data_7HF9
# 
_entry.id   7HF9 
# 
_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   7HF9         pdb_00007hf9 10.2210/pdb7hf9/pdb 
WWPDB D_1001407399 ?            ?                   
# 
_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                        7HF9 
_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 '4-{[(5-methyl-7H-pyrrolo[2,3-d]pyrimidin-4-yl)amino]methyl}oxan-4-ol' 262.308   1   ?                      ? ? 
?                                                                                    
3 non-polymer syn 'CHLORIDE ION'                                                         35.453    1   ?                      ? ? 
?                                                                                    
4 water       nat water                                                                  18.015    407 ?                      ? ? 
?                                                                                    
# 
_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 '4-{[(5-methyl-7H-pyrrolo[2,3-d]pyrimidin-4-yl)amino]methyl}oxan-4-ol' A1BAV 
3 'CHLORIDE ION'                                                         CL    
4 water                                                                  HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   SER n 
1 2   MET n 
1 3   VAL n 
1 4   ASN n 
1 5   SER n 
1 6   PHE n 
1 7   SER n 
1 8   GLY n 
1 9   TYR n 
1 10  LEU n 
1 11  LYS n 
1 12  LEU n 
1 13  THR n 
1 14  ASP n 
1 15  ASN n 
1 16  VAL n 
1 17  TYR n 
1 18  ILE n 
1 19  LYS n 
1 20  ASN n 
1 21  ALA n 
1 22  ASP n 
1 23  ILE n 
1 24  VAL n 
1 25  GLU n 
1 26  GLU n 
1 27  ALA n 
1 28  LYS n 
1 29  LYS n 
1 30  VAL n 
1 31  LYS n 
1 32  PRO n 
1 33  THR n 
1 34  VAL n 
1 35  VAL n 
1 36  VAL n 
1 37  ASN n 
1 38  ALA n 
1 39  ALA n 
1 40  ASN n 
1 41  VAL n 
1 42  TYR n 
1 43  LEU n 
1 44  LYS n 
1 45  HIS n 
1 46  GLY n 
1 47  GLY n 
1 48  GLY n 
1 49  VAL n 
1 50  ALA n 
1 51  GLY n 
1 52  ALA n 
1 53  LEU n 
1 54  ASN n 
1 55  LYS n 
1 56  ALA n 
1 57  THR n 
1 58  ASN n 
1 59  ASN n 
1 60  ALA n 
1 61  MET n 
1 62  GLN n 
1 63  VAL n 
1 64  GLU n 
1 65  SER n 
1 66  ASP n 
1 67  ASP n 
1 68  TYR n 
1 69  ILE n 
1 70  ALA n 
1 71  THR n 
1 72  ASN n 
1 73  GLY n 
1 74  PRO n 
1 75  LEU n 
1 76  LYS n 
1 77  VAL n 
1 78  GLY n 
1 79  GLY n 
1 80  SER n 
1 81  CYS n 
1 82  VAL n 
1 83  LEU n 
1 84  SER n 
1 85  GLY n 
1 86  HIS n 
1 87  ASN n 
1 88  LEU n 
1 89  ALA n 
1 90  LYS n 
1 91  HIS n 
1 92  CYS n 
1 93  LEU n 
1 94  HIS n 
1 95  VAL n 
1 96  VAL n 
1 97  GLY n 
1 98  PRO n 
1 99  ASN n 
1 100 VAL n 
1 101 ASN n 
1 102 LYS n 
1 103 GLY n 
1 104 GLU n 
1 105 ASP n 
1 106 ILE n 
1 107 GLN n 
1 108 LEU n 
1 109 LEU n 
1 110 LYS n 
1 111 SER n 
1 112 ALA n 
1 113 TYR n 
1 114 GLU n 
1 115 ASN n 
1 116 PHE n 
1 117 ASN n 
1 118 GLN n 
1 119 HIS n 
1 120 GLU n 
1 121 VAL n 
1 122 LEU n 
1 123 LEU n 
1 124 ALA n 
1 125 PRO n 
1 126 LEU n 
1 127 LEU n 
1 128 SER n 
1 129 ALA n 
1 130 GLY n 
1 131 ILE n 
1 132 PHE n 
1 133 GLY n 
1 134 ALA n 
1 135 ASP n 
1 136 PRO n 
1 137 ILE n 
1 138 HIS n 
1 139 SER n 
1 140 LEU n 
1 141 ARG n 
1 142 VAL n 
1 143 CYS n 
1 144 VAL n 
1 145 ASP n 
1 146 THR n 
1 147 VAL n 
1 148 ARG n 
1 149 THR n 
1 150 ASN n 
1 151 VAL n 
1 152 TYR n 
1 153 LEU n 
1 154 ALA n 
1 155 VAL n 
1 156 PHE n 
1 157 ASP n 
1 158 LYS n 
1 159 ASN n 
1 160 LEU n 
1 161 TYR n 
1 162 ASP n 
1 163 LYS n 
1 164 LEU n 
1 165 VAL n 
1 166 SER n 
1 167 SER n 
1 168 PHE n 
1 169 LEU n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   169 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'rep, 1a-1b' 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Severe acute respiratory syndrome coronavirus 2' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     2697049 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          plasmid 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       'pET22b(+)' 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
A1BAV non-polymer         . '4-{[(5-methyl-7H-pyrrolo[2,3-d]pyrimidin-4-yl)amino]methyl}oxan-4-ol' ? 'C13 H18 N4 O2'  262.308 
ALA   'L-peptide linking' y ALANINE                                                                ? 'C3 H7 N O2'     89.093  
ARG   'L-peptide linking' y ARGININE                                                               ? 'C6 H15 N4 O2 1' 175.209 
ASN   'L-peptide linking' y ASPARAGINE                                                             ? 'C4 H8 N2 O3'    132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID'                                                        ? 'C4 H7 N O4'     133.103 
CL    non-polymer         . 'CHLORIDE ION'                                                         ? 'Cl -1'          35.453  
CYS   'L-peptide linking' y CYSTEINE                                                               ? 'C3 H7 N O2 S'   121.158 
GLN   'L-peptide linking' y GLUTAMINE                                                              ? 'C5 H10 N2 O3'   146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'                                                        ? 'C5 H9 N O4'     147.129 
GLY   'peptide linking'   y GLYCINE                                                                ? 'C2 H5 N O2'     75.067  
HIS   'L-peptide linking' y HISTIDINE                                                              ? 'C6 H10 N3 O2 1' 156.162 
HOH   non-polymer         . WATER                                                                  ? 'H2 O'           18.015  
ILE   'L-peptide linking' y ISOLEUCINE                                                             ? 'C6 H13 N O2'    131.173 
LEU   'L-peptide linking' y LEUCINE                                                                ? 'C6 H13 N O2'    131.173 
LYS   'L-peptide linking' y LYSINE                                                                 ? 'C6 H15 N2 O2 1' 147.195 
MET   'L-peptide linking' y METHIONINE                                                             ? 'C5 H11 N O2 S'  149.211 
PHE   'L-peptide linking' y PHENYLALANINE                                                          ? 'C9 H11 N O2'    165.189 
PRO   'L-peptide linking' y PROLINE                                                                ? 'C5 H9 N O2'     115.130 
SER   'L-peptide linking' y SERINE                                                                 ? 'C3 H7 N O3'     105.093 
THR   'L-peptide linking' y THREONINE                                                              ? 'C4 H9 N O3'     119.119 
TYR   'L-peptide linking' y TYROSINE                                                               ? 'C9 H11 N O3'    181.189 
VAL   'L-peptide linking' y VALINE                                                                 ? 'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   SER 1   1   ?   ?   ?   A . n 
A 1 2   MET 2   2   ?   ?   ?   A . n 
A 1 3   VAL 3   3   3   VAL VAL A . n 
A 1 4   ASN 4   4   4   ASN ASN A . n 
A 1 5   SER 5   5   5   SER SER A . n 
A 1 6   PHE 6   6   6   PHE PHE A . n 
A 1 7   SER 7   7   7   SER SER A . n 
A 1 8   GLY 8   8   8   GLY GLY A . n 
A 1 9   TYR 9   9   9   TYR TYR A . n 
A 1 10  LEU 10  10  10  LEU LEU A . n 
A 1 11  LYS 11  11  11  LYS LYS A . n 
A 1 12  LEU 12  12  12  LEU LEU A . n 
A 1 13  THR 13  13  13  THR THR A . n 
A 1 14  ASP 14  14  14  ASP ASP A . n 
A 1 15  ASN 15  15  15  ASN ASN A . n 
A 1 16  VAL 16  16  16  VAL VAL A . n 
A 1 17  TYR 17  17  17  TYR TYR A . n 
A 1 18  ILE 18  18  18  ILE ILE A . n 
A 1 19  LYS 19  19  19  LYS LYS A . n 
A 1 20  ASN 20  20  20  ASN ASN A . n 
A 1 21  ALA 21  21  21  ALA ALA A . n 
A 1 22  ASP 22  22  22  ASP ASP A . n 
A 1 23  ILE 23  23  23  ILE ILE A . n 
A 1 24  VAL 24  24  24  VAL VAL A . n 
A 1 25  GLU 25  25  25  GLU GLU A . n 
A 1 26  GLU 26  26  26  GLU GLU A . n 
A 1 27  ALA 27  27  27  ALA ALA A . n 
A 1 28  LYS 28  28  28  LYS LYS A . n 
A 1 29  LYS 29  29  29  LYS LYS A . n 
A 1 30  VAL 30  30  30  VAL VAL A . n 
A 1 31  LYS 31  31  31  LYS LYS A . n 
A 1 32  PRO 32  32  32  PRO PRO A . n 
A 1 33  THR 33  33  33  THR THR A . n 
A 1 34  VAL 34  34  34  VAL VAL A . n 
A 1 35  VAL 35  35  35  VAL VAL A . n 
A 1 36  VAL 36  36  36  VAL VAL A . n 
A 1 37  ASN 37  37  37  ASN ASN A . n 
A 1 38  ALA 38  38  38  ALA ALA A . n 
A 1 39  ALA 39  39  39  ALA ALA A . n 
A 1 40  ASN 40  40  40  ASN ASN A . n 
A 1 41  VAL 41  41  41  VAL VAL A . n 
A 1 42  TYR 42  42  42  TYR TYR A . n 
A 1 43  LEU 43  43  43  LEU LEU A . n 
A 1 44  LYS 44  44  44  LYS LYS A . n 
A 1 45  HIS 45  45  45  HIS HIS A . n 
A 1 46  GLY 46  46  46  GLY GLY A . n 
A 1 47  GLY 47  47  47  GLY GLY A . n 
A 1 48  GLY 48  48  48  GLY GLY A . n 
A 1 49  VAL 49  49  49  VAL VAL A . n 
A 1 50  ALA 50  50  50  ALA ALA A . n 
A 1 51  GLY 51  51  51  GLY GLY A . n 
A 1 52  ALA 52  52  52  ALA ALA A . n 
A 1 53  LEU 53  53  53  LEU LEU A . n 
A 1 54  ASN 54  54  54  ASN ASN A . n 
A 1 55  LYS 55  55  55  LYS LYS A . n 
A 1 56  ALA 56  56  56  ALA ALA A . n 
A 1 57  THR 57  57  57  THR THR A . n 
A 1 58  ASN 58  58  58  ASN ASN A . n 
A 1 59  ASN 59  59  59  ASN ASN A . n 
A 1 60  ALA 60  60  60  ALA ALA A . n 
A 1 61  MET 61  61  61  MET MET A . n 
A 1 62  GLN 62  62  62  GLN GLN A . n 
A 1 63  VAL 63  63  63  VAL VAL A . n 
A 1 64  GLU 64  64  64  GLU GLU A . n 
A 1 65  SER 65  65  65  SER SER A . n 
A 1 66  ASP 66  66  66  ASP ASP A . n 
A 1 67  ASP 67  67  67  ASP ASP A . n 
A 1 68  TYR 68  68  68  TYR TYR A . n 
A 1 69  ILE 69  69  69  ILE ILE A . n 
A 1 70  ALA 70  70  70  ALA ALA A . n 
A 1 71  THR 71  71  71  THR THR A . n 
A 1 72  ASN 72  72  72  ASN ASN A . n 
A 1 73  GLY 73  73  73  GLY GLY A . n 
A 1 74  PRO 74  74  74  PRO PRO A . n 
A 1 75  LEU 75  75  75  LEU LEU A . n 
A 1 76  LYS 76  76  76  LYS LYS A . n 
A 1 77  VAL 77  77  77  VAL VAL A . n 
A 1 78  GLY 78  78  78  GLY GLY A . n 
A 1 79  GLY 79  79  79  GLY GLY A . n 
A 1 80  SER 80  80  80  SER SER A . n 
A 1 81  CYS 81  81  81  CYS CYS A . n 
A 1 82  VAL 82  82  82  VAL VAL A . n 
A 1 83  LEU 83  83  83  LEU LEU A . n 
A 1 84  SER 84  84  84  SER SER A . n 
A 1 85  GLY 85  85  85  GLY GLY A . n 
A 1 86  HIS 86  86  86  HIS HIS A . n 
A 1 87  ASN 87  87  87  ASN ASN A . n 
A 1 88  LEU 88  88  88  LEU LEU A . n 
A 1 89  ALA 89  89  89  ALA ALA A . n 
A 1 90  LYS 90  90  90  LYS LYS A . n 
A 1 91  HIS 91  91  91  HIS HIS A . n 
A 1 92  CYS 92  92  92  CYS CYS A . n 
A 1 93  LEU 93  93  93  LEU LEU A . n 
A 1 94  HIS 94  94  94  HIS HIS A . n 
A 1 95  VAL 95  95  95  VAL VAL A . n 
A 1 96  VAL 96  96  96  VAL VAL A . n 
A 1 97  GLY 97  97  97  GLY GLY A . n 
A 1 98  PRO 98  98  98  PRO PRO A . n 
A 1 99  ASN 99  99  99  ASN ASN A . n 
A 1 100 VAL 100 100 100 VAL VAL A . n 
A 1 101 ASN 101 101 101 ASN ASN A . n 
A 1 102 LYS 102 102 102 LYS LYS A . n 
A 1 103 GLY 103 103 103 GLY GLY A . n 
A 1 104 GLU 104 104 104 GLU GLU A . n 
A 1 105 ASP 105 105 105 ASP ASP A . n 
A 1 106 ILE 106 106 106 ILE ILE A . n 
A 1 107 GLN 107 107 107 GLN GLN A . n 
A 1 108 LEU 108 108 108 LEU LEU A . n 
A 1 109 LEU 109 109 109 LEU LEU A . n 
A 1 110 LYS 110 110 110 LYS LYS A . n 
A 1 111 SER 111 111 111 SER SER A . n 
A 1 112 ALA 112 112 112 ALA ALA A . n 
A 1 113 TYR 113 113 113 TYR TYR A . n 
A 1 114 GLU 114 114 114 GLU GLU A . n 
A 1 115 ASN 115 115 115 ASN ASN A . n 
A 1 116 PHE 116 116 116 PHE PHE A . n 
A 1 117 ASN 117 117 117 ASN ASN A . n 
A 1 118 GLN 118 118 118 GLN GLN A . n 
A 1 119 HIS 119 119 119 HIS HIS A . n 
A 1 120 GLU 120 120 120 GLU GLU A . n 
A 1 121 VAL 121 121 121 VAL VAL A . n 
A 1 122 LEU 122 122 122 LEU LEU A . n 
A 1 123 LEU 123 123 123 LEU LEU A . n 
A 1 124 ALA 124 124 124 ALA ALA A . n 
A 1 125 PRO 125 125 125 PRO PRO A . n 
A 1 126 LEU 126 126 126 LEU LEU A . n 
A 1 127 LEU 127 127 127 LEU LEU A . n 
A 1 128 SER 128 128 128 SER SER A . n 
A 1 129 ALA 129 129 129 ALA ALA A . n 
A 1 130 GLY 130 130 130 GLY GLY A . n 
A 1 131 ILE 131 131 131 ILE ILE A . n 
A 1 132 PHE 132 132 132 PHE PHE A . n 
A 1 133 GLY 133 133 133 GLY GLY A . n 
A 1 134 ALA 134 134 134 ALA ALA A . n 
A 1 135 ASP 135 135 135 ASP ASP A . n 
A 1 136 PRO 136 136 136 PRO PRO A . n 
A 1 137 ILE 137 137 137 ILE ILE A . n 
A 1 138 HIS 138 138 138 HIS HIS A . n 
A 1 139 SER 139 139 139 SER SER A . n 
A 1 140 LEU 140 140 140 LEU LEU A . n 
A 1 141 ARG 141 141 141 ARG ARG A . n 
A 1 142 VAL 142 142 142 VAL VAL A . n 
A 1 143 CYS 143 143 143 CYS CYS A . n 
A 1 144 VAL 144 144 144 VAL VAL A . n 
A 1 145 ASP 145 145 145 ASP ASP A . n 
A 1 146 THR 146 146 146 THR THR A . n 
A 1 147 VAL 147 147 147 VAL VAL A . n 
A 1 148 ARG 148 148 148 ARG ARG A . n 
A 1 149 THR 149 149 149 THR THR A . n 
A 1 150 ASN 150 150 150 ASN ASN A . n 
A 1 151 VAL 151 151 151 VAL VAL A . n 
A 1 152 TYR 152 152 152 TYR TYR A . n 
A 1 153 LEU 153 153 153 LEU LEU A . n 
A 1 154 ALA 154 154 154 ALA ALA A . n 
A 1 155 VAL 155 155 155 VAL VAL A . n 
A 1 156 PHE 156 156 156 PHE PHE A . n 
A 1 157 ASP 157 157 157 ASP ASP A . n 
A 1 158 LYS 158 158 158 LYS LYS A . n 
A 1 159 ASN 159 159 159 ASN ASN A . n 
A 1 160 LEU 160 160 160 LEU LEU A . n 
A 1 161 TYR 161 161 161 TYR TYR A . n 
A 1 162 ASP 162 162 162 ASP ASP A . n 
A 1 163 LYS 163 163 163 LYS LYS A . n 
A 1 164 LEU 164 164 164 LEU LEU A . n 
A 1 165 VAL 165 165 165 VAL VAL A . n 
A 1 166 SER 166 166 166 SER SER A . n 
A 1 167 SER 167 167 167 SER SER A . n 
A 1 168 PHE 168 168 168 PHE PHE A . n 
A 1 169 LEU 169 169 169 LEU LEU A . n 
B 1 1   SER 1   1   1   SER SER B . n 
B 1 2   MET 2   2   2   MET MET B . n 
B 1 3   VAL 3   3   3   VAL VAL B . n 
B 1 4   ASN 4   4   4   ASN ASN B . n 
B 1 5   SER 5   5   5   SER SER B . n 
B 1 6   PHE 6   6   6   PHE PHE B . n 
B 1 7   SER 7   7   7   SER SER B . n 
B 1 8   GLY 8   8   8   GLY GLY B . n 
B 1 9   TYR 9   9   9   TYR TYR B . n 
B 1 10  LEU 10  10  10  LEU LEU B . n 
B 1 11  LYS 11  11  11  LYS LYS B . n 
B 1 12  LEU 12  12  12  LEU LEU B . n 
B 1 13  THR 13  13  13  THR THR B . n 
B 1 14  ASP 14  14  14  ASP ASP B . n 
B 1 15  ASN 15  15  15  ASN ASN B . n 
B 1 16  VAL 16  16  16  VAL VAL B . n 
B 1 17  TYR 17  17  17  TYR TYR B . n 
B 1 18  ILE 18  18  18  ILE ILE B . n 
B 1 19  LYS 19  19  19  LYS LYS B . n 
B 1 20  ASN 20  20  20  ASN ASN B . n 
B 1 21  ALA 21  21  21  ALA ALA B . n 
B 1 22  ASP 22  22  22  ASP ASP B . n 
B 1 23  ILE 23  23  23  ILE ILE B . n 
B 1 24  VAL 24  24  24  VAL VAL B . n 
B 1 25  GLU 25  25  25  GLU GLU B . n 
B 1 26  GLU 26  26  26  GLU GLU B . n 
B 1 27  ALA 27  27  27  ALA ALA B . n 
B 1 28  LYS 28  28  28  LYS LYS B . n 
B 1 29  LYS 29  29  29  LYS LYS B . n 
B 1 30  VAL 30  30  30  VAL VAL B . n 
B 1 31  LYS 31  31  31  LYS LYS B . n 
B 1 32  PRO 32  32  32  PRO PRO B . n 
B 1 33  THR 33  33  33  THR THR B . n 
B 1 34  VAL 34  34  34  VAL VAL B . n 
B 1 35  VAL 35  35  35  VAL VAL B . n 
B 1 36  VAL 36  36  36  VAL VAL B . n 
B 1 37  ASN 37  37  37  ASN ASN B . n 
B 1 38  ALA 38  38  38  ALA ALA B . n 
B 1 39  ALA 39  39  39  ALA ALA B . n 
B 1 40  ASN 40  40  40  ASN ASN B . n 
B 1 41  VAL 41  41  41  VAL VAL B . n 
B 1 42  TYR 42  42  42  TYR TYR B . n 
B 1 43  LEU 43  43  43  LEU LEU B . n 
B 1 44  LYS 44  44  44  LYS LYS B . n 
B 1 45  HIS 45  45  45  HIS HIS B . n 
B 1 46  GLY 46  46  46  GLY GLY B . n 
B 1 47  GLY 47  47  47  GLY GLY B . n 
B 1 48  GLY 48  48  48  GLY GLY B . n 
B 1 49  VAL 49  49  49  VAL VAL B . n 
B 1 50  ALA 50  50  50  ALA ALA B . n 
B 1 51  GLY 51  51  51  GLY GLY B . n 
B 1 52  ALA 52  52  52  ALA ALA B . n 
B 1 53  LEU 53  53  53  LEU LEU B . n 
B 1 54  ASN 54  54  54  ASN ASN B . n 
B 1 55  LYS 55  55  55  LYS LYS B . n 
B 1 56  ALA 56  56  56  ALA ALA B . n 
B 1 57  THR 57  57  57  THR THR B . n 
B 1 58  ASN 58  58  58  ASN ASN B . n 
B 1 59  ASN 59  59  59  ASN ASN B . n 
B 1 60  ALA 60  60  60  ALA ALA B . n 
B 1 61  MET 61  61  61  MET MET B . n 
B 1 62  GLN 62  62  62  GLN GLN B . n 
B 1 63  VAL 63  63  63  VAL VAL B . n 
B 1 64  GLU 64  64  64  GLU GLU B . n 
B 1 65  SER 65  65  65  SER SER B . n 
B 1 66  ASP 66  66  66  ASP ASP B . n 
B 1 67  ASP 67  67  67  ASP ASP B . n 
B 1 68  TYR 68  68  68  TYR TYR B . n 
B 1 69  ILE 69  69  69  ILE ILE B . n 
B 1 70  ALA 70  70  70  ALA ALA B . n 
B 1 71  THR 71  71  71  THR THR B . n 
B 1 72  ASN 72  72  72  ASN ASN B . n 
B 1 73  GLY 73  73  73  GLY GLY B . n 
B 1 74  PRO 74  74  74  PRO PRO B . n 
B 1 75  LEU 75  75  75  LEU LEU B . n 
B 1 76  LYS 76  76  76  LYS LYS B . n 
B 1 77  VAL 77  77  77  VAL VAL B . n 
B 1 78  GLY 78  78  78  GLY GLY B . n 
B 1 79  GLY 79  79  79  GLY GLY B . n 
B 1 80  SER 80  80  80  SER SER B . n 
B 1 81  CYS 81  81  81  CYS CYS B . n 
B 1 82  VAL 82  82  82  VAL VAL B . n 
B 1 83  LEU 83  83  83  LEU LEU B . n 
B 1 84  SER 84  84  84  SER SER B . n 
B 1 85  GLY 85  85  85  GLY GLY B . n 
B 1 86  HIS 86  86  86  HIS HIS B . n 
B 1 87  ASN 87  87  87  ASN ASN B . n 
B 1 88  LEU 88  88  88  LEU LEU B . n 
B 1 89  ALA 89  89  89  ALA ALA B . n 
B 1 90  LYS 90  90  90  LYS LYS B . n 
B 1 91  HIS 91  91  91  HIS HIS B . n 
B 1 92  CYS 92  92  92  CYS CYS B . n 
B 1 93  LEU 93  93  93  LEU LEU B . n 
B 1 94  HIS 94  94  94  HIS HIS B . n 
B 1 95  VAL 95  95  95  VAL VAL B . n 
B 1 96  VAL 96  96  96  VAL VAL B . n 
B 1 97  GLY 97  97  97  GLY GLY B . n 
B 1 98  PRO 98  98  98  PRO PRO B . n 
B 1 99  ASN 99  99  99  ASN ASN B . n 
B 1 100 VAL 100 100 100 VAL VAL B . n 
B 1 101 ASN 101 101 101 ASN ASN B . n 
B 1 102 LYS 102 102 102 LYS LYS B . n 
B 1 103 GLY 103 103 103 GLY GLY B . n 
B 1 104 GLU 104 104 104 GLU GLU B . n 
B 1 105 ASP 105 105 105 ASP ASP B . n 
B 1 106 ILE 106 106 106 ILE ILE B . n 
B 1 107 GLN 107 107 107 GLN GLN B . n 
B 1 108 LEU 108 108 108 LEU LEU B . n 
B 1 109 LEU 109 109 109 LEU LEU B . n 
B 1 110 LYS 110 110 110 LYS LYS B . n 
B 1 111 SER 111 111 111 SER SER B . n 
B 1 112 ALA 112 112 112 ALA ALA B . n 
B 1 113 TYR 113 113 113 TYR TYR B . n 
B 1 114 GLU 114 114 114 GLU GLU B . n 
B 1 115 ASN 115 115 115 ASN ASN B . n 
B 1 116 PHE 116 116 116 PHE PHE B . n 
B 1 117 ASN 117 117 117 ASN ASN B . n 
B 1 118 GLN 118 118 118 GLN GLN B . n 
B 1 119 HIS 119 119 119 HIS HIS B . n 
B 1 120 GLU 120 120 120 GLU GLU B . n 
B 1 121 VAL 121 121 121 VAL VAL B . n 
B 1 122 LEU 122 122 122 LEU LEU B . n 
B 1 123 LEU 123 123 123 LEU LEU B . n 
B 1 124 ALA 124 124 124 ALA ALA B . n 
B 1 125 PRO 125 125 125 PRO PRO B . n 
B 1 126 LEU 126 126 126 LEU LEU B . n 
B 1 127 LEU 127 127 127 LEU LEU B . n 
B 1 128 SER 128 128 128 SER SER B . n 
B 1 129 ALA 129 129 129 ALA ALA B . n 
B 1 130 GLY 130 130 130 GLY GLY B . n 
B 1 131 ILE 131 131 131 ILE ILE B . n 
B 1 132 PHE 132 132 132 PHE PHE B . n 
B 1 133 GLY 133 133 133 GLY GLY B . n 
B 1 134 ALA 134 134 134 ALA ALA B . n 
B 1 135 ASP 135 135 135 ASP ASP B . n 
B 1 136 PRO 136 136 136 PRO PRO B . n 
B 1 137 ILE 137 137 137 ILE ILE B . n 
B 1 138 HIS 138 138 138 HIS HIS B . n 
B 1 139 SER 139 139 139 SER SER B . n 
B 1 140 LEU 140 140 140 LEU LEU B . n 
B 1 141 ARG 141 141 141 ARG ARG B . n 
B 1 142 VAL 142 142 142 VAL VAL B . n 
B 1 143 CYS 143 143 143 CYS CYS B . n 
B 1 144 VAL 144 144 144 VAL VAL B . n 
B 1 145 ASP 145 145 145 ASP ASP B . n 
B 1 146 THR 146 146 146 THR THR B . n 
B 1 147 VAL 147 147 147 VAL VAL B . n 
B 1 148 ARG 148 148 148 ARG ARG B . n 
B 1 149 THR 149 149 149 THR THR B . n 
B 1 150 ASN 150 150 150 ASN ASN B . n 
B 1 151 VAL 151 151 151 VAL VAL B . n 
B 1 152 TYR 152 152 152 TYR TYR B . n 
B 1 153 LEU 153 153 153 LEU LEU B . n 
B 1 154 ALA 154 154 154 ALA ALA B . n 
B 1 155 VAL 155 155 155 VAL VAL B . n 
B 1 156 PHE 156 156 156 PHE PHE B . n 
B 1 157 ASP 157 157 157 ASP ASP B . n 
B 1 158 LYS 158 158 158 LYS LYS B . n 
B 1 159 ASN 159 159 159 ASN ASN B . n 
B 1 160 LEU 160 160 160 LEU LEU B . n 
B 1 161 TYR 161 161 161 TYR TYR B . n 
B 1 162 ASP 162 162 162 ASP ASP B . n 
B 1 163 LYS 163 163 163 LYS LYS B . n 
B 1 164 LEU 164 164 164 LEU LEU B . n 
B 1 165 VAL 165 165 165 VAL VAL B . n 
B 1 166 SER 166 166 166 SER SER B . n 
B 1 167 SER 167 167 167 SER SER B . n 
B 1 168 PHE 168 168 168 PHE PHE B . n 
B 1 169 LEU 169 169 169 LEU LEU B . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 A1BAV 1   201 201  A1BAV LA1 A . 
D 3 CL    1   202 1    CL    CL  A . 
E 4 HOH   1   301 93   HOH   HOH A . 
E 4 HOH   2   302 86   HOH   HOH A . 
E 4 HOH   3   303 292  HOH   HOH A . 
E 4 HOH   4   304 18   HOH   HOH A . 
E 4 HOH   5   305 196  HOH   HOH A . 
E 4 HOH   6   306 1289 HOH   HOH A . 
E 4 HOH   7   307 493  HOH   HOH A . 
E 4 HOH   8   308 625  HOH   HOH A . 
E 4 HOH   9   309 409  HOH   HOH A . 
E 4 HOH   10  310 229  HOH   HOH A . 
E 4 HOH   11  311 247  HOH   HOH A . 
E 4 HOH   12  312 662  HOH   HOH A . 
E 4 HOH   13  313 661  HOH   HOH A . 
E 4 HOH   14  314 393  HOH   HOH A . 
E 4 HOH   15  315 109  HOH   HOH A . 
E 4 HOH   16  316 209  HOH   HOH A . 
E 4 HOH   17  317 199  HOH   HOH A . 
E 4 HOH   18  318 76   HOH   HOH A . 
E 4 HOH   19  319 153  HOH   HOH A . 
E 4 HOH   20  320 1295 HOH   HOH A . 
E 4 HOH   21  321 151  HOH   HOH A . 
E 4 HOH   22  322 225  HOH   HOH A . 
E 4 HOH   23  323 192  HOH   HOH A . 
E 4 HOH   24  324 39   HOH   HOH A . 
E 4 HOH   25  325 124  HOH   HOH A . 
E 4 HOH   26  326 236  HOH   HOH A . 
E 4 HOH   27  327 136  HOH   HOH A . 
E 4 HOH   28  328 15   HOH   HOH A . 
E 4 HOH   29  329 1301 HOH   HOH A . 
E 4 HOH   30  330 164  HOH   HOH A . 
E 4 HOH   31  331 140  HOH   HOH A . 
E 4 HOH   32  332 964  HOH   HOH A . 
E 4 HOH   33  333 36   HOH   HOH A . 
E 4 HOH   34  334 105  HOH   HOH A . 
E 4 HOH   35  335 469  HOH   HOH A . 
E 4 HOH   36  336 320  HOH   HOH A . 
E 4 HOH   37  337 42   HOH   HOH A . 
E 4 HOH   38  338 21   HOH   HOH A . 
E 4 HOH   39  339 337  HOH   HOH A . 
E 4 HOH   40  340 241  HOH   HOH A . 
E 4 HOH   41  341 354  HOH   HOH A . 
E 4 HOH   42  342 1094 HOH   HOH A . 
E 4 HOH   43  343 630  HOH   HOH A . 
E 4 HOH   44  344 1300 HOH   HOH A . 
E 4 HOH   45  345 17   HOH   HOH A . 
E 4 HOH   46  346 281  HOH   HOH A . 
E 4 HOH   47  347 92   HOH   HOH A . 
E 4 HOH   48  348 8    HOH   HOH A . 
E 4 HOH   49  349 66   HOH   HOH A . 
E 4 HOH   50  350 139  HOH   HOH A . 
E 4 HOH   51  351 396  HOH   HOH A . 
E 4 HOH   52  352 165  HOH   HOH A . 
E 4 HOH   53  353 405  HOH   HOH A . 
E 4 HOH   54  354 159  HOH   HOH A . 
E 4 HOH   55  355 57   HOH   HOH A . 
E 4 HOH   56  356 70   HOH   HOH A . 
E 4 HOH   57  357 19   HOH   HOH A . 
E 4 HOH   58  358 1283 HOH   HOH A . 
E 4 HOH   59  359 45   HOH   HOH A . 
E 4 HOH   60  360 2    HOH   HOH A . 
E 4 HOH   61  361 169  HOH   HOH A . 
E 4 HOH   62  362 56   HOH   HOH A . 
E 4 HOH   63  363 296  HOH   HOH A . 
E 4 HOH   64  364 138  HOH   HOH A . 
E 4 HOH   65  365 186  HOH   HOH A . 
E 4 HOH   66  366 1290 HOH   HOH A . 
E 4 HOH   67  367 5    HOH   HOH A . 
E 4 HOH   68  368 154  HOH   HOH A . 
E 4 HOH   69  369 939  HOH   HOH A . 
E 4 HOH   70  370 102  HOH   HOH A . 
E 4 HOH   71  371 46   HOH   HOH A . 
E 4 HOH   72  372 162  HOH   HOH A . 
E 4 HOH   73  373 33   HOH   HOH A . 
E 4 HOH   74  374 155  HOH   HOH A . 
E 4 HOH   75  375 81   HOH   HOH A . 
E 4 HOH   76  376 134  HOH   HOH A . 
E 4 HOH   77  377 218  HOH   HOH A . 
E 4 HOH   78  378 27   HOH   HOH A . 
E 4 HOH   79  379 26   HOH   HOH A . 
E 4 HOH   80  380 148  HOH   HOH A . 
E 4 HOH   81  381 1310 HOH   HOH A . 
E 4 HOH   82  382 49   HOH   HOH A . 
E 4 HOH   83  383 12   HOH   HOH A . 
E 4 HOH   84  384 1309 HOH   HOH A . 
E 4 HOH   85  385 1313 HOH   HOH A . 
E 4 HOH   86  386 35   HOH   HOH A . 
E 4 HOH   87  387 461  HOH   HOH A . 
E 4 HOH   88  388 4    HOH   HOH A . 
E 4 HOH   89  389 366  HOH   HOH A . 
E 4 HOH   90  390 85   HOH   HOH A . 
E 4 HOH   91  391 58   HOH   HOH A . 
E 4 HOH   92  392 83   HOH   HOH A . 
E 4 HOH   93  393 1308 HOH   HOH A . 
E 4 HOH   94  394 116  HOH   HOH A . 
E 4 HOH   95  395 78   HOH   HOH A . 
E 4 HOH   96  396 132  HOH   HOH A . 
E 4 HOH   97  397 24   HOH   HOH A . 
E 4 HOH   98  398 6    HOH   HOH A . 
E 4 HOH   99  399 1315 HOH   HOH A . 
E 4 HOH   100 400 333  HOH   HOH A . 
E 4 HOH   101 401 74   HOH   HOH A . 
E 4 HOH   102 402 1275 HOH   HOH A . 
E 4 HOH   103 403 303  HOH   HOH A . 
E 4 HOH   104 404 3    HOH   HOH A . 
E 4 HOH   105 405 96   HOH   HOH A . 
E 4 HOH   106 406 67   HOH   HOH A . 
E 4 HOH   107 407 397  HOH   HOH A . 
E 4 HOH   108 408 1068 HOH   HOH A . 
E 4 HOH   109 409 34   HOH   HOH A . 
E 4 HOH   110 410 278  HOH   HOH A . 
E 4 HOH   111 411 121  HOH   HOH A . 
E 4 HOH   112 412 68   HOH   HOH A . 
E 4 HOH   113 413 25   HOH   HOH A . 
E 4 HOH   114 414 53   HOH   HOH A . 
E 4 HOH   115 415 125  HOH   HOH A . 
E 4 HOH   116 416 156  HOH   HOH A . 
E 4 HOH   117 417 195  HOH   HOH A . 
E 4 HOH   118 418 582  HOH   HOH A . 
E 4 HOH   119 419 381  HOH   HOH A . 
E 4 HOH   120 420 123  HOH   HOH A . 
E 4 HOH   121 421 351  HOH   HOH A . 
E 4 HOH   122 422 1279 HOH   HOH A . 
E 4 HOH   123 423 95   HOH   HOH A . 
E 4 HOH   124 424 212  HOH   HOH A . 
E 4 HOH   125 425 51   HOH   HOH A . 
E 4 HOH   126 426 122  HOH   HOH A . 
E 4 HOH   127 427 7    HOH   HOH A . 
E 4 HOH   128 428 115  HOH   HOH A . 
E 4 HOH   129 429 1222 HOH   HOH A . 
E 4 HOH   130 430 1286 HOH   HOH A . 
E 4 HOH   131 431 16   HOH   HOH A . 
E 4 HOH   132 432 1189 HOH   HOH A . 
E 4 HOH   133 433 73   HOH   HOH A . 
E 4 HOH   134 434 71   HOH   HOH A . 
E 4 HOH   135 435 1296 HOH   HOH A . 
E 4 HOH   136 436 40   HOH   HOH A . 
E 4 HOH   137 437 80   HOH   HOH A . 
E 4 HOH   138 438 188  HOH   HOH A . 
E 4 HOH   139 439 94   HOH   HOH A . 
E 4 HOH   140 440 97   HOH   HOH A . 
E 4 HOH   141 441 1238 HOH   HOH A . 
E 4 HOH   142 442 952  HOH   HOH A . 
E 4 HOH   143 443 104  HOH   HOH A . 
E 4 HOH   144 444 944  HOH   HOH A . 
E 4 HOH   145 445 576  HOH   HOH A . 
