS   B C    1 
ATOM   4329 O O    . LYS   B 1 28  ? 54.562 -18.781 -15.389 1.00 19.41 ?  28  LYS   B O    1 
ATOM   4330 C CB   . LYS   B 1 28  ? 55.756 -20.211 -12.754 1.00 20.43 ?  28  LYS   B CB   1 
ATOM   4331 C CG   . LYS   B 1 28  ? 56.158 -19.880 -11.319 1.00 23.26 ?  28  LYS   B CG   1 
ATOM   4332 C CD   . LYS   B 1 28  ? 57.588 -20.284 -10.996 1.00 27.10 ?  28  LYS   B CD   1 
ATOM   4333 C CE   . LYS   B 1 28  ? 57.692 -21.753 -10.667 1.00 29.96 ?  28  LYS   B CE   1 
ATOM   4334 N NZ   . LYS   B 1 28  ? 59.051 -22.096 -10.162 1.00 30.78 ?  28  LYS   B NZ   1 
ATOM   4335 H H    . LYS   B 1 28  ? 53.553 -20.937 -11.952 1.00 18.43 ?  28  LYS   B H    1 
ATOM   4336 H HA   . LYS   B 1 28  ? 54.437 -18.666 -12.917 1.00 21.12 ?  28  LYS   B HA   1 
ATOM   4337 H HB2  . LYS   B 1 28  ? 55.712 -21.174 -12.833 1.00 24.50 ?  28  LYS   B HB2  1 
ATOM   4338 H HB3  . LYS   B 1 28  ? 56.445 -19.859 -13.341 1.00 24.50 ?  28  LYS   B HB3  1 
ATOM   4339 H HG2  . LYS   B 1 28  ? 56.077 -18.921 -11.184 1.00 27.90 ?  28  LYS   B HG2  1 
ATOM   4340 H HG3  . LYS   B 1 28  ? 55.566 -20.349 -10.711 1.00 27.90 ?  28  LYS   B HG3  1 
ATOM   4341 H HD2  . LYS   B 1 28  ? 58.150 -20.103 -11.765 1.00 32.51 ?  28  LYS   B HD2  1 
ATOM   4342 H HD3  . LYS   B 1 28  ? 57.895 -19.776 -10.229 1.00 32.51 ?  28  LYS   B HD3  1 
ATOM   4343 H HE2  . LYS   B 1 28  ? 57.044 -21.974 -9.979  1.00 35.94 ?  28  LYS   B HE2  1 
ATOM   4344 H HE3  . LYS   B 1 28  ? 57.522 -22.276 -11.467 1.00 35.94 ?  28  LYS   B HE3  1 
ATOM   4345 H HZ1  . LYS   B 1 28  ? 59.096 -22.964 -9.972  1.00 36.93 ?  28  LYS   B HZ1  1 
ATOM   4346 H HZ2  . LYS   B 1 28  ? 59.662 -21.903 -10.778 1.00 36.93 ?  28  LYS   B HZ2  1 
ATOM   4347 H HZ3  . LYS   B 1 28  ? 59.227 -21.630 -9.424  1.00 36.93 ?  28  LYS   B HZ3  1 
ATOM   4348 N N    . LYS   B 1 29  ? 53.450 -20.717 -15.109 1.00 19.20 ?  29  LYS   B N    1 
ATOM   4349 C CA   . LYS   B 1 29  ? 53.165 -20.861 -16.533 1.00 21.56 ?  29  LYS   B CA   1 
ATOM   4350 C C    . LYS   B 1 29  ? 51.918 -20.097 -16.971 1.00 20.55 ?  29  LYS   B C    1 
ATOM   4351 O O    . LYS   B 1 29  ? 51.920 -19.477 -18.040 1.00 21.81 ?  29  LYS   B O    1 
ATOM   4352 C CB   . LYS   B 1 29  ? 53.007 -22.343 -16.884 1.00 25.93 ?  29  LYS   B CB   1 
ATOM   4353 C CG   . LYS   B 1 29  ? 52.856 -22.608 -18.373 1.00 29.85 ?  29  LYS   B CG   1 
ATOM   4354 C CD   . LYS   B 1 29  ? 53.100 -24.073 -18.711 1.00 32.93 ?  29  LYS   B CD   1 
ATOM   4355 C CE   . LYS   B 1 29  ? 52.041 -24.977 -18.101 1.00 35.02 ?  29  LYS   B CE   1 
ATOM   4356 N NZ   . LYS   B 1 29  ? 52.286 -26.412 -18.426 1.00 36.22 ?  29  LYS   B NZ   1 
ATOM   4357 H H    . LYS   B 1 29  ? 53.128 -21.349 -14.613 1.00 23.04 ?  29  LYS   B H    1 
ATOM   4358 H HA   . LYS   B 1 29  ? 53.918 -20.517 -17.033 1.00 25.86 ?  29  LYS   B HA   1 
ATOM   4359 H HB2  . LYS   B 1 29  ? 53.794 -22.821 -16.576 1.00 31.11 ?  29  LYS   B HB2  1 
ATOM   4360 H HB3  . LYS   B 1 29  ? 52.219 -22.687 -16.439 1.00 31.11 ?  29  LYS   B HB3  1 
ATOM   4361 H HG2  . LYS   B 1 29  ? 51.955 -22.379 -18.647 1.00 35.81 ?  29  LYS   B HG2  1 
ATOM   4362 H HG3  . LYS   B 1 29  ? 53.502 -22.072 -18.860 1.00 35.81 ?  29  LYS   B HG3  1 
ATOM   4363 H HD2  . LYS   B 1 29  ? 53.078 -24.187 -19.674 1.00 39.51 ?  29  LYS   B HD2  1 
ATOM   4364 H HD3  . LYS   B 1 29  ? 53.965 -24.343 -18.363 1.00 39.51 ?  29  LYS   B HD3  1 
ATOM   4365 H HE2  . LYS   B 1 29  ? 52.053 -24.880 -17.136 1.00 42.02 ?  29  LYS   B HE2  1 
ATOM   4366 H HE3  . LYS   B 1 29  ? 51.171 -24.730 -18.452 1.00 42.02 ?  29  LYS   B HE3  1 
ATOM   4367 H HZ1  . LYS   B 1 29  ? 51.654 -26.919 -18.059 1.00 43.45 ?  29  LYS   B HZ1  1 
ATOM   4368 H HZ2  . LYS   B 1 29  ? 52.275 -26.530 -19.308 1.00 43.45 ?  29  LYS   B HZ2  1 
ATOM   4369 H HZ3  . LYS   B 1 29  ? 53.079 -26.664 -18.110 1.00 43.45 ?  29  LYS   B HZ3  1 
ATOM   4370 N N    . VAL   B 1 30  ? 50.849 -20.150 -16.171 1.00 18.95 ?  30  VAL   B N    1 
ATOM   4371 C CA   . VAL   B 1 30  ? 49.558 -19.566 -16.544 1.00 19.36 ?  30  VAL   B CA   1 
ATOM   4372 C C    . VAL   B 1 30  ? 49.550 -18.052 -16.388 1.00 18.42 ?  30  VAL   B C    1 
ATOM   4373 O O    . VAL   B 1 30  ? 48.807 -17.349 -17.091 1.00 19.16 ?  30  VAL   B O    1 
ATOM   4374 C CB   . VAL   B 1 30  ? 48.454 -20.192 -15.667 1.00 20.64 ?  30  VAL   B CB   1 
ATOM   4375 C CG1  . VAL   B 1 30  ? 47.166 -19.373 -15.727 1.00 20.66 ?  30  VAL   B CG1  1 
ATOM   4376 C CG2  . VAL   B 1 30  ? 48.203 -21.643 -16.068 1.00 21.46 ?  30  VAL   B CG2  1 
ATOM   4377 H H    . VAL   B 1 30  ? 50.838 -20.550 -15.398 1.00 22.73 ?  30  VAL   B H    1 
ATOM   4378 H HA   . VAL   B 1 30  ? 49.365 -19.798 -17.467 1.00 23.22 ?  30  VAL   B HA   1 
ATOM   4379 H HB   . VAL   B 1 30  ? 48.751 -20.202 -14.744 1.00 24.76 ?  30  VAL   B HB   1 
ATOM   4380 H HG11 . VAL   B 1 30  ? 46.423 -19.947 -15.482 1.00 24.78 ?  30  VAL   B HG11 1 
ATOM   4381 H HG12 . VAL   B 1 30  ? 47.228 -18.636 -15.102 1.00 24.78 ?  30  VAL   B HG12 1 
ATOM   4382 H HG13 . VAL   B 1 30  ? 47.036 -19.049 -16.628 1.00 24.78 ?  30  VAL   B HG13 1 
ATOM   4383 H HG21 . VAL   B 1 30  ? 47.507 -22.018 -15.497 1.00 25.74 ?  30  VAL   B HG21 1 
ATOM   4384 H HG22 . VAL   B 1 30  ? 47.912 -21.672 -16.994 1.00 25.74 ?  30  VAL   B HG22 1 
ATOM   4385 H HG23 . VAL   B 1 30  ? 49.020 -22.150 -15.960 1.00 25.74 ?  30  VAL   B HG23 1 
ATOM   4386 N N    . LYS   B 1 31  ? 50.330 -17.542 -15.450 1.00 18.01 ?  31  LYS   B N    1 
ATOM   4387 C CA   . LYS   B 1 31  ? 50.355 -16.133 -15.091 1.00 18.51 ?  31  LYS   B CA   1 
ATOM   4388 C C    . LYS   B 1 31  ? 48.954 -15.665 -14.697 1.00 16.23 ?  31  LYS   B C    1 
ATOM   4389 O O    . LYS   B 1 31  ? 48.405 -14.750 -15.323 1.00 17.29 ?  31  LYS   B O    1 
ATOM   4390 C CB   . LYS   B 1 31  ? 50.980 -15.312 -16.227 1.00 21.59 ?  31  LYS   B CB   1 
ATOM   4391 C CG   . LYS   B 1 31  ? 52.397 -15.771 -16.589 1.00 24.75 ?  31  LYS   B CG   1 
ATOM   4392 C CD   . LYS   B 1 31  ? 52.990 -14.948 -17.713 1.00 27.86 ?  31  LYS   B CD   1 
ATOM   4393 C CE   . LYS   B 1 31  ? 54.473 -15.210 -17.860 1.00 30.24 ?  31  LYS   B CE   1 
ATOM   4394 N NZ   . LYS   B 1 31  ? 55.210 -14.833 -16.621 1.00 31.31 ?  31  LYS   B NZ   1 
ATOM   4395 H H    . LYS   B 1 31  ? 50.882 -18.025 -15.002 1.00 21.61 ?  31  LYS   B H    1 
ATOM   4396 H HA   . LYS   B 1 31  ? 50.915 -16.045 -14.321 1.00 22.20 ?  31  LYS   B HA   1 
ATOM   4397 H HB2  . LYS   B 1 31  ? 50.429 -15.392 -17.023 1.00 25.90 ?  31  LYS   B HB2  1 
ATOM   4398 H HB3  . LYS   B 1 31  ? 51.028 -14.389 -15.946 1.00 25.90 ?  31  LYS   B HB3  1 
ATOM   4399 H HG2  . LYS   B 1 31  ? 52.964 -15.685 -15.807 1.00 29.69 ?  31  LYS   B HG2  1 
ATOM   4400 H HG3  . LYS   B 1 31  ? 52.368 -16.701 -16.876 1.00 29.69 ?  31  LYS   B HG3  1 
ATOM   4401 H HD2  . LYS   B 1 31  ? 52.551 -15.186 -18.545 1.00 33.42 ?  31  LYS   B HD2  1 
ATOM   4402 H HD3  . LYS   B 1 31  ? 52.860 -14.009 -17.519 1.00 33.42 ?  31  LYS   B HD3  1 
ATOM   4403 H HE2  . LYS   B 1 31  ? 54.620 -16.155 -18.026 1.00 36.27 ?  31  LYS   B HE2  1 
ATOM   4404 H HE3  . LYS   B 1 31  ? 54.821 -14.681 -18.595 1.00 36.27 ?  31  LYS   B HE3  1 
ATOM   4405 H HZ1  . LYS   B 1 31  ? 56.087 -14.857 -16.768 1.00 37.57 ?  31  LYS   B HZ1  1 
ATOM   4406 H HZ2  . LYS   B 1 31  ? 54.981 -14.010 -16.370 1.00 37.57 ?  31  LYS   B HZ2  1 
ATOM   4407 H HZ3  . LYS   B 1 31  ? 55.013 -15.400 -15.963 1.00 37.57 ?  31  LYS   B HZ3  1 
ATOM   4408 N N    . PRO   B 1 32  ? 48.346 -16.269 -13.664 1.00 13.70 ?  32  PRO   B N    1 
ATOM   4409 C CA   . PRO   B 1 32  ? 46.965 -15.916 -13.304 1.00 12.69 ?  32  PRO   B CA   1 
ATOM   4410 C C    . PRO   B 1 32  ? 46.882 -14.569 -12.607 1.00 12.94 ?  32  PRO   B C    1 
ATOM   4411 O O    . PRO   B 1 32  ? 47.807 -14.144 -11.908 1.00 14.28 ?  32  PRO   B O    1 
ATOM   4412 C CB   . PRO   B 1 32  ? 46.569 -17.031 -12.329 1.00 12.91 ?  32  PRO   B CB   1 
ATOM   4413 C CG   . PRO   B 1 32  ? 47.878 -17.380 -11.662 1.00 13.14 ?  32  PRO   B CG   1 
ATOM   4414 C CD   . PRO   B 1 32  ? 48.920 -17.265 -12.737 1.00 13.55 ?  32  PRO   B CD   1 
ATOM   4415 H HA   . PRO   B 1 32  ? 46.380 -15.931 -14.082 1.00 15.22 ?  32  PRO   B HA   1 
ATOM   4416 H HB2  . PRO   B 1 32  ? 45.926 -16.696 -11.681 1.00 15.48 ?  32  PRO   B HB2  1 
ATOM   4417 H HB3  . PRO   B 1 32  ? 46.212 -17.791 -12.813 1.00 15.48 ?  32  PRO   B HB3  1 
ATOM   4418 H HG2  . PRO   B 1 32  ? 48.060 -16.750 -10.944 1.00 15.76 ?  32  PRO   B HG2  1 
ATOM   4419 H HG3  . PRO   B 1 32  ? 47.843 -18.286 -11.318 1.00 15.76 ?  32  PRO   B HG3  1 
ATOM   4420 H HD2  . PRO   B 1 32  ? 49.752 -16.935 -12.368 1.00 16.25 ?  32  PRO   B HD2  1 
ATOM   4421 H HD3  . PRO   B 1 32  ? 49.036 -18.116 -13.184 1.00 16.25 ?  32  PRO   B HD3  1 
ATOM   4422 N N    . THR   B 1 33  ? 45.730 -13.915 -12.773 1.00 12.59 ?  33  THR   B N    1 
ATOM   4423 C CA   . THR   B 1 33  ? 45.436 -12.738 -11.963 1.00 12.67 ?  33  THR   B CA   1 
ATOM   4424 C C    . THR   B 1 33  ? 45.387 -13.093 -10.483 1.00 12.17 ?  33  THR   B C    1 
ATOM   4425 O O    . THR   B 1 33  ? 45.849 -12.311 -9.638  1.00 12.99 ?  33  THR   B O    1 
ATOM   4426 C CB   . THR   B 1 33  ? 44.116 -12.105 -12.409 1.00 13.32 ?  33  THR   B CB   1 
ATOM   4427 O OG1  . THR   B 1 33  ? 44.151 -11.854 -13.815 1.00 13.49 ?  33  THR   B OG1  1 
ATOM   4428 C CG2  . THR   B 1 33  ? 43.862 -10.801 -11.668 1.00 14.58 ?  33  THR   B CG2  1 
ATOM   4429 H H    . THR   B 1 33  ? 45.110 -14.133 -13.335 1.00 15.09 ?  33  THR   B H    1 
ATOM   4430 H HA   . THR   B 1 33  ? 46.134 -12.086 -12.093 1.00 15.20 ?  33  THR   B HA   1 
ATOM   4431 H HB   . THR   B 1 33  ? 43.380 -12.711 -12.214 1.00 15.98 ?  33  THR   B HB   1 
ATOM   4432 H HG1  . THR   B 1 33  ? 43.425 -11.491 -14.067 1.00 16.17 ?  33  THR   B HG1  1 
ATOM   4433 H HG21 . THR   B 1 33  ? 43.101 -10.341 -12.054 1.00 17.49 ?  33  THR   B HG21 1 
ATOM   4434 H HG22 . THR   B 1 33  ? 43.681 -10.980 -10.732 1.00 17.49 ?  33  THR   B HG22 1 
ATOM   4435 H HG23 . THR   B 1 33  ? 44.643 -10.228 -11.734 1.00 17.49 ?  33  THR   B HG23 1 
ATOM   4436 N N    . VAL   B 1 34  ? 44.842 -14.266 -10.147 1.00 11.59 ?  34  VAL   B N    1 
ATOM   4437 C CA   . VAL   B 1 34  ? 44.647 -14.664 -8.757  1.00 10.99 ?  34  VAL   B CA   1 
ATOM   4438 C C    . VAL   B 1 34  ? 45.079 -16.112 -8.592  1.00 10.17 ?  34  VAL   B C    1 
ATOM   4439 O O    . VAL   B 1 34  ? 44.560 -17.000 -9.279  1.00 10.87 ?  34  VAL   B O    1 
ATOM   4440 C CB   . VAL   B 1 34  ? 43.178 -14.525 -8.313  1.00 11.95 ?  34  VAL   B CB   1 
ATOM   4441 C CG1  . VAL   B 1 34  ? 43.013 -14.969 -6.868  1.00 12.43 ?  34  VAL   B CG1  1 
ATOM   4442 C CG2  . VAL   B 1 34  ? 42.677 -13.100 -8.520  1.00 12.95 ?  34  VAL   B CG2  1 
ATOM   4443 H H    . VAL   B 1 34  ? 44.590 -14.862 -10.716 1.00 13.90 ?  34  VAL   B H    1 
ATOM   4444 H HA   . VAL   B 1 34  ? 45.197 -14.110 -8.180  1.00 13.18 ?  34  VAL   B HA   1 
ATOM   4445 H HB   . VAL   B 1 34  ? 42.633 -15.108 -8.868  1.00 14.33 ?  34  VAL   B HB   1 
ATOM   4446 H HG11 . VAL   B 1 34  ? 42.151 -14.659 -6.541  1.00 14.91 ?  34  VAL   B HG11 1 
ATOM   4447 H HG12 . VAL   B 1 34  ? 43.047 -15.938 -6.826  1.00 14.91 ?  34  VAL   B HG12 1 
ATOM   4448 H HG13 . VAL   B 1 34  ? 43.724 -14.586 -6.335  1.00 14.91 ?  34  VAL   B HG13 1 
ATOM   4449 H HG21 . VAL   B 1 34  ? 41.761 -13.038 -8.205  1.00 15.53 ?  34  VAL   B HG21 1 
ATOM   4450 H HG22 . VAL   B 1 34  ? 43.242 -12.490 -8.028  1.00 15.53 ?  34  VAL   B HG22 1 
ATOM   4451 H HG23 . VAL   B 1 34  ? 42.710 -12.888 -9.471  1.00 15.53 ?  34  VAL   B HG23 1 
ATOM   4452 N N    . VAL   B 1 35  ? 45.990 -16.359 -7.654  1.00 9.98  ?  35  VAL   B N    1 
ATOM   4453 C CA   . VAL   B 1 35  ? 46.226 -17.700 -7.131  1.00 9.89  ?  35  VAL   B CA   1 
ATOM   4454 C C    . VAL   B 1 35  ? 45.686 -17.756 -5.711  1.00 9.47  ?  35  VAL   B C    1 
ATOM   4455 O O    . VAL   B 1 35  ? 45.905 -16.832 -4.919  1.00 10.01 ?  35  VAL   B O    1 
ATOM   4456 C CB   . VAL   B 1 35  ? 47.710 -18.119 -7.215  1.00 10.49 ?  35  VAL   B CB   1 
ATOM   4457 C CG1  . VAL   B 1 35  ? 48.607 -17.283 -6.294  1.00 11.02 ?  35  VAL   B CG1  1 
ATOM   4458 C CG2  . VAL   B 1 35  ? 47.859 -19.620 -6.909  1.00 11.11 ?  35  VAL   B CG2  1 
ATOM   4459 H H    . VAL   B 1 35  ? 46.496 -15.754 -7.303  1.00 11.97 ?  35  VAL   B H    1 
ATOM   4460 H HA   . VAL   B 1 35  ? 45.714 -18.331 -7.661  1.00 11.85 ?  35  VAL   B HA   1 
ATOM   4461 H HB   . VAL   B 1 35  ? 48.015 -17.983 -8.127  1.00 12.58 ?  35  VAL   B HB   1 
ATOM   4462 H HG11 . VAL   B 1 35  ? 49.529 -17.504 -6.473  1.00 13.21 ?  35  VAL   B HG11 1 
ATOM   4463 H HG12 . VAL   B 1 35  ? 48.439 -16.348 -6.464  1.00 13.21 ?  35  VAL   B HG12 1 
ATOM   4464 H HG13 . VAL   B 1 35  ? 48.386 -17.499 -5.370  1.00 13.21 ?  35  VAL   B HG13 1 
ATOM   4465 H HG21 . VAL   B 1 35  ? 48.787 -19.878 -7.007  1.00 13.32 ?  35  VAL   B HG21 1 
ATOM   4466 H HG22 . VAL   B 1 35  ? 47.563 -19.793 -5.998  1.00 13.32 ?  35  VAL   B HG22 1 
ATOM   4467 H HG23 . VAL   B 1 35  ? 47.308 -20.133 -7.529  1.00 13.32 ?  35  VAL   B HG23 1 
ATOM   4468 N N    . VAL   B 1 36  ? 44.967 -18.832 -5.394  1.00 9.48  ?  36  VAL   B N    1 
ATOM   4469 C CA   . VAL   B 1 36  ? 44.422 -19.041 -4.062  1.00 9.12  ?  36  VAL   B CA   1 
ATOM   4470 C C    . VAL   B 1 36  ? 45.433 -19.804 -3.213  1.00 8.99  ?  36  VAL   B C    1 
ATOM   4471 O O    . VAL   B 1 36  ? 45.974 -20.835 -3.638  1.00 10.19 ?  36  VAL   B O    1 
ATOM   4472 C CB   . VAL   B 1 36  ? 43.088 -19.804 -4.140  1.00 9.64  ?  36  VAL   B CB   1 
ATOM   4473 C CG1  . VAL   B 1 36  ? 42.582 -20.163 -2.751  1.00 10.40 ?  36  VAL   B CG1  1 
ATOM   4474 C CG2  . VAL   B 1 36  ? 42.060 -18.974 -4.892  1.00 10.24 ?  36  VAL   B CG2  1 
ATOM   4475 H H    . VAL   B 1 36  ? 44.781 -19.462 -5.950  1.00 11.36 ?  36  VAL   B H    1 
ATOM   4476 H HA   . VAL   B 1 36  ? 44.255 -18.181 -3.644  1.00 10.94 ?  36  VAL   B HA   1 
ATOM   4477 H HB   . VAL   B 1 36  ? 43.226 -20.629 -4.633  1.00 11.56 ?  36  VAL   B HB   1 
ATOM   4478 H HG11 . VAL   B 1 36  ? 41.645 -20.405 -2.813  1.00 12.47 ?  36  VAL   B HG11 1 
ATOM   4479 H HG12 . VAL   B 1 36  ? 43.096 -20.903 -2.405  1.00 12.47 ?  36  VAL   B HG12 1 
ATOM   4480 H HG13 . VAL   B 1 36  ? 42.681 -19.386 -2.173  1.00 12.47 ?  36  VAL   B HG13 1 
ATOM   4481 H HG21 . VAL   B 1 36  ? 41.219 -19.452 -4.910  1.00 12.28 ?  36  VAL   B HG21 1 
ATOM   4482 H HG22 . VAL   B 1 36  ? 41.951 -18.123 -4.442  1.00 12.28 ?  36  VAL   B HG22 1 
ATOM   4483 H HG23 . VAL   B 1 36  ? 42.376 -18.827 -5.801  1.00 12.28 ?  36  VAL   B HG23 1 
ATOM   4484 N N    . ASN   B 1 37  ? 45.653 -19.316 -1.996  1.00 9.33  ?  37  ASN   B N    1 
ATOM   4485 C CA   . ASN   B 1 37  ? 46.409 -20.040 -0.990  1.00 9.61  ?  37  ASN   B CA   1 
ATOM   4486 C C    . ASN   B 1 37  ? 45.461 -20.712 -0.006  1.00 9.54  ?  37  ASN   B C    1 
ATOM   4487 O O    . ASN   B 1 37  ? 44.451 -20.136 0.408   1.00 10.07 ?  37  ASN   B O    1 
ATOM   4488 C CB   . ASN   B 1 37  ? 47.337 -19.093 -0.231  1.00 9.81  ?  37  ASN   B CB   1 
ATOM   4489 C CG   . ASN   B 1 37  ? 48.188 -19.807 0.782   1.00 10.01 ?  37  ASN   B CG   1 
ATOM   4490 O OD1  . ASN   B 1 37  ? 48.531 -20.981 0.604   1.00 10.63 ?  37  ASN   B OD1  1 
ATOM   4491 N ND2  . ASN   B 1 37  ? 48.535 -19.112 1.856   1.00 10.22 ?  37  ASN   B ND2  1 
ATOM   4492 H H    . ASN   B 1 37  ? 45.366 -18.552 -1.719  1.00 11.19 ?  37  ASN   B H    1 
ATOM   4493 H HA   . ASN   B 1 37  ? 46.943 -20.732 -1.411  1.00 11.52 ?  37  ASN   B HA   1 
ATOM   4494 H HB2  . ASN   B 1 37  ? 47.929 -18.665 -0.867  1.00 11.77 ?  37  ASN   B HB2  1 
ATOM   4495 H HB3  . ASN   B 1 37  ? 46.808 -18.434 0.236   1.00 11.77 ?  37  ASN   B HB3  1 
ATOM   4496 H HD21 . ASN   B 1 37  ? 49.019 -19.481 2.467   1.00 12.25 ?  37  ASN   B HD21 1 
ATOM   4497 H HD22 . ASN   B 1 37  ? 48.273 -18.308 1.950   1.00 12.25 ?  37  ASN   B HD22 1 
ATOM   4498 N N    . ALA   B 1 38  ? 45.813 -21.940 0.373   1.00 9.74  ?  38  ALA   B N    1 
ATOM   4499 C CA   . ALA   B 1 38  ? 45.154 -22.686 1.445   1.00 10.11 ?  38  ALA   B CA   1 
ATOM   4500 C C    . ALA   B 1 38  ? 45.741 -22.202 2.768   1.00 10.21 ?  38  ALA   B C    1 
ATOM   4501 O O    . ALA   B 1 38  ? 46.642 -22.813 3.355   1.00 11.00 ?  38  ALA   B O    1 
ATOM   4502 C CB   . ALA   B 1 38  ? 45.374 -24.182 1.256   1.00 11.43 ?  38  ALA   B CB   1 
ATOM   4503 H H    . ALA   B 1 38  ? 46.467 -22.372 0.027   1.00 11.68 ?  38  ALA   B H    1 
ATOM   4504 H HA   . ALA   B 1 38  ? 44.199 -22.505 1.440   1.00 12.13 ?  38  ALA   B HA   1 
ATOM   4505 H HB1  . ALA   B 1 38  ? 44.922 -24.663 1.976   1.00 13.70 ?  38  ALA   B HB1  1 
ATOM   4506 H HB2  . ALA   B 1 38  ? 44.997 -24.452 0.403   1.00 13.70 ?  38  ALA   B HB2  1 
ATOM   4507 H HB3  . ALA   B 1 38  ? 46.320 -24.372 1.279   1.00 13.70 ?  38  ALA   B HB3  1 
ATOM   4508 N N    . ALA   B 1 39  ? 45.225 -21.063 3.229   1.00 10.09 ?  39  ALA   B N    1 
ATOM   4509 C CA   . ALA   B 1 39  ? 45.777 -20.332 4.358   1.00 10.49 ?  39  ALA   B CA   1 
ATOM   4510 C C    . ALA   B 1 39  ? 45.155 -20.784 5.680   1.00 10.18 ?  39  ALA   B C    1 
ATOM   4511 O O    . ALA   B 1 39  ? 44.127 -21.465 5.724   1.00 11.22 ?  39  ALA   B O    1 
ATOM   4512 C CB   . ALA   B 1 39  ? 45.534 -18.829 4.167   1.00 11.20 ?  39  ALA   B CB   1 
ATOM   4513 H H    . ALA   B 1 39  ? 44.528 -20.688 2.890   1.00 12.10 ?  39  ALA   B H    1 
ATOM   4514 H HA   . ALA   B 1 39  ? 46.730 -20.484 4.402   1.00 12.58 ?  39  ALA   B HA   1 
ATOM   4515 H HB1  . ALA   B 1 39  ? 45.909 -18.351 4.924   1.00 13.43 ?  39  ALA   B HB1  1 
ATOM   4516 H HB2  . ALA   B 1 39  ? 45.971 -18.542 3.348   1.00 13.43 ?  39  ALA   B HB2  1 
ATOM   4517 H HB3  . ALA   B 1 39  ? 44.582 -18.664 4.108   1.00 13.43 ?  39  ALA   B HB3  1 
ATOM   4518 N N    . ASN   B 1 40  ? 45.794 -20.358 6.769   1.00 11.04 ?  40  ASN   B N    1 
ATOM   4519 C CA   . ASN   B 1 40  ? 45.236 -20.411 8.110   1.00 11.69 ?  40  ASN   B CA   1 
ATOM   4520 C C    . ASN   B 1 40  ? 45.061 -18.984 8.635   1.00 11.23 ?  40  ASN   B C    1 
ATOM   4521 O O    . ASN   B 1 40  ? 45.465 -18.003 8.004   1.00 11.39 ?  40  ASN   B O    1 
ATOM   4522 C CB   . ASN   B 1 40  ? 46.087 -21.286 9.048   1.00 12.68 ?  40  ASN   B CB   1 
ATOM   4523 C CG   . ASN   B 1 40  ? 47.543 -20.884 9.070   1.00 13.63 ?  40  ASN   B CG   1 
ATOM   4524 O OD1  . ASN   B 1 40  ? 47.864 -19.703 9.132   1.00 15.44 ?  40  ASN   B OD1  1 
ATOM   4525 N ND2  . ASN   B 1 40  ? 48.434 -21.863 9.025   1.00 13.84 ?  40  ASN   B ND2  1 
ATOM   4526 H H    . ASN   B 1 40  ? 46.589 -20.025 6.747   1.00 13.23 ?  40  ASN   B H    1 
ATOM   4527 H HA   . ASN   B 1 40  ? 44.355 -20.809 8.064   1.00 14.02 ?  40  ASN   B HA   1 
ATOM   4528 H HB2  . ASN   B 1 40  ? 45.741 -21.209 9.951   1.00 15.21 ?  40  ASN   B HB2  1 
ATOM   4529 H HB3  . ASN   B 1 40  ? 46.034 -22.208 8.751   1.00 15.21 ?  40  ASN   B HB3  1 
ATOM   4530 H HD21 . ASN   B 1 40  ? 49.276 -21.682 9.035   1.00 16.60 ?  40  ASN   B HD21 1 
ATOM   4531 H HD22 . ASN   B 1 40  ? 48.172 -22.681 8.984   1.00 16.60 ?  40  ASN   B HD22 1 
ATOM   4532 N N    . VAL   B 1 41  ? 44.406 -18.857 9.791   1.00 11.78 ?  41  VAL   B N    1 
ATOM   4533 C CA   . VAL   B 1 41  ? 43.948 -17.536 10.231  1.00 12.52 ?  41  VAL   B CA   1 
ATOM   4534 C C    . VAL   B 1 41  ? 45.100 -16.585 10.540  1.00 12.30 ?  41  VAL   B C    1 
ATOM   4535 O O    . VAL   B 1 41  ? 44.923 -15.363 10.477  1.00 12.50 ?  41  VAL   B O    1 
ATOM   4536 C CB   . VAL   B 1 41  ? 42.969 -17.618 11.418  1.00 14.03 ?  41  VAL   B CB   1 
ATOM   4537 C CG1  . VAL   B 1 41  ? 41.675 -18.304 11.013  1.00 14.49 ?  41  VAL   B CG1  1 
ATOM   4538 C CG2  . VAL   B 1 41  ? 43.618 -18.308 12.604  1.00 15.16 ?  41  VAL   B CG2  1 
ATOM   4539 H H    . VAL   B 1 41  ? 44.219 -19.500 10.324  1.00 14.13 ?  41  VAL   B H    1 
ATOM   4540 H HA   . VAL   B 1 41  ? 43.453 -17.139 9.497   1.00 15.02 ?  41  VAL   B HA   1 
ATOM   4541 H HB   . VAL   B 1 41  ? 42.742 -16.715 11.694  1.00 16.83 ?  41  VAL   B HB   1 
ATOM   4542 H HG11 . VAL   B 1 41  ? 41.069 -18.313 11.771  1.00 17.38 ?  41  VAL   B HG11 1 
ATOM   4543 H HG12 . VAL   B 1 41  ? 41.275 -17.819 10.275  1.00 17.38 ?  41  VAL   B HG12 1 
ATOM   4544 H HG13 . VAL   B 1 41  ? 41.874 -19.215 10.741  1.00 17.38 ?  41  VAL   B HG13 1 
ATOM   4545 H HG21 . VAL   B 1 41  ? 42.986 -18.335 13.337  1.00 18.18 ?  41  VAL   B HG21 1 
ATOM   4546 H HG22 . VAL   B 1 41  ? 43.866 -19.210 12.347  1.00 18.18 ?  41  VAL   B HG22 1 
ATOM   4547 H HG23 . VAL   B 1 41  ? 44.409 -17.810 12.865  1.00 18.18 ?  41  VAL   B HG23 1 
ATOM   4548 N N    . TYR   B 1 42  ? 46.267 -17.106 10.915  1.00 12.77 ?  42  TYR   B N    1 
ATOM   4549 C CA   . TYR   B 1 42  ? 47.425 -16.264 11.188  1.00 13.49 ?  42  TYR   B CA   1 
ATOM   4550 C C    . TYR   B 1 42  ? 48.387 -16.186 10.007  1.00 12.42 ?  42  TYR   B C    1 
ATOM   4551 O O    . TYR   B 1 42  ? 49.473 -15.612 10.139  1.00 13.50 ?  42  TYR   B O    1 
ATOM   4552 C CB   . TYR   B 1 42  ? 48.122 -16.677 12.494  1.00 15.37 ?  42  TYR   B CB   1 
ATOM   4553 C CG   . TYR   B 1 42  ? 47.518 -15.991 13.719  1.00 15.71 ?  42  TYR   B CG   1 
ATOM   4554 C CD1  . TYR   B 1 42  ? 47.743 -14.638 13.959  1.00 15.05 ?  42  TYR   B CD1  1 
ATOM   4555 C CD2  . TYR   B 1 42  ? 46.725 -16.685 14.620  1.00 17.57 ?  42  TYR   B CD2  1 
ATOM   4556 C CE1  . TYR   B 1 42  ? 47.197 -13.999 15.057  1.00 16.30 ?  42  TYR   B CE1  1 
ATOM   4557 C CE2  . TYR   B 1 42  ? 46.176 -16.054 15.727  1.00 17.81 ?  42  TYR   B CE2  1 
ATOM   4558 C CZ   . TYR   B 1 42  ? 46.414 -14.707 15.941  1.00 17.95 ?  42  TYR   B CZ   1 
ATOM   4559 O OH   . TYR   B 1 42  ? 45.878 -14.068 17.041  1.00 20.66 ?  42  TYR   B OH   1 
ATOM   4560 H H    . TYR   B 1 42  ? 46.410 -17.956 11.009  1.00 15.31 ?  42  TYR   B H    1 
ATOM   4561 H HA   . TYR   B 1 42  ? 47.098 -15.368 11.327  1.00 16.18 ?  42  TYR   B HA   1 
ATOM   4562 H HB2  . TYR   B 1 42  ? 48.033 -17.634 12.614  1.00 18.43 ?  42  TYR   B HB2  1 
ATOM   4563 H HB3  . TYR   B 1 42  ? 49.057 -16.431 12.441  1.00 18.43 ?  42  TYR   B HB3  1 
ATOM   4564 H HD1  . TYR   B 1 42  ? 48.274 -14.154 13.360  1.00 18.05 ?  42  TYR   B HD1  1 
ATOM   4565 H HD2  . TYR   B 1 42  ? 46.559 -17.590 14.477  1.00 21.08 ?  42  TYR   B HD2  1 
ATOM   4566 H HE1  . TYR   B 1 42  ? 47.366 -13.095 15.198  1.00 19.55 ?  42  TYR   B HE1  1 
ATOM   4567 H HE2  . TYR   B 1 42  ? 45.646 -16.534 16.320  1.00 21.36 ?  42  TYR   B HE2  1 
ATOM   4568 H HH   . TYR   B 1 42  ? 46.109 -13.262 17.035  1.00 24.79 ?  42  TYR   B HH   1 
ATOM   4569 N N    . LEU   B 1 43  ? 47.988 -16.698 8.847   1.00 11.31 ?  43  LEU   B N    1 
ATOM   4570 C CA   . LEU   B 1 43  ? 48.805 -16.625 7.641   1.00 11.22 ?  43  LEU   B CA   1 
ATOM   4571 C C    . LEU   B 1 43  ? 50.216 -17.134 7.900   1.00 11.65 ?  43  LEU   B C    1 
ATOM   4572 O O    . LEU   B 1 43  ? 51.198 -16.537 7.457   1.00 12.40 ?  43  LEU   B O    1 
ATOM   4573 C CB   . LEU   B 1 43  ? 48.818 -15.218 7.039   1.00 11.74 ?  43  LEU   B CB   1 
ATOM   4574 C CG   . LEU   B 1 43  ? 47.459 -14.611 6.665   1.00 11.80 ?  43  LEU   B CG   1 
ATOM   4575 C CD1  . LEU   B 1 43  ? 47.666 -13.219 6.076   1.00 13.08 ?  43  LEU   B CD1  1 
ATOM   4576 C CD2  . LEU   B 1 43  ? 46.694 -15.506 5.700   1.00 12.05 ?  43  LEU   B CD2  1 
ATOM   4577 H H    . LEU   B 1 43  ? 47.243 -17.114 8.732   1.00 13.56 ?  43  LEU   B H    1 
ATOM   4578 H HA   . LEU   B 1 43  ? 48.407 -17.213 6.974   1.00 13.46 ?  43  LEU   B HA   1 
ATOM   4579 H HB2  . LEU   B 1 43  ? 49.233 -14.619 7.677   1.00 14.08 ?  43  LEU   B HB2  1 
ATOM   4580 H HB3  . LEU   B 1 43  ? 49.350 -15.243 6.227   1.00 14.08 ?  43  LEU   B HB3  1 
ATOM   4581 H HG   . LEU   B 1 43  ? 46.928 -14.517 7.467   1.00 14.15 ?  43  LEU   B HG   1 
ATOM   4582 H HD11 . LEU   B 1 43  ? 46.802 -12.842 5.842   1.00 15.69 ?  43  LEU   B HD11 1 
ATOM   4583 H HD12 . LEU   B 1 43  ? 48.102 -12.656 6.737   1.00 15.69 ?  43  LEU   B HD12 1 
ATOM   4584 H HD13 . LEU   B 1 43  ? 48.221 -13.286 5.283   1.00 15.69 ?  43  LEU   B HD13 1 
ATOM   4585 H HD21 . LEU   B 1 43  ? 45.894 -15.043 5.404   1.00 14.45 ?  43  LEU   B HD21 1 
ATOM   4586 H HD22 . LEU   B 1 43  ? 47.259 -15.710 4.937   1.00 14.45 ?  43  LEU   B HD22 1 
ATOM   4587 H HD23 . LEU   B 1 43  ? 46.449 -16.328 6.156   1.00 14.45 ?  43  LEU   B HD23 1 
ATOM   4588 N N    . LYS   B 1 44  ? 50.315 -18.256 8.612   1.00 11.52 ?  44  LYS   B N    1 
ATOM   4589 C CA   . LYS   B 1 44  ? 51.583 -18.934 8.843   1.00 12.20 ?  44  LYS   B CA   1 
ATOM   4590 C C    . LYS   B 1 44  ? 51.697 -20.050 7.812   1.00 11.79 ?  44  LYS   B C    1 
ATOM   4591 O O    . LYS   B 1 44  ? 50.996 -21.063 7.896   1.00 13.01 ?  44  LYS   B O    1 
ATOM   4592 C CB   . LYS   B 1 44  ? 51.651 -19.452 10.277  1.00 13.73 ?  44  LYS   B CB   1 
ATOM   4593 C CG   . LYS   B 1 44  ? 51.824 -18.342 11.306  1.00 16.26 ?  44  LYS   B CG   1 
ATOM   4594 C CD   . LYS   B 1 44  ? 53.007 -17.455 10.923  1.00 19.21 ?  44  LYS   B CD   1 
ATOM   4595 C CE   . LYS   B 1 44  ? 53.509 -16.610 12.067  1.00 21.68 ?  44  LYS   B CE   1 
ATOM   4596 N NZ   . LYS   B 1 44  ? 54.675 -15.779 11.676  1.00 22.95 ?  44  LYS   B NZ   1 
ATOM   4597 H H    . LYS   B 1 44  ? 49.641 -18.641 8.987   1.00 13.82 ?  44  LYS   B H    1 
ATOM   4598 H HA   . LYS   B 1 44  ? 52.309 -18.313 8.681   1.00 14.63 ?  44  LYS   B HA   1 
ATOM   4599 H HB2  . LYS   B 1 44  ? 50.821 -19.919 10.482  1.00 16.47 ?  44  LYS   B HB2  1 
ATOM   4600 H HB3  . LYS   B 1 44  ? 52.399 -20.056 10.358  1.00 16.47 ?  44  LYS   B HB3  1 
ATOM   4601 H HG2  . LYS   B 1 44  ? 51.023 -17.800 11.339  1.00 19.51 ?  44  LYS   B HG2  1 
ATOM   4602 H HG3  . LYS   B 1 44  ? 52.004 -18.739 12.176  1.00 19.51 ?  44  LYS   B HG3  1 
ATOM   4603 H HD2  . LYS   B 1 44  ? 53.733 -18.025 10.609  1.00 23.04 ?  44  LYS   B HD2  1 
ATOM   4604 H HD3  . LYS   B 1 44  ? 52.727 -16.860 10.210  1.00 23.04 ?  44  LYS   B HD3  1 
ATOM   4605 H HE2  . LYS   B 1 44  ? 52.803 -16.010 12.333  1.00 26.00 ?  44  LYS   B HE2  1 
ATOM   4606 H HE3  . LYS   B 1 44  ? 53.770 -17.188 12.802  1.00 26.00 ?  44  LYS   B HE3  1 
ATOM   4607 H HZ1  . LYS   B 1 44  ? 54.943 -15.289 12.368  1.00 27.54 ?  44  LYS   B HZ1  1 
ATOM   4608 H HZ2  . LYS   B 1 44  ? 55.346 -16.296 11.407  1.00 27.54 ?  44  LYS   B HZ2  1 
ATOM   4609 H HZ3  . LYS   B 1 44  ? 54.447 -15.232 11.008  1.00 27.54 ?  44  LYS   B HZ3  1 
ATOM   4610 N N    . HIS   B 1 45  ? 52.542 -19.827 6.810   1.00 11.42 ?  45  HIS   B N    1 
ATOM   4611 C CA   . HIS   B 1 45  ? 52.562 -20.658 5.608   1.00 11.73 ?  45  HIS   B CA   1 
ATOM   4612 C C    . HIS   B 1 45  ? 53.578 -21.782 5.768   1.00 14.00 ?  45  HIS   B C    1 
ATOM   4613 O O    . HIS   B 1 45  ? 54.637 -21.798 5.150   1.00 16.21 ?  45  HIS   B O    1 
ATOM   4614 C CB   . HIS   B 1 45  ? 52.881 -19.802 4.396   1.00 11.63 ?  45  HIS   B CB   1 
ATOM   4615 C CG   . HIS   B 1 45  ? 52.010 -18.600 4.285   1.00 11.59 ?  45  HIS   B CG   1 
ATOM   4616 N ND1  . HIS   B 1 45  ? 50.632 -18.678 4.248   1.00 11.78 ?  45  HIS   B ND1  1 
ATOM   4617 C CD2  . HIS   B 1 45  ? 52.326 -17.286 4.225   1.00 12.25 ?  45  HIS   B CD2  1 
ATOM   4618 C CE1  . HIS   B 1 45  ? 50.145 -17.455 4.145   1.00 11.48 ?  45  HIS   B CE1  1 
ATOM   4619 N NE2  . HIS   B 1 45  ? 51.148 -16.593 4.129   1.00 12.24 ?  45  HIS   B NE2  1 
ATOM   4620 H H    . HIS   B 1 45  ? 53.113 -19.184 6.796   1.00 13.70 ?  45  HIS   B H    1 
ATOM   4621 H HA   . HIS   B 1 45  ? 51.681 -21.050 5.474   1.00 14.07 ?  45  HIS   B HA   1 
ATOM   4622 H HB2  . HIS   B 1 45  ? 53.801 -19.505 4.451   1.00 13.94 ?  45  HIS   B HB2  1 
ATOM   4623 H HB3  . HIS   B 1 45  ? 52.758 -20.340 3.590   1.00 13.94 ?  45  HIS   B HB3  1 
ATOM   4624 H HD2  . HIS   B 1 45  ? 53.181 -16.920 4.236   1.00 14.69 ?  45  HIS   B HD2  1 
ATOM   4625 H HE1  . HIS   B 1 45  ? 49.241 -17.238 4.084   1.00 13.77 ?  45  HIS   B HE1  1 
ATOM   4626 H HE2  . HIS   B 1 45  ? 51.070 -15.738 4.078   1.00 14.68 ?  45  HIS   B HE2  1 
ATOM   4627 N N    A GLY   B 1 46  ? 53.216 -22.750 6.603   0.88 14.61 ?  46  GLY   B N    1 
ATOM   4628 N N    B GLY   B 1 46  ? 53.221 -22.741 6.615   0.12 14.77 ?  46  GLY   B N    1 
ATOM   4629 C CA   A GLY   B 1 46  ? 54.137 -23.814 6.957   0.88 16.29 ?  46  GLY   B CA   1 
ATOM   4630 C CA   B GLY   B 1 46  ? 54.141 -23.807 6.950   0.12 15.67 ?  46  GLY   B CA   1 
ATOM   4631 C C    A GLY   B 1 46  ? 54.177 -25.012 6.029   0.88 17.96 ?  46  GLY   B C    1 
ATOM   4632 C C    B GLY   B 1 46  ? 54.165 -24.965 5.974   0.12 16.59 ?  46  GLY   B C    1 
ATOM   4633 O O    A GLY   B 1 46  ? 55.243 -25.409 5.551   0.88 21.00 ?  46  GLY   B O    1 
ATOM   4634 O O    B GLY   B 1 46  ? 55.210 -25.268 5.390   0.12 16.96 ?  46  GLY   B O    1 
ATOM   4635 H H    A GLY   B 1 46  ? 52.449 -22.791 7.000   0.88 17.52 ?  46  GLY   B H    1 
ATOM   4636 H H    B GLY   B 1 46  ? 52.455 -22.788 7.012   0.12 17.71 ?  46  GLY   B H    1 
ATOM   4637 H HA2  A GLY   B 1 46  ? 55.030 -23.442 7.010   0.88 19.54 ?  46  GLY   B HA2  1 
ATOM   4638 H HA2  B GLY   B 1 46  ? 55.036 -23.440 6.998   0.12 18.80 ?  46  GLY   B HA2  1 
ATOM   4639 H HA3  A GLY   B 1 46  ? 53.899 -24.144 7.838   0.88 19.54 ?  46  GLY   B HA3  1 
ATOM   4640 H HA3  B GLY   B 1 46  ? 53.911 -24.154 7.824   0.12 18.80 ?  46  GLY   B HA3  1 
ATOM   4641 N N    . GLY   B 1 47  ? 53.021 -25.620 5.782   1.00 17.28 ?  47  GLY   B N    1 
ATOM   4642 C CA   . GLY   B 1 47  ? 52.958 -26.887 5.084   1.00 15.38 ?  47  GLY   B CA   1 
ATOM   4643 C C    . GLY   B 1 47  ? 52.052 -26.860 3.870   1.00 13.24 ?  47  GLY   B C    1 
ATOM   4644 O O    . GLY   B 1 47  ? 51.406 -25.855 3.572   1.00 13.26 ?  47  GLY   B O    1 
ATOM   4645 H H    A GLY   B 1 47  ? 52.254 -25.326 6.037   0.88 20.72 ?  47  GLY   B H    1 
ATOM   4646 H H    B GLY   B 1 47  ? 52.257 -25.338 6.058   0.12 20.72 ?  47  GLY   B H    1 
ATOM   4647 H HA2  . GLY   B 1 47  ? 53.845 -27.144 4.791   1.00 18.45 ?  47  GLY   B HA2  1 
ATOM   4648 H HA3  . GLY   B 1 47  ? 52.633 -27.568 5.694   1.00 18.45 ?  47  GLY   B HA3  1 
ATOM   4649 N N    . GLY   B 1 48  ? 52.005 -28.001 3.184   1.00 12.36 ?  48  GLY   B N    1 
ATOM   4650 C CA   . GLY   B 1 48  ? 51.085 -28.146 2.073   1.00 12.16 ?  48  GLY   B CA   1 
ATOM   4651 C C    . GLY   B 1 48  ? 51.227 -27.033 1.061   1.00 11.59 ?  48  GLY   B C    1 
ATOM   4652 O O    . GLY   B 1 48  ? 52.331 -26.572 0.747   1.00 12.05 ?  48  GLY   B O    1 
ATOM   4653 H H    . GLY   B 1 48  ? 52.496 -28.688 3.337   1.00 14.82 ?  48  GLY   B H    1 
ATOM   4654 H HA2  . GLY   B 1 48  ? 51.245 -28.992 1.629   1.00 14.58 ?  48  GLY   B HA2  1 
ATOM   4655 H HA3  . GLY   B 1 48  ? 50.173 -28.141 2.406   1.00 14.58 ?  48  GLY   B HA3  1 
ATOM   4656 N N    . VAL   B 1 49  ? 50.080 -26.602 0.532   1.00 11.56 ?  49  VAL   B N    1 
ATOM   4657 C CA   . VAL   B 1 49  ? 50.061 -25.573 -0.503  1.00 11.58 ?  49  VAL   B CA   1 
ATOM   4658 C C    . VAL   B 1 49  ? 50.723 -24.289 -0.010  1.00 10.72 ?  49  VAL   B C    1 
ATOM   4659 O O    . VAL   B 1 49  ? 51.509 -23.663 -0.732  1.00 11.53 ?  49  VAL   B O    1 
ATOM   4660 C CB   . VAL   B 1 49  ? 48.617 -25.320 -0.980  1.00 12.90 ?  49  VAL   B CB   1 
ATOM   4661 C CG1  . VAL   B 1 49  ? 48.545 -24.067 -1.839  1.00 12.92 ?  49  VAL   B CG1  1 
ATOM   4662 C CG2  . VAL   B 1 49  ? 48.087 -26.523 -1.747  1.00 14.43 ?  49  VAL   B CG2  1 
ATOM   4663 H H    . VAL   B 1 49  ? 49.296 -26.886 0.754   1.00 13.87 ?  49  VAL   B H    1 
ATOM   4664 H HA   . VAL   B 1 49  ? 50.565 -25.887 -1.270  1.00 13.89 ?  49  VAL   B HA   1 
ATOM   4665 H HB   . VAL   B 1 49  ? 48.048 -25.182 -0.208  1.00 15.47 ?  49  VAL   B HB   1 
ATOM   4666 H HG11 . VAL   B 1 49  ? 47.716 -24.076 -2.343  1.00 15.50 ?  49  VAL   B HG11 1 
ATOM   4667 H HG12 . VAL   B 1 49  ? 48.563 -23.282 -1.261  1.00 15.50 ?  49  VAL   B HG12 1 
ATOM   4668 H HG13 . VAL   B 1 49  ? 49.300 -24.049 -2.444  1.00 15.50 ?  49  VAL   B HG13 1 
ATOM   4669 H HG21 . VAL   B 1 49  ? 47.177 -26.342 -2.033  1.00 17.30 ?  49  VAL   B HG21 1 
ATOM   4670 H HG22 . VAL   B 1 49  ? 48.651 -26.675 -2.524  1.00 17.30 ?  49  VAL   B HG22 1 
ATOM   4671 H HG23 . VAL   B 1 49  ? 48.105 -27.298 -1.168  1.00 17.30 ?  49  VAL   B HG23 1 
ATOM   4672 N N    . ALA   B 1 50  ? 50.383 -23.849 1.203   1.00 10.51 ?  50  ALA   B N    1 
ATOM   4673 C CA   . ALA   B 1 50  ? 50.898 -22.569 1.681   1.00 10.53 ?  50  ALA   B CA   1 
ATOM   4674 C C    . ALA   B 1 50  ? 52.417 -22.598 1.789   1.00 10.86 ?  50  ALA   B C    1 
ATOM   4675 O O    . ALA   B 1 50  ? 53.098 -21.631 1.418   1.00 10.99 ?  50  ALA   B O    1 
ATOM   4676 C CB   . ALA   B 1 50  ? 50.269 -22.213 3.026   1.00 11.06 ?  50  ALA   B CB   1 
ATOM   4677 H H    . ALA   B 1 50  ? 49.871 -24.264 1.755   1.00 12.60 ?  50  ALA   B H    1 
ATOM   4678 H HA   . ALA   B 1 50  ? 50.667 -21.878 1.050   1.00 12.63 ?  50  ALA   B HA   1 
ATOM   4679 H HB1  . ALA   B 1 50  ? 50.623 -21.360 3.328   1.00 13.27 ?  50  ALA   B HB1  1 
ATOM   4680 H HB2  . ALA   B 1 50  ? 49.306 -22.147 2.917   1.00 13.27 ?  50  ALA   B HB2  1 
ATOM   4681 H HB3  . ALA   B 1 50  ? 50.480 -22.904 3.674   1.00 13.27 ?  50  ALA   B HB3  1 
ATOM   4682 N N    . GLY   B 1 51  ? 52.969 -23.692 2.303   1.00 11.47 ?  51  GLY   B N    1 
ATOM   4683 C CA   . GLY   B 1 51  ? 54.414 -23.798 2.374   1.00 12.08 ?  51  GLY   B CA   1 
ATOM   4684 C C    . GLY   B 1 51  ? 55.063 -23.744 1.006   1.00 11.95 ?  51  GLY   B C    1 
ATOM   4685 O O    . GLY   B 1 51  ? 56.100 -23.104 0.826   1.00 12.85 ?  51  GLY   B O    1 
ATOM   4686 H H    . GLY   B 1 51  ? 52.540 -24.375 2.608   1.00 13.75 ?  51  GLY   B H    1 
ATOM   4687 H HA2  . GLY   B 1 51  ? 54.766 -23.069 2.912   1.00 14.49 ?  51  GLY   B HA2  1 
ATOM   4688 H HA3  . GLY   B 1 51  ? 54.660 -24.636 2.798   1.00 14.49 ?  51  GLY   B HA3  1 
ATOM   4689 N N    . ALA   B 1 52  ? 54.458 -24.406 0.020   1.00 11.80 ?  52  ALA   B N    1 
ATOM   4690 C CA   . ALA   B 1 52  ? 55.015 -24.408 -1.326  1.00 12.13 ?  52  ALA   B CA   1 
ATOM   4691 C C    . ALA   B 1 52  ? 54.934 -23.030 -1.977  1.00 11.64 ?  52  ALA   B C    1 
ATOM   4692 O O    . ALA   B 1 52  ? 55.907 -22.576 -2.601  1.00 12.35 ?  52  ALA   B O    1 
ATOM   4693 C CB   . ALA   B 1 52  ? 54.315 -25.455 -2.184  1.00 12.87 ?  52  ALA   B CB   1 
ATOM   4694 H H    . ALA   B 1 52  ? 53.723 -24.847 0.105   1.00 14.15 ?  52  ALA   B H    1 
ATOM   4695 H HA   . ALA   B 1 52  ? 55.952 -24.649 -1.267  1.00 14.54 ?  52  ALA   B HA   1 
ATOM   4696 H HB1  . ALA   B 1 52  ? 54.707 -25.444 -3.072  1.00 15.43 ?  52  ALA   B HB1  1 
ATOM   4697 H HB2  . ALA   B 1 52  ? 54.446 -26.330 -1.779  1.00 15.43 ?  52  ALA   B HB2  1 
ATOM   4698 H HB3  . ALA   B 1 52  ? 53.373 -25.248 -2.231  1.00 15.43 ?  52  ALA   B HB3  1 
ATOM   4699 N N    . LEU   B 1 53  ? 53.788 -22.354 -1.861  1.00 11.08 ?  53  LEU   B N    1 
ATOM   4700 C CA   . LEU   B 1 53  ? 53.679 -21.016 -2.430  1.00 11.36 ?  53  LEU   B CA   1 
ATOM   4701 C C    . LEU   B 1 53  ? 54.684 -20.077 -1.778  1.00 11.05 ?  53  LEU   B C    1 
ATOM   4702 O O    . LEU   B 1 53  ? 55.389 -19.326 -2.462  1.00 11.84 ?  53  LEU   B O    1 
ATOM   4703 C CB   . LEU   B 1 53  ? 52.253 -20.476 -2.266  1.00 11.66 ?  53  LEU   B CB   1 
ATOM   4704 C CG   . LEU   B 1 53  ? 51.128 -21.203 -3.009  1.00 11.97 ?  53  LEU   B CG   1 
ATOM   4705 C CD1  . LEU   B 1 53  ? 49.783 -20.604 -2.651  1.00 13.48 ?  53  LEU   B CD1  1 
ATOM   4706 C CD2  . LEU   B 1 53  ? 51.339 -21.162 -4.519  1.00 13.76 ?  53  LEU   B CD2  1 
ATOM   4707 H H    . LEU   B 1 53  ? 53.079 -22.643 -1.466  1.00 13.28 ?  53  LEU   B H    1 
ATOM   4708 H HA   . LEU   B 1 53  ? 53.877 -21.061 -3.382  1.00 13.62 ?  53  LEU   B HA   1 
ATOM   4709 H HB2  . LEU   B 1 53  ? 52.031 -20.504 -1.325  1.00 13.99 ?  53  LEU   B HB2  1 
ATOM   4710 H HB3  . LEU   B 1 53  ? 52.243 -19.559 -2.573  1.00 13.99 ?  53  LEU   B HB3  1 
ATOM   4711 H HG   . LEU   B 1 53  ? 51.114 -22.134 -2.736  1.00 14.35 ?  53  LEU   B HG   1 
ATOM   4712 H HD11 . LEU   B 1 53  ? 49.086 -21.081 -3.130  1.00 16.17 ?  53  LEU   B HD11 1 
ATOM   4713 H HD12 . LEU   B 1 53  ? 49.644 -20.694 -1.694  1.00 16.17 ?  53  LEU   B HD12 1 
ATOM   4714 H HD13 . LEU   B 1 53  ? 49.777 -19.669 -2.901  1.00 16.17 ?  53  LEU   B HD13 1 
ATOM   4715 H HD21 . LEU   B 1 53  ? 50.610 -21.628 -4.956  1.00 16.50 ?  53  LEU   B HD21 1 
ATOM   4716 H HD22 . LEU   B 1 53  ? 51.359 -20.236 -4.810  1.00 16.50 ?  53  LEU   B HD22 1 
ATOM   4717 H HD23 . LEU   B 1 53  ? 52.181 -21.593 -4.732  1.00 16.50 ?  53  LEU   B HD23 1 
ATOM   4718 N N    . ASN   B 1 54  ? 54.771 -20.108 -0.451  1.00 10.81 ?  54  ASN   B N    1 
ATOM   4719 C CA   . ASN   B 1 54  ? 55.688 -19.199 0.220   1.00 11.49 ?  54  ASN   B CA   1 
ATOM   4720 C C    . ASN   B 1 54  ? 57.131 -19.474 -0.184  1.00 11.95 ?  54  ASN   B C    1 
ATOM   4721 O O    . ASN   B 1 54  ? 57.905 -18.537 -0.416  1.00 12.33 ?  54  ASN   B O    1 
ATOM   4722 C CB   . ASN   B 1 54  ? 55.531 -19.281 1.729   1.00 12.23 ?  54  ASN   B CB   1 
ATOM   4723 C CG   . ASN   B 1 54  ? 56.510 -18.369 2.438   1.00 12.42 ?  54  ASN   B CG   1 
ATOM   4724 O OD1  . ASN   B 1 54  ? 56.522 -17.157 2.202   1.00 12.55 ?  54  ASN   B OD1  1 
ATOM   4725 N ND2  . ASN   B 1 54  ? 57.368 -18.944 3.273   1.00 13.93 ?  54  ASN   B ND2  1 
ATOM   4726 H H    . ASN   B 1 54  ? 54.322 -20.628 0.065   1.00 12.96 ?  54  ASN   B H    1 
ATOM   4727 H HA   . ASN   B 1 54  ? 55.475 -18.293 -0.053  1.00 13.78 ?  54  ASN   B HA   1 
ATOM   4728 H HB2  . ASN   B 1 54  ? 54.632 -19.002 1.969   1.00 14.67 ?  54  ASN   B HB2  1 
ATOM   4729 H HB3  . ASN   B 1 54  ? 55.693 -20.189 2.018   1.00 14.67 ?  54  ASN   B HB3  1 
ATOM   4730 H HD21 . ASN   B 1 54  ? 57.955 -18.468 3.686   1.00 16.71 ?  54  ASN   B HD21 1 
ATOM   4731 H HD22 . ASN   B 1 54  ? 57.347 -19.797 3.397   1.00 16.71 ?  54  ASN   B HD22 1 
ATOM   4732 N N    . LYS   B 1 55  ? 57.518 -20.750 -0.253  1.00 12.54 ?  55  LYS   B N    1 
ATOM   4733 C CA   . LYS   B 1 55  ? 58.872 -21.092 -0.677  1.00 13.36 ?  55  LYS   B CA   1 
ATOM   4734 C C    . LYS   B 1 55  ? 59.169 -20.544 -2.066  1.00 13.16 ?  55  LYS   B C    1 
ATOM   4735 O O    . LYS   B 1 55  ? 60.268 -20.035 -2.315  1.00 13.70 ?  55  LYS   B O    1 
ATOM   4736 C CB   . LYS   B 1 55  ? 59.065 -22.607 -0.635  1.00 14.75 ?  55  LYS   B CB   1 
ATOM   4737 C CG   . LYS   B 1 55  ? 60.458 -23.060 -1.028  1.00 18.54 ?  55  LYS   B CG   1 
ATOM   4738 C CD   . LYS   B 1 55  ? 60.629 -24.559 -0.851  1.00 21.73 ?  55  LYS   B CD   1 
ATOM   4739 C CE   . LYS   B 1 55  ? 60.611 -24.969 0.620   1.00 24.63 ?  55  LYS   B CE   1 
ATOM   4740 N NZ   . LYS   B 1 55  ? 60.977 -26.392 0.809   1.00 26.16 ?  55  LYS   B NZ   1 
ATOM   4741 H H    . LYS   B 1 55  ? 57.019 -21.422 -0.064  1.00 15.04 ?  55  LYS   B H    1 
ATOM   4742 H HA   . LYS   B 1 55  ? 59.505 -20.693 -0.063  1.00 16.02 ?  55  LYS   B HA   1 
ATOM   4743 H HB2  . LYS   B 1 55  ? 58.894 -22.912 0.268   1.00 17.69 ?  55  LYS   B HB2  1 
ATOM   4744 H HB3  . LYS   B 1 55  ? 58.438 -23.021 -1.247  1.00 17.69 ?  55  LYS   B HB3  1 
ATOM   4745 H HG2  . LYS   B 1 55  ? 60.616 -22.849 -1.962  1.00 22.24 ?  55  LYS   B HG2  1 
ATOM   4746 H HG3  . LYS   B 1 55  ? 61.113 -22.612 -0.469  1.00 22.24 ?  55  LYS   B HG3  1 
ATOM   4747 H HD2  . LYS   B 1 55  ? 59.903 -25.022 -1.299  1.00 26.07 ?  55  LYS   B HD2  1 
ATOM   4748 H HD3  . LYS   B 1 55  ? 61.482 -24.835 -1.226  1.00 26.07 ?  55  LYS   B HD3  1 
ATOM   4749 H HE2  . LYS   B 1 55  ? 61.247 -24.417 1.107   1.00 29.55 ?  55  LYS   B HE2  1 
ATOM   4750 H HE3  . LYS   B 1 55  ? 59.716 -24.831 0.975   1.00 29.55 ?  55  LYS   B HE3  1 
ATOM   4751 H HZ1  . LYS   B 1 55  ? 60.929 -26.604 1.672   1.00 31.39 ?  55  LYS   B HZ1  1 
ATOM   4752 H HZ2  . LYS   B 1 55  ? 60.414 -26.910 0.352   1.00 31.39 ?  55  LYS   B HZ2  1 
ATOM   4753 H HZ3  . LYS   B 1 55  ? 61.803 -26.534 0.518   1.00 31.39 ?  55  LYS   B HZ3  1 
ATOM   4754 N N    . ALA   B 1 56  ? 58.200 -20.628 -2.984  1.00 12.83 ?  56  ALA   B N    1 
ATOM   4755 C CA   . ALA   B 1 56  ? 58.421 -20.120 -4.333  1.00 13.61 ?  56  ALA   B CA   1 
ATOM   4756 C C    . ALA   B 1 56  ? 58.698 -18.624 -4.326  1.00 13.34 ?  56  ALA   B C    1 
ATOM   4757 O O    . ALA   B 1 56  ? 59.427 -18.124 -5.193  1.00 14.42 ?  56  ALA   B O    1 
ATOM   4758 C CB   . ALA   B 1 56  ? 57.223 -20.446 -5.227  1.00 14.47 ?  56  ALA   B CB   1 
ATOM   4759 H H    . ALA   B 1 56  ? 57.417 -20.962 -2.853  1.00 15.39 ?  56  ALA   B H    1 
ATOM   4760 H HA   . ALA   B 1 56  ? 59.198 -20.554 -4.710  1.00 16.32 ?  56  ALA   B HA   1 
ATOM   4761 H HB1  . ALA   B 1 56  ? 57.395 -20.106 -6.124  1.00 17.36 ?  56  ALA   B HB1  1 
ATOM   4762 H HB2  . ALA   B 1 56  ? 57.109 -21.409 -5.260  1.00 17.36 ?  56  ALA   B HB2  1 
ATOM   4763 H HB3  . ALA   B 1 56  ? 56.429 -20.028 -4.865  1.00 17.36 ?  56  ALA   B HB3  1 
ATOM   4764 N N    . THR   B 1 57  ? 58.131 -17.896 -3.361  1.00 13.10 ?  57  THR   B N    1 
ATOM   4765 C CA   . THR   B 1 57  ? 58.366 -16.462 -3.229  1.00 13.25 ?  57  THR   B CA   1 
ATOM   4766 C C    . THR   B 1 57  ? 59.616 -16.139 -2.420  1.00 13.93 ?  57  THR   B C    1 
ATOM   4767 O O    . THR   B 1 57  ? 59.851 -14.966 -2.109  1.00 14.41 ?  57  THR   B O    1 
ATOM   4768 C CB   . THR   B 1 57  ? 57.166 -15.737 -2.587  1.00 12.60 ?  57  THR   B CB   1 
ATOM   4769 O OG1  . THR   B 1 57  ? 57.151 -15.950 -1.167  1.00 12.66 ?  57  THR   B OG1  1 
ATOM   4770 C CG2  . THR   B 1 57  ? 55.843 -16.158 -3.214  1.00 12.45 ?  57  THR   B CG2  1 
ATOM   4771 H H    . THR   B 1 57  ? 57.586 -18.211 -2.770  1.00 15.71 ?  57  THR   B H    1 
ATOM   4772 H HA   . THR   B 1 57  ? 58.483 -16.088 -4.117  1.00 15.89 ?  57  THR   B HA   1 
ATOM   4773 H HB   . THR   B 1 57  ? 57.267 -14.785 -2.750  1.00 15.11 ?  57  THR   B HB   1 
ATOM   4774 H HG1  . THR   B 1 57  ? 57.090 -16.769 -1.001  1.00 15.18 ?  57  THR   B HG1  1 
ATOM   4775 H HG21 . THR   B 1 57  ? 55.119 -15.622 -2.856  1.00 14.93 ?  57  THR   B HG21 1 
ATOM   4776 H HG22 . THR   B 1 57  ? 55.878 -16.042 -4.176  1.00 14.93 ?  57  THR   B HG22 1 
ATOM   4777 H HG23 . THR   B 1 57  ? 55.666 -17.093 -3.019  1.00 14.93 ?  57  THR   B HG23 1 
ATOM   4778 N N    . ASN   B 1 58  ? 60.413 -17.142 -2.061  1.00 14.66 ?  58  ASN   B N    1 
ATOM   4779 C CA   . ASN   B 1 58  ? 61.615 -16.920 -1.262  1.00 17.18 ?  58  ASN   B CA   1 
ATOM   4780 C C    . ASN   B 1 58  ? 61.277 -16.217 0.054   1.00 15.13 ?  58  ASN   B C    1 
ATOM   4781 O O    . ASN   B 1 58  ? 62.013 -15.344 0.525   1.00 15.70 ?  58  ASN   B O    1 
ATOM   4782 C CB   . ASN   B 1 58  ? 62.685 -16.157 -2.048  1.00 24.22 ?  58  ASN   B CB   1 
ATOM   4783 C CG   . ASN   B 1 58  ? 64.056 -16.255 -1.411  1.00 31.91 ?  58  ASN   B CG   1 
ATOM   4784 O OD1  . ASN   B 1 58  ? 64.368 -17.234 -0.733  1.00 34.54 ?  58  ASN   B OD1  1 
ATOM   4785 N ND2  . ASN   B 1 58  ? 64.884 -15.237 -1.623  1.00 36.67 ?  58  ASN   B ND2  1 
ATOM   4786 H H    . ASN   B 1 58  ? 60.274 -17.971 -2.263  1.00 17.58 ?  58  ASN   B H    1 
ATOM   4787 H HA   . ASN   B 1 58  ? 61.990 -17.788 -1.041  1.00 20.60 ?  58  ASN   B HA   1 
ATOM   4788 H HB2  . ASN   B 1 58  ? 62.743 -16.526 -2.946  1.00 29.06 ?  58  ASN   B HB2  1 
ATOM   4789 H HB3  . ASN   B 1 58  ? 62.442 -15.221 -2.090  1.00 29.06 ?  58  ASN   B HB3  1 
ATOM   4790 H HD21 . ASN   B 1 58  ? 65.675 -15.245 -1.285  1.00 43.99 ?  58  ASN   B HD21 1 
ATOM   4791 H HD22 . ASN   B 1 58  ? 64.629 -14.569 -2.101  1.00 43.99 ?  58  ASN   B HD22 1 
ATOM   4792 N N    . ASN   B 1 59  ? 60.155 -16.609 0.659   1.00 14.18 ?  59  ASN   B N    1 
ATOM   4793 C CA   . ASN   B 1 59  ? 59.678 -16.139 1.960   1.00 14.21 ?  59  ASN   B CA   1 
ATOM   4794 C C    . ASN   B 1 59  ? 59.078 -14.735 1.907   1.00 13.57 ?  59  ASN   B C    1 
ATOM   4795 O O    . ASN   B 1 59  ? 58.645 -14.236 2.952   1.00 13.56 ?  59  ASN   B O    1 
ATOM   4796 C CB   . ASN   B 1 59  ? 60.750 -16.196 3.064   1.00 15.19 ?  59  ASN   B CB   1 
ATOM   4797 C CG   . ASN   B 1 59  ? 60.163 -16.390 4.445   1.00 16.13 ?  59  ASN   B CG   1 
ATOM   4798 O OD1  . ASN   B 1 59  ? 59.331 -17.272 4.661   1.00 16.36 ?  59  ASN   B OD1  1 
ATOM   4799 N ND2  . ASN   B 1 59  ? 60.588 -15.561 5.390   1.00 16.75 ?  59  ASN   B ND2  1 
ATOM   4800 H H    . ASN   B 1 59  ? 59.622 -17.191 0.313   1.00 17.01 ?  59  ASN   B H    1 
ATOM   4801 H HA   . ASN   B 1 59  ? 58.970 -16.738 2.241   1.00 17.04 ?  59  ASN   B HA   1 
ATOM   4802 H HB2  . ASN   B 1 59  ? 61.348 -16.940 2.897   1.00 18.21 ?  59  ASN   B HB2  1 
ATOM   4803 H HB3  . ASN   B 1 59  ? 61.246 -15.364 3.073   1.00 18.21 ?  59  ASN   B HB3  1 
ATOM   4804 H HD21 . ASN   B 1 59  ? 60.284 -15.632 6.195   1.00 20.09 ?  59  ASN   B HD21 1 
ATOM   4805 H HD22 . ASN   B 1 59  ? 61.172 -14.960 5.206   1.00 20.09 ?  59  ASN   B HD22 1 
ATOM   4806 N N    . ALA   B 1 60  ? 59.019 -14.084 0.741   1.00 13.31 ?  60  ALA   B N    1 
ATOM   4807 C CA   . ALA   B 1 60  ? 58.424 -12.752 0.679   1.00 13.27 ?  60  ALA   B CA   1 
ATOM   4808 C C    . ALA   B 1 60  ? 56.952 -12.777 1.072   1.00 12.55 ?  60  ALA   B C    1 
ATOM   4809 O O    . ALA   B 1 60  ? 56.450 -11.827 1.688   1.00 12.98 ?  60  ALA   B O    1 
ATOM   4810 C CB   . ALA   B 1 60  ? 58.592 -12.164 -0.721  1.00 14.10 ?  60  ALA   B CB   1 
ATOM   4811 H H    . ALA   B 1 60  ? 59.313 -14.392 -0.005  1.00 15.97 ?  60  ALA   B H    1 
ATOM   4812 H HA   . ALA   B 1 60  ? 58.889 -12.176 1.305   1.00 15.91 ?  60  ALA   B HA   1 
ATOM   4813 H HB1  . ALA   B 1 60  ? 58.195 -11.282 -0.739  1.00 16.91 ?  60  ALA   B HB1  1 
ATOM   4814 H HB2  . ALA   B 1 60  ? 59.541 -12.104 -0.925  1.00 16.91 ?  60  ALA   B HB2  1 
ATOM   4815 H HB3  . ALA   B 1 60  ? 58.153 -12.743 -1.362  1.00 16.91 ?  60  ALA   B HB3  1 
ATOM   4816 N N    . MET   B 1 61  ? 56.243 -13.851 0.726   1.00 12.12 ?  61  MET   B N    1 
ATOM   4817 C CA   . MET   B 1 61  ? 54.847 -13.973 1.124   1.00 11.84 ?  61  MET   B CA   1 
ATOM   4818 C C    . MET   B 1 61  ? 54.714 -13.990 2.646   1.00 11.74 ?  61  MET   B C    1 
ATOM   4819 O O    . MET   B 1 61  ? 53.814 -13.346 3.201   1.00 11.62 ?  61  MET   B O    1 
ATOM   4820 C CB   . MET   B 1 61  ? 54.266 -15.237 0.491   1.00 11.51 ?  61  MET   B CB   1 
ATOM   4821 C CG   . MET   B 1 61  ? 52.825 -15.534 0.902   1.00 11.26 ?  61  MET   B CG   1 
ATOM   4822 S SD   . MET   B 1 61  ? 52.187 -17.037 0.142   1.00 12.05 ?  61  MET   B SD   1 
ATOM   4823 C CE   . MET   B 1 61  ? 51.953 -16.465 -1.538  1.00 13.45 ?  61  MET   B CE   1 
ATOM   4824 H H    . MET   B 1 61  ? 56.543 -14.515 0.264   1.00 14.54 ?  61  MET   B H    1 
ATOM   4825 H HA   . MET   B 1 61  ? 54.353 -13.217 0.770   1.00 14.20 ?  61  MET   B HA   1 
ATOM   4826 H HB2  . MET   B 1 61  ? 54.280 -15.143 -0.476  1.00 13.80 ?  61  MET   B HB2  1 
ATOM   4827 H HB3  . MET   B 1 61  ? 54.809 -15.998 0.752   1.00 13.80 ?  61  MET   B HB3  1 
ATOM   4828 H HG2  . MET   B 1 61  ? 52.783 -15.650 1.866   1.00 13.50 ?  61  MET   B HG2  1 
ATOM   4829 H HG3  . MET   B 1 61  ? 52.257 -14.796 0.632   1.00 13.50 ?  61  MET   B HG3  1 
ATOM   4830 H HE1  . MET   B 1 61  ? 51.569 -17.181 -2.065  1.00 16.13 ?  61  MET   B HE1  1 
ATOM   4831 H HE2  . MET   B 1 61  ? 51.358 -15.699 -1.532  1.00 16.13 ?  61  MET   B HE2  1 
ATOM   4832 H HE3  . MET   B 1 61  ? 52.815 -16.208 -1.908  1.00 16.13 ?  61  MET   B HE3  1 
ATOM   4833 N N    . GLN   B 1 62  ? 55.598 -14.709 3.344   1.00 11.58 ?  62  GLN   B N    1 
ATOM   4834 C CA   . GLN   B 1 62  ? 55.495 -14.767 4.799   1.00 12.01 ?  62  GLN   B CA   1 
ATOM   4835 C C    . GLN   B 1 62  ? 55.776 -13.413 5.435   1.00 12.36 ?  62  GLN   B C    1 
ATOM   4836 O O    . GLN   B 1 62  ? 55.092 -13.015 6.382   1.00 12.77 ?  62  GLN   B O    1 
ATOM   4837 C CB   . GLN   B 1 62  ? 56.447 -15.820 5.362   1.00 12.13 ?  62  GLN   B CB   1 
ATOM   4838 C CG   . GLN   B 1 62  ? 56.222 -16.096 6.841   1.00 12.62 ?  62  GLN   B CG   1 
ATOM   4839 C CD   . GLN   B 1 62  ? 54.848 -16.688 7.082   1.00 12.22 ?  62  GLN   B CD   1 
ATOM   4840 O OE1  . GLN   B 1 62  ? 54.591 -17.833 6.722   1.00 12.67 ?  62  GLN   B OE1  1 
ATOM   4841 N NE2  . GLN   B 1 62  ? 53.939 -15.894 7.638   1.00 12.89 ?  62  GLN   B NE2  1 
ATOM   4842 H H    . GLN   B 1 62  ? 56.241 -15.167 3.001   1.00 13.88 ?  62  GLN   B H    1 
ATOM   4843 H HA   . GLN   B 1 62  ? 54.590 -15.022 5.034   1.00 14.40 ?  62  GLN   B HA   1 
ATOM   4844 H HB2  . GLN   B 1 62  ? 56.324 -16.651 4.878   1.00 14.55 ?  62  GLN   B HB2  1 
ATOM   4845 H HB3  . GLN   B 1 62  ? 57.362 -15.507 5.251   1.00 14.55 ?  62  GLN   B HB3  1 
ATOM   4846 H HG2  . GLN   B 1 62  ? 56.888 -16.736 7.147   1.00 15.13 ?  62  GLN   B HG2  1 
ATOM   4847 H HG3  . GLN   B 1 62  ? 56.296 -15.271 7.339   1.00 15.13 ?  62  GLN   B HG3  1 
ATOM   4848 H HE21 . GLN   B 1 62  ? 54.150 -15.093 7.866   1.00 15.45 ?  62  GLN   B HE21 1 
ATOM   4849 H HE22 . GLN   B 1 62  ? 53.146 -16.190 7.784   1.00 15.45 ?  62  GLN   B HE22 1 
ATOM   4850 N N    . VAL   B 1 63  ? 56.793 -12.700 4.946   1.00 12.93 ?  63  VAL   B N    1 
ATOM   4851 C CA   . VAL   B 1 63  ? 57.098 -11.384 5.502   1.00 13.70 ?  63  VAL   B CA   1 
ATOM   4852 C C    . VAL   B 1 63  ? 55.905 -10.453 5.322   1.00 13.15 ?  63  VAL   B C    1 
ATOM   4853 O O    . VAL   B 1 63  ? 55.491 -9.746  6.251   1.00 13.58 ?  63  VAL   B O    1 
ATOM   4854 C CB   . VAL   B 1 63  ? 58.385 -10.822 4.874   1.00 14.95 ?  63  VAL   B CB   1 
ATOM   4855 C CG1  . VAL   B 1 63  ? 58.620 -9.393  5.335   1.00 15.80 ?  63  VAL   B CG1  1 
ATOM   4856 C CG2  . VAL   B 1 63  ? 59.568 -11.701 5.255   1.00 15.49 ?  63  VAL   B CG2  1 
ATOM   4857 H H    . VAL   B 1 63  ? 57.309 -12.950 4.302   1.00 15.51 ?  63  VAL   B H    1 
ATOM   4858 H HA   . VAL   B 1 63  ? 57.256 -11.480 6.451   1.00 16.43 ?  63  VAL   B HA   1 
ATOM   4859 H HB   . VAL   B 1 63  ? 58.309 -10.825 3.908   1.00 17.93 ?  63  VAL   B HB   1 
ATOM   4860 H HG11 . VAL   B 1 63  ? 59.536 -9.144  5.140   1.00 18.96 ?  63  VAL   B HG11 1 
ATOM   4861 H HG12 . VAL   B 1 63  ? 58.009 -8.805  4.866   1.00 18.96 ?  63  VAL   B HG12 1 
ATOM   4862 H HG13 . VAL   B 1 63  ? 58.463 -9.342  6.293   1.00 18.96 ?  63  VAL   B HG13 1 
ATOM   4863 H HG21 . VAL   B 1 63  ? 60.380 -11.324 4.879   1.00 18.58 ?  63  VAL   B HG21 1 
ATOM   4864 H HG22 . VAL   B 1 63  ? 59.641 -11.731 6.225   1.00 18.58 ?  63  VAL   B HG22 1 
ATOM   4865 H HG23 . VAL   B 1 63  ? 59.427 -12.594 4.908   1.00 18.58 ?  63  VAL   B HG23 1 
ATOM   4866 N N    . GLU   B 1 64  ? 55.337 -10.439 4.116   1.00 12.77 ?  64  GLU   B N    1 
ATOM   4867 C CA   . GLU   B 1 64  ? 54.170 -9.602  3.848   1.00 12.35 ?  64  GLU   B CA   1 
ATOM   4868 C C    . GLU   B 1 64  ? 52.991 -10.006 4.727   1.00 11.90 ?  64  GLU   B C    1 
ATOM   4869 O O    . GLU   B 1 64  ? 52.242 -9.149  5.225   1.00 12.52 ?  64  GLU   B O    1 
ATOM   4870 C CB   . GLU   B 1 64  ? 53.801 -9.746  2.371   1.00 12.49 ?  64  GLU   B CB   1 
ATOM   4871 C CG   . GLU   B 1 64  ? 52.539 -9.010  1.945   1.00 12.62 ?  64  GLU   B CG   1 
ATOM   4872 C CD   . GLU   B 1 64  ? 51.997 -9.509  0.609   1.00 13.44 ?  64  GLU   B CD   1 
ATOM   4873 O OE1  . GLU   B 1 64  ? 52.184 -10.713 0.286   1.00 14.16 ?  64  GLU   B OE1  1 
ATOM   4874 O OE2  . GLU   B 1 64  ? 51.372 -8.695  -0.118  1.00 14.19 -1 64  GLU   B OE2  1 
ATOM   4875 H H    . GLU   B 1 64  ? 55.615 -10.894 3.436   1.00 15.32 ?  64  GLU   B H    1 
ATOM   4876 H HA   . GLU   B 1 64  ? 54.386 -8.675  4.023   1.00 14.81 ?  64  GLU   B HA   1 
ATOM   4877 H HB2  . GLU   B 1 64  ? 54.531 -9.395  1.831   1.00 14.98 ?  64  GLU   B HB2  1 
ATOM   4878 H HB3  . GLU   B 1 64  ? 53.674 -10.683 2.172   1.00 14.98 ?  64  GLU   B HB3  1 
ATOM   4879 H HG2  . GLU   B 1 64  ? 51.844 -9.135  2.613   1.00 15.13 ?  64  GLU   B HG2  1 
ATOM   4880 H HG3  . GLU   B 1 64  ? 52.738 -8.064  1.855   1.00 15.13 ?  64  GLU   B HG3  1 
ATOM   4881 N N    . SER   B 1 65  ? 52.808 -11.314 4.913   1.00 11.71 ?  65  SER   B N    1 
ATOM   4882 C CA   . SER   B 1 65  ? 51.698 -11.819 5.710   1.00 11.71 ?  65  SER   B CA   1 
ATOM   4883 C C    . SER   B 1 65  ? 51.834 -11.420 7.174   1.00 11.85 ?  65  SER   B C    1 
ATOM   4884 O O    . SER   B 1 65  ? 50.836 -11.051 7.811   1.00 12.24 ?  65  SER   B O    1 
ATOM   4885 C CB   . SER   B 1 65  ? 51.610 -13.340 5.573   1.00 11.77 ?  65  SER   B CB   1 
ATOM   4886 O OG   . SER   B 1 65  ? 51.269 -13.731 4.249   1.00 12.20 ?  65  SER   B OG   1 
ATOM   4887 H H    . SER   B 1 65  ? 53.316 -11.934 4.593   1.00 14.05 ?  65  SER   B H    1 
ATOM   4888 H HA   . SER   B 1 65  ? 50.868 -11.443 5.372   1.00 14.05 ?  65  SER   B HA   1 
ATOM   4889 H HB2  . SER   B 1 65  ? 52.466 -13.726 5.802   1.00 14.11 ?  65  SER   B HB2  1 
ATOM   4890 H HB3  . SER   B 1 65  ? 50.926 -13.669 6.181   1.00 14.11 ?  65  SER   B HB3  1 
ATOM   4891 H HG   . SER   B 1 65  ? 51.850 -13.443 3.707   1.00 14.63 ?  65  SER   B HG   1 
ATOM   4892 N N    . ASP   B 1 66  ? 53.042 -11.530 7.739   1.00 12.31 ?  66  ASP   B N    1 
ATOM   4893 C CA   . ASP   B 1 66  ? 53.234 -11.140 9.134   1.00 12.67 ?  66  ASP   B CA   1 
ATOM   4894 C C    . ASP   B 1 66  ? 52.919 -9.661  9.336   1.00 12.82 ?  66  ASP   B C    1 
ATOM   4895 O O    . ASP   B 1 66  ? 52.338 -9.273  10.356  1.00 13.45 ?  66  ASP   B O    1 
ATOM   4896 C CB   . ASP   B 1 66  ? 54.666 -11.449 9.576   1.00 14.18 ?  66  ASP   B CB   1 
ATOM   4897 C CG   . ASP   B 1 66  ? 54.934 -12.941 9.733   1.00 15.82 ?  66  ASP   B CG   1 
ATOM   4898 O OD1  . ASP   B 1 66  ? 53.984 -13.753 9.654   1.00 16.46 ?  66  ASP   B OD1  1 
ATOM   4899 O OD2  . ASP   B 1 66  ? 56.113 -13.302 9.946   1.00 18.22 -1 66  ASP   B OD2  1 
ATOM   4900 H H    . ASP   B 1 66  ? 53.739 -11.831 7.346   1.00 14.76 ?  66  ASP   B H    1 
ATOM   4901 H HA   . ASP   B 1 66  ? 52.633 -11.647 9.697   1.00 15.19 ?  66  ASP   B HA   1 
ATOM   4902 H HB2  . ASP   B 1 66  ? 55.283 -11.104 8.910   1.00 17.01 ?  66  ASP   B HB2  1 
ATOM   4903 H HB3  . ASP   B 1 66  ? 54.831 -11.018 10.431  1.00 17.01 ?  66  ASP   B HB3  1 
ATOM   4904 N N    . ASP   B 1 67  ? 53.300 -8.815  8.377   1.00 12.50 ?  67  ASP   B N    1 
ATOM   4905 C CA   . ASP   B 1 67  ? 52.949 -7.404  8.471   1.00 13.13 ?  67  ASP   B CA   1 
ATOM   4906 C C    . ASP   B 1 67  ? 51.435 -7.200  8.386   1.00 13.16 ?  67  ASP   B C    1 
ATOM   4907 O O    . ASP   B 1 67  ? 50.866 -6.394  9.134   1.00 13.76 ?  67  ASP   B O    1 
ATOM   4908 C CB   . ASP   B 1 67  ? 53.671 -6.624  7.378   1.00 14.41 ?  67  ASP   B CB   1 
ATOM   4909 C CG   . ASP   B 1 67  ? 53.252 -5.184  7.346   1.00 15.36 ?  67  ASP   B CG   1 
ATOM   4910 O OD1  . ASP   B 1 67  ? 53.757 -4.389  8.173   1.00 16.53 ?  67  ASP   B OD1  1 
ATOM   4911 O OD2  . ASP   B 1 67  ? 52.388 -4.871  6.510   1.00 16.65 -1 67  ASP   B OD2  1 
ATOM   4912 H H    . ASP   B 1 67  ? 53.761 -9.028  7.681   1.00 14.99 ?  67  ASP   B H    1 
ATOM   4913 H HA   . ASP   B 1 67  ? 53.250 -7.059  9.324   1.00 15.75 ?  67  ASP   B HA   1 
ATOM   4914 H HB2  . ASP   B 1 67  ? 54.628 -6.649  7.541   1.00 17.28 ?  67  ASP   B HB2  1 
ATOM   4915 H HB3  . ASP   B 1 67  ? 53.475 -7.026  6.513   1.00 17.28 ?  67  ASP   B HB3  1 
ATOM   4916 N N    . TYR   B 1 68  ? 50.761 -7.927  7.487   1.00 12.84 ?  68  TYR   B N    1 
ATOM   4917 C CA   . TYR   B 1 68  ? 49.302 -7.850  7.415   1.00 13.58 ?  68  TYR   B CA   1 
ATOM   4918 C C    . TYR   B 1 68  ? 48.665 -8.197  8.758   1.00 13.10 ?  68  TYR   B C    1 
ATOM   4919 O O    . TYR   B 1 68  ? 47.730 -7.521  9.206   1.00 13.56 ?  68  TYR   B O    1 
ATOM   4920 C CB   . TYR   B 1 68  ? 48.766 -8.780  6.319   1.00 14.37 ?  68  TYR   B CB   1 
ATOM   4921 C CG   . TYR   B 1 68  ? 47.259 -8.934  6.379   1.00 15.57 ?  68  TYR   B CG   1 
ATOM   4922 C CD1  . TYR   B 1 68  ? 46.670 -9.890  7.201   1.00 16.41 ?  68  TYR   B CD1  1 
ATOM   4923 C CD2  . TYR   B 1 68  ? 46.428 -8.098  5.655   1.00 16.61 ?  68  TYR   B CD2  1 
ATOM   4924 C CE1  . TYR   B 1 68  ? 45.305 -10.016 7.289   1.00 17.42 ?  68  TYR   B CE1  1 
ATOM   4925 C CE2  . TYR   B 1 68  ? 45.048 -8.224  5.730   1.00 17.19 ?  68  TYR   B CE2  1 
ATOM   4926 C CZ   . TYR   B 1 68  ? 44.503 -9.182  6.551   1.00 17.48 ?  68  TYR   B CZ   1 
ATOM   4927 O OH   . TYR   B 1 68  ? 43.135 -9.299  6.641   1.00 18.58 ?  68  TYR   B OH   1 
ATOM   4928 H H    . TYR   B 1 68  ? 51.120 -8.469  6.920   1.00 15.40 ?  68  TYR   B H    1 
ATOM   4929 H HA   . TYR   B 1 68  ? 49.050 -6.945  7.192   1.00 16.29 ?  68  TYR   B HA   1 
ATOM   4930 H HB2  . TYR   B 1 68  ? 48.992 -8.410  5.454   1.00 17.23 ?  68  TYR   B HB2  1 
ATOM   4931 H HB3  . TYR   B 1 68  ? 49.162 -9.658  6.425   1.00 17.23 ?  68  TYR   B HB3  1 
ATOM   4932 H HD1  . TYR   B 1 68  ? 47.208 -10.461 7.703   1.00 19.69 ?  68  TYR   B HD1  1 
ATOM   4933 H HD2  . TYR   B 1 68  ? 46.801 -7.445  5.114   1.00 19.92 ?  68  TYR   B HD2  1 
ATOM   4934 H HE1  . TYR   B 1 68  ? 44.924 -10.675 7.832   1.00 20.89 ?  68  TYR   B HE1  1 
ATOM   4935 H HE2  . TYR   B 1 68  ? 44.495 -7.660  5.242   1.00 20.62 ?  68  TYR   B HE2  1 
ATOM   4936 H HH   . TYR   B 1 68  ? 42.752 -8.744  6.131   1.00 22.29 ?  68  TYR   B HH   1 
ATOM   4937 N N    . ILE   B 1 69  ? 49.146 -9.263  9.405   1.00 12.93 ?  69  ILE   B N    1 
ATOM   4938 C CA   . ILE   B 1 69  ? 48.588 -9.694  10.684  1.00 13.45 ?  69  ILE   B CA   1 
ATOM   4939 C C    . ILE   B 1 69  ? 48.845 -8.651  11.765  1.00 13.19 ?  69  ILE   B C    1 
ATOM   4940 O O    . ILE   B 1 69  ? 47.975 -8.375  12.598  1.00 13.62 ?  69  ILE   B O    1 
ATOM   4941 C CB   . ILE   B 1 69  ? 49.158 -11.072 11.072  1.00 14.38 ?  69  ILE   B CB   1 
ATOM   4942 C CG1  . ILE   B 1 69  ? 48.629 -12.168 10.136  1.00 14.78 ?  69  ILE   B CG1  1 
ATOM   4943 C CG2  . ILE   B 1 69  ? 48.871 -11.385 12.535  1.00 15.62 ?  69  ILE   B CG2  1 
ATOM   4944 C CD1  . ILE   B 1 69  ? 47.164 -12.503 10.312  1.00 14.86 ?  69  ILE   B CD1  1 
ATOM   4945 H H    . ILE   B 1 69  ? 49.799 -9.747  9.128   1.00 15.51 ?  69  ILE   B H    1 
ATOM   4946 H HA   . ILE   B 1 69  ? 47.631 -9.785  10.589  1.00 16.13 ?  69  ILE   B HA   1 
ATOM   4947 H HB   . ILE   B 1 69  ? 50.123 -11.031 10.966  1.00 17.25 ?  69  ILE   B HB   1 
ATOM   4948 H HG12 . ILE   B 1 69  ? 48.757 -11.873 9.219   1.00 17.73 ?  69  ILE   B HG12 1 
ATOM   4949 H HG13 . ILE   B 1 69  ? 49.142 -12.976 10.291  1.00 17.73 ?  69  ILE   B HG13 1 
ATOM   4950 H HG21 . ILE   B 1 69  ? 49.005 -12.337 12.681  1.00 18.73 ?  69  ILE   B HG21 1 
ATOM   4951 H HG22 . ILE   B 1 69  ? 49.483 -10.882 13.097  1.00 18.73 ?  69  ILE   B HG22 1 
ATOM   4952 H HG23 . ILE   B 1 69  ? 47.956 -11.146 12.738  1.00 18.73 ?  69  ILE   B HG23 1 
ATOM   4953 H HD11 . ILE   B 1 69  ? 46.923 -13.188 9.668   1.00 17.82 ?  69  ILE   B HD11 1 
ATOM   4954 H HD12 . ILE   B 1 69  ? 47.022 -12.837 11.213  1.00 17.82 ?  69  ILE   B HD12 1 
ATOM   4955 H HD13 . ILE   B 1 69  ? 46.634 -11.708 10.164  1.00 17.82 ?  69  ILE   B HD13 1 
ATOM   4956 N N    . ALA   B 1 70  ? 50.042 -8.069  11.792  1.00 13.37 ?  70  ALA   B N    1 
ATOM   4957 C CA   . ALA   B 1 70  ? 50.320 -7.032  12.781  1.00 13.18 ?  70  ALA   B CA   1 
ATOM   4958 C C    . ALA   B 1 70  ? 49.323 -5.886  12.666  1.00 13.37 ?  70  ALA   B C    1 
ATOM   4959 O O    . ALA   B 1 70  ? 48.873 -5.344  13.679  1.00 13.95 ?  70  ALA   B O    1 
ATOM   4960 C CB   . ALA   B 1 70  ? 51.753 -6.525  12.620  1.00 13.91 ?  70  ALA   B CB   1 
ATOM   4961 H H    . ALA   B 1 70  ? 50.690 -8.252  11.267  1.00 16.03 ?  70  ALA   B H    1 
ATOM   4962 H HA   . ALA   B 1 70  ? 50.240 -7.412  13.673  1.00 15.80 ?  70  ALA   B HA   1 
ATOM   4963 H HB1  . ALA   B 1 70  ? 51.936 -5.862  13.305  1.00 16.68 ?  70  ALA   B HB1  1 
ATOM   4964 H HB2  . ALA   B 1 70  ? 52.367 -7.272  12.715  1.00 16.68 ?  70  ALA   B HB2  1 
ATOM   4965 H HB3  . ALA   B 1 70  ? 51.852 -6.129  11.740  1.00 16.68 ?  70  ALA   B HB3  1 
ATOM   4966 N N    . THR   B 1 71  ? 48.955 -5.516  11.441  1.00 13.98 ?  71  THR   B N    1 
ATOM   4967 C CA   . THR   B 1 71  ? 48.064 -4.381  11.228  1.00 14.76 ?  71  THR   B CA   1 
ATOM   4968 C C    . THR   B 1 71  ? 46.596 -4.743  11.433  1.00 15.38 ?  71  THR   B C    1 
ATOM   4969 O O    . THR   B 1 71  ? 45.818 -3.922  11.940  1.00 16.80 ?  71  THR   B O    1 
ATOM   4970 C CB   . THR   B 1 71  ? 48.284 -3.819  9.821   1.00 16.54 ?  71  THR   B CB   1 
ATOM   4971 O OG1  . THR   B 1 71  ? 49.608 -3.283  9.727   1.00 18.45 ?  71  THR   B OG1  1 
ATOM   4972 C CG2  . THR   B 1 71  ? 47.267 -2.734  9.494   1.00 17.64 ?  71  THR   B CG2  1 
ATOM   4973 H H    . THR   B 1 71  ? 49.210 -5.906  10.720  1.00 16.77 ?  71  THR   B H    1 
ATOM   4974 H HA   . THR   B 1 71  ? 48.289 -3.682  11.863  1.00 17.71 ?  71  THR   B HA   1 
ATOM   4975 H HB   . THR   B 1 71  ? 48.191 -4.530  9.170   1.00 19.84 ?  71  THR   B HB   1 
ATOM   4976 H HG1  . THR   B 1 71  ? 49.741 -2.957  8.960   1.00 22.13 ?  71  THR   B HG1  1 
ATOM   4977 H HG21 . THR   B 1 71  ? 47.576 -2.207  8.739   1.00 21.16 ?  71  THR   B HG21 1 
ATOM   4978 H HG22 . THR   B 1 71  ? 46.414 -3.133  9.269   1.00 21.16 ?  71  THR   B HG22 1 
ATOM   4979 H HG23 . THR   B 1 71  ? 47.152 -2.145  10.258  1.00 21.16 ?  71  THR   B HG23 1 
ATOM   4980 N N    . ASN   B 1 72  ? 46.196 -5.956  11.041  1.00 14.83 ?  72  ASN   B N    1 
ATOM   4981 C CA   . ASN   B 1 72  ? 44.792 -6.306  10.910  1.00 15.31 ?  72  ASN   B CA   1 
ATOM   4982 C C    . ASN   B 1 72  ? 44.317 -7.405  11.846  1.00 15.92 ?  72  ASN   B C    1 
ATOM   4983 O O    . ASN   B 1 72  ? 43.102 -7.560  12.010  1.00 16.89 ?  72  ASN   B O    1 
ATOM   4984 C CB   . ASN   B 1 72  ? 44.490 -6.736  9.466   1.00 16.15 ?  72  ASN   B CB   1 
ATOM   4985 C CG   . ASN   B 1 72  ? 44.769 -5.636  8.475   1.00 17.25 ?  72  ASN   B CG   1 
ATOM   4986 O OD1  . ASN   B 1 72  ? 45.786 -5.645  7.779   1.00 18.23 ?  72  ASN   B OD1  1 
ATOM   4987 N ND2  . ASN   B 1 72  ? 43.890 -4.654  8.435   1.00 18.81 ?  72  ASN   B ND2  1 
ATOM   4988 H H    . ASN   B 1 72  ? 46.739 -6.599  10.838  1.00 17.79 ?  72  ASN   B H    1 
ATOM   4989 H HA   . ASN   B 1 72  ? 44.266 -5.516  11.091  1.00 18.37 ?  72  ASN   B HA   1 
ATOM   4990 H HB2  . ASN   B 1 72  ? 45.051 -7.497  9.237   1.00 19.37 ?  72  ASN   B HB2  1 
ATOM   4991 H HB3  . ASN   B 1 72  ? 43.557 -6.975  9.396   1.00 19.37 ?  72  ASN   B HB3  1 
ATOM   4992 H HD21 . ASN   B 1 72  ? 43.997 -4.000  7.888   1.00 22.56 ?  72  ASN   B HD21 1 
ATOM   4993 H HD22 . ASN   B 1 72  ? 43.193 -4.681  8.940   1.00 22.56 ?  72  ASN   B HD22 1 
ATOM   4994 N N    . GLY   B 1 73  ? 45.215 -8.163  12.462  1.00 15.34 ?  73  GLY   B N    1 
ATOM   4995 C CA   . GLY   B 1 73  ? 44.811 -9.296  13.256  1.00 14.84 ?  73  GLY   B CA   1 
ATOM   4996 C C    . GLY   B 1 73  ? 44.455 -10.482 12.387  1.00 13.38 ?  73  GLY   B C    1 
ATOM   4997 O O    . GLY   B 1 73  ? 44.450 -10.405 11.156  1.00 13.52 ?  73  GLY   B O    1 
ATOM   4998 H H    . GLY   B 1 73  ? 46.068 -8.030  12.439  1.00 18.40 ?  73  GLY   B H    1 
ATOM   4999 H HA2  . GLY   B 1 73  ? 45.535 -9.547  13.853  1.00 17.80 ?  73  GLY   B HA2  1 
ATOM   5000 H HA3  . GLY   B 1 73  ? 44.038 -9.056  13.794  1.00 17.80 ?  73  GLY   B HA3  1 
ATOM   5001 N N    . PRO   B 1 74  ? 44.152 -11.606 13.026  1.00 13.71 ?  74  PRO   B N    1 
ATOM   5002 C CA   . PRO   B 1 74  ? 43.912 -12.840 12.279  1.00 13.42 ?  74  PRO   B CA   1 
ATOM   5003 C C    . PRO   B 1 74  ? 42.609 -12.792 11.491  1.00 12.77 ?  74  PRO   B C    1 
ATOM   5004 O O    . PRO   B 1 74  ? 41.665 -12.058 11.810  1.00 13.98 ?  74  PRO   B O    1 
ATOM   5005 C CB   . PRO   B 1 74  ? 43.854 -13.905 13.379  1.00 14.64 ?  74  PRO   B CB   1 
ATOM   5006 C CG   . PRO   B 1 74  ? 43.395 -13.162 14.589  1.00 15.93 ?  74  PRO   B CG   1 
ATOM   5007 C CD   . PRO   B 1 74  ? 44.039 -11.808 14.480  1.00 15.33 ?  74  PRO   B CD   1 
ATOM   5008 H HA   . PRO   B 1 74  ? 44.657 -13.020 11.677  1.00 16.10 ?  74  PRO   B HA   1 
ATOM   5009 H HB2  . PRO   B 1 74  ? 43.220 -14.592 13.128  1.00 17.55 ?  74  PRO   B HB2  1 
ATOM   5010 H HB3  . PRO   B 1 74  ? 44.738 -14.279 13.515  1.00 17.55 ?  74  PRO   B HB3  1 
ATOM   5011 H HG2  . PRO   B 1 74  ? 42.428 -13.086 14.575  1.00 19.11 ?  74  PRO   B HG2  1 
ATOM   5012 H HG3  . PRO   B 1 74  ? 43.695 -13.621 15.385  1.00 19.11 ?  74  PRO   B HG3  1 
ATOM   5013 H HD2  . PRO   B 1 74  ? 43.466 -11.127 14.876  1.00 18.38 ?  74  PRO   B HD2  1 
ATOM   5014 H HD3  . PRO   B 1 74  ? 44.917 -11.811 14.888  1.00 18.38 ?  74  PRO   B HD3  1 
ATOM   5015 N N    . LEU   B 1 75  ? 42.579 -13.606 10.438  1.00 12.14 ?  75  LEU   B N    1 
ATOM   5016 C CA   . LEU   B 1 75  ? 41.365 -13.826 9.671   1.00 12.22 ?  75  LEU   B CA   1 
ATOM   5017 C C    . LEU   B 1 75  ? 40.394 -14.690 10.473  1.00 12.60 ?  75  LEU   B C    1 
ATOM   5018 O O    . LEU   B 1 75  ? 40.734 -15.244 11.520  1.00 13.59 ?  75  LEU   B O    1 
ATOM   5019 C CB   . LEU   B 1 75  ? 41.688 -14.531 8.352   1.00 12.15 ?  75  LEU   B CB   1 
ATOM   5020 C CG   . LEU   B 1 75  ? 42.530 -13.775 7.316   1.00 14.02 ?  75  LEU   B CG   1 
ATOM   5021 C CD1  . LEU   B 1 75  ? 42.714 -14.605 6.047   1.00 15.52 ?  75  LEU   B CD1  1 
ATOM   5022 C CD2  . LEU   B 1 75  ? 41.945 -12.430 6.978   1.00 17.01 ?  75  LEU   B CD2  1 
ATOM   5023 H H    . LEU   B 1 75  ? 43.256 -14.049 10.143  1.00 14.56 ?  75  LEU   B H    1 
ATOM   5024 H HA   . LEU   B 1 75  ? 40.936 -12.979 9.476   1.00 14.65 ?  75  LEU   B HA   1 
ATOM   5025 H HB2  . LEU   B 1 75  ? 42.166 -15.350 8.557   1.00 14.57 ?  75  LEU   B HB2  1 
ATOM   5026 H HB3  . LEU   B 1 75  ? 40.849 -14.759 7.917   1.00 14.57 ?  75  LEU   B HB3  1 
ATOM   5027 H HG   . LEU   B 1 75  ? 43.411 -13.625 7.688   1.00 16.82 ?  75  LEU   B HG   1 
ATOM   5028 H HD11 . LEU   B 1 75  ? 43.256 -14.100 5.413   1.00 18.61 ?  75  LEU   B HD11 1 
ATOM   5029 H HD12 . LEU   B 1 75  ? 43.165 -15.435 6.270   1.00 18.61 ?  75  LEU   B HD12 1 
ATOM   5030 H HD13 . LEU   B 1 75  ? 41.847 -14.793 5.657   1.00 18.61 ?  75  LEU   B HD13 1 
ATOM   5031 H HD21 . LEU   B 1 75  ? 42.466 -12.027 6.267   1.00 20.40 ?  75  LEU   B HD21 1 
ATOM   5032 H HD22 . LEU   B 1 75  ? 41.027 -12.549 6.691   1.00 20.40 ?  75  LEU   B HD22 1 
ATOM   5033 H HD23 . LEU   B 1 75  ? 41.974 -11.868 7.769   1.00 20.40 ?  75  LEU   B HD23 1 
ATOM   5034 N N    . LYS   B 1 76  ? 39.164 -14.790 9.968   1.00 13.74 ?  76  LYS   B N    1 
ATOM   5035 C CA   . LYS   B 1 76  ? 38.178 -15.753 10.444  1.00 14.82 ?  76  LYS   B CA   1 
ATOM   5036 C C    . LYS   B 1 76  ? 38.268 -17.024 9.602   1.00 13.43 ?  76  LYS   B C    1 
ATOM   5037 O O    . LYS   B 1 76  ? 38.539 -16.962 8.403   1.00 13.07 ?  76  LYS   B O    1 
ATOM   5038 C CB   . LYS   B 1 76  ? 36.758 -15.184 10.267  1.00 17.21 ?  76  LYS   B CB   1 
ATOM   5039 C CG   . LYS   B 1 76  ? 36.493 -13.781 10.849  1.00 19.39 ?  76  LYS   B CG   1 
ATOM   5040 C CD   . LYS   B 1 76  ? 35.087 -13.257 10.500  1.00 20.94 ?  76  LYS   B CD   1 
ATOM   5041 C CE   . LYS   B 1 76  ? 34.833 -11.876 11.093  1.00 22.67 ?  76  LYS   B CE   1 
ATOM   5042 N NZ   . LYS   B 1 76  ? 33.523 -11.307 10.665  1.00 23.46 ?  76  LYS   B NZ   1 
ATOM   5043 H H    . LYS   B 1 76  ? 38.869 -14.296 9.334   1.00 16.48 ?  76  LYS   B H    1 
ATOM   5044 H HA   . LYS   B 1 76  ? 38.323 -15.975 11.379  1.00 17.78 ?  76  LYS   B HA   1 
ATOM   5045 H HB2  . LYS   B 1 76  ? 36.565 -15.137 9.316   1.00 20.64 ?  76  LYS   B HB2  1 
ATOM   5046 H HB3  . LYS   B 1 76  ? 36.127 -15.789 10.689  1.00 20.64 ?  76  LYS   B HB3  1 
ATOM   5047 H HG2  . LYS   B 1 76  ? 36.572 -13.819 11.814  1.00 23.25 ?  76  LYS   B HG2  1 
ATOM   5048 H HG3  . LYS   B 1 76  ? 37.146 -13.160 10.486  1.00 23.25 ?  76  LYS   B HG3  1 
ATOM   5049 H HD2  . LYS   B 1 76  ? 34.999 -13.192 9.535   1.00 25.12 ?  76  LYS   B HD2  1 
ATOM   5050 H HD3  . LYS   B 1 76  ? 34.421 -13.866 10.855  1.00 25.12 ?  76  LYS   B HD3  1 
ATOM   5051 H HE2  . LYS   B 1 76  ? 34.833 -11.942 12.061  1.00 27.20 ?  76  LYS   B HE2  1 
ATOM   5052 H HE3  . LYS   B 1 76  ? 35.535 -11.272 10.801  1.00 27.20 ?  76  LYS   B HE3  1 
ATOM   5053 H HZ1  . LYS   B 1 76  ? 33.407 -10.502 11.029  1.00 28.15 ?  76  LYS   B HZ1  1 
ATOM   5054 H HZ2  . LYS   B 1 76  ? 33.499 -11.229 9.779   1.00 28.15 ?  76  LYS   B HZ2  1 
ATOM   5055 H HZ3  . LYS   B 1 76  ? 32.859 -11.839 10.926  1.00 28.15 ?  76  LYS   B HZ3  1 
ATOM   5056 N N    . VAL   B 1 77  ? 38.015 -18.184 10.223  1.00 13.85 ?  77  VAL   B N    1 
ATOM   5057 C CA   . VAL   B 1 77  ? 37.807 -19.392 9.427   1.00 13.97 ?  77  VAL   B CA   1 
ATOM   5058 C C    . VAL   B 1 77  ? 36.613 -19.152 8.514   1.00 12.88 ?  77  VAL   B C    1 
ATOM   5059 O O    . VAL   B 1 77  ? 35.551 -18.696 8.962   1.00 12.95 ?  77  VAL   B O    1 
ATOM   5060 C CB   . VAL   B 1 77  ? 37.614 -20.627 10.322  1.00 15.15 ?  77  VAL   B CB   1 
ATOM   5061 C CG1  . VAL   B 1 77  ? 37.344 -21.857 9.459   1.00 15.90 ?  77  VAL   B CG1  1 
ATOM   5062 C CG2  . VAL   B 1 77  ? 38.840 -20.855 11.206  1.00 16.51 ?  77  VAL   B CG2  1 
ATOM   5063 H H    . VAL   B 1 77  ? 37.969 -18.292 11.070  1.00 16.61 ?  77  VAL   B H    1 
ATOM   5064 H HA   . VAL   B 1 77  ? 38.583 -19.543 8.866   1.00 16.75 ?  77  VAL   B HA   1 
ATOM   5065 H HB   . VAL   B 1 77  ? 36.843 -20.484 10.896  1.00 18.17 ?  77  VAL   B HB   1 
ATOM   5066 H HG11 . VAL   B 1 77  ? 37.402 -22.650 10.015  1.00 19.07 ?  77  VAL   B HG11 1 
ATOM   5067 H HG12 . VAL   B 1 77  ? 36.454 -21.792 9.075   1.00 19.07 ?  77  VAL   B HG12 1 
ATOM   5068 H HG13 . VAL   B 1 77  ? 38.006 -21.900 8.753   1.00 19.07 ?  77  VAL   B HG13 1 
ATOM   5069 H HG21 . VAL   B 1 77  ? 38.700 -21.658 11.728  1.00 19.81 ?  77  VAL   B HG21 1 
ATOM   5070 H HG22 . VAL   B 1 77  ? 39.617 -20.953 10.639  1.00 19.81 ?  77  VAL   B HG22 1 
ATOM   5071 H HG23 . VAL   B 1 77  ? 38.947 -20.090 11.792  1.00 19.81 ?  77  VAL   B HG23 1 
ATOM   5072 N N    . GLY   B 1 78  ? 36.792 -19.428 7.225   1.00 12.34 ?  78  GLY   B N    1 
ATOM   5073 C CA   . GLY   B 1 78  ? 35.816 -19.098 6.212   1.00 11.93 ?  78  GLY   B CA   1 
ATOM   5074 C C    . GLY   B 1 78  ? 36.060 -17.780 5.514   1.00 11.44 ?  78  GLY   B C    1 
ATOM   5075 O O    . GLY   B 1 78  ? 35.384 -17.494 4.521   1.00 11.76 ?  78  GLY   B O    1 
ATOM   5076 H H    . GLY   B 1 78  ? 37.491 -19.816 6.911   1.00 14.80 ?  78  GLY   B H    1 
ATOM   5077 H HA2  . GLY   B 1 78  ? 35.807 -19.793 5.540   1.00 14.30 ?  78  GLY   B HA2  1 
ATOM   5078 H HA3  . GLY   B 1 78  ? 34.936 -19.055 6.617   1.00 14.30 ?  78  GLY   B HA3  1 
ATOM   5079 N N    . GLY   B 1 79  ? 37.007 -16.974 6.001   1.00 11.65 ?  79  GLY   B N    1 
ATOM   5080 C CA   . GLY   B 1 79  ? 37.307 -15.680 5.427   1.00 11.35 ?  79  GLY   B CA   1 
ATOM   5081 C C    . GLY   B 1 79  ? 38.546 -15.698 4.542   1.00 11.16 ?  79  GLY   B C    1 
ATOM   5082 O O    . GLY   B 1 79  ? 39.160 -16.733 4.288   1.00 11.58 ?  79  GLY   B O    1 
ATOM   5083 H H    . GLY   B 1 79  ? 37.505 -17.167 6.671   1.00 13.97 ?  79  GLY   B H    1 
ATOM   5084 H HA2  . GLY   B 1 79  ? 36.558 -15.374 4.891   1.00 13.61 ?  79  GLY   B HA2  1 
ATOM   5085 H HA3  . GLY   B 1 79  ? 37.456 -15.035 6.138   1.00 13.61 ?  79  GLY   B HA3  1 
ATOM   5086 N N    . SER   B 1 80  ? 38.909 -14.502 4.070   1.00 11.08 ?  80  SER   B N    1 
ATOM   5087 C CA   . SER   B 1 80  ? 40.018 -14.366 3.137   1.00 10.98 ?  80  SER   B CA   1 
ATOM   5088 C C    . SER   B 1 80  ? 40.597 -12.959 3.201   1.00 10.79 ?  80  SER   B C    1 
ATOM   5089 O O    . SER   B 1 80  ? 39.976 -12.026 3.717   1.00 12.11 ?  80  SER   B O    1 
ATOM   5090 C CB   . SER   B 1 80  ? 39.581 -14.649 1.696   1.00 11.34 ?  80  SER   B CB   1 
ATOM   5091 O OG   . SER   B 1 80  ? 38.738 -13.627 1.186   1.00 12.35 ?  80  SER   B OG   1 
ATOM   5092 H H    . SER   B 1 80  ? 38.530 -13.758 4.273   1.00 13.29 ?  80  SER   B H    1 
ATOM   5093 H HA   . SER   B 1 80  ? 40.710 -14.997 3.380   1.00 13.17 ?  80  SER   B HA   1 
ATOM   5094 H HB2  . SER   B 1 80  ? 40.366 -14.712 1.132   1.00 13.60 ?  80  SER   B HB2  1 
ATOM   5095 H HB3  . SER   B 1 80  ? 39.093 -15.489 1.675   1.00 13.60 ?  80  SER   B HB3  1 
ATOM   5096 H HG   . SER   B 1 80  ? 38.048 -13.560 1.664   1.00 14.81 ?  80  SER   B HG   1 
ATOM   5097 N N    . CYS   B 1 81  ? 41.788 -12.812 2.620   1.00 10.59 ?  81  CYS   B N    1 
ATOM   5098 C CA   . CYS   B 1 81  ? 42.328 -11.497 2.311   1.00 10.78 ?  81  CYS   B CA   1 
ATOM   5099 C C    . CYS   B 1 81  ? 43.098 -11.575 1.002   1.00 10.45 ?  81  CYS   B C    1 
ATOM   5100 O O    . CYS   B 1 81  ? 43.609 -12.635 0.626   1.00 11.22 ?  81  CYS   B O    1 
ATOM   5101 C CB   . CYS   B 1 81  ? 43.223 -10.940 3.429   1.00 11.64 ?  81  CYS   B CB   1 
ATOM   5102 S SG   . CYS   B 1 81  ? 44.737 -11.883 3.683   1.00 11.94 ?  81  CYS   B SG   1 
ATOM   5103 H H    . CYS   B 1 81  ? 42.302 -13.464 2.384   1.00 12.70 ?  81  CYS   B H    1 
ATOM   5104 H HA   . CYS   B 1 81  ? 41.592 -10.876 2.183   1.00 12.93 ?  81  CYS   B HA   1 
ATOM   5105 H HB2  . CYS   B 1 81  ? 43.474 -10.029 3.210   1.00 13.96 ?  81  CYS   B HB2  1 
ATOM   5106 H HB3  . CYS   B 1 81  ? 42.720 -10.948 4.263   1.00 13.96 ?  81  CYS   B HB3  1 
ATOM   5107 H HG   . CYS   B 1 81  ? 45.367 -11.384 4.577   1.00 14.32 ?  81  CYS   B HG   1 
ATOM   5108 N N    . VAL   B 1 82  ? 43.196 -10.433 0.327   1.00 10.77 ?  82  VAL   B N    1 
ATOM   5109 C CA   . VAL   B 1 82  ? 43.961 -10.304 -0.910  1.00 10.86 ?  82  VAL   B CA   1 