E 4 HOH   146 446 1119 HOH   HOH A . 
E 4 HOH   147 447 330  HOH   HOH A . 
E 4 HOH   148 448 79   HOH   HOH A . 
E 4 HOH   149 449 107  HOH   HOH A . 
E 4 HOH   150 450 509  HOH   HOH A . 
E 4 HOH   151 451 163  HOH   HOH A . 
E 4 HOH   152 452 1276 HOH   HOH A . 
E 4 HOH   153 453 1134 HOH   HOH A . 
E 4 HOH   154 454 361  HOH   HOH A . 
E 4 HOH   155 455 726  HOH   HOH A . 
E 4 HOH   156 456 408  HOH   HOH A . 
E 4 HOH   157 457 756  HOH   HOH A . 
E 4 HOH   158 458 63   HOH   HOH A . 
E 4 HOH   159 459 801  HOH   HOH A . 
E 4 HOH   160 460 126  HOH   HOH A . 
E 4 HOH   161 461 280  HOH   HOH A . 
E 4 HOH   162 462 319  HOH   HOH A . 
E 4 HOH   163 463 556  HOH   HOH A . 
E 4 HOH   164 464 250  HOH   HOH A . 
E 4 HOH   165 465 1307 HOH   HOH A . 
E 4 HOH   166 466 342  HOH   HOH A . 
E 4 HOH   167 467 1306 HOH   HOH A . 
E 4 HOH   168 468 1287 HOH   HOH A . 
E 4 HOH   169 469 695  HOH   HOH A . 
E 4 HOH   170 470 267  HOH   HOH A . 
E 4 HOH   171 471 135  HOH   HOH A . 
E 4 HOH   172 472 370  HOH   HOH A . 
E 4 HOH   173 473 202  HOH   HOH A . 
E 4 HOH   174 474 919  HOH   HOH A . 
E 4 HOH   175 475 224  HOH   HOH A . 
E 4 HOH   176 476 674  HOH   HOH A . 
E 4 HOH   177 477 309  HOH   HOH A . 
E 4 HOH   178 478 318  HOH   HOH A . 
E 4 HOH   179 479 1299 HOH   HOH A . 
E 4 HOH   180 480 521  HOH   HOH A . 
E 4 HOH   181 481 805  HOH   HOH A . 
E 4 HOH   182 482 711  HOH   HOH A . 
E 4 HOH   183 483 331  HOH   HOH A . 
E 4 HOH   184 484 263  HOH   HOH A . 
E 4 HOH   185 485 326  HOH   HOH A . 
E 4 HOH   186 486 315  HOH   HOH A . 
E 4 HOH   187 487 152  HOH   HOH A . 
E 4 HOH   188 488 1314 HOH   HOH A . 
E 4 HOH   189 489 356  HOH   HOH A . 
E 4 HOH   190 490 208  HOH   HOH A . 
E 4 HOH   191 491 941  HOH   HOH A . 
E 4 HOH   192 492 1071 HOH   HOH A . 
E 4 HOH   193 493 180  HOH   HOH A . 
E 4 HOH   194 494 1284 HOH   HOH A . 
E 4 HOH   195 495 350  HOH   HOH A . 
E 4 HOH   196 496 363  HOH   HOH A . 
E 4 HOH   197 497 371  HOH   HOH A . 
E 4 HOH   198 498 313  HOH   HOH A . 
E 4 HOH   199 499 376  HOH   HOH A . 
E 4 HOH   200 500 429  HOH   HOH A . 
E 4 HOH   201 501 185  HOH   HOH A . 
E 4 HOH   202 502 772  HOH   HOH A . 
E 4 HOH   203 503 1074 HOH   HOH A . 
E 4 HOH   204 504 346  HOH   HOH A . 
E 4 HOH   205 505 1292 HOH   HOH A . 
E 4 HOH   206 506 1078 HOH   HOH A . 
F 4 HOH   1   201 64   HOH   HOH B . 
F 4 HOH   2   202 549  HOH   HOH B . 
F 4 HOH   3   203 358  HOH   HOH B . 
F 4 HOH   4   204 398  HOH   HOH B . 
F 4 HOH   5   205 364  HOH   HOH B . 
F 4 HOH   6   206 654  HOH   HOH B . 
F 4 HOH   7   207 240  HOH   HOH B . 
F 4 HOH   8   208 758  HOH   HOH B . 
F 4 HOH   9   209 1249 HOH   HOH B . 
F 4 HOH   10  210 900  HOH   HOH B . 
F 4 HOH   11  211 743  HOH   HOH B . 
F 4 HOH   12  212 120  HOH   HOH B . 
F 4 HOH   13  213 353  HOH   HOH B . 
F 4 HOH   14  214 531  HOH   HOH B . 
F 4 HOH   15  215 50   HOH   HOH B . 
F 4 HOH   16  216 1140 HOH   HOH B . 
F 4 HOH   17  217 343  HOH   HOH B . 
F 4 HOH   18  218 282  HOH   HOH B . 
F 4 HOH   19  219 276  HOH   HOH B . 
F 4 HOH   20  220 264  HOH   HOH B . 
F 4 HOH   21  221 232  HOH   HOH B . 
F 4 HOH   22  222 131  HOH   HOH B . 
F 4 HOH   23  223 444  HOH   HOH B . 
F 4 HOH   24  224 332  HOH   HOH B . 
F 4 HOH   25  225 75   HOH   HOH B . 
F 4 HOH   26  226 1278 HOH   HOH B . 
F 4 HOH   27  227 452  HOH   HOH B . 
F 4 HOH   28  228 128  HOH   HOH B . 
F 4 HOH   29  229 723  HOH   HOH B . 
F 4 HOH   30  230 54   HOH   HOH B . 
F 4 HOH   31  231 205  HOH   HOH B . 
F 4 HOH   32  232 82   HOH   HOH B . 
F 4 HOH   33  233 272  HOH   HOH B . 
F 4 HOH   34  234 127  HOH   HOH B . 
F 4 HOH   35  235 1312 HOH   HOH B . 
F 4 HOH   36  236 166  HOH   HOH B . 
F 4 HOH   37  237 181  HOH   HOH B . 
F 4 HOH   38  238 231  HOH   HOH B . 
F 4 HOH   39  239 69   HOH   HOH B . 
F 4 HOH   40  240 60   HOH   HOH B . 
F 4 HOH   41  241 1    HOH   HOH B . 
F 4 HOH   42  242 110  HOH   HOH B . 
F 4 HOH   43  243 172  HOH   HOH B . 
F 4 HOH   44  244 14   HOH   HOH B . 
F 4 HOH   45  245 129  HOH   HOH B . 
F 4 HOH   46  246 133  HOH   HOH B . 
F 4 HOH   47  247 52   HOH   HOH B . 
F 4 HOH   48  248 9    HOH   HOH B . 
F 4 HOH   49  249 30   HOH   HOH B . 
F 4 HOH   50  250 325  HOH   HOH B . 
F 4 HOH   51  251 300  HOH   HOH B . 
F 4 HOH   52  252 144  HOH   HOH B . 
F 4 HOH   53  253 103  HOH   HOH B . 
F 4 HOH   54  254 31   HOH   HOH B . 
F 4 HOH   55  255 271  HOH   HOH B . 
F 4 HOH   56  256 252  HOH   HOH B . 
F 4 HOH   57  257 10   HOH   HOH B . 
F 4 HOH   58  258 302  HOH   HOH B . 
F 4 HOH   59  259 47   HOH   HOH B . 
F 4 HOH   60  260 59   HOH   HOH B . 
F 4 HOH   61  261 143  HOH   HOH B . 
F 4 HOH   62  262 62   HOH   HOH B . 
F 4 HOH   63  263 1106 HOH   HOH B . 
F 4 HOH   64  264 347  HOH   HOH B . 
F 4 HOH   65  265 391  HOH   HOH B . 
F 4 HOH   66  266 41   HOH   HOH B . 
F 4 HOH   67  267 61   HOH   HOH B . 
F 4 HOH   68  268 72   HOH   HOH B . 
F 4 HOH   69  269 150  HOH   HOH B . 
F 4 HOH   70  270 221  HOH   HOH B . 
F 4 HOH   71  271 84   HOH   HOH B . 
F 4 HOH   72  272 77   HOH   HOH B . 
F 4 HOH   73  273 20   HOH   HOH B . 
F 4 HOH   74  274 117  HOH   HOH B . 
F 4 HOH   75  275 1277 HOH   HOH B . 
F 4 HOH   76  276 11   HOH   HOH B . 
F 4 HOH   77  277 242  HOH   HOH B . 
F 4 HOH   78  278 243  HOH   HOH B . 
F 4 HOH   79  279 114  HOH   HOH B . 
F 4 HOH   80  280 287  HOH   HOH B . 
F 4 HOH   81  281 22   HOH   HOH B . 
F 4 HOH   82  282 147  HOH   HOH B . 
F 4 HOH   83  283 43   HOH   HOH B . 
F 4 HOH   84  284 387  HOH   HOH B . 
F 4 HOH   85  285 106  HOH   HOH B . 
F 4 HOH   86  286 635  HOH   HOH B . 
F 4 HOH   87  287 299  HOH   HOH B . 
F 4 HOH   88  288 416  HOH   HOH B . 
F 4 HOH   89  289 13   HOH   HOH B . 
F 4 HOH   90  290 235  HOH   HOH B . 
F 4 HOH   91  291 175  HOH   HOH B . 
F 4 HOH   92  292 216  HOH   HOH B . 
F 4 HOH   93  293 1066 HOH   HOH B . 
F 4 HOH   94  294 99   HOH   HOH B . 
F 4 HOH   95  295 1305 HOH   HOH B . 
F 4 HOH   96  296 297  HOH   HOH B . 
F 4 HOH   97  297 704  HOH   HOH B . 
F 4 HOH   98  298 32   HOH   HOH B . 
F 4 HOH   99  299 141  HOH   HOH B . 
F 4 HOH   100 300 112  HOH   HOH B . 
F 4 HOH   101 301 316  HOH   HOH B . 
F 4 HOH   102 302 137  HOH   HOH B . 
F 4 HOH   103 303 89   HOH   HOH B . 
F 4 HOH   104 304 88   HOH   HOH B . 
F 4 HOH   105 305 160  HOH   HOH B . 
F 4 HOH   106 306 38   HOH   HOH B . 
F 4 HOH   107 307 142  HOH   HOH B . 
F 4 HOH   108 308 215  HOH   HOH B . 
F 4 HOH   109 309 311  HOH   HOH B . 
F 4 HOH   110 310 48   HOH   HOH B . 
F 4 HOH   111 311 220  HOH   HOH B . 
F 4 HOH   112 312 101  HOH   HOH B . 
F 4 HOH   113 313 118  HOH   HOH B . 
F 4 HOH   114 314 37   HOH   HOH B . 
F 4 HOH   115 315 1291 HOH   HOH B . 
F 4 HOH   116 316 1126 HOH   HOH B . 
F 4 HOH   117 317 91   HOH   HOH B . 
F 4 HOH   118 318 341  HOH   HOH B . 
F 4 HOH   119 319 170  HOH   HOH B . 
F 4 HOH   120 320 23   HOH   HOH B . 
F 4 HOH   121 321 182  HOH   HOH B . 
F 4 HOH   122 322 28   HOH   HOH B . 
F 4 HOH   123 323 44   HOH   HOH B . 
F 4 HOH   124 324 177  HOH   HOH B . 
F 4 HOH   125 325 1274 HOH   HOH B . 
F 4 HOH   126 326 100  HOH   HOH B . 
F 4 HOH   127 327 1285 HOH   HOH B . 
F 4 HOH   128 328 161  HOH   HOH B . 
F 4 HOH   129 329 29   HOH   HOH B . 
F 4 HOH   130 330 339  HOH   HOH B . 
F 4 HOH   131 331 717  HOH   HOH B . 
F 4 HOH   132 332 98   HOH   HOH B . 
F 4 HOH   133 333 334  HOH   HOH B . 
F 4 HOH   134 334 197  HOH   HOH B . 
F 4 HOH   135 335 234  HOH   HOH B . 
F 4 HOH   136 336 55   HOH   HOH B . 
F 4 HOH   137 337 445  HOH   HOH B . 
F 4 HOH   138 338 1294 HOH   HOH B . 
F 4 HOH   139 339 207  HOH   HOH B . 
F 4 HOH   140 340 65   HOH   HOH B . 
F 4 HOH   141 341 619  HOH   HOH B . 
F 4 HOH   142 342 1293 HOH   HOH B . 
F 4 HOH   143 343 178  HOH   HOH B . 
F 4 HOH   144 344 90   HOH   HOH B . 
F 4 HOH   145 345 362  HOH   HOH B . 
F 4 HOH   146 346 960  HOH   HOH B . 
F 4 HOH   147 347 463  HOH   HOH B . 
F 4 HOH   148 348 191  HOH   HOH B . 
F 4 HOH   149 349 335  HOH   HOH B . 
F 4 HOH   150 350 1304 HOH   HOH B . 
F 4 HOH   151 351 304  HOH   HOH B . 
F 4 HOH   152 352 623  HOH   HOH B . 
F 4 HOH   153 353 1046 HOH   HOH B . 
F 4 HOH   154 354 87   HOH   HOH B . 
F 4 HOH   155 355 1280 HOH   HOH B . 
F 4 HOH   156 356 541  HOH   HOH B . 
F 4 HOH   157 357 290  HOH   HOH B . 
F 4 HOH   158 358 203  HOH   HOH B . 
F 4 HOH   159 359 479  HOH   HOH B . 
F 4 HOH   160 360 389  HOH   HOH B . 
F 4 HOH   161 361 1077 HOH   HOH B . 
F 4 HOH   162 362 283  HOH   HOH B . 
F 4 HOH   163 363 718  HOH   HOH B . 
F 4 HOH   164 364 1072 HOH   HOH B . 
F 4 HOH   165 365 1316 HOH   HOH B . 
F 4 HOH   166 366 898  HOH   HOH B . 
F 4 HOH   167 367 340  HOH   HOH B . 
F 4 HOH   168 368 373  HOH   HOH B . 
F 4 HOH   169 369 667  HOH   HOH B . 
F 4 HOH   170 370 1303 HOH   HOH B . 
F 4 HOH   171 371 291  HOH   HOH B . 
F 4 HOH   172 372 615  HOH   HOH B . 
F 4 HOH   173 373 190  HOH   HOH B . 
F 4 HOH   174 374 310  HOH   HOH B . 
F 4 HOH   175 375 183  HOH   HOH B . 
F 4 HOH   176 376 149  HOH   HOH B . 
F 4 HOH   177 377 431  HOH   HOH B . 
F 4 HOH   178 378 1163 HOH   HOH B . 
F 4 HOH   179 379 1173 HOH   HOH B . 
F 4 HOH   180 380 1000 HOH   HOH B . 
F 4 HOH   181 381 418  HOH   HOH B . 
F 4 HOH   182 382 1311 HOH   HOH B . 
F 4 HOH   183 383 176  HOH   HOH B . 
F 4 HOH   184 384 424  HOH   HOH B . 
F 4 HOH   185 385 491  HOH   HOH B . 
F 4 HOH   186 386 470  HOH   HOH B . 
F 4 HOH   187 387 248  HOH   HOH B . 
F 4 HOH   188 388 981  HOH   HOH B . 
F 4 HOH   189 389 1298 HOH   HOH B . 
F 4 HOH   190 390 265  HOH   HOH B . 
F 4 HOH   191 391 184  HOH   HOH B . 
F 4 HOH   192 392 360  HOH   HOH B . 
F 4 HOH   193 393 410  HOH   HOH B . 
F 4 HOH   194 394 355  HOH   HOH B . 
F 4 HOH   195 395 274  HOH   HOH B . 
F 4 HOH   196 396 566  HOH   HOH B . 
F 4 HOH   197 397 314  HOH   HOH B . 
F 4 HOH   198 398 157  HOH   HOH B . 
F 4 HOH   199 399 792  HOH   HOH B . 
F 4 HOH   200 400 321  HOH   HOH B . 
F 4 HOH   201 401 558  HOH   HOH B . 
# 
loop_
_software.pdbx_ordinal 
_software.name 
_software.version 
_software.date 
_software.type 
_software.contact_author 
_software.contact_author_email 
_software.classification 
_software.location 
_software.language 
_software.citation_id 
1 PHENIX      1.21.1_5286    ?               package 'Paul D. Adams'   PDAdams@lbl.gov                         refinement        
http://www.phenix-online.org/                                                C++ ? 
2 Aimless     0.7.15         02/11/23        program 'Phil Evans'      ?                                       'data scaling'    
http://www.mrc-lmb.cam.ac.uk/harry/pre/aimless.html                          ?   ? 
3 PDB_EXTRACT 3.28           'Apr. 15, 2021' package PDB               deposit@deposit.rcsb.org                'data extraction' 
http://sw-tools.pdb.org/apps/PDB_EXTRACT/                                    C++ ? 
4 XDS         'Jun 30, 2023' 'Jun. 30, 2023' program 'Wolfgang Kabsch' Wolfgang.Kabsch@mpimf-heidelberg.mpg.de 'data reduction'  
http://xds.mpimf-heidelberg.mpg.de                                           ?   ? 
5 PHASER      2.8.3          'May 17, 2020'  program 'Randy J. Read'   cimr-phaser@lists.cam.ac.uk             phasing           
https://www.phaser.cimr.cam.ac.uk/index.php/Phaser_Crystallographic_Software ?   ? 
# 
_cell.entry_id           7HF9 
_cell.length_a           88.803 
_cell.length_b           88.803 
_cell.length_c           39.544 
_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                         7HF9 
_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          7HF9 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_Matthews      2.15 
_exptl_crystal.density_percent_sol   42.73 
_exptl_crystal.density_meas          ? 
_exptl_crystal.description           ? 
_exptl_crystal.preparation           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.pH              9.5 
_exptl_crystal_grow.temp            292 
_exptl_crystal_grow.pdbx_details    '100 mM CHES, 28% PEG 3000' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp_details    ? 
# 
_diffrn.id                               1 
_diffrn.crystal_id                       1 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.pdbx_serial_crystal_experiment   ? 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               PIXEL 
_diffrn_detector.type                   'DECTRIS PILATUS3 6M' 
_diffrn_detector.pdbx_collection_date   2023-08-11 
_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                        'SSRL BEAMLINE BL9-2' 
_diffrn_source.pdbx_wavelength_list        0.88557 
_diffrn_source.pdbx_synchrotron_site       SSRL 
_diffrn_source.pdbx_synchrotron_beamline   BL9-2 
_diffrn_source.pdbx_wavelength             ? 
# 
_reflns.entry_id                     7HF9 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             44.400 
_reflns.d_resolution_high            1.010 
_reflns.number_obs                   160689 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         99.600 
_reflns.pdbx_Rmerge_I_obs            0.040 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        17.700 
_reflns.B_iso_Wilson_estimate        11.820 
_reflns.pdbx_redundancy              6.600 
_reflns.pdbx_Rrim_I_all              0.043 
_reflns.pdbx_Rpim_I_all              0.017 
_reflns.pdbx_CC_half                 0.999 
_reflns.pdbx_netI_over_av_sigmaI     ? 
_reflns.pdbx_number_measured_all     1054177 
_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 1.010 1.030  ? 48935 7822 ? 1.568 ? ? ? 6.300 ? 1.100  ? ? ? ? ? ? 98.500 1.711 0.675 0.722 
1 2 5.530 44.400 ? 7538  1071 ? 0.026 ? ? ? 7.000 ? 71.400 ? ? ? ? ? ? 99.900 0.028 0.010 0.999 
# 
_refine.entry_id                                 7HF9 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_d_res_high                            1.0100 
_refine.ls_d_res_low                             44.4000 
_refine.pdbx_ls_sigma_F                          1.340 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.ls_percent_reflns_obs                    99.5200 
_refine.ls_number_reflns_obs                     160600 
_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                          0.1482 
_refine.ls_R_factor_R_work                       0.1475 
_refine.ls_wR_factor_R_work                      ? 
_refine.ls_R_factor_R_free                       0.1624 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_percent_reflns_R_free                 4.8200 
_refine.ls_number_reflns_R_free                  7739 
_refine.ls_number_reflns_R_work                  152861 
_refine.ls_R_factor_R_free_error                 ? 
_refine.B_iso_mean                               19.0617 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.overall_SU_R_free                        ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.overall_SU_ML                            0.1100 
_refine.overall_SU_B                             ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.pdbx_solvent_vdw_probe_radii             1.1000 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.B_iso_max                                64.300 
_refine.B_iso_min                                8.910 
_refine.pdbx_overall_phase_error                 19.1500 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_R_factor_R_free_error_details         ? 
# 
_refine_hist.cycle_id                         final 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.d_res_high                       1.0100 
_refine_hist.d_res_low                        44.4000 
_refine_hist.pdbx_number_atoms_ligand         38 
_refine_hist.number_atoms_solvent             407 
_refine_hist.number_atoms_total               2987 
_refine_hist.pdbx_number_residues_total       336 
_refine_hist.pdbx_B_iso_mean_ligand           14.13 
_refine_hist.pdbx_B_iso_mean_solvent          29.40 
_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 
1.0100 1.0200  30 98.0000  4974 . 0.3611 0.3882 . 246 0.0000 5220 . 'X-RAY DIFFRACTION' 
1.0200 1.0300  30 100.0000 5133 . 0.3163 0.3267 . 213 0.0000 5346 . 'X-RAY DIFFRACTION' 
1.0300 1.0500  30 100.0000 5081 . 0.2928 0.2928 . 293 0.0000 5374 . 'X-RAY DIFFRACTION' 
1.0500 1.0600  30 100.0000 4967 . 0.2709 0.2680 . 291 0.0000 5258 . 'X-RAY DIFFRACTION' 
1.0600 1.0700  30 100.0000 5132 . 0.2676 0.2854 . 265 0.0000 5397 . 'X-RAY DIFFRACTION' 
1.0700 1.0900  30 100.0000 5031 . 0.2406 0.2851 . 245 0.0000 5276 . 'X-RAY DIFFRACTION' 
1.0900 1.1000  30 99.0000  5065 . 0.2198 0.2394 . 254 0.0000 5319 . 'X-RAY DIFFRACTION' 
1.1000 1.1200  30 98.0000  4982 . 0.2015 0.2035 . 260 0.0000 5242 . 'X-RAY DIFFRACTION' 
1.1200 1.1400  30 100.0000 5131 . 0.1767 0.2073 . 221 0.0000 5352 . 'X-RAY DIFFRACTION' 
1.1400 1.1600  30 100.0000 5137 . 0.1621 0.1701 . 259 0.0000 5396 . 'X-RAY DIFFRACTION' 
1.1600 1.1800  30 100.0000 5051 . 0.1468 0.1629 . 264 0.0000 5315 . 'X-RAY DIFFRACTION' 
1.1800 1.2000  30 100.0000 5136 . 0.1450 0.1750 . 262 0.0000 5398 . 'X-RAY DIFFRACTION' 
1.2000 1.2200  30 100.0000 5014 . 0.1321 0.1663 . 282 0.0000 5296 . 'X-RAY DIFFRACTION' 
1.2200 1.2500  30 100.0000 5138 . 0.1326 0.1423 . 227 0.0000 5365 . 'X-RAY DIFFRACTION' 
1.2500 1.2700  30 98.0000  4997 . 0.1378 0.1671 . 234 0.0000 5231 . 'X-RAY DIFFRACTION' 
1.2700 1.3000  30 98.0000  5035 . 0.1333 0.1609 . 244 0.0000 5279 . 'X-RAY DIFFRACTION' 
1.3000 1.3300  30 100.0000 5059 . 0.1333 0.1441 . 297 0.0000 5356 . 'X-RAY DIFFRACTION' 
1.3400 1.3700  30 100.0000 5112 . 0.1366 0.1591 . 268 0.0000 5380 . 'X-RAY DIFFRACTION' 
1.3700 1.4100  30 100.0000 5164 . 0.1285 0.1668 . 228 0.0000 5392 . 'X-RAY DIFFRACTION' 
1.4100 1.4600  30 100.0000 5070 . 0.1260 0.1454 . 264 0.0000 5334 . 'X-RAY DIFFRACTION' 
1.4600 1.5100  30 100.0000 5117 . 0.1197 0.1378 . 254 0.0000 5371 . 'X-RAY DIFFRACTION' 
1.5100 1.5700  30 99.0000  5063 . 0.1202 0.1272 . 262 0.0000 5325 . 'X-RAY DIFFRACTION' 
1.5700 1.6400  30 99.0000  5069 . 0.1199 0.1340 . 268 0.0000 5337 . 'X-RAY DIFFRACTION' 
1.6400 1.7300  30 100.0000 5168 . 0.1264 0.1486 . 227 0.0000 5395 . 'X-RAY DIFFRACTION' 
1.7300 1.8400  30 100.0000 5111 . 0.1347 0.1383 . 266 0.0000 5377 . 'X-RAY DIFFRACTION' 
1.8400 1.9800  30 100.0000 5137 . 0.1365 0.1379 . 280 0.0000 5417 . 'X-RAY DIFFRACTION' 
1.9800 2.1800  30 100.0000 5101 . 0.1384 0.1571 . 282 0.0000 5383 . 'X-RAY DIFFRACTION' 
2.1800 2.4900  30 100.0000 5166 . 0.1388 0.1376 . 264 0.0000 5430 . 'X-RAY DIFFRACTION' 
2.4900 3.1400  30 100.0000 5194 . 0.1515 0.1648 . 257 0.0000 5451 . 'X-RAY DIFFRACTION' 
3.1400 44.4000 30 100.0000 5326 . 0.1497 0.1740 . 262 0.0000 5588 . 'X-RAY DIFFRACTION' 
# 
_struct.entry_id                  7HF9 
_struct.title                     
'PanDDA analysis group deposition -- Crystal structure of SARS-CoV-2 NSP3 macrodomain in complex with AVI-0004194' 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_details        ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HF9 
_struct_keywords.pdbx_keywords   'VIRAL PROTEIN, Hydrolase' 
_struct_keywords.text            'Macrodomain, ADP-ribose, SARS-CoV-2, fragment-based drug discovery, VIRAL PROTEIN, Hydrolase' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 4 ? 
F N N 4 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    R1AB_SARS2 
_struct_ref.pdbx_db_accession          P0DTD1 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;VNSFSGYLKLTDNVYIKNADIVEEAKKVKPTVVVNAANVYLKHGGGVAGALNKATNNAMQVESDDYIATNGPLKVGGSCV
LSGHNLAKHCLHVVGPNVNKGEDIQLLKSAYENFNQHEVLLAPLLSAGIFGADPIHSLRVCVDTVRTNVYLAVFDKNLYD
KLVSSFL
;
_struct_ref.pdbx_align_begin           1025 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 7HF9 A 3 ? 169 ? P0DTD1 1025 ? 1191 ? 3 169 
2 1 7HF9 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 7HF9 SER A 1 ? UNP P0DTD1 ? ? 'expression tag' 1 1 
1 7HF9 MET A 2 ? UNP P0DTD1 ? ? 'expression tag' 2 2 
2 7HF9 SER B 1 ? UNP P0DTD1 ? ? 'expression tag' 1 3 
2 7HF9 MET B 2 ? UNP P0DTD1 ? ? 'expression tag' 2 4 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C,D,E 
2 1 B,F     
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 ASP A 22  ? LYS A 31  ? ASP A 22  LYS A 31  1 ? 10 
HELX_P HELX_P2  AA2 GLY A 47  ? THR A 57  ? GLY A 47  THR A 57  1 ? 11 
HELX_P HELX_P3  AA3 ASN A 59  ? GLY A 73  ? ASN A 59  GLY A 73  1 ? 15 
HELX_P HELX_P4  AA4 ASN A 99  ? GLY A 103 ? ASN A 99  GLY A 103 5 ? 5  
HELX_P HELX_P5  AA5 GLN A 107 ? ASN A 115 ? GLN A 107 ASN A 115 1 ? 9  
HELX_P HELX_P6  AA6 PHE A 116 ? HIS A 119 ? PHE A 116 HIS A 119 5 ? 4  
HELX_P HELX_P7  AA7 ALA A 129 ? GLY A 133 ? ALA A 129 GLY A 133 5 ? 5  
HELX_P HELX_P8  AA8 ASP A 135 ? VAL A 147 ? ASP A 135 VAL A 147 1 ? 13 
HELX_P HELX_P9  AA9 ASP A 157 ? SER A 167 ? ASP A 157 SER A 167 1 ? 11 
HELX_P HELX_P10 AB1 ASP B 22  ? LYS B 31  ? ASP B 22  LYS B 31  1 ? 10 
HELX_P HELX_P11 AB2 GLY B 47  ? THR B 57  ? GLY B 47  THR B 57  1 ? 11 
HELX_P HELX_P12 AB3 ASN B 59  ? GLY B 73  ? ASN B 59  GLY B 73  1 ? 15 
HELX_P HELX_P13 AB4 ASN B 99  ? GLY B 103 ? ASN B 99  GLY B 103 5 ? 5  
HELX_P HELX_P14 AB5 ASP B 105 ? GLN B 107 ? ASP B 105 GLN B 107 5 ? 3  
HELX_P HELX_P15 AB6 LEU B 108 ? ASN B 115 ? LEU B 108 ASN B 115 1 ? 8  
HELX_P HELX_P16 AB7 PHE B 116 ? HIS B 119 ? PHE B 116 HIS B 119 5 ? 4  
HELX_P HELX_P17 AB8 ALA B 129 ? GLY B 133 ? ALA B 129 GLY B 133 5 ? 5  
HELX_P HELX_P18 AB9 ASP B 135 ? VAL B 147 ? ASP B 135 VAL B 147 1 ? 13 
HELX_P HELX_P19 AC1 ASP B 157 ? LEU B 169 ? ASP B 157 LEU B 169 1 ? 13 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 4 ? 
AA2 ? 3 ? 
AA3 ? 4 ? 
AA4 ? 3 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? parallel      
AA1 3 4 ? parallel      
AA2 1 2 ? parallel      
AA2 2 3 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? parallel      
AA3 3 4 ? parallel      
AA4 1 2 ? parallel      
AA4 2 3 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 LEU A 10  ? LYS A 11  ? LEU A 10  LYS A 11  
AA1 2 VAL A 16  ? ASN A 20  ? VAL A 16  ASN A 20  
AA1 3 ASN A 150 ? VAL A 155 ? ASN A 150 VAL A 155 
AA1 4 VAL A 121 ? ALA A 124 ? VAL A 121 ALA A 124 
AA2 1 VAL A 34  ? ALA A 38  ? VAL A 34  ALA A 38  
AA2 2 HIS A 91  ? VAL A 95  ? HIS A 91  VAL A 95  
AA2 3 SER A 80  ? SER A 84  ? SER A 80  SER A 84  
AA3 1 LEU B 10  ? LYS B 11  ? LEU B 10  LYS B 11  
AA3 2 VAL B 16  ? ASN B 20  ? VAL B 16  ASN B 20  
AA3 3 ASN B 150 ? VAL B 155 ? ASN B 150 VAL B 155 
AA3 4 VAL B 121 ? ALA B 124 ? VAL B 121 ALA B 124 
AA4 1 VAL B 34  ? ALA B 38  ? VAL B 34  ALA B 38  
AA4 2 HIS B 91  ? VAL B 95  ? HIS B 91  VAL B 95  
AA4 3 SER B 80  ? SER B 84  ? SER B 80  SER B 84  
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N LEU A 10  ? N LEU A 10  O ILE A 18  ? O ILE A 18  
AA1 2 3 N LYS A 19  ? N LYS A 19  O VAL A 155 ? O VAL A 155 
AA1 3 4 O TYR A 152 ? O TYR A 152 N LEU A 122 ? N LEU A 122 
AA2 1 2 N ASN A 37  ? N ASN A 37  O VAL A 95  ? O VAL A 95  
AA2 2 3 O CYS A 92  ? O CYS A 92  N LEU A 83  ? N LEU A 83  
AA3 1 2 N LEU B 10  ? N LEU B 10  O ILE B 18  ? O ILE B 18  
AA3 2 3 N TYR B 17  ? N TYR B 17  O LEU B 153 ? O LEU B 153 
AA3 3 4 O TYR B 152 ? O TYR B 152 N LEU B 122 ? N LEU B 122 
AA4 1 2 N ASN B 37  ? N ASN B 37  O LEU B 93  ? O LEU B 93  
AA4 2 3 O CYS B 92  ? O CYS B 92  N LEU B 83  ? N LEU B 83  
# 
_pdbx_entry_details.entry_id                   7HF9 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
_pdbx_validate_symm_contact.id                1 
_pdbx_validate_symm_contact.PDB_model_num     1 
_pdbx_validate_symm_contact.auth_atom_id_1    O 
_pdbx_validate_symm_contact.auth_asym_id_1    A 
_pdbx_validate_symm_contact.auth_comp_id_1    ASP 
_pdbx_validate_symm_contact.auth_seq_id_1     66 
_pdbx_validate_symm_contact.PDB_ins_code_1    ? 
_pdbx_validate_symm_contact.label_alt_id_1    ? 
_pdbx_validate_symm_contact.site_symmetry_1   1_555 
_pdbx_validate_symm_contact.auth_atom_id_2    HG 
_pdbx_validate_symm_contact.auth_asym_id_2    B 
_pdbx_validate_symm_contact.auth_comp_id_2    SER 
_pdbx_validate_symm_contact.auth_seq_id_2     1 
_pdbx_validate_symm_contact.PDB_ins_code_2    ? 
_pdbx_validate_symm_contact.label_alt_id_2    B 
_pdbx_validate_symm_contact.site_symmetry_2   2_655 
_pdbx_validate_symm_contact.dist              1.59 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 HIS A 86  ? ? 56.32   -133.64 
2 1 SER A 128 ? B 59.25   -8.39   
3 1 PHE A 156 ? B -100.76 52.54   
4 1 ASP A 157 ? B -172.27 119.56  
5 1 HIS B 86  ? ? 57.18   -127.91 
# 
_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 504 ? 5.92 . 
2 1 O ? A HOH 505 ? 6.03 . 
3 1 O ? A HOH 506 ? 7.58 . 
4 1 O ? B HOH 401 ? 6.32 . 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1 1 Y 1 A SER 1 ? A SER 1 
2 1 Y 1 A MET 2 ? A MET 2 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
A1BAV N2   N  Y N 1   
A1BAV C3   C  Y N 2   
A1BAV C6   C  Y N 3   
A1BAV C9   C  N N 4   
A1BAV C12  C  N N 5   
A1BAV C1   C  N N 6   
A1BAV C10  C  N N 7   
A1BAV C11  C  N N 8   
A1BAV C13  C  Y N 9   
A1BAV C2   C  Y N 10  
A1BAV C4   C  Y N 11  
A1BAV C5   C  Y N 12  
A1BAV C7   C  N N 13  
A1BAV C8   C  N N 14  
A1BAV N1   N  Y N 15  
A1BAV N3   N  Y N 16  
A1BAV N4   N  N N 17  
A1BAV O1   O  N N 18  
A1BAV O2   O  N N 19  
A1BAV H4   H  N N 20  
A1BAV H11  H  N N 21  
A1BAV H12  H  N N 22  
A1BAV H17  H  N N 23  
A1BAV H18  H  N N 24  
A1BAV H3   H  N N 25  
A1BAV H1   H  N N 26  
A1BAV H2   H  N N 27  
A1BAV H13  H  N N 28  
A1BAV H14  H  N N 29  
A1BAV H16  H  N N 30  
A1BAV H15  H  N N 31  
A1BAV H6   H  N N 32  
A1BAV H8   H  N N 33  
A1BAV H9   H  N N 34  
A1BAV H5   H  N N 35  
A1BAV H7   H  N N 36  
A1BAV H10  H  N N 37  
ALA   N    N  N N 38  
ALA   CA   C  N S 39  
ALA   C    C  N N 40  
ALA   O    O  N N 41  
ALA   CB   C  N N 42  
ALA   OXT  O  N N 43  
ALA   H    H  N N 44  
ALA   H2   H  N N 45  
ALA   HA   H  N N 46  
ALA   HB1  H  N N 47  
ALA   HB2  H  N N 48  
ALA   HB3  H  N N 49  
ALA   HXT  H  N N 50  
ARG   N    N  N N 51  
ARG   CA   C  N S 52  
ARG   C    C  N N 53  
ARG   O    O  N N 54  
ARG   CB   C  N N 55  
ARG   CG   C  N N 56  
ARG   CD   C  N N 57  
ARG   NE   N  N N 58  
ARG   CZ   C  N N 59  
ARG   NH1  N  N N 60  
ARG   NH2  N  N N 61  
ARG   OXT  O  N N 62  
ARG   H    H  N N 63  
ARG   H2   H  N N 64  
ARG   HA   H  N N 65  
ARG   HB2  H  N N 66  
ARG   HB3  H  N N 67  
ARG   HG2  H  N N 68  
ARG   HG3  H  N N 69  
ARG   HD2  H  N N 70  
ARG   HD3  H  N N 71  
ARG   HE   H  N N 72  
ARG   HH11 H  N N 73  
ARG   HH12 H  N N 74  
ARG   HH21 H  N N 75  
ARG   HH22 H  N N 76  
ARG   HXT  H  N N 77  
ASN   N    N  N N 78  
ASN   CA   C  N S 79  
ASN   C    C  N N 80  
ASN   O    O  N N 81  
ASN   CB   C  N N 82  
ASN   CG   C  N N 83  
ASN   OD1  O  N N 84  
ASN   ND2  N  N N 85  
ASN   OXT  O  N N 86  
ASN   H    H  N N 87  
ASN   H2   H  N N 88  
ASN   HA   H  N N 89  
ASN   HB2  H  N N 90  
ASN   HB3  H  N N 91  
ASN   HD21 H  N N 92  
ASN   HD22 H  N N 93  
ASN   HXT  H  N N 94  
ASP   N    N  N N 95  
ASP   CA   C  N S 96  
ASP   C    C  N N 97  
ASP   O    O  N N 98  
ASP   CB   C  N N 99  
ASP   CG   C  N N 100 
ASP   OD1  O  N N 101 
ASP   OD2  O  N N 102 
ASP   OXT  O  N N 103 
ASP   H    H  N N 104 
ASP   H2   H  N N 105 
ASP   HA   H  N N 106 
ASP   HB2  H  N N 107 
ASP   HB3  H  N N 108 
ASP   HD2  H  N N 109 
ASP   HXT  H  N N 110 
CL    CL   CL N N 111 
CYS   N    N  N N 112 
CYS   CA   C  N R 113 
CYS   C    C  N N 114 
CYS   O    O  N N 115 
CYS   CB   C  N N 116 
CYS   SG   S  N N 117 
CYS   OXT  O  N N 118 
CYS   H    H  N N 119 
CYS   H2   H  N N 120 
CYS   HA   H  N N 121 
CYS   HB2  H  N N 122 
CYS   HB3  H  N N 123 
CYS   HG   H  N N 124 
CYS   HXT  H  N N 125 
GLN   N    N  N N 126 
GLN   CA   C  N S 127 
GLN   C    C  N N 128 
GLN   O    O  N N 129 
GLN   CB   C  N N 130 
GLN   CG   C  N N 131 
GLN   CD   C  N N 132 
GLN   OE1  O  N N 133 
GLN   NE2  N  N N 134 
GLN   OXT  O  N N 135 
GLN   H    H  N N 136 
GLN   H2   H  N N 137 
GLN   HA   H  N N 138 
GLN   HB2  H  N N 139 
GLN   HB3  H  N N 140 
GLN   HG2  H  N N 141 
GLN   HG3  H  N N 142 
GLN   HE21 H  N N 143 
GLN   HE22 H  N N 144 
GLN   HXT  H  N N 145 
GLU   N    N  N N 146 
GLU   CA   C  N S 147 
GLU   C    C  N N 148 
GLU   O    O  N N 149 
GLU   CB   C  N N 150 
GLU   CG   C  N N 151 
GLU   CD   C  N N 152 
GLU   OE1  O  N N 153 
GLU   OE2  O  N N 154 
GLU   OXT  O  N N 155 
GLU   H    H  N N 156 
GLU   H2   H  N N 157 
GLU   HA   H  N N 158 
GLU   HB2  H  N N 159 
GLU   HB3  H  N N 160 
GLU   HG2  H  N N 161 
GLU   HG3  H  N N 162 
GLU   HE2  H  N N 163 
GLU   HXT  H  N N 164 
GLY   N    N  N N 165 
GLY   CA   C  N N 166 
GLY   C    C  N N 167 
GLY   O    O  N N 168 
GLY   OXT  O  N N 169 
GLY   H    H  N N 170 
GLY   H2   H  N N 171 
GLY   HA2  H  N N 172 
GLY   HA3  H  N N 173 
GLY   HXT  H  N N 174 
HIS   N    N  N N 175 
HIS   CA   C  N S 176 
HIS   C    C  N N 177 
HIS   O    O  N N 178 
HIS   CB   C  N N 179 
HIS   CG   C  Y N 180 
HIS   ND1  N  Y N 181 
HIS   CD2  C  Y N 182 
HIS   CE1  C  Y N 183 
HIS   NE2  N  Y N 184 
HIS   OXT  O  N N 185 
HIS   H    H  N N 186 
HIS   H2   H  N N 187 
HIS   HA   H  N N 188 
HIS   HB2  H  N N 189 
HIS   HB3  H  N N 190 
HIS   HD1  H  N N 191 
HIS   HD2  H  N N 192 
HIS   HE1  H  N N 193 
HIS   HE2  H  N N 194 
HIS   HXT  H  N N 195 
HOH   O    O  N N 196 
HOH   H1   H  N N 197 
HOH   H2   H  N N 198 
ILE   N    N  N N 199 
ILE   CA   C  N S 200 
ILE   C    C  N N 201 
ILE   O    O  N N 202 
ILE   CB   C  N S 203 
ILE   CG1  C  N N 204 
ILE   CG2  C  N N 205 
ILE   CD1  C  N N 206 
ILE   OXT  O  N N 207 
ILE   H    H  N N 208 
ILE   H2   H  N N 209 
ILE   HA   H  N N 210 
ILE   HB   H  N N 211 
ILE   HG12 H  N N 212 
ILE   HG13 H  N N 213 
ILE   HG21 H  N N 214 
ILE   HG22 H  N N 215 
ILE   HG23 H  N N 216 
ILE   HD11 H  N N 217 
ILE   HD12 H  N N 218 
ILE   HD13 H  N N 219 
ILE   HXT  H  N N 220 
LEU   N    N  N N 221 
LEU   CA   C  N S 222 
LEU   C    C  N N 223 
LEU   O    O  N N 224 
LEU   CB   C  N N 225 
LEU   CG   C  N N 226 
LEU   CD1  C  N N 227 
LEU   CD2  C  N N 228 
LEU   OXT  O  N N 229 
LEU   H    H  N N 230 
LEU   H2   H  N N 231 
LEU   HA   H  N N 232 
LEU   HB2  H  N N 233 
LEU   HB3  H  N N 234 
LEU   HG   H  N N 235 
LEU   HD11 H  N N 236 
LEU   HD12 H  N N 237 
LEU   HD13 H  N N 238 
LEU   HD21 H  N N 239 
LEU   HD22 H  N N 240 
LEU   HD23 H  N N 241 
LEU   HXT  H  N N 242 
LYS   N    N  N N 243 
LYS   CA   C  N S 244 
LYS   C    C  N N 245 
LYS   O    O  N N 246 
LYS   CB   C  N N 247 
LYS   CG   C  N N 248 
LYS   CD   C  N N 249 
LYS   CE   C  N N 250 
LYS   NZ   N  N N 251 
LYS   OXT  O  N N 252 
LYS   H    H  N N 253 
LYS   H2   H  N N 254 
LYS   HA   H  N N 255 
LYS   HB2  H  N N 256 
LYS   HB3  H  N N 257 
LYS   HG2  H  N N 258 
LYS   HG3  H  N N 259 
LYS   HD2  H  N N 260 
LYS   HD3  H  N N 261 
LYS   HE2  H  N N 262 
LYS   HE3  H  N N 263 
LYS   HZ1  H  N N 264 
LYS   HZ2  H  N N 265 
LYS   HZ3  H  N N 266 
LYS   HXT  H  N N 267 
MET   N    N  N N 268 
MET   CA   C  N S 269 
MET   C    C  N N 270 
MET   O    O  N N 271 
MET   CB   C  N N 272 
MET   CG   C  N N 273 
MET   SD   S  N N 274 
MET   CE   C  N N 275 
MET   OXT  O  N N 276 
MET   H    H  N N 277 
MET   H2   H  N N 278 
MET   HA   H  N N 279 
MET   HB2  H  N N 280 
MET   HB3  H  N N 281 
MET   HG2  H  N N 282 
MET   HG3  H  N N 283 
MET   HE1  H  N N 284 
MET   HE2  H  N N 285 
MET   HE3  H  N N 286 
MET   HXT  H  N N 287 
PHE   N    N  N N 288 
PHE   CA   C  N S 289 
PHE   C    C  N N 290 
PHE   O    O  N N 291 
PHE   CB   C  N N 292 
PHE   CG   C  Y N 293 
PHE   CD1  C  Y N 294 
PHE   CD2  C  Y N 295 
PHE   CE1  C  Y N 296 
PHE   CE2  C  Y N 297 
PHE   CZ   C  Y N 298 
PHE   OXT  O  N N 299 
PHE   H    H  N N 300 
PHE   H2   H  N N 301 
PHE   HA   H  N N 302 
PHE   HB2  H  N N 303 
PHE   HB3  H  N N 304 
PHE   HD1  H  N N 305 
PHE   HD2  H  N N 306 
PHE   HE1  H  N N 307 
PHE   HE2  H  N N 308 
PHE   HZ   H  N N 309 
PHE   HXT  H  N N 310 
PRO   N    N  N N 311 
PRO   CA   C  N S 312 
PRO   C    C  N N 313 
PRO   O    O  N N 314 
PRO   CB   C  N N 315 
PRO   CG   C  N N 316 
PRO   CD   C  N N 317 
PRO   OXT  O  N N 318 
PRO   H    H  N N 319 
PRO   HA   H  N N 320 
PRO   HB2  H  N N 321 
PRO   HB3  H  N N 322 
PRO   HG2  H  N N 323 
PRO   HG3  H  N N 324 
PRO   HD2  H  N N 325 
PRO   HD3  H  N N 326 
PRO   HXT  H  N N 327 
SER   N    N  N N 328 
SER   CA   C  N S 329 
SER   C    C  N N 330 
SER   O    O  N N 331 
SER   CB   C  N N 332 
SER   OG   O  N N 333 
SER   OXT  O  N N 334 
SER   H    H  N N 335 
SER   H2   H  N N 336 
SER   HA   H  N N 337 
SER   HB2  H  N N 338 
SER   HB3  H  N N 339 
SER   HG   H  N N 340 
SER   HXT  H  N N 341 
THR   N    N  N N 342 
THR   CA   C  N S 343 
THR   C    C  N N 344 
THR   O    O  N N 345 
THR   CB   C  N R 346 
THR   OG1  O  N N 347 
THR   CG2  C  N N 348 
THR   OXT  O  N N 349 
THR   H    H  N N 350 
THR   H2   H  N N 351 
THR   HA   H  N N 352 
THR   HB   H  N N 353 
THR   HG1  H  N N 354 
THR   HG21 H  N N 355 
THR   HG22 H  N N 356 
THR   HG23 H  N N 357 
THR   HXT  H  N N 358 
TYR   N    N  N N 359 
TYR   CA   C  N S 360 
TYR   C    C  N N 361 
TYR   O    O  N N 362 
TYR   CB   C  N N 363 
TYR   CG   C  Y N 364 
TYR   CD1  C  Y N 365 
TYR   CD2  C  Y N 366 
TYR   CE1  C  Y N 367 
TYR   CE2  C  Y N 368 
TYR   CZ   C  Y N 369 
TYR   OH   O  N N 370 
TYR   OXT  O  N N 371 
TYR   H    H  N N 372 
TYR   H2   H  N N 373 
TYR   HA   H  N N 374 
TYR   HB2  H  N N 375 
TYR   HB3  H  N N 376 
TYR   HD1  H  N N 377 
TYR   HD2  H  N N 378 
TYR   HE1  H  N N 379 
TYR   HE2  H  N N 380 
TYR   HH   H  N N 381 
TYR   HXT  H  N N 382 
VAL   N    N  N N 383 
VAL   CA   C  N S 384 
VAL   C    C  N N 385 
VAL   O    O  N N 386 
VAL   CB   C  N N 387 
VAL   CG1  C  N N 388 
VAL   CG2  C  N N 389 
VAL   OXT  O  N N 390 
VAL   H    H  N N 391 
VAL   H2   H  N N 392 
VAL   HA   H  N N 393 
VAL   HB   H  N N 394 
VAL   HG11 H  N N 395 
VAL   HG12 H  N N 396 
VAL   HG13 H  N N 397 
VAL   HG21 H  N N 398 
VAL   HG22 H  N N 399 
VAL   HG23 H  N N 400 
VAL   HXT  H  N N 401 
# 
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 
A1BAV O2  C10  sing N N 1   
A1BAV O2  C11  sing N N 2   
A1BAV C10 C9   sing N N 3   
A1BAV C12 C11  sing N N 4   
A1BAV C12 C8   sing N N 5   
A1BAV C9  C8   sing N N 6   
A1BAV C8  C7   sing N N 7   
A1BAV C8  O1   sing N N 8   
A1BAV C7  N4   sing N N 9   
A1BAV N4  C6   sing N N 10  
A1BAV C1  C2   sing N N 11  
A1BAV C6  C13  doub Y N 12  
A1BAV C6  N3   sing Y N 13  
A1BAV C2  C13  sing Y N 14  
A1BAV C2  C3   doub Y N 15  
A1BAV C13 C4   sing Y N 16  
A1BAV N3  C5   doub Y N 17  
A1BAV C3  N1   sing Y N 18  
A1BAV C4  N1   sing Y N 19  
A1BAV C4  N2   doub Y N 20  
A1BAV C5  N2   sing Y N 21  
A1BAV C3  H4   sing N N 22  
A1BAV C9  H11  sing N N 23  
A1BAV C9  H12  sing N N 24  
A1BAV C12 H17  sing N N 25  
A1BAV C12 H18  sing N N 26  
A1BAV C1  H3   sing N N 27  
A1BAV C1  H1   sing N N 28  
A1BAV C1  H2   sing N N 29  
A1BAV C10 H13  sing N N 30  
A1BAV C10 H14  sing N N 31  
A1BAV C11 H16  sing N N 32  
A1BAV C11 H15  sing N N 33  
A1BAV C5  H6   sing N N 34  
A1BAV C7  H8   sing N N 35  
A1BAV C7  H9   sing N N 36  
A1BAV N1  H5   sing N N 37  
A1BAV N4  H7   sing N N 38  
A1BAV O1  H10  sing N N 39  
ALA   N   CA   sing N N 40  
ALA   N   H    sing N N 41  
ALA   N   H2   sing N N 42  
ALA   CA  C    sing N N 43  
ALA   CA  CB   sing N N 44  
ALA   CA  HA   sing N N 45  
ALA   C   O    doub N N 46  
ALA   C   OXT  sing N N 47  
ALA   CB  HB1  sing N N 48  
ALA   CB  HB2  sing N N 49  
ALA   CB  HB3  sing N N 50  
ALA   OXT HXT  sing N N 51  
ARG   N   CA   sing N N 52  
ARG   N   H    sing N N 53  
ARG   N   H2   sing N N 54  
ARG   CA  C    sing N N 55  
ARG   CA  CB   sing N N 56  
ARG   CA  HA   sing N N 57  
ARG   C   O    doub N N 58  
ARG   C   OXT  sing N N 59  
ARG   CB  CG   sing N N 60  
ARG   CB  HB2  sing N N 61  
ARG   CB  HB3  sing N N 62  
ARG   CG  CD   sing N N 63  
ARG   CG  HG2  sing N N 64  
ARG   CG  HG3  sing N N 65  
ARG   CD  NE   sing N N 66  
ARG   CD  HD2  sing N N 67  
ARG   CD  HD3  sing N N 68  
ARG   NE  CZ   sing N N 69  
ARG   NE  HE   sing N N 70  
ARG   CZ  NH1  sing N N 71  
ARG   CZ  NH2  doub N N 72  
ARG   NH1 HH11 sing N N 73  
ARG   NH1 HH12 sing N N 74  
ARG   NH2 HH21 sing N N 75  
ARG   NH2 HH22 sing N N 76  
ARG   OXT HXT  sing N N 77  
ASN   N   CA   sing N N 78  
ASN   N   H    sing N N 79  
ASN   N   H2   sing N N 80  
ASN   CA  C    sing N N 81  
ASN   CA  CB   sing N N 82  
ASN   CA  HA   sing N N 83  
ASN   C   O    doub N N 84  
ASN   C   OXT  sing N N 85  
ASN   CB  CG   sing N N 86  
ASN   CB  HB2  sing N N 87  
ASN   CB  HB3  sing N N 88  
ASN   CG  OD1  doub N N 89  
ASN   CG  ND2  sing N N 90  
ASN   ND2 HD21 sing N N 91  
ASN   ND2 HD22 sing N N 92  
ASN   OXT HXT  sing N N 93  
ASP   N   CA   sing N N 94  
ASP   N   H    sing N N 95  
ASP   N   H2   sing N N 96  
ASP   CA  C    sing N N 97  
ASP   CA  CB   sing N N 98  
ASP   CA  HA   sing N N 99  
ASP   C   O    doub N N 100 
ASP   C   OXT  sing N N 101 
ASP   CB  CG   sing N N 102 
ASP   CB  HB2  sing N N 103 
ASP   CB  HB3  sing N N 104 
ASP   CG  OD1  doub N N 105 
ASP   CG  OD2  sing N N 106 
ASP   OD2 HD2  sing N N 107 
ASP   OXT HXT  sing N N 108 
CYS   N   CA   sing N N 109 
CYS   N   H    sing N N 110 
CYS   N   H2   sing N N 111 
CYS   CA  C    sing N N 112 
CYS   CA  CB   sing N N 113 
CYS   CA  HA   sing N N 114 
CYS   C   O    doub N N 115 
CYS   C   OXT  sing N N 116 
CYS   CB  SG   sing N N 117 
CYS   CB  HB2  sing N N 118 
CYS   CB  HB3  sing N N 119 
CYS   SG  HG   sing N N 120 
CYS   OXT HXT  sing N N 121 
GLN   N   CA   sing N N 122 
GLN   N   H    sing N N 123 
GLN   N   H2   sing N N 124 
GLN   CA  C    sing N N 125 
GLN   CA  CB   sing N N 126 
GLN   CA  HA   sing N N 127 
GLN   C   O    doub N N 128 
GLN   C   OXT  sing N N 129 
GLN   CB  CG   sing N N 130 
GLN   CB  HB2  sing N N 131 
GLN   CB  HB3  sing N N 132 
GLN   CG  CD   sing N N 133 
GLN   CG  HG2  sing N N 134 
GLN   CG  HG3  sing N N 135 
GLN   CD  OE1  doub N N 136 
GLN   CD  NE2  sing N N 137 
GLN   NE2 HE21 sing N N 138 
GLN   NE2 HE22 sing N N 139 
GLN   OXT HXT  sing N N 140 
GLU   N   CA   sing N N 141 
GLU   N   H    sing N N 142 
GLU   N   H2   sing N N 143 
GLU   CA  C    sing N N 144 
GLU   CA  CB   sing N N 145 
GLU   CA  HA   sing N N 146 
GLU   C   O    doub N N 147 
GLU   C   OXT  sing N N 148 
GLU   CB  CG   sing N N 149 
GLU   CB  HB2  sing N N 150 
GLU   CB  HB3  sing N N 151 
GLU   CG  CD   sing N N 152 
GLU   CG  HG2  sing N N 153 
GLU   CG  HG3  sing N N 154 
GLU   CD  OE1  doub N N 155 
GLU   CD  OE2  sing N N 156 
GLU   OE2 HE2  sing N N 157 
GLU   OXT HXT  sing N N 158 
GLY   N   CA   sing N N 159 
GLY   N   H    sing N N 160 
GLY   N   H2   sing N N 161 
GLY   CA  C    sing N N 162 
GLY   CA  HA2  sing N N 163 
GLY   CA  HA3  sing N N 164 
GLY   C   O    doub N N 165 
GLY   C   OXT  sing N N 166 
GLY   OXT HXT  sing N N 167 
HIS   N   CA   sing N N 168 
HIS   N   H    sing N N 169 
HIS   N   H2   sing N N 170 
HIS   CA  C    sing N N 171 
HIS   CA  CB   sing N N 172 
HIS   CA  HA   sing N N 173 
HIS   C   O    doub N N 174 
HIS   C   OXT  sing N N 175 
HIS   CB  CG   sing N N 176 
HIS   CB  HB2  sing N N 177 
HIS   CB  HB3  sing N N 178 
HIS   CG  ND1  sing Y N 179 
HIS   CG  CD2  doub Y N 180 
HIS   ND1 CE1  doub Y N 181 
HIS   ND1 HD1  sing N N 182 
HIS   CD2 NE2  sing Y N 183 
HIS   CD2 HD2  sing N N 184 
HIS   CE1 NE2  sing Y N 185 
HIS   CE1 HE1  sing N N 186 
HIS   NE2 HE2  sing N N 187 
HIS   OXT HXT  sing N N 188 
HOH   O   H1   sing N N 189 
HOH   O   H2   sing N N 190 
ILE   N   CA   sing N N 191 
ILE   N   H    sing N N 192 
ILE   N   H2   sing N N 193 
ILE   CA  C    sing N N 194 
ILE   CA  CB   sing N N 195 
ILE   CA  HA   sing N N 196 
ILE   C   O    doub N N 197 
ILE   C   OXT  sing N N 198 
ILE   CB  CG1  sing N N 199 
ILE   CB  CG2  sing N N 200 
ILE   CB  HB   sing N N 201 
ILE   CG1 CD1  sing N N 202 
ILE   CG1 HG12 sing N N 203 
ILE   CG1 HG13 sing N N 204 
ILE   CG2 HG21 sing N N 205 
ILE   CG2 HG22 sing N N 206 
ILE   CG2 HG23 sing N N 207 
ILE   CD1 HD11 sing N N 208 
ILE   CD1 HD12 sing N N 209 
ILE   CD1 HD13 sing N N 210 
ILE   OXT HXT  sing N N 211 
LEU   N   CA   sing N N 212 
LEU   N   H    sing N N 213 
LEU   N   H2   sing N N 214 
LEU   CA  C    sing N N 215 
LEU   CA  CB   sing N N 216 
LEU   CA  HA   sing N N 217 
LEU   C   O    doub N N 218 
LEU   C   OXT  sing N N 219 
LEU   CB  CG   sing N N 220 
LEU   CB  HB2  sing N N 221 
LEU   CB  HB3  sing N N 222 
LEU   CG  CD1  sing N N 223 
LEU   CG  CD2  sing N N 224 
LEU   CG  HG   sing N N 225 
LEU   CD1 HD11 sing N N 226 
LEU   CD1 HD12 sing N N 227 
LEU   CD1 HD13 sing N N 228 
LEU   CD2 HD21 sing N N 229 
LEU   CD2 HD22 sing N N 230 
LEU   CD2 HD23 sing N N 231 
LEU   OXT HXT  sing N N 232 
LYS   N   CA   sing N N 233 
LYS   N   H    sing N N 234 
LYS   N   H2   sing N N 235 
LYS   CA  C    sing N N 236 
LYS   CA  CB   sing N N 237 
LYS   CA  HA   sing N N 238 
LYS   C   O    doub N N 239 
LYS   C   OXT  sing N N 240 
LYS   CB  CG   sing N N 241 
LYS   CB  HB2  sing N N 242 
LYS   CB  HB3  sing N N 243 
LYS   CG  CD   sing N N 244 
LYS   CG  HG2  sing N N 245 
LYS   CG  HG3  sing N N 246 
LYS   CD  CE   sing N N 247 
LYS   CD  HD2  sing N N 248 
LYS   CD  HD3  sing N N 249 
LYS   CE  NZ   sing N N 250 
LYS   CE  HE2  sing N N 251 
LYS   CE  HE3  sing N N 252 
LYS   NZ  HZ1  sing N N 253 
LYS   NZ  HZ2  sing N N 254 
LYS   NZ  HZ3  sing N N 255 
LYS   OXT HXT  sing N N 256 
MET   N   CA   sing N N 257 
MET   N   H    sing N N 258 
MET   N   H2   sing N N 259 
MET   CA  C    sing N N 260 
MET   CA  CB   sing N N 261 
MET   CA  HA   sing N N 262 
MET   C   O    doub N N 263 
MET   C   OXT  sing N N 264 
MET   CB  CG   sing N N 265 
MET   CB  HB2  sing N N 266 
MET   CB  HB3  sing N N 267 
MET   CG  SD   sing N N 268 
MET   CG  HG2  sing N N 269 
MET   CG  HG3  sing N N 270 
MET   SD  CE   sing N N 271 
MET   CE  HE1  sing N N 272 
MET   CE  HE2  sing N N 273 
MET   CE  HE3  sing N N 274 
MET   OXT HXT  sing N N 275 
PHE   N   CA   sing N N 276 
PHE   N   H    sing N N 277 
PHE   N   H2   sing N N 278 
PHE   CA  C    sing N N 279 
PHE   CA  CB   sing N N 280 
PHE   CA  HA   sing N N 281 
PHE   C   O    doub N N 282 
PHE   C   OXT  sing N N 283 
PHE   CB  CG   sing N N 284 
PHE   CB  HB2  sing N N 285 
PHE   CB  HB3  sing N N 286 
PHE   CG  CD1  doub Y N 287 
PHE   CG  CD2  sing Y N 288 
PHE   CD1 CE1  sing Y N 289 
PHE   CD1 HD1  sing N N 290 
PHE   CD2 CE2  doub Y N 291 
PHE   CD2 HD2  sing N N 292 
PHE   CE1 CZ   doub Y N 293 
PHE   CE1 HE1  sing N N 294 
PHE   CE2 CZ   sing Y N 295 
PHE   CE2 HE2  sing N N 296 
PHE   CZ  HZ   sing N N 297 
PHE   OXT HXT  sing N N 298 
PRO   N   CA   sing N N 299 
PRO   N   CD   sing N N 300 
PRO   N   H    sing N N 301 
PRO   CA  C    sing N N 302 
PRO   CA  CB   sing N N 303 
PRO   CA  HA   sing N N 304 
PRO   C   O    doub N N 305 
PRO   C   OXT  sing N N 306 
PRO   CB  CG   sing N N 307 
PRO   CB  HB2  sing N N 308 
PRO   CB  HB3  sing N N 309 
PRO   CG  CD   sing N N 310 
PRO   CG  HG2  sing N N 311 
PRO   CG  HG3  sing N N 312 
PRO   CD  HD2  sing N N 313 
PRO   CD  HD3  sing N N 314 
PRO   OXT HXT  sing N N 315 
SER   N   CA   sing N N 316 
SER   N   H    sing N N 317 
SER   N   H2   sing N N 318 
SER   CA  C    sing N N 319 
SER   CA  CB   sing N N 320 
SER   CA  HA   sing N N 321 
SER   C   O    doub N N 322 
SER   C   OXT  sing N N 323 
SER   CB  OG   sing N N 324 
SER   CB  HB2  sing N N 325 
SER   CB  HB3  sing N N 326 
SER   OG  HG   sing N N 327 
SER   OXT HXT  sing N N 328 
THR   N   CA   sing N N 329 
THR   N   H    sing N N 330 
THR   N   H2   sing N N 331 
THR   CA  C    sing N N 332 
THR   CA  CB   sing N N 333 
THR   CA  HA   sing N N 334 
THR   C   O    doub N N 335 
THR   C   OXT  sing N N 336 
THR   CB  OG1  sing N N 337 
THR   CB  CG2  sing N N 338 
THR   CB  HB   sing N N 339 
THR   OG1 HG1  sing N N 340 
THR   CG2 HG21 sing N N 341 
THR   CG2 HG22 sing N N 342 
THR   CG2 HG23 sing N N 343 
THR   OXT HXT  sing N N 344 
TYR   N   CA   sing N N 345 
TYR   N   H    sing N N 346 
TYR   N   H2   sing N N 347 
TYR   CA  C    sing N N 348 
TYR   CA  CB   sing N N 349 
TYR   CA  HA   sing N N 350 
TYR   C   O    doub N N 351 
TYR   C   OXT  sing N N 352 
TYR   CB  CG   sing N N 353 
TYR   CB  HB2  sing N N 354 
TYR   CB  HB3  sing N N 355 
TYR   CG  CD1  doub Y N 356 
TYR   CG  CD2  sing Y N 357 
TYR   CD1 CE1  sing Y N 358 
TYR   CD1 HD1  sing N N 359 
TYR   CD2 CE2  doub Y N 360 
TYR   CD2 HD2  sing N N 361 
TYR   CE1 CZ   doub Y N 362 
TYR   CE1 HE1  sing N N 363 
TYR   CE2 CZ   sing Y N 364 
TYR   CE2 HE2  sing N N 365 
TYR   CZ  OH   sing N N 366 
TYR   OH  HH   sing N N 367 
TYR   OXT HXT  sing N N 368 
VAL   N   CA   sing N N 369 
VAL   N   H    sing N N 370 
VAL   N   H2   sing N N 371 
VAL   CA  C    sing N N 372 
VAL   CA  CB   sing N N 373 
VAL   CA  HA   sing N N 374 
VAL   C   O    doub N N 375 
VAL   C   OXT  sing N N 376 
VAL   CB  CG1  sing N N 377 
VAL   CB  CG2  sing N N 378 
VAL   CB  HB   sing N N 379 
VAL   CG1 HG11 sing N N 380 
VAL   CG1 HG12 sing N N 381 
VAL   CG1 HG13 sing N N 382 
VAL   CG2 HG21 sing N N 383 
VAL   CG2 HG22 sing N N 384 
VAL   CG2 HG23 sing N N 385 
VAL   OXT HXT  sing N N 386 
# 
_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                    7HF9 
_atom_sites.fract_transf_matrix[1][1]   0.011261 
_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]   0.011261 
_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]   0.025288 
_atom_sites.fract_transf_vector[1]      0.000000 
_atom_sites.fract_transf_vector[2]      0.000000 
_atom_sites.fract_transf_vector[3]      0.000000 
# 
loop_
_atom_type.symbol 
C  
CL 
H  
N  
O  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N    A VAL   A 1 3   ? 19.699 -16.338 22.284  0.82 49.22 ?  3   VAL   A N    1 
ATOM   2    N  N    B VAL   A 1 3   ? 19.633 -16.320 22.343  0.18 48.17 ?  3   VAL   A N    1 
ATOM   3    C  CA   A VAL   A 1 3   ? 18.740 -15.256 22.470  0.82 48.90 ?  3   VAL   A CA   1 
ATOM   4    C  CA   B VAL   A 1 3   ? 18.698 -15.219 22.538  0.18 47.96 ?  3   VAL   A CA   1 
ATOM   5    C  C    A VAL   A 1 3   ? 19.393 -13.912 22.167  0.82 47.50 ?  3   VAL   A C    1 
ATOM   6    C  C    B VAL   A 1 3   ? 19.367 -13.891 22.209  0.18 47.01 ?  3   VAL   A C    1 
ATOM   7    O  O    A VAL   A 1 3   ? 20.509 -13.640 22.610  0.82 47.77 ?  3   VAL   A O    1 
ATOM   8    O  O    B VAL   A 1 3   ? 20.470 -13.609 22.677  0.18 47.32 ?  3   VAL   A O    1 
ATOM   9    C  CB   A VAL   A 1 3   ? 18.132 -15.285 23.889  0.82 49.66 ?  3   VAL   A CB   1 
ATOM   10   C  CB   B VAL   A 1 3   ? 18.129 -15.214 23.970  0.18 48.46 ?  3   VAL   A CB   1 
ATOM   11   C  CG1  A VAL   A 1 3   ? 17.127 -14.153 24.066  0.82 49.89 ?  3   VAL   A CG1  1 
ATOM   12   C  CG1  B VAL   A 1 3   ? 17.161 -14.053 24.155  0.18 48.61 ?  3   VAL   A CG1  1 
ATOM   13   C  CG2  A VAL   A 1 3   ? 17.473 -16.633 24.154  0.82 49.87 ?  3   VAL   A CG2  1 
ATOM   14   C  CG2  B VAL   A 1 3   ? 17.444 -16.538 24.276  0.18 48.61 ?  3   VAL   A CG2  1 
ATOM   15   H  HA   A VAL   A 1 3   ? 18.013 -15.371 21.844  0.82 58.72 ?  3   VAL   A HA   1 
ATOM   16   H  HA   B VAL   A 1 3   ? 17.952 -15.329 21.930  0.18 57.58 ?  3   VAL   A HA   1 
ATOM   17   H  HB   A VAL   A 1 3   ? 18.838 -15.163 24.542  0.82 59.63 ?  3   VAL   A HB   1 
ATOM   18   H  HB   B VAL   A 1 3   ? 18.856 -15.100 24.602  0.18 58.19 ?  3   VAL   A HB   1 
ATOM   19   H  HG11 A VAL   A 1 3   ? 16.628 -14.300 24.885  0.82 59.91 ?  3   VAL   A HG11 1 
ATOM   20   H  HG11 B VAL   A 1 3   ? 16.675 -14.178 24.985  0.18 58.37 ?  3   VAL   A HG11 1 
ATOM   21   H  HG12 A VAL   A 1 3   ? 17.604 -13.310 24.118  0.82 59.91 ?  3   VAL   A HG12 1 
ATOM   22   H  HG12 B VAL   A 1 3   ? 17.662 -13.223 24.188  0.18 58.37 ?  3   VAL   A HG12 1 
ATOM   23   H  HG13 A VAL   A 1 3   ? 16.522 -14.147 23.308  0.82 59.91 ?  3   VAL   A HG13 1 
ATOM   24   H  HG13 B VAL   A 1 3   ? 16.541 -14.038 23.409  0.18 58.37 ?  3   VAL   A HG13 1 
ATOM   25   H  HG21 A VAL   A 1 3   ? 17.040 -16.608 25.022  0.82 59.88 ?  3   VAL   A HG21 1 
ATOM   26   H  HG21 B VAL   A 1 3   ? 17.038 -16.488 25.155  0.18 58.37 ?  3   VAL   A HG21 1 
ATOM   27   H  HG22 A VAL   A 1 3   ? 16.816 -16.804 23.461  0.82 59.88 ?  3   VAL   A HG22 1 
ATOM   28   H  HG22 B VAL   A 1 3   ? 16.763 -16.702 23.605  0.18 58.37 ?  3   VAL   A HG22 1 
ATOM   29   H  HG23 A VAL   A 1 3   ? 18.153 -17.325 24.143  0.82 59.88 ?  3   VAL   A HG23 1 
ATOM   30   H  HG23 B VAL   A 1 3   ? 18.105 -17.248 24.257  0.18 58.37 ?  3   VAL   A HG23 1 
ATOM   31   N  N    . ASN   A 1 4   ? 18.694 -13.079 21.396  1.00 45.50 ?  4   ASN   A N    1 
ATOM   32   C  CA   . ASN   A 1 4   ? 19.146 -11.732 21.071  1.00 41.67 ?  4   ASN   A CA   1 