ATOM   5110 C C    . VAL   B 1 82  ? 45.302 -9.664  -0.589  1.00 11.08 ?  82  VAL   B C    1 
ATOM   5111 O O    . VAL   B 1 82  ? 45.355 -8.546  -0.058  1.00 12.12 ?  82  VAL   B O    1 
ATOM   5112 C CB   . VAL   B 1 82  ? 43.215 -9.461  -1.956  1.00 12.08 ?  82  VAL   B CB   1 
ATOM   5113 C CG1  . VAL   B 1 82  ? 44.079 -9.278  -3.200  1.00 13.28 ?  82  VAL   B CG1  1 
ATOM   5114 C CG2  . VAL   B 1 82  ? 41.879 -10.080 -2.311  1.00 12.74 ?  82  VAL   B CG2  1 
ATOM   5115 H H    . VAL   B 1 82  ? 42.813 -9.695  0.567   1.00 12.91 ?  82  VAL   B H    1 
ATOM   5116 H HA   . VAL   B 1 82  ? 44.120 -11.178 -1.287  1.00 13.03 ?  82  VAL   B HA   1 
ATOM   5117 H HB   . VAL   B 1 82  ? 43.039 -8.579  -1.590  1.00 14.49 ?  82  VAL   B HB   1 
ATOM   5118 H HG11 . VAL   B 1 82  ? 43.523 -8.982  -3.936  1.00 15.93 ?  82  VAL   B HG11 1 
ATOM   5119 H HG12 . VAL   B 1 82  ? 44.760 -8.603  -3.017  1.00 15.93 ?  82  VAL   B HG12 1 
ATOM   5120 H HG13 . VAL   B 1 82  ? 44.502 -10.120 -3.420  1.00 15.93 ?  82  VAL   B HG13 1 
ATOM   5121 H HG21 . VAL   B 1 82  ? 41.441 -9.538  -2.992  1.00 15.28 ?  82  VAL   B HG21 1 
ATOM   5122 H HG22 . VAL   B 1 82  ? 42.024 -10.978 -2.656  1.00 15.28 ?  82  VAL   B HG22 1 
ATOM   5123 H HG23 . VAL   B 1 82  ? 41.323 -10.119 -1.518  1.00 15.28 ?  82  VAL   B HG23 1 
ATOM   5124 N N    . LEU   B 1 83  ? 46.381 -10.351 -0.952  1.00 10.85 ?  83  LEU   B N    1 
ATOM   5125 C CA   . LEU   B 1 83  ? 47.736 -9.834  -0.836  1.00 10.64 ?  83  LEU   B CA   1 
ATOM   5126 C C    . LEU   B 1 83  ? 48.435 -9.968  -2.188  1.00 10.53 ?  83  LEU   B C    1 
ATOM   5127 O O    . LEU   B 1 83  ? 47.835 -10.383 -3.185  1.00 10.66 ?  83  LEU   B O    1 
ATOM   5128 C CB   . LEU   B 1 83  ? 48.493 -10.509 0.316   1.00 11.06 ?  83  LEU   B CB   1 
ATOM   5129 C CG   . LEU   B 1 83  ? 47.969 -10.152 1.711   1.00 12.28 ?  83  LEU   B CG   1 
ATOM   5130 C CD1  . LEU   B 1 83  ? 48.597 -11.013 2.787   1.00 12.92 ?  83  LEU   B CD1  1 
ATOM   5131 C CD2  . LEU   B 1 83  ? 48.178 -8.667  2.035   1.00 13.31 ?  83  LEU   B CD2  1 
ATOM   5132 H H    . LEU   B 1 83  ? 46.345 -11.144 -1.284  1.00 13.01 ?  83  LEU   B H    1 
ATOM   5133 H HA   . LEU   B 1 83  ? 47.683 -8.889  -0.637  1.00 12.76 ?  83  LEU   B HA   1 
ATOM   5134 H HB2  . LEU   B 1 83  ? 48.430 -11.466 0.215   1.00 13.26 ?  83  LEU   B HB2  1 
ATOM   5135 H HB3  . LEU   B 1 83  ? 49.424 -10.233 0.275   1.00 13.26 ?  83  LEU   B HB3  1 
ATOM   5136 H HG   . LEU   B 1 83  ? 47.014 -10.313 1.728   1.00 14.73 ?  83  LEU   B HG   1 
ATOM   5137 H HD11 . LEU   B 1 83  ? 48.229 -10.762 3.650   1.00 15.50 ?  83  LEU   B HD11 1 
ATOM   5138 H HD12 . LEU   B 1 83  ? 48.390 -11.945 2.602   1.00 15.50 ?  83  LEU   B HD12 1 
ATOM   5139 H HD13 . LEU   B 1 83  ? 49.556 -10.880 2.783   1.00 15.50 ?  83  LEU   B HD13 1 
ATOM   5140 H HD21 . LEU   B 1 83  ? 47.975 -8.517  2.971   1.00 15.96 ?  83  LEU   B HD21 1 
ATOM   5141 H HD22 . LEU   B 1 83  ? 49.102 -8.432  1.854   1.00 15.96 ?  83  LEU   B HD22 1 
ATOM   5142 H HD23 . LEU   B 1 83  ? 47.587 -8.135  1.478   1.00 15.96 ?  83  LEU   B HD23 1 
ATOM   5143 N N    . SER   B 1 84  ? 49.712 -9.598  -2.237  1.00 11.57 ?  84  SER   B N    1 
ATOM   5144 C CA   . SER   B 1 84  ? 50.446 -9.707  -3.488  1.00 12.02 ?  84  SER   B CA   1 
ATOM   5145 C C    . SER   B 1 84  ? 50.594 -11.164 -3.911  1.00 11.22 ?  84  SER   B C    1 
ATOM   5146 O O    . SER   B 1 84  ? 50.713 -12.067 -3.084  1.00 11.00 ?  84  SER   B O    1 
ATOM   5147 C CB   . SER   B 1 84  ? 51.845 -9.115  -3.337  1.00 13.79 ?  84  SER   B CB   1 
ATOM   5148 O OG   . SER   B 1 84  ? 52.586 -9.318  -4.526  1.00 15.44 ?  84  SER   B OG   1 
ATOM   5149 H H    . SER   B 1 84  ? 50.164 -9.279  -1.574  1.00 13.88 ?  84  SER   B H    1 
ATOM   5150 H HA   . SER   B 1 84  ? 49.979 -9.230  -4.186  1.00 14.41 ?  84  SER   B HA   1 
ATOM   5151 H HB2  . SER   B 1 84  ? 51.767 -8.158  -3.163  1.00 16.54 ?  84  SER   B HB2  1 
ATOM   5152 H HB3  . SER   B 1 84  ? 52.303 -9.546  -2.601  1.00 16.54 ?  84  SER   B HB3  1 
ATOM   5153 H HG   . SER   B 1 84  ? 53.354 -8.978  -4.449  1.00 18.52 ?  84  SER   B HG   1 
ATOM   5154 N N    . GLY   B 1 85  ? 50.654 -11.379 -5.219  1.00 12.38 ?  85  GLY   B N    1 
ATOM   5155 C CA   . GLY   B 1 85  ? 51.007 -12.670 -5.764  1.00 12.89 ?  85  GLY   B CA   1 
ATOM   5156 C C    . GLY   B 1 85  ? 52.481 -12.865 -6.059  1.00 12.10 ?  85  GLY   B C    1 
ATOM   5157 O O    . GLY   B 1 85  ? 52.863 -13.943 -6.516  1.00 12.55 ?  85  GLY   B O    1 
ATOM   5158 H H    . GLY   B 1 85  ? 50.510 -10.783 -5.813  1.00 14.84 ?  85  GLY   B H    1 
ATOM   5159 H HA2  . GLY   B 1 85  ? 50.738 -13.362 -5.139  1.00 15.46 ?  85  GLY   B HA2  1 
ATOM   5160 H HA3  . GLY   B 1 85  ? 50.526 -12.805 -6.588  1.00 15.46 ?  85  GLY   B HA3  1 
ATOM   5161 N N    . HIS   B 1 86  ? 53.333 -11.869 -5.830  1.00 12.02 ?  86  HIS   B N    1 
ATOM   5162 C CA   . HIS   B 1 86  ? 54.797 -12.043 -5.917  1.00 12.10 ?  86  HIS   B CA   1 
ATOM   5163 C C    . HIS   B 1 86  ? 55.168 -12.550 -7.310  1.00 12.13 ?  86  HIS   B C    1 
ATOM   5164 O O    . HIS   B 1 86  ? 54.779 -11.932 -8.313  1.00 13.00 ?  86  HIS   B O    1 
ATOM   5165 C CB   . HIS   B 1 86  ? 55.285 -12.893 -4.744  1.00 12.48 ?  86  HIS   B CB   1 
ATOM   5166 C CG   . HIS   B 1 86  ? 54.972 -12.289 -3.417  1.00 12.69 ?  86  HIS   B CG   1 
ATOM   5167 N ND1  . HIS   B 1 86  ? 55.794 -11.365 -2.809  1.00 13.87 ?  86  HIS   B ND1  1 
ATOM   5168 C CD2  . HIS   B 1 86  ? 53.895 -12.432 -2.609  1.00 12.97 ?  86  HIS   B CD2  1 
ATOM   5169 C CE1  . HIS   B 1 86  ? 55.240 -10.977 -1.675  1.00 13.59 ?  86  HIS   B CE1  1 
ATOM   5170 N NE2  . HIS   B 1 86  ? 54.087 -11.606 -1.531  1.00 13.06 ?  86  HIS   B NE2  1 
ATOM   5171 H H    . HIS   B 1 86  ? 53.095 -11.072 -5.626  1.00 14.42 ?  86  HIS   B H    1 
ATOM   5172 H HA   . HIS   B 1 86  ? 55.209 -11.174 -5.819  1.00 14.51 ?  86  HIS   B HA   1 
ATOM   5173 H HB2  . HIS   B 1 86  ? 54.867 -13.766 -4.786  1.00 14.96 ?  86  HIS   B HB2  1 
ATOM   5174 H HB3  . HIS   B 1 86  ? 56.253 -12.991 -4.806  1.00 14.96 ?  86  HIS   B HB3  1 
ATOM   5175 H HD2  . HIS   B 1 86  ? 53.161 -12.985 -2.761  1.00 15.55 ?  86  HIS   B HD2  1 
ATOM   5176 H HE1  . HIS   B 1 86  ? 55.608 -10.373 -1.073  1.00 16.30 ?  86  HIS   B HE1  1 
ATOM   5177 H HE2  . HIS   B 1 86  ? 53.553 -11.526 -0.864  1.00 15.67 ?  86  HIS   B HE2  1 
ATOM   5178 N N    . ASN   B 1 87  ? 55.933 -13.635 -7.423  1.00 12.46 ?  87  ASN   B N    1 
ATOM   5179 C CA   . ASN   B 1 87  ? 56.328 -14.209 -8.701  1.00 13.31 ?  87  ASN   B CA   1 
ATOM   5180 C C    . ASN   B 1 87  ? 55.341 -15.248 -9.206  1.00 12.98 ?  87  ASN   B C    1 
ATOM   5181 O O    . ASN   B 1 87  ? 55.650 -15.958 -10.166 1.00 14.51 ?  87  ASN   B O    1 
ATOM   5182 C CB   . ASN   B 1 87  ? 57.721 -14.843 -8.587  1.00 14.98 ?  87  ASN   B CB   1 
ATOM   5183 C CG   . ASN   B 1 87  ? 57.782 -15.952 -7.543  1.00 15.75 ?  87  ASN   B CG   1 
ATOM   5184 O OD1  . ASN   B 1 87  ? 57.139 -15.874 -6.495  1.00 14.91 ?  87  ASN   B OD1  1 
ATOM   5185 N ND2  . ASN   B 1 87  ? 58.546 -17.008 -7.841  1.00 17.68 ?  87  ASN   B ND2  1 
ATOM   5186 H H    . ASN   B 1 87  ? 56.239 -14.076 -6.750  1.00 14.94 ?  87  ASN   B H    1 
ATOM   5187 H HA   . ASN   B 1 87  ? 56.375 -13.505 -9.360  1.00 15.96 ?  87  ASN   B HA   1 
ATOM   5188 H HB2  . ASN   B 1 87  ? 57.967 -15.226 -9.446  1.00 17.97 ?  87  ASN   B HB2  1 
ATOM   5189 H HB3  . ASN   B 1 87  ? 58.359 -14.160 -8.335  1.00 17.97 ?  87  ASN   B HB3  1 
ATOM   5190 H HD21 . ASN   B 1 87  ? 58.616 -17.659 -7.285  1.00 21.21 ?  87  ASN   B HD21 1 
ATOM   5191 H HD22 . ASN   B 1 87  ? 58.979 -17.029 -8.586  1.00 21.21 ?  87  ASN   B HD22 1 
ATOM   5192 N N    . LEU   B 1 88  ? 54.166 -15.347 -8.586  1.00 12.06 ?  88  LEU   B N    1 
ATOM   5193 C CA   . LEU   B 1 88  ? 53.185 -16.376 -8.909  1.00 12.25 ?  88  LEU   B CA   1 
ATOM   5194 C C    . LEU   B 1 88  ? 51.950 -15.858 -9.626  1.00 11.96 ?  88  LEU   B C    1 
ATOM   5195 O O    . LEU   B 1 88  ? 51.348 -16.603 -10.409 1.00 13.38 ?  88  LEU   B O    1 
ATOM   5196 C CB   . LEU   B 1 88  ? 52.715 -17.054 -7.620  1.00 13.05 ?  88  LEU   B CB   1 
ATOM   5197 C CG   . LEU   B 1 88  ? 53.827 -17.724 -6.824  1.00 15.29 ?  88  LEU   B CG   1 
ATOM   5198 C CD1  . LEU   B 1 88  ? 53.344 -18.027 -5.416  1.00 16.73 ?  88  LEU   B CD1  1 
ATOM   5199 C CD2  . LEU   B 1 88  ? 54.258 -18.989 -7.532  1.00 18.00 ?  88  LEU   B CD2  1 
ATOM   5200 H H    . LEU   B 1 88  ? 53.910 -14.822 -7.953  1.00 14.47 ?  88  LEU   B H    1 
ATOM   5201 H HA   . LEU   B 1 88  ? 53.594 -17.045 -9.469  1.00 14.69 ?  88  LEU   B HA   1 
ATOM   5202 H HB2  . LEU   B 1 88  ? 52.303 -16.389 -7.045  1.00 15.65 ?  88  LEU   B HB2  1 
ATOM   5203 H HB3  . LEU   B 1 88  ? 52.064 -17.737 -7.846  1.00 15.65 ?  88  LEU   B HB3  1 
ATOM   5204 H HG   . LEU   B 1 88  ? 54.591 -17.126 -6.767  1.00 18.33 ?  88  LEU   B HG   1 
ATOM   5205 H HD11 . LEU   B 1 88  ? 53.977 -18.622 -4.987  1.00 20.06 ?  88  LEU   B HD11 1 
ATOM   5206 H HD12 . LEU   B 1 88  ? 53.281 -17.195 -4.920  1.00 20.06 ?  88  LEU   B HD12 1 
ATOM   5207 H HD13 . LEU   B 1 88  ? 52.473 -18.447 -5.469  1.00 20.06 ?  88  LEU   B HD13 1 
ATOM   5208 H HD21 . LEU   B 1 88  ? 54.926 -19.439 -6.993  1.00 21.59 ?  88  LEU   B HD21 1 
ATOM   5209 H HD22 . LEU   B 1 88  ? 53.485 -19.562 -7.650  1.00 21.59 ?  88  LEU   B HD22 1 
ATOM   5210 H HD23 . LEU   B 1 88  ? 54.633 -18.756 -8.397  1.00 21.59 ?  88  LEU   B HD23 1 
ATOM   5211 N N    . ALA   B 1 89  ? 51.549 -14.621 -9.359  1.00 11.34 ?  89  ALA   B N    1 
ATOM   5212 C CA   . ALA   B 1 89  ? 50.257 -14.129 -9.808  1.00 10.77 ?  89  ALA   B CA   1 
ATOM   5213 C C    . ALA   B 1 89  ? 50.227 -12.639 -9.533  1.00 11.34 ?  89  ALA   B C    1 
ATOM   5214 O O    . ALA   B 1 89  ? 51.067 -12.117 -8.799  1.00 12.18 ?  89  ALA   B O    1 
ATOM   5215 C CB   . ALA   B 1 89  ? 49.116 -14.798 -9.045  1.00 11.23 ?  89  ALA   B CB   1 
ATOM   5216 H H    . ALA   B 1 89  ? 51.998 -14.042 -8.901  1.00 13.60 ?  89  ALA   B H    1 
ATOM   5217 H HA   . ALA   B 1 89  ? 50.144 -14.284 -10.760 1.00 12.92 ?  89  ALA   B HA   1 
ATOM   5218 H HB1  . ALA   B 1 89  ? 48.267 -14.464 -9.386  1.00 13.47 ?  89  ALA   B HB1  1 
ATOM   5219 H HB2  . ALA   B 1 89  ? 49.166 -15.758 -9.183  1.00 13.47 ?  89  ALA   B HB2  1 
ATOM   5220 H HB3  . ALA   B 1 89  ? 49.200 -14.592 -8.105  1.00 13.47 ?  89  ALA   B HB3  1 
ATOM   5221 N N    . LYS   B 1 90  ? 49.232 -11.952 -10.092 1.00 12.06 ?  90  LYS   B N    1 
ATOM   5222 C CA   . LYS   B 1 90  ? 49.042 -10.564 -9.687  1.00 12.29 ?  90  LYS   B CA   1 
ATOM   5223 C C    . LYS   B 1 90  ? 48.730 -10.489 -8.198  1.00 12.23 ?  90  LYS   B C    1 
ATOM   5224 O O    . LYS   B 1 90  ? 49.370 -9.737  -7.448  1.00 13.32 ?  90  LYS   B O    1 
ATOM   5225 C CB   . LYS   B 1 90  ? 47.959 -9.903  -10.538 1.00 13.98 ?  90  LYS   B CB   1 
ATOM   5226 C CG   . LYS   B 1 90  ? 47.666 -8.461  -10.156 1.00 14.70 ?  90  LYS   B CG   1 
ATOM   5227 C CD   . LYS   B 1 90  ? 48.865 -7.557  -10.281 1.00 17.06 ?  90  LYS   B CD   1 
ATOM   5228 C CE   . LYS   B 1 90  ? 48.427 -6.141  -10.008 1.00 19.25 ?  90  LYS   B CE   1 
ATOM   5229 N NZ   . LYS   B 1 90  ? 49.569 -5.205  -9.908  1.00 19.25 ?  90  LYS   B NZ   1 
ATOM   5230 H H    . LYS   B 1 90  ? 48.680 -12.253 -10.680 1.00 14.46 ?  90  LYS   B H    1 
ATOM   5231 H HA   . LYS   B 1 90  ? 49.869 -10.087 -9.838  1.00 14.74 ?  90  LYS   B HA   1 
ATOM   5232 H HB2  . LYS   B 1 90  ? 48.247 -9.908  -11.467 1.00 16.76 ?  90  LYS   B HB2  1 
ATOM   5233 H HB3  . LYS   B 1 90  ? 47.137 -10.409 -10.451 1.00 16.76 ?  90  LYS   B HB3  1 
ATOM   5234 H HG2  . LYS   B 1 90  ? 46.971 -8.118  -10.739 1.00 17.63 ?  90  LYS   B HG2  1 
ATOM   5235 H HG3  . LYS   B 1 90  ? 47.361 -8.433  -9.233  1.00 17.63 ?  90  LYS   B HG3  1 
ATOM   5236 H HD2  . LYS   B 1 90  ? 49.539 -7.806  -9.628  1.00 20.46 ?  90  LYS   B HD2  1 
ATOM   5237 H HD3  . LYS   B 1 90  ? 49.224 -7.607  -11.181 1.00 20.46 ?  90  LYS   B HD3  1 
ATOM   5238 H HE2  . LYS   B 1 90  ? 47.857 -5.835  -10.733 1.00 23.09 ?  90  LYS   B HE2  1 
ATOM   5239 H HE3  . LYS   B 1 90  ? 47.943 -6.108  -9.169  1.00 23.09 ?  90  LYS   B HE3  1 
ATOM   5240 H HZ1  . LYS   B 1 90  ? 49.278 -4.376  -9.749  1.00 23.10 ?  90  LYS   B HZ1  1 
ATOM   5241 H HZ2  . LYS   B 1 90  ? 50.111 -5.450  -9.246  1.00 23.10 ?  90  LYS   B HZ2  1 
ATOM   5242 H HZ3  . LYS   B 1 90  ? 50.032 -5.201  -10.671 1.00 23.10 ?  90  LYS   B HZ3  1 
ATOM   5243 N N    . HIS   B 1 91  ? 47.776 -11.309 -7.750  1.00 10.82 ?  91  HIS   B N    1 
ATOM   5244 C CA   . HIS   B 1 91  ? 47.309 -11.334 -6.377  1.00 10.91 ?  91  HIS   B CA   1 
ATOM   5245 C C    . HIS   B 1 91  ? 47.311 -12.760 -5.857  1.00 10.13 ?  91  HIS   B C    1 
ATOM   5246 O O    . HIS   B 1 91  ? 47.080 -13.714 -6.609  1.00 10.66 ?  91  HIS   B O    1 
ATOM   5247 C CB   . HIS   B 1 91  ? 45.855 -10.855 -6.258  1.00 12.41 ?  91  HIS   B CB   1 
ATOM   5248 C CG   . HIS   B 1 91  ? 45.643 -9.448  -6.690  1.00 15.70 ?  91  HIS   B CG   1 
ATOM   5249 N ND1  . HIS   B 1 91  ? 46.240 -8.375  -6.063  1.00 18.02 ?  91  HIS   B ND1  1 
ATOM   5250 C CD2  . HIS   B 1 91  ? 44.869 -8.928  -7.669  1.00 17.89 ?  91  HIS   B CD2  1 
ATOM   5251 C CE1  . HIS   B 1 91  ? 45.861 -7.253  -6.650  1.00 18.81 ?  91  HIS   B CE1  1 
ATOM   5252 N NE2  . HIS   B 1 91  ? 45.023 -7.562  -7.625  1.00 18.84 ?  91  HIS   B NE2  1 
ATOM   5253 H H    . HIS   B 1 91  ? 47.367 -11.880 -8.248  1.00 12.97 ?  91  HIS   B H    1 
ATOM   5254 H HA   . HIS   B 1 91  ? 47.878 -10.779 -5.812  1.00 13.08 ?  91  HIS   B HA   1 
ATOM   5255 H HB2  . HIS   B 1 91  ? 45.292 -11.417 -6.807  1.00 14.88 ?  91  HIS   B HB2  1 
ATOM   5256 H HB3  . HIS   B 1 91  ? 45.576 -10.920 -5.327  1.00 14.88 ?  91  HIS   B HB3  1 
ATOM   5257 H HD1  . HIS   B 1 91  ? 46.782 -8.425  -5.394  1.00 21.62 ?  91  HIS   B HD1  1 
ATOM   5258 H HD2  . HIS   B 1 91  ? 44.340 -9.393  -8.267  1.00 21.46 ?  91  HIS   B HD2  1 
ATOM   5259 H HE1  . HIS   B 1 91  ? 46.135 -6.391  -6.409  1.00 22.56 ?  91  HIS   B HE1  1 
ATOM   5260 N N    . CYS   B 1 92  ? 47.504 -12.888 -4.553  1.00 10.13 ?  92  CYS   B N    1 
ATOM   5261 C CA   . CYS   B 1 92  ? 47.208 -14.122 -3.842  1.00 9.86  ?  92  CYS   B CA   1 
ATOM   5262 C C    . CYS   B 1 92  ? 45.988 -13.894 -2.959  1.00 9.43  ?  92  CYS   B C    1 
ATOM   5263 O O    . CYS   B 1 92  ? 45.988 -12.996 -2.108  1.00 10.52 ?  92  CYS   B O    1 
ATOM   5264 C CB   . CYS   B 1 92  ? 48.390 -14.587 -2.997  1.00 10.13 ?  92  CYS   B CB   1 
ATOM   5265 S SG   . CYS   B 1 92  ? 48.029 -16.124 -2.096  1.00 10.66 ?  92  CYS   B SG   1 
ATOM   5266 H H    . CYS   B 1 92  ? 47.827 -12.266 -4.045  1.00 12.15 ?  92  CYS   B H    1 
ATOM   5267 H HA   . CYS   B 1 92  ? 47.004 -14.817 -4.487  1.00 11.83 ?  92  CYS   B HA   1 
ATOM   5268 H HB2  . CYS   B 1 92  ? 49.150 -14.742 -3.571  1.00 12.15 ?  92  CYS   B HB2  1 
ATOM   5269 H HB3  . CYS   B 1 92  ? 48.595 -13.899 -2.343  1.00 12.15 ?  92  CYS   B HB3  1 
ATOM   5270 H HG   . CYS   B 1 92  ? 49.006 -16.439 -1.473  1.00 12.78 ?  92  CYS   B HG   1 
ATOM   5271 N N    . LEU   B 1 93  ? 44.950 -14.698 -3.176  1.00 9.40  ?  93  LEU   B N    1 
ATOM   5272 C CA   . LEU   B 1 93  ? 43.775 -14.714 -2.314  1.00 9.72  ?  93  LEU   B CA   1 
ATOM   5273 C C    . LEU   B 1 93  ? 44.003 -15.783 -1.252  1.00 9.20  ?  93  LEU   B C    1 
ATOM   5274 O O    . LEU   B 1 93  ? 43.954 -16.986 -1.547  1.00 9.67  ?  93  LEU   B O    1 
ATOM   5275 C CB   . LEU   B 1 93  ? 42.513 -15.005 -3.120  1.00 10.15 ?  93  LEU   B CB   1 
ATOM   5276 C CG   . LEU   B 1 93  ? 41.215 -15.036 -2.313  1.00 10.74 ?  93  LEU   B CG   1 
ATOM   5277 C CD1  . LEU   B 1 93  ? 40.862 -13.644 -1.810  1.00 11.17 ?  93  LEU   B CD1  1 
ATOM   5278 C CD2  . LEU   B 1 93  ? 40.091 -15.624 -3.148  1.00 10.94 ?  93  LEU   B CD2  1 
ATOM   5279 H H    . LEU   B 1 93  ? 44.908 -15.271 -3.828  1.00 11.27 ?  93  LEU   B H    1 
ATOM   5280 H HA   . LEU   B 1 93  ? 43.683 -13.855 -1.882  1.00 11.65 ?  93  LEU   B HA   1 
ATOM   5281 H HB2  . LEU   B 1 93  ? 42.417 -14.315 -3.796  1.00 12.17 ?  93  LEU   B HB2  1 
ATOM   5282 H HB3  . LEU   B 1 93  ? 42.608 -15.867 -3.545  1.00 12.17 ?  93  LEU   B HB3  1 
ATOM   5283 H HG   . LEU   B 1 93  ? 41.339 -15.601 -1.538  1.00 12.88 ?  93  LEU   B HG   1 
ATOM   5284 H HD11 . LEU   B 1 93  ? 40.009 -13.677 -1.355  1.00 13.40 ?  93  LEU   B HD11 1 
ATOM   5285 H HD12 . LEU   B 1 93  ? 41.553 -13.343 -1.195  1.00 13.40 ?  93  LEU   B HD12 1 
ATOM   5286 H HD13 . LEU   B 1 93  ? 40.812 -13.036 -2.567  1.00 13.40 ?  93  LEU   B HD13 1 
ATOM   5287 H HD21 . LEU   B 1 93  ? 39.274 -15.629 -2.624  1.00 13.11 ?  93  LEU   B HD21 1 
ATOM   5288 H HD22 . LEU   B 1 93  ? 39.969 -15.085 -3.945  1.00 13.11 ?  93  LEU   B HD22 1 
ATOM   5289 H HD23 . LEU   B 1 93  ? 40.327 -16.533 -3.398  1.00 13.11 ?  93  LEU   B HD23 1 
ATOM   5290 N N    . HIS   B 1 94  ? 44.285 -15.350 -0.027  1.00 9.30  ?  94  HIS   B N    1 
ATOM   5291 C CA   . HIS   B 1 94  ? 44.503 -16.261 1.091   1.00 9.39  ?  94  HIS   B CA   1 
ATOM   5292 C C    . HIS   B 1 94  ? 43.142 -16.617 1.667   1.00 9.81  ?  94  HIS   B C    1 
ATOM   5293 O O    . HIS   B 1 94  ? 42.471 -15.745 2.222   1.00 11.20 ?  94  HIS   B O    1 
ATOM   5294 C CB   . HIS   B 1 94  ? 45.374 -15.588 2.150   1.00 9.81  ?  94  HIS   B CB   1 
ATOM   5295 C CG   . HIS   B 1 94  ? 46.755 -15.284 1.678   1.00 9.96  ?  94  HIS   B CG   1 
ATOM   5296 N ND1  . HIS   B 1 94  ? 47.788 -16.195 1.763   1.00 10.08 ?  94  HIS   B ND1  1 
ATOM   5297 C CD2  . HIS   B 1 94  ? 47.258 -14.172 1.085   1.00 10.21 ?  94  HIS   B CD2  1 
ATOM   5298 C CE1  . HIS   B 1 94  ? 48.873 -15.640 1.251   1.00 10.24 ?  94  HIS   B CE1  1 
ATOM   5299 N NE2  . HIS   B 1 94  ? 48.582 -14.416 0.834   1.00 10.30 ?  94  HIS   B NE2  1 
ATOM   5300 H H    . HIS   B 1 94  ? 44.361 -14.516 0.185   1.00 11.15 ?  94  HIS   B H    1 
ATOM   5301 H HA   . HIS   B 1 94  ? 44.941 -17.069 0.783   1.00 11.26 ?  94  HIS   B HA   1 
ATOM   5302 H HB2  . HIS   B 1 94  ? 44.958 -14.753 2.414   1.00 11.76 ?  94  HIS   B HB2  1 
ATOM   5303 H HB3  . HIS   B 1 94  ? 45.447 -16.178 2.916   1.00 11.76 ?  94  HIS   B HB3  1 
ATOM   5304 H HD2  . HIS   B 1 94  ? 46.796 -13.390 0.887   1.00 12.25 ?  94  HIS   B HD2  1 
ATOM   5305 H HE1  . HIS   B 1 94  ? 49.709 -16.046 1.196   1.00 12.28 ?  94  HIS   B HE1  1 
ATOM   5306 H HE2  . HIS   B 1 94  ? 49.136 -13.870 0.466   1.00 12.35 ?  94  HIS   B HE2  1 
ATOM   5307 N N    . VAL   B 1 95  ? 42.711 -17.869 1.508   1.00 9.76  ?  95  VAL   B N    1 
ATOM   5308 C CA   . VAL   B 1 95  ? 41.385 -18.312 1.943   1.00 9.94  ?  95  VAL   B CA   1 
ATOM   5309 C C    . VAL   B 1 95  ? 41.555 -19.349 3.038   1.00 10.09 ?  95  VAL   B C    1 
ATOM   5310 O O    . VAL   B 1 95  ? 42.322 -20.305 2.874   1.00 10.55 ?  95  VAL   B O    1 
ATOM   5311 C CB   . VAL   B 1 95  ? 40.569 -18.914 0.786   1.00 9.97  ?  95  VAL   B CB   1 
ATOM   5312 C CG1  . VAL   B 1 95  ? 39.192 -19.357 1.270   1.00 11.11 ?  95  VAL   B CG1  1 
ATOM   5313 C CG2  . VAL   B 1 95  ? 40.450 -17.930 -0.349  1.00 10.38 ?  95  VAL   B CG2  1 
ATOM   5314 H H    . VAL   B 1 95  ? 43.175 -18.495 1.144   1.00 11.70 ?  95  VAL   B H    1 
ATOM   5315 H HA   . VAL   B 1 95  ? 40.889 -17.562 2.308   1.00 11.92 ?  95  VAL   B HA   1 
ATOM   5316 H HB   . VAL   B 1 95  ? 41.026 -19.698 0.450   1.00 11.96 ?  95  VAL   B HB   1 
ATOM   5317 H HG11 . VAL   B 1 95  ? 38.628 -19.549 0.498   1.00 13.32 ?  95  VAL   B HG11 1 
ATOM   5318 H HG12 . VAL   B 1 95  ? 39.282 -20.159 1.810   1.00 13.32 ?  95  VAL   B HG12 1 
ATOM   5319 H HG13 . VAL   B 1 95  ? 38.791 -18.647 1.795   1.00 13.32 ?  95  VAL   B HG13 1 
ATOM   5320 H HG21 . VAL   B 1 95  ? 39.871 -18.304 -1.030  1.00 12.44 ?  95  VAL   B HG21 1 
ATOM   5321 H HG22 . VAL   B 1 95  ? 40.074 -17.104 -0.008  1.00 12.44 ?  95  VAL   B HG22 1 
ATOM   5322 H HG23 . VAL   B 1 95  ? 41.333 -17.769 -0.712  1.00 12.44 ?  95  VAL   B HG23 1 
ATOM   5323 N N    . VAL   B 1 96  ? 40.823 -19.181 4.134   1.00 10.52 ?  96  VAL   B N    1 
ATOM   5324 C CA   . VAL   B 1 96  ? 40.904 -20.097 5.270   1.00 10.77 ?  96  VAL   B CA   1 
ATOM   5325 C C    . VAL   B 1 96  ? 39.714 -21.055 5.226   1.00 10.97 ?  96  VAL   B C    1 
ATOM   5326 O O    . VAL   B 1 96  ? 38.596 -20.696 5.610   1.00 11.66 ?  96  VAL   B O    1 
ATOM   5327 C CB   . VAL   B 1 96  ? 40.959 -19.350 6.606   1.00 11.53 ?  96  VAL   B CB   1 
ATOM   5328 C CG1  . VAL   B 1 96  ? 41.141 -20.345 7.747   1.00 12.24 ?  96  VAL   B CG1  1 
ATOM   5329 C CG2  . VAL   B 1 96  ? 42.071 -18.319 6.613   1.00 12.29 ?  96  VAL   B CG2  1 
ATOM   5330 H H    . VAL   B 1 96  ? 40.259 -18.543 4.248   1.00 12.61 ?  96  VAL   B H    1 
ATOM   5331 H HA   . VAL   B 1 96  ? 41.717 -20.626 5.195   1.00 12.91 ?  96  VAL   B HA   1 
ATOM   5332 H HB   . VAL   B 1 96  ? 40.117 -18.889 6.745   1.00 13.83 ?  96  VAL   B HB   1 
ATOM   5333 H HG11 . VAL   B 1 96  ? 41.329 -19.856 8.567   1.00 14.68 ?  96  VAL   B HG11 1 
ATOM   5334 H HG12 . VAL   B 1 96  ? 40.330 -20.864 7.856   1.00 14.68 ?  96  VAL   B HG12 1 
ATOM   5335 H HG13 . VAL   B 1 96  ? 41.886 -20.933 7.542   1.00 14.68 ?  96  VAL   B HG13 1 
ATOM   5336 H HG21 . VAL   B 1 96  ? 42.121 -17.909 7.494   1.00 14.74 ?  96  VAL   B HG21 1 
ATOM   5337 H HG22 . VAL   B 1 96  ? 42.911 -18.750 6.400   1.00 14.74 ?  96  VAL   B HG22 1 
ATOM   5338 H HG23 . VAL   B 1 96  ? 41.874 -17.634 5.949   1.00 14.74 ?  96  VAL   B HG23 1 
ATOM   5339 N N    . GLY   B 1 97  ? 39.952 -22.291 4.793   1.00 11.12 ?  97  GLY   B N    1 
ATOM   5340 C CA   . GLY   B 1 97  ? 38.978 -23.347 4.949   1.00 11.59 ?  97  GLY   B CA   1 
ATOM   5341 C C    . GLY   B 1 97  ? 39.092 -23.954 6.328   1.00 12.39 ?  97  GLY   B C    1 
ATOM   5342 O O    . GLY   B 1 97  ? 40.131 -23.829 6.989   1.00 12.97 ?  97  GLY   B O    1 
ATOM   5343 H H    . GLY   B 1 97  ? 40.684 -22.537 4.406   1.00 13.34 ?  97  GLY   B H    1 
ATOM   5344 H HA2  . GLY   B 1 97  ? 38.086 -22.977 4.829   1.00 13.89 ?  97  GLY   B HA2  1 
ATOM   5345 H HA3  . GLY   B 1 97  ? 39.124 -24.030 4.277   1.00 13.89 ?  97  GLY   B HA3  1 
ATOM   5346 N N    . PRO   B 1 98  ? 38.045 -24.638 6.787   1.00 13.11 ?  98  PRO   B N    1 
ATOM   5347 C CA   . PRO   B 1 98  ? 38.132 -25.333 8.074   1.00 13.85 ?  98  PRO   B CA   1 
ATOM   5348 C C    . PRO   B 1 98  ? 39.158 -26.453 8.029   1.00 13.33 ?  98  PRO   B C    1 
ATOM   5349 O O    . PRO   B 1 98  ? 39.265 -27.189 7.047   1.00 13.81 ?  98  PRO   B O    1 
ATOM   5350 C CB   . PRO   B 1 98  ? 36.716 -25.880 8.269   1.00 14.18 ?  98  PRO   B CB   1 
ATOM   5351 C CG   . PRO   B 1 98  ? 36.168 -26.012 6.891   1.00 13.81 ?  98  PRO   B CG   1 
ATOM   5352 C CD   . PRO   B 1 98  ? 36.732 -24.831 6.146   1.00 12.91 ?  98  PRO   B CD   1 
ATOM   5353 H HA   . PRO   B 1 98  ? 38.352 -24.711 8.781   1.00 16.61 ?  98  PRO   B HA   1 
ATOM   5354 H HB2  . PRO   B 1 98  ? 36.758 -26.746 8.705   1.00 17.01 ?  98  PRO   B HB2  1 
ATOM   5355 H HB3  . PRO   B 1 98  ? 36.193 -25.255 8.788   1.00 17.01 ?  98  PRO   B HB3  1 
ATOM   5356 H HG2  . PRO   B 1 98  ? 36.473 -26.847 6.497   1.00 16.56 ?  98  PRO   B HG2  1 
ATOM   5357 H HG3  . PRO   B 1 98  ? 35.203 -25.974 6.917   1.00 16.56 ?  98  PRO   B HG3  1 
ATOM   5358 H HD2  . PRO   B 1 98  ? 36.837 -25.044 5.200   1.00 15.48 ?  98  PRO   B HD2  1 
ATOM   5359 H HD3  . PRO   B 1 98  ? 36.180 -24.047 6.274   1.00 15.48 ?  98  PRO   B HD3  1 
ATOM   5360 N N    . ASN   B 1 99  ? 39.906 -26.584 9.116   1.00 14.40 ?  99  ASN   B N    1 
ATOM   5361 C CA   . ASN   B 1 99  ? 40.882 -27.655 9.275   1.00 15.34 ?  99  ASN   B CA   1 
ATOM   5362 C C    . ASN   B 1 99  ? 40.244 -28.739 10.143  1.00 17.22 ?  99  ASN   B C    1 
ATOM   5363 O O    . ASN   B 1 99  ? 40.148 -28.595 11.364  1.00 17.80 ?  99  ASN   B O    1 
ATOM   5364 C CB   . ASN   B 1 99  ? 42.155 -27.100 9.899   1.00 15.84 ?  99  ASN   B CB   1 
ATOM   5365 C CG   . ASN   B 1 99  ? 43.284 -28.106 9.909   1.00 16.79 ?  99  ASN   B CG   1 
ATOM   5366 O OD1  . ASN   B 1 99  ? 43.058 -29.297 10.079  1.00 17.53 ?  99  ASN   B OD1  1 
ATOM   5367 N ND2  . ASN   B 1 99  ? 44.505 -27.631 9.720   1.00 17.11 ?  99  ASN   B ND2  1 
ATOM   5368 H H    . ASN   B 1 99  ? 39.864 -26.056 9.793   1.00 17.27 ?  99  ASN   B H    1 
ATOM   5369 H HA   . ASN   B 1 99  ? 41.097 -28.042 8.412   1.00 18.40 ?  99  ASN   B HA   1 
ATOM   5370 H HB2  . ASN   B 1 99  ? 42.444 -26.332 9.394   1.00 18.99 ?  99  ASN   B HB2  1 
ATOM   5371 H HB3  . ASN   B 1 99  ? 41.968 -26.849 10.820  1.00 18.99 ?  99  ASN   B HB3  1 
ATOM   5372 H HD21 . ASN   B 1 99  ? 45.178 -28.165 9.720   1.00 20.53 ?  99  ASN   B HD21 1 
ATOM   5373 H HD22 . ASN   B 1 99  ? 44.618 -26.789 9.601   1.00 20.53 ?  99  ASN   B HD22 1 
ATOM   5374 N N    A VAL   B 1 100 ? 39.787 -29.817 9.499   0.88 18.98 ?  100 VAL   B N    1 
ATOM   5375 N N    B VAL   B 1 100 ? 39.794 -29.822 9.501   0.12 19.20 ?  100 VAL   B N    1 
ATOM   5376 C CA   A VAL   B 1 100 ? 39.162 -30.919 10.227  0.88 21.65 ?  100 VAL   B CA   1 
ATOM   5377 C CA   B VAL   B 1 100 ? 39.168 -30.921 10.233  0.12 21.26 ?  100 VAL   B CA   1 
ATOM   5378 C C    A VAL   B 1 100 ? 40.156 -31.592 11.166  0.88 21.92 ?  100 VAL   B C    1 
ATOM   5379 C C    B VAL   B 1 100 ? 40.163 -31.577 11.179  0.12 21.97 ?  100 VAL   B C    1 
ATOM   5380 O O    A VAL   B 1 100 ? 39.769 -32.112 12.220  0.88 22.45 ?  100 VAL   B O    1 
ATOM   5381 O O    B VAL   B 1 100 ? 39.785 -32.057 12.255  0.12 22.17 ?  100 VAL   B O    1 
ATOM   5382 C CB   A VAL   B 1 100 ? 38.521 -31.916 9.239   0.88 24.45 ?  100 VAL   B CB   1 
ATOM   5383 C CB   B VAL   B 1 100 ? 38.542 -31.935 9.253   0.12 22.48 ?  100 VAL   B CB   1 
ATOM   5384 C CG1  A VAL   B 1 100 ? 38.037 -33.164 9.964   0.88 25.47 ?  100 VAL   B CG1  1 
ATOM   5385 C CG1  B VAL   B 1 100 ? 37.994 -33.145 10.000  0.12 22.93 ?  100 VAL   B CG1  1 
ATOM   5386 C CG2  A VAL   B 1 100 ? 37.370 -31.257 8.491   0.88 25.19 ?  100 VAL   B CG2  1 
ATOM   5387 C CG2  B VAL   B 1 100 ? 37.443 -31.270 8.440   0.12 22.83 ?  100 VAL   B CG2  1 
ATOM   5388 H H    A VAL   B 1 100 ? 39.814 -29.925 8.646   0.88 22.77 ?  100 VAL   B H    1 
ATOM   5389 H H    B VAL   B 1 100 ? 39.837 -29.943 8.652   0.12 23.03 ?  100 VAL   B H    1 
ATOM   5390 H HA   A VAL   B 1 100 ? 38.444 -30.560 10.772  0.88 25.97 ?  100 VAL   B HA   1 
ATOM   5391 H HA   B VAL   B 1 100 ? 38.450 -30.565 10.775  0.12 25.50 ?  100 VAL   B HA   1 
ATOM   5392 H HB   A VAL   B 1 100 ? 39.184 -32.191 8.589   0.88 29.33 ?  100 VAL   B HB   1 
ATOM   5393 H HB   B VAL   B 1 100 ? 39.223 -32.248 8.639   0.12 26.96 ?  100 VAL   B HB   1 
ATOM   5394 H HG11 A VAL   B 1 100 ? 37.449 -33.664 9.374   0.88 30.55 ?  100 VAL   B HG11 1 
ATOM   5395 H HG11 B VAL   B 1 100 ? 37.425 -33.655 9.399   0.12 27.51 ?  100 VAL   B HG11 1 
ATOM   5396 H HG12 A VAL   B 1 100 ? 38.801 -33.712 10.204  0.88 30.55 ?  100 VAL   B HG12 1 
ATOM   5397 H HG12 B VAL   B 1 100 ? 38.733 -33.698 10.298  0.12 27.51 ?  100 VAL   B HG12 1 
ATOM   5398 H HG13 A VAL   B 1 100 ? 37.553 -32.900 10.762  0.88 30.55 ?  100 VAL   B HG13 1 
ATOM   5399 H HG13 B VAL   B 1 100 ? 37.477 -32.841 10.761  0.12 27.51 ?  100 VAL   B HG13 1 
ATOM   5400 H HG21 A VAL   B 1 100 ? 36.985 -31.900 7.873   0.88 30.22 ?  100 VAL   B HG21 1 
ATOM   5401 H HG21 B VAL   B 1 100 ? 37.046 -31.928 7.848   0.12 27.39 ?  100 VAL   B HG21 1 
ATOM   5402 H HG22 A VAL   B 1 100 ? 36.697 -30.974 9.131   0.88 30.22 ?  100 VAL   B HG22 1 
ATOM   5403 H HG22 B VAL   B 1 100 ? 36.770 -30.922 9.046   0.12 27.39 ?  100 VAL   B HG22 1 
ATOM   5404 H HG23 A VAL   B 1 100 ? 37.707 -30.492 8.004   0.88 30.22 ?  100 VAL   B HG23 1 
ATOM   5405 H HG23 B VAL   B 1 100 ? 37.829 -30.548 7.922   0.12 27.39 ?  100 VAL   B HG23 1 
ATOM   5406 N N    . ASN   B 1 101 ? 41.442 -31.615 10.802  1.00 22.37 ?  101 ASN   B N    1 
ATOM   5407 C CA   . ASN   B 1 101 ? 42.470 -32.158 11.689  1.00 24.52 ?  101 ASN   B CA   1 
ATOM   5408 C C    . ASN   B 1 101 ? 42.648 -31.329 12.955  1.00 26.52 ?  101 ASN   B C    1 
ATOM   5409 O O    . ASN   B 1 101 ? 43.284 -31.805 13.904  1.00 27.66 ?  101 ASN   B O    1 
ATOM   5410 C CB   . ASN   B 1 101 ? 43.807 -32.278 10.951  1.00 24.96 ?  101 ASN   B CB   1 
ATOM   5411 C CG   . ASN   B 1 101 ? 43.813 -33.406 9.939   1.00 24.82 ?  101 ASN   B CG   1 
ATOM   5412 O OD1  . ASN   B 1 101 ? 43.150 -34.421 10.128  1.00 25.80 ?  101 ASN   B OD1  1 
ATOM   5413 N ND2  . ASN   B 1 101 ? 44.559 -33.229 8.854   1.00 24.53 ?  101 ASN   B ND2  1 
ATOM   5414 H H    A ASN   B 1 101 ? 41.737 -31.334 10.044  0.88 26.83 ?  101 ASN   B H    1 
ATOM   5415 H H    B ASN   B 1 101 ? 41.734 -31.337 10.042  0.12 26.83 ?  101 ASN   B H    1 
ATOM   5416 H HA   . ASN   B 1 101 ? 42.204 -33.046 11.961  1.00 29.42 ?  101 ASN   B HA   1 
ATOM   5417 H HB2  . ASN   B 1 101 ? 43.991 -31.452 10.477  1.00 29.94 ?  101 ASN   B HB2  1 
ATOM   5418 H HB3  . ASN   B 1 101 ? 44.510 -32.451 11.596  1.00 29.94 ?  101 ASN   B HB3  1 
ATOM   5419 H HD21 . ASN   B 1 101 ? 44.596 -33.842 8.252   1.00 29.43 ?  101 ASN   B HD21 1 
ATOM   5420 H HD22 . ASN   B 1 101 ? 45.007 -32.501 8.754   1.00 29.43 ?  101 ASN   B HD22 1 
ATOM   5421 N N    . LYS   B 1 102 ? 42.114 -30.106 12.982  1.00 28.51 ?  102 LYS   B N    1 
ATOM   5422 C CA   . LYS   B 1 102 ? 42.086 -29.263 14.170  1.00 30.96 ?  102 LYS   B CA   1 
ATOM   5423 C C    . LYS   B 1 102 ? 40.705 -29.213 14.813  1.00 30.20 ?  102 LYS   B C    1 
ATOM   5424 O O    . LYS   B 1 102 ? 40.488 -28.415 15.729  1.00 30.63 ?  102 LYS   B O    1 
ATOM   5425 C CB   . LYS   B 1 102 ? 42.518 -27.838 13.820  1.00 34.43 ?  102 LYS   B CB   1 
ATOM   5426 C CG   . LYS   B 1 102 ? 43.982 -27.678 13.451  1.00 37.70 ?  102 LYS   B CG   1 
ATOM   5427 C CD   . LYS   B 1 102 ? 44.255 -26.250 12.999  1.00 40.64 ?  102 LYS   B CD   1 
ATOM   5428 C CE   . LYS   B 1 102 ? 45.738 -25.981 12.810  1.00 42.94 ?  102 LYS   B CE   1 
ATOM   5429 N NZ   . LYS   B 1 102 ? 45.980 -24.580 12.353  1.00 44.24 ?  102 LYS   B NZ   1 
ATOM   5430 H H    . LYS   B 1 102 ? 41.743 -29.733 12.300  1.00 34.20 ?  102 LYS   B H    1 
ATOM   5431 H HA   . LYS   B 1 102 ? 42.717 -29.614 14.818  1.00 37.14 ?  102 LYS   B HA   1 
ATOM   5432 H HB2  . LYS   B 1 102 ? 41.990 -27.533 13.066  1.00 41.31 ?  102 LYS   B HB2  1 
ATOM   5433 H HB3  . LYS   B 1 102 ? 42.346 -27.268 14.587  1.00 41.31 ?  102 LYS   B HB3  1 
ATOM   5434 H HG2  . LYS   B 1 102 ? 44.535 -27.867 14.225  1.00 45.23 ?  102 LYS   B HG2  1 
ATOM   5435 H HG3  . LYS   B 1 102 ? 44.200 -28.279 12.722  1.00 45.23 ?  102 LYS   B HG3  1 
ATOM   5436 H HD2  . LYS   B 1 102 ? 43.809 -26.095 12.151  1.00 48.76 ?  102 LYS   B HD2  1 
ATOM   5437 H HD3  . LYS   B 1 102 ? 43.918 -25.635 13.670  1.00 48.76 ?  102 LYS   B HD3  1 
ATOM   5438 H HE2  . LYS   B 1 102 ? 46.197 -26.109 13.656  1.00 51.52 ?  102 LYS   B HE2  1 
ATOM   5439 H HE3  . LYS   B 1 102 ? 46.092 -26.586 12.140  1.00 51.52 ?  102 LYS   B HE3  1 
ATOM   5440 H HZ1  . LYS   B 1 102 ? 46.852 -24.440 12.248  1.00 53.08 ?  102 LYS   B HZ1  1 
ATOM   5441 H HZ2  . LYS   B 1 102 ? 45.568 -24.439 11.576  1.00 53.08 ?  102 LYS   B HZ2  1 
ATOM   5442 H HZ3  . LYS   B 1 102 ? 45.664 -24.005 12.955  1.00 53.08 ?  102 LYS   B HZ3  1 
ATOM   5443 N N    A GLY   B 1 103 ? 39.764 -30.028 14.344  0.88 29.27 ?  103 GLY   B N    1 
ATOM   5444 N N    B GLY   B 1 103 ? 39.770 -30.039 14.348  0.12 29.98 ?  103 GLY   B N    1 
ATOM   5445 C CA   A GLY   B 1 103 ? 38.434 -30.055 14.917  0.88 28.99 ?  103 GLY   B CA   1 
ATOM   5446 C CA   B GLY   B 1 103 ? 38.442 -30.084 14.924  0.12 29.69 ?  103 GLY   B CA   1 
ATOM   5447 C C    A GLY   B 1 103 ? 37.505 -28.964 14.434  0.88 27.98 ?  103 GLY   B C    1 
ATOM   5448 C C    B GLY   B 1 103 ? 37.516 -28.975 14.484  0.12 29.13 ?  103 GLY   B C    1 
ATOM   5449 O O    A GLY   B 1 103 ? 36.402 -28.828 14.976  0.88 28.67 ?  103 GLY   B O    1 
ATOM   5450 O O    B GLY   B 1 103 ? 36.479 -28.764 15.120  0.12 29.31 ?  103 GLY   B O    1 
ATOM   5451 H H    A GLY   B 1 103 ? 39.873 -30.571 13.688  0.88 35.12 ?  103 GLY   B H    1 
ATOM   5452 H H    B GLY   B 1 103 ? 39.885 -30.584 13.695  0.12 35.97 ?  103 GLY   B H    1 
ATOM   5453 H HA2  A GLY   B 1 103 ? 38.021 -30.906 14.710  0.88 34.78 ?  103 GLY   B HA2  1 
ATOM   5454 H HA2  B GLY   B 1 103 ? 38.029 -30.932 14.692  0.12 35.62 ?  103 GLY   B HA2  1 
ATOM   5455 H HA3  A GLY   B 1 103 ? 38.508 -29.985 15.884  0.88 34.78 ?  103 GLY   B HA3  1 
ATOM   5456 H HA3  B GLY   B 1 103 ? 38.514 -30.042 15.889  0.12 35.62 ?  103 GLY   B HA3  1 
ATOM   5457 N N    A GLU   B 1 104 ? 37.908 -28.187 13.434  0.88 26.09 ?  104 GLU   B N    1 
ATOM   5458 N N    B GLU   B 1 104 ? 37.853 -28.258 13.416  0.12 28.25 ?  104 GLU   B N    1 
ATOM   5459 C CA   A GLU   B 1 104 ? 37.076 -27.094 12.958  0.88 24.25 ?  104 GLU   B CA   1 
ATOM   5460 C CA   B GLU   B 1 104 ? 37.023 -27.154 12.958  0.12 27.33 ?  104 GLU   B CA   1 
ATOM   5461 C C    A GLU   B 1 104 ? 35.906 -27.627 12.135  0.88 25.05 ?  104 GLU   B C    1 
ATOM   5462 C C    B GLU   B 1 104 ? 35.862 -27.668 12.114  0.12 27.26 ?  104 GLU   B C    1 
ATOM   5463 O O    A GLU   B 1 104 ? 35.966 -28.714 11.554  0.88 26.08 ?  104 GLU   B O    1 
ATOM   5464 O O    B GLU   B 1 104 ? 35.948 -28.713 11.463  0.12 27.29 ?  104 GLU   B O    1 
ATOM   5465 C CB   A GLU   B 1 104 ? 37.922 -26.101 12.162  0.88 22.56 ?  104 GLU   B CB   1 
ATOM   5466 C CB   B GLU   B 1 104 ? 37.866 -26.151 12.171  0.12 26.56 ?  104 GLU   B CB   1 
ATOM   5467 C CG   A GLU   B 1 104 ? 39.016 -25.489 13.019  0.88 21.14 ?  104 GLU   B CG   1 
ATOM   5468 C CG   B GLU   B 1 104 ? 38.959 -25.508 13.015  0.12 25.89 ?  104 GLU   B CG   1 
ATOM   5469 C CD   A GLU   B 1 104 ? 39.966 -24.591 12.260  0.88 19.73 ?  104 GLU   B CD   1 
ATOM   5470 C CD   B GLU   B 1 104 ? 39.879 -24.612 12.208  0.12 25.38 ?  104 GLU   B CD   1 
ATOM   5471 O OE1  A GLU   B 1 104 ? 39.977 -24.604 11.010  0.88 18.14 ?  104 GLU   B OE1  1 
ATOM   5472 O OE1  B GLU   B 1 104 ? 39.786 -24.620 10.963  0.12 25.15 ?  104 GLU   B OE1  1 
ATOM   5473 O OE2  A GLU   B 1 104 ? 40.714 -23.864 12.942  0.88 20.41 -1 104 GLU   B OE2  1 
ATOM   5474 O OE2  B GLU   B 1 104 ? 40.697 -23.897 12.824  0.12 25.31 -1 104 GLU   B OE2  1 
ATOM   5475 H H    A GLU   B 1 104 ? 38.658 -28.268 13.024  0.88 31.30 ?  104 GLU   B H    1 
ATOM   5476 H H    B GLU   B 1 104 ? 38.559 -28.388 12.942  0.12 33.89 ?  104 GLU   B H    1 
ATOM   5477 H HA   A GLU   B 1 104 ? 36.713 -26.622 13.724  0.88 29.09 ?  104 GLU   B HA   1 
ATOM   5478 H HA   B GLU   B 1 104 ? 36.653 -26.696 13.726  0.12 32.79 ?  104 GLU   B HA   1 
ATOM   5479 H HB2  A GLU   B 1 104 ? 38.341 -26.559 11.418  0.88 27.07 ?  104 GLU   B HB2  1 
ATOM   5480 H HB2  B GLU   B 1 104 ? 38.292 -26.607 11.428  0.12 31.86 ?  104 GLU   B HB2  1 
ATOM   5481 H HB3  A GLU   B 1 104 ? 37.354 -25.383 11.839  0.88 27.07 ?  104 GLU   B HB3  1 
ATOM   5482 H HB3  B GLU   B 1 104 ? 37.290 -25.444 11.840  0.12 31.86 ?  104 GLU   B HB3  1 
ATOM   5483 H HG2  A GLU   B 1 104 ? 38.610 -24.955 13.722  0.88 25.36 ?  104 GLU   B HG2  1 
ATOM   5484 H HG2  B GLU   B 1 104 ? 38.546 -24.968 13.708  0.12 31.06 ?  104 GLU   B HG2  1 
ATOM   5485 H HG3  A GLU   B 1 104 ? 39.547 -26.197 13.416  0.88 25.36 ?  104 GLU   B HG3  1 
ATOM   5486 H HG3  B GLU   B 1 104 ? 39.497 -26.207 13.421  0.12 31.06 ?  104 GLU   B HG3  1 
ATOM   5487 N N    A ASP   B 1 105 ? 34.832 -26.842 12.098  0.88 25.14 ?  105 ASP   B N    1 
ATOM   5488 N N    B ASP   B 1 105 ? 34.765 -26.913 12.133  0.12 27.23 ?  105 ASP   B N    1 
ATOM   5489 C CA   A ASP   B 1 105 ? 33.554 -27.301 11.569  0.88 25.87 ?  105 ASP   B CA   1 
ATOM   5490 C CA   B ASP   B 1 105 ? 33.512 -27.370 11.545  0.12 27.27 ?  105 ASP   B CA   1 
ATOM   5491 C C    A ASP   B 1 105 ? 33.597 -27.342 10.046  0.88 24.14 ?  105 ASP   B C    1 
ATOM   5492 C C    B ASP   B 1 105 ? 33.617 -27.394 10.025  0.12 26.42 ?  105 ASP   B C    1 
ATOM   5493 O O    A ASP   B 1 105 ? 33.721 -26.301 9.391   0.88 23.34 ?  105 ASP   B O    1 
ATOM   5494 O O    B ASP   B 1 105 ? 33.870 -26.363 9.393   0.12 26.26 ?  105 ASP   B O    1 
ATOM   5495 C CB   A ASP   B 1 105 ? 32.437 -26.378 12.054  0.88 28.80 ?  105 ASP   B CB   1 
ATOM   5496 C CB   B ASP   B 1 105 ? 32.373 -26.455 11.989  0.12 28.11 ?  105 ASP   B CB   1 
ATOM   5497 C CG   A ASP   B 1 105 ? 31.055 -26.881 11.673  0.88 31.25 ?  105 ASP   B CG   1 
ATOM   5498 C CG   B ASP   B 1 105 ? 31.006 -27.029 11.667  0.12 28.86 ?  105 ASP   B CG   1 
ATOM   5499 O OD1  A ASP   B 1 105 ? 30.962 -27.912 10.974  0.88 31.64 ?  105 ASP   B OD1  1 
ATOM   5500 O OD1  B ASP   B 1 105 ? 30.943 -28.078 10.993  0.12 29.08 ?  105 ASP   B OD1  1 
ATOM   5501 O OD2  A ASP   B 1 105 ? 30.057 -26.249 12.084  0.88 32.84 -1 105 ASP   B OD2  1 
ATOM   5502 O OD2  B ASP   B 1 105 ? 29.994 -26.434 12.094  0.12 29.20 -1 105 ASP   B OD2  1 
ATOM   5503 H H    A ASP   B 1 105 ? 34.825 -26.027 12.369  0.88 30.16 ?  105 ASP   B H    1 
ATOM   5504 H H    B ASP   B 1 105 ? 34.723 -26.128 12.479  0.12 32.67 ?  105 ASP   B H    1 
ATOM   5505 H HA   A ASP   B 1 105 ? 33.372 -28.196 11.897  0.88 31.04 ?  105 ASP   B HA   1 
ATOM   5506 H HA   B ASP   B 1 105 ? 33.317 -28.269 11.853  0.12 32.71 ?  105 ASP   B HA   1 
ATOM   5507 H HB2  A ASP   B 1 105 ? 32.485 -26.307 13.023  0.88 34.55 ?  105 ASP   B HB2  1 
ATOM   5508 H HB2  B ASP   B 1 105 ? 32.429 -26.323 12.950  0.12 33.72 ?  105 ASP   B HB2  1 
ATOM   5509 H HB3  A ASP   B 1 105 ? 32.561 -25.500 11.656  0.88 34.55 ?  105 ASP   B HB3  1 
ATOM   5510 H HB3  B ASP   B 1 105 ? 32.454 -25.602 11.534  0.12 33.72 ?  105 ASP   B HB3  1 
ATOM   5511 N N    A ILE   B 1 106 ? 33.479 -28.550 9.484   0.88 23.96 ?  106 ILE   B N    1 
ATOM   5512 N N    B ILE   B 1 106 ? 33.416 -28.578 9.439   0.12 25.76 ?  106 ILE   B N    1 
ATOM   5513 C CA   A ILE   B 1 106 ? 33.466 -28.729 8.037   0.88 23.06 ?  106 ILE   B CA   1 
ATOM   5514 C CA   B ILE   B 1 106 ? 33.442 -28.728 7.989   0.12 25.12 ?  106 ILE   B CA   1 
ATOM   5515 C C    A ILE   B 1 106 ? 32.365 -27.905 7.373   0.88 22.03 ?  106 ILE   B C    1 
ATOM   5516 C C    B ILE   B 1 106 ? 32.348 -27.908 7.316   0.12 24.53 ?  106 ILE   B C    1 
ATOM   5517 O O    A ILE   B 1 106 ? 32.466 -27.574 6.186   0.88 21.09 ?  106 ILE   B O    1 
ATOM   5518 O O    B ILE   B 1 106 ? 32.439 -27.618 6.119   0.12 24.42 ?  106 ILE   B O    1 
ATOM   5519 C CB   A ILE   B 1 106 ? 33.363 -30.238 7.708   0.88 24.06 ?  106 ILE   B CB   1 
ATOM   5520 C CB   B ILE   B 1 106 ? 33.353 -30.227 7.620   0.12 25.14 ?  106 ILE   B CB   1 
ATOM   5521 C CG1  A ILE   B 1 106 ? 33.609 -30.494 6.222   0.88 24.46 ?  106 ILE   B CG1  1 
ATOM   5522 C CG1  B ILE   B 1 106 ? 33.614 -30.443 6.127   0.12 25.11 ?  106 ILE   B CG1  1 
ATOM   5523 C CG2  A ILE   B 1 106 ? 32.007 -30.792 8.135   0.88 24.93 ?  106 ILE   B CG2  1 
ATOM   5524 C CG2  B ILE   B 1 106 ? 31.996 -30.797 8.013   0.12 25.23 ?  106 ILE   B CG2  1 
ATOM   5525 C CD1  A ILE   B 1 106 ? 34.964 -30.023 5.751   0.88 24.66 ?  106 ILE   B CD1  1 
ATOM   5526 C CD1  B ILE   B 1 106 ? 34.969 -29.949 5.668   0.12 25.11 ?  106 ILE   B CD1  1 
ATOM   5527 H H    A ILE   B 1 106 ? 33.418 -29.282 9.929   0.88 28.74 ?  106 ILE   B H    1 
ATOM   5528 H H    B ILE   B 1 106 ? 33.275 -29.310 9.863   0.12 30.90 ?  106 ILE   B H    1 
ATOM   5529 H HA   A ILE   B 1 106 ? 34.314 -28.413 7.693   0.88 27.66 ?  106 ILE   B HA   1 
ATOM   5530 H HA   B ILE   B 1 106 ? 34.292 -28.396 7.668   0.12 30.14 ?  106 ILE   B HA   1 
ATOM   5531 H HB   A ILE   B 1 106 ? 34.048 -30.708 8.212   0.88 28.87 ?  106 ILE   B HB   1 
ATOM   5532 H HB   B ILE   B 1 106 ? 34.035 -30.702 8.117   0.12 30.15 ?  106 ILE   B HB   1 
ATOM   5533 H HG12 A ILE   B 1 106 ? 33.556 -31.451 6.054   0.88 29.34 ?  106 ILE   B HG12 1 
ATOM   5534 H HG12 B ILE   B 1 106 ? 33.569 -31.395 5.937   0.12 30.12 ?  106 ILE   B HG12 1 
ATOM   5535 H HG13 A ILE   B 1 106 ? 32.935 -30.032 5.704   0.88 29.34 ?  106 ILE   B HG13 1 
ATOM   5536 H HG13 B ILE   B 1 106 ? 32.937 -29.976 5.615   0.12 30.12 ?  106 ILE   B HG13 1 
ATOM   5537 H HG21 A ILE   B 1 106 ? 32.016 -31.759 8.038   0.88 29.91 ?  106 ILE   B HG21 1 
ATOM   5538 H HG21 B ILE   B 1 106 ? 32.011 -31.759 7.889   0.12 30.27 ?  106 ILE   B HG21 1 
ATOM   5539 H HG22 A ILE   B 1 106 ? 31.847 -30.557 9.063   0.88 29.91 ?  106 ILE   B HG22 1 
ATOM   5540 H HG22 B ILE   B 1 106 ? 31.823 -30.587 8.944   0.12 30.27 ?  106 ILE   B HG22 1 
ATOM   5541 H HG23 A ILE   B 1 106 ? 31.316 -30.411 7.573   0.88 29.91 ?  106 ILE   B HG23 1 
ATOM   5542 H HG23 B ILE   B 1 106 ? 31.310 -30.402 7.452   0.12 30.27 ?  106 ILE   B HG23 1 
ATOM   5543 H HD11 A ILE   B 1 106 ? 35.167 -30.441 4.901   0.88 29.59 ?  106 ILE   B HD11 1 
ATOM   5544 H HD11 B ILE   B 1 106 ? 35.164 -30.330 4.799   0.12 30.12 ?  106 ILE   B HD11 1 
ATOM   5545 H HD12 A ILE   B 1 106 ? 34.946 -29.058 5.648   0.88 29.59 ?  106 ILE   B HD12 1 
ATOM   5546 H HD12 B ILE   B 1 106 ? 34.948 -28.981 5.608   0.12 30.12 ?  106 ILE   B HD12 1 
ATOM   5547 H HD13 A ILE   B 1 106 ? 35.634 -30.273 6.409   0.88 29.59 ?  106 ILE   B HD13 1 
ATOM   5548 H HD13 B ILE   B 1 106 ? 35.640 -30.229 6.310   0.12 30.12 ?  106 ILE   B HD13 1 
ATOM   5549 N N    A GLN   B 1 107 ? 31.320 -27.542 8.118   0.88 22.76 ?  107 GLN   B N    1 
ATOM   5550 N N    B GLN   B 1 107 ? 31.308 -27.522 8.062   0.12 24.12 ?  107 GLN   B N    1 
ATOM   5551 C CA   A GLN   B 1 107 ? 30.244 -26.734 7.554   0.88 23.18 ?  107 GLN   B CA   1 
ATOM   5552 C CA   B GLN   B 1 107 ? 30.234 -26.716 7.493   0.12 23.69 ?  107 GLN   B CA   1 
ATOM   5553 C C    A GLN   B 1 107 ? 30.729 -25.379 7.043   0.88 21.18 ?  107 GLN   B C    1 
ATOM   5554 C C    B GLN   B 1 107 ? 30.724 -25.350 7.029   0.12 21.39 ?  107 GLN   B C    1 
ATOM   5555 O O    A GLN   B 1 107 ? 30.087 -24.797 6.166   0.88 21.99 ?  107 GLN   B O    1 
ATOM   5556 O O    B GLN   B 1 107 ? 30.070 -24.723 6.189   0.12 21.48 ?  107 GLN   B O    1 
ATOM   5557 C CB   A GLN   B 1 107 ? 29.141 -26.548 8.600   0.88 26.67 ?  107 GLN   B CB   1 
ATOM   5558 C CB   B GLN   B 1 107 ? 29.113 -26.554 8.525   0.12 25.61 ?  107 GLN   B CB   1 
ATOM   5559 C CG   A GLN   B 1 107 ? 27.809 -26.062 8.040   0.88 30.48 ?  107 GLN   B CG   1 
ATOM   5560 C CG   B GLN   B 1 107 ? 27.789 -26.055 7.958   0.12 27.39 ?  107 GLN   B CG   1 
ATOM   5561 C CD   A GLN   B 1 107 ? 27.726 -24.549 7.939   0.88 33.40 ?  107 GLN   B CD   1 
ATOM   5562 C CD   B GLN   B 1 107 ? 27.684 -24.541 7.947   0.12 28.81 ?  107 GLN   B CD   1 
ATOM   5563 O OE1  A GLN   B 1 107 ? 28.568 -23.830 8.482   0.88 34.55 ?  107 GLN   B OE1  1 
ATOM   5564 O OE1  B GLN   B 1 107 ? 28.519 -23.842 8.523   0.12 29.37 ?  107 GLN   B OE1  1 
ATOM   5565 N NE2  A GLN   B 1 107 ? 26.703 -24.057 7.245   0.88 34.44 ?  107 GLN   B NE2  1 
ATOM   5566 N NE2  B GLN   B 1 107 ? 26.650 -24.027 7.291   0.12 29.26 ?  107 GLN   B NE2  1 
ATOM   5567 H H    A GLN   B 1 107 ? 31.218 -27.747 8.942   0.88 27.30 ?  107 GLN   B H    1 
ATOM   5568 H H    B GLN   B 1 107 ? 31.202 -27.717 8.890   0.12 28.94 ?  107 GLN   B H    1 
ATOM   5569 H HA   A GLN   B 1 107 ? 29.860 -27.218 6.803   0.88 27.80 ?  107 GLN   B HA   1 
ATOM   5570 H HA   B GLN   B 1 107 ? 29.865 -27.182 6.726   0.12 28.42 ?  107 GLN   B HA   1 
ATOM   5571 H HB2  A GLN   B 1 107 ? 28.983 -27.398 9.034   0.88 31.99 ?  107 GLN   B HB2  1 
ATOM   5572 H HB2  B GLN   B 1 107 ? 28.945 -27.414 8.935   0.12 30.72 ?  107 GLN   B HB2  1 
ATOM   5573 H HB3  A GLN   B 1 107 ? 29.444 -25.899 9.254   0.88 31.99 ?  107 GLN   B HB3  1 
ATOM   5574 H HB3  B GLN   B 1 107 ? 29.402 -25.922 9.202   0.12 30.72 ?  107 GLN   B HB3  1 
ATOM   5575 H HG2  A GLN   B 1 107 ? 27.686 -26.426 7.150   0.88 36.57 ?  107 GLN   B HG2  1 
ATOM   5576 H HG2  B GLN   B 1 107 ? 27.697 -26.367 7.045   0.12 32.86 ?  107 GLN   B HG2  1 
ATOM   5577 H HG3  A GLN   B 1 107 ? 27.093 -26.367 8.623   0.88 36.57 ?  107 GLN   B HG3  1 
ATOM   5578 H HG3  B GLN   B 1 107 ? 27.062 -26.404 8.501   0.12 32.86 ?  107 GLN   B HG3  1 
ATOM   5579 H HE21 A GLN   B 1 107 ? 26.134 -24.590 6.878   0.88 41.32 ?  107 GLN   B HE21 1 
ATOM   5580 H HE21 B GLN   B 1 107 ? 26.087 -24.546 6.899   0.12 35.10 ?  107 GLN   B HE21 1 
ATOM   5581 H HE22 A GLN   B 1 107 ? 26.607 -23.206 7.162   0.88 41.32 ?  107 GLN   B HE22 1 
ATOM   5582 H HE22 B GLN   B 1 107 ? 26.545 -23.174 7.258   0.12 35.10 ?  107 GLN   B HE22 1 
ATOM   5583 N N    . LEU   B 1 108 ? 31.858 -24.876 7.550   1.00 19.08 ?  108 LEU   B N    1 
ATOM   5584 C CA   . LEU   B 1 108 ? 32.409 -23.579 7.145   1.00 17.07 ?  108 LEU   B CA   1 
ATOM   5585 C C    . LEU   B 1 108 ? 33.055 -23.599 5.769   1.00 14.90 ?  108 LEU   B C    1 
ATOM   5586 O O    . LEU   B 1 108 ? 33.486 -22.542 5.282   1.00 14.87 ?  108 LEU   B O    1 
ATOM   5587 C CB   . LEU   B 1 108 ? 33.420 -23.099 8.184   1.00 17.59 ?  108 LEU   B CB   1 
ATOM   5588 C CG   . LEU   B 1 108 ? 32.794 -22.622 9.494   1.00 18.71 ?  108 LEU   B CG   1 
ATOM   5589 C CD1  . LEU   B 1 108 ? 33.822 -22.564 10.609  1.00 19.02 ?  108 LEU   B CD1  1 
ATOM   5590 C CD2  . LEU   B 1 108 ? 32.169 -21.255 9.287   1.00 19.89 ?  108 LEU   B CD2  1 
ATOM   5591 H H    A LEU   B 1 108 ? 32.324 -25.273 8.148   0.88 22.89 ?  108 LEU   B H    1 
ATOM   5592 H H    B LEU   B 1 108 ? 32.321 -25.285 8.143   0.12 22.89 ?  108 LEU   B H    1 
ATOM   5593 H HA   . LEU   B 1 108 ? 31.686 -22.937 7.116   1.00 20.48 ?  108 LEU   B HA   1 
ATOM   5594 H HB2  . LEU   B 1 108 ? 34.019 -23.831 8.396   1.00 21.10 ?  108 LEU   B HB2  1 
ATOM   5595 H HB3  . LEU   B 1 108 ? 33.921 -22.360 7.811   1.00 21.10 ?  108 LEU   B HB3  1 
ATOM   5596 H HG   . LEU   B 1 108 ? 32.091 -23.238 9.761   1.00 22.44 ?  108 LEU   B HG   1 
ATOM   5597 H HD11 . LEU   B 1 108 ? 33.385 -22.275 11.428  1.00 22.81 ?  108 LEU   B HD11 1 
ATOM   5598 H HD12 . LEU   B 1 108 ? 34.203 -23.446 10.734  1.00 22.81 ?  108 LEU   B HD12 1 
ATOM   5599 H HD13 . LEU   B 1 108 ? 34.516 -21.932 10.366  1.00 22.81 ?  108 LEU   B HD13 1 
ATOM   5600 H HD21 . LEU   B 1 108 ? 31.847 -20.923 10.139  1.00 23.86 ?  108 LEU   B HD21 1 
ATOM   5601 H HD22 . LEU   B 1 108 ? 32.840 -20.654 8.930   1.00 23.86 ?  108 LEU   B HD22 1 
ATOM   5602 H HD23 . LEU   B 1 108 ? 31.431 -21.336 8.663   1.00 23.86 ?  108 LEU   B HD23 1 
ATOM   5603 N N    . LEU   B 1 109 ? 33.125 -24.767 5.136   1.00 13.94 ?  109 LEU   B N    1 
ATOM   5604 C CA   . LEU   B 1 109 ? 33.756 -24.872 3.829   1.00 13.17 ?  109 LEU   B CA   1 
ATOM   5605 C C    . LEU   B 1 109 ? 32.991 -24.088 2.769   1.00 12.70 ?  109 LEU   B C    1 
ATOM   5606 O O    . LEU   B 1 109 ? 33.605 -23.493 1.876   1.00 12.53 ?  109 LEU   B O    1 
ATOM   5607 C CB   . LEU   B 1 109 ? 33.867 -26.347 3.447   1.00 13.23 ?  109 LEU   B CB   1 
ATOM   5608 C CG   . LEU   B 1 109 ? 34.651 -26.682 2.182   1.00 13.24 ?  109 LEU   B CG   1 
ATOM   5609 C CD1  . LEU   B 1 109 ? 36.034 -26.038 2.204   1.00 13.27 ?  109 LEU   B CD1  1 
ATOM   5610 C CD2  . LEU   B 1 109 ? 34.760 -28.194 2.020   1.00 13.81 ?  109 LEU   B CD2  1 
ATOM   5611 H H    . LEU   B 1 109 ? 32.822 -25.509 5.437   1.00 16.71 ?  109 LEU   B H    1 
ATOM   5612 H HA   . LEU   B 1 109 ? 34.651 -24.507 3.874   1.00 15.79 ?  109 LEU   B HA   1 
ATOM   5613 H HB2  . LEU   B 1 109 ? 34.298 -26.817 4.176   1.00 15.87 ?  109 LEU   B HB2  1 
ATOM   5614 H HB3  . LEU   B 1 109 ? 32.971 -26.700 3.325   1.00 15.87 ?  109 LEU   B HB3  1 
ATOM   5615 H HG   . LEU   B 1 109 ? 34.170 -26.343 1.409   1.00 15.88 ?  109 LEU   B HG   1 
ATOM   5616 H HD11 . LEU   B 1 109 ? 36.569 -26.405 1.483   1.00 15.92 ?  109 LEU   B HD11 1 
ATOM   5617 H HD12 . LEU   B 1 109 ? 35.937 -25.081 2.090   1.00 15.92 ?  109 LEU   B HD12 1 
ATOM   5618 H HD13 . LEU   B 1 109 ? 36.457 -26.230 3.057   1.00 15.92 ?  109 LEU   B HD13 1 
ATOM   5619 H HD21 . LEU   B 1 109 ? 35.333 -28.391 1.261   1.00 16.56 ?  109 LEU   B HD21 1 
ATOM   5620 H HD22 . LEU   B 1 109 ? 35.140 -28.572 2.827   1.00 16.56 ?  109 LEU   B HD22 1 
ATOM   5621 H HD23 . LEU   B 1 109 ? 33.874 -28.563 1.867   1.00 16.56 ?  109 LEU   B HD23 1 
ATOM   5622 N N    . LYS   B 1 110 ? 31.656 -24.060 2.847   1.00 12.40 ?  110 LYS   B N    1 
ATOM   5623 C CA   . LYS   B 1 110 ? 30.897 -23.298 1.859   1.00 12.24 ?  110 LYS   B CA   1 
ATOM   5624 C C    . LYS   B 1 110 ? 31.231 -21.808 1.951   1.00 11.95 ?  110 LYS   B C    1 
ATOM   5625 O O    . LYS   B 1 110 ? 31.484 -21.152 0.933   1.00 11.63 ?  110 LYS   B O    1 
ATOM   5626 C CB   . LYS   B 1 110 ? 29.391 -23.546 2.009   1.00 12.96 ?  110 LYS   B CB   1 
ATOM   5627 C CG   . LYS   B 1 110 ? 28.588 -22.917 0.876   1.00 13.35 ?  110 LYS   B CG   1 
ATOM   5628 C CD   . LYS   B 1 110 ? 27.124 -23.354 0.895   1.00 13.37 ?  110 LYS   B CD   1 
ATOM   5629 C CE   . LYS   B 1 110 ? 26.354 -22.819 -0.313  1.00 13.94 ?  110 LYS   B CE   1 
ATOM   5630 N NZ   . LYS   B 1 110 ? 26.683 -23.525 -1.578  1.00 14.26 ?  110 LYS   B NZ   1 
ATOM   5631 H H    . LYS   B 1 110 ? 31.185 -24.467 3.437   1.00 14.87 ?  110 LYS   B H    1 
ATOM   5632 H HA   . LYS   B 1 110 ? 31.154 -23.600 0.970   1.00 14.68 ?  110 LYS   B HA   1 
ATOM   5633 H HB2  . LYS   B 1 110 ? 29.224 -24.505 1.996   1.00 15.55 ?  110 LYS   B HB2  1 
ATOM   5634 H HB3  . LYS   B 1 110 ? 29.086 -23.167 2.844   1.00 15.55 ?  110 LYS   B HB3  1 
ATOM   5635 H HG2  . LYS   B 1 110 ? 28.608 -21.949 0.967   1.00 16.01 ?  110 LYS   B HG2  1 
ATOM   5636 H HG3  . LYS   B 1 110 ? 28.966 -23.178 0.023   1.00 16.01 ?  110 LYS   B HG3  1 
ATOM   5637 H HD2  . LYS   B 1 110 ? 27.077 -24.325 0.878   1.00 16.03 ?  110 LYS   B HD2  1 
ATOM   5638 H HD3  . LYS   B 1 110 ? 26.694 -23.016 1.699   1.00 16.03 ?  110 LYS   B HD3  1 
ATOM   5639 H HE2  . LYS   B 1 110 ? 25.403 -22.921 -0.158  1.00 16.72 ?  110 LYS   B HE2  1 
ATOM   5640 H HE3  . LYS   B 1 110 ? 26.572 -21.882 -0.434  1.00 16.72 ?  110 LYS   B HE3  1 
ATOM   5641 H HZ1  . LYS   B 1 110 ? 26.218 -23.181 -2.251  1.00 17.10 ?  110 LYS   B HZ1  1 
ATOM   5642 H HZ2  . LYS   B 1 110 ? 27.553 -23.443 -1.754  1.00 17.10 ?  110 LYS   B HZ2  1 
ATOM   5643 H HZ3  . LYS   B 1 110 ? 26.487 -24.391 -1.502  1.00 17.10 ?  110 LYS   B HZ3  1 
ATOM   5644 N N    . SER   B 1 111 ? 31.255 -21.261 3.171   1.00 12.26 ?  111 SER   B N    1 
ATOM   5645 C CA   . SER   B 1 111 ? 31.646 -19.863 3.350   1.00 12.18 ?  111 SER   B CA   1 
ATOM   5646 C C    . SER   B 1 111 ? 33.027 -19.600 2.761   1.00 11.51 ?  111 SER   B C    1 
ATOM   5647 O O    . SER   B 1 111 ? 33.253 -18.565 2.116   1.00 11.87 ?  111 SER   B O    1 
ATOM   5648 C CB   . SER   B 1 111 ? 31.640 -19.508 4.834   1.00 13.11 ?  111 SER   B CB   1 
ATOM   5649 O OG   . SER   B 1 111 ? 30.331 -19.506 5.358   1.00 14.97 ?  111 SER   B OG   1 
ATOM   5650 H H    . SER   B 1 111 ? 31.052 -21.676 3.896   1.00 14.71 ?  111 SER   B H    1 
ATOM   5651 H HA   . SER   B 1 111 ? 31.012 -19.293 2.895   1.00 14.60 ?  111 SER   B HA   1 
ATOM   5652 H HB2  . SER   B 1 111 ? 32.164 -20.162 5.319   1.00 15.72 ?  111 SER   B HB2  1 
ATOM   5653 H HB3  . SER   B 1 111 ? 32.018 -18.626 4.949   1.00 15.72 ?  111 SER   B HB3  1 
ATOM   5654 H HG   . SER   B 1 111 ? 30.342 -19.307 6.180   1.00 17.96 ?  111 SER   B HG   1 
ATOM   5655 N N    . ALA   B 1 112 ? 33.963 -20.523 2.979   1.00 11.65 ?  112 ALA   B N    1 
ATOM   5656 C CA   . ALA   B 1 112 ? 35.307 -20.350 2.438   1.00 11.57 ?  112 ALA   B CA   1 
ATOM   5657 C C    . ALA   B 1 112 ? 35.275 -20.249 0.917   1.00 10.66 ?  112 ALA   B C    1 
ATOM   5658 O O    . ALA   B 1 112 ? 35.905 -19.362 0.328   1.00 11.09 ?  112 ALA   B O    1 
ATOM   5659 C CB   . ALA   B 1 112 ? 36.214 -21.494 2.900   1.00 12.01 ?  112 ALA   B CB   1 
ATOM   5660 H H    . ALA   B 1 112 ? 33.849 -21.251 3.434   1.00 13.97 ?  112 ALA   B H    1 
ATOM   5661 H HA   . ALA   B 1 112 ? 35.674 -19.523 2.783   1.00 13.87 ?  112 ALA   B HA   1 
ATOM   5662 H HB1  . ALA   B 1 112 ? 37.105 -21.351 2.539   1.00 14.40 ?  112 ALA   B HB1  1 
ATOM   5663 H HB2  . ALA   B 1 112 ? 36.252 -21.493 3.871   1.00 14.40 ?  112 ALA   B HB2  1 
ATOM   5664 H HB3  . ALA   B 1 112 ? 35.856 -22.333 2.582   1.00 14.40 ?  112 ALA   B HB3  1 
ATOM   5665 N N    . TYR   B 1 113 ? 34.540 -21.149 0.257   1.00 10.64 ?  113 TYR   B N    1 
ATOM   5666 C CA   . TYR   B 1 113 ? 34.469 -21.097 -1.197  1.00 10.46 ?  113 TYR   B CA   1 
ATOM   5667 C C    . TYR   B 1 113 ? 33.763 -19.848 -1.708  1.00 10.46 ?  113 TYR   B C    1 
ATOM   5668 O O    . TYR   B 1 113 ? 34.035 -19.414 -2.832  1.00 10.43 ?  113 TYR   B O    1 
ATOM   5669 C CB   . TYR   B 1 113 ? 33.800 -22.356 -1.749  1.00 11.06 ?  113 TYR   B CB   1 
ATOM   5670 C CG   . TYR   B 1 113 ? 34.758 -23.504 -2.007  1.00 11.27 ?  113 TYR   B CG   1 
ATOM   5671 C CD1  . TYR   B 1 113 ? 35.755 -23.398 -2.972  1.00 11.71 ?  113 TYR   B CD1  1 
ATOM   5672 C CD2  . TYR   B 1 113 ? 34.657 -24.694 -1.304  1.00 11.42 ?  113 TYR   B CD2  1 
ATOM   5673 C CE1  . TYR   B 1 113 ? 36.630 -24.431 -3.222  1.00 11.73 ?  113 TYR   B CE1  1 
ATOM   5674 C CE2  . TYR   B 1 113 ? 35.526 -25.743 -1.551  1.00 11.84 ?  113 TYR   B CE2  1 
ATOM   5675 C CZ   . TYR   B 1 113 ? 36.509 -25.610 -2.513  1.00 11.98 ?  113 TYR   B CZ   1 
ATOM   5676 O OH   . TYR   B 1 113 ? 37.387 -26.629 -2.790  1.00 12.50 ?  113 TYR   B OH   1 
ATOM   5677 H H    . TYR   B 1 113 ? 34.081 -21.780 0.625   1.00 12.76 ?  113 TYR   B H    1 
ATOM   5678 H HA   . TYR   B 1 113 ? 35.370 -21.080 -1.538  1.00 12.55 ?  113 TYR   B HA   1 
ATOM   5679 H HB2  . TYR   B 1 113 ? 33.136 -22.672 -1.112  1.00 13.26 ?  113 TYR   B HB2  1 
ATOM   5680 H HB3  . TYR   B 1 113 ? 33.366 -22.141 -2.590  1.00 13.26 ?  113 TYR   B HB3  1 
ATOM   5681 H HD1  . TYR   B 1 113 ? 35.838 -22.605 -3.457  1.00 14.05 ?  113 TYR   B HD1  1 
ATOM   5682 H HD2  . TYR   B 1 113 ? 33.990 -24.789 -0.667  1.00 13.70 ?  113 TYR   B HD2  1 
ATOM   5683 H HE1  . TYR   B 1 113 ? 37.292 -24.337 -3.879  1.00 14.07 ?  113 TYR   B HE1  1 
ATOM   5684 H HE2  . TYR   B 1 113 ? 35.440 -26.535 -1.081  1.00 14.20 ?  113 TYR   B HE2  1 
ATOM   5685 H HH   . TYR   B 1 113 ? 37.210 -27.295 -2.308  1.00 14.99 ?  113 TYR   B HH   1 
ATOM   5686 N N    . GLU   B 1 114 ? 32.842 -19.274 -0.928  1.00 10.53 ?  114 GLU   B N    1 
ATOM   5687 C CA   . GLU   B 1 114 ? 32.158 -18.067 -1.383  1.00 10.45 ?  114 GLU   B CA   1 
ATOM   5688 C C    . GLU   B 1 114 ? 33.137 -16.941 -1.681  1.00 10.45 ?  114 GLU   B C    1 
ATOM   5689 O O    . GLU   B 1 114 ? 32.851 -16.080 -2.519  1.00 10.66 ?  114 GLU   B O    1 
ATOM   5690 C CB   . GLU   B 1 114 ? 31.096 -17.641 -0.366  1.00 10.83 ?  114 GLU   B CB   1 
ATOM   5691 C CG   . GLU   B 1 114 ? 29.883 -18.561 -0.434  1.00 11.08 ?  114 GLU   B CG   1 
ATOM   5692 C CD   . GLU   B 1 114 ? 28.861 -18.374 0.676   1.00 11.21 ?  114 GLU   B CD   1 
ATOM   5693 O OE1  . GLU   B 1 114 ? 29.154 -17.763 1.725   1.00 11.64 ?  114 GLU   B OE1  1 
ATOM   5694 O OE2  . GLU   B 1 114 ? 27.736 -18.906 0.507   1.00 12.31 -1 114 GLU   B OE2  1 
ATOM   5695 H H    . GLU   B 1 114 ? 32.595 -19.565 -0.154  1.00 12.62 ?  114 GLU   B H    1 
ATOM   5696 H HA   . GLU   B 1 114 ? 31.697 -18.268 -2.206  1.00 12.53 ?  114 GLU   B HA   1 
ATOM   5697 H HB2  . GLU   B 1 114 ? 31.467 -17.692 0.533   1.00 12.99 ?  114 GLU   B HB2  1 
ATOM   5698 H HB3  . GLU   B 1 114 ? 30.804 -16.739 -0.559  1.00 12.99 ?  114 GLU   B HB3  1 
ATOM   5699 H HG2  . GLU   B 1 114 ? 29.435 -18.414 -1.277  1.00 13.29 ?  114 GLU   B HG2  1 
ATOM   5700 H HG3  . GLU   B 1 114 ? 30.198 -19.483 -0.392  1.00 13.29 ?  114 GLU   B HG3  1 
ATOM   5701 N N    . ASN   B 1 115 ? 34.302 -16.933 -1.025  1.00 10.54 ?  115 ASN   B N    1 
ATOM   5702 C CA   . ASN   B 1 115 ? 35.297 -15.904 -1.321  1.00 10.64 ?  115 ASN   B CA   1 
ATOM   5703 C C    . ASN   B 1 115 ? 35.704 -15.920 -2.788  1.00 10.08 ?  115 ASN   B C    1 
ATOM   5704 O O    . ASN   B 1 115 ? 36.090 -14.880 -3.340  1.00 10.77 ?  115 ASN   B O    1 
ATOM   5705 C CB   . ASN   B 1 115 ? 36.536 -16.085 -0.437  1.00 10.82 ?  115 ASN   B CB   1 
ATOM   5706 C CG   . ASN   B 1 115 ? 36.267 -15.819 1.027   1.00 11.34 ?  115 ASN   B CG   1 
ATOM   5707 O OD1  . ASN   B 1 115 ? 36.273 -14.674 1.471   1.00 13.19 ?  115 ASN   B OD1  1 
ATOM   5708 N ND2  . ASN   B 1 115 ? 36.104 -16.886 1.802   1.00 11.41 ?  115 ASN   B ND2  1 
ATOM   5709 H H    . ASN   B 1 115 ? 34.532 -17.491 -0.405  1.00 12.64 ?  115 ASN   B H    1 
ATOM   5710 H HA   . ASN   B 1 115 ? 34.921 -15.030 -1.123  1.00 12.76 ?  115 ASN   B HA   1 
ATOM   5711 H HB2  . ASN   B 1 115 ? 36.855 -16.996 -0.524  1.00 12.98 ?  115 ASN   B HB2  1 
ATOM   5712 H HB3  . ASN   B 1 115 ? 37.224 -15.464 -0.727  1.00 12.98 ?  115 ASN   B HB3  1 
ATOM   5713 H HD21 . ASN   B 1 115 ? 35.960 -16.787 2.647   1.00 13.68 ?  115 ASN   B HD21 1 
ATOM   5714 H HD22 . ASN   B 1 115 ? 36.124 -17.676 1.463   1.00 13.68 ?  115 ASN   B HD22 1 
ATOM   5715 N N    . PHE   B 1 116 ? 35.678 -17.096 -3.426  1.00 10.02 ?  116 PHE   B N    1 
ATOM   5716 C CA   . PHE   B 1 116 ? 36.108 -17.188 -4.816  1.00 10.27 ?  116 PHE   B CA   1 
ATOM   5717 C C    . PHE   B 1 116 ? 35.207 -16.362 -5.725  1.00 10.03 ?  116 PHE   B C    1 
ATOM   5718 O O    . PHE   B 1 116 ? 35.640 -15.934 -6.799  1.00 10.51 ?  116 PHE   B O    1 
ATOM   5719 C CB   . PHE   B 1 116 ? 36.080 -18.638 -5.340  1.00 10.03 ?  116 PHE   B CB   1 
ATOM   5720 C CG   . PHE   B 1 116 ? 37.151 -19.590 -4.788  1.00 10.01 ?  116 PHE   B CG   1 
ATOM   5721 C CD1  . PHE   B 1 116 ? 37.803 -19.402 -3.581  1.00 10.85 ?  116 PHE   B CD1  1 
ATOM   5722 C CD2  . PHE   B 1 116 ? 37.456 -20.722 -5.526  1.00 10.44 ?  116 PHE   B CD2  1 
ATOM   5723 C CE1  . PHE   B 1 116 ? 38.734 -20.342 -3.126  1.00 10.98 ?  116 PHE   B CE1  1 
ATOM   5724 C CE2  . PHE   B 1 116 ? 38.376 -21.659 -5.080  1.00 10.45 ?  116 PHE   B CE2  1 
ATOM   5725 C CZ   . PHE   B 1 116 ? 39.016 -21.467 -3.883  1.00 10.68 ?  116 PHE   B CZ   1 
ATOM   5726 H H    . PHE   B 1 116 ? 35.415 -17.842 -3.080  1.00 12.01 ?  116 PHE   B H    1 
ATOM   5727 H HA   . PHE   B 1 116 ? 37.010 -16.856 -4.898  1.00 12.31 ?  116 PHE   B HA   1 
ATOM   5728 H HB2  . PHE   B 1 116 ? 35.209 -19.019 -5.127  1.00 12.03 ?  116 PHE   B HB2  1 
ATOM   5729 H HB3  . PHE   B 1 116 ? 36.183 -18.611 -6.306  1.00 12.03 ?  116 PHE   B HB3  1 
ATOM   5730 H HD1  . PHE   B 1 116 ? 37.602 -18.653 -3.063  1.00 13.02 ?  116 PHE   B HD1  1 
ATOM   5731 H HD2  . PHE   B 1 116 ? 37.015 -20.875 -6.332  1.00 12.51 ?  116 PHE   B HD2  1 
ATOM   5732 H HE1  . PHE   B 1 116 ? 39.175 -20.207 -2.318  1.00 13.16 ?  116 PHE   B HE1  1 
ATOM   5733 H HE2  . PHE   B 1 116 ? 38.569 -22.409 -5.593  1.00 12.53 ?  116 PHE   B HE2  1 
ATOM   5734 H HZ   . PHE   B 1 116 ? 39.652 -22.079 -3.585  1.00 12.80 ?  116 PHE   B HZ   1 
ATOM   5735 N N    . ASN   B 1 117 ? 33.938 -16.162 -5.340  1.00 10.23 ?  117 ASN   B N    1 
ATOM   5736 C CA   . ASN   B 1 117 ? 32.991 -15.462 -6.206  1.00 10.70 ?  117 ASN   B CA   1 
ATOM   5737 C C    . ASN   B 1 117 ? 33.303 -13.982 -6.353  1.00 10.98 ?  117 ASN   B C    1 
ATOM   5738 O O    . ASN   B 1 117 ? 32.705 -13.323 -7.205  1.00 12.05 ?  117 ASN   B O    1 
ATOM   5739 C CB   . ASN   B 1 117 ? 31.568 -15.683 -5.711  1.00 10.70 ?  117 ASN   B CB   1 
ATOM   5740 C CG   . ASN   B 1 117 ? 31.117 -17.089 -5.959  1.00 10.72 ?  117 ASN   B CG   1 
ATOM   5741 O OD1  . ASN   B 1 117 ? 31.470 -17.680 -6.979  1.00 11.69 ?  117 ASN   B OD1  1 
ATOM   5742 N ND2  . ASN   B 1 117 ? 30.386 -17.660 -5.019  1.00 11.06 ?  117 ASN   B ND2  1 
ATOM   5743 H H    . ASN   B 1 117 ? 33.611 -16.417 -4.581  1.00 12.27 ?  117 ASN   B H    1 
ATOM   5744 H HA   . ASN   B 1 117 ? 33.049 -15.857 -7.084  1.00 12.83 ?  117 ASN   B HA   1 
ATOM   5745 H HB2  . ASN   B 1 117 ? 31.528 -15.514 -4.752  1.00 12.83 ?  117 ASN   B HB2  1 
ATOM   5746 H HB3  . ASN   B 1 117 ? 30.970 -15.075 -6.177  1.00 12.83 ?  117 ASN   B HB3  1 
ATOM   5747 H HD21 . ASN   B 1 117 ? 30.106 -18.465 -5.118  1.00 13.26 ?  117 ASN   B HD21 1 
ATOM   5748 H HD22 . ASN   B 1 117 ? 30.165 -17.212 -4.314  1.00 13.26 ?  117 ASN   B HD22 1 
ATOM   5749 N N    . GLN   B 1 118 ? 34.237 -13.457 -5.571  1.00 10.64 ?  118 GLN   B N    1 
ATOM   5750 C CA   . GLN   B 1 118 ? 34.666 -12.067 -5.704  1.00 11.17 ?  118 GLN   B CA   1 
ATOM   5751 C C    . GLN   B 1 118 ? 35.737 -11.878 -6.773  1.00 11.36 ?  118 GLN   B C    1 
ATOM   5752 O O    . GLN   B 1 118 ? 36.210 -10.751 -6.951  1.00 12.66 ?  118 GLN   B O    1 
ATOM   5753 C CB   . GLN   B 1 118 ? 35.141 -11.539 -4.347  1.00 11.89 ?  118 GLN   B CB   1 
ATOM   5754 C CG   . GLN   B 1 118 ? 34.054 -11.581 -3.282  1.00 12.18 ?  118 GLN   B CG   1 
ATOM   5755 C CD   . GLN   B 1 118 ? 32.883 -10.677 -3.614  1.00 11.88 ?  118 GLN   B CD   1 
ATOM   5756 O OE1  . GLN   B 1 118 ? 33.069 -9.531  -4.048  1.00 12.48 ?  118 GLN   B OE1  1 
ATOM   5757 N NE2  . GLN   B 1 118 ? 31.674 -11.174 -3.414  1.00 12.31 ?  118 GLN   B NE2  1 
ATOM   5758 H H    . GLN   B 1 118 ? 34.654 -13.886 -4.948  1.00 12.76 ?  118 GLN   B H    1 
ATOM   5759 H HA   . GLN   B 1 118 ? 33.901 -11.537 -5.972  1.00 13.40 ?  118 GLN   B HA   1 
ATOM   5760 H HB2  . GLN   B 1 118 ? 35.885 -12.073 -4.037  1.00 14.26 ?  118 GLN   B HB2  1 
ATOM   5761 H HB3  . GLN   B 1 118 ? 35.419 -10.611 -4.447  1.00 14.26 ?  118 GLN   B HB3  1 
ATOM   5762 H HG2  . GLN   B 1 118 ? 33.721 -12.490 -3.208  1.00 14.61 ?  118 GLN   B HG2  1 
ATOM   5763 H HG3  . GLN   B 1 118 ? 34.429 -11.295 -2.434  1.00 14.61 ?  118 GLN   B HG3  1 
ATOM   5764 H HE21 . GLN   B 1 118 ? 31.584 -11.974 -3.110  1.00 14.76 ?  118 GLN   B HE21 1 
ATOM   5765 H HE22 . GLN   B 1 118 ? 30.985 -10.696 -3.588  1.00 14.76 ?  118 GLN   B HE22 1 
ATOM   5766 N N    . HIS   B 1 119 ? 36.088 -12.931 -7.513  1.00 10.60 ?  119 HIS   B N    1 
ATOM   5767 C CA   . HIS   B 1 119 ? 37.132 -12.884 -8.529  1.00 11.27 ?  119 HIS   B CA   1 
ATOM   5768 C C    . HIS   B 1 119 ? 36.650 -13.616 -9.768  1.00 10.99 ?  119 HIS   B C    1 
ATOM   5769 O O    . HIS   B 1 119 ? 36.143 -14.734 -9.666  1.00 11.85 ?  119 HIS   B O    1 
ATOM   5770 C CB   . HIS   B 1 119 ? 38.409 -13.519 -7.982  1.00 11.75 ?  119 HIS   B CB   1 
ATOM   5771 C CG   . HIS   B 1 119 ? 38.897 -12.817 -6.763  1.00 12.86 ?  119 HIS   B CG   1 
ATOM   5772 N ND1  . HIS   B 1 119 ? 39.691 -11.692 -6.826  1.00 14.62 ?  119 HIS   B ND1  1 
ATOM   5773 C CD2  . HIS   B 1 119 ? 38.611 -13.008 -5.456  1.00 14.05 ?  119 HIS   B CD2  1 
ATOM   5774 C CE1  . HIS   B 1 119 ? 39.906 -11.245 -5.603  1.00 15.75 ?  119 HIS   B CE1  1 
ATOM   5775 N NE2  . HIS   B 1 119 ? 39.258 -12.021 -4.753  1.00 15.57 ?  119 HIS   B NE2  1 
ATOM   5776 H H    . HIS   B 1 119 ? 35.713 -13.704 -7.448  1.00 12.71 ?  119 HIS   B H    1 
ATOM   5777 H HA   . HIS   B 1 119 ? 37.314 -11.960 -8.767  1.00 13.51 ?  119 HIS   B HA   1 
ATOM   5778 H HB2  . HIS   B 1 119 ? 38.233 -14.442 -7.755  1.00 14.09 ?  119 HIS   B HB2  1 
ATOM   5779 H HB3  . HIS   B 1 119 ? 39.102 -13.467 -8.663  1.00 14.09 ?  119 HIS   B HB3  1 
ATOM   5780 H HD2  . HIS   B 1 119 ? 38.086 -13.687 -5.100  1.00 16.86 ?  119 HIS   B HD2  1 
ATOM   5781 H HE1  . HIS   B 1 119 ? 40.437 -10.515 -5.376  1.00 18.90 ?  119 HIS   B HE1  1 
ATOM   5782 H HE2  . HIS   B 1 119 ? 39.270 -11.942 -3.897  1.00 18.67 ?  119 HIS   B HE2  1 
ATOM   5783 N N    . GLU   B 1 120 ? 36.805 -12.998 -10.940 1.00 11.48 ?  120 GLU   B N    1 
ATOM   5784 C CA   . GLU   B 1 120 ? 36.214 -13.579 -12.142 1.00 12.88 ?  120 GLU   B CA   1 
ATOM   5785 C C    . GLU   B 1 120 ? 36.889 -14.880 -12.556 1.00 11.90 ?  120 GLU   B C    1 
ATOM   5786 O O    . GLU   B 1 120 ? 36.228 -15.753 -13.128 1.00 12.24 ?  120 GLU   B O    1 
ATOM   5787 C CB   . GLU   B 1 120 ? 36.227 -12.571 -13.289 1.00 16.77 ?  120 GLU   B CB   1 
ATOM   5788 C CG   . GLU   B 1 120 ? 35.278 -11.411 -13.064 1.00 22.77 ?  120 GLU   B CG   1 
ATOM   5789 C CD   . GLU   B 1 120 ? 35.107 -10.536 -14.287 1.00 28.11 ?  120 GLU   B CD   1 
ATOM   5790 O OE1  . GLU   B 1 120 ? 36.104 -10.317 -15.008 1.00 29.91 ?  120 GLU   B OE1  1 
ATOM   5791 O OE2  . GLU   B 1 120 ? 33.974 -10.066 -14.521 1.00 30.87 -1 120 GLU   B OE2  1 
ATOM   5792 H H    . GLU   B 1 120 ? 37.237 -12.261 -11.067 1.00 13.77 ?  120 GLU   B H    1 
ATOM   5793 H HA   . GLU   B 1 120 ? 35.291 -13.787 -11.954 1.00 15.45 ?  120 GLU   B HA   1 
ATOM   5794 H HB2  . GLU   B 1 120 ? 37.118 -12.210 -13.391 1.00 20.11 ?  120 GLU   B HB2  1 
ATOM   5795 H HB3  . GLU   B 1 120 ? 35.955 -13.020 -14.108 1.00 20.11 ?  120 GLU   B HB3  1 
ATOM   5796 H HG2  . GLU   B 1 120 ? 34.406 -11.759 -12.817 1.00 27.31 ?  120 GLU   B HG2  1 
ATOM   5797 H HG3  . GLU   B 1 120 ? 35.626 -10.852 -12.356 1.00 27.31 ?  120 GLU   B HG3  1 
ATOM   5798 N N    . VAL   B 1 121 ? 38.189 -15.022 -12.295 1.00 11.48 ?  121 VAL   B N    1 
ATOM   5799 C CA   . VAL   B 1 121 ? 38.936 -16.228 -12.643 1.00 11.43 ?  121 VAL   B CA   1 
ATOM   5800 C C    . VAL   B 1 121 ? 40.048 -16.433 -11.621 1.00 10.87 ?  121 VAL   B C    1 
ATOM   5801 O O    . VAL   B 1 121 ? 40.720 -15.476 -11.219 1.00 11.54 ?  121 VAL   B O    1 
ATOM   5802 C CB   . VAL   B 1 121 ? 39.449 -16.187 -14.103 1.00 13.05 ?  121 VAL   B CB   1 
ATOM   5803 C CG1  . VAL   B 1 121 ? 40.305 -14.953 -14.369 1.00 14.27 ?  121 VAL   B CG1  1 
ATOM   5804 C CG2  . VAL   B 1 121 ? 40.198 -17.463 -14.452 1.00 14.47 ?  121 VAL   B CG2  1 
ATOM   5805 H H    . VAL   B 1 121 ? 38.672 -14.421 -11.914 1.00 13.76 ?  121 VAL   B H    1 
ATOM   5806 H HA   . VAL   B 1 121 ? 38.330 -16.983 -12.579 1.00 13.71 ?  121 VAL   B HA   1 
ATOM   5807 H HB   . VAL   B 1 121 ? 38.680 -16.137 -14.698 1.00 15.65 ?  121 VAL   B HB   1 
ATOM   5808 H HG11 . VAL   B 1 121 ? 40.615 -14.975 -15.289 1.00 17.11 ?  121 VAL   B HG11 1 
ATOM   5809 H HG12 . VAL   B 1 121 ? 39.765 -14.158 -14.224 1.00 17.11 ?  121 VAL   B HG12 1 
ATOM   5810 H HG13 . VAL   B 1 121 ? 41.060 -14.957 -13.765 1.00 17.11 ?  121 VAL   B HG13 1 
ATOM   5811 H HG21 . VAL   B 1 121 ? 40.399 -17.463 -15.404 1.00 17.35 ?  121 VAL   B HG21 1 
ATOM   5812 H HG22 . VAL   B 1 121 ? 41.026 -17.493 -13.945 1.00 17.35 ?  121 VAL   B HG22 1 
ATOM   5813 H HG23 . VAL   B 1 121 ? 39.646 -18.227 -14.232 1.00 17.35 ?  121 VAL   B HG23 1 
ATOM   5814 N N    . LEU   B 1 122 ? 40.231 -17.686 -11.190 1.00 10.47 ?  122 LEU   B N    1 
ATOM   5815 C CA   . LEU   B 1 122 ? 41.209 -18.038 -10.164 1.00 10.31 ?  122 LEU   B CA   1 
ATOM   5816 C C    . LEU   B 1 122 ? 41.867 -19.367 -10.494 1.00 10.24 ?  122 LEU   B C    1 
ATOM   5817 O O    . LEU   B 1 122 ? 41.213 -20.287 -11.005 1.00 11.22 ?  122 LEU   B O    1 
ATOM   5818 C CB   . LEU   B 1 122 ? 40.555 -18.273 -8.790  1.00 11.85 ?  122 LEU   B CB   1 
ATOM   5819 C CG   . LEU   B 1 122 ? 39.524 -17.252 -8.299  1.00 11.94 ?  122 LEU   B CG   1 
ATOM   5820 C CD1  . LEU   B 1 122 ? 38.120 -17.595 -8.775  1.00 13.00 ?  122 LEU   B CD1  1 
ATOM   5821 C CD2  . LEU   B 1 122 ? 39.583 -17.146 -6.788  1.00 11.73 ?  122 LEU   B CD2  1 
ATOM   5822 H H    . LEU   B 1 122 ? 39.785 -18.366 -11.479 1.00 12.55 ?  122 LEU   B H    1 
ATOM   5823 H HA   . LEU   B 1 122 ? 41.884 -17.341 -10.086 1.00 12.36 ?  122 LEU   B HA   1 
ATOM   5824 H HB2  . LEU   B 1 122 ? 40.110 -19.131 -8.816  1.00 14.21 ?  122 LEU   B HB2  1 
ATOM   5825 H HB3  . LEU   B 1 122 ? 41.261 -18.299 -8.125  1.00 14.21 ?  122 LEU   B HB3  1 
ATOM   5826 H HG   . LEU   B 1 122 ? 39.752 -16.381 -8.659  1.00 14.32 ?  122 LEU   B HG   1 
ATOM   5827 H HD11 . LEU   B 1 122 ? 37.496 -16.947 -8.404  1.00 15.59 ?  122 LEU   B HD11 1 
ATOM   5828 H HD12 . LEU   B 1 122 ? 38.096 -17.552 -9.744  1.00 15.59 ?  122 LEU   B HD12 1 
ATOM   5829 H HD13 . LEU   B 1 122 ? 37.891 -18.484 -8.473  1.00 15.59 ?  122 LEU   B HD13 1 
ATOM   5830 H HD21 . LEU   B 1 122 ? 38.904 -16.528 -6.481  1.00 14.06 ?  122 LEU   B HD21 1 
ATOM   5831 H HD22 . LEU   B 1 122 ? 39.435 -18.024 -6.400  1.00 14.06 ?  122 LEU   B HD22 1 
ATOM   5832 H HD23 . LEU   B 1 122 ? 40.465 -16.821 -6.527  1.00 14.06 ?  122 LEU   B HD23 1 
ATOM   5833 N N    . LEU   B 1 123 ? 43.156 -19.474 -10.139 1.00 10.05 ?  123 LEU   B N    1 
ATOM   5834 C CA   . LEU   B 1 123 ? 43.873 -20.743 -10.015 1.00 10.24 ?  123 LEU   B CA   1 
ATOM   5835 C C    . LEU   B 1 123 ? 43.844 -21.138 -8.544  1.00 9.79  ?  123 LEU   B C    1 
ATOM   5836 O O    . LEU   B 1 123 ? 44.184 -20.314 -7.687  1.00 10.32 ?  123 LEU   B O    1 
ATOM   5837 C CB   . LEU   B 1 123 ? 45.321 -20.560 -10.476 1.00 10.44 ?  123 LEU   B CB   1 
ATOM   5838 C CG   . LEU   B 1 123 ? 46.263 -21.742 -10.238 1.00 11.16 ?  123 LEU   B CG   1 
ATOM   5839 C CD1  . LEU   B 1 123 ? 45.842 -22.982 -11.023 1.00 11.71 ?  123 LEU   B CD1  1 
ATOM   5840 C CD2  . LEU   B 1 123 ? 47.689 -21.347 -10.598 1.00 12.15 ?  123 LEU   B CD2  1 
ATOM   5841 H H    . LEU   B 1 123 ? 43.652 -18.792 -9.947  1.00 12.05 ?  123 LEU   B H    1 
ATOM   5842 H HA   . LEU   B 1 123 ? 43.439 -21.429 -10.551 1.00 12.28 ?  123 LEU   B HA   1 
ATOM   5843 H HB2  . LEU   B 1 123 ? 45.317 -20.387 -11.431 1.00 12.52 ?  123 LEU   B HB2  1 
ATOM   5844 H HB3  . LEU   B 1 123 ? 45.695 -19.800 -10.010 1.00 12.52 ?  123 LEU   B HB3  1 
ATOM   5845 H HG   . LEU   B 1 123 ? 46.253 -21.977 -9.296  1.00 13.39 ?  123 LEU   B HG   1 
ATOM   5846 H HD11 . LEU   B 1 123 ? 46.475 -23.695 -10.854 1.00 14.04 ?  123 LEU   B HD11 1 
ATOM   5847 H HD12 . LEU   B 1 123 ? 44.955 -23.252 -10.732 1.00 14.04 ?  123 LEU   B HD12 1 
ATOM   5848 H HD13 . LEU   B 1 123 ? 45.828 -22.766 -11.968 1.00 14.04 ?  123 LEU   B HD13 1 
ATOM   5849 H HD21 . LEU   B 1 123 ? 48.278 -22.101 -10.445 1.00 14.57 ?  123 LEU   B HD21 1 
ATOM   5850 H HD22 . LEU   B 1 123 ? 47.717 -21.088 -11.533 1.00 14.57 ?  123 LEU   B HD22 1 
ATOM   5851 H HD23 . LEU   B 1 123 ? 47.956 -20.599 -10.040 1.00 14.57 ?  123 LEU   B HD23 1 
ATOM   5852 N N    . ALA   B 1 124 ? 43.409 -22.368 -8.238  1.00 10.04 ?  124 ALA   B N    1 
ATOM   5853 C CA   . ALA   B 1 124 ? 43.155 -22.694 -6.843  1.00 10.14 ?  124 ALA   B CA   1 
ATOM   5854 C C    . ALA   B 1 124 ? 43.423 -24.154 -6.511  1.00 9.74  ?  124 ALA   B C    1 
ATOM   5855 O O    . ALA   B 1 124 ? 43.295 -25.031 -7.379  1.00 10.38 ?  124 ALA   B O    1 
ATOM   5856 C CB   . ALA   B 1 124 ? 41.698 -22.378 -6.475  1.00 10.51 ?  124 ALA   B CB   1 
ATOM   5857 H H    . ALA   B 1 124 ? 43.244 -23.005 -8.801  1.00 12.04 ?  124 ALA   B H    1 
ATOM   5858 H HA   . ALA   B 1 124 ? 43.728 -22.143 -6.296  1.00 12.15 ?  124 ALA   B HA   1 
ATOM   5859 H HB1  . ALA   B 1 124 ? 41.548 -22.603 -5.542  1.00 12.60 ?  124 ALA   B HB1  1 
ATOM   5860 H HB2  . ALA   B 1 124 ? 41.535 -21.432 -6.616  1.00 12.60 ?  124 ALA   B HB2  1 
ATOM   5861 H HB3  . ALA   B 1 124 ? 41.105 -22.902 -7.038  1.00 12.60 ?  124 ALA   B HB3  1 
ATOM   5862 N N    . PRO   B 1 125 ? 43.718 -24.444 -5.249  1.00 9.98  ?  125 PRO   B N    1 
ATOM   5863 C CA   . PRO   B 1 125 ? 43.661 -25.809 -4.728  1.00 10.86 ?  125 PRO   B CA   1 
ATOM   5864 C C    . PRO   B 1 125 ? 42.258 -26.088 -4.189  1.00 10.81 ?  125 PRO   B C    1 
ATOM   5865 O O    . PRO   B 1 125 ? 41.460 -25.173 -3.983  1.00 11.38 ?  125 PRO   B O    1 
ATOM   5866 C CB   . PRO   B 1 125 ? 44.644 -25.730 -3.557  1.00 11.90 ?  125 PRO   B CB   1 
ATOM   5867 C CG   . PRO   B 1 125 ? 44.393 -24.344 -2.986  1.00 11.98 ?  125 PRO   B CG   1 
ATOM   5868 C CD   . PRO   B 1 125 ? 44.041 -23.473 -4.184  1.00 10.68 ?  125 PRO   B CD   1 
ATOM   5869 H HA   . PRO   B 1 125 ? 43.940 -26.474 -5.375  1.00 13.02 ?  125 PRO   B HA   1 
ATOM   5870 H HB2  . PRO   B 1 125 ? 44.439 -26.415 -2.897  1.00 14.27 ?  125 PRO   B HB2  1 
ATOM   5871 H HB3  . PRO   B 1 125 ? 45.556 -25.813 -3.873  1.00 14.27 ?  125 PRO   B HB3  1 
ATOM   5872 H HG2  . PRO   B 1 125 ? 43.653 -24.369 -2.356  1.00 14.36 ?  125 PRO   B HG2  1 
ATOM   5873 H HG3  . PRO   B 1 125 ? 45.197 -24.013 -2.545  1.00 14.36 ?  125 PRO   B HG3  1 
ATOM   5874 H HD2  . PRO   B 1 125 ? 43.272 -22.915 -3.991  1.00 12.80 ?  125 PRO   B HD2  1 
ATOM   5875 H HD3  . PRO   B 1 125 ? 44.810 -22.927 -4.443  1.00 12.80 ?  125 PRO   B HD3  1 
ATOM   5876 N N    . LEU   B 1 126 ? 41.988 -27.367 -3.916  1.00 11.42 ?  126 LEU   B N    1 
ATOM   5877 C CA   . LEU   B 1 126 ? 40.769 -27.734 -3.206  1.00 11.87 ?  126 LEU   B CA   1 
ATOM   5878 C C    . LEU   B 1 126 ? 40.883 -27.334 -1.744  1.00 12.16 ?  126 LEU   B C    1 
ATOM   5879 O O    . LEU   B 1 126 ? 41.767 -27.804 -1.022  1.00 13.79 ?  126 LEU   B O    1 
ATOM   5880 C CB   . LEU   B 1 126 ? 40.518 -29.232 -3.319  1.00 13.07 ?  126 LEU   B CB   1 
ATOM   5881 C CG   . LEU   B 1 126 ? 39.988 -29.710 -4.670  1.00 14.00 ?  126 LEU   B CG   1 
ATOM   5882 C CD1  . LEU   B 1 126 ? 40.040 -31.225 -4.758  1.00 15.68 ?  126 LEU   B CD1  1 
ATOM   5883 C CD2  . LEU   B 1 126 ? 38.565 -29.209 -4.909  1.00 14.08 ?  126 LEU   B CD2  1 
ATOM   5884 H H    . LEU   B 1 126 ? 42.498 -28.032 -4.118  1.00 13.70 ?  126 LEU   B H    1 
ATOM   5885 H HA   . LEU   B 1 126 ? 40.018 -27.261 -3.595  1.00 14.24 ?  126 LEU   B HA   1 
ATOM   5886 H HB2  . LEU   B 1 126 ? 41.351 -29.695 -3.154  1.00 15.67 ?  126 LEU   B HB2  1 
ATOM   5887 H HB3  . LEU   B 1 126 ? 39.865 -29.483 -2.647  1.00 15.67 ?  126 LEU   B HB3  1 
ATOM   5888 H HG   . LEU   B 1 126 ? 40.551 -29.352 -5.373  1.00 16.79 ?  126 LEU   B HG   1 
ATOM   5889 H HD11 . LEU   B 1 126 ? 39.697 -31.505 -5.622  1.00 18.80 ?  126 LEU   B HD11 1 
ATOM   5890 H HD12 . LEU   B 1 126 ? 40.958 -31.518 -4.654  1.00 18.80 ?  126 LEU   B HD12 1 
ATOM   5891 H HD13 . LEU   B 1 126 ? 39.491 -31.602 -4.049  1.00 18.80 ?  126 LEU   B HD13 1 
ATOM   5892 H HD21 . LEU   B 1 126 ? 38.210 -29.629 -5.707  1.00 16.89 ?  126 LEU   B HD21 1 
ATOM   5893 H HD22 . LEU   B 1 126 ? 38.016 -29.438 -4.142  1.00 16.89 ?  126 LEU   B HD22 1 
ATOM   5894 H HD23 . LEU   B 1 126 ? 38.583 -28.244 -5.023  1.00 16.89 ?  126 LEU   B HD23 1 
ATOM   5895 N N    . LEU   B 1 127 ? 39.955 -26.499 -1.291  1.00 11.79 ?  127 LEU   B N    1 
ATOM   5896 C CA   . LEU   B 1 127 ? 40.008 -26.005 0.072   1.00 11.97 ?  127 LEU   B CA   1 
ATOM   5897 C C    . LEU   B 1 127 ? 39.732 -27.125 1.065   1.00 11.75 ?  127 LEU   B C    1 
ATOM   5898 O O    . LEU   B 1 127 ? 38.908 -28.019 0.832   1.00 12.15 ?  127 LEU   B O    1 
ATOM   5899 C CB   . LEU   B 1 127 ? 38.988 -24.884 0.275   1.00 12.74 ?  127 LEU   B CB   1 
ATOM   5900 C CG   . LEU   B 1 127 ? 39.165 -23.619 -0.559  1.00 13.19 ?  127 LEU   B CG   1 
ATOM   5901 C CD1  . LEU   B 1 127 ? 38.044 -22.647 -0.219  1.00 13.31 ?  127 LEU   B CD1  1 
ATOM   5902 C CD2  . LEU   B 1 127 ? 40.524 -22.979 -0.329  1.00 13.60 ?  127 LEU   B CD2  1 
ATOM   5903 H H    . LEU   B 1 127 ? 39.285 -26.197 -1.753  1.00 14.14 ?  127 LEU   B H    1 
ATOM   5904 H HA   . LEU   B 1 127 ? 40.893 -25.643 0.247   1.00 14.36 ?  127 LEU   B HA   1 
ATOM   5905 H HB2  . LEU   B 1 127 ? 38.105 -25.238 0.075   1.00 15.28 ?  127 LEU   B HB2  1 
ATOM   5906 H HB3  . LEU   B 1 127 ? 39.014 -24.614 1.208   1.00 15.28 ?  127 LEU   B HB3  1 
ATOM   5907 H HG   . LEU   B 1 127 ? 39.080 -23.840 -1.498  1.00 15.81 ?  127 LEU   B HG   1 
ATOM   5908 H HD11 . LEU   B 1 127 ? 38.154 -21.835 -0.744  1.00 15.97 ?  127 LEU   B HD11 1 
ATOM   5909 H HD12 . LEU   B 1 127 ? 37.187 -23.054 -0.422  1.00 15.97 ?  127 LEU   B HD12 1 
ATOM   5910 H HD13 . LEU   B 1 127 ? 38.088 -22.428 0.728   1.00 15.97 ?  127 LEU   B HD13 1 
ATOM   5911 H HD21 . LEU   B 1 127 ? 40.557 -22.125 -0.790  1.00 16.31 ?  127 LEU   B HD21 1 
ATOM   5912 H HD22 . LEU   B 1 127 ? 40.653 -22.844 0.624   1.00 16.31 ?  127 LEU   B HD22 1 
ATOM   5913 H HD23 . LEU   B 1 127 ? 41.210 -23.569 -0.675  1.00 16.31 ?  127 LEU   B HD23 1 
ATOM   5914 N N    . SER   B 1 128 ? 40.420 -27.047 2.194   1.00 11.97 ?  128 SER   B N    1 
ATOM   5915 C CA   . SER   B 1 128 ? 40.309 -27.964 3.319   1.00 12.51 ?  128 SER   B CA   1 
ATOM   5916 C C    . SER   B 1 128 ? 40.800 -29.372 2.995   1.00 13.37 ?  128 SER   B C    1 
ATOM   5917 O O    . SER   B 1 128 ? 40.713 -30.252 3.853   1.00 14.57 ?  128 SER   B O    1 
ATOM   5918 C CB   . SER   B 1 128 ? 38.911 -27.973 3.954   1.00 12.82 ?  128 SER   B CB   1 
ATOM   5919 O OG   . SER   B 1 128 ? 38.597 -26.700 4.509   1.00 13.44 ?  128 SER   B OG   1 
ATOM   5920 H H    . SER   B 1 128 ? 40.990 -26.419 2.345   1.00 14.36 ?  128 SER   B H    1 
ATOM   5921 H HA   . SER   B 1 128 ? 40.901 -27.628 4.004   1.00 15.01 ?  128 SER   B HA   1 
ATOM   5922 H HB2  . SER   B 1 128 ? 38.252 -28.207 3.282   1.00 15.38 ?  128 SER   B HB2  1 
ATOM   5923 H HB3  . SER   B 1 128 ? 38.897 -28.648 4.667   1.00 15.38 ?  128 SER   B HB3  1 
ATOM   5924 H HG   . SER   B 1 128 ? 39.162 -26.506 5.097   1.00 16.11 ?  128 SER   B HG   1 
ATOM   5925 N N    . ALA   B 1 129 ? 41.371 -29.594 1.808   1.00 14.20 ?  129 ALA   B N    1 
ATOM   5926 C CA   . ALA   B 1 129 ? 41.913 -30.895 1.452   1.00 15.30 ?  129 ALA   B CA   1 
ATOM   5927 C C    . ALA   B 1 129 ? 43.303 -31.075 2.049   1.00 14.32 ?  129 ALA   B C    1 
ATOM   5928 O O    . ALA   B 1 129 ? 43.862 -30.177 2.694   1.00 14.32 ?  129 ALA   B O    1 
ATOM   5929 C CB   . ALA   B 1 129 ? 41.952 -31.063 -0.065  1.00 17.21 ?  129 ALA   B CB   1 
ATOM   5930 H H    . ALA   B 1 129 ? 41.453 -29.001 1.186   1.00 17.03 ?  129 ALA   B H    1 
ATOM   5931 H HA   . ALA   B 1 129 ? 41.337 -31.583 1.813   1.00 18.35 ?  129 ALA   B HA   1 
ATOM   5932 H HB1  . ALA   B 1 129 ? 42.308 -31.943 -0.275  1.00 20.65 ?  129 ALA   B HB1  1 
ATOM   5933 H HB2  . ALA   B 1 129 ? 41.053 -30.980 -0.416  1.00 20.65 ?  129 ALA   B HB2  1 
ATOM   5934 H HB3  . ALA   B 1 129 ? 42.522 -30.378 -0.447  1.00 20.65 ?  129 ALA   B HB3  1 
ATOM   5935 N N    . GLY   B 1 130 ? 43.861 -32.264 1.829   1.00 14.37 ?  130 GLY   B N    1 
ATOM   5936 C CA   . GLY   B 1 130 ? 45.249 -32.504 2.178   1.00 15.03 ?  130 GLY   B CA   1 
ATOM   5937 C C    . GLY   B 1 130 ? 45.464 -32.403 3.669   1.00 14.98 ?  130 GLY   B C    1 
ATOM   5938 O O    . GLY   B 1 130 ? 44.762 -33.037 4.470   1.00 15.67 ?  130 GLY   B O    1 
ATOM   5939 H H    . GLY   B 1 130 ? 43.458 -32.938 1.475   1.00 17.24 ?  130 GLY   B H    1 
ATOM   5940 H HA2  . GLY   B 1 130 ? 45.508 -33.394 1.885   1.00 18.03 ?  130 GLY   B HA2  1 
ATOM   5941 H HA3  . GLY   B 1 130 ? 45.815 -31.855 1.734   1.00 18.03 ?  130 GLY   B HA3  1 
ATOM   5942 N N    . ILE   B 1 131 ? 46.439 -31.572 4.053   1.00 15.39 ?  131 ILE   B N    1 
ATOM   5943 C CA   . ILE   B 1 131 ? 46.796 -31.435 5.459   1.00 16.11 ?  131 ILE   B CA   1 
ATOM   5944 C C    . ILE   B 1 131 ? 45.680 -30.835 6.295   1.00 15.38 ?  131 ILE   B C    1 
ATOM   5945 O O    . ILE   B 1 131 ? 45.757 -30.897 7.527   1.00 16.67 ?  131 ILE   B O    1 
ATOM   5946 C CB   . ILE   B 1 131 ? 48.115 -30.656 5.663   1.00 17.86 ?  131 ILE   B CB   1 
ATOM   5947 C CG1  . ILE   B 1 131 ? 47.958 -29.179 5.272   1.00 18.75 ?  131 ILE   B CG1  1 
ATOM   5948 C CG2  . ILE   B 1 131 ? 49.246 -31.308 4.873   1.00 18.86 ?  131 ILE   B CG2  1 
ATOM   5949 C CD1  . ILE   B 1 131 ? 49.188 -28.333 5.579   1.00 19.72 ?  131 ILE   B CD1  1 
ATOM   5950 H H    . ILE   B 1 131 ? 46.904 -31.085 3.517   1.00 18.46 ?  131 ILE   B H    1 
ATOM   5951 H HA   . ILE   B 1 131 ? 46.942 -32.324 5.806   1.00 19.32 ?  131 ILE   B HA   1 
ATOM   5952 H HB   . ILE   B 1 131 ? 48.336 -30.695 6.607   1.00 21.43 ?  131 ILE   B HB   1 
ATOM   5953 H HG12 . ILE   B 1 131 ? 47.785 -29.128 4.319   1.00 22.49 ?  131 ILE   B HG12 1 
ATOM   5954 H HG13 . ILE   B 1 131 ? 47.209 -28.796 5.760   1.00 22.49 ?  131 ILE   B HG13 1 
ATOM   5955 H HG21 . ILE   B 1 131 ? 50.086 -30.914 5.150   1.00 22.62 ?  131 ILE   B HG21 1 
ATOM   5956 H HG22 . ILE   B 1 131 ? 49.245 -32.258 5.054   1.00 22.62 ?  131 ILE   B HG22 1 
ATOM   5957 H HG23 . ILE   B 1 131 ? 49.097 -31.148 3.928   1.00 22.62 ?  131 ILE   B HG23 1 
ATOM   5958 H HD11 . ILE   B 1 131 ? 48.977 -27.402 5.409   1.00 23.65 ?  131 ILE   B HD11 1 
ATOM   5959 H HD12 . ILE   B 1 131 ? 49.428 -28.455 6.511   1.00 23.65 ?  131 ILE   B HD12 1 
ATOM   5960 H HD13 . ILE   B 1 131 ? 49.916 -28.619 5.008   1.00 23.65 ?  131 ILE   B HD13 1 
ATOM   5961 N N    . PHE   B 1 132 ? 44.647 -30.259 5.666   1.00 14.23 ?  132 PHE   B N    1 
ATOM   5962 C CA   . PHE   B 1 132 ? 43.488 -29.752 6.396   1.00 14.36 ?  132 PHE   B CA   1 
ATOM   5963 C C    . PHE   B 1 132 ? 42.460 -30.839 6.719   1.00 15.73 ?  132 PHE   B C    1 
ATOM   5964 O O    . PHE   B 1 132 ? 41.546 -30.585 7.510   1.00 17.27 ?  132 PHE   B O    1 
ATOM   5965 C CB   . PHE   B 1 132 ? 42.816 -28.614 5.616   1.00 13.62 ?  132 PHE   B CB   1 
ATOM   5966 C CG   . PHE   B 1 132 ? 43.519 -27.272 5.732   1.00 13.72 ?  132 PHE   B CG   1 
ATOM   5967 C CD1  . PHE   B 1 132 ? 44.811 -27.089 5.260   1.00 14.90 ?  132 PHE   B CD1  1 
ATOM   5968 C CD2  . PHE   B 1 132 ? 42.850 -26.177 6.262   1.00 13.52 ?  132 PHE   B CD2  1 
ATOM   5969 C CE1  . PHE   B 1 132 ? 45.430 -25.850 5.353   1.00 15.37 ?  132 PHE   B CE1  1 
ATOM   5970 C CE2  . PHE   B 1 132 ? 43.461 -24.933 6.352   1.00 14.00 ?  132 PHE   B CE2  1 
ATOM   5971 C CZ   . PHE   B 1 132 ? 44.751 -24.773 5.900   1.00 15.01 ?  132 PHE   B CZ   1 
ATOM   5972 H H    . PHE   B 1 132 ? 44.594 -30.153 4.812   1.00 17.07 ?  132 PHE   B H    1 
ATOM   5973 H HA   . PHE   B 1 132 ? 43.796 -29.382 7.235   1.00 17.22 ?  132 PHE   B HA   1 
ATOM   5974 H HB2  . PHE   B 1 132 ? 42.801 -28.851 4.678   1.00 16.34 ?  132 PHE   B HB2  1 
ATOM   5975 H HB3  . PHE   B 1 132 ? 41.912 -28.502 5.944   1.00 16.34 ?  132 PHE   B HB3  1 
ATOM   5976 H HD1  . PHE   B 1 132 ? 45.277 -27.812 4.898   1.00 17.87 ?  132 PHE   B HD1  1 
ATOM   5977 H HD2  . PHE   B 1 132 ? 41.979 -26.281 6.569   1.00 16.22 ?  132 PHE   B HD2  1 
ATOM   5978 H HE1  . PHE   B 1 132 ? 46.306 -25.745 5.048   1.00 18.43 ?  132 PHE   B HE1  1 
ATOM   5979 H HE2  . PHE   B 1 132 ? 43.004 -24.210 6.721   1.00 16.79 ?  132 PHE   B HE2  1 
ATOM   5980 H HZ   . PHE   B 1 132 ? 45.169 -23.939 5.963   1.00 18.00 ?  132 PHE   B HZ   1 
ATOM   5981 N N    . GLY   B 1 133 ? 42.568 -32.032 6.125   1.00 15.25 ?  133 GLY   B N    1 
ATOM   5982 C CA   . GLY   B 1 133 ? 41.857 -33.200 6.618   1.00 16.11 ?  133 GLY   B CA   1 
ATOM   5983 C C    . GLY   B 1 133 ? 40.462 -33.462 6.080   1.00 16.45 ?  133 GLY   B C    1 
ATOM   5984 O O    . GLY   B 1 133 ? 39.872 -34.481 6.452   1.00 18.35 ?  133 GLY   B O    1 
ATOM   5985 H H    . GLY   B 1 133 ? 43.055 -32.182 5.431   1.00 18.29 ?  133 GLY   B H    1 
ATOM   5986 H HA2  . GLY   B 1 133 ? 42.388 -33.983 6.420   1.00 19.33 ?  133 GLY   B HA2  1 
ATOM   5987 H HA3  . GLY   B 1 133 ? 41.788 -33.125 7.582   1.00 19.33 ?  133 GLY   B HA3  1 
ATOM   5988 N N    . ALA   B 1 134 ? 39.906 -32.600 5.237   1.00 15.67 ?  134 ALA   B N    1 
ATOM   5989 C CA   . ALA   B 1 134 ? 38.581 -32.872 4.700   1.00 15.72 ?  134 ALA   B CA   1 
ATOM   5990 C C    . ALA   B 1 134 ? 38.666 -33.862 3.543   1.00 15.83 ?  134 ALA   B C    1 
ATOM   5991 O O    . ALA   B 1 134 ? 39.721 -34.052 2.929   1.00 17.07 ?  134 ALA   B O    1 
ATOM   5992 C CB   . ALA   B 1 134 ? 37.908 -31.578 4.237   1.00 16.28 ?  134 ALA   B CB   1 
ATOM   5993 H H    . ALA   B 1 134 ? 40.265 -31.863 4.966   1.00 18.80 ?  134 ALA   B H    1 
ATOM   5994 H HA   . ALA   B 1 134 ? 38.029 -33.261 5.398   1.00 18.85 ?  134 ALA   B HA   1 
ATOM   5995 H HB1  . ALA   B 1 134 ? 37.020 -31.787 3.905   1.00 19.52 ?  134 ALA   B HB1  1 
ATOM   5996 H HB2  . ALA   B 1 134 ? 37.844 -30.967 4.989   1.00 19.52 ?  134 ALA   B HB2  1 
ATOM   5997 H HB3  . ALA   B 1 134 ? 38.440 -31.181 3.532   1.00 19.52 ?  134 ALA   B HB3  1 
ATOM   5998 N N    . ASP   B 1 135 ? 37.533 -34.487 3.251   1.00 15.99 ?  135 ASP   B N    1 
ATOM   5999 C CA   . ASP   B 1 135 ? 37.437 -35.388 2.112   1.00 16.60 ?  135 ASP   B CA   1 
ATOM   6000 C C    . ASP   B 1 135 ? 37.536 -34.556 0.840   1.00 15.52 ?  135 ASP   B C    1 
ATOM   6001 O O    . ASP   B 1 135 ? 36.688 -33.681 0.618   1.00 15.52 ?  135 ASP   B O    1 
ATOM   6002 C CB   . ASP   B 1 135 ? 36.096 -36.117 2.174   1.00 18.19 ?  135 ASP   B CB   1 
ATOM   6003 C CG   . ASP   B 1 135 ? 35.900 -37.104 1.036   1.00 20.15 ?  135 ASP   B CG   1 
ATOM   6004 O OD1  . ASP   B 1 135 ? 36.757 -37.162 0.130   1.00 19.99 ?  135 ASP   B OD1  1 
ATOM   6005 O OD2  . ASP   B 1 135 ? 34.891 -37.848 1.065   1.00 23.00 -1 135 ASP   B OD2  1 
ATOM   6006 H H    . ASP   B 1 135 ? 36.802 -34.403 3.696   1.00 19.18 ?  135 ASP   B H    1 
ATOM   6007 H HA   . ASP   B 1 135 ? 38.156 -36.041 2.147   1.00 19.91 ?  135 ASP   B HA   1 
ATOM   6008 H HB2  . ASP   B 1 135 ? 36.050 -36.615 3.004   1.00 21.82 ?  135 ASP   B HB2  1 
ATOM   6009 H HB3  . ASP   B 1 135 ? 35.384 -35.461 2.139   1.00 21.82 ?  135 ASP   B HB3  1 
ATOM   6010 N N    . PRO   B 1 136 ? 38.542 -34.769 -0.011  1.00 15.74 ?  136 PRO   B N    1 
ATOM   6011 C CA   . PRO   B 1 136 ? 38.649 -33.941 -1.223  1.00 15.13 ?  136 PRO   B CA   1 
ATOM   6012 C C    . PRO   B 1 136 ? 37.466 -34.092 -2.157  1.00 14.48 ?  136 PRO   B C    1 
ATOM   6013 O O    . PRO   B 1 136 ? 37.142 -33.144 -2.880  1.00 13.78 ?  136 PRO   B O    1 
ATOM   6014 C CB   . PRO   B 1 136 ? 39.963 -34.412 -1.862  1.00 16.17 ?  136 PRO   B CB   1 
ATOM   6015 C CG   . PRO   B 1 136 ? 40.163 -35.802 -1.327  1.00 17.08 ?  136 PRO   B CG   1 
ATOM   6016 C CD   . PRO   B 1 136 ? 39.610 -35.778 0.068   1.00 16.80 ?  136 PRO   B CD   1 
ATOM   6017 H HA   . PRO   B 1 136 ? 38.737 -33.005 -0.985  1.00 18.15 ?  136 PRO   B HA   1 
ATOM   6018 H HB2  . PRO   B 1 136 ? 39.876 -34.429 -2.831  1.00 19.40 ?  136 PRO   B HB2  1 
ATOM   6019 H HB3  . PRO   B 1 136 ? 40.690 -33.831 -1.593  1.00 19.40 ?  136 PRO   B HB3  1 
ATOM   6020 H HG2  . PRO   B 1 136 ? 39.679 -36.441 -1.873  1.00 20.48 ?  136 PRO   B HG2  1 
ATOM   6021 H HG3  . PRO   B 1 136 ? 41.111 -36.016 -1.310  1.00 20.48 ?  136 PRO   B HG3  1 
ATOM   6022 H HD2  . PRO   B 1 136 ? 39.234 -36.643 0.302   1.00 20.15 ?  136 PRO   B HD2  1 
ATOM   6023 H HD3  . PRO   B 1 136 ? 40.288 -35.503 0.705   1.00 20.15 ?  136 PRO   B HD3  1 
ATOM   6024 N N    . ILE   B 1 137 ? 36.807 -35.255 -2.163  1.00 14.85 ?  137 ILE   B N    1 
ATOM   6025 C CA   . ILE   B 1 137 ? 35.593 -35.421 -2.957  1.00 15.18 ?  137 ILE   B CA   1 
ATOM   6026 C C    . ILE   B 1 137 ? 34.520 -34.452 -2.481  1.00 14.91 ?  137 ILE   B C    1 
ATOM   6027 O O    . ILE   B 1 137 ? 33.802 -33.844 -3.284  1.00 14.45 ?  137 ILE   B O    1 
ATOM   6028 C CB   . ILE   B 1 137 ? 35.120 -36.889 -2.895  1.00 17.32 ?  137 ILE   B CB   1 
ATOM   6029 C CG1  . ILE   B 1 137 ? 36.108 -37.794 -3.637  1.00 19.66 ?  137 ILE   B CG1  1 
ATOM   6030 C CG2  . ILE   B 1 137 ? 33.716 -37.034 -3.471  1.00 17.67 ?  137 ILE   B CG2  1 
ATOM   6031 C CD1  . ILE   B 1 137 ? 35.804 -39.276 -3.506  1.00 22.01 ?  137 ILE   B CD1  1 
ATOM   6032 H H    . ILE   B 1 137 ? 37.040 -35.957 -1.726  1.00 17.81 ?  137 ILE   B H    1 
ATOM   6033 H HA   . ILE   B 1 137 ? 35.787 -35.218 -3.887  1.00 18.20 ?  137 ILE   B HA   1 
ATOM   6034 H HB   . ILE   B 1 137 ? 35.092 -37.164 -1.969  1.00 20.78 ?  137 ILE   B HB   1 
ATOM   6035 H HG12 . ILE   B 1 137 ? 36.087 -37.577 -4.582  1.00 23.58 ?  137 ILE   B HG12 1 
ATOM   6036 H HG13 . ILE   B 1 137 ? 36.994 -37.646 -3.282  1.00 23.58 ?  137 ILE   B HG13 1 
ATOM   6037 H HG21 . ILE   B 1 137 ? 33.498 -37.978 -3.564  1.00 21.20 ?  137 ILE   B HG21 1 
ATOM   6038 H HG22 . ILE   B 1 137 ? 33.077 -36.621 -2.869  1.00 21.20 ?  137 ILE   B HG22 1 
ATOM   6039 H HG23 . ILE   B 1 137 ? 33.680 -36.606 -4.339  1.00 21.20 ?  137 ILE   B HG23 1 
ATOM   6040 H HD11 . ILE   B 1 137 ? 36.560 -39.779 -3.845  1.00 26.40 ?  137 ILE   B HD11 1 
ATOM   6041 H HD12 . ILE   B 1 137 ? 35.657 -39.490 -2.571  1.00 26.40 ?  137 ILE   B HD12 1 
ATOM   6042 H HD13 . ILE   B 1 137 ? 35.010 -39.491 -4.023  1.00 26.40 ?  137 ILE   B HD13 1 
ATOM   6043 N N    . HIS   B 1 138 ? 34.384 -34.307 -1.167  1.00 14.84 ?  138 HIS   B N    1 
ATOM   6044 C CA   . HIS   B 1 138 ? 33.435 -33.342 -0.632  1.00 15.12 ?  138 HIS   B CA   1 
ATOM   6045 C C    . HIS   B 1 138 ? 33.856 -31.914 -0.945  1.00 14.25 ?  138 HIS   B C    1 
ATOM   6046 O O    . HIS   B 1 138 ? 33.009 -31.072 -1.255  1.00 14.68 ?  138 HIS   B O    1 
ATOM   6047 C CB   . HIS   B 1 138 ? 33.306 -33.525 0.871   1.00 16.34 ?  138 HIS   B CB   1 
ATOM   6048 C CG   . HIS   B 1 138 ? 32.370 -32.549 1.504   1.00 17.35 ?  138 HIS   B CG   1 
ATOM   6049 N ND1  . HIS   B 1 138 ? 31.032 -32.487 1.178   1.00 18.51 ?  138 HIS   B ND1  1 
ATOM   6050 C CD2  . HIS   B 1 138 ? 32.581 -31.570 2.415   1.00 17.83 ?  138 HIS   B CD2  1 
ATOM   6051 C CE1  . HIS   B 1 138 ? 30.454 -31.527 1.877   1.00 18.44 ?  138 HIS   B CE1  1 
ATOM   6052 N NE2  . HIS   B 1 138 ? 31.373 -30.953 2.635   1.00 18.12 ?  138 HIS   B NE2  1 
ATOM   6053 H H    . HIS   B 1 138 ? 34.828 -34.746 -0.581  1.00 17.80 ?  138 HIS   B H    1 
ATOM   6054 H HA   . HIS   B 1 138 ? 32.564 -33.501 -1.036  1.00 18.13 ?  138 HIS   B HA   1 
ATOM   6055 H HB2  . HIS   B 1 138 ? 32.968 -34.416 1.050   1.00 19.59 ?  138 HIS   B HB2  1 
ATOM   6056 H HB3  . HIS   B 1 138 ? 34.175 -33.408 1.276   1.00 19.59 ?  138 HIS   B HB3  1 
ATOM   6057 H HD1  . HIS   B 1 138 ? 30.632 -33.005 0.613   1.00 22.20 ?  138 HIS   B HD1  1 
ATOM   6058 H HD2  . HIS   B 1 138 ? 33.382 -31.360 2.826   1.00 21.39 ?  138 HIS   B HD2  1 
ATOM   6059 H HE1  . HIS   B 1 138 ? 29.547 -31.302 1.840   1.00 22.12 ?  138 HIS   B HE1  1 
ATOM   6060 N N    . SER   B 1 139 ? 35.151 -31.612 -0.863  1.00 13.86 ?  139 SER   B N    1 
ATOM   6061 C CA   . SER   B 1 139 ? 35.589 -30.260 -1.179  1.00 13.37 ?  139 SER   B CA   1 
ATOM   6062 C C    . SER   B 1 139 ? 35.254 -29.905 -2.618  1.00 12.49 ?  139 SER   B C    1 
ATOM   6063 O O    . SER   B 1 139 ? 34.808 -28.787 -2.896  1.00 12.62 ?  139 SER   B O    1 
ATOM   6064 C CB   . SER   B 1 139 ? 37.083 -30.123 -0.910  1.00 13.71 ?  139 SER   B CB   1 
ATOM   6065 O OG   . SER   B 1 139 ? 37.490 -28.788 -1.165  1.00 13.96 ?  139 SER   B OG   1 
ATOM   6066 H H    . SER   B 1 139 ? 35.770 -32.159 -0.643  1.00 16.62 ?  139 SER   B H    1 
ATOM   6067 H HA   . SER   B 1 139 ? 35.118 -29.640 -0.611  1.00 16.04 ?  139 SER   B HA   1 
ATOM   6068 H HB2  . SER   B 1 139 ? 37.258 -30.340 0.019   1.00 16.44 ?  139 SER   B HB2  1 
ATOM   6069 H HB3  . SER   B 1 139 ? 37.572 -30.728 -1.492  1.00 16.44 ?  139 SER   B HB3  1 
ATOM   6070 H HG   . SER   B 1 139 ? 38.316 -28.711 -1.018  1.00 16.74 ?  139 SER   B HG   1 
ATOM   6071 N N    . LEU   B 1 140 ? 35.443 -30.846 -3.545  1.00 12.21 ?  140 LEU   B N    1 
ATOM   6072 C CA   . LEU   B 1 140 ? 35.077 -30.600 -4.933  1.00 12.37 ?  140 LEU   B CA   1 
ATOM   6073 C C    . LEU   B 1 140 ? 33.572 -30.376 -5.065  1.00 12.71 ?  140 LEU   B C    1 
ATOM   6074 O O    . LEU   B 1 140 ? 33.132 -29.490 -5.801  1.00 12.52 ?  140 LEU   B O    1 
ATOM   6075 C CB   . LEU   B 1 140 ? 35.547 -31.762 -5.812  1.00 12.69 ?  140 LEU   B CB   1 
ATOM   6076 C CG   . LEU   B 1 140 ? 35.178 -31.652 -7.284  1.00 12.85 ?  140 LEU   B CG   1 
ATOM   6077 C CD1  . LEU   B 1 140 ? 35.729 -30.372 -7.899  1.00 13.84 ?  140 LEU   B CD1  1 
ATOM   6078 C CD2  . LEU   B 1 140 ? 35.658 -32.876 -8.043  1.00 13.93 ?  140 LEU   B CD2  1 
ATOM   6079 H H    . LEU   B 1 140 ? 35.774 -31.625 -3.401  1.00 14.64 ?  140 LEU   B H    1 
ATOM   6080 H HA   . LEU   B 1 140 ? 35.529 -29.798 -5.242  1.00 14.83 ?  140 LEU   B HA   1 
ATOM   6081 H HB2  . LEU   B 1 140 ? 36.519 -31.817 -5.764  1.00 15.21 ?  140 LEU   B HB2  1 
ATOM   6082 H HB3  . LEU   B 1 140 ? 35.161 -32.584 -5.480  1.00 15.21 ?  140 LEU   B HB3  1 
ATOM   6083 H HG   . LEU   B 1 140 ? 34.213 -31.616 -7.361  1.00 15.41 ?  140 LEU   B HG   1 
ATOM   6084 H HD11 . LEU   B 1 140 ? 35.585 -30.400 -8.858  1.00 16.59 ?  140 LEU   B HD11 1 
ATOM   6085 H HD12 . LEU   B 1 140 ? 35.258 -29.612 -7.519  1.00 16.59 ?  140 LEU   B HD12 1 
ATOM   6086 H HD13 . LEU   B 1 140 ? 36.673 -30.310 -7.705  1.00 16.59 ?  140 LEU   B HD13 1 
ATOM   6087 H HD21 . LEU   B 1 140 ? 35.404 -32.780 -8.977  1.00 16.71 ?  140 LEU   B HD21 1 
ATOM   6088 H HD22 . LEU   B 1 140 ? 36.616 -32.939 -7.963  1.00 16.71 ?  140 LEU   B HD22 1 
ATOM   6089 H HD23 . LEU   B 1 140 ? 35.231 -33.658 -7.665  1.00 16.71 ?  140 LEU   B HD23 1 
ATOM   6090 N N    . ARG   B 1 141 ? 32.772 -31.168 -4.349  1.00 12.88 ?  141 ARG   B N    1 
ATOM   6091 C CA   . ARG   B 1 141 ? 31.321 -30.989 -4.337  1.00 13.90 ?  141 ARG   B CA   1 
ATOM   6092 C C    . ARG   B 1 141 ? 30.944 -29.577 -3.903  1.00 13.28 ?  141 ARG   B C    1 
ATOM   6093 O O    . ARG   B 1 141 ? 30.138 -28.896 -4.556  1.00 13.32 ?  141 ARG   B O    1 
ATOM   6094 C CB   . ARG   B 1 141 ? 30.739 -32.023 -3.365  1.00 15.58 ?  141 ARG   B CB   1 
ATOM   6095 C CG   . ARG   B 1 141 ? 29.279 -31.915 -3.020  1.00 17.49 ?  141 ARG   B CG   1 
ATOM   6096 C CD   . ARG   B 1 141 ? 28.461 -32.542 -4.078  1.00 19.33 ?  141 ARG   B CD   1 
ATOM   6097 N NE   . ARG   B 1 141 ? 28.215 -31.628 -5.182  1.00 19.72 ?  141 ARG   B NE   1 
ATOM   6098 C CZ   . ARG   B 1 141 ? 28.204 -31.974 -6.461  1.00 19.43 ?  141 ARG   B CZ   1 
ATOM   6099 N NH1  . ARG   B 1 141 ? 28.628 -33.163 -6.861  1.00 19.37 ?  141 ARG   B NH1  1 
ATOM   6100 N NH2  . ARG   B 1 141 ? 27.751 -31.106 -7.361  1.00 20.13 ?  141 ARG   B NH2  1 
ATOM   6101 H H    . ARG   B 1 141 ? 33.051 -31.816 -3.864  1.00 15.45 ?  141 ARG   B H    1 
ATOM   6102 H HA   . ARG   B 1 141 ? 30.962 -31.151 -5.223  1.00 16.67 ?  141 ARG   B HA   1 
ATOM   6103 H HB2  . ARG   B 1 141 ? 30.890 -32.905 -3.744  1.00 18.68 ?  141 ARG   B HB2  1 
ATOM   6104 H HB3  . ARG   B 1 141 ? 31.233 -31.957 -2.533  1.00 18.68 ?  141 ARG   B HB3  1 
ATOM   6105 H HG2  . ARG   B 1 141 ? 29.119 -32.375 -2.184  1.00 20.97 ?  141 ARG   B HG2  1 
ATOM   6106 H HG3  . ARG   B 1 141 ? 29.026 -30.979 -2.941  1.00 20.97 ?  141 ARG   B HG3  1 
ATOM   6107 H HD2  . ARG   B 1 141 ? 28.924 -33.330 -4.414  1.00 23.18 ?  141 ARG   B HD2  1 
ATOM   6108 H HD3  . ARG   B 1 141 ? 27.610 -32.804 -3.702  1.00 23.18 ?  141 ARG   B HD3  1 
ATOM   6109 H HE   . ARG   B 1 141 ? 28.047 -30.807 -4.987  1.00 23.66 ?  141 ARG   B HE   1 
ATOM   6110 H HH11 . ARG   B 1 141 ? 28.910 -33.741 -6.291  1.00 23.23 ?  141 ARG   B HH11 1 
ATOM   6111 H HH12 . ARG   B 1 141 ? 28.617 -33.360 -7.696  1.00 23.23 ?  141 ARG   B HH12 1 
ATOM   6112 H HH21 . ARG   B 1 141 ? 27.481 -30.327 -7.113  1.00 24.15 ?  141 ARG   B HH21 1 
ATOM   6113 H HH22 . ARG   B 1 141 ? 27.757 -31.309 -8.198  1.00 24.15 ?  141 ARG   B HH22 1 
ATOM   6114 N N    . VAL   B 1 142 ? 31.493 -29.133 -2.776  1.00 13.07 ?  142 VAL   B N    1 
ATOM   6115 C CA   . VAL   B 1 142 ? 31.155 -27.803 -2.288  1.00 12.87 ?  142 VAL   B CA   1 
ATOM   6116 C C    . VAL   B 1 142 ? 31.628 -26.743 -3.275  1.00 12.76 ?  142 VAL   B C    1 
ATOM   6117 O O    . VAL   B 1 142 ? 30.929 -25.757 -3.532  1.00 13.10 ?  142 VAL   B O    1 
ATOM   6118 C CB   . VAL   B 1 142 ? 31.698 -27.578 -0.864  1.00 13.48 ?  142 VAL   B CB   1 
ATOM   6119 C CG1  . VAL   B 1 142 ? 31.375 -26.155 -0.389  1.00 13.33 ?  142 VAL   B CG1  1 
ATOM   6120 C CG2  . VAL   B 1 142 ? 31.121 -28.603 0.095   1.00 14.33 ?  142 VAL   B CG2  1 
ATOM   6121 H H    . VAL   B 1 142 ? 32.053 -29.568 -2.291  1.00 15.67 ?  142 VAL   B H    1 
ATOM   6122 H HA   . VAL   B 1 142 ? 30.194 -27.732 -2.239  1.00 15.44 ?  142 VAL   B HA   1 
ATOM   6123 H HB   . VAL   B 1 142 ? 32.663 -27.679 -0.871  1.00 16.17 ?  142 VAL   B HB   1 
ATOM   6124 H HG11 . VAL   B 1 142 ? 31.553 -26.094 0.560   1.00 15.98 ?  142 VAL   B HG11 1 
ATOM   6125 H HG12 . VAL   B 1 142 ? 31.933 -25.525 -0.873  1.00 15.98 ?  142 VAL   B HG12 1 
ATOM   6126 H HG13 . VAL   B 1 142 ? 30.438 -25.972 -0.565  1.00 15.98 ?  142 VAL   B HG13 1 
ATOM   6127 H HG21 . VAL   B 1 142 ? 31.446 -28.414 0.988   1.00 17.19 ?  142 VAL   B HG21 1 
ATOM   6128 H HG22 . VAL   B 1 142 ? 30.153 -28.541 0.073   1.00 17.19 ?  142 VAL   B HG22 1 
ATOM   6129 H HG23 . VAL   B 1 142 ? 31.403 -29.487 -0.183  1.00 17.19 ?  142 VAL   B HG23 1 
ATOM   6130 N N    . CYS   B 1 143 ? 32.810 -26.940 -3.861  1.00 12.18 ?  143 CYS   B N    1 
ATOM   6131 C CA   . CYS   B 1 143 ? 33.303 -25.996 -4.858  1.00 12.08 ?  143 CYS   B CA   1 
ATOM   6132 C C    . CYS   B 1 143 ? 32.302 -25.848 -5.999  1.00 12.00 ?  143 CYS   B C    1 
ATOM   6133 O O    . CYS   B 1 143 ? 31.893 -24.738 -6.354  1.00 12.31 ?  143 CYS   B O    1 
ATOM   6134 C CB   . CYS   B 1 143 ? 34.663 -26.476 -5.382  1.00 12.53 ?  143 CYS   B CB   1 
ATOM   6135 S SG   . CYS   B 1 143 ? 35.411 -25.382 -6.600  1.00 12.68 ?  143 CYS   B SG   1 
ATOM   6136 H H    . CYS   B 1 143 ? 33.338 -27.599 -3.703  1.00 14.61 ?  143 CYS   B H    1 
ATOM   6137 H HA   . CYS   B 1 143 ? 33.430 -25.125 -4.450  1.00 14.48 ?  143 CYS   B HA   1 
ATOM   6138 H HB2  . CYS   B 1 143 ? 35.284 -26.550 -4.641  1.00 15.03 ?  143 CYS   B HB2  1 
ATOM   6139 H HB3  . CYS   B 1 143 ? 34.551 -27.342 -5.798  1.00 15.03 ?  143 CYS   B HB3  1 
ATOM   6140 H HG   . CYS   B 1 143 ? 36.481 -25.821 -6.925  1.00 15.20 ?  143 CYS   B HG   1 
ATOM   6141 N N    . VAL   B 1 144 ? 31.897 -26.969 -6.589  1.00 12.57 ?  144 VAL   B N    1 
ATOM   6142 C CA   . VAL   B 1 144 ? 30.992 -26.909 -7.731  1.00 13.51 ?  144 VAL   B CA   1 
ATOM   6143 C C    . VAL   B 1 144 ? 29.653 -26.300 -7.354  1.00 13.53 ?  144 VAL   B C    1 
ATOM   6144 O O    . VAL   B 1 144 ? 29.036 -25.590 -8.161  1.00 14.74 ?  144 VAL   B O    1 
ATOM   6145 C CB   . VAL   B 1 144 ? 30.834 -28.319 -8.308  1.00 15.91 ?  144 VAL   B CB   1 
ATOM   6146 C CG1  . VAL   B 1 144 ? 29.561 -28.434 -9.145  1.00 18.08 ?  144 VAL   B CG1  1 
ATOM   6147 C CG2  . VAL   B 1 144 ? 32.086 -28.711 -9.087  1.00 15.96 ?  144 VAL   B CG2  1 
ATOM   6148 H H    . VAL   B 1 144 ? 32.133 -27.764 -6.358  1.00 15.07 ?  144 VAL   B H    1 
ATOM   6149 H HA   . VAL   B 1 144 ? 31.383 -26.353 -8.421  1.00 16.21 ?  144 VAL   B HA   1 
ATOM   6150 H HB   . VAL   B 1 144 ? 30.747 -28.947 -7.572  1.00 19.08 ?  144 VAL   B HB   1 
ATOM   6151 H HG11 . VAL   B 1 144 ? 29.634 -29.218 -9.717  1.00 21.69 ?  144 VAL   B HG11 1 
ATOM   6152 H HG12 . VAL   B 1 144 ? 28.800 -28.535 -8.553  1.00 21.69 ?  144 VAL   B HG12 1 
ATOM   6153 H HG13 . VAL   B 1 144 ? 29.466 -27.641 -9.689  1.00 21.69 ?  144 VAL   B HG13 1 
ATOM   6154 H HG21 . VAL   B 1 144 ? 31.971 -29.607 -9.442  1.00 19.14 ?  144 VAL   B HG21 1 
ATOM   6155 H HG22 . VAL   B 1 144 ? 32.210 -28.082 -9.816  1.00 19.14 ?  144 VAL   B HG22 1 
ATOM   6156 H HG23 . VAL   B 1 144 ? 32.848 -28.684 -8.491  1.00 19.14 ?  144 VAL   B HG23 1 
ATOM   6157 N N    . ASP   B 1 145 ? 29.192 -26.541 -6.133  1.00 13.52 ?  145 ASP   B N    1 
ATOM   6158 C CA   . ASP   B 1 145 ? 27.882 -26.076 -5.699  1.00 14.21 ?  145 ASP   B CA   1 
ATOM   6159 C C    . ASP   B 1 145 ? 27.909 -24.654 -5.154  1.00 13.58 ?  145 ASP   B C    1 
ATOM   6160 O O    . ASP   B 1 145 ? 26.848 -24.113 -4.825  1.00 15.67 ?  145 ASP   B O    1 
ATOM   6161 C CB   . ASP   B 1 145 ? 27.298 -27.006 -4.623  1.00 15.98 ?  145 ASP   B CB   1 
ATOM   6162 C CG   . ASP   B 1 145 ? 26.932 -28.376 -5.142  1.00 17.65 ?  145 ASP   B CG   1 
ATOM   6163 O OD1  . ASP   B 1 145 ? 26.823 -28.559 -6.370  1.00 18.12 ?  145 ASP   B OD1  1 
ATOM   6164 O OD2  . ASP   B 1 145 ? 26.747 -29.268 -4.294  1.00 19.98 -1 145 ASP   B OD2  1 
ATOM   6165 H H    . ASP   B 1 145 ? 29.631 -26.963 -5.528  1.00 16.22 ?  145 ASP   B H    1 
ATOM   6166 H HA   . ASP   B 1 145 ? 27.285 -26.069 -6.459  1.00 17.05 ?  145 ASP   B HA   1 
ATOM   6167 H HB2  . ASP   B 1 145 ? 27.948 -27.126 -3.925  1.00 19.16 ?  145 ASP   B HB2  1 
ATOM   6168 H HB3  . ASP   B 1 145 ? 26.490 -26.598 -4.269  1.00 19.16 ?  145 ASP   B HB3  1 
ATOM   6169 N N    . THR   B 1 146 ? 29.084 -24.040 -5.035  1.00 12.27 ?  146 THR   B N    1 
ATOM   6170 C CA   . THR   B 1 146 ? 29.220 -22.721 -4.425  1.00 12.04 ?  146 THR   B CA   1 
ATOM   6171 C C    . THR   B 1 146 ? 29.852 -21.690 -5.343  1.00 11.81 ?  146 THR   B C    1 
ATOM   6172 O O    . THR   B 1 146 ? 29.395 -20.533 -5.388  1.00 12.35 ?  146 THR   B O    1 
ATOM   6173 C CB   . THR   B 1 146 ? 30.043 -22.832 -3.134  1.00 12.41 ?  146 THR   B CB   1 
ATOM   6174 O OG1  . THR   B 1 146 ? 29.468 -23.829 -2.278  1.00 12.66 ?  146 THR   B OG1  1 
ATOM   6175 C CG2  . THR   B 1 146 ? 30.117 -21.490 -2.412  1.00 12.62 ?  146 THR   B CG2  1 
ATOM   6176 H H    . THR   B 1 146 ? 29.836 -24.371 -5.302  1.00 14.71 ?  146 THR   B H    1 
ATOM   6177 H HA   . THR   B 1 146 ? 28.347 -22.392 -4.185  1.00 14.43 ?  146 THR   B HA   1 
ATOM   6178 H HB   . THR   B 1 146 ? 30.951 -23.091 -3.357  1.00 14.89 ?  146 THR   B HB   1 
ATOM   6179 H HG1  . THR   B 1 146 ? 29.507 -24.584 -2.663  1.00 15.18 ?  146 THR   B HG1  1 
ATOM   6180 H HG21 . THR   B 1 146 ? 30.464 -21.617 -1.516  1.00 15.13 ?  146 THR   B HG21 1 
ATOM   6181 H HG22 . THR   B 1 146 ? 30.706 -20.886 -2.894  1.00 15.13 ?  146 THR   B HG22 1 
ATOM   6182 H HG23 . THR   B 1 146 ? 29.235 -21.096 -2.357  1.00 15.13 ?  146 THR   B HG23 1 
ATOM   6183 N N    . VAL   B 1 147 ? 30.915 -22.063 -6.046  1.00 11.83 ?  147 VAL   B N    1 
ATOM   6184 C CA   . VAL   B 1 147 ? 31.637 -21.116 -6.882  1.00 11.55 ?  147 VAL   B CA   1 
ATOM   6185 C C    . VAL   B 1 147 ? 30.903 -20.981 -8.203  1.00 11.75 ?  147 VAL   B C    1 
ATOM   6186 O O    . VAL   B 1 147 ? 30.539 -21.987 -8.830  1.00 12.43 ?  147 VAL   B O    1 
ATOM   6187 C CB   . VAL   B 1 147 ? 33.089 -21.574 -7.091  1.00 11.85 ?  147 VAL   B CB   1 
ATOM   6188 C CG1  . VAL   B 1 147 ? 33.848 -20.549 -7.911  1.00 11.97 ?  147 VAL   B CG1  1 
ATOM   6189 C CG2  . VAL   B 1 147 ? 33.774 -21.791 -5.752  1.00 11.96 ?  147 VAL   B CG2  1 
ATOM   6190 H H    . VAL   B 1 147 ? 31.242 -22.862 -6.062  1.00 14.19 ?  147 VAL   B H    1 
ATOM   6191 H HA   . VAL   B 1 147 ? 31.657 -20.250 -6.452  1.00 13.85 ?  147 VAL   B HA   1 
ATOM   6192 H HB   . VAL   B 1 147 ? 33.102 -22.416 -7.578  1.00 14.21 ?  147 VAL   B HB   1 
ATOM   6193 H HG11 . VAL   B 1 147 ? 34.795 -20.767 -7.898  1.00 14.36 ?  147 VAL   B HG11 1 
ATOM   6194 H HG12 . VAL   B 1 147 ? 33.520 -20.560 -8.822  1.00 14.36 ?  147 VAL   B HG12 1 
ATOM   6195 H HG13 . VAL   B 1 147 ? 33.711 -19.670 -7.519  1.00 14.36 ?  147 VAL   B HG13 1 
ATOM   6196 H HG21 . VAL   B 1 147 ? 34.716 -21.986 -5.902  1.00 14.34 ?  147 VAL   B HG21 1 
ATOM   6197 H HG22 . VAL   B 1 147 ? 33.689 -20.984 -5.220  1.00 14.34 ?  147 VAL   B HG22 1 
ATOM   6198 H HG23 . VAL   B 1 147 ? 33.355 -22.535 -5.296  1.00 14.34 ?  147 VAL   B HG23 1 
ATOM   6199 N N    . ARG   B 1 148 ? 30.693 -19.736 -8.625  1.00 11.75 ?  148 ARG   B N    1 
ATOM   6200 C CA   . ARG   B 1 148 ? 30.069 -19.416 -9.898  1.00 11.78 ?  148 ARG   B CA   1 
ATOM   6201 C C    . ARG   B 1 148 ? 31.024 -18.741 -10.870 1.00 12.05 ?  148 ARG   B C    1 
ATOM   6202 O O    . ARG   B 1 148 ? 30.743 -18.724 -12.071 1.00 13.29 ?  148 ARG   B O    1 
ATOM   6203 C CB   . ARG   B 1 148 ? 28.835 -18.529 -9.674  1.00 12.35 ?  148 ARG   B CB   1 
ATOM   6204 C CG   . ARG   B 1 148 ? 27.758 -19.236 -8.857  1.00 13.07 ?  148 ARG   B CG   1 
ATOM   6205 C CD   . ARG   B 1 148 ? 26.551 -18.352 -8.546  1.00 13.90 ?  148 ARG   B CD   1 
ATOM   6206 N NE   . ARG   B 1 148 ? 26.932 -17.150 -7.815  1.00 13.61 ?  148 ARG   B NE   1 
ATOM   6207 C CZ   . ARG   B 1 148 ? 27.230 -17.117 -6.523  1.00 12.82 ?  148 ARG   B CZ   1 
ATOM   6208 N NH1  . ARG   B 1 148 ? 27.170 -18.204 -5.768  1.00 12.95 ?  148 ARG   B NH1  1 
ATOM   6209 N NH2  . ARG   B 1 148 ? 27.631 -15.969 -5.979  1.00 13.11 ?  148 ARG   B NH2  1 
ATOM   6210 H H    . ARG   B 1 148 ? 30.916 -19.038 -8.169  1.00 14.09 ?  148 ARG   B H    1 
ATOM   6211 H HA   . ARG   B 1 148 ? 29.769 -20.240 -10.305 1.00 14.12 ?  148 ARG   B HA   1 
ATOM   6212 H HB2  . ARG   B 1 148 ? 29.103 -17.728 -9.192  1.00 14.81 ?  148 ARG   B HB2  1 
ATOM   6213 H HB3  . ARG   B 1 148 ? 28.459 -18.290 -10.533 1.00 14.81 ?  148 ARG   B HB3  1 
ATOM   6214 H HG2  . ARG   B 1 148 ? 27.439 -20.004 -9.357  1.00 15.67 ?  148 ARG   B HG2  1 
ATOM   6215 H HG3  . ARG   B 1 148 ? 28.138 -19.526 -8.014  1.00 15.67 ?  148 ARG   B HG3  1 
ATOM   6216 H HD2  . ARG   B 1 148 ? 26.132 -18.079 -9.375  1.00 16.67 ?  148 ARG   B HD2  1 
ATOM   6217 H HD3  . ARG   B 1 148 ? 25.920 -18.851 -8.002  1.00 16.67 ?  148 ARG   B HD3  1 
ATOM   6218 H HE   . ARG   B 1 148 ? 26.967 -16.411 -8.249  1.00 16.32 ?  148 ARG   B HE   1 
ATOM   6219 H HH11 . ARG   B 1 148 ? 26.913 -18.956 -6.103  1.00 15.53 ?  148 ARG   B HH11 1 
ATOM   6220 H HH12 . ARG   B 1 148 ? 27.364 -18.161 -4.928  1.00 15.53 ?  148 ARG   B HH12 1 
ATOM   6221 H HH21 . ARG   B 1 148 ? 27.676 -15.260 -6.459  1.00 15.72 ?  148 ARG   B HH21 1 
ATOM   6222 H HH22 . ARG   B 1 148 ? 27.825 -15.934 -5.141  1.00 15.72 ?  148 ARG   B HH22 1 
ATOM   6223 N N    . THR   B 1 149 ? 32.130 -18.188 -10.382 1.00 12.00 ?  149 THR   B N    1 
ATOM   6224 C CA   . THR   B 1 149 ? 33.169 -17.628 -11.229 1.00 12.09 ?  149 THR   B CA   1 
ATOM   6225 C C    . THR   B 1 149 ? 34.057 -18.765 -11.739 1.00 11.57 ?  149 THR   B C    1 
ATOM   6226 O O    . THR   B 1 149 ? 33.870 -19.935 -11.394 1.00 12.02 ?  149 THR   B O    1 
ATOM   6227 C CB   . THR   B 1 149 ? 33.943 -16.577 -10.442 1.00 12.14 ?  149 THR   B CB   1 
ATOM   6228 O OG1  . THR   B 1 149 ? 34.392 -17.175 -9.225  1.00 12.09 ?  149 THR   B OG1  1 
ATOM   6229 C CG2  . THR   B 1 149 ? 33.054 -15.367 -10.147 1.00 12.66 ?  149 THR   B CG2  1 
ATOM   6230 H H    . THR   B 1 149 ? 32.296 -18.120 -9.543  1.00 14.38 ?  149 THR   B H    1 
ATOM   6231 H HA   . THR   B 1 149 ? 32.762 -17.191 -11.994 1.00 14.50 ?  149 THR   B HA   1 
ATOM   6232 H HB   . THR   B 1 149 ? 34.708 -16.287 -10.956 1.00 14.56 ?  149 THR   B HB   1 
ATOM   6233 H HG1  . THR   B 1 149 ? 34.810 -16.607 -8.763  1.00 14.50 ?  149 THR   B HG1  1 
ATOM   6234 H HG21 . THR   B 1 149 ? 33.560 -14.698 -9.656  1.00 15.18 ?  149 THR   B HG21 1 
ATOM   6235 H HG22 . THR   B 1 149 ? 32.742 -14.975 -10.978 1.00 15.18 ?  149 THR   B HG22 1 
ATOM   6236 H HG23 . THR   B 1 149 ? 32.289 -15.633 -9.616  1.00 15.18 ?  149 THR   B HG23 1 
ATOM   6237 N N    . ASN   B 1 150 ? 35.020 -18.443 -12.591 1.00 11.68 ?  150 ASN   B N    1 
ATOM   6238 C CA   . ASN   B 1 150 ? 35.788 -19.467 -13.286 1.00 11.95 ?  150 ASN   B CA   1 
ATOM   6239 C C    . ASN   B 1 150 ? 36.949 -19.917 -12.412 1.00 11.81 ?  150 ASN   B C    1 
ATOM   6240 O O    . ASN   B 1 150 ? 37.878 -19.146 -12.150 1.00 12.68 ?  150 ASN   B O    1 
ATOM   6241 C CB   . ASN   B 1 150 ? 36.258 -18.935 -14.632 1.00 13.98 ?  150 ASN   B CB   1 
ATOM   6242 C CG   . ASN   B 1 150 ? 35.111 -18.722 -15.578 1.00 16.51 ?  150 ASN   B CG   1 
ATOM   6243 O OD1  . ASN   B 1 150 ? 34.217 -19.554 -15.659 1.00 17.30 ?  150 ASN   B OD1  1 
ATOM   6244 N ND2  . ASN   B 1 150 ? 35.102 -17.594 -16.266 1.00 18.25 ?  150 ASN   B ND2  1 
ATOM   6245 H H    . ASN   B 1 150 ? 35.260 -17.633 -12.776 1.00 14.01 ?  150 ASN   B H    1 
ATOM   6246 H HA   . ASN   B 1 150 ? 35.209 -20.232 -13.449 1.00 14.34 ?  150 ASN   B HA   1 
ATOM   6247 H HB2  . ASN   B 1 150 ? 36.701 -18.081 -14.496 1.00 16.76 ?  150 ASN   B HB2  1 
ATOM   6248 H HB3  . ASN   B 1 150 ? 36.867 -19.571 -15.030 1.00 16.76 ?  150 ASN   B HB3  1 
ATOM   6249 H HD21 . ASN   B 1 150 ? 34.464 -17.429 -16.820 1.00 21.89 ?  150 ASN   B HD21 1 
ATOM   6250 H HD22 . ASN   B 1 150 ? 35.745 -17.027 -16.174 1.00 21.89 ?  150 ASN   B HD22 1 
ATOM   6251 N N    . VAL   B 1 151 ? 36.908 -21.166 -11.965 1.00 11.32 ?  151 VAL   B N    1 
ATOM   6252 C CA   . VAL   B 1 151 ? 37.929 -21.696 -11.074 1.00 11.49 ?  151 VAL   B CA   1 
ATOM   6253 C C    . VAL   B 1 151 ? 38.638 -22.863 -11.749 1.00 11.36 ?  151 VAL   B C    1 
ATOM   6254 O O    . VAL   B 1 151 ? 37.996 -23.795 -12.258 1.00 12.41 ?  151 VAL   B O    1 
ATOM   6255 C CB   . VAL   B 1 151 ? 37.374 -22.034 -9.674  1.00 12.79 ?  151 VAL   B CB   1 
ATOM   6256 C CG1  . VAL   B 1 151 ? 36.214 -23.035 -9.742  1.00 13.66 ?  151 VAL   B CG1  1 
ATOM   6257 C CG2  . VAL   B 1 151 ? 38.492 -22.518 -8.762  1.00 13.30 ?  151 VAL   B CG2  1 
ATOM   6258 H H    . VAL   B 1 151 ? 36.287 -21.732 -12.165 1.00 13.57 ?  151 VAL   B H    1 
ATOM   6259 H HA   . VAL   B 1 151 ? 38.595 -21.001 -10.945 1.00 13.78 ?  151 VAL   B HA   1 
ATOM   6260 H HB   . VAL   B 1 151 ? 37.026 -21.217 -9.283  1.00 15.33 ?  151 VAL   B HB   1 
ATOM   6261 H HG11 . VAL   B 1 151 ? 35.905 -23.221 -8.840  1.00 16.38 ?  151 VAL   B HG11 1 
ATOM   6262 H HG12 . VAL   B 1 151 ? 35.493 -22.649 -10.263 1.00 16.38 ?  151 VAL   B HG12 1 
ATOM   6263 H HG13 . VAL   B 1 151 ? 36.524 -23.853 -10.160 1.00 16.38 ?  151 VAL   B HG13 1 
ATOM   6264 H HG21 . VAL   B 1 151 ? 38.148 -22.600 -7.857  1.00 15.96 ?  151 VAL   B HG21 1 
ATOM   6265 H HG22 . VAL   B 1 151 ? 38.808 -23.381 -9.073  1.00 15.96 ?  151 VAL   B HG22 1 
ATOM   6266 H HG23 . VAL   B 1 151 ? 39.219 -21.874 -8.778  1.00 15.96 ?  151 VAL   B HG23 1 
ATOM   6267 N N    . TYR   B 1 152 ? 39.968 -22.775 -11.768 1.00 10.74 ?  152 TYR   B N    1 
ATOM   6268 C CA   . TYR   B 1 152 ? 40.870 -23.757 -12.350 1.00 11.10 ?  152 TYR   B CA   1 
ATOM   6269 C C    . TYR   B 1 152 ? 41.592 -24.432 -11.190 1.00 10.58 ?  152 TYR   B C    1 
ATOM   6270 O O    . TYR   B 1 152 ? 42.440 -23.818 -10.536 1.00 11.18 ?  152 TYR   B O    1 
ATOM   6271 C CB   . TYR   B 1 152 ? 41.840 -23.049 -13.297 1.00 11.81 ?  152 TYR   B CB   1 
ATOM   6272 C CG   . TYR   B 1 152 ? 41.159 -22.588 -14.562 1.00 12.51 ?  152 TYR   B CG   1 
ATOM   6273 C CD1  . TYR   B 1 152 ? 40.487 -21.371 -14.624 1.00 13.09 ?  152 TYR   B CD1  1 
ATOM   6274 C CD2  . TYR   B 1 152 ? 41.162 -23.391 -15.690 1.00 13.54 ?  152 TYR   B CD2  1 
ATOM   6275 C CE1  . TYR   B 1 152 ? 39.846 -20.970 -15.783 1.00 14.31 ?  152 TYR   B CE1  1 
ATOM   6276 C CE2  . TYR   B 1 152 ? 40.532 -23.001 -16.848 1.00 14.36 ?  152 TYR   B CE2  1 
ATOM   6277 C CZ   . TYR   B 1 152 ? 39.875 -21.788 -16.895 1.00 14.75 ?  152 TYR   B CZ   1 
ATOM   6278 O OH   . TYR   B 1 152 ? 39.250 -21.418 -18.061 1.00 16.92 ?  152 TYR   B OH   1 
ATOM   6279 H H    . TYR   B 1 152 ? 40.400 -22.111 -11.421 1.00 12.88 ?  152 TYR   B H    1 
ATOM   6280 H HA   . TYR   B 1 152 ? 40.365 -24.425 -12.844 1.00 13.31 ?  152 TYR   B HA   1 
ATOM   6281 H HB2  . TYR   B 1 152 ? 42.206 -22.273 -12.845 1.00 14.17 ?  152 TYR   B HB2  1 
ATOM   6282 H HB3  . TYR   B 1 152 ? 42.554 -23.660 -13.536 1.00 14.17 ?  152 TYR   B HB3  1 
ATOM   6283 H HD1  . TYR   B 1 152 ? 40.465 -20.821 -13.871 1.00 15.70 ?  152 TYR   B HD1  1 
ATOM   6284 H HD2  . TYR   B 1 152 ? 41.603 -24.213 -15.662 1.00 16.23 ?  152 TYR   B HD2  1 
ATOM   6285 H HE1  . TYR   B 1 152 ? 39.403 -20.157 -15.815 1.00 17.17 ?  152 TYR   B HE1  1 
ATOM   6286 H HE2  . TYR   B 1 152 ? 40.551 -23.556 -17.593 1.00 17.23 ?  152 TYR   B HE2  1 
ATOM   6287 H HH   . TYR   B 1 152 ? 39.356 -22.022 -18.639 1.00 20.29 ?  152 TYR   B HH   1 
ATOM   6288 N N    . LEU   B 1 153 ? 41.231 -25.690 -10.925 1.00 10.97 ?  153 LEU   B N    1 
ATOM   6289 C CA   . LEU   B 1 153 ? 41.733 -26.441 -9.783  1.00 10.81 ?  153 LEU   B CA   1 
ATOM   6290 C C    . LEU   B 1 153 ? 42.964 -27.240 -10.176 1.00 11.17 ?  153 LEU   B C    1 
ATOM   6291 O O    . LEU   B 1 153 ? 42.947 -27.966 -11.172 1.00 12.25 ?  153 LEU   B O    1 
ATOM   6292 C CB   . LEU   B 1 153 ? 40.655 -27.399 -9.270  1.00 11.27 ?  153 LEU   B CB   1 
ATOM   6293 C CG   . LEU   B 1 153 ? 39.399 -26.743 -8.700  1.00 12.11 ?  153 LEU   B CG   1 
ATOM   6294 C CD1  . LEU   B 1 153 ? 38.313 -27.798 -8.551  1.00 12.71 ?  153 LEU   B CD1  1 
ATOM   6295 C CD2  . LEU   B 1 153 ? 39.700 -26.094 -7.362  1.00 12.52 ?  153 LEU   B CD2  1 
ATOM   6296 H H    . LEU   B 1 153 ? 40.669 -26.141 -11.407 1.00 13.15 ?  153 LEU   B H    1 
ATOM   6297 H HA   . LEU   B 1 153 ? 41.959 -25.827 -9.071  1.00 12.96 ?  153 LEU   B HA   1 
ATOM   6298 H HB2  . LEU   B 1 153 ? 40.372 -27.971 -10.001 1.00 13.51 ?  153 LEU   B HB2  1 
ATOM   6299 H HB3  . LEU   B 1 153 ? 41.038 -27.947 -8.563  1.00 13.51 ?  153 LEU   B HB3  1 
ATOM   6300 H HG   . LEU   B 1 153 ? 39.082 -26.056 -9.309  1.00 14.52 ?  153 LEU   B HG   1 
ATOM   6301 H HD11 . LEU   B 1 153 ? 37.512 -27.374 -8.204  1.00 15.24 ?  153 LEU   B HD11 1 
ATOM   6302 H HD12 . LEU   B 1 153 ? 38.137 -28.187 -9.417  1.00 15.24 ?  153 LEU   B HD12 1 
ATOM   6303 H HD13 . LEU   B 1 153 ? 38.624 -28.476 -7.933  1.00 15.24 ?  153 LEU   B HD13 1 
ATOM   6304 H HD21 . LEU   B 1 153 ? 38.886 -25.724 -6.993  1.00 15.01 ?  153 LEU   B HD21 1 
ATOM   6305 H HD22 . LEU   B 1 153 ? 40.061 -26.767 -6.760  1.00 15.01 ?  153 LEU   B HD22 1 
ATOM   6306 H HD23 . LEU   B 1 153 ? 40.356 -25.388 -7.492  1.00 15.01 ?  153 LEU   B HD23 1 
ATOM   6307 N N    . ALA   B 1 154 ? 44.014 -27.131 -9.371  1.00 11.26 ?  154 ALA   B N    1 
ATOM   6308 C CA   . ALA   B 1 154 ? 45.242 -27.887 -9.559  1.00 12.34 ?  154 ALA   B CA   1 
ATOM   6309 C C    . ALA   B 1 154 ? 45.307 -28.967 -8.488  1.00 12.62 ?  154 ALA   B C    1 
ATOM   6310 O O    . ALA   B 1 154 ? 45.226 -28.669 -7.289  1.00 13.96 ?  154 ALA   B O    1 
ATOM   6311 C CB   . ALA   B 1 154 ? 46.468 -26.979 -9.494  1.00 13.36 ?  154 ALA   B CB   1 
ATOM   6312 H H    . ALA   B 1 154 ? 44.033 -26.602 -8.686  1.00 13.50 ?  154 ALA   B H    1 
ATOM   6313 H HA   . ALA   B 1 154 ? 45.226 -28.314 -10.424 1.00 14.80 ?  154 ALA   B HA   1 
ATOM   6314 H HB1  . ALA   B 1 154 ? 47.267 -27.515 -9.620  1.00 16.03 ?  154 ALA   B HB1  1 
ATOM   6315 H HB2  . ALA   B 1 154 ? 46.406 -26.308 -10.193 1.00 16.03 ?  154 ALA   B HB2  1 
ATOM   6316 H HB3  . ALA   B 1 154 ? 46.500 -26.544 -8.624  1.00 16.03 ?  154 ALA   B HB3  1 
ATOM   6317 N N    . VAL   B 1 155 ? 45.434 -30.214 -8.922  1.00 12.06 ?  155 VAL   B N    1 
ATOM   6318 C CA   . VAL   B 1 155 ? 45.536 -31.362 -8.031  1.00 12.15 ?  155 VAL   B CA   1 
ATOM   6319 C C    . VAL   B 1 155 ? 46.876 -32.032 -8.308  1.00 12.28 ?  155 VAL   B C    1 
ATOM   6320 O O    . VAL   B 1 155 ? 47.112 -32.524 -9.418  1.00 13.89 ?  155 VAL   B O    1 
ATOM   6321 C CB   . VAL   B 1 155 ? 44.378 -32.353 -8.235  1.00 13.66 ?  155 VAL   B CB   1 
ATOM   6322 C CG1  . VAL   B 1 155 ? 44.556 -33.557 -7.332  1.00 13.73 ?  155 VAL   B CG1  1 
ATOM   6323 C CG2  . VAL   B 1 155 ? 43.037 -31.669 -7.969  1.00 14.70 ?  155 VAL   B CG2  1 
ATOM   6324 H H    . VAL   B 1 155 ? 45.468 -30.428 -9.755  1.00 14.47 ?  155 VAL   B H    1 
ATOM   6325 H HA   . VAL   B 1 155 ? 45.523 -31.067 -7.109  1.00 14.58 ?  155 VAL   B HA   1 
ATOM   6326 H HB   . VAL   B 1 155 ? 44.379 -32.662 -9.156  1.00 16.39 ?  155 VAL   B HB   1 
ATOM   6327 H HG11 . VAL   B 1 155 ? 43.728 -34.060 -7.300  1.00 16.47 ?  155 VAL   B HG11 1 
ATOM   6328 H HG12 . VAL   B 1 155 ? 45.266 -34.123 -7.687  1.00 16.47 ?  155 VAL   B HG12 1 
ATOM   6329 H HG13 . VAL   B 1 155 ? 44.794 -33.256 -6.441  1.00 16.47 ?  155 VAL   B HG13 1 
ATOM   6330 H HG21 . VAL   B 1 155 ? 42.324 -32.319 -8.065  1.00 17.63 ?  155 VAL   B HG21 1 
ATOM   6331 H HG22 . VAL   B 1 155 ? 43.039 -31.313 -7.065  1.00 17.63 ?  155 VAL   B HG22 1 
ATOM   6332 H HG23 . VAL   B 1 155 ? 42.916 -30.948 -8.607  1.00 17.63 ?  155 VAL   B HG23 1 
ATOM   6333 N N    . PHE   B 1 156 ? 47.743 -32.074 -7.292  1.00 12.75 ?  156 PHE   B N    1 
ATOM   6334 C CA   . PHE   B 1 156 ? 49.122 -32.530 -7.489  1.00 13.77 ?  156 PHE   B CA   1 
ATOM   6335 C C    . PHE   B 1 156 ? 49.222 -34.029 -7.774  1.00 14.57 ?  156 PHE   B C    1 
ATOM   6336 O O    . PHE   B 1 156 ? 49.954 -34.454 -8.678  1.00 16.28 ?  156 PHE   B O    1 
ATOM   6337 C CB   . PHE   B 1 156 ? 49.948 -32.165 -6.257  1.00 14.05 ?  156 PHE   B CB   1 
ATOM   6338 C CG   . PHE   B 1 156 ? 51.372 -32.627 -6.318  1.00 14.78 ?  156 PHE   B CG   1 
ATOM   6339 C CD1  . PHE   B 1 156 ? 52.253 -32.077 -7.226  1.00 16.38 ?  156 PHE   B CD1  1 
ATOM   6340 C CD2  . PHE   B 1 156 ? 51.829 -33.598 -5.453  1.00 14.89 ?  156 PHE   B CD2  1 
ATOM   6341 C CE1  . PHE   B 1 156 ? 53.572 -32.485 -7.277  1.00 17.17 ?  156 PHE   B CE1  1 
ATOM   6342 C CE2  . PHE   B 1 156 ? 53.149 -34.015 -5.500  1.00 16.29 ?  156 PHE   B CE2  1 
ATOM   6343 C CZ   . PHE   B 1 156 ? 54.013 -33.459 -6.419  1.00 16.76 ?  156 PHE   B CZ   1 
ATOM   6344 H H    . PHE   B 1 156 ? 47.556 -31.843 -6.482  1.00 15.29 ?  156 PHE   B H    1 
ATOM   6345 H HA   . PHE   B 1 156 ? 49.495 -32.059 -8.243  1.00 16.51 ?  156 PHE   B HA   1 
ATOM   6346 H HB2  . PHE   B 1 156 ? 49.957 -31.200 -6.163  1.00 16.85 ?  156 PHE   B HB2  1 
ATOM   6347 H HB3  . PHE   B 1 156 ? 49.543 -32.567 -5.473  1.00 16.85 ?  156 PHE   B HB3  1 
ATOM   6348 H HD1  . PHE   B 1 156 ? 51.958 -31.411 -7.809  1.00 19.65 ?  156 PHE   B HD1  1 
ATOM   6349 H HD2  . PHE   B 1 156 ? 51.242 -33.980 -4.837  1.00 17.86 ?  156 PHE   B HD2  1 
ATOM   6350 H HE1  . PHE   B 1 156 ? 54.153 -32.103 -7.899  1.00 20.60 ?  156 PHE   B HE1  1 
ATOM   6351 H HE2  . PHE   B 1 156 ? 53.445 -34.681 -4.921  1.00 19.54 ?  156 PHE   B HE2  1 
ATOM   6352 H HZ   . PHE   B 1 156 ? 54.897 -33.740 -6.453  1.00 20.10 ?  156 PHE   B HZ   1 
ATOM   6353 N N    . ASP   B 1 157 ? 48.544 -34.847 -6.983  1.00 15.04 ?  157 ASP   B N    1 
ATOM   6354 C CA   . ASP   B 1 157 ? 48.697 -36.294 -7.074  1.00 16.24 ?  157 ASP   B CA   1 
ATOM   6355 C C    . ASP   B 1 157 ? 47.784 -36.840 -8.168  1.00 16.29 ?  157 ASP   B C    1 
ATOM   6356 O O    . ASP   B 1 157 ? 46.556 -36.721 -8.071  1.00 15.57 ?  157 ASP   B O    1 
ATOM   6357 C CB   . ASP   B 1 157 ? 48.328 -36.911 -5.731  1.00 17.78 ?  157 ASP   B CB   1 
ATOM   6358 C CG   . ASP   B 1 157 ? 48.465 -38.419 -5.718  1.00 19.48 ?  157 ASP   B CG   1 
ATOM   6359 O OD1  . ASP   B 1 157 ? 48.787 -39.023 -6.769  1.00 19.94 ?  157 ASP   B OD1  1 
ATOM   6360 O OD2  . ASP   B 1 157 ? 48.267 -39.005 -4.635  1.00 21.57 -1 157 ASP   B OD2  1 
ATOM   6361 H H    . ASP   B 1 157 ? 47.988 -34.595 -6.386  1.00 18.04 ?  157 ASP   B H    1 
ATOM   6362 H HA   . ASP   B 1 157 ? 49.621 -36.526 -7.282  1.00 19.48 ?  157 ASP   B HA   1 
ATOM   6363 H HB2  . ASP   B 1 157 ? 48.897 -36.540 -5.044  1.00 21.33 ?  157 ASP   B HB2  1 
ATOM   6364 H HB3  . ASP   B 1 157 ? 47.397 -36.698 -5.537  1.00 21.33 ?  157 ASP   B HB3  1 
ATOM   6365 N N    . LYS   B 1 158 ? 48.382 -37.454 -9.197  1.00 17.17 ?  158 LYS   B N    1 
ATOM   6366 C CA   . LYS   B 1 158 ? 47.604 -38.064 -10.278 1.00 18.31 ?  158 LYS   B CA   1 
ATOM   6367 C C    . LYS   B 1 158 ? 46.546 -39.030 -9.748  1.00 18.15 ?  158 LYS   B C    1 
ATOM   6368 O O    . LYS   B 1 158 ? 45.444 -39.122 -10.301 1.00 18.26 ?  158 LYS   B O    1 
ATOM   6369 C CB   . LYS   B 1 158 ? 48.550 -38.779 -11.252 1.00 19.84 ?  158 LYS   B CB   1 
ATOM   6370 C CG   . LYS   B 1 158 ? 47.869 -39.666 -12.283 1.00 21.95 ?  158 LYS   B CG   1 
ATOM   6371 C CD   . LYS   B 1 158 ? 47.035 -38.871 -13.262 1.00 24.10 ?  158 LYS   B CD   1 
ATOM   6372 C CE   . LYS   B 1 158 ? 46.433 -39.779 -14.322 1.00 25.76 ?  158 LYS   B CE   1 
ATOM   6373 N NZ   . LYS   B 1 158 ? 45.376 -39.089 -15.114 1.00 26.04 ?  158 LYS   B NZ   1 
ATOM   6374 H H    . LYS   B 1 158 ? 49.240 -37.533 -9.295  1.00 20.60 ?  158 LYS   B H    1 
ATOM   6375 H HA   . LYS   B 1 158 ? 47.154 -37.365 -10.775 1.00 21.96 ?  158 LYS   B HA   1 
ATOM   6376 H HB2  . LYS   B 1 158 ? 49.060 -38.112 -11.744 1.00 23.80 ?  158 LYS   B HB2  1 
ATOM   6377 H HB3  . LYS   B 1 158 ? 49.159 -39.339 -10.746 1.00 23.80 ?  158 LYS   B HB3  1 
ATOM   6378 H HG2  . LYS   B 1 158 ? 48.550 -40.137 -12.790 1.00 26.34 ?  158 LYS   B HG2  1 
ATOM   6379 H HG3  . LYS   B 1 158 ? 47.294 -40.312 -11.841 1.00 26.34 ?  158 LYS   B HG3  1 
ATOM   6380 H HD2  . LYS   B 1 158 ? 46.313 -38.430 -12.789 1.00 28.91 ?  158 LYS   B HD2  1 
ATOM   6381 H HD3  . LYS   B 1 158 ? 47.597 -38.216 -13.706 1.00 28.91 ?  158 LYS   B HD3  1 
ATOM   6382 H HE2  . LYS   B 1 158 ? 47.128 -40.065 -14.933 1.00 30.91 ?  158 LYS   B HE2  1 
ATOM   6383 H HE3  . LYS   B 1 158 ? 46.029 -40.550 -13.890 1.00 30.91 ?  158 LYS   B HE3  1 
ATOM   6384 H HZ1  . LYS   B 1 158 ? 45.039 -39.641 -15.724 1.00 31.24 ?  158 LYS   B HZ1  1 
ATOM   6385 H HZ2  . LYS   B 1 158 ? 44.718 -38.818 -14.576 1.00 31.24 ?  158 LYS   B HZ2  1 
ATOM   6386 H HZ3  . LYS   B 1 158 ? 45.719 -38.378 -15.526 1.00 31.24 ?  158 LYS   B HZ3  1 
ATOM   6387 N N    . ASN   B 1 159 ? 46.868 -39.786 -8.697  1.00 18.59 ?  159 ASN   B N    1 
ATOM   6388 C CA   . ASN   B 1 159 ? 45.912 -40.768 -8.195  1.00 19.20 ?  159 ASN   B CA   1 
ATOM   6389 C C    . ASN   B 1 159 ? 44.716 -40.100 -7.518  1.00 18.23 ?  159 ASN   B C    1 
ATOM   6390 O O    . ASN   B 1 159 ? 43.584 -40.589 -7.637  1.00 18.67 ?  159 ASN   B O    1 
ATOM   6391 C CB   . ASN   B 1 159 ? 46.614 -41.754 -7.269  1.00 20.55 ?  159 ASN   B CB   1 
ATOM   6392 C CG   . ASN   B 1 159 ? 47.647 -42.582 -7.996  1.00 22.23 ?  159 ASN   B CG   1 
ATOM   6393 O OD1  . ASN   B 1 159 ? 47.387 -43.095 -9.090  1.00 23.12 ?  159 ASN   B OD1  1 
ATOM   6394 N ND2  . ASN   B 1 159 ? 48.828 -42.712 -7.404  1.00 23.17 ?  159 ASN   B ND2  1 
ATOM   6395 H H    . ASN   B 1 159 ? 47.606 -39.734 -8.265  1.00 22.30 ?  159 ASN   B H    1 
ATOM   6396 H HA   . ASN   B 1 159 ? 45.574 -41.270 -8.954  1.00 23.03 ?  159 ASN   B HA   1 
ATOM   6397 H HB2  . ASN   B 1 159 ? 47.063 -41.267 -6.564  1.00 24.65 ?  159 ASN   B HB2  1 
ATOM   6398 H HB3  . ASN   B 1 159 ? 45.957 -42.361 -6.898  1.00 24.65 ?  159 ASN   B HB3  1 
ATOM   6399 H HD21 . ASN   B 1 159 ? 49.454 -43.173 -7.780  1.00 27.79 ?  159 ASN   B HD21 1 
ATOM   6400 H HD22 . ASN   B 1 159 ? 48.969 -42.348 -6.638  1.00 27.79 ?  159 ASN   B HD22 1 
ATOM   6401 N N    . LEU   B 1 160 ? 44.927 -38.968 -6.837  1.00 17.12 ?  160 LEU   B N    1 
ATOM   6402 C CA   . LEU   B 1 160 ? 43.791 -38.233 -6.295  1.00 16.06 ?  160 LEU   B CA   1 
ATOM   6403 C C    . LEU   B 1 160 ? 43.005 -37.567 -7.412  1.00 15.45 ?  160 LEU   B C    1 
ATOM   6404 O O    . LEU   B 1 160 ? 41.766 -37.569 -7.396  1.00 15.09 ?  160 LEU   B O    1 
ATOM   6405 C CB   . LEU   B 1 160 ? 44.254 -37.206 -5.264  1.00 15.86 ?  160 LEU   B CB   1 
ATOM   6406 C CG   . LEU   B 1 160 ? 43.128 -36.307 -4.733  1.00 15.51 ?  160 LEU   B CG   1 
ATOM   6407 C CD1  . LEU   B 1 160 ? 42.002 -37.126 -4.110  1.00 16.23 ?  160 LEU   B CD1  1 
ATOM   6408 C CD2  . LEU   B 1 160 ? 43.670 -35.304 -3.730  1.00 15.64 ?  160 LEU   B CD2  1 
ATOM   6409 H H    . LEU   B 1 160 ? 45.703 -38.614 -6.688  1.00 20.53 ?  160 LEU   B H    1 
ATOM   6410 H HA   . LEU   B 1 160 ? 43.206 -38.860 -5.854  1.00 19.26 ?  160 LEU   B HA   1 
ATOM   6411 H HB2  . LEU   B 1 160 ? 44.645 -37.679 -4.510  1.00 19.02 ?  160 LEU   B HB2  1 
ATOM   6412 H HB3  . LEU   B 1 160 ? 44.929 -36.635 -5.671  1.00 19.02 ?  160 LEU   B HB3  1 
ATOM   6413 H HG   . LEU   B 1 160 ? 42.756 -35.805 -5.472  1.00 18.61 ?  160 LEU   B HG   1 
ATOM   6414 H HD11 . LEU   B 1 160 ? 41.366 -36.521 -3.701  1.00 19.47 ?  160 LEU   B HD11 1 
ATOM   6415 H HD12 . LEU   B 1 160 ? 41.566 -37.646 -4.803  1.00 19.47 ?  160 LEU   B HD12 1 
ATOM   6416 H HD13 . LEU   B 1 160 ? 42.376 -37.718 -3.437  1.00 19.47 ?  160 LEU   B HD13 1 
ATOM   6417 H HD21 . LEU   B 1 160 ? 42.944 -34.733 -3.435  1.00 18.76 ?  160 LEU   B HD21 1 
ATOM   6418 H HD22 . LEU   B 1 160 ? 44.046 -35.781 -2.975  1.00 18.76 ?  160 LEU   B HD22 1 
ATOM   6419 H HD23 . LEU   B 1 160 ? 44.358 -34.768 -4.159  1.00 18.76 ?  160 LEU   B HD23 1 
ATOM   6420 N N    . TYR   B 1 161 ? 43.705 -36.992 -8.392  1.00 15.46 ?  161 TYR   B N    1 
ATOM   6421 C CA   . TYR   B 1 161 ? 43.035 -36.427 -9.558  1.00 15.25 ?  161 TYR   B CA   1 
ATOM   6422 C C    . TYR   B 1 161 ? 42.090 -37.446 -10.184 1.00 15.11 ?  161 TYR   B C    1 
ATOM   6423 O O    . TYR   B 1 161 ? 40.921 -37.150 -10.448 1.00 14.70 ?  161 TYR   B O    1 
ATOM   6424 C CB   . TYR   B 1 161 ? 44.080 -35.951 -10.572 1.00 15.90 ?  161 TYR   B CB   1 
ATOM   6425 C CG   . TYR   B 1 161 ? 43.505 -35.480 -11.883 1.00 16.37 ?  161 TYR   B CG   1 
ATOM   6426 C CD1  . TYR   B 1 161 ? 43.117 -34.159 -12.052 1.00 16.31 ?  161 TYR   B CD1  1 
ATOM   6427 C CD2  . TYR   B 1 161 ? 43.331 -36.358 -12.947 1.00 17.03 ?  161 TYR   B CD2  1 
ATOM   6428 C CE1  . TYR   B 1 161 ? 42.584 -33.723 -13.238 1.00 17.39 ?  161 TYR   B CE1  1 
ATOM   6429 C CE2  . TYR   B 1 161 ? 42.791 -35.930 -14.138 1.00 18.13 ?  161 TYR   B CE2  1 
ATOM   6430 C CZ   . TYR   B 1 161 ? 42.424 -34.610 -14.280 1.00 18.05 ?  161 TYR   B CZ   1 
ATOM   6431 O OH   . TYR   B 1 161 ? 41.885 -34.173 -15.464 1.00 19.73 ?  161 TYR   B OH   1 
ATOM   6432 H H    . TYR   B 1 161 ? 44.561 -36.927 -8.414  1.00 18.54 ?  161 TYR   B H    1 
ATOM   6433 H HA   . TYR   B 1 161 ? 42.511 -35.661 -9.286  1.00 18.29 ?  161 TYR   B HA   1 
ATOM   6434 H HB2  . TYR   B 1 161 ? 44.574 -35.208 -10.187 1.00 19.07 ?  161 TYR   B HB2  1 
ATOM   6435 H HB3  . TYR   B 1 161 ? 44.689 -36.680 -10.766 1.00 19.07 ?  161 TYR   B HB3  1 
ATOM   6436 H HD1  . TYR   B 1 161 ? 43.235 -33.553 -11.355 1.00 19.57 ?  161 TYR   B HD1  1 
ATOM   6437 H HD2  . TYR   B 1 161 ? 43.573 -37.251 -12.855 1.00 20.43 ?  161 TYR   B HD2  1 
ATOM   6438 H HE1  . TYR   B 1 161 ? 42.343 -32.826 -13.336 1.00 20.86 ?  161 TYR   B HE1  1 
ATOM   6439 H HE2  . TYR   B 1 161 ? 42.677 -36.523 -14.844 1.00 21.74 ?  161 TYR   B HE2  1 
ATOM   6440 H HH   . TYR   B 1 161 ? 41.841 -34.810 -16.009 1.00 23.67 ?  161 TYR   B HH   1 
ATOM   6441 N N    . ASP   B 1 162 ? 42.583 -38.666 -10.413 1.00 15.52 ?  162 ASP   B N    1 
ATOM   6442 C CA   . ASP   B 1 162 ? 41.753 -39.699 -11.026 1.00 16.10 ?  162 ASP   B CA   1 
ATOM   6443 C C    . ASP   B 1 162 ? 40.548 -40.034 -10.154 1.00 15.29 ?  162 ASP   B C    1 
ATOM   6444 O O    . ASP   B 1 162 ? 39.444 -40.254 -10.667 1.00 15.79 ?  162 ASP   B O    1 
ATOM   6445 C CB   . ASP   B 1 162 ? 42.578 -40.963 -11.283 1.00 17.75 ?  162 ASP   B CB   1 
ATOM   6446 C CG   . ASP   B 1 162 ? 43.585 -40.802 -12.407 1.00 18.90 ?  162 ASP   B CG   1 
ATOM   6447 O OD1  . ASP   B 1 162 ? 43.454 -39.858 -13.210 1.00 18.98 ?  162 ASP   B OD1  1 
ATOM   6448 O OD2  . ASP   B 1 162 ? 44.494 -41.654 -12.500 1.00 20.61 -1 162 ASP   B OD2  1 
ATOM   6449 H H    . ASP   B 1 162 ? 43.384 -38.915 -10.228 1.00 18.62 ?  162 ASP   B H    1 
ATOM   6450 H HA   . ASP   B 1 162 ? 41.422 -39.374 -11.876 1.00 19.31 ?  162 ASP   B HA   1 
ATOM   6451 H HB2  . ASP   B 1 162 ? 43.066 -41.190 -10.480 1.00 21.29 ?  162 ASP   B HB2  1 
ATOM   6452 H HB3  . ASP   B 1 162 ? 41.980 -41.683 -11.530 1.00 21.29 ?  162 ASP   B HB3  1 
ATOM   6453 N N    . LYS   B 1 163 ? 40.741 -40.105 -8.835  1.00 15.09 ?  163 LYS   B N    1 
ATOM   6454 C CA   . LYS   B 1 163 ? 39.617 -40.386 -7.947  1.00 15.81 ?  163 LYS   B CA   1 
ATOM   6455 C C    . LYS   B 1 163 ? 38.572 -39.279 -8.013  1.00 14.66 ?  163 LYS   B C    1 
ATOM   6456 O O    . LYS   B 1 163 ? 37.363 -39.549 -8.023  1.00 15.68 ?  163 LYS   B O    1 
ATOM   6457 C CB   . LYS   B 1 163 ? 40.101 -40.566 -6.511  1.00 19.17 ?  163 LYS   B CB   1 
ATOM   6458 C CG   . LYS   B 1 163 ? 39.007 -41.067 -5.590  1.00 25.13 ?  163 LYS   B CG   1 
ATOM   6459 C CD   . LYS   B 1 163 ? 39.477 -41.265 -4.163  1.00 30.36 ?  163 LYS   B CD   1 
ATOM   6460 C CE   . LYS   B 1 163 ? 38.395 -41.958 -3.342  1.00 33.90 ?  163 LYS   B CE   1 
ATOM   6461 N NZ   . LYS   B 1 163 ? 38.464 -41.616 -1.894  1.00 36.50 ?  163 LYS   B NZ   1 
ATOM   6462 H H    . LYS   B 1 163 ? 41.499 -39.996 -8.439  1.00 18.10 ?  163 LYS   B H    1 
ATOM   6463 H HA   . LYS   B 1 163 ? 39.197 -41.211 -8.227  1.00 18.96 ?  163 LYS   B HA   1 
ATOM   6464 H HB2  . LYS   B 1 163 ? 40.824 -41.214 -6.499  1.00 22.99 ?  163 LYS   B HB2  1 
ATOM   6465 H HB3  . LYS   B 1 163 ? 40.412 -39.714 -6.170  1.00 22.99 ?  163 LYS   B HB3  1 
ATOM   6466 H HG2  . LYS   B 1 163 ? 38.282 -40.424 -5.578  1.00 30.15 ?  163 LYS   B HG2  1 
ATOM   6467 H HG3  . LYS   B 1 163 ? 38.684 -41.922 -5.921  1.00 30.15 ?  163 LYS   B HG3  1 
ATOM   6468 H HD2  . LYS   B 1 163 ? 40.271 -41.825 -4.158  1.00 36.42 ?  163 LYS   B HD2  1 
ATOM   6469 H HD3  . LYS   B 1 163 ? 39.665 -40.404 -3.761  1.00 36.42 ?  163 LYS   B HD3  1 
ATOM   6470 H HE2  . LYS   B 1 163 ? 37.523 -41.697 -3.677  1.00 40.67 ?  163 LYS   B HE2  1 
ATOM   6471 H HE3  . LYS   B 1 163 ? 38.504 -42.918 -3.426  1.00 40.67 ?  163 LYS   B HE3  1 
ATOM   6472 H HZ1  . LYS   B 1 163 ? 37.816 -42.038 -1.451  1.00 43.79 ?  163 LYS   B HZ1  1 
ATOM   6473 H HZ2  . LYS   B 1 163 ? 39.251 -41.863 -1.561  1.00 43.79 ?  163 LYS   B HZ2  1 
ATOM   6474 H HZ3  . LYS   B 1 163 ? 38.364 -40.738 -1.784  1.00 43.79 ?  163 LYS   B HZ3  1 
ATOM   6475 N N    . LEU   B 1 164 ? 39.023 -38.026 -8.058  1.00 13.62 ?  164 LEU   B N    1 
ATOM   6476 C CA   . LEU   B 1 164 ? 38.114 -36.888 -8.118  1.00 13.22 ?  164 LEU   B CA   1 
ATOM   6477 C C    . LEU   B 1 164 ? 37.332 -36.869 -9.426  1.00 13.51 ?  164 LEU   B C    1 
ATOM   6478 O O    . LEU   B 1 164 ? 36.109 -36.679 -9.428  1.00 14.56 ?  164 LEU   B O    1 
ATOM   6479 C CB   . LEU   B 1 164 ? 38.916 -35.597 -7.958  1.00 12.82 ?  164 LEU   B CB   1 
ATOM   6480 C CG   . LEU   B 1 164 ? 39.445 -35.323 -6.556  1.00 13.79 ?  164 LEU   B CG   1 
ATOM   6481 C CD1  . LEU   B 1 164 ? 40.530 -34.262 -6.610  1.00 13.91 ?  164 LEU   B CD1  1 
ATOM   6482 C CD2  . LEU   B 1 164 ? 38.329 -34.892 -5.627  1.00 15.44 ?  164 LEU   B CD2  1 
ATOM   6483 H H    . LEU   B 1 164 ? 39.859 -37.806 -8.052  1.00 16.34 ?  164 LEU   B H    1 
ATOM   6484 H HA   . LEU   B 1 164 ? 37.485 -36.943 -7.388  1.00 15.85 ?  164 LEU   B HA   1 
ATOM   6485 H HB2  . LEU   B 1 164 ? 39.685 -35.635 -8.555  1.00 15.37 ?  164 LEU   B HB2  1 
ATOM   6486 H HB3  . LEU   B 1 164 ? 38.355 -34.849 -8.209  1.00 15.37 ?  164 LEU   B HB3  1 
ATOM   6487 H HG   . LEU   B 1 164 ? 39.841 -36.132 -6.202  1.00 16.54 ?  164 LEU   B HG   1 
ATOM   6488 H HD11 . LEU   B 1 164 ? 40.854 -34.086 -5.710  1.00 16.68 ?  164 LEU   B HD11 1 
ATOM   6489 H HD12 . LEU   B 1 164 ? 41.266 -34.581 -7.163  1.00 16.68 ?  164 LEU   B HD12 1 
ATOM   6490 H HD13 . LEU   B 1 164 ? 40.168 -33.446 -6.993  1.00 16.68 ?  164 LEU   B HD13 1 
ATOM   6491 H HD21 . LEU   B 1 164 ? 38.707 -34.664 -4.764  1.00 18.52 ?  164 LEU   B HD21 1 
ATOM   6492 H HD22 . LEU   B 1 164 ? 37.880 -34.122 -6.007  1.00 18.52 ?  164 LEU   B HD22 1 
ATOM   6493 H HD23 . LEU   B 1 164 ? 37.702 -35.627 -5.530  1.00 18.52 ?  164 LEU   B HD23 1 
ATOM   6494 N N    . VAL   B 1 165 ? 38.021 -37.042 -10.554 1.00 14.82 ?  165 VAL   B N    1 
ATOM   6495 C CA   . VAL   B 1 165 ? 37.366 -36.971 -11.856 1.00 16.07 ?  165 VAL   B CA   1 
ATOM   6496 C C    . VAL   B 1 165 ? 36.448 -38.170 -12.049 1.00 17.62 ?  165 VAL   B C    1 
ATOM   6497 O O    . VAL   B 1 165 ? 35.294 -38.037 -12.474 1.00 18.34 ?  165 VAL   B O    1 
ATOM   6498 C CB   . VAL   B 1 165 ? 38.416 -36.883 -12.979 1.00 16.94 ?  165 VAL   B CB   1 
ATOM   6499 C CG1  . VAL   B 1 165 ? 37.760 -36.990 -14.336 1.00 18.19 ?  165 VAL   B CG1  1 
ATOM   6500 C CG2  . VAL   B 1 165 ? 39.208 -35.594 -12.866 1.00 16.98 ?  165 VAL   B CG2  1 
ATOM   6501 H H    . VAL   B 1 165 ? 38.867 -37.191 -10.591 1.00 17.78 ?  165 VAL   B H    1 
ATOM   6502 H HA   . VAL   B 1 165 ? 36.823 -36.172 -11.897 1.00 19.28 ?  165 VAL   B HA   1 
ATOM   6503 H HB   . VAL   B 1 165 ? 39.043 -37.617 -12.888 1.00 20.32 ?  165 VAL   B HB   1 
ATOM   6504 H HG11 . VAL   B 1 165 ? 38.382 -36.690 -15.013 1.00 21.81 ?  165 VAL   B HG11 1 
ATOM   6505 H HG12 . VAL   B 1 165 ? 37.525 -37.919 -14.495 1.00 21.81 ?  165 VAL   B HG12 1 
ATOM   6506 H HG13 . VAL   B 1 165 ? 36.964 -36.440 -14.345 1.00 21.81 ?  165 VAL   B HG13 1 
ATOM   6507 H HG21 . VAL   B 1 165 ? 39.844 -35.544 -13.598 1.00 20.36 ?  165 VAL   B HG21 1 
ATOM   6508 H HG22 . VAL   B 1 165 ? 38.597 -34.840 -12.911 1.00 20.36 ?  165 VAL   B HG22 1 
ATOM   6509 H HG23 . VAL   B 1 165 ? 39.682 -35.581 -12.018 1.00 20.36 ?  165 VAL   B HG23 1 
ATOM   6510 N N    . SER   B 1 166 ? 36.957 -39.366 -11.741 1.00 18.64 ?  166 SER   B N    1 
ATOM   6511 C CA   . SER   B 1 166 ? 36.201 -40.578 -12.017 1.00 19.66 ?  166 SER   B CA   1 
ATOM   6512 C C    . SER   B 1 166 ? 34.948 -40.669 -11.160 1.00 19.91 ?  166 SER   B C    1 
ATOM   6513 O O    . SER   B 1 166 ? 33.976 -41.297 -11.578 1.00 21.30 ?  166 SER   B O    1 
ATOM   6514 C CB   . SER   B 1 166 ? 37.074 -41.830 -11.860 1.00 20.68 ?  166 SER   B CB   1 
ATOM   6515 O OG   . SER   B 1 166 ? 37.442 -42.045 -10.510 1.00 20.56 ?  166 SER   B OG   1 
ATOM   6516 H H    . SER   B 1 166 ? 37.733 -39.500 -11.389 1.00 22.36 ?  166 SER   B H    1 
ATOM   6517 H HA   . SER   B 1 166 ? 35.913 -40.554 -12.942 1.00 23.58 ?  166 SER   B HA   1 
ATOM   6518 H HB2  . SER   B 1 166 ? 36.575 -42.603 -12.173 1.00 24.80 ?  166 SER   B HB2  1 
ATOM   6519 H HB3  . SER   B 1 166 ? 37.876 -41.724 -12.401 1.00 24.80 ?  166 SER   B HB3  1 
ATOM   6520 H HG   . SER   B 1 166 ? 37.898 -41.394 -10.234 1.00 24.66 ?  166 SER   B HG   1 
ATOM   6521 N N    . SER   B 1 167 ? 34.931 -40.053 -9.978  1.00 18.52 ?  167 SER   B N    1 
ATOM   6522 C CA   . SER   B 1 167 ? 33.772 -40.116 -9.095  1.00 17.94 ?  167 SER   B CA   1 
ATOM   6523 C C    . SER   B 1 167 ? 32.850 -38.903 -9.201  1.00 18.01 ?  167 SER   B C    1 
ATOM   6524 O O    . SER   B 1 167 ? 31.772 -38.907 -8.595  1.00 18.16 ?  167 SER   B O    1 
ATOM   6525 C CB   . SER   B 1 167 ? 34.208 -40.298 -7.634  1.00 17.72 ?  167 SER   B CB   1 
ATOM   6526 O OG   . SER   B 1 167 ? 34.885 -39.145 -7.156  1.00 17.68 ?  167 SER   B OG   1 
ATOM   6527 H H    . SER   B 1 167 ? 35.584 -39.594 -9.667  1.00 22.22 ?  167 SER   B H    1 
ATOM   6528 H HA   . SER   B 1 167 ? 33.250 -40.898 -9.337  1.00 21.52 ?  167 SER   B HA   1 
ATOM   6529 H HB2  . SER   B 1 167 ? 33.419 -40.454 -7.090  1.00 21.25 ?  167 SER   B HB2  1 
ATOM   6530 H HB3  . SER   B 1 167 ? 34.801 -41.067 -7.578  1.00 21.25 ?  167 SER   B HB3  1 
ATOM   6531 H HG   . SER   B 1 167 ? 35.573 -39.010 -7.620  1.00 21.20 ?  167 SER   B HG   1 
ATOM   6532 N N    . PHE   B 1 168 ? 33.227 -37.870 -9.956  1.00 17.61 ?  168 PHE   B N    1 
ATOM   6533 C CA   . PHE   B 1 168 ? 32.397 -36.666 -10.015 1.00 17.09 ?  168 PHE   B CA   1 
ATOM   6534 C C    . PHE   B 1 168 ? 31.077 -36.922 -10.736 1.00 15.07 ?  168 PHE   B C    1 
ATOM   6535 O O    . PHE   B 1 168 ? 30.039 -36.327 -10.389 1.00 15.60 ?  168 PHE   B O    1 
ATOM   6536 C CB   . PHE   B 1 168 ? 33.150 -35.535 -10.707 1.00 17.53 ?  168 PHE   B CB   1 
ATOM   6537 C CG   . PHE   B 1 168 ? 32.349 -34.283 -10.823 1.00 17.64 ?  168 PHE   B CG   1 
ATOM   6538 C CD1  . PHE   B 1 168 ? 32.036 -33.548 -9.686  1.00 18.88 ?  168 PHE   B CD1  1 
ATOM   6539 C CD2  . PHE   B 1 168 ? 31.891 -33.843 -12.048 1.00 17.33 ?  168 PHE   B CD2  1 
ATOM   6540 C CE1  . PHE   B 1 168 ? 31.282 -32.395 -9.769  1.00 19.41 ?  168 PHE   B CE1  1 
ATOM   6541 C CE2  . PHE   B 1 168 ? 31.147 -32.676 -12.144 1.00 18.30 ?  168 PHE   B CE2  1 
ATOM   6542 C CZ   . PHE   B 1 168 ? 30.835 -31.954 -11.000 1.00 18.69 ?  168 PHE   B CZ   1 
ATOM   6543 H H    . PHE   B 1 168 ? 33.946 -37.838 -10.430 1.00 21.13 ?  168 PHE   B H    1 
ATOM   6544 H HA   . PHE   B 1 168 ? 32.190 -36.383 -9.114  1.00 20.50 ?  168 PHE   B HA   1 
ATOM   6545 H HB2  . PHE   B 1 168 ? 33.947 -35.330 -10.194 1.00 21.03 ?  168 PHE   B HB2  1 
ATOM   6546 H HB3  . PHE   B 1 168 ? 33.392 -35.814 -11.601 1.00 21.03 ?  168 PHE   B HB3  1 
ATOM   6547 H HD1  . PHE   B 1 168 ? 32.331 -33.848 -8.856  1.00 22.65 ?  168 PHE   B HD1  1 
ATOM   6548 H HD2  . PHE   B 1 168 ? 32.095 -34.319 -12.816 1.00 20.79 ?  168 PHE   B HD2  1 
ATOM   6549 H HE1  . PHE   B 1 168 ? 31.078 -31.916 -8.998  1.00 23.28 ?  168 PHE   B HE1  1 
ATOM   6550 H HE2  . PHE   B 1 168 ? 30.839 -32.383 -12.975 1.00 21.95 ?  168 PHE   B HE2  1 
ATOM   6551 H HZ   . PHE   B 1 168 ? 30.326 -31.175 -11.064 1.00 22.42 ?  168 PHE   B HZ   1 
ATOM   6552 N N    . LEU   B 1 169 ? 31.102 -37.805 -11.731 1.00 15.49 ?  169 LEU   B N    1 
ATOM   6553 C CA   . LEU   B 1 169 ? 29.923 -38.111 -12.526 1.00 17.68 ?  169 LEU   B CA   1 
ATOM   6554 C C    . LEU   B 1 169 ? 29.925 -39.548 -13.031 1.00 20.25 ?  169 LEU   B C    1 
ATOM   6555 O O    . LEU   B 1 169 ? 29.010 -39.973 -13.740 1.00 22.56 ?  169 LEU   B O    1 
ATOM   6556 C CB   . LEU   B 1 169 ? 29.840 -37.157 -13.717 1.00 19.55 ?  169 LEU   B CB   1 
ATOM   6557 C CG   . LEU   B 1 169 ? 28.570 -36.312 -13.810 1.00 22.63 ?  169 LEU   B CG   1 
ATOM   6558 C CD1  . LEU   B 1 169 ? 28.532 -35.591 -15.142 1.00 23.71 ?  169 LEU   B CD1  1 
ATOM   6559 C CD2  . LEU   B 1 169 ? 27.328 -37.163 -13.619 1.00 22.99 ?  169 LEU   B CD2  1 
ATOM   6560 O OXT  . LEU   B 1 169 ? 30.848 -40.307 -12.751 1.00 21.08 -1 169 LEU   B OXT  1 
ATOM   6561 H H    . LEU   B 1 169 ? 31.804 -38.245 -11.975 1.00 18.58 ?  169 LEU   B H    1 
ATOM   6562 H HA   . LEU   B 1 169 ? 29.137 -37.985 -11.976 1.00 21.21 ?  169 LEU   B HA   1 
ATOM   6563 H HB2  . LEU   B 1 169 ? 30.590 -36.542 -13.673 1.00 23.46 ?  169 LEU   B HB2  1 
ATOM   6564 H HB3  . LEU   B 1 169 ? 29.897 -37.674 -14.536 1.00 23.46 ?  169 LEU   B HB3  1 
ATOM   6565 H HG   . LEU   B 1 169 ? 28.585 -35.640 -13.109 1.00 27.14 ?  169 LEU   B HG   1 
ATOM   6566 H HD11 . LEU   B 1 169 ? 27.733 -35.043 -15.181 1.00 28.45 ?  169 LEU   B HD11 1 
ATOM   6567 H HD12 . LEU   B 1 169 ? 29.321 -35.034 -15.221 1.00 28.45 ?  169 LEU   B HD12 1 
ATOM   6568 H HD13 . LEU   B 1 169 ? 28.518 -36.249 -15.854 1.00 28.45 ?  169 LEU   B HD13 1 
ATOM   6569 H HD21 . LEU   B 1 169 ? 26.570 -36.714 -14.020 1.00 27.58 ?  169 LEU   B HD21 1 
ATOM   6570 H HD22 . LEU   B 1 169 ? 27.468 -38.025 -14.045 1.00 27.58 ?  169 LEU   B HD22 1 
ATOM   6571 H HD23 . LEU   B 1 169 ? 27.176 -37.287 -12.670 1.00 27.58 ?  169 LEU   B HD23 1 
HETATM 6572 S S    B DMS   C 2 .   ? 12.622 5.348   6.280   0.12 20.48 ?  401 DMS   A S    1 
HETATM 6573 O O    B DMS   C 2 .   ? 13.858 6.213   6.322   0.12 20.41 ?  401 DMS   A O    1 
HETATM 6574 C C1   B DMS   C 2 .   ? 12.192 5.132   4.527   0.12 20.53 ?  401 DMS   A C1   1 
HETATM 6575 C C2   B DMS   C 2 .   ? 11.237 6.374   6.845   0.12 20.57 ?  401 DMS   A C2   1 
HETATM 6576 H H11  B DMS   C 2 .   ? 11.625 4.266   4.483   0.12 24.63 ?  401 DMS   A H11  1 
HETATM 6577 H H12  B DMS   C 2 .   ? 13.078 5.066   3.988   0.12 24.63 ?  401 DMS   A H12  1 
HETATM 6578 H H13  B DMS   C 2 .   ? 11.650 5.982   4.301   0.12 24.63 ?  401 DMS   A H13  1 
HETATM 6579 H H21  B DMS   C 2 .   ? 11.489 7.339   6.587   0.12 24.67 ?  401 DMS   A H21  1 
HETATM 6580 H H22  B DMS   C 2 .   ? 11.147 6.240   7.879   0.12 24.67 ?  401 DMS   A H22  1 
HETATM 6581 H H23  B DMS   C 2 .   ? 10.434 6.016   6.317   0.12 24.67 ?  401 DMS   A H23  1 
HETATM 6582 O O1   B A1A77 D 3 .   ? 10.830 1.073   2.867   0.06 15.16 ?  402 A1A77 A O1   1 
HETATM 6583 C C1   B A1A77 D 3 .   ? 14.332 -2.297  -0.502  0.06 14.84 ?  402 A1A77 A C1   1 
HETATM 6584 C C2   B A1A77 D 3 .   ? 14.782 -0.014  0.187   0.06 14.87 ?  402 A1A77 A C2   1 
HETATM 6585 C C3   B A1A77 D 3 .   ? 14.761 0.978   1.372   0.06 14.70 ?  402 A1A77 A C3   1 
HETATM 6586 C C4   B A1A77 D 3 .   ? 14.349 0.885   3.789   0.06 14.03 ?  402 A1A77 A C4   1 
HETATM 6587 C C5   B A1A77 D 3 .   ? 14.716 0.055   5.924   0.06 13.85 ?  402 A1A77 A C5   1 
HETATM 6588 C C6   B A1A77 D 3 .   ? 15.325 2.178   5.551   0.06 13.32 ?  402 A1A77 A C6   1 
HETATM 6589 C C7   B A1A77 D 3 .   ? 14.893 2.130   4.201   0.06 13.50 ?  402 A1A77 A C7   1 
HETATM 6590 C C8   B A1A77 D 3 .   ? 15.160 3.418   3.623   0.06 13.32 ?  402 A1A77 A C8   1 
HETATM 6591 C C10  B A1A77 D 3 .   ? 12.761 -0.275  2.353   0.06 14.90 ?  402 A1A77 A C10  1 
HETATM 6592 C C11  B A1A77 D 3 .   ? 11.490 0.405   1.814   0.06 15.06 ?  402 A1A77 A C11  1 
HETATM 6593 C C12  B A1A77 D 3 .   ? 13.234 -1.482  1.516   0.06 15.01 ?  402 A1A77 A C12  1 
HETATM 6594 C C9   B A1A77 D 3 .   ? 15.723 4.193   4.608   0.06 13.08 ?  402 A1A77 A C9   1 
HETATM 6595 N N1   B A1A77 D 3 .   ? 13.868 0.672   2.490   0.06 14.56 ?  402 A1A77 A N1   1 
HETATM 6596 N N2   B A1A77 D 3 .   ? 14.277 -0.134  4.683   0.06 14.01 ?  402 A1A77 A N2   1 
HETATM 6597 N N3   B A1A77 D 3 .   ? 15.253 1.159   6.439   0.06 13.58 ?  402 A1A77 A N3   1 
HETATM 6598 N N4   B A1A77 D 3 .   ? 15.822 3.444   5.767   0.06 13.04 ?  402 A1A77 A N4   1 
HETATM 6599 N N5   B A1A77 D 3 .   ? 13.777 -1.112  0.189   0.06 14.90 ?  402 A1A77 A N5   1 
HETATM 6600 H H15  B A1A77 D 3 .   ? 11.279 1.887   3.036   0.06 18.18 ?  402 A1A77 A H15  1 
HETATM 6601 H H2   B A1A77 D 3 .   ? 14.552 -2.070  -1.544  0.06 17.80 ?  402 A1A77 A H2   1 
HETATM 6602 H H3   B A1A77 D 3 .   ? 15.259 -2.622  -0.023  0.06 17.80 ?  402 A1A77 A H3   1 
HETATM 6603 H H4   B A1A77 D 3 .   ? 13.633 -3.132  -0.469  0.06 17.80 ?  402 A1A77 A H4   1 
HETATM 6604 H H5   B A1A77 D 3 .   ? 15.775 -0.450  0.101   0.06 17.84 ?  402 A1A77 A H5   1 
HETATM 6605 H H6   B A1A77 D 3 .   ? 14.647 0.561   -0.731  0.06 17.84 ?  402 A1A77 A H6   1 
HETATM 6606 H H7   B A1A77 D 3 .   ? 15.780 1.077   1.755   0.06 17.63 ?  402 A1A77 A H7   1 
HETATM 6607 H H8   B A1A77 D 3 .   ? 14.508 1.971   1.007   0.06 17.63 ?  402 A1A77 A H8   1 
HETATM 6608 H H9   B A1A77 D 3 .   ? 14.628 -0.790  6.594   0.06 16.61 ?  402 A1A77 A H9   1 
HETATM 6609 H H10  B A1A77 D 3 .   ? 14.944 3.710   2.609   0.06 15.98 ?  402 A1A77 A H10  1 
HETATM 6610 H H1   B A1A77 D 3 .   ? 12.492 -0.671  3.333   0.06 17.87 ?  402 A1A77 A H1   1 
HETATM 6611 H H14  B A1A77 D 3 .   ? 10.793 -0.338  1.443   0.06 18.06 ?  402 A1A77 A H14  1 
HETATM 6612 H H13  B A1A77 D 3 .   ? 11.698 1.090   1.000   0.06 18.06 ?  402 A1A77 A H13  1 
HETATM 6613 H H17  B A1A77 D 3 .   ? 14.029 -1.988  2.036   0.06 18.00 ?  402 A1A77 A H17  1 
HETATM 6614 H H16  B A1A77 D 3 .   ? 12.445 -2.226  1.427   0.06 18.00 ?  402 A1A77 A H16  1 
HETATM 6615 H H11  B A1A77 D 3 .   ? 16.064 5.217   4.579   0.06 15.68 ?  402 A1A77 A H11  1 
HETATM 6616 H H12  B A1A77 D 3 .   ? 16.209 3.799   6.632   0.06 15.64 ?  402 A1A77 A H12  1 
HETATM 6617 H H18  B A1A77 D 3 .   ? 12.994 -0.794  -0.359  0.06 17.87 ?  402 A1A77 A H18  1 
HETATM 6618 O O1   C A1A77 E 3 .   ? 10.826 1.332   3.316   0.06 15.67 ?  403 A1A77 A O1   1 
HETATM 6619 C C1   C A1A77 E 3 .   ? 13.582 -2.106  -0.737  0.06 14.93 ?  403 A1A77 A C1   1 
HETATM 6620 C C2   C A1A77 E 3 .   ? 14.538 -0.052  0.207   0.06 15.02 ?  403 A1A77 A C2   1 
HETATM 6621 C C3   C A1A77 E 3 .   ? 14.570 0.961   1.366   0.06 14.86 ?  403 A1A77 A C3   1 
HETATM 6622 C C4   C A1A77 E 3 .   ? 14.343 0.750   3.840   0.06 14.05 ?  403 A1A77 A C4   1 
HETATM 6623 C C5   C A1A77 E 3 .   ? 14.696 0.007   6.014   0.06 13.80 ?  403 A1A77 A C5   1 
HETATM 6624 C C6   C A1A77 E 3 .   ? 15.308 2.106   5.574   0.06 13.28 ?  403 A1A77 A C6   1 
HETATM 6625 C C7   C A1A77 E 3 .   ? 14.886 2.011   4.217   0.06 13.48 ?  403 A1A77 A C7   1 
HETATM 6626 C C8   C A1A77 E 3 .   ? 15.156 3.281   3.591   0.06 13.26 ?  403 A1A77 A C8   1 
HETATM 6627 C C10  C A1A77 E 3 .   ? 12.532 -0.098  2.388   0.06 15.09 ?  403 A1A77 A C10  1 
HETATM 6628 C C11  C A1A77 E 3 .   ? 11.471 0.986   2.109   0.06 15.38 ?  403 A1A77 A C11  1 
HETATM 6629 C C12  C A1A77 E 3 .   ? 12.549 -1.209  1.308   0.06 15.13 ?  403 A1A77 A C12  1 
HETATM 6630 C C9   C A1A77 E 3 .   ? 15.714 4.091   4.549   0.06 13.02 ?  403 A1A77 A C9   1 
HETATM 6631 N N1   C A1A77 E 3 .   ? 13.864 0.483   2.545   0.06 14.68 ?  403 A1A77 A N1   1 
HETATM 6632 N N2   C A1A77 E 3 .   ? 14.260 -0.230  4.773   0.06 13.95 ?  403 A1A77 A N2   1 
HETATM 6633 N N3   C A1A77 E 3 .   ? 15.232 1.123   6.514   0.06 13.53 ?  403 A1A77 A N3   1 
HETATM 6634 N N4   C A1A77 E 3 .   ? 15.803 3.383   5.737   0.06 12.99 ?  403 A1A77 A N4   1 
HETATM 6635 N N5   C A1A77 E 3 .   ? 13.799 -1.314  0.495   0.06 15.02 ?  403 A1A77 A N5   1 
HETATM 6636 H H15  C A1A77 E 3 .   ? 9.997  1.738   3.109   0.06 18.80 ?  403 A1A77 A H15  1 
HETATM 6637 H H2   C A1A77 E 3 .   ? 14.532 -2.441  -1.158  0.06 17.91 ?  403 A1A77 A H2   1 
HETATM 6638 H H3   C A1A77 E 3 .   ? 13.063 -1.516  -1.491  0.06 17.91 ?  403 A1A77 A H3   1 
HETATM 6639 H H4   C A1A77 E 3 .   ? 12.974 -2.986  -0.526  0.06 17.91 ?  403 A1A77 A H4   1 
HETATM 6640 H H5   C A1A77 E 3 .   ? 14.113 0.416   -0.684  0.06 18.02 ?  403 A1A77 A H5   1 
HETATM 6641 H H6   C A1A77 E 3 .   ? 15.562 -0.311  -0.055  0.06 18.02 ?  403 A1A77 A H6   1 
HETATM 6642 H H7   C A1A77 E 3 .   ? 14.134 1.900   1.029   0.06 17.82 ?  403 A1A77 A H7   1 
HETATM 6643 H H8   C A1A77 E 3 .   ? 15.602 1.187   1.636   0.06 17.82 ?  403 A1A77 A H8   1 
HETATM 6644 H H9   C A1A77 E 3 .   ? 14.603 -0.816  6.705   0.06 16.54 ?  403 A1A77 A H9   1 
HETATM 6645 H H10  C A1A77 E 3 .   ? 14.953 3.541   2.562   0.06 15.90 ?  403 A1A77 A H10  1 
HETATM 6646 H H1   C A1A77 E 3 .   ? 12.252 -0.588  3.325   0.06 18.10 ?  403 A1A77 A H1   1 
HETATM 6647 H H14  C A1A77 E 3 .   ? 10.705 0.607   1.433   0.06 18.45 ?  403 A1A77 A H14  1 
HETATM 6648 H H13  C A1A77 E 3 .   ? 11.895 1.874   1.645   0.06 18.45 ?  403 A1A77 A H13  1 
HETATM 6649 H H17  C A1A77 E 3 .   ? 12.413 -2.164  1.809   0.06 18.14 ?  403 A1A77 A H17  1 
HETATM 6650 H H16  C A1A77 E 3 .   ? 11.691 -1.112  0.641   0.06 18.14 ?  403 A1A77 A H16  1 
HETATM 6651 H H11  C A1A77 E 3 .   ? 16.055 5.116   4.484   0.06 15.62 ?  403 A1A77 A H11  1 
HETATM 6652 H H12  C A1A77 E 3 .   ? 16.183 3.772   6.587   0.06 15.57 ?  403 A1A77 A H12  1 
HETATM 6653 H H18  C A1A77 E 3 .   ? 14.428 -1.860  1.063   0.06 18.01 ?  403 A1A77 A H18  1 
HETATM 6654 O O    . HOH   F 4 .   ? 7.985  -12.615 -0.801  1.00 21.36 ?  501 HOH   A O    1 
HETATM 6655 O O    . HOH   F 4 .   ? 26.792 11.377  1.695   1.00 15.51 ?  502 HOH   A O    1 
HETATM 6656 O O    . HOH   F 4 .   ? 4.803  3.881   0.684   1.00 27.53 ?  503 HOH   A O    1 
HETATM 6657 O O    . HOH   F 4 .   ? 12.174 0.300   14.910  1.00 32.93 ?  504 HOH   A O    1 
HETATM 6658 O O    . HOH   F 4 .   ? 14.802 -4.745  20.573  1.00 40.42 ?  505 HOH   A O    1 
HETATM 6659 O O    . HOH   F 4 .   ? 30.877 6.227   -12.288 1.00 29.54 ?  506 HOH   A O    1 
HETATM 6660 O O    . HOH   F 4 .   ? 7.640  -6.256  -6.530  1.00 38.77 ?  507 HOH   A O    1 
HETATM 6661 O O    . HOH   F 4 .   ? 34.370 -1.885  12.490  1.00 36.87 ?  508 HOH   A O    1 
HETATM 6662 O O    . HOH   F 4 .   ? 15.207 -12.256 18.744  1.00 34.02 ?  509 HOH   A O    1 
HETATM 6663 O O    . HOH   F 4 .   ? 24.569 1.975   -7.009  1.00 18.57 ?  510 HOH   A O    1 
HETATM 6664 O O    . HOH   F 4 .   ? 6.958  -8.212  11.872  1.00 20.84 ?  511 HOH   A O    1 
HETATM 6665 O O    . HOH   F 4 .   ? 27.890 0.838   -7.144  1.00 13.35 ?  512 HOH   A O    1 
HETATM 6666 O O    . HOH   F 4 .   ? 13.284 -1.414  -6.577  1.00 18.71 ?  513 HOH   A O    1 
HETATM 6667 O O    . HOH   F 4 .   ? 28.913 0.435   -9.731  1.00 20.65 ?  514 HOH   A O    1 
HETATM 6668 O O    . HOH   F 4 .   ? 42.409 10.545  5.184   1.00 19.47 ?  515 HOH   A O    1 
HETATM 6669 O O    . HOH   F 4 .   ? 36.107 -5.098  -0.542  1.00 27.89 ?  516 HOH   A O    1 
HETATM 6670 O O    . HOH   F 4 .   ? -1.556 -5.104  7.741   1.00 40.61 ?  517 HOH   A O    1 
HETATM 6671 O O    . HOH   F 4 .   ? 8.061  -21.524 3.972   1.00 43.83 ?  518 HOH   A O    1 
HETATM 6672 O O    . HOH   F 4 .   ? 19.875 -12.505 -8.951  1.00 24.81 ?  519 HOH   A O    1 