ATOM   33   C  C    . ASN   A 1 4   ? 17.999 -10.756 21.309  1.00 38.42 ?  4   ASN   A C    1 
ATOM   34   O  O    . ASN   A 1 4   ? 16.878 -11.150 21.646  1.00 38.11 ?  4   ASN   A O    1 
ATOM   35   C  CB   . ASN   A 1 4   ? 19.704 -11.636 19.643  1.00 40.88 ?  4   ASN   A CB   1 
ATOM   36   C  CG   . ASN   A 1 4   ? 18.685 -12.003 18.587  1.00 40.04 ?  4   ASN   A CG   1 
ATOM   37   O  OD1  . ASN   A 1 4   ? 17.587 -11.448 18.547  1.00 39.79 ?  4   ASN   A OD1  1 
ATOM   38   N  ND2  . ASN   A 1 4   ? 19.046 -12.944 17.720  1.00 39.64 ?  4   ASN   A ND2  1 
ATOM   39   H  H    A ASN   A 1 4   ? 17.938 -13.283 21.037  0.82 54.64 ?  4   ASN   A H    1 
ATOM   40   H  H    B ASN   A 1 4   ? 17.951 -13.293 21.017  0.18 54.64 ?  4   ASN   A H    1 
ATOM   41   H  HA   . ASN   A 1 4   ? 19.864 -11.494 21.672  1.00 50.04 ?  4   ASN   A HA   1 
ATOM   42   H  HB2  . ASN   A 1 4   ? 19.991 -10.722 19.478  1.00 49.10 ?  4   ASN   A HB2  1 
ATOM   43   H  HB3  . ASN   A 1 4   ? 20.457 -12.239 19.556  1.00 49.10 ?  4   ASN   A HB3  1 
ATOM   44   H  HD21 . ASN   A 1 4   ? 18.505 -13.189 17.098  1.00 47.61 ?  4   ASN   A HD21 1 
ATOM   45   H  HD22 . ASN   A 1 4   ? 19.823 -13.310 17.782  1.00 47.61 ?  4   ASN   A HD22 1 
ATOM   46   N  N    . SER   A 1 5   ? 18.284 -9.467  21.128  1.00 35.25 ?  5   SER   A N    1 
ATOM   47   C  CA   . SER   A 1 5   ? 17.368 -8.404  21.519  1.00 32.25 ?  5   SER   A CA   1 
ATOM   48   C  C    . SER   A 1 5   ? 16.487 -7.907  20.375  1.00 28.75 ?  5   SER   A C    1 
ATOM   49   O  O    . SER   A 1 5   ? 15.754 -6.931  20.558  1.00 28.84 ?  5   SER   A O    1 
ATOM   50   C  CB   . SER   A 1 5   ? 18.140 -7.235  22.135  1.00 32.89 ?  5   SER   A CB   1 
ATOM   51   O  OG   . SER   A 1 5   ? 19.051 -6.678  21.205  1.00 33.17 ?  5   SER   A OG   1 
ATOM   52   H  H    . SER   A 1 5   ? 19.015 -9.183  20.771  1.00 42.34 ?  5   SER   A H    1 
ATOM   53   H  HA   . SER   A 1 5   ? 16.785 -8.751  22.209  1.00 38.74 ?  5   SER   A HA   1 
ATOM   54   H  HB2  . SER   A 1 5   ? 17.509 -6.549  22.407  1.00 39.51 ?  5   SER   A HB2  1 
ATOM   55   H  HB3  . SER   A 1 5   ? 18.635 -7.552  22.908  1.00 39.51 ?  5   SER   A HB3  1 
ATOM   56   H  HG   . SER   A 1 5   ? 19.466 -6.034  21.559  1.00 39.85 ?  5   SER   A HG   1 
ATOM   57   N  N    . PHE   A 1 6   ? 16.534 -8.543  19.208  1.00 24.87 ?  6   PHE   A N    1 
ATOM   58   C  CA   . PHE   A 1 6   ? 15.620 -8.174  18.133  1.00 21.43 ?  6   PHE   A CA   1 
ATOM   59   C  C    . PHE   A 1 6   ? 14.193 -8.537  18.534  1.00 21.47 ?  6   PHE   A C    1 
ATOM   60   O  O    . PHE   A 1 6   ? 13.928 -9.662  18.965  1.00 22.70 ?  6   PHE   A O    1 
ATOM   61   C  CB   . PHE   A 1 6   ? 16.013 -8.879  16.838  1.00 19.49 ?  6   PHE   A CB   1 
ATOM   62   C  CG   . PHE   A 1 6   ? 17.289 -8.354  16.228  1.00 18.07 ?  6   PHE   A CG   1 
ATOM   63   C  CD1  . PHE   A 1 6   ? 17.301 -7.154  15.536  1.00 17.69 ?  6   PHE   A CD1  1 
ATOM   64   C  CD2  . PHE   A 1 6   ? 18.470 -9.066  16.342  1.00 18.19 ?  6   PHE   A CD2  1 
ATOM   65   C  CE1  . PHE   A 1 6   ? 18.473 -6.672  14.976  1.00 17.76 ?  6   PHE   A CE1  1 
ATOM   66   C  CE2  . PHE   A 1 6   ? 19.640 -8.594  15.782  1.00 18.44 ?  6   PHE   A CE2  1 
ATOM   67   C  CZ   . PHE   A 1 6   ? 19.643 -7.394  15.098  1.00 18.07 ?  6   PHE   A CZ   1 
ATOM   68   H  H    . PHE   A 1 6   ? 17.077 -9.182  19.016  1.00 29.88 ?  6   PHE   A H    1 
ATOM   69   H  HA   . PHE   A 1 6   ? 15.661 -7.220  17.992  1.00 25.75 ?  6   PHE   A HA   1 
ATOM   70   H  HB2  . PHE   A 1 6   ? 16.138 -9.825  17.021  1.00 23.42 ?  6   PHE   A HB2  1 
ATOM   71   H  HB3  . PHE   A 1 6   ? 15.301 -8.764  16.190  1.00 23.42 ?  6   PHE   A HB3  1 
ATOM   72   H  HD1  . PHE   A 1 6   ? 16.512 -6.665  15.451  1.00 21.27 ?  6   PHE   A HD1  1 
ATOM   73   H  HD2  . PHE   A 1 6   ? 18.472 -9.874  16.804  1.00 21.87 ?  6   PHE   A HD2  1 
ATOM   74   H  HE1  . PHE   A 1 6   ? 18.471 -5.864  14.512  1.00 21.34 ?  6   PHE   A HE1  1 
ATOM   75   H  HE2  . PHE   A 1 6   ? 20.427 -9.080  15.870  1.00 22.16 ?  6   PHE   A HE2  1 
ATOM   76   H  HZ   . PHE   A 1 6   ? 20.430 -7.070  14.721  1.00 21.72 ?  6   PHE   A HZ   1 
ATOM   77   N  N    A SER   A 1 7   ? 13.260 -7.607  18.324  0.82 21.09 ?  7   SER   A N    1 
ATOM   78   N  N    B SER   A 1 7   ? 13.292 -7.564  18.452  0.18 20.84 ?  7   SER   A N    1 
ATOM   79   C  CA   A SER   A 1 7   ? 11.881 -7.770  18.774  0.82 21.91 ?  7   SER   A CA   1 
ATOM   80   C  CA   B SER   A 1 7   ? 11.966 -7.659  19.045  0.18 20.42 ?  7   SER   A CA   1 
ATOM   81   C  C    A SER   A 1 7   ? 10.899 -7.485  17.644  0.82 20.50 ?  7   SER   A C    1 
ATOM   82   C  C    B SER   A 1 7   ? 10.901 -7.430  17.983  0.18 19.44 ?  7   SER   A C    1 
ATOM   83   O  O    A SER   A 1 7   ? 11.132 -6.605  16.813  0.82 20.54 ?  7   SER   A O    1 
ATOM   84   O  O    B SER   A 1 7   ? 11.014 -6.512  17.164  0.18 19.40 ?  7   SER   A O    1 
ATOM   85   C  CB   A SER   A 1 7   ? 11.594 -6.826  19.948  0.82 23.95 ?  7   SER   A CB   1 
ATOM   86   C  CB   B SER   A 1 7   ? 11.808 -6.617  20.162  0.18 20.73 ?  7   SER   A CB   1 
ATOM   87   O  OG   A SER   A 1 7   ? 10.258 -6.957  20.394  0.82 25.60 ?  7   SER   A OG   1 
ATOM   88   O  OG   B SER   A 1 7   ? 10.446 -6.296  20.377  0.18 20.87 ?  7   SER   A OG   1 
ATOM   89   H  H    A SER   A 1 7   ? 13.403 -6.867  17.914  0.82 25.35 ?  7   SER   A H    1 
ATOM   90   H  H    B SER   A 1 7   ? 13.429 -6.822  18.045  0.18 25.05 ?  7   SER   A H    1 
ATOM   91   H  HA   A SER   A 1 7   ? 11.740 -8.680  19.075  0.82 26.33 ?  7   SER   A HA   1 
ATOM   92   H  HA   B SER   A 1 7   ? 11.835 -8.540  19.433  0.18 24.55 ?  7   SER   A HA   1 
ATOM   93   H  HB2  A SER   A 1 7   ? 12.191 -7.045  20.683  0.82 28.78 ?  7   SER   A HB2  1 
ATOM   94   H  HB2  B SER   A 1 7   ? 12.175 -6.979  20.986  0.18 24.92 ?  7   SER   A HB2  1 
ATOM   95   H  HB3  A SER   A 1 7   ? 11.746 -5.911  19.663  0.82 28.78 ?  7   SER   A HB3  1 
ATOM   96   H  HB3  B SER   A 1 7   ? 12.291 -5.814  19.913  0.18 24.92 ?  7   SER   A HB3  1 
ATOM   97   H  HG   A SER   A 1 7   ? 10.116 -6.431  21.035  0.82 30.76 ?  7   SER   A HG   1 
ATOM   98   H  HG   B SER   A 1 7   ? 10.377 -5.718  20.984  0.18 25.09 ?  7   SER   A HG   1 
ATOM   99   N  N    A GLY   A 1 8   ? 9.792  -8.231  17.622  0.82 19.58 ?  8   GLY   A N    1 
ATOM   100  N  N    B GLY   A 1 8   ? 9.868  -8.269  18.002  0.18 18.50 ?  8   GLY   A N    1 
ATOM   101  C  CA   A GLY   A 1 8   ? 8.716  -7.962  16.687  0.82 19.13 ?  8   GLY   A CA   1 
ATOM   102  C  CA   B GLY   A 1 8   ? 8.754  -8.113  17.093  0.18 17.62 ?  8   GLY   A CA   1 
ATOM   103  C  C    A GLY   A 1 8   ? 8.912  -8.490  15.284  0.82 17.89 ?  8   GLY   A C    1 
ATOM   104  C  C    B GLY   A 1 8   ? 8.993  -8.599  15.684  0.18 16.54 ?  8   GLY   A C    1 
ATOM   105  O  O    A GLY   A 1 8   ? 8.179  -8.071  14.379  0.82 18.45 ?  8   GLY   A O    1 
ATOM   106  O  O    B GLY   A 1 8   ? 8.193  -8.280  14.797  0.18 16.70 ?  8   GLY   A O    1 
ATOM   107  H  H    A GLY   A 1 8   ? 9.646  -8.901  18.141  0.82 23.54 ?  8   GLY   A H    1 
ATOM   108  H  H    B GLY   A 1 8   ? 9.794  -8.939  18.536  0.18 22.23 ?  8   GLY   A H    1 
ATOM   109  H  HA2  A GLY   A 1 8   ? 7.897  -8.347  17.035  0.82 22.99 ?  8   GLY   A HA2  1 
ATOM   110  H  HA2  B GLY   A 1 8   ? 7.992  -8.595  17.445  0.18 21.18 ?  8   GLY   A HA2  1 
ATOM   111  H  HA3  A GLY   A 1 8   ? 8.590  -7.001  16.627  0.82 22.99 ?  8   GLY   A HA3  1 
ATOM   112  H  HA3  B GLY   A 1 8   ? 8.520  -7.173  17.044  0.18 21.18 ?  8   GLY   A HA3  1 
ATOM   113  N  N    A TYR   A 1 9   ? 9.875  -9.383  15.067  0.82 16.50 ?  9   TYR   A N    1 
ATOM   114  N  N    B TYR   A 1 9   ? 10.059 -9.357  15.443  0.18 15.58 ?  9   TYR   A N    1 
ATOM   115  C  CA   A TYR   A 1 9   ? 10.132 -9.938  13.746  0.82 14.94 ?  9   TYR   A CA   1 
ATOM   116  C  CA   B TYR   A 1 9   ? 10.354 -9.831  14.098  0.18 14.63 ?  9   TYR   A CA   1 
ATOM   117  C  C    A TYR   A 1 9   ? 9.235  -11.142 13.483  0.82 14.57 ?  9   TYR   A C    1 
ATOM   118  C  C    B TYR   A 1 9   ? 9.563  -11.091 13.772  0.18 13.96 ?  9   TYR   A C    1 
ATOM   119  O  O    A TYR   A 1 9   ? 8.901  -11.912 14.390  0.82 16.26 ?  9   TYR   A O    1 
ATOM   120  O  O    B TYR   A 1 9   ? 9.432  -11.997 14.600  0.18 14.07 ?  9   TYR   A O    1 
ATOM   121  C  CB   A TYR   A 1 9   ? 11.606 -10.356 13.603  0.82 15.00 ?  9   TYR   A CB   1 
ATOM   122  C  CB   B TYR   A 1 9   ? 11.851 -10.098 13.941  0.18 14.36 ?  9   TYR   A CB   1 
ATOM   123  C  CG   A TYR   A 1 9   ? 12.540 -9.175  13.458  0.82 14.82 ?  9   TYR   A CG   1 
ATOM   124  C  CG   B TYR   A 1 9   ? 12.647 -8.843  13.663  0.18 13.87 ?  9   TYR   A CG   1 
ATOM   125  C  CD1  A TYR   A 1 9   ? 12.877 -8.398  14.557  0.82 15.31 ?  9   TYR   A CD1  1 
ATOM   126  C  CD1  B TYR   A 1 9   ? 12.957 -7.954  14.682  0.18 13.75 ?  9   TYR   A CD1  1 
ATOM   127  C  CD2  A TYR   A 1 9   ? 13.055 -8.817  12.217  0.82 14.57 ?  9   TYR   A CD2  1 
ATOM   128  C  CD2  B TYR   A 1 9   ? 13.072 -8.539  12.376  0.18 13.51 ?  9   TYR   A CD2  1 
ATOM   129  C  CE1  A TYR   A 1 9   ? 13.701 -7.297  14.431  0.82 15.74 ?  9   TYR   A CE1  1 
ATOM   130  C  CE1  B TYR   A 1 9   ? 13.674 -6.800  14.429  0.18 13.57 ?  9   TYR   A CE1  1 
ATOM   131  C  CE2  A TYR   A 1 9   ? 13.882 -7.721  12.079  0.82 15.07 ?  9   TYR   A CE2  1 
ATOM   132  C  CE2  B TYR   A 1 9   ? 13.790 -7.389  12.114  0.18 13.41 ?  9   TYR   A CE2  1 
ATOM   133  C  CZ   A TYR   A 1 9   ? 14.199 -6.965  13.189  0.82 15.72 ?  9   TYR   A CZ   1 
ATOM   134  C  CZ   B TYR   A 1 9   ? 14.087 -6.524  13.143  0.18 13.29 ?  9   TYR   A CZ   1 
ATOM   135  O  OH   A TYR   A 1 9   ? 15.015 -5.873  13.049  0.82 16.62 ?  9   TYR   A OH   1 
ATOM   136  O  OH   B TYR   A 1 9   ? 14.799 -5.378  12.882  0.18 12.92 ?  9   TYR   A OH   1 
ATOM   137  H  H    A TYR   A 1 9   ? 10.403 -9.679  15.676  0.82 19.83 ?  9   TYR   A H    1 
ATOM   138  H  H    B TYR   A 1 9   ? 10.634 -9.599  16.039  0.18 18.73 ?  9   TYR   A H    1 
ATOM   139  H  HA   A TYR   A 1 9   ? 9.949  -9.260  13.073  0.82 17.97 ?  9   TYR   A HA   1 
ATOM   140  H  HA   B TYR   A 1 9   ? 10.107 -9.145  13.461  0.18 17.59 ?  9   TYR   A HA   1 
ATOM   141  H  HB2  A TYR   A 1 9   ? 11.874 -10.859 14.387  0.82 18.04 ?  9   TYR   A HB2  1 
ATOM   142  H  HB2  B TYR   A 1 9   ? 12.197 -10.505 14.751  0.18 17.27 ?  9   TYR   A HB2  1 
ATOM   143  H  HB3  A TYR   A 1 9   ? 11.693 -10.905 12.808  0.82 18.04 ?  9   TYR   A HB3  1 
ATOM   144  H  HB3  B TYR   A 1 9   ? 11.971 -10.699 13.192  0.18 17.27 ?  9   TYR   A HB3  1 
ATOM   145  H  HD1  A TYR   A 1 9   ? 12.528 -8.620  15.392  0.82 18.41 ?  9   TYR   A HD1  1 
ATOM   146  H  HD1  B TYR   A 1 9   ? 12.677 -8.140  15.550  0.18 16.53 ?  9   TYR   A HD1  1 
ATOM   147  H  HD2  A TYR   A 1 9   ? 12.838 -9.326  11.467  0.82 17.52 ?  9   TYR   A HD2  1 
ATOM   148  H  HD2  B TYR   A 1 9   ? 12.872 -9.121  11.679  0.18 16.25 ?  9   TYR   A HD2  1 
ATOM   149  H  HE1  A TYR   A 1 9   ? 13.918 -6.787  15.176  0.82 18.93 ?  9   TYR   A HE1  1 
ATOM   150  H  HE1  B TYR   A 1 9   ? 13.875 -6.214  15.122  0.18 16.32 ?  9   TYR   A HE1  1 
ATOM   151  H  HE2  A TYR   A 1 9   ? 14.229 -7.495  11.243  0.82 18.12 ?  9   TYR   A HE2  1 
ATOM   152  H  HE2  B TYR   A 1 9   ? 14.070 -7.197  11.247  0.18 16.13 ?  9   TYR   A HE2  1 
ATOM   153  H  HH   A TYR   A 1 9   ? 15.142 -5.506  13.795  0.82 19.99 ?  9   TYR   A HH   1 
ATOM   154  H  HH   B TYR   A 1 9   ? 14.911 -4.940  13.591  0.18 15.54 ?  9   TYR   A HH   1 
ATOM   155  N  N    A LEU   A 1 10  ? 8.853  -11.295 12.220  0.82 14.06 ?  10  LEU   A N    1 
ATOM   156  N  N    B LEU   A 1 10  ? 9.046  -11.142 12.546  0.18 13.18 ?  10  LEU   A N    1 
ATOM   157  C  CA   A LEU   A 1 10  ? 8.249  -12.522 11.729  0.82 14.07 ?  10  LEU   A CA   1 
ATOM   158  C  CA   B LEU   A 1 10  ? 8.298  -12.292 12.055  0.18 12.56 ?  10  LEU   A CA   1 
ATOM   159  C  C    A LEU   A 1 10  ? 9.377  -13.447 11.281  0.82 13.61 ?  10  LEU   A C    1 
ATOM   160  C  C    B LEU   A 1 10  ? 9.285  -13.296 11.470  0.18 12.33 ?  10  LEU   A C    1 
ATOM   161  O  O    A LEU   A 1 10  ? 10.347 -13.004 10.654  0.82 13.94 ?  10  LEU   A O    1 
ATOM   162  O  O    B LEU   A 1 10  ? 10.071 -12.955 10.579  0.18 12.58 ?  10  LEU   A O    1 
ATOM   163  C  CB   A LEU   A 1 10  ? 7.335  -12.199 10.546  0.82 15.21 ?  10  LEU   A CB   1 
ATOM   164  C  CB   B LEU   A 1 10  ? 7.293  -11.852 10.991  0.18 11.92 ?  10  LEU   A CB   1 
ATOM   165  C  CG   A LEU   A 1 10  ? 6.613  -13.391 9.915   0.82 17.62 ?  10  LEU   A CG   1 
ATOM   166  C  CG   B LEU   A 1 10  ? 6.340  -12.926 10.457  0.18 11.33 ?  10  LEU   A CG   1 
ATOM   167  C  CD1  A LEU   A 1 10  ? 5.526  -13.930 10.831  0.82 19.14 ?  10  LEU   A CD1  1 
ATOM   168  C  CD1  B LEU   A 1 10  ? 4.980  -12.312 10.160  0.18 11.47 ?  10  LEU   A CD1  1 
ATOM   169  C  CD2  A LEU   A 1 10  ? 6.049  -13.022 8.551   0.82 19.42 ?  10  LEU   A CD2  1 
ATOM   170  C  CD2  B LEU   A 1 10  ? 6.894  -13.612 9.211   0.18 10.97 ?  10  LEU   A CD2  1 
ATOM   171  H  H    A LEU   A 1 10  ? 8.949  -10.689 11.608  0.82 16.91 ?  10  LEU   A H    1 
ATOM   172  H  H    B LEU   A 1 10  ? 9.125  -10.510 11.968  0.18 15.86 ?  10  LEU   A H    1 
ATOM   173  H  HA   A LEU   A 1 10  ? 7.733  -12.948 12.435  0.82 16.92 ?  10  LEU   A HA   1 
ATOM   174  H  HA   B LEU   A 1 10  ? 7.819  -12.709 12.789  0.18 15.11 ?  10  LEU   A HA   1 
ATOM   175  H  HB2  A LEU   A 1 10  ? 6.657  -11.575 10.846  0.82 18.29 ?  10  LEU   A HB2  1 
ATOM   176  H  HB2  B LEU   A 1 10  ? 6.748  -11.142 11.366  0.18 14.35 ?  10  LEU   A HB2  1 
ATOM   177  H  HB3  A LEU   A 1 10  ? 7.872  -11.786 9.854   0.82 18.29 ?  10  LEU   A HB3  1 
ATOM   178  H  HB3  B LEU   A 1 10  ? 7.790  -11.507 10.234  0.18 14.35 ?  10  LEU   A HB3  1 
ATOM   179  H  HG   A LEU   A 1 10  ? 7.255  -14.104 9.779   0.82 21.18 ?  10  LEU   A HG   1 
ATOM   180  H  HG   B LEU   A 1 10  ? 6.218  -13.600 11.141  0.18 13.64 ?  10  LEU   A HG   1 
ATOM   181  H  HD11 A LEU   A 1 10  ? 5.098  -14.685 10.400  0.82 23.01 ?  10  LEU   A HD11 1 
ATOM   182  H  HD11 B LEU   A 1 10  ? 4.395  -12.996 9.802   0.18 13.81 ?  10  LEU   A HD11 1 
ATOM   183  H  HD12 A LEU   A 1 10  ? 5.929  -14.211 11.669  0.82 23.01 ?  10  LEU   A HD12 1 
ATOM   184  H  HD12 B LEU   A 1 10  ? 4.607  -11.954 10.983  0.18 13.81 ?  10  LEU   A HD12 1 
ATOM   185  H  HD13 A LEU   A 1 10  ? 4.877  -13.229 10.996  0.82 23.01 ?  10  LEU   A HD13 1 
ATOM   186  H  HD13 B LEU   A 1 10  ? 5.092  -11.597 9.512   0.18 13.81 ?  10  LEU   A HD13 1 
ATOM   187  H  HD21 A LEU   A 1 10  ? 5.596  -13.797 8.183   0.82 23.35 ?  10  LEU   A HD21 1 
ATOM   188  H  HD21 B LEU   A 1 10  ? 6.217  -14.213 8.856   0.18 13.20 ?  10  LEU   A HD21 1 
ATOM   189  H  HD22 A LEU   A 1 10  ? 5.424  -12.290 8.658   0.82 23.35 ?  10  LEU   A HD22 1 
ATOM   190  H  HD22 B LEU   A 1 10  ? 7.114  -12.938 8.551   0.18 13.20 ?  10  LEU   A HD22 1 
ATOM   191  H  HD23 A LEU   A 1 10  ? 6.779  -12.757 7.972   0.82 23.35 ?  10  LEU   A HD23 1 
ATOM   192  H  HD23 B LEU   A 1 10  ? 7.686  -14.115 9.451   0.18 13.20 ?  10  LEU   A HD23 1 
ATOM   193  N  N    A LYS   A 1 11  ? 9.261  -14.729 11.627  0.82 13.05 ?  11  LYS   A N    1 
ATOM   194  N  N    B LYS   A 1 11  ? 9.249  -14.523 11.978  0.18 11.88 ?  11  LYS   A N    1 
ATOM   195  C  CA   A LYS   A 1 11  ? 10.271 -15.725 11.291  0.82 13.21 ?  11  LYS   A CA   1 
ATOM   196  C  CA   B LYS   A 1 11  ? 10.155 -15.563 11.511  0.18 11.64 ?  11  LYS   A CA   1 
ATOM   197  C  C    A LYS   A 1 11  ? 9.923  -16.322 9.934   0.82 12.99 ?  11  LYS   A C    1 
ATOM   198  C  C    B LYS   A 1 11  ? 9.734  -16.035 10.125  0.18 11.00 ?  11  LYS   A C    1 
ATOM   199  O  O    A LYS   A 1 11  ? 8.865  -16.935 9.787   0.82 14.85 ?  11  LYS   A O    1 
ATOM   200  O  O    B LYS   A 1 11  ? 8.605  -16.497 9.936   0.18 10.50 ?  11  LYS   A O    1 
ATOM   201  C  CB   A LYS   A 1 11  ? 10.309 -16.803 12.377  0.82 12.94 ?  11  LYS   A CB   1 
ATOM   202  C  CB   B LYS   A 1 11  ? 10.147 -16.725 12.501  0.18 11.88 ?  11  LYS   A CB   1 
ATOM   203  C  CG   A LYS   A 1 11  ? 11.333 -17.908 12.179  0.82 13.16 ?  11  LYS   A CG   1 
ATOM   204  C  CG   B LYS   A 1 11  ? 11.205 -17.784 12.246  0.18 12.12 ?  11  LYS   A CG   1 
ATOM   205  C  CD   A LYS   A 1 11  ? 11.418 -18.769 13.443  0.82 13.67 ?  11  LYS   A CD   1 
ATOM   206  C  CD   B LYS   A 1 11  ? 11.230 -18.798 13.380  0.18 12.36 ?  11  LYS   A CD   1 
ATOM   207  C  CE   A LYS   A 1 11  ? 12.408 -19.920 13.313  0.82 13.93 ?  11  LYS   A CE   1 
ATOM   208  C  CE   B LYS   A 1 11  ? 12.292 -19.867 13.168  0.18 12.37 ?  11  LYS   A CE   1 
ATOM   209  N  NZ   A LYS   A 1 11  ? 13.776 -19.452 13.000  0.82 13.79 ?  11  LYS   A NZ   1 
ATOM   210  N  NZ   B LYS   A 1 11  ? 13.670 -19.305 13.146  0.18 12.09 ?  11  LYS   A NZ   1 
ATOM   211  H  H    A LYS   A 1 11  ? 8.582  -15.057 12.049  0.82 15.70 ?  11  LYS   A H    1 
ATOM   212  H  H    B LYS   A 1 11  ? 8.713  -14.771 12.603  0.18 14.29 ?  11  LYS   A H    1 
ATOM   213  H  HA   A LYS   A 1 11  ? 11.141 -15.303 11.233  0.82 15.88 ?  11  LYS   A HA   1 
ATOM   214  H  HA   B LYS   A 1 11  ? 11.053 -15.208 11.451  0.18 14.00 ?  11  LYS   A HA   1 
ATOM   215  H  HB2  A LYS   A 1 11  ? 10.506 -16.371 13.223  0.82 15.57 ?  11  LYS   A HB2  1 
ATOM   216  H  HB2  B LYS   A 1 11  ? 10.294 -16.371 13.392  0.18 14.29 ?  11  LYS   A HB2  1 
ATOM   217  H  HB3  A LYS   A 1 11  ? 9.434  -17.219 12.423  0.82 15.57 ?  11  LYS   A HB3  1 
ATOM   218  H  HB3  B LYS   A 1 11  ? 9.280  -17.159 12.462  0.18 14.29 ?  11  LYS   A HB3  1 
ATOM   219  H  HG2  A LYS   A 1 11  ? 11.060 -18.471 11.437  0.82 15.83 ?  11  LYS   A HG2  1 
ATOM   220  H  HG2  B LYS   A 1 11  ? 11.001 -18.251 11.420  0.18 14.59 ?  11  LYS   A HG2  1 
ATOM   221  H  HG3  A LYS   A 1 11  ? 12.202 -17.517 12.012  0.82 15.83 ?  11  LYS   A HG3  1 
ATOM   222  H  HG3  B LYS   A 1 11  ? 12.076 -17.361 12.190  0.18 14.59 ?  11  LYS   A HG3  1 
ATOM   223  H  HD2  A LYS   A 1 11  ? 11.695 -18.213 14.185  0.82 16.44 ?  11  LYS   A HD2  1 
ATOM   224  H  HD2  B LYS   A 1 11  ? 11.423 -18.338 14.212  0.18 14.87 ?  11  LYS   A HD2  1 
ATOM   225  H  HD3  A LYS   A 1 11  ? 10.540 -19.148 13.624  0.82 16.44 ?  11  LYS   A HD3  1 
ATOM   226  H  HD3  B LYS   A 1 11  ? 10.366 -19.236 13.434  0.18 14.87 ?  11  LYS   A HD3  1 
ATOM   227  H  HE2  A LYS   A 1 11  ? 12.441 -20.406 14.152  0.82 16.76 ?  11  LYS   A HE2  1 
ATOM   228  H  HE2  B LYS   A 1 11  ? 12.241 -20.511 13.891  0.18 14.88 ?  11  LYS   A HE2  1 
ATOM   229  H  HE3  A LYS   A 1 11  ? 12.120 -20.509 12.598  0.82 16.76 ?  11  LYS   A HE3  1 
ATOM   230  H  HE3  B LYS   A 1 11  ? 12.133 -20.306 12.318  0.18 14.88 ?  11  LYS   A HE3  1 
ATOM   231  H  HZ1  A LYS   A 1 11  ? 14.330 -20.147 12.939  0.82 16.58 ?  11  LYS   A HZ1  1 
ATOM   232  H  HZ1  B LYS   A 1 11  ? 14.257 -19.948 12.959  0.18 14.55 ?  11  LYS   A HZ1  1 
ATOM   233  H  HZ2  A LYS   A 1 11  ? 13.779 -19.014 12.224  0.82 16.58 ?  11  LYS   A HZ2  1 
ATOM   234  H  HZ2  B LYS   A 1 11  ? 13.731 -18.669 12.526  0.18 14.55 ?  11  LYS   A HZ2  1 
ATOM   235  H  HZ3  A LYS   A 1 11  ? 14.066 -18.907 13.640  0.82 16.58 ?  11  LYS   A HZ3  1 
ATOM   236  H  HZ3  B LYS   A 1 11  ? 13.870 -18.955 13.939  0.18 14.55 ?  11  LYS   A HZ3  1 
ATOM   237  N  N    A LEU   A 1 12  ? 10.796 -16.148 8.942   0.82 12.31 ?  12  LEU   A N    1 
ATOM   238  N  N    B LEU   A 1 12  ? 10.632 -15.896 9.149   0.18 11.38 ?  12  LEU   A N    1 
ATOM   239  C  CA   A LEU   A 1 12  ? 10.530 -16.734 7.631   0.82 12.77 ?  12  LEU   A CA   1 
ATOM   240  C  CA   B LEU   A 1 12  ? 10.400 -16.411 7.803   0.18 11.78 ?  12  LEU   A CA   1 
ATOM   241  C  C    A LEU   A 1 12  ? 11.115 -18.130 7.488   0.82 12.70 ?  12  LEU   A C    1 
ATOM   242  C  C    B LEU   A 1 12  ? 10.957 -17.820 7.626   0.18 11.86 ?  12  LEU   A C    1 
ATOM   243  O  O    A LEU   A 1 12  ? 10.492 -18.998 6.869   0.82 12.86 ?  12  LEU   A O    1 
ATOM   244  O  O    B LEU   A 1 12  ? 10.258 -18.708 7.130   0.18 11.76 ?  12  LEU   A O    1 
ATOM   245  C  CB   A LEU   A 1 12  ? 11.083 -15.849 6.512   0.82 13.47 ?  12  LEU   A CB   1 
ATOM   246  C  CB   B LEU   A 1 12  ? 11.009 -15.468 6.758   0.18 12.23 ?  12  LEU   A CB   1 
ATOM   247  C  CG   A LEU   A 1 12  ? 10.453 -14.464 6.378   0.82 14.51 ?  12  LEU   A CG   1 
ATOM   248  C  CG   B LEU   A 1 12  ? 10.183 -14.236 6.389   0.18 12.74 ?  12  LEU   A CG   1 
ATOM   249  C  CD1  A LEU   A 1 12  ? 11.177 -13.682 5.292   0.82 15.51 ?  12  LEU   A CD1  1 
ATOM   250  C  CD1  B LEU   A 1 12  ? 10.925 -13.381 5.372   0.18 12.82 ?  12  LEU   A CD1  1 
ATOM   251  C  CD2  A LEU   A 1 12  ? 8.963  -14.566 6.083   0.82 15.35 ?  12  LEU   A CD2  1 
ATOM   252  C  CD2  B LEU   A 1 12  ? 8.823  -14.651 5.850   0.18 13.28 ?  12  LEU   A CD2  1 
ATOM   253  H  H    A LEU   A 1 12  ? 11.532 -15.696 8.995   0.82 14.81 ?  12  LEU   A H    1 
ATOM   254  H  H    B LEU   A 1 12  ? 11.380 -15.485 9.240   0.18 13.70 ?  12  LEU   A H    1 
ATOM   255  H  HA   A LEU   A 1 12  ? 9.570  -16.800 7.509   0.82 15.37 ?  12  LEU   A HA   1 
ATOM   256  H  HA   B LEU   A 1 12  ? 9.444  -16.452 7.647   0.18 14.17 ?  12  LEU   A HA   1 
ATOM   257  H  HB2  A LEU   A 1 12  ? 12.031 -15.720 6.663   0.82 16.21 ?  12  LEU   A HB2  1 
ATOM   258  H  HB2  B LEU   A 1 12  ? 11.862 -15.151 7.091   0.18 14.72 ?  12  LEU   A HB2  1 
ATOM   259  H  HB3  A LEU   A 1 12  ? 10.952 -16.309 5.666   0.82 16.21 ?  12  LEU   A HB3  1 
ATOM   260  H  HB3  B LEU   A 1 12  ? 11.150 -15.972 5.941   0.18 14.72 ?  12  LEU   A HB3  1 
ATOM   261  H  HG   A LEU   A 1 12  ? 10.559 -13.986 7.212   0.82 17.45 ?  12  LEU   A HG   1 
ATOM   262  H  HG   B LEU   A 1 12  ? 10.043 -13.700 7.184   0.18 15.32 ?  12  LEU   A HG   1 
ATOM   263  H  HD11 A LEU   A 1 12  ? 10.772 -12.805 5.208   0.82 18.65 ?  12  LEU   A HD11 1 
ATOM   264  H  HD11 B LEU   A 1 12  ? 10.386 -12.603 5.161   0.18 15.42 ?  12  LEU   A HD11 1 
ATOM   265  H  HD12 A LEU   A 1 12  ? 12.112 -13.593 5.537   0.82 18.65 ?  12  LEU   A HD12 1 
ATOM   266  H  HD12 B LEU   A 1 12  ? 11.774 -13.105 5.750   0.18 15.42 ?  12  LEU   A HD12 1 
ATOM   267  H  HD13 A LEU   A 1 12  ? 11.102 -14.162 4.451   0.82 18.65 ?  12  LEU   A HD13 1 
ATOM   268  H  HD13 B LEU   A 1 12  ? 11.076 -13.906 4.569   0.18 15.42 ?  12  LEU   A HD13 1 
ATOM   269  H  HD21 A LEU   A 1 12  ? 8.621  -13.687 5.858   0.82 18.46 ?  12  LEU   A HD21 1 
ATOM   270  H  HD21 B LEU   A 1 12  ? 8.440  -13.914 5.352   0.18 15.98 ?  12  LEU   A HD21 1 
ATOM   271  H  HD22 A LEU   A 1 12  ? 8.827  -15.174 5.338   0.82 18.46 ?  12  LEU   A HD22 1 
ATOM   272  H  HD22 B LEU   A 1 12  ? 8.937  -15.420 5.268   0.18 15.98 ?  12  LEU   A HD22 1 
ATOM   273  H  HD23 A LEU   A 1 12  ? 8.506  -14.907 6.870   0.82 18.46 ?  12  LEU   A HD23 1 
ATOM   274  H  HD23 B LEU   A 1 12  ? 8.246  -14.886 6.594   0.18 15.98 ?  12  LEU   A HD23 1 
ATOM   275  N  N    A THR   A 1 13  ? 12.317 -18.342 8.013   0.82 12.54 ?  13  THR   A N    1 
ATOM   276  N  N    B THR   A 1 13  ? 12.211 -18.036 8.012   0.18 12.06 ?  13  THR   A N    1 
ATOM   277  C  CA   A THR   A 1 13  ? 13.014 -19.617 7.914   0.82 12.93 ?  13  THR   A CA   1 
ATOM   278  C  CA   B THR   A 1 13  ? 12.843 -19.345 7.908   0.18 12.27 ?  13  THR   A CA   1 
ATOM   279  C  C    A THR   A 1 13  ? 13.789 -19.841 9.207   0.82 12.89 ?  13  THR   A C    1 
ATOM   280  C  C    B THR   A 1 13  ? 13.611 -19.609 9.199   0.18 12.63 ?  13  THR   A C    1 
ATOM   281  O  O    A THR   A 1 13  ? 13.708 -19.053 10.155  0.82 13.03 ?  13  THR   A O    1 
ATOM   282  O  O    B THR   A 1 13  ? 13.488 -18.876 10.185  0.18 12.85 ?  13  THR   A O    1 
ATOM   283  C  CB   A THR   A 1 13  ? 13.988 -19.651 6.729   0.82 13.75 ?  13  THR   A CB   1 
ATOM   284  C  CB   B THR   A 1 13  ? 13.764 -19.423 6.682   0.18 12.53 ?  13  THR   A CB   1 
ATOM   285  O  OG1  A THR   A 1 13  ? 15.056 -18.743 6.994   0.82 13.32 ?  13  THR   A OG1  1 
ATOM   286  O  OG1  B THR   A 1 13  ? 14.772 -18.411 6.779   0.18 12.54 ?  13  THR   A OG1  1 
ATOM   287  C  CG2  A THR   A 1 13  ? 13.315 -19.272 5.417   0.82 15.13 ?  13  THR   A CG2  1 
ATOM   288  C  CG2  B THR   A 1 13  ? 12.985 -19.240 5.386   0.18 12.82 ?  13  THR   A CG2  1 
ATOM   289  H  H    A THR   A 1 13  ? 12.766 -17.741 8.427   0.82 15.09 ?  13  THR   A H    1 
ATOM   290  H  H    B THR   A 1 13  ? 12.723 -17.429 8.343   0.18 14.51 ?  13  THR   A H    1 
ATOM   291  H  HA   A THR   A 1 13  ? 12.371 -20.336 7.805   0.82 15.55 ?  13  THR   A HA   1 
ATOM   292  H  HA   B THR   A 1 13  ? 12.154 -20.023 7.815   0.18 14.76 ?  13  THR   A HA   1 
ATOM   293  H  HB   A THR   A 1 13  ? 14.347 -20.546 6.632   0.82 16.53 ?  13  THR   A HB   1 
ATOM   294  H  HB   B THR   A 1 13  ? 14.186 -20.296 6.656   0.18 15.07 ?  13  THR   A HB   1 
ATOM   295  H  HG1  A THR   A 1 13  ? 15.746 -19.168 7.217   0.82 16.02 ?  13  THR   A HG1  1 
ATOM   296  H  HG1  B THR   A 1 13  ? 15.286 -18.453 6.115   0.18 15.08 ?  13  THR   A HG1  1 
ATOM   297  H  HG21 A THR   A 1 13  ? 13.921 -19.440 4.675   0.82 18.20 ?  13  THR   A HG21 1 
ATOM   298  H  HG21 B THR   A 1 13  ? 13.581 -19.348 4.626   0.18 15.43 ?  13  THR   A HG21 1 
ATOM   299  H  HG22 A THR   A 1 13  ? 12.516 -19.808 5.291   0.82 18.20 ?  13  THR   A HG22 1 
ATOM   300  H  HG22 B THR   A 1 13  ? 12.279 -19.902 5.327   0.18 15.43 ?  13  THR   A HG22 1 
ATOM   301  H  HG23 A THR   A 1 13  ? 13.073 -18.337 5.423   0.82 18.20 ?  13  THR   A HG23 1 
ATOM   302  H  HG23 B THR   A 1 13  ? 12.594 -18.355 5.356   0.18 15.43 ?  13  THR   A HG23 1 
ATOM   303  N  N    A ASP   A 1 14  ? 14.588 -20.906 9.216   0.82 13.40 ?  14  ASP   A N    1 
ATOM   304  N  N    B ASP   A 1 14  ? 14.422 -20.667 9.178   0.18 12.90 ?  14  ASP   A N    1 
ATOM   305  C  CA   A ASP   A 1 14  ? 15.447 -21.179 10.360  0.82 13.54 ?  14  ASP   A CA   1 
ATOM   306  C  CA   B ASP   A 1 14  ? 15.231 -21.015 10.340  0.18 13.17 ?  14  ASP   A CA   1 
ATOM   307  C  C    A ASP   A 1 14  ? 16.275 -19.959 10.751  0.82 13.25 ?  14  ASP   A C    1 
ATOM   308  C  C    B ASP   A 1 14  ? 16.145 -19.865 10.746  0.18 12.84 ?  14  ASP   A C    1 
ATOM   309  O  O    A ASP   A 1 14  ? 16.530 -19.734 11.939  0.82 14.50 ?  14  ASP   A O    1 
ATOM   310  O  O    B ASP   A 1 14  ? 16.334 -19.605 11.940  0.18 13.07 ?  14  ASP   A O    1 
ATOM   311  C  CB   A ASP   A 1 14  ? 16.376 -22.351 10.042  0.82 16.37 ?  14  ASP   A CB   1 
ATOM   312  C  CB   B ASP   A 1 14  ? 16.053 -22.266 10.030  0.18 14.21 ?  14  ASP   A CB   1 
ATOM   313  C  CG   A ASP   A 1 14  ? 17.263 -22.714 11.211  0.82 20.29 ?  14  ASP   A CG   1 
ATOM   314  C  CG   B ASP   A 1 14  ? 17.086 -22.560 11.098  0.18 15.24 ?  14  ASP   A CG   1 
ATOM   315  O  OD1  A ASP   A 1 14  ? 16.714 -23.147 12.248  0.82 21.97 ?  14  ASP   A OD1  1 
ATOM   316  O  OD1  B ASP   A 1 14  ? 16.696 -23.004 12.199  0.18 15.52 ?  14  ASP   A OD1  1 
ATOM   317  O  OD2  A ASP   A 1 14  ? 18.497 -22.570 11.088  0.82 23.12 -1 14  ASP   A OD2  1 
ATOM   318  O  OD2  B ASP   A 1 14  ? 18.286 -22.334 10.837  0.18 15.93 -1 14  ASP   A OD2  1 
ATOM   319  H  H    A ASP   A 1 14  ? 14.655 -21.476 8.571   0.82 16.12 ?  14  ASP   A H    1 
ATOM   320  H  H    B ASP   A 1 14  ? 14.519 -21.193 8.509   0.18 15.51 ?  14  ASP   A H    1 
ATOM   321  H  HA   A ASP   A 1 14  ? 14.894 -21.428 11.117  0.82 16.28 ?  14  ASP   A HA   1 
ATOM   322  H  HA   B ASP   A 1 14  ? 14.650 -21.215 11.090  0.18 15.85 ?  14  ASP   A HA   1 
ATOM   323  H  HB2  A ASP   A 1 14  ? 15.829 -23.129 9.810   0.82 19.68 ?  14  ASP   A HB2  1 
ATOM   324  H  HB2  B ASP   A 1 14  ? 15.452 -23.029 9.958   0.18 17.10 ?  14  ASP   A HB2  1 
ATOM   325  H  HB3  A ASP   A 1 14  ? 16.941 -22.116 9.295   0.82 19.68 ?  14  ASP   A HB3  1 
ATOM   326  H  HB3  B ASP   A 1 14  ? 16.521 -22.139 9.189   0.18 17.10 ?  14  ASP   A HB3  1 
ATOM   327  N  N    . ASN   A 1 15  ? 16.715 -19.160 9.768   1.00 12.75 ?  15  ASN   A N    1 
ATOM   328  C  CA   . ASN   A 1 15  ? 17.704 -18.118 10.032  1.00 13.44 ?  15  ASN   A CA   1 
ATOM   329  C  C    . ASN   A 1 15  ? 17.336 -16.717 9.560   1.00 13.60 ?  15  ASN   A C    1 
ATOM   330  O  O    . ASN   A 1 15  ? 18.121 -15.794 9.795   1.00 15.17 ?  15  ASN   A O    1 
ATOM   331  C  CB   . ASN   A 1 15  ? 19.075 -18.512 9.447   1.00 13.28 ?  15  ASN   A CB   1 
ATOM   332  C  CG   . ASN   A 1 15  ? 19.058 -18.605 7.940   1.00 13.57 ?  15  ASN   A CG   1 
ATOM   333  O  OD1  . ASN   A 1 15  ? 18.329 -19.417 7.364   1.00 14.41 ?  15  ASN   A OD1  1 
ATOM   334  N  ND2  . ASN   A 1 15  ? 19.864 -17.770 7.286   1.00 13.71 ?  15  ASN   A ND2  1 
ATOM   335  H  H    A ASN   A 1 15  ? 16.457 -19.206 8.952   0.82 15.34 ?  15  ASN   A H    1 
ATOM   336  H  H    B ASN   A 1 15  ? 16.547 -19.275 8.934   0.18 15.34 ?  15  ASN   A H    1 
ATOM   337  H  HA   . ASN   A 1 15  ? 17.831 -18.057 10.990  1.00 16.17 ?  15  ASN   A HA   1 
ATOM   338  H  HB2  . ASN   A 1 15  ? 19.736 -17.841 9.705   1.00 15.97 ?  15  ASN   A HB2  1 
ATOM   339  H  HB3  . ASN   A 1 15  ? 19.339 -19.377 9.799   1.00 15.97 ?  15  ASN   A HB3  1 
ATOM   340  H  HD21 . ASN   A 1 15  ? 19.891 -17.780 6.426   1.00 16.49 ?  15  ASN   A HD21 1 
ATOM   341  H  HD22 . ASN   A 1 15  ? 20.365 -17.213 7.720   1.00 16.49 ?  15  ASN   A HD22 1 
ATOM   342  N  N    A VAL   A 1 16  ? 16.212 -16.542 8.867   0.82 13.00 ?  16  VAL   A N    1 
ATOM   343  N  N    B VAL   A 1 16  ? 16.153 -16.499 8.989   0.18 13.07 ?  16  VAL   A N    1 
ATOM   344  C  CA   A VAL   A 1 16  ? 15.829 -15.264 8.280   0.82 13.05 ?  16  VAL   A CA   1 
ATOM   345  C  CA   B VAL   A 1 16  ? 15.773 -15.189 8.467   0.18 12.61 ?  16  VAL   A CA   1 
ATOM   346  C  C    A VAL   A 1 16  ? 14.550 -14.772 8.942   0.82 12.49 ?  16  VAL   A C    1 
ATOM   347  C  C    B VAL   A 1 16  ? 14.538 -14.675 9.198   0.18 12.25 ?  16  VAL   A C    1 
ATOM   348  O  O    A VAL   A 1 16  ? 13.538 -15.487 8.981   0.82 11.95 ?  16  VAL   A O    1 
ATOM   349  O  O    B VAL   A 1 16  ? 13.600 -15.434 9.470   0.18 12.13 ?  16  VAL   A O    1 
ATOM   350  C  CB   A VAL   A 1 16  ? 15.665 -15.347 6.752   0.82 13.67 ?  16  VAL   A CB   1 
ATOM   351  C  CB   B VAL   A 1 16  ? 15.551 -15.223 6.940   0.18 12.50 ?  16  VAL   A CB   1 
ATOM   352  C  CG1  A VAL   A 1 16  ? 15.220 -13.992 6.187   0.82 14.49 ?  16  VAL   A CG1  1 
ATOM   353  C  CG1  B VAL   A 1 16  ? 15.180 -13.839 6.420   0.18 12.57 ?  16  VAL   A CG1  1 
ATOM   354  C  CG2  A VAL   A 1 16  ? 16.957 -15.803 6.096   0.82 14.95 ?  16  VAL   A CG2  1 
ATOM   355  C  CG2  B VAL   A 1 16  ? 16.797 -15.743 6.238   0.18 12.86 ?  16  VAL   A CG2  1 
ATOM   356  H  H    A VAL   A 1 16  ? 15.640 -17.167 8.728   0.82 15.64 ?  16  VAL   A H    1 
ATOM   357  H  H    B VAL   A 1 16  ? 15.543 -17.098 8.902   0.18 15.72 ?  16  VAL   A H    1 
ATOM   358  H  HA   A VAL   A 1 16  ? 16.530 -14.616 8.462   0.82 15.70 ?  16  VAL   A HA   1 
ATOM   359  H  HA   B VAL   A 1 16  ? 16.491 -14.562 8.641   0.18 15.17 ?  16  VAL   A HA   1 
ATOM   360  H  HB   A VAL   A 1 16  ? 14.982 -16.001 6.545   0.82 16.44 ?  16  VAL   A HB   1 
ATOM   361  H  HB   B VAL   A 1 16  ? 14.820 -15.825 6.740   0.18 15.03 ?  16  VAL   A HB   1 
ATOM   362  H  HG11 A VAL   A 1 16  ? 15.322 -14.008 5.224   0.82 17.42 ?  16  VAL   A HG11 1 
ATOM   363  H  HG11 B VAL   A 1 16  ? 15.221 -13.848 5.451   0.18 15.13 ?  16  VAL   A HG11 1 
ATOM   364  H  HG12 A VAL   A 1 16  ? 14.287 -13.849 6.417   0.82 17.42 ?  16  VAL   A HG12 1 
ATOM   365  H  HG12 B VAL   A 1 16  ? 14.281 -13.622 6.710   0.18 15.13 ?  16  VAL   A HG12 1 
ATOM   366  H  HG13 A VAL   A 1 16  ? 15.770 -13.296 6.570   0.82 17.42 ?  16  VAL   A HG13 1 
ATOM   367  H  HG13 B VAL   A 1 16  ? 15.809 -13.191 6.771   0.18 15.13 ?  16  VAL   A HG13 1 
ATOM   368  H  HG21 A VAL   A 1 16  ? 16.848 -15.781 5.133   0.82 17.98 ?  16  VAL   A HG21 1 
ATOM   369  H  HG21 B VAL   A 1 16  ? 16.674 -15.668 5.280   0.18 15.47 ?  16  VAL   A HG21 1 
ATOM   370  H  HG22 A VAL   A 1 16  ? 17.675 -15.206 6.360   0.82 17.98 ?  16  VAL   A HG22 1 
ATOM   371  H  HG22 B VAL   A 1 16  ? 17.561 -15.213 6.516   0.18 15.47 ?  16  VAL   A HG22 1 
ATOM   372  H  HG23 A VAL   A 1 16  ? 17.159 -16.707 6.386   0.82 17.98 ?  16  VAL   A HG23 1 
ATOM   373  H  HG23 B VAL   A 1 16  ? 16.934 -16.671 6.484   0.18 15.47 ?  16  VAL   A HG23 1 
ATOM   374  N  N    A TYR   A 1 17  ? 14.600 -13.525 9.407   0.82 12.52 ?  17  TYR   A N    1 
ATOM   375  N  N    B TYR   A 1 17  ? 14.545 -13.373 9.507   0.18 12.19 ?  17  TYR   A N    1 
ATOM   376  C  CA   A TYR   A 1 17  ? 13.532 -12.844 10.117  0.82 12.81 ?  17  TYR   A CA   1 
ATOM   377  C  CA   B TYR   A 1 17  ? 13.458 -12.697 10.205  0.18 12.15 ?  17  TYR   A CA   1 
ATOM   378  C  C    A TYR   A 1 17  ? 13.257 -11.519 9.416   0.82 13.11 ?  17  TYR   A C    1 
ATOM   379  C  C    B TYR   A 1 17  ? 13.207 -11.349 9.544   0.18 12.39 ?  17  TYR   A C    1 
ATOM   380  O  O    A TYR   A 1 17  ? 14.144 -10.966 8.762   0.82 12.61 ?  17  TYR   A O    1 
ATOM   381  O  O    B TYR   A 1 17  ? 14.157 -10.644 9.195   0.18 12.05 ?  17  TYR   A O    1 
ATOM   382  C  CB   A TYR   A 1 17  ? 13.963 -12.590 11.567  0.82 13.35 ?  17  TYR   A CB   1 
ATOM   383  C  CB   B TYR   A 1 17  ? 13.821 -12.473 11.679  0.18 12.02 ?  17  TYR   A CB   1 
ATOM   384  C  CG   A TYR   A 1 17  ? 14.173 -13.859 12.367  0.82 13.84 ?  17  TYR   A CG   1 
ATOM   385  C  CG   B TYR   A 1 17  ? 13.929 -13.745 12.485  0.18 11.79 ?  17  TYR   A CG   1 
ATOM   386  C  CD1  A TYR   A 1 17  ? 15.345 -14.603 12.260  0.82 14.68 ?  17  TYR   A CD1  1 
ATOM   387  C  CD1  B TYR   A 1 17  ? 15.067 -14.540 12.424  0.18 11.78 ?  17  TYR   A CD1  1 
ATOM   388  C  CD2  A TYR   A 1 17  ? 13.189 -14.324 13.228  0.82 14.00 ?  17  TYR   A CD2  1 
ATOM   389  C  CD2  B TYR   A 1 17  ? 12.891 -14.151 13.311  0.18 11.61 ?  17  TYR   A CD2  1 
ATOM   390  C  CE1  A TYR   A 1 17  ? 15.524 -15.777 12.986  0.82 15.00 ?  17  TYR   A CE1  1 
ATOM   391  C  CE1  B TYR   A 1 17  ? 15.165 -15.709 13.161  0.18 11.62 ?  17  TYR   A CE1  1 
ATOM   392  C  CE2  A TYR   A 1 17  ? 13.357 -15.496 13.958  0.82 14.20 ?  17  TYR   A CE2  1 
ATOM   393  C  CE2  B TYR   A 1 17  ? 12.977 -15.317 14.050  0.18 11.28 ?  17  TYR   A CE2  1 
ATOM   394  C  CZ   A TYR   A 1 17  ? 14.528 -16.216 13.837  0.82 14.50 ?  17  TYR   A CZ   1 
ATOM   395  C  CZ   B TYR   A 1 17  ? 14.117 -16.091 13.974  0.18 11.39 ?  17  TYR   A CZ   1 
ATOM   396  O  OH   A TYR   A 1 17  ? 14.692 -17.372 14.567  0.82 15.13 ?  17  TYR   A OH   1 
ATOM   397  O  OH   B TYR   A 1 17  ? 14.201 -17.250 14.712  0.18 11.59 ?  17  TYR   A OH   1 
ATOM   398  H  H    A TYR   A 1 17  ? 15.299 -13.026 9.306   0.82 15.07 ?  17  TYR   A H    1 
ATOM   399  H  H    B TYR   A 1 17  ? 15.198 -12.842 9.321   0.18 14.67 ?  17  TYR   A H    1 
ATOM   400  H  HA   A TYR   A 1 17  ? 12.732 -13.387 10.103  0.82 15.41 ?  17  TYR   A HA   1 
ATOM   401  H  HA   B TYR   A 1 17  ? 12.648 -13.225 10.159  0.18 14.62 ?  17  TYR   A HA   1 
ATOM   402  H  HB2  A TYR   A 1 17  ? 14.798 -12.099 11.566  0.82 16.05 ?  17  TYR   A HB2  1 
ATOM   403  H  HB2  B TYR   A 1 17  ? 14.675 -12.018 11.730  0.18 14.46 ?  17  TYR   A HB2  1 
ATOM   404  H  HB3  A TYR   A 1 17  ? 13.275 -12.073 12.007  0.82 16.05 ?  17  TYR   A HB3  1 
ATOM   405  H  HB3  B TYR   A 1 17  ? 13.135 -11.928 12.087  0.18 14.46 ?  17  TYR   A HB3  1 
ATOM   406  H  HD1  A TYR   A 1 17  ? 16.018 -14.319 11.687  0.82 17.65 ?  17  TYR   A HD1  1 
ATOM   407  H  HD1  B TYR   A 1 17  ? 15.773 -14.284 11.875  0.18 14.17 ?  17  TYR   A HD1  1 
ATOM   408  H  HD2  A TYR   A 1 17  ? 12.394 -13.854 13.317  0.82 16.84 ?  17  TYR   A HD2  1 
ATOM   409  H  HD2  B TYR   A 1 17  ? 12.120 -13.633 13.367  0.18 13.97 ?  17  TYR   A HD2  1 
ATOM   410  H  HE1  A TYR   A 1 17  ? 16.314 -16.269 12.904  0.82 18.04 ?  17  TYR   A HE1  1 
ATOM   411  H  HE1  B TYR   A 1 17  ? 15.933 -16.233 13.107  0.18 13.99 ?  17  TYR   A HE1  1 
ATOM   412  H  HE2  A TYR   A 1 17  ? 12.684 -15.797 14.533  0.82 17.08 ?  17  TYR   A HE2  1 
ATOM   413  H  HE2  B TYR   A 1 17  ? 12.273 -15.577 14.599  0.18 13.58 ?  17  TYR   A HE2  1 
ATOM   414  H  HH   A TYR   A 1 17  ? 15.449 -17.709 14.424  0.82 18.19 ?  17  TYR   A HH   1 
ATOM   415  H  HH   B TYR   A 1 17  ? 13.448 -17.437 15.033  0.18 13.95 ?  17  TYR   A HH   1 
ATOM   416  N  N    A ILE   A 1 18  ? 12.040 -10.983 9.563   0.82 13.35 ?  18  ILE   A N    1 
ATOM   417  N  N    B ILE   A 1 18  ? 11.931 -10.984 9.382   0.18 12.73 ?  18  ILE   A N    1 
ATOM   418  C  CA   A ILE   A 1 18  ? 11.653 -9.781  8.822   0.82 13.92 ?  18  ILE   A CA   1 
ATOM   419  C  CA   B ILE   A 1 18  ? 11.549 -9.756  8.690   0.18 13.26 ?  18  ILE   A CA   1 
ATOM   420  C  C    A ILE   A 1 18  ? 10.696 -8.922  9.643   0.82 14.58 ?  18  ILE   A C    1 
ATOM   421  C  C    B ILE   A 1 18  ? 10.624 -8.926  9.573   0.18 13.94 ?  18  ILE   A C    1 
ATOM   422  O  O    A ILE   A 1 18  ? 9.849  -9.432  10.384  0.82 15.16 ?  18  ILE   A O    1 
ATOM   423  O  O    B ILE   A 1 18  ? 9.886  -9.459  10.407  0.18 14.06 ?  18  ILE   A O    1 
ATOM   424  C  CB   A ILE   A 1 18  ? 11.083 -10.159 7.433   0.82 14.10 ?  18  ILE   A CB   1 
ATOM   425  C  CB   B ILE   A 1 18  ? 10.893 -10.053 7.320   0.18 13.25 ?  18  ILE   A CB   1 
ATOM   426  C  CG1  A ILE   A 1 18  ? 11.027 -8.944  6.505   0.82 14.72 ?  18  ILE   A CG1  1 
ATOM   427  C  CG1  B ILE   A 1 18  ? 10.755 -8.773  6.490   0.18 13.50 ?  18  ILE   A CG1  1 
ATOM   428  C  CG2  A ILE   A 1 18  ? 9.730  -10.866 7.562   0.82 14.87 ?  18  ILE   A CG2  1 
ATOM   429  C  CG2  B ILE   A 1 18  ? 9.537  -10.724 7.503   0.18 13.47 ?  18  ILE   A CG2  1 
ATOM   430  C  CD1  A ILE   A 1 18  ? 10.758 -9.307  5.074   0.82 15.91 ?  18  ILE   A CD1  1 
ATOM   431  C  CD1  B ILE   A 1 18  ? 10.091 -8.983  5.148   0.18 13.96 ?  18  ILE   A CD1  1 
ATOM   432  H  H    A ILE   A 1 18  ? 11.433 -11.308 10.074  0.82 16.06 ?  18  ILE   A H    1 
ATOM   433  H  H    B ILE   A 1 18  ? 11.262 -11.445 9.664   0.18 15.31 ?  18  ILE   A H    1 
ATOM   434  H  HA   A ILE   A 1 18  ? 12.460 -9.259  8.669   0.82 16.75 ?  18  ILE   A HA   1 
ATOM   435  H  HA   B ILE   A 1 18  ? 12.345 -9.228  8.526   0.18 15.95 ?  18  ILE   A HA   1 
ATOM   436  H  HB   A ILE   A 1 18  ? 11.700 -10.792 7.035   0.82 16.96 ?  18  ILE   A HB   1 
ATOM   437  H  HB   B ILE   A 1 18  ? 11.469 -10.664 6.838   0.18 15.94 ?  18  ILE   A HB   1 
ATOM   438  H  HG12 A ILE   A 1 18  ? 10.326 -8.350  6.799   0.82 17.70 ?  18  ILE   A HG12 1 
ATOM   439  H  HG12 B ILE   A 1 18  ? 10.220 -8.132  6.978   0.18 16.24 ?  18  ILE   A HG12 1 
ATOM   440  H  HG13 A ILE   A 1 18  ? 11.886 -8.486  6.533   0.82 17.70 ?  18  ILE   A HG13 1 
ATOM   441  H  HG13 B ILE   A 1 18  ? 11.640 -8.409  6.326   0.18 16.24 ?  18  ILE   A HG13 1 
ATOM   442  H  HG21 A ILE   A 1 18  ? 9.477  -11.217 6.692   0.82 17.88 ?  18  ILE   A HG21 1 
ATOM   443  H  HG21 B ILE   A 1 18  ? 9.265  -11.120 6.660   0.18 16.20 ?  18  ILE   A HG21 1 
ATOM   444  H  HG22 A ILE   A 1 18  ? 9.816  -11.593 8.198   0.82 17.88 ?  18  ILE   A HG22 1 
ATOM   445  H  HG22 B ILE   A 1 18  ? 9.618  -11.413 8.180   0.18 16.20 ?  18  ILE   A HG22 1 
ATOM   446  H  HG23 A ILE   A 1 18  ? 9.068  -10.231 7.869   0.82 17.88 ?  18  ILE   A HG23 1 
ATOM   447  H  HG23 B ILE   A 1 18  ? 8.889  -10.060 7.781   0.18 16.20 ?  18  ILE   A HG23 1 
ATOM   448  H  HD11 A ILE   A 1 18  ? 10.807 -8.502  4.530   0.82 19.13 ?  18  ILE   A HD11 1 
ATOM   449  H  HD11 B ILE   A 1 18  ? 10.179 -8.173  4.622   0.18 16.79 ?  18  ILE   A HD11 1 
ATOM   450  H  HD12 A ILE   A 1 18  ? 11.421 -9.947  4.775   0.82 19.13 ?  18  ILE   A HD12 1 
ATOM   451  H  HD12 B ILE   A 1 18  ? 10.525 -9.721  4.693   0.18 16.79 ?  18  ILE   A HD12 1 
ATOM   452  H  HD13 A ILE   A 1 18  ? 9.870  -9.693  5.008   0.82 19.13 ?  18  ILE   A HD13 1 
ATOM   453  H  HD13 B ILE   A 1 18  ? 9.153  -9.185  5.288   0.18 16.79 ?  18  ILE   A HD13 1 
ATOM   454  N  N    A LYS   A 1 19  ? 10.825 -7.601  9.483   0.82 15.15 ?  19  LYS   A N    1 
ATOM   455  N  N    B LYS   A 1 19  ? 10.668 -7.605  9.379   0.18 14.62 ?  19  LYS   A N    1 
ATOM   456  C  CA   A LYS   A 1 19  ? 10.020 -6.638  10.225  0.82 15.97 ?  19  LYS   A CA   1 
ATOM   457  C  CA   B LYS   A 1 19  ? 9.824  -6.684  10.132  0.18 15.21 ?  19  LYS   A CA   1 
ATOM   458  C  C    A LYS   A 1 19  ? 9.789  -5.398  9.370   0.82 16.23 ?  19  LYS   A C    1 
ATOM   459  C  C    B LYS   A 1 19  ? 9.796  -5.345  9.410   0.18 15.49 ?  19  LYS   A C    1 
ATOM   460  O  O    A LYS   A 1 19  ? 10.645 -5.011  8.568   0.82 15.70 ?  19  LYS   A O    1 
ATOM   461  O  O    B LYS   A 1 19  ? 10.850 -4.821  9.040   0.18 15.67 ?  19  LYS   A O    1 
ATOM   462  C  CB   A LYS   A 1 19  ? 10.750 -6.246  11.516  0.82 16.77 ?  19  LYS   A CB   1 
ATOM   463  C  CB   B LYS   A 1 19  ? 10.368 -6.503  11.555  0.18 15.53 ?  19  LYS   A CB   1 
ATOM   464  C  CG   A LYS   A 1 19  ? 9.998  -5.363  12.496  0.82 18.50 ?  19  LYS   A CG   1 
ATOM   465  C  CG   B LYS   A 1 19  ? 9.757  -5.342  12.324  0.18 15.75 ?  19  LYS   A CG   1 
ATOM   466  C  CD   A LYS   A 1 19  ? 10.934 -5.033  13.657  0.82 19.77 ?  19  LYS   A CD   1 
ATOM   467  C  CD   B LYS   A 1 19  ? 10.444 -5.158  13.664  0.18 15.85 ?  19  LYS   A CD   1 
ATOM   468  C  CE   A LYS   A 1 19  ? 10.302 -4.146  14.710  0.82 20.45 ?  19  LYS   A CE   1 
ATOM   469  C  CE   B LYS   A 1 19  ? 9.874  -3.973  14.423  0.18 15.94 ?  19  LYS   A CE   1 
ATOM   470  N  NZ   A LYS   A 1 19  ? 11.227 -3.964  15.868  0.82 20.55 ?  19  LYS   A NZ   1 
ATOM   471  N  NZ   B LYS   A 1 19  ? 10.585 -3.748  15.711  0.18 15.66 ?  19  LYS   A NZ   1 
ATOM   472  H  H    A LYS   A 1 19  ? 11.396 -7.237  8.944   0.82 18.22 ?  19  LYS   A H    1 
ATOM   473  H  H    B LYS   A 1 19  ? 11.187 -7.210  8.815   0.18 17.59 ?  19  LYS   A H    1 
ATOM   474  H  HA   A LYS   A 1 19  ? 9.167  -7.040  10.450  0.82 19.20 ?  19  LYS   A HA   1 
ATOM   475  H  HA   B LYS   A 1 19  ? 8.922  -7.028  10.190  0.18 18.29 ?  19  LYS   A HA   1 
ATOM   476  H  HB2  A LYS   A 1 19  ? 10.981 -7.058  11.988  0.82 20.17 ?  19  LYS   A HB2  1 
ATOM   477  H  HB2  B LYS   A 1 19  ? 10.193 -7.314  12.061  0.18 18.67 ?  19  LYS   A HB2  1 
ATOM   478  H  HB3  A LYS   A 1 19  ? 11.560 -5.774  11.270  0.82 20.17 ?  19  LYS   A HB3  1 
ATOM   479  H  HB3  B LYS   A 1 19  ? 11.323 -6.350  11.507  0.18 18.67 ?  19  LYS   A HB3  1 
ATOM   480  H  HG2  A LYS   A 1 19  ? 9.731  -4.538  12.062  0.82 22.24 ?  19  LYS   A HG2  1 
ATOM   481  H  HG2  B LYS   A 1 19  ? 9.865  -4.518  11.825  0.18 18.93 ?  19  LYS   A HG2  1 
ATOM   482  H  HG3  A LYS   A 1 19  ? 9.225  -5.838  12.841  0.82 22.24 ?  19  LYS   A HG3  1 
ATOM   483  H  HG3  B LYS   A 1 19  ? 8.817  -5.521  12.481  0.18 18.93 ?  19  LYS   A HG3  1 
ATOM   484  H  HD2  A LYS   A 1 19  ? 11.203 -5.860  14.087  0.82 23.77 ?  19  LYS   A HD2  1 
ATOM   485  H  HD2  B LYS   A 1 19  ? 10.317 -5.954  14.201  0.18 19.06 ?  19  LYS   A HD2  1 
ATOM   486  H  HD3  A LYS   A 1 19  ? 11.714 -4.575  13.308  0.82 23.77 ?  19  LYS   A HD3  1 
ATOM   487  H  HD3  B LYS   A 1 19  ? 11.391 -4.999  13.518  0.18 19.06 ?  19  LYS   A HD3  1 
ATOM   488  H  HE2  A LYS   A 1 19  ? 10.115 -3.272  14.327  0.82 24.57 ?  19  LYS   A HE2  1 
ATOM   489  H  HE2  B LYS   A 1 19  ? 9.968  -3.172  13.883  0.18 19.17 ?  19  LYS   A HE2  1 
ATOM   490  H  HE3  A LYS   A 1 19  ? 9.484  -4.555  15.032  0.82 24.57 ?  19  LYS   A HE3  1 
ATOM   491  H  HE3  B LYS   A 1 19  ? 8.939  -4.138  14.618  0.18 19.17 ?  19  LYS   A HE3  1 
ATOM   492  H  HZ1  A LYS   A 1 19  ? 10.814 -3.528  16.523  0.82 24.70 ?  19  LYS   A HZ1  1 
ATOM   493  H  HZ1  B LYS   A 1 19  ? 10.233 -3.050  16.136  0.18 18.82 ?  19  LYS   A HZ1  1 
ATOM   494  H  HZ2  A LYS   A 1 19  ? 11.494 -4.758  16.170  0.82 24.70 ?  19  LYS   A HZ2  1 
ATOM   495  H  HZ2  B LYS   A 1 19  ? 10.512 -4.468  16.229  0.18 18.82 ?  19  LYS   A HZ2  1 
ATOM   496  H  HZ3  A LYS   A 1 19  ? 11.941 -3.497  15.616  0.82 24.70 ?  19  LYS   A HZ3  1 
ATOM   497  H  HZ3  B LYS   A 1 19  ? 11.448 -3.589  15.560  0.18 18.82 ?  19  LYS   A HZ3  1 
ATOM   498  N  N    A ASN   A 1 20  ? 8.623  -4.774  9.546   0.82 17.49 ?  20  ASN   A N    1 
ATOM   499  N  N    B ASN   A 1 20  ? 8.595  -4.793  9.215   0.18 15.59 ?  20  ASN   A N    1 
ATOM   500  C  CA   A ASN   A 1 20  ? 8.356  -3.456  8.971   0.82 18.90 ?  20  ASN   A CA   1 
ATOM   501  C  CA   B ASN   A 1 20  ? 8.466  -3.439  8.689   0.18 15.77 ?  20  ASN   A CA   1 
ATOM   502  C  C    A ASN   A 1 20  ? 8.978  -2.447  9.922   0.82 19.44 ?  20  ASN   A C    1 
ATOM   503  C  C    B ASN   A 1 20  ? 9.054  -2.449  9.684   0.18 16.10 ?  20  ASN   A C    1 
ATOM   504  O  O    A ASN   A 1 20  ? 8.446  -2.184  11.003  0.82 20.71 ?  20  ASN   A O    1 
ATOM   505  O  O    B ASN   A 1 20  ? 8.535  -2.296  10.794  0.18 16.43 ?  20  ASN   A O    1 
ATOM   506  C  CB   A ASN   A 1 20  ? 6.854  -3.236  8.815   0.82 20.19 ?  20  ASN   A CB   1 
ATOM   507  C  CB   B ASN   A 1 20  ? 7.000  -3.095  8.405   0.18 15.65 ?  20  ASN   A CB   1 
ATOM   508  C  CG   A ASN   A 1 20  ? 6.494  -1.829  8.326   0.82 21.79 ?  20  ASN   A CG   1 
ATOM   509  C  CG   B ASN   A 1 20  ? 6.724  -1.601  8.477   0.18 15.64 ?  20  ASN   A CG   1 
ATOM   510  O  OD1  A ASN   A 1 20  ? 5.493  -1.251  8.761   0.82 23.14 ?  20  ASN   A OD1  1 
ATOM   511  O  OD1  B ASN   A 1 20  ? 6.037  -1.130  9.384   0.18 15.88 ?  20  ASN   A OD1  1 
ATOM   512  N  ND2  A ASN   A 1 20  ? 7.295  -1.283  7.417   0.82 22.47 ?  20  ASN   A ND2  1 
ATOM   513  N  ND2  B ASN   A 1 20  ? 7.266  -0.849  7.524   0.18 15.51 ?  20  ASN   A ND2  1 
ATOM   514  H  H    A ASN   A 1 20  ? 7.971  -5.096  10.002  0.82 21.02 ?  20  ASN   A H    1 
ATOM   515  H  H    B ASN   A 1 20  ? 7.846  -5.183  9.375   0.18 18.74 ?  20  ASN   A H    1 
ATOM   516  H  HA   A ASN   A 1 20  ? 8.786  -3.382  8.106   0.82 22.71 ?  20  ASN   A HA   1 
ATOM   517  H  HA   B ASN   A 1 20  ? 8.959  -3.366  7.859   0.18 18.97 ?  20  ASN   A HA   1 
ATOM   518  H  HB2  A ASN   A 1 20  ? 6.516  -3.873  8.171   0.82 24.26 ?  20  ASN   A HB2  1 
ATOM   519  H  HB2  B ASN   A 1 20  ? 6.773  -3.390  7.509   0.18 18.82 ?  20  ASN   A HB2  1 
ATOM   520  H  HB3  A ASN   A 1 20  ? 6.432  -3.374  9.676   0.82 24.26 ?  20  ASN   A HB3  1 
ATOM   521  H  HB3  B ASN   A 1 20  ? 6.432  -3.538  9.054   0.18 18.82 ?  20  ASN   A HB3  1 
ATOM   522  H  HD21 A ASN   A 1 20  ? 7.126  -0.497  7.119   0.82 27.00 ?  20  ASN   A HD21 1 
ATOM   523  H  HD21 B ASN   A 1 20  ? 7.138  0.002   7.522   0.18 18.65 ?  20  ASN   A HD21 1 
ATOM   524  H  HD22 A ASN   A 1 20  ? 7.983  -1.714  7.131   0.82 27.00 ?  20  ASN   A HD22 1 
ATOM   525  H  HD22 B ASN   A 1 20  ? 7.744  -1.212  6.909   0.18 18.65 ?  20  ASN   A HD22 1 
ATOM   526  N  N    A ALA   A 1 21  ? 10.127 -1.896  9.538   0.82 19.15 ?  21  ALA   A N    1 
ATOM   527  N  N    B ALA   A 1 21  ? 10.141 -1.782  9.306   0.18 15.97 ?  21  ALA   A N    1 
ATOM   528  C  CA   A ALA   A 1 21  ? 10.838 -1.000  10.436  0.82 18.87 ?  21  ALA   A CA   1 
ATOM   529  C  CA   B ALA   A 1 21  ? 10.767 -0.815  10.195  0.18 15.69 ?  21  ALA   A CA   1 
ATOM   530  C  C    A ALA   A 1 21  ? 11.784 -0.121  9.644   0.82 18.39 ?  21  ALA   A C    1 
ATOM   531  C  C    B ALA   A 1 21  ? 11.815 -0.033  9.423   0.18 15.41 ?  21  ALA   A C    1 
ATOM   532  O  O    A ALA   A 1 21  ? 12.215 -0.480  8.545   0.82 18.96 ?  21  ALA   A O    1 
ATOM   533  O  O    B ALA   A 1 21  ? 12.295 -0.468  8.371   0.18 15.70 ?  21  ALA   A O    1 
ATOM   534  C  CB   A ALA   A 1 21  ? 11.624 -1.782  11.490  0.82 19.91 ?  21  ALA   A CB   1 
ATOM   535  C  CB   B ALA   A 1 21  ? 11.416 -1.501  11.399  0.18 16.07 ?  21  ALA   A CB   1 
ATOM   536  H  H    A ALA   A 1 21  ? 10.508 -2.014  8.772   0.82 23.02 ?  21  ALA   A H    1 
ATOM   537  H  H    B ALA   A 1 21  ? 10.536 -1.877  8.547   0.18 19.21 ?  21  ALA   A H    1 
ATOM   538  H  HA   A ALA   A 1 21  ? 10.201 -0.426  10.888  0.82 22.69 ?  21  ALA   A HA   1 
ATOM   539  H  HA   B ALA   A 1 21  ? 10.098 -0.193  10.519  0.18 18.86 ?  21  ALA   A HA   1 
ATOM   540  H  HB1  A ALA   A 1 21  ? 12.024 -1.153  12.107  0.82 23.94 ?  21  ALA   A HB1  1 
ATOM   541  H  HB1  B ALA   A 1 21  ? 11.826 -0.827  11.963  0.18 19.32 ?  21  ALA   A HB1  1 
ATOM   542  H  HB2  A ALA   A 1 21  ? 11.008 -2.365  11.965  0.82 23.94 ?  21  ALA   A HB2  1 
ATOM   543  H  HB2  B ALA   A 1 21  ? 10.735 -1.979  11.894  0.18 19.32 ?  21  ALA   A HB2  1 