HETATM 6673 O O    . HOH   F 4 .   ? 28.247 -6.335  19.620  1.00 41.41 ?  520 HOH   A O    1 
HETATM 6674 O O    . HOH   F 4 .   ? 30.253 -13.316 -8.555  1.00 19.67 ?  521 HOH   A O    1 
HETATM 6675 O O    . HOH   F 4 .   ? 31.002 -18.145 7.762   1.00 19.27 ?  522 HOH   A O    1 
HETATM 6676 O O    . HOH   F 4 .   ? 6.485  -5.681  11.275  1.00 20.93 ?  523 HOH   A O    1 
HETATM 6677 O O    . HOH   F 4 .   ? 33.970 -0.998  -8.899  1.00 26.34 ?  524 HOH   A O    1 
HETATM 6678 O O    . HOH   F 4 .   ? 26.487 -19.327 -1.821  1.00 13.24 ?  525 HOH   A O    1 
HETATM 6679 O O    . HOH   F 4 .   ? 14.753 -14.025 16.735  1.00 21.17 ?  526 HOH   A O    1 
HETATM 6680 O O    . HOH   F 4 .   ? 9.084  -10.168 19.360  1.00 41.12 ?  527 HOH   A O    1 
HETATM 6681 O O    . HOH   F 4 .   ? 17.168 -18.091 15.127  1.00 23.89 ?  528 HOH   A O    1 
HETATM 6682 O O    . HOH   F 4 .   ? 37.524 2.795   10.216  1.00 27.28 ?  529 HOH   A O    1 
HETATM 6683 O O    . HOH   F 4 .   ? 27.257 13.755  2.930   1.00 27.42 ?  530 HOH   A O    1 
HETATM 6684 O O    . HOH   F 4 .   ? 16.236 16.650  8.742   1.00 26.98 ?  531 HOH   A O    1 
HETATM 6685 O O    . HOH   F 4 .   ? 3.553  -9.261  10.002  1.00 34.58 ?  532 HOH   A O    1 
HETATM 6686 O O    . HOH   F 4 .   ? 11.653 -10.860 -10.073 1.00 39.85 ?  533 HOH   A O    1 
HETATM 6687 O O    . HOH   F 4 .   ? 28.315 -0.141  -13.378 1.00 33.68 ?  534 HOH   A O    1 
HETATM 6688 O O    . HOH   F 4 .   ? 14.134 -4.536  -11.837 1.00 29.53 ?  535 HOH   A O    1 
HETATM 6689 O O    . HOH   F 4 .   ? 0.754  -4.582  0.268   1.00 31.60 ?  536 HOH   A O    1 
HETATM 6690 O O    . HOH   F 4 .   ? 24.011 3.949   -4.847  1.00 22.08 ?  537 HOH   A O    1 
HETATM 6691 O O    . HOH   F 4 .   ? 22.437 5.320   19.084  1.00 42.65 ?  538 HOH   A O    1 
HETATM 6692 O O    . HOH   F 4 .   ? 18.907 -21.993 6.895   1.00 30.97 ?  539 HOH   A O    1 
HETATM 6693 O O    . HOH   F 4 .   ? 15.556 11.946  8.020   1.00 30.22 ?  540 HOH   A O    1 
HETATM 6694 O O    . HOH   F 4 .   ? 38.256 10.083  7.169   1.00 39.40 ?  541 HOH   A O    1 
HETATM 6695 O O    . HOH   F 4 .   ? 20.599 -19.680 -5.091  1.00 27.85 ?  542 HOH   A O    1 
HETATM 6696 O O    . HOH   F 4 .   ? 38.553 4.960   6.947   1.00 15.11 ?  543 HOH   A O    1 
HETATM 6697 O O    A HOH   F 4 .   ? 17.482 -1.726  0.482   0.88 17.87 ?  544 HOH   A O    1 
HETATM 6698 O O    . HOH   F 4 .   ? 18.680 -19.396 13.563  1.00 33.99 ?  545 HOH   A O    1 
HETATM 6699 O O    . HOH   F 4 .   ? 17.170 -17.867 -5.035  1.00 26.28 ?  546 HOH   A O    1 
HETATM 6700 O O    . HOH   F 4 .   ? 39.723 -1.011  -5.203  1.00 19.71 ?  547 HOH   A O    1 
HETATM 6701 O O    . HOH   F 4 .   ? 9.864  -21.373 5.734   1.00 17.87 ?  548 HOH   A O    1 
HETATM 6702 O O    . HOH   F 4 .   ? 15.109 3.844   17.837  1.00 37.42 ?  549 HOH   A O    1 
HETATM 6703 O O    . HOH   F 4 .   ? 42.547 4.285   5.352   1.00 31.13 ?  550 HOH   A O    1 
HETATM 6704 O O    . HOH   F 4 .   ? 22.273 -19.274 11.378  1.00 33.19 ?  551 HOH   A O    1 
HETATM 6705 O O    . HOH   F 4 .   ? 44.289 7.084   6.481   1.00 26.38 ?  552 HOH   A O    1 
HETATM 6706 O O    . HOH   F 4 .   ? 21.219 -2.384  -2.096  1.00 15.26 ?  553 HOH   A O    1 
HETATM 6707 O O    A HOH   F 4 .   ? 14.267 0.548   6.847   0.88 22.16 ?  554 HOH   A O    1 
HETATM 6708 O O    . HOH   F 4 .   ? 24.000 -2.105  -2.072  1.00 10.12 ?  555 HOH   A O    1 
HETATM 6709 O O    A HOH   F 4 .   ? -0.640 -8.524  2.452   0.88 38.83 ?  556 HOH   A O    1 
HETATM 6710 O O    . HOH   F 4 .   ? 27.528 -6.180  -14.040 1.00 37.41 ?  557 HOH   A O    1 
HETATM 6711 O O    . HOH   F 4 .   ? 35.775 -12.680 6.828   1.00 15.09 ?  558 HOH   A O    1 
HETATM 6712 O O    A HOH   F 4 .   ? 14.626 -3.673  3.137   0.88 17.61 ?  559 HOH   A O    1 
HETATM 6713 O O    . HOH   F 4 .   ? 31.799 -9.337  -6.663  1.00 20.94 ?  560 HOH   A O    1 
HETATM 6714 O O    . HOH   F 4 .   ? 33.656 -7.171  4.275   1.00 15.80 ?  561 HOH   A O    1 
HETATM 6715 O O    . HOH   F 4 .   ? 31.068 -13.937 -2.496  1.00 12.99 ?  562 HOH   A O    1 
HETATM 6716 O O    . HOH   F 4 .   ? 31.678 8.205   14.856  1.00 22.53 ?  563 HOH   A O    1 
HETATM 6717 O O    . HOH   F 4 .   ? 22.744 12.503  1.648   1.00 14.13 ?  564 HOH   A O    1 
HETATM 6718 O O    . HOH   F 4 .   ? 37.356 11.926  4.940   1.00 31.61 ?  565 HOH   A O    1 
HETATM 6719 O O    . HOH   F 4 .   ? 43.873 8.439   -3.122  1.00 25.90 ?  566 HOH   A O    1 
HETATM 6720 O O    . HOH   F 4 .   ? 37.203 -2.822  9.733   1.00 41.21 ?  567 HOH   A O    1 
HETATM 6721 O O    . HOH   F 4 .   ? 27.525 -10.647 14.032  1.00 15.86 ?  568 HOH   A O    1 
HETATM 6722 O O    . HOH   F 4 .   ? 21.878 -21.913 8.394   1.00 26.81 ?  569 HOH   A O    1 
HETATM 6723 O O    . HOH   F 4 .   ? 16.520 -22.049 0.975   1.00 26.82 ?  570 HOH   A O    1 
HETATM 6724 O O    . HOH   F 4 .   ? 30.806 3.071   8.273   1.00 11.43 ?  571 HOH   A O    1 
HETATM 6725 O O    . HOH   F 4 .   ? 14.348 -21.249 -4.253  1.00 29.63 ?  572 HOH   A O    1 
HETATM 6726 O O    . HOH   F 4 .   ? 18.559 9.422   9.034   1.00 19.97 ?  573 HOH   A O    1 
HETATM 6727 O O    . HOH   F 4 .   ? 13.532 -15.241 -7.457  1.00 26.94 ?  574 HOH   A O    1 
HETATM 6728 O O    . HOH   F 4 .   ? 21.340 3.119   -0.312  1.00 12.75 ?  575 HOH   A O    1 
HETATM 6729 O O    . HOH   F 4 .   ? 17.027 -19.309 4.903   1.00 14.03 ?  576 HOH   A O    1 
HETATM 6730 O O    . HOH   F 4 .   ? 24.330 -7.833  14.460  1.00 16.27 ?  577 HOH   A O    1 
HETATM 6731 O O    . HOH   F 4 .   ? 28.585 -10.590 -14.067 1.00 40.32 ?  578 HOH   A O    1 
HETATM 6732 O O    . HOH   F 4 .   ? 24.386 3.576   -1.789  1.00 13.98 ?  579 HOH   A O    1 
HETATM 6733 O O    . HOH   F 4 .   ? 18.936 -0.675  -1.632  1.00 13.06 ?  580 HOH   A O    1 
HETATM 6734 O O    A HOH   F 4 .   ? -0.487 -3.120  3.158   0.88 35.33 ?  581 HOH   A O    1 
HETATM 6735 O O    . HOH   F 4 .   ? 31.740 -7.273  -9.857  1.00 21.05 ?  582 HOH   A O    1 
HETATM 6736 O O    . HOH   F 4 .   ? 9.284  -12.201 17.396  1.00 48.42 ?  583 HOH   A O    1 
HETATM 6737 O O    . HOH   F 4 .   ? 43.330 7.846   2.684   1.00 24.83 ?  584 HOH   A O    1 
HETATM 6738 O O    . HOH   F 4 .   ? 22.671 -12.005 21.863  1.00 39.97 ?  585 HOH   A O    1 
HETATM 6739 O O    . HOH   F 4 .   ? 24.763 -17.563 12.692  1.00 22.55 ?  586 HOH   A O    1 
HETATM 6740 O O    . HOH   F 4 .   ? 13.995 -5.002  17.566  1.00 24.41 ?  587 HOH   A O    1 
HETATM 6741 O O    . HOH   F 4 .   ? 21.224 10.321  15.036  1.00 33.49 ?  588 HOH   A O    1 
HETATM 6742 O O    A HOH   F 4 .   ? 20.071 4.546   -7.498  0.88 18.01 ?  589 HOH   A O    1 
HETATM 6743 O O    . HOH   F 4 .   ? 10.432 -22.158 -1.220  1.00 46.07 ?  590 HOH   A O    1 
HETATM 6744 O O    . HOH   F 4 .   ? 14.484 -0.495  -12.048 1.00 28.04 ?  591 HOH   A O    1 
HETATM 6745 O O    . HOH   F 4 .   ? 25.695 -0.786  -7.325  1.00 15.04 ?  592 HOH   A O    1 
HETATM 6746 O O    . HOH   F 4 .   ? 30.716 1.869   16.708  1.00 19.70 ?  593 HOH   A O    1 
HETATM 6747 O O    . HOH   F 4 .   ? 27.367 2.312   18.728  1.00 30.33 ?  594 HOH   A O    1 
HETATM 6748 O O    B HOH   F 4 .   ? 15.162 -2.866  3.485   0.12 13.50 ?  595 HOH   A O    1 
HETATM 6749 O O    . HOH   F 4 .   ? 23.447 11.353  4.130   1.00 11.56 ?  596 HOH   A O    1 
HETATM 6750 O O    . HOH   F 4 .   ? 37.534 -2.012  5.751   1.00 25.93 ?  597 HOH   A O    1 
HETATM 6751 O O    . HOH   F 4 .   ? 14.884 8.537   5.042   1.00 39.06 ?  598 HOH   A O    1 
HETATM 6752 O O    . HOH   F 4 .   ? 32.776 -9.263  5.906   1.00 19.27 ?  599 HOH   A O    1 
HETATM 6753 O O    . HOH   F 4 .   ? 21.792 -13.807 -8.108  1.00 43.23 ?  600 HOH   A O    1 
HETATM 6754 O O    . HOH   F 4 .   ? 20.573 -20.031 2.765   1.00 16.45 ?  601 HOH   A O    1 
HETATM 6755 O O    . HOH   F 4 .   ? 26.921 4.143   -0.626  1.00 12.20 ?  602 HOH   A O    1 
HETATM 6756 O O    A HOH   F 4 .   ? 15.792 -0.967  5.313   0.88 26.38 ?  603 HOH   A O    1 
HETATM 6757 O O    . HOH   F 4 .   ? 15.830 2.118   24.825  1.00 51.29 ?  604 HOH   A O    1 
HETATM 6758 O O    . HOH   F 4 .   ? 14.106 -23.097 7.438   1.00 17.07 ?  605 HOH   A O    1 
HETATM 6759 O O    . HOH   F 4 .   ? 15.236 -21.612 14.220  1.00 16.49 ?  606 HOH   A O    1 
HETATM 6760 O O    . HOH   F 4 .   ? 14.418 -24.734 11.602  1.00 33.02 ?  607 HOH   A O    1 
HETATM 6761 O O    . HOH   F 4 .   ? 38.064 -1.347  -1.967  1.00 18.25 ?  608 HOH   A O    1 
HETATM 6762 O O    . HOH   F 4 .   ? 41.587 1.506   4.921   1.00 36.82 ?  609 HOH   A O    1 
HETATM 6763 O O    . HOH   F 4 .   ? 30.097 -10.149 12.999  1.00 20.55 ?  610 HOH   A O    1 
HETATM 6764 O O    . HOH   F 4 .   ? 16.003 6.971   3.044   1.00 15.30 ?  611 HOH   A O    1 
HETATM 6765 O O    . HOH   F 4 .   ? 23.927 -20.289 -1.380  1.00 14.88 ?  612 HOH   A O    1 
HETATM 6766 O O    . HOH   F 4 .   ? 11.032 1.631   12.838  1.00 24.19 ?  613 HOH   A O    1 
HETATM 6767 O O    . HOH   F 4 .   ? 40.899 -8.254  -6.719  1.00 35.67 ?  614 HOH   A O    1 
HETATM 6768 O O    . HOH   F 4 .   ? 6.704  -3.448  13.009  1.00 30.81 ?  615 HOH   A O    1 
HETATM 6769 O O    . HOH   F 4 .   ? 30.367 -12.953 13.488  1.00 18.56 ?  616 HOH   A O    1 
HETATM 6770 O O    A HOH   F 4 .   ? 23.943 -15.711 -9.300  0.88 27.96 ?  617 HOH   A O    1 
HETATM 6771 O O    . HOH   F 4 .   ? 27.115 -3.289  19.342  1.00 34.77 ?  618 HOH   A O    1 
HETATM 6772 O O    . HOH   F 4 .   ? 35.070 -5.219  -3.104  1.00 17.52 ?  619 HOH   A O    1 
HETATM 6773 O O    . HOH   F 4 .   ? 44.934 -0.624  2.952   1.00 40.15 ?  620 HOH   A O    1 
HETATM 6774 O O    . HOH   F 4 .   ? 36.731 -4.955  5.367   1.00 22.84 ?  621 HOH   A O    1 
HETATM 6775 O O    . HOH   F 4 .   ? 32.567 -10.651 3.159   1.00 29.70 ?  622 HOH   A O    1 
HETATM 6776 O O    . HOH   F 4 .   ? 32.664 -4.316  -9.908  1.00 26.85 ?  623 HOH   A O    1 
HETATM 6777 O O    A HOH   F 4 .   ? 11.054 -0.399  1.983   0.88 24.24 ?  624 HOH   A O    1 
HETATM 6778 O O    . HOH   F 4 .   ? 11.695 -10.777 17.123  1.00 24.07 ?  625 HOH   A O    1 
HETATM 6779 O O    A HOH   F 4 .   ? 18.539 -2.446  -16.301 0.88 39.44 ?  626 HOH   A O    1 
HETATM 6780 O O    . HOH   F 4 .   ? 15.154 -8.100  -9.631  1.00 21.62 ?  627 HOH   A O    1 
HETATM 6781 O O    . HOH   F 4 .   ? 5.140  2.661   5.290   1.00 31.66 ?  628 HOH   A O    1 
HETATM 6782 O O    . HOH   F 4 .   ? 16.206 -14.195 20.305  1.00 44.95 ?  629 HOH   A O    1 
HETATM 6783 O O    . HOH   F 4 .   ? 22.684 8.106   18.398  1.00 40.12 ?  630 HOH   A O    1 
HETATM 6784 O O    . HOH   F 4 .   ? 10.402 -13.740 -1.624  1.00 17.41 ?  631 HOH   A O    1 
HETATM 6785 O O    . HOH   F 4 .   ? 21.333 -9.288  21.325  1.00 44.39 ?  632 HOH   A O    1 
HETATM 6786 O O    . HOH   F 4 .   ? 37.714 -8.822  -3.504  1.00 23.81 ?  633 HOH   A O    1 
HETATM 6787 O O    . HOH   F 4 .   ? 19.465 -11.139 24.082  1.00 66.79 ?  634 HOH   A O    1 
HETATM 6788 O O    . HOH   F 4 .   ? 20.585 -17.808 24.817  1.00 47.40 ?  635 HOH   A O    1 
HETATM 6789 O O    A HOH   F 4 .   ? 18.845 2.024   -0.707  0.88 11.90 ?  636 HOH   A O    1 
HETATM 6790 O O    . HOH   F 4 .   ? 23.572 -8.049  17.087  1.00 20.42 ?  637 HOH   A O    1 
HETATM 6791 O O    A HOH   F 4 .   ? 16.239 2.938   -1.392  0.88 15.26 ?  638 HOH   A O    1 
HETATM 6792 O O    A HOH   F 4 .   ? 9.380  -16.340 -1.959  0.88 40.55 ?  639 HOH   A O    1 
HETATM 6793 O O    . HOH   F 4 .   ? 23.326 -20.971 1.300   1.00 16.93 ?  640 HOH   A O    1 
HETATM 6794 O O    . HOH   F 4 .   ? 18.465 4.887   -15.072 1.00 46.69 ?  641 HOH   A O    1 
HETATM 6795 O O    . HOH   F 4 .   ? 34.409 -8.077  -0.551  1.00 27.47 ?  642 HOH   A O    1 
HETATM 6796 O O    . HOH   F 4 .   ? 18.469 -16.097 16.406  1.00 34.80 ?  643 HOH   A O    1 
HETATM 6797 O O    . HOH   F 4 .   ? 21.575 -14.728 18.060  1.00 45.79 ?  644 HOH   A O    1 
HETATM 6798 O O    . HOH   F 4 .   ? 30.565 14.769  2.826   1.00 17.71 ?  645 HOH   A O    1 
HETATM 6799 O O    . HOH   F 4 .   ? 23.213 7.601   -3.177  1.00 27.97 ?  646 HOH   A O    1 
HETATM 6800 O O    . HOH   F 4 .   ? 31.328 -12.787 -0.004  1.00 18.08 ?  647 HOH   A O    1 
HETATM 6801 O O    A HOH   F 4 .   ? 14.016 -0.359  3.508   0.88 23.02 ?  648 HOH   A O    1 
HETATM 6802 O O    . HOH   F 4 .   ? 29.812 -16.045 10.618  1.00 33.25 ?  649 HOH   A O    1 
HETATM 6803 O O    B HOH   F 4 .   ? 18.266 1.933   -0.497  0.12 10.57 ?  650 HOH   A O    1 
HETATM 6804 O O    . HOH   F 4 .   ? 25.407 8.238   -4.759  1.00 23.38 ?  651 HOH   A O    1 
HETATM 6805 O O    . HOH   F 4 .   ? 27.759 7.055   -6.314  1.00 34.56 ?  652 HOH   A O    1 
HETATM 6806 O O    . HOH   F 4 .   ? 29.807 -1.976  -12.738 1.00 45.11 ?  653 HOH   A O    1 
HETATM 6807 O O    . HOH   F 4 .   ? 32.480 -15.928 10.820  1.00 35.38 ?  654 HOH   A O    1 
HETATM 6808 O O    . HOH   F 4 .   ? 19.928 -17.354 -5.082  1.00 24.11 ?  655 HOH   A O    1 
HETATM 6809 O O    . HOH   F 4 .   ? 24.847 5.620   20.776  1.00 49.68 ?  656 HOH   A O    1 
HETATM 6810 O O    . HOH   F 4 .   ? 24.583 14.500  7.908   1.00 34.62 ?  657 HOH   A O    1 
HETATM 6811 O O    . HOH   F 4 .   ? 23.204 -22.359 -3.370  1.00 35.47 ?  658 HOH   A O    1 
HETATM 6812 O O    B HOH   F 4 .   ? 15.631 2.791   -1.069  0.12 8.98  ?  659 HOH   A O    1 
HETATM 6813 O O    . HOH   F 4 .   ? 23.487 13.690  5.541   1.00 18.35 ?  660 HOH   A O    1 
HETATM 6814 O O    . HOH   F 4 .   ? 26.897 11.613  -1.266  1.00 28.23 ?  661 HOH   A O    1 
HETATM 6815 O O    . HOH   F 4 .   ? 15.738 -21.534 3.710   1.00 21.57 ?  662 HOH   A O    1 
HETATM 6816 O O    . HOH   F 4 .   ? 27.495 -11.404 16.572  1.00 35.74 ?  663 HOH   A O    1 
HETATM 6817 O O    . HOH   F 4 .   ? 18.746 10.808  11.383  1.00 31.91 ?  664 HOH   A O    1 
HETATM 6818 O O    . HOH   F 4 .   ? 12.378 1.639   17.423  1.00 39.38 ?  665 HOH   A O    1 
HETATM 6819 O O    . HOH   F 4 .   ? 21.991 5.226   -5.909  1.00 28.44 ?  666 HOH   A O    1 
HETATM 6820 O O    . HOH   F 4 .   ? 39.631 -6.998  -3.505  1.00 44.30 ?  667 HOH   A O    1 
HETATM 6821 O O    . HOH   F 4 .   ? 11.988 -13.383 16.413  1.00 44.79 ?  668 HOH   A O    1 
HETATM 6822 O O    . HOH   F 4 .   ? 25.830 10.768  -3.674  1.00 23.08 ?  669 HOH   A O    1 
HETATM 6823 O O    . HOH   F 4 .   ? 20.524 -16.141 -7.336  1.00 28.65 ?  670 HOH   A O    1 
HETATM 6824 O O    . HOH   F 4 .   ? 11.051 -15.020 -6.099  1.00 33.81 ?  671 HOH   A O    1 
HETATM 6825 O O    . HOH   F 4 .   ? 14.004 -10.315 -10.832 1.00 30.94 ?  672 HOH   A O    1 
HETATM 6826 O O    . HOH   F 4 .   ? 35.170 7.400   12.234  1.00 44.86 ?  673 HOH   A O    1 
HETATM 6827 O O    . HOH   F 4 .   ? 28.822 8.999   17.463  1.00 33.49 ?  674 HOH   A O    1 
HETATM 6828 O O    . HOH   F 4 .   ? 18.137 -16.259 -8.782  1.00 41.90 ?  675 HOH   A O    1 
HETATM 6829 O O    . HOH   F 4 .   ? 28.676 -7.878  -15.253 1.00 45.83 ?  676 HOH   A O    1 
HETATM 6830 O O    . HOH   F 4 .   ? 17.348 -18.758 19.830  1.00 46.31 ?  677 HOH   A O    1 
HETATM 6831 O O    . HOH   F 4 .   ? 23.129 11.824  -4.049  1.00 18.43 ?  678 HOH   A O    1 
HETATM 6832 O O    . HOH   F 4 .   ? 40.908 -3.974  -0.343  1.00 33.59 ?  679 HOH   A O    1 
HETATM 6833 O O    . HOH   F 4 .   ? 30.871 0.705   19.148  1.00 37.04 ?  680 HOH   A O    1 
HETATM 6834 O O    . HOH   F 4 .   ? 16.802 -20.606 16.198  1.00 26.45 ?  681 HOH   A O    1 
HETATM 6835 O O    . HOH   F 4 .   ? 28.678 -4.796  -12.224 1.00 38.87 ?  682 HOH   A O    1 
HETATM 6836 O O    . HOH   F 4 .   ? 15.695 -17.208 -6.980  1.00 32.12 ?  683 HOH   A O    1 
HETATM 6837 O O    . HOH   F 4 .   ? 30.708 5.831   -14.708 1.00 35.00 ?  684 HOH   A O    1 
HETATM 6838 O O    . HOH   F 4 .   ? 41.678 9.269   -4.104  1.00 30.09 ?  685 HOH   A O    1 
HETATM 6839 O O    . HOH   F 4 .   ? 31.457 -0.609  -10.544 1.00 25.32 ?  686 HOH   A O    1 
HETATM 6840 O O    . HOH   F 4 .   ? 44.476 10.471  -1.597  1.00 31.53 ?  687 HOH   A O    1 
HETATM 6841 O O    . HOH   F 4 .   ? 23.313 -12.895 19.332  1.00 43.27 ?  688 HOH   A O    1 
HETATM 6842 O O    . HOH   F 4 .   ? 15.949 -6.805  -11.750 1.00 42.74 ?  689 HOH   A O    1 
HETATM 6843 O O    . HOH   F 4 .   ? 18.470 -23.248 1.901   1.00 43.80 ?  690 HOH   A O    1 
HETATM 6844 O O    . HOH   F 4 .   ? 39.151 2.365   7.568   1.00 31.18 ?  691 HOH   A O    1 
HETATM 6845 O O    . HOH   F 4 .   ? 40.439 -0.244  -7.866  1.00 33.21 ?  692 HOH   A O    1 
HETATM 6846 O O    . HOH   F 4 .   ? 20.014 -22.339 4.181   1.00 27.35 ?  693 HOH   A O    1 
HETATM 6847 O O    . HOH   F 4 .   ? 14.094 -25.404 8.889   1.00 29.47 ?  694 HOH   A O    1 
HETATM 6848 O O    . HOH   F 4 .   ? 16.147 -23.381 5.708   1.00 26.52 ?  695 HOH   A O    1 
HETATM 6849 O O    . HOH   F 4 .   ? 8.159  -3.003  -5.597  1.00 39.78 ?  696 HOH   A O    1 
HETATM 6850 O O    . HOH   F 4 .   ? 30.732 -5.782  -11.836 1.00 46.69 ?  697 HOH   A O    1 
HETATM 6851 O O    . HOH   F 4 .   ? 37.395 -6.647  7.506   1.00 24.25 ?  698 HOH   A O    1 
HETATM 6852 O O    . HOH   F 4 .   ? 23.131 -23.774 1.683   1.00 29.08 ?  699 HOH   A O    1 
HETATM 6853 O O    . HOH   F 4 .   ? 39.553 -0.028  6.580   1.00 29.28 ?  700 HOH   A O    1 
HETATM 6854 O O    . HOH   F 4 .   ? 28.964 14.413  0.918   1.00 43.86 ?  701 HOH   A O    1 
HETATM 6855 O O    . HOH   F 4 .   ? 38.020 13.937  6.742   1.00 45.64 ?  702 HOH   A O    1 
HETATM 6856 O O    . HOH   F 4 .   ? 22.047 -24.054 4.453   1.00 24.84 ?  703 HOH   A O    1 
HETATM 6857 O O    . HOH   F 4 .   ? 36.458 -6.532  10.139  1.00 42.41 ?  704 HOH   A O    1 
HETATM 6858 O O    . HOH   F 4 .   ? 24.075 8.988   -7.220  1.00 33.97 ?  705 HOH   A O    1 
HETATM 6859 O O    . HOH   F 4 .   ? 17.070 -7.108  -14.450 1.00 46.85 ?  706 HOH   A O    1 
HETATM 6860 O O    . HOH   F 4 .   ? 16.444 -21.102 18.811  1.00 33.66 ?  707 HOH   A O    1 
HETATM 6861 O O    . HOH   F 4 .   ? 15.877 -12.247 27.518  1.00 41.57 ?  708 HOH   A O    1 
HETATM 6862 O O    . HOH   F 4 .   ? 14.643 -22.818 19.893  1.00 31.82 ?  709 HOH   A O    1 
HETATM 6863 O O    . HOH   G 4 .   ? 29.850 -22.405 5.467   1.00 19.46 ?  201 HOH   B O    1 
HETATM 6864 O O    . HOH   G 4 .   ? 27.818 -41.694 -15.173 1.00 34.99 ?  202 HOH   B O    1 
HETATM 6865 O O    . HOH   G 4 .   ? 48.129 -6.905  15.549  1.00 34.31 ?  203 HOH   B O    1 
HETATM 6866 O O    . HOH   G 4 .   ? 49.371 -22.655 -19.757 1.00 48.54 ?  204 HOH   B O    1 
HETATM 6867 O O    . HOH   G 4 .   ? 59.178 -18.727 6.787   1.00 35.97 ?  205 HOH   B O    1 
HETATM 6868 O O    . HOH   G 4 .   ? 47.427 -7.405  -3.969  1.00 38.76 ?  206 HOH   B O    1 
HETATM 6869 O O    . HOH   G 4 .   ? 41.832 -35.887 -17.414 1.00 29.71 ?  207 HOH   B O    1 
HETATM 6870 O O    . HOH   G 4 .   ? 27.721 -29.184 -1.885  1.00 35.74 ?  208 HOH   B O    1 
HETATM 6871 O O    . HOH   G 4 .   ? 37.959 -39.447 -0.192  1.00 42.14 ?  209 HOH   B O    1 
HETATM 6872 O O    . HOH   G 4 .   ? 50.236 -3.392  7.189   1.00 33.84 ?  210 HOH   B O    1 
HETATM 6873 O O    . HOH   G 4 .   ? 41.383 -7.736  5.479   1.00 37.58 ?  211 HOH   B O    1 
HETATM 6874 O O    . HOH   G 4 .   ? 58.188 -12.976 8.379   1.00 32.72 ?  212 HOH   B O    1 
HETATM 6875 O O    . HOH   G 4 .   ? 56.356 -19.715 7.219   1.00 32.17 ?  213 HOH   B O    1 
HETATM 6876 O O    . HOH   G 4 .   ? 29.777 -34.164 -0.430  1.00 32.14 ?  214 HOH   B O    1 
HETATM 6877 O O    . HOH   G 4 .   ? 55.359 -16.484 -14.357 1.00 34.73 ?  215 HOH   B O    1 
HETATM 6878 O O    . HOH   G 4 .   ? 54.466 -9.352  -8.793  1.00 18.20 ?  216 HOH   B O    1 
HETATM 6879 O O    . HOH   G 4 .   ? 30.206 -40.999 -8.196  1.00 15.90 ?  217 HOH   B O    1 
HETATM 6880 O O    . HOH   G 4 .   ? 57.709 -24.427 5.015   1.00 34.63 ?  218 HOH   B O    1 
HETATM 6881 O O    . HOH   G 4 .   ? 29.913 -26.314 3.981   1.00 27.20 ?  219 HOH   B O    1 
HETATM 6882 O O    . HOH   G 4 .   ? 52.902 -13.419 -20.378 1.00 35.38 ?  220 HOH   B O    1 
HETATM 6883 O O    . HOH   G 4 .   ? 50.769 -6.109  0.165   1.00 26.28 ?  221 HOH   B O    1 
HETATM 6884 O O    . HOH   G 4 .   ? 57.370 -16.228 -12.216 1.00 18.54 ?  222 HOH   B O    1 
HETATM 6885 O O    . HOH   G 4 .   ? 35.959 -43.213 -8.594  1.00 30.57 ?  223 HOH   B O    1 
HETATM 6886 O O    . HOH   G 4 .   ? 39.307 -10.926 6.080   1.00 26.55 ?  224 HOH   B O    1 
HETATM 6887 O O    . HOH   G 4 .   ? 56.686 -30.765 -7.777  1.00 29.56 ?  225 HOH   B O    1 
HETATM 6888 O O    . HOH   G 4 .   ? 37.136 -19.737 -18.064 1.00 37.08 ?  226 HOH   B O    1 
HETATM 6889 O O    . HOH   G 4 .   ? 41.506 -39.128 -14.936 1.00 20.98 ?  227 HOH   B O    1 
HETATM 6890 O O    . HOH   G 4 .   ? 44.447 -7.253  2.138   1.00 33.57 ?  228 HOH   B O    1 
HETATM 6891 O O    . HOH   G 4 .   ? 34.548 -36.347 -7.243  1.00 16.66 ?  229 HOH   B O    1 
HETATM 6892 O O    . HOH   G 4 .   ? 57.187 -26.823 -7.630  1.00 38.59 ?  230 HOH   B O    1 
HETATM 6893 O O    . HOH   G 4 .   ? 44.979 -43.493 -10.563 1.00 26.68 ?  231 HOH   B O    1 
HETATM 6894 O O    . HOH   G 4 .   ? 40.626 -16.034 14.117  1.00 24.11 ?  232 HOH   B O    1 
HETATM 6895 O O    . HOH   G 4 .   ? 48.550 -36.457 -15.531 1.00 41.19 ?  233 HOH   B O    1 
HETATM 6896 O O    . HOH   G 4 .   ? 41.382 -9.656  13.055  1.00 21.95 ?  234 HOH   B O    1 
HETATM 6897 O O    . HOH   G 4 .   ? 30.837 -28.770 4.235   1.00 23.82 ?  235 HOH   B O    1 
HETATM 6898 O O    . HOH   G 4 .   ? 46.388 -1.606  13.273  1.00 27.05 ?  236 HOH   B O    1 
HETATM 6899 O O    . HOH   G 4 .   ? 28.406 -19.684 -13.129 1.00 23.35 ?  237 HOH   B O    1 
HETATM 6900 O O    . HOH   G 4 .   ? 32.806 -43.767 -11.392 1.00 18.95 ?  238 HOH   B O    1 
HETATM 6901 O O    . HOH   G 4 .   ? 45.131 -34.988 6.833   1.00 38.44 ?  239 HOH   B O    1 
HETATM 6902 O O    . HOH   G 4 .   ? 35.097 -7.994  -3.024  1.00 17.55 ?  240 HOH   B O    1 
HETATM 6903 O O    . HOH   G 4 .   ? 51.675 -6.494  4.416   1.00 19.33 ?  241 HOH   B O    1 
HETATM 6904 O O    . HOH   G 4 .   ? 50.725 -12.971 -0.492  1.00 11.59 ?  242 HOH   B O    1 
HETATM 6905 O O    . HOH   G 4 .   ? 39.501 -11.137 0.311   1.00 16.37 ?  243 HOH   B O    1 
HETATM 6906 O O    . HOH   G 4 .   ? 43.111 -43.216 -8.295  1.00 27.78 ?  244 HOH   B O    1 
HETATM 6907 O O    . HOH   G 4 .   ? 25.428 -25.965 -1.407  1.00 31.69 ?  245 HOH   B O    1 
HETATM 6908 O O    . HOH   G 4 .   ? 42.564 -25.368 2.598   1.00 14.27 ?  246 HOH   B O    1 
HETATM 6909 O O    . HOH   G 4 .   ? 42.633 -22.879 3.824   1.00 11.13 ?  247 HOH   B O    1 
HETATM 6910 O O    . HOH   G 4 .   ? 48.042 -24.487 -17.776 1.00 28.88 ?  248 HOH   B O    1 
HETATM 6911 O O    . HOH   G 4 .   ? 44.522 -27.781 -0.744  1.00 21.39 ?  249 HOH   B O    1 
HETATM 6912 O O    . HOH   G 4 .   ? 29.722 -25.204 -10.821 1.00 15.90 ?  250 HOH   B O    1 
HETATM 6913 O O    . HOH   G 4 .   ? 43.181 -32.363 -17.123 1.00 22.12 ?  251 HOH   B O    1 
HETATM 6914 O O    . HOH   G 4 .   ? 40.327 -12.745 -11.535 1.00 14.49 ?  252 HOH   B O    1 
HETATM 6915 O O    . HOH   G 4 .   ? 57.613 -24.385 -3.841  1.00 21.47 ?  253 HOH   B O    1 
HETATM 6916 O O    . HOH   G 4 .   ? 41.859 -23.529 9.270   1.00 15.96 ?  254 HOH   B O    1 
HETATM 6917 O O    . HOH   G 4 .   ? 34.210 -18.502 11.392  1.00 22.76 ?  255 HOH   B O    1 
HETATM 6918 O O    . HOH   G 4 .   ? 38.936 -12.058 12.367  1.00 34.41 ?  256 HOH   B O    1 
HETATM 6919 O O    . HOH   G 4 .   ? 49.784 -0.546  10.249  1.00 30.87 ?  257 HOH   B O    1 
HETATM 6920 O O    . HOH   G 4 .   ? 38.468 -11.043 -2.256  1.00 18.41 ?  258 HOH   B O    1 
HETATM 6921 O O    . HOH   G 4 .   ? 34.885 -24.656 13.841  1.00 27.09 ?  259 HOH   B O    1 
HETATM 6922 O O    . HOH   G 4 .   ? 49.326 -28.699 -6.945  1.00 14.70 ?  260 HOH   B O    1 
HETATM 6923 O O    . HOH   G 4 .   ? 31.820 -17.974 -14.545 1.00 29.75 ?  261 HOH   B O    1 
HETATM 6924 O O    . HOH   G 4 .   ? 33.516 -17.020 8.014   1.00 18.47 ?  262 HOH   B O    1 
HETATM 6925 O O    . HOH   G 4 .   ? 30.867 -15.738 2.629   1.00 12.76 ?  263 HOH   B O    1 
HETATM 6926 O O    . HOH   G 4 .   ? 57.506 -9.244  1.423   1.00 19.28 ?  264 HOH   B O    1 
HETATM 6927 O O    . HOH   G 4 .   ? 58.174 -10.613 -4.085  1.00 19.49 ?  265 HOH   B O    1 
HETATM 6928 O O    . HOH   G 4 .   ? 51.521 -13.832 10.992  1.00 27.44 ?  266 HOH   B O    1 
HETATM 6929 O O    . HOH   G 4 .   ? 42.365 -9.899  9.347   1.00 20.28 ?  267 HOH   B O    1 
HETATM 6930 O O    . HOH   G 4 .   ? 28.489 -30.809 -14.793 1.00 28.41 ?  268 HOH   B O    1 
HETATM 6931 O O    . HOH   G 4 .   ? 50.973 -39.950 -8.273  1.00 29.38 ?  269 HOH   B O    1 
HETATM 6932 O O    . HOH   G 4 .   ? 48.012 -22.763 5.809   1.00 16.42 ?  270 HOH   B O    1 
HETATM 6933 O O    . HOH   G 4 .   ? 28.267 -34.338 -9.474  1.00 20.28 ?  271 HOH   B O    1 
HETATM 6934 O O    . HOH   G 4 .   ? 27.146 -31.815 -10.029 1.00 20.93 ?  272 HOH   B O    1 
HETATM 6935 O O    . HOH   G 4 .   ? 56.943 -8.643  8.411   1.00 19.61 ?  273 HOH   B O    1 
HETATM 6936 O O    . HOH   G 4 .   ? 46.606 -31.256 -4.827  1.00 20.70 ?  274 HOH   B O    1 
HETATM 6937 O O    . HOH   G 4 .   ? 43.368 -15.792 -12.185 1.00 13.43 ?  275 HOH   B O    1 
HETATM 6938 O O    . HOH   G 4 .   ? 34.915 -33.332 -19.252 1.00 27.74 ?  276 HOH   B O    1 
HETATM 6939 O O    . HOH   G 4 .   ? 56.191 -23.467 -14.760 1.00 25.99 ?  277 HOH   B O    1 
HETATM 6940 O O    . HOH   G 4 .   ? 34.478 -12.784 2.597   1.00 23.55 ?  278 HOH   B O    1 
HETATM 6941 O O    . HOH   G 4 .   ? 57.104 -12.116 12.328  1.00 37.32 ?  279 HOH   B O    1 
HETATM 6942 O O    . HOH   G 4 .   ? 46.854 -29.552 9.783   1.00 30.09 ?  280 HOH   B O    1 
HETATM 6943 O O    . HOH   G 4 .   ? 27.953 -22.882 -8.014  1.00 16.17 ?  281 HOH   B O    1 
HETATM 6944 O O    . HOH   G 4 .   ? 41.172 -5.508  11.533  1.00 43.63 ?  282 HOH   B O    1 
HETATM 6945 O O    . HOH   G 4 .   ? 48.408 -25.046 3.091   1.00 12.63 ?  283 HOH   B O    1 
HETATM 6946 O O    . HOH   G 4 .   ? 30.586 -42.235 -10.655 1.00 28.30 ?  284 HOH   B O    1 
HETATM 6947 O O    . HOH   G 4 .   ? 33.523 -15.296 -13.981 1.00 20.13 ?  285 HOH   B O    1 
HETATM 6948 O O    . HOH   G 4 .   ? 48.714 -20.031 5.907   1.00 13.45 ?  286 HOH   B O    1 
HETATM 6949 O O    . HOH   G 4 .   ? 42.398 -34.683 3.769   1.00 24.79 ?  287 HOH   B O    1 
HETATM 6950 O O    . HOH   G 4 .   ? 36.823 -12.766 -1.533  1.00 25.50 ?  288 HOH   B O    1 
HETATM 6951 O O    . HOH   G 4 .   ? 37.347 -35.662 7.170   1.00 33.78 ?  289 HOH   B O    1 
HETATM 6952 O O    . HOH   G 4 .   ? 42.824 -20.295 -20.797 1.00 36.20 ?  290 HOH   B O    1 
HETATM 6953 O O    . HOH   G 4 .   ? 47.068 -33.977 -4.665  1.00 16.30 ?  291 HOH   B O    1 
HETATM 6954 O O    . HOH   G 4 .   ? 57.663 -22.091 3.029   1.00 25.46 ?  292 HOH   B O    1 
HETATM 6955 O O    . HOH   G 4 .   ? 51.229 -37.592 -9.643  1.00 23.49 ?  293 HOH   B O    1 
HETATM 6956 O O    . HOH   G 4 .   ? 42.260 -9.988  -14.941 1.00 36.01 ?  294 HOH   B O    1 
HETATM 6957 O O    . HOH   G 4 .   ? 52.505 -10.426 13.000  1.00 21.80 ?  295 HOH   B O    1 
HETATM 6958 O O    . HOH   G 4 .   ? 35.066 -33.589 4.459   1.00 26.86 ?  296 HOH   B O    1 
HETATM 6959 O O    . HOH   G 4 .   ? 27.577 -26.730 -15.652 1.00 32.67 ?  297 HOH   B O    1 
HETATM 6960 O O    . HOH   G 4 .   ? 45.370 -33.371 -15.979 1.00 22.60 ?  298 HOH   B O    1 
HETATM 6961 O O    . HOH   G 4 .   ? 48.120 -32.639 -16.579 1.00 41.78 ?  299 HOH   B O    1 
HETATM 6962 O O    . HOH   G 4 .   ? 42.706 -12.244 -18.507 1.00 27.46 ?  300 HOH   B O    1 
HETATM 6963 O O    . HOH   G 4 .   ? 52.599 -35.655 -8.607  1.00 27.44 ?  301 HOH   B O    1 
HETATM 6964 O O    . HOH   G 4 .   ? 40.228 -10.821 -9.548  1.00 16.17 ?  302 HOH   B O    1 
HETATM 6965 O O    . HOH   G 4 .   ? 45.899 -40.387 -3.665  1.00 27.95 ?  303 HOH   B O    1 
HETATM 6966 O O    . HOH   G 4 .   ? 43.546 -15.358 18.211  1.00 30.94 ?  304 HOH   B O    1 
HETATM 6967 O O    . HOH   G 4 .   ? 44.611 -27.461 1.963   1.00 14.45 ?  305 HOH   B O    1 
HETATM 6968 O O    . HOH   G 4 .   ? 59.751 -15.300 8.173   1.00 31.06 ?  306 HOH   B O    1 
HETATM 6969 O O    . HOH   G 4 .   ? 25.957 -21.493 -3.546  1.00 15.38 ?  307 HOH   B O    1 
HETATM 6970 O O    . HOH   G 4 .   ? 37.534 -18.225 13.106  1.00 29.77 ?  308 HOH   B O    1 
HETATM 6971 O O    . HOH   G 4 .   ? 49.958 -24.633 5.806   1.00 32.87 ?  309 HOH   B O    1 
HETATM 6972 O O    . HOH   G 4 .   ? 32.809 -34.584 -5.944  1.00 15.74 ?  310 HOH   B O    1 
HETATM 6973 O O    . HOH   G 4 .   ? 53.439 -30.209 4.489   1.00 17.94 ?  311 HOH   B O    1 
HETATM 6974 O O    . HOH   G 4 .   ? 62.821 -20.206 -0.869  1.00 37.90 ?  312 HOH   B O    1 
HETATM 6975 O O    . HOH   G 4 .   ? 41.236 -24.471 15.770  1.00 41.83 ?  313 HOH   B O    1 
HETATM 6976 O O    . HOH   G 4 .   ? 44.038 -29.344 -4.685  1.00 22.31 ?  314 HOH   B O    1 
HETATM 6977 O O    . HOH   G 4 .   ? 52.559 -29.225 -13.048 1.00 23.38 ?  315 HOH   B O    1 
HETATM 6978 O O    . HOH   G 4 .   ? 37.841 -10.242 -10.758 1.00 16.22 ?  316 HOH   B O    1 
HETATM 6979 O O    . HOH   G 4 .   ? 41.733 -8.095  1.377   1.00 24.55 ?  317 HOH   B O    1 
HETATM 6980 O O    . HOH   G 4 .   ? 52.988 -15.970 -12.783 1.00 26.95 ?  318 HOH   B O    1 
HETATM 6981 O O    . HOH   G 4 .   ? 38.354 -12.789 7.933   1.00 17.47 ?  319 HOH   B O    1 
HETATM 6982 O O    . HOH   G 4 .   ? 51.662 -5.952  -7.942  1.00 44.18 ?  320 HOH   B O    1 
HETATM 6983 O O    . HOH   G 4 .   ? 43.199 -21.431 10.656  1.00 14.91 ?  321 HOH   B O    1 
HETATM 6984 O O    . HOH   G 4 .   ? 62.679 -13.561 4.687   1.00 27.00 ?  322 HOH   B O    1 
HETATM 6985 O O    . HOH   G 4 .   ? 59.961 -17.103 -10.463 1.00 33.15 ?  323 HOH   B O    1 
HETATM 6986 O O    . HOH   G 4 .   ? 38.346 -9.369  -13.286 1.00 28.60 ?  324 HOH   B O    1 
HETATM 6987 O O    . HOH   G 4 .   ? 26.336 -21.026 -6.274  1.00 15.66 ?  325 HOH   B O    1 
HETATM 6988 O O    . HOH   G 4 .   ? 37.145 -30.595 -21.058 1.00 29.56 ?  326 HOH   B O    1 
HETATM 6989 O O    . HOH   G 4 .   ? 44.575 -24.632 9.557   1.00 18.39 ?  327 HOH   B O    1 
HETATM 6990 O O    . HOH   G 4 .   ? 44.191 -1.779  7.556   1.00 43.14 ?  328 HOH   B O    1 
HETATM 6991 O O    . HOH   G 4 .   ? 51.408 -32.910 -10.837 1.00 38.72 ?  329 HOH   B O    1 
HETATM 6992 O O    . HOH   G 4 .   ? 36.726 -12.415 4.269   1.00 17.56 ?  330 HOH   B O    1 
HETATM 6993 O O    . HOH   G 4 .   ? 39.468 -23.459 -20.297 1.00 34.22 ?  331 HOH   B O    1 
HETATM 6994 O O    . HOH   G 4 .   ? 33.637 -31.145 11.055  1.00 33.86 ?  332 HOH   B O    1 
HETATM 6995 O O    . HOH   G 4 .   ? 43.122 -34.623 0.052   1.00 19.54 ?  333 HOH   B O    1 
HETATM 6996 O O    . HOH   G 4 .   ? 45.741 -36.239 -16.126 1.00 33.13 ?  334 HOH   B O    1 
HETATM 6997 O O    . HOH   G 4 .   ? 47.151 -24.489 8.143   1.00 24.45 ?  335 HOH   B O    1 
HETATM 6998 O O    . HOH   G 4 .   ? 27.911 -14.755 -9.457  1.00 33.64 ?  336 HOH   B O    1 
HETATM 6999 O O    . HOH   G 4 .   ? 42.884 -43.456 -14.401 1.00 42.67 ?  337 HOH   B O    1 
HETATM 7000 O O    . HOH   G 4 .   ? 53.642 -12.576 -22.305 1.00 34.59 ?  338 HOH   B O    1 
HETATM 7001 O O    . HOH   G 4 .   ? 48.574 -11.880 -13.881 1.00 26.32 ?  339 HOH   B O    1 
HETATM 7002 O O    . HOH   G 4 .   ? 47.472 -27.444 1.993   1.00 14.03 ?  340 HOH   B O    1 
HETATM 7003 O O    . HOH   G 4 .   ? 46.828 -19.890 12.264  1.00 31.41 ?  341 HOH   B O    1 
HETATM 7004 O O    . HOH   G 4 .   ? 37.019 -15.075 -16.538 1.00 38.65 ?  342 HOH   B O    1 
HETATM 7005 O O    . HOH   G 4 .   ? 37.076 -45.175 -9.823  1.00 34.97 ?  343 HOH   B O    1 
HETATM 7006 O O    . HOH   G 4 .   ? 38.436 -12.261 -16.281 1.00 40.70 ?  344 HOH   B O    1 
HETATM 7007 O O    . HOH   G 4 .   ? 28.881 -42.946 -12.325 1.00 35.91 ?  345 HOH   B O    1 
HETATM 7008 O O    . HOH   G 4 .   ? 33.006 -14.701 1.027   1.00 17.55 ?  346 HOH   B O    1 
HETATM 7009 O O    . HOH   G 4 .   ? 39.794 -44.279 -11.237 1.00 37.32 ?  347 HOH   B O    1 
HETATM 7010 O O    . HOH   G 4 .   ? 40.388 -43.443 -9.176  1.00 25.23 ?  348 HOH   B O    1 
HETATM 7011 O O    . HOH   G 4 .   ? 27.757 -26.599 -0.631  1.00 29.10 ?  349 HOH   B O    1 
HETATM 7012 O O    . HOH   G 4 .   ? 55.633 -8.264  10.805  1.00 25.01 ?  350 HOH   B O    1 
HETATM 7013 O O    . HOH   G 4 .   ? 38.509 -22.298 15.050  1.00 40.73 ?  351 HOH   B O    1 
HETATM 7014 O O    . HOH   G 4 .   ? 33.795 -9.161  -8.820  1.00 31.08 ?  352 HOH   B O    1 
HETATM 7015 O O    . HOH   G 4 .   ? 62.570 -20.165 -4.892  1.00 43.69 ?  353 HOH   B O    1 
HETATM 7016 O O    . HOH   G 4 .   ? 44.181 -37.342 -17.856 1.00 31.85 ?  354 HOH   B O    1 
HETATM 7017 O O    . HOH   G 4 .   ? 34.600 -10.340 7.505   1.00 23.04 ?  355 HOH   B O    1 
HETATM 7018 O O    . HOH   G 4 .   ? 23.227 -23.690 6.759   1.00 32.66 ?  356 HOH   B O    1 
HETATM 7019 O O    . HOH   G 4 .   ? 56.611 -7.299  3.101   1.00 27.38 ?  357 HOH   B O    1 
HETATM 7020 O O    . HOH   G 4 .   ? 36.169 -8.476  -9.708  1.00 33.25 ?  358 HOH   B O    1 
HETATM 7021 O O    . HOH   G 4 .   ? 34.108 -7.807  11.413  1.00 39.62 ?  359 HOH   B O    1 
HETATM 7022 O O    . HOH   G 4 .   ? 61.499 -19.904 1.624   1.00 32.30 ?  360 HOH   B O    1 
HETATM 7023 O O    . HOH   G 4 .   ? 43.146 -12.686 -21.239 1.00 37.09 ?  361 HOH   B O    1 
HETATM 7024 O O    . HOH   G 4 .   ? 56.914 -21.555 -16.426 1.00 39.78 ?  362 HOH   B O    1 
HETATM 7025 O O    . HOH   G 4 .   ? 40.227 -8.837  9.900   1.00 36.48 ?  363 HOH   B O    1 
HETATM 7026 O O    . HOH   G 4 .   ? 27.150 -25.943 -11.484 1.00 31.47 ?  364 HOH   B O    1 
HETATM 7027 O O    . HOH   G 4 .   ? 54.211 -5.741  2.951   1.00 36.05 ?  365 HOH   B O    1 
HETATM 7028 O O    . HOH   G 4 .   ? 32.498 -23.607 14.063  1.00 38.80 ?  366 HOH   B O    1 
HETATM 7029 O O    . HOH   G 4 .   ? 36.241 -8.722  8.969   1.00 34.40 ?  367 HOH   B O    1 
HETATM 7030 O O    . HOH   G 4 .   ? 39.880 -7.021  7.805   1.00 40.44 ?  368 HOH   B O    1 
HETATM 7031 O O    . HOH   G 4 .   ? 59.044 -10.492 9.136   1.00 37.84 ?  369 HOH   B O    1 
HETATM 7032 O O    . HOH   G 4 .   ? 40.019 -11.382 -13.972 1.00 32.07 ?  370 HOH   B O    1 
HETATM 7033 O O    . HOH   G 4 .   ? 48.442 -26.513 8.767   1.00 38.73 ?  371 HOH   B O    1 
HETATM 7034 O O    . HOH   G 4 .   ? 41.790 -9.994  -17.467 1.00 54.55 ?  372 HOH   B O    1 
HETATM 7035 O O    . HOH   G 4 .   ? 56.044 -7.796  -0.571  1.00 36.78 ?  373 HOH   B O    1 
HETATM 7036 O O    . HOH   G 4 .   ? 52.002 -12.910 13.366  1.00 30.32 ?  374 HOH   B O    1 
HETATM 7037 O O    . HOH   G 4 .   ? 38.028 -10.578 10.045  1.00 28.73 ?  375 HOH   B O    1 
HETATM 7038 O O    . HOH   G 4 .   ? 36.550 -22.792 13.286  1.00 24.88 ?  376 HOH   B O    1 
HETATM 7039 O O    . HOH   G 4 .   ? 63.066 -12.369 6.948   1.00 35.24 ?  377 HOH   B O    1 
HETATM 7040 O O    . HOH   G 4 .   ? 41.800 -6.737  -4.846  1.00 45.49 ?  378 HOH   B O    1 
HETATM 7041 O O    . HOH   G 4 .   ? 44.061 -5.598  -3.526  1.00 40.08 ?  379 HOH   B O    1 
HETATM 7042 O O    . HOH   G 4 .   ? 40.059 -7.636  3.259   1.00 34.73 ?  380 HOH   B O    1 
HETATM 7043 O O    . HOH   G 4 .   ? 42.636 -17.057 -23.227 1.00 41.57 ?  381 HOH   B O    1 
HETATM 7044 O O    . HOH   G 4 .   ? 39.742 -14.137 15.700  1.00 51.72 ?  382 HOH   B O    1 
HETATM 7045 O O    . HOH   G 4 .   ? 52.827 -29.884 7.143   1.00 22.74 ?  383 HOH   B O    1 
HETATM 7046 O O    . HOH   G 4 .   ? 60.465 -22.262 2.774   1.00 44.70 ?  384 HOH   B O    1 
HETATM 7047 O O    . HOH   G 4 .   ? 46.797 -5.381  2.918   1.00 41.08 ?  385 HOH   B O    1 
HETATM 7048 O O    . HOH   G 4 .   ? 23.918 -20.840 -7.703  1.00 26.94 ?  386 HOH   B O    1 
HETATM 7049 O O    . HOH   G 4 .   ? 35.386 -33.713 7.266   1.00 39.04 ?  387 HOH   B O    1 
HETATM 7050 O O    . HOH   G 4 .   ? 40.934 -9.809  15.834  1.00 44.51 ?  388 HOH   B O    1 
HETATM 7051 O O    . HOH   G 4 .   ? 25.803 -18.910 -11.953 1.00 36.45 ?  389 HOH   B O    1 
HETATM 7052 O O    . HOH   G 4 .   ? 35.343 -20.318 13.359  1.00 28.88 ?  390 HOH   B O    1 
HETATM 7053 O O    . HOH   G 4 .   ? 40.684 -6.625  -0.850  1.00 23.80 ?  391 HOH   B O    1 
HETATM 7054 O O    . HOH   G 4 .   ? 44.022 -31.783 -3.911  1.00 33.30 ?  392 HOH   B O    1 
HETATM 7055 O O    . HOH   G 4 .   ? 27.945 -27.096 2.234   1.00 31.13 ?  393 HOH   B O    1 
HETATM 7056 O O    . HOH   G 4 .   ? 26.635 -27.974 -13.566 1.00 34.09 ?  394 HOH   B O    1 
HETATM 7057 O O    . HOH   G 4 .   ? 34.380 -33.451 9.567   1.00 31.08 ?  395 HOH   B O    1 
HETATM 7058 O O    . HOH   G 4 .   ? 50.613 -30.800 8.660   1.00 26.84 ?  396 HOH   B O    1 
HETATM 7059 O O    . HOH   G 4 .   ? 24.599 -20.697 -10.447 1.00 35.16 ?  397 HOH   B O    1 
HETATM 7060 O O    . HOH   G 4 .   ? 26.863 -30.644 -12.708 1.00 28.07 ?  398 HOH   B O    1 
HETATM 7061 O O    . HOH   G 4 .   ? 45.756 -20.245 15.175  1.00 49.82 ?  399 HOH   B O    1 
HETATM 7062 O O    . HOH   G 4 .   ? 57.564 -6.421  -2.381  1.00 32.90 ?  400 HOH   B O    1 
HETATM 7063 O O    . HOH   G 4 .   ? 40.886 -11.750 -22.306 1.00 42.53 ?  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   ? 0.6143 0.5997 0.6611 -0.0015 -0.0247 0.0895  3   VAL   A N   
2    N N   B VAL   A 3   ? 0.6032 0.5968 0.6188 -0.0057 -0.0142 0.0466  3   VAL   A N   
3    C CA  A VAL   A 3   ? 0.6120 0.5975 0.6517 -0.0028 -0.0241 0.0874  3   VAL   A CA  
4    C CA  B VAL   A 3   ? 0.6012 0.5950 0.6149 -0.0063 -0.0145 0.0484  3   VAL   A CA  
5    C C   A VAL   A 3   ? 0.5970 0.5872 0.6216 -0.0068 -0.0238 0.0833  3   VAL   A C   
6    C C   B VAL   A 3   ? 0.5918 0.5862 0.6007 -0.0090 -0.0179 0.0612  3   VAL   A C   
7    O O   A VAL   A 3   ? 0.5991 0.5891 0.6298 -0.0047 -0.0248 0.0868  3   VAL   A O   
8    O O   B VAL   A 3   ? 0.5947 0.5884 0.6072 -0.0083 -0.0185 0.0611  3   VAL   A O   
9    C CB  A VAL   A 3   ? 0.6220 0.6036 0.6647 -0.0008 -0.0218 0.0889  3   VAL   A CB  
10   C CB  B VAL   A 3   ? 0.6064 0.6000 0.6215 -0.0045 -0.0115 0.0393  3   VAL   A CB  
11   C CG1 A VAL   A 3   ? 0.6256 0.6058 0.6682 -0.0003 -0.0210 0.0893  3   VAL   A CG1 
12   C CG1 B VAL   A 3   ? 0.6082 0.6016 0.6236 -0.0040 -0.0105 0.0360  3   VAL   A CG1 
13   C CG2 A VAL   A 3   ? 0.6252 0.6054 0.6683 0.0002  -0.0204 0.0905  3   VAL   A CG2 
14   C CG2 B VAL   A 3   ? 0.6081 0.6016 0.6236 -0.0039 -0.0104 0.0362  3   VAL   A CG2 
31   N N   . ASN   A 4   ? 0.5770 0.5733 0.5746 -0.0128 -0.0207 0.0748  4   ASN   A N   
32   C CA  . ASN   A 4   ? 0.5404 0.5437 0.4959 -0.0228 -0.0191 0.0780  4   ASN   A CA  
33   C C   . ASN   A 4   ? 0.4928 0.5076 0.4440 -0.0320 -0.0040 0.0571  4   ASN   A C   
34   O O   . ASN   A 4   ? 0.4946 0.5100 0.4348 -0.0333 -0.0059 0.0617  4   ASN   A O   
35   C CB  . ASN   A 4   ? 0.5494 0.5478 0.4648 -0.0235 -0.0320 0.0986  4   ASN   A CB  
36   C CG  . ASN   A 4   ? 0.5569 0.5499 0.4348 -0.0244 -0.0428 0.1185  4   ASN   A CG  
37   O OD1 . ASN   A 4   ? 0.5611 0.5501 0.4212 -0.0245 -0.0476 0.1259  4   ASN   A OD1 
38   N ND2 . ASN   A 4   ? 0.5584 0.5507 0.4271 -0.0242 -0.0454 0.1276  4   ASN   A ND2 
46   N N   . SER   A 5   ? 0.4409 0.4644 0.3968 -0.0400 0.0092  0.0306  5   SER   A N   
47   C CA  . SER   A 5   ? 0.3882 0.4236 0.3526 -0.0452 0.0235  0.0023  5   SER   A CA  
48   C C   . SER   A 5   ? 0.3316 0.3687 0.2929 -0.0431 0.0343  -0.0174 5   SER   A C   
49   O O   . SER   A 5   ? 0.3377 0.3791 0.2937 -0.0319 0.0346  -0.0337 5   SER   A O   
50   C CB  . SER   A 5   ? 0.3944 0.4358 0.3721 -0.0503 0.0274  -0.0048 5   SER   A CB  
51   O OG  . SER   A 5   ? 0.3986 0.4416 0.3824 -0.0522 0.0333  -0.0101 5   SER   A OG  
57   N N   A PHE   A 6   ? 0.2886 0.3285 0.2537 -0.0601 0.0498  -0.0149 6   PHE   A N   
58   N N   B PHE   A 6   ? 0.3100 0.3408 0.2742 -0.0350 0.0302  -0.0164 6   PHE   A N   
59   C CA  A PHE   A 6   ? 0.2518 0.2897 0.2223 -0.0724 0.0610  0.0033  6   PHE   A CA  
60   C CA  B PHE   A 6   ? 0.2883 0.3123 0.2528 -0.0269 0.0251  -0.0130 6   PHE   A CA  
61   C C   A PHE   A 6   ? 0.2496 0.2944 0.2381 -0.0815 0.0724  0.0079  6   PHE   A C   
62   C C   B PHE   A 6   ? 0.2756 0.2955 0.2522 -0.0215 0.0213  -0.0093 6   PHE   A C   
63   O O   A PHE   A 6   ? 0.2556 0.3067 0.2619 -0.0834 0.0642  0.0204  6   PHE   A O   
64   O O   B PHE   A 6   ? 0.2758 0.2963 0.2553 -0.0231 0.0193  -0.0087 6   PHE   A O   
65   C CB  A PHE   A 6   ? 0.2315 0.2554 0.2021 -0.0615 0.0523  0.0151  6   PHE   A CB  
66   C CB  B PHE   A 6   ? 0.2804 0.3006 0.2344 -0.0239 0.0227  -0.0139 6   PHE   A CB  
67   C CG  A PHE   A 6   ? 0.2160 0.2341 0.1899 -0.0502 0.0437  0.0229  6   PHE   A CG  
68   C CG  B PHE   A 6   ? 0.2729 0.2898 0.2178 -0.0223 0.0203  -0.0145 6   PHE   A CG  
69   C CD1 A PHE   A 6   ? 0.2074 0.2264 0.1938 -0.0416 0.0344  0.0305  6   PHE   A CD1 
70   C CD1 B PHE   A 6   ? 0.2697 0.2852 0.2116 -0.0213 0.0188  -0.0140 6   PHE   A CD1 
71   C CD2 A PHE   A 6   ? 0.2194 0.2310 0.2068 -0.0329 0.0336  0.0173  6   PHE   A CD2 
72   C CD2 B PHE   A 6   ? 0.2705 0.2853 0.2113 -0.0209 0.0195  -0.0157 6   PHE   A CD2 
73   C CE1 A PHE   A 6   ? 0.2048 0.2207 0.1960 -0.0377 0.0317  0.0340  6   PHE   A CE1 
74   C CE1 B PHE   A 6   ? 0.2679 0.2821 0.2069 -0.0210 0.0186  -0.0141 6   PHE   A CE1 
75   C CE2 A PHE   A 6   ? 0.2148 0.2284 0.2149 -0.0270 0.0288  0.0136  6   PHE   A CE2 
76   C CE2 B PHE   A 6   ? 0.2686 0.2822 0.2064 -0.0203 0.0193  -0.0150 6   PHE   A CE2 
77   C CZ  A PHE   A 6   ? 0.2086 0.2228 0.2055 -0.0317 0.0295  0.0204  6   PHE   A CZ  
78   C CZ  B PHE   A 6   ? 0.2676 0.2810 0.2055 -0.0206 0.0188  -0.0145 6   PHE   A CZ  
97   N N   A SER   A 7   ? 0.2394 0.2866 0.2341 -0.0844 0.0881  -0.0003 7   SER   A N   
98   N N   B SER   A 7   ? 0.2625 0.2779 0.2492 -0.0149 0.0180  -0.0063 7   SER   A N   
99   C CA  A SER   A 7   ? 0.2468 0.2908 0.2613 -0.0713 0.0858  -0.0192 7   SER   A CA  
100  C CA  B SER   A 7   ? 0.2516 0.2620 0.2489 -0.0083 0.0148  -0.0038 7   SER   A CA  
101  C C   A SER   A 7   ? 0.2272 0.2565 0.2579 -0.0709 0.0959  -0.0224 7   SER   A C   
102  C C   B SER   A 7   ? 0.2394 0.2460 0.2378 -0.0044 0.0145  -0.0022 7   SER   A C   
103  O O   A SER   A 7   ? 0.2346 0.2466 0.2607 -0.0748 0.0952  -0.0204 7   SER   A O   
104  O O   B SER   A 7   ? 0.2398 0.2447 0.2364 -0.0040 0.0133  -0.0013 7   SER   A O   
105  C CB  A SER   A 7   ? 0.2709 0.3223 0.2901 -0.0537 0.0807  -0.0182 7   SER   A CB  
106  C CB  B SER   A 7   ? 0.2532 0.2625 0.2590 -0.0059 0.0136  -0.0009 7   SER   A CB  
107  O OG  A SER   A 7   ? 0.2874 0.3378 0.3182 -0.0424 0.0775  -0.0171 7   SER   A OG  
108  O OG  B SER   A 7   ? 0.2540 0.2620 0.2662 -0.0044 0.0131  0.0028  7   SER   A OG  
119  N N   A GLY   A 8   ? 0.2103 0.2373 0.2632 -0.0662 0.0913  -0.0310 8   GLY   A N   
120  N N   B GLY   A 8   ? 0.2284 0.2330 0.2293 -0.0023 0.0148  -0.0019 8   GLY   A N   
121  C CA  A GLY   A 8   ? 0.1992 0.2201 0.2743 -0.0513 0.0807  -0.0309 8   GLY   A CA  
122  C CA  B GLY   A 8   ? 0.2170 0.2193 0.2194 -0.0012 0.0127  -0.0015 8   GLY   A CA  
123  C C   A GLY   A 8   ? 0.1827 0.2061 0.2615 -0.0403 0.0657  -0.0200 8   GLY   A C   
124  C C   B GLY   A 8   ? 0.2055 0.2059 0.2062 -0.0002 0.0101  -0.0011 8   GLY   A C   
125  O O   A GLY   A 8   ? 0.1863 0.2084 0.2896 -0.0197 0.0614  -0.0301 8   GLY   A O   
126  O O   B GLY   A 8   ? 0.2045 0.2046 0.2094 -0.0005 0.0087  -0.0034 8   GLY   A O   
133  N N   A TYR   A 9   ? 0.1669 0.1899 0.2312 -0.0342 0.0474  -0.0035 9   TYR   A N   
134  N N   B TYR   A 9   ? 0.1943 0.1946 0.1941 0.0018  0.0082  0.0018  9   TYR   A N   
135  C CA  A TYR   A 9   ? 0.1537 0.1722 0.1992 -0.0344 0.0358  0.0064  9   TYR   A CA  
136  C CA  B TYR   A 9   ? 0.1842 0.1847 0.1838 0.0030  0.0088  0.0017  9   TYR   A CA  
137  C C   A TYR   A 9   ? 0.1600 0.1596 0.1998 -0.0267 0.0354  0.0294  9   TYR   A C   
138  C C   B TYR   A 9   ? 0.1794 0.1772 0.1803 0.0065  0.0131  0.0018  9   TYR   A C   
139  O O   A TYR   A 9   ? 0.1923 0.1734 0.2219 -0.0388 0.0289  0.0297  9   TYR   A O   
140  O O   B TYR   A 9   ? 0.1812 0.1787 0.1842 0.0089  0.0196  0.0005  9   TYR   A O   
141  C CB  A TYR   A 9   ? 0.1487 0.1819 0.1964 -0.0252 0.0248  -0.0023 9   TYR   A CB  
142  C CB  B TYR   A 9   ? 0.1791 0.1847 0.1795 0.0010  0.0036  -0.0004 9   TYR   A CB  
143  C CG  A TYR   A 9   ? 0.1447 0.1862 0.2030 -0.0151 0.0312  -0.0101 9   TYR   A CG  
144  C CG  B TYR   A 9   ? 0.1732 0.1842 0.1713 -0.0017 0.0007  -0.0027 9   TYR   A CG  
145  C CD1 A TYR   A 9   ? 0.1458 0.1959 0.2135 -0.0212 0.0461  -0.0137 9   TYR   A CD1 
146  C CD1 B TYR   A 9   ? 0.1703 0.1855 0.1697 -0.0043 -0.0017 -0.0032 9   TYR   A CD1 
147  C CD2 A TYR   A 9   ? 0.1389 0.1751 0.2055 -0.0133 0.0291  0.0029  9   TYR   A CD2 
148  C CD2 B TYR   A 9   ? 0.1714 0.1831 0.1650 -0.0030 -0.0017 -0.0066 9   TYR   A CD2 
149  C CE1 A TYR   A 9   ? 0.1528 0.1976 0.2252 -0.0227 0.0508  -0.0211 9   TYR   A CE1 
150  C CE1 B TYR   A 9   ? 0.1692 0.1854 0.1670 -0.0058 -0.0029 -0.0070 9   TYR   A CE1 
151  C CE2 A TYR   A 9   ? 0.1422 0.1814 0.2138 -0.0117 0.0378  -0.0040 9   TYR   A CE2 
152  C CE2 B TYR   A 9   ? 0.1712 0.1840 0.1656 -0.0046 -0.0007 -0.0103 9   TYR   A CE2 
153  C CZ  A TYR   A 9   ? 0.1453 0.1947 0.2286 -0.0309 0.0504  -0.0079 9   TYR   A CZ  
154  C CZ  B TYR   A 9   ? 0.1715 0.1858 0.1657 -0.0068 -0.0027 -0.0090 9   TYR   A CZ  
155  O OH  A TYR   A 9   ? 0.1526 0.2123 0.2434 -0.0420 0.0541  -0.0093 9   TYR   A OH  
156  O OH  B TYR   A 9   ? 0.1757 0.1886 0.1706 -0.0077 -0.0027 -0.0080 9   TYR   A OH  
175  N N   A LEU   A 10  ? 0.1398 0.1464 0.1996 -0.0203 0.0240  0.0265  10  LEU   A N   
176  N N   B LEU   A 10  ? 0.1749 0.1730 0.1758 0.0057  0.0083  0.0020  10  LEU   A N   
177  C CA  A LEU   A 10  ? 0.1364 0.1488 0.2015 -0.0255 0.0164  0.0433  10  LEU   A CA  
178  C CA  B LEU   A 10  ? 0.1707 0.1708 0.1702 0.0032  0.0026  -0.0006 10  LEU   A CA  
179  C C   A LEU   A 10  ? 0.1310 0.1440 0.1896 -0.0205 0.0166  0.0427  10  LEU   A C   
180  C C   B LEU   A 10  ? 0.1620 0.1616 0.1520 -0.0026 -0.0028 0.0020  10  LEU   A C   
181  O O   A LEU   A 10  ? 0.1339 0.1406 0.2057 -0.0214 0.0270  0.0453  10  LEU   A O   
182  O O   B LEU   A 10  ? 0.1613 0.1599 0.1563 -0.0034 -0.0010 0.0061  10  LEU   A O   
183  C CB  A LEU   A 10  ? 0.1383 0.1576 0.2377 -0.0240 -0.0023 0.0559  10  LEU   A CB  
184  C CB  B LEU   A 10  ? 0.1742 0.1764 0.1828 0.0061  -0.0005 -0.0054 10  LEU   A CB  
185  C CG  A LEU   A 10  ? 0.1572 0.1772 0.2865 -0.0171 -0.0294 0.0714  10  LEU   A CG  
186  C CG  B LEU   A 10  ? 0.1781 0.1835 0.1952 0.0087  -0.0036 -0.0079 10  LEU   A CG  
187  C CD1 A LEU   A 10  ? 0.1732 0.1900 0.3279 -0.0251 -0.0167 0.0691  10  LEU   A CD1 
188  C CD1 B LEU   A 10  ? 0.1797 0.1876 0.1977 0.0100  -0.0053 -0.0071 10  LEU   A CD1 
189  C CD2 A LEU   A 10  ? 0.1845 0.2001 0.3071 -0.0069 -0.0216 0.0568  10  LEU   A CD2 
190  C CD2 B LEU   A 10  ? 0.1788 0.1842 0.2016 0.0088  -0.0038 -0.0101 10  LEU   A CD2 
213  N N   A LYS   A 11  ? 0.1380 0.1437 0.1793 -0.0219 0.0152  0.0395  11  LYS   A N   
214  N N   B LYS   A 11  ? 0.1557 0.1538 0.1344 -0.0084 -0.0093 0.0014  11  LYS   A N   
215  C CA  A LYS   A 11  ? 0.1390 0.1435 0.1735 -0.0242 0.0153  0.0368  11  LYS   A CA  
216  C CA  B LYS   A 11  ? 0.1528 0.1476 0.1281 -0.0112 -0.0063 0.0035  11  LYS   A CA  
217  C C   A LYS   A 11  ? 0.1338 0.1519 0.1788 -0.0290 0.0201  0.0322  11  LYS   A C   
218  C C   B LYS   A 11  ? 0.1459 0.1416 0.1202 -0.0150 -0.0054 -0.0004 11  LYS   A C   
219  O O   A LYS   A 11  ? 0.1424 0.1900 0.2147 -0.0587 0.0306  0.0097  11  LYS   A O   
220  O O   B LYS   A 11  ? 0.1448 0.1401 0.1204 -0.0177 -0.0045 -0.0091 11  LYS   A O   
221  C CB  A LYS   A 11  ? 0.1485 0.1427 0.1755 -0.0266 0.0135  0.0312  11  LYS   A CB  
222  C CB  B LYS   A 11  ? 0.1547 0.1458 0.1330 -0.0105 -0.0043 0.0050  11  LYS   A CB  
223  C CG  A LYS   A 11  ? 0.1592 0.1389 0.1704 -0.0237 0.0184  0.0304  11  LYS   A CG  
224  C CG  B LYS   A 11  ? 0.1561 0.1449 0.1357 -0.0083 -0.0021 0.0057  11  LYS   A CG  
225  C CD  A LYS   A 11  ? 0.1760 0.1456 0.1735 -0.0189 0.0203  0.0337  11  LYS   A CD  
226  C CD  B LYS   A 11  ? 0.1574 0.1460 0.1404 -0.0059 -0.0006 0.0076  11  LYS   A CD  
227  C CE  A LYS   A 11  ? 0.1884 0.1400 0.1787 -0.0170 0.0148  0.0389  11  LYS   A CE  
228  C CE  B LYS   A 11  ? 0.1583 0.1458 0.1430 -0.0042 -0.0007 0.0097  11  LYS   A CE  
229  N NZ  A LYS   A 11  ? 0.1865 0.1339 0.1872 -0.0072 0.0013  0.0256  11  LYS   A NZ  
230  N NZ  B LYS   A 11  ? 0.1571 0.1455 0.1424 -0.0017 -0.0024 0.0108  11  LYS   A NZ  
257  N N   A LEU   A 12  ? 0.1245 0.1373 0.1569 -0.0238 0.0164  0.0238  12  LEU   A N   
258  N N   B LEU   A 12  ? 0.1406 0.1429 0.1229 -0.0126 -0.0030 0.0014  12  LEU   A N   
259  C CA  A LEU   A 12  ? 0.1286 0.1504 0.1585 -0.0200 0.0112  0.0278  12  LEU   A CA  
260  C CA  B LEU   A 12  ? 0.1370 0.1442 0.1248 -0.0116 0.0056  0.0034  12  LEU   A CA  
261  C C   A LEU   A 12  ? 0.1345 0.1440 0.1639 -0.0254 0.0111  0.0304  12  LEU   A C   
262  C C   B LEU   A 12  ? 0.1378 0.1451 0.1279 -0.0094 0.0118  0.0049  12  LEU   A C   
263  O O   A LEU   A 12  ? 0.1387 0.1494 0.1722 -0.0198 0.0104  0.0176  12  LEU   A O   
264  O O   B LEU   A 12  ? 0.1394 0.1439 0.1266 -0.0048 0.0105  0.0051  12  LEU   A O   
265  C CB  A LEU   A 12  ? 0.1367 0.1505 0.1705 -0.0187 0.0047  0.0340  12  LEU   A CB  
266  C CB  B LEU   A 12  ? 0.1352 0.1450 0.1263 -0.0113 0.0110  0.0039  12  LEU   A CB  
267  C CG  A LEU   A 12  ? 0.1504 0.1597 0.1974 -0.0118 0.0126  0.0379  12  LEU   A CG  
268  C CG  B LEU   A 12  ? 0.1340 0.1441 0.1304 -0.0099 0.0141  0.0014  12  LEU   A CG  
269  C CD1 A LEU   A 12  ? 0.1671 0.1653 0.2115 0.0002  0.0142  0.0495  12  LEU   A CD1 
270  C CD1 B LEU   A 12  ? 0.1336 0.1457 0.1354 -0.0069 0.0208  0.0010  12  LEU   A CD1 
271  C CD2 A LEU   A 12  ? 0.1503 0.1655 0.2139 -0.0029 0.0076  0.0239  12  LEU   A CD2 
272  C CD2 B LEU   A 12  ? 0.1331 0.1445 0.1250 -0.0114 0.0102  -0.0030 12  LEU   A CD2 
295  N N   A THR   A 13  ? 0.1297 0.1378 0.1765 -0.0226 0.0114  0.0236  13  THR   A N   
296  N N   B THR   A 13  ? 0.1390 0.1458 0.1345 -0.0130 0.0140  0.0028  13  THR   A N   
297  C CA  A THR   A 13  ? 0.1354 0.1371 0.1847 -0.0215 0.0155  0.0253  13  THR   A CA  
298  C CA  B THR   A 13  ? 0.1408 0.1500 0.1437 -0.0153 0.0188  0.0065  13  THR   A CA  
299  C C   A THR   A 13  ? 0.1321 0.1342 0.1853 -0.0229 0.0134  0.0272  13  THR   A C   
300  C C   B THR   A 13  ? 0.1440 0.1515 0.1568 -0.0197 0.0190  0.0113  13  THR   A C   
301  O O   A THR   A 13  ? 0.1341 0.1367 0.1838 -0.0157 0.0103  0.0270  13  THR   A O   
302  O O   B THR   A 13  ? 0.1461 0.1531 0.1608 -0.0207 0.0192  0.0132  13  THR   A O   
303  C CB  A THR   A 13  ? 0.1380 0.1508 0.1968 -0.0165 0.0188  0.0304  13  THR   A CB  
304  C CB  B THR   A 13  ? 0.1390 0.1555 0.1442 -0.0113 0.0229  0.0086  13  THR   A CB  
305  O OG1 A THR   A 13  ? 0.1385 0.1502 0.2020 -0.0195 0.0117  0.0321  13  THR   A OG1 
306  O OG1 B THR   A 13  ? 0.1362 0.1587 0.1469 -0.0135 0.0302  0.0110  13  THR   A OG1 
307  C CG2 A THR   A 13  ? 0.1520 0.1746 0.2117 -0.0201 0.0276  0.0179  13  THR   A CG2 
308  C CG2 B THR   A 13  ? 0.1394 0.1587 0.1428 -0.0066 0.0225  0.0070  13  THR   A CG2 
323  N N   A ASP   A 14  ? 0.1361 0.1361 0.1983 -0.0203 0.0116  0.0320  14  ASP   A N   
324  N N   B ASP   A 14  ? 0.1449 0.1506 0.1706 -0.0206 0.0145  0.0149  14  ASP   A N   
325  C CA  A ASP   A 14  ? 0.1383 0.1422 0.2100 -0.0121 0.0032  0.0411  14  ASP   A CA  
326  C CA  B ASP   A 14  ? 0.1467 0.1503 0.1828 -0.0195 0.0098  0.0219  14  ASP   A CA  
327  C C   A ASP   A 14  ? 0.1405 0.1468 0.1876 -0.0162 -0.0058 0.0440  14  ASP   A C   
328  C C   B ASP   A 14  ? 0.1405 0.1455 0.1773 -0.0218 0.0067  0.0328  14  ASP   A C   
329  O O   A ASP   A 14  ? 0.1584 0.1650 0.2050 -0.0325 -0.0101 0.0507  14  ASP   A O   
330  O O   B ASP   A 14  ? 0.1433 0.1490 0.1777 -0.0279 0.0074  0.0351  14  ASP   A O   
331  C CB  A ASP   A 14  ? 0.1541 0.1660 0.2725 -0.0170 0.0089  0.0651  14  ASP   A CB  
332  C CB  B ASP   A 14  ? 0.1544 0.1530 0.2057 -0.0141 0.0055  0.0212  14  ASP   A CB  
333  C CG  A ASP   A 14  ? 0.1835 0.2249 0.3624 -0.0146 0.0119  0.0691  14  ASP   A CG  
334  C CG  B ASP   A 14  ? 0.1585 0.1603 0.2268 -0.0112 0.0006  0.0219  14  ASP   A CG  
335  O OD1 A ASP   A 14  ? 0.2066 0.2430 0.3894 -0.0007 -0.0038 0.0725  14  ASP   A OD1 
336  O OD1 B ASP   A 14  ? 0.1628 0.1639 0.2340 -0.0093 -0.0037 0.0194  14  ASP   A OD1 
337  O OD2 A ASP   A 14  ? 0.2053 0.2651 0.4098 -0.0056 0.0045  0.0547  14  ASP   A OD2 
338  O OD2 B ASP   A 14  ? 0.1598 0.1647 0.2323 -0.0077 -0.0052 0.0256  14  ASP   A OD2 
347  N N   . ASN   A 15  ? 0.1330 0.1397 0.1806 -0.0204 0.0059  0.0421  15  ASN   A N   
348  C CA  . ASN   A 15  ? 0.1313 0.1372 0.1939 -0.0171 -0.0023 0.0341  15  ASN   A CA  
349  C C   . ASN   A 15  ? 0.1326 0.1372 0.2088 -0.0151 0.0060  0.0300  15  ASN   A C   
350  O O   . ASN   A 15  ? 0.1358 0.1379 0.2585 -0.0151 -0.0170 0.0312  15  ASN   A O   
351  C CB  . ASN   A 15  ? 0.1278 0.1324 0.1960 -0.0119 0.0002  0.0285  15  ASN   A CB  
352  C CG  . ASN   A 15  ? 0.1310 0.1437 0.1987 -0.0081 0.0064  0.0266  15  ASN   A CG  
353  O OD1 . ASN   A 15  ? 0.1445 0.1525 0.2165 -0.0232 0.0094  0.0254  15  ASN   A OD1 
354  N ND2 . ASN   A 15  ? 0.1323 0.1561 0.1857 -0.0146 0.0163  0.0201  15  ASN   A ND2 
362  N N   A VAL   A 16  ? 0.1356 0.1301 0.1970 -0.0118 0.0078  0.0350  16  VAL   A N   
363  N N   B VAL   A 16  ? 0.1360 0.1391 0.1851 -0.0139 0.0050  0.0269  16  VAL   A N   
364  C CA  A VAL   A 16  ? 0.1313 0.1350 0.1881 -0.0085 0.0172  0.0397  16  VAL   A CA  
365  C CA  B VAL   A 16  ? 0.1398 0.1414 0.1634 -0.0133 0.0063  0.0248  16  VAL   A CA  
366  C C   A VAL   A 16  ? 0.1247 0.1330 0.1870 -0.0120 0.0086  0.0374  16  VAL   A C   
367  C C   B VAL   A 16  ? 0.1430 0.1408 0.1509 -0.0124 0.0032  0.0251  16  VAL   A C   
368  O O   A VAL   A 16  ? 0.1150 0.1341 0.1907 -0.0178 0.0130  0.0264  16  VAL   A O   
369  O O   B VAL   A 16  ? 0.1431 0.1424 0.1497 -0.0108 0.0050  0.0247  16  VAL   A O   
370  C CB  A VAL   A 16  ? 0.1397 0.1543 0.1939 0.0021  0.0296  0.0462  16  VAL   A CB  
371  C CB  B VAL   A 16  ? 0.1409 0.1454 0.1573 -0.0136 0.0100  0.0219  16  VAL   A CB  
372  C CG1 A VAL   A 16  ? 0.1493 0.1644 0.2041 0.0114  0.0315  0.0485  16  VAL   A CG1 
373  C CG1 B VAL   A 16  ? 0.1426 0.1482 0.1579 -0.0115 0.0093  0.0220  16  VAL   A CG1 
374  C CG2 A VAL   A 16  ? 0.1460 0.1677 0.2147 0.0084  0.0433  0.0471  16  VAL   A CG2 
375  C CG2 B VAL   A 16  ? 0.1400 0.1473 0.1589 -0.0151 0.0114  0.0174  16  VAL   A CG2 
394  N N   A TYR   A 17  ? 0.1232 0.1275 0.1896 -0.0123 0.0203  0.0334  17  TYR   A N   
395  N N   B TYR   A 17  ? 0.1448 0.1378 0.1412 -0.0136 0.0015  0.0221  17  TYR   A N   
396  C CA  A TYR   A 17  ? 0.1269 0.1332 0.1808 -0.0139 0.0169  0.0404  17  TYR   A CA  
397  C CA  B TYR   A 17  ? 0.1452 0.1347 0.1328 -0.0170 0.0006  0.0214  17  TYR   A CA  
398  C C   A TYR   A 17  ? 0.1279 0.1268 0.1990 -0.0103 0.0203  0.0328  17  TYR   A C   
399  C C   B TYR   A 17  ? 0.1450 0.1378 0.1274 -0.0134 0.0009  0.0214  17  TYR   A C   
400  O O   A TYR   A 17  ? 0.1215 0.1334 0.2084 -0.0125 0.0232  0.0446  17  TYR   A O   
401  O O   B TYR   A 17  ? 0.1443 0.1399 0.1309 -0.0132 0.0009  0.0287  17  TYR   A O   
402  C CB  A TYR   A 17  ? 0.1441 0.1366 0.1806 -0.0164 0.0106  0.0341  17  TYR   A CB  
403  C CB  B TYR   A 17  ? 0.1491 0.1300 0.1343 -0.0199 -0.0019 0.0179  17  TYR   A CB  
404  C CG  A TYR   A 17  ? 0.1622 0.1498 0.1840 -0.0192 0.0004  0.0271  17  TYR   A CG  
405  C CG  B TYR   A 17  ? 0.1529 0.1269 0.1356 -0.0244 -0.0051 0.0140  17  TYR   A CG  
406  C CD1 A TYR   A 17  ? 0.1685 0.1570 0.1917 -0.0052 0.0034  0.0303  17  TYR   A CD1 
407  C CD1 B TYR   A 17  ? 0.1538 0.1262 0.1365 -0.0241 -0.0041 0.0173  17  TYR   A CD1 
408  C CD2 A TYR   A 17  ? 0.1753 0.1573 0.1762 -0.0294 0.0083  0.0271  17  TYR   A CD2 
409  C CD2 B TYR   A 17  ? 0.1563 0.1252 0.1344 -0.0292 -0.0056 0.0125  17  TYR   A CD2 
410  C CE1 A TYR   A 17  ? 0.1865 0.1581 0.1977 -0.0069 -0.0015 0.0282  17  TYR   A CE1 
411  C CE1 B TYR   A 17  ? 0.1555 0.1240 0.1385 -0.0269 -0.0055 0.0176  17  TYR   A CE1 
412  C CE2 A TYR   A 17  ? 0.1897 0.1595 0.1798 -0.0288 0.0062  0.0147  17  TYR   A CE2 
413  C CE2 B TYR   A 17  ? 0.1595 0.1239 0.1366 -0.0314 -0.0091 0.0093  17  TYR   A CE2 
414  C CZ  A TYR   A 17  ? 0.1949 0.1568 0.1910 -0.0170 -0.0035 0.0273  17  TYR   A CZ  
415  C CZ  B TYR   A 17  ? 0.1596 0.1217 0.1380 -0.0319 -0.0088 0.0146  17  TYR   A CZ  
416  O OH  A TYR   A 17  ? 0.2064 0.1626 0.2018 -0.0098 0.0028  0.0357  17  TYR   A OH  
417  O OH  B TYR   A 17  ? 0.1646 0.1186 0.1375 -0.0342 -0.0125 0.0154  17  TYR   A OH  
436  N N   A ILE   A 18  ? 0.1297 0.1284 0.1974 -0.0106 0.0239  0.0367  18  ILE   A N   
437  N N   B ILE   A 18  ? 0.1423 0.1409 0.1197 -0.0121 0.0008  0.0156  18  ILE   A N   
438  C CA  A ILE   A 18  ? 0.1349 0.1321 0.2008 -0.0089 0.0235  0.0305  18  ILE   A CA  
439  C CA  B ILE   A 18  ? 0.1395 0.1459 0.1130 -0.0074 0.0034  0.0079  18  ILE   A CA  
440  C C   A ILE   A 18  ? 0.1315 0.1383 0.2039 -0.0144 0.0216  0.0308  18  ILE   A C   
441  C C   B ILE   A 18  ? 0.1398 0.1539 0.1047 -0.0021 -0.0002 0.0042  18  ILE   A C   
442  O O   A ILE   A 18  ? 0.1314 0.1519 0.2083 -0.0204 0.0298  0.0409  18  ILE   A O   
443  O O   B ILE   A 18  ? 0.1396 0.1577 0.1019 -0.0039 0.0011  0.0065  18  ILE   A O   
444  C CB  A ILE   A 18  ? 0.1467 0.1415 0.1869 -0.0032 0.0194  0.0455  18  ILE   A CB  
445  C CB  B ILE   A 18  ? 0.1358 0.1458 0.1099 -0.0093 0.0084  0.0097  18  ILE   A CB  
446  C CG1 A ILE   A 18  ? 0.1558 0.1517 0.1917 0.0006  0.0151  0.0535  18  ILE   A CG1 
447  C CG1 B ILE   A 18  ? 0.1373 0.1478 0.1162 -0.0115 0.0164  0.0124  18  ILE   A CG1 
448  C CG2 A ILE   A 18  ? 0.1504 0.1429 0.1934 -0.0112 0.0200  0.0396  18  ILE   A CG2 
449  C CG2 B ILE   A 18  ? 0.1361 0.1487 0.1109 -0.0100 0.0037  0.0121  18  ILE   A CG2 
450  C CD1 A ILE   A 18  ? 0.1821 0.1700 0.2151 0.0065  0.0003  0.0543  18  ILE   A CD1 
451  C CD1 B ILE   A 18  ? 0.1383 0.1502 0.1256 -0.0132 0.0198  0.0111  18  ILE   A CD1 
474  N N   A LYS   A 19  ? 0.1347 0.1416 0.2161 -0.0089 0.0369  0.0312  19  LYS   A N   
475  N N   B LYS   A 19  ? 0.1429 0.1584 0.1086 0.0043  0.0007  -0.0022 19  LYS   A N   
476  C CA  A LYS   A 19  ? 0.1500 0.1503 0.2446 -0.0008 0.0445  0.0370  19  LYS   A CA  
477  C CA  B LYS   A 19  ? 0.1479 0.1645 0.1214 0.0107  -0.0005 -0.0067 19  LYS   A CA  
478  C C   A LYS   A 19  ? 0.1407 0.1493 0.2758 0.0025  0.0487  0.0443  19  LYS   A C   
479  C C   B LYS   A 19  ? 0.1491 0.1654 0.1315 0.0172  0.0016  -0.0118 19  LYS   A C   
480  O O   A LYS   A 19  ? 0.1396 0.1480 0.2785 -0.0015 0.0413  0.0506  19  LYS   A O   
481  O O   B LYS   A 19  ? 0.1498 0.1637 0.1256 0.0188  0.0013  -0.0138 19  LYS   A O   
482  C CB  A LYS   A 19  ? 0.1589 0.1648 0.2542 -0.0090 0.0546  0.0269  19  LYS   A CB  
483  C CB  B LYS   A 19  ? 0.1505 0.1698 0.1301 0.0099  0.0010  -0.0078 19  LYS   A CB  
484  C CG  A LYS   A 19  ? 0.1906 0.1828 0.2573 -0.0082 0.0587  0.0060  19  LYS   A CG  
485  C CG  B LYS   A 19  ? 0.1538 0.1752 0.1420 0.0091  -0.0016 -0.0089 19  LYS   A CG  
486  C CD  A LYS   A 19  ? 0.2208 0.2073 0.2569 -0.0127 0.0645  0.0024  19  LYS   A CD  
487  C CD  B LYS   A 19  ? 0.1569 0.1797 0.1522 0.0063  -0.0026 -0.0072 19  LYS   A CD  
488  C CE  A LYS   A 19  ? 0.2431 0.2197 0.2682 -0.0184 0.0614  -0.0073 19  LYS   A CE  
489  C CE  B LYS   A 19  ? 0.1599 0.1836 0.1602 0.0032  -0.0055 -0.0066 19  LYS   A CE  
490  N NZ  A LYS   A 19  ? 0.2549 0.2277 0.2643 -0.0300 0.0704  -0.0178 19  LYS   A NZ  
491  N NZ  B LYS   A 19  ? 0.1646 0.1856 0.1673 -0.0013 -0.0028 -0.0065 19  LYS   A NZ  
518  N N   A ASN   A 20  ? 0.1443 0.1504 0.3154 0.0003  0.0473  0.0554  20  ASN   A N   
519  N N   B ASN   A 20  ? 0.1526 0.1698 0.1588 0.0196  0.0070  -0.0123 20  ASN   A N   
520  C CA  A ASN   A 20  ? 0.1588 0.1693 0.3471 0.0216  0.0644  0.0554  20  ASN   A CA  
521  C CA  B ASN   A 20  ? 0.1562 0.1749 0.1890 0.0191  0.0113  -0.0123 20  ASN   A CA  
522  C C   A ASN   A 20  ? 0.1755 0.1679 0.3506 0.0181  0.0782  0.0430  20  ASN   A C   
523  C C   B ASN   A 20  ? 0.1607 0.1770 0.1971 0.0153  0.0194  -0.0093 20  ASN   A C   
524  O O   A ASN   A 20  ? 0.2010 0.1789 0.3571 0.0043  0.0796  0.0320  20  ASN   A O   
525  O O   B ASN   A 20  ? 0.1592 0.1777 0.2041 0.0181  0.0241  -0.0099 20  ASN   A O   
526  C CB  A ASN   A 20  ? 0.1655 0.1842 0.3750 0.0326  0.0683  0.0732  20  ASN   A CB  
527  C CB  B ASN   A 20  ? 0.1554 0.1761 0.2099 0.0207  0.0088  -0.0134 20  ASN   A CB  
528  C CG  A ASN   A 20  ? 0.1809 0.1940 0.4171 0.0467  0.0688  0.0865  20  ASN   A CG  
529  C CG  B ASN   A 20  ? 0.1563 0.1771 0.2301 0.0211  0.0077  -0.0156 20  ASN   A CG  
530  O OD1 A ASN   A 20  ? 0.2066 0.2087 0.4572 0.0499  0.0836  0.0798  20  ASN   A OD1 
531  O OD1 B ASN   A 20  ? 0.1558 0.1775 0.2396 0.0202  0.0102  -0.0195 20  ASN   A OD1 
532  N ND2 A ASN   A 20  ? 0.1875 0.1929 0.4287 0.0431  0.0528  0.0922  20  ASN   A ND2 
533  N ND2 B ASN   A 20  ? 0.1605 0.1777 0.2377 0.0218  0.0064  -0.0132 20  ASN   A ND2 
546  N N   A ALA   A 21  ? 0.1788 0.1690 0.3520 0.0142  0.0659  0.0334  21  ALA   A N   
547  N N   B ALA   A 21  ? 0.1654 0.1781 0.1983 0.0090  0.0173  -0.0075 21  ALA   A N   
548  C CA  A ALA   A 21  ? 0.1780 0.1672 0.3437 0.0059  0.0661  0.0325  21  ALA   A CA  
549  C CA  B ALA   A 21  ? 0.1697 0.1788 0.2008 0.0028  0.0197  -0.0063 21  ALA   A CA  
550  C C   A ALA   A 21  ? 0.1732 0.1672 0.3352 0.0043  0.0626  0.0343  21  ALA   A C   
551  C C   B ALA   A 21  ? 0.1719 0.1787 0.2006 -0.0009 0.0226  -0.0038 21  ALA   A C   
552  O O   A ALA   A 21  ? 0.1786 0.1706 0.3327 0.0035  0.0577  0.0360  21  ALA   A O   
553  O O   B ALA   A 21  ? 0.1715 0.1747 0.1972 -0.0027 0.0277  -0.0034 21  ALA   A O   
554  C CB  A ALA   A 21  ? 0.1965 0.1750 0.3537 -0.0022 0.0521  0.0387  21  ALA   A CB  
555  C CB  B ALA   A 21  ? 0.1697 0.1788 0.2037 0.0037  0.0199  -0.0069 21  ALA   A CB  
566  N N   A ASP   A 22  ? 0.1784 0.1667 0.3374 -0.0032 0.0527  0.0360  22  ASP   A N   
567  N N   B ASP   A 22  ? 0.1760 0.1830 0.2029 -0.0045 0.0220  -0.0007 22  ASP   A N   
568  C CA  A ASP   A 22  ? 0.1805 0.1706 0.3225 -0.0058 0.0450  0.0349  22  ASP   A CA  
569  C CA  B ASP   A 22  ? 0.1799 0.1871 0.2023 -0.0081 0.0198  -0.0005 22  ASP   A CA  
570  C C   A ASP   A 22  ? 0.1693 0.1801 0.2701 -0.0134 0.0546  0.0360  22  ASP   A C   
571  C C   B ASP   A 22  ? 0.1777 0.1853 0.1901 -0.0138 0.0194  0.0026  22  ASP   A C   
572  O O   A ASP   A 22  ? 0.1791 0.1910 0.2731 -0.0141 0.0590  0.0356  22  ASP   A O   
573  O O   B ASP   A 22  ? 0.1775 0.1822 0.1906 -0.0158 0.0182  -0.0004 22  ASP   A O   
574  C CB  A ASP   A 22  ? 0.2024 0.1742 0.3773 -0.0014 0.0366  0.0261  22  ASP   A CB  
575  C CB  B ASP   A 22  ? 0.1859 0.1913 0.2157 -0.0052 0.0203  -0.0016 22  ASP   A CB  
576  C CG  A ASP   A 22  ? 0.2203 0.1784 0.4288 -0.0075 0.0169  0.0359  22  ASP   A CG  
577  C CG  B ASP   A 22  ? 0.1891 0.1925 0.2254 -0.0036 0.0194  -0.0005 22  ASP   A CG  
578  O OD1 A ASP   A 22  ? 0.2131 0.1752 0.4426 -0.0270 0.0032  0.0557  22  ASP   A OD1 
579  O OD1 B ASP   A 22  ? 0.1908 0.1905 0.2262 -0.0016 0.0192  0.0007  22  ASP   A OD1 
580  O OD2 A ASP   A 22  ? 0.2457 0.1873 0.4618 0.0034  0.0204  0.0284  22  ASP   A OD2 
581  O OD2 B ASP   A 22  ? 0.1890 0.1953 0.2302 -0.0047 0.0187  -0.0003 22  ASP   A OD2 
590  N N   A ILE   A 23  ? 0.1691 0.1848 0.2348 -0.0075 0.0453  0.0296  23  ILE   A N   
591  N N   B ILE   A 23  ? 0.1778 0.1882 0.1800 -0.0146 0.0168  0.0074  23  ILE   A N   
592  C CA  A ILE   A 23  ? 0.1662 0.1763 0.2032 -0.0138 0.0420  0.0266  23  ILE   A CA  
593  C CA  B ILE   A 23  ? 0.1781 0.1915 0.1735 -0.0170 0.0118  0.0115  23  ILE   A CA  
594  C C   A ILE   A 23  ? 0.1657 0.1838 0.1979 -0.0100 0.0554  0.0135  23  ILE   A C   
595  C C   B ILE   A 23  ? 0.1832 0.1977 0.1797 -0.0181 0.0145  0.0102  23  ILE   A C   
596  O O   A ILE   A 23  ? 0.1729 0.1875 0.1972 -0.0019 0.0516  0.0098  23  ILE   A O   
597  O O   B ILE   A 23  ? 0.1826 0.1957 0.1780 -0.0177 0.0155  0.0097  23  ILE   A O   
598  C CB  A ILE   A 23  ? 0.1756 0.1740 0.1784 -0.0112 0.0305  0.0238  23  ILE   A CB  
599  C CB  B ILE   A 23  ? 0.1745 0.1881 0.1606 -0.0171 0.0056  0.0138  23  ILE   A CB  
600  C CG1 A ILE   A 23  ? 0.1862 0.1771 0.1655 -0.0099 0.0267  0.0139  23  ILE   A CG1 
601  C CG1 B ILE   A 23  ? 0.1721 0.1864 0.1552 -0.0182 0.0011  0.0119  23  ILE   A CG1 
602  C CG2 A ILE   A 23  ? 0.1776 0.1722 0.1848 -0.0094 0.0318  0.0308  23  ILE   A CG2 
603  C CG2 B ILE   A 23  ? 0.1745 0.1868 0.1586 -0.0159 0.0053  0.0147  23  ILE   A CG2 
604  C CD1 A ILE   A 23  ? 0.1919 0.1759 0.1640 -0.0116 0.0190  0.0018  23  ILE   A CD1 
605  C CD1 B ILE   A 23  ? 0.1702 0.1853 0.1543 -0.0181 -0.0020 0.0109  23  ILE   A CD1 
628  N N   A VAL   A 24  ? 0.1788 0.1907 0.2178 -0.0230 0.0578  0.0135  24  VAL   A N   
629  N N   B VAL   A 24  ? 0.1904 0.2063 0.1933 -0.0186 0.0136  0.0099  24  VAL   A N   
630  C CA  A VAL   A 24  ? 0.1978 0.2008 0.2405 -0.0279 0.0572  0.0048  24  VAL   A CA  
631  C CA  B VAL   A 24  ? 0.1990 0.2141 0.2047 -0.0170 0.0136  0.0092  24  VAL   A CA  
632  C C   A VAL   A 24  ? 0.2068 0.2157 0.2445 -0.0318 0.0619  -0.0056 24  VAL   A C   
633  C C   B VAL   A 24  ? 0.2069 0.2223 0.2132 -0.0176 0.0165  0.0050  24  VAL   A C   
634  O O   A VAL   A 24  ? 0.2140 0.2134 0.2430 -0.0226 0.0646  -0.0109 24  VAL   A O   
635  O O   B VAL   A 24  ? 0.2076 0.2222 0.2118 -0.0156 0.0169  0.0050  24  VAL   A O   
636  C CB  A VAL   A 24  ? 0.2068 0.2065 0.2657 -0.0331 0.0603  0.0132  24  VAL   A CB  
637  C CB  B VAL   A 24  ? 0.1991 0.2154 0.2102 -0.0153 0.0115  0.0133  24  VAL   A CB  
638  C CG1 A VAL   A 24  ? 0.2174 0.2163 0.2820 -0.0300 0.0527  0.0033  24  VAL   A CG1 
639  C CG1 B VAL   A 24  ? 0.2013 0.2162 0.2132 -0.0141 0.0089  0.0141  24  VAL   A CG1 
640  C CG2 A VAL   A 24  ? 0.2191 0.2147 0.2784 -0.0254 0.0713  0.0264  24  VAL   A CG2 
641  C CG2 B VAL   A 24  ? 0.1991 0.2162 0.2110 -0.0141 0.0115  0.0147  24  VAL   A CG2 
660  N N   A GLU   A 25  ? 0.2131 0.2465 0.2512 -0.0364 0.0790  -0.0167 25  GLU   A N   
661  N N   B GLU   A 25  ? 0.2137 0.2308 0.2248 -0.0205 0.0210  0.0013  25  GLU   A N   
662  C CA  A GLU   A 25  ? 0.2310 0.2759 0.2609 -0.0339 0.0963  -0.0188 25  GLU   A CA  
663  C CA  B GLU   A 25  ? 0.2212 0.2392 0.2387 -0.0251 0.0248  0.0001  25  GLU   A CA  
664  C C   A GLU   A 25  ? 0.2239 0.2771 0.2343 -0.0460 0.0985  -0.0171 25  GLU   A C   
665  C C   B GLU   A 25  ? 0.2190 0.2405 0.2276 -0.0318 0.0292  -0.0009 25  GLU   A C   
666  O O   A GLU   A 25  ? 0.2331 0.2850 0.2410 -0.0490 0.0979  -0.0136 25  GLU   A O   
667  O O   B GLU   A 25  ? 0.2202 0.2417 0.2284 -0.0322 0.0269  -0.0027 25  GLU   A O   
668  C CB  A GLU   A 25  ? 0.2561 0.3027 0.3009 -0.0239 0.1049  -0.0159 25  GLU   A CB  
669  C CB  B GLU   A 25  ? 0.2297 0.2449 0.2631 -0.0233 0.0243  0.0009  25  GLU   A CB  
670  C CG  A GLU   A 25  ? 0.2868 0.3270 0.3578 -0.0195 0.0917  -0.0157 25  GLU   A CG  
671  C CG  B GLU   A 25  ? 0.2384 0.2504 0.2888 -0.0220 0.0222  0.0019  25  GLU   A CG  
672  C CD  A GLU   A 25  ? 0.3106 0.3495 0.4060 -0.0174 0.0832  -0.0140 25  GLU   A CD  
673  C CD  B GLU   A 25  ? 0.2448 0.2548 0.3097 -0.0210 0.0200  0.0024  25  GLU   A CD  
674  O OE1 A GLU   A 25  ? 0.3206 0.3588 0.4169 -0.0140 0.0717  -0.0204 25  GLU   A OE1 
675  O OE1 B GLU   A 25  ? 0.2468 0.2558 0.3160 -0.0199 0.0196  0.0031  25  GLU   A OE1 
676  O OE2 A GLU   A 25  ? 0.3194 0.3566 0.4330 -0.0165 0.0810  -0.0202 25  GLU   A OE2 
677  O OE2 B GLU   A 25  ? 0.2472 0.2559 0.3181 -0.0218 0.0206  0.0020  25  GLU   A OE2 
690  N N   A GLU   A 26  ? 0.2161 0.2679 0.2331 -0.0588 0.0970  -0.0186 26  GLU   A N   
691  N N   B GLU   A 26  ? 0.2164 0.2397 0.2174 -0.0391 0.0378  -0.0021 26  GLU   A N   
692  C CA  A GLU   A 26  ? 0.2273 0.2582 0.2119 -0.0704 0.0896  -0.0077 26  GLU   A CA  
693  C CA  B GLU   A 26  ? 0.2154 0.2381 0.2070 -0.0456 0.0441  -0.0019 26  GLU   A CA  
694  C C   A GLU   A 26  ? 0.2207 0.2402 0.1824 -0.0691 0.0763  -0.0072 26  GLU   A C   
695  C C   B GLU   A 26  ? 0.2111 0.2313 0.1908 -0.0535 0.0555  -0.0062 26  GLU   A C   
696  O O   A GLU   A 26  ? 0.2268 0.2393 0.1762 -0.0761 0.0696  -0.0094 26  GLU   A O   
697  O O   B GLU   A 26  ? 0.2125 0.2311 0.1902 -0.0512 0.0590  -0.0067 26  GLU   A O   
698  C CB  A GLU   A 26  ? 0.2526 0.2553 0.2512 -0.0820 0.0778  0.0046  26  GLU   A CB  
699  C CB  B GLU   A 26  ? 0.2191 0.2416 0.2146 -0.0452 0.0349  0.0018  26  GLU   A CB  
700  C CG  A GLU   A 26  ? 0.2755 0.2602 0.3060 -0.0870 0.0814  -0.0023 26  GLU   A CG  
701  C CG  B GLU   A 26  ? 0.2222 0.2444 0.2209 -0.0442 0.0306  0.0027  26  GLU   A CG  
702  C CD  A GLU   A 26  ? 0.2879 0.2592 0.3341 -0.0948 0.1060  -0.0074 26  GLU   A CD  
703  C CD  B GLU   A 26  ? 0.2241 0.2457 0.2236 -0.0438 0.0284  0.0034  26  GLU   A CD  
704  O OE1 A GLU   A 26  ? 0.2791 0.2863 0.3271 -0.0740 0.1388  -0.0530 26  GLU   A OE1 
705  O OE1 B GLU   A 26  ? 0.2278 0.2514 0.2325 -0.0366 0.0305  0.0024  26  GLU   A OE1 
706  O OE2 A GLU   A 26  ? 0.3067 0.2586 0.3475 -0.0915 0.1011  0.0010  26  GLU   A OE2 
707  O OE2 B GLU   A 26  ? 0.2220 0.2435 0.2132 -0.0483 0.0273  0.0021  26  GLU   A OE2 
720  N N   . ALA   A 27  ? 0.2051 0.2247 0.1776 -0.0627 0.0624  -0.0107 27  ALA   A N   
721  C CA  . ALA   A 27  ? 0.2114 0.2223 0.1628 -0.0546 0.0598  -0.0137 27  ALA   A CA  
722  C C   . ALA   A 27  ? 0.2414 0.2349 0.1755 -0.0628 0.0686  -0.0300 27  ALA   A C   
723  O O   . ALA   A 27  ? 0.2466 0.2311 0.1824 -0.0651 0.0540  -0.0257 27  ALA   A O   
724  C CB  . ALA   A 27  ? 0.1933 0.2101 0.1651 -0.0528 0.0474  -0.0095 27  ALA   A CB  
731  N N   . LYS   A 28  ? 0.2765 0.2587 0.1934 -0.0606 0.0736  -0.0595 28  LYS   A N   
732  C CA  . LYS   A 28  ? 0.3210 0.2986 0.2353 -0.0540 0.0709  -0.0752 28  LYS   A CA  
733  C C   . LYS   A 28  ? 0.3402 0.3320 0.2245 -0.0603 0.0831  -0.0623 28  LYS   A C   
734  O O   . LYS   A 28  ? 0.3474 0.3421 0.2630 -0.0576 0.0643  -0.0552 28  LYS   A O   
735  C CB  . LYS   A 28  ? 0.3439 0.3146 0.2888 -0.0374 0.0642  -0.0892 28  LYS   A CB  
736  C CG  . LYS   A 28  ? 0.3616 0.3304 0.3436 -0.0259 0.0590  -0.0912 28  LYS   A CG  
737  C CD  . LYS   A 28  ? 0.3765 0.3516 0.4073 -0.0172 0.0529  -0.0875 28  LYS   A CD  
738  C CE  . LYS   A 28  ? 0.3890 0.3661 0.4524 -0.0141 0.0479  -0.0872 28  LYS   A CE  
739  N NZ  . LYS   A 28  ? 0.3986 0.3737 0.4803 -0.0100 0.0475  -0.0836 28  LYS   A NZ  
753  N N   . LYS   A 29  ? 0.3478 0.3549 0.2037 -0.0721 0.1130  -0.0416 29  LYS   A N   
754  C CA  . LYS   A 29  ? 0.3669 0.3814 0.2309 -0.0793 0.1197  -0.0238 29  LYS   A CA  
755  C C   . LYS   A 29  ? 0.3642 0.3698 0.1929 -0.0882 0.1111  -0.0214 29  LYS   A C   
756  O O   . LYS   A 29  ? 0.3764 0.3794 0.2085 -0.0796 0.1043  -0.0237 29  LYS   A O   
757  C CB  . LYS   A 29  ? 0.3839 0.4150 0.2981 -0.0758 0.1317  -0.0112 29  LYS   A CB  
758  C CG  . LYS   A 29  ? 0.4029 0.4419 0.3773 -0.0708 0.1306  -0.0059 29  LYS   A CG  
759  C CD  . LYS   A 29  ? 0.4206 0.4645 0.4533 -0.0654 0.1254  -0.0057 29  LYS   A CD  
760  C CE  . LYS   A 29  ? 0.4329 0.4817 0.5073 -0.0617 0.1228  -0.0061 29  LYS   A CE  
761  N NZ  . LYS   A 29  ? 0.4385 0.4924 0.5382 -0.0598 0.1222  -0.0072 29  LYS   A NZ  
775  N N   . VAL   A 30  ? 0.3463 0.3479 0.1782 -0.1042 0.1027  -0.0150 30  VAL   A N   
776  C CA  . VAL   A 30  ? 0.3379 0.3296 0.1714 -0.1149 0.0732  0.0051  30  VAL   A CA  
777  C C   . VAL   A 30  ? 0.3360 0.3139 0.1388 -0.1142 0.0564  0.0137  30  VAL   A C   
778  O O   . VAL   A 30  ? 0.3441 0.3170 0.1421 -0.1137 0.0472  0.0188  30  VAL   A O   
779  C CB  . VAL   A 30  ? 0.3338 0.3267 0.2081 -0.1243 0.0499  0.0108  30  VAL   A CB  
780  C CG1 . VAL   A 30  ? 0.3368 0.3258 0.2217 -0.1251 0.0312  0.0132  30  VAL   A CG1 
781  C CG2 . VAL   A 30  ? 0.3320 0.3288 0.2380 -0.1261 0.0519  0.0115  30  VAL   A CG2 
791  N N   . LYS   A 31  ? 0.3234 0.2948 0.1269 -0.1116 0.0395  0.0022  31  LYS   A N   
792  C CA  . LYS   A 31  ? 0.3319 0.2916 0.1331 -0.0989 0.0164  -0.0037 31  LYS   A CA  
793  C C   . LYS   A 31  ? 0.3080 0.2671 0.1003 -0.0762 0.0078  0.0312  31  LYS   A C   
794  O O   . LYS   A 31  ? 0.3142 0.2750 0.1215 -0.0719 -0.0148 0.0462  31  LYS   A O   
795  C CB  . LYS   A 31  ? 0.3716 0.3210 0.2464 -0.0925 -0.0050 -0.0308 31  LYS   A CB  
796  C CG  . LYS   A 31  ? 0.4138 0.3545 0.3863 -0.0788 -0.0224 -0.0433 31  LYS   A CG  
797  C CD  . LYS   A 31  ? 0.4459 0.3844 0.4931 -0.0694 -0.0383 -0.0522 31  LYS   A CD  
798  C CE  . LYS   A 31  ? 0.4670 0.4043 0.5607 -0.0644 -0.0525 -0.0618 31  LYS   A CE  
799  N NZ  . LYS   A 31  ? 0.4782 0.4097 0.5970 -0.0621 -0.0589 -0.0675 31  LYS   A NZ  
813  N N   . PRO   A 32  ? 0.2722 0.2381 0.0871 -0.0652 0.0106  0.0232  32  PRO   A N   
814  C CA  . PRO   A 32  ? 0.2658 0.2222 0.1162 -0.0618 -0.0031 0.0290  32  PRO   A CA  
815  C C   . PRO   A 32  ? 0.2570 0.2165 0.1295 -0.0535 -0.0121 0.0384  32  PRO   A C   
816  O O   . PRO   A 32  ? 0.2518 0.2109 0.1383 -0.0564 -0.0257 0.0394  32  PRO   A O   
817  C CB  . PRO   A 32  ? 0.2568 0.2263 0.1326 -0.0596 -0.0068 0.0213  32  PRO   A CB  
818  C CG  . PRO   A 32  ? 0.2538 0.2307 0.0931 -0.0538 -0.0070 0.0187  32  PRO   A CG  
819  C CD  . PRO   A 32  ? 0.2600 0.2321 0.0828 -0.0597 0.0059  0.0174  32  PRO   A CD  
827  N N   . THR   A 33  ? 0.2606 0.2115 0.1275 -0.0515 -0.0141 0.0434  33  THR   A N   
828  C CA  . THR   A 33  ? 0.2572 0.2135 0.1392 -0.0377 -0.0265 0.0440  33  THR   A CA  
829  C C   . THR   A 33  ? 0.2241 0.1961 0.1349 -0.0393 -0.0270 0.0327  33  THR   A C   
830  O O   . THR   A 33  ? 0.2160 0.2013 0.1393 -0.0378 -0.0384 0.0336  33  THR   A O   
831  C CB  . THR   A 33  ? 0.2846 0.2308 0.1535 -0.0293 -0.0363 0.0622  33  THR   A CB  
832  O OG1 . THR   A 33  ? 0.3067 0.2448 0.1861 -0.0179 -0.0283 0.0728  33  THR   A OG1 
833  C CG2 . THR   A 33  ? 0.2884 0.2389 0.1773 -0.0226 -0.0424 0.0602  33  THR   A CG2 
841  N N   . VAL   A 34  ? 0.1980 0.1820 0.1205 -0.0354 -0.0201 0.0291  34  VAL   A N   
842  C CA  . VAL   A 34  ? 0.1779 0.1644 0.1118 -0.0290 -0.0091 0.0314  34  VAL   A CA  
843  C C   . VAL   A 34  ? 0.1621 0.1608 0.1051 -0.0250 -0.0016 0.0209  34  VAL   A C   
844  O O   . VAL   A 34  ? 0.1643 0.1623 0.1342 -0.0309 -0.0003 0.0280  34  VAL   A O   
845  C CB  . VAL   A 34  ? 0.1818 0.1596 0.1368 -0.0249 -0.0049 0.0216  34  VAL   A CB  
846  C CG1 . VAL   A 34  ? 0.1854 0.1596 0.1393 -0.0241 0.0079  0.0097  34  VAL   A CG1 
847  C CG2 . VAL   A 34  ? 0.1881 0.1694 0.1658 -0.0110 -0.0142 0.0175  34  VAL   A CG2 
857  N N   . VAL   A 35  ? 0.1514 0.1505 0.1005 -0.0240 -0.0009 0.0160  35  VAL   A N   
858  C CA  . VAL   A 35  ? 0.1437 0.1481 0.0964 -0.0251 0.0033  0.0123  35  VAL   A CA  
859  C C   . VAL   A 35  ? 0.1319 0.1348 0.1081 -0.0193 0.0022  0.0155  35  VAL   A C   
860  O O   . VAL   A 35  ? 0.1309 0.1453 0.1213 -0.0237 0.0083  0.0079  35  VAL   A O   
861  C CB  . VAL   A 35  ? 0.1498 0.1520 0.1178 -0.0175 0.0144  -0.0011 35  VAL   A CB  
862  C CG1 . VAL   A 35  ? 0.1583 0.1542 0.1289 -0.0082 0.0082  -0.0093 35  VAL   A CG1 
863  C CG2 . VAL   A 35  ? 0.1499 0.1540 0.1463 -0.0108 0.0205  -0.0059 35  VAL   A CG2 
873  N N   . VAL   A 36  ? 0.1242 0.1356 0.0980 -0.0190 0.0095  0.0151  36  VAL   A N   
874  C CA  . VAL   A 36  ? 0.1205 0.1240 0.1078 -0.0087 0.0041  0.0083  36  VAL   A CA  
875  C C   . VAL   A 36  ? 0.1172 0.1246 0.1110 -0.0140 0.0107  0.0088  36  VAL   A C   
876  O O   . VAL   A 36  ? 0.1222 0.1246 0.1393 -0.0029 0.0211  0.0102  36  VAL   A O   
877  C CB  . VAL   A 36  ? 0.1216 0.1159 0.1177 -0.0115 0.0040  0.0073  36  VAL   A CB  
878  C CG1 . VAL   A 36  ? 0.1249 0.1216 0.1293 -0.0167 0.0039  -0.0036 36  VAL   A CG1 
879  C CG2 . VAL   A 36  ? 0.1334 0.1200 0.1313 -0.0075 -0.0031 0.0153  36  VAL   A CG2 
889  N N   . ASN   A 37  ? 0.1119 0.1164 0.1066 -0.0049 0.0045  0.0100  37  ASN   A N   
890  C CA  . ASN   A 37  ? 0.1095 0.1158 0.1040 0.0014  0.0058  0.0149  37  ASN   A CA  
891  C C   . ASN   A 37  ? 0.1125 0.1134 0.1062 -0.0039 0.0131  0.0213  37  ASN   A C   
892  O O   . ASN   A 37  ? 0.1211 0.1193 0.1063 0.0061  0.0084  0.0095  37  ASN   A O   
893  C CB  . ASN   A 37  ? 0.1167 0.1164 0.1181 -0.0015 0.0023  0.0097  37  ASN   A CB  
894  C CG  . ASN   A 37  ? 0.1165 0.1155 0.1262 0.0009  0.0081  0.0095  37  ASN   A CG  
895  O OD1 . ASN   A 37  ? 0.1154 0.1172 0.1483 0.0011  0.0105  0.0142  37  ASN   A OD1 
896  N ND2 . ASN   A 37  ? 0.1173 0.1185 0.1316 -0.0011 0.0010  0.0255  37  ASN   A ND2 
903  N N   A ALA   A 38  ? 0.1137 0.1227 0.1153 0.0000  0.0120  0.0097  38  ALA   A N   
904  N N   B ALA   A 38  ? 0.1142 0.1182 0.1114 -0.0052 0.0068  0.0172  38  ALA   A N   
905  C CA  A ALA   A 38  ? 0.1172 0.1282 0.1206 -0.0045 0.0018  0.0059  38  ALA   A CA  
906  C CA  B ALA   A 38  ? 0.1173 0.1234 0.1194 -0.0084 0.0000  0.0166  38  ALA   A CA  
907  C C   A ALA   A 38  ? 0.1137 0.1293 0.1107 0.0037  -0.0072 0.0001  38  ALA   A C   
908  C C   B ALA   A 38  ? 0.1170 0.1250 0.1226 -0.0058 -0.0061 0.0127  38  ALA   A C   
909  O O   A ALA   A 38  ? 0.1094 0.1233 0.1268 0.0043  -0.0093 0.0042  38  ALA   A O   
910  O O   B ALA   A 38  ? 0.1117 0.1259 0.1312 -0.0054 -0.0140 0.0134  38  ALA   A O   
911  C CB  A ALA   A 38  ? 0.1199 0.1535 0.1468 -0.0138 -0.0029 0.0089  38  ALA   A CB  
912  C CB  B ALA   A 38  ? 0.1195 0.1248 0.1261 -0.0108 -0.0026 0.0140  38  ALA   A CB  
923  N N   A ALA   A 39  ? 0.1122 0.1250 0.1263 0.0036  0.0035  0.0096  39  ALA   A N   
924  N N   B ALA   A 39  ? 0.1205 0.1245 0.1217 -0.0047 -0.0034 0.0152  39  ALA   A N   
925  C CA  A ALA   A 39  ? 0.1126 0.1156 0.1225 0.0052  0.0086  0.0066  39  ALA   A CA  
926  C CA  B ALA   A 39  ? 0.1213 0.1233 0.1176 -0.0048 -0.0058 0.0155  39  ALA   A CA  
927  C C   A ALA   A 39  ? 0.1202 0.1173 0.1201 0.0003  0.0062  0.0058  39  ALA   A C   
928  C C   B ALA   A 39  ? 0.1189 0.1188 0.1133 -0.0036 -0.0023 0.0129  39  ALA   A C   
929  O O   A ALA   A 39  ? 0.1348 0.1216 0.1244 -0.0045 0.0112  0.0074  39  ALA   A O   
930  O O   B ALA   A 39  ? 0.1221 0.1180 0.1130 -0.0033 -0.0016 0.0098  39  ALA   A O   
931  C CB  A ALA   A 39  ? 0.1105 0.1226 0.1381 0.0067  -0.0042 0.0053  39  ALA   A CB  
932  C CB  B ALA   A 39  ? 0.1256 0.1255 0.1164 -0.0040 -0.0057 0.0157  39  ALA   A CB  
943  N N   A ASN   A 40  ? 0.1287 0.1229 0.1146 -0.0058 0.0202  0.0060  40  ASN   A N   
944  N N   B ASN   A 40  ? 0.1197 0.1171 0.1104 -0.0031 -0.0014 0.0123  40  ASN   A N   
945  C CA  A ASN   A 40  ? 0.1342 0.1186 0.1288 -0.0007 0.0075  0.0055  40  ASN   A CA  
946  C CA  B ASN   A 40  ? 0.1190 0.1154 0.1167 -0.0020 -0.0052 0.0110  40  ASN   A CA  
947  C C   A ASN   A 40  ? 0.1353 0.1103 0.1068 -0.0069 0.0188  0.0133  40  ASN   A C   
948  C C   B ASN   A 40  ? 0.1178 0.1138 0.1117 -0.0016 -0.0042 0.0113  40  ASN   A C   
949  O O   A ASN   A 40  ? 0.1314 0.1133 0.1156 -0.0120 0.0199  0.0117  40  ASN   A O   
950  O O   B ASN   A 40  ? 0.1142 0.1117 0.1127 -0.0002 -0.0068 0.0096  40  ASN   A O   
951  C CB  A ASN   A 40  ? 0.1470 0.1275 0.1393 0.0049  -0.0057 0.0089  40  ASN   A CB  
952  C CB  B ASN   A 40  ? 0.1232 0.1146 0.1235 -0.0019 -0.0062 0.0082  40  ASN   A CB  
953  C CG  A ASN   A 40  ? 0.1514 0.1264 0.1702 0.0050  -0.0063 0.0154  40  ASN   A CG  
954  C CG  B ASN   A 40  ? 0.1254 0.1140 0.1293 -0.0032 -0.0062 0.0019  40  ASN   A CG  
955  O OD1 A ASN   A 40  ? 0.1595 0.1296 0.1979 0.0063  0.0005  0.0124  40  ASN   A OD1 
956  O OD1 B ASN   A 40  ? 0.1303 0.1158 0.1455 -0.0021 -0.0071 -0.0106 40  ASN   A OD1 
957  N ND2 A ASN   A 40  ? 0.1543 0.1309 0.1862 -0.0004 0.0052  0.0042  40  ASN   A ND2 
958  N ND2 B ASN   A 40  ? 0.1258 0.1147 0.1272 -0.0075 0.0025  0.0025  40  ASN   A ND2 
971  N N   A VAL   A 41  ? 0.1425 0.1162 0.1163 -0.0032 0.0155  0.0165  41  VAL   A N   
972  N N   B VAL   A 41  ? 0.1211 0.1166 0.1077 -0.0001 -0.0012 0.0178  41  VAL   A N   
973  C CA  A VAL   A 41  ? 0.1411 0.1239 0.1342 -0.0011 0.0247  0.0138  41  VAL   A CA  
974  C CA  B VAL   A 41  ? 0.1242 0.1207 0.1036 0.0029  0.0028  0.0203  41  VAL   A CA  
975  C C   A VAL   A 41  ? 0.1347 0.1204 0.1341 -0.0000 0.0248  0.0149  41  VAL   A C   
976  C C   B VAL   A 41  ? 0.1266 0.1228 0.1069 0.0013  -0.0002 0.0213  41  VAL   A C   
977  O O   A VAL   A 41  ? 0.1337 0.1148 0.1572 0.0045  0.0281  0.0016  41  VAL   A O   
978  O O   B VAL   A 41  ? 0.1282 0.1192 0.1113 0.0021  -0.0023 0.0176  41  VAL   A O   
979  C CB  A VAL   A 41  ? 0.1541 0.1371 0.1348 -0.0087 0.0342  0.0097  41  VAL   A CB  
980  C CB  B VAL   A 41  ? 0.1249 0.1226 0.1050 0.0057  0.0126  0.0213  41  VAL   A CB  
981  C CG1 A VAL   A 41  ? 0.1648 0.1489 0.1347 -0.0006 0.0310  -0.0008 41  VAL   A CG1 
982  C CG1 B VAL   A 41  ? 0.1291 0.1246 0.1070 0.0062  0.0184  0.0151  41  VAL   A CG1 
983  C CG2 A VAL   A 41  ? 0.1683 0.1456 0.1330 -0.0118 0.0384  0.0076  41  VAL   A CG2 
984  C CG2 B VAL   A 41  ? 0.1238 0.1243 0.1083 0.0059  0.0099  0.0238  41  VAL   A CG2 
1003 N N   A TYR   A 42  ? 0.1249 0.1196 0.1529 0.0005  0.0280  0.0215  42  TYR   A N   
1004 N N   B TYR   A 42  ? 0.1279 0.1267 0.1070 0.0024  -0.0001 0.0263  42  TYR   A N   
1005 C CA  A TYR   A 42  ? 0.1267 0.1140 0.1523 -0.0073 0.0240  0.0227  42  TYR   A CA  
1006 C CA  B TYR   A 42  ? 0.1312 0.1306 0.1129 0.0040  -0.0009 0.0266  42  TYR   A CA  
1007 C C   A TYR   A 42  ? 0.1173 0.1124 0.1561 -0.0030 0.0172  0.0211  42  TYR   A C   
1008 C C   B TYR   A 42  ? 0.1333 0.1339 0.1065 0.0044  -0.0044 0.0295  42  TYR   A C   
1009 O O   A TYR   A 42  ? 0.1208 0.1177 0.1739 -0.0104 0.0166  0.0054  42  TYR   A O   
1010 O O   B TYR   A 42  ? 0.1329 0.1355 0.1056 0.0035  -0.0043 0.0300  42  TYR   A O   
1011 C CB  A TYR   A 42  ? 0.1495 0.1267 0.1513 -0.0030 0.0281  0.0296  42  TYR   A CB  
1012 C CB  B TYR   A 42  ? 0.1341 0.1313 0.1272 0.0076  -0.0043 0.0249  42  TYR   A CB  
1013 C CG  A TYR   A 42  ? 0.1687 0.1398 0.1530 -0.0090 0.0190  0.0351  42  TYR   A CG  
1014 C CG  B TYR   A 42  ? 0.1377 0.1344 0.1396 0.0103  -0.0070 0.0207  42  TYR   A CG  
1015 C CD1 A TYR   A 42  ? 0.1757 0.1510 0.1575 -0.0107 0.0266  0.0316  42  TYR   A CD1 
1016 C CD1 B TYR   A 42  ? 0.1376 0.1354 0.1395 0.0102  -0.0082 0.0208  42  TYR   A CD1 
1017 C CD2 A TYR   A 42  ? 0.1736 0.1646 0.1646 -0.0063 0.0112  0.0256  42  TYR   A CD2 
1018 C CD2 B TYR   A 42  ? 0.1419 0.1402 0.1497 0.0112  -0.0068 0.0164  42  TYR   A CD2 
1019 C CE1 A TYR   A 42  ? 0.1779 0.1639 0.1519 -0.0122 0.0272  0.0352  42  TYR   A CE1 
1020 C CE1 B TYR   A 42  ? 0.1379 0.1396 0.1439 0.0083  -0.0059 0.0159  42  TYR   A CE1 
1021 C CE2 A TYR   A 42  ? 0.1831 0.1780 0.1752 -0.0171 0.0124  0.0288  42  TYR   A CE2 
1022 C CE2 B TYR   A 42  ? 0.1411 0.1436 0.1531 0.0130  -0.0062 0.0153  42  TYR   A CE2 
1023 C CZ  A TYR   A 42  ? 0.1887 0.1791 0.1575 -0.0195 0.0233  0.0361  42  TYR   A CZ  
1024 C CZ  B TYR   A 42  ? 0.1390 0.1437 0.1511 0.0108  -0.0056 0.0101  42  TYR   A CZ  
1025 O OH  A TYR   A 42  ? 0.1978 0.2025 0.1786 -0.0268 0.0182  0.0251  42  TYR   A OH  
1026 O OH  B TYR   A 42  ? 0.1376 0.1501 0.1583 0.0094  -0.0089 0.0040  42  TYR   A OH  
1045 N N   A LEU   A 43  ? 0.1193 0.1132 0.1419 -0.0067 0.0108  0.0083  43  LEU   A N   
1046 N N   B LEU   A 43  ? 0.1336 0.1348 0.1145 0.0062  -0.0076 0.0259  43  LEU   A N   
1047 C CA  A LEU   A 43  ? 0.1158 0.1132 0.1384 -0.0040 0.0113  0.0061  43  LEU   A CA  
1048 C CA  B LEU   A 43  ? 0.1364 0.1363 0.1219 0.0058  -0.0075 0.0186  43  LEU   A CA  
1049 C C   A LEU   A 43  ? 0.1166 0.1156 0.1410 -0.0003 0.0112  0.0042  43  LEU   A C   
1050 C C   B LEU   A 43  ? 0.1411 0.1409 0.1240 0.0027  -0.0086 0.0125  43  LEU   A C   
1051 O O   A LEU   A 43  ? 0.1368 0.1226 0.1570 0.0039  -0.0030 0.0023  43  LEU   A O   
1052 O O   B LEU   A 43  ? 0.1432 0.1422 0.1184 0.0009  -0.0152 0.0114  43  LEU   A O   
1053 C CB  A LEU   A 43  ? 0.1242 0.1132 0.1442 -0.0065 0.0143  0.0055  43  LEU   A CB  
1054 C CB  B LEU   A 43  ? 0.1335 0.1317 0.1268 0.0079  -0.0065 0.0171  43  LEU   A CB  
1055 C CG  A LEU   A 43  ? 0.1260 0.1142 0.1565 -0.0043 0.0063  0.0107  43  LEU   A CG  
1056 C CG  B LEU   A 43  ? 0.1296 0.1277 0.1284 0.0116  -0.0060 0.0156  43  LEU   A CG  
1057 C CD1 A LEU   A 43  ? 0.1311 0.1260 0.1722 -0.0026 -0.0023 0.0161  43  LEU   A CD1 
1058 C CD1 B LEU   A 43  ? 0.1298 0.1282 0.1294 0.0104  -0.0063 0.0154  43  LEU   A CD1 
1059 C CD2 A LEU   A 43  ? 0.1398 0.1158 0.1544 0.0007  0.0015  0.0130  43  LEU   A CD2 
1060 C CD2 B LEU   A 43  ? 0.1297 0.1236 0.1275 0.0162  -0.0067 0.0213  43  LEU   A CD2 
1083 N N   A LYS   A 44  ? 0.1225 0.1173 0.1402 -0.0017 0.0070  0.0114  44  LYS   A N   
1084 N N   B LYS   A 44  ? 0.1441 0.1452 0.1346 0.0033  -0.0061 0.0083  44  LYS   A N   
1085 C CA  A LYS   A 44  ? 0.1333 0.1188 0.1411 -0.0044 0.0167  0.0197  44  LYS   A CA  
1086 C CA  B LYS   A 44  ? 0.1495 0.1492 0.1467 0.0027  -0.0036 0.0038  44  LYS   A CA  
1087 C C   A LYS   A 44  ? 0.1222 0.1194 0.1298 0.0018  0.0098  0.0144  44  LYS   A C   
1088 C C   B LYS   A 44  ? 0.1434 0.1436 0.1338 0.0022  -0.0029 0.0014  44  LYS   A C   
1089 O O   A LYS   A 44  ? 0.1292 0.1352 0.1450 0.0050  0.0036  0.0008  44  LYS   A O   
1090 O O   B LYS   A 44  ? 0.1440 0.1431 0.1297 0.0045  -0.0032 -0.0018 44  LYS   A O   
1091 C CB  A LYS   A 44  ? 0.1601 0.1337 0.1824 0.0030  0.0310  0.0352  44  LYS   A CB  
1092 C CB  B LYS   A 44  ? 0.1622 0.1602 0.1775 0.0041  0.0022  0.0014  44  LYS   A CB  
1093 C CG  A LYS   A 44  ? 0.1918 0.1640 0.2506 -0.0098 0.0554  0.0468  44  LYS   A CG  
1094 C CG  B LYS   A 44  ? 0.1736 0.1693 0.2088 0.0059  0.0091  -0.0000 44  LYS   A CG  
1095 C CD  A LYS   A 44  ? 0.2321 0.2187 0.3662 -0.0189 0.0390  0.0356  44  LYS   A CD  
1096 C CD  B LYS   A 44  ? 0.1857 0.1799 0.2425 0.0058  0.0071  -0.0030 44  LYS   A CD  
1097 C CE  A LYS   A 44  ? 0.2507 0.2497 0.4390 -0.0213 0.0297  0.0351  44  LYS   A CE  
1098 C CE  B LYS   A 44  ? 0.1901 0.1831 0.2629 0.0059  0.0051  -0.0036 44  LYS   A CE  
1099 N NZ  A LYS   A 44  ? 0.2599 0.2711 0.4770 -0.0216 0.0294  0.0372  44  LYS   A NZ  
1100 N NZ  B LYS   A 44  ? 0.1899 0.1816 0.2720 0.0058  0.0051  -0.0051 44  LYS   A NZ  
1127 N N   A HIS   A 45  ? 0.1121 0.1150 0.1329 0.0000  0.0045  0.0156  45  HIS   A N   
1128 N N   B HIS   A 45  ? 0.1390 0.1394 0.1303 -0.0018 -0.0044 0.0025  45  HIS   A N   
1129 C CA  A HIS   A 45  ? 0.1168 0.1189 0.1352 0.0014  -0.0040 0.0114  45  HIS   A CA  
1130 C CA  B HIS   A 45  ? 0.1333 0.1368 0.1265 -0.0042 -0.0043 0.0034  45  HIS   A CA  
1131 C C   A HIS   A 45  ? 0.1206 0.1315 0.1499 0.0097  0.0012  0.0145  45  HIS   A C   
1132 C C   B HIS   A 45  ? 0.1315 0.1362 0.1261 -0.0094 0.0010  0.0055  45  HIS   A C   
1133 O O   A HIS   A 45  ? 0.1344 0.1312 0.1664 0.0151  0.0025  0.0010  45  HIS   A O   
1134 O O   B HIS   A 45  ? 0.1327 0.1356 0.1300 -0.0092 0.0008  0.0048  45  HIS   A O   
1135 C CB  A HIS   A 45  ? 0.1136 0.1141 0.1369 -0.0010 0.0033  0.0050  45  HIS   A CB  
1136 C CB  B HIS   A 45  ? 0.1268 0.1346 0.1255 0.0011  -0.0086 -0.0015 45  HIS   A CB  
1137 C CG  A HIS   A 45  ? 0.1153 0.1131 0.1187 -0.0055 0.0088  0.0063  45  HIS   A CG  
1138 C CG  B HIS   A 45  ? 0.1168 0.1304 0.1141 0.0031  -0.0026 -0.0037 45  HIS   A CG  
1139 N ND1 A HIS   A 45  ? 0.1129 0.1164 0.1354 -0.0012 0.0079  0.0131  45  HIS   A ND1 
1140 N ND1 B HIS   A 45  ? 0.1127 0.1290 0.1165 0.0057  -0.0047 -0.0004 45  HIS   A ND1 
1141 C CD2 A HIS   A 45  ? 0.1144 0.1185 0.1341 -0.0077 -0.0015 0.0217  45  HIS   A CD2 
1142 C CD2 B HIS   A 45  ? 0.1104 0.1252 0.1056 0.0052  0.0006  -0.0080 45  HIS   A CD2 
1143 C CE1 A HIS   A 45  ? 0.1166 0.1172 0.1294 -0.0074 0.0025  0.0214  45  HIS   A CE1 
1144 C CE1 B HIS   A 45  ? 0.1098 0.1235 0.1047 0.0049  -0.0049 -0.0078 45  HIS   A CE1 
1145 N NE2 A HIS   A 45  ? 0.1176 0.1224 0.1261 -0.0032 -0.0016 0.0233  45  HIS   A NE2 
1146 N NE2 B HIS   A 45  ? 0.1079 0.1227 0.0986 0.0046  -0.0035 -0.0135 45  HIS   A NE2 
1161 N N   A GLY   A 46  ? 0.1293 0.1439 0.1571 0.0156  -0.0101 0.0203  46  GLY   A N   
1162 N N   B GLY   A 46  ? 0.1305 0.1347 0.1247 -0.0162 0.0049  0.0079  46  GLY   A N   
1163 C CA  A GLY   A 46  ? 0.1325 0.1518 0.1753 0.0157  -0.0056 0.0300  46  GLY   A CA  
1164 C CA  B GLY   A 46  ? 0.1274 0.1348 0.1209 -0.0177 0.0105  0.0078  46  GLY   A CA  
1165 C C   A GLY   A 46  ? 0.1389 0.1460 0.1712 0.0255  -0.0119 0.0416  46  GLY   A C   
1166 C C   B GLY   A 46  ? 0.1244 0.1351 0.1151 -0.0163 0.0201  0.0089  46  GLY   A C   
1167 O O   A GLY   A 46  ? 0.1447 0.1520 0.1822 0.0242  -0.0158 0.0321  46  GLY   A O   
1168 O O   B GLY   A 46  ? 0.1223 0.1355 0.1127 -0.0189 0.0287  0.0067  46  GLY   A O   
1175 N N   A GLY   A 47  ? 0.1416 0.1459 0.1653 0.0235  -0.0080 0.0314  47  GLY   A N   
1176 N N   B GLY   A 47  ? 0.1252 0.1350 0.1171 -0.0145 0.0204  0.0044  47  GLY   A N   
1177 C CA  A GLY   A 47  ? 0.1440 0.1454 0.1675 0.0228  -0.0213 0.0197  47  GLY   A CA  
1178 C CA  B GLY   A 47  ? 0.1230 0.1303 0.1123 -0.0140 0.0145  0.0070  47  GLY   A CA  
1179 C C   A GLY   A 47  ? 0.1424 0.1344 0.1557 0.0201  -0.0275 0.0072  47  GLY   A C   
1180 C C   B GLY   A 47  ? 0.1197 0.1229 0.0991 -0.0120 0.0103  0.0087  47  GLY   A C   
1181 O O   A GLY   A 47  ? 0.1422 0.1325 0.1638 0.0261  -0.0245 0.0109  47  GLY   A O   
1182 O O   B GLY   A 47  ? 0.1202 0.1222 0.0922 -0.0134 0.0031  0.0158  47  GLY   A O   
1189 N N   A GLY   A 48  ? 0.1397 0.1406 0.1546 0.0173  -0.0319 0.0011  48  GLY   A N   
1190 N N   B GLY   A 48  ? 0.1168 0.1183 0.0988 -0.0092 0.0115  0.0112  48  GLY   A N   
1191 C CA  A GLY   A 48  ? 0.1354 0.1387 0.1644 0.0109  -0.0286 -0.0049 48  GLY   A CA  
1192 C CA  B GLY   A 48  ? 0.1144 0.1108 0.0948 -0.0073 0.0117  0.0122  48  GLY   A CA  
1193 C C   A GLY   A 48  ? 0.1269 0.1332 0.1472 0.0021  -0.0124 -0.0036 48  GLY   A C   
1194 C C   B GLY   A 48  ? 0.1140 0.1075 0.0986 -0.0046 0.0106  0.0141  48  GLY   A C   
1195 O O   A GLY   A 48  ? 0.1373 0.1292 0.1497 0.0041  -0.0103 -0.0090 48  GLY   A O   
1196 O O   B GLY   A 48  ? 0.1183 0.1025 0.0925 -0.0087 0.0176  0.0203  48  GLY   A O   
1203 N N   A VAL   A 49  ? 0.1172 0.1265 0.1585 -0.0043 -0.0181 -0.0009 49  VAL   A N   
1204 N N   B VAL   A 49  ? 0.1062 0.1082 0.1048 0.0013  0.0010  0.0068  49  VAL   A N   
1205 C CA  A VAL   A 49  ? 0.1252 0.1246 0.1483 -0.0093 0.0008  -0.0003 49  VAL   A CA  
1206 C CA  B VAL   A 49  ? 0.0998 0.1146 0.1119 0.0097  -0.0028 0.0061  49  VAL   A CA  
1207 C C   A VAL   A 49  ? 0.1242 0.1171 0.1302 0.0005  0.0062  -0.0018 49  VAL   A C   
1208 C C   B VAL   A 49  ? 0.1006 0.1132 0.1048 0.0156  -0.0018 -0.0050 49  VAL   A C   
1209 O O   A VAL   A 49  ? 0.1178 0.1206 0.1317 -0.0019 0.0087  -0.0008 49  VAL   A O   
1210 O O   B VAL   A 49  ? 0.1006 0.1125 0.1039 0.0239  -0.0014 -0.0030 49  VAL   A O   
1211 C CB  A VAL   A 49  ? 0.1499 0.1270 0.1612 -0.0118 0.0001  0.0027  49  VAL   A CB  
1212 C CB  B VAL   A 49  ? 0.0926 0.1173 0.1233 0.0169  -0.0110 0.0112  49  VAL   A CB  
1213 C CG1 A VAL   A 49  ? 0.1682 0.1234 0.1778 -0.0052 0.0061  0.0103  49  VAL   A CG1 
1214 C CG1 B VAL   A 49  ? 0.0843 0.1195 0.1301 0.0225  -0.0154 0.0153  49  VAL   A CG1 
1215 C CG2 A VAL   A 49  ? 0.1628 0.1422 0.2129 -0.0326 -0.0066 0.0015  49  VAL   A CG2 
1216 C CG2 B VAL   A 49  ? 0.0914 0.1185 0.1293 0.0185  -0.0103 0.0112  49  VAL   A CG2 
1235 N N   A ALA   A 50  ? 0.1178 0.1123 0.1252 -0.0035 -0.0072 0.0046  50  ALA   A N   
1236 N N   B ALA   A 50  ? 0.1024 0.1114 0.1027 0.0139  0.0014  -0.0136 50  ALA   A N   
1237 C CA  A ALA   A 50  ? 0.1193 0.1134 0.1275 -0.0092 -0.0022 0.0123  50  ALA   A CA  
1238 C CA  B ALA   A 50  ? 0.1037 0.1095 0.1015 0.0099  -0.0002 -0.0189 50  ALA   A CA  
1239 C C   A ALA   A 50  ? 0.1136 0.1182 0.1302 -0.0087 -0.0017 0.0050  50  ALA   A C   
1240 C C   B ALA   A 50  ? 0.1048 0.1077 0.0973 0.0096  -0.0032 -0.0220 50  ALA   A C   
1241 O O   A ALA   A 50  ? 0.1176 0.1180 0.1441 -0.0012 -0.0041 0.0079  50  ALA   A O   
1242 O O   B ALA   A 50  ? 0.1043 0.1064 0.0908 0.0111  -0.0018 -0.0202 50  ALA   A O   
1243 C CB  A ALA   A 50  ? 0.1163 0.1138 0.1314 -0.0010 -0.0011 0.0125  50  ALA   A CB  
1244 C CB  B ALA   A 50  ? 0.1021 0.1074 0.1038 0.0081  0.0043  -0.0273 50  ALA   A CB  
1255 N N   A GLY   A 51  ? 0.1208 0.1088 0.1389 0.0011  -0.0156 0.0058  51  GLY   A N   
1256 N N   B GLY   A 51  ? 0.1074 0.1064 0.1058 0.0090  -0.0102 -0.0248 51  GLY   A N   
1257 C CA  A GLY   A 51  ? 0.1296 0.1088 0.1430 0.0059  -0.0129 0.0024  51  GLY   A CA  
1258 C CA  B GLY   A 51  ? 0.1102 0.1074 0.1072 0.0094  -0.0118 -0.0271 51  GLY   A CA  
1259 C C   A GLY   A 51  ? 0.1177 0.1198 0.1379 0.0040  -0.0064 -0.0015 51  GLY   A C   
1260 C C   B GLY   A 51  ? 0.1097 0.1109 0.1166 0.0107  -0.0103 -0.0256 51  GLY   A C   
1261 O O   A GLY   A 51  ? 0.1204 0.1250 0.1504 -0.0012 -0.0068 -0.0081 51  GLY   A O   
1262 O O   B GLY   A 51  ? 0.1119 0.1096 0.1212 0.0137  -0.0070 -0.0294 51  GLY   A O   
1269 N N   A ALA   A 52  ? 0.1140 0.1282 0.1403 -0.0000 -0.0027 -0.0076 52  ALA   A N   
1270 N N   B ALA   A 52  ? 0.1092 0.1145 0.1174 0.0072  -0.0064 -0.0238 52  ALA   A N   
1271 C CA  A ALA   A 52  ? 0.1188 0.1355 0.1500 0.0014  -0.0000 -0.0064 52  ALA   A CA  
1272 C CA  B ALA   A 52  ? 0.1083 0.1163 0.1230 0.0053  -0.0005 -0.0185 52  ALA   A CA  
1273 C C   A ALA   A 52  ? 0.1174 0.1324 0.1293 -0.0082 0.0035  -0.0080 52  ALA   A C   
1274 C C   B ALA   A 52  ? 0.1050 0.1160 0.1221 0.0008  0.0030  -0.0127 52  ALA   A C   
1275 O O   A ALA   A 52  ? 0.1291 0.1398 0.1411 -0.0047 0.0050  -0.0099 52  ALA   A O   
1276 O O   B ALA   A 52  ? 0.1055 0.1116 0.1308 -0.0027 0.0113  -0.0099 52  ALA   A O   
1277 C CB  A ALA   A 52  ? 0.1253 0.1587 0.1683 -0.0085 -0.0018 -0.0052 52  ALA   A CB  
1278 C CB  B ALA   A 52  ? 0.1068 0.1185 0.1237 0.0055  -0.0003 -0.0204 52  ALA   A CB  
1289 N N   A LEU   A 53  ? 0.1138 0.1302 0.1246 -0.0047 -0.0030 -0.0019 53  LEU   A N   
1290 N N   B LEU   A 53  ? 0.1039 0.1196 0.1207 0.0022  0.0013  -0.0099 53  LEU   A N   
1291 C CA  A LEU   A 53  ? 0.1221 0.1349 0.1186 -0.0026 0.0051  0.0012  53  LEU   A CA  
1292 C CA  B LEU   A 53  ? 0.1032 0.1227 0.1155 0.0043  0.0014  -0.0081 53  LEU   A CA  
1293 C C   A LEU   A 53  ? 0.1195 0.1377 0.0973 0.0055  0.0011  0.0019  53  LEU   A C   
1294 C C   B LEU   A 53  ? 0.1076 0.1265 0.1135 0.0053  0.0049  -0.0076 53  LEU   A C   
1295 O O   A LEU   A 53  ? 0.1342 0.1473 0.1115 -0.0090 0.0000  0.0009  53  LEU   A O   
1296 O O   B LEU   A 53  ? 0.1086 0.1275 0.1187 0.0048  0.0069  -0.0034 53  LEU   A O   
1297 C CB  A LEU   A 53  ? 0.1303 0.1366 0.1204 -0.0048 0.0067  0.0114  53  LEU   A CB  
1298 C CB  B LEU   A 53  ? 0.0971 0.1211 0.1092 0.0027  -0.0009 -0.0115 53  LEU   A CB  
1299 C CG  A LEU   A 53  ? 0.1438 0.1320 0.1350 -0.0094 0.0083  0.0054  53  LEU   A CG  
1300 C CG  B LEU   A 53  ? 0.0947 0.1194 0.1057 -0.0001 -0.0019 -0.0167 53  LEU   A CG  
1301 C CD1 A LEU   A 53  ? 0.1483 0.1401 0.1505 -0.0003 0.0010  0.0070  53  LEU   A CD1 
1302 C CD1 B LEU   A 53  ? 0.0924 0.1189 0.0984 -0.0027 0.0017  -0.0241 53  LEU   A CD1 
1303 C CD2 A LEU   A 53  ? 0.1666 0.1496 0.1475 -0.0215 0.0152  0.0082  53  LEU   A CD2 
1304 C CD2 B LEU   A 53  ? 0.0925 0.1173 0.1020 0.0004  0.0015  -0.0201 53  LEU   A CD2 
1327 N N   A ASN   A 54  ? 0.1175 0.1277 0.1085 0.0004  0.0006  0.0037  54  ASN   A N   
1328 N N   B ASN   A 54  ? 0.1118 0.1311 0.1173 0.0034  0.0035  -0.0070 54  ASN   A N   
1329 C CA  A ASN   A 54  ? 0.1117 0.1206 0.1196 -0.0036 -0.0026 -0.0061 54  ASN   A CA  
1330 C CA  B ASN   A 54  ? 0.1163 0.1352 0.1174 0.0005  -0.0002 -0.0093 54  ASN   A CA  
1331 C C   A ASN   A 54  ? 0.1220 0.1265 0.1249 -0.0076 -0.0039 0.0010  54  ASN   A C   
1332 C C   B ASN   A 54  ? 0.1229 0.1381 0.1185 -0.0004 0.0014  -0.0126 54  ASN   A C   
1333 O O   A ASN   A 54  ? 0.1247 0.1357 0.1401 -0.0040 -0.0055 -0.0132 54  ASN   A O   
1334 O O   B ASN   A 54  ? 0.1231 0.1389 0.1134 0.0004  0.0026  -0.0177 54  ASN   A O   
1335 C CB  A ASN   A 54  ? 0.1058 0.1198 0.1386 -0.0072 -0.0092 -0.0074 54  ASN   A CB  
1336 C CB  B ASN   A 54  ? 0.1174 0.1379 0.1185 0.0018  -0.0011 -0.0056 54  ASN   A CB  
1337 C CG  A ASN   A 54  ? 0.1111 0.1223 0.1416 -0.0031 -0.0056 -0.0067 54  ASN   A CG  
1338 C CG  B ASN   A 54  ? 0.1179 0.1394 0.1169 0.0033  -0.0016 -0.0019 54  ASN   A CG  
1339 O OD1 A ASN   A 54  ? 0.1108 0.1232 0.1349 -0.0039 -0.0067 0.0000  54  ASN   A OD1 
1340 O OD1 B ASN   A 54  ? 0.1181 0.1420 0.1219 -0.0001 -0.0009 0.0008  54  ASN   A OD1 
1341 N ND2 A ASN   A 54  ? 0.1164 0.1243 0.1528 -0.0079 -0.0061 0.0065  54  ASN   A ND2 
1342 N ND2 B ASN   A 54  ? 0.1192 0.1386 0.1121 0.0053  -0.0019 0.0023  54  ASN   A ND2 
1355 N N   A LYS   A 55  ? 0.1171 0.1269 0.1400 -0.0034 -0.0020 -0.0093 55  LYS   A N   
1356 N N   B LYS   A 55  ? 0.1274 0.1406 0.1273 -0.0003 0.0033  -0.0154 55  LYS   A N   
1357 C CA  A LYS   A 55  ? 0.1216 0.1332 0.1399 0.0026  -0.0054 -0.0164 55  LYS   A CA  
1358 C CA  B LYS   A 55  ? 0.1327 0.1450 0.1376 0.0011  0.0054  -0.0158 55  LYS   A CA  
1359 C C   A LYS   A 55  ? 0.1210 0.1434 0.1415 -0.0023 0.0010  -0.0219 55  LYS   A C   
1360 C C   B LYS   A 55  ? 0.1309 0.1477 0.1402 -0.0019 0.0064  -0.0174 55  LYS   A C   
1361 O O   A LYS   A 55  ? 0.1321 0.1542 0.1500 0.0002  -0.0049 -0.0300 55  LYS   A O   
1362 O O   B LYS   A 55  ? 0.1320 0.1479 0.1395 0.0012  0.0087  -0.0185 55  LYS   A O   
1363 C CB  A LYS   A 55  ? 0.1269 0.1421 0.1676 0.0100  -0.0116 -0.0207 55  LYS   A CB  
1364 C CB  B LYS   A 55  ? 0.1382 0.1478 0.1498 0.0033  0.0081  -0.0135 55  LYS   A CB  
1365 C CG  A LYS   A 55  ? 0.1413 0.1623 0.1780 0.0174  -0.0138 -0.0268 55  LYS   A CG  
1366 C CG  B LYS   A 55  ? 0.1425 0.1515 0.1617 0.0053  0.0091  -0.0151 55  LYS   A CG  
1367 C CD  A LYS   A 55  ? 0.1526 0.1857 0.1901 0.0242  -0.0036 -0.0242 55  LYS   A CD  
1368 C CD  B LYS   A 55  ? 0.1477 0.1545 0.1754 0.0078  0.0095  -0.0159 55  LYS   A CD  
1369 C CE  A LYS   A 55  ? 0.1650 0.2052 0.1948 0.0286  -0.0190 -0.0238 55  LYS   A CE  
1370 C CE  B LYS   A 55  ? 0.1527 0.1583 0.1839 0.0086  0.0083  -0.0173 55  LYS   A CE  
1371 N NZ  A LYS   A 55  ? 0.1716 0.2113 0.2013 0.0272  -0.0180 -0.0197 55  LYS   A NZ  
1372 N NZ  B LYS   A 55  ? 0.1547 0.1605 0.1883 0.0109  0.0078  -0.0180 55  LYS   A NZ  
1399 N N   . ALA   A 56  ? 0.1305 0.1507 0.1411 -0.0073 0.0057  -0.0200 56  ALA   A N   
1400 C CA  . ALA   A 56  ? 0.1465 0.1670 0.1400 -0.0104 0.0105  -0.0178 56  ALA   A CA  
1401 C C   . ALA   A 56  ? 0.1467 0.1779 0.1117 -0.0093 0.0132  -0.0225 56  ALA   A C   
1402 O O   . ALA   A 56  ? 0.1550 0.2109 0.1316 0.0008  0.0143  -0.0181 56  ALA   A O   
1403 C CB  . ALA   A 56  ? 0.1565 0.1864 0.1516 -0.0198 0.0140  -0.0115 56  ALA   A CB  
1410 N N   . THR   A 57  ? 0.1331 0.1565 0.1163 -0.0078 0.0103  -0.0168 57  THR   A N   
1411 C CA  . THR   A 57  ? 0.1380 0.1531 0.1272 -0.0082 0.0023  -0.0137 57  THR   A CA  
1412 C C   . THR   A 57  ? 0.1370 0.1576 0.1364 -0.0065 -0.0034 -0.0189 57  THR   A C   
1413 O O   . THR   A 57  ? 0.1353 0.1620 0.1544 -0.0130 -0.0077 -0.0283 57  THR   A O   
1414 C CB  . THR   A 57  ? 0.1375 0.1528 0.1294 -0.0054 0.0024  -0.0135 57  THR   A CB  
1415 O OG1 . THR   A 57  ? 0.1282 0.1475 0.1267 -0.0029 0.0032  -0.0136 57  THR   A OG1 
1416 C CG2 . THR   A 57  ? 0.1414 0.1541 0.1238 -0.0089 -0.0026 -0.0051 57  THR   A CG2 
1424 N N   . ASN   A 58  ? 0.1399 0.1536 0.1529 -0.0065 0.0030  -0.0271 58  ASN   A N   
1425 C CA  . ASN   A 58  ? 0.1600 0.1495 0.1780 -0.0108 0.0086  -0.0336 58  ASN   A CA  
1426 C C   . ASN   A 58  ? 0.1387 0.1382 0.1656 -0.0023 -0.0023 -0.0215 58  ASN   A C   
1427 O O   . ASN   A 58  ? 0.1406 0.1488 0.1738 -0.0128 -0.0030 -0.0264 58  ASN   A O   
1428 C CB  . ASN   A 58  ? 0.2030 0.1678 0.2058 -0.0176 0.0266  -0.0522 58  ASN   A CB  
1429 C CG  . ASN   A 58  ? 0.2423 0.1909 0.2658 -0.0144 0.0278  -0.0424 58  ASN   A CG  
1430 O OD1 . ASN   A 58  ? 0.2659 0.1913 0.3027 0.0170  0.0549  -0.0366 58  ASN   A OD1 
1431 N ND2 . ASN   A 58  ? 0.2500 0.1998 0.2850 -0.0196 0.0107  -0.0445 58  ASN   A ND2 
1438 N N   . ASN   A 59  ? 0.1270 0.1355 0.1468 -0.0048 -0.0108 -0.0164 59  ASN   A N   
1439 C CA  . ASN   A 59  ? 0.1254 0.1264 0.1481 -0.0058 -0.0079 -0.0089 59  ASN   A CA  
1440 C C   . ASN   A 59  ? 0.1243 0.1263 0.1393 -0.0065 -0.0101 -0.0070 59  ASN   A C   
1441 O O   . ASN   A 59  ? 0.1226 0.1294 0.1475 -0.0056 -0.0009 -0.0013 59  ASN   A O   
1442 C CB  . ASN   A 59  ? 0.1259 0.1214 0.1619 -0.0007 -0.0191 -0.0079 59  ASN   A CB  
1443 C CG  . ASN   A 59  ? 0.1285 0.1265 0.1603 -0.0037 -0.0256 -0.0007 59  ASN   A CG  
1444 O OD1 . ASN   A 59  ? 0.1431 0.1361 0.1566 -0.0101 -0.0280 0.0018  59  ASN   A OD1 
1445 N ND2 . ASN   A 59  ? 0.1387 0.1322 0.1737 -0.0101 -0.0222 -0.0005 59  ASN   A ND2 
1452 N N   . ALA   A 60  ? 0.1203 0.1277 0.1371 -0.0029 -0.0062 -0.0073 60  ALA   A N   
1453 C CA  . ALA   A 60  ? 0.1200 0.1298 0.1503 -0.0018 -0.0123 -0.0051 60  ALA   A CA  
1454 C C   . ALA   A 60  ? 0.1213 0.1258 0.1513 0.0000  -0.0070 -0.0035 60  ALA   A C   
1455 O O   . ALA   A 60  ? 0.1173 0.1277 0.1694 -0.0017 -0.0129 -0.0094 60  ALA   A O   
1456 C CB  . ALA   A 60  ? 0.1345 0.1443 0.1472 -0.0021 -0.0162 -0.0177 60  ALA   A CB  
1462 N N   . MET   A 61  ? 0.1181 0.1241 0.1414 -0.0061 0.0006  -0.0071 61  MET   A N   
1463 C CA  . MET   A 61  ? 0.1182 0.1210 0.1316 -0.0040 -0.0012 -0.0018 61  MET   A CA  
1464 C C   . MET   A 61  ? 0.1116 0.1141 0.1362 -0.0047 -0.0060 -0.0030 61  MET   A C   
1465 O O   . MET   A 61  ? 0.1165 0.1185 0.1476 -0.0029 0.0058  -0.0002 61  MET   A O   
1466 C CB  . MET   A 61  ? 0.1194 0.1218 0.1271 -0.0085 0.0001  -0.0037 61  MET   A CB  
1467 C CG  . MET   A 61  ? 0.1224 0.1301 0.1444 0.0017  -0.0015 -0.0001 61  MET   A CG  
1468 S SD  . MET   A 61  ? 0.1265 0.1265 0.1754 -0.0103 0.0007  -0.0189 61  MET   A SD  
1469 C CE  . MET   A 61  ? 0.1484 0.1461 0.1865 -0.0148 0.0142  -0.0162 61  MET   A CE  
1479 N N   . GLN   A 62  ? 0.1123 0.1146 0.1385 -0.0054 -0.0044 -0.0049 62  GLN   A N   
1480 C CA  . GLN   A 62  ? 0.1229 0.1148 0.1483 -0.0013 0.0008  -0.0001 62  GLN   A CA  
1481 C C   . GLN   A 62  ? 0.1212 0.1078 0.1579 -0.0004 0.0090  0.0039  62  GLN   A C   
1482 O O   . GLN   A 62  ? 0.1232 0.1207 0.1605 -0.0015 0.0043  0.0011  62  GLN   A O   
1483 C CB  . GLN   A 62  ? 0.1209 0.1102 0.1529 -0.0024 0.0030  0.0025  62  GLN   A CB  
1484 C CG  . GLN   A 62  ? 0.1234 0.1106 0.1483 -0.0040 -0.0064 0.0124  62  GLN   A CG  
1485 C CD  . GLN   A 62  ? 0.1315 0.1161 0.1479 -0.0031 0.0022  0.0116  62  GLN   A CD  
1486 O OE1 . GLN   A 62  ? 0.1349 0.1292 0.1558 -0.0071 -0.0003 0.0035  62  GLN   A OE1 
1487 N NE2 . GLN   A 62  ? 0.1367 0.1204 0.1647 -0.0000 0.0020  -0.0060 62  GLN   A NE2 
1496 N N   . VAL   A 63  ? 0.1173 0.1193 0.1644 -0.0058 0.0054  -0.0140 63  VAL   A N   
1497 C CA  . VAL   A 63  ? 0.1174 0.1285 0.1838 -0.0154 -0.0015 -0.0190 63  VAL   A CA  
1498 C C   . VAL   A 63  ? 0.1093 0.1248 0.1736 -0.0156 -0.0105 -0.0126 63  VAL   A C   
1499 O O   . VAL   A 63  ? 0.1134 0.1264 0.1882 -0.0125 -0.0016 -0.0087 63  VAL   A O   
1500 C CB  . VAL   A 63  ? 0.1335 0.1445 0.2162 -0.0143 -0.0057 -0.0388 63  VAL   A CB  
1501 C CG1 . VAL   A 63  ? 0.1444 0.1617 0.2499 -0.0184 -0.0105 -0.0581 63  VAL   A CG1 
1502 C CG2 . VAL   A 63  ? 0.1451 0.1341 0.2322 -0.0121 0.0138  -0.0358 63  VAL   A CG2 
1512 N N   . GLU   A 64  ? 0.1149 0.1283 0.1632 -0.0045 -0.0054 -0.0105 64  GLU   A N   
1513 C CA  . GLU   A 64  ? 0.1139 0.1305 0.1639 -0.0089 -0.0032 -0.0028 64  GLU   A CA  
1514 C C   . GLU   A 64  ? 0.1131 0.1239 0.1587 -0.0095 0.0047  -0.0031 64  GLU   A C   
1515 O O   . GLU   A 64  ? 0.1191 0.1297 0.1648 -0.0033 0.0007  -0.0064 64  GLU   A O   
1516 C CB  . GLU   A 64  ? 0.1247 0.1387 0.1620 -0.0087 -0.0004 -0.0069 64  GLU   A CB  
1517 C CG  . GLU   A 64  ? 0.1337 0.1466 0.1656 -0.0121 0.0013  -0.0051 64  GLU   A CG  
1518 C CD  . GLU   A 64  ? 0.1415 0.1510 0.1810 -0.0183 0.0078  -0.0060 64  GLU   A CD  
1519 O OE1 . GLU   A 64  ? 0.1405 0.1591 0.1959 -0.0213 0.0186  -0.0035 64  GLU   A OE1 
1520 O OE2 . GLU   A 64  ? 0.1578 0.1530 0.1768 -0.0216 -0.0003 0.0012  64  GLU   A OE2 
1527 N N   . SER   A 65  ? 0.1064 0.1247 0.1555 -0.0013 0.0027  -0.0020 65  SER   A N   
1528 C CA  . SER   A 65  ? 0.1159 0.1160 0.1504 -0.0044 -0.0023 -0.0055 65  SER   A CA  
1529 C C   . SER   A 65  ? 0.1138 0.1242 0.1557 -0.0040 -0.0025 -0.0008 65  SER   A C   
1530 O O   . SER   A 65  ? 0.1239 0.1273 0.1740 -0.0004 0.0146  -0.0069 65  SER   A O   
1531 C CB  . SER   A 65  ? 0.1151 0.1183 0.1523 -0.0082 0.0069  0.0035  65  SER   A CB  
1532 O OG  . SER   A 65  ? 0.1166 0.1284 0.1585 -0.0090 -0.0074 0.0097  65  SER   A OG  
1538 N N   . ASP   A 66  ? 0.1180 0.1212 0.1574 -0.0026 0.0128  0.0073  66  ASP   A N   
1539 C CA  . ASP   A 66  ? 0.1310 0.1289 0.1713 -0.0015 0.0107  0.0129  66  ASP   A CA  
1540 C C   . ASP   A 66  ? 0.1268 0.1290 0.1807 -0.0050 0.0175  0.0154  66  ASP   A C   
1541 O O   . ASP   A 66  ? 0.1321 0.1416 0.1950 -0.0040 0.0248  0.0211  66  ASP   A O   
1542 C CB  . ASP   A 66  ? 0.1396 0.1414 0.1960 0.0060  0.0089  0.0230  66  ASP   A CB  
1543 C CG  . ASP   A 66  ? 0.1597 0.1537 0.2180 0.0057  -0.0018 0.0388  66  ASP   A CG  
1544 O OD1 . ASP   A 66  ? 0.1576 0.1842 0.1920 -0.0063 -0.0047 0.0412  66  ASP   A OD1 
1545 O OD2 . ASP   A 66  ? 0.1773 0.1636 0.3035 0.0307  -0.0202 0.0180  66  ASP   A OD2 
1550 N N   . ASP   A 67  ? 0.1136 0.1261 0.1988 -0.0032 0.0115  0.0139  67  ASP   A N   
1551 C CA  . ASP   A 67  ? 0.1192 0.1430 0.2015 -0.0027 0.0031  0.0258  67  ASP   A CA  
1552 C C   . ASP   A 67  ? 0.1185 0.1464 0.1972 -0.0002 0.0092  0.0236  67  ASP   A C   
1553 O O   . ASP   A 67  ? 0.1170 0.1548 0.2125 -0.0010 0.0257  0.0338  67  ASP   A O   
1554 C CB  . ASP   A 67  ? 0.1305 0.1575 0.2350 -0.0009 -0.0161 0.0287  67  ASP   A CB  
1555 C CG  . ASP   A 67  ? 0.1289 0.1692 0.2687 -0.0041 -0.0301 0.0320  67  ASP   A CG  
1556 O OD1 . ASP   A 67  ? 0.1316 0.1869 0.3442 -0.0107 -0.0392 0.0481  67  ASP   A OD1 
1557 O OD2 . ASP   A 67  ? 0.1287 0.1711 0.2530 0.0025  -0.0200 0.0253  67  ASP   A OD2 
1562 N N   . TYR   A 68  ? 0.1197 0.1371 0.1876 0.0034  0.0157  0.0246  68  TYR   A N   
1563 C CA  . TYR   A 68  ? 0.1336 0.1332 0.1812 0.0050  0.0240  0.0244  68  TYR   A CA  
1564 C C   . TYR   A 68  ? 0.1266 0.1322 0.1827 0.0006  0.0230  0.0164  68  TYR   A C   
1565 O O   . TYR   A 68  ? 0.1337 0.1331 0.1929 0.0073  0.0323  0.0171  68  TYR   A O   
1566 C CB  . TYR   A 68  ? 0.1348 0.1309 0.1997 0.0102  0.0445  0.0272  68  TYR   A CB  
1567 C CG  . TYR   A 68  ? 0.1405 0.1480 0.2337 0.0064  0.0600  0.0227  68  TYR   A CG  
1568 C CD1 . TYR   A 68  ? 0.1531 0.1565 0.2608 -0.0161 0.0470  -0.0107 68  TYR   A CD1 
1569 C CD2 . TYR   A 68  ? 0.1592 0.1485 0.2678 0.0124  0.0622  0.0342  68  TYR   A CD2 
1570 C CE1 . TYR   A 68  ? 0.1547 0.1641 0.2918 -0.0162 0.0478  -0.0090 68  TYR   A CE1 
1571 C CE2 . TYR   A 68  ? 0.1557 0.1563 0.2840 0.0014  0.0672  0.0172  68  TYR   A CE2 
1572 C CZ  . TYR   A 68  ? 0.1593 0.1628 0.2969 -0.0186 0.0557  -0.0058 68  TYR   A CZ  
1573 O OH  . TYR   A 68  ? 0.1877 0.1590 0.3074 -0.0105 0.0271  -0.0317 68  TYR   A OH  
1583 N N   . ILE   A 69  ? 0.1225 0.1275 0.1754 -0.0001 0.0207  0.0155  69  ILE   A N   
1584 C CA  . ILE   A 69  ? 0.1302 0.1279 0.1708 0.0022  0.0134  0.0008  69  ILE   A CA  
1585 C C   . ILE   A 69  ? 0.1330 0.1303 0.1617 0.0012  0.0160  0.0158  69  ILE   A C   
1586 O O   . ILE   A 69  ? 0.1414 0.1404 0.1621 -0.0044 0.0229  0.0165  69  ILE   A O   
1587 C CB  . ILE   A 69  ? 0.1363 0.1538 0.1768 0.0051  0.0154  -0.0018 69  ILE   A CB  
1588 C CG1 . ILE   A 69  ? 0.1350 0.1636 0.1858 0.0067  0.0186  -0.0156 69  ILE   A CG1 
1589 C CG2 . ILE   A 69  ? 0.1560 0.1697 0.1945 0.0118  0.0102  -0.0034 69  ILE   A CG2 
1590 C CD1 . ILE   A 69  ? 0.1365 0.1703 0.2053 0.0004  0.0166  -0.0185 69  ILE   A CD1 
1602 N N   . ALA   A 70  ? 0.1374 0.1307 0.1740 -0.0042 0.0189  0.0148  70  ALA   A N   
1603 C CA  . ALA   A 70  ? 0.1406 0.1426 0.1893 -0.0172 0.0223  0.0243  70  ALA   A CA  
1604 C C   . ALA   A 70  ? 0.1372 0.1612 0.1830 -0.0146 0.0287  0.0232  70  ALA   A C   
1605 O O   . ALA   A 70  ? 0.1546 0.1942 0.2103 0.0049  0.0443  0.0396  70  ALA   A O   
1606 C CB  . ALA   A 70  ? 0.1429 0.1428 0.2100 -0.0228 0.0156  0.0161  70  ALA   A CB  
1612 N N   . THR   A 71  ? 0.1285 0.1581 0.1760 -0.0034 0.0176  0.0207  71  THR   A N   
1613 C CA  . THR   A 71  ? 0.1406 0.1733 0.2066 0.0068  0.0195  0.0222  71  THR   A CA  
1614 C C   . THR   A 71  ? 0.1327 0.1644 0.2251 0.0147  0.0354  0.0228  71  THR   A C   
1615 O O   . THR   A 71  ? 0.1388 0.1922 0.2608 0.0117  0.0450  0.0011  71  THR   A O   
1616 C CB  . THR   A 71  ? 0.1650 0.1955 0.2321 0.0152  -0.0158 0.0246  71  THR   A CB  
1617 O OG1 . THR   A 71  ? 0.1855 0.2115 0.2470 0.0100  -0.0333 0.0146  71  THR   A OG1 
1618 C CG2 . THR   A 71  ? 0.1810 0.2139 0.2601 0.0171  -0.0275 0.0343  71  THR   A CG2 
1626 N N   . ASN   A 72  ? 0.1363 0.1498 0.2072 0.0164  0.0299  0.0240  72  ASN   A N   
1627 C CA  . ASN   A 72  ? 0.1396 0.1508 0.2085 0.0186  0.0408  0.0254  72  ASN   A CA  
1628 C C   . ASN   A 72  ? 0.1550 0.1491 0.2048 0.0139  0.0481  0.0157  72  ASN   A C   
1629 O O   . ASN   A 72  ? 0.1702 0.1464 0.2330 0.0178  0.0455  0.0044  72  ASN   A O   
1630 C CB  . ASN   A 72  ? 0.1635 0.1603 0.2042 0.0155  0.0382  0.0180  72  ASN   A CB  
1631 C CG  . ASN   A 72  ? 0.1832 0.1657 0.2100 0.0252  0.0349  0.0209  72  ASN   A CG  
1632 O OD1 . ASN   A 72  ? 0.2024 0.1970 0.2295 0.0233  0.0453  0.0244  72  ASN   A OD1 
1633 N ND2 . ASN   A 72  ? 0.1965 0.1738 0.2218 0.0481  0.0172  0.0156  72  ASN   A ND2 
1640 N N   . GLY   A 73  ? 0.1574 0.1466 0.1837 0.0061  0.0461  0.0074  73  GLY   A N   
1641 C CA  . GLY   A 73  ? 0.1618 0.1464 0.1696 -0.0103 0.0456  0.0052  73  GLY   A CA  
1642 C C   . GLY   A 73  ? 0.1626 0.1394 0.1599 0.0025  0.0534  0.0159  73  GLY   A C   
1643 O O   . GLY   A 73  ? 0.1565 0.1428 0.1789 0.0102  0.0407  0.0255  73  GLY   A O   
1647 N N   . PRO   A 74  ? 0.1697 0.1393 0.1642 -0.0125 0.0458  0.0100  74  PRO   A N   
1648 C CA  . PRO   A 74  ? 0.1657 0.1360 0.1674 -0.0029 0.0422  0.0136  74  PRO   A CA  
1649 C C   . PRO   A 74  ? 0.1539 0.1242 0.1621 0.0006  0.0294  0.0066  74  PRO   A C   
1650 O O   . PRO   A 74  ? 0.1620 0.1281 0.1892 0.0029  0.0346  -0.0045 74  PRO   A O   
1651 C CB  . PRO   A 74  ? 0.1789 0.1645 0.1822 -0.0037 0.0452  0.0256  74  PRO   A CB  
1652 C CG  . PRO   A 74  ? 0.2031 0.1931 0.2341 -0.0153 0.0354  0.0105  74  PRO   A CG  
1653 C CD  . PRO   A 74  ? 0.1880 0.1702 0.1901 -0.0194 0.0394  0.0033  74  PRO   A CD  
1661 N N   . LEU   A 75  ? 0.1502 0.1165 0.1563 -0.0013 0.0266  0.0065  75  LEU   A N   
1662 C CA  . LEU   A 75  ? 0.1528 0.1182 0.1383 0.0045  0.0134  0.0076  75  LEU   A CA  
1663 C C   . LEU   A 75  ? 0.1633 0.1304 0.1402 0.0075  0.0140  0.0157  75  LEU   A C   
1664 O O   . LEU   A 75  ? 0.1999 0.1473 0.1480 0.0116  0.0103  0.0088  75  LEU   A O   
1665 C CB  . LEU   A 75  ? 0.1564 0.1248 0.1284 -0.0087 0.0100  0.0185  75  LEU   A CB  
1666 C CG  . LEU   A 75  ? 0.1754 0.1572 0.1479 -0.0348 0.0095  0.0185  75  LEU   A CG  
1667 C CD1 . LEU   A 75  ? 0.1867 0.2020 0.1634 -0.0334 0.0098  0.0005  75  LEU   A CD1 
1668 C CD2 . LEU   A 75  ? 0.2013 0.2001 0.1946 -0.0162 0.0091  0.0244  75  LEU   A CD2 
1680 N N   . LYS   A 76  ? 0.1648 0.1291 0.1563 -0.0054 0.0129  0.0034  76  LYS   A N   
1681 C CA  . LYS   A 76  ? 0.1617 0.1502 0.1595 -0.0080 0.0149  -0.0106 76  LYS   A CA  
1682 C C   . LYS   A 76  ? 0.1592 0.1330 0.1328 -0.0032 0.0186  -0.0011 76  LYS   A C   
1683 O O   . LYS   A 76  ? 0.1599 0.1273 0.1274 -0.0029 0.0175  0.0078  76  LYS   A O   
1684 C CB  . LYS   A 76  ? 0.1618 0.1720 0.1955 0.0013  0.0167  -0.0298 76  LYS   A CB  
1685 C CG  . LYS   A 76  ? 0.1696 0.1643 0.2518 0.0078  0.0108  -0.0296 76  LYS   A CG  
1686 C CD  . LYS   A 76  ? 0.1752 0.1664 0.2936 0.0118  0.0003  -0.0375 76  LYS   A CD  
1687 C CE  . LYS   A 76  ? 0.1879 0.1874 0.3481 0.0055  0.0083  -0.0478 76  LYS   A CE  
1688 N NZ  . LYS   A 76  ? 0.1898 0.1847 0.3847 -0.0058 0.0005  -0.0563 76  LYS   A NZ  
1702 N N   . VAL   A 77  ? 0.1686 0.1384 0.1342 -0.0044 0.0276  0.0088  77  VAL   A N   
1703 C CA  . VAL   A 77  ? 0.1652 0.1397 0.1338 0.0071  0.0198  0.0117  77  VAL   A CA  
1704 C C   . VAL   A 77  ? 0.1565 0.1360 0.1230 0.0095  0.0182  0.0042  77  VAL   A C   
1705 O O   . VAL   A 77  ? 0.1642 0.1408 0.1248 0.0123  0.0282  -0.0007 77  VAL   A O   
1706 C CB  . VAL   A 77  ? 0.1826 0.1563 0.1458 0.0031  0.0119  0.0216  77  VAL   A CB  
1707 C CG1 . VAL   A 77  ? 0.1753 0.1704 0.1703 0.0098  0.0043  0.0093  77  VAL   A CG1 
1708 C CG2 . VAL   A 77  ? 0.2089 0.1674 0.1635 -0.0032 -0.0021 0.0271  77  VAL   A CG2 
1718 N N   . GLY   A 78  ? 0.1560 0.1337 0.1192 0.0049  0.0208  0.0085  78  GLY   A N   
1719 C CA  . GLY   A 78  ? 0.1493 0.1296 0.1365 0.0032  0.0242  0.0120  78  GLY   A CA  
1720 C C   . GLY   A 78  ? 0.1393 0.1240 0.1347 0.0037  0.0226  0.0091  78  GLY   A C   
1721 O O   . GLY   A 78  ? 0.1350 0.1288 0.1511 0.0006  0.0151  0.0212  78  GLY   A O   
1725 N N   . GLY   A 79  ? 0.1415 0.1210 0.1340 0.0015  0.0200  0.0111  79  GLY   A N   
1726 C CA  . GLY   A 79  ? 0.1385 0.1282 0.1471 -0.0035 0.0150  0.0074  79  GLY   A CA  
1727 C C   . GLY   A 79  ? 0.1254 0.1207 0.1369 -0.0018 0.0119  0.0014  79  GLY   A C   
1728 O O   . GLY   A 79  ? 0.1294 0.1268 0.1478 0.0175  0.0134  0.0048  79  GLY   A O   
1732 N N   . SER   A 80  ? 0.1205 0.1323 0.1598 -0.0025 0.0186  -0.0072 80  SER   A N   
1733 C CA  . SER   A 80  ? 0.1205 0.1275 0.1442 -0.0036 0.0090  0.0014  80  SER   A CA  
1734 C C   . SER   A 80  ? 0.1204 0.1243 0.1494 -0.0038 0.0126  0.0107  80  SER   A C   
1735 O O   . SER   A 80  ? 0.1198 0.1488 0.1823 0.0098  0.0148  -0.0000 80  SER   A O   
1736 C CB  . SER   A 80  ? 0.1362 0.1277 0.1642 -0.0087 0.0122  0.0064  80  SER   A CB  
1737 O OG  . SER   A 80  ? 0.1564 0.1290 0.2045 0.0026  -0.0012 0.0191  80  SER   A OG  
1743 N N   . CYS   A 81  ? 0.1143 0.1214 0.1414 0.0012  -0.0011 0.0079  81  CYS   A N   
1744 C CA  . CYS   A 81  ? 0.1145 0.1307 0.1418 -0.0020 -0.0050 0.0214  81  CYS   A CA  
1745 C C   . CYS   A 81  ? 0.1173 0.1269 0.1406 -0.0073 -0.0014 0.0253  81  CYS   A C   
1746 O O   . CYS   A 81  ? 0.1173 0.1526 0.1548 0.0017  0.0016  0.0302  81  CYS   A O   
1747 C CB  . CYS   A 81  ? 0.1245 0.1408 0.1563 -0.0105 -0.0027 0.0235  81  CYS   A CB  
1748 S SG  . CYS   A 81  ? 0.1353 0.1252 0.1589 -0.0134 0.0019  0.0095  81  CYS   A SG  
1754 N N   . VAL   A 82  ? 0.1182 0.1305 0.1466 -0.0027 -0.0128 0.0156  82  VAL   A N   
1755 C CA  . VAL   A 82  ? 0.1312 0.1406 0.1428 -0.0003 -0.0107 0.0216  82  VAL   A CA  
1756 C C   . VAL   A 82  ? 0.1288 0.1413 0.1480 -0.0017 -0.0086 0.0215  82  VAL   A C   
1757 O O   . VAL   A 82  ? 0.1209 0.1509 0.1741 -0.0013 -0.0050 -0.0010 82  VAL   A O   
1758 C CB  . VAL   A 82  ? 0.1605 0.1496 0.1479 0.0020  -0.0066 0.0246  82  VAL   A CB  
1759 C CG1 . VAL   A 82  ? 0.1843 0.1658 0.1680 0.0077  0.0021  0.0212  82  VAL   A CG1 
1760 C CG2 . VAL   A 82  ? 0.1650 0.1546 0.1745 -0.0011 -0.0068 0.0284  82  VAL   A CG2 
1770 N N   . LEU   A 83  ? 0.1214 0.1342 0.1423 -0.0077 -0.0122 0.0093  83  LEU   A N   
1771 C CA  . LEU   A 83  ? 0.1237 0.1396 0.1355 -0.0107 -0.0134 0.0027  83  LEU   A CA  
1772 C C   . LEU   A 83  ? 0.1298 0.1422 0.1274 -0.0059 -0.0092 0.0086  83  LEU   A C   
1773 O O   . LEU   A 83  ? 0.1423 0.1418 0.1356 -0.0123 -0.0046 0.0131  83  LEU   A O   
1774 C CB  . LEU   A 83  ? 0.1321 0.1469 0.1427 -0.0108 -0.0139 0.0118  83  LEU   A CB  
1775 C CG  . LEU   A 83  ? 0.1459 0.1570 0.1487 -0.0089 0.0059  0.0066  83  LEU   A CG  
1776 C CD1 . LEU   A 83  ? 0.1561 0.1537 0.1594 -0.0245 0.0042  0.0154  83  LEU   A CD1 
1777 C CD2 . LEU   A 83  ? 0.1411 0.1732 0.1669 -0.0133 0.0151  0.0098  83  LEU   A CD2 
1789 N N   . SER   A 84  ? 0.1466 0.1465 0.1314 -0.0116 -0.0093 0.0120  84  SER   A N   
1790 C CA  . SER   A 84  ? 0.1563 0.1523 0.1216 -0.0098 -0.0085 0.0066  84  SER   A CA  
1791 C C   . SER   A 84  ? 0.1607 0.1461 0.1211 -0.0157 -0.0010 0.0070  84  SER   A C   
1792 O O   . SER   A 84  ? 0.1542 0.1596 0.1237 -0.0141 -0.0059 0.0051  84  SER   A O   
1793 C CB  . SER   A 84  ? 0.1619 0.1735 0.1378 -0.0103 -0.0100 -0.0013 84  SER   A CB  
1794 O OG  . SER   A 84  ? 0.1689 0.1917 0.1466 -0.0072 -0.0186 -0.0123 84  SER   A OG  
1800 N N   . GLY   A 85  ? 0.1740 0.1605 0.1261 -0.0201 0.0110  0.0057  85  GLY   A N   
1801 C CA  . GLY   A 85  ? 0.1731 0.1674 0.1415 -0.0286 0.0154  -0.0025 85  GLY   A CA  
1802 C C   . GLY   A 85  ? 0.1714 0.1752 0.1222 -0.0224 0.0018  -0.0024 85  GLY   A C   
1803 O O   . GLY   A 85  ? 0.1693 0.1868 0.1320 -0.0278 0.0121  -0.0134 85  GLY   A O   
1807 N N   . HIS   A 86  ? 0.1749 0.1602 0.1186 -0.0172 0.0012  -0.0010 86  HIS   A N   
1808 C CA  . HIS   A 86  ? 0.1887 0.1731 0.1153 -0.0198 -0.0037 0.0020  86  HIS   A CA  
1809 C C   . HIS   A 86  ? 0.2092 0.1794 0.1174 -0.0181 -0.0067 -0.0014 86  HIS   A C   
1810 O O   . HIS   A 86  ? 0.2191 0.2031 0.1291 -0.0111 0.0103  0.0024  86  HIS   A O   
1811 C CB  . HIS   A 86  ? 0.1811 0.1636 0.1291 -0.0157 0.0023  0.0005  86  HIS   A CB  
1812 C CG  . HIS   A 86  ? 0.1765 0.1646 0.1345 -0.0102 0.0090  0.0068  86  HIS   A CG  
1813 N ND1 . HIS   A 86  ? 0.1812 0.1675 0.1684 -0.0238 0.0024  0.0080  86  HIS   A ND1 
1814 C CD2 . HIS   A 86  ? 0.1767 0.1626 0.1217 -0.0005 0.0047  0.0098  86  HIS   A CD2 
1815 C CE1 . HIS   A 86  ? 0.1768 0.1686 0.1616 -0.0147 0.0157  0.0142  86  HIS   A CE1 
1816 N NE2 . HIS   A 86  ? 0.1768 0.1622 0.1394 0.0019  0.0136  0.0265  86  HIS   A NE2 
1824 N N   . ASN   A 87  ? 0.2228 0.1872 0.1194 -0.0131 0.0192  -0.0105 87  ASN   A N   
1825 C CA  . ASN   A 87  ? 0.2443 0.2019 0.1307 -0.0139 0.0448  -0.0097 87  ASN   A CA  
1826 C C   . ASN   A 87  ? 0.2427 0.2187 0.1663 -0.0180 0.0609  0.0010  87  ASN   A C   
1827 O O   . ASN   A 87  ? 0.2629 0.2369 0.2123 -0.0297 0.0850  -0.0062 87  ASN   A O   
1828 C CB  . ASN   A 87  ? 0.2608 0.2117 0.1450 -0.0065 0.0470  -0.0170 87  ASN   A CB  
1829 C CG  . ASN   A 87  ? 0.2715 0.2171 0.1531 0.0025  0.0568  -0.0091 87  ASN   A CG  
1830 O OD1 . ASN   A 87  ? 0.2881 0.2156 0.1631 0.0195  0.0544  -0.0011 87  ASN   A OD1 
1831 N ND2 . ASN   A 87  ? 0.2743 0.2378 0.1685 0.0020  0.0564  -0.0046 87  ASN   A ND2 
1838 N N   . LEU   A 88  ? 0.2148 0.2110 0.1667 -0.0263 0.0395  0.0124  88  LEU   A N   
1839 C CA  . LEU   A 88  ? 0.1942 0.2110 0.1795 -0.0345 0.0390  0.0211  88  LEU   A CA  
1840 C C   . LEU   A 88  ? 0.1908 0.2106 0.1735 -0.0320 0.0364  0.0253  88  LEU   A C   
1841 O O   . LEU   A 88  ? 0.1941 0.2198 0.2068 -0.0350 0.0388  0.0392  88  LEU   A O   
1842 C CB  . LEU   A 88  ? 0.1948 0.2212 0.1943 -0.0430 0.0037  0.0336  88  LEU   A CB  
1843 C CG  . LEU   A 88  ? 0.2136 0.2351 0.2228 -0.0389 -0.0134 0.0337  88  LEU   A CG  
1844 C CD1 . LEU   A 88  ? 0.2243 0.2434 0.2158 -0.0382 -0.0158 0.0176  88  LEU   A CD1 
1845 C CD2 . LEU   A 88  ? 0.2257 0.2441 0.2586 -0.0310 -0.0141 0.0252  88  LEU   A CD2 
1857 N N   . ALA   A 89  ? 0.1915 0.1977 0.1450 -0.0263 0.0272  0.0040  89  ALA   A N   
1858 C CA  . ALA   A 89  ? 0.1992 0.1935 0.1286 -0.0232 0.0166  0.0140  89  ALA   A CA  
1859 C C   . ALA   A 89  ? 0.2016 0.1980 0.1328 -0.0213 0.0008  0.0105  89  ALA   A C   
1860 O O   . ALA   A 89  ? 0.1982 0.1962 0.1693 -0.0283 -0.0060 -0.0168 89  ALA   A O   
1861 C CB  . ALA   A 89  ? 0.1942 0.1923 0.1199 -0.0202 0.0095  0.0149  89  ALA   A CB  
1867 N N   . LYS   A 90  ? 0.2116 0.2132 0.1345 -0.0244 -0.0197 0.0177  90  LYS   A N   
1868 C CA  . LYS   A 90  ? 0.2217 0.2257 0.1347 -0.0251 -0.0318 0.0154  90  LYS   A CA  
1869 C C   . LYS   A 90  ? 0.1990 0.2112 0.1259 -0.0233 -0.0290 0.0054  90  LYS   A C   
1870 O O   . LYS   A 90  ? 0.2030 0.2308 0.1590 -0.0281 -0.0333 -0.0039 90  LYS   A O   
1871 C CB  . LYS   A 90  ? 0.2475 0.2566 0.1716 -0.0229 -0.0382 0.0333  90  LYS   A CB  
1872 C CG  . LYS   A 90  ? 0.2769 0.2872 0.2716 -0.0209 -0.0274 0.0402  90  LYS   A CG  
1873 C CD  . LYS   A 90  ? 0.3062 0.3111 0.3658 -0.0205 -0.0127 0.0507  90  LYS   A CD  
1874 C CE  . LYS   A 90  ? 0.3288 0.3313 0.4358 -0.0198 -0.0013 0.0528  90  LYS   A CE  
1875 N NZ  . LYS   A 90  ? 0.3433 0.3485 0.4838 -0.0182 0.0027  0.0465  90  LYS   A NZ  
1889 N N   . HIS   A 91  ? 0.1868 0.1790 0.1031 -0.0217 -0.0282 0.0124  91  HIS   A N   
1890 C CA  . HIS   A 91  ? 0.1736 0.1649 0.1109 -0.0168 -0.0299 0.0130  91  HIS   A CA  
1891 C C   . HIS   A 91  ? 0.1512 0.1532 0.1011 -0.0152 -0.0157 0.0140  91  HIS   A C   
1892 O O   . HIS   A 91  ? 0.1515 0.1665 0.1222 -0.0233 -0.0063 0.0142  91  HIS   A O   
1893 C CB  . HIS   A 91  ? 0.1871 0.1889 0.1595 0.0067  -0.0408 0.0126  91  HIS   A CB  
1894 C CG  . HIS   A 91  ? 0.2264 0.2358 0.2339 0.0146  -0.0671 0.0069  91  HIS   A CG  
1895 N ND1 . HIS   A 91  ? 0.2387 0.2626 0.2757 0.0174  -0.0737 -0.0101 91  HIS   A ND1 
1896 C CD2 . HIS   A 91  ? 0.2501 0.2560 0.2592 0.0210  -0.0789 0.0155  91  HIS   A CD2 
1897 C CE1 . HIS   A 91  ? 0.2490 0.2721 0.2893 0.0213  -0.0748 0.0008  91  HIS   A CE1 
1898 N NE2 . HIS   A 91  ? 0.2601 0.2697 0.2842 0.0270  -0.0795 0.0080  91  HIS   A NE2 
1906 N N   . CYS   A 92  ? 0.1411 0.1482 0.1116 -0.0137 -0.0098 0.0151  92  CYS   A N   
1907 C CA  . CYS   A 92  ? 0.1328 0.1399 0.1216 -0.0106 -0.0019 0.0113  92  CYS   A CA  
1908 C C   . CYS   A 92  ? 0.1252 0.1371 0.1156 -0.0151 0.0008  0.0138  92  CYS   A C   
1909 O O   . CYS   A 92  ? 0.1279 0.1452 0.1328 -0.0171 -0.0037 0.0088  92  CYS   A O   
1910 C CB  . CYS   A 92  ? 0.1371 0.1422 0.1337 -0.0020 -0.0032 0.0107  92  CYS   A CB  
1911 S SG  . CYS   A 92  ? 0.1329 0.1300 0.1366 -0.0108 -0.0022 0.0097  92  CYS   A SG  
1917 N N   . LEU   A 93  ? 0.1259 0.1236 0.1203 -0.0090 0.0053  0.0150  93  LEU   A N   
1918 C CA  . LEU   A 93  ? 0.1173 0.1243 0.1224 -0.0065 -0.0001 0.0113  93  LEU   A CA  
1919 C C   . LEU   A 93  ? 0.1145 0.1103 0.1189 -0.0033 0.0046  0.0058  93  LEU   A C   
1920 O O   . LEU   A 93  ? 0.1135 0.1216 0.1183 -0.0021 0.0032  0.0112  93  LEU   A O   
1921 C CB  . LEU   A 93  ? 0.1235 0.1217 0.1386 -0.0046 -0.0044 0.0203  93  LEU   A CB  
1922 C CG  . LEU   A 93  ? 0.1292 0.1239 0.1347 -0.0031 -0.0008 0.0191  93  LEU   A CG  
1923 C CD1 . LEU   A 93  ? 0.1349 0.1261 0.1520 0.0012  0.0086  0.0135  93  LEU   A CD1 
1924 C CD2 . LEU   A 93  ? 0.1467 0.1226 0.1504 -0.0105 0.0009  0.0132  93  LEU   A CD2 
1936 N N   . HIS   A 94  ? 0.1102 0.1075 0.1245 -0.0031 0.0041  0.0117  94  HIS   A N   
1937 C CA  . HIS   A 94  ? 0.1097 0.1138 0.1270 -0.0065 0.0012  0.0123  94  HIS   A CA  
1938 C C   . HIS   A 94  ? 0.1078 0.1100 0.1279 -0.0068 0.0025  0.0099  94  HIS   A C   
1939 O O   . HIS   A 94  ? 0.1086 0.1313 0.1566 0.0028  0.0013  -0.0069 94  HIS   A O   
1940 C CB  . HIS   A 94  ? 0.1090 0.1122 0.1320 -0.0028 -0.0021 0.0142  94  HIS   A CB  
1941 C CG  . HIS   A 94  ? 0.1128 0.1141 0.1211 -0.0066 -0.0061 0.0199  94  HIS   A CG  
1942 N ND1 . HIS   A 94  ? 0.1156 0.1146 0.1332 -0.0036 0.0040  0.0157  94  HIS   A ND1 
1943 C CD2 . HIS   A 94  ? 0.1193 0.1219 0.1331 -0.0031 -0.0042 0.0113  94  HIS   A CD2 
1944 C CE1 . HIS   A 94  ? 0.1182 0.1131 0.1312 -0.0036 -0.0042 0.0063  94  HIS   A CE1 
1945 N NE2 . HIS   A 94  ? 0.1247 0.1173 0.1328 -0.0085 -0.0028 0.0042  94  HIS   A NE2 
1953 N N   . VAL   A 95  ? 0.1090 0.1069 0.1031 -0.0027 0.0079  0.0028  95  VAL   A N   
1954 C CA  . VAL   A 95  ? 0.1136 0.1149 0.1102 -0.0028 0.0113  0.0143  95  VAL   A CA  
1955 C C   . VAL   A 95  ? 0.1135 0.1127 0.0993 -0.0102 0.0055  0.0073  95  VAL   A C   
1956 O O   . VAL   A 95  ? 0.1220 0.1207 0.1177 0.0076  0.0070  0.0068  95  VAL   A O   
1957 C CB  . VAL   A 95  ? 0.1179 0.1174 0.1338 -0.0117 0.0031  0.0050  95  VAL   A CB  
1958 C CG1 . VAL   A 95  ? 0.1308 0.1204 0.1452 -0.0135 0.0066  -0.0034 95  VAL   A CG1 
1959 C CG2 . VAL   A 95  ? 0.1222 0.1194 0.1330 -0.0141 0.0094  0.0204  95  VAL   A CG2 
1969 N N   . VAL   A 96  ? 0.1203 0.1171 0.0943 -0.0051 0.0018  0.0126  96  VAL   A N   
1970 C CA  . VAL   A 96  ? 0.1258 0.1137 0.1137 -0.0023 0.0109  0.0139  96  VAL   A CA  
1971 C C   . VAL   A 96  ? 0.1306 0.1240 0.1166 -0.0020 0.0144  0.0128  96  VAL   A C   
1972 O O   . VAL   A 96  ? 0.1368 0.1291 0.1390 -0.0044 0.0174  -0.0017 96  VAL   A O   
1973 C CB  . VAL   A 96  ? 0.1327 0.1211 0.1188 -0.0022 0.0229  0.0121  96  VAL   A CB  
1974 C CG1 . VAL   A 96  ? 0.1435 0.1307 0.1088 -0.0027 0.0160  0.0127  96  VAL   A CG1 
1975 C CG2 . VAL   A 96  ? 0.1322 0.1308 0.1314 -0.0135 0.0149  0.0135  96  VAL   A CG2 
1985 N N   A GLY   A 97  ? 0.1256 0.1280 0.1202 -0.0093 0.0104  0.0116  97  GLY   A N   
1986 N N   B GLY   A 97  ? 0.1348 0.1323 0.1188 -0.0033 0.0099  0.0113  97  GLY   A N   
1987 C CA  A GLY   A 97  ? 0.1333 0.1388 0.1217 -0.0055 0.0015  0.0141  97  GLY   A CA  
1988 C CA  B GLY   A 97  ? 0.1407 0.1394 0.1219 -0.0043 0.0062  0.0117  97  GLY   A CA  
1989 C C   A GLY   A 97  ? 0.1365 0.1506 0.1061 -0.0040 0.0068  0.0062  97  GLY   A C   
1990 C C   B GLY   A 97  ? 0.1461 0.1468 0.1273 -0.0055 0.0042  0.0110  97  GLY   A C   
1991 O O   A GLY   A 97  ? 0.1465 0.1517 0.1280 -0.0070 0.0031  0.0128  97  GLY   A O   
1992 O O   B GLY   A 97  ? 0.1478 0.1484 0.1286 -0.0079 0.0031  0.0131  97  GLY   A O   
1999 N N   A PRO   A 98  ? 0.1503 0.1535 0.0909 0.0039  -0.0003 0.0165  98  PRO   A N   
2000 N N   B PRO   A 98  ? 0.1523 0.1522 0.1372 -0.0038 0.0017  0.0092  98  PRO   A N   
2001 C CA  A PRO   A 98  ? 0.1562 0.1708 0.1114 -0.0005 0.0003  0.0066  98  PRO   A CA  
2002 C CA  B PRO   A 98  ? 0.1584 0.1575 0.1461 -0.0048 -0.0009 0.0049  98  PRO   A CA  
2003 C C   A PRO   A 98  ? 0.1594 0.1799 0.1002 -0.0123 0.0007  0.0231  98  PRO   A C   
2004 C C   B PRO   A 98  ? 0.1702 0.1655 0.1540 -0.0036 -0.0007 0.0071  98  PRO   A C   
2005 O O   A PRO   A 98  ? 0.1558 0.1594 0.1265 -0.0080 -0.0029 0.0203  98  PRO   A O   
2006 O O   B PRO   A 98  ? 0.1702 0.1685 0.1613 -0.0051 0.0029  0.0049  98  PRO   A O   
2007 C CB  A PRO   A 98  ? 0.1683 0.1753 0.1000 0.0040  -0.0046 -0.0027 98  PRO   A CB  
2008 C CB  B PRO   A 98  ? 0.1559 0.1537 0.1411 -0.0051 -0.0014 0.0037  98  PRO   A CB  
2009 C CG  A PRO   A 98  ? 0.1720 0.1665 0.1115 0.0050  -0.0111 -0.0055 98  PRO   A CG  
2010 C CG  B PRO   A 98  ? 0.1556 0.1515 0.1420 -0.0040 -0.0015 0.0064  98  PRO   A CG  
2011 C CD  A PRO   A 98  ? 0.1626 0.1522 0.1008 0.0069  -0.0049 0.0111  98  PRO   A CD  
2012 C CD  B PRO   A 98  ? 0.1531 0.1514 0.1395 -0.0029 -0.0014 0.0093  98  PRO   A CD  
2027 N N   A ASN   A 99  ? 0.1680 0.2039 0.1126 -0.0094 0.0011  0.0461  99  ASN   A N   
2028 N N   B ASN   A 99  ? 0.1848 0.1721 0.1597 0.0009  -0.0015 0.0107  99  ASN   A N   
2029 C CA  A ASN   A 99  ? 0.1896 0.2191 0.1267 -0.0147 -0.0029 0.0652  99  ASN   A CA  
2030 C CA  B ASN   A 99  ? 0.1980 0.1802 0.1718 0.0057  -0.0010 0.0115  99  ASN   A CA  
2031 C C   A ASN   A 99  ? 0.2089 0.2617 0.1093 -0.0250 0.0025  0.0640  99  ASN   A C   
2032 C C   B ASN   A 99  ? 0.2094 0.1901 0.1859 0.0068  -0.0075 0.0145  99  ASN   A C   
2033 O O   A ASN   A 99  ? 0.2212 0.2918 0.1221 -0.0132 -0.0059 0.0555  99  ASN   A O   
2034 O O   B ASN   A 99  ? 0.2095 0.1896 0.1827 0.0076  -0.0148 0.0194  99  ASN   A O   
2035 C CB  A ASN   A 99  ? 0.1888 0.2074 0.1549 -0.0150 -0.0175 0.0732  99  ASN   A CB  
2036 C CB  B ASN   A 99  ? 0.1992 0.1775 0.1721 0.0107  0.0015  0.0074  99  ASN   A CB  
2037 C CG  A ASN   A 99  ? 0.1867 0.2027 0.1922 -0.0157 -0.0223 0.0516  99  ASN   A CG  
2038 C CG  B ASN   A 99  ? 0.2000 0.1755 0.1743 0.0156  0.0063  0.0008  99  ASN   A CG  
2039 O OD1 A ASN   A 99  ? 0.2007 0.2183 0.1915 -0.0063 -0.0270 0.0402  99  ASN   A OD1 
2040 O OD1 B ASN   A 99  ? 0.1969 0.1696 0.1610 0.0217  0.0118  0.0061  99  ASN   A OD1 
2041 N ND2 A ASN   A 99  ? 0.1829 0.1948 0.2232 -0.0073 -0.0219 0.0537  99  ASN   A ND2 
2042 N ND2 B ASN   A 99  ? 0.2033 0.1812 0.1880 0.0148  0.0032  -0.0072 99  ASN   A ND2 
2055 N N   A VAL   A 100 ? 0.2264 0.2747 0.1144 -0.0420 -0.0235 0.0531  100 VAL   A N   
2056 N N   B VAL   A 100 ? 0.2211 0.2013 0.2052 0.0063  -0.0071 0.0145  100 VAL   A N   
2057 C CA  A VAL   A 100 ? 0.2535 0.3027 0.1463 -0.0502 -0.0328 0.0553  100 VAL   A CA  
2058 C CA  B VAL   A 100 ? 0.2325 0.2115 0.2257 0.0076  -0.0076 0.0087  100 VAL   A CA  
2059 C C   A VAL   A 100 ? 0.2667 0.3226 0.1440 -0.0542 -0.0444 0.0858  100 VAL   A C   
2060 C C   B VAL   A 100 ? 0.2410 0.2175 0.2334 0.0091  -0.0088 0.0042  100 VAL   A C   
2061 O O   A VAL   A 100 ? 0.2768 0.3353 0.1620 -0.0520 -0.0214 0.0843  100 VAL   A O   
2062 O O   B VAL   A 100 ? 0.2403 0.2155 0.2333 0.0083  -0.0092 -0.0010 100 VAL   A O   
2063 C CB  A VAL   A 100 ? 0.2716 0.3088 0.1885 -0.0559 -0.0377 0.0389  100 VAL   A CB  
2064 C CB  B VAL   A 100 ? 0.2358 0.2165 0.2382 0.0091  -0.0050 0.0051  100 VAL   A CB  
2065 C CG1 A VAL   A 100 ? 0.2729 0.3166 0.2100 -0.0601 -0.0345 0.0319  100 VAL   A CG1 
2066 C CG1 B VAL   A 100 ? 0.2359 0.2166 0.2423 0.0101  -0.0025 0.0025  100 VAL   A CG1 
2067 C CG2 A VAL   A 100 ? 0.2826 0.3114 0.1977 -0.0584 -0.0301 0.0344  100 VAL   A CG2 
2068 C CG2 B VAL   A 100 ? 0.2369 0.2189 0.2446 0.0101  -0.0049 0.0042  100 VAL   A CG2 
2087 N N   A ASN   A 101 ? 0.2784 0.3306 0.1764 -0.0561 -0.0539 0.1147  101 ASN   A N   
2088 N N   B ASN   A 101 ? 0.2512 0.2273 0.2407 0.0098  -0.0082 0.0028  101 ASN   A N   
2089 C CA  A ASN   A 101 ? 0.3055 0.3404 0.2132 -0.0584 -0.0537 0.1324  101 ASN   A CA  
2090 C CA  B ASN   A 101 ? 0.2621 0.2382 0.2483 0.0103  -0.0059 0.0024  101 ASN   A CA  
2091 C C   A ASN   A 101 ? 0.3298 0.3675 0.2368 -0.0620 -0.0236 0.1618  101 ASN   A C   
2092 C C   B ASN   A 101 ? 0.2723 0.2511 0.2598 0.0089  -0.0036 0.0034  101 ASN   A C   
2093 O O   A ASN   A 101 ? 0.3435 0.3714 0.2776 -0.0566 -0.0250 0.1567  101 ASN   A O   
2094 O O   B ASN   A 101 ? 0.2741 0.2509 0.2575 0.0088  -0.0039 0.0030  101 ASN   A O   
2095 C CB  A ASN   A 101 ? 0.3107 0.3237 0.2113 -0.0543 -0.0783 0.1172  101 ASN   A CB  
2096 C CB  B ASN   A 101 ? 0.2629 0.2376 0.2460 0.0111  -0.0060 0.0022  101 ASN   A CB  
2097 C CG  A ASN   A 101 ? 0.3173 0.3081 0.2063 -0.0543 -0.0916 0.0841  101 ASN   A CG  
2098 C CG  B ASN   A 101 ? 0.2644 0.2387 0.2478 0.0112  -0.0061 0.0035  101 ASN   A CG  
2099 O OD1 A ASN   A 101 ? 0.3173 0.3121 0.2240 -0.0485 -0.0872 0.0437  101 ASN   A OD1 
2100 O OD1 B ASN   A 101 ? 0.2661 0.2384 0.2519 0.0119  -0.0062 0.0050  101 ASN   A OD1 
2101 N ND2 A ASN   A 101 ? 0.3228 0.2925 0.1985 -0.0589 -0.0937 0.0915  101 ASN   A ND2 
2102 N ND2 B ASN   A 101 ? 0.2654 0.2398 0.2473 0.0112  -0.0043 0.0022  101 ASN   A ND2 
2115 N N   A LYS   A 102 ? 0.3367 0.3952 0.2608 -0.0702 -0.0014 0.1558  102 LYS   A N   
2116 N N   B LYS   A 102 ? 0.2802 0.2636 0.2773 0.0079  -0.0019 0.0054  102 LYS   A N   
2117 C CA  A LYS   A 102 ? 0.3510 0.4213 0.2646 -0.0702 0.0050  0.1426  102 LYS   A CA  
2118 C CA  B LYS   A 102 ? 0.2874 0.2759 0.2885 0.0055  -0.0017 0.0079  102 LYS   A CA  
2119 C C   A LYS   A 102 ? 0.3567 0.4419 0.2380 -0.0585 0.0044  0.1341  102 LYS   A C   
2120 C C   B LYS   A 102 ? 0.2916 0.2816 0.2897 0.0048  -0.0025 0.0107  102 LYS   A C   
2121 O O   A LYS   A 102 ? 0.3619 0.4558 0.2406 -0.0528 0.0087  0.1232  102 LYS   A O   
2122 O O   B LYS   A 102 ? 0.2929 0.2820 0.2919 0.0062  -0.0019 0.0121  102 LYS   A O   
2123 C CB  A LYS   A 102 ? 0.3625 0.4271 0.3073 -0.0766 -0.0004 0.1207  102 LYS   A CB  
2124 C CB  B LYS   A 102 ? 0.2900 0.2817 0.2969 0.0052  -0.0027 0.0082  102 LYS   A CB  
2125 C CG  A LYS   A 102 ? 0.3740 0.4303 0.3471 -0.0802 -0.0098 0.0920  102 LYS   A CG  
2126 C CG  B LYS   A 102 ? 0.2924 0.2874 0.3037 0.0048  -0.0047 0.0083  102 LYS   A CG  
2127 C CD  A LYS   A 102 ? 0.3866 0.4350 0.3828 -0.0805 -0.0216 0.0621  102 LYS   A CD  
2128 C CD  B LYS   A 102 ? 0.2943 0.2921 0.3091 0.0048  -0.0069 0.0085  102 LYS   A CD  
2129 C CE  A LYS   A 102 ? 0.3972 0.4391 0.4114 -0.0791 -0.0296 0.0414  102 LYS   A CE  
2130 C CE  B LYS   A 102 ? 0.2964 0.2956 0.3136 0.0051  -0.0084 0.0088  102 LYS   A CE  
2131 N NZ  A LYS   A 102 ? 0.4034 0.4405 0.4256 -0.0813 -0.0308 0.0283  102 LYS   A NZ  
2132 N NZ  B LYS   A 102 ? 0.2976 0.2974 0.3163 0.0057  -0.0096 0.0083  102 LYS   A NZ  
2159 N N   A GLY   A 103 ? 0.3551 0.4521 0.2337 -0.0473 -0.0076 0.1084  103 GLY   A N   
2160 N N   B GLY   A 103 ? 0.2939 0.2876 0.2879 0.0042  -0.0061 0.0110  103 GLY   A N   
2161 C CA  A GLY   A 103 ? 0.3535 0.4553 0.2177 -0.0384 -0.0096 0.0906  103 GLY   A CA  
2162 C CA  B GLY   A 103 ? 0.2956 0.2918 0.2844 0.0045  -0.0091 0.0126  103 GLY   A CA  
2163 C C   A GLY   A 103 ? 0.3474 0.4577 0.2194 -0.0331 -0.0019 0.0657  103 GLY   A C   
2164 C C   B GLY   A 103 ? 0.2970 0.2954 0.2799 0.0041  -0.0108 0.0118  103 GLY   A C   
2165 O O   A GLY   A 103 ? 0.3575 0.4671 0.2405 -0.0268 -0.0019 0.0483  103 GLY   A O   
2166 O O   B GLY   A 103 ? 0.2979 0.2969 0.2813 0.0057  -0.0121 0.0122  103 GLY   A O   
2173 N N   A GLU   A 104 ? 0.3253 0.4454 0.1757 -0.0376 0.0031  0.0552  104 GLU   A N   
2174 N N   B GLU   A 104 ? 0.2964 0.2963 0.2721 0.0016  -0.0124 0.0128  104 GLU   A N   
2175 C CA  A GLU   A 104 ? 0.2977 0.4297 0.1488 -0.0494 0.0069  0.0471  104 GLU   A CA  
2176 C CA  B GLU   A 104 ? 0.2961 0.2967 0.2659 -0.0013 -0.0129 0.0122  104 GLU   A CA  
2177 C C   A GLU   A 104 ? 0.2911 0.4338 0.1491 -0.0540 0.0158  0.0236  104 GLU   A C   
2178 C C   B GLU   A 104 ? 0.2977 0.2990 0.2709 -0.0002 -0.0102 0.0103  104 GLU   A C   
2179 O O   A GLU   A 104 ? 0.2829 0.4326 0.1800 -0.0549 0.0084  0.0199  104 GLU   A O   
2180 O O   B GLU   A 104 ? 0.2982 0.2975 0.2704 0.0003  -0.0118 0.0126  104 GLU   A O   
2181 C CB  A GLU   A 104 ? 0.2717 0.4057 0.1297 -0.0559 0.0121  0.0682  104 GLU   A CB  
2182 C CB  B GLU   A 104 ? 0.2950 0.2951 0.2592 -0.0049 -0.0146 0.0126  104 GLU   A CB  
2183 C CG  A GLU   A 104 ? 0.2529 0.3907 0.1409 -0.0573 0.0109  0.0802  104 GLU   A CG  
2184 C CG  B GLU   A 104 ? 0.2946 0.2946 0.2564 -0.0075 -0.0164 0.0129  104 GLU   A CG  
2185 C CD  A GLU   A 104 ? 0.2332 0.3748 0.1432 -0.0576 0.0079  0.0898  104 GLU   A CD  
2186 C CD  B GLU   A 104 ? 0.2947 0.2945 0.2550 -0.0099 -0.0176 0.0121  104 GLU   A CD  
2187 O OE1 A GLU   A 104 ? 0.2156 0.3621 0.1323 -0.0569 0.0020  0.0835  104 GLU   A OE1 
2188 O OE1 B GLU   A 104 ? 0.2951 0.2958 0.2539 -0.0103 -0.0193 0.0122  104 GLU   A OE1 
2189 O OE2 A GLU   A 104 ? 0.2455 0.3701 0.1676 -0.0559 0.0085  0.1040  104 GLU   A OE2 
2190 O OE2 B GLU   A 104 ? 0.2951 0.2940 0.2570 -0.0106 -0.0177 0.0106  104 GLU   A OE2 
2203 N N   A ASP   A 105 ? 0.2957 0.4393 0.1631 -0.0547 0.0248  -0.0050 105 ASP   A N   
2204 N N   B ASP   A 105 ? 0.2997 0.3023 0.2816 0.0001  -0.0068 0.0057  105 ASP   A N   
2205 C CA  A ASP   A 105 ? 0.2988 0.4414 0.1982 -0.0480 0.0325  -0.0374 105 ASP   A CA  
2206 C CA  B ASP   A 105 ? 0.3014 0.3046 0.2949 0.0011  -0.0027 -0.0007 105 ASP   A CA  
2207 C C   A ASP   A 105 ? 0.2680 0.4233 0.1669 -0.0539 0.0217  -0.0532 105 ASP   A C   
2208 C C   B ASP   A 105 ? 0.2995 0.3021 0.2850 -0.0030 -0.0009 -0.0039 105 ASP   A C   
2209 O O   A ASP   A 105 ? 0.2477 0.4076 0.1265 -0.0537 0.0160  -0.0689 105 ASP   A O   
2210 O O   B ASP   A 105 ? 0.2997 0.3019 0.2780 -0.0024 -0.0008 -0.0036 105 ASP   A O   
2211 C CB  A ASP   A 105 ? 0.3289 0.4640 0.2697 -0.0372 0.0481  -0.0532 105 ASP   A CB  
2212 C CB  B ASP   A 105 ? 0.3050 0.3086 0.3190 0.0059  -0.0001 -0.0040 105 ASP   A CB  
2213 C CG  A ASP   A 105 ? 0.3553 0.4805 0.3325 -0.0265 0.0531  -0.0699 105 ASP   A CG  
2214 C CG  B ASP   A 105 ? 0.3083 0.3114 0.3403 0.0105  0.0025  -0.0078 105 ASP   A CG  
2215 O OD1 A ASP   A 105 ? 0.3625 0.4856 0.3376 -0.0253 0.0542  -0.0859 105 ASP   A OD1 
2216 O OD1 B ASP   A 105 ? 0.3091 0.3115 0.3457 0.0114  0.0024  -0.0097 105 ASP   A OD1 
2217 O OD2 A ASP   A 105 ? 0.3710 0.4878 0.3800 -0.0229 0.0547  -0.0650 105 ASP   A OD2 
2218 O OD2 B ASP   A 105 ? 0.3099 0.3129 0.3503 0.0129  0.0043  -0.0086 105 ASP   A OD2 
2227 N N   A ILE   A 106 ? 0.2537 0.4065 0.1921 -0.0565 0.0005  -0.0531 106 ILE   A N   
2228 N N   B ILE   A 106 ? 0.2967 0.2995 0.2830 -0.0080 -0.0002 -0.0070 106 ILE   A N   
2229 C CA  A ILE   A 106 ? 0.2313 0.3910 0.2172 -0.0653 -0.0208 -0.0668 106 ILE   A CA  
2230 C CA  B ILE   A 106 ? 0.2927 0.2969 0.2824 -0.0147 0.0012  -0.0107 106 ILE   A CA  
2231 C C   A ILE   A 106 ? 0.2161 0.3652 0.2271 -0.0785 -0.0231 -0.0821 106 ILE   A C   
2232 C C   B ILE   A 106 ? 0.2847 0.2895 0.2782 -0.0217 0.0081  -0.0151 106 ILE   A C   
2233 O O   A ILE   A 106 ? 0.1968 0.3572 0.2301 -0.0803 -0.0011 -0.0864 106 ILE   A O   
2234 O O   B ILE   A 106 ? 0.2846 0.2897 0.2763 -0.0220 0.0093  -0.0165 106 ILE   A O   
2235 C CB  A ILE   A 106 ? 0.2335 0.4030 0.2670 -0.0538 -0.0351 -0.0476 106 ILE   A CB  
2236 C CB  B ILE   A 106 ? 0.2963 0.3016 0.2893 -0.0147 -0.0039 -0.0078 106 ILE   A CB  
2237 C CG1 A ILE   A 106 ? 0.2268 0.4057 0.2987 -0.0415 -0.0393 -0.0285 106 ILE   A CG1 
2238 C CG1 B ILE   A 106 ? 0.2972 0.3034 0.2935 -0.0144 -0.0058 -0.0049 106 ILE   A CG1 
2239 C CG2 A ILE   A 106 ? 0.2376 0.4061 0.2796 -0.0537 -0.0431 -0.0502 106 ILE   A CG2 
2240 C CG2 B ILE   A 106 ? 0.2975 0.3029 0.2907 -0.0147 -0.0057 -0.0083 106 ILE   A CG2 
2241 C CD1 A ILE   A 106 ? 0.2247 0.4045 0.3164 -0.0312 -0.0329 -0.0204 106 ILE   A CD1 
2242 C CD1 B ILE   A 106 ? 0.2978 0.3037 0.2957 -0.0138 -0.0061 -0.0038 106 ILE   A CD1 
2265 N N   A GLN   A 107 ? 0.2321 0.3455 0.2548 -0.0784 -0.0176 -0.0931 107 GLN   A N   
2266 N N   B GLN   A 107 ? 0.2760 0.2808 0.2779 -0.0280 0.0151  -0.0191 107 GLN   A N   
2267 C CA  A GLN   A 107 ? 0.2602 0.3264 0.3261 -0.0628 0.0062  -0.0907 107 GLN   A CA  
2268 C CA  B GLN   A 107 ? 0.2668 0.2728 0.2837 -0.0340 0.0213  -0.0259 107 GLN   A CA  
2269 C C   A GLN   A 107 ? 0.2363 0.2744 0.3008 -0.0511 0.0324  -0.0634 107 GLN   A C   
2270 C C   B GLN   A 107 ? 0.2401 0.2528 0.2580 -0.0409 0.0301  -0.0376 107 GLN   A C   
2271 O O   A GLN   A 107 ? 0.2423 0.2653 0.3481 -0.0424 0.0429  -0.0603 107 GLN   A O   
2272 O O   B GLN   A 107 ? 0.2438 0.2532 0.2663 -0.0413 0.0309  -0.0342 107 GLN   A O   
2273 C CB  A GLN   A 107 ? 0.3066 0.3584 0.4231 -0.0664 -0.0041 -0.1007 107 GLN   A CB  
2274 C CB  B GLN   A 107 ? 0.2823 0.2842 0.3148 -0.0346 0.0177  -0.0192 107 GLN   A CB  
2275 C CG  A GLN   A 107 ? 0.3540 0.3926 0.5240 -0.0662 -0.0126 -0.1007 107 GLN   A CG  
2276 C CG  B GLN   A 107 ? 0.2952 0.2943 0.3448 -0.0356 0.0137  -0.0132 107 GLN   A CG  
2277 C CD  A GLN   A 107 ? 0.3874 0.4174 0.6099 -0.0662 -0.0162 -0.0956 107 GLN   A CD  
2278 C CD  B GLN   A 107 ? 0.3060 0.3026 0.3704 -0.0362 0.0105  -0.0067 107 GLN   A CD  
2279 O OE1 A GLN   A 107 ? 0.3990 0.4268 0.6449 -0.0666 -0.0166 -0.0936 107 GLN   A OE1 
2280 O OE1 B GLN   A 107 ? 0.3084 0.3043 0.3788 -0.0367 0.0089  -0.0041 107 GLN   A OE1 
2281 N NE2 A GLN   A 107 ? 0.4011 0.4274 0.6373 -0.0681 -0.0186 -0.0968 107 GLN   A NE2 
2282 N NE2 B GLN   A 107 ? 0.3106 0.3067 0.3798 -0.0364 0.0104  -0.0043 107 GLN   A NE2 
2299 N N   . LEU   A 108 ? 0.2095 0.2327 0.2336 -0.0475 0.0339  -0.0522 108 LEU   A N   
2300 C CA  . LEU   A 108 ? 0.1830 0.1862 0.1934 -0.0230 0.0318  -0.0173 108 LEU   A CA  
2301 C C   . LEU   A 108 ? 0.1571 0.1479 0.1894 -0.0087 0.0226  0.0075  108 LEU   A C   
2302 O O   . LEU   A 108 ? 0.1501 0.1430 0.2132 -0.0015 0.0257  0.0128  108 LEU   A O   
2303 C CB  . LEU   A 108 ? 0.1876 0.1954 0.1742 -0.0302 0.0362  -0.0150 108 LEU   A CB  
2304 C CG  . LEU   A 108 ? 0.2018 0.2176 0.1954 -0.0219 0.0455  -0.0162 108 LEU   A CG  
2305 C CD1 . LEU   A 108 ? 0.2196 0.2239 0.1927 -0.0292 0.0575  -0.0151 108 LEU   A CD1 
2306 C CD2 . LEU   A 108 ? 0.1998 0.2399 0.2386 -0.0141 0.0441  -0.0054 108 LEU   A CD2 
2319 N N   . LEU   A 109 ? 0.1438 0.1471 0.1825 -0.0003 0.0226  0.0236  109 LEU   A N   
2320 C CA  . LEU   A 109 ? 0.1401 0.1365 0.1671 -0.0023 0.0071  0.0219  109 LEU   A CA  
2321 C C   . LEU   A 109 ? 0.1268 0.1296 0.1561 -0.0090 0.0064  0.0120  109 LEU   A C   
2322 O O   . LEU   A 109 ? 0.1384 0.1210 0.1740 -0.0046 -0.0026 0.0052  109 LEU   A O   
2323 C CB  . LEU   A 109 ? 0.1467 0.1430 0.1793 0.0053  -0.0031 0.0298  109 LEU   A CB  
2324 C CG  . LEU   A 109 ? 0.1390 0.1508 0.1929 0.0020  0.0055  0.0334  109 LEU   A CG  
2325 C CD1 . LEU   A 109 ? 0.1453 0.1426 0.2067 -0.0006 0.0116  0.0136  109 LEU   A CD1 
2326 C CD2 . LEU   A 109 ? 0.1424 0.1680 0.2116 0.0027  0.0057  0.0369  109 LEU   A CD2 
2338 N N   . LYS   A 110 ? 0.1324 0.1259 0.1567 -0.0060 0.0039  0.0085  110 LYS   A N   
2339 C CA  . LYS   A 110 ? 0.1286 0.1219 0.1575 -0.0075 0.0073  0.0100  110 LYS   A CA  
2340 C C   . LYS   A 110 ? 0.1298 0.1172 0.1503 -0.0107 0.0020  -0.0030 110 LYS   A C   
2341 O O   . LYS   A 110 ? 0.1274 0.1203 0.1535 -0.0095 0.0076  -0.0058 110 LYS   A O   
2342 C CB  . LYS   A 110 ? 0.1380 0.1307 0.1737 -0.0074 -0.0026 0.0001  110 LYS   A CB  
2343 C CG  . LYS   A 110 ? 0.1397 0.1265 0.1782 -0.0053 -0.0028 -0.0060 110 LYS   A CG  
2344 C CD  . LYS   A 110 ? 0.1426 0.1323 0.1886 -0.0056 -0.0072 -0.0079 110 LYS   A CD  
2345 C CE  . LYS   A 110 ? 0.1542 0.1375 0.2204 -0.0085 0.0140  -0.0082 110 LYS   A CE  
2346 N NZ  . LYS   A 110 ? 0.1528 0.1390 0.2310 -0.0166 0.0201  -0.0053 110 LYS   A NZ  
2360 N N   . SER   A 111 ? 0.1282 0.1209 0.1523 -0.0044 0.0002  0.0045  111 SER   A N   
2361 C CA  . SER   A 111 ? 0.1258 0.1249 0.1551 -0.0008 0.0091  0.0022  111 SER   A CA  
2362 C C   . SER   A 111 ? 0.1206 0.1227 0.1574 -0.0086 0.0079  0.0067  111 SER   A C   
2363 O O   . SER   A 111 ? 0.1322 0.1139 0.1686 -0.0053 0.0092  0.0035  111 SER   A O   
2364 C CB  . SER   A 111 ? 0.1420 0.1496 0.1614 -0.0047 0.0190  -0.0092 111 SER   A CB  
2365 O OG  . SER   A 111 ? 0.1895 0.1682 0.1765 -0.0016 0.0228  -0.0124 111 SER   A OG  
2371 N N   . ALA   A 112 ? 0.1234 0.1135 0.1566 -0.0032 0.0105  0.0083  112 ALA   A N   
2372 C CA  . ALA   A 112 ? 0.1271 0.1130 0.1473 -0.0064 0.0198  0.0033  112 ALA   A CA  
2373 C C   . ALA   A 112 ? 0.1240 0.1107 0.1551 -0.0009 0.0114  -0.0016 112 ALA   A C   
2374 O O   . ALA   A 112 ? 0.1272 0.1097 0.1613 -0.0122 0.0135  0.0084  112 ALA   A O   
2375 C CB  . ALA   A 112 ? 0.1389 0.1142 0.1503 -0.0085 0.0162  0.0056  112 ALA   A CB  
2381 N N   . TYR   A 113 ? 0.1143 0.1114 0.1608 -0.0057 0.0113  0.0069  113 TYR   A N   
2382 C CA  . TYR   A 113 ? 0.1134 0.1129 0.1559 -0.0038 0.0122  0.0118  113 TYR   A CA  
2383 C C   . TYR   A 113 ? 0.1122 0.1086 0.1442 -0.0086 0.0091  0.0037  113 TYR   A C   
2384 O O   . TYR   A 113 ? 0.1165 0.1153 0.1559 -0.0026 0.0164  0.0008  113 TYR   A O   
2385 C CB  . TYR   A 113 ? 0.1146 0.1214 0.1610 -0.0053 -0.0011 0.0160  113 TYR   A CB  
2386 C CG  . TYR   A 113 ? 0.1175 0.1251 0.1517 -0.0107 0.0083  0.0167  113 TYR   A CG  
2387 C CD1 . TYR   A 113 ? 0.1175 0.1373 0.1387 -0.0046 0.0088  0.0181  113 TYR   A CD1 
2388 C CD2 . TYR   A 113 ? 0.1194 0.1327 0.1503 -0.0093 0.0086  0.0184  113 TYR   A CD2 
2389 C CE1 . TYR   A 113 ? 0.1251 0.1464 0.1450 -0.0039 0.0085  0.0198  113 TYR   A CE1 
2390 C CE2 . TYR   A 113 ? 0.1239 0.1375 0.1507 -0.0103 -0.0004 0.0195  113 TYR   A CE2 
2391 C CZ  . TYR   A 113 ? 0.1205 0.1402 0.1518 0.0032  0.0104  0.0235  113 TYR   A CZ  
2392 O OH  . TYR   A 113 ? 0.1218 0.1496 0.1808 0.0104  0.0101  0.0265  113 TYR   A OH  
2402 N N   . GLU   A 114 ? 0.1146 0.1119 0.1580 -0.0059 0.0110  0.0061  114 GLU   A N   
2403 C CA  . GLU   A 114 ? 0.1159 0.1054 0.1721 0.0021  0.0083  0.0137  114 GLU   A CA  
2404 C C   . GLU   A 114 ? 0.1095 0.1107 0.1640 0.0028  0.0161  0.0076  114 GLU   A C   
2405 O O   . GLU   A 114 ? 0.1228 0.1111 0.1628 -0.0015 0.0079  0.0048  114 GLU   A O   
2406 C CB  . GLU   A 114 ? 0.1179 0.1110 0.1641 -0.0061 0.0076  0.0112  114 GLU   A CB  
2407 C CG  . GLU   A 114 ? 0.1259 0.1136 0.1682 0.0002  0.0064  0.0026  114 GLU   A CG  
2408 C CD  . GLU   A 114 ? 0.1343 0.1194 0.1756 -0.0057 0.0055  -0.0003 114 GLU   A CD  
2409 O OE1 . GLU   A 114 ? 0.1365 0.1174 0.1804 -0.0098 0.0171  -0.0060 114 GLU   A OE1 
2410 O OE2 . GLU   A 114 ? 0.1508 0.1238 0.1923 -0.0075 0.0134  -0.0118 114 GLU   A OE2 
2417 N N   . ASN   A 115 ? 0.1149 0.1127 0.1524 -0.0030 0.0101  0.0028  115 ASN   A N   
2418 C CA  . ASN   A 115 ? 0.1188 0.1147 0.1470 -0.0064 0.0124  0.0087  115 ASN   A CA  
2419 C C   . ASN   A 115 ? 0.1196 0.1130 0.1426 -0.0068 0.0059  0.0055  115 ASN   A C   
2420 O O   . ASN   A 115 ? 0.1237 0.1265 0.1442 -0.0090 0.0095  0.0146  115 ASN   A O   
2421 C CB  . ASN   A 115 ? 0.1255 0.1229 0.1427 -0.0095 0.0107  0.0051  115 ASN   A CB  
2422 C CG  . ASN   A 115 ? 0.1245 0.1468 0.1523 -0.0158 0.0164  0.0129  115 ASN   A CG  
2423 O OD1 . ASN   A 115 ? 0.1282 0.2391 0.1809 -0.0157 0.0263  0.0231  115 ASN   A OD1 
2424 N ND2 . ASN   A 115 ? 0.1277 0.1306 0.1536 -0.0143 0.0205  0.0112  115 ASN   A ND2 
2431 N N   . PHE   A 116 ? 0.1157 0.1138 0.1466 0.0010  0.0149  0.0131  116 PHE   A N   
2432 C CA  . PHE   A 116 ? 0.1141 0.1221 0.1384 -0.0040 0.0114  0.0109  116 PHE   A CA  
2433 C C   . PHE   A 116 ? 0.1122 0.1266 0.1436 -0.0091 0.0159  0.0199  116 PHE   A C   
2434 O O   . PHE   A 116 ? 0.1193 0.1351 0.1502 0.0011  0.0129  0.0234  116 PHE   A O   
2435 C CB  . PHE   A 116 ? 0.1174 0.1102 0.1530 -0.0018 0.0169  0.0106  116 PHE   A CB  
2436 C CG  . PHE   A 116 ? 0.1212 0.1154 0.1406 -0.0068 0.0137  0.0054  116 PHE   A CG  
2437 C CD1 . PHE   A 116 ? 0.1216 0.1176 0.1522 -0.0087 0.0179  0.0083  116 PHE   A CD1 
2438 C CD2 . PHE   A 116 ? 0.1258 0.1195 0.1603 -0.0082 0.0193  0.0147  116 PHE   A CD2 
2439 C CE1 . PHE   A 116 ? 0.1259 0.1117 0.1630 -0.0123 0.0102  0.0063  116 PHE   A CE1 
2440 C CE2 . PHE   A 116 ? 0.1258 0.1172 0.1662 -0.0062 0.0137  0.0064  116 PHE   A CE2 
2441 C CZ  . PHE   A 116 ? 0.1258 0.1062 0.1596 -0.0023 0.0065  0.0100  116 PHE   A CZ  
2451 N N   . ASN   A 117 ? 0.1166 0.1170 0.1592 -0.0016 0.0095  0.0142  117 ASN   A N   
2452 C CA  . ASN   A 117 ? 0.1218 0.1191 0.1660 -0.0004 0.0146  0.0180  117 ASN   A CA  
2453 C C   . ASN   A 117 ? 0.1223 0.1300 0.1711 -0.0005 0.0162  0.0214  117 ASN   A C   
2454 O O   . ASN   A 117 ? 0.1329 0.1326 0.1912 -0.0035 -0.0044 0.0321  117 ASN   A O   
2455 C CB  . ASN   A 117 ? 0.1180 0.1209 0.1726 -0.0032 0.0140  0.0261  117 ASN   A CB  
2456 C CG  . ASN   A 117 ? 0.1181 0.1232 0.1694 -0.0044 0.0140  0.0230  117 ASN   A CG  
2457 O OD1 . ASN   A 117 ? 0.1235 0.1415 0.1735 -0.0111 0.0157  0.0125  117 ASN   A OD1 
2458 N ND2 . ASN   A 117 ? 0.1139 0.1226 0.1709 -0.0006 0.0085  0.0190  117 ASN   A ND2 
2465 N N   . GLN   A 118 ? 0.1178 0.1306 0.1708 -0.0056 0.0025  0.0209  118 GLN   A N   
2466 C CA  . GLN   A 118 ? 0.1266 0.1379 0.1713 -0.0080 0.0003  0.0170  118 GLN   A CA  
2467 C C   . GLN   A 118 ? 0.1290 0.1425 0.1655 -0.0065 -0.0065 0.0213  118 GLN   A C   
2468 O O   . GLN   A 118 ? 0.1294 0.1728 0.1941 0.0021  -0.0131 0.0027  118 GLN   A O   
2469 C CB  . GLN   A 118 ? 0.1265 0.1424 0.1850 -0.0046 0.0047  0.0168  118 GLN   A CB  
2470 C CG  . GLN   A 118 ? 0.1227 0.1422 0.1896 -0.0006 0.0051  0.0267  118 GLN   A CG  
2471 C CD  . GLN   A 118 ? 0.1203 0.1427 0.1957 0.0014  0.0092  0.0199  118 GLN   A CD  