ATOM   544  H  HB3  A ALA   A 1 21  ? 12.306 -2.308  11.051  0.82 23.94 ?  21  ALA   A HB3  1 
ATOM   545  H  HB3  B ALA   A 1 21  ? 12.092 -2.121  11.081  0.18 19.32 ?  21  ALA   A HB3  1 
ATOM   546  N  N    A ASP   A 1 22  ? 12.079 1.043   10.224  0.82 18.08 ?  22  ASP   A N    1 
ATOM   547  N  N    B ASP   A 1 22  ? 12.158 1.134   9.964   0.18 15.09 ?  22  ASP   A N    1 
ATOM   548  C  CA   A ASP   A 1 22  ? 13.107 1.953   9.736   0.82 17.99 ?  22  ASP   A CA   1 
ATOM   549  C  CA   B ASP   A 1 22  ? 13.298 1.898   9.484   0.18 15.03 ?  22  ASP   A CA   1 
ATOM   550  C  C    A ASP   A 1 22  ? 14.443 1.457   10.276  0.82 16.72 ?  22  ASP   A C    1 
ATOM   551  C  C    B ASP   A 1 22  ? 14.562 1.301   10.088  0.18 14.69 ?  22  ASP   A C    1 
ATOM   552  O  O    A ASP   A 1 22  ? 14.663 1.462   11.490  0.82 17.64 ?  22  ASP   A O    1 
ATOM   553  O  O    B ASP   A 1 22  ? 14.656 1.136   11.308  0.18 14.84 ?  22  ASP   A O    1 
ATOM   554  C  CB   A ASP   A 1 22  ? 12.789 3.350   10.263  0.82 19.61 ?  22  ASP   A CB   1 
ATOM   555  C  CB   B ASP   A 1 22  ? 13.160 3.359   9.914   0.18 15.46 ?  22  ASP   A CB   1 
ATOM   556  C  CG   A ASP   A 1 22  ? 13.775 4.403   9.801   0.82 20.87 ?  22  ASP   A CG   1 
ATOM   557  C  CG   B ASP   A 1 22  ? 14.200 4.259   9.265   0.18 15.62 ?  22  ASP   A CG   1 
ATOM   558  O  OD1  A ASP   A 1 22  ? 14.850 4.058   9.277   0.82 21.02 ?  22  ASP   A OD1  1 
ATOM   559  O  OD1  B ASP   A 1 22  ? 15.252 3.741   8.834   0.18 15.58 ?  22  ASP   A OD1  1 
ATOM   560  O  OD2  A ASP   A 1 22  ? 13.474 5.601   9.983   0.82 22.32 -1 22  ASP   A OD2  1 
ATOM   561  O  OD2  B ASP   A 1 22  ? 13.968 5.485   9.182   0.18 15.96 -1 22  ASP   A OD2  1 
ATOM   562  H  H    A ASP   A 1 22  ? 11.668 1.342   10.925  0.82 21.73 ?  22  ASP   A H    1 
ATOM   563  H  H    B ASP   A 1 22  ? 11.741 1.506   10.618  0.18 18.14 ?  22  ASP   A H    1 
ATOM   564  H  HA   A ASP   A 1 22  ? 13.125 1.957   8.767   0.82 21.63 ?  22  ASP   A HA   1 
ATOM   565  H  HA   B ASP   A 1 22  ? 13.351 1.860   8.515   0.18 18.08 ?  22  ASP   A HA   1 
ATOM   566  H  HB2  A ASP   A 1 22  ? 11.901 3.602   9.968   0.82 23.57 ?  22  ASP   A HB2  1 
ATOM   567  H  HB2  B ASP   A 1 22  ? 12.278 3.682   9.666   0.18 18.59 ?  22  ASP   A HB2  1 
ATOM   568  H  HB3  A ASP   A 1 22  ? 12.825 3.336   11.231  0.82 23.57 ?  22  ASP   A HB3  1 
ATOM   569  H  HB3  B ASP   A 1 22  ? 13.267 3.415   10.880  0.18 18.59 ?  22  ASP   A HB3  1 
ATOM   570  N  N    A ILE   A 1 23  ? 15.331 1.017   9.378   0.82 16.17 ?  23  ILE   A N    1 
ATOM   571  N  N    B ILE   A 1 23  ? 15.528 0.957   9.233   0.18 14.60 ?  23  ILE   A N    1 
ATOM   572  C  CA   A ILE   A 1 23  ? 16.594 0.410   9.794   0.82 15.17 ?  23  ILE   A CA   1 
ATOM   573  C  CA   B ILE   A 1 23  ? 16.775 0.376   9.715   0.18 14.41 ?  23  ILE   A CA   1 
ATOM   574  C  C    A ILE   A 1 23  ? 17.407 1.353   10.672  0.82 15.28 ?  23  ILE   A C    1 
ATOM   575  C  C    B ILE   A 1 23  ? 17.550 1.356   10.583  0.18 15.07 ?  23  ILE   A C    1 
ATOM   576  O  O    A ILE   A 1 23  ? 18.119 0.907   11.579  0.82 15.22 ?  23  ILE   A O    1 
ATOM   577  O  O    B ILE   A 1 23  ? 18.377 0.936   11.399  0.18 14.90 ?  23  ILE   A O    1 
ATOM   578  C  CB   A ILE   A 1 23  ? 17.383 -0.098  8.566   0.82 14.49 ?  23  ILE   A CB   1 
ATOM   579  C  CB   B ILE   A 1 23  ? 17.632 -0.171  8.548   0.18 13.69 ?  23  ILE   A CB   1 
ATOM   580  C  CG1  A ILE   A 1 23  ? 18.570 -0.959  9.006   0.82 14.78 ?  23  ILE   A CG1  1 
ATOM   581  C  CG1  B ILE   A 1 23  ? 18.629 -1.213  9.065   0.18 13.64 ?  23  ILE   A CG1  1 
ATOM   582  C  CG2  A ILE   A 1 23  ? 17.832 1.062   7.678   0.82 14.67 ?  23  ILE   A CG2  1 
ATOM   583  C  CG2  B ILE   A 1 23  ? 18.367 0.957   7.834   0.18 13.49 ?  23  ILE   A CG2  1 
ATOM   584  C  CD1  A ILE   A 1 23  ? 19.276 -1.668  7.854   0.82 15.18 ?  23  ILE   A CD1  1 
ATOM   585  C  CD1  B ILE   A 1 23  ? 19.475 -1.849  7.979   0.18 13.67 ?  23  ILE   A CD1  1 
ATOM   586  H  H    A ILE   A 1 23  ? 15.219 1.054   8.531   0.82 19.45 ?  23  ILE   A H    1 
ATOM   587  H  H    B ILE   A 1 23  ? 15.482 1.039   8.386   0.18 17.55 ?  23  ILE   A H    1 
ATOM   588  H  HA   A ILE   A 1 23  ? 16.394 -0.366  10.335  0.82 18.24 ?  23  ILE   A HA   1 
ATOM   589  H  HA   B ILE   A 1 23  ? 16.550 -0.382  10.271  0.18 17.33 ?  23  ILE   A HA   1 
ATOM   590  H  HB   A ILE   A 1 23  ? 16.790 -0.658  8.043   0.82 17.42 ?  23  ILE   A HB   1 
ATOM   591  H  HB   B ILE   A 1 23  ? 17.045 -0.605  7.910   0.18 16.46 ?  23  ILE   A HB   1 
ATOM   592  H  HG12 A ILE   A 1 23  ? 19.225 -0.395  9.446   0.82 17.77 ?  23  ILE   A HG12 1 
ATOM   593  H  HG12 B ILE   A 1 23  ? 19.232 -0.787  9.694   0.18 16.41 ?  23  ILE   A HG12 1 
ATOM   594  H  HG13 A ILE   A 1 23  ? 18.255 -1.640  9.620   0.82 17.77 ?  23  ILE   A HG13 1 
ATOM   595  H  HG13 B ILE   A 1 23  ? 18.139 -1.923  9.509   0.18 16.41 ?  23  ILE   A HG13 1 
ATOM   596  H  HG21 A ILE   A 1 23  ? 18.196 0.708   6.850   0.82 17.64 ?  23  ILE   A HG21 1 
ATOM   597  H  HG21 B ILE   A 1 23  ? 18.684 0.633   6.975   0.18 16.22 ?  23  ILE   A HG21 1 
ATOM   598  H  HG22 A ILE   A 1 23  ? 17.064 1.625   7.482   0.82 17.64 ?  23  ILE   A HG22 1 
ATOM   599  H  HG22 B ILE   A 1 23  ? 17.755 1.696   7.704   0.18 16.22 ?  23  ILE   A HG22 1 
ATOM   600  H  HG23 A ILE   A 1 23  ? 18.507 1.579   8.142   0.82 17.64 ?  23  ILE   A HG23 1 
ATOM   601  H  HG23 B ILE   A 1 23  ? 19.119 1.239   8.378   0.18 16.22 ?  23  ILE   A HG23 1 
ATOM   602  H  HD11 A ILE   A 1 23  ? 19.961 -2.252  8.215   0.82 18.25 ?  23  ILE   A HD11 1 
ATOM   603  H  HD11 B ILE   A 1 23  ? 19.993 -2.573  8.366   0.18 16.45 ?  23  ILE   A HD11 1 
ATOM   604  H  HD12 A ILE   A 1 23  ? 18.624 -2.189  7.359   0.82 18.25 ?  23  ILE   A HD12 1 
ATOM   605  H  HD12 B ILE   A 1 23  ? 18.890 -2.195  7.287   0.18 16.45 ?  23  ILE   A HD12 1 
ATOM   606  H  HD13 A ILE   A 1 23  ? 19.679 -1.004  7.274   0.82 18.25 ?  23  ILE   A HD13 1 
ATOM   607  H  HD13 B ILE   A 1 23  ? 20.069 -1.180  7.606   0.18 16.45 ?  23  ILE   A HD13 1 
ATOM   608  N  N    . VAL   A 1 24  ? 17.307 2.661   10.431  1.00 16.12 ?  24  VAL   A N    1 
ATOM   609  C  CA   . VAL   A 1 24  ? 17.985 3.637   11.281  1.00 17.36 ?  24  VAL   A CA   1 
ATOM   610  C  C    . VAL   A 1 24  ? 17.466 3.539   12.708  1.00 18.34 ?  24  VAL   A C    1 
ATOM   611  O  O    . VAL   A 1 24  ? 18.240 3.503   13.671  1.00 18.44 ?  24  VAL   A O    1 
ATOM   612  C  CB   . VAL   A 1 24  ? 17.802 5.053   10.711  1.00 18.43 ?  24  VAL   A CB   1 
ATOM   613  C  CG1  . VAL   A 1 24  ? 18.317 6.100   11.695  1.00 19.36 ?  24  VAL   A CG1  1 
ATOM   614  C  CG2  . VAL   A 1 24  ? 18.500 5.176   9.365   1.00 19.35 ?  24  VAL   A CG2  1 
ATOM   615  H  H    A VAL   A 1 24  ? 16.862 3.006   9.785   0.82 19.38 ?  24  VAL   A H    1 
ATOM   616  H  H    B VAL   A 1 24  ? 16.783 3.000   9.845   0.18 19.38 ?  24  VAL   A H    1 
ATOM   617  H  HA   . VAL   A 1 24  ? 18.937 3.443   11.297  1.00 20.86 ?  24  VAL   A HA   1 
ATOM   618  H  HB   . VAL   A 1 24  ? 16.857 5.215   10.570  1.00 22.15 ?  24  VAL   A HB   1 
ATOM   619  H  HG11 . VAL   A 1 24  ? 18.445 6.937   11.222  1.00 23.28 ?  24  VAL   A HG11 1 
ATOM   620  H  HG12 . VAL   A 1 24  ? 17.664 6.218   12.402  1.00 23.28 ?  24  VAL   A HG12 1 
ATOM   621  H  HG13 . VAL   A 1 24  ? 19.160 5.798   12.065  1.00 23.28 ?  24  VAL   A HG13 1 
ATOM   622  H  HG21 . VAL   A 1 24  ? 18.246 6.017   8.954   1.00 23.26 ?  24  VAL   A HG21 1 
ATOM   623  H  HG22 . VAL   A 1 24  ? 19.460 5.156   9.504   1.00 23.26 ?  24  VAL   A HG22 1 
ATOM   624  H  HG23 . VAL   A 1 24  ? 18.231 4.437   8.797   1.00 23.26 ?  24  VAL   A HG23 1 
ATOM   625  N  N    A GLU   A 1 25  ? 16.141 3.524   12.865  0.82 19.57 ?  25  GLU   A N    1 
ATOM   626  N  N    B GLU   A 1 25  ? 16.141 3.453   12.862  0.18 18.93 ?  25  GLU   A N    1 
ATOM   627  C  CA   A GLU   A 1 25  ? 15.558 3.462   14.201  0.82 21.27 ?  25  GLU   A CA   1 
ATOM   628  C  CA   B GLU   A 1 25  ? 15.549 3.331   14.190  0.18 19.76 ?  25  GLU   A CA   1 
ATOM   629  C  C    A GLU   A 1 25  ? 15.805 2.103   14.844  0.82 20.40 ?  25  GLU   A C    1 
ATOM   630  C  C    B GLU   A 1 25  ? 15.845 1.969   14.807  0.18 19.30 ?  25  GLU   A C    1 
ATOM   631  O  O    A GLU   A 1 25  ? 16.060 2.020   16.051  0.82 20.93 ?  25  GLU   A O    1 
ATOM   632  O  O    B GLU   A 1 25  ? 16.124 1.874   16.008  0.18 19.43 ?  25  GLU   A O    1 
ATOM   633  C  CB   A GLU   A 1 25  ? 14.066 3.800   14.142  0.82 23.59 ?  25  GLU   A CB   1 
ATOM   634  C  CB   B GLU   A 1 25  ? 14.041 3.579   14.113  0.18 21.01 ?  25  GLU   A CB   1 
ATOM   635  C  CG   A GLU   A 1 25  ? 13.796 5.246   13.747  0.82 26.39 ?  25  GLU   A CG   1 
ATOM   636  C  CG   B GLU   A 1 25  ? 13.676 4.964   13.605  0.18 22.35 ?  25  GLU   A CG   1 
ATOM   637  C  CD   A GLU   A 1 25  ? 14.539 6.233   14.633  0.82 28.83 ?  25  GLU   A CD   1 
ATOM   638  C  CD   B GLU   A 1 25  ? 14.232 6.068   14.477  0.18 23.43 ?  25  GLU   A CD   1 
ATOM   639  O  OE1  A GLU   A 1 25  ? 14.583 6.013   15.863  0.82 29.70 ?  25  GLU   A OE1  1 
ATOM   640  O  OE1  B GLU   A 1 25  ? 14.291 5.878   15.711  0.18 23.81 ?  25  GLU   A OE1  1 
ATOM   641  O  OE2  A GLU   A 1 25  ? 15.102 7.211   14.098  0.82 29.85 -1 25  GLU   A OE2  1 
ATOM   642  O  OE2  B GLU   A 1 25  ? 14.615 7.123   13.929  0.18 23.83 -1 25  GLU   A OE2  1 
ATOM   643  H  H    A GLU   A 1 25  ? 15.568 3.549   12.223  0.82 23.52 ?  25  GLU   A H    1 
ATOM   644  H  H    B GLU   A 1 25  ? 15.573 3.462   12.218  0.18 22.76 ?  25  GLU   A H    1 
ATOM   645  H  HA   A GLU   A 1 25  ? 15.989 4.124   14.760  0.82 25.56 ?  25  GLU   A HA   1 
ATOM   646  H  HA   B GLU   A 1 25  ? 15.932 4.004   14.770  0.18 23.75 ?  25  GLU   A HA   1 
ATOM   647  H  HB2  A GLU   A 1 25  ? 13.633 3.231   13.486  0.82 28.35 ?  25  GLU   A HB2  1 
ATOM   648  H  HB2  B GLU   A 1 25  ? 13.644 2.931   13.509  0.18 25.25 ?  25  GLU   A HB2  1 
ATOM   649  H  HB3  A GLU   A 1 25  ? 13.670 3.657   15.016  0.82 28.35 ?  25  GLU   A HB3  1 
ATOM   650  H  HB3  B GLU   A 1 25  ? 13.659 3.481   14.999  0.18 25.25 ?  25  GLU   A HB3  1 
ATOM   651  H  HG2  A GLU   A 1 25  ? 14.094 5.387   12.835  0.82 31.70 ?  25  GLU   A HG2  1 
ATOM   652  H  HG2  B GLU   A 1 25  ? 14.030 5.077   12.709  0.18 26.86 ?  25  GLU   A HG2  1 
ATOM   653  H  HG3  A GLU   A 1 25  ? 12.840 5.420   13.811  0.82 31.70 ?  25  GLU   A HG3  1 
ATOM   654  H  HG3  B GLU   A 1 25  ? 12.711 5.057   13.596  0.18 26.86 ?  25  GLU   A HG3  1 
ATOM   655  N  N    A GLU   A 1 26  ? 15.760 1.031   14.051  0.82 19.76 ?  26  GLU   A N    1 
ATOM   656  N  N    B GLU   A 1 26  ? 15.793 0.903   14.004  0.18 18.83 ?  26  GLU   A N    1 
ATOM   657  C  CA   A GLU   A 1 26  ? 16.082 -0.294  14.575  0.82 19.47 ?  26  GLU   A CA   1 
ATOM   658  C  CA   B GLU   A 1 26  ? 16.108 -0.424  14.523  0.18 18.38 ?  26  GLU   A CA   1 
ATOM   659  C  C    A GLU   A 1 26  ? 17.511 -0.337  15.101  0.82 18.21 ?  26  GLU   A C    1 
ATOM   660  C  C    B GLU   A 1 26  ? 17.545 -0.492  15.016  0.18 17.59 ?  26  GLU   A C    1 
ATOM   661  O  O    A GLU   A 1 26  ? 17.767 -0.838  16.202  0.82 17.91 ?  26  GLU   A O    1 
ATOM   662  O  O    B GLU   A 1 26  ? 17.834 -1.142  16.028  0.18 17.47 ?  26  GLU   A O    1 
ATOM   663  C  CB   A GLU   A 1 26  ? 15.912 -1.344  13.477  0.82 20.92 ?  26  GLU   A CB   1 
ATOM   664  C  CB   B GLU   A 1 26  ? 15.873 -1.478  13.443  0.18 18.78 ?  26  GLU   A CB   1 
ATOM   665  C  CG   A GLU   A 1 26  ? 14.538 -1.956  13.348  0.82 22.77 ?  26  GLU   A CG   1 
ATOM   666  C  CG   B GLU   A 1 26  ? 14.415 -1.801  13.205  0.18 19.20 ?  26  GLU   A CG   1 
ATOM   667  C  CD   A GLU   A 1 26  ? 14.124 -2.751  14.571  0.82 23.13 ?  26  GLU   A CD   1 
ATOM   668  C  CD   B GLU   A 1 26  ? 13.755 -2.436  14.408  0.18 19.20 ?  26  GLU   A CD   1 
ATOM   669  O  OE1  A GLU   A 1 26  ? 14.548 -3.922  14.768  0.82 23.40 ?  26  GLU   A OE1  1 
ATOM   670  O  OE1  B GLU   A 1 26  ? 14.429 -3.211  15.119  0.18 19.38 ?  26  GLU   A OE1  1 
ATOM   671  O  OE2  A GLU   A 1 26  ? 13.348 -2.187  15.347  0.82 23.69 -1 26  GLU   A OE2  1 
ATOM   672  O  OE2  B GLU   A 1 26  ? 12.567 -2.144  14.650  0.18 19.03 -1 26  GLU   A OE2  1 
ATOM   673  H  H    A GLU   A 1 26  ? 15.553 1.048   13.217  0.82 23.75 ?  26  GLU   A H    1 
ATOM   674  H  H    B GLU   A 1 26  ? 15.585 0.922   13.171  0.18 22.63 ?  26  GLU   A H    1 
ATOM   675  H  HA   A GLU   A 1 26  ? 15.480 -0.504  15.306  0.82 23.40 ?  26  GLU   A HA   1 
ATOM   676  H  HA   B GLU   A 1 26  ? 15.526 -0.621  15.272  0.18 22.09 ?  26  GLU   A HA   1 
ATOM   677  H  HB2  A GLU   A 1 26  ? 16.125 -0.933  12.626  0.82 25.14 ?  26  GLU   A HB2  1 
ATOM   678  H  HB2  B GLU   A 1 26  ? 16.244 -1.156  12.606  0.18 22.57 ?  26  GLU   A HB2  1 
ATOM   679  H  HB3  A GLU   A 1 26  ? 16.533 -2.067  13.652  0.82 25.14 ?  26  GLU   A HB3  1 
ATOM   680  H  HB3  B GLU   A 1 26  ? 16.321 -2.299  13.703  0.18 22.57 ?  26  GLU   A HB3  1 
ATOM   681  H  HG2  A GLU   A 1 26  ? 13.890 -1.242  13.210  0.82 27.36 ?  26  GLU   A HG2  1 
ATOM   682  H  HG2  B GLU   A 1 26  ? 13.938 -0.982  13.018  0.18 23.08 ?  26  GLU   A HG2  1 
ATOM   683  H  HG3  A GLU   A 1 26  ? 14.523 -2.562  12.595  0.82 27.36 ?  26  GLU   A HG3  1 
ATOM   684  H  HG3  B GLU   A 1 26  ? 14.347 -2.412  12.456  0.18 23.08 ?  26  GLU   A HG3  1 
ATOM   685  N  N    . ALA   A 1 27  ? 18.462 0.171   14.314  1.00 16.95 ?  27  ALA   A N    1 
ATOM   686  C  CA   . ALA   A 1 27  ? 19.857 0.153   14.737  1.00 16.39 ?  27  ALA   A CA   1 
ATOM   687  C  C    . ALA   A 1 27  ? 20.053 0.957   16.014  1.00 17.60 ?  27  ALA   A C    1 
ATOM   688  O  O    . ALA   A 1 27  ? 20.735 0.505   16.942  1.00 17.97 ?  27  ALA   A O    1 
ATOM   689  C  CB   . ALA   A 1 27  ? 20.754 0.688   13.618  1.00 16.02 ?  27  ALA   A CB   1 
ATOM   690  H  H    A ALA   A 1 27  ? 18.326 0.523   13.541  0.82 20.38 ?  27  ALA   A H    1 
ATOM   691  H  H    B ALA   A 1 27  ? 18.304 0.631   13.604  0.18 20.38 ?  27  ALA   A H    1 
ATOM   692  H  HA   . ALA   A 1 27  ? 20.119 -0.761  14.916  1.00 19.70 ?  27  ALA   A HA   1 
ATOM   693  H  HB1  . ALA   A 1 27  ? 21.679 0.669   13.919  1.00 19.26 ?  27  ALA   A HB1  1 
ATOM   694  H  HB2  . ALA   A 1 27  ? 20.652 0.127   12.834  1.00 19.26 ?  27  ALA   A HB2  1 
ATOM   695  H  HB3  . ALA   A 1 27  ? 20.496 1.600   13.410  1.00 19.26 ?  27  ALA   A HB3  1 
ATOM   696  N  N    . LYS   A 1 28  ? 19.452 2.147   16.090  1.00 19.97 ?  28  LYS   A N    1 
ATOM   697  C  CA   . LYS   A 1 28  ? 19.597 2.969   17.289  1.00 23.27 ?  28  LYS   A CA   1 
ATOM   698  C  C    . LYS   A 1 28  ? 19.069 2.256   18.527  1.00 24.44 ?  28  LYS   A C    1 
ATOM   699  O  O    . LYS   A 1 28  ? 19.627 2.416   19.618  1.00 26.08 ?  28  LYS   A O    1 
ATOM   700  C  CB   . LYS   A 1 28  ? 18.916 4.326   17.094  1.00 25.42 ?  28  LYS   A CB   1 
ATOM   701  C  CG   . LYS   A 1 28  ? 19.709 5.272   16.202  1.00 27.54 ?  28  LYS   A CG   1 
ATOM   702  C  CD   . LYS   A 1 28  ? 19.221 6.707   16.305  1.00 30.08 ?  28  LYS   A CD   1 
ATOM   703  C  CE   . LYS   A 1 28  ? 17.902 6.901   15.586  1.00 31.86 ?  28  LYS   A CE   1 
ATOM   704  N  NZ   . LYS   A 1 28  ? 17.508 8.338   15.552  1.00 33.03 ?  28  LYS   A NZ   1 
ATOM   705  H  H    . LYS   A 1 28  ? 18.962 2.491   15.476  1.00 24.01 ?  28  LYS   A H    1 
ATOM   706  H  HA   . LYS   A 1 28  ? 20.537 3.136   17.439  1.00 27.96 ?  28  LYS   A HA   1 
ATOM   707  H  HB2  . LYS   A 1 28  ? 18.049 4.192   16.684  1.00 30.54 ?  28  LYS   A HB2  1 
ATOM   708  H  HB3  . LYS   A 1 28  ? 18.810 4.756   17.958  1.00 30.54 ?  28  LYS   A HB3  1 
ATOM   709  H  HG2  . LYS   A 1 28  ? 20.642 5.252   16.465  1.00 33.08 ?  28  LYS   A HG2  1 
ATOM   710  H  HG3  . LYS   A 1 28  ? 19.617 4.990   15.278  1.00 33.08 ?  28  LYS   A HG3  1 
ATOM   711  H  HD2  . LYS   A 1 28  ? 19.095 6.935   17.240  1.00 36.13 ?  28  LYS   A HD2  1 
ATOM   712  H  HD3  . LYS   A 1 28  ? 19.878 7.297   15.903  1.00 36.13 ?  28  LYS   A HD3  1 
ATOM   713  H  HE2  . LYS   A 1 28  ? 17.987 6.587   14.672  1.00 38.27 ?  28  LYS   A HE2  1 
ATOM   714  H  HE3  . LYS   A 1 28  ? 17.209 6.406   16.049  1.00 38.27 ?  28  LYS   A HE3  1 
ATOM   715  H  HZ1  . LYS   A 1 28  ? 16.733 8.430   15.126  1.00 39.67 ?  28  LYS   A HZ1  1 
ATOM   716  H  HZ2  . LYS   A 1 28  ? 17.422 8.649   16.381  1.00 39.67 ?  28  LYS   A HZ2  1 
ATOM   717  H  HZ3  . LYS   A 1 28  ? 18.130 8.814   15.128  1.00 39.67 ?  28  LYS   A HZ3  1 
ATOM   718  N  N    . LYS   A 1 29  ? 18.018 1.448   18.376  1.00 24.82 ?  29  LYS   A N    1 
ATOM   719  C  CA   . LYS   A 1 29  ? 17.429 0.752   19.517  1.00 26.45 ?  29  LYS   A CA   1 
ATOM   720  C  C    . LYS   A 1 29  ? 18.242 -0.480  19.904  1.00 25.51 ?  29  LYS   A C    1 
ATOM   721  O  O    . LYS   A 1 29  ? 18.529 -0.700  21.087  1.00 26.25 ?  29  LYS   A O    1 
ATOM   722  C  CB   . LYS   A 1 29  ? 15.991 0.348   19.182  1.00 29.32 ?  29  LYS   A CB   1 
ATOM   723  C  CG   . LYS   A 1 29  ? 15.234 -0.288  20.337  1.00 32.21 ?  29  LYS   A CG   1 
ATOM   724  C  CD   . LYS   A 1 29  ? 14.861 0.748   21.384  1.00 34.99 ?  29  LYS   A CD   1 
ATOM   725  C  CE   . LYS   A 1 29  ? 13.997 0.146   22.480  1.00 36.87 ?  29  LYS   A CE   1 
ATOM   726  N  NZ   . LYS   A 1 29  ? 13.559 1.175   23.463  1.00 37.97 ?  29  LYS   A NZ   1 
ATOM   727  H  H    . LYS   A 1 29  ? 17.632 1.285   17.624  1.00 29.83 ?  29  LYS   A H    1 
ATOM   728  H  HA   . LYS   A 1 29  ? 17.404 1.350   20.278  1.00 31.78 ?  29  LYS   A HA   1 
ATOM   729  H  HB2  . LYS   A 1 29  ? 15.499 1.139   18.913  1.00 35.23 ?  29  LYS   A HB2  1 
ATOM   730  H  HB3  . LYS   A 1 29  ? 16.006 -0.293  18.455  1.00 35.23 ?  29  LYS   A HB3  1 
ATOM   731  H  HG2  . LYS   A 1 29  ? 14.416 -0.689  20.002  1.00 38.69 ?  29  LYS   A HG2  1 
ATOM   732  H  HG3  . LYS   A 1 29  ? 15.787 -0.965  20.761  1.00 38.69 ?  29  LYS   A HG3  1 
ATOM   733  H  HD2  . LYS   A 1 29  ? 15.669 1.098   21.790  1.00 42.03 ?  29  LYS   A HD2  1 
ATOM   734  H  HD3  . LYS   A 1 29  ? 14.361 1.463   20.960  1.00 42.03 ?  29  LYS   A HD3  1 
ATOM   735  H  HE2  . LYS   A 1 29  ? 13.206 -0.250  22.082  1.00 44.29 ?  29  LYS   A HE2  1 
ATOM   736  H  HE3  . LYS   A 1 29  ? 14.507 -0.529  22.955  1.00 44.29 ?  29  LYS   A HE3  1 
ATOM   737  H  HZ1  . LYS   A 1 29  ? 13.055 0.798   24.093  1.00 45.60 ?  29  LYS   A HZ1  1 
ATOM   738  H  HZ2  . LYS   A 1 29  ? 14.268 1.552   23.846  1.00 45.60 ?  29  LYS   A HZ2  1 
ATOM   739  H  HZ3  . LYS   A 1 29  ? 13.083 1.805   23.052  1.00 45.60 ?  29  LYS   A HZ3  1 
ATOM   740  N  N    . VAL   A 1 30  ? 18.599 -1.305  18.920  1.00 24.23 ?  30  VAL   A N    1 
ATOM   741  C  CA   . VAL   A 1 30  ? 19.242 -2.584  19.202  1.00 23.36 ?  30  VAL   A CA   1 
ATOM   742  C  C    . VAL   A 1 30  ? 20.748 -2.437  19.411  1.00 21.95 ?  30  VAL   A C    1 
ATOM   743  O  O    . VAL   A 1 30  ? 21.341 -3.171  20.210  1.00 22.32 ?  30  VAL   A O    1 
ATOM   744  C  CB   . VAL   A 1 30  ? 18.921 -3.573  18.067  1.00 24.11 ?  30  VAL   A CB   1 
ATOM   745  C  CG1  . VAL   A 1 30  ? 19.677 -4.882  18.254  1.00 24.51 ?  30  VAL   A CG1  1 
ATOM   746  C  CG2  . VAL   A 1 30  ? 17.418 -3.822  17.988  1.00 24.75 ?  30  VAL   A CG2  1 
ATOM   747  H  H    . VAL   A 1 30  ? 18.460 -1.157  18.083  1.00 29.11 ?  30  VAL   A H    1 
ATOM   748  H  HA   . VAL   A 1 30  ? 18.862 -2.949  20.015  1.00 28.07 ?  30  VAL   A HA   1 
ATOM   749  H  HB   . VAL   A 1 30  ? 19.202 -3.189  17.222  1.00 28.97 ?  30  VAL   A HB   1 
ATOM   750  H  HG11 . VAL   A 1 30  ? 19.291 -5.554  17.669  1.00 29.45 ?  30  VAL   A HG11 1 
ATOM   751  H  HG12 . VAL   A 1 30  ? 20.609 -4.746  18.030  1.00 29.45 ?  30  VAL   A HG12 1 
ATOM   752  H  HG13 . VAL   A 1 30  ? 19.592 -5.164  19.178  1.00 29.45 ?  30  VAL   A HG13 1 
ATOM   753  H  HG21 . VAL   A 1 30  ? 17.244 -4.489  17.304  1.00 29.74 ?  30  VAL   A HG21 1 
ATOM   754  H  HG22 . VAL   A 1 30  ? 17.107 -4.142  18.848  1.00 29.74 ?  30  VAL   A HG22 1 
ATOM   755  H  HG23 . VAL   A 1 30  ? 16.973 -2.992  17.761  1.00 29.74 ?  30  VAL   A HG23 1 
ATOM   756  N  N    . LYS   A 1 31  ? 21.388 -1.500  18.719  1.00 20.49 ?  31  LYS   A N    1 
ATOM   757  C  CA   . LYS   A 1 31  ? 22.843 -1.411  18.658  1.00 21.06 ?  31  LYS   A CA   1 
ATOM   758  C  C    . LYS   A 1 31  ? 23.437 -2.772  18.288  1.00 19.18 ?  31  LYS   A C    1 
ATOM   759  O  O    . LYS   A 1 31  ? 24.225 -3.343  19.048  1.00 19.79 ?  31  LYS   A O    1 
ATOM   760  C  CB   . LYS   A 1 31  ? 23.439 -0.889  19.960  1.00 25.66 ?  31  LYS   A CB   1 
ATOM   761  C  CG   . LYS   A 1 31  ? 22.765 0.371   20.481  1.00 31.34 ?  31  LYS   A CG   1 
ATOM   762  C  CD   . LYS   A 1 31  ? 23.776 1.455   20.825  1.00 35.76 ?  31  LYS   A CD   1 
ATOM   763  C  CE   . LYS   A 1 31  ? 23.158 2.527   21.714  1.00 38.72 ?  31  LYS   A CE   1 
ATOM   764  N  NZ   . LYS   A 1 31  ? 21.956 3.163   21.106  1.00 40.40 ?  31  LYS   A NZ   1 
ATOM   765  H  H    . LYS   A 1 31  ? 20.991 -0.884  18.270  1.00 24.63 ?  31  LYS   A H    1 
ATOM   766  H  HA   . LYS   A 1 31  ? 23.081 -0.788  17.960  1.00 25.30 ?  31  LYS   A HA   1 
ATOM   767  H  HB2  . LYS   A 1 31  ? 23.360 -1.576  20.637  1.00 30.83 ?  31  LYS   A HB2  1 
ATOM   768  H  HB3  . LYS   A 1 31  ? 24.377 -0.685  19.808  1.00 30.83 ?  31  LYS   A HB3  1 
ATOM   769  H  HG2  . LYS   A 1 31  ? 22.169 0.720   19.799  1.00 37.65 ?  31  LYS   A HG2  1 
ATOM   770  H  HG3  . LYS   A 1 31  ? 22.266 0.156   21.284  1.00 37.65 ?  31  LYS   A HG3  1 
ATOM   771  H  HD2  . LYS   A 1 31  ? 24.524 1.060   21.300  1.00 42.95 ?  31  LYS   A HD2  1 
ATOM   772  H  HD3  . LYS   A 1 31  ? 24.084 1.879   20.007  1.00 42.95 ?  31  LYS   A HD3  1 
ATOM   773  H  HE2  . LYS   A 1 31  ? 22.891 2.123   22.554  1.00 46.50 ?  31  LYS   A HE2  1 
ATOM   774  H  HE3  . LYS   A 1 31  ? 23.815 3.222   21.875  1.00 46.50 ?  31  LYS   A HE3  1 
ATOM   775  H  HZ1  . LYS   A 1 31  ? 21.633 3.788   21.652  1.00 48.52 ?  31  LYS   A HZ1  1 
ATOM   776  H  HZ2  . LYS   A 1 31  ? 22.171 3.541   20.330  1.00 48.52 ?  31  LYS   A HZ2  1 
ATOM   777  H  HZ3  . LYS   A 1 31  ? 21.326 2.550   20.964  1.00 48.52 ?  31  LYS   A HZ3  1 
ATOM   778  N  N    . PRO   A 1 32  ? 23.071 -3.314  17.132  1.00 17.09 ?  32  PRO   A N    1 
ATOM   779  C  CA   . PRO   A 1 32  ? 23.546 -4.645  16.758  1.00 17.04 ?  32  PRO   A CA   1 
ATOM   780  C  C    . PRO   A 1 32  ? 25.047 -4.649  16.542  1.00 16.90 ?  32  PRO   A C    1 
ATOM   781  O  O    . PRO   A 1 32  ? 25.681 -3.613  16.332  1.00 16.65 ?  32  PRO   A O    1 
ATOM   782  C  CB   . PRO   A 1 32  ? 22.808 -4.919  15.445  1.00 17.36 ?  32  PRO   A CB   1 
ATOM   783  C  CG   . PRO   A 1 32  ? 22.606 -3.550  14.860  1.00 16.72 ?  32  PRO   A CG   1 
ATOM   784  C  CD   . PRO   A 1 32  ? 22.310 -2.680  16.043  1.00 16.50 ?  32  PRO   A CD   1 
ATOM   785  H  HA   . PRO   A 1 32  ? 23.305 -5.308  17.421  1.00 20.48 ?  32  PRO   A HA   1 
ATOM   786  H  HB2  . PRO   A 1 32  ? 23.357 -5.471  14.861  1.00 20.87 ?  32  PRO   A HB2  1 
ATOM   787  H  HB3  . PRO   A 1 32  ? 21.958 -5.353  15.627  1.00 20.87 ?  32  PRO   A HB3  1 
ATOM   788  H  HG2  . PRO   A 1 32  ? 23.413 -3.271  14.407  1.00 20.10 ?  32  PRO   A HG2  1 
ATOM   789  H  HG3  . PRO   A 1 32  ? 21.853 -3.573  14.246  1.00 20.10 ?  32  PRO   A HG3  1 
ATOM   790  H  HD2  . PRO   A 1 32  ? 22.633 -1.782  15.876  1.00 19.84 ?  32  PRO   A HD2  1 
ATOM   791  H  HD3  . PRO   A 1 32  ? 21.363 -2.693  16.239  1.00 19.84 ?  32  PRO   A HD3  1 
ATOM   792  N  N    . THR   A 1 33  ? 25.615 -5.854  16.587  1.00 16.92 ?  33  THR   A N    1 
ATOM   793  C  CA   . THR   A 1 33  ? 27.025 -6.010  16.260  1.00 16.96 ?  33  THR   A CA   1 
ATOM   794  C  C    . THR   A 1 33  ? 27.305 -5.550  14.837  1.00 15.26 ?  33  THR   A C    1 
ATOM   795  O  O    . THR   A 1 33  ? 28.330 -4.900  14.578  1.00 15.69 ?  33  THR   A O    1 
ATOM   796  C  CB   . THR   A 1 33  ? 27.434 -7.469  16.459  1.00 18.82 ?  33  THR   A CB   1 
ATOM   797  O  OG1  . THR   A 1 33  ? 27.126 -7.864  17.800  1.00 20.51 ?  33  THR   A OG1  1 
ATOM   798  C  CG2  . THR   A 1 33  ? 28.924 -7.659  16.211  1.00 19.59 ?  33  THR   A CG2  1 
ATOM   799  H  H    . THR   A 1 33  ? 25.213 -6.587  16.796  1.00 20.34 ?  33  THR   A H    1 
ATOM   800  H  HA   . THR   A 1 33  ? 27.557 -5.470  16.860  1.00 20.39 ?  33  THR   A HA   1 
ATOM   801  H  HB   . THR   A 1 33  ? 26.949 -8.039  15.839  1.00 22.62 ?  33  THR   A HB   1 
ATOM   802  H  HG1  . THR   A 1 33  ? 27.547 -7.381  18.347  1.00 24.66 ?  33  THR   A HG1  1 
ATOM   803  H  HG21 . THR   A 1 33  ? 29.198 -8.549  16.487  1.00 23.54 ?  33  THR   A HG21 1 
ATOM   804  H  HG22 . THR   A 1 33  ? 29.123 -7.548  15.269  1.00 23.54 ?  33  THR   A HG22 1 
ATOM   805  H  HG23 . THR   A 1 33  ? 29.429 -7.006  16.721  1.00 23.54 ?  33  THR   A HG23 1 
ATOM   806  N  N    . VAL   A 1 34  ? 26.401 -5.862  13.905  1.00 13.78 ?  34  VAL   A N    1 
ATOM   807  C  CA   . VAL   A 1 34  ? 26.571 -5.517  12.498  1.00 12.97 ?  34  VAL   A CA   1 
ATOM   808  C  C    . VAL   A 1 34  ? 25.267 -4.952  11.947  1.00 12.53 ?  34  VAL   A C    1 
ATOM   809  O  O    . VAL   A 1 34  ? 24.225 -5.619  11.999  1.00 13.13 ?  34  VAL   A O    1 
ATOM   810  C  CB   . VAL   A 1 34  ? 27.012 -6.717  11.639  1.00 13.35 ?  34  VAL   A CB   1 
ATOM   811  C  CG1  . VAL   A 1 34  ? 27.171 -6.289  10.185  1.00 13.70 ?  34  VAL   A CG1  1 
ATOM   812  C  CG2  . VAL   A 1 34  ? 28.303 -7.328  12.170  1.00 14.59 ?  34  VAL   A CG2  1 
ATOM   813  H  H    . VAL   A 1 34  ? 25.666 -6.281  14.069  1.00 16.57 ?  34  VAL   A H    1 
ATOM   814  H  HA   . VAL   A 1 34  ? 27.249 -4.827  12.418  1.00 15.60 ?  34  VAL   A HA   1 
ATOM   815  H  HB   . VAL   A 1 34  ? 26.321 -7.397  11.674  1.00 16.06 ?  34  VAL   A HB   1 
ATOM   816  H  HG11 . VAL   A 1 34  ? 27.677 -6.967  9.713   1.00 16.48 ?  34  VAL   A HG11 1 
ATOM   817  H  HG12 . VAL   A 1 34  ? 26.295 -6.188  9.783   1.00 16.48 ?  34  VAL   A HG12 1 
ATOM   818  H  HG13 . VAL   A 1 34  ? 27.649 -5.443  10.157  1.00 16.48 ?  34  VAL   A HG13 1 
ATOM   819  H  HG21 . VAL   A 1 34  ? 28.567 -8.063  11.591  1.00 17.54 ?  34  VAL   A HG21 1 
ATOM   820  H  HG22 . VAL   A 1 34  ? 28.997 -6.650  12.177  1.00 17.54 ?  34  VAL   A HG22 1 
ATOM   821  H  HG23 . VAL   A 1 34  ? 28.153 -7.658  13.070  1.00 17.54 ?  34  VAL   A HG23 1 
ATOM   822  N  N    . VAL   A 1 35  ? 25.329 -3.735  11.401  1.00 11.56 ?  35  VAL   A N    1 
ATOM   823  C  CA   . VAL   A 1 35  ? 24.291 -3.214  10.520  1.00 11.20 ?  35  VAL   A CA   1 
ATOM   824  C  C    . VAL   A 1 35  ? 24.836 -3.211  9.099   1.00 10.87 ?  35  VAL   A C    1 
ATOM   825  O  O    . VAL   A 1 35  ? 25.980 -2.803  8.862   1.00 11.40 ?  35  VAL   A O    1 
ATOM   826  C  CB   . VAL   A 1 35  ? 23.768 -1.820  10.937  1.00 11.83 ?  35  VAL   A CB   1 
ATOM   827  C  CG1  . VAL   A 1 35  ? 24.845 -0.733  10.801  1.00 12.34 ?  35  VAL   A CG1  1 
ATOM   828  C  CG2  . VAL   A 1 35  ? 22.520 -1.460  10.124  1.00 12.40 ?  35  VAL   A CG2  1 
ATOM   829  H  H    . VAL   A 1 35  ? 25.976 -3.185  11.523  1.00 13.91 ?  35  VAL   A H    1 
ATOM   830  H  HA   . VAL   A 1 35  ? 23.532 -3.821  10.540  1.00 13.47 ?  35  VAL   A HA   1 
ATOM   831  H  HB   . VAL   A 1 35  ? 23.502 -1.853  11.865  1.00 14.24 ?  35  VAL   A HB   1 
ATOM   832  H  HG11 . VAL   A 1 35  ? 24.511 0.100   11.177  1.00 14.84 ?  35  VAL   A HG11 1 
ATOM   833  H  HG12 . VAL   A 1 35  ? 25.642 -1.011  11.282  1.00 14.84 ?  35  VAL   A HG12 1 
ATOM   834  H  HG13 . VAL   A 1 35  ? 25.060 -0.601  9.862   1.00 14.84 ?  35  VAL   A HG13 1 
ATOM   835  H  HG21 . VAL   A 1 35  ? 22.171 -0.613  10.435  1.00 14.91 ?  35  VAL   A HG21 1 
ATOM   836  H  HG22 . VAL   A 1 35  ? 22.762 -1.392  9.183   1.00 14.91 ?  35  VAL   A HG22 1 
ATOM   837  H  HG23 . VAL   A 1 35  ? 21.855 -2.157  10.240  1.00 14.91 ?  35  VAL   A HG23 1 
ATOM   838  N  N    . VAL   A 1 36  ? 24.016 -3.659  8.152   1.00 10.18 ?  36  VAL   A N    1 
ATOM   839  C  CA   . VAL   A 1 36  ? 24.388 -3.666  6.743   1.00 10.13 ?  36  VAL   A CA   1 
ATOM   840  C  C    . VAL   A 1 36  ? 23.922 -2.375  6.091   1.00 10.35 ?  36  VAL   A C    1 
ATOM   841  O  O    . VAL   A 1 36  ? 22.763 -1.968  6.243   1.00 10.95 ?  36  VAL   A O    1 
ATOM   842  C  CB   . VAL   A 1 36  ? 23.776 -4.877  6.024   1.00 10.19 ?  36  VAL   A CB   1 
ATOM   843  C  CG1  . VAL   A 1 36  ? 24.038 -4.800  4.539   1.00 11.03 ?  36  VAL   A CG1  1 
ATOM   844  C  CG2  . VAL   A 1 36  ? 24.310 -6.179  6.600   1.00 11.02 ?  36  VAL   A CG2  1 
ATOM   845  H  H    . VAL   A 1 36  ? 23.223 -3.970  8.303   1.00 12.25 ?  36  VAL   A H    1 
ATOM   846  H  HA   . VAL   A 1 36  ? 25.357 -3.725  6.669   1.00 12.19 ?  36  VAL   A HA   1 
ATOM   847  H  HB   . VAL   A 1 36  ? 22.819 -4.866  6.158   1.00 12.26 ?  36  VAL   A HB   1 
ATOM   848  H  HG11 . VAL   A 1 36  ? 23.900 -5.677  4.146   1.00 13.27 ?  36  VAL   A HG11 1 
ATOM   849  H  HG12 . VAL   A 1 36  ? 23.423 -4.163  4.139   1.00 13.27 ?  36  VAL   A HG12 1 
ATOM   850  H  HG13 . VAL   A 1 36  ? 24.954 -4.514  4.390   1.00 13.27 ?  36  VAL   A HG13 1 
ATOM   851  H  HG21 . VAL   A 1 36  ? 23.912 -6.926  6.121   1.00 13.27 ?  36  VAL   A HG21 1 
ATOM   852  H  HG22 . VAL   A 1 36  ? 25.275 -6.203  6.502   1.00 13.27 ?  36  VAL   A HG22 1 
ATOM   853  H  HG23 . VAL   A 1 36  ? 24.073 -6.234  7.541   1.00 13.27 ?  36  VAL   A HG23 1 
ATOM   854  N  N    . ASN   A 1 37  ? 24.827 -1.749  5.339   1.00 9.94  ?  37  ASN   A N    1 
ATOM   855  C  CA   . ASN   A 1 37  ? 24.495 -0.625  4.479   1.00 9.66  ?  37  ASN   A CA   1 
ATOM   856  C  C    . ASN   A 1 37  ? 24.353 -1.078  3.036   1.00 9.73  ?  37  ASN   A C    1 
ATOM   857  O  O    . ASN   A 1 37  ? 25.129 -1.914  2.551   1.00 10.09 ?  37  ASN   A O    1 
ATOM   858  C  CB   . ASN   A 1 37  ? 25.576 0.453   4.559   1.00 10.05 ?  37  ASN   A CB   1 
ATOM   859  C  CG   . ASN   A 1 37  ? 25.251 1.658   3.709   1.00 10.37 ?  37  ASN   A CG   1 
ATOM   860  O  OD1  . ASN   A 1 37  ? 24.078 2.001   3.541   1.00 10.89 ?  37  ASN   A OD1  1 
ATOM   861  N  ND2  . ASN   A 1 37  ? 26.280 2.318   3.186   1.00 10.49 ?  37  ASN   A ND2  1 
ATOM   862  H  H    . ASN   A 1 37  ? 25.667 -1.964  5.320   1.00 11.97 ?  37  ASN   A H    1 
ATOM   863  H  HA   . ASN   A 1 37  ? 23.660 -0.238  4.771   1.00 11.63 ?  37  ASN   A HA   1 
ATOM   864  H  HB2  . ASN   A 1 37  ? 25.665 0.749   5.481   1.00 12.10 ?  37  ASN   A HB2  1 
ATOM   865  H  HB3  . ASN   A 1 37  ? 26.423 0.083   4.252   1.00 12.10 ?  37  ASN   A HB3  1 
ATOM   866  H  HD21 . ASN   A 1 37  ? 26.139 3.006   2.693   1.00 12.62 ?  37  ASN   A HD21 1 
ATOM   867  H  HD22 . ASN   A 1 37  ? 27.080 2.050   3.324   1.00 12.62 ?  37  ASN   A HD22 1 
ATOM   868  N  N    A ALA   A 1 38  ? 23.337 -0.525  2.370   0.82 10.28 ?  38  ALA   A N    1 
ATOM   869  N  N    B ALA   A 1 38  ? 23.356 -0.517  2.347   0.18 9.91  ?  38  ALA   A N    1 
ATOM   870  C  CA   A ALA   A 1 38  ? 23.131 -0.661  0.930   0.82 10.57 ?  38  ALA   A CA   1 
ATOM   871  C  CA   B ALA   A 1 38  ? 23.163 -0.754  0.914   0.18 10.24 ?  38  ALA   A CA   1 
ATOM   872  C  C    A ALA   A 1 38  ? 24.056 0.325   0.221   0.82 10.46 ?  38  ALA   A C    1 
ATOM   873  C  C    B ALA   A 1 38  ? 24.030 0.245   0.148   0.18 10.14 ?  38  ALA   A C    1 
ATOM   874  O  O    A ALA   A 1 38  ? 23.661 1.422   -0.189  0.82 10.45 ?  38  ALA   A O    1 
ATOM   875  O  O    B ALA   A 1 38  ? 23.569 1.262   -0.377  0.18 9.92  ?  38  ALA   A O    1 
ATOM   876  C  CB   A ALA   A 1 38  ? 21.671 -0.390  0.586   0.82 11.83 ?  38  ALA   A CB   1 
ATOM   877  C  CB   B ALA   A 1 38  ? 21.689 -0.643  0.546   0.18 10.82 ?  38  ALA   A CB   1 
ATOM   878  H  H    A ALA   A 1 38  ? 22.741 -0.036  2.752   0.82 12.37 ?  38  ALA   A H    1 
ATOM   879  H  H    B ALA   A 1 38  ? 22.773 0.012   2.695   0.18 11.93 ?  38  ALA   A H    1 
ATOM   880  H  HA   A ALA   A 1 38  ? 23.358 -1.559  0.649   0.82 12.72 ?  38  ALA   A HA   1 
ATOM   881  H  HA   B ALA   A 1 38  ? 23.461 -1.654  0.700   0.18 12.33 ?  38  ALA   A HA   1 
ATOM   882  H  HB1  A ALA   A 1 38  ? 21.546 -0.488  -0.369  0.82 14.24 ?  38  ALA   A HB1  1 
ATOM   883  H  HB1  B ALA   A 1 38  ? 21.593 -0.787  -0.407  0.18 13.02 ?  38  ALA   A HB1  1 
ATOM   884  H  HB2  A ALA   A 1 38  ? 21.112 -1.032  1.059   0.82 14.24 ?  38  ALA   A HB2  1 
ATOM   885  H  HB2  B ALA   A 1 38  ? 21.185 -1.315  1.035   0.18 13.02 ?  38  ALA   A HB2  1 
ATOM   886  H  HB3  A ALA   A 1 38  ? 21.440 0.510   0.862   0.82 14.24 ?  38  ALA   A HB3  1 
ATOM   887  H  HB3  B ALA   A 1 38  ? 21.373 0.242   0.779   0.18 13.02 ?  38  ALA   A HB3  1 
ATOM   888  N  N    . ALA   A 1 39  ? 25.318 -0.076  0.084   1.00 10.49 ?  39  ALA   A N    1 
ATOM   889  C  CA   . ALA   A 1 39  ? 26.359 0.809   -0.410  1.00 10.58 ?  39  ALA   A CA   1 
ATOM   890  C  C    . ALA   A 1 39  ? 26.485 0.750   -1.928  1.00 10.36 ?  39  ALA   A C    1 
ATOM   891  O  O    . ALA   A 1 39  ? 26.008 -0.174  -2.587  1.00 10.77 ?  39  ALA   A O    1 
ATOM   892  C  CB   . ALA   A 1 39  ? 27.693 0.406   0.225   1.00 11.42 ?  39  ALA   A CB   1 
ATOM   893  H  H    A ALA   A 1 39  ? 25.593 -0.871  0.276   0.82 12.63 ?  39  ALA   A H    1 
ATOM   894  H  H    B ALA   A 1 39  ? 25.624 -0.841  0.341   0.18 12.63 ?  39  ALA   A H    1 
ATOM   895  H  HA   . ALA   A 1 39  ? 26.151 1.721   -0.151  1.00 12.73 ?  39  ALA   A HA   1 
ATOM   896  H  HB1  . ALA   A 1 39  ? 28.384 0.997   -0.104  1.00 13.75 ?  39  ALA   A HB1  1 
ATOM   897  H  HB2  . ALA   A 1 39  ? 27.615 0.491   1.192   1.00 13.75 ?  39  ALA   A HB2  1 
ATOM   898  H  HB3  . ALA   A 1 39  ? 27.889 -0.510  -0.012  1.00 13.75 ?  39  ALA   A HB3  1 
ATOM   899  N  N    A ASN   A 1 40  ? 27.173 1.755   -2.476  0.82 10.67 ?  40  ASN   A N    1 
ATOM   900  N  N    B ASN   A 1 40  ? 27.116 1.775   -2.486  0.18 10.41 ?  40  ASN   A N    1 
ATOM   901  C  CA   A ASN   A 1 40  ? 27.703 1.711   -3.833  0.82 10.95 ?  40  ASN   A CA   1 
ATOM   902  C  CA   B ASN   A 1 40  ? 27.556 1.750   -3.871  0.18 10.67 ?  40  ASN   A CA   1 
ATOM   903  C  C    A ASN   A 1 40  ? 29.229 1.610   -3.780  0.82 10.31 ?  40  ASN   A C    1 
ATOM   904  C  C    B ASN   A 1 40  ? 29.073 1.614   -3.906  0.18 10.55 ?  40  ASN   A C    1 
ATOM   905  O  O    A ASN   A 1 40  ? 29.838 1.719   -2.711  0.82 10.29 ?  40  ASN   A O    1 
ATOM   906  O  O    B ASN   A 1 40  ? 29.750 1.660   -2.876  0.18 10.68 ?  40  ASN   A O    1 
ATOM   907  C  CB   A ASN   A 1 40  ? 27.197 2.892   -4.682  0.82 11.85 ?  40  ASN   A CB   1 
ATOM   908  C  CB   B ASN   A 1 40  ? 27.094 3.000   -4.630  0.18 11.16 ?  40  ASN   A CB   1 
ATOM   909  C  CG   A ASN   A 1 40  ? 27.579 4.241   -4.115  0.82 12.50 ?  40  ASN   A CG   1 
ATOM   910  C  CG   B ASN   A 1 40  ? 27.463 4.284   -3.921  0.18 11.75 ?  40  ASN   A CG   1 
ATOM   911  O  OD1  A ASN   A 1 40  ? 28.755 4.491   -3.819  0.82 14.16 ?  40  ASN   A OD1  1 
ATOM   912  O  OD1  B ASN   A 1 40  ? 28.640 4.636   -3.819  0.18 12.49 ?  40  ASN   A OD1  1 
ATOM   913  N  ND2  A ASN   A 1 40  ? 26.586 5.127   -3.972  0.82 12.79 ?  40  ASN   A ND2  1 
ATOM   914  N  ND2  B ASN   A 1 40  ? 26.454 5.000   -3.438  0.18 11.78 ?  40  ASN   A ND2  1 
ATOM   915  H  H    A ASN   A 1 40  ? 27.358 2.483   -2.064  0.82 12.84 ?  40  ASN   A H    1 
ATOM   916  H  H    B ASN   A 1 40  ? 27.301 2.505   -2.073  0.18 12.53 ?  40  ASN   A H    1 
ATOM   917  H  HA   A ASN   A 1 40  ? 27.385 0.900   -4.258  0.82 13.17 ?  40  ASN   A HA   1 
ATOM   918  H  HA   B ASN   A 1 40  ? 27.166 0.974   -4.311  0.18 12.84 ?  40  ASN   A HA   1 
ATOM   919  H  HB2  A ASN   A 1 40  ? 27.571 2.817   -5.577  0.82 14.26 ?  40  ASN   A HB2  1 
ATOM   920  H  HB2  B ASN   A 1 40  ? 27.512 3.007   -5.504  0.18 13.44 ?  40  ASN   A HB2  1 
ATOM   921  H  HB3  A ASN   A 1 40  ? 26.229 2.849   -4.729  0.82 14.26 ?  40  ASN   A HB3  1 
ATOM   922  H  HB3  B ASN   A 1 40  ? 26.130 2.968   -4.726  0.18 13.44 ?  40  ASN   A HB3  1 
ATOM   923  H  HD21 A ASN   A 1 40  ? 26.752 5.914   -3.660  0.82 15.38 ?  40  ASN   A HD21 1 
ATOM   924  H  HD21 B ASN   A 1 40  ? 26.610 5.739   -3.029  0.18 14.17 ?  40  ASN   A HD21 1 
ATOM   925  H  HD22 A ASN   A 1 40  ? 25.782 4.911   -4.182  0.82 15.38 ?  40  ASN   A HD22 1 
ATOM   926  H  HD22 B ASN   A 1 40  ? 25.643 4.725   -3.535  0.18 14.17 ?  40  ASN   A HD22 1 
ATOM   927  N  N    A VAL   A 1 41  ? 29.846 1.365   -4.941  0.82 10.84 ?  41  VAL   A N    1 
ATOM   928  N  N    B VAL   A 1 41  ? 29.608 1.437   -5.114  0.18 10.55 ?  41  VAL   A N    1 
ATOM   929  C  CA   A VAL   A 1 41  ? 31.278 1.062   -4.970  0.82 11.41 ?  41  VAL   A CA   1 
ATOM   930  C  CA   B VAL   A 1 41  ? 31.031 1.129   -5.241  0.18 10.71 ?  41  VAL   A CA   1 
ATOM   931  C  C    A VAL   A 1 41  ? 32.132 2.219   -4.492  0.82 11.36 ?  41  VAL   A C    1 
ATOM   932  C  C    B VAL   A 1 41  ? 31.907 2.255   -4.709  0.18 11.13 ?  41  VAL   A C    1 
ATOM   933  O  O    A VAL   A 1 41  ? 33.281 2.002   -4.085  0.82 11.85 ?  41  VAL   A O    1 
ATOM   934  O  O    B VAL   A 1 41  ? 33.039 2.009   -4.272  0.18 11.13 ?  41  VAL   A O    1 
ATOM   935  C  CB   A VAL   A 1 41  ? 31.763 0.569   -6.353  0.82 11.93 ?  41  VAL   A CB   1 
ATOM   936  C  CB   B VAL   A 1 41  ? 31.394 0.752   -6.690  0.18 10.68 ?  41  VAL   A CB   1 
ATOM   937  C  CG1  A VAL   A 1 41  ? 31.072 -0.729  -6.727  0.82 12.89 ?  41  VAL   A CG1  1 
ATOM   938  C  CG1  B VAL   A 1 41  ? 30.790 -0.594  -7.049  0.18 11.18 ?  41  VAL   A CG1  1 
ATOM   939  C  CG2  A VAL   A 1 41  ? 31.595 1.637   -7.437  0.82 12.12 ?  41  VAL   A CG2  1 
ATOM   940  C  CG2  B VAL   A 1 41  ? 30.944 1.835   -7.658  0.18 10.71 ?  41  VAL   A CG2  1 
ATOM   941  H  H    A VAL   A 1 41  ? 29.466 1.361   -5.712  0.82 13.05 ?  41  VAL   A H    1 
ATOM   942  H  H    B VAL   A 1 41  ? 29.170 1.481   -5.854  0.18 12.70 ?  41  VAL   A H    1 
ATOM   943  H  HA   A VAL   A 1 41  ? 31.439 0.334   -4.352  0.82 13.73 ?  41  VAL   A HA   1 
ATOM   944  H  HA   B VAL   A 1 41  ? 31.209 0.351   -4.693  0.18 12.90 ?  41  VAL   A HA   1 
ATOM   945  H  HB   A VAL   A 1 41  ? 32.713 0.372   -6.292  0.82 14.35 ?  41  VAL   A HB   1 
ATOM   946  H  HB   B VAL   A 1 41  ? 32.358 0.672   -6.754  0.18 12.85 ?  41  VAL   A HB   1 
ATOM   947  H  HG11 A VAL   A 1 41  ? 31.410 -1.039  -7.582  0.82 15.51 ?  41  VAL   A HG11 1 
ATOM   948  H  HG11 B VAL   A 1 41  ? 31.001 -0.796  -7.972  0.18 13.46 ?  41  VAL   A HG11 1 
ATOM   949  H  HG12 A VAL   A 1 41  ? 31.249 -1.394  -6.041  0.82 15.51 ?  41  VAL   A HG12 1 
ATOM   950  H  HG12 B VAL   A 1 41  ? 31.168 -1.275  -6.467  0.18 13.46 ?  41  VAL   A HG12 1 
ATOM   951  H  HG13 A VAL   A 1 41  ? 30.115 -0.571  -6.790  0.82 15.51 ?  41  VAL   A HG13 1 
ATOM   952  H  HG13 B VAL   A 1 41  ? 29.830 -0.554  -6.928  0.18 13.46 ?  41  VAL   A HG13 1 
ATOM   953  H  HG21 A VAL   A 1 41  ? 31.840 1.256   -8.299  0.82 14.59 ?  41  VAL   A HG21 1 
ATOM   954  H  HG21 B VAL   A 1 41  ? 31.309 1.640   -8.533  0.18 12.89 ?  41  VAL   A HG21 1 
ATOM   955  H  HG22 A VAL   A 1 41  ? 30.674 1.929   -7.455  0.82 14.59 ?  41  VAL   A HG22 1 
ATOM   956  H  HG22 B VAL   A 1 41  ? 29.976 1.847   -7.699  0.18 12.89 ?  41  VAL   A HG22 1 
ATOM   957  H  HG23 A VAL   A 1 41  ? 32.180 2.387   -7.236  0.82 14.59 ?  41  VAL   A HG23 1 
ATOM   958  H  HG23 B VAL   A 1 41  ? 31.274 2.691   -7.346  0.18 12.89 ?  41  VAL   A HG23 1 
ATOM   959  N  N    A TYR   A 1 42  ? 31.617 3.447   -4.563  0.82 11.07 ?  42  TYR   A N    1 
ATOM   960  N  N    B TYR   A 1 42  ? 31.425 3.498   -4.742  0.18 11.42 ?  42  TYR   A N    1 
ATOM   961  C  CA   A TYR   A 1 42  ? 32.350 4.637   -4.152  0.82 11.31 ?  42  TYR   A CA   1 
ATOM   962  C  CA   B TYR   A 1 42  ? 32.220 4.635   -4.287  0.18 11.93 ?  42  TYR   A CA   1 
ATOM   963  C  C    A TYR   A 1 42  ? 32.093 5.006   -2.703  0.82 11.06 ?  42  TYR   A C    1 
ATOM   964  C  C    B TYR   A 1 42  ? 31.943 5.025   -2.841  0.18 11.87 ?  42  TYR   A C    1 
ATOM   965  O  O    A TYR   A 1 42  ? 32.656 5.995   -2.217  0.82 11.63 ?  42  TYR   A O    1 
ATOM   966  O  O    B TYR   A 1 42  ? 32.533 5.994   -2.353  0.18 12.02 ?  42  TYR   A O    1 
ATOM   967  C  CB   A TYR   A 1 42  ? 31.999 5.826   -5.067  0.82 12.25 ?  42  TYR   A CB   1 
ATOM   968  C  CB   B TYR   A 1 42  ? 31.996 5.851   -5.192  0.18 12.56 ?  42  TYR   A CB   1 
ATOM   969  C  CG   A TYR   A 1 42  ? 32.181 5.512   -6.537  0.82 13.14 ?  42  TYR   A CG   1 
ATOM   970  C  CG   B TYR   A 1 42  ? 32.164 5.561   -6.662  0.18 13.11 ?  42  TYR   A CG   1 
ATOM   971  C  CD1  A TYR   A 1 42  ? 33.445 5.321   -7.076  0.82 13.97 ?  42  TYR   A CD1  1 
ATOM   972  C  CD1  B TYR   A 1 42  ? 33.423 5.363   -7.215  0.18 13.42 ?  42  TYR   A CD1  1 
ATOM   973  C  CD2  A TYR   A 1 42  ? 31.089 5.386   -7.386  0.82 14.36 ?  42  TYR   A CD2  1 
ATOM   974  C  CD2  B TYR   A 1 42  ? 31.063 5.491   -7.500  0.18 13.54 ?  42  TYR   A CD2  1 
ATOM   975  C  CE1  A TYR   A 1 42  ? 33.618 5.017   -8.417  0.82 14.58 ?  42  TYR   A CE1  1 
ATOM   976  C  CE1  B TYR   A 1 42  ? 33.575 5.097   -8.564  0.18 13.75 ?  42  TYR   A CE1  1 
ATOM   977  C  CE2  A TYR   A 1 42  ? 31.256 5.090   -8.732  0.82 15.35 ?  42  TYR   A CE2  1 
ATOM   978  C  CE2  B TYR   A 1 42  ? 31.204 5.229   -8.846  0.18 13.91 ?  42  TYR   A CE2  1 
ATOM   979  C  CZ   A TYR   A 1 42  ? 32.523 4.906   -9.240  0.82 15.41 ?  42  TYR   A CZ   1 
ATOM   980  C  CZ   B TYR   A 1 42  ? 32.461 5.032   -9.375  0.18 14.05 ?  42  TYR   A CZ   1 
ATOM   981  O  OH   A TYR   A 1 42  ? 32.684 4.604   -10.573 0.82 16.92 ?  42  TYR   A OH   1 
ATOM   982  O  OH   B TYR   A 1 42  ? 32.594 4.772   -10.719 0.18 14.54 ?  42  TYR   A OH   1 
ATOM   983  H  H    A TYR   A 1 42  ? 30.828 3.616   -4.859  0.82 13.32 ?  42  TYR   A H    1 
ATOM   984  H  H    B TYR   A 1 42  ? 30.637 3.710   -5.032  0.18 13.74 ?  42  TYR   A H    1 
ATOM   985  H  HA   A TYR   A 1 42  ? 33.300 4.470   -4.252  0.82 13.61 ?  42  TYR   A HA   1 
ATOM   986  H  HA   B TYR   A 1 42  ? 33.156 4.395   -4.353  0.18 14.36 ?  42  TYR   A HA   1 
ATOM   987  H  HB2  A TYR   A 1 42  ? 31.072 6.075   -4.927  0.82 14.74 ?  42  TYR   A HB2  1 
ATOM   988  H  HB2  B TYR   A 1 42  ? 31.096 6.181   -5.055  0.18 15.11 ?  42  TYR   A HB2  1 
ATOM   989  H  HB3  A TYR   A 1 42  ? 32.578 6.578   -4.849  0.82 14.74 ?  42  TYR   A HB3  1 
ATOM   990  H  HB3  B TYR   A 1 42  ? 32.639 6.538   -4.950  0.18 15.11 ?  42  TYR   A HB3  1 
ATOM   991  H  HD1  A TYR   A 1 42  ? 34.192 5.393   -6.527  0.82 16.80 ?  42  TYR   A HD1  1 
ATOM   992  H  HD1  B TYR   A 1 42  ? 34.176 5.405   -6.668  0.18 16.14 ?  42  TYR   A HD1  1 
ATOM   993  H  HD2  A TYR   A 1 42  ? 30.232 5.515   -7.049  0.82 17.27 ?  42  TYR   A HD2  1 
ATOM   994  H  HD2  B TYR   A 1 42  ? 30.213 5.624   -7.145  0.18 16.29 ?  42  TYR   A HD2  1 
ATOM   995  H  HE1  A TYR   A 1 42  ? 34.473 4.892   -8.763  0.82 17.53 ?  42  TYR   A HE1  1 
ATOM   996  H  HE1  B TYR   A 1 42  ? 34.423 4.964   -8.922  0.18 16.54 ?  42  TYR   A HE1  1 
ATOM   997  H  HE2  A TYR   A 1 42  ? 30.512 5.014   -9.290  0.82 18.46 ?  42  TYR   A HE2  1 
ATOM   998  H  HE2  B TYR   A 1 42  ? 30.454 5.184   -9.393  0.18 16.73 ?  42  TYR   A HE2  1 
ATOM   999  H  HH   A TYR   A 1 42  ? 33.501 4.512   -10.752 0.82 20.34 ?  42  TYR   A HH   1 
ATOM   1000 H  HH   B TYR   A 1 42  ? 33.405 4.666   -10.910 0.18 17.49 ?  42  TYR   A HH   1 
ATOM   1001 N  N    A LEU   A 1 43  ? 31.252 4.239   -2.012  0.82 10.65 ?  43  LEU   A N    1 
ATOM   1002 N  N    B LEU   A 1 43  ? 31.063 4.303   -2.150  0.18 11.96 ?  43  LEU   A N    1 
ATOM   1003 C  CA   A LEU   A 1 43  ? 30.800 4.576   -0.663  0.82 10.61 ?  43  LEU   A CA   1 
ATOM   1004 C  CA   B LEU   A 1 43  ? 30.689 4.621   -0.771  0.18 12.12 ?  43  LEU   A CA   1 
ATOM   1005 C  C    A LEU   A 1 43  ? 30.318 6.023   -0.572  0.82 10.45 ?  43  LEU   A C    1 
ATOM   1006 C  C    B LEU   A 1 43  ? 30.210 6.065   -0.633  0.18 12.55 ?  43  LEU   A C    1 
ATOM   1007 O  O    A LEU   A 1 43  ? 30.585 6.727   0.404   0.82 11.89 ?  43  LEU   A O    1 
ATOM   1008 O  O    B LEU   A 1 43  ? 30.480 6.740   0.363   0.18 12.65 ?  43  LEU   A O    1 
ATOM   1009 C  CB   A LEU   A 1 43  ? 31.851 4.262   0.400   0.82 10.97 ?  43  LEU   A CB   1 
ATOM   1010 C  CB   B LEU   A 1 43  ? 31.814 4.307   0.218   0.18 11.81 ?  43  LEU   A CB   1 
ATOM   1011 C  CG   A LEU   A 1 43  ? 32.347 2.815   0.484   0.82 11.33 ?  43  LEU   A CG   1 
ATOM   1012 C  CG   B LEU   A 1 43  ? 32.254 2.844   0.310   0.18 11.72 ?  43  LEU   A CG   1 
ATOM   1013 C  CD1  A LEU   A 1 43  ? 33.397 2.694   1.579   0.82 12.19 ?  43  LEU   A CD1  1 
ATOM   1014 C  CD1  B LEU   A 1 43  ? 33.368 2.695   1.334   0.18 11.70 ?  43  LEU   A CD1  1 
ATOM   1015 C  CD2  A LEU   A 1 43  ? 31.211 1.831   0.719   0.82 12.15 ?  43  LEU   A CD2  1 
ATOM   1016 C  CD2  B LEU   A 1 43  ? 31.079 1.938   0.654   0.18 11.83 ?  43  LEU   A CD2  1 
ATOM   1017 H  H    A LEU   A 1 43  ? 30.925 3.497   -2.307  0.82 12.82 ?  43  LEU   A H    1 
ATOM   1018 H  H    B LEU   A 1 43  ? 30.661 3.612   -2.462  0.18 14.39 ?  43  LEU   A H    1 
ATOM   1019 H  HA   A LEU   A 1 43  ? 30.035 4.010   -0.465  0.82 12.77 ?  43  LEU   A HA   1 
ATOM   1020 H  HA   B LEU   A 1 43  ? 29.940 4.058   -0.534  0.18 14.58 ?  43  LEU   A HA   1 
ATOM   1021 H  HB2  A LEU   A 1 43  ? 32.627 4.821   0.239   0.82 13.20 ?  43  LEU   A HB2  1 
ATOM   1022 H  HB2  B LEU   A 1 43  ? 32.593 4.827   -0.027  0.18 14.21 ?  43  LEU   A HB2  1 
ATOM   1023 H  HB3  A LEU   A 1 43  ? 31.475 4.479   1.269   0.82 13.20 ?  43  LEU   A HB3  1 
ATOM   1024 H  HB3  B LEU   A 1 43  ? 31.517 4.570   1.105   0.18 14.21 ?  43  LEU   A HB3  1 
ATOM   1025 H  HG   A LEU   A 1 43  ? 32.774 2.582   -0.357  0.82 13.63 ?  43  LEU   A HG   1 
ATOM   1026 H  HG   B LEU   A 1 43  ? 32.602 2.567   -0.551  0.18 14.11 ?  43  LEU   A HG   1 
ATOM   1027 H  HD11 A LEU   A 1 43  ? 33.706 1.774   1.623   0.82 14.66 ?  43  LEU   A HD11 1 
ATOM   1028 H  HD11 B LEU   A 1 43  ? 33.636 1.764   1.377   0.18 14.08 ?  43  LEU   A HD11 1 
ATOM   1029 H  HD12 A LEU   A 1 43  ? 34.140 3.282   1.374   0.82 14.66 ?  43  LEU   A HD12 1 
ATOM   1030 H  HD12 B LEU   A 1 43  ? 34.121 3.244   1.064   0.18 14.08 ?  43  LEU   A HD12 1 
ATOM   1031 H  HD13 A LEU   A 1 43  ? 32.999 2.947   2.428   0.82 14.66 ?  43  LEU   A HD13 1 
ATOM   1032 H  HD13 B LEU   A 1 43  ? 33.041 2.985   2.201   0.18 14.08 ?  43  LEU   A HD13 1 
ATOM   1033 H  HD21 A LEU   A 1 43  ? 31.585 0.946   0.855   0.82 14.61 ?  43  LEU   A HD21 1 
ATOM   1034 H  HD21 B LEU   A 1 43  ? 31.415 1.053   0.866   0.18 14.23 ?  43  LEU   A HD21 1 
ATOM   1035 H  HD22 A LEU   A 1 43  ? 30.715 2.106   1.504   0.82 14.61 ?  43  LEU   A HD22 1 
ATOM   1036 H  HD22 B LEU   A 1 43  ? 30.610 2.306   1.419   0.18 14.23 ?  43  LEU   A HD22 1 
ATOM   1037 H  HD23 A LEU   A 1 43  ? 30.632 1.829   -0.058  0.82 14.61 ?  43  LEU   A HD23 1 
ATOM   1038 H  HD23 B LEU   A 1 43  ? 30.483 1.892   -0.109  0.18 14.23 ?  43  LEU   A HD23 1 
ATOM   1039 N  N    A LYS   A 1 44  ? 29.586 6.462   -1.599  0.82 10.44 ?  44  LYS   A N    1 
ATOM   1040 N  N    B LYS   A 1 44  ? 29.483 6.541   -1.642  0.18 13.11 ?  44  LYS   A N    1 
ATOM   1041 C  CA   A LYS   A 1 44  ? 28.939 7.774   -1.601  0.82 11.24 ?  44  LYS   A CA   1 
ATOM   1042 C  CA   B LYS   A 1 44  ? 28.854 7.859   -1.597  0.18 13.96 ?  44  LYS   A CA   1 
ATOM   1043 C  C    A LYS   A 1 44  ? 27.513 7.584   -1.102  0.82 10.41 ?  44  LYS   A C    1 
ATOM   1044 C  C    B LYS   A 1 44  ? 27.447 7.683   -1.042  0.18 13.04 ?  44  LYS   A C    1 
ATOM   1045 O  O    A LYS   A 1 44  ? 26.646 7.075   -1.819  0.82 11.36 ?  44  LYS   A O    1 
ATOM   1046 O  O    B LYS   A 1 44  ? 26.525 7.291   -1.762  0.18 12.89 ?  44  LYS   A O    1 
ATOM   1047 C  CB   A LYS   A 1 44  ? 28.979 8.400   -2.989  0.82 13.73 ?  44  LYS   A CB   1 
ATOM   1048 C  CB   B LYS   A 1 44  ? 28.837 8.497   -2.982  0.18 15.82 ?  44  LYS   A CB   1 
ATOM   1049 C  CG   A LYS   A 1 44  ? 30.352 8.892   -3.415  0.82 17.11 ?  44  LYS   A CG   1 
ATOM   1050 C  CG   B LYS   A 1 44  ? 30.206 8.913   -3.496  0.18 17.65 ?  44  LYS   A CG   1 
ATOM   1051 C  CD   A LYS   A 1 44  ? 31.007 9.799   -2.373  0.82 22.63 ?  44  LYS   A CD   1 
ATOM   1052 C  CD   B LYS   A 1 44  ? 30.971 9.727   -2.460  0.18 19.65 ?  44  LYS   A CD   1 
ATOM   1053 C  CE   A LYS   A 1 44  ? 32.324 10.357  -2.881  0.82 25.77 ?  44  LYS   A CE   1 