2472 O OE1 . GLN   A 118 ? 0.1255 0.1581 0.2080 0.0101  -0.0048 0.0102  118 GLN   A OE1 
2473 N NE2 . GLN   A 118 ? 0.1308 0.1399 0.2029 0.0056  0.0036  0.0224  118 GLN   A NE2 
2482 N N   . HIS   A 119 ? 0.1308 0.1393 0.1575 -0.0022 -0.0019 0.0236  119 HIS   A N   
2483 C CA  . HIS   A 119 ? 0.1372 0.1457 0.1704 -0.0033 0.0057  0.0232  119 HIS   A CA  
2484 C C   . HIS   A 119 ? 0.1450 0.1489 0.1573 -0.0082 0.0041  0.0287  119 HIS   A C   
2485 O O   . HIS   A 119 ? 0.1492 0.1603 0.1621 -0.0256 0.0022  0.0248  119 HIS   A O   
2486 C CB  . HIS   A 119 ? 0.1403 0.1449 0.1908 0.0002  0.0211  0.0216  119 HIS   A CB  
2487 C CG  . HIS   A 119 ? 0.1432 0.1456 0.2323 0.0030  0.0251  0.0319  119 HIS   A CG  
2488 N ND1 . HIS   A 119 ? 0.1510 0.1695 0.2810 -0.0090 0.0176  0.0228  119 HIS   A ND1 
2489 C CD2 . HIS   A 119 ? 0.1567 0.1594 0.2463 0.0151  0.0353  0.0518  119 HIS   A CD2 
2490 C CE1 . HIS   A 119 ? 0.1528 0.1659 0.2942 -0.0152 0.0291  0.0441  119 HIS   A CE1 
2491 N NE2 . HIS   A 119 ? 0.1673 0.1631 0.2810 0.0040  0.0456  0.0601  119 HIS   A NE2 
2499 N N   . GLU   A 120 ? 0.1548 0.1680 0.1589 -0.0013 0.0025  0.0410  120 GLU   A N   
2500 C CA  . GLU   A 120 ? 0.1680 0.1943 0.1753 0.0051  0.0061  0.0706  120 GLU   A CA  
2501 C C   . GLU   A 120 ? 0.1547 0.1798 0.1593 -0.0091 -0.0023 0.0601  120 GLU   A C   
2502 O O   . GLU   A 120 ? 0.1554 0.1767 0.1689 -0.0097 0.0003  0.0550  120 GLU   A O   
2503 C CB  . GLU   A 120 ? 0.2241 0.2575 0.2317 0.0211  0.0074  0.1242  120 GLU   A CB  
2504 C CG  . GLU   A 120 ? 0.3106 0.3248 0.3458 0.0369  0.0099  0.1340  120 GLU   A CG  
2505 C CD  . GLU   A 120 ? 0.3760 0.3774 0.4603 0.0495  0.0206  0.1262  120 GLU   A CD  
2506 O OE1 . GLU   A 120 ? 0.3991 0.4012 0.4894 0.0514  0.0241  0.1216  120 GLU   A OE1 
2507 O OE2 . GLU   A 120 ? 0.4159 0.4159 0.5132 0.0535  0.0251  0.1249  120 GLU   A OE2 
2514 N N   . VAL   A 121 ? 0.1528 0.1826 0.1400 -0.0083 0.0052  0.0446  121 VAL   A N   
2515 C CA  . VAL   A 121 ? 0.1625 0.1883 0.1297 -0.0082 0.0120  0.0458  121 VAL   A CA  
2516 C C   . VAL   A 121 ? 0.1520 0.1697 0.1181 -0.0153 0.0082  0.0336  121 VAL   A C   
2517 O O   . VAL   A 121 ? 0.1541 0.1773 0.1444 -0.0223 -0.0058 0.0238  121 VAL   A O   
2518 C CB  . VAL   A 121 ? 0.2015 0.2220 0.1657 0.0025  0.0285  0.0558  121 VAL   A CB  
2519 C CG1 . VAL   A 121 ? 0.2077 0.2362 0.1757 0.0086  0.0363  0.0591  121 VAL   A CG1 
2520 C CG2 . VAL   A 121 ? 0.2237 0.2399 0.2051 -0.0030 0.0232  0.0434  121 VAL   A CG2 
2530 N N   . LEU   A 122 ? 0.1457 0.1524 0.1383 -0.0160 0.0110  0.0324  122 LEU   A N   
2531 C CA  . LEU   A 122 ? 0.1486 0.1408 0.1408 -0.0176 0.0248  0.0282  122 LEU   A CA  
2532 C C   . LEU   A 122 ? 0.1414 0.1396 0.1380 -0.0154 0.0135  0.0241  122 LEU   A C   
2533 O O   . LEU   A 122 ? 0.1403 0.1464 0.1778 -0.0208 0.0089  0.0224  122 LEU   A O   
2534 C CB  . LEU   A 122 ? 0.1664 0.1465 0.1781 -0.0098 0.0206  0.0316  122 LEU   A CB  
2535 C CG  . LEU   A 122 ? 0.1687 0.1532 0.1651 -0.0112 0.0267  0.0227  122 LEU   A CG  
2536 C CD1 . LEU   A 122 ? 0.1841 0.1522 0.1811 -0.0152 0.0249  0.0242  122 LEU   A CD1 
2537 C CD2 . LEU   A 122 ? 0.1632 0.1458 0.1570 -0.0094 0.0261  0.0229  122 LEU   A CD2 
2549 N N   A LEU   A 123 ? 0.1379 0.1380 0.1300 -0.0172 0.0111  0.0206  123 LEU   A N   
2550 N N   B LEU   A 123 ? 0.1424 0.1362 0.1348 -0.0129 0.0092  0.0177  123 LEU   A N   
2551 C CA  A LEU   A 123 ? 0.1408 0.1392 0.1315 -0.0146 0.0197  0.0201  123 LEU   A CA  
2552 C CA  B LEU   A 123 ? 0.1439 0.1347 0.1353 -0.0105 0.0068  0.0121  123 LEU   A CA  
2553 C C   A LEU   A 123 ? 0.1314 0.1296 0.1171 -0.0125 0.0149  0.0249  123 LEU   A C   
2554 C C   B LEU   A 123 ? 0.1447 0.1319 0.1268 -0.0076 0.0037  0.0084  123 LEU   A C   
2555 O O   A LEU   A 123 ? 0.1245 0.1390 0.1287 -0.0217 0.0089  0.0244  123 LEU   A O   
2556 O O   B LEU   A 123 ? 0.1437 0.1304 0.1248 -0.0049 0.0049  0.0023  123 LEU   A O   
2557 C CB  A LEU   A 123 ? 0.1495 0.1475 0.1298 -0.0182 0.0262  0.0204  123 LEU   A CB  
2558 C CB  B LEU   A 123 ? 0.1442 0.1356 0.1414 -0.0120 0.0057  0.0106  123 LEU   A CB  
2559 C CG  A LEU   A 123 ? 0.1523 0.1571 0.1446 -0.0140 0.0303  0.0097  123 LEU   A CG  
2560 C CG  B LEU   A 123 ? 0.1438 0.1351 0.1452 -0.0132 0.0066  0.0106  123 LEU   A CG  
2561 C CD1 A LEU   A 123 ? 0.1552 0.1622 0.1708 -0.0015 0.0209  -0.0009 123 LEU   A CD1 
2562 C CD1 B LEU   A 123 ? 0.1442 0.1341 0.1505 -0.0128 0.0073  0.0097  123 LEU   A CD1 
2563 C CD2 A LEU   A 123 ? 0.1729 0.1666 0.1612 -0.0107 0.0179  -0.0013 123 LEU   A CD2 
2564 C CD2 B LEU   A 123 ? 0.1474 0.1366 0.1482 -0.0128 0.0044  0.0088  123 LEU   A CD2 
2587 N N   A ALA   A 124 ? 0.1235 0.1245 0.1189 -0.0127 0.0134  0.0198  124 ALA   A N   
2588 N N   B ALA   A 124 ? 0.1458 0.1312 0.1247 -0.0081 -0.0012 0.0092  124 ALA   A N   
2589 C CA  A ALA   A 124 ? 0.1181 0.1276 0.1315 -0.0057 0.0045  0.0255  124 ALA   A CA  
2590 C CA  B ALA   A 124 ? 0.1474 0.1341 0.1255 -0.0093 -0.0031 0.0132  124 ALA   A CA  
2591 C C   A ALA   A 124 ? 0.1167 0.1254 0.1337 -0.0122 0.0112  0.0186  124 ALA   A C   
2592 C C   B ALA   A 124 ? 0.1461 0.1337 0.1196 -0.0060 -0.0070 0.0160  124 ALA   A C   
2593 O O   A ALA   A 124 ? 0.1127 0.1322 0.1587 -0.0097 0.0196  0.0284  124 ALA   A O   
2594 O O   B ALA   A 124 ? 0.1441 0.1333 0.1190 -0.0005 -0.0103 0.0182  124 ALA   A O   
2595 C CB  A ALA   A 124 ? 0.1186 0.1237 0.1509 -0.0070 0.0043  0.0269  124 ALA   A CB  
2596 C CB  B ALA   A 124 ? 0.1516 0.1350 0.1308 -0.0138 0.0014  0.0148  124 ALA   A CB  
2607 N N   A PRO   A 125 ? 0.1175 0.1263 0.1359 -0.0058 0.0072  0.0316  125 PRO   A N   
2608 N N   B PRO   A 125 ? 0.1449 0.1322 0.1125 -0.0033 -0.0106 0.0163  125 PRO   A N   
2609 C CA  A PRO   A 125 ? 0.1241 0.1306 0.1382 -0.0074 0.0075  0.0254  125 PRO   A CA  
2610 C CA  B PRO   A 125 ? 0.1455 0.1333 0.1156 -0.0052 -0.0079 0.0104  125 PRO   A CA  
2611 C C   A PRO   A 125 ? 0.1167 0.1343 0.1382 -0.0093 0.0129  0.0248  125 PRO   A C   
2612 C C   B PRO   A 125 ? 0.1469 0.1366 0.1224 -0.0084 -0.0036 0.0050  125 PRO   A C   
2613 O O   A PRO   A 125 ? 0.1238 0.1334 0.1615 0.0018  0.0052  0.0239  125 PRO   A O   
2614 O O   B PRO   A 125 ? 0.1465 0.1368 0.1253 -0.0082 -0.0024 0.0061  125 PRO   A O   
2615 C CB  A PRO   A 125 ? 0.1398 0.1269 0.1337 -0.0165 0.0115  0.0239  125 PRO   A CB  
2616 C CB  B PRO   A 125 ? 0.1460 0.1319 0.1126 -0.0039 -0.0078 0.0104  125 PRO   A CB  
2617 C CG  A PRO   A 125 ? 0.1410 0.1257 0.1413 -0.0190 0.0133  0.0188  125 PRO   A CG  
2618 C CG  B PRO   A 125 ? 0.1454 0.1322 0.1148 -0.0034 -0.0084 0.0109  125 PRO   A CG  
2619 C CD  A PRO   A 125 ? 0.1248 0.1296 0.1396 -0.0157 0.0174  0.0284  125 PRO   A CD  
2620 C CD  B PRO   A 125 ? 0.1445 0.1319 0.1150 -0.0032 -0.0075 0.0140  125 PRO   A CD  
2635 N N   A LEU   A 126 ? 0.1143 0.1423 0.1415 -0.0031 0.0119  0.0203  126 LEU   A N   
2636 N N   B LEU   A 126 ? 0.1504 0.1388 0.1310 -0.0106 -0.0033 -0.0006 126 LEU   A N   
2637 C CA  A LEU   A 126 ? 0.1203 0.1355 0.1513 -0.0086 0.0061  0.0263  126 LEU   A CA  
2638 C CA  B LEU   A 126 ? 0.1521 0.1403 0.1388 -0.0120 -0.0010 0.0002  126 LEU   A CA  
2639 C C   A LEU   A 126 ? 0.1248 0.1288 0.1484 -0.0054 0.0039  0.0225  126 LEU   A C   
2640 C C   B LEU   A 126 ? 0.1493 0.1432 0.1419 -0.0076 0.0025  0.0036  126 LEU   A C   
2641 O O   A LEU   A 126 ? 0.1363 0.1358 0.1652 -0.0003 0.0126  0.0241  126 LEU   A O   
2642 O O   B LEU   A 126 ? 0.1539 0.1457 0.1594 -0.0090 0.0076  -0.0047 126 LEU   A O   
2643 C CB  A LEU   A 126 ? 0.1258 0.1450 0.1572 -0.0125 -0.0036 0.0288  126 LEU   A CB  
2644 C CB  B LEU   A 126 ? 0.1572 0.1397 0.1479 -0.0157 0.0007  0.0006  126 LEU   A CB  
2645 C CG  A LEU   A 126 ? 0.1262 0.1700 0.1977 -0.0131 0.0127  0.0325  126 LEU   A CG  
2646 C CG  B LEU   A 126 ? 0.1585 0.1358 0.1566 -0.0165 0.0008  -0.0030 126 LEU   A CG  
2647 C CD1 A LEU   A 126 ? 0.1306 0.1859 0.2250 -0.0165 0.0098  0.0337  126 LEU   A CD1 
2648 C CD1 B LEU   A 126 ? 0.1590 0.1353 0.1611 -0.0188 -0.0012 -0.0020 126 LEU   A CD1 
2649 C CD2 A LEU   A 126 ? 0.1364 0.1633 0.2030 -0.0290 0.0084  0.0347  126 LEU   A CD2 
2650 C CD2 B LEU   A 126 ? 0.1599 0.1357 0.1587 -0.0137 -0.0025 -0.0058 126 LEU   A CD2 
2673 N N   A LEU   A 127 ? 0.1272 0.1342 0.1468 0.0027  0.0034  0.0296  127 LEU   A N   
2674 N N   B LEU   A 127 ? 0.1410 0.1405 0.1238 -0.0038 0.0009  0.0158  127 LEU   A N   
2675 C CA  A LEU   A 127 ? 0.1265 0.1397 0.1414 -0.0015 0.0003  0.0249  127 LEU   A CA  
2676 C CA  B LEU   A 127 ? 0.1308 0.1382 0.1164 -0.0028 0.0030  0.0211  127 LEU   A CA  
2677 C C   A LEU   A 127 ? 0.1226 0.1285 0.1261 -0.0026 0.0015  0.0172  127 LEU   A C   
2678 C C   B LEU   A 127 ? 0.1277 0.1407 0.1241 -0.0107 0.0014  0.0185  127 LEU   A C   
2679 O O   A LEU   A 127 ? 0.1350 0.1332 0.1431 -0.0102 -0.0012 0.0239  127 LEU   A O   
2680 O O   B LEU   A 127 ? 0.1294 0.1388 0.1190 -0.0156 0.0064  0.0250  127 LEU   A O   
2681 C CB  A LEU   A 127 ? 0.1307 0.1565 0.1450 0.0061  0.0087  0.0279  127 LEU   A CB  
2682 C CB  B LEU   A 127 ? 0.1257 0.1357 0.1108 0.0019  0.0052  0.0225  127 LEU   A CB  
2683 C CG  A LEU   A 127 ? 0.1345 0.1674 0.1514 0.0114  -0.0042 0.0321  127 LEU   A CG  
2684 C CG  B LEU   A 127 ? 0.1196 0.1318 0.0978 0.0061  0.0089  0.0271  127 LEU   A CG  
2685 C CD1 A LEU   A 127 ? 0.1421 0.1611 0.1734 0.0043  0.0041  0.0334  127 LEU   A CD1 
2686 C CD1 B LEU   A 127 ? 0.1174 0.1294 0.0921 0.0086  0.0090  0.0275  127 LEU   A CD1 
2687 C CD2 A LEU   A 127 ? 0.1487 0.1782 0.1634 0.0128  -0.0138 0.0264  127 LEU   A CD2 
2688 C CD2 B LEU   A 127 ? 0.1201 0.1315 0.0942 0.0094  0.0040  0.0225  127 LEU   A CD2 
2711 N N   A SER   A 128 ? 0.1308 0.1293 0.1258 -0.0093 -0.0003 0.0195  128 SER   A N   
2712 N N   B SER   A 128 ? 0.1258 0.1442 0.1320 -0.0151 -0.0032 0.0156  128 SER   A N   
2713 C CA  A SER   A 128 ? 0.1396 0.1333 0.1245 -0.0107 -0.0050 0.0195  128 SER   A CA  
2714 C CA  B SER   A 128 ? 0.1249 0.1471 0.1304 -0.0156 -0.0064 0.0103  128 SER   A CA  
2715 C C   A SER   A 128 ? 0.1432 0.1347 0.1260 -0.0000 -0.0101 0.0207  128 SER   A C   
2716 C C   B SER   A 128 ? 0.1278 0.1465 0.1261 -0.0134 -0.0069 0.0130  128 SER   A C   
2717 O O   A SER   A 128 ? 0.1556 0.1511 0.1444 0.0025  -0.0139 0.0128  128 SER   A O   
2718 O O   B SER   A 128 ? 0.1237 0.1463 0.1254 -0.0133 -0.0022 0.0146  128 SER   A O   
2719 C CB  A SER   A 128 ? 0.1376 0.1433 0.1333 -0.0105 0.0008  0.0203  128 SER   A CB  
2720 C CB  B SER   A 128 ? 0.1205 0.1490 0.1300 -0.0186 -0.0102 0.0112  128 SER   A CB  
2721 O OG  A SER   A 128 ? 0.1408 0.1591 0.1364 -0.0061 0.0015  0.0189  128 SER   A OG  
2722 O OG  B SER   A 128 ? 0.1153 0.1517 0.1296 -0.0201 -0.0103 0.0109  128 SER   A OG  
2733 N N   A ALA   A 129 ? 0.1351 0.1412 0.1591 -0.0003 -0.0061 0.0295  129 ALA   A N   
2734 N N   B ALA   A 129 ? 0.1355 0.1478 0.1230 -0.0076 -0.0130 0.0147  129 ALA   A N   
2735 C CA  A ALA   A 129 ? 0.1363 0.1412 0.1802 0.0040  -0.0035 0.0301  129 ALA   A CA  
2736 C CA  B ALA   A 129 ? 0.1452 0.1507 0.1331 -0.0028 -0.0108 0.0126  129 ALA   A CA  
2737 C C   A ALA   A 129 ? 0.1396 0.1407 0.1585 -0.0023 -0.0126 0.0175  129 ALA   A C   
2738 C C   B ALA   A 129 ? 0.1586 0.1580 0.1453 -0.0017 -0.0110 0.0115  129 ALA   A C   
2739 O O   A ALA   A 129 ? 0.1427 0.1470 0.1461 -0.0117 -0.0100 0.0285  129 ALA   A O   
2740 O O   B ALA   A 129 ? 0.1594 0.1583 0.1474 -0.0011 -0.0148 0.0145  129 ALA   A O   
2741 C CB  A ALA   A 129 ? 0.1435 0.1627 0.2075 0.0091  0.0125  0.0444  129 ALA   A CB  
2742 C CB  B ALA   A 129 ? 0.1442 0.1516 0.1384 -0.0019 -0.0101 0.0097  129 ALA   A CB  
2753 N N   A GLY   A 130 ? 0.1441 0.1369 0.2008 0.0010  -0.0002 0.0077  130 GLY   A N   
2754 N N   B GLY   A 130 ? 0.1692 0.1651 0.1524 -0.0035 -0.0077 0.0071  130 GLY   A N   
2755 C CA  A GLY   A 130 ? 0.1571 0.1424 0.2047 -0.0017 0.0007  0.0048  130 GLY   A CA  
2756 C CA  B GLY   A 130 ? 0.1791 0.1721 0.1634 -0.0044 -0.0070 0.0053  130 GLY   A CA  
2757 C C   A GLY   A 130 ? 0.1600 0.1396 0.1888 0.0046  -0.0080 0.0076  130 GLY   A C   
2758 C C   B GLY   A 130 ? 0.1875 0.1773 0.1762 -0.0071 -0.0058 0.0049  130 GLY   A C   
2759 O O   A GLY   A 130 ? 0.1670 0.1354 0.1948 0.0080  -0.0313 0.0065  130 GLY   A O   
2760 O O   B GLY   A 130 ? 0.1901 0.1779 0.1829 -0.0095 -0.0115 0.0057  130 GLY   A O   
2767 N N   A ILE   A 131 ? 0.1665 0.1364 0.1793 -0.0039 -0.0110 0.0116  131 ILE   A N   
2768 N N   B ILE   A 131 ? 0.1934 0.1803 0.1793 -0.0077 -0.0039 0.0064  131 ILE   A N   
2769 C CA  A ILE   A 131 ? 0.1804 0.1366 0.1592 -0.0079 -0.0246 0.0107  131 ILE   A CA  
2770 C CA  B ILE   A 131 ? 0.1981 0.1834 0.1814 -0.0093 -0.0041 0.0072  131 ILE   A CA  
2771 C C   A ILE   A 131 ? 0.1709 0.1369 0.1437 -0.0103 -0.0271 0.0192  131 ILE   A C   
2772 C C   B ILE   A 131 ? 0.1983 0.1836 0.1786 -0.0079 -0.0072 0.0109  131 ILE   A C   
2773 O O   A ILE   A 131 ? 0.1808 0.1394 0.1656 0.0014  -0.0170 0.0250  131 ILE   A O   
2774 O O   B ILE   A 131 ? 0.1995 0.1827 0.1779 -0.0074 -0.0092 0.0131  131 ILE   A O   
2775 C CB  A ILE   A 131 ? 0.2051 0.1459 0.1617 -0.0186 -0.0262 0.0008  131 ILE   A CB  
2776 C CB  B ILE   A 131 ? 0.2028 0.1869 0.1909 -0.0108 -0.0042 0.0067  131 ILE   A CB  
2777 C CG1 A ILE   A 131 ? 0.2141 0.1779 0.1622 -0.0322 -0.0297 0.0009  131 ILE   A CG1 
2778 C CG1 B ILE   A 131 ? 0.2068 0.1910 0.1982 -0.0121 -0.0038 0.0073  131 ILE   A CG1 
2779 C CG2 A ILE   A 131 ? 0.2217 0.1332 0.1817 -0.0118 -0.0161 -0.0142 131 ILE   A CG2 
2780 C CG2 B ILE   A 131 ? 0.2033 0.1870 0.1935 -0.0117 -0.0047 0.0065  131 ILE   A CG2 
2781 C CD1 A ILE   A 131 ? 0.2226 0.1952 0.1916 -0.0361 -0.0342 -0.0132 131 ILE   A CD1 
2782 C CD1 B ILE   A 131 ? 0.2081 0.1920 0.2026 -0.0126 -0.0020 0.0083  131 ILE   A CD1 
2805 N N   A PHE   A 132 ? 0.1625 0.1374 0.1366 0.0003  -0.0176 0.0216  132 PHE   A N   
2806 N N   B PHE   A 132 ? 0.1985 0.1850 0.1794 -0.0067 -0.0084 0.0126  132 PHE   A N   
2807 C CA  A PHE   A 132 ? 0.1668 0.1417 0.1327 -0.0018 -0.0120 0.0132  132 PHE   A CA  
2808 C CA  B PHE   A 132 ? 0.1984 0.1855 0.1782 -0.0063 -0.0093 0.0132  132 PHE   A CA  
2809 C C   A PHE   A 132 ? 0.1744 0.1573 0.1332 -0.0053 -0.0169 0.0155  132 PHE   A C   
2810 C C   B PHE   A 132 ? 0.1981 0.1861 0.1842 -0.0047 -0.0131 0.0178  132 PHE   A C   
2811 O O   A PHE   A 132 ? 0.1838 0.1737 0.1488 -0.0110 -0.0179 0.0092  132 PHE   A O   
2812 O O   B PHE   A 132 ? 0.2016 0.1885 0.1888 -0.0048 -0.0148 0.0214  132 PHE   A O   
2813 C CB  A PHE   A 132 ? 0.1622 0.1353 0.1297 0.0017  -0.0112 0.0191  132 PHE   A CB  
2814 C CB  B PHE   A 132 ? 0.1983 0.1854 0.1704 -0.0077 -0.0054 0.0078  132 PHE   A CB  
2815 C CG  A PHE   A 132 ? 0.1623 0.1323 0.1282 0.0071  -0.0086 0.0164  132 PHE   A CG  
2816 C CG  B PHE   A 132 ? 0.1988 0.1868 0.1687 -0.0068 -0.0029 0.0007  132 PHE   A CG  
2817 C CD1 A PHE   A 132 ? 0.1621 0.1450 0.1499 0.0151  -0.0097 -0.0004 132 PHE   A CD1 
2818 C CD1 B PHE   A 132 ? 0.1993 0.1885 0.1722 -0.0062 -0.0034 -0.0029 132 PHE   A CD1 
2819 C CD2 A PHE   A 132 ? 0.1620 0.1454 0.1409 0.0107  -0.0117 0.0062  132 PHE   A CD2 
2820 C CD2 B PHE   A 132 ? 0.1997 0.1867 0.1688 -0.0057 -0.0013 -0.0044 132 PHE   A CD2 
2821 C CE1 A PHE   A 132 ? 0.1596 0.1487 0.1544 0.0116  -0.0157 -0.0071 132 PHE   A CE1 
2822 C CE1 B PHE   A 132 ? 0.1997 0.1895 0.1744 -0.0068 -0.0014 -0.0056 132 PHE   A CE1 
2823 C CE2 A PHE   A 132 ? 0.1571 0.1485 0.1513 0.0162  -0.0137 0.0056  132 PHE   A CE2 
2824 C CE2 B PHE   A 132 ? 0.2005 0.1884 0.1745 -0.0062 -0.0001 -0.0078 132 PHE   A CE2 
2825 C CZ  A PHE   A 132 ? 0.1565 0.1466 0.1487 0.0055  -0.0218 0.0039  132 PHE   A CZ  
2826 C CZ  B PHE   A 132 ? 0.2001 0.1891 0.1754 -0.0063 -0.0001 -0.0089 132 PHE   A CZ  
2845 N N   A GLY   A 133 ? 0.1813 0.1596 0.1352 -0.0053 -0.0339 0.0178  133 GLY   A N   
2846 N N   B GLY   A 133 ? 0.1936 0.1838 0.1820 -0.0033 -0.0152 0.0158  133 GLY   A N   
2847 C CA  A GLY   A 133 ? 0.1884 0.1693 0.1439 -0.0102 -0.0343 0.0079  133 GLY   A CA  
2848 C CA  B GLY   A 133 ? 0.1897 0.1821 0.1832 -0.0027 -0.0154 0.0095  133 GLY   A CA  
2849 C C   A GLY   A 133 ? 0.1888 0.1778 0.1508 -0.0092 -0.0410 -0.0004 133 GLY   A C   
2850 C C   B GLY   A 133 ? 0.1868 0.1811 0.1845 -0.0018 -0.0183 0.0033  133 GLY   A C   
2851 O O   A GLY   A 133 ? 0.2070 0.1928 0.1740 -0.0059 -0.0541 -0.0147 133 GLY   A O   
2852 O O   B GLY   A 133 ? 0.1869 0.1803 0.1841 0.0015  -0.0211 0.0002  133 GLY   A O   
2859 N N   A ALA   A 134 ? 0.1793 0.1680 0.1401 -0.0151 -0.0251 0.0015  134 ALA   A N   
2860 N N   B ALA   A 134 ? 0.1844 0.1806 0.1816 -0.0033 -0.0167 0.0018  134 ALA   A N   
2861 C CA  A ALA   A 134 ? 0.1709 0.1721 0.1665 -0.0161 -0.0267 -0.0000 134 ALA   A CA  
2862 C CA  B ALA   A 134 ? 0.1822 0.1795 0.1745 -0.0042 -0.0147 -0.0003 134 ALA   A CA  
2863 C C   A ALA   A 134 ? 0.1696 0.1842 0.1666 -0.0155 -0.0233 0.0201  134 ALA   A C   
2864 C C   B ALA   A 134 ? 0.1816 0.1792 0.1772 -0.0047 -0.0110 0.0019  134 ALA   A C   
2865 O O   A ALA   A 134 ? 0.1831 0.1901 0.1973 -0.0136 0.0053  0.0240  134 ALA   A O   
2866 O O   B ALA   A 134 ? 0.1843 0.1798 0.1846 -0.0059 -0.0078 0.0032  134 ALA   A O   
2867 C CB  A ALA   A 134 ? 0.1789 0.1655 0.1918 -0.0136 -0.0226 -0.0029 134 ALA   A CB  
2868 C CB  B ALA   A 134 ? 0.1824 0.1780 0.1691 -0.0038 -0.0153 -0.0057 134 ALA   A CB  
2879 N N   A ASP   A 135 ? 0.1762 0.1982 0.1893 -0.0211 -0.0319 0.0367  135 ASP   A N   
2880 N N   B ASP   A 135 ? 0.1820 0.1812 0.1782 -0.0043 -0.0103 0.0017  135 ASP   A N   
2881 C CA  A ASP   A 135 ? 0.1767 0.2089 0.2210 -0.0302 -0.0471 0.0460  135 ASP   A CA  
2882 C CA  B ASP   A 135 ? 0.1814 0.1822 0.1808 -0.0043 -0.0099 0.0014  135 ASP   A CA  
2883 C C   A ASP   A 135 ? 0.1625 0.1954 0.2256 -0.0233 -0.0321 0.0592  135 ASP   A C   
2884 C C   B ASP   A 135 ? 0.1811 0.1820 0.1830 -0.0015 -0.0071 0.0008  135 ASP   A C   
2885 O O   A ASP   A 135 ? 0.1601 0.1809 0.2202 -0.0251 -0.0361 0.0536  135 ASP   A O   
2886 O O   B ASP   A 135 ? 0.1814 0.1809 0.1816 -0.0010 -0.0062 0.0031  135 ASP   A O   
2887 C CB  A ASP   A 135 ? 0.2017 0.2408 0.2636 -0.0508 -0.0675 0.0357  135 ASP   A CB  
2888 C CB  B ASP   A 135 ? 0.1810 0.1837 0.1823 -0.0070 -0.0125 -0.0004 135 ASP   A CB  
2889 C CG  A ASP   A 135 ? 0.2190 0.2725 0.3137 -0.0685 -0.0732 0.0304  135 ASP   A CG  
2890 C CG  B ASP   A 135 ? 0.1806 0.1852 0.1849 -0.0103 -0.0122 -0.0046 135 ASP   A CG  
2891 O OD1 A ASP   A 135 ? 0.2109 0.2817 0.3196 -0.0764 -0.0816 0.0470  135 ASP   A OD1 
2892 O OD1 B ASP   A 135 ? 0.1809 0.1834 0.1901 -0.0104 -0.0109 -0.0055 135 ASP   A OD1 
2893 O OD2 A ASP   A 135 ? 0.2547 0.2938 0.3673 -0.0679 -0.0461 0.0241  135 ASP   A OD2 
2894 O OD2 B ASP   A 135 ? 0.1796 0.1885 0.1835 -0.0134 -0.0137 -0.0069 135 ASP   A OD2 
2903 N N   A PRO   A 136 ? 0.1541 0.1951 0.2343 -0.0075 -0.0144 0.0767  136 PRO   A N   
2904 N N   B PRO   A 136 ? 0.1817 0.1829 0.1883 0.0002  -0.0052 -0.0019 136 PRO   A N   
2905 C CA  A PRO   A 136 ? 0.1467 0.1954 0.2398 -0.0065 -0.0057 0.0689  136 PRO   A CA  
2906 C CA  B PRO   A 136 ? 0.1816 0.1868 0.1896 -0.0002 -0.0051 -0.0025 136 PRO   A CA  
2907 C C   A PRO   A 136 ? 0.1235 0.1910 0.2297 -0.0030 -0.0052 0.0587  136 PRO   A C   
2908 C C   B PRO   A 136 ? 0.1814 0.1912 0.1871 -0.0014 -0.0065 -0.0005 136 PRO   A C   
2909 O O   A PRO   A 136 ? 0.1227 0.1818 0.2195 -0.0061 0.0003  0.0584  136 PRO   A O   
2910 O O   B PRO   A 136 ? 0.1825 0.1900 0.1834 0.0014  -0.0053 -0.0029 136 PRO   A O   
2911 C CB  A PRO   A 136 ? 0.1682 0.1974 0.2669 0.0005  -0.0004 0.0721  136 PRO   A CB  
2912 C CB  B PRO   A 136 ? 0.1833 0.1854 0.1942 0.0003  -0.0057 -0.0047 136 PRO   A CB  
2913 C CG  A PRO   A 136 ? 0.1823 0.2103 0.2869 0.0021  -0.0009 0.0701  136 PRO   A CG  
2914 C CG  B PRO   A 136 ? 0.1856 0.1835 0.1972 0.0011  -0.0056 -0.0039 136 PRO   A CG  
2915 C CD  A PRO   A 136 ? 0.1688 0.2033 0.2619 0.0032  0.0016  0.0862  136 PRO   A CD  
2916 C CD  B PRO   A 136 ? 0.1836 0.1823 0.1962 0.0012  -0.0046 -0.0030 136 PRO   A CD  
2931 N N   A ILE   A 137 ? 0.1236 0.1896 0.2409 -0.0021 -0.0169 0.0595  137 ILE   A N   
2932 N N   B ILE   A 137 ? 0.1810 0.1941 0.1912 -0.0044 -0.0075 0.0026  137 ILE   A N   
2933 C CA  A ILE   A 137 ? 0.1302 0.1967 0.2472 -0.0135 -0.0248 0.0516  137 ILE   A CA  
2934 C CA  B ILE   A 137 ? 0.1809 0.1990 0.1972 -0.0062 -0.0063 0.0051  137 ILE   A CA  
2935 C C   A ILE   A 137 ? 0.1341 0.1907 0.2196 -0.0181 -0.0282 0.0455  137 ILE   A C   
2936 C C   B ILE   A 137 ? 0.1761 0.1996 0.1934 -0.0083 -0.0039 0.0077  137 ILE   A C   
2937 O O   A ILE   A 137 ? 0.1350 0.1822 0.2283 -0.0237 -0.0117 0.0397  137 ILE   A O   
2938 O O   B ILE   A 137 ? 0.1772 0.2019 0.1953 -0.0094 -0.0025 0.0078  137 ILE   A O   
2939 C CB  A ILE   A 137 ? 0.1392 0.2156 0.2760 -0.0164 -0.0427 0.0488  137 ILE   A CB  
2940 C CB  B ILE   A 137 ? 0.1860 0.2022 0.2091 -0.0060 -0.0086 0.0067  137 ILE   A CB  
2941 C CG1 A ILE   A 137 ? 0.1538 0.2392 0.3090 -0.0111 -0.0427 0.0478  137 ILE   A CG1 
2942 C CG1 B ILE   A 137 ? 0.1886 0.2037 0.2169 -0.0056 -0.0117 0.0129  137 ILE   A CG1 
2943 C CG2 A ILE   A 137 ? 0.1474 0.2144 0.2859 -0.0185 -0.0455 0.0388  137 ILE   A CG2 
2944 C CG2 B ILE   A 137 ? 0.1888 0.2037 0.2127 -0.0050 -0.0079 0.0044  137 ILE   A CG2 
2945 C CD1 A ILE   A 137 ? 0.1757 0.2572 0.3409 -0.0052 -0.0353 0.0436  137 ILE   A CD1 
2946 C CD1 B ILE   A 137 ? 0.1906 0.2032 0.2223 -0.0065 -0.0132 0.0170  137 ILE   A CD1 
2969 N N   A HIS   A 138 ? 0.1377 0.2022 0.2067 -0.0165 -0.0187 0.0397  138 HIS   A N   
2970 N N   B HIS   A 138 ? 0.1692 0.1977 0.1909 -0.0098 -0.0011 0.0093  138 HIS   A N   
2971 C CA  A HIS   A 138 ? 0.1439 0.2077 0.1905 -0.0204 -0.0183 0.0313  138 HIS   A CA  
2972 C CA  B HIS   A 138 ? 0.1612 0.1928 0.1885 -0.0108 -0.0002 0.0151  138 HIS   A CA  
2973 C C   A HIS   A 138 ? 0.1342 0.1942 0.1816 -0.0161 -0.0151 0.0366  138 HIS   A C   
2974 C C   B HIS   A 138 ? 0.1460 0.1862 0.1838 -0.0123 -0.0007 0.0276  138 HIS   A C   
2975 O O   A HIS   A 138 ? 0.1443 0.1936 0.1911 -0.0202 -0.0101 0.0259  138 HIS   A O   
2976 O O   B HIS   A 138 ? 0.1490 0.1862 0.1830 -0.0141 0.0009  0.0250  138 HIS   A O   
2977 C CB  A HIS   A 138 ? 0.1614 0.2242 0.1844 -0.0273 -0.0309 0.0198  138 HIS   A CB  
2978 C CB  B HIS   A 138 ? 0.1665 0.1944 0.1929 -0.0087 0.0000  0.0087  138 HIS   A CB  
2979 C CG  A HIS   A 138 ? 0.1844 0.2358 0.1922 -0.0274 -0.0281 0.0133  138 HIS   A CG  
2980 C CG  B HIS   A 138 ? 0.1720 0.1954 0.2006 -0.0069 0.0001  0.0039  138 HIS   A CG  
2981 N ND1 A HIS   A 138 ? 0.1973 0.2465 0.2216 -0.0288 -0.0259 0.0014  138 HIS   A ND1 
2982 N ND1 B HIS   A 138 ? 0.1753 0.1974 0.2089 -0.0061 0.0001  -0.0002 138 HIS   A ND1 
2983 C CD2 A HIS   A 138 ? 0.1859 0.2403 0.1952 -0.0208 -0.0255 0.0174  138 HIS   A CD2 
2984 C CD2 B HIS   A 138 ? 0.1724 0.1946 0.2036 -0.0047 0.0007  0.0036  138 HIS   A CD2 
2985 C CE1 A HIS   A 138 ? 0.2022 0.2517 0.2215 -0.0212 -0.0247 -0.0016 138 HIS   A CE1 
2986 C CE1 B HIS   A 138 ? 0.1763 0.1973 0.2107 -0.0047 0.0004  -0.0004 138 HIS   A CE1 
2987 N NE2 A HIS   A 138 ? 0.1955 0.2487 0.2008 -0.0186 -0.0183 0.0050  138 HIS   A NE2 
2988 N NE2 B HIS   A 138 ? 0.1746 0.1958 0.2082 -0.0041 0.0020  0.0010  138 HIS   A NE2 
3003 N N   . SER   A 139 ? 0.1301 0.1791 0.1841 -0.0134 -0.0036 0.0417  139 SER   A N   
3004 C CA  . SER   A 139 ? 0.1258 0.1730 0.1812 -0.0130 -0.0069 0.0427  139 SER   A CA  
3005 C C   . SER   A 139 ? 0.1213 0.1616 0.1770 -0.0125 -0.0015 0.0353  139 SER   A C   
3006 O O   . SER   A 139 ? 0.1193 0.1597 0.1857 -0.0118 0.0019  0.0342  139 SER   A O   
3007 C CB  . SER   A 139 ? 0.1276 0.1715 0.1879 -0.0166 -0.0093 0.0461  139 SER   A CB  
3008 O OG  . SER   A 139 ? 0.1323 0.1683 0.1915 -0.0231 -0.0141 0.0479  139 SER   A OG  
3015 N N   A LEU   A 140 ? 0.1172 0.1687 0.1800 -0.0078 0.0018  0.0499  140 LEU   A N   
3016 N N   B LEU   A 140 ? 0.1231 0.1560 0.1609 -0.0135 0.0023  0.0343  140 LEU   A N   
3017 C CA  A LEU   A 140 ? 0.1148 0.1615 0.1812 -0.0064 -0.0010 0.0490  140 LEU   A CA  
3018 C CA  B LEU   A 140 ? 0.1250 0.1474 0.1467 -0.0147 0.0050  0.0304  140 LEU   A CA  
3019 C C   A LEU   A 140 ? 0.1075 0.1631 0.1783 -0.0112 0.0044  0.0378  140 LEU   A C   
3020 C C   B LEU   A 140 ? 0.1280 0.1485 0.1508 -0.0156 0.0047  0.0239  140 LEU   A C   
3021 O O   A LEU   A 140 ? 0.1151 0.1641 0.1921 -0.0034 0.0054  0.0348  140 LEU   A O   
3022 O O   B LEU   A 140 ? 0.1306 0.1483 0.1533 -0.0143 0.0010  0.0233  140 LEU   A O   
3023 C CB  A LEU   A 140 ? 0.1208 0.1683 0.1903 -0.0089 0.0021  0.0444  140 LEU   A CB  
3024 C CB  B LEU   A 140 ? 0.1226 0.1397 0.1335 -0.0165 0.0076  0.0345  140 LEU   A CB  
3025 C CG  A LEU   A 140 ? 0.1213 0.1770 0.1962 -0.0193 0.0071  0.0450  140 LEU   A CG  
3026 C CG  B LEU   A 140 ? 0.1219 0.1357 0.1263 -0.0155 0.0082  0.0400  140 LEU   A CG  
3027 C CD1 A LEU   A 140 ? 0.1349 0.1823 0.1992 -0.0073 0.0034  0.0464  140 LEU   A CD1 
3028 C CD1 B LEU   A 140 ? 0.1237 0.1335 0.1167 -0.0152 0.0106  0.0430  140 LEU   A CD1 
3029 C CD2 A LEU   A 140 ? 0.1305 0.1858 0.2165 -0.0167 0.0124  0.0453  140 LEU   A CD2 
3030 C CD2 B LEU   A 140 ? 0.1211 0.1371 0.1286 -0.0130 0.0053  0.0403  140 LEU   A CD2 
3053 N N   A ARG   A 141 ? 0.1173 0.1695 0.1924 -0.0135 -0.0075 0.0327  141 ARG   A N   
3054 N N   B ARG   A 141 ? 0.1288 0.1503 0.1562 -0.0170 0.0067  0.0199  141 ARG   A N   
3055 C CA  A ARG   A 141 ? 0.1345 0.1885 0.2117 -0.0251 -0.0146 0.0151  141 ARG   A CA  
3056 C CA  B ARG   A 141 ? 0.1286 0.1541 0.1594 -0.0201 0.0098  0.0140  141 ARG   A CA  
3057 C C   A ARG   A 141 ? 0.1354 0.1687 0.1928 -0.0189 -0.0120 0.0203  141 ARG   A C   
3058 C C   B ARG   A 141 ? 0.1318 0.1537 0.1579 -0.0162 0.0070  0.0121  141 ARG   A C   
3059 O O   A ARG   A 141 ? 0.1358 0.1626 0.2004 -0.0215 0.0042  0.0166  141 ARG   A O   
3060 O O   B ARG   A 141 ? 0.1330 0.1539 0.1616 -0.0167 0.0082  0.0093  141 ARG   A O   
3061 C CB  A ARG   A 141 ? 0.1438 0.2203 0.2498 -0.0353 -0.0240 -0.0043 141 ARG   A CB  
3062 C CB  B ARG   A 141 ? 0.1247 0.1579 0.1644 -0.0257 0.0143  0.0113  141 ARG   A CB  
3063 C CG  A ARG   A 141 ? 0.1822 0.2532 0.2945 -0.0324 -0.0197 -0.0136 141 ARG   A CG  
3064 C CG  B ARG   A 141 ? 0.1264 0.1629 0.1744 -0.0263 0.0161  0.0068  141 ARG   A CG  
3065 C CD  A ARG   A 141 ? 0.1990 0.2662 0.3081 -0.0416 -0.0207 -0.0103 141 ARG   A CD  
3066 C CD  B ARG   A 141 ? 0.1248 0.1603 0.1794 -0.0283 0.0144  0.0076  141 ARG   A CD  
3067 N NE  A ARG   A 141 ? 0.1967 0.2732 0.3137 -0.0483 -0.0267 -0.0051 141 ARG   A NE  
3068 N NE  B ARG   A 141 ? 0.1240 0.1612 0.1844 -0.0266 0.0207  0.0148  141 ARG   A NE  
3069 C CZ  A ARG   A 141 ? 0.1980 0.2866 0.3235 -0.0536 -0.0220 -0.0025 141 ARG   A CZ  
3070 C CZ  B ARG   A 141 ? 0.1276 0.1612 0.1953 -0.0246 0.0190  0.0179  141 ARG   A CZ  
3071 N NH1 A ARG   A 141 ? 0.1993 0.2937 0.3267 -0.0483 -0.0175 -0.0085 141 ARG   A NH1 
3072 N NH1 B ARG   A 141 ? 0.1285 0.1642 0.2021 -0.0243 0.0170  0.0164  141 ARG   A NH1 
3073 N NH2 A ARG   A 141 ? 0.1963 0.2938 0.3385 -0.0513 -0.0267 0.0018  141 ARG   A NH2 
3074 N NH2 B ARG   A 141 ? 0.1288 0.1627 0.1992 -0.0211 0.0206  0.0203  141 ARG   A NH2 
3101 N N   A VAL   A 142 ? 0.1258 0.1591 0.1856 -0.0148 -0.0078 0.0154  142 VAL   A N   
3102 N N   B VAL   A 142 ? 0.1308 0.1536 0.1551 -0.0123 0.0066  0.0113  142 VAL   A N   
3103 C CA  A VAL   A 142 ? 0.1293 0.1534 0.1827 -0.0154 0.0073  0.0125  142 VAL   A CA  
3104 C CA  B VAL   A 142 ? 0.1317 0.1529 0.1531 -0.0093 0.0053  0.0099  142 VAL   A CA  
3105 C C   A VAL   A 142 ? 0.1173 0.1492 0.1716 -0.0206 0.0050  0.0168  142 VAL   A C   
3106 C C   B VAL   A 142 ? 0.1257 0.1502 0.1554 -0.0115 0.0041  0.0110  142 VAL   A C   
3107 O O   A VAL   A 142 ? 0.1223 0.1507 0.1834 -0.0060 0.0086  0.0160  142 VAL   A O   
3108 O O   B VAL   A 142 ? 0.1272 0.1508 0.1527 -0.0088 0.0054  0.0094  142 VAL   A O   
3109 C CB  A VAL   A 142 ? 0.1339 0.1624 0.1758 -0.0140 0.0078  0.0158  142 VAL   A CB  
3110 C CB  B VAL   A 142 ? 0.1356 0.1563 0.1478 -0.0055 0.0029  0.0117  142 VAL   A CB  
3111 C CG1 A VAL   A 142 ? 0.1312 0.1542 0.1762 -0.0188 0.0101  0.0123  142 VAL   A CG1 
3112 C CG1 B VAL   A 142 ? 0.1373 0.1572 0.1464 -0.0057 0.0020  0.0124  142 VAL   A CG1 
3113 C CG2 A VAL   A 142 ? 0.1442 0.1779 0.1963 -0.0073 0.0014  0.0201  142 VAL   A CG2 
3114 C CG2 B VAL   A 142 ? 0.1392 0.1579 0.1477 -0.0015 -0.0000 0.0150  142 VAL   A CG2 
3133 N N   . CYS   A 143 ? 0.1195 0.1485 0.1667 -0.0149 0.0001  0.0130  143 CYS   A N   
3134 C CA  . CYS   A 143 ? 0.1173 0.1429 0.1731 -0.0156 0.0042  0.0183  143 CYS   A CA  
3135 C C   . CYS   A 143 ? 0.1159 0.1370 0.1732 -0.0102 0.0060  0.0231  143 CYS   A C   
3136 O O   . CYS   A 143 ? 0.1207 0.1381 0.1710 -0.0069 0.0051  0.0237  143 CYS   A O   
3137 C CB  . CYS   A 143 ? 0.1338 0.1438 0.1831 -0.0095 0.0108  0.0235  143 CYS   A CB  
3138 S SG  . CYS   A 143 ? 0.1457 0.1507 0.1711 0.0038  0.0145  0.0192  143 CYS   A SG  
3145 N N   . VAL   A 144 ? 0.1191 0.1425 0.1898 -0.0079 0.0104  0.0349  144 VAL   A N   
3146 C CA  . VAL   A 144 ? 0.1254 0.1520 0.2255 -0.0144 0.0210  0.0276  144 VAL   A CA  
3147 C C   . VAL   A 144 ? 0.1258 0.1423 0.2181 -0.0228 -0.0020 0.0168  144 VAL   A C   
3148 O O   . VAL   A 144 ? 0.1405 0.1460 0.2219 -0.0064 -0.0034 0.0243  144 VAL   A O   
3149 C CB  . VAL   A 144 ? 0.1501 0.1713 0.2861 -0.0021 0.0360  0.0343  144 VAL   A CB  
3150 C CG1 . VAL   A 144 ? 0.1592 0.1908 0.3232 -0.0072 0.0181  0.0307  144 VAL   A CG1 
3151 C CG2 . VAL   A 144 ? 0.1362 0.1745 0.2934 -0.0049 0.0424  0.0559  144 VAL   A CG2 
3161 N N   . ASP   A 145 ? 0.1286 0.1421 0.2220 -0.0205 0.0027  0.0092  145 ASP   A N   
3162 C CA  . ASP   A 145 ? 0.1424 0.1473 0.2256 -0.0262 -0.0000 0.0075  145 ASP   A CA  
3163 C C   . ASP   A 145 ? 0.1420 0.1396 0.2157 -0.0166 0.0036  -0.0027 145 ASP   A C   
3164 O O   . ASP   A 145 ? 0.1569 0.1514 0.2745 -0.0169 -0.0027 -0.0363 145 ASP   A O   
3165 C CB  . ASP   A 145 ? 0.1550 0.1810 0.2424 -0.0304 -0.0143 0.0097  145 ASP   A CB  
3166 C CG  . ASP   A 145 ? 0.1713 0.2182 0.2721 -0.0472 -0.0237 0.0143  145 ASP   A CG  
3167 O OD1 . ASP   A 145 ? 0.1668 0.2285 0.2902 -0.0572 -0.0178 0.0150  145 ASP   A OD1 
3168 O OD2 . ASP   A 145 ? 0.1928 0.2403 0.2749 -0.0545 -0.0372 0.0140  145 ASP   A OD2 
3173 N N   . THR   A 146 ? 0.1282 0.1342 0.1839 -0.0136 0.0071  0.0082  146 THR   A N   
3174 C CA  . THR   A 146 ? 0.1268 0.1293 0.1678 -0.0065 0.0060  0.0073  146 THR   A CA  
3175 C C   . THR   A 146 ? 0.1256 0.1235 0.1731 0.0012  0.0096  0.0139  146 THR   A C   
3176 O O   . THR   A 146 ? 0.1353 0.1373 0.1893 0.0036  0.0044  0.0070  146 THR   A O   
3177 C CB  . THR   A 146 ? 0.1249 0.1323 0.1646 -0.0053 0.0055  0.0108  146 THR   A CB  
3178 O OG1 . THR   A 146 ? 0.1237 0.1507 0.1751 -0.0010 0.0067  0.0058  146 THR   A OG1 
3179 C CG2 . THR   A 146 ? 0.1253 0.1335 0.1863 -0.0067 0.0065  0.0120  146 THR   A CG2 
3187 N N   . VAL   A 147 ? 0.1192 0.1286 0.1695 -0.0001 0.0114  0.0183  147 VAL   A N   
3188 C CA  . VAL   A 147 ? 0.1208 0.1308 0.1708 -0.0086 0.0213  0.0165  147 VAL   A CA  
3189 C C   . VAL   A 147 ? 0.1265 0.1244 0.1818 -0.0095 0.0177  0.0236  147 VAL   A C   
3190 O O   . VAL   A 147 ? 0.1240 0.1310 0.1951 -0.0131 0.0121  0.0192  147 VAL   A O   
3191 C CB  . VAL   A 147 ? 0.1343 0.1291 0.1623 -0.0107 0.0190  0.0200  147 VAL   A CB  
3192 C CG1 . VAL   A 147 ? 0.1662 0.1391 0.1614 -0.0067 0.0168  0.0288  147 VAL   A CG1 
3193 C CG2 . VAL   A 147 ? 0.1424 0.1288 0.1722 -0.0130 0.0095  0.0199  147 VAL   A CG2 
3203 N N   . ARG   A 148 ? 0.1245 0.1282 0.1863 -0.0099 0.0147  0.0315  148 ARG   A N   
3204 C CA  . ARG   A 148 ? 0.1317 0.1286 0.1867 -0.0100 0.0059  0.0368  148 ARG   A CA  
3205 C C   . ARG   A 148 ? 0.1422 0.1323 0.1846 -0.0128 0.0118  0.0481  148 ARG   A C   
3206 O O   . ARG   A 148 ? 0.1694 0.1444 0.1997 -0.0167 0.0224  0.0415  148 ARG   A O   
3207 C CB  . ARG   A 148 ? 0.1363 0.1296 0.2049 -0.0015 0.0199  0.0323  148 ARG   A CB  
3208 C CG  . ARG   A 148 ? 0.1524 0.1302 0.2300 -0.0042 0.0344  0.0194  148 ARG   A CG  
3209 C CD  . ARG   A 148 ? 0.1697 0.1315 0.2483 -0.0034 0.0382  0.0388  148 ARG   A CD  
3210 N NE  . ARG   A 148 ? 0.1590 0.1378 0.2468 0.0042  0.0437  0.0408  148 ARG   A NE  
3211 C CZ  . ARG   A 148 ? 0.1598 0.1259 0.2337 0.0030  0.0478  0.0337  148 ARG   A CZ  
3212 N NH1 . ARG   A 148 ? 0.1644 0.1319 0.2461 -0.0070 0.0436  0.0140  148 ARG   A NH1 
3213 N NH2 . ARG   A 148 ? 0.1546 0.1453 0.2347 0.0159  0.0486  0.0385  148 ARG   A NH2 
3227 N N   . THR   A 149 ? 0.1412 0.1407 0.1674 -0.0166 0.0072  0.0368  149 THR   A N   
3228 C CA  . THR   A 149 ? 0.1405 0.1464 0.1669 -0.0149 0.0061  0.0368  149 THR   A CA  
3229 C C   . THR   A 149 ? 0.1378 0.1423 0.1633 -0.0194 0.0102  0.0431  149 THR   A C   
3230 O O   . THR   A 149 ? 0.1379 0.1492 0.1842 -0.0215 0.0118  0.0378  149 THR   A O   
3231 C CB  . THR   A 149 ? 0.1420 0.1588 0.1796 -0.0104 0.0096  0.0324  149 THR   A CB  
3232 O OG1 . THR   A 149 ? 0.1464 0.1478 0.1837 -0.0228 0.0064  0.0263  149 THR   A OG1 
3233 C CG2 . THR   A 149 ? 0.1388 0.1658 0.1940 -0.0066 0.0051  0.0353  149 THR   A CG2 
3241 N N   . ASN   A 150 ? 0.1405 0.1414 0.1717 -0.0081 0.0038  0.0451  150 ASN   A N   
3242 C CA  . ASN   A 150 ? 0.1545 0.1509 0.1743 -0.0080 0.0120  0.0375  150 ASN   A CA  
3243 C C   . ASN   A 150 ? 0.1356 0.1446 0.1730 -0.0121 0.0027  0.0329  150 ASN   A C   
3244 O O   . ASN   A 150 ? 0.1471 0.1563 0.2110 -0.0120 -0.0115 0.0291  150 ASN   A O   
3245 C CB  . ASN   A 150 ? 0.1931 0.1791 0.2043 -0.0150 0.0349  0.0529  150 ASN   A CB  
3246 C CG  . ASN   A 150 ? 0.2473 0.2134 0.2702 -0.0138 0.0149  0.0618  150 ASN   A CG  
3247 O OD1 . ASN   A 150 ? 0.2701 0.2238 0.2927 -0.0217 0.0135  0.0778  150 ASN   A OD1 
3248 N ND2 . ASN   A 150 ? 0.2746 0.2352 0.3073 -0.0063 0.0030  0.0599  150 ASN   A ND2 
3255 N N   . VAL   A 151 ? 0.1335 0.1361 0.1731 -0.0148 0.0074  0.0293  151 VAL   A N   
3256 C CA  . VAL   A 151 ? 0.1397 0.1333 0.1653 -0.0173 0.0145  0.0305  151 VAL   A CA  
3257 C C   . VAL   A 151 ? 0.1334 0.1294 0.1742 -0.0222 0.0171  0.0378  151 VAL   A C   
3258 O O   . VAL   A 151 ? 0.1413 0.1378 0.2013 -0.0170 0.0137  0.0303  151 VAL   A O   
3259 C CB  . VAL   A 151 ? 0.1663 0.1530 0.1679 -0.0034 0.0193  0.0288  151 VAL   A CB  
3260 C CG1 . VAL   A 151 ? 0.1622 0.1782 0.1838 -0.0075 0.0075  0.0288  151 VAL   A CG1 
3261 C CG2 . VAL   A 151 ? 0.1794 0.1563 0.1700 -0.0005 0.0276  0.0239  151 VAL   A CG2 
3271 N N   . TYR   A 152 ? 0.1317 0.1323 0.1730 -0.0144 0.0155  0.0334  152 TYR   A N   
3272 C CA  . TYR   A 152 ? 0.1339 0.1405 0.1594 -0.0147 0.0215  0.0281  152 TYR   A CA  
3273 C C   . TYR   A 152 ? 0.1285 0.1373 0.1583 -0.0139 0.0238  0.0330  152 TYR   A C   
3274 O O   . TYR   A 152 ? 0.1380 0.1367 0.1638 -0.0235 0.0209  0.0253  152 TYR   A O   
3275 C CB  . TYR   A 152 ? 0.1499 0.1457 0.1606 -0.0105 0.0280  0.0273  152 TYR   A CB  
3276 C CG  . TYR   A 152 ? 0.1641 0.1631 0.1536 -0.0165 0.0355  0.0334  152 TYR   A CG  
3277 C CD1 . TYR   A 152 ? 0.1765 0.1859 0.1776 -0.0051 0.0350  0.0442  152 TYR   A CD1 
3278 C CD2 . TYR   A 152 ? 0.1698 0.1738 0.1492 -0.0265 0.0292  0.0287  152 TYR   A CD2 
3279 C CE1 . TYR   A 152 ? 0.1983 0.1970 0.1850 -0.0038 0.0182  0.0518  152 TYR   A CE1 
3280 C CE2 . TYR   A 152 ? 0.1905 0.1893 0.1587 -0.0308 0.0287  0.0341  152 TYR   A CE2 
3281 C CZ  . TYR   A 152 ? 0.2117 0.1929 0.1691 -0.0197 0.0209  0.0540  152 TYR   A CZ  
3282 O OH  . TYR   A 152 ? 0.2408 0.2145 0.1976 -0.0102 0.0207  0.0681  152 TYR   A OH  
3292 N N   A LEU   A 153 ? 0.1263 0.1372 0.1724 -0.0195 0.0245  0.0380  153 LEU   A N   
3293 N N   B LEU   A 153 ? 0.1315 0.1422 0.1419 -0.0091 0.0185  0.0281  153 LEU   A N   
3294 C CA  A LEU   A 153 ? 0.1232 0.1298 0.1867 -0.0042 0.0199  0.0384  153 LEU   A CA  
3295 C CA  B LEU   A 153 ? 0.1347 0.1459 0.1296 -0.0017 0.0139  0.0232  153 LEU   A CA  
3296 C C   A LEU   A 153 ? 0.1279 0.1345 0.2041 -0.0101 0.0330  0.0338  153 LEU   A C   
3297 C C   B LEU   A 153 ? 0.1374 0.1510 0.1195 0.0010  0.0097  0.0211  153 LEU   A C   
3298 O O   A LEU   A 153 ? 0.1311 0.1379 0.2264 -0.0114 0.0411  0.0281  153 LEU   A O   
3299 O O   B LEU   A 153 ? 0.1357 0.1524 0.1139 0.0048  0.0069  0.0197  153 LEU   A O   
3300 C CB  A LEU   A 153 ? 0.1182 0.1345 0.1960 -0.0065 0.0057  0.0404  153 LEU   A CB  
3301 C CB  B LEU   A 153 ? 0.1350 0.1461 0.1342 0.0030  0.0113  0.0234  153 LEU   A CB  
3302 C CG  A LEU   A 153 ? 0.1259 0.1391 0.1838 -0.0101 0.0182  0.0334  153 LEU   A CG  
3303 C CG  B LEU   A 153 ? 0.1364 0.1453 0.1315 0.0079  0.0126  0.0258  153 LEU   A CG  
3304 C CD1 A LEU   A 153 ? 0.1314 0.1386 0.1895 -0.0128 0.0027  0.0366  153 LEU   A CD1 
3305 C CD1 B LEU   A 153 ? 0.1374 0.1443 0.1367 0.0094  0.0118  0.0305  153 LEU   A CD1 
3306 C CD2 A LEU   A 153 ? 0.1397 0.1447 0.1777 -0.0151 0.0257  0.0094  153 LEU   A CD2 
3307 C CD2 B LEU   A 153 ? 0.1371 0.1471 0.1318 0.0091  0.0121  0.0215  153 LEU   A CD2 
3330 N N   A ALA   A 154 ? 0.1234 0.1304 0.2107 -0.0070 0.0314  0.0390  154 ALA   A N   
3331 N N   B ALA   A 154 ? 0.1403 0.1533 0.1193 0.0006  0.0102  0.0200  154 ALA   A N   
3332 C CA  A ALA   A 154 ? 0.1383 0.1356 0.2181 -0.0054 0.0362  0.0333  154 ALA   A CA  
3333 C CA  B ALA   A 154 ? 0.1465 0.1571 0.1288 0.0005  0.0093  0.0201  154 ALA   A CA  
3334 C C   A ALA   A 154 ? 0.1359 0.1305 0.2212 0.0014  0.0301  0.0435  154 ALA   A C   
3335 C C   B ALA   A 154 ? 0.1499 0.1597 0.1331 -0.0023 0.0074  0.0191  154 ALA   A C   
3336 O O   A ALA   A 154 ? 0.1432 0.1417 0.2183 -0.0038 0.0312  0.0410  154 ALA   A O   
3337 O O   B ALA   A 154 ? 0.1512 0.1583 0.1278 -0.0056 0.0103  0.0226  154 ALA   A O   
3338 C CB  A ALA   A 154 ? 0.1481 0.1382 0.2258 0.0065  0.0282  0.0234  154 ALA   A CB  
3339 C CB  B ALA   A 154 ? 0.1474 0.1558 0.1271 0.0015  0.0068  0.0207  154 ALA   A CB  
3350 N N   A VAL   A 155 ? 0.1440 0.1441 0.2326 0.0066  0.0271  0.0581  155 VAL   A N   
3351 N N   B VAL   A 155 ? 0.1533 0.1635 0.1427 -0.0011 0.0021  0.0178  155 VAL   A N   
3352 C CA  A VAL   A 155 ? 0.1492 0.1578 0.2554 0.0060  0.0225  0.0681  155 VAL   A CA  
3353 C CA  B VAL   A 155 ? 0.1578 0.1677 0.1512 0.0003  -0.0018 0.0195  155 VAL   A CA  
3354 C C   A VAL   A 155 ? 0.1596 0.1636 0.2999 0.0151  0.0201  0.0880  155 VAL   A C   
3355 C C   B VAL   A 155 ? 0.1670 0.1757 0.1691 0.0052  -0.0055 0.0182  155 VAL   A C   
3356 O O   A VAL   A 155 ? 0.1570 0.1661 0.3143 0.0224  0.0352  0.0764  155 VAL   A O   
3357 O O   B VAL   A 155 ? 0.1654 0.1741 0.1728 0.0082  -0.0067 0.0191  155 VAL   A O   
3358 C CB  A VAL   A 155 ? 0.1530 0.1673 0.2354 0.0064  0.0116  0.0631  155 VAL   A CB  
3359 C CB  B VAL   A 155 ? 0.1520 0.1636 0.1456 -0.0036 -0.0034 0.0240  155 VAL   A CB  
3360 C CG1 A VAL   A 155 ? 0.1654 0.1805 0.2447 0.0105  0.0029  0.0654  155 VAL   A CG1 
3361 C CG1 B VAL   A 155 ? 0.1496 0.1624 0.1473 -0.0069 -0.0079 0.0269  155 VAL   A CG1 
3362 C CG2 A VAL   A 155 ? 0.1693 0.1788 0.2368 0.0161  0.0033  0.0575  155 VAL   A CG2 
3363 C CG2 B VAL   A 155 ? 0.1489 0.1618 0.1398 -0.0069 -0.0006 0.0244  155 VAL   A CG2 
3382 N N   A PHE   A 156 ? 0.1799 0.1733 0.3383 0.0182  0.0175  0.1052  156 PHE   A N   
3383 N N   B PHE   A 156 ? 0.1796 0.1853 0.1841 0.0074  -0.0046 0.0151  156 PHE   A N   
3384 C CA  A PHE   A 156 ? 0.2021 0.1787 0.3826 0.0251  0.0173  0.1102  156 PHE   A CA  
3385 C CA  B PHE   A 156 ? 0.1911 0.1945 0.1983 0.0103  -0.0026 0.0157  156 PHE   A CA  
3386 C C   A PHE   A 156 ? 0.1976 0.1847 0.3954 0.0359  0.0236  0.1180  156 PHE   A C   
3387 C C   B PHE   A 156 ? 0.2017 0.2040 0.2103 0.0118  -0.0001 0.0182  156 PHE   A C   
3388 O O   A PHE   A 156 ? 0.2081 0.1985 0.4224 0.0304  0.0294  0.0917  156 PHE   A O   
3389 O O   B PHE   A 156 ? 0.2011 0.2023 0.2117 0.0144  0.0025  0.0226  156 PHE   A O   
3390 C CB  A PHE   A 156 ? 0.2345 0.1821 0.4009 0.0180  0.0024  0.1219  156 PHE   A CB  
3391 C CB  B PHE   A 156 ? 0.1914 0.1952 0.2049 0.0114  -0.0008 0.0136  156 PHE   A CB  
3392 C CG  A PHE   A 156 ? 0.2732 0.1933 0.4196 0.0247  -0.0112 0.1142  156 PHE   A CG  
3393 C CG  B PHE   A 156 ? 0.1924 0.1958 0.2094 0.0117  0.0003  0.0122  156 PHE   A CG  
3394 C CD1 A PHE   A 156 ? 0.2902 0.2058 0.4310 0.0307  -0.0147 0.0947  156 PHE   A CD1 
3395 C CD1 B PHE   A 156 ? 0.1937 0.1970 0.2112 0.0107  -0.0008 0.0122  156 PHE   A CD1 
3396 C CD2 A PHE   A 156 ? 0.2923 0.2012 0.4264 0.0329  -0.0150 0.1233  156 PHE   A CD2 
3397 C CD2 B PHE   A 156 ? 0.1937 0.1965 0.2106 0.0124  0.0018  0.0125  156 PHE   A CD2 
3398 C CE1 A PHE   A 156 ? 0.3048 0.2146 0.4453 0.0344  -0.0122 0.0830  156 PHE   A CE1 
3399 C CE1 B PHE   A 156 ? 0.1945 0.1961 0.2107 0.0110  -0.0009 0.0131  156 PHE   A CE1 
3400 C CE2 A PHE   A 156 ? 0.3085 0.2151 0.4385 0.0388  -0.0169 0.1001  156 PHE   A CE2 
3401 C CE2 B PHE   A 156 ? 0.1950 0.1971 0.2131 0.0129  0.0016  0.0127  156 PHE   A CE2 
3402 C CZ  A PHE   A 156 ? 0.3101 0.2186 0.4472 0.0426  -0.0154 0.0787  156 PHE   A CZ  
3403 C CZ  B PHE   A 156 ? 0.1948 0.1966 0.2112 0.0126  0.0005  0.0130  156 PHE   A CZ  
3422 N N   A ASP   A 157 ? 0.2013 0.1932 0.3820 0.0340  0.0241  0.1386  157 ASP   A N   
3423 N N   B ASP   A 157 ? 0.2118 0.2149 0.2196 0.0115  -0.0031 0.0157  157 ASP   A N   
3424 C CA  A ASP   A 157 ? 0.2170 0.2139 0.3815 0.0343  0.0164  0.1398  157 ASP   A CA  
3425 C CA  B ASP   A 157 ? 0.2209 0.2263 0.2320 0.0113  -0.0032 0.0168  157 ASP   A CA  
3426 C C   A ASP   A 157 ? 0.1974 0.2256 0.3817 0.0389  0.0289  0.1425  157 ASP   A C   
3427 C C   B ASP   A 157 ? 0.2283 0.2369 0.2425 0.0107  -0.0042 0.0171  157 ASP   A C   
3428 O O   A ASP   A 157 ? 0.1841 0.2159 0.3713 0.0348  0.0311  0.1482  157 ASP   A O   
3429 O O   B ASP   A 157 ? 0.2286 0.2378 0.2402 0.0109  -0.0050 0.0152  157 ASP   A O   
3430 C CB  A ASP   A 157 ? 0.2494 0.2261 0.3985 0.0383  -0.0008 0.1295  157 ASP   A CB  
3431 C CB  B ASP   A 157 ? 0.2209 0.2262 0.2330 0.0114  -0.0012 0.0174  157 ASP   A CB  
3432 C CG  A ASP   A 157 ? 0.2803 0.2384 0.4245 0.0474  -0.0210 0.1229  157 ASP   A CG  
3433 C CG  B ASP   A 157 ? 0.2208 0.2253 0.2325 0.0137  0.0020  0.0185  157 ASP   A CG  
3434 O OD1 A ASP   A 157 ? 0.3114 0.2476 0.4539 0.0458  -0.0406 0.1057  157 ASP   A OD1 
3435 O OD1 B ASP   A 157 ? 0.2185 0.2215 0.2278 0.0144  0.0021  0.0210  157 ASP   A OD1 
3436 O OD2 A ASP   A 157 ? 0.2685 0.2389 0.4346 0.0477  -0.0172 0.1304  157 ASP   A OD2 
3437 O OD2 B ASP   A 157 ? 0.2194 0.2257 0.2358 0.0142  0.0051  0.0172  157 ASP   A OD2 
3446 N N   A LYS   A 158 ? 0.1998 0.2495 0.4009 0.0460  0.0358  0.1336  158 LYS   A N   
3447 N N   B LYS   A 158 ? 0.2353 0.2460 0.2540 0.0088  -0.0049 0.0190  158 LYS   A N   
3448 C CA  A LYS   A 158 ? 0.1947 0.2772 0.4113 0.0569  0.0484  0.1287  158 LYS   A CA  
3449 C CA  B LYS   A 158 ? 0.2429 0.2552 0.2640 0.0077  -0.0050 0.0211  158 LYS   A CA  
3450 C C   A LYS   A 158 ? 0.1783 0.2893 0.3987 0.0634  0.0408  0.1499  158 LYS   A C   
3451 C C   B LYS   A 158 ? 0.2452 0.2601 0.2660 0.0079  -0.0035 0.0271  158 LYS   A C   
3452 O O   A LYS   A 158 ? 0.1744 0.2908 0.3947 0.0513  0.0515  0.1555  158 LYS   A O   
3453 O O   B LYS   A 158 ? 0.2449 0.2615 0.2623 0.0071  -0.0048 0.0300  158 LYS   A O   
3454 C CB  A LYS   A 158 ? 0.2127 0.2913 0.4319 0.0584  0.0714  0.1212  158 LYS   A CB  
3455 C CB  B LYS   A 158 ? 0.2476 0.2598 0.2740 0.0072  -0.0064 0.0168  158 LYS   A CB  
3456 C CG  A LYS   A 158 ? 0.2312 0.3080 0.4574 0.0615  0.0902  0.1160  158 LYS   A CG  
3457 C CG  B LYS   A 158 ? 0.2508 0.2644 0.2849 0.0062  -0.0072 0.0148  158 LYS   A CG  
3458 C CD  A LYS   A 158 ? 0.2443 0.3240 0.4768 0.0579  0.1107  0.1200  158 LYS   A CD  
3459 C CD  B LYS   A 158 ? 0.2527 0.2672 0.2941 0.0061  -0.0076 0.0136  158 LYS   A CD  
3460 C CE  A LYS   A 158 ? 0.2544 0.3352 0.4929 0.0500  0.1275  0.1275  158 LYS   A CE  
3461 C CE  B LYS   A 158 ? 0.2542 0.2687 0.3012 0.0059  -0.0086 0.0126  158 LYS   A CE  
3462 N NZ  A LYS   A 158 ? 0.2611 0.3403 0.5016 0.0442  0.1378  0.1333  158 LYS   A NZ  
3463 N NZ  B LYS   A 158 ? 0.2556 0.2696 0.3061 0.0055  -0.0084 0.0112  158 LYS   A NZ  
3490 N N   A ASN   A 159 ? 0.1773 0.3059 0.4088 0.0670  0.0261  0.1505  159 ASN   A N   
3491 N N   B ASN   A 159 ? 0.2479 0.2637 0.2747 0.0095  0.0004  0.0283  159 ASN   A N   
3492 C CA  A ASN   A 159 ? 0.1792 0.3193 0.4124 0.0636  0.0101  0.1615  159 ASN   A CA  
3493 C CA  B ASN   A 159 ? 0.2508 0.2668 0.2824 0.0100  0.0045  0.0288  159 ASN   A CA  
3494 C C   A ASN   A 159 ? 0.1617 0.3138 0.3759 0.0424  0.0111  0.1562  159 ASN   A C   
3495 C C   B ASN   A 159 ? 0.2457 0.2633 0.2644 0.0102  0.0039  0.0272  159 ASN   A C   
3496 O O   A ASN   A 159 ? 0.1528 0.3234 0.3653 0.0356  0.0034  0.1435  159 ASN   A O   
3497 O O   B ASN   A 159 ? 0.2453 0.2667 0.2634 0.0106  0.0025  0.0282  159 ASN   A O   
3498 C CB  A ASN   A 159 ? 0.2027 0.3376 0.4586 0.0684  0.0087  0.1705  159 ASN   A CB  
3499 C CB  B ASN   A 159 ? 0.2579 0.2725 0.3083 0.0099  0.0092  0.0295  159 ASN   A CB  
3500 C CG  A ASN   A 159 ? 0.2321 0.3554 0.5097 0.0601  0.0202  0.1661  159 ASN   A CG  
3501 C CG  B ASN   A 159 ? 0.2638 0.2775 0.3304 0.0076  0.0131  0.0282  159 ASN   A CG  
3502 O OD1 A ASN   A 159 ? 0.2427 0.3641 0.5257 0.0545  0.0297  0.1644  159 ASN   A OD1 
3503 O OD1 B ASN   A 159 ? 0.2650 0.2792 0.3391 0.0062  0.0151  0.0272  159 ASN   A OD1 
3504 N ND2 A ASN   A 159 ? 0.2466 0.3620 0.5344 0.0588  0.0211  0.1610  159 ASN   A ND2 
3505 N ND2 B ASN   A 159 ? 0.2666 0.2797 0.3381 0.0068  0.0143  0.0275  159 ASN   A ND2 
3518 N N   A LEU   A 160 ? 0.1500 0.2918 0.3522 0.0301  -0.0030 0.1567  160 LEU   A N   
3519 N N   B LEU   A 160 ? 0.2393 0.2550 0.2481 0.0096  0.0026  0.0248  160 LEU   A N   
3520 C CA  A LEU   A 160 ? 0.1512 0.2731 0.3313 0.0128  0.0056  0.1473  160 LEU   A CA  
3521 C CA  B LEU   A 160 ? 0.2329 0.2458 0.2321 0.0080  0.0025  0.0217  160 LEU   A CA  
3522 C C   A LEU   A 160 ? 0.1356 0.2651 0.3243 0.0051  0.0183  0.1375  160 LEU   A C   
3523 C C   B LEU   A 160 ? 0.2270 0.2387 0.2244 0.0064  0.0045  0.0206  160 LEU   A C   
3524 O O   A LEU   A 160 ? 0.1310 0.2762 0.3418 -0.0016 0.0155  0.1287  160 LEU   A O   
3525 O O   B LEU   A 160 ? 0.2269 0.2389 0.2252 0.0059  0.0033  0.0195  160 LEU   A O   
3526 C CB  A LEU   A 160 ? 0.1619 0.2686 0.3127 -0.0002 0.0074  0.1376  160 LEU   A CB  
3527 C CB  B LEU   A 160 ? 0.2323 0.2446 0.2255 0.0072  0.0013  0.0190  160 LEU   A CB  
3528 C CG  A LEU   A 160 ? 0.1718 0.2726 0.3060 -0.0156 0.0190  0.1153  160 LEU   A CG  
3529 C CG  B LEU   A 160 ? 0.2317 0.2438 0.2209 0.0061  0.0001  0.0176  160 LEU   A CG  
3530 C CD1 A LEU   A 160 ? 0.1866 0.2811 0.3079 -0.0197 0.0178  0.1032  160 LEU   A CD1 
3531 C CD1 B LEU   A 160 ? 0.2312 0.2441 0.2192 0.0056  0.0003  0.0164  160 LEU   A CD1 
3532 C CD2 A LEU   A 160 ? 0.1699 0.2732 0.3024 -0.0209 0.0303  0.1033  160 LEU   A CD2 
3533 C CD2 B LEU   A 160 ? 0.2318 0.2434 0.2198 0.0051  0.0001  0.0186  160 LEU   A CD2 
3556 N N   A TYR   A 161 ? 0.1358 0.2439 0.3155 0.0124  0.0207  0.1340  161 TYR   A N   
3557 N N   B TYR   A 161 ? 0.2210 0.2313 0.2170 0.0070  0.0078  0.0220  161 TYR   A N   
3558 C CA  A TYR   A 161 ? 0.1363 0.2290 0.3124 0.0099  0.0280  0.1309  161 TYR   A CA  
3559 C CA  B TYR   A 161 ? 0.2164 0.2256 0.2132 0.0078  0.0097  0.0220  161 TYR   A CA  
3560 C C   A TYR   A 161 ? 0.1331 0.2407 0.3251 0.0085  0.0220  0.1234  161 TYR   A C   
3561 C C   B TYR   A 161 ? 0.2174 0.2307 0.2199 0.0083  0.0090  0.0224  161 TYR   A C   
3562 O O   A TYR   A 161 ? 0.1281 0.2437 0.3235 0.0037  0.0222  0.1188  161 TYR   A O   
3563 O O   B TYR   A 161 ? 0.2165 0.2298 0.2181 0.0079  0.0094  0.0195  161 TYR   A O   
3564 C CB  A TYR   A 161 ? 0.1504 0.2130 0.3193 0.0112  0.0256  0.1109  161 TYR   A CB  
3565 C CB  B TYR   A 161 ? 0.2113 0.2166 0.2052 0.0079  0.0109  0.0227  161 TYR   A CB  
3566 C CG  A TYR   A 161 ? 0.1501 0.2012 0.3138 0.0098  0.0202  0.0916  161 TYR   A CG  
3567 C CG  B TYR   A 161 ? 0.2059 0.2080 0.1989 0.0080  0.0117  0.0244  161 TYR   A CG  
3568 C CD1 A TYR   A 161 ? 0.1462 0.1919 0.3201 0.0052  0.0148  0.0758  161 TYR   A CD1 
3569 C CD1 B TYR   A 161 ? 0.2047 0.2050 0.1992 0.0081  0.0097  0.0244  161 TYR   A CD1 
3570 C CD2 A TYR   A 161 ? 0.1530 0.2107 0.3089 0.0116  0.0091  0.0791  161 TYR   A CD2 
3571 C CD2 B TYR   A 161 ? 0.2038 0.2037 0.1954 0.0080  0.0129  0.0284  161 TYR   A CD2 
3572 C CE1 A TYR   A 161 ? 0.1572 0.1879 0.3196 0.0016  0.0067  0.0739  161 TYR   A CE1 
3573 C CE1 B TYR   A 161 ? 0.2045 0.2043 0.1993 0.0083  0.0089  0.0258  161 TYR   A CE1 
3574 C CE2 A TYR   A 161 ? 0.1562 0.2021 0.3040 0.0031  0.0089  0.0840  161 TYR   A CE2 
3575 C CE2 B TYR   A 161 ? 0.2032 0.2025 0.1957 0.0077  0.0125  0.0313  161 TYR   A CE2 
3576 C CZ  A TYR   A 161 ? 0.1667 0.1919 0.3134 0.0005  0.0007  0.0847  161 TYR   A CZ  
3577 C CZ  B TYR   A 161 ? 0.2057 0.2035 0.1995 0.0086  0.0101  0.0309  161 TYR   A CZ  
3578 O OH  A TYR   A 161 ? 0.1819 0.1968 0.3266 -0.0043 -0.0046 0.0883  161 TYR   A OH  
3579 O OH  B TYR   A 161 ? 0.2094 0.2037 0.2078 0.0094  0.0104  0.0338  161 TYR   A OH  
3598 N N   A ASP   A 162 ? 0.1336 0.2524 0.3395 0.0090  0.0292  0.1233  162 ASP   A N   
3599 N N   B ASP   A 162 ? 0.2197 0.2369 0.2285 0.0085  0.0081  0.0277  162 ASP   A N   
3600 C CA  A ASP   A 162 ? 0.1351 0.2747 0.3433 0.0064  0.0341  0.1216  162 ASP   A CA  
3601 C CA  B ASP   A 162 ? 0.2235 0.2433 0.2387 0.0092  0.0052  0.0296  162 ASP   A CA  
3602 C C   A ASP   A 162 ? 0.1259 0.2921 0.3420 -0.0018 0.0354  0.1243  162 ASP   A C   
3603 C C   B ASP   A 162 ? 0.2308 0.2485 0.2476 0.0087  0.0051  0.0252  162 ASP   A C   
3604 O O   A ASP   A 162 ? 0.1305 0.2905 0.3589 -0.0114 0.0351  0.1205  162 ASP   A O   
3605 O O   B ASP   A 162 ? 0.2313 0.2500 0.2508 0.0080  0.0077  0.0239  162 ASP   A O   
3606 C CB  A ASP   A 162 ? 0.1431 0.2805 0.3562 0.0079  0.0458  0.1132  162 ASP   A CB  
3607 C CB  B ASP   A 162 ? 0.2204 0.2442 0.2436 0.0097  0.0030  0.0358  162 ASP   A CB  
3608 C CG  A ASP   A 162 ? 0.1593 0.2939 0.3774 0.0191  0.0488  0.0941  162 ASP   A CG  
3609 C CG  B ASP   A 162 ? 0.2175 0.2445 0.2457 0.0098  0.0011  0.0431  162 ASP   A CG  
3610 O OD1 A ASP   A 162 ? 0.1740 0.3033 0.3828 0.0100  0.0485  0.0887  162 ASP   A OD1 
3611 O OD1 B ASP   A 162 ? 0.2165 0.2445 0.2485 0.0107  0.0011  0.0471  162 ASP   A OD1 
3612 O OD2 A ASP   A 162 ? 0.1768 0.2990 0.4002 0.0369  0.0472  0.0785  162 ASP   A OD2 
3613 O OD2 B ASP   A 162 ? 0.2172 0.2445 0.2455 0.0107  0.0003  0.0468  162 ASP   A OD2 
3622 N N   A LYS   A 163 ? 0.1405 0.3165 0.3433 -0.0070 0.0108  0.1195  163 LYS   A N   
3623 N N   B LYS   A 163 ? 0.2379 0.2528 0.2553 0.0088  0.0033  0.0223  163 LYS   A N   
3624 C CA  A LYS   A 163 ? 0.1497 0.3331 0.3285 -0.0129 0.0017  0.1149  163 LYS   A CA  
3625 C CA  B LYS   A 163 ? 0.2437 0.2557 0.2610 0.0087  0.0022  0.0164  163 LYS   A CA  
3626 C C   A LYS   A 163 ? 0.1407 0.3250 0.3136 -0.0125 0.0167  0.1063  163 LYS   A C   
3627 C C   B LYS   A 163 ? 0.2400 0.2503 0.2439 0.0071  0.0021  0.0114  163 LYS   A C   
3628 O O   A LYS   A 163 ? 0.1360 0.3423 0.3378 -0.0175 0.0168  0.0927  163 LYS   A O   
3629 O O   B LYS   A 163 ? 0.2416 0.2518 0.2453 0.0034  0.0014  0.0111  163 LYS   A O   
3630 C CB  A LYS   A 163 ? 0.1851 0.3601 0.3563 -0.0069 -0.0206 0.1075  163 LYS   A CB  
3631 C CB  B LYS   A 163 ? 0.2524 0.2626 0.2842 0.0104  0.0022  0.0155  163 LYS   A CB  
3632 C CG  A LYS   A 163 ? 0.2269 0.3843 0.3971 -0.0075 -0.0196 0.1013  163 LYS   A CG  
3633 C CG  B LYS   A 163 ? 0.2602 0.2684 0.3068 0.0118  0.0005  0.0138  163 LYS   A CG  
3634 C CD  A LYS   A 163 ? 0.2674 0.4049 0.4433 -0.0098 -0.0207 0.0929  163 LYS   A CD  
3635 C CD  B LYS   A 163 ? 0.2669 0.2737 0.3259 0.0134  -0.0004 0.0120  163 LYS   A CD  
3636 C CE  A LYS   A 163 ? 0.2937 0.4185 0.4781 -0.0134 -0.0191 0.0878  163 LYS   A CE  
3637 C CE  B LYS   A 163 ? 0.2719 0.2769 0.3386 0.0152  -0.0019 0.0119  163 LYS   A CE  
3638 N NZ  A LYS   A 163 ? 0.3045 0.4267 0.4986 -0.0161 -0.0193 0.0863  163 LYS   A NZ  
3639 N NZ  B LYS   A 163 ? 0.2750 0.2788 0.3458 0.0161  -0.0021 0.0113  163 LYS   A NZ  
3666 N N   A LEU   A 164 ? 0.1285 0.2928 0.2889 -0.0228 0.0030  0.1000  164 LEU   A N   
3667 N N   B LEU   A 164 ? 0.2347 0.2430 0.2272 0.0095  0.0015  0.0061  164 LEU   A N   
3668 C CA  A LEU   A 164 ? 0.1331 0.2662 0.2685 -0.0254 0.0114  0.0919  164 LEU   A CA  
3669 C CA  B LEU   A 164 ? 0.2285 0.2353 0.2136 0.0105  0.0015  0.0002  164 LEU   A CA  
3670 C C   A LEU   A 164 ? 0.1382 0.2576 0.2675 -0.0229 0.0235  0.0808  164 LEU   A C   
3671 C C   B LEU   A 164 ? 0.2259 0.2320 0.2119 0.0067  0.0005  -0.0018 164 LEU   A C   
3672 O O   A LEU   A 164 ? 0.1515 0.2652 0.2681 -0.0306 0.0469  0.0570  164 LEU   A O   
3673 O O   B LEU   A 164 ? 0.2249 0.2313 0.2130 0.0046  0.0026  -0.0033 164 LEU   A O   
3674 C CB  A LEU   A 164 ? 0.1313 0.2525 0.2515 -0.0312 0.0167  0.0948  164 LEU   A CB  
3675 C CB  B LEU   A 164 ? 0.2257 0.2310 0.2039 0.0153  0.0027  -0.0040 164 LEU   A CB  
3676 C CG  A LEU   A 164 ? 0.1420 0.2495 0.2575 -0.0231 0.0082  0.0763  164 LEU   A CG  
3677 C CG  B LEU   A 164 ? 0.2238 0.2277 0.1980 0.0184  0.0028  -0.0069 164 LEU   A CG  
3678 C CD1 A LEU   A 164 ? 0.1343 0.2462 0.2565 -0.0147 0.0063  0.0670  164 LEU   A CD1 
3679 C CD1 B LEU   A 164 ? 0.2230 0.2260 0.1966 0.0202  0.0046  -0.0105 164 LEU   A CD1 
3680 C CD2 A LEU   A 164 ? 0.1555 0.2519 0.2637 -0.0244 0.0117  0.0659  164 LEU   A CD2 
3681 C CD2 B LEU   A 164 ? 0.2230 0.2266 0.1955 0.0192  0.0016  -0.0051 164 LEU   A CD2 
3704 N N   A VAL   A 165 ? 0.1392 0.2449 0.2677 -0.0202 0.0262  0.0808  165 VAL   A N   
3705 N N   B VAL   A 165 ? 0.2254 0.2306 0.2113 0.0036  -0.0016 -0.0010 165 VAL   A N   
3706 C CA  A VAL   A 165 ? 0.1471 0.2390 0.2603 -0.0196 0.0342  0.0805  165 VAL   A CA  
3707 C CA  B VAL   A 165 ? 0.2262 0.2301 0.2146 0.0011  -0.0032 0.0003  165 VAL   A CA  
3708 C C   A VAL   A 165 ? 0.1353 0.2505 0.2584 -0.0095 0.0386  0.0819  165 VAL   A C   
3709 C C   B VAL   A 165 ? 0.2293 0.2315 0.2192 0.0016  0.0017  0.0008  165 VAL   A C   
3710 O O   A VAL   A 165 ? 0.1341 0.2505 0.2537 -0.0099 0.0350  0.0768  165 VAL   A O   
3711 O O   B VAL   A 165 ? 0.2291 0.2319 0.2204 0.0014  0.0030  0.0014  165 VAL   A O   
3712 C CB  A VAL   A 165 ? 0.1642 0.2282 0.2669 -0.0242 0.0370  0.0678  165 VAL   A CB  
3713 C CB  B VAL   A 165 ? 0.2245 0.2295 0.2145 -0.0027 -0.0087 0.0009  165 VAL   A CB  
3714 C CG1 A VAL   A 165 ? 0.1700 0.2294 0.2682 -0.0250 0.0390  0.0578  165 VAL   A CG1 
3715 C CG1 B VAL   A 165 ? 0.2242 0.2302 0.2138 -0.0048 -0.0120 0.0004  165 VAL   A CG1 
3716 C CG2 A VAL   A 165 ? 0.1776 0.2244 0.2723 -0.0249 0.0303  0.0721  165 VAL   A CG2 
3717 C CG2 B VAL   A 165 ? 0.2237 0.2283 0.2150 -0.0037 -0.0096 0.0003  165 VAL   A CG2 
3736 N N   A SER   A 166 ? 0.1261 0.2641 0.2896 -0.0101 0.0310  0.0782  166 SER   A N   
3737 N N   B SER   A 166 ? 0.2316 0.2330 0.2250 0.0024  0.0046  -0.0006 166 SER   A N   
3738 C CA  A SER   A 166 ? 0.1303 0.2913 0.3061 -0.0155 0.0233  0.0668  166 SER   A CA  
3739 C CA  B SER   A 166 ? 0.2349 0.2351 0.2308 0.0026  0.0049  -0.0001 166 SER   A CA  
3740 C C   A SER   A 166 ? 0.1352 0.3179 0.2983 -0.0238 0.0074  0.0547  166 SER   A C   
3741 C C   B SER   A 166 ? 0.2358 0.2370 0.2265 0.0044  0.0033  0.0006  166 SER   A C   
3742 O O   A SER   A 166 ? 0.1558 0.3317 0.3296 -0.0363 0.0153  0.0329  166 SER   A O   
3743 O O   B SER   A 166 ? 0.2350 0.2359 0.2273 0.0063  0.0028  0.0002  166 SER   A O   
3744 C CB  A SER   A 166 ? 0.1513 0.2999 0.3479 -0.0076 0.0102  0.0548  166 SER   A CB  
3745 C CB  B SER   A 166 ? 0.2363 0.2356 0.2423 0.0021  0.0065  -0.0014 166 SER   A CB  
3746 O OG  A SER   A 166 ? 0.1889 0.3064 0.3799 -0.0112 0.0128  0.0567  166 SER   A OG  
3747 O OG  B SER   A 166 ? 0.2387 0.2358 0.2492 0.0008  0.0094  -0.0021 166 SER   A OG  
3758 N N   A SER   A 167 ? 0.1459 0.3312 0.2648 -0.0089 -0.0035 0.0563  167 SER   A N   
3759 N N   B SER   A 167 ? 0.2394 0.2427 0.2265 0.0038  0.0032  -0.0003 167 SER   A N   
3760 C CA  A SER   A 167 ? 0.1702 0.3448 0.2532 0.0038  -0.0144 0.0470  167 SER   A CA  
3761 C CA  B SER   A 167 ? 0.2423 0.2493 0.2289 0.0004  0.0061  -0.0023 167 SER   A CA  
3762 C C   A SER   A 167 ? 0.1724 0.3460 0.2418 0.0089  -0.0066 0.0403  167 SER   A C   
3763 C C   B SER   A 167 ? 0.2458 0.2561 0.2361 -0.0007 0.0085  -0.0009 167 SER   A C   
3764 O O   A SER   A 167 ? 0.1887 0.3480 0.2507 0.0135  -0.0179 0.0430  167 SER   A O   
3765 O O   B SER   A 167 ? 0.2470 0.2562 0.2380 -0.0033 0.0090  -0.0014 167 SER   A O   
3766 C CB  A SER   A 167 ? 0.1822 0.3561 0.2562 0.0074  -0.0083 0.0503  167 SER   A CB  
3767 C CB  B SER   A 167 ? 0.2432 0.2505 0.2287 -0.0018 0.0054  -0.0047 167 SER   A CB  
3768 O OG  A SER   A 167 ? 0.1871 0.3620 0.2581 0.0031  0.0100  0.0595  167 SER   A OG  
3769 O OG  B SER   A 167 ? 0.2443 0.2510 0.2286 -0.0036 0.0043  -0.0069 167 SER   A OG  
3780 N N   A PHE   A 168 ? 0.1645 0.3447 0.2321 0.0127  0.0014  0.0313  168 PHE   A N   
3781 N N   B PHE   A 168 ? 0.2487 0.2629 0.2436 0.0006  0.0089  0.0015  168 PHE   A N   
3782 C CA  A PHE   A 168 ? 0.1648 0.3412 0.2467 0.0090  0.0166  0.0184  168 PHE   A CA  
3783 C CA  B PHE   A 168 ? 0.2529 0.2690 0.2528 0.0024  0.0088  0.0032  168 PHE   A CA  
3784 C C   A PHE   A 168 ? 0.1834 0.3661 0.2873 -0.0042 0.0624  -0.0029 168 PHE   A C   
3785 C C   B PHE   A 168 ? 0.2642 0.2776 0.2762 0.0018  0.0084  0.0011  168 PHE   A C   
3786 O O   A PHE   A 168 ? 0.1868 0.3703 0.3206 -0.0161 0.0707  0.0027  168 PHE   A O   
3787 O O   B PHE   A 168 ? 0.2635 0.2764 0.2773 0.0007  0.0128  0.0000  168 PHE   A O   
3788 C CB  A PHE   A 168 ? 0.1622 0.3126 0.2250 0.0056  -0.0034 0.0291  168 PHE   A CB  
3789 C CB  B PHE   A 168 ? 0.2458 0.2664 0.2403 0.0045  0.0091  0.0090  168 PHE   A CB  
3790 C CG  A PHE   A 168 ? 0.1573 0.2856 0.2100 -0.0046 -0.0043 0.0402  168 PHE   A CG  
3791 C CG  B PHE   A 168 ? 0.2399 0.2640 0.2300 0.0059  0.0098  0.0146  168 PHE   A CG  
3792 C CD1 A PHE   A 168 ? 0.1571 0.2814 0.2168 -0.0098 -0.0128 0.0546  168 PHE   A CD1 
3793 C CD1 B PHE   A 168 ? 0.2373 0.2635 0.2284 0.0068  0.0101  0.0170  168 PHE   A CD1 
3794 C CD2 A PHE   A 168 ? 0.1541 0.2726 0.2050 -0.0064 0.0136  0.0333  168 PHE   A CD2 
3795 C CD2 B PHE   A 168 ? 0.2377 0.2633 0.2253 0.0065  0.0107  0.0171  168 PHE   A CD2 
3796 C CE1 A PHE   A 168 ? 0.1484 0.2767 0.2101 -0.0133 -0.0105 0.0561  168 PHE   A CE1 
3797 C CE1 B PHE   A 168 ? 0.2358 0.2629 0.2268 0.0071  0.0110  0.0193  168 PHE   A CE1 
3798 C CE2 A PHE   A 168 ? 0.1555 0.2645 0.2080 -0.0098 0.0143  0.0462  168 PHE   A CE2 
3799 C CE2 B PHE   A 168 ? 0.2366 0.2629 0.2239 0.0070  0.0116  0.0197  168 PHE   A CE2 
3800 C CZ  A PHE   A 168 ? 0.1516 0.2676 0.2163 -0.0123 0.0041  0.0513  168 PHE   A CZ  
3801 C CZ  B PHE   A 168 ? 0.2360 0.2629 0.2253 0.0067  0.0119  0.0203  168 PHE   A CZ  
3820 N N   A LEU   A 169 ? 0.2304 0.3858 0.3333 -0.0153 0.0649  -0.0254 169 LEU   A N   
3821 N N   B LEU   A 169 ? 0.2763 0.2870 0.2985 0.0027  0.0048  -0.0002 169 LEU   A N   
3822 C CA  A LEU   A 169 ? 0.2968 0.4075 0.4111 -0.0187 0.0329  -0.0370 169 LEU   A CA  
3823 C CA  B LEU   A 169 ? 0.2879 0.2955 0.3170 0.0024  0.0016  -0.0006 169 LEU   A CA  
3824 C C   A LEU   A 169 ? 0.3167 0.4093 0.4501 -0.0229 0.0242  -0.0315 169 LEU   A C   
3825 C C   B LEU   A 169 ? 0.2921 0.2979 0.3286 0.0027  -0.0022 0.0000  169 LEU   A C   
3826 O O   A LEU   A 169 ? 0.3268 0.4093 0.4600 -0.0229 0.0224  -0.0310 169 LEU   A O   
3827 O O   B LEU   A 169 ? 0.2938 0.2989 0.3333 0.0010  -0.0033 0.0007  169 LEU   A O   
3828 C CB  A LEU   A 169 ? 0.3321 0.4240 0.4389 -0.0201 0.0130  -0.0486 169 LEU   A CB  
3829 C CB  B LEU   A 169 ? 0.2942 0.3006 0.3215 0.0020  0.0030  -0.0014 169 LEU   A CB  
3830 C CG  A LEU   A 169 ? 0.3603 0.4362 0.4602 -0.0233 -0.0019 -0.0627 169 LEU   A CG  
3831 C CG  B LEU   A 169 ? 0.2985 0.3043 0.3244 0.0016  0.0039  -0.0011 169 LEU   A CG  
3832 C CD1 A LEU   A 169 ? 0.3709 0.4402 0.4718 -0.0234 -0.0072 -0.0663 169 LEU   A CD1 
3833 C CD1 B LEU   A 169 ? 0.3004 0.3060 0.3256 0.0015  0.0036  -0.0013 169 LEU   A CD1 
3834 C CD2 A LEU   A 169 ? 0.3697 0.4404 0.4629 -0.0257 -0.0036 -0.0675 169 LEU   A CD2 
3835 C CD2 B LEU   A 169 ? 0.2997 0.3050 0.3256 0.0016  0.0043  -0.0009 169 LEU   A CD2 
3836 O OXT A LEU   A 169 ? 0.3128 0.4105 0.4598 -0.0236 0.0260  -0.0304 169 LEU   A OXT 
3837 O OXT B LEU   A 169 ? 0.2938 0.2988 0.3322 0.0034  -0.0031 0.0015  169 LEU   A OXT 
3860 N N   A SER   B 1   ? 0.3708 0.3619 0.3795 -0.1098 -0.0783 0.0402  1   SER   B N   
3861 N N   B SER   B 1   ? 0.3538 0.3537 0.3518 -0.0274 -0.0200 0.0116  1   SER   B N   
3862 C CA  A SER   B 1   ? 0.3553 0.3620 0.3763 -0.1171 -0.0874 0.0395  1   SER   B CA  
3863 C CA  B SER   B 1   ? 0.3514 0.3531 0.3510 -0.0278 -0.0197 0.0119  1   SER   B CA  
3864 C C   A SER   B 1   ? 0.3207 0.3605 0.3483 -0.1209 -0.0979 0.0594  1   SER   B C   
3865 C C   B SER   B 1   ? 0.3448 0.3503 0.3488 -0.0283 -0.0204 0.0158  1   SER   B C   
3866 O O   A SER   B 1   ? 0.3248 0.3570 0.3147 -0.1162 -0.1009 0.0599  1   SER   B O   
3867 O O   B SER   B 1   ? 0.3461 0.3504 0.3435 -0.0278 -0.0212 0.0151  1   SER   B O   
3868 C CB  A SER   B 1   ? 0.3721 0.3636 0.3996 -0.1144 -0.0770 0.0221  1   SER   B CB  
3869 C CB  B SER   B 1   ? 0.3541 0.3543 0.3532 -0.0274 -0.0177 0.0084  1   SER   B CB  
3870 O OG  A SER   B 1   ? 0.3885 0.3725 0.4375 -0.1097 -0.0636 0.0147  1   SER   B OG  
3871 O OG  B SER   B 1   ? 0.3565 0.3561 0.3590 -0.0273 -0.0160 0.0067  1   SER   B OG  
3886 N N   A MET   B 2   ? 0.2928 0.3619 0.3542 -0.1174 -0.0912 0.0941  2   MET   B N   
3887 N N   B MET   B 2   ? 0.3363 0.3465 0.3514 -0.0288 -0.0198 0.0221  2   MET   B N   
3888 C CA  A MET   B 2   ? 0.2748 0.3625 0.3697 -0.0960 -0.0867 0.1152  2   MET   B CA  
3889 C CA  B MET   B 2   ? 0.3263 0.3409 0.3543 -0.0284 -0.0193 0.0276  2   MET   B CA  
3890 C C   A MET   B 2   ? 0.2382 0.3365 0.3356 -0.0775 -0.0917 0.1415  2   MET   B C   
3891 C C   B MET   B 2   ? 0.3030 0.3216 0.3212 -0.0319 -0.0210 0.0350  2   MET   B C   
3892 O O   A MET   B 2   ? 0.2305 0.3493 0.3364 -0.0593 -0.0995 0.1430  2   MET   B O   
3893 O O   B MET   B 2   ? 0.3047 0.3243 0.3209 -0.0309 -0.0191 0.0336  2   MET   B O   
3894 C CB  A MET   B 2   ? 0.3074 0.3963 0.4494 -0.0748 -0.0642 0.0959  2   MET   B CB  
3895 C CB  B MET   B 2   ? 0.3390 0.3539 0.3923 -0.0238 -0.0167 0.0252  2   MET   B CB  
3896 C CG  A MET   B 2   ? 0.3371 0.4281 0.5218 -0.0524 -0.0451 0.0849  2   MET   B CG  
3897 C CG  B MET   B 2   ? 0.3495 0.3648 0.4264 -0.0194 -0.0149 0.0244  2   MET   B CG  
3898 S SD  A MET   B 2   ? 0.3637 0.4559 0.5869 -0.0340 -0.0324 0.0737  2   MET   B SD  
3899 S SD  B MET   B 2   ? 0.3576 0.3737 0.4545 -0.0156 -0.0143 0.0240  2   MET   B SD  
3900 C CE  A MET   B 2   ? 0.3659 0.4609 0.5921 -0.0324 -0.0238 0.0724  2   MET   B CE  
3901 C CE  B MET   B 2   ? 0.3599 0.3761 0.4630 -0.0151 -0.0130 0.0229  2   MET   B CE  
3920 N N   A VAL   B 3   ? 0.2099 0.2931 0.3062 -0.0852 -0.0831 0.1565  3   VAL   B N   
3921 N N   B VAL   B 3   ? 0.2763 0.2980 0.2893 -0.0371 -0.0252 0.0442  3   VAL   B N   
3922 C CA  A VAL   B 3   ? 0.2065 0.2554 0.3002 -0.0755 -0.0653 0.1405  3   VAL   B CA  
3923 C CA  B VAL   B 3   ? 0.2495 0.2736 0.2608 -0.0416 -0.0300 0.0527  3   VAL   B CA  
3924 C C   A VAL   B 3   ? 0.1932 0.2428 0.2574 -0.0630 -0.0642 0.1179  3   VAL   B C   
3925 C C   B VAL   B 3   ? 0.2181 0.2489 0.2335 -0.0475 -0.0414 0.0678  3   VAL   B C   
3926 O O   A VAL   B 3   ? 0.1964 0.2546 0.2652 -0.0606 -0.0673 0.1259  3   VAL   B O   
3927 O O   B VAL   B 3   ? 0.2189 0.2517 0.2261 -0.0455 -0.0402 0.0682  3   VAL   B O   
3928 C CB  A VAL   B 3   ? 0.2272 0.2491 0.3480 -0.0689 -0.0590 0.1232  3   VAL   B CB  
3929 C CB  B VAL   B 3   ? 0.2538 0.2745 0.2639 -0.0407 -0.0252 0.0461  3   VAL   B CB  
3930 C CG1 A VAL   B 3   ? 0.2345 0.2417 0.3677 -0.0685 -0.0592 0.1174  3   VAL   B CG1 
3931 C CG1 B VAL   B 3   ? 0.2553 0.2744 0.2659 -0.0407 -0.0240 0.0433  3   VAL   B CG1 
3932 C CG2 A VAL   B 3   ? 0.2323 0.2544 0.3654 -0.0659 -0.0527 0.1236  3   VAL   B CG2 
3933 C CG2 B VAL   B 3   ? 0.2552 0.2754 0.2652 -0.0403 -0.0233 0.0449  3   VAL   B CG2 
3952 N N   . ASN   B 4   ? 0.1867 0.2206 0.2192 -0.0561 -0.0541 0.0838  4   ASN   B N   
3953 C CA  . ASN   B 4   ? 0.1834 0.2128 0.1857 -0.0559 -0.0423 0.0412  4   ASN   B CA  
3954 C C   . ASN   B 4   ? 0.1920 0.2233 0.1789 -0.0585 -0.0242 0.0294  4   ASN   B C   
3955 O O   . ASN   B 4   ? 0.1942 0.2310 0.2027 -0.0551 -0.0200 0.0114  4   ASN   B O   
3956 C CB  . ASN   B 4   ? 0.1797 0.2026 0.1719 -0.0468 -0.0444 0.0361  4   ASN   B CB  
3957 C CG  . ASN   B 4   ? 0.1768 0.1853 0.1655 -0.0439 -0.0396 0.0304  4   ASN   B CG  
3958 O OD1 . ASN   B 4   ? 0.1763 0.1708 0.1673 -0.0441 -0.0412 0.0260  4   ASN   B OD1 
3959 N ND2 . ASN   B 4   ? 0.1920 0.1899 0.1727 -0.0217 -0.0297 0.0261  4   ASN   B ND2 
3967 N N   . SER   B 5   ? 0.2098 0.2380 0.1789 -0.0553 -0.0075 0.0252  5   SER   B N   
3968 C CA  . SER   B 5   ? 0.2365 0.2687 0.2148 -0.0458 0.0130  0.0290  5   SER   B CA  
3969 C C   . SER   B 5   ? 0.2510 0.2741 0.2469 -0.0609 0.0415  0.0305  5   SER   B C   
3970 O O   . SER   B 5   ? 0.2647 0.2742 0.3144 -0.0557 0.0641  0.0323  5   SER   B O   
3971 C CB  . SER   B 5   ? 0.2460 0.2883 0.2389 -0.0378 0.0142  0.0401  5   SER   B CB  
3972 O OG  . SER   B 5   ? 0.2661 0.3123 0.2865 -0.0282 0.0115  0.0485  5   SER   B OG  
3978 N N   . PHE   B 6   ? 0.2665 0.2886 0.2225 -0.0665 0.0515  0.0261  6   PHE   B N   
3979 C CA  . PHE   B 6   ? 0.2718 0.2912 0.1934 -0.0838 0.0538  0.0114  6   PHE   B CA  
3980 C C   . PHE   B 6   ? 0.3187 0.3180 0.2335 -0.0889 0.0742  -0.0115 6   PHE   B C   
3981 O O   . PHE   B 6   ? 0.3328 0.3437 0.2677 -0.0809 0.0561  -0.0283 6   PHE   B O   
3982 C CB  . PHE   B 6   ? 0.2395 0.2720 0.1752 -0.0774 0.0234  0.0075  6   PHE   B CB  
3983 C CG  . PHE   B 6   ? 0.2090 0.2430 0.1597 -0.0678 0.0074  0.0048  6   PHE   B CG  
3984 C CD1 . PHE   B 6   ? 0.2075 0.2142 0.1421 -0.0585 -0.0027 0.0034  6   PHE   B CD1 
3985 C CD2 . PHE   B 6   ? 0.1878 0.2396 0.1587 -0.0558 0.0084  0.0292  6   PHE   B CD2 
3986 C CE1 . PHE   B 6   ? 0.2002 0.1937 0.1524 -0.0518 -0.0044 -0.0027 6   PHE   B CE1 
3987 C CE2 . PHE   B 6   ? 0.1892 0.2237 0.1832 -0.0432 0.0140  0.0235  6   PHE   B CE2 
3988 C CZ  . PHE   B 6   ? 0.1914 0.1989 0.1641 -0.0456 0.0105  0.0044  6   PHE   B CZ  
3998 N N   . SER   B 7   ? 0.3510 0.3049 0.2441 -0.1072 0.1022  -0.0307 7   SER   B N   
3999 C CA  . SER   B 7   ? 0.3823 0.3173 0.2903 -0.1052 0.1203  -0.0403 7   SER   B CA  
4000 C C   . SER   B 7   ? 0.3819 0.3002 0.2770 -0.1057 0.1344  -0.0537 7   SER   B C   
4001 O O   . SER   B 7   ? 0.3886 0.3026 0.3040 -0.1069 0.1326  -0.0529 7   SER   B O   
4002 C CB  . SER   B 7   ? 0.4040 0.3364 0.3530 -0.1016 0.1307  -0.0378 7   SER   B CB  
4003 O OG  . SER   B 7   ? 0.4187 0.3471 0.4029 -0.0971 0.1319  -0.0303 7   SER   B OG  
4009 N N   . GLY   B 8   ? 0.3791 0.2873 0.2834 -0.0917 0.1318  -0.0662 8   GLY   B N   
4010 C CA  . GLY   B 8   ? 0.3638 0.2696 0.2886 -0.0864 0.1301  -0.0711 8   GLY   B CA  
4011 C C   . GLY   B 8   ? 0.3427 0.2454 0.2824 -0.0832 0.1348  -0.0594 8   GLY   B C   
4012 O O   . GLY   B 8   ? 0.3526 0.2522 0.3154 -0.0719 0.1387  -0.0658 8   GLY   B O   
4016 N N   . TYR   B 9   ? 0.3237 0.2238 0.2524 -0.0728 0.1118  -0.0600 9   TYR   B N   
4017 C CA  . TYR   B 9   ? 0.3000 0.1973 0.2253 -0.0602 0.0841  -0.0450 9   TYR   B CA  
4018 C C   . TYR   B 9   ? 0.2926 0.2007 0.2095 -0.0529 0.0479  -0.0368 9   TYR   B C   
4019 O O   . TYR   B 9   ? 0.3072 0.2241 0.2443 -0.0517 0.0477  -0.0216 9   TYR   B O   
4020 C CB  . TYR   B 9   ? 0.2917 0.1782 0.2261 -0.0534 0.0833  -0.0365 9   TYR   B CB  
4021 C CG  . TYR   B 9   ? 0.2834 0.1622 0.2299 -0.0577 0.0750  -0.0437 9   TYR   B CG  
4022 C CD1 . TYR   B 9   ? 0.2864 0.1630 0.2486 -0.0736 0.0773  -0.0366 9   TYR   B CD1 
4023 C CD2 . TYR   B 9   ? 0.2694 0.1581 0.2238 -0.0505 0.0731  -0.0476 9   TYR   B CD2 
4024 C CE1 . TYR   B 9   ? 0.2804 0.1733 0.2568 -0.0776 0.0794  -0.0477 9   TYR   B CE1 
4025 C CE2 . TYR   B 9   ? 0.2686 0.1583 0.2370 -0.0501 0.0727  -0.0476 9   TYR   B CE2 
4026 C CZ  . TYR   B 9   ? 0.2722 0.1748 0.2518 -0.0664 0.0755  -0.0580 9   TYR   B CZ  
4027 O OH  . TYR   B 9   ? 0.2710 0.1891 0.2646 -0.0766 0.0714  -0.0720 9   TYR   B OH  
4037 N N   . LEU   B 10  ? 0.2687 0.1782 0.1848 -0.0489 0.0202  -0.0358 10  LEU   B N   
4038 C CA  . LEU   B 10  ? 0.2648 0.1758 0.1869 -0.0536 -0.0085 -0.0349 10  LEU   B CA  
4039 C C   . LEU   B 10  ? 0.2464 0.1780 0.1819 -0.0534 -0.0187 -0.0299 10  LEU   B C   
4040 O O   . LEU   B 10  ? 0.2310 0.1759 0.1837 -0.0459 -0.0130 -0.0248 10  LEU   B O   
4041 C CB  . LEU   B 10  ? 0.2805 0.1719 0.2050 -0.0558 -0.0276 -0.0201 10  LEU   B CB  
4042 C CG  . LEU   B 10  ? 0.2978 0.1801 0.2441 -0.0488 -0.0555 -0.0058 10  LEU   B CG  
4043 C CD1 . LEU   B 10  ? 0.3061 0.1932 0.2703 -0.0453 -0.0561 -0.0039 10  LEU   B CD1 
4044 C CD2 . LEU   B 10  ? 0.3086 0.1854 0.2737 -0.0502 -0.0518 0.0114  10  LEU   B CD2 
4056 N N   . LYS   B 11  ? 0.2589 0.2030 0.1851 -0.0472 -0.0245 -0.0248 11  LYS   B N   
4057 C CA  . LYS   B 11  ? 0.2760 0.2267 0.2119 -0.0386 -0.0344 -0.0299 11  LYS   B CA  
4058 C C   . LYS   B 11  ? 0.2595 0.2076 0.2167 -0.0587 -0.0301 -0.0419 11  LYS   B C   
4059 O O   . LYS   B 11  ? 0.2764 0.2247 0.2525 -0.0750 -0.0277 -0.0730 11  LYS   B O   
4060 C CB  . LYS   B 11  ? 0.3092 0.2743 0.2680 -0.0132 -0.0373 -0.0231 11  LYS   B CB  
4061 C CG  . LYS   B 11  ? 0.3383 0.3058 0.3343 0.0024  -0.0374 -0.0214 11  LYS   B CG  
4062 C CD  . LYS   B 11  ? 0.3608 0.3284 0.3954 0.0120  -0.0354 -0.0242 11  LYS   B CD  
4063 C CE  . LYS   B 11  ? 0.3779 0.3437 0.4437 0.0138  -0.0341 -0.0241 11  LYS   B CE  
4064 N NZ  . LYS   B 11  ? 0.3887 0.3534 0.4706 0.0139  -0.0339 -0.0220 11  LYS   B NZ  
4078 N N   . LEU   B 12  ? 0.2263 0.1814 0.2157 -0.0506 -0.0231 -0.0429 12  LEU   B N   
4079 C CA  . LEU   B 12  ? 0.2120 0.1682 0.2317 -0.0458 -0.0223 -0.0351 12  LEU   B CA  
4080 C C   . LEU   B 12  ? 0.2020 0.1678 0.2419 -0.0461 -0.0348 -0.0309 12  LEU   B C   
4081 O O   . LEU   B 12  ? 0.2023 0.1678 0.2609 -0.0549 -0.0436 -0.0233 12  LEU   B O   
4082 C CB  . LEU   B 12  ? 0.2109 0.1491 0.2334 -0.0341 -0.0151 -0.0329 12  LEU   B CB  
4083 C CG  . LEU   B 12  ? 0.2131 0.1460 0.2453 -0.0347 -0.0099 -0.0236 12  LEU   B CG  
4084 C CD1 . LEU   B 12  ? 0.2214 0.1463 0.2388 -0.0209 -0.0132 -0.0124 12  LEU   B CD1 
4085 C CD2 . LEU   B 12  ? 0.2200 0.1504 0.2659 -0.0365 -0.0011 -0.0357 12  LEU   B CD2 
4097 N N   . THR   B 13  ? 0.1939 0.1725 0.2462 -0.0432 -0.0405 -0.0374 13  THR   B N   
4098 C CA  . THR   B 13  ? 0.1916 0.1782 0.2431 -0.0520 -0.0448 -0.0299 13  THR   B CA  
4099 C C   . THR   B 13  ? 0.2289 0.1921 0.2525 -0.0620 -0.0538 -0.0265 13  THR   B C   
4100 O O   . THR   B 13  ? 0.2469 0.1962 0.2677 -0.0609 -0.0217 -0.0283 13  THR   B O   
4101 C CB  . THR   B 13  ? 0.1755 0.1784 0.2453 -0.0475 -0.0426 -0.0215 13  THR   B CB  
4102 O OG1 . THR   B 13  ? 0.1696 0.1749 0.2510 -0.0406 -0.0266 -0.0221 13  THR   B OG1 
4103 C CG2 . THR   B 13  ? 0.1888 0.1840 0.2528 -0.0395 -0.0292 -0.0113 13  THR   B CG2 
4111 N N   . ASP   B 14  ? 0.2491 0.2057 0.2704 -0.0640 -0.0890 -0.0110 14  ASP   B N   
4112 C CA  . ASP   B 14  ? 0.2639 0.2279 0.2987 -0.0658 -0.1028 0.0093  14  ASP   B CA  
4113 C C   . ASP   B 14  ? 0.2509 0.2109 0.2615 -0.0663 -0.0813 0.0151  14  ASP   B C   
4114 O O   . ASP   B 14  ? 0.2811 0.2311 0.2659 -0.0749 -0.0813 0.0271  14  ASP   B O   
4115 C CB  . ASP   B 14  ? 0.2923 0.2753 0.3769 -0.0573 -0.1212 0.0157  14  ASP   B CB  
4116 C CG  . ASP   B 14  ? 0.3235 0.3151 0.4544 -0.0474 -0.1183 0.0098  14  ASP   B CG  
4117 O OD1 . ASP   B 14  ? 0.3436 0.3321 0.4749 -0.0474 -0.1144 -0.0034 14  ASP   B OD1 
4118 O OD2 . ASP   B 14  ? 0.3295 0.3351 0.4896 -0.0454 -0.1196 0.0122  14  ASP   B OD2 
4123 N N   . ASN   B 15  ? 0.2073 0.1791 0.2285 -0.0476 -0.0710 0.0086  15  ASN   B N   
4124 C CA  . ASN   B 15  ? 0.1707 0.1592 0.2145 -0.0323 -0.0410 0.0012  15  ASN   B CA  
4125 C C   . ASN   B 15  ? 0.1553 0.1442 0.2043 -0.0180 -0.0339 -0.0076 15  ASN   B C   
4126 O O   . ASN   B 15  ? 0.1530 0.1390 0.2253 -0.0212 -0.0397 -0.0163 15  ASN   B O   
4127 C CB  . ASN   B 15  ? 0.1609 0.1562 0.2264 -0.0159 -0.0398 -0.0001 15  ASN   B CB  
4128 C CG  . ASN   B 15  ? 0.1495 0.1599 0.2320 -0.0185 -0.0175 -0.0015 15  ASN   B CG  
4129 O OD1 . ASN   B 15  ? 0.1564 0.1836 0.2566 -0.0363 -0.0255 0.0063  15  ASN   B OD1 
4130 N ND2 . ASN   B 15  ? 0.1508 0.1367 0.2225 -0.0105 0.0038  -0.0129 15  ASN   B ND2 
4137 N N   . VAL   B 16  ? 0.1601 0.1348 0.2044 -0.0272 -0.0387 -0.0029 16  VAL   B N   
4138 C CA  . VAL   B 16  ? 0.1586 0.1344 0.1875 -0.0270 -0.0268 -0.0232 16  VAL   B CA  
4139 C C   . VAL   B 16  ? 0.1561 0.1449 0.1844 -0.0325 -0.0334 -0.0147 16  VAL   B C   
4140 O O   . VAL   B 16  ? 0.1624 0.1591 0.2015 -0.0275 -0.0219 -0.0230 16  VAL   B O   
4141 C CB  . VAL   B 16  ? 0.1654 0.1355 0.2005 -0.0116 -0.0160 -0.0214 16  VAL   B CB  
4142 C CG1 . VAL   B 16  ? 0.1759 0.1347 0.1980 0.0057  -0.0100 -0.0149 16  VAL   B CG1 
4143 C CG2 . VAL   B 16  ? 0.1688 0.1419 0.2285 -0.0059 -0.0113 -0.0200 16  VAL   B CG2 
4153 N N   . TYR   B 17  ? 0.1622 0.1534 0.1865 -0.0313 -0.0225 -0.0216 17  TYR   B N   
4154 C CA  . TYR   B 17  ? 0.1698 0.1673 0.1803 -0.0304 -0.0195 -0.0084 17  TYR   B CA  
4155 C C   . TYR   B 17  ? 0.1647 0.1447 0.1756 -0.0336 -0.0118 -0.0167 17  TYR   B C   
4156 O O   . TYR   B 17  ? 0.1605 0.1492 0.1854 -0.0278 -0.0238 -0.0306 17  TYR   B O   
4157 C CB  . TYR   B 17  ? 0.1976 0.2063 0.2004 -0.0164 -0.0147 0.0269  17  TYR   B CB  
4158 C CG  . TYR   B 17  ? 0.2255 0.2499 0.2366 -0.0088 -0.0254 0.0291  17  TYR   B CG  
4159 C CD1 . TYR   B 17  ? 0.2413 0.2658 0.2536 -0.0041 -0.0357 0.0375  17  TYR   B CD1 
4160 C CD2 . TYR   B 17  ? 0.2457 0.2787 0.2561 0.0016  -0.0314 0.0242  17  TYR   B CD2 
4161 C CE1 . TYR   B 17  ? 0.2583 0.2919 0.2697 0.0020  -0.0448 0.0320  17  TYR   B CE1 
4162 C CE2 . TYR   B 17  ? 0.2605 0.3008 0.2779 0.0091  -0.0455 0.0284  17  TYR   B CE2 
4163 C CZ  . TYR   B 17  ? 0.2697 0.3070 0.2818 0.0102  -0.0540 0.0307  17  TYR   B CZ  
4164 O OH  . TYR   B 17  ? 0.2856 0.3245 0.3020 0.0174  -0.0655 0.0297  17  TYR   B OH  
4174 N N   . ILE   B 18  ? 0.1741 0.1433 0.1724 -0.0291 -0.0031 -0.0194 18  ILE   B N   
4175 C CA  . ILE   B 18  ? 0.1778 0.1395 0.1687 -0.0284 -0.0052 -0.0185 18  ILE   B CA  
4176 C C   . ILE   B 18  ? 0.1900 0.1437 0.1640 -0.0371 -0.0038 -0.0314 18  ILE   B C   
4177 O O   . ILE   B 18  ? 0.2114 0.1580 0.1783 -0.0307 0.0077  -0.0400 18  ILE   B O   
4178 C CB  . ILE   B 18  ? 0.1823 0.1411 0.1887 -0.0369 -0.0057 -0.0126 18  ILE   B CB  
4179 C CG1 . ILE   B 18  ? 0.1829 0.1434 0.1943 -0.0371 -0.0025 -0.0023 18  ILE   B CG1 
4180 C CG2 . ILE   B 18  ? 0.1855 0.1489 0.1928 -0.0385 -0.0036 -0.0136 18  ILE   B CG2 
4181 C CD1 . ILE   B 18  ? 0.1894 0.1719 0.2195 -0.0344 -0.0199 0.0162  18  ILE   B CD1 
4193 N N   . LYS   B 19  ? 0.1898 0.1464 0.1828 -0.0231 0.0266  -0.0374 19  LYS   B N   
4194 C CA  . LYS   B 19  ? 0.1983 0.1486 0.1974 -0.0244 0.0255  -0.0375 19  LYS   B CA  
4195 C C   . LYS   B 19  ? 0.1806 0.1485 0.2055 -0.0211 0.0289  -0.0429 19  LYS   B C   
4196 O O   . LYS   B 19  ? 0.1786 0.1521 0.1945 -0.0163 0.0227  -0.0367 19  LYS   B O   
4197 C CB  . LYS   B 19  ? 0.2211 0.1672 0.2074 -0.0298 0.0379  -0.0179 19  LYS   B CB  
4198 C CG  . LYS   B 19  ? 0.2435 0.1926 0.2279 -0.0347 0.0497  -0.0203 19  LYS   B CG  
4199 C CD  . LYS   B 19  ? 0.2686 0.2257 0.2426 -0.0402 0.0526  -0.0185 19  LYS   B CD  
4200 C CE  . LYS   B 19  ? 0.2927 0.2516 0.2647 -0.0437 0.0482  -0.0215 19  LYS   B CE  
4201 N NZ  . LYS   B 19  ? 0.3094 0.2665 0.2730 -0.0508 0.0509  -0.0188 19  LYS   B NZ  
4215 N N   . ASN   B 20  ? 0.1791 0.1615 0.2345 -0.0151 0.0323  -0.0536 20  ASN   B N   
4216 C CA  . ASN   B 20  ? 0.1809 0.1725 0.2567 -0.0089 0.0358  -0.0665 20  ASN   B CA  
4217 C C   . ASN   B 20  ? 0.1800 0.1895 0.2629 -0.0169 0.0450  -0.0754 20  ASN   B C   
4218 O O   . ASN   B 20  ? 0.1987 0.2223 0.2815 -0.0279 0.0476  -0.0735 20  ASN   B O   
4219 C CB  . ASN   B 20  ? 0.2095 0.1765 0.2830 0.0095  0.0280  -0.0647 20  ASN   B CB  
4220 C CG  . ASN   B 20  ? 0.2344 0.1809 0.3024 0.0329  0.0241  -0.0670 20  ASN   B CG  
4221 O OD1 . ASN   B 20  ? 0.2586 0.2073 0.3305 0.0507  0.0237  -0.0697 20  ASN   B OD1 
4222 N ND2 . ASN   B 20  ? 0.2282 0.1769 0.2925 0.0312  0.0154  -0.0669 20  ASN   B ND2 
4229 N N   . ALA   B 21  ? 0.1810 0.1754 0.2624 -0.0221 0.0492  -0.0657 21  ALA   B N   
4230 C CA  . ALA   B 21  ? 0.1884 0.1812 0.2748 -0.0285 0.0359  -0.0501 21  ALA   B CA  
4231 C C   . ALA   B 21  ? 0.1869 0.1589 0.2720 -0.0202 0.0375  -0.0354 21  ALA   B C   
4232 O O   . ALA   B 21  ? 0.1898 0.1507 0.2694 -0.0298 0.0371  -0.0294 21  ALA   B O   
4233 C CB  . ALA   B 21  ? 0.2037 0.2053 0.2865 -0.0412 0.0309  -0.0329 21  ALA   B CB  
4239 N N   . ASP   B 22  ? 0.1773 0.1516 0.2618 -0.0209 0.0320  -0.0329 22  ASP   B N   
4240 C CA  . ASP   B 22  ? 0.1738 0.1430 0.2472 -0.0114 0.0283  -0.0278 22  ASP   B CA  
4241 C C   . ASP   B 22  ? 0.1691 0.1416 0.2050 -0.0143 0.0213  -0.0127 22  ASP   B C   
4242 O O   . ASP   B 22  ? 0.1742 0.1440 0.2085 -0.0101 0.0099  -0.0071 22  ASP   B O   
4243 C CB  . ASP   B 22  ? 0.1841 0.1517 0.2958 -0.0058 0.0241  -0.0142 22  ASP   B CB  
4244 C CG  . ASP   B 22  ? 0.1917 0.1662 0.3318 0.0013  -0.0051 -0.0110 22  ASP   B CG  
4245 O OD1 . ASP   B 22  ? 0.2027 0.1594 0.3294 0.0060  -0.0212 -0.0104 22  ASP   B OD1 
4246 O OD2 . ASP   B 22  ? 0.1994 0.1955 0.3739 0.0097  -0.0198 -0.0209 22  ASP   B OD2 
4251 N N   . ILE   B 23  ? 0.1722 0.1364 0.1794 -0.0098 0.0079  0.0067  23  ILE   B N   
4252 C CA  . ILE   B 23  ? 0.1654 0.1368 0.1631 -0.0080 0.0016  0.0008  23  ILE   B CA  
4253 C C   . ILE   B 23  ? 0.1525 0.1373 0.1678 -0.0028 -0.0023 0.0002  23  ILE   B C   
4254 O O   . ILE   B 23  ? 0.1485 0.1400 0.1591 -0.0098 -0.0006 0.0048  23  ILE   B O   
4255 C CB  . ILE   B 23  ? 0.1647 0.1399 0.1823 -0.0166 0.0047  0.0134  23  ILE   B CB  
4256 C CG1 . ILE   B 23  ? 0.1641 0.1495 0.1888 -0.0145 0.0054  0.0283  23  ILE   B CG1 
4257 C CG2 . ILE   B 23  ? 0.1708 0.1587 0.1932 -0.0152 -0.0000 0.0044  23  ILE   B CG2 
4258 C CD1 . ILE   B 23  ? 0.1693 0.1669 0.2050 -0.0104 0.0058  0.0255  23  ILE   B CD1 
4270 N N   . VAL   B 24  ? 0.1542 0.1383 0.1801 -0.0068 0.0008  -0.0010 24  VAL   B N   
4271 C CA  . VAL   B 24  ? 0.1497 0.1414 0.2009 -0.0021 -0.0102 -0.0069 24  VAL   B CA  
4272 C C   . VAL   B 24  ? 0.1497 0.1460 0.2091 -0.0125 -0.0068 -0.0019 24  VAL   B C   
4273 O O   . VAL   B 24  ? 0.1477 0.1523 0.2231 -0.0147 -0.0042 0.0124  24  VAL   B O   
4274 C CB  . VAL   B 24  ? 0.1595 0.1604 0.2132 0.0051  -0.0177 -0.0059 24  VAL   B CB  
4275 C CG1 . VAL   B 24  ? 0.1602 0.1637 0.2348 -0.0066 -0.0179 0.0007  24  VAL   B CG1 
4276 C CG2 . VAL   B 24  ? 0.1684 0.1848 0.2154 0.0099  -0.0188 -0.0106 24  VAL   B CG2 
4286 N N   . GLU   B 25  ? 0.1713 0.1564 0.2123 -0.0107 0.0058  0.0033  25  GLU   B N   
4287 C CA  . GLU   B 25  ? 0.1816 0.1830 0.2360 0.0017  0.0204  -0.0066 25  GLU   B CA  
4288 C C   . GLU   B 25  ? 0.1761 0.1755 0.2066 -0.0072 0.0197  -0.0009 25  GLU   B C   
4289 O O   . GLU   B 25  ? 0.1794 0.1903 0.2195 -0.0052 0.0284  0.0037  25  GLU   B O   
4290 C CB  . GLU   B 25  ? 0.2155 0.2224 0.2930 0.0256  0.0346  -0.0128 25  GLU   B CB  
4291 C CG  . GLU   B 25  ? 0.2526 0.2817 0.3875 0.0310  0.0304  -0.0168 25  GLU   B CG  
4292 C CD  . GLU   B 25  ? 0.2942 0.3336 0.4658 0.0261  0.0270  -0.0223 25  GLU   B CD  
4293 O OE1 . GLU   B 25  ? 0.3050 0.3540 0.4930 0.0296  0.0340  -0.0221 25  GLU   B OE1 
4294 O OE2 . GLU   B 25  ? 0.3039 0.3514 0.4985 0.0242  0.0202  -0.0287 25  GLU   B OE2 
4301 N N   . GLU   B 26  ? 0.1755 0.1645 0.1799 -0.0212 0.0100  -0.0001 26  GLU   B N   
4302 C CA  . GLU   B 26  ? 0.1726 0.1772 0.1907 -0.0330 -0.0009 0.0010  26  GLU   B CA  
4303 C C   . GLU   B 26  ? 0.1569 0.1742 0.1781 -0.0226 0.0100  0.0154  26  GLU   B C   
4304 O O   . GLU   B 26  ? 0.1758 0.1953 0.1846 -0.0200 0.0036  0.0252  26  GLU   B O   
4305 C CB  . GLU   B 26  ? 0.2045 0.2009 0.2173 -0.0472 0.0013  0.0079  26  GLU   B CB  
4306 C CG  . GLU   B 26  ? 0.2445 0.2348 0.2670 -0.0497 0.0140  -0.0089 26  GLU   B CG  
4307 C CD  . GLU   B 26  ? 0.2702 0.2560 0.2807 -0.0666 0.0290  -0.0355 26  GLU   B CD  
4308 O OE1 . GLU   B 26  ? 0.2923 0.2394 0.2785 -0.0793 0.0661  -0.0298 26  GLU   B OE1 
4309 O OE2 . GLU   B 26  ? 0.2672 0.2924 0.3175 -0.0575 0.0270  -0.0261 26  GLU   B OE2 
4316 N N   . ALA   B 27  ? 0.1423 0.1571 0.1783 -0.0190 0.0147  0.0141  27  ALA   B N   
4317 C CA  . ALA   B 27  ? 0.1497 0.1542 0.1978 -0.0078 0.0071  0.0302  27  ALA   B CA  
4318 C C   . ALA   B 27  ? 0.1493 0.1675 0.2127 -0.0092 0.0169  0.0392  27  ALA   B C   
4319 O O   . ALA   B 27  ? 0.1585 0.1738 0.2199 -0.0030 0.0148  0.0446  27  ALA   B O   
4320 C CB  . ALA   B 27  ? 0.1680 0.1397 0.2007 -0.0140 0.0058  0.0246  27  ALA   B CB  
4326 N N   . LYS   B 28  ? 0.1430 0.1868 0.2539 -0.0150 0.0256  0.0582  28  LYS   B N   
4327 C CA  . LYS   B 28  ? 0.1611 0.2278 0.2802 -0.0085 0.0541  0.0870  28  LYS   B CA  
4328 C C   . LYS   B 28  ? 0.1834 0.2425 0.2660 0.0026  0.0671  0.0795  28  LYS   B C   
4329 O O   . LYS   B 28  ? 0.2103 0.2474 0.2796 0.0003  0.0653  0.0767  28  LYS   B O   
4330 C CB  . LYS   B 28  ? 0.1785 0.2665 0.3311 0.0071  0.0697  0.1094  28  LYS   B CB  
4331 C CG  . LYS   B 28  ? 0.1989 0.3110 0.3737 0.0179  0.0716  0.1243  28  LYS   B CG  
4332 C CD  . LYS   B 28  ? 0.2388 0.3669 0.4240 0.0281  0.0833  0.1278  28  LYS   B CD  
4333 C CE  . LYS   B 28  ? 0.2697 0.4040 0.4645 0.0380  0.0880  0.1326  28  LYS   B CE  
4334 N NZ  . LYS   B 28  ? 0.2732 0.4117 0.4847 0.0459  0.0889  0.1387  28  LYS   B NZ  
4348 N N   . LYS   B 29  ? 0.2023 0.2646 0.2628 0.0242  0.0664  0.0685  29  LYS   B N   
4349 C CA  . LYS   B 29  ? 0.2411 0.2928 0.2853 0.0258  0.0650  0.0650  29  LYS   B CA  
4350 C C   . LYS   B 29  ? 0.2364 0.2932 0.2513 0.0256  0.0541  0.0726  29  LYS   B C   
4351 O O   . LYS   B 29  ? 0.2565 0.3112 0.2611 0.0297  0.0475  0.0729  29  LYS   B O   
4352 C CB  . LYS   B 29  ? 0.2954 0.3264 0.3634 0.0235  0.0605  0.0526  29  LYS   B CB  
4353 C CG  . LYS   B 29  ? 0.3398 0.3536 0.4407 0.0187  0.0618  0.0505  29  LYS   B CG  
4354 C CD  . LYS   B 29  ? 0.3748 0.3729 0.5036 0.0116  0.0684  0.0440  29  LYS   B CD  
4355 C CE  . LYS   B 29  ? 0.3985 0.3854 0.5468 0.0063  0.0753  0.0391  29  LYS   B CE  
4356 N NZ  . LYS   B 29  ? 0.4101 0.3929 0.5730 0.0042  0.0774  0.0364  29  LYS   B NZ  
4370 N N   . VAL   B 30  ? 0.2079 0.2759 0.2362 0.0146  0.0485  0.0738  30  VAL   B N   
4371 C CA  . VAL   B 30  ? 0.1972 0.2665 0.2718 0.0025  0.0135  0.0759  30  VAL   B CA  
4372 C C   . VAL   B 30  ? 0.1753 0.2578 0.2666 -0.0015 0.0167  0.0929  30  VAL   B C   
4373 O O   . VAL   B 30  ? 0.1870 0.2751 0.2660 0.0026  0.0206  0.1025  30  VAL   B O   
4374 C CB  . VAL   B 30  ? 0.2076 0.2645 0.3120 -0.0140 -0.0150 0.0680  30  VAL   B CB  
4375 C CG1 . VAL   B 30  ? 0.2069 0.2689 0.3091 -0.0188 -0.0087 0.0615  30  VAL   B CG1 
4376 C CG2 . VAL   B 30  ? 0.2204 0.2641 0.3309 -0.0199 -0.0275 0.0587  30  VAL   B CG2 
4386 N N   . LYS   B 31  ? 0.1638 0.2212 0.2994 -0.0156 0.0126  0.1029  31  LYS   B N   
4387 C CA  . LYS   B 31  ? 0.1587 0.2161 0.3284 -0.0307 0.0083  0.1038  31  LYS   B CA  
4388 C C   . LYS   B 31  ? 0.1514 0.1803 0.2848 -0.0295 -0.0096 0.0803  31  LYS   B C   
4389 O O   . LYS   B 31  ? 0.1621 0.1943 0.3006 -0.0272 -0.0112 0.0966  31  LYS   B O   
4390 C CB  . LYS   B 31  ? 0.1761 0.2630 0.3811 -0.0285 0.0291  0.1177  31  LYS   B CB  
4391 C CG  . LYS   B 31  ? 0.2077 0.3124 0.4203 -0.0276 0.0421  0.1174  31  LYS   B CG  
4392 C CD  . LYS   B 31  ? 0.2430 0.3589 0.4565 -0.0215 0.0374  0.1083  31  LYS   B CD  
4393 C CE  . LYS   B 31  ? 0.2682 0.3887 0.4919 -0.0175 0.0267  0.0983  31  LYS   B CE  
4394 N NZ  . LYS   B 31  ? 0.2789 0.4040 0.5069 -0.0108 0.0165  0.0874  31  LYS   B NZ  
4408 N N   . PRO   B 32  ? 0.1558 0.1498 0.2149 -0.0290 -0.0334 0.0437  32  PRO   B N   
4409 C CA  . PRO   B 32  ? 0.1648 0.1458 0.1716 -0.0291 -0.0339 0.0314  32  PRO   B CA  
4410 C C   . PRO   B 32  ? 0.1737 0.1344 0.1835 -0.0321 -0.0483 0.0348  32  PRO   B C   
4411 O O   . PRO   B 32  ? 0.1890 0.1406 0.2128 -0.0366 -0.0638 0.0330  32  PRO   B O   
4412 C CB  . PRO   B 32  ? 0.1808 0.1419 0.1677 -0.0297 -0.0273 0.0123  32  PRO   B CB  
4413 C CG  . PRO   B 32  ? 0.1955 0.1306 0.1732 -0.0257 -0.0440 0.0180  32  PRO   B CG  
4414 C CD  . PRO   B 32  ? 0.1806 0.1341 0.2001 -0.0179 -0.0461 0.0269  32  PRO   B CD  
4422 N N   . THR   B 33  ? 0.1772 0.1321 0.1689 -0.0242 -0.0420 0.0224  33  THR   B N   
4423 C CA  . THR   B 33  ? 0.1858 0.1363 0.1593 -0.0286 -0.0403 0.0211  33  THR   B CA  
4424 C C   . THR   B 33  ? 0.1854 0.1277 0.1492 -0.0263 -0.0402 0.0140  33  THR   B C   
4425 O O   . THR   B 33  ? 0.2066 0.1320 0.1551 -0.0403 -0.0448 0.0159  33  THR   B O   
4426 C CB  . THR   B 33  ? 0.1937 0.1455 0.1669 -0.0136 -0.0463 0.0263  33  THR   B CB  
4427 O OG1 . THR   B 33  ? 0.1844 0.1546 0.1734 -0.0200 -0.0419 0.0318  33  THR   B OG1 
4428 C CG2 . THR   B 33  ? 0.2164 0.1553 0.1823 -0.0049 -0.0433 0.0224  33  THR   B CG2 
4436 N N   . VAL   B 34  ? 0.1699 0.1245 0.1460 -0.0314 -0.0386 0.0127  34  VAL   B N   
4437 C CA  . VAL   B 34  ? 0.1555 0.1228 0.1394 -0.0251 -0.0304 0.0097  34  VAL   B CA  
4438 C C   . VAL   B 34  ? 0.1431 0.1193 0.1239 -0.0277 -0.0170 0.0030  34  VAL   B C   
4439 O O   . VAL   B 34  ? 0.1581 0.1244 0.1305 -0.0271 -0.0268 0.0068  34  VAL   B O   
4440 C CB  . VAL   B 34  ? 0.1627 0.1281 0.1631 -0.0091 -0.0286 -0.0017 34  VAL   B CB  
4441 C CG1 . VAL   B 34  ? 0.1639 0.1461 0.1623 -0.0084 -0.0175 -0.0075 34  VAL   B CG1 
4442 C CG2 . VAL   B 34  ? 0.1709 0.1355 0.1855 -0.0065 -0.0243 -0.0040 34  VAL   B CG2 
4452 N N   . VAL   B 35  ? 0.1399 0.1159 0.1235 -0.0229 -0.0154 0.0055  35  VAL   B N   
4453 C CA  . VAL   B 35  ? 0.1350 0.1150 0.1257 -0.0201 -0.0075 0.0033  35  VAL   B CA  
4454 C C   . VAL   B 35  ? 0.1226 0.1140 0.1232 -0.0190 -0.0096 0.0026  35  VAL   B C   
4455 O O   . VAL   B 35  ? 0.1292 0.1172 0.1339 -0.0210 -0.0003 -0.0050 35  VAL   B O   
4456 C CB  . VAL   B 35  ? 0.1321 0.1366 0.1298 -0.0178 0.0037  0.0058  35  VAL   B CB  
4457 C CG1 . VAL   B 35  ? 0.1250 0.1489 0.1448 -0.0225 0.0035  0.0018  35  VAL   B CG1 
4458 C CG2 . VAL   B 35  ? 0.1349 0.1356 0.1515 -0.0063 0.0056  -0.0001 35  VAL   B CG2 
4468 N N   . VAL   B 36  ? 0.1262 0.1173 0.1165 -0.0142 -0.0099 0.0041  36  VAL   B N   
4469 C CA  . VAL   B 36  ? 0.1231 0.1116 0.1119 -0.0106 -0.0056 -0.0014 36  VAL   B CA  
4470 C C   . VAL   B 36  ? 0.1168 0.1103 0.1146 -0.0109 -0.0012 0.0022  36  VAL   B C   
4471 O O   . VAL   B 36  ? 0.1259 0.1207 0.1407 -0.0100 0.0015  -0.0050 36  VAL   B O   
4472 C CB  . VAL   B 36  ? 0.1227 0.1160 0.1276 -0.0127 -0.0026 0.0017  36  VAL   B CB  
4473 C CG1 . VAL   B 36  ? 0.1204 0.1257 0.1489 -0.0158 -0.0029 0.0037  36  VAL   B CG1 
4474 C CG2 . VAL   B 36  ? 0.1296 0.1162 0.1432 -0.0125 -0.0119 0.0026  36  VAL   B CG2 
4484 N N   . ASN   B 37  ? 0.1233 0.1170 0.1142 -0.0011 -0.0065 0.0037  37  ASN   B N   
4485 C CA  . ASN   B 37  ? 0.1215 0.1189 0.1247 0.0034  -0.0085 0.0058  37  ASN   B CA  
4486 C C   . ASN   B 37  ? 0.1204 0.1178 0.1244 0.0044  -0.0060 -0.0025 37  ASN   B C   
4487 O O   . ASN   B 37  ? 0.1303 0.1253 0.1271 0.0024  0.0033  0.0078  37  ASN   B O   
4488 C CB  . ASN   B 37  ? 0.1240 0.1260 0.1229 0.0020  -0.0131 0.0027  37  ASN   B CB  
4489 C CG  . ASN   B 37  ? 0.1287 0.1222 0.1293 -0.0001 -0.0096 0.0027  37  ASN   B CG  
4490 O OD1 . ASN   B 37  ? 0.1344 0.1282 0.1412 0.0072  -0.0103 0.0012  37  ASN   B OD1 
4491 N ND2 . ASN   B 37  ? 0.1339 0.1221 0.1323 0.0020  -0.0170 0.0076  37  ASN   B ND2 
4498 N N   . ALA   B 38  ? 0.1309 0.1149 0.1244 0.0099  0.0030  -0.0002 38  ALA   B N   
4499 C CA  . ALA   B 38  ? 0.1400 0.1191 0.1251 0.0031  0.0074  0.0033  38  ALA   B CA  
4500 C C   . ALA   B 38  ? 0.1370 0.1171 0.1340 0.0013  0.0090  0.0066  38  ALA   B C   
4501 O O   . ALA   B 38  ? 0.1469 0.1274 0.1434 0.0074  0.0037  0.0073  38  ALA   B O   
4502 C CB  . ALA   B 38  ? 0.1604 0.1302 0.1435 -0.0095 0.0073  0.0068  38  ALA   B CB  
4508 N N   . ALA   B 39  ? 0.1372 0.1211 0.1251 0.0069  0.0034  -0.0003 39  ALA   B N   
4509 C CA  . ALA   B 39  ? 0.1493 0.1280 0.1213 0.0037  -0.0022 0.0029  39  ALA   B CA  
4510 C C   . ALA   B 39  ? 0.1450 0.1345 0.1073 0.0077  -0.0046 -0.0050 39  ALA   B C   
4511 O O   . ALA   B 39  ? 0.1468 0.1402 0.1395 -0.0004 -0.0003 0.0065  39  ALA   B O   
4512 C CB  . ALA   B 39  ? 0.1495 0.1357 0.1404 -0.0047 0.0000  -0.0035 39  ALA   B CB  
4518 N N   . ASN   B 40  ? 0.1483 0.1552 0.1158 -0.0033 0.0037  -0.0080 40  ASN   B N   
4519 C CA  . ASN   B 40  ? 0.1539 0.1610 0.1293 -0.0009 0.0027  -0.0061 40  ASN   B CA  
4520 C C   . ASN   B 40  ? 0.1575 0.1594 0.1098 0.0030  -0.0032 -0.0013 40  ASN   B C   
4521 O O   . ASN   B 40  ? 0.1595 0.1511 0.1220 0.0035  -0.0082 0.0018  40  ASN   B O   
4522 C CB  . ASN   B 40  ? 0.1690 0.1616 0.1512 0.0061  -0.0095 0.0094  40  ASN   B CB  
4523 C CG  . ASN   B 40  ? 0.1752 0.1642 0.1785 0.0037  -0.0231 0.0111  40  ASN   B CG  
4524 O OD1 . ASN   B 40  ? 0.1735 0.1624 0.2508 0.0002  -0.0363 0.0117  40  ASN   B OD1 
4525 N ND2 . ASN   B 40  ? 0.1791 0.1655 0.1812 0.0033  -0.0166 0.0137  40  ASN   B ND2 
4532 N N   . VAL   B 41  ? 0.1667 0.1666 0.1143 0.0089  0.0057  -0.0014 41  VAL   B N   
4533 C CA  . VAL   B 41  ? 0.1744 0.1794 0.1219 0.0093  0.0024  -0.0151 41  VAL   B CA  
4534 C C   . VAL   B 41  ? 0.1713 0.1758 0.1203 0.0194  -0.0024 -0.0147 41  VAL   B C   
4535 O O   . VAL   B 41  ? 0.1728 0.1714 0.1309 0.0169  -0.0115 -0.0206 41  VAL   B O   
4536 C CB  . VAL   B 41  ? 0.1888 0.1955 0.1488 -0.0042 0.0216  -0.0220 41  VAL   B CB  
4537 C CG1 . VAL   B 41  ? 0.1838 0.2011 0.1656 -0.0078 0.0354  -0.0250 41  VAL   B CG1 
4538 C CG2 . VAL   B 41  ? 0.1996 0.2140 0.1624 -0.0108 0.0264  -0.0223 41  VAL   B CG2 
4548 N N   . TYR   B 42  ? 0.1776 0.1765 0.1309 0.0205  -0.0153 -0.0001 42  TYR   B N   
4549 C CA  . TYR   B 42  ? 0.1851 0.1826 0.1448 0.0186  -0.0217 -0.0126 42  TYR   B CA  
4550 C C   . TYR   B 42  ? 0.1663 0.1599 0.1457 0.0200  -0.0185 -0.0189 42  TYR   B C   
4551 O O   . TYR   B 42  ? 0.1690 0.1673 0.1767 0.0134  -0.0266 -0.0239 42  TYR   B O   
4552 C CB  . TYR   B 42  ? 0.2080 0.2144 0.1614 0.0143  -0.0274 0.0015  42  TYR   B CB  
4553 C CG  . TYR   B 42  ? 0.2114 0.2336 0.1521 0.0063  -0.0274 0.0132  42  TYR   B CG  
4554 C CD1 . TYR   B 42  ? 0.2064 0.2396 0.1258 -0.0016 -0.0141 -0.0005 42  TYR   B CD1 
4555 C CD2 . TYR   B 42  ? 0.2252 0.2487 0.1937 0.0060  -0.0115 0.0201  42  TYR   B CD2 
4556 C CE1 . TYR   B 42  ? 0.2192 0.2558 0.1442 0.0035  -0.0047 0.0038  42  TYR   B CE1 
4557 C CE2 . TYR   B 42  ? 0.2273 0.2599 0.1893 0.0093  0.0081  0.0312  42  TYR   B CE2 
4558 C CZ  . TYR   B 42  ? 0.2369 0.2699 0.1753 0.0179  0.0153  0.0164  42  TYR   B CZ  
4559 O OH  . TYR   B 42  ? 0.2693 0.2922 0.2237 0.0298  0.0267  0.0228  42  TYR   B OH  
4569 N N   . LEU   B 43  ? 0.1556 0.1443 0.1297 0.0091  -0.0132 -0.0172 43  LEU   B N   
4570 C CA  . LEU   B 43  ? 0.1544 0.1441 0.1280 0.0075  -0.0126 -0.0020 43  LEU   B CA  
4571 C C   . LEU   B 43  ? 0.1593 0.1494 0.1339 0.0042  -0.0168 -0.0049 43  LEU   B C   
4572 O O   . LEU   B 43  ? 0.1559 0.1537 0.1615 0.0060  -0.0234 0.0032  43  LEU   B O   
4573 C CB  . LEU   B 43  ? 0.1511 0.1422 0.1526 -0.0005 -0.0276 -0.0076 43  LEU   B CB  
4574 C CG  . LEU   B 43  ? 0.1579 0.1388 0.1518 0.0039  -0.0263 -0.0084 43  LEU   B CG  
4575 C CD1 . LEU   B 43  ? 0.1674 0.1441 0.1855 0.0034  -0.0396 -0.0070 43  LEU   B CD1 
4576 C CD2 . LEU   B 43  ? 0.1554 0.1402 0.1623 -0.0035 -0.0273 -0.0099 43  LEU   B CD2 
4588 N N   . LYS   B 44  ? 0.1549 0.1470 0.1359 0.0099  -0.0091 -0.0058 44  LYS   B N   
4589 C CA  . LYS   B 44  ? 0.1694 0.1547 0.1394 0.0080  -0.0137 0.0089  44  LYS   B CA  
4590 C C   . LYS   B 44  ? 0.1603 0.1482 0.1394 0.0125  -0.0095 0.0052  44  LYS   B C   
4591 O O   . LYS   B 44  ? 0.1770 0.1449 0.1723 0.0058  -0.0009 -0.0008 44  LYS   B O   
4592 C CB  . LYS   B 44  ? 0.1926 0.1733 0.1559 0.0109  -0.0215 0.0061  44  LYS   B CB  
4593 C CG  . LYS   B 44  ? 0.2266 0.2009 0.1904 0.0113  -0.0416 0.0028  44  LYS   B CG  
4594 C CD  . LYS   B 44  ? 0.2582 0.2233 0.2483 -0.0031 -0.0482 0.0024  44  LYS   B CD  
4595 C CE  . LYS   B 44  ? 0.2865 0.2479 0.2892 -0.0063 -0.0528 0.0078  44  LYS   B CE  
4596 N NZ  . LYS   B 44  ? 0.2982 0.2582 0.3158 -0.0025 -0.0583 0.0163  44  LYS   B NZ  
4610 N N   . HIS   B 45  ? 0.1524 0.1517 0.1299 0.0042  -0.0105 0.0077  45  HIS   B N   
4611 C CA  . HIS   B 45  ? 0.1575 0.1484 0.1398 0.0087  -0.0061 -0.0054 45  HIS   B CA  
4612 C C   . HIS   B 45  ? 0.1810 0.1689 0.1819 0.0147  -0.0190 -0.0052 45  HIS   B C   
4613 O O   . HIS   B 45  ? 0.1907 0.1974 0.2276 0.0406  0.0073  0.0003  45  HIS   B O   
4614 C CB  . HIS   B 45  ? 0.1469 0.1501 0.1449 -0.0010 -0.0049 -0.0083 45  HIS   B CB  
4615 C CG  . HIS   B 45  ? 0.1512 0.1468 0.1424 -0.0062 -0.0020 -0.0071 45  HIS   B CG  
4616 N ND1 . HIS   B 45  ? 0.1546 0.1447 0.1484 -0.0008 -0.0133 -0.0100 45  HIS   B ND1 
4617 C CD2 . HIS   B 45  ? 0.1605 0.1504 0.1545 -0.0093 -0.0079 -0.0039 45  HIS   B CD2 
4618 C CE1 . HIS   B 45  ? 0.1628 0.1362 0.1371 -0.0005 -0.0243 -0.0125 45  HIS   B CE1 
4619 N NE2 . HIS   B 45  ? 0.1687 0.1445 0.1517 0.0039  -0.0160 -0.0043 45  HIS   B NE2 
4627 N N   A GLY   B 46  ? 0.1908 0.1602 0.2041 0.0168  -0.0422 0.0082  46  GLY   B N   
4628 N N   B GLY   B 46  ? 0.1877 0.1763 0.1972 0.0153  -0.0242 -0.0008 46  GLY   B N   
4629 C CA  A GLY   B 46  ? 0.2009 0.1731 0.2450 0.0180  -0.0488 0.0037  46  GLY   B CA  
4630 C CA  B GLY   B 46  ? 0.1933 0.1858 0.2165 0.0148  -0.0275 0.0018  46  GLY   B CA  
4631 C C   A GLY   B 46  ? 0.2034 0.1909 0.2883 0.0264  -0.0411 0.0031  46  GLY   B C   
4632 C C   B GLY   B 46  ? 0.1971 0.1945 0.2387 0.0154  -0.0277 0.0038  46  GLY   B C   
4633 O O   A GLY   B 46  ? 0.2154 0.2138 0.3687 0.0304  -0.0159 -0.0206 46  GLY   B O   
4634 O O   B GLY   B 46  ? 0.2002 0.1993 0.2449 0.0164  -0.0272 0.0070  46  GLY   B O   
4641 N N   . GLY   B 47  ? 0.1988 0.2010 0.2567 0.0117  -0.0228 0.0003  47  GLY   B N   
4642 C CA  . GLY   B 47  ? 0.1874 0.1747 0.2223 0.0034  -0.0140 -0.0020 47  GLY   B CA  
4643 C C   . GLY   B 47  ? 0.1681 0.1507 0.1841 0.0048  0.0037  0.0066  47  GLY   B C   
4644 O O   . GLY   B 47  ? 0.1775 0.1393 0.1872 0.0045  -0.0068 0.0087  47  GLY   B O   
4649 N N   . GLY   B 48  ? 0.1514 0.1393 0.1790 0.0049  -0.0031 0.0138  48  GLY   B N   
4650 C CA  . GLY   B 48  ? 0.1507 0.1367 0.1745 0.0006  0.0012  0.0073  48  GLY   B CA  
4651 C C   . GLY   B 48  ? 0.1419 0.1331 0.1655 0.0007  0.0058  0.0047  48  GLY   B C   
4652 O O   . GLY   B 48  ? 0.1380 0.1349 0.1848 0.0029  -0.0055 0.0065  48  GLY   B O   
4656 N N   . VAL   B 49  ? 0.1439 0.1383 0.1571 0.0108  0.0007  0.0022  49  VAL   B N   
4657 C CA  . VAL   B 49  ? 0.1462 0.1453 0.1486 0.0136  -0.0098 -0.0057 49  VAL   B CA  
4658 C C   . VAL   B 49  ? 0.1384 0.1377 0.1313 0.0099  -0.0053 0.0041  49  VAL   B C   
4659 O O   . VAL   B 49  ? 0.1477 0.1448 0.1457 0.0065  -0.0030 0.0082  49  VAL   B O   
4660 C CB  . VAL   B 49  ? 0.1485 0.1638 0.1778 0.0046  -0.0200 -0.0037 49  VAL   B CB  
4661 C CG1 . VAL   B 49  ? 0.1492 0.1708 0.1709 0.0088  -0.0235 0.0038  49  VAL   B CG1 
4662 C CG2 . VAL   B 49  ? 0.1655 0.1781 0.2045 -0.0009 -0.0368 -0.0042 49  VAL   B CG2 
4672 N N   . ALA   B 50  ? 0.1343 0.1302 0.1347 0.0018  -0.0011 0.0045  50  ALA   B N   
4673 C CA  . ALA   B 50  ? 0.1311 0.1268 0.1422 0.0065  -0.0042 0.0046  50  ALA   B CA  
4674 C C   . ALA   B 50  ? 0.1386 0.1319 0.1420 0.0053  0.0047  0.0054  50  ALA   B C   
4675 O O   . ALA   B 50  ? 0.1416 0.1344 0.1417 0.0081  0.0007  0.0020  50  ALA   B O   
4676 C CB  . ALA   B 50  ? 0.1389 0.1285 0.1530 -0.0009 0.0041  0.0058  50  ALA   B CB  
4682 N N   . GLY   B 51  ? 0.1376 0.1408 0.1574 0.0105  -0.0109 0.0132  51  GLY   B N   
4683 C CA  . GLY   B 51  ? 0.1425 0.1475 0.1690 0.0147  -0.0157 0.0119  51  GLY   B CA  
4684 C C   . GLY   B 51  ? 0.1401 0.1428 0.1712 0.0221  -0.0141 0.0110  51  GLY   B C   
4685 O O   . GLY   B 51  ? 0.1428 0.1513 0.1942 0.0101  -0.0101 0.0037  51  GLY   B O   
4689 N N   . ALA   B 52  ? 0.1380 0.1381 0.1724 0.0179  -0.0069 0.0158  52  ALA   B N   
4690 C CA  . ALA   B 52  ? 0.1454 0.1448 0.1706 0.0178  0.0023  0.0022  52  ALA   B CA  
4691 C C   . ALA   B 52  ? 0.1387 0.1434 0.1603 0.0093  0.0031  0.0032  52  ALA   B C   
4692 O O   . ALA   B 52  ? 0.1431 0.1481 0.1779 0.0118  0.0058  0.0038  52  ALA   B O   
4693 C CB  . ALA   B 52  ? 0.1618 0.1498 0.1772 0.0068  0.0096  0.0008  52  ALA   B CB  
4699 N N   . LEU   B 53  ? 0.1299 0.1393 0.1516 0.0164  0.0033  0.0033  53  LEU   B N   
4700 C CA  . LEU   B 53  ? 0.1297 0.1474 0.1544 0.0130  -0.0005 0.0052  53  LEU   B CA  
4701 C C   . LEU   B 53  ? 0.1362 0.1378 0.1460 0.0120  0.0046  0.0088  53  LEU   B C   
4702 O O   . LEU   B 53  ? 0.1417 0.1511 0.1572 0.0021  0.0064  0.0136  53  LEU   B O   
4703 C CB  . LEU   B 53  ? 0.1312 0.1511 0.1609 0.0114  0.0013  0.0181  53  LEU   B CB  
4704 C CG  . LEU   B 53  ? 0.1287 0.1632 0.1627 0.0056  0.0030  0.0269  53  LEU   B CG  
4705 C CD1 . LEU   B 53  ? 0.1377 0.1830 0.1914 0.0134  -0.0033 0.0065  53  LEU   B CD1 
4706 C CD2 . LEU   B 53  ? 0.1443 0.1906 0.1880 -0.0094 -0.0055 -0.0033 53  LEU   B CD2 
4718 N N   . ASN   B 54  ? 0.1344 0.1309 0.1453 0.0040  -0.0030 0.0087  54  ASN   B N   
4719 C CA  . ASN   B 54  ? 0.1386 0.1407 0.1573 0.0067  -0.0001 0.0048  54  ASN   B CA  
4720 C C   . ASN   B 54  ? 0.1367 0.1445 0.1731 0.0032  0.0045  0.0084  54  ASN   B C   
4721 O O   . ASN   B 54  ? 0.1351 0.1516 0.1819 -0.0020 0.0053  0.0017  54  ASN   B O   
4722 C CB  . ASN   B 54  ? 0.1428 0.1549 0.1671 0.0060  0.0059  0.0049  54  ASN   B CB  
4723 C CG  . ASN   B 54  ? 0.1407 0.1674 0.1639 0.0051  -0.0038 0.0040  54  ASN   B CG  
4724 O OD1 . ASN   B 54  ? 0.1390 0.1615 0.1761 0.0001  -0.0104 -0.0104 54  ASN   B OD1 
4725 N ND2 . ASN   B 54  ? 0.1507 0.1900 0.1885 -0.0003 -0.0247 0.0167  54  ASN   B ND2 
4732 N N   . LYS   B 55  ? 0.1352 0.1500 0.1914 0.0096  0.0017  0.0063  55  LYS   B N   
4733 C CA  . LYS   B 55  ? 0.1433 0.1632 0.2011 0.0198  0.0003  0.0080  55  LYS   B CA  
4734 C C   . LYS   B 55  ? 0.1383 0.1634 0.1983 0.0162  0.0060  -0.0008 55  LYS   B C   
4735 O O   . LYS   B 55  ? 0.1308 0.1778 0.2119 0.0129  0.0069  -0.0025 55  LYS   B O   
4736 C CB  . LYS   B 55  ? 0.1560 0.1736 0.2307 0.0283  0.0117  0.0148  55  LYS   B CB  
4737 C CG  . LYS   B 55  ? 0.1946 0.2032 0.3066 0.0356  0.0316  0.0260  55  LYS   B CG  
4738 C CD  . LYS   B 55  ? 0.2264 0.2235 0.3758 0.0463  0.0503  0.0365  55  LYS   B CD  
4739 C CE  . LYS   B 55  ? 0.2533 0.2428 0.4397 0.0476  0.0602  0.0381  55  LYS   B CE  
4740 N NZ  . LYS   B 55  ? 0.2629 0.2566 0.4745 0.0486  0.0502  0.0439  55  LYS   B NZ  
4754 N N   . ALA   B 56  ? 0.1394 0.1688 0.1793 0.0103  0.0008  -0.0106 56  ALA   B N   
4755 C CA  . ALA   B 56  ? 0.1500 0.1840 0.1832 0.0052  0.0042  -0.0049 56  ALA   B CA  
4756 C C   . ALA   B 56  ? 0.1494 0.1769 0.1804 0.0065  0.0132  0.0016  56  ALA   B C   
4757 O O   . ALA   B 56  ? 0.1626 0.1901 0.1951 0.0042  0.0292  0.0045  56  ALA   B O   
4758 C CB  . ALA   B 56  ? 0.1607 0.2063 0.1829 -0.0089 0.0041  -0.0102 56  ALA   B CB  
4764 N N   . THR   B 57  ? 0.1431 0.1687 0.1860 0.0055  0.0113  0.0076  57  THR   B N   
4765 C CA  . THR   B 57  ? 0.1481 0.1684 0.1869 0.0010  0.0173  0.0144  57  THR   B CA  
4766 C C   . THR   B 57  ? 0.1485 0.1774 0.2035 -0.0028 0.0202  0.0160  57  THR   B C   
4767 O O   . THR   B 57  ? 0.1556 0.1783 0.2135 -0.0141 0.0120  0.0118  57  THR   B O   
4768 C CB  . THR   B 57  ? 0.1541 0.1552 0.1694 0.0007  0.0163  0.0179  57  THR   B CB  
4769 O OG1 . THR   B 57  ? 0.1535 0.1471 0.1804 0.0018  0.0187  0.0043  57  THR   B OG1 
4770 C CG2 . THR   B 57  ? 0.1476 0.1574 0.1680 0.0014  0.0148  0.0148  57  THR   B CG2 
4778 N N   . ASN   B 58  ? 0.1341 0.1963 0.2267 -0.0130 0.0099  0.0008  58  ASN   B N   
4779 C CA  . ASN   B 58  ? 0.1518 0.2384 0.2624 -0.0207 0.0391  0.0006  58  ASN   B CA  
4780 C C   . ASN   B 58  ? 0.1371 0.2162 0.2216 -0.0177 0.0073  0.0031  58  ASN   B C   
4781 O O   . ASN   B 58  ? 0.1456 0.2248 0.2262 -0.0190 0.0038  -0.0024 58  ASN   B O   
4782 C CB  . ASN   B 58  ? 0.2310 0.3083 0.3811 -0.0381 0.0756  0.0070  58  ASN   B CB  
4783 C CG  . ASN   B 58  ? 0.3251 0.3664 0.5210 -0.0438 0.0900  0.0288  58  ASN   B CG  
4784 O OD1 . ASN   B 58  ? 0.3504 0.3901 0.5719 -0.0442 0.0912  0.0342  58  ASN   B OD1 
4785 N ND2 . ASN   B 58  ? 0.4118 0.4118 0.5694 -0.0472 0.0959  0.0350  58  ASN   B ND2 
4792 N N   . ASN   B 59  ? 0.1367 0.2011 0.2010 -0.0128 -0.0019 0.0096  59  ASN   B N   
4793 C CA  . ASN   B 59  ? 0.1406 0.1975 0.2017 -0.0089 -0.0147 0.0187  59  ASN   B CA  
4794 C C   . ASN   B 59  ? 0.1352 0.1893 0.1912 -0.0140 -0.0124 0.0058  59  ASN   B C   
4795 O O   . ASN   B 59  ? 0.1378 0.1920 0.1852 -0.0125 -0.0139 0.0016  59  ASN   B O   
4796 C CB  . ASN   B 59  ? 0.1502 0.2133 0.2135 -0.0025 -0.0254 0.0167  59  ASN   B CB  
4797 C CG  . ASN   B 59  ? 0.1645 0.2268 0.2216 0.0041  -0.0332 0.0138  59  ASN   B CG  
4798 O OD1 . ASN   B 59  ? 0.1678 0.2309 0.2229 0.0066  -0.0201 0.0233  59  ASN   B OD1 
4799 N ND2 . ASN   B 59  ? 0.1720 0.2330 0.2314 -0.0061 -0.0323 0.0094  59  ASN   B ND2 
4806 N N   . ALA   B 60  ? 0.1393 0.1747 0.1919 -0.0102 -0.0053 0.0021  60  ALA   B N   
4807 C CA  . ALA   B 60  ? 0.1479 0.1648 0.1914 -0.0206 -0.0032 0.0073  60  ALA   B CA  
4808 C C   . ALA   B 60  ? 0.1458 0.1565 0.1744 -0.0122 -0.0061 0.0072  60  ALA   B C   
4809 O O   . ALA   B 60  ? 0.1506 0.1569 0.1855 -0.0131 -0.0046 -0.0032 60  ALA   B O   
4810 C CB  . ALA   B 60  ? 0.1631 0.1656 0.2069 -0.0197 0.0029  0.0081  60  ALA   B CB  
4816 N N   . MET   B 61  ? 0.1371 0.1528 0.1706 -0.0098 -0.0033 0.0110  61  MET   B N   
4817 C CA  . MET   B 61  ? 0.1349 0.1466 0.1686 -0.0075 -0.0098 0.0075  61  MET   B CA  
4818 C C   . MET   B 61  ? 0.1410 0.1414 0.1636 -0.0129 -0.0108 0.0100  61  MET   B C   
4819 O O   . MET   B 61  ? 0.1451 0.1417 0.1548 -0.0023 -0.0084 -0.0055 61  MET   B O   
4820 C CB  . MET   B 61  ? 0.1327 0.1464 0.1581 -0.0037 -0.0046 0.0006  61  MET   B CB  
4821 C CG  . MET   B 61  ? 0.1345 0.1463 0.1471 -0.0025 0.0009  0.0015  61  MET   B CG  
4822 S SD  . MET   B 61  ? 0.1358 0.1453 0.1767 -0.0032 -0.0030 -0.0073 61  MET   B SD  
4823 C CE  . MET   B 61  ? 0.1424 0.1669 0.2016 -0.0035 -0.0038 -0.0243 61  MET   B CE  
4833 N N   . GLN   B 62  ? 0.1377 0.1484 0.1538 -0.0067 -0.0113 0.0077  62  GLN   B N   
4834 C CA  . GLN   B 62  ? 0.1419 0.1499 0.1645 -0.0024 -0.0110 0.0053  62  GLN   B CA  
4835 C C   . GLN   B 62  ? 0.1430 0.1591 0.1674 -0.0013 -0.0202 -0.0039 62  GLN   B C   
4836 O O   . GLN   B 62  ? 0.1574 0.1591 0.1687 -0.0047 -0.0254 -0.0135 62  GLN   B O   
4837 C CB  . GLN   B 62  ? 0.1447 0.1515 0.1648 0.0009  -0.0099 0.0037  62  GLN   B CB  
4838 C CG  . GLN   B 62  ? 0.1479 0.1624 0.1693 0.0017  -0.0190 -0.0013 62  GLN   B CG  
4839 C CD  . GLN   B 62  ? 0.1472 0.1571 0.1599 0.0039  -0.0272 0.0084  62  GLN   B CD  
4840 O OE1 . GLN   B 62  ? 0.1515 0.1584 0.1713 0.0011  -0.0262 -0.0051 62  GLN   B OE1 
4841 N NE2 . GLN   B 62  ? 0.1481 0.1654 0.1761 0.0015  -0.0236 -0.0044 62  GLN   B NE2 
4850 N N   . VAL   B 63  ? 0.1416 0.1646 0.1850 -0.0068 -0.0214 -0.0091 63  VAL   B N   
4851 C CA  . VAL   B 63  ? 0.1561 0.1669 0.1973 -0.0132 -0.0305 -0.0086 63  VAL   B CA  
4852 C C   . VAL   B 63  ? 0.1542 0.1538 0.1916 -0.0139 -0.0287 -0.0149 63  VAL   B C   
4853 O O   . VAL   B 63  ? 0.1630 0.1534 0.1998 -0.0106 -0.0408 -0.0131 63  VAL   B O   
4854 C CB  . VAL   B 63  ? 0.1588 0.1763 0.2329 -0.0180 -0.0250 -0.0059 63  VAL   B CB  
4855 C CG1 . VAL   B 63  ? 0.1665 0.1814 0.2526 -0.0249 -0.0202 -0.0057 63  VAL   B CG1 
4856 C CG2 . VAL   B 63  ? 0.1566 0.1909 0.2410 -0.0137 -0.0279 -0.0133 63  VAL   B CG2 
4866 N N   . GLU   B 64  ? 0.1528 0.1453 0.1874 -0.0087 -0.0229 -0.0056 64  GLU   B N   
4867 C CA  . GLU   B 64  ? 0.1547 0.1385 0.1760 -0.0119 -0.0320 -0.0116 64  GLU   B CA  
4868 C C   . GLU   B 64  ? 0.1511 0.1384 0.1627 -0.0042 -0.0267 -0.0141 64  GLU   B C   
4869 O O   . GLU   B 64  ? 0.1599 0.1493 0.1664 -0.0101 -0.0270 -0.0126 64  GLU   B O   
4870 C CB  . GLU   B 64  ? 0.1511 0.1466 0.1769 -0.0125 -0.0214 -0.0024 64  GLU   B CB  
4871 C CG  . GLU   B 64  ? 0.1572 0.1510 0.1712 -0.0223 -0.0257 -0.0134 64  GLU   B CG  
4872 C CD  . GLU   B 64  ? 0.1654 0.1636 0.1817 -0.0279 -0.0189 -0.0138 64  GLU   B CD  
4873 O OE1 . GLU   B 64  ? 0.1659 0.1836 0.1885 -0.0299 -0.0211 -0.0241 64  GLU   B OE1 
4874 O OE2 . GLU   B 64  ? 0.1803 0.1687 0.1902 -0.0305 -0.0339 -0.0188 64  GLU   B OE2 
4881 N N   . SER   B 65  ? 0.1502 0.1353 0.1595 -0.0088 -0.0155 -0.0162 65  SER   B N   
4882 C CA  . SER   B 65  ? 0.1465 0.1373 0.1612 -0.0038 -0.0161 -0.0153 65  SER   B CA  
4883 C C   . SER   B 65  ? 0.1502 0.1412 0.1590 -0.0011 -0.0202 -0.0128 65  SER   B C   
4884 O O   . SER   B 65  ? 0.1580 0.1501 0.1571 -0.0022 -0.0222 -0.0245 65  SER   B O   
4885 C CB  . SER   B 65  ? 0.1444 0.1451 0.1576 -0.0103 -0.0166 -0.0090 65  SER   B CB  
4886 O OG  . SER   B 65  ? 0.1538 0.1446 0.1651 -0.0051 -0.0139 -0.0201 65  SER   B OG  
4892 N N   . ASP   B 66  ? 0.1594 0.1483 0.1600 -0.0012 -0.0278 -0.0129 66  ASP   B N   
4893 C CA  . ASP   B 66  ? 0.1696 0.1571 0.1546 0.0032  -0.0289 -0.0091 66  ASP   B CA  
4894 C C   . ASP   B 66  ? 0.1701 0.1614 0.1556 -0.0022 -0.0240 -0.0192 66  ASP   B C   
4895 O O   . ASP   B 66  ? 0.1716 0.1668 0.1725 0.0052  -0.0291 -0.0258 66  ASP   B O   
4896 C CB  . ASP   B 66  ? 0.1855 0.1730 0.1802 0.0103  -0.0400 -0.0104 66  ASP   B CB  
4897 C CG  . ASP   B 66  ? 0.2083 0.1830 0.2099 0.0185  -0.0522 -0.0010 66  ASP   B CG  
4898 O OD1 . ASP   B 66  ? 0.2303 0.1805 0.2145 0.0090  -0.0511 -0.0021 66  ASP   B OD1 
4899 O OD2 . ASP   B 66  ? 0.2231 0.2077 0.2615 0.0364  -0.0496 -0.0053 66  ASP   B OD2 
4904 N N   . ASP   B 67  ? 0.1666 0.1515 0.1569 -0.0082 -0.0226 -0.0200 67  ASP   B N   
4905 C CA  . ASP   B 67  ? 0.1811 0.1500 0.1678 -0.0096 -0.0263 -0.0174 67  ASP   B CA  
4906 C C   . ASP   B 67  ? 0.1794 0.1458 0.1750 -0.0011 -0.0243 -0.0210 67  ASP   B C   
4907 O O   . ASP   B 67  ? 0.1849 0.1515 0.1863 -0.0026 -0.0208 -0.0224 67  ASP   B O   
4908 C CB  . ASP   B 67  ? 0.2057 0.1608 0.1809 -0.0112 -0.0373 -0.0118 67  ASP   B CB  
4909 C CG  . ASP   B 67  ? 0.2370 0.1687 0.1779 -0.0054 -0.0653 -0.0179 67  ASP   B CG  
4910 O OD1 . ASP   B 67  ? 0.2576 0.1751 0.1954 -0.0105 -0.0665 -0.0118 67  ASP   B OD1 
4911 O OD2 . ASP   B 67  ? 0.2531 0.1761 0.2033 0.0043  -0.0724 -0.0129 67  ASP   B OD2 
4916 N N   . TYR   B 68  ? 0.1713 0.1505 0.1661 0.0012  -0.0353 -0.0269 68  TYR   B N   
4917 C CA  . TYR   B 68  ? 0.1688 0.1672 0.1801 0.0049  -0.0376 -0.0349 68  TYR   B CA  
4918 C C   . TYR   B 68  ? 0.1606 0.1614 0.1758 0.0027  -0.0332 -0.0401 68  TYR   B C   
4919 O O   . TYR   B 68  ? 0.1629 0.1722 0.1800 0.0062  -0.0307 -0.0498 68  TYR   B O   
4920 C CB  . TYR   B 68  ? 0.1737 0.1876 0.1847 0.0082  -0.0411 -0.0464 68  TYR   B CB  
4921 C CG  . TYR   B 68  ? 0.1846 0.2043 0.2027 0.0154  -0.0349 -0.0688 68  TYR   B CG  
4922 C CD1 . TYR   B 68  ? 0.1869 0.2084 0.2284 -0.0022 -0.0394 -0.0787 68  TYR   B CD1 
4923 C CD2 . TYR   B 68  ? 0.1872 0.2206 0.2233 0.0192  -0.0447 -0.0627 68  TYR   B CD2 
4924 C CE1 . TYR   B 68  ? 0.1898 0.2215 0.2505 0.0005  -0.0367 -0.0778 68  TYR   B CE1 
4925 C CE2 . TYR   B 68  ? 0.1899 0.2242 0.2393 0.0147  -0.0369 -0.0778 68  TYR   B CE2 
4926 C CZ  . TYR   B 68  ? 0.1837 0.2239 0.2565 0.0054  -0.0352 -0.0815 68  TYR   B CZ  
4927 O OH  . TYR   B 68  ? 0.1788 0.2420 0.2851 0.0027  -0.0318 -0.0616 68  TYR   B OH  
4937 N N   . ILE   B 69  ? 0.1622 0.1538 0.1755 0.0039  -0.0289 -0.0363 69  ILE   B N   
4938 C CA  . ILE   B 69  ? 0.1686 0.1608 0.1817 -0.0013 -0.0250 -0.0386 69  ILE   B CA  
4939 C C   . ILE   B 69  ? 0.1677 0.1571 0.1762 0.0097  -0.0329 -0.0294 69  ILE   B C   
4940 O O   . ILE   B 69  ? 0.1728 0.1708 0.1738 0.0065  -0.0232 -0.0338 69  ILE   B O   
4941 C CB  . ILE   B 69  ? 0.1754 0.1692 0.2019 -0.0017 -0.0009 -0.0318 69  ILE   B CB  
4942 C CG1 . ILE   B 69  ? 0.1758 0.1723 0.2135 -0.0086 0.0038  -0.0327 69  ILE   B CG1 
4943 C CG2 . ILE   B 69  ? 0.1897 0.1798 0.2239 0.0039  0.0052  -0.0239 69  ILE   B CG2 
4944 C CD1 . ILE   B 69  ? 0.1672 0.1774 0.2200 -0.0186 0.0056  -0.0369 69  ILE   B CD1 
4956 N N   . ALA   B 70  ? 0.1674 0.1587 0.1819 0.0086  -0.0382 -0.0294 70  ALA   B N   
4957 C CA  . ALA   B 70  ? 0.1725 0.1635 0.1647 0.0025  -0.0417 -0.0263 70  ALA   B CA  
4958 C C   . ALA   B 70  ? 0.1768 0.1596 0.1715 -0.0026 -0.0461 -0.0354 70  ALA   B C   
4959 O O   . ALA   B 70  ? 0.1860 0.1653 0.1789 -0.0001 -0.0401 -0.0411 70  ALA   B O   
4960 C CB  . ALA   B 70  ? 0.1742 0.1788 0.1755 -0.0004 -0.0386 -0.0271 70  ALA   B CB  
4966 N N   . THR   B 71  ? 0.1845 0.1614 0.1853 0.0031  -0.0523 -0.0376 71  THR   B N   
4967 C CA  . THR   B 71  ? 0.1977 0.1654 0.1977 0.0066  -0.0665 -0.0401 71  THR   B CA  
4968 C C   . THR   B 71  ? 0.1939 0.1678 0.2228 0.0222  -0.0646 -0.0510 71  THR   B C   
4969 O O   . THR   B 71  ? 0.2028 0.1734 0.2622 0.0226  -0.0567 -0.0655 71  THR   B O   
4970 C CB  . THR   B 71  ? 0.2188 0.1913 0.2185 0.0008  -0.0743 -0.0208 71  THR   B CB  
4971 O OG1 . THR   B 71  ? 0.2332 0.2164 0.2513 -0.0149 -0.0698 0.0028  71  THR   B OG1 
4972 C CG2 . THR   B 71  ? 0.2347 0.1934 0.2421 0.0044  -0.0657 -0.0053 71  THR   B CG2 
4980 N N   . ASN   B 72  ? 0.1764 0.1725 0.2147 0.0146  -0.0584 -0.0691 72  ASN   B N   
4981 C CA  . ASN   B 72  ? 0.1766 0.1877 0.2175 0.0169  -0.0443 -0.0723 72  ASN   B CA  
4982 C C   . ASN   B 72  ? 0.1807 0.1990 0.2250 0.0029  -0.0197 -0.0729 72  ASN   B C   
4983 O O   . ASN   B 72  ? 0.1806 0.2149 0.2461 0.0068  -0.0060 -0.0706 72  ASN   B O   
4984 C CB  . ASN   B 72  ? 0.1833 0.2014 0.2290 0.0127  -0.0594 -0.0632 72  ASN   B CB  
4985 C CG  . ASN   B 72  ? 0.1997 0.2132 0.2424 0.0295  -0.0585 -0.0394 72  ASN   B CG  
4986 O OD1 . ASN   B 72  ? 0.2228 0.2298 0.2402 0.0193  -0.0452 -0.0444 72  ASN   B OD1 
4987 N ND2 . ASN   B 72  ? 0.2132 0.2197 0.2818 0.0427  -0.0425 -0.0088 72  ASN   B ND2 
4994 N N   . GLY   B 73  ? 0.1820 0.1976 0.2031 -0.0036 -0.0277 -0.0714 73  GLY   B N   
4995 C CA  . GLY   B 73  ? 0.1786 0.2056 0.1797 -0.0019 -0.0240 -0.0558 73  GLY   B CA  
4996 C C   . GLY   B 73  ? 0.1737 0.2018 0.1328 0.0057  -0.0207 -0.0549 73  GLY   B C   
4997 O O   . GLY   B 73  ? 0.1689 0.1902 0.1547 0.0061  -0.0213 -0.0374 73  GLY   B O   
5001 N N   . PRO   B 74  ? 0.1751 0.2123 0.1337 0.0048  -0.0278 -0.0420 74  PRO   B N   
5002 C CA  . PRO   B 74  ? 0.1707 0.2124 0.1270 0.0086  -0.0209 -0.0261 74  PRO   B CA  
5003 C C   . PRO   B 74  ? 0.1579 0.1951 0.1322 0.0065  -0.0165 -0.0250 74  PRO   B C   
5004 O O   . PRO   B 74  ? 0.1616 0.1972 0.1723 0.0072  -0.0110 -0.0381 74  PRO   B O   
5005 C CB  . PRO   B 74  ? 0.1868 0.2312 0.1381 0.0016  -0.0181 -0.0209 74  PRO   B CB  
5006 C CG  . PRO   B 74  ? 0.2041 0.2392 0.1621 0.0021  -0.0124 -0.0232 74  PRO   B CG  
5007 C CD  . PRO   B 74  ? 0.1987 0.2296 0.1541 0.0041  -0.0128 -0.0365 74  PRO   B CD  
5015 N N   . LEU   B 75  ? 0.1529 0.1843 0.1242 0.0093  -0.0168 -0.0228 75  LEU   B N   
5016 C CA  . LEU   B 75  ? 0.1519 0.1820 0.1304 0.0066  -0.0145 -0.0102 75  LEU   B CA  
5017 C C   . LEU   B 75  ? 0.1591 0.1917 0.1278 0.0083  -0.0065 -0.0079 75  LEU   B C   
5018 O O   . LEU   B 75  ? 0.1739 0.2042 0.1383 0.0019  -0.0083 -0.0030 75  LEU   B O   
5019 C CB  . LEU   B 75  ? 0.1598 0.1829 0.1190 -0.0020 -0.0191 0.0037  75  LEU   B CB  
5020 C CG  . LEU   B 75  ? 0.1920 0.1976 0.1431 -0.0246 -0.0084 -0.0018 75  LEU   B CG  
5021 C CD1 . LEU   B 75  ? 0.2233 0.2120 0.1543 -0.0371 0.0069  -0.0045 75  LEU   B CD1 
5022 C CD2 . LEU   B 75  ? 0.2267 0.2157 0.2040 -0.0202 0.0025  0.0043  75  LEU   B CD2 
5034 N N   . LYS   B 76  ? 0.1572 0.2101 0.1548 0.0042  -0.0014 -0.0040 76  LYS   B N   
5035 C CA  . LYS   B 76  ? 0.1660 0.2201 0.1771 -0.0028 0.0213  -0.0073 76  LYS   B CA  
5036 C C   . LYS   B 76  ? 0.1597 0.2040 0.1467 0.0073  0.0072  0.0123  76  LYS   B C   
5037 O O   . LYS   B 76  ? 0.1615 0.1860 0.1489 0.0059  0.0038  0.0130  76  LYS   B O   
5038 C CB  . LYS   B 76  ? 0.1816 0.2295 0.2428 -0.0070 0.0433  -0.0438 76  LYS   B CB  
5039 C CG  . LYS   B 76  ? 0.1955 0.2480 0.2930 0.0014  0.0318  -0.0512 76  LYS   B CG  
5040 C CD  . LYS   B 76  ? 0.1981 0.2571 0.3404 0.0086  0.0154  -0.0632 76  LYS   B CD  
5041 C CE  . LYS   B 76  ? 0.2052 0.2694 0.3870 0.0151  0.0009  -0.0722 76  LYS   B CE  
5042 N NZ  . LYS   B 76  ? 0.2059 0.2742 0.4113 0.0128  -0.0166 -0.0859 76  LYS   B NZ  
5056 N N   . VAL   B 77  ? 0.1693 0.2099 0.1470 0.0146  0.0098  0.0202  77  VAL   B N   
5057 C CA  . VAL   B 77  ? 0.1699 0.1983 0.1625 0.0181  0.0183  0.0377  77  VAL   B CA  
5058 C C   . VAL   B 77  ? 0.1550 0.1790 0.1555 0.0197  0.0191  0.0271  77  VAL   B C   
5059 O O   . VAL   B 77  ? 0.1584 0.1733 0.1604 0.0258  0.0264  0.0216  77  VAL   B O   
5060 C CB  . VAL   B 77  ? 0.1797 0.2065 0.1893 0.0209  0.0288  0.0518  77  VAL   B CB  
5061 C CG1 . VAL   B 77  ? 0.1844 0.1929 0.2268 0.0109  0.0309  0.0617  77  VAL   B CG1 
5062 C CG2 . VAL   B 77  ? 0.1934 0.2266 0.2075 0.0200  0.0113  0.0609  77  VAL   B CG2 
5072 N N   . GLY   B 78  ? 0.1543 0.1689 0.1457 0.0128  0.0161  0.0214  78  GLY   B N   
5073 C CA  . GLY   B 78  ? 0.1487 0.1639 0.1405 0.0112  0.0218  0.0114  78  GLY   B CA  
5074 C C   . GLY   B 78  ? 0.1468 0.1574 0.1306 0.0081  0.0130  0.0129  78  GLY   B C   
5075 O O   . GLY   B 78  ? 0.1523 0.1484 0.1462 0.0166  0.0154  0.0150  78  GLY   B O   
5079 N N   . GLY   B 79  ? 0.1399 0.1630 0.1396 0.0107  0.0146  0.0080  79  GLY   B N   
5080 C CA  . GLY   B 79  ? 0.1433 0.1489 0.1390 0.0102  0.0113  0.0059  79  GLY   B CA  
5081 C C   . GLY   B 79  ? 0.1354 0.1401 0.1486 0.0134  0.0150  0.0027  79  GLY   B C   
5082 O O   . GLY   B 79  ? 0.1435 0.1401 0.1562 0.0103  0.0187  0.0131  79  GLY   B O   
5086 N N   . SER   B 80  ? 0.1356 0.1359 0.1497 0.0062  0.0166  -0.0020 80  SER   B N   
5087 C CA  . SER   B 80  ? 0.1307 0.1316 0.1551 0.0035  0.0079  0.0015  80  SER   B CA  
5088 C C   . SER   B 80  ? 0.1344 0.1297 0.1460 0.0064  -0.0048 -0.0004 80  SER   B C   
5089 O O   . SER   B 80  ? 0.1463 0.1319 0.1821 0.0121  0.0022  -0.0049 80  SER   B O   
5090 C CB  . SER   B 80  ? 0.1380 0.1383 0.1545 -0.0027 0.0057  0.0049  80  SER   B CB  
5091 O OG  . SER   B 80  ? 0.1465 0.1528 0.1699 -0.0025 -0.0132 0.0127  80  SER   B OG  
5097 N N   . CYS   B 81  ? 0.1342 0.1211 0.1472 0.0011  -0.0017 -0.0066 81  CYS   B N   
5098 C CA  . CYS   B 81  ? 0.1343 0.1187 0.1565 0.0044  -0.0034 -0.0060 81  CYS   B CA  
5099 C C   . CYS   B 81  ? 0.1355 0.1170 0.1446 0.0022  -0.0122 -0.0028 81  CYS   B C   
5100 O O   . CYS   B 81  ? 0.1550 0.1205 0.1510 0.0059  -0.0043 -0.0098 81  CYS   B O   
5101 C CB  . CYS   B 81  ? 0.1530 0.1355 0.1538 -0.0059 -0.0087 -0.0057 81  CYS   B CB  
5102 S SG  . CYS   B 81  ? 0.1525 0.1497 0.1516 -0.0024 -0.0253 -0.0103 81  CYS   B SG  
5108 N N   . VAL   B 82  ? 0.1408 0.1167 0.1516 0.0017  -0.0104 -0.0073 82  VAL   B N   
5109 C CA  . VAL   B 82  ? 0.1429 0.1217 0.1482 -0.0023 -0.0102 -0.0018 82  VAL   B CA  
5110 C C   . VAL   B 82  ? 0.1510 0.1136 0.1566 0.0020  -0.0079 -0.0027 82  VAL   B C   
5111 O O   . VAL   B 82  ? 0.1602 0.1153 0.1850 -0.0012 -0.0073 -0.0174 82  VAL   B O   
5112 C CB  . VAL   B 82  ? 0.1521 0.1404 0.1665 -0.0012 -0.0136 0.0055  82  VAL   B CB  
5113 C CG1 . VAL   B 82  ? 0.1715 0.1601 0.1731 0.0053  -0.0103 0.0139  82  VAL   B CG1 
5114 C CG2 . VAL   B 82  ? 0.1578 0.1540 0.1721 -0.0050 -0.0236 0.0122  82  VAL   B CG2 
5124 N N   . LEU   B 83  ? 0.1428 0.1146 0.1549 -0.0126 -0.0181 -0.0080 83  LEU   B N   
5125 C CA  . LEU   B 83  ? 0.1429 0.1171 0.1443 -0.0125 -0.0174 -0.0016 83  LEU   B CA  
5126 C C   . LEU   B 83  ? 0.1415 0.1168 0.1419 -0.0136 -0.0154 -0.0013 83  LEU   B C   
5127 O O   . LEU   B 83  ? 0.1428 0.1272 0.1351 -0.0177 -0.0155 0.0015  83  LEU   B O   
5128 C CB  . LEU   B 83  ? 0.1477 0.1299 0.1424 -0.0137 -0.0234 -0.0080 83  LEU   B CB  
5129 C CG  . LEU   B 83  ? 0.1639 0.1560 0.1467 -0.0154 -0.0137 -0.0092 83  LEU   B CG  
5130 C CD1 . LEU   B 83  ? 0.1784 0.1650 0.1475 -0.0154 -0.0202 -0.0093 83  LEU   B CD1 
5131 C CD2 . LEU   B 83  ? 0.1790 0.1624 0.1643 -0.0063 -0.0089 -0.0259 83  LEU   B CD2 
5143 N N   . SER   B 84  ? 0.1462 0.1301 0.1634 -0.0187 -0.0122 0.0010  84  SER   B N   
5144 C CA  . SER   B 84  ? 0.1481 0.1482 0.1602 -0.0257 -0.0152 0.0152  84  SER   B CA  
5145 C C   . SER   B 84  ? 0.1386 0.1670 0.1207 -0.0180 -0.0158 0.0192  84  SER   B C   
5146 O O   . SER   B 84  ? 0.1475 0.1548 0.1156 -0.0168 -0.0099 0.0023  84  SER   B O   
5147 C CB  . SER   B 84  ? 0.1619 0.1520 0.2101 -0.0287 0.0090  0.0202  84  SER   B CB  
5148 O OG  . SER   B 84  ? 0.1665 0.1698 0.2503 -0.0373 0.0130  0.0257  84  SER   B OG  
5154 N N   . GLY   B 85  ? 0.1439 0.1906 0.1358 -0.0225 -0.0109 0.0245  85  GLY   B N   
5155 C CA  . GLY   B 85  ? 0.1428 0.1966 0.1503 -0.0351 0.0023  0.0006  85  GLY   B CA  
5156 C C   . GLY   B 85  ? 0.1406 0.1757 0.1436 -0.0426 0.0009  0.0057  85  GLY   B C   
5157 O O   . GLY   B 85  ? 0.1529 0.1755 0.1486 -0.0516 0.0187  -0.0107 85  GLY   B O   
5161 N N   . HIS   B 86  ? 0.1429 0.1574 0.1565 -0.0325 -0.0174 0.0181  86  HIS   B N   
5162 C CA  . HIS   B 86  ? 0.1449 0.1557 0.1591 -0.0347 -0.0151 0.0206  86  HIS   B CA  
5163 C C   . HIS   B 86  ? 0.1453 0.1716 0.1438 -0.0444 -0.0093 0.0373  86  HIS   B C   
5164 O O   . HIS   B 86  ? 0.1612 0.1825 0.1501 -0.0337 0.0003  0.0329  86  HIS   B O   
5165 C CB  . HIS   B 86  ? 0.1533 0.1566 0.1642 -0.0194 -0.0257 0.0120  86  HIS   B CB  
5166 C CG  . HIS   B 86  ? 0.1530 0.1632 0.1661 -0.0134 -0.0204 0.0131  86  HIS   B CG  
5167 N ND1 . HIS   B 86  ? 0.1644 0.1865 0.1759 -0.0236 -0.0236 -0.0015 86  HIS   B ND1 
5168 C CD2 . HIS   B 86  ? 0.1560 0.1692 0.1675 -0.0123 -0.0190 0.0110  86  HIS   B CD2 
5169 C CE1 . HIS   B 86  ? 0.1701 0.1840 0.1625 -0.0147 -0.0103 -0.0142 86  HIS   B CE1 
5170 N NE2 . HIS   B 86  ? 0.1628 0.1773 0.1563 -0.0042 -0.0154 0.0008  86  HIS   B NE2 
5178 N N   . ASN   B 87  ? 0.1416 0.1746 0.1571 -0.0363 -0.0067 0.0306  87  ASN   B N   
5179 C CA  . ASN   B 87  ? 0.1483 0.1959 0.1614 -0.0305 0.0172  0.0223  87  ASN   B CA  
5180 C C   . ASN   B 87  ? 0.1648 0.1796 0.1487 -0.0323 0.0262  0.0146  87  ASN   B C   
5181 O O   . ASN   B 87  ? 0.1857 0.1869 0.1786 -0.0285 0.0439  0.0101  87  ASN   B O   
5182 C CB  . ASN   B 87  ? 0.1516 0.2266 0.1912 -0.0280 0.0244  0.0140  87  ASN   B CB  
5183 C CG  . ASN   B 87  ? 0.1593 0.2430 0.1962 0.0017  0.0345  0.0299  87  ASN   B CG  
5184 O OD1 . ASN   B 87  ? 0.1529 0.2275 0.1861 0.0107  0.0427  0.0477  87  ASN   B OD1 
5185 N ND2 . ASN   B 87  ? 0.1946 0.2523 0.2248 0.0069  0.0363  0.0239  87  ASN   B ND2 
5192 N N   . LEU   B 88  ? 0.1550 0.1638 0.1395 -0.0336 0.0150  0.0160  88  LEU   B N   
5193 C CA  . LEU   B 88  ? 0.1621 0.1588 0.1445 -0.0331 0.0079  -0.0011 88  LEU   B CA  
5194 C C   . LEU   B 88  ? 0.1628 0.1482 0.1434 -0.0320 -0.0000 0.0026  88  LEU   B C   
5195 O O   . LEU   B 88  ? 0.1872 0.1574 0.1638 -0.0219 -0.0243 -0.0080 88  LEU   B O   
5196 C CB  . LEU   B 88  ? 0.1718 0.1625 0.1615 -0.0360 -0.0037 0.0115  88  LEU   B CB  
5197 C CG  . LEU   B 88  ? 0.2087 0.1937 0.1784 -0.0316 -0.0260 0.0289  88  LEU   B CG  
5198 C CD1 . LEU   B 88  ? 0.2201 0.2212 0.1942 -0.0404 -0.0165 0.0471  88  LEU   B CD1 
5199 C CD2 . LEU   B 88  ? 0.2400 0.2163 0.2276 0.0024  -0.0460 0.0041  88  LEU   B CD2 
5211 N N   . ALA   B 89  ? 0.1527 0.1464 0.1319 -0.0315 0.0163  0.0012  89  ALA   B N   
5212 C CA  . ALA   B 89  ? 0.1484 0.1398 0.1212 -0.0311 0.0020  0.0066  89  ALA   B CA  
5213 C C   . ALA   B 89  ? 0.1555 0.1444 0.1309 -0.0360 0.0151  0.0034  89  ALA   B C   
5214 O O   . ALA   B 89  ? 0.1418 0.1548 0.1660 -0.0393 0.0112  -0.0222 89  ALA   B O   
5215 C CB  . ALA   B 89  ? 0.1414 0.1385 0.1468 -0.0345 0.0066  0.0144  89  ALA   B CB  
5221 N N   . LYS   B 90  ? 0.1885 0.1350 0.1348 -0.0389 -0.0044 0.0099  90  LYS   B N   
5222 C CA  . LYS   B 90  ? 0.2043 0.1337 0.1291 -0.0423 -0.0099 0.0091  90  LYS   B CA  
5223 C C   . LYS   B 90  ? 0.1913 0.1262 0.1473 -0.0401 -0.0068 0.0005  90  LYS   B C   
5224 O O   . LYS   B 90  ? 0.1990 0.1456 0.1614 -0.0580 0.0006  0.0017  90  LYS   B O   
5225 C CB  . LYS   B 90  ? 0.2225 0.1414 0.1671 -0.0344 -0.0010 0.0203  90  LYS   B CB  
5226 C CG  . LYS   B 90  ? 0.2266 0.1542 0.1778 -0.0177 0.0226  0.0168  90  LYS   B CG  
5227 C CD  . LYS   B 90  ? 0.2525 0.1755 0.2202 -0.0075 0.0444  0.0026  90  LYS   B CD  
5228 C CE  . LYS   B 90  ? 0.2659 0.1946 0.2710 -0.0145 0.0508  -0.0083 90  LYS   B CE  
5229 N NZ  . LYS   B 90  ? 0.2716 0.1874 0.2726 -0.0285 0.0613  -0.0086 90  LYS   B NZ  
5243 N N   . HIS   B 91  ? 0.1645 0.1163 0.1301 -0.0292 -0.0102 0.0065  91  HIS   B N   
5244 C CA  . HIS   B 91  ? 0.1526 0.1208 0.1410 -0.0241 -0.0109 0.0008  91  HIS   B CA  
5245 C C   . HIS   B 91  ? 0.1396 0.1232 0.1220 -0.0268 -0.0067 0.0037  91  HIS   B C   
5246 O O   . HIS   B 91  ? 0.1554 0.1266 0.1229 -0.0272 -0.0144 -0.0001 91  HIS   B O   
5247 C CB  . HIS   B 91  ? 0.1729 0.1222 0.1764 -0.0071 -0.0066 0.0110  91  HIS   B CB  
5248 C CG  . HIS   B 91  ? 0.2141 0.1428 0.2396 -0.0005 0.0218  0.0242  91  HIS   B CG  
5249 N ND1 . HIS   B 91  ? 0.2417 0.1493 0.2938 0.0029  0.0302  0.0081  91  HIS   B ND1 
5250 C CD2 . HIS   B 91  ? 0.2278 0.1710 0.2810 0.0184  0.0036  0.0563  91  HIS   B CD2 
5251 C CE1 . HIS   B 91  ? 0.2439 0.1619 0.3089 0.0187  0.0230  0.0198  91  HIS   B CE1 
5252 N NE2 . HIS   B 91  ? 0.2356 0.1744 0.3058 0.0357  0.0146  0.0613  91  HIS   B NE2 
5260 N N   . CYS   B 92  ? 0.1374 0.1213 0.1262 -0.0265 -0.0125 0.0010  92  CYS   B N   
5261 C CA  . CYS   B 92  ? 0.1343 0.1211 0.1194 -0.0182 -0.0068 0.0015  92  CYS   B CA  
5262 C C   . CYS   B 92  ? 0.1279 0.1169 0.1134 -0.0120 -0.0067 0.0010  92  CYS   B C   
5263 O O   . CYS   B 92  ? 0.1397 0.1232 0.1367 -0.0145 -0.0018 -0.0036 92  CYS   B O   
5264 C CB  . CYS   B 92  ? 0.1320 0.1255 0.1275 -0.0175 -0.0064 0.0018  92  CYS   B CB  
5265 S SG  . CYS   B 92  ? 0.1352 0.1290 0.1407 -0.0107 -0.0096 0.0050  92  CYS   B SG  
5271 N N   . LEU   B 93  ? 0.1217 0.1167 0.1188 -0.0105 -0.0028 -0.0057 93  LEU   B N   
5272 C CA  . LEU   B 93  ? 0.1264 0.1160 0.1267 -0.0024 -0.0090 0.0001  93  LEU   B CA  
5273 C C   . LEU   B 93  ? 0.1187 0.1123 0.1186 -0.0005 -0.0034 0.0048  93  LEU   B C   
5274 O O   . LEU   B 93  ? 0.1266 0.1144 0.1263 -0.0074 -0.0024 0.0019  93  LEU   B O   
5275 C CB  . LEU   B 93  ? 0.1273 0.1179 0.1403 -0.0022 -0.0072 0.0032  93  LEU   B CB  
5276 C CG  . LEU   B 93  ? 0.1232 0.1299 0.1551 -0.0000 -0.0011 0.0099  93  LEU   B CG  
5277 C CD1 . LEU   B 93  ? 0.1275 0.1427 0.1542 0.0041  -0.0037 -0.0055 93  LEU   B CD1 
5278 C CD2 . LEU   B 93  ? 0.1233 0.1298 0.1624 -0.0034 -0.0034 0.0004  93  LEU   B CD2 
5290 N N   . HIS   B 94  ? 0.1238 0.1118 0.1178 -0.0055 -0.0080 0.0018  94  HIS   B N   
5291 C CA  . HIS   B 94  ? 0.1256 0.1105 0.1206 -0.0035 -0.0052 0.0039  94  HIS   B CA  
5292 C C   . HIS   B 94  ? 0.1191 0.1148 0.1388 -0.0009 -0.0057 0.0045  94  HIS   B C   
5293 O O   . HIS   B 94  ? 0.1277 0.1217 0.1762 -0.0021 0.0117  -0.0093 94  HIS   B O   
5294 C CB  . HIS   B 94  ? 0.1272 0.1191 0.1263 -0.0009 -0.0043 0.0042  94  HIS   B CB  
5295 C CG  . HIS   B 94  ? 0.1326 0.1183 0.1273 -0.0062 -0.0202 0.0028  94  HIS   B CG  
5296 N ND1 . HIS   B 94  ? 0.1324 0.1218 0.1286 -0.0070 -0.0209 -0.0034 94  HIS   B ND1 
5297 C CD2 . HIS   B 94  ? 0.1304 0.1222 0.1356 -0.0019 -0.0172 0.0050  94  HIS   B CD2 
5298 C CE1 . HIS   B 94  ? 0.1356 0.1247 0.1287 -0.0114 -0.0221 -0.0019 94  HIS   B CE1 
5299 N NE2 . HIS   B 94  ? 0.1287 0.1282 0.1345 -0.0127 -0.0156 0.0011  94  HIS   B NE2 
5307 N N   . VAL   B 95  ? 0.1179 0.1143 0.1384 0.0002  -0.0010 0.0025  95  VAL   B N   
5308 C CA  . VAL   B 95  ? 0.1203 0.1220 0.1354 0.0023  0.0054  0.0076  95  VAL   B CA  
5309 C C   . VAL   B 95  ? 0.1268 0.1240 0.1324 -0.0006 0.0102  0.0021  95  VAL   B C   
5310 O O   . VAL   B 95  ? 0.1300 0.1225 0.1482 0.0044  0.0123  0.0120  95  VAL   B O   
5311 C CB  . VAL   B 95  ? 0.1262 0.1208 0.1319 -0.0027 -0.0059 0.0037  95  VAL   B CB  
5312 C CG1 . VAL   B 95  ? 0.1360 0.1362 0.1498 -0.0112 0.0040  0.0048  95  VAL   B CG1 
5313 C CG2 . VAL   B 95  ? 0.1333 0.1192 0.1419 0.0006  -0.0049 0.0004  95  VAL   B CG2 
5323 N N   . VAL   B 96  ? 0.1391 0.1276 0.1330 0.0098  0.0056  0.0075  96  VAL   B N   
5324 C CA  . VAL   B 96  ? 0.1421 0.1412 0.1259 0.0091  0.0026  0.0145  96  VAL   B CA  
5325 C C   . VAL   B 96  ? 0.1435 0.1414 0.1319 0.0116  0.0148  0.0157  96  VAL   B C   
5326 O O   . VAL   B 96  ? 0.1428 0.1493 0.1509 0.0081  0.0163  0.0062  96  VAL   B O   
5327 C CB  . VAL   B 96  ? 0.1498 0.1573 0.1310 0.0058  0.0079  0.0035  96  VAL   B CB  
5328 C CG1 . VAL   B 96  ? 0.1534 0.1668 0.1449 0.0150  0.0118  0.0028  96  VAL   B CG1 
5329 C CG2 . VAL   B 96  ? 0.1660 0.1577 0.1432 0.0064  0.0086  -0.0068 96  VAL   B CG2 
5339 N N   . GLY   B 97  ? 0.1484 0.1413 0.1329 0.0043  0.0083  0.0173  97  GLY   B N   
5340 C CA  . GLY   B 97  ? 0.1588 0.1417 0.1397 0.0026  0.0129  0.0172  97  GLY   B CA  
5341 C C   . GLY   B 97  ? 0.1761 0.1506 0.1443 0.0078  0.0052  0.0102  97  GLY   B C   
5342 O O   . GLY   B 97  ? 0.1831 0.1589 0.1508 -0.0025 0.0009  0.0094  97  GLY   B O   
5346 N N   . PRO   B 98  ? 0.1880 0.1549 0.1553 0.0079  0.0209  0.0225  98  PRO   B N   
5347 C CA  . PRO   B 98  ? 0.1981 0.1665 0.1616 0.0157  0.0337  0.0260  98  PRO   B CA  
5348 C C   . PRO   B 98  ? 0.2076 0.1708 0.1280 0.0278  0.0334  0.0427  98  PRO   B C   
5349 O O   . PRO   B 98  ? 0.2011 0.1663 0.1575 0.0307  0.0381  0.0339  98  PRO   B O   
5350 C CB  . PRO   B 98  ? 0.1841 0.1685 0.1863 0.0062  0.0463  0.0215  98  PRO   B CB  
5351 C CG  . PRO   B 98  ? 0.1816 0.1623 0.1809 0.0091  0.0359  0.0282  98  PRO   B CG  
5352 C CD  . PRO   B 98  ? 0.1704 0.1527 0.1672 0.0097  0.0250  0.0274  98  PRO   B CD  
5360 N N   . ASN   B 99  ? 0.2197 0.1874 0.1398 0.0382  0.0315  0.0292  99  ASN   B N   
5361 C CA  . ASN   B 99  ? 0.2353 0.1928 0.1548 0.0470  0.0247  0.0414  99  ASN   B CA  
5362 C C   . ASN   B 99  ? 0.2582 0.2228 0.1733 0.0391  0.0363  0.0619  99  ASN   B C   
5363 O O   . ASN   B 99  ? 0.2693 0.2260 0.1811 0.0346  0.0281  0.0577  99  ASN   B O   
5364 C CB  . ASN   B 99  ? 0.2448 0.1873 0.1696 0.0441  0.0180  0.0375  99  ASN   B CB  
5365 C CG  . ASN   B 99  ? 0.2474 0.1965 0.1939 0.0399  0.0014  0.0344  99  ASN   B CG  
5366 O OD1 . ASN   B 99  ? 0.2497 0.1995 0.2168 0.0413  0.0012  0.0372  99  ASN   B OD1 
5367 N ND2 . ASN   B 99  ? 0.2486 0.1989 0.2027 0.0409  -0.0208 0.0277  99  ASN   B ND2 
5374 N N   A VAL   B 100 ? 0.2699 0.2372 0.2140 0.0253  0.0420  0.0798  100 VAL   B N   
5375 N N   B VAL   B 100 ? 0.2791 0.2384 0.2120 0.0340  0.0309  0.0708  100 VAL   B N   
5376 C CA  A VAL   B 100 ? 0.2950 0.2535 0.2742 0.0141  0.0457  0.0884  100 VAL   B CA  
5377 C CA  B VAL   B 100 ? 0.3018 0.2527 0.2532 0.0291  0.0243  0.0768  100 VAL   B CA  
5378 C C   A VAL   B 100 ? 0.3160 0.2576 0.2594 0.0206  0.0432  0.1039  100 VAL   B C   
5379 C C   B VAL   B 100 ? 0.3187 0.2589 0.2572 0.0301  0.0234  0.0951  100 VAL   B C   
5380 O O   A VAL   B 100 ? 0.3237 0.2681 0.2614 0.0166  0.0580  0.0947  100 VAL   B O   
5381 O O   B VAL   B 100 ? 0.3208 0.2626 0.2587 0.0286  0.0240  0.0944  100 VAL   B O   
5382 C CB  A VAL   B 100 ? 0.3046 0.2700 0.3545 -0.0079 0.0413  0.0910  100 VAL   B CB  
5383 C CB  B VAL   B 100 ? 0.3076 0.2606 0.2858 0.0227  0.0184  0.0677  100 VAL   B CB  
5384 C CG1 A VAL   B 100 ? 0.3103 0.2752 0.3822 -0.0129 0.0412  0.0922  100 VAL   B CG1 
5385 C CG1 B VAL   B 100 ? 0.3105 0.2638 0.2970 0.0208  0.0167  0.0653  100 VAL   B CG1 
5386 C CG2 A VAL   B 100 ? 0.3068 0.2754 0.3751 -0.0140 0.0432  0.0973  100 VAL   B CG2 
5387 C CG2 B VAL   B 100 ? 0.3088 0.2628 0.2958 0.0206  0.0170  0.0656  100 VAL   B CG2 
5406 N N   . ASN   B 101 ? 0.3328 0.2620 0.2550 0.0334  0.0231  0.1112  101 ASN   B N   
5407 C CA  . ASN   B 101 ? 0.3718 0.2781 0.2819 0.0431  0.0014  0.1241  101 ASN   B CA  
5408 C C   . ASN   B 101 ? 0.4110 0.3131 0.2837 0.0474  -0.0119 0.1317  101 ASN   B C   
5409 O O   . ASN   B 101 ? 0.4179 0.3271 0.3061 0.0528  -0.0120 0.1068  101 ASN   B O   
5410 C CB  . ASN   B 101 ? 0.3733 0.2683 0.3067 0.0388  0.0050  0.1095  101 ASN   B CB  
5411 C CG  . ASN   B 101 ? 0.3723 0.2554 0.3152 0.0346  0.0100  0.1119  101 ASN   B CG  
5412 O OD1 . ASN   B 101 ? 0.3773 0.2581 0.3449 0.0262  0.0257  0.1032  101 ASN   B OD1 
5413 N ND2 . ASN   B 101 ? 0.3674 0.2526 0.3122 0.0341  0.0042  0.1017  101 ASN   B ND2 
5421 N N   . LYS   B 102 ? 0.4403 0.3439 0.2990 0.0377  -0.0047 0.1247  102 LYS   B N   
5422 C CA  . LYS   B 102 ? 0.4679 0.3833 0.3251 0.0258  0.0085  0.0986  102 LYS   B CA  
5423 C C   . LYS   B 102 ? 0.4589 0.3810 0.3074 0.0265  0.0203  0.0982  102 LYS   B C   
5424 O O   . LYS   B 102 ? 0.4672 0.3845 0.3122 0.0288  0.0096  0.0930  102 LYS   B O   
5425 C CB  . LYS   B 102 ? 0.5005 0.4218 0.3859 0.0146  0.0199  0.0641  102 LYS   B CB  
5426 C CG  . LYS   B 102 ? 0.5252 0.4552 0.4520 0.0073  0.0308  0.0298  102 LYS   B CG  
5427 C CD  . LYS   B 102 ? 0.5456 0.4832 0.5153 0.0014  0.0412  0.0025  102 LYS   B CD  
5428 C CE  . LYS   B 102 ? 0.5619 0.5027 0.5669 -0.0039 0.0484  -0.0159 102 LYS   B CE  
5429 N NZ  . LYS   B 102 ? 0.5717 0.5125 0.5968 -0.0069 0.0514  -0.0263 102 LYS   B NZ  
5443 N N   A GLY   B 103 ? 0.4500 0.3738 0.2884 0.0272  0.0494  0.1092  103 GLY   B N   
5444 N N   B GLY   B 103 ? 0.4461 0.3788 0.3142 0.0222  0.0158  0.0865  103 GLY   B N   
5445 C CA  A GLY   B 103 ? 0.4395 0.3671 0.2951 0.0275  0.0769  0.1022  103 GLY   B CA  
5446 C CA  B GLY   B 103 ? 0.4314 0.3741 0.3225 0.0185  0.0128  0.0702  103 GLY   B CA  
5447 C C   A GLY   B 103 ? 0.4240 0.3555 0.2837 0.0228  0.1042  0.0930  103 GLY   B C   
5448 C C   B GLY   B 103 ? 0.4145 0.3671 0.3250 0.0146  0.0103  0.0526  103 GLY   B C   
5449 O O   A GLY   B 103 ? 0.4298 0.3629 0.2968 0.0210  0.1061  0.0925  103 GLY   B O   
5450 O O   B GLY   B 103 ? 0.4153 0.3684 0.3298 0.0149  0.0089  0.0525  103 GLY   B O   
5457 N N   A GLU   B 104 ? 0.4009 0.3335 0.2570 0.0202  0.1206  0.0732  104 GLU   B N   
5458 N N   B GLU   B 104 ? 0.3961 0.3575 0.3198 0.0099  0.0092  0.0347  104 GLU   B N   
5459 C CA  A GLU   B 104 ? 0.3782 0.3145 0.2287 0.0205  0.1223  0.0528  104 GLU   B CA  
5460 C CA  B GLU   B 104 ? 0.3778 0.3481 0.3127 0.0055  0.0086  0.0179  104 GLU   B CA  
5461 C C   A GLU   B 104 ? 0.3830 0.3156 0.2531 0.0086  0.1424  0.0434  104 GLU   B C   
5462 C C   B GLU   B 104 ? 0.3708 0.3461 0.3190 0.0018  0.0133  0.0097  104 GLU   B C   
5463 O O   A GLU   B 104 ? 0.3855 0.3176 0.2876 0.0074  0.1369  0.0308  104 GLU   B O   
5464 O O   B GLU   B 104 ? 0.3704 0.3461 0.3202 0.0012  0.0136  0.0066  104 GLU   B O   
5465 C CB  A GLU   B 104 ? 0.3565 0.2918 0.2091 0.0311  0.0883  0.0359  104 GLU   B CB  
5466 C CB  B GLU   B 104 ? 0.3676 0.3405 0.3010 0.0044  0.0040  0.0097  104 GLU   B CB  
5467 C CG  A GLU   B 104 ? 0.3384 0.2742 0.1906 0.0388  0.0464  0.0047  104 GLU   B CG  
5468 C CG  B GLU   B 104 ? 0.3590 0.3341 0.2907 0.0031  -0.0006 0.0020  104 GLU   B CG  
5469 C CD  A GLU   B 104 ? 0.3222 0.2567 0.1707 0.0422  0.0103  -0.0025 104 GLU   B CD  
5470 C CD  B GLU   B 104 ? 0.3523 0.3288 0.2831 0.0017  -0.0039 -0.0030 104 GLU   B CD  
5471 O OE1 A GLU   B 104 ? 0.3007 0.2382 0.1504 0.0443  0.0156  0.0041  104 GLU   B OE1 
5472 O OE1 B GLU   B 104 ? 0.3494 0.3263 0.2799 0.0010  -0.0031 -0.0037 104 GLU   B OE1 
5473 O OE2 A GLU   B 104 ? 0.3285 0.2671 0.1797 0.0370  -0.0206 -0.0172 104 GLU   B OE2 
5474 O OE2 B GLU   B 104 ? 0.3507 0.3280 0.2829 0.0011  -0.0072 -0.0063 104 GLU   B OE2 
5487 N N   A ASP   B 105 ? 0.3811 0.3185 0.2556 -0.0042 0.1676  0.0473  105 ASP   B N   
5488 N N   B ASP   B 105 ? 0.3644 0.3448 0.3254 -0.0012 0.0178  0.0062  105 ASP   B N   
5489 C CA  A ASP   B 105 ? 0.3810 0.3200 0.2820 -0.0144 0.1858  0.0336  105 ASP   B CA  
5490 C CA  B ASP   B 105 ? 0.3588 0.3435 0.3339 -0.0038 0.0216  0.0031  105 ASP   B CA  
5491 C C   A ASP   B 105 ? 0.3664 0.2859 0.2648 -0.0229 0.1754  0.0238  105 ASP   B C   
5492 C C   B ASP   B 105 ? 0.3500 0.3360 0.3180 -0.0050 0.0232  0.0012  105 ASP   B C   
5493 O O   A ASP   B 105 ? 0.3526 0.2759 0.2582 -0.0229 0.1715  0.0217  105 ASP   B O   
5494 O O   B ASP   B 105 ? 0.3494 0.3353 0.3130 -0.0052 0.0232  0.0010  105 ASP   B O   
5495 C CB  A ASP   B 105 ? 0.3938 0.3499 0.3505 -0.0073 0.1995  0.0150  105 ASP   B CB  
5496 C CB  B ASP   B 105 ? 0.3614 0.3487 0.3579 -0.0042 0.0235  0.0016  105 ASP   B CB  
5497 C CG  A ASP   B 105 ? 0.4023 0.3709 0.4141 -0.0056 0.2179  0.0051  105 ASP   B CG  
5498 C CG  B ASP   B 105 ? 0.3638 0.3529 0.3800 -0.0049 0.0252  0.0011  105 ASP   B CG  
5499 O OD1 A ASP   B 105 ? 0.4028 0.3780 0.4215 -0.0143 0.2289  0.0147  105 ASP   B OD1 
5500 O OD1 B ASP   B 105 ? 0.3638 0.3539 0.3870 -0.0059 0.0258  0.0019  105 ASP   B OD1 
5501 O OD2 A ASP   B 105 ? 0.4069 0.3815 0.4594 0.0006  0.2141  -0.0082 105 ASP   B OD2 
5502 O OD2 B ASP   B 105 ? 0.3650 0.3552 0.3891 -0.0049 0.0255  0.0004  105 ASP   B OD2 
5511 N N   A ILE   B 106 ? 0.3615 0.2605 0.2882 -0.0267 0.1522  0.0198  106 ILE   B N   
5512 N N   B ILE   B 106 ? 0.3413 0.3287 0.3088 -0.0053 0.0235  0.0001  106 ILE   B N   
5513 C CA  A ILE   B 106 ? 0.3420 0.2323 0.3018 -0.0386 0.1553  0.0144  106 ILE   B CA  
5514 C CA  B ILE   B 106 ? 0.3312 0.3210 0.3023 -0.0057 0.0257  -0.0012 106 ILE   B CA  
5515 C C   A ILE   B 106 ? 0.3095 0.2308 0.2966 -0.0387 0.1519  -0.0096 106 ILE   B C   
5516 C C   B ILE   B 106 ? 0.3189 0.3143 0.2987 -0.0057 0.0298  -0.0039 106 ILE   B C   
5517 O O   A ILE   B 106 ? 0.2970 0.2114 0.2929 -0.0434 0.1451  -0.0210 106 ILE   B O   
5518 O O   B ILE   B 106 ? 0.3184 0.3137 0.2958 -0.0060 0.0273  -0.0047 106 ILE   B O   
5519 C CB  A ILE   B 106 ? 0.3608 0.2240 0.3295 -0.0435 0.1449  0.0260  106 ILE   B CB  
5520 C CB  B ILE   B 106 ? 0.3331 0.3203 0.3017 -0.0060 0.0236  0.0002  106 ILE   B CB  
5521 C CG1 A ILE   B 106 ? 0.3705 0.2228 0.3360 -0.0310 0.1341  0.0254  106 ILE   B CG1 
5522 C CG1 B ILE   B 106 ? 0.3336 0.3194 0.3009 -0.0049 0.0221  0.0011  106 ILE   B CG1 
5523 C CG2 A ILE   B 106 ? 0.3664 0.2288 0.3521 -0.0524 0.1483  0.0324  106 ILE   B CG2 
5524 C CG2 B ILE   B 106 ? 0.3339 0.3209 0.3039 -0.0066 0.0235  0.0005  106 ILE   B CG2 
5525 C CD1 A ILE   B 106 ? 0.3759 0.2243 0.3369 -0.0183 0.1296  0.0266  106 ILE   B CD1 
5526 C CD1 B ILE   B 106 ? 0.3339 0.3190 0.3010 -0.0038 0.0214  0.0019  106 ILE   B CD1 
5549 N N   A GLN   B 107 ? 0.2977 0.2547 0.3124 -0.0368 0.1404  -0.0125 107 GLN   B N   
5550 N N   B GLN   B 107 ? 0.3069 0.3078 0.3020 -0.0058 0.0364  -0.0054 107 GLN   B N   
5551 C CA  A GLN   B 107 ? 0.2807 0.2756 0.3244 -0.0369 0.1316  -0.0079 107 GLN   B CA  
5552 C CA  B GLN   B 107 ? 0.2936 0.2996 0.3070 -0.0058 0.0439  -0.0056 107 GLN   B CA  
5553 C C   A GLN   B 107 ? 0.2523 0.2592 0.2934 -0.0216 0.0993  -0.0156 107 GLN   B C   
5554 C C   B GLN   B 107 ? 0.2640 0.2736 0.2751 -0.0047 0.0592  -0.0089 107 GLN   B C   
5555 O O   A GLN   B 107 ? 0.2490 0.2592 0.3273 -0.0136 0.0773  -0.0299 107 GLN   B O   
5556 O O   B GLN   B 107 ? 0.2656 0.2756 0.2749 -0.0050 0.0559  -0.0108 107 GLN   B O   
5557 C CB  A GLN   B 107 ? 0.3085 0.3159 0.3888 -0.0387 0.1265  0.0029  107 GLN   B CB  
5558 C CB  B GLN   B 107 ? 0.3095 0.3160 0.3475 -0.0053 0.0354  -0.0035 107 GLN   B CB  
5559 C CG  A GLN   B 107 ? 0.3417 0.3558 0.4608 -0.0321 0.0975  0.0066  107 GLN   B CG  
5560 C CG  B GLN   B 107 ? 0.3235 0.3304 0.3868 -0.0042 0.0265  -0.0019 107 GLN   B CG  
5561 C CD  A GLN   B 107 ? 0.3659 0.3841 0.5192 -0.0289 0.0757  0.0113  107 GLN   B CD  
5562 C CD  B GLN   B 107 ? 0.3341 0.3414 0.4191 -0.0034 0.0198  -0.0000 107 GLN   B CD  
5563 O OE1 A GLN   B 107 ? 0.3758 0.3958 0.5411 -0.0242 0.0750  0.0094  107 GLN   B OE1 
5564 O OE1 B GLN   B 107 ? 0.3386 0.3465 0.4307 -0.0028 0.0190  0.0000  107 GLN   B OE1 
5565 N NE2 A GLN   B 107 ? 0.3749 0.3942 0.5395 -0.0270 0.0635  0.0171  107 GLN   B NE2 
5566 N NE2 B GLN   B 107 ? 0.3371 0.3439 0.4306 -0.0029 0.0169  0.0015  107 GLN   B NE2 
5583 N N   . LEU   B 108 ? 0.2311 0.2430 0.2509 -0.0029 0.0773  -0.0099 108 LEU   B N   
5584 C CA  . LEU   B 108 ? 0.2131 0.2154 0.2201 0.0193  0.0530  0.0052  108 LEU   B CA  
5585 C C   . LEU   B 108 ? 0.1839 0.1758 0.2063 0.0253  0.0344  0.0220  108 LEU   B C   
5586 O O   . LEU   B 108 ? 0.1844 0.1651 0.2155 0.0215  0.0289  0.0145  108 LEU   B O   
5587 C CB  . LEU   B 108 ? 0.2279 0.2331 0.2072 0.0226  0.0550  0.0051  108 LEU   B CB  
5588 C CG  . LEU   B 108 ? 0.2411 0.2611 0.2087 0.0263  0.0493  -0.0141 108 LEU   B CG  
5589 C CD1 . LEU   B 108 ? 0.2489 0.2749 0.1989 0.0139  0.0465  -0.0099 108 LEU   B CD1 
5590 C CD2 . LEU   B 108 ? 0.2550 0.2724 0.2284 0.0331  0.0403  -0.0259 108 LEU   B CD2 
5603 N N   . LEU   B 109 ? 0.1712 0.1610 0.1973 0.0178  0.0344  0.0195  109 LEU   B N   
5604 C CA  . LEU   B 109 ? 0.1534 0.1386 0.2084 0.0117  0.0326  0.0258  109 LEU   B CA  
5605 C C   . LEU   B 109 ? 0.1445 0.1283 0.2097 0.0064  0.0331  0.0179  109 LEU   B C   
5606 O O   . LEU   B 109 ? 0.1404 0.1266 0.2091 0.0068  0.0313  0.0299  109 LEU   B O   
5607 C CB  . LEU   B 109 ? 0.1649 0.1323 0.2056 0.0116  0.0223  0.0331  109 LEU   B CB  
5608 C CG  . LEU   B 109 ? 0.1625 0.1295 0.2112 0.0081  0.0147  0.0204  109 LEU   B CG  
5609 C CD1 . LEU   B 109 ? 0.1581 0.1391 0.2071 0.0154  0.0211  0.0156  109 LEU   B CD1 
5610 C CD2 . LEU   B 109 ? 0.1700 0.1368 0.2178 0.0067  0.0094  0.0170  109 LEU   B CD2 
5622 N N   . LYS   B 110 ? 0.1409 0.1264 0.2039 0.0018  0.0319  0.0241  110 LYS   B N   
5623 C CA  . LYS   B 110 ? 0.1373 0.1246 0.2031 0.0031  0.0268  0.0136  110 LYS   B CA  
5624 C C   . LYS   B 110 ? 0.1338 0.1252 0.1949 0.0024  0.0231  0.0128  110 LYS   B C   
5625 O O   . LYS   B 110 ? 0.1298 0.1251 0.1871 -0.0034 0.0163  0.0027  110 LYS   B O   
5626 C CB  . LYS   B 110 ? 0.1408 0.1286 0.2232 -0.0029 0.0284  0.0087  110 LYS   B CB  
5627 C CG  . LYS   B 110 ? 0.1409 0.1313 0.2350 -0.0042 0.0138  0.0118  110 LYS   B CG  
5628 C CD  . LYS   B 110 ? 0.1437 0.1279 0.2364 -0.0070 0.0179  0.0099  110 LYS   B CD  
5629 C CE  . LYS   B 110 ? 0.1407 0.1418 0.2472 -0.0013 0.0149  0.0067  110 LYS   B CE  
5630 N NZ  . LYS   B 110 ? 0.1412 0.1584 0.2422 0.0025  0.0111  -0.0012 110 LYS   B NZ  
5644 N N   . SER   B 111 ? 0.1416 0.1266 0.1977 -0.0024 0.0255  0.0116  111 SER   B N   
5645 C CA  . SER   B 111 ? 0.1441 0.1321 0.1865 0.0009  0.0183  0.0112  111 SER   B CA  
5646 C C   . SER   B 111 ? 0.1389 0.1261 0.1722 0.0013  0.0125  0.0051  111 SER   B C   
5647 O O   . SER   B 111 ? 0.1371 0.1296 0.1842 0.0009  0.0075  0.0078  111 SER   B O   
5648 C CB  . SER   B 111 ? 0.1582 0.1486 0.1912 0.0038  0.0294  0.0189  111 SER   B CB  
5649 O OG  . SER   B 111 ? 0.1777 0.1882 0.2029 0.0058  0.0431  0.0187  111 SER   B OG  
5655 N N   . ALA   B 112 ? 0.1294 0.1276 0.1858 0.0064  0.0172  0.0125  112 ALA   B N   
5656 C CA  . ALA   B 112 ? 0.1284 0.1352 0.1760 0.0012  0.0083  0.0046  112 ALA   B CA  
5657 C C   . ALA   B 112 ? 0.1164 0.1257 0.1629 0.0022  0.0080  0.0010  112 ALA   B C   
5658 O O   . ALA   B 112 ? 0.1197 0.1281 0.1735 -0.0027 0.0095  -0.0003 112 ALA   B O   
5659 C CB  . ALA   B 112 ? 0.1361 0.1398 0.1804 0.0047  0.0087  0.0103  112 ALA   B CB  
5665 N N   . TYR   B 113 ? 0.1180 0.1142 0.1721 -0.0004 0.0107  0.0072  113 TYR   B N   
5666 C CA  . TYR   B 113 ? 0.1161 0.1138 0.1676 -0.0029 0.0112  -0.0015 113 TYR   B CA  
5667 C C   . TYR   B 113 ? 0.1164 0.1130 0.1682 -0.0071 0.0124  0.0005  113 TYR   B C   
5668 O O   . TYR   B 113 ? 0.1199 0.1169 0.1597 -0.0046 0.0104  -0.0045 113 TYR   B O   
5669 C CB  . TYR   B 113 ? 0.1257 0.1124 0.1820 -0.0035 0.0152  0.0082  113 TYR   B CB  
5670 C CG  . TYR   B 113 ? 0.1261 0.1125 0.1895 -0.0028 0.0113  0.0063  113 TYR   B CG  
5671 C CD1 . TYR   B 113 ? 0.1320 0.1152 0.1978 -0.0019 0.0152  0.0139  113 TYR   B CD1 
5672 C CD2 . TYR   B 113 ? 0.1340 0.1122 0.1878 -0.0008 0.0093  0.0060  113 TYR   B CD2 
5673 C CE1 . TYR   B 113 ? 0.1318 0.1199 0.1941 0.0014  0.0185  0.0045  113 TYR   B CE1 
5674 C CE2 . TYR   B 113 ? 0.1390 0.1119 0.1991 -0.0020 0.0095  0.0151  113 TYR   B CE2 
5675 C CZ  . TYR   B 113 ? 0.1339 0.1166 0.2047 0.0037  0.0063  0.0038  113 TYR   B CZ  
5676 O OH  . TYR   B 113 ? 0.1380 0.1129 0.2239 0.0110  0.0180  0.0077  113 TYR   B OH  
5686 N N   . GLU   B 114 ? 0.1163 0.1072 0.1764 -0.0017 0.0168  0.0048  114 GLU   B N   
5687 C CA  . GLU   B 114 ? 0.1159 0.1077 0.1735 -0.0020 0.0092  0.0043  114 GLU   B CA  
5688 C C   . GLU   B 114 ? 0.1140 0.1118 0.1712 0.0021  0.0136  -0.0023 114 GLU   B C   
5689 O O   . GLU   B 114 ? 0.1157 0.1116 0.1777 0.0018  0.0057  0.0024  114 GLU   B O   
5690 C CB  . GLU   B 114 ? 0.1188 0.1149 0.1778 -0.0005 0.0082  0.0082  114 GLU   B CB  
5691 C CG  . GLU   B 114 ? 0.1287 0.1181 0.1742 -0.0034 0.0131  0.0060  114 GLU   B CG  
5692 C CD  . GLU   B 114 ? 0.1251 0.1188 0.1820 -0.0052 0.0144  0.0031  114 GLU   B CD  
5693 O OE1 . GLU   B 114 ? 0.1216 0.1370 0.1837 -0.0028 0.0200  0.0021  114 GLU   B OE1 
5694 O OE2 . GLU   B 114 ? 0.1206 0.1378 0.2094 -0.0135 0.0136  0.0081  114 GLU   B OE2 
5701 N N   . ASN   B 115 ? 0.1197 0.1090 0.1718 0.0002  0.0058  0.0056  115 ASN   B N   
5702 C CA  . ASN   B 115 ? 0.1180 0.1175 0.1687 -0.0055 0.0065  0.0025  115 ASN   B CA  
5703 C C   . ASN   B 115 ? 0.1116 0.1114 0.1602 -0.0093 0.0025  -0.0030 115 ASN   B C   
5704 O O   . ASN   B 115 ? 0.1238 0.1164 0.1692 -0.0098 0.0029  -0.0017 115 ASN   B O   
5705 C CB  . ASN   B 115 ? 0.1270 0.1270 0.1571 -0.0076 0.0058  0.0030  115 ASN   B CB  
5706 C CG  . ASN   B 115 ? 0.1429 0.1288 0.1593 0.0052  0.0060  -0.0024 115 ASN   B CG  
5707 O OD1 . ASN   B 115 ? 0.1845 0.1408 0.1759 0.0022  0.0099  -0.0148 115 ASN   B OD1 
5708 N ND2 . ASN   B 115 ? 0.1352 0.1361 0.1622 -0.0001 0.0039  0.0031  115 ASN   B ND2 
5715 N N   . PHE   B 116 ? 0.1153 0.1110 0.1543 -0.0021 0.0071  -0.0016 116 PHE   B N   
5716 C CA  . PHE   B 116 ? 0.1207 0.1113 0.1581 -0.0069 0.0026  0.0023  116 PHE   B CA  
5717 C C   . PHE   B 116 ? 0.1240 0.1027 0.1544 -0.0068 -0.0011 0.0058  116 PHE   B C   
5718 O O   . PHE   B 116 ? 0.1262 0.1166 0.1564 -0.0004 -0.0035 0.0036  116 PHE   B O   
5719 C CB  . PHE   B 116 ? 0.1162 0.1121 0.1529 -0.0040 -0.0069 0.0028  116 PHE   B CB  
5720 C CG  . PHE   B 116 ? 0.1141 0.1117 0.1546 -0.0053 0.0011  -0.0000 116 PHE   B CG  
5721 C CD1 . PHE   B 116 ? 0.1228 0.1206 0.1691 0.0014  -0.0004 -0.0014 116 PHE   B CD1 
5722 C CD2 . PHE   B 116 ? 0.1230 0.1213 0.1522 -0.0020 0.0069  -0.0000 116 PHE   B CD2 
5723 C CE1 . PHE   B 116 ? 0.1251 0.1247 0.1672 -0.0050 -0.0086 0.0011  116 PHE   B CE1 
5724 C CE2 . PHE   B 116 ? 0.1249 0.1208 0.1512 0.0001  0.0057  0.0033  116 PHE   B CE2 
5725 C CZ  . PHE   B 116 ? 0.1181 0.1225 0.1651 0.0014  -0.0054 0.0001  116 PHE   B CZ  
5735 N N   . ASN   B 117 ? 0.1185 0.1072 0.1631 -0.0036 -0.0019 0.0049  117 ASN   B N   
5736 C CA  . ASN   B 117 ? 0.1282 0.1099 0.1685 0.0016  -0.0018 -0.0005 117 ASN   B CA  
5737 C C   . ASN   B 117 ? 0.1262 0.1092 0.1817 0.0033  -0.0001 0.0019  117 ASN   B C   
5738 O O   . ASN   B 117 ? 0.1378 0.1195 0.2005 -0.0038 -0.0232 0.0054  117 ASN   B O   
5739 C CB  . ASN   B 117 ? 0.1253 0.1150 0.1662 0.0036  0.0023  -0.0019 117 ASN   B CB  
5740 C CG  . ASN   B 117 ? 0.1197 0.1145 0.1734 0.0018  0.0073  -0.0087 117 ASN   B CG  
5741 O OD1 . ASN   B 117 ? 0.1403 0.1186 0.1852 -0.0112 0.0112  -0.0075 117 ASN   B OD1 
5742 N ND2 . ASN   B 117 ? 0.1267 0.1174 0.1761 -0.0012 0.0085  -0.0083 117 ASN   B ND2 
5749 N N   . GLN   B 118 ? 0.1245 0.1058 0.1740 -0.0048 -0.0116 -0.0028 118 GLN   B N   
5750 C CA  . GLN   B 118 ? 0.1284 0.1143 0.1818 -0.0009 -0.0095 0.0028  118 GLN   B CA  
5751 C C   . GLN   B 118 ? 0.1342 0.1146 0.1828 -0.0050 -0.0027 -0.0042 118 GLN   B C   
5752 O O   . GLN   B 118 ? 0.1476 0.1125 0.2207 -0.0079 0.0088  -0.0004 118 GLN   B O   
5753 C CB  . GLN   B 118 ? 0.1392 0.1192 0.1936 0.0021  -0.0132 -0.0036 118 GLN   B CB  
5754 C CG  . GLN   B 118 ? 0.1476 0.1212 0.1940 0.0086  -0.0048 -0.0123 118 GLN   B CG  
5755 C CD  . GLN   B 118 ? 0.1510 0.1158 0.1846 -0.0001 -0.0044 -0.0171 118 GLN   B CD  
5756 O OE1 . GLN   B 118 ? 0.1597 0.1187 0.1957 0.0005  0.0069  -0.0004 118 GLN   B OE1 
5757 N NE2 . GLN   B 118 ? 0.1577 0.1149 0.1951 0.0010  -0.0085 -0.0012 118 GLN   B NE2 
5766 N N   . HIS   B 119 ? 0.1384 0.1150 0.1494 -0.0073 -0.0004 0.0043  119 HIS   B N   
5767 C CA  . HIS   B 119 ? 0.1500 0.1292 0.1489 -0.0023 -0.0115 0.0050  119 HIS   B CA  
5768 C C   . HIS   B 119 ? 0.1440 0.1275 0.1461 -0.0018 -0.0188 0.0040  119 HIS   B C   
5769 O O   . HIS   B 119 ? 0.1529 0.1248 0.1728 -0.0251 -0.0091 0.0080  119 HIS   B O   
5770 C CB  . HIS   B 119 ? 0.1462 0.1380 0.1623 0.0014  -0.0164 -0.0046 119 HIS   B CB  
5771 C CG  . HIS   B 119 ? 0.1503 0.1598 0.1786 0.0119  -0.0302 -0.0201 119 HIS   B CG  
5772 N ND1 . HIS   B 119 ? 0.1690 0.1770 0.2093 0.0043  -0.0406 -0.0384 119 HIS   B ND1 
5773 C CD2 . HIS   B 119 ? 0.1702 0.1814 0.1824 0.0374  -0.0403 -0.0211 119 HIS   B CD2 
5774 C CE1 . HIS   B 119 ? 0.1879 0.1921 0.2186 0.0198  -0.0460 -0.0457 119 HIS   B CE1 
5775 N NE2 . HIS   B 119 ? 0.1891 0.2026 0.1998 0.0346  -0.0451 -0.0346 119 HIS   B NE2 
5783 N N   . GLU   B 120 ? 0.1617 0.1301 0.1443 -0.0056 -0.0217 0.0092  120 GLU   B N   
5784 C CA  . GLU   B 120 ? 0.1871 0.1431 0.1593 -0.0011 -0.0337 0.0192  120 GLU   B CA  
5785 C C   . GLU   B 120 ? 0.1665 0.1328 0.1528 -0.0113 -0.0221 0.0220  120 GLU   B C   
5786 O O   . GLU   B 120 ? 0.1607 0.1441 0.1604 -0.0105 -0.0250 0.0105  120 GLU   B O   
5787 C CB  . GLU   B 120 ? 0.2490 0.1719 0.2162 0.0158  -0.0618 0.0329  120 GLU   B CB  
5788 C CG  . GLU   B 120 ? 0.3038 0.2397 0.3216 0.0260  -0.0809 0.0554  120 GLU   B CG  
5789 C CD  . GLU   B 120 ? 0.3438 0.3029 0.4214 0.0252  -0.0887 0.0728  120 GLU   B CD  
5790 O OE1 . GLU   B 120 ? 0.3612 0.3225 0.4526 0.0195  -0.0850 0.0886  120 GLU   B OE1 
5791 O OE2 . GLU   B 120 ? 0.3675 0.3307 0.4748 0.0232  -0.0885 0.0645  120 GLU   B OE2 
5798 N N   . VAL   B 121 ? 0.1564 0.1273 0.1524 -0.0160 -0.0120 0.0133  121 VAL   B N   
5799 C CA  . VAL   B 121 ? 0.1567 0.1385 0.1390 -0.0131 -0.0148 0.0100  121 VAL   B CA  
5800 C C   . VAL   B 121 ? 0.1454 0.1338 0.1339 -0.0196 -0.0117 0.0084  121 VAL   B C   
5801 O O   . VAL   B 121 ? 0.1528 0.1309 0.1548 -0.0249 -0.0148 0.0047  121 VAL   B O   
5802 C CB  . VAL   B 121 ? 0.1759 0.1740 0.1461 -0.0008 -0.0218 0.0151  121 VAL   B CB  
5803 C CG1 . VAL   B 121 ? 0.1832 0.1850 0.1739 -0.0098 -0.0025 0.0111  121 VAL   B CG1 
5804 C CG2 . VAL   B 121 ? 0.1975 0.1980 0.1542 0.0043  -0.0193 0.0088  121 VAL   B CG2 
5814 N N   . LEU   B 122 ? 0.1381 0.1244 0.1351 -0.0143 -0.0175 0.0063  122 LEU   B N   
5815 C CA  . LEU   B 122 ? 0.1316 0.1317 0.1284 -0.0158 -0.0144 0.0040  122 LEU   B CA  
5816 C C   . LEU   B 122 ? 0.1329 0.1209 0.1352 -0.0239 -0.0123 0.0027  122 LEU   B C   
5817 O O   . LEU   B 122 ? 0.1455 0.1239 0.1571 -0.0266 -0.0201 -0.0003 122 LEU   B O   
5818 C CB  . LEU   B 122 ? 0.1524 0.1396 0.1582 -0.0044 -0.0152 0.0115  122 LEU   B CB  
5819 C CG  . LEU   B 122 ? 0.1432 0.1494 0.1611 -0.0151 -0.0048 0.0081  122 LEU   B CG  
5820 C CD1 . LEU   B 122 ? 0.1503 0.1678 0.1758 -0.0189 -0.0058 0.0095  122 LEU   B CD1 
5821 C CD2 . LEU   B 122 ? 0.1447 0.1538 0.1471 -0.0116 -0.0019 -0.0032 122 LEU   B CD2 
5833 N N   . LEU   B 123 ? 0.1346 0.1155 0.1318 -0.0211 -0.0081 0.0040  123 LEU   B N   
5834 C CA  . LEU   B 123 ? 0.1377 0.1185 0.1331 -0.0227 -0.0174 -0.0039 123 LEU   B CA  
5835 C C   . LEU   B 123 ? 0.1318 0.1156 0.1246 -0.0244 -0.0112 0.0002  123 LEU   B C   
5836 O O   . LEU   B 123 ? 0.1441 0.1184 0.1298 -0.0281 -0.0107 0.0028  123 LEU   B O   
5837 C CB  . LEU   B 123 ? 0.1421 0.1213 0.1334 -0.0247 -0.0062 -0.0084 123 LEU   B CB  
5838 C CG  . LEU   B 123 ? 0.1418 0.1238 0.1585 -0.0177 -0.0003 0.0056  123 LEU   B CG  
5839 C CD1 . LEU   B 123 ? 0.1490 0.1318 0.1640 -0.0138 0.0037  -0.0100 123 LEU   B CD1 
5840 C CD2 . LEU   B 123 ? 0.1495 0.1333 0.1789 -0.0111 0.0030  0.0152  123 LEU   B CD2 
5852 N N   . ALA   B 124 ? 0.1324 0.1135 0.1357 -0.0174 -0.0006 -0.0057 124 ALA   B N   
5853 C CA  . ALA   B 124 ? 0.1243 0.1141 0.1467 -0.0121 -0.0014 -0.0092 124 ALA   B CA  
5854 C C   . ALA   B 124 ? 0.1200 0.1135 0.1366 -0.0138 0.0020  -0.0050 124 ALA   B C   
5855 O O   . ALA   B 124 ? 0.1338 0.1183 0.1424 -0.0122 -0.0074 -0.0003 124 ALA   B O   
5856 C CB  . ALA   B 124 ? 0.1319 0.1209 0.1465 -0.0074 0.0053  -0.0039 124 ALA   B CB  
5862 N N   . PRO   B 125 ? 0.1330 0.1161 0.1300 -0.0143 -0.0103 0.0089  125 PRO   B N   
5863 C CA  . PRO   B 125 ? 0.1425 0.1196 0.1505 -0.0148 -0.0094 0.0137  125 PRO   B CA  
5864 C C   . PRO   B 125 ? 0.1310 0.1114 0.1684 -0.0128 -0.0074 0.0052  125 PRO   B C   
5865 O O   . PRO   B 125 ? 0.1385 0.1098 0.1841 -0.0108 0.0005  0.0099  125 PRO   B O   
5866 C CB  . PRO   B 125 ? 0.1450 0.1434 0.1636 -0.0205 -0.0167 0.0283  125 PRO   B CB  
5867 C CG  . PRO   B 125 ? 0.1544 0.1480 0.1527 -0.0254 -0.0171 0.0127  125 PRO   B CG  
5868 C CD  . PRO   B 125 ? 0.1427 0.1260 0.1369 -0.0260 -0.0045 0.0083  125 PRO   B CD  
5876 N N   . LEU   B 126 ? 0.1366 0.1091 0.1883 -0.0128 0.0108  0.0123  126 LEU   B N   
5877 C CA  . LEU   B 126 ? 0.1425 0.1201 0.1886 -0.0092 0.0140  0.0120  126 LEU   B CA  
5878 C C   . LEU   B 126 ? 0.1419 0.1274 0.1929 0.0023  0.0230  0.0173  126 LEU   B C   
5879 O O   . LEU   B 126 ? 0.1631 0.1529 0.2081 0.0192  0.0029  -0.0037 126 LEU   B O   
5880 C CB  . LEU   B 126 ? 0.1590 0.1270 0.2105 -0.0089 0.0218  0.0079  126 LEU   B CB  
5881 C CG  . LEU   B 126 ? 0.1757 0.1334 0.2228 -0.0212 0.0235  -0.0067 126 LEU   B CG  
5882 C CD1 . LEU   B 126 ? 0.1873 0.1416 0.2667 -0.0215 0.0183  -0.0111 126 LEU   B CD1 
5883 C CD2 . LEU   B 126 ? 0.1734 0.1452 0.2164 -0.0351 0.0169  -0.0047 126 LEU   B CD2 
5895 N N   . LEU   B 127 ? 0.1402 0.1205 0.1872 0.0009  0.0257  0.0137  127 LEU   B N   
5896 C CA  . LEU   B 127 ? 0.1375 0.1260 0.1914 -0.0067 0.0295  0.0184  127 LEU   B CA  
5897 C C   . LEU   B 127 ? 0.1345 0.1204 0.1913 0.0006  0.0216  0.0116  127 LEU   B C   
5898 O O   . LEU   B 127 ? 0.1387 0.1293 0.1936 -0.0107 0.0102  0.0138  127 LEU   B O   
5899 C CB  . LEU   B 127 ? 0.1531 0.1290 0.2019 -0.0011 0.0247  0.0233  127 LEU   B CB  
5900 C CG  . LEU   B 127 ? 0.1631 0.1268 0.2112 0.0022  0.0206  0.0194  127 LEU   B CG  
5901 C CD1 . LEU   B 127 ? 0.1676 0.1293 0.2090 0.0049  0.0126  0.0063  127 LEU   B CD1 
5902 C CD2 . LEU   B 127 ? 0.1655 0.1310 0.2201 -0.0073 0.0184  0.0273  127 LEU   B CD2 
5914 N N   . SER   B 128 ? 0.1439 0.1222 0.1887 0.0014  0.0051  0.0082  128 SER   B N   
5915 C CA  . SER   B 128 ? 0.1519 0.1334 0.1901 0.0096  -0.0014 0.0194  128 SER   B CA  
5916 C C   . SER   B 128 ? 0.1633 0.1339 0.2110 0.0120  -0.0198 0.0173  128 SER   B C   
5917 O O   . SER   B 128 ? 0.1776 0.1381 0.2380 0.0080  -0.0162 0.0309  128 SER   B O   
5918 C CB  . SER   B 128 ? 0.1593 0.1339 0.1939 0.0106  0.0026  0.0258  128 SER   B CB  
5919 O OG  . SER   B 128 ? 0.1675 0.1444 0.1987 0.0116  0.0133  0.0280  128 SER   B OG  
5925 N N   . ALA   B 129 ? 0.1737 0.1367 0.2291 0.0285  -0.0133 0.0011  129 ALA   B N   
5926 C CA  . ALA   B 129 ? 0.1885 0.1465 0.2462 0.0298  -0.0071 -0.0066 129 ALA   B CA  
5927 C C   . ALA   B 129 ? 0.1741 0.1402 0.2298 0.0192  0.0107  0.0033  129 ALA   B C   
5928 O O   . ALA   B 129 ? 0.1666 0.1460 0.2313 0.0133  -0.0005 0.0125  129 ALA   B O   
5929 C CB  . ALA   B 129 ? 0.2067 0.1706 0.2768 0.0325  0.0023  -0.0158 129 ALA   B CB  
5935 N N   . GLY   B 130 ? 0.1766 0.1361 0.2333 0.0265  0.0115  -0.0080 130 GLY   B N   
5936 C CA  . GLY   B 130 ? 0.1806 0.1460 0.2446 0.0260  0.0300  -0.0084 130 GLY   B CA  
5937 C C   . GLY   B 130 ? 0.1814 0.1467 0.2413 0.0179  0.0183  0.0014  130 GLY   B C   
5938 O O   . GLY   B 130 ? 0.1965 0.1559 0.2428 0.0184  0.0105  0.0124  130 GLY   B O   
5942 N N   . ILE   B 131 ? 0.1739 0.1601 0.2508 0.0322  0.0169  0.0043  131 ILE   B N   
5943 C CA  . ILE   B 131 ? 0.1930 0.1759 0.2432 0.0291  0.0043  0.0147  131 ILE   B CA  
5944 C C   . ILE   B 131 ? 0.2051 0.1680 0.2111 0.0187  -0.0001 0.0216  131 ILE   B C   
5945 O O   . ILE   B 131 ? 0.2300 0.1824 0.2211 0.0250  -0.0187 0.0177  131 ILE   B O   
5946 C CB  . ILE   B 131 ? 0.1949 0.2108 0.2730 0.0260  -0.0052 0.0205  131 ILE   B CB  
5947 C CG1 . ILE   B 131 ? 0.2018 0.2289 0.2816 0.0085  0.0042  0.0190  131 ILE   B CG1 
5948 C CG2 . ILE   B 131 ? 0.1939 0.2300 0.2925 0.0302  -0.0058 0.0126  131 ILE   B CG2 
5949 C CD1 . ILE   B 131 ? 0.2112 0.2461 0.2919 -0.0098 -0.0047 0.0242  131 ILE   B CD1 
5961 N N   . PHE   B 132 ? 0.1893 0.1495 0.2019 0.0144  0.0123  0.0212  132 PHE   B N   
5962 C CA  . PHE   B 132 ? 0.1969 0.1529 0.1958 0.0084  0.0312  0.0144  132 PHE   B CA  
5963 C C   . PHE   B 132 ? 0.2169 0.1672 0.2137 0.0090  0.0422  0.0164  132 PHE   B C   
5964 O O   . PHE   B 132 ? 0.2332 0.1851 0.2379 0.0068  0.0550  0.0203  132 PHE   B O   
5965 C CB  . PHE   B 132 ? 0.1812 0.1519 0.1844 0.0117  0.0256  0.0178  132 PHE   B CB  
5966 C CG  . PHE   B 132 ? 0.1771 0.1567 0.1874 0.0166  0.0228  0.0137  132 PHE   B CG  
5967 C CD1 . PHE   B 132 ? 0.1823 0.1583 0.2255 0.0077  0.0244  0.0133  132 PHE   B CD1 
5968 C CD2 . PHE   B 132 ? 0.1821 0.1591 0.1726 0.0241  0.0234  0.0244  132 PHE   B CD2 
5969 C CE1 . PHE   B 132 ? 0.1866 0.1626 0.2348 0.0074  0.0192  0.0179  132 PHE   B CE1 
5970 C CE2 . PHE   B 132 ? 0.1870 0.1632 0.1816 0.0173  0.0176  0.0217  132 PHE   B CE2 
5971 C CZ  . PHE   B 132 ? 0.1886 0.1626 0.2190 0.0104  0.0070  0.0292  132 PHE   B CZ  
5981 N N   . GLY   B 133 ? 0.2147 0.1569 0.2079 0.0083  0.0326  0.0298  133 GLY   B N   
5982 C CA  . GLY   B 133 ? 0.2233 0.1672 0.2217 -0.0085 0.0265  0.0381  133 GLY   B CA  
5983 C C   . GLY   B 133 ? 0.2235 0.1742 0.2272 -0.0217 0.0294  0.0355  133 GLY   B C   
5984 O O   . GLY   B 133 ? 0.2384 0.1891 0.2698 -0.0365 0.0284  0.0467  133 GLY   B O   
5988 N N   . ALA   B 134 ? 0.2105 0.1737 0.2114 -0.0223 0.0311  0.0161  134 ALA   B N   
5989 C CA  . ALA   B 134 ? 0.2038 0.1700 0.2234 -0.0154 0.0392  0.0045  134 ALA   B CA  
5990 C C   . ALA   B 134 ? 0.2096 0.1614 0.2306 -0.0105 0.0336  0.0147  134 ALA   B C   
5991 O O   . ALA   B 134 ? 0.2160 0.1807 0.2520 -0.0011 0.0293  0.0083  134 ALA   B O   
5992 C CB  . ALA   B 134 ? 0.2043 0.1710 0.2432 -0.0099 0.0330  0.0000  134 ALA   B CB  
5998 N N   . ASP   B 135 ? 0.2227 0.1531 0.2318 -0.0145 0.0171  0.0213  135 ASP   B N   
5999 C CA  . ASP   B 135 ? 0.2386 0.1452 0.2468 -0.0119 0.0068  0.0289  135 ASP   B CA  
6000 C C   . ASP   B 135 ? 0.2205 0.1371 0.2322 -0.0034 0.0046  0.0208  135 ASP   B C   
6001 O O   . ASP   B 135 ? 0.2157 0.1327 0.2413 -0.0040 0.0030  0.0217  135 ASP   B O   
6002 C CB  . ASP   B 135 ? 0.2660 0.1558 0.2694 -0.0290 0.0065  0.0326  135 ASP   B CB  
6003 C CG  . ASP   B 135 ? 0.2948 0.1590 0.3118 -0.0445 0.0011  0.0280  135 ASP   B CG  
6004 O OD1 . ASP   B 135 ? 0.3034 0.1477 0.3084 -0.0308 -0.0091 0.0273  135 ASP   B OD1 
6005 O OD2 . ASP   B 135 ? 0.3155 0.1934 0.3650 -0.0583 0.0001  0.0102  135 ASP   B OD2 
6010 N N   . PRO   B 136 ? 0.2133 0.1460 0.2388 0.0151  -0.0067 0.0171  136 PRO   B N   
6011 C CA  . PRO   B 136 ? 0.1939 0.1385 0.2426 0.0131  -0.0046 0.0060  136 PRO   B CA  
6012 C C   . PRO   B 136 ? 0.1774 0.1300 0.2428 0.0086  0.0018  0.0021  136 PRO   B C   
6013 O O   . PRO   B 136 ? 0.1626 0.1257 0.2350 0.0092  0.0059  0.0086  136 PRO   B O   
6014 C CB  . PRO   B 136 ? 0.2004 0.1601 0.2540 0.0273  -0.0069 -0.0039 136 PRO   B CB  
6015 C CG  . PRO   B 136 ? 0.2169 0.1668 0.2651 0.0312  -0.0086 -0.0047 136 PRO   B CG  
6016 C CD  . PRO   B 136 ? 0.2202 0.1612 0.2569 0.0338  -0.0047 0.0017  136 PRO   B CD  
6024 N N   . ILE   B 137 ? 0.1850 0.1221 0.2572 0.0084  -0.0048 0.0059  137 ILE   B N   
6025 C CA  . ILE   B 137 ? 0.1911 0.1175 0.2680 -0.0089 0.0006  0.0029  137 ILE   B CA  
6026 C C   . ILE   B 137 ? 0.1828 0.1256 0.2582 -0.0127 0.0066  0.0098  137 ILE   B C   
6027 O O   . ILE   B 137 ? 0.1682 0.1270 0.2538 -0.0142 0.0029  0.0060  137 ILE   B O   
6028 C CB  . ILE   B 137 ? 0.2213 0.1278 0.3091 -0.0075 -0.0027 0.0025  137 ILE   B CB  
6029 C CG1 . ILE   B 137 ? 0.2499 0.1423 0.3548 0.0034  0.0026  -0.0167 137 ILE   B CG1 
6030 C CG2 . ILE   B 137 ? 0.2245 0.1294 0.3177 -0.0303 -0.0076 0.0117  137 ILE   B CG2 
6031 C CD1 . ILE   B 137 ? 0.2725 0.1719 0.3919 0.0167  -0.0026 -0.0082 137 ILE   B CD1 
6043 N N   . HIS   B 138 ? 0.1892 0.1198 0.2549 -0.0096 0.0159  0.0107  138 HIS   B N   
6044 C CA  . HIS   B 138 ? 0.1926 0.1321 0.2497 -0.0027 0.0298  0.0130  138 HIS   B CA  
6045 C C   . HIS   B 138 ? 0.1744 0.1302 0.2368 -0.0013 0.0331  0.0199  138 HIS   B C   
6046 O O   . HIS   B 138 ? 0.1655 0.1387 0.2535 0.0025  0.0341  0.0303  138 HIS   B O   
6047 C CB  . HIS   B 138 ? 0.2152 0.1427 0.2629 -0.0050 0.0446  0.0115  138 HIS   B CB  
6048 C CG  . HIS   B 138 ? 0.2323 0.1609 0.2658 -0.0066 0.0603  0.0256  138 HIS   B CG  
6049 N ND1 . HIS   B 138 ? 0.2384 0.1783 0.2865 -0.0030 0.0700  0.0204  138 HIS   B ND1 
6050 C CD2 . HIS   B 138 ? 0.2462 0.1681 0.2633 -0.0073 0.0654  0.0170  138 HIS   B CD2 
6051 C CE1 . HIS   B 138 ? 0.2437 0.1777 0.2794 -0.0044 0.0734  0.0244  138 HIS   B CE1 
6052 N NE2 . HIS   B 138 ? 0.2534 0.1670 0.2680 0.0015  0.0691  0.0158  138 HIS   B NE2 
6060 N N   . SER   B 139 ? 0.1710 0.1211 0.2343 0.0040  0.0289  0.0086  139 SER   B N   
6061 C CA  . SER   B 139 ? 0.1677 0.1146 0.2258 -0.0016 0.0238  0.0007  139 SER   B CA  
6062 C C   . SER   B 139 ? 0.1449 0.1102 0.2196 -0.0046 0.0191  -0.0002 139 SER   B C   
6063 O O   . SER   B 139 ? 0.1483 0.1126 0.2186 0.0004  0.0079  0.0042  139 SER   B O   
6064 C CB  . SER   B 139 ? 0.1764 0.1176 0.2270 0.0011  0.0099  0.0071  139 SER   B CB  
6065 O OG  . SER   B 139 ? 0.1784 0.1199 0.2320 -0.0014 -0.0067 0.0110  139 SER   B OG  
6071 N N   . LEU   B 140 ? 0.1440 0.1071 0.2126 -0.0067 0.0214  -0.0051 140 LEU   B N   
6072 C CA  . LEU   B 140 ? 0.1393 0.1103 0.2203 -0.0063 0.0124  0.0030  140 LEU   B CA  
6073 C C   . LEU   B 140 ? 0.1380 0.1118 0.2331 -0.0061 0.0016  -0.0023 140 LEU   B C   
6074 O O   . LEU   B 140 ? 0.1346 0.1209 0.2204 -0.0040 0.0042  -0.0002 140 LEU   B O   
6075 C CB  . LEU   B 140 ? 0.1390 0.1085 0.2345 -0.0094 0.0193  -0.0069 140 LEU   B CB  
6076 C CG  . LEU   B 140 ? 0.1510 0.1122 0.2251 -0.0111 0.0075  0.0004  140 LEU   B CG  
6077 C CD1 . LEU   B 140 ? 0.1610 0.1241 0.2406 -0.0135 0.0124  -0.0004 140 LEU   B CD1 
6078 C CD2 . LEU   B 140 ? 0.1677 0.1263 0.2354 -0.0053 0.0056  -0.0085 140 LEU   B CD2 
6090 N N   . ARG   B 141 ? 0.1309 0.1132 0.2453 -0.0099 0.0118  -0.0011 141 ARG   B N   
6091 C CA  . ARG   B 141 ? 0.1358 0.1144 0.2779 -0.0148 0.0288  -0.0016 141 ARG   B CA  
6092 C C   . ARG   B 141 ? 0.1310 0.1144 0.2592 -0.0104 0.0183  -0.0022 141 ARG   B C   
6093 O O   . ARG   B 141 ? 0.1375 0.1164 0.2521 -0.0103 0.0055  -0.0130 141 ARG   B O   
6094 C CB  . ARG   B 141 ? 0.1536 0.1269 0.3114 -0.0196 0.0350  -0.0047 141 ARG   B CB  
6095 C CG  . ARG   B 141 ? 0.1844 0.1507 0.3293 -0.0202 0.0380  -0.0011 141 ARG   B CG  
6096 C CD  . ARG   B 141 ? 0.2253 0.1760 0.3330 -0.0168 0.0251  -0.0088 141 ARG   B CD  
6097 N NE  . ARG   B 141 ? 0.2427 0.1726 0.3341 -0.0349 0.0334  -0.0121 141 ARG   B NE  
6098 C CZ  . ARG   B 141 ? 0.2579 0.1563 0.3239 -0.0319 0.0446  -0.0222 141 ARG   B CZ  
6099 N NH1 . ARG   B 141 ? 0.2672 0.1520 0.3167 -0.0265 0.0415  -0.0241 141 ARG   B NH1 
6100 N NH2 . ARG   B 141 ? 0.2671 0.1678 0.3300 -0.0165 0.0346  -0.0222 141 ARG   B NH2 
6114 N N   . VAL   B 142 ? 0.1376 0.1117 0.2472 -0.0071 0.0184  -0.0086 142 VAL   B N   
6115 C CA  . VAL   B 142 ? 0.1329 0.1167 0.2394 -0.0087 0.0177  -0.0024 142 VAL   B CA  
6116 C C   . VAL   B 142 ? 0.1296 0.1162 0.2390 -0.0032 0.0143  -0.0056 142 VAL   B C   
6117 O O   . VAL   B 142 ? 0.1355 0.1118 0.2506 0.0009  0.0169  -0.0040 142 VAL   B O   
6118 C CB  . VAL   B 142 ? 0.1437 0.1289 0.2396 -0.0049 0.0294  0.0098  142 VAL   B CB  
6119 C CG1 . VAL   B 142 ? 0.1438 0.1232 0.2394 0.0013  0.0266  0.0037  142 VAL   B CG1 
6120 C CG2 . VAL   B 142 ? 0.1652 0.1298 0.2496 -0.0015 0.0309  0.0097  142 VAL   B CG2 
6130 N N   . CYS   B 143 ? 0.1312 0.1153 0.2164 -0.0043 0.0108  0.0037  143 CYS   B N   
6131 C CA  . CYS   B 143 ? 0.1284 0.1124 0.2180 -0.0023 0.0071  0.0047  143 CYS   B CA  
6132 C C   . CYS   B 143 ? 0.1221 0.1147 0.2192 -0.0042 0.0105  -0.0007 143 CYS   B C   
6133 O O   . CYS   B 143 ? 0.1264 0.1159 0.2255 -0.0053 0.0040  -0.0039 143 CYS   B O   
6134 C CB  . CYS   B 143 ? 0.1332 0.1215 0.2215 -0.0065 0.0067  -0.0020 143 CYS   B CB  
6135 S SG  . CYS   B 143 ? 0.1349 0.1355 0.2112 -0.0047 0.0123  0.0039  143 CYS   B SG  
6141 N N   . VAL   B 144 ? 0.1340 0.1173 0.2262 -0.0077 0.0075  -0.0104 144 VAL   B N   
6142 C CA  . VAL   B 144 ? 0.1384 0.1266 0.2485 -0.0131 -0.0029 -0.0179 144 VAL   B CA  
6143 C C   . VAL   B 144 ? 0.1349 0.1285 0.2505 -0.0093 -0.0011 -0.0029 144 VAL   B C   
6144 O O   . VAL   B 144 ? 0.1414 0.1484 0.2703 -0.0010 0.0028  0.0125  144 VAL   B O   
6145 C CB  . VAL   B 144 ? 0.1582 0.1423 0.3038 -0.0108 -0.0139 -0.0280 144 VAL   B CB  
6146 C CG1 . VAL   B 144 ? 0.1814 0.1777 0.3279 0.0016  -0.0275 -0.0274 144 VAL   B CG1 
6147 C CG2 . VAL   B 144 ? 0.1694 0.1408 0.2962 -0.0021 -0.0249 -0.0295 144 VAL   B CG2 
6157 N N   . ASP   B 145 ? 0.1327 0.1227 0.2584 -0.0046 -0.0008 -0.0098 145 ASP   B N   
6158 C CA  . ASP   B 145 ? 0.1308 0.1302 0.2789 -0.0078 0.0095  -0.0122 145 ASP   B CA  
6159 C C   . ASP   B 145 ? 0.1263 0.1288 0.2608 -0.0047 0.0141  -0.0085 145 ASP   B C   
6160 O O   . ASP   B 145 ? 0.1323 0.1466 0.3162 -0.0107 0.0202  -0.0237 145 ASP   B O   
6161 C CB  . ASP   B 145 ? 0.1461 0.1393 0.3217 -0.0125 0.0244  -0.0075 145 ASP   B CB  
6162 C CG  . ASP   B 145 ? 0.1627 0.1391 0.3687 -0.0254 0.0296  -0.0041 145 ASP   B CG  
6163 O OD1 . ASP   B 145 ? 0.1643 0.1422 0.3820 -0.0251 -0.0010 -0.0112 145 ASP   B OD1 
6164 O OD2 . ASP   B 145 ? 0.1943 0.1501 0.4148 -0.0264 0.0493  0.0088  145 ASP   B OD2 
6169 N N   . THR   B 146 ? 0.1206 0.1209 0.2246 -0.0081 0.0087  -0.0025 146 THR   B N   
6170 C CA  . THR   B 146 ? 0.1294 0.1162 0.2117 -0.0053 0.0105  -0.0050 146 THR   B CA  
6171 C C   . THR   B 146 ? 0.1270 0.1126 0.2091 -0.0050 0.0031  -0.0024 146 THR   B C   
6172 O O   . THR   B 146 ? 0.1320 0.1181 0.2193 -0.0024 0.0022  0.0020  146 THR   B O   
6173 C CB  . THR   B 146 ? 0.1335 0.1195 0.2187 -0.0080 0.0164  -0.0003 146 THR   B CB  
6174 O OG1 . THR   B 146 ? 0.1358 0.1164 0.2290 -0.0066 0.0168  0.0089  146 THR   B OG1 
6175 C CG2 . THR   B 146 ? 0.1441 0.1251 0.2101 -0.0029 0.0116  -0.0040 146 THR   B CG2 
6183 N N   . VAL   B 147 ? 0.1347 0.1174 0.1975 -0.0039 0.0155  0.0008  147 VAL   B N   
6184 C CA  . VAL   B 147 ? 0.1296 0.1164 0.1930 -0.0099 0.0027  -0.0028 147 VAL   B CA  
6185 C C   . VAL   B 147 ? 0.1252 0.1194 0.2018 -0.0164 -0.0016 -0.0044 147 VAL   B C   
6186 O O   . VAL   B 147 ? 0.1386 0.1305 0.2030 -0.0190 -0.0241 -0.0081 147 VAL   B O   
6187 C CB  . VAL   B 147 ? 0.1329 0.1294 0.1879 -0.0054 0.0014  0.0033  147 VAL   B CB  
6188 C CG1 . VAL   B 147 ? 0.1309 0.1421 0.1819 -0.0103 0.0012  0.0018  147 VAL   B CG1 
6189 C CG2 . VAL   B 147 ? 0.1398 0.1283 0.1863 -0.0075 -0.0002 0.0059  147 VAL   B CG2 
6199 N N   . ARG   B 148 ? 0.1296 0.1193 0.1975 -0.0094 -0.0117 -0.0101 148 ARG   B N   
6200 C CA  . ARG   B 148 ? 0.1336 0.1256 0.1884 -0.0082 -0.0193 -0.0105 148 ARG   B CA  
6201 C C   . ARG   B 148 ? 0.1410 0.1358 0.1809 -0.0104 -0.0201 -0.0122 148 ARG   B C   
6202 O O   . ARG   B 148 ? 0.1588 0.1654 0.1808 -0.0229 -0.0255 -0.0048 148 ARG   B O   
6203 C CB  . ARG   B 148 ? 0.1388 0.1345 0.1960 -0.0049 -0.0202 -0.0175 148 ARG   B CB  
6204 C CG  . ARG   B 148 ? 0.1399 0.1513 0.2053 -0.0089 -0.0135 -0.0337 148 ARG   B CG  
6205 C CD  . ARG   B 148 ? 0.1471 0.1656 0.2153 0.0055  -0.0170 -0.0354 148 ARG   B CD  
6206 N NE  . ARG   B 148 ? 0.1493 0.1614 0.2065 0.0216  -0.0192 -0.0302 148 ARG   B NE  
6207 C CZ  . ARG   B 148 ? 0.1434 0.1535 0.1903 0.0187  -0.0171 -0.0221 148 ARG   B CZ  
6208 N NH1 . ARG   B 148 ? 0.1391 0.1586 0.1943 0.0008  -0.0023 -0.0175 148 ARG   B NH1 
6209 N NH2 . ARG   B 148 ? 0.1665 0.1429 0.1888 0.0172  -0.0144 -0.0131 148 ARG   B NH2 
6223 N N   . THR   B 149 ? 0.1429 0.1311 0.1817 -0.0124 -0.0149 -0.0024 149 THR   B N   
6224 C CA  . THR   B 149 ? 0.1476 0.1334 0.1784 -0.0121 -0.0157 0.0047  149 THR   B CA  
6225 C C   . THR   B 149 ? 0.1471 0.1291 0.1637 -0.0134 -0.0239 0.0063  149 THR   B C   
6226 O O   . THR   B 149 ? 0.1519 0.1285 0.1763 -0.0176 -0.0067 0.0016  149 THR   B O   
6227 C CB  . THR   B 149 ? 0.1485 0.1321 0.1809 -0.0185 -0.0205 -0.0017 149 THR   B CB  
6228 O OG1 . THR   B 149 ? 0.1507 0.1350 0.1738 -0.0230 -0.0245 -0.0018 149 THR   B OG1 
6229 C CG2 . THR   B 149 ? 0.1538 0.1340 0.1932 -0.0056 -0.0109 -0.0018 149 THR   B CG2 
6237 N N   . ASN   B 150 ? 0.1546 0.1253 0.1638 -0.0131 -0.0227 -0.0013 150 ASN   B N   
6238 C CA  . ASN   B 150 ? 0.1573 0.1411 0.1558 -0.0163 -0.0200 -0.0100 150 ASN   B CA  
6239 C C   . ASN   B 150 ? 0.1480 0.1334 0.1673 -0.0111 -0.0198 -0.0030 150 ASN   B C   
6240 O O   . ASN   B 150 ? 0.1590 0.1325 0.1902 -0.0203 -0.0379 -0.0036 150 ASN   B O   
6241 C CB  . ASN   B 150 ? 0.1752 0.1778 0.1780 -0.0184 -0.0301 0.0032  150 ASN   B CB  
6242 C CG  . ASN   B 150 ? 0.1997 0.2194 0.2082 -0.0189 -0.0311 0.0199  150 ASN   B CG  
6243 O OD1 . ASN   B 150 ? 0.2086 0.2359 0.2129 -0.0300 -0.0494 0.0168  150 ASN   B OD1 
6244 N ND2 . ASN   B 150 ? 0.2122 0.2394 0.2418 -0.0081 -0.0398 0.0507  150 ASN   B ND2 
6251 N N   . VAL   B 151 ? 0.1411 0.1315 0.1575 -0.0134 -0.0206 0.0011  151 VAL   B N   
6252 C CA  . VAL   B 151 ? 0.1382 0.1349 0.1635 -0.0201 -0.0158 -0.0017 151 VAL   B CA  
6253 C C   . VAL   B 151 ? 0.1391 0.1290 0.1637 -0.0281 -0.0186 0.0002  151 VAL   B C   
6254 O O   . VAL   B 151 ? 0.1475 0.1390 0.1850 -0.0262 -0.0098 -0.0137 151 VAL   B O   
6255 C CB  . VAL   B 151 ? 0.1586 0.1501 0.1772 -0.0041 -0.0094 -0.0068 151 VAL   B CB  
6256 C CG1 . VAL   B 151 ? 0.1677 0.1510 0.2004 -0.0157 0.0036  -0.0163 151 VAL   B CG1 
6257 C CG2 . VAL   B 151 ? 0.1722 0.1622 0.1711 0.0062  -0.0129 0.0057  151 VAL   B CG2 
6267 N N   . TYR   B 152 ? 0.1379 0.1174 0.1530 -0.0226 -0.0122 -0.0069 152 TYR   B N   
6268 C CA  . TYR   B 152 ? 0.1392 0.1309 0.1516 -0.0268 -0.0073 -0.0122 152 TYR   B CA  
6269 C C   . TYR   B 152 ? 0.1353 0.1206 0.1462 -0.0204 -0.0055 -0.0081 152 TYR   B C   
6270 O O   . TYR   B 152 ? 0.1449 0.1270 0.1531 -0.0245 -0.0095 -0.0010 152 TYR   B O   
6271 C CB  . TYR   B 152 ? 0.1501 0.1434 0.1554 -0.0235 -0.0040 0.0029  152 TYR   B CB  
6272 C CG  . TYR   B 152 ? 0.1667 0.1526 0.1562 -0.0344 -0.0048 -0.0029 152 TYR   B CG  
6273 C CD1 . TYR   B 152 ? 0.1803 0.1647 0.1524 -0.0245 -0.0160 0.0024  152 TYR   B CD1 
6274 C CD2 . TYR   B 152 ? 0.1869 0.1706 0.1567 -0.0303 -0.0020 -0.0078 152 TYR   B CD2 
6275 C CE1 . TYR   B 152 ? 0.1983 0.1824 0.1631 -0.0205 -0.0232 0.0165  152 TYR   B CE1 
6276 C CE2 . TYR   B 152 ? 0.1985 0.1911 0.1562 -0.0323 -0.0081 -0.0054 152 TYR   B CE2 
6277 C CZ  . TYR   B 152 ? 0.2067 0.2028 0.1510 -0.0279 -0.0328 0.0149  152 TYR   B CZ  
6278 O OH  . TYR   B 152 ? 0.2282 0.2336 0.1811 -0.0185 -0.0394 0.0152  152 TYR   B OH  
6288 N N   . LEU   B 153 ? 0.1393 0.1212 0.1562 -0.0253 -0.0061 -0.0083 153 LEU   B N   
6289 C CA  . LEU   B 153 ? 0.1479 0.1152 0.1476 -0.0179 0.0029  -0.0079 153 LEU   B CA  
6290 C C   . LEU   B 153 ? 0.1481 0.1159 0.1606 -0.0186 0.0017  -0.0159 153 LEU   B C   
6291 O O   . LEU   B 153 ? 0.1547 0.1388 0.1719 -0.0115 -0.0059 -0.0287 153 LEU   B O   
6292 C CB  . LEU   B 153 ? 0.1471 0.1158 0.1652 -0.0211 0.0005  -0.0072 153 LEU   B CB  
6293 C CG  . LEU   B 153 ? 0.1432 0.1291 0.1877 -0.0193 0.0009  -0.0055 153 LEU   B CG  
6294 C CD1 . LEU   B 153 ? 0.1454 0.1421 0.1952 -0.0267 0.0098  -0.0010 153 LEU   B CD1 
6295 C CD2 . LEU   B 153 ? 0.1476 0.1437 0.1843 -0.0295 0.0134  -0.0031 153 LEU   B CD2 
6307 N N   . ALA   B 154 ? 0.1428 0.1184 0.1667 -0.0032 -0.0063 -0.0115 154 ALA   B N   
6308 C CA  . ALA   B 154 ? 0.1513 0.1282 0.1894 0.0008  -0.0125 -0.0215 154 ALA   B CA  
6309 C C   . ALA   B 154 ? 0.1583 0.1294 0.1919 0.0062  -0.0209 -0.0249 154 ALA   B C   
6310 O O   . ALA   B 154 ? 0.1895 0.1340 0.2069 0.0058  -0.0015 -0.0119 154 ALA   B O   
6311 C CB  . ALA   B 154 ? 0.1450 0.1468 0.2159 -0.0014 -0.0066 -0.0323 154 ALA   B CB  
6317 N N   . VAL   B 155 ? 0.1353 0.1208 0.2023 0.0020  -0.0080 -0.0163 155 VAL   B N   
6318 C CA  . VAL   B 155 ? 0.1289 0.1223 0.2106 0.0004  -0.0107 -0.0081 155 VAL   B CA  
6319 C C   . VAL   B 155 ? 0.1314 0.1232 0.2119 -0.0013 -0.0056 -0.0178 155 VAL   B C   
6320 O O   . VAL   B 155 ? 0.1487 0.1417 0.2372 0.0067  -0.0043 -0.0332 155 VAL   B O   
6321 C CB  . VAL   B 155 ? 0.1351 0.1382 0.2459 -0.0030 -0.0146 0.0027  155 VAL   B CB  
6322 C CG1 . VAL   B 155 ? 0.1384 0.1364 0.2470 -0.0100 -0.0155 -0.0044 155 VAL   B CG1 
6323 C CG2 . VAL   B 155 ? 0.1335 0.1498 0.2753 -0.0060 -0.0129 0.0278  155 VAL   B CG2 
6333 N N   . PHE   B 156 ? 0.1227 0.1330 0.2288 0.0063  -0.0019 -0.0155 156 PHE   B N   
6334 C CA  . PHE   B 156 ? 0.1270 0.1407 0.2554 0.0062  -0.0029 -0.0169 156 PHE   B CA  
6335 C C   . PHE   B 156 ? 0.1268 0.1464 0.2803 0.0149  -0.0098 -0.0331 156 PHE   B C   
6336 O O   . PHE   B 156 ? 0.1516 0.1672 0.3000 0.0251  0.0010  -0.0381 156 PHE   B O   
6337 C CB  . PHE   B 156 ? 0.1332 0.1371 0.2635 0.0022  -0.0126 -0.0125 156 PHE   B CB  
6338 C CG  . PHE   B 156 ? 0.1388 0.1468 0.2758 -0.0016 -0.0163 0.0016  156 PHE   B CG  
6339 C CD1 . PHE   B 156 ? 0.1413 0.1732 0.3079 0.0068  -0.0078 0.0298  156 PHE   B CD1 
6340 C CD2 . PHE   B 156 ? 0.1444 0.1529 0.2685 0.0069  -0.0250 0.0022  156 PHE   B CD2 
6341 C CE1 . PHE   B 156 ? 0.1437 0.1862 0.3227 0.0065  -0.0069 0.0344  156 PHE   B CE1 
6342 C CE2 . PHE   B 156 ? 0.1509 0.1747 0.2932 0.0138  -0.0194 0.0128  156 PHE   B CE2 
6343 C CZ  . PHE   B 156 ? 0.1414 0.1823 0.3130 0.0150  -0.0196 0.0199  156 PHE   B CZ  
6353 N N   . ASP   B 157 ? 0.1322 0.1357 0.3035 0.0100  -0.0201 -0.0192 157 ASP   B N   
6354 C CA  . ASP   B 157 ? 0.1438 0.1430 0.3301 0.0051  -0.0261 -0.0254 157 ASP   B CA  
6355 C C   . ASP   B 157 ? 0.1427 0.1380 0.3382 0.0076  -0.0196 -0.0401 157 ASP   B C   
6356 O O   . ASP   B 157 ? 0.1352 0.1390 0.3173 0.0048  -0.0195 -0.0337 157 ASP   B O   
6357 C CB  . ASP   B 157 ? 0.1682 0.1579 0.3497 0.0011  -0.0485 -0.0109 157 ASP   B CB  
6358 C CG  . ASP   B 157 ? 0.1980 0.1692 0.3730 -0.0001 -0.0359 -0.0120 157 ASP   B CG  
6359 O OD1 . ASP   B 157 ? 0.2094 0.1650 0.3831 0.0112  -0.0263 -0.0087 157 ASP   B OD1 
6360 O OD2 . ASP   B 157 ? 0.2239 0.1947 0.4010 -0.0037 -0.0132 -0.0068 157 ASP   B OD2 
6365 N N   . LYS   B 158 ? 0.1416 0.1634 0.3475 0.0031  -0.0053 -0.0630 158 LYS   B N   
6366 C CA  . LYS   B 158 ? 0.1540 0.1797 0.3618 0.0031  -0.0011 -0.0734 158 LYS   B CA  
6367 C C   . LYS   B 158 ? 0.1547 0.1670 0.3677 0.0055  -0.0078 -0.0734 158 LYS   B C   
6368 O O   . LYS   B 158 ? 0.1587 0.1642 0.3711 -0.0054 -0.0055 -0.0831 158 LYS   B O   
6369 C CB  . LYS   B 158 ? 0.1782 0.2150 0.3606 0.0076  0.0101  -0.0979 158 LYS   B CB  
6370 C CG  . LYS   B 158 ? 0.2080 0.2539 0.3722 0.0122  0.0166  -0.1015 158 LYS   B CG  
6371 C CD  . LYS   B 158 ? 0.2334 0.2965 0.3857 0.0116  0.0222  -0.0963 158 LYS   B CD  
6372 C CE  . LYS   B 158 ? 0.2532 0.3257 0.4000 0.0121  0.0201  -0.0892 158 LYS   B CE  
6373 N NZ  . LYS   B 158 ? 0.2528 0.3372 0.3996 0.0113  0.0223  -0.0874 158 LYS   B NZ  
6387 N N   . ASN   B 159 ? 0.1585 0.1613 0.3866 0.0064  -0.0155 -0.0592 159 ASN   B N   
6388 C CA  . ASN   B 159 ? 0.1722 0.1517 0.4057 0.0189  -0.0281 -0.0478 159 ASN   B CA  
6389 C C   . ASN   B 159 ? 0.1586 0.1388 0.3951 0.0155  -0.0400 -0.0379 159 ASN   B C   
6390 O O   . ASN   B 159 ? 0.1638 0.1327 0.4128 0.0020  -0.0492 -0.0281 159 ASN   B O   
6391 C CB  . ASN   B 159 ? 0.1911 0.1598 0.4299 0.0278  -0.0372 -0.0425 159 ASN   B CB  
6392 C CG  . ASN   B 159 ? 0.2165 0.1768 0.4513 0.0262  -0.0485 -0.0551 159 ASN   B CG  
6393 O OD1 . ASN   B 159 ? 0.2309 0.1907 0.4570 0.0285  -0.0481 -0.0643 159 ASN   B OD1 
6394 N ND2 . ASN   B 159 ? 0.2228 0.1895 0.4679 0.0300  -0.0526 -0.0480 159 ASN   B ND2 
6401 N N   . LEU   B 160 ? 0.1470 0.1356 0.3678 0.0084  -0.0379 -0.0268 160 LEU   B N   
6402 C CA  . LEU   B 160 ? 0.1438 0.1411 0.3253 0.0083  -0.0320 -0.0162 160 LEU   B CA  
6403 C C   . LEU   B 160 ? 0.1394 0.1321 0.3156 -0.0038 -0.0200 -0.0319 160 LEU   B C   
6404 O O   . LEU   B 160 ? 0.1338 0.1343 0.3051 -0.0062 -0.0222 -0.0183 160 LEU   B O   
6405 C CB  . LEU   B 160 ? 0.1452 0.1519 0.3055 0.0059  -0.0339 -0.0101 160 LEU   B CB  
6406 C CG  . LEU   B 160 ? 0.1494 0.1628 0.2772 0.0106  -0.0293 -0.0008 160 LEU   B CG  
6407 C CD1 . LEU   B 160 ? 0.1576 0.1800 0.2793 0.0055  -0.0140 -0.0049 160 LEU   B CD1 
6408 C CD2 . LEU   B 160 ? 0.1503 0.1682 0.2758 0.0177  -0.0280 -0.0060 160 LEU   B CD2 
6420 N N   . TYR   B 161 ? 0.1362 0.1380 0.3132 -0.0069 -0.0033 -0.0374 161 TYR   B N   
6421 C CA  . TYR   B 161 ? 0.1444 0.1392 0.2960 -0.0147 0.0111  -0.0430 161 TYR   B CA  
6422 C C   . TYR   B 161 ? 0.1494 0.1374 0.2875 -0.0099 0.0097  -0.0389 161 TYR   B C   
6423 O O   . TYR   B 161 ? 0.1509 0.1354 0.2723 -0.0127 0.0025  -0.0397 161 TYR   B O   
6424 C CB  . TYR   B 161 ? 0.1588 0.1499 0.2953 -0.0228 0.0296  -0.0460 161 TYR   B CB  
6425 C CG  . TYR   B 161 ? 0.1799 0.1523 0.2897 -0.0268 0.0392  -0.0563 161 TYR   B CG  
6426 C CD1 . TYR   B 161 ? 0.1894 0.1494 0.2810 -0.0373 0.0334  -0.0551 161 TYR   B CD1 
6427 C CD2 . TYR   B 161 ? 0.2013 0.1586 0.2874 -0.0243 0.0339  -0.0539 161 TYR   B CD2 
6428 C CE1 . TYR   B 161 ? 0.2035 0.1683 0.2890 -0.0375 0.0300  -0.0525 161 TYR   B CE1 
6429 C CE2 . TYR   B 161 ? 0.2196 0.1760 0.2931 -0.0287 0.0313  -0.0455 161 TYR   B CE2 
6430 C CZ  . TYR   B 161 ? 0.2174 0.1797 0.2889 -0.0413 0.0274  -0.0383 161 TYR   B CZ  
6431 O OH  . TYR   B 161 ? 0.2421 0.2031 0.3045 -0.0448 0.0288  -0.0310 161 TYR   B OH  
6441 N N   . ASP   B 162 ? 0.1523 0.1349 0.3024 -0.0078 -0.0049 -0.0469 162 ASP   B N   
6442 C CA  . ASP   B 162 ? 0.1649 0.1439 0.3029 -0.0067 -0.0086 -0.0473 162 ASP   B CA  
6443 C C   . ASP   B 162 ? 0.1586 0.1303 0.2922 -0.0122 -0.0044 -0.0434 162 ASP   B C   
6444 O O   . ASP   B 162 ? 0.1669 0.1396 0.2935 -0.0184 -0.0123 -0.0308 162 ASP   B O   
6445 C CB  . ASP   B 162 ? 0.1849 0.1628 0.3266 0.0009  -0.0122 -0.0611 162 ASP   B CB  
6446 C CG  . ASP   B 162 ? 0.1870 0.1874 0.3438 0.0085  -0.0106 -0.0731 162 ASP   B CG  
6447 O OD1 . ASP   B 162 ? 0.1851 0.2050 0.3313 0.0039  0.0039  -0.0794 162 ASP   B OD1 
6448 O OD2 . ASP   B 162 ? 0.2044 0.2018 0.3767 0.0217  -0.0019 -0.0737 162 ASP   B OD2 
6453 N N   . LYS   B 163 ? 0.1574 0.1259 0.2902 -0.0142 -0.0174 -0.0318 163 LYS   B N   
6454 C CA  . LYS   B 163 ? 0.1682 0.1386 0.2937 -0.0210 -0.0152 -0.0128 163 LYS   B CA  
6455 C C   . LYS   B 163 ? 0.1416 0.1321 0.2832 -0.0175 -0.0152 -0.0104 163 LYS   B C   
6456 O O   . LYS   B 163 ? 0.1447 0.1387 0.3126 -0.0208 -0.0153 -0.0046 163 LYS   B O   
6457 C CB  . LYS   B 163 ? 0.2194 0.1726 0.3363 -0.0182 -0.0182 0.0070  163 LYS   B CB  
6458 C CG  . LYS   B 163 ? 0.2981 0.2541 0.4028 -0.0250 -0.0085 0.0145  163 LYS   B CG  
6459 C CD  . LYS   B 163 ? 0.3609 0.3263 0.4664 -0.0334 -0.0088 0.0119  163 LYS   B CD  
6460 C CE  . LYS   B 163 ? 0.4062 0.3717 0.5102 -0.0405 -0.0080 0.0129  163 LYS   B CE  
6461 N NZ  . LYS   B 163 ? 0.4361 0.4129 0.5379 -0.0442 -0.0069 0.0112  163 LYS   B NZ  
6475 N N   . LEU   B 164 ? 0.1311 0.1255 0.2610 -0.0121 -0.0133 -0.0047 164 LEU   B N   
6476 C CA  . LEU   B 164 ? 0.1320 0.1218 0.2485 -0.0102 -0.0192 -0.0041 164 LEU   B CA  
6477 C C   . LEU   B 164 ? 0.1394 0.1269 0.2470 -0.0091 -0.0259 -0.0034 164 LEU   B C   
6478 O O   . LEU   B 164 ? 0.1431 0.1454 0.2647 -0.0124 -0.0256 -0.0021 164 LEU   B O   
6479 C CB  . LEU   B 164 ? 0.1304 0.1240 0.2326 -0.0067 -0.0179 -0.0003 164 LEU   B CB  
6480 C CG  . LEU   B 164 ? 0.1401 0.1384 0.2454 -0.0083 -0.0094 0.0003  164 LEU   B CG  
6481 C CD1 . LEU   B 164 ? 0.1442 0.1375 0.2467 -0.0120 -0.0171 -0.0074 164 LEU   B CD1 
6482 C CD2 . LEU   B 164 ? 0.1586 0.1752 0.2527 -0.0061 -0.0001 -0.0186 164 LEU   B CD2 
6494 N N   . VAL   B 165 ? 0.1671 0.1370 0.2590 -0.0142 -0.0304 -0.0184 165 VAL   B N   
6495 C CA  . VAL   B 165 ? 0.1993 0.1470 0.2643 -0.0259 -0.0462 -0.0138 165 VAL   B CA  
6496 C C   . VAL   B 165 ? 0.2249 0.1549 0.2897 -0.0327 -0.0684 -0.0113 165 VAL   B C   
6497 O O   . VAL   B 165 ? 0.2388 0.1648 0.2931 -0.0352 -0.0669 -0.0029 165 VAL   B O   
6498 C CB  . VAL   B 165 ? 0.2183 0.1623 0.2631 -0.0123 -0.0163 -0.0229 165 VAL   B CB  
6499 C CG1 . VAL   B 165 ? 0.2361 0.1694 0.2854 -0.0142 -0.0062 -0.0259 165 VAL   B CG1 
6500 C CG2 . VAL   B 165 ? 0.2095 0.1738 0.2617 -0.0126 -0.0002 -0.0179 165 VAL   B CG2 
6510 N N   . SER   B 166 ? 0.2333 0.1462 0.3287 -0.0356 -0.0745 -0.0250 166 SER   B N   
6511 C CA  . SER   B 166 ? 0.2261 0.1453 0.3755 -0.0372 -0.0616 -0.0300 166 SER   B CA  
6512 C C   . SER   B 166 ? 0.2114 0.1556 0.3892 -0.0340 -0.0685 -0.0126 166 SER   B C   
6513 O O   . SER   B 166 ? 0.2138 0.1761 0.4194 -0.0411 -0.0848 -0.0307 166 SER   B O   
6514 C CB  . SER   B 166 ? 0.2295 0.1581 0.3980 -0.0258 -0.0529 -0.0358 166 SER   B CB  
6515 O OG  . SER   B 166 ? 0.2197 0.1547 0.4068 -0.0175 -0.0554 -0.0166 166 SER   B OG  
6521 N N   . SER   B 167 ? 0.1941 0.1516 0.3581 -0.0301 -0.0702 0.0228  167 SER   B N   
6522 C CA  . SER   B 167 ? 0.1860 0.1548 0.3409 -0.0337 -0.0520 0.0242  167 SER   B CA  
6523 C C   . SER   B 167 ? 0.1866 0.1676 0.3299 -0.0432 -0.0479 0.0396  167 SER   B C   
6524 O O   . SER   B 167 ? 0.1897 0.1766 0.3235 -0.0491 -0.0429 0.0389  167 SER   B O   
6525 C CB  . SER   B 167 ? 0.1762 0.1637 0.3334 -0.0279 -0.0238 0.0238  167 SER   B CB  
6526 O OG  . SER   B 167 ? 0.1729 0.1751 0.3236 -0.0161 -0.0091 0.0268  167 SER   B OG  
6532 N N   . PHE   B 168 ? 0.1829 0.1641 0.3223 -0.0391 -0.0354 0.0467  168 PHE   B N   
6533 C CA  . PHE   B 168 ? 0.1898 0.1599 0.2996 -0.0414 -0.0284 0.0337  168 PHE   B CA  
6534 C C   . PHE   B 168 ? 0.1632 0.1525 0.2570 -0.0223 -0.0111 0.0189  168 PHE   B C   
6535 O O   . PHE   B 168 ? 0.1922 0.1450 0.2555 0.0056  -0.0124 0.0020  168 PHE   B O   
6536 C CB  . PHE   B 168 ? 0.2045 0.1628 0.2990 -0.0507 -0.0471 0.0455  168 PHE   B CB  
6537 C CG  . PHE   B 168 ? 0.2293 0.1481 0.2931 -0.0537 -0.0558 0.0211  168 PHE   B CG  
6538 C CD1 . PHE   B 168 ? 0.2592 0.1558 0.3023 -0.0448 -0.0589 0.0159  168 PHE   B CD1 
6539 C CD2 . PHE   B 168 ? 0.2177 0.1476 0.2932 -0.0442 -0.0567 0.0267  168 PHE   B CD2 
6540 C CE1 . PHE   B 168 ? 0.2687 0.1672 0.3015 -0.0306 -0.0502 0.0199  168 PHE   B CE1 
6541 C CE2 . PHE   B 168 ? 0.2400 0.1581 0.2971 -0.0294 -0.0586 0.0230  168 PHE   B CE2 
6542 C CZ  . PHE   B 168 ? 0.2559 0.1531 0.3010 -0.0228 -0.0564 0.0271  168 PHE   B CZ  
6552 N N   . LEU   B 169 ? 0.1663 0.1685 0.2537 -0.0029 0.0026  -0.0001 169 LEU   B N   
6553 C CA  . LEU   B 169 ? 0.1890 0.1951 0.2877 -0.0096 -0.0020 -0.0204 169 LEU   B CA  
6554 C C   . LEU   B 169 ? 0.2154 0.2179 0.3361 0.0054  -0.0054 -0.0460 169 LEU   B C   
6555 O O   . LEU   B 169 ? 0.2330 0.2373 0.3870 0.0021  -0.0078 -0.0669 169 LEU   B O   
6556 C CB  . LEU   B 169 ? 0.2087 0.2322 0.3021 -0.0203 -0.0102 0.0038  169 LEU   B CB  
6557 C CG  . LEU   B 169 ? 0.2470 0.2671 0.3456 -0.0090 -0.0113 0.0089  169 LEU   B CG  
6558 C CD1 . LEU   B 169 ? 0.2620 0.2848 0.3542 -0.0076 -0.0151 0.0211  169 LEU   B CD1 
6559 C CD2 . LEU   B 169 ? 0.2475 0.2734 0.3525 0.0043  -0.0008 -0.0014 169 LEU   B CD2 
6560 O OXT . LEU   B 169 ? 0.2351 0.2331 0.3328 0.0337  0.0035  -0.0512 169 LEU   B OXT 
6572 S S   B DMS   C .   ? 0.2740 0.2380 0.2662 0.0032  0.0110  -0.0012 401 DMS   A S   
6573 O O   B DMS   C .   ? 0.2726 0.2384 0.2646 0.0016  0.0102  -0.0010 401 DMS   A O   
6574 C C1  B DMS   C .   ? 0.2728 0.2387 0.2686 0.0033  0.0104  -0.0035 401 DMS   A C1  
6575 C C2  B DMS   C .   ? 0.2738 0.2386 0.2690 0.0047  0.0118  -0.0024 401 DMS   A C2  
6582 O O1  B A1A77 D .   ? 0.1876 0.1908 0.1975 0.0016  0.0071  -0.0044 402 A1A77 A O1  
6583 C C1  B A1A77 D .   ? 0.1823 0.1939 0.1877 0.0014  0.0088  -0.0050 402 A1A77 A C1  
6584 C C2  B A1A77 D .   ? 0.1816 0.1944 0.1891 0.0007  0.0093  -0.0047 402 A1A77 A C2  
6585 C C3  B A1A77 D .   ? 0.1800 0.1920 0.1866 0.0024  0.0088  -0.0011 402 A1A77 A C3  
6586 C C4  B A1A77 D .   ? 0.1679 0.1875 0.1775 -0.0001 0.0089  0.0038  402 A1A77 A C4  
6587 C C5  B A1A77 D .   ? 0.1645 0.1869 0.1750 -0.0020 0.0121  0.0063  402 A1A77 A C5  
6588 C C6  B A1A77 D .   ? 0.1571 0.1831 0.1659 -0.0022 0.0101  0.0082  402 A1A77 A C6  
6589 C C7  B A1A77 D .   ? 0.1599 0.1843 0.1686 -0.0013 0.0086  0.0070  402 A1A77 A C7  
6590 C C8  B A1A77 D .   ? 0.1560 0.1837 0.1664 -0.0025 0.0076  0.0080  402 A1A77 A C8  
6591 C C10 B A1A77 D .   ? 0.1816 0.1937 0.1908 0.0033  0.0063  -0.0022 402 A1A77 A C10 
6592 C C11 B A1A77 D .   ? 0.1850 0.1924 0.1947 0.0018  0.0078  -0.0030 402 A1A77 A C11 
6593 C C12 B A1A77 D .   ? 0.1832 0.1951 0.1919 0.0041  0.0054  -0.0029 402 A1A77 A C12 
6594 C C9  B A1A77 D .   ? 0.1501 0.1818 0.1649 -0.0033 0.0072  0.0107  402 A1A77 A C9  
6595 N N1  B A1A77 D .   ? 0.1767 0.1915 0.1848 0.0026  0.0081  -0.0001 402 A1A77 A N1  
6596 N N2  B A1A77 D .   ? 0.1667 0.1874 0.1780 -0.0019 0.0125  0.0052  402 A1A77 A N2  
6597 N N3  B A1A77 D .   ? 0.1610 0.1853 0.1699 -0.0025 0.0129  0.0079  402 A1A77 A N3  
6598 N N4  B A1A77 D .   ? 0.1516 0.1812 0.1626 -0.0019 0.0078  0.0095  402 A1A77 A N4  
6599 N N5  B A1A77 D .   ? 0.1824 0.1942 0.1896 0.0016  0.0081  -0.0042 402 A1A77 A N5  
6618 O O1  C A1A77 E .   ? 0.1907 0.1989 0.2060 -0.0105 0.0130  0.0044  403 A1A77 A O1  
6619 C C1  C A1A77 E .   ? 0.1829 0.1940 0.1905 -0.0140 0.0117  -0.0086 403 A1A77 A C1  
6620 C C2  C A1A77 E .   ? 0.1830 0.1943 0.1936 -0.0138 0.0141  -0.0072 403 A1A77 A C2  
6621 C C3  C A1A77 E .   ? 0.1811 0.1927 0.1907 -0.0111 0.0135  -0.0040 403 A1A77 A C3  
6622 C C4  C A1A77 E .   ? 0.1678 0.1876 0.1784 -0.0083 0.0113  0.0046  403 A1A77 A C4  
6623 C C5  C A1A77 E .   ? 0.1636 0.1860 0.1745 -0.0094 0.0135  0.0078  403 A1A77 A C5  
6624 C C6  C A1A77 E .   ? 0.1565 0.1822 0.1658 -0.0080 0.0116  0.0097  403 A1A77 A C6  
6625 C C7  C A1A77 E .   ? 0.1595 0.1838 0.1688 -0.0074 0.0106  0.0089  403 A1A77 A C7  
6626 C C8  C A1A77 E .   ? 0.1551 0.1830 0.1656 -0.0070 0.0095  0.0102  403 A1A77 A C8  
6627 C C10 C A1A77 E .   ? 0.1823 0.1950 0.1960 -0.0099 0.0120  -0.0029 403 A1A77 A C10 
6628 C C11 C A1A77 E .   ? 0.1866 0.1964 0.2014 -0.0099 0.0129  0.0013  403 A1A77 A C11 
6629 C C12 C A1A77 E .   ? 0.1825 0.1953 0.1968 -0.0118 0.0120  -0.0061 403 A1A77 A C12 
6630 C C9  C A1A77 E .   ? 0.1495 0.1814 0.1640 -0.0075 0.0091  0.0125  403 A1A77 A C9  
6631 N N1  C A1A77 E .   ? 0.1772 0.1922 0.1885 -0.0091 0.0123  -0.0021 403 A1A77 A N1  
6632 N N2  C A1A77 E .   ? 0.1657 0.1868 0.1775 -0.0101 0.0139  0.0072  403 A1A77 A N2  
6633 N N3  C A1A77 E .   ? 0.1600 0.1844 0.1697 -0.0091 0.0143  0.0092  403 A1A77 A N3  
6634 N N4  C A1A77 E .   ? 0.1510 0.1803 0.1620 -0.0068 0.0091  0.0112  403 A1A77 A N4  
6635 N N5  C A1A77 E .   ? 0.1825 0.1943 0.1937 -0.0138 0.0128  -0.0071 403 A1A77 A N5  
6654 O O   . HOH   F .   ? 0.1440 0.4049 0.2626 -0.0131 0.0161  0.0823  501 HOH   A O   
6655 O O   . HOH   F .   ? 0.2068 0.1686 0.2138 0.0210  -0.0260 0.0016  502 HOH   A O   
6656 O O   . HOH   F .   ? 0.4475 0.2279 0.3708 -0.0343 -0.0255 0.0504  503 HOH   A O   
6657 O O   . HOH   F .   ? 0.4028 0.3150 0.5334 -0.0148 0.1526  -0.0483 504 HOH   A O   
6658 O O   . HOH   F .   ? 0.3901 0.6841 0.4617 -0.1023 0.0552  0.0375  505 HOH   A O   
6659 O O   . HOH   F .   ? 0.5157 0.3091 0.2976 -0.1167 0.0596  0.0808  506 HOH   A O   
6660 O O   . HOH   F .   ? 0.2946 0.6309 0.5476 0.0042  -0.0707 0.1596  507 HOH   A O   
6661 O O   . HOH   F .   ? 0.5871 0.4681 0.3458 0.1902  -0.1128 0.0576  508 HOH   A O   
6662 O O   . HOH   F .   ? 0.4786 0.3360 0.4781 -0.0454 0.1422  0.0913  509 HOH   A O   
6663 O O   . HOH   F .   ? 0.2191 0.2092 0.2771 0.0039  -0.0507 0.0306  510 HOH   A O   
6664 O O   . HOH   F .   ? 0.2400 0.2274 0.3244 -0.0214 0.0545  0.0691  511 HOH   A O   
6665 O O   . HOH   F .   ? 0.1979 0.1567 0.1527 -0.0031 0.0176  0.0171  512 HOH   A O   
6666 O O   . HOH   F .   ? 0.2068 0.1762 0.3279 -0.0055 -0.0585 -0.0300 513 HOH   A O   
6667 O O   . HOH   F .   ? 0.2937 0.3201 0.1706 -0.0432 0.0409  0.0629  514 HOH   A O   
6668 O O   . HOH   F .   ? 0.2026 0.1800 0.3570 -0.0461 0.0059  -0.0231 515 HOH   A O   
6669 O O   . HOH   F .   ? 0.3966 0.3258 0.3372 -0.0387 0.1738  0.0026  516 HOH   A O   
6670 O O   . HOH   F .   ? 0.5483 0.4853 0.5096 0.0140  0.0626  0.2375  517 HOH   A O   
6671 O O   . HOH   F .   ? 0.7377 0.3833 0.5443 -0.0509 -0.1306 0.0444  518 HOH   A O   
6672 O O   . HOH   F .   ? 0.1824 0.3406 0.4197 -0.0296 0.0253  -0.1075 519 HOH   A O   
6673 O O   . HOH   F .   ? 0.6544 0.5889 0.3300 -0.0336 -0.0012 0.1304  520 HOH   A O   
6674 O O   . HOH   F .   ? 0.1699 0.2926 0.2850 0.0357  -0.0151 -0.0209 521 HOH   A O   
6675 O O   . HOH   F .   ? 0.2563 0.2281 0.2478 0.0672  0.0408  0.0505  522 HOH   A O   
6676 O O   . HOH   F .   ? 0.1636 0.2503 0.3813 -0.0099 0.0721  0.0653  523 HOH   A O   
6677 O O   . HOH   F .   ? 0.3089 0.4466 0.2452 -0.0175 0.0579  0.0408  524 HOH   A O   
6678 O O   . HOH   F .   ? 0.1451 0.1495 0.2085 -0.0224 0.0047  0.0032  525 HOH   A O   
6679 O O   . HOH   F .   ? 0.2904 0.2552 0.2588 -0.0701 0.0418  0.0420  526 HOH   A O   
6680 O O   . HOH   F .   ? 0.6267 0.4788 0.4570 -0.1174 0.1756  0.1703  527 HOH   A O   
6681 O O   . HOH   F .   ? 0.2608 0.2353 0.4118 -0.0386 -0.0929 0.0948  528 HOH   A O   
6682 O O   . HOH   F .   ? 0.2080 0.4355 0.3931 -0.0201 -0.0468 0.1708  529 HOH   A O   
6683 O O   . HOH   F .   ? 0.3810 0.1999 0.4610 0.0203  -0.1425 0.0630  530 HOH   A O   
6684 O O   . HOH   F .   ? 0.3001 0.4139 0.3111 0.1200  -0.0642 -0.1299 531 HOH   A O   
6685 O O   . HOH   F .   ? 0.2981 0.4915 0.5244 -0.0423 0.1146  0.2153  532 HOH   A O   
6686 O O   . HOH   F .   ? 0.5382 0.5845 0.3915 -0.1135 -0.1070 -0.0711 533 HOH   A O   
6687 O O   . HOH   F .   ? 0.4579 0.5441 0.2776 -0.0988 0.1213  0.0871  534 HOH   A O   
6688 O O   . HOH   F .   ? 0.4116 0.3530 0.3573 -0.0691 -0.0630 -0.0403 535 HOH   A O   
6689 O O   . HOH   F .   ? 0.2490 0.5294 0.4222 -0.0284 -0.0667 0.0920  536 HOH   A O   
6690 O O   . HOH   F .   ? 0.2102 0.2248 0.4039 0.0161  -0.0571 -0.0502 537 HOH   A O   
6691 O O   . HOH   F .   ? 0.6397 0.4793 0.5015 0.0895  0.2623  -0.0918 538 HOH   A O   
6692 O O   . HOH   F .   ? 0.5269 0.1918 0.4580 0.0814  0.0123  0.0069  539 HOH   A O   
6693 O O   . HOH   F .   ? 0.3141 0.3800 0.4543 0.1149  -0.0084 0.0540  540 HOH   A O   
6694 O O   . HOH   F .   ? 0.5961 0.4395 0.4613 -0.0184 -0.0690 -0.0879 541 HOH   A O   
6695 O O   . HOH   F .   ? 0.3049 0.3816 0.3716 -0.1035 -0.0830 -0.0289 542 HOH   A O   
6696 O O   . HOH   F .   ? 0.1426 0.2114 0.2202 0.0055  -0.0092 0.0523  543 HOH   A O   
6697 O O   A HOH   F .   ? 0.3540 0.1470 0.1779 0.0341  0.0351  0.0216  544 HOH   A O   
6698 O O   . HOH   F .   ? 0.4570 0.4239 0.4105 -0.1764 -0.0626 0.2045  545 HOH   A O   
6699 O O   . HOH   F .   ? 0.2600 0.4195 0.3189 -0.0556 0.0563  -0.0140 546 HOH   A O   
6700 O O   . HOH   F .   ? 0.1881 0.1950 0.3658 0.0173  0.0892  -0.0122 547 HOH   A O   
6701 O O   . HOH   F .   ? 0.2527 0.1915 0.2350 -0.0409 0.0012  -0.0071 548 HOH   A O   
6702 O O   . HOH   F .   ? 0.4676 0.4749 0.4794 0.1671  0.1717  -0.0228 549 HOH   A O   
6703 O O   . HOH   F .   ? 0.3607 0.4476 0.3744 0.2064  0.0541  0.0361  550 HOH   A O   
6704 O O   . HOH   F .   ? 0.5684 0.3943 0.2985 0.0410  0.1016  0.1338  551 HOH   A O   
6705 O O   . HOH   F .   ? 0.2340 0.3868 0.3816 0.0820  -0.0774 -0.0244 552 HOH   A O   
6706 O O   . HOH   F .   ? 0.1403 0.1702 0.2695 0.0044  -0.0254 -0.0512 553 HOH   A O   
6707 O O   A HOH   F .   ? 0.2141 0.3976 0.2301 0.0833  0.0225  0.0073  554 HOH   A O   
6708 O O   . HOH   F .   ? 0.1288 0.1239 0.1317 -0.0022 0.0149  0.0100  555 HOH   A O   
6709 O O   A HOH   F .   ? 0.6005 0.3337 0.5412 -0.0054 -0.0976 0.0724  556 HOH   A O   
6710 O O   . HOH   F .   ? 0.3833 0.6461 0.3922 -0.1071 -0.0162 0.1242  557 HOH   A O   
6711 O O   . HOH   F .   ? 0.1464 0.1830 0.2440 0.0108  -0.0128 0.0062  558 HOH   A O   
6712 O O   A HOH   F .   ? 0.1627 0.2519 0.2545 0.0588  0.0532  0.0838  559 HOH   A O   
6713 O O   . HOH   F .   ? 0.3870 0.2015 0.2071 0.1056  0.0442  0.0088  560 HOH   A O   
6714 O O   . HOH   F .   ? 0.1874 0.1863 0.2267 -0.0362 0.0114  0.0281  561 HOH   A O   
6715 O O   . HOH   F .   ? 0.1496 0.1273 0.2166 -0.0092 0.0226  -0.0102 562 HOH   A O   
6716 O O   . HOH   F .   ? 0.2912 0.3401 0.2245 -0.0672 -0.0234 -0.0765 563 HOH   A O   
6717 O O   . HOH   F .   ? 0.1672 0.1585 0.2113 0.0148  -0.0190 0.0249  564 HOH   A O   
6718 O O   . HOH   F .   ? 0.4906 0.2937 0.4168 -0.1813 0.1794  -0.0740 565 HOH   A O   
6719 O O   . HOH   F .   ? 0.2783 0.4162 0.2894 0.0503  0.0850  0.1717  566 HOH   A O   
6720 O O   . HOH   F .   ? 0.3854 0.6958 0.4845 -0.0749 -0.1402 0.0118  567 HOH   A O   
6721 O O   . HOH   F .   ? 0.1983 0.2066 0.1977 -0.0180 -0.0323 0.0275  568 HOH   A O   
6722 O O   . HOH   F .   ? 0.3698 0.2195 0.4295 -0.1078 0.0752  0.0204  569 HOH   A O   
6723 O O   . HOH   F .   ? 0.3061 0.2238 0.4893 -0.0658 -0.0282 -0.0030 570 HOH   A O   
6724 O O   . HOH   F .   ? 0.1381 0.1434 0.1526 -0.0095 -0.0072 -0.0017 571 HOH   A O   
6725 O O   . HOH   F .   ? 0.2880 0.3432 0.4945 -0.0779 -0.0953 -0.0935 572 HOH   A O   
6726 O O   . HOH   F .   ? 0.1799 0.2280 0.3507 0.0185  0.0731  -0.0621 573 HOH   A O   
6727 O O   . HOH   F .   ? 0.3728 0.2943 0.3563 -0.1103 -0.0211 -0.0198 574 HOH   A O   
6728 O O   . HOH   F .   ? 0.1387 0.1733 0.1724 0.0096  -0.0233 -0.0313 575 HOH   A O   
6729 O O   . HOH   F .   ? 0.1627 0.1630 0.2073 -0.0163 0.0153  0.0274  576 HOH   A O   
6730 O O   . HOH   F .   ? 0.2541 0.1844 0.1797 -0.0577 0.0325  0.0121  577 HOH   A O   
6731 O O   . HOH   F .   ? 0.5105 0.6471 0.3745 0.1883  -0.0327 -0.0434 578 HOH   A O   
6732 O O   . HOH   F .   ? 0.1840 0.1754 0.1720 0.0024  0.0019  0.0164  579 HOH   A O   
6733 O O   . HOH   F .   ? 0.1574 0.1499 0.1889 -0.0008 -0.0196 0.0073  580 HOH   A O   
6734 O O   A HOH   F .   ? 0.2743 0.5011 0.5669 0.0992  0.0517  0.1144  581 HOH   A O   
6735 O O   . HOH   F .   ? 0.3012 0.2933 0.2051 0.0195  0.0817  0.0041  582 HOH   A O   
6736 O O   . HOH   F .   ? 0.7234 0.4172 0.6990 -0.1394 0.0903  -0.0073 583 HOH   A O   
6737 O O   . HOH   F .   ? 0.2108 0.3688 0.3637 -0.0353 -0.0142 0.0787  584 HOH   A O   
6738 O O   . HOH   F .   ? 0.5167 0.4769 0.5250 -0.1205 -0.0436 0.0833  585 HOH   A O   
6739 O O   . HOH   F .   ? 0.3064 0.2216 0.3288 -0.0076 -0.0399 0.0801  586 HOH   A O   
6740 O O   . HOH   F .   ? 0.2639 0.2617 0.4018 -0.0791 0.1159  -0.0277 587 HOH   A O   
6741 O O   . HOH   F .   ? 0.2948 0.6143 0.3636 0.0835  0.0847  -0.1210 588 HOH   A O   
6742 O O   A HOH   F .   ? 0.2320 0.2170 0.2352 0.0157  0.0058  0.0737  589 HOH   A O   
6743 O O   . HOH   F .   ? 0.6321 0.5947 0.5236 -0.0229 0.0039  0.0012  590 HOH   A O   
6744 O O   . HOH   F .   ? 0.3991 0.4149 0.2514 0.0055  -0.1220 0.0213  591 HOH   A O   
6745 O O   . HOH   F .   ? 0.1675 0.2176 0.1866 -0.0101 0.0033  0.0652  592 HOH   A O   
6746 O O   . HOH   F .   ? 0.2921 0.2480 0.2086 -0.0570 -0.0690 0.0233  593 HOH   A O   
6747 O O   . HOH   F .   ? 0.4959 0.4665 0.1901 0.0044  0.0942  0.0864  594 HOH   A O   
6748 O O   B HOH   F .   ? 0.1612 0.2118 0.1399 0.0180  0.0118  0.0403  595 HOH   A O   
6749 O O   . HOH   F .   ? 0.1292 0.1370 0.1731 0.0028  -0.0145 0.0046  596 HOH   A O   
6750 O O   . HOH   F .   ? 0.2504 0.3801 0.3547 -0.0373 0.1040  -0.0882 597 HOH   A O   
6751 O O   . HOH   F .   ? 0.3232 0.8339 0.3272 0.0463  0.1137  0.0149  598 HOH   A O   
6752 O O   . HOH   F .   ? 0.1776 0.1795 0.3750 0.0384  0.1082  0.0947  599 HOH   A O   
6753 O O   . HOH   F .   ? 0.4848 0.6445 0.5130 0.1376  0.0194  0.1925  600 HOH   A O   
6754 O O   . HOH   F .   ? 0.2012 0.1604 0.2635 0.0034  -0.0224 0.0040  601 HOH   A O   
6755 O O   . HOH   F .   ? 0.1691 0.1337 0.1607 -0.0207 0.0112  0.0025  602 HOH   A O   
6756 O O   A HOH   F .   ? 0.3175 0.2161 0.4686 -0.0715 0.1326  -0.0195 603 HOH   A O   
6757 O O   . HOH   F .   ? 0.5960 0.7095 0.6434 0.0630  -0.0230 0.0283  604 HOH   A O   
6758 O O   . HOH   F .   ? 0.2378 0.1694 0.2413 -0.0082 0.0084  0.0206  605 HOH   A O   
6759 O O   . HOH   F .   ? 0.1845 0.1957 0.2465 -0.0088 -0.0105 0.0713  606 HOH   A O   
6760 O O   . HOH   F .   ? 0.3953 0.3729 0.4865 0.1339  0.0865  -0.0823 607 HOH   A O   
6761 O O   . HOH   F .   ? 0.2501 0.2104 0.2329 -0.0602 0.0046  0.0523  608 HOH   A O   
6762 O O   . HOH   F .   ? 0.4388 0.6089 0.3513 -0.0625 -0.0096 0.1349  609 HOH   A O   
6763 O O   . HOH   F .   ? 0.1897 0.2428 0.3485 -0.0144 -0.0207 0.0133  610 HOH   A O   
6764 O O   . HOH   F .   ? 0.1654 0.1688 0.2470 0.0192  -0.0296 0.0298  611 HOH   A O   
6765 O O   . HOH   F .   ? 0.1433 0.1611 0.2611 -0.0044 0.0026  0.0117  612 HOH   A O   
6766 O O   . HOH   F .   ? 0.2602 0.3080 0.3510 -0.0244 0.1086  -0.0226 613 HOH   A O   
6767 O O   . HOH   F .   ? 0.3088 0.3536 0.6928 -0.0207 0.1136  -0.0393 614 HOH   A O   
6768 O O   . HOH   F .   ? 0.2984 0.3442 0.5279 -0.0087 0.1235  -0.0277 615 HOH   A O   
6769 O O   . HOH   F .   ? 0.2049 0.2639 0.2365 -0.0078 -0.0539 0.0426  616 HOH   A O   
6770 O O   A HOH   F .   ? 0.4312 0.2767 0.3544 0.0653  -0.0764 -0.0404 617 HOH   A O   
6771 O O   . HOH   F .   ? 0.5313 0.4648 0.3249 -0.0166 -0.1299 0.0288  618 HOH   A O   
6772 O O   . HOH   F .   ? 0.3332 0.1289 0.2034 0.0005  -0.0607 0.0057  619 HOH   A O   
6773 O O   . HOH   F .   ? 0.6402 0.3927 0.4925 0.2059  -0.0589 0.1431  620 HOH   A O   
6774 O O   . HOH   F .   ? 0.2144 0.4073 0.2460 0.1432  -0.0088 0.0050  621 HOH   A O   
6775 O O   . HOH   F .   ? 0.4313 0.2233 0.4740 -0.0786 -0.2173 0.0978  622 HOH   A O   
6776 O O   . HOH   F .   ? 0.2720 0.5775 0.1707 -0.0707 0.0488  0.0038  623 HOH   A O   
6777 O O   A HOH   F .   ? 0.3441 0.2454 0.3316 0.0396  0.0810  0.1161  624 HOH   A O   
6778 O O   . HOH   F .   ? 0.3951 0.2680 0.2513 -0.0419 -0.0177 0.0161  625 HOH   A O   
6779 O O   A HOH   F .   ? 0.6406 0.5096 0.3484 -0.0886 0.0470  0.1826  626 HOH   A O   
6780 O O   . HOH   F .   ? 0.2596 0.2794 0.2824 -0.0004 -0.0109 -0.0483 627 HOH   A O   
6781 O O   . HOH   F .   ? 0.3669 0.2757 0.5604 0.0856  0.1038  0.0513  628 HOH   A O   
6782 O O   . HOH   F .   ? 0.5786 0.5831 0.5461 -0.1173 -0.0812 -0.1067 629 HOH   A O   
6783 O O   . HOH   F .   ? 0.4952 0.6455 0.3836 0.0694  0.2195  -0.0812 630 HOH   A O   
6784 O O   . HOH   F .   ? 0.1550 0.2120 0.2945 -0.0220 -0.0073 0.0550  631 HOH   A O   
6785 O O   . HOH   F .   ? 0.5092 0.5520 0.6255 -0.1578 0.0160  -0.0976 632 HOH   A O   
6786 O O   . HOH   F .   ? 0.1760 0.2018 0.5267 -0.0236 -0.0811 0.0592  633 HOH   A O   
6787 O O   . HOH   F .   ? 0.8833 0.9176 0.7369 -0.0678 0.0270  -0.0404 634 HOH   A O   
6788 O O   . HOH   F .   ? 0.5944 0.6353 0.5714 0.0860  -0.1195 0.0673  635 HOH   A O   
6789 O O   A HOH   F .   ? 0.1711 0.1350 0.1460 -0.0079 0.0006  0.0051  636 HOH   A O   
6790 O O   . HOH   F .   ? 0.3683 0.2463 0.1613 -0.0833 0.0436  0.0382  637 HOH   A O   
6791 O O   A HOH   F .   ? 0.1988 0.1594 0.2218 0.0192  -0.0513 -0.0194 638 HOH   A O   
6792 O O   A HOH   F .   ? 0.5207 0.4225 0.5976 0.1157  0.0294  -0.0809 639 HOH   A O   
6793 O O   . HOH   F .   ? 0.2435 0.1550 0.2446 -0.0010 0.0101  0.0056  640 HOH   A O   
6794 O O   . HOH   F .   ? 0.6667 0.6897 0.4177 0.2245  -0.0792 0.1635  641 HOH   A O   
6795 O O   . HOH   F .   ? 0.4175 0.3297 0.2964 0.2148  -0.0444 -0.0488 642 HOH   A O   
6796 O O   . HOH   F .   ? 0.4340 0.4085 0.4796 -0.0980 -0.1075 -0.1154 643 HOH   A O   
6797 O O   . HOH   F .   ? 0.5535 0.4855 0.7008 0.0936  -0.1269 0.1175  644 HOH   A O   
6798 O O   . HOH   F .   ? 0.2314 0.1978 0.2438 0.0145  0.0280  0.0196  645 HOH   A O   
6799 O O   . HOH   F .   ? 0.2703 0.2702 0.5221 0.0065  0.0997  -0.0810 646 HOH   A O   
6800 O O   . HOH   F .   ? 0.2091 0.2523 0.2255 0.0013  -0.0132 -0.0514 647 HOH   A O   
6801 O O   A HOH   F .   ? 0.2948 0.1901 0.3899 0.0476  0.1360  0.1008  648 HOH   A O   
6802 O O   . HOH   F .   ? 0.5326 0.3434 0.3872 -0.0097 0.0442  0.1059  649 HOH   A O   
6803 O O   B HOH   F .   ? 0.1482 0.1122 0.1411 -0.0651 0.0357  -0.0464 650 HOH   A O   
6804 O O   . HOH   F .   ? 0.2503 0.2921 0.3459 0.0589  -0.0192 0.0511  651 HOH   A O   
6805 O O   . HOH   F .   ? 0.4657 0.4337 0.4138 -0.0008 -0.0210 0.0923  652 HOH   A O   
6806 O O   . HOH   F .   ? 0.6555 0.5775 0.4810 -0.0635 0.1552  0.0928  653 HOH   A O   
6807 O O   . HOH   F .   ? 0.5084 0.3425 0.4933 0.0499  0.0790  0.0376  654 HOH   A O   
6808 O O   . HOH   F .   ? 0.3122 0.2803 0.3235 -0.0746 0.0111  -0.0689 655 HOH   A O   
6809 O O   . HOH   F .   ? 0.6654 0.7607 0.4614 -0.0255 -0.0719 0.0032  656 HOH   A O   
6810 O O   . HOH   F .   ? 0.3294 0.5125 0.4736 0.0778  -0.0840 0.1586  657 HOH   A O   
6811 O O   . HOH   F .   ? 0.2900 0.5381 0.5195 -0.1549 0.0706  -0.1440 658 HOH   A O   
6812 O O   B HOH   F .   ? 0.0952 0.1144 0.1316 -0.0292 0.0284  -0.0214 659 HOH   A O   
6813 O O   . HOH   F .   ? 0.2770 0.1725 0.2476 0.0353  -0.0861 -0.0242 660 HOH   A O   
6814 O O   . HOH   F .   ? 0.3086 0.4082 0.3558 -0.0544 -0.0519 0.0151  661 HOH   A O   
6815 O O   . HOH   F .   ? 0.2435 0.2601 0.3161 -0.0810 0.0448  -0.0333 662 HOH   A O   
6816 O O   . HOH   F .   ? 0.4038 0.5955 0.3585 -0.0950 -0.0839 0.2080  663 HOH   A O   
6817 O O   . HOH   F .   ? 0.2849 0.3865 0.5409 0.0559  0.0396  -0.1719 664 HOH   A O   
6818 O O   . HOH   F .   ? 0.5796 0.4753 0.4413 0.0557  0.1121  0.0611  665 HOH   A O   
6819 O O   . HOH   F .   ? 0.2734 0.2464 0.5607 0.0543  -0.1266 -0.0334 666 HOH   A O   
6820 O O   . HOH   F .   ? 0.6279 0.3252 0.7302 0.0528  0.0387  0.2123  667 HOH   A O   
6821 O O   . HOH   F .   ? 0.6829 0.4759 0.5430 0.1862  0.2859  0.2210  668 HOH   A O   
6822 O O   . HOH   F .   ? 0.2715 0.2463 0.3593 0.0088  0.0548  -0.0077 669 HOH   A O   
6823 O O   . HOH   F .   ? 0.3018 0.4547 0.3320 -0.0417 -0.0225 -0.0668 670 HOH   A O   
6824 O O   . HOH   F .   ? 0.4122 0.5092 0.3631 0.0147  -0.0559 -0.0529 671 HOH   A O   
6825 O O   . HOH   F .   ? 0.4048 0.4368 0.3341 -0.0571 -0.0316 -0.0231 672 HOH   A O   
6826 O O   . HOH   F .   ? 0.5198 0.6496 0.5351 -0.1569 -0.1010 0.0978  673 HOH   A O   
6827 O O   . HOH   F .   ? 0.3936 0.4165 0.4624 -0.1973 0.0026  -0.0050 674 HOH   A O   
6828 O O   . HOH   F .   ? 0.5807 0.5292 0.4822 0.1453  -0.1197 -0.0979 675 HOH   A O   
6829 O O   . HOH   F .   ? 0.5444 0.5612 0.6358 0.0993  0.1554  -0.1122 676 HOH   A O   
6830 O O   . HOH   F .   ? 0.6649 0.5027 0.5919 -0.0807 0.0905  -0.0659 677 HOH   A O   
6831 O O   . HOH   F .   ? 0.2257 0.2174 0.2571 0.0221  0.0103  0.0101  678 HOH   A O   
6832 O O   . HOH   F .   ? 0.5057 0.4139 0.3567 0.0502  0.0585  -0.1283 679 HOH   A O   
6833 O O   . HOH   F .   ? 0.7203 0.3760 0.3110 -0.0483 -0.1110 -0.0012 680 HOH   A O   
6834 O O   . HOH   F .   ? 0.4213 0.2445 0.3392 -0.0567 -0.1247 0.0630  681 HOH   A O   
6835 O O   . HOH   F .   ? 0.6484 0.3776 0.4510 -0.0529 0.2174  -0.0198 682 HOH   A O   
6836 O O   . HOH   F .   ? 0.4220 0.5372 0.2612 -0.0383 0.0152  0.0493  683 HOH   A O   
6837 O O   . HOH   F .   ? 0.6047 0.2571 0.4681 -0.0860 0.0294  0.0811  684 HOH   A O   
6838 O O   . HOH   F .   ? 0.2840 0.5003 0.3590 0.1039  0.1109  0.2256  685 HOH   A O   
6839 O O   . HOH   F .   ? 0.3655 0.3485 0.2481 -0.0577 0.1069  -0.0317 686 HOH   A O   
6840 O O   . HOH   F .   ? 0.2912 0.4544 0.4524 0.0531  0.1329  0.1450  687 HOH   A O   
6841 O O   . HOH   F .   ? 0.5485 0.6470 0.4485 -0.0609 0.1552  0.1071  688 HOH   A O   
6842 O O   . HOH   F .   ? 0.6433 0.4706 0.5102 -0.0628 -0.1033 -0.0780 689 HOH   A O   
6843 O O   . HOH   F .   ? 0.5583 0.5609 0.5449 -0.0876 -0.1255 0.0422  690 HOH   A O   
6844 O O   . HOH   F .   ? 0.2517 0.2573 0.6758 -0.0125 -0.1238 0.0403  691 HOH   A O   
6845 O O   . HOH   F .   ? 0.4747 0.3231 0.4642 -0.0318 0.2422  0.0246  692 HOH   A O   
6846 O O   . HOH   F .   ? 0.2873 0.1980 0.5538 0.0136  0.0658  0.0792  693 HOH   A O   
6847 O O   . HOH   F .   ? 0.4117 0.2715 0.4364 -0.1053 0.0806  0.0464  694 HOH   A O   
6848 O O   . HOH   F .   ? 0.2428 0.2821 0.4826 -0.0116 0.1025  -0.0667 695 HOH   A O   
6849 O O   . HOH   F .   ? 0.5255 0.5510 0.4350 0.1081  -0.1358 0.0524  696 HOH   A O   
6850 O O   . HOH   F .   ? 0.3695 0.8851 0.5193 -0.1092 -0.0204 0.2942  697 HOH   A O   
6851 O O   . HOH   F .   ? 0.2543 0.3140 0.3532 0.0605  -0.0716 0.0440  698 HOH   A O   
6852 O O   . HOH   F .   ? 0.4371 0.2441 0.4238 -0.1261 0.0141  0.0230  699 HOH   A O   
6853 O O   . HOH   F .   ? 0.3074 0.4051 0.4002 0.0955  -0.0061 0.0383  700 HOH   A O   
6854 O O   . HOH   F .   ? 0.5109 0.6644 0.4914 0.1145  -0.0576 0.0832  701 HOH   A O   
6855 O O   . HOH   F .   ? 0.6945 0.4746 0.5649 0.0290  -0.0168 0.0768  702 HOH   A O   
6856 O O   . HOH   F .   ? 0.2915 0.2296 0.4226 -0.0004 0.0298  0.0575  703 HOH   A O   
6857 O O   . HOH   F .   ? 0.4496 0.7000 0.4617 0.2956  -0.0062 0.1195  704 HOH   A O   
6858 O O   . HOH   F .   ? 0.2597 0.6495 0.3814 0.0565  0.0381  0.0065  705 HOH   A O   
6859 O O   . HOH   F .   ? 0.5565 0.6665 0.5570 -0.0493 0.0374  -0.1189 706 HOH   A O   
6860 O O   . HOH   F .   ? 0.4199 0.4875 0.3717 0.1389  -0.0291 0.0967  707 HOH   A O   
6861 O O   . HOH   F .   ? 0.4474 0.6122 0.5201 -0.0450 -0.0922 0.0792  708 HOH   A O   
6862 O O   . HOH   F .   ? 0.3198 0.3658 0.5236 -0.0403 -0.0929 0.2198  709 HOH   A O   
6863 O O   . HOH   G .   ? 0.2282 0.2079 0.3034 0.0334  0.0749  0.0353  201 HOH   B O   
6864 O O   . HOH   G .   ? 0.2957 0.5328 0.5011 -0.0131 0.1546  -0.1984 202 HOH   B O   
6865 O O   . HOH   G .   ? 0.5615 0.5077 0.2343 0.0986  -0.0718 -0.1404 203 HOH   B O   
6866 O O   . HOH   G .   ? 0.6296 0.6435 0.5713 0.2256  0.0225  -0.0034 204 HOH   B O   
6867 O O   . HOH   G .   ? 0.3236 0.6706 0.3726 0.0711  0.0110  0.2421  205 HOH   B O   
6868 O O   . HOH   G .   ? 0.5160 0.3904 0.5663 0.0495  -0.1035 0.2435  206 HOH   B O   
6869 O O   . HOH   G .   ? 0.4809 0.3126 0.3355 -0.0203 -0.0019 -0.1266 207 HOH   B O   
6870 O O   . HOH   G .   ? 0.3563 0.3688 0.6327 -0.0539 0.1110  -0.0289 208 HOH   B O   
6871 O O   . HOH   G .   ? 0.6961 0.3954 0.5096 0.0390  0.1837  0.0036  209 HOH   B O   
6872 O O   . HOH   G .   ? 0.3936 0.5229 0.3694 0.2267  -0.0555 -0.0132 210 HOH   B O   
6873 O O   . HOH   G .   ? 0.4805 0.5526 0.3946 0.2849  -0.0968 -0.0078 211 HOH   B O   
6874 O O   . HOH   G .   ? 0.4979 0.3786 0.3665 -0.0502 -0.1264 0.0714  212 HOH   B O   
6875 O O   . HOH   G .   ? 0.2720 0.2830 0.6673 0.0569  -0.1026 0.0364  213 HOH   B O   
6876 O O   . HOH   G .   ? 0.3869 0.3549 0.4795 -0.1546 0.0229  0.0610  214 HOH   B O   
6877 O O   . HOH   G .   ? 0.6093 0.3028 0.4073 -0.1938 0.0783  0.0083  215 HOH   B O   
6878 O O   . HOH   G .   ? 0.1928 0.2213 0.2774 -0.0010 0.0196  -0.0341 216 HOH   B O   
6879 O O   . HOH   G .   ? 0.1547 0.1848 0.2648 -0.0183 -0.0018 -0.0019 217 HOH   B O   
6880 O O   . HOH   G .   ? 0.3156 0.5200 0.4802 0.2031  0.0190  -0.0781 218 HOH   B O   
6881 O O   . HOH   G .   ? 0.3197 0.1931 0.5207 0.0205  0.1979  0.0784  219 HOH   B O   
6882 O O   . HOH   G .   ? 0.4038 0.4462 0.4945 -0.1162 0.0119  -0.1259 220 HOH   B O   
6883 O O   . HOH   G .   ? 0.4708 0.1978 0.3298 -0.0065 -0.1032 0.0020  221 HOH   B O   
6884 O O   . HOH   G .   ? 0.2549 0.1725 0.2772 -0.0275 0.1084  0.0030  222 HOH   B O   
6885 O O   . HOH   G .   ? 0.3541 0.2322 0.5753 -0.0007 0.0439  0.0173  223 HOH   B O   
6886 O O   . HOH   G .   ? 0.2561 0.3853 0.3675 -0.0806 0.0533  -0.0709 224 HOH   B O   
6887 O O   . HOH   G .   ? 0.3171 0.3446 0.4614 0.0539  -0.1311 -0.0186 225 HOH   B O   
6888 O O   . HOH   G .   ? 0.3841 0.6700 0.3546 0.2232  -0.0011 -0.0473 226 HOH   B O   
6889 O O   . HOH   G .   ? 0.2076 0.2066 0.3829 -0.0301 -0.0175 -0.0459 227 HOH   B O   
6890 O O   . HOH   G .   ? 0.4008 0.4553 0.4195 0.0159  0.1010  -0.1462 228 HOH   B O   
6891 O O   . HOH   G .   ? 0.1674 0.1915 0.2740 -0.0070 -0.0009 -0.0061 229 HOH   B O   
6892 O O   . HOH   G .   ? 0.4124 0.4432 0.6106 -0.0211 -0.1548 -0.0788 230 HOH   B O   
6893 O O   . HOH   G .   ? 0.3666 0.2485 0.3986 0.0839  -0.0417 -0.0690 231 HOH   B O   
6894 O O   . HOH   G .   ? 0.3567 0.3517 0.2076 0.0473  0.0663  0.0457  232 HOH   B O   
6895 O O   . HOH   G .   ? 0.6764 0.3965 0.4921 0.1576  -0.0368 -0.1156 233 HOH   B O   
6896 O O   . HOH   G .   ? 0.2863 0.2523 0.2956 0.0456  0.0136  -0.0898 234 HOH   B O   
6897 O O   . HOH   G .   ? 0.3025 0.2204 0.3821 0.0042  0.1312  0.0109  235 HOH   B O   
6898 O O   . HOH   G .   ? 0.3537 0.3112 0.3628 0.0740  -0.0976 -0.1347 236 HOH   B O   
6899 O O   . HOH   G .   ? 0.2111 0.3813 0.2948 -0.0376 -0.0579 -0.0547 237 HOH   B O   
6900 O O   . HOH   G .   ? 0.2081 0.2236 0.2882 -0.0487 0.0017  -0.0294 238 HOH   B O   
6901 O O   . HOH   G .   ? 0.5183 0.5978 0.3446 0.0293  -0.0433 0.0683  239 HOH   B O   
6902 O O   . HOH   G .   ? 0.2000 0.1265 0.3405 0.0131  -0.0609 -0.0163 240 HOH   B O   
6903 O O   . HOH   G .   ? 0.3560 0.1767 0.2019 0.0240  -0.0638 -0.0178 241 HOH   B O   
6904 O O   . HOH   G .   ? 0.1427 0.1389 0.1588 -0.0107 -0.0043 -0.0007 242 HOH   B O   
6905 O O   . HOH   G .   ? 0.2223 0.1885 0.2111 -0.0272 -0.0468 0.0031  243 HOH   B O   
6906 O O   . HOH   G .   ? 0.2886 0.1663 0.6008 -0.0038 -0.1314 -0.0275 244 HOH   B O   
6907 O O   . HOH   G .   ? 0.4879 0.3186 0.3976 -0.2252 0.0282  -0.0053 245 HOH   B O   
6908 O O   . HOH   G .   ? 0.1515 0.1407 0.2500 -0.0106 0.0076  -0.0136 246 HOH   B O   
6909 O O   . HOH   G .   ? 0.1396 0.1253 0.1579 -0.0027 -0.0020 0.0034  247 HOH   B O   
6910 O O   . HOH   G .   ? 0.4134 0.3347 0.3490 -0.0907 0.0788  -0.0817 248 HOH   B O   
6911 O O   . HOH   G .   ? 0.1981 0.3876 0.2271 -0.0408 -0.0187 0.0680  249 HOH   B O   
6912 O O   . HOH   G .   ? 0.1574 0.1574 0.2894 -0.0177 -0.0129 0.0019  250 HOH   B O   
6913 O O   . HOH   G .   ? 0.3099 0.2395 0.2911 -0.0424 0.0291  -0.0536 251 HOH   B O   
6914 O O   . HOH   G .   ? 0.2022 0.1432 0.2054 -0.0268 -0.0266 0.0207  252 HOH   B O   
6915 O O   . HOH   G .   ? 0.2804 0.2284 0.3068 0.0876  0.0962  0.0140  253 HOH   B O   
6916 O O   . HOH   G .   ? 0.2159 0.2060 0.1846 0.0134  0.0024  0.0052  254 HOH   B O   
6917 O O   . HOH   G .   ? 0.3180 0.3606 0.1862 0.0432  0.0545  0.0115  255 HOH   B O   
6918 O O   . HOH   G .   ? 0.3429 0.4554 0.5091 0.0340  0.0431  -0.1045 256 HOH   B O   
6919 O O   . HOH   G .   ? 0.3949 0.3404 0.4376 -0.0249 -0.1120 -0.1000 257 HOH   B O   
6920 O O   . HOH   G .   ? 0.2383 0.2132 0.2482 0.0823  -0.0735 -0.0583 258 HOH   B O   
6921 O O   . HOH   G .   ? 0.4760 0.3018 0.2516 0.0414  0.0842  -0.0280 259 HOH   B O   
6922 O O   . HOH   G .   ? 0.1945 0.1462 0.2180 -0.0241 -0.0163 0.0114  260 HOH   B O   
6923 O O   . HOH   G .   ? 0.3064 0.4596 0.3643 -0.0216 -0.0958 0.1163  261 HOH   B O   
6924 O O   . HOH   G .   ? 0.1788 0.2601 0.2629 0.0409  0.0433  0.1024  262 HOH   B O   
6925 O O   . HOH   G .   ? 0.1296 0.1529 0.2024 -0.0063 0.0074  0.0061  263 HOH   B O   
6926 O O   . HOH   G .   ? 0.2436 0.1970 0.2921 -0.0578 0.0134  -0.0043 264 HOH   B O   
6927 O O   . HOH   G .   ? 0.2239 0.3056 0.2110 -0.0541 0.0234  0.0511  265 HOH   B O   
6928 O O   . HOH   G .   ? 0.2906 0.4323 0.3195 -0.1086 -0.0311 -0.0691 266 HOH   B O   
6929 O O   . HOH   G .   ? 0.2646 0.2685 0.2373 -0.0387 -0.0852 0.0161  267 HOH   B O   
6930 O O   . HOH   G .   ? 0.2101 0.4186 0.4507 -0.0490 -0.0288 -0.1571 268 HOH   B O   
6931 O O   . HOH   G .   ? 0.2161 0.4002 0.5000 0.0976  -0.0468 -0.0554 269 HOH   B O   
6932 O O   . HOH   G .   ? 0.2163 0.2012 0.2065 0.0180  -0.0043 0.0043  270 HOH   B O   
6933 O O   . HOH   G .   ? 0.1667 0.1354 0.4685 -0.0115 -0.0290 -0.0042 271 HOH   B O   
6934 O O   . HOH   G .   ? 0.2414 0.1824 0.3715 0.0055  -0.0826 -0.0529 272 HOH   B O   
6935 O O   . HOH   G .   ? 0.2445 0.2637 0.2370 -0.0520 -0.0746 -0.0296 273 HOH   B O   
6936 O O   . HOH   G .   ? 0.2452 0.3105 0.2308 0.1134  -0.0272 -0.0124 274 HOH   B O   
6937 O O   . HOH   G .   ? 0.1764 0.1744 0.1594 -0.0409 -0.0377 0.0122  275 HOH   B O   
6938 O O   . HOH   G .   ? 0.2481 0.2934 0.5125 -0.0298 0.0051  -0.1135 276 HOH   B O   
6939 O O   . HOH   G .   ? 0.2494 0.3927 0.3453 0.0337  0.1009  0.0086  277 HOH   B O   
6940 O O   . HOH   G .   ? 0.2385 0.3529 0.3035 -0.0538 0.0513  -0.1282 278 HOH   B O   
6941 O O   . HOH   G .   ? 0.4039 0.5154 0.4986 0.0053  -0.1369 0.0065  279 HOH   B O   
6942 O O   . HOH   G .   ? 0.3537 0.3562 0.4333 0.1243  -0.0682 -0.0875 280 HOH   B O   
6943 O O   . HOH   G .   ? 0.1529 0.1542 0.3072 -0.0147 0.0103  -0.0036 281 HOH   B O   
6944 O O   . HOH   G .   ? 0.2824 0.6501 0.7253 0.0889  -0.0609 -0.0913 282 HOH   B O   
6945 O O   . HOH   G .   ? 0.1570 0.1442 0.1786 0.0024  0.0065  0.0021  283 HOH   B O   
6946 O O   . HOH   G .   ? 0.4350 0.3711 0.2694 0.0621  0.0023  -0.1111 284 HOH   B O   
6947 O O   . HOH   G .   ? 0.2341 0.2583 0.2723 0.0200  -0.0636 0.0294  285 HOH   B O   
6948 O O   . HOH   G .   ? 0.1572 0.2013 0.1528 -0.0138 -0.0158 -0.0016 286 HOH   B O   
6949 O O   . HOH   G .   ? 0.2679 0.2004 0.4736 0.0095  0.0584  0.0279  287 HOH   B O   
6950 O O   . HOH   G .   ? 0.3771 0.2119 0.3796 -0.0888 -0.2055 0.0721  288 HOH   B O   
6951 O O   . HOH   G .   ? 0.4348 0.3449 0.5037 -0.0887 0.0124  0.1580  289 HOH   B O   
6952 O O   . HOH   G .   ? 0.5101 0.6104 0.2549 0.0622  -0.0296 0.1336  290 HOH   B O   
6953 O O   . HOH   G .   ? 0.1621 0.1789 0.2781 0.0179  -0.0133 -0.0013 291 HOH   B O   
6954 O O   . HOH   G .   ? 0.2381 0.3325 0.3967 -0.0282 -0.1011 0.0977  292 HOH   B O   
6955 O O   . HOH   G .   ? 0.1611 0.2936 0.4378 0.0017  0.0129  -0.1070 293 HOH   B O   
6956 O O   . HOH   G .   ? 0.3561 0.7001 0.3121 0.1965  -0.0861 0.0024  294 HOH   B O   
6957 O O   . HOH   G .   ? 0.3560 0.2667 0.2057 0.0537  -0.0712 -0.0130 295 HOH   B O   
6958 O O   . HOH   G .   ? 0.2759 0.3513 0.3933 -0.1118 0.1125  -0.0702 296 HOH   B O   
6959 O O   . HOH   G .   ? 0.2727 0.4714 0.4972 -0.1034 -0.1300 0.1201  297 HOH   B O   
6960 O O   . HOH   G .   ? 0.2995 0.2913 0.2680 -0.0129 0.0095  -0.1241 298 HOH   B O   
6961 O O   . HOH   G .   ? 0.6692 0.4206 0.4977 0.1407  0.0589  0.0029  299 HOH   B O   
6962 O O   . HOH   G .   ? 0.4305 0.3914 0.2215 0.1163  -0.0714 0.0513  300 HOH   B O   
6963 O O   . HOH   G .   ? 0.1943 0.2629 0.5853 0.0442  -0.0539 -0.1256 301 HOH   B O   
6964 O O   . HOH   G .   ? 0.2016 0.1544 0.2585 -0.0229 -0.0299 -0.0076 302 HOH   B O   
6965 O O   . HOH   G .   ? 0.2848 0.2604 0.5168 -0.0211 -0.0704 0.1064  303 HOH   B O   
6966 O O   . HOH   G .   ? 0.5179 0.4244 0.2332 0.1156  -0.0916 -0.0369 304 HOH   B O   
6967 O O   . HOH   G .   ? 0.1718 0.1508 0.2263 0.0090  0.0180  0.0083  305 HOH   B O   
6968 O O   . HOH   G .   ? 0.2419 0.6750 0.2631 0.0458  -0.0230 -0.0605 306 HOH   B O   
6969 O O   . HOH   G .   ? 0.1535 0.1439 0.2870 0.0061  -0.0053 -0.0071 307 HOH   B O   
6970 O O   . HOH   G .   ? 0.4462 0.4706 0.2144 -0.0077 0.0856  0.0609  308 HOH   B O   
6971 O O   . HOH   G .   ? 0.5866 0.3680 0.2943 0.2578  0.1015  0.0678  309 HOH   B O   
6972 O O   . HOH   G .   ? 0.1595 0.1842 0.2544 -0.0294 -0.0099 0.0107  310 HOH   B O   
6973 O O   . HOH   G .   ? 0.2082 0.1477 0.3257 0.0292  -0.0994 -0.0009 311 HOH   B O   
6974 O O   . HOH   G .   ? 0.4736 0.4105 0.5558 0.0769  0.0030  0.0728  312 HOH   B O   
6975 O O   . HOH   G .   ? 0.5790 0.5214 0.4889 -0.1017 -0.0015 0.1311  313 HOH   B O   
6976 O O   . HOH   G .   ? 0.3236 0.1893 0.3345 0.0770  0.1183  0.0512  314 HOH   B O   
6977 O O   . HOH   G .   ? 0.2783 0.2960 0.3142 -0.0405 0.0956  -0.0644 315 HOH   B O   
6978 O O   . HOH   G .   ? 0.2329 0.1447 0.2386 -0.0116 -0.0129 0.0244  316 HOH   B O   
6979 O O   . HOH   G .   ? 0.4230 0.2349 0.2750 0.1546  0.1124  0.0287  317 HOH   B O   
6980 O O   . HOH   G .   ? 0.5004 0.2801 0.2434 -0.1787 0.0935  -0.0311 318 HOH   B O   
6981 O O   . HOH   G .   ? 0.1588 0.2731 0.2320 -0.0116 -0.0205 0.0626  319 HOH   B O   
6982 O O   . HOH   G .   ? 0.6428 0.5677 0.4679 0.3019  0.0354  0.0227  320 HOH   B O   
6983 O O   . HOH   G .   ? 0.1978 0.1965 0.1724 -0.0084 0.0213  0.0166  321 HOH   B O   
6984 O O   . HOH   G .   ? 0.2164 0.3092 0.5003 -0.0155 -0.0526 -0.0090 322 HOH   B O   
6985 O O   . HOH   G .   ? 0.4151 0.3525 0.4919 0.1077  0.2093  0.1835  323 HOH   B O   
6986 O O   . HOH   G .   ? 0.5200 0.2388 0.3276 0.0369  0.0544  0.0878  324 HOH   B O   
6987 O O   . HOH   G .   ? 0.1522 0.1527 0.2900 -0.0131 -0.0073 -0.0168 325 HOH   B O   
6988 O O   . HOH   G .   ? 0.4266 0.4230 0.2736 0.0415  -0.0439 -0.0659 326 HOH   B O   
6989 O O   . HOH   G .   ? 0.2683 0.2029 0.2277 0.0171  -0.0233 0.0243  327 HOH   B O   
6990 O O   . HOH   G .   ? 0.5561 0.5225 0.5604 0.0560  -0.0871 0.2299  328 HOH   B O   
6991 O O   . HOH   G .   ? 0.3036 0.3803 0.7872 -0.0360 -0.0852 0.2397  329 HOH   B O   
6992 O O   . HOH   G .   ? 0.1862 0.1983 0.2829 0.0351  0.0462  0.0180  330 HOH   B O   
6993 O O   . HOH   G .   ? 0.4812 0.4967 0.3224 -0.0000 -0.0951 0.0430  331 HOH   B O   
6994 O O   . HOH   G .   ? 0.6170 0.3285 0.3412 -0.0015 0.1190  0.1128  332 HOH   B O   
6995 O O   . HOH   G .   ? 0.1742 0.2706 0.2976 0.0353  -0.0175 -0.0645 333 HOH   B O   
6996 O O   . HOH   G .   ? 0.5053 0.3426 0.4107 0.0121  0.0879  -0.1473 334 HOH   B O   
6997 O O   . HOH   G .   ? 0.2552 0.1948 0.4791 0.0038  0.0004  0.0232  335 HOH   B O   
6998 O O   . HOH   G .   ? 0.7947 0.2044 0.2790 0.0270  -0.0671 0.0077  336 HOH   B O   
6999 O O   . HOH   G .   ? 0.5538 0.4577 0.6099 -0.0694 -0.0605 -0.1163 337 HOH   B O   
7000 O O   . HOH   G .   ? 0.2142 0.5738 0.5261 -0.0573 0.0226  -0.0902 338 HOH   B O   
7001 O O   . HOH   G .   ? 0.2223 0.2228 0.5550 -0.0429 0.0045  0.1336  339 HOH   B O   
7002 O O   . HOH   G .   ? 0.1672 0.1426 0.2234 0.0056  -0.0163 0.0044  340 HOH   B O   
7003 O O   . HOH   G .   ? 0.5609 0.3407 0.2920 0.0778  -0.1367 -0.0774 341 HOH   B O   
7004 O O   . HOH   G .   ? 0.4400 0.6995 0.3290 -0.0289 -0.0165 0.1602  342 HOH   B O   
7005 O O   . HOH   G .   ? 0.3787 0.5853 0.3645 -0.0829 -0.0808 -0.0760 343 HOH   B O   
7006 O O   . HOH   G .   ? 0.6392 0.6265 0.2808 -0.0057 -0.0712 0.1145  344 HOH   B O   
7007 O O   . HOH   G .   ? 0.1751 0.5475 0.6420 -0.0096 -0.0279 0.0576  345 HOH   B O   
7008 O O   . HOH   G .   ? 0.1954 0.1876 0.2837 -0.0088 0.0520  -0.0054 346 HOH   B O   
7009 O O   . HOH   G .   ? 0.4236 0.4880 0.5062 0.0088  -0.0949 0.0411  347 HOH   B O   
7010 O O   . HOH   G .   ? 0.2676 0.2143 0.4769 -0.0267 -0.0884 -0.0495 348 HOH   B O   
7011 O O   . HOH   G .   ? 0.2117 0.3786 0.5154 0.0221  0.0374  0.0107  349 HOH   B O   
7012 O O   . HOH   G .   ? 0.3719 0.2167 0.3616 -0.0660 0.0061  -0.0793 350 HOH   B O   
7013 O O   . HOH   G .   ? 0.4885 0.5782 0.4807 -0.1322 0.0229  0.1116  351 HOH   B O   
7014 O O   . HOH   G .   ? 0.2380 0.5645 0.3786 0.1567  -0.0422 -0.1389 352 HOH   B O   
7015 O O   . HOH   G .   ? 0.4490 0.6216 0.5894 0.0872  0.0204  -0.0479 353 HOH   B O   
7016 O O   . HOH   G .   ? 0.3443 0.4084 0.4575 -0.1514 -0.0013 0.0215  354 HOH   B O   
7017 O O   . HOH   G .   ? 0.3013 0.1850 0.3891 0.0463  -0.1139 -0.0493 355 HOH   B O   
7018 O O   . HOH   G .   ? 0.4508 0.2522 0.5378 -0.0699 0.1534  0.0451  356 HOH   B O   
7019 O O   . HOH   G .   ? 0.3660 0.2787 0.3954 -0.1006 -0.0042 -0.0644 357 HOH   B O   
7020 O O   . HOH   G .   ? 0.4789 0.3309 0.4534 0.0291  0.1305  -0.0264 358 HOH   B O   
7021 O O   . HOH   G .   ? 0.4475 0.5380 0.5199 0.1700  -0.1209 0.1438  359 HOH   B O   
7022 O O   . HOH   G .   ? 0.4370 0.3490 0.4415 0.0350  -0.1533 -0.0143 360 HOH   B O   
7023 O O   . HOH   G .   ? 0.4481 0.4705 0.4907 -0.0157 -0.0268 0.0317  361 HOH   B O   
7024 O O   . HOH   G .   ? 0.5203 0.3774 0.6137 0.0199  0.0707  0.1159  362 HOH   B O   
7025 O O   . HOH   G .   ? 0.4434 0.6403 0.3025 0.2223  0.0095  0.0679  363 HOH   B O   
7026 O O   . HOH   G .   ? 0.2024 0.3427 0.6508 -0.0679 -0.0398 -0.0660 364 HOH   B O   
7027 O O   . HOH   G .   ? 0.4959 0.3075 0.5663 -0.1316 -0.0563 0.0152  365 HOH   B O   
7028 O O   . HOH   G .   ? 0.6320 0.4183 0.4239 0.0875  0.1017  0.0614  366 HOH   B O   
7029 O O   . HOH   G .   ? 0.4864 0.3381 0.4824 0.0922  -0.1459 0.0064  367 HOH   B O   
7030 O O   . HOH   G .   ? 0.4439 0.5106 0.5819 0.2304  0.1210  0.1106  368 HOH   B O   
7031 O O   . HOH   G .   ? 0.5529 0.5671 0.3178 0.1510  -0.1331 0.0625  369 HOH   B O   
7032 O O   . HOH   G .   ? 0.6078 0.2184 0.3925 -0.0004 -0.0107 0.0740  370 HOH   B O   
7033 O O   . HOH   G .   ? 0.4821 0.5688 0.4205 -0.0424 -0.0625 -0.1088 371 HOH   B O   
7034 O O   . HOH   G .   ? 0.7586 0.7736 0.5404 0.2827  -0.1356 0.1166  372 HOH   B O   
7035 O O   . HOH   G .   ? 0.6652 0.4273 0.3049 -0.1008 -0.1088 -0.0987 373 HOH   B O   
7036 O O   . HOH   G .   ? 0.3670 0.3426 0.4423 0.0618  -0.1415 -0.0337 374 HOH   B O   
7037 O O   . HOH   G .   ? 0.2366 0.4269 0.4282 0.0357  -0.0786 -0.0705 375 HOH   B O   
7038 O O   . HOH   G .   ? 0.3505 0.3990 0.1957 0.0212  0.0340  -0.0034 376 HOH   B O   
7039 O O   . HOH   G .   ? 0.4014 0.4578 0.4796 -0.0999 -0.0497 0.0568  377 HOH   B O   
7040 O O   . HOH   G .   ? 0.4761 0.7009 0.5513 0.1548  0.0735  0.2859  378 HOH   B O   
7041 O O   . HOH   G .   ? 0.6824 0.3478 0.4927 -0.0712 -0.0247 0.0038  379 HOH   B O   
7042 O O   . HOH   G .   ? 0.3443 0.5038 0.4716 0.0516  -0.0204 0.0220  380 HOH   B O   
7043 O O   . HOH   G .   ? 0.4949 0.6725 0.4121 -0.1272 0.0316  -0.1501 381 HOH   B O   
7044 O O   . HOH   G .   ? 0.6042 0.7004 0.6604 0.0183  0.1844  0.1270  382 HOH   B O   
7045 O O   . HOH   G .   ? 0.2909 0.2490 0.3241 0.0017  0.0076  0.0485  383 HOH   B O   
7046 O O   . HOH   G .   ? 0.3827 0.7534 0.5622 0.0782  0.2123  0.1368  384 HOH   B O   
7047 O O   . HOH   G .   ? 0.7018 0.4132 0.4458 0.1126  0.1040  -0.0773 385 HOH   B O   
7048 O O   . HOH   G .   ? 0.2190 0.4216 0.3829 -0.0695 -0.0804 -0.0182 386 HOH   B O   
7049 O O   . HOH   G .   ? 0.5298 0.4355 0.5178 -0.0440 0.0317  -0.0049 387 HOH   B O   
7050 O O   . HOH   G .   ? 0.6899 0.5903 0.4109 0.2370  -0.0205 0.0775  388 HOH   B O   
7051 O O   . HOH   G .   ? 0.5104 0.4485 0.4261 -0.0394 -0.0664 -0.0411 389 HOH   B O   
7052 O O   . HOH   G .   ? 0.4785 0.3517 0.2670 0.0291  0.0377  -0.0164 390 HOH   B O   
7053 O O   . HOH   G .   ? 0.3894 0.2191 0.2959 0.0747  -0.0238 0.0221  391 HOH   B O   
7054 O O   . HOH   G .   ? 0.4929 0.4120 0.3604 0.0177  0.0219  0.0570  392 HOH   B O   
7055 O O   . HOH   G .   ? 0.4673 0.2268 0.4887 -0.0647 0.0594  0.0377  393 HOH   B O   
7056 O O   . HOH   G .   ? 0.2315 0.4509 0.6130 -0.1368 -0.0519 -0.0056 394 HOH   B O   
7057 O O   . HOH   G .   ? 0.3888 0.3803 0.4119 0.0109  0.0709  0.0673  395 HOH   B O   
7058 O O   . HOH   G .   ? 0.3049 0.3615 0.3534 0.0388  0.0070  -0.0758 396 HOH   B O   
7059 O O   . HOH   G .   ? 0.4515 0.5565 0.3278 0.1437  -0.0337 -0.0835 397 HOH   B O   
7060 O O   . HOH   G .   ? 0.1960 0.2781 0.5926 -0.0550 -0.0790 0.0173  398 HOH   B O   
7061 O O   . HOH   G .   ? 0.5737 0.6152 0.7041 0.1534  -0.0742 0.2412  399 HOH   B O   
7062 O O   . HOH   G .   ? 0.5662 0.3923 0.2916 -0.2051 -0.0197 0.0987  400 HOH   B O   
7063 O O   . HOH   G .   ? 0.5791 0.6361 0.4006 0.1260  -0.0572 0.0292  401 HOH   B O   
# 