ATOM   1054 C  CE   B LYS   A 1 44  ? 32.293 10.223  -3.008  0.18 20.84 ?  44  LYS   A CE   1 
ATOM   1055 N  NZ   A LYS   A 1 44  ? 33.182 10.877  -1.782  0.82 27.26 ?  44  LYS   A NZ   1 
ATOM   1056 N  NZ   B LYS   A 1 44  ? 33.157 10.792  -1.938  0.18 21.34 ?  44  LYS   A NZ   1 
ATOM   1057 H  H    A LYS   A 1 44  ? 29.447 6.004   -2.316  0.82 12.56 ?  44  LYS   A H    1 
ATOM   1058 H  H    B LYS   A 1 44  ? 29.336 6.113   -2.373  0.18 15.77 ?  44  LYS   A H    1 
ATOM   1059 H  HA   A LYS   A 1 44  ? 29.392 8.352   -0.970  0.82 13.52 ?  44  LYS   A HA   1 
ATOM   1060 H  HA   B LYS   A 1 44  ? 29.337 8.432   -0.982  0.18 16.79 ?  44  LYS   A HA   1 
ATOM   1061 H  HB2  A LYS   A 1 44  ? 28.689 7.741   -3.637  0.82 16.51 ?  44  LYS   A HB2  1 
ATOM   1062 H  HB2  B LYS   A 1 44  ? 28.467 7.860   -3.614  0.18 19.02 ?  44  LYS   A HB2  1 
ATOM   1063 H  HB3  A LYS   A 1 44  ? 28.378 9.161   -3.001  0.82 16.51 ?  44  LYS   A HB3  1 
ATOM   1064 H  HB3  B LYS   A 1 44  ? 28.281 9.291   -2.955  0.18 19.02 ?  44  LYS   A HB3  1 
ATOM   1065 H  HG2  A LYS   A 1 44  ? 30.934 8.130   -3.560  0.82 20.58 ?  44  LYS   A HG2  1 
ATOM   1066 H  HG2  B LYS   A 1 44  ? 30.724 8.120   -3.703  0.18 21.22 ?  44  LYS   A HG2  1 
ATOM   1067 H  HG3  A LYS   A 1 44  ? 30.265 9.403   -4.239  0.82 20.58 ?  44  LYS   A HG3  1 
ATOM   1068 H  HG3  B LYS   A 1 44  ? 30.097 9.460   -4.291  0.18 21.22 ?  44  LYS   A HG3  1 
ATOM   1069 H  HD2  A LYS   A 1 44  ? 30.409 10.534  -2.169  0.82 27.19 ?  44  LYS   A HD2  1 
ATOM   1070 H  HD2  B LYS   A 1 44  ? 30.433 10.491  -2.193  0.18 23.62 ?  44  LYS   A HD2  1 
ATOM   1071 H  HD3  A LYS   A 1 44  ? 31.192 9.281   -1.572  0.82 27.19 ?  44  LYS   A HD3  1 
ATOM   1072 H  HD3  B LYS   A 1 44  ? 31.166 9.168   -1.691  0.18 23.62 ?  44  LYS   A HD3  1 
ATOM   1073 H  HE2  A LYS   A 1 44  ? 32.812 9.650   -3.333  0.82 30.97 ?  44  LYS   A HE2  1 
ATOM   1074 H  HE2  B LYS   A 1 44  ? 32.766 9.481   -3.416  0.18 25.04 ?  44  LYS   A HE2  1 
ATOM   1075 H  HE3  A LYS   A 1 44  ? 32.143 11.082  -3.495  0.82 30.97 ?  44  LYS   A HE3  1 
ATOM   1076 H  HE3  B LYS   A 1 44  ? 32.125 10.916  -3.664  0.18 25.04 ?  44  LYS   A HE3  1 
ATOM   1077 H  HZ1  A LYS   A 1 44  ? 33.942 11.197  -2.117  0.82 32.75 ?  44  LYS   A HZ1  1 
ATOM   1078 H  HZ1  B LYS   A 1 44  ? 33.925 11.076  -2.287  0.18 25.65 ?  44  LYS   A HZ1  1 
ATOM   1079 H  HZ2  A LYS   A 1 44  ? 32.758 11.533  -1.352  0.82 32.75 ?  44  LYS   A HZ2  1 
ATOM   1080 H  HZ2  B LYS   A 1 44  ? 32.746 11.480  -1.549  0.18 25.65 ?  44  LYS   A HZ2  1 
ATOM   1081 H  HZ3  A LYS   A 1 44  ? 33.369 10.228  -1.205  0.82 32.75 ?  44  LYS   A HZ3  1 
ATOM   1082 H  HZ3  B LYS   A 1 44  ? 33.329 10.173  -1.323  0.18 25.65 ?  44  LYS   A HZ3  1 
ATOM   1083 N  N    A HIS   A 1 45  ? 27.280 7.971   0.146   0.82 10.25 ?  45  HIS   A N    1 
ATOM   1084 N  N    B HIS   A 1 45  ? 27.283 7.974   0.248   0.18 12.71 ?  45  HIS   A N    1 
ATOM   1085 C  CA   A HIS   A 1 45  ? 26.049 7.616   0.848   0.82 10.29 ?  45  HIS   A CA   1 
ATOM   1086 C  CA   B HIS   A 1 45  ? 26.007 7.772   0.932   0.18 12.49 ?  45  HIS   A CA   1 
ATOM   1087 C  C    A HIS   A 1 45  ? 25.013 8.733   0.691   0.82 10.84 ?  45  HIS   A C    1 
ATOM   1088 C  C    B HIS   A 1 45  ? 25.169 9.035   0.768   0.18 12.64 ?  45  HIS   A C    1 
ATOM   1089 O  O    A HIS   A 1 45  ? 24.688 9.465   1.625   0.82 11.89 ?  45  HIS   A O    1 
ATOM   1090 O  O    B HIS   A 1 45  ? 25.067 9.879   1.660   0.18 12.93 ?  45  HIS   A O    1 
ATOM   1091 C  CB   A HIS   A 1 45  ? 26.351 7.350   2.311   0.82 10.18 ?  45  HIS   A CB   1 
ATOM   1092 C  CB   B HIS   A 1 45  ? 26.240 7.436   2.397   0.18 12.13 ?  45  HIS   A CB   1 
ATOM   1093 C  CG   A HIS   A 1 45  ? 27.467 6.382   2.530   0.82 9.61  ?  45  HIS   A CG   1 
ATOM   1094 C  CG   B HIS   A 1 45  ? 27.382 6.498   2.625   0.18 11.54 ?  45  HIS   A CG   1 
ATOM   1095 N  ND1  A HIS   A 1 45  ? 27.452 5.095   2.028   0.82 10.22 ?  45  HIS   A ND1  1 
ATOM   1096 N  ND1  B HIS   A 1 45  ? 27.378 5.195   2.175   0.18 11.55 ?  45  HIS   A ND1  1 
ATOM   1097 C  CD2  A HIS   A 1 45  ? 28.642 6.527   3.188   0.82 10.34 ?  45  HIS   A CD2  1 
ATOM   1098 C  CD2  B HIS   A 1 45  ? 28.568 6.676   3.254   0.18 11.22 ?  45  HIS   A CD2  1 
ATOM   1099 C  CE1  A HIS   A 1 45  ? 28.578 4.495   2.376   0.82 10.21 ?  45  HIS   A CE1  1 
ATOM   1100 C  CE1  B HIS   A 1 45  ? 28.513 4.613   2.517   0.18 11.02 ?  45  HIS   A CE1  1 
ATOM   1101 N  NE2  A HIS   A 1 45  ? 29.312 5.336   3.086   0.82 10.43 ?  45  HIS   A NE2  1 
ATOM   1102 N  NE2  B HIS   A 1 45  ? 29.251 5.489   3.175   0.18 10.85 ?  45  HIS   A NE2  1 
ATOM   1103 H  H    A HIS   A 1 45  ? 27.822 8.442   0.618   0.82 12.34 ?  45  HIS   A H    1 
ATOM   1104 H  H    B HIS   A 1 45  ? 27.901 8.299   0.753   0.18 15.29 ?  45  HIS   A H    1 
ATOM   1105 H  HA   A HIS   A 1 45  ? 25.679 6.805   0.462   0.82 12.39 ?  45  HIS   A HA   1 
ATOM   1106 H  HA   B HIS   A 1 45  ? 25.537 7.032   0.518   0.18 15.02 ?  45  HIS   A HA   1 
ATOM   1107 H  HB2  A HIS   A 1 45  ? 26.586 8.184   2.742   0.82 12.25 ?  45  HIS   A HB2  1 
ATOM   1108 H  HB2  B HIS   A 1 45  ? 26.426 8.255   2.881   0.18 14.60 ?  45  HIS   A HB2  1 
ATOM   1109 H  HB3  A HIS   A 1 45  ? 25.552 6.980   2.733   0.82 12.25 ?  45  HIS   A HB3  1 
ATOM   1110 H  HB3  B HIS   A 1 45  ? 25.440 7.020   2.752   0.18 14.60 ?  45  HIS   A HB3  1 
ATOM   1111 H  HD2  A HIS   A 1 45  ? 28.942 7.292   3.630   0.82 12.44 ?  45  HIS   A HD2  1 
ATOM   1112 H  HD2  B HIS   A 1 45  ? 28.862 7.458   3.663   0.18 13.50 ?  45  HIS   A HD2  1 
ATOM   1113 H  HE1  A HIS   A 1 45  ? 28.810 3.615   2.174   0.82 12.29 ?  45  HIS   A HE1  1 
ATOM   1114 H  HE1  B HIS   A 1 45  ? 28.750 3.734   2.329   0.18 13.26 ?  45  HIS   A HE1  1 
ATOM   1115 H  HE2  A HIS   A 1 45  ? 30.089 5.165   3.419   0.82 12.55 ?  45  HIS   A HE2  1 
ATOM   1116 H  HE2  B HIS   A 1 45  ? 30.033 5.340   3.497   0.18 13.06 ?  45  HIS   A HE2  1 
ATOM   1117 N  N    A GLY   A 1 46  ? 24.476 8.836   -0.519  0.82 11.91 ?  46  GLY   A N    1 
ATOM   1118 N  N    B GLY   A 1 46  ? 24.562 9.165   -0.408  0.18 12.50 ?  46  GLY   A N    1 
ATOM   1119 C  CA   A GLY   A 1 46  ? 23.669 9.992   -0.869  0.82 12.54 ?  46  GLY   A CA   1 
ATOM   1120 C  CA   B GLY   A 1 46  ? 23.765 10.337  -0.708  0.18 12.17 ?  46  GLY   A CA   1 
ATOM   1121 C  C    A GLY   A 1 46  ? 22.184 9.879   -0.603  0.82 12.83 ?  46  GLY   A C    1 
ATOM   1122 C  C    B GLY   A 1 46  ? 22.298 10.174  -0.364  0.18 11.45 ?  46  GLY   A C    1 
ATOM   1123 O  O    A GLY   A 1 46  ? 21.525 10.883  -0.311  0.82 13.44 ?  46  GLY   A O    1 
ATOM   1124 O  O    B GLY   A 1 46  ? 21.649 11.131  0.071   0.18 11.40 ?  46  GLY   A O    1 
ATOM   1125 H  H    A GLY   A 1 46  ? 24.552 8.255   -1.145  0.82 14.33 ?  46  GLY   A H    1 
ATOM   1126 H  H    B GLY   A 1 46  ? 24.598 8.587   -1.045  0.18 15.04 ?  46  GLY   A H    1 
ATOM   1127 H  HA2  A GLY   A 1 46  ? 23.984 10.761  -0.371  0.82 15.08 ?  46  GLY   A HA2  1 
ATOM   1128 H  HA2  B GLY   A 1 46  ? 24.112 11.094  -0.208  0.18 14.64 ?  46  GLY   A HA2  1 
ATOM   1129 H  HA3  A GLY   A 1 46  ? 23.771 10.178  -1.809  0.82 15.08 ?  46  GLY   A HA3  1 
ATOM   1130 H  HA3  B GLY   A 1 46  ? 23.840 10.538  -1.652  0.18 14.64 ?  46  GLY   A HA3  1 
ATOM   1131 N  N    A GLY   A 1 47  ? 21.641 8.672   -0.718  0.82 12.60 ?  47  GLY   A N    1 
ATOM   1132 N  N    B GLY   A 1 47  ? 21.766 8.972   -0.551  0.18 11.50 ?  47  GLY   A N    1 
ATOM   1133 C  CA   A GLY   A 1 47  ? 20.205 8.489   -0.652  0.82 12.90 ?  47  GLY   A CA   1 
ATOM   1134 C  CA   B GLY   A 1 47  ? 20.363 8.723   -0.310  0.18 11.78 ?  47  GLY   A CA   1 
ATOM   1135 C  C    A GLY   A 1 47  ? 19.874 7.051   -0.320  0.82 12.20 ?  47  GLY   A C    1 
ATOM   1136 C  C    B GLY   A 1 47  ? 20.106 7.250   -0.072  0.18 11.55 ?  47  GLY   A C    1 
ATOM   1137 O  O    A GLY   A 1 47  ? 20.755 6.218   -0.094  0.82 12.41 ?  47  GLY   A O    1 
ATOM   1138 O  O    B GLY   A 1 47  ? 21.033 6.439   -0.004  0.18 11.68 ?  47  GLY   A O    1 
ATOM   1139 H  H    A GLY   A 1 47  ? 22.081 7.939   -0.815  0.82 15.16 ?  47  GLY   A H    1 
ATOM   1140 H  H    B GLY   A 1 47  ? 22.206 8.281   -0.811  0.18 13.84 ?  47  GLY   A H    1 
ATOM   1141 H  HA2  A GLY   A 1 47  ? 19.817 9.063   0.031   0.82 15.52 ?  47  GLY   A HA2  1 
ATOM   1142 H  HA2  B GLY   A 1 47  ? 20.065 9.225   0.469   0.18 14.17 ?  47  GLY   A HA2  1 
ATOM   1143 H  HA3  A GLY   A 1 47  ? 19.801 8.706   -1.506  0.82 15.52 ?  47  GLY   A HA3  1 
ATOM   1144 H  HA3  B GLY   A 1 47  ? 19.840 9.010   -1.078  0.18 14.17 ?  47  GLY   A HA3  1 
ATOM   1145 N  N    A GLY   A 1 48  ? 18.578 6.760   -0.316  0.82 12.40 ?  48  GLY   A N    1 
ATOM   1146 N  N    B GLY   A 1 48  ? 18.824 6.913   0.053   0.18 11.54 ?  48  GLY   A N    1 
ATOM   1147 C  CA   A GLY   A 1 48  ? 18.146 5.438   0.072   0.82 12.60 ?  48  GLY   A CA   1 
ATOM   1148 C  CA   B GLY   A 1 48  ? 18.440 5.540   0.319   0.18 11.59 ?  48  GLY   A CA   1 
ATOM   1149 C  C    A GLY   A 1 48  ? 18.585 5.120   1.488   0.82 11.71 ?  48  GLY   A C    1 
ATOM   1150 C  C    B GLY   A 1 48  ? 18.877 5.098   1.707   0.18 11.16 ?  48  GLY   A C    1 
ATOM   1151 O  O    A GLY   A 1 48  ? 18.732 6.004   2.344   0.82 11.99 ?  48  GLY   A O    1 
ATOM   1152 O  O    B GLY   A 1 48  ? 19.003 5.899   2.639   0.18 11.25 ?  48  GLY   A O    1 
ATOM   1153 H  H    A GLY   A 1 48  ? 17.937 7.302   -0.525  0.82 14.92 ?  48  GLY   A H    1 
ATOM   1154 H  H    B GLY   A 1 48  ? 18.169 7.461   -0.007  0.18 13.89 ?  48  GLY   A H    1 
ATOM   1155 H  HA2  A GLY   A 1 48  ? 17.180 5.367   0.022   0.82 15.16 ?  48  GLY   A HA2  1 
ATOM   1156 H  HA2  B GLY   A 1 48  ? 17.474 5.452   0.229   0.18 13.94 ?  48  GLY   A HA2  1 
ATOM   1157 H  HA3  A GLY   A 1 48  ? 18.535 4.775   -0.526  0.82 15.16 ?  48  GLY   A HA3  1 
ATOM   1158 H  HA3  B GLY   A 1 48  ? 18.860 4.950   -0.326  0.18 13.94 ?  48  GLY   A HA3  1 
ATOM   1159 N  N    A VAL   A 1 49  ? 18.802 3.828   1.741   0.82 11.25 ?  49  VAL   A N    1 
ATOM   1160 N  N    B VAL   A 1 49  ? 19.105 3.788   1.846   0.18 10.81 ?  49  VAL   A N    1 
ATOM   1161 C  CA   A VAL   A 1 49  ? 19.271 3.387   3.051   0.82 11.43 ?  49  VAL   A CA   1 
ATOM   1162 C  CA   B VAL   A 1 49  ? 19.636 3.259   3.099   0.18 10.26 ?  49  VAL   A CA   1 
ATOM   1163 C  C    A VAL   A 1 49  ? 20.592 4.061   3.414   0.82 10.35 ?  49  VAL   A C    1 
ATOM   1164 C  C    B VAL   A 1 49  ? 20.934 3.969   3.460   0.18 9.75  ?  49  VAL   A C    1 
ATOM   1165 O  O    A VAL   A 1 49  ? 20.789 4.490   4.557   0.82 10.41 ?  49  VAL   A O    1 
ATOM   1166 O  O    B VAL   A 1 49  ? 21.173 4.308   4.626   0.18 9.63  ?  49  VAL   A O    1 
ATOM   1167 C  CB   A VAL   A 1 49  ? 19.378 1.849   3.082   0.82 12.72 ?  49  VAL   A CB   1 
ATOM   1168 C  CB   B VAL   A 1 49  ? 19.840 1.735   2.998   0.18 9.81  ?  49  VAL   A CB   1 
ATOM   1169 C  CG1  A VAL   A 1 49  ? 20.136 1.381   4.318   0.82 13.42 ?  49  VAL   A CG1  1 
ATOM   1170 C  CG1  B VAL   A 1 49  ? 20.676 1.236   4.171   0.18 9.25  ?  49  VAL   A CG1  1 
ATOM   1171 C  CG2  A VAL   A 1 49  ? 17.988 1.215   3.032   0.82 14.66 ?  49  VAL   A CG2  1 
ATOM   1172 C  CG2  B VAL   A 1 49  ? 18.505 1.008   2.939   0.18 9.84  ?  49  VAL   A CG2  1 
ATOM   1173 H  H    A VAL   A 1 49  ? 18.687 3.186   1.178   0.82 13.54 ?  49  VAL   A H    1 
ATOM   1174 H  H    B VAL   A 1 49  ? 18.972 3.196   1.235   0.18 13.01 ?  49  VAL   A H    1 
ATOM   1175 H  HA   A VAL   A 1 49  ? 18.620 3.639   3.722   0.82 13.75 ?  49  VAL   A HA   1 
ATOM   1176 H  HA   B VAL   A 1 49  ? 18.998 3.425   3.810   0.18 12.34 ?  49  VAL   A HA   1 
ATOM   1177 H  HB   A VAL   A 1 49  ? 19.872 1.544   2.303   0.82 15.30 ?  49  VAL   A HB   1 
ATOM   1178 H  HB   B VAL   A 1 49  ? 20.322 1.536   2.181   0.18 11.81 ?  49  VAL   A HB   1 
ATOM   1179 H  HG11 A VAL   A 1 49  ? 19.953 0.438   4.463   0.82 16.15 ?  49  VAL   A HG11 1 
ATOM   1180 H  HG11 B VAL   A 1 49  ? 20.551 0.279   4.265   0.18 11.13 ?  49  VAL   A HG11 1 
ATOM   1181 H  HG12 A VAL   A 1 49  ? 21.084 1.516   4.183   0.82 16.15 ?  49  VAL   A HG12 1 
ATOM   1182 H  HG12 B VAL   A 1 49  ? 21.612 1.428   4.001   0.18 11.13 ?  49  VAL   A HG12 1 
ATOM   1183 H  HG13 A VAL   A 1 49  ? 19.829 1.893   5.085   0.82 16.15 ?  49  VAL   A HG13 1 
ATOM   1184 H  HG13 B VAL   A 1 49  ? 20.386 1.685   4.981   0.18 11.13 ?  49  VAL   A HG13 1 
ATOM   1185 H  HG21 A VAL   A 1 49  ? 18.080 0.249   3.049   0.82 17.63 ?  49  VAL   A HG21 1 
ATOM   1186 H  HG21 B VAL   A 1 49  ? 18.666 0.056   2.838   0.18 11.85 ?  49  VAL   A HG21 1 
ATOM   1187 H  HG22 A VAL   A 1 49  ? 17.482 1.514   3.803   0.82 17.63 ?  49  VAL   A HG22 1 
ATOM   1188 H  HG22 B VAL   A 1 49  ? 18.018 1.175   3.762   0.18 11.85 ?  49  VAL   A HG22 1 
ATOM   1189 H  HG23 A VAL   A 1 49  ? 17.549 1.493   2.215   0.82 17.63 ?  49  VAL   A HG23 1 
ATOM   1190 H  HG23 B VAL   A 1 49  ? 17.998 1.339   2.181   0.18 11.85 ?  49  VAL   A HG23 1 
ATOM   1191 N  N    A ALA   A 1 50  ? 21.530 4.124   2.465   0.82 10.11 ?  50  ALA   A N    1 
ATOM   1192 N  N    B ALA   A 1 50  ? 21.789 4.205   2.463   0.18 9.55  ?  50  ALA   A N    1 
ATOM   1193 C  CA   A ALA   A 1 50  ? 22.849 4.672   2.771   0.82 10.15 ?  50  ALA   A CA   1 
ATOM   1194 C  CA   B ALA   A 1 50  ? 23.100 4.789   2.727   0.18 9.55  ?  50  ALA   A CA   1 
ATOM   1195 C  C    A ALA   A 1 50  ? 22.758 6.129   3.190   0.82 10.19 ?  50  ALA   A C    1 
ATOM   1196 C  C    B ALA   A 1 50  ? 22.971 6.216   3.243   0.18 9.43  ?  50  ALA   A C    1 
ATOM   1197 O  O    A ALA   A 1 50  ? 23.407 6.550   4.158   0.82 10.68 ?  50  ALA   A O    1 
ATOM   1198 O  O    B ALA   A 1 50  ? 23.560 6.571   4.273   0.18 9.26  ?  50  ALA   A O    1 
ATOM   1199 C  CB   A ALA   A 1 50  ? 23.766 4.538   1.559   0.82 10.14 ?  50  ALA   A CB   1 
ATOM   1200 C  CB   B ALA   A 1 50  ? 23.958 4.733   1.461   0.18 9.63  ?  50  ALA   A CB   1 
ATOM   1201 H  H    A ALA   A 1 50  ? 21.428 3.866   1.649   0.82 12.17 ?  50  ALA   A H    1 
ATOM   1202 H  H    B ALA   A 1 50  ? 21.631 4.042   1.633   0.18 11.50 ?  50  ALA   A H    1 
ATOM   1203 H  HA   A ALA   A 1 50  ? 23.239 4.175   3.505   0.82 12.22 ?  50  ALA   A HA   1 
ATOM   1204 H  HA   B ALA   A 1 50  ? 23.545 4.270   3.409   0.18 11.50 ?  50  ALA   A HA   1 
ATOM   1205 H  HB1  A ALA   A 1 50  ? 24.635 4.909   1.781   0.82 12.21 ?  50  ALA   A HB1  1 
ATOM   1206 H  HB1  B ALA   A 1 50  ? 24.831 5.109   1.651   0.18 11.60 ?  50  ALA   A HB1  1 
ATOM   1207 H  HB2  A ALA   A 1 50  ? 23.853 3.601   1.332   0.82 12.21 ?  50  ALA   A HB2  1 
ATOM   1208 H  HB2  B ALA   A 1 50  ? 24.055 3.805   1.184   0.18 11.60 ?  50  ALA   A HB2  1 
ATOM   1209 H  HB3  A ALA   A 1 50  ? 23.379 5.027   0.816   0.82 12.21 ?  50  ALA   A HB3  1 
ATOM   1210 H  HB3  B ALA   A 1 50  ? 23.525 5.241   0.757   0.18 11.60 ?  50  ALA   A HB3  1 
ATOM   1211 N  N    A GLY   A 1 51  ? 21.975 6.923   2.463   0.82 10.24 ?  51  GLY   A N    1 
ATOM   1212 N  N    B GLY   A 1 51  ? 22.201 7.051   2.545   0.18 9.53  ?  51  GLY   A N    1 
ATOM   1213 C  CA   A GLY   A 1 51  ? 21.829 8.313   2.836   0.82 10.91 ?  51  GLY   A CA   1 
ATOM   1214 C  CA   B GLY   A 1 51  ? 22.011 8.412   3.009   0.18 9.53  ?  51  GLY   A CA   1 
ATOM   1215 C  C    A GLY   A 1 51  ? 21.244 8.469   4.222   0.82 10.92 ?  51  GLY   A C    1 
ATOM   1216 C  C    B GLY   A 1 51  ? 21.324 8.475   4.357   0.18 9.91  ?  51  GLY   A C    1 
ATOM   1217 O  O    A GLY   A 1 51  ? 21.648 9.353   4.980   0.82 11.48 ?  51  GLY   A O    1 
ATOM   1218 O  O    B GLY   A 1 51  ? 21.615 9.358   5.169   0.18 10.10 ?  51  GLY   A O    1 
ATOM   1219 H  H    A GLY   A 1 51  ? 21.533 6.682   1.768   0.82 12.32 ?  51  GLY   A H    1 
ATOM   1220 H  H    B GLY   A 1 51  ? 21.781 6.849   1.821   0.18 11.47 ?  51  GLY   A H    1 
ATOM   1221 H  HA2  A GLY   A 1 51  ? 22.697 8.748   2.821   0.82 13.13 ?  51  GLY   A HA2  1 
ATOM   1222 H  HA2  B GLY   A 1 51  ? 22.874 8.851   3.079   0.18 11.48 ?  51  GLY   A HA2  1 
ATOM   1223 H  HA3  A GLY   A 1 51  ? 21.247 8.762   2.204   0.82 13.13 ?  51  GLY   A HA3  1 
ATOM   1224 H  HA3  B GLY   A 1 51  ? 21.471 8.899   2.366   0.18 11.48 ?  51  GLY   A HA3  1 
ATOM   1225 N  N    A ALA   A 1 52  ? 20.270 7.619   4.565   0.82 11.02 ?  52  ALA   A N    1 
ATOM   1226 N  N    B ALA   A 1 52  ? 20.404 7.543   4.616   0.18 10.31 ?  52  ALA   A N    1 
ATOM   1227 C  CA   A ALA   A 1 52  ? 19.635 7.690   5.876   0.82 11.55 ?  52  ALA   A CA   1 
ATOM   1228 C  CA   B ALA   A 1 52  ? 19.724 7.503   5.906   0.18 10.50 ?  52  ALA   A CA   1 
ATOM   1229 C  C    A ALA   A 1 52  ? 20.591 7.266   6.988   0.82 10.74 ?  52  ALA   A C    1 
ATOM   1230 C  C    B ALA   A 1 52  ? 20.688 7.119   7.023   0.18 10.32 ?  52  ALA   A C    1 
ATOM   1231 O  O    A ALA   A 1 52  ? 20.676 7.924   8.030   0.82 11.97 ?  52  ALA   A O    1 
ATOM   1232 O  O    B ALA   A 1 52  ? 20.729 7.772   8.072   0.18 10.68 ?  52  ALA   A O    1 
ATOM   1233 C  CB   A ALA   A 1 52  ? 18.368 6.837   5.884   0.82 13.06 ?  52  ALA   A CB   1 
ATOM   1234 C  CB   B ALA   A 1 52  ? 18.546 6.530   5.842   0.18 10.90 ?  52  ALA   A CB   1 
ATOM   1235 H  H    A ALA   A 1 52  ? 19.977 6.984   4.060   0.82 13.26 ?  52  ALA   A H    1 
ATOM   1236 H  H    B ALA   A 1 52  ? 20.162 6.930   4.062   0.18 12.41 ?  52  ALA   A H    1 
ATOM   1237 H  HA   A ALA   A 1 52  ? 19.376 8.602   6.043   0.82 13.90 ?  52  ALA   A HA   1 
ATOM   1238 H  HA   B ALA   A 1 52  ? 19.372 8.382   6.102   0.18 12.63 ?  52  ALA   A HA   1 
ATOM   1239 H  HB1  A ALA   A 1 52  ? 17.953 6.896   6.761   0.82 15.71 ?  52  ALA   A HB1  1 
ATOM   1240 H  HB1  B ALA   A 1 52  ? 18.097 6.521   6.703   0.18 13.12 ?  52  ALA   A HB1  1 
ATOM   1241 H  HB2  A ALA   A 1 52  ? 17.757 7.170   5.208   0.82 15.71 ?  52  ALA   A HB2  1 
ATOM   1242 H  HB2  B ALA   A 1 52  ? 17.929 6.826   5.153   0.18 13.12 ?  52  ALA   A HB2  1 
ATOM   1243 H  HB3  A ALA   A 1 52  ? 18.601 5.914   5.692   0.82 15.71 ?  52  ALA   A HB3  1 
ATOM   1244 H  HB3  B ALA   A 1 52  ? 18.876 5.643   5.631   0.18 13.12 ?  52  ALA   A HB3  1 
ATOM   1245 N  N    A LEU   A 1 53  ? 21.305 6.151   6.802   0.82 10.63 ?  53  LEU   A N    1 
ATOM   1246 N  N    B LEU   A 1 53  ? 21.468 6.054   6.821   0.18 10.05 ?  53  LEU   A N    1 
ATOM   1247 C  CA   A LEU   A 1 53  ? 22.277 5.731   7.812   0.82 10.85 ?  53  LEU   A CA   1 
ATOM   1248 C  CA   B LEU   A 1 53  ? 22.465 5.675   7.820   0.18 9.69  ?  53  LEU   A CA   1 
ATOM   1249 C  C    A LEU   A 1 53  ? 23.338 6.802   8.012   0.82 10.32 ?  53  LEU   A C    1 
ATOM   1250 C  C    B LEU   A 1 53  ? 23.487 6.786   8.020   0.18 9.71  ?  53  LEU   A C    1 
ATOM   1251 O  O    A LEU   A 1 53  ? 23.668 7.165   9.148   0.82 11.58 ?  53  LEU   A O    1 
ATOM   1252 O  O    B LEU   A 1 53  ? 23.839 7.119   9.157   0.18 10.01 ?  53  LEU   A O    1 
ATOM   1253 C  CB   A LEU   A 1 53  ? 22.924 4.397   7.424   0.82 11.20 ?  53  LEU   A CB   1 
ATOM   1254 C  CB   B LEU   A 1 53  ? 23.171 4.381   7.407   0.18 9.35  ?  53  LEU   A CB   1 
ATOM   1255 C  CG   A LEU   A 1 53  ? 22.031 3.151   7.472   0.82 11.55 ?  53  LEU   A CG   1 
ATOM   1256 C  CG   B LEU   A 1 53  ? 22.415 3.052   7.503   0.18 9.09  ?  53  LEU   A CG   1 
ATOM   1257 C  CD1  A LEU   A 1 53  ? 22.758 1.944   6.889   0.82 11.82 ?  53  LEU   A CD1  1 
ATOM   1258 C  CD1  B LEU   A 1 53  ? 23.265 1.931   6.923   0.18 9.15  ?  53  LEU   A CD1  1 
ATOM   1259 C  CD2  A LEU   A 1 53  ? 21.551 2.851   8.886   0.82 13.21 ?  53  LEU   A CD2  1 
ATOM   1260 C  CD2  B LEU   A 1 53  ? 22.036 2.729   8.938   0.18 8.91  ?  53  LEU   A CD2  1 
ATOM   1261 H  H    A LEU   A 1 53  ? 21.250 5.631   6.115   0.82 12.80 ?  53  LEU   A H    1 
ATOM   1262 H  H    B LEU   A 1 53  ? 21.441 5.545   6.129   0.18 12.10 ?  53  LEU   A H    1 
ATOM   1263 H  HA   A LEU   A 1 53  ? 21.818 5.604   8.656   0.82 13.06 ?  53  LEU   A HA   1 
ATOM   1264 H  HA   B LEU   A 1 53  ? 22.020 5.516   8.667   0.18 11.67 ?  53  LEU   A HA   1 
ATOM   1265 H  HB2  A LEU   A 1 53  ? 23.259 4.472   6.517   0.82 13.48 ?  53  LEU   A HB2  1 
ATOM   1266 H  HB2  B LEU   A 1 53  ? 23.444 4.477   6.483   0.18 11.26 ?  53  LEU   A HB2  1 
ATOM   1267 H  HB3  A LEU   A 1 53  ? 23.669 4.233   8.025   0.82 13.48 ?  53  LEU   A HB3  1 
ATOM   1268 H  HB3  B LEU   A 1 53  ? 23.962 4.289   7.960   0.18 11.26 ?  53  LEU   A HB3  1 
ATOM   1269 H  HG   A LEU   A 1 53  ? 21.249 3.312   6.922   0.82 13.90 ?  53  LEU   A HG   1 
ATOM   1270 H  HG   B LEU   A 1 53  ? 21.601 3.109   6.981   0.18 10.95 ?  53  LEU   A HG   1 
ATOM   1271 H  HD11 A LEU   A 1 53  ? 22.169 1.173   6.932   0.82 14.23 ?  53  LEU   A HD11 1 
ATOM   1272 H  HD11 B LEU   A 1 53  ? 22.776 1.096   6.990   0.18 11.02 ?  53  LEU   A HD11 1 
ATOM   1273 H  HD12 A LEU   A 1 53  ? 22.993 2.130   5.968   0.82 14.23 ?  53  LEU   A HD12 1 
ATOM   1274 H  HD12 B LEU   A 1 53  ? 23.457 2.129   5.993   0.18 11.02 ?  53  LEU   A HD12 1 
ATOM   1275 H  HD13 A LEU   A 1 53  ? 23.559 1.776   7.410   0.82 14.23 ?  53  LEU   A HD13 1 
ATOM   1276 H  HD13 B LEU   A 1 53  ? 24.094 1.869   7.425   0.18 11.02 ?  53  LEU   A HD13 1 
ATOM   1277 H  HD21 A LEU   A 1 53  ? 21.040 2.026   8.878   0.82 15.89 ?  53  LEU   A HD21 1 
ATOM   1278 H  HD21 B LEU   A 1 53  ? 21.602 1.861   8.964   0.18 10.73 ?  53  LEU   A HD21 1 
ATOM   1279 H  HD22 A LEU   A 1 53  ? 22.320 2.757   9.469   0.82 15.89 ?  53  LEU   A HD22 1 
ATOM   1280 H  HD22 B LEU   A 1 53  ? 22.838 2.714   9.482   0.18 10.73 ?  53  LEU   A HD22 1 
ATOM   1281 H  HD23 A LEU   A 1 53  ? 20.991 3.581   9.193   0.82 15.89 ?  53  LEU   A HD23 1 
ATOM   1282 H  HD23 B LEU   A 1 53  ? 21.427 3.411   9.265   0.18 10.73 ?  53  LEU   A HD23 1 
ATOM   1283 N  N    A ASN   A 1 54  ? 23.869 7.339   6.916   0.82 10.03 ?  54  ASN   A N    1 
ATOM   1284 N  N    B ASN   A 1 54  ? 23.975 7.374   6.926   0.18 9.86  ?  54  ASN   A N    1 
ATOM   1285 C  CA   A ASN   A 1 54  ? 24.929 8.330   7.051   0.82 9.96  ?  54  ASN   A CA   1 
ATOM   1286 C  CA   B ASN   A 1 54  ? 25.000 8.407   7.045   0.18 9.97  ?  54  ASN   A CA   1 
ATOM   1287 C  C    A ASN   A 1 54  ? 24.430 9.577   7.780   0.82 10.80 ?  54  ASN   A C    1 
ATOM   1288 C  C    B ASN   A 1 54  ? 24.461 9.648   7.744   0.18 10.38 ?  54  ASN   A C    1 
ATOM   1289 O  O    A ASN   A 1 54  ? 25.120 10.120  8.651   0.82 11.05 ?  54  ASN   A O    1 
ATOM   1290 O  O    B ASN   A 1 54  ? 25.162 10.259  8.560   0.18 10.30 ?  54  ASN   A O    1 
ATOM   1291 C  CB   A ASN   A 1 54  ? 25.492 8.700   5.687   0.82 10.52 ?  54  ASN   A CB   1 
ATOM   1292 C  CB   B ASN   A 1 54  ? 25.563 8.769   5.672   0.18 10.17 ?  54  ASN   A CB   1 
ATOM   1293 C  CG   A ASN   A 1 54  ? 26.519 9.788   5.797   0.82 10.60 ?  54  ASN   A CG   1 
ATOM   1294 C  CG   B ASN   A 1 54  ? 26.501 9.957   5.732   0.18 10.31 ?  54  ASN   A CG   1 
ATOM   1295 O  OD1  A ASN   A 1 54  ? 27.509 9.641   6.524   0.82 10.25 ?  54  ASN   A OD1  1 
ATOM   1296 O  OD1  B ASN   A 1 54  ? 27.621 9.847   6.231   0.18 10.77 ?  54  ASN   A OD1  1 
ATOM   1297 N  ND2  A ASN   A 1 54  ? 26.290 10.904  5.119   0.82 11.03 ?  54  ASN   A ND2  1 
ATOM   1298 N  ND2  B ASN   A 1 54  ? 26.047 11.103  5.235   0.18 10.24 ?  54  ASN   A ND2  1 
ATOM   1299 H  H    A ASN   A 1 54  ? 23.632 7.155   6.111   0.82 12.07 ?  54  ASN   A H    1 
ATOM   1300 H  H    B ASN   A 1 54  ? 23.733 7.193   6.124   0.18 11.87 ?  54  ASN   A H    1 
ATOM   1301 H  HA   A ASN   A 1 54  ? 25.646 7.947   7.575   0.82 11.99 ?  54  ASN   A HA   1 
ATOM   1302 H  HA   B ASN   A 1 54  ? 25.726 8.062   7.583   0.18 12.01 ?  54  ASN   A HA   1 
ATOM   1303 H  HB2  A ASN   A 1 54  ? 25.914 7.912   5.294   0.82 12.66 ?  54  ASN   A HB2  1 
ATOM   1304 H  HB2  B ASN   A 1 54  ? 26.061 8.011   5.326   0.18 12.24 ?  54  ASN   A HB2  1 
ATOM   1305 H  HB3  A ASN   A 1 54  ? 24.774 9.009   5.114   0.82 12.66 ?  54  ASN   A HB3  1 
ATOM   1306 H  HB3  B ASN   A 1 54  ? 24.833 8.990   5.076   0.18 12.24 ?  54  ASN   A HB3  1 
ATOM   1307 H  HD21 A ASN   A 1 54  ? 26.854 11.550  5.159   0.82 13.28 ?  54  ASN   A HD21 1 
ATOM   1308 H  HD21 B ASN   A 1 54  ? 26.544 11.807  5.254   0.18 12.33 ?  54  ASN   A HD21 1 
ATOM   1309 H  HD22 A ASN   A 1 54  ? 25.583 10.974  4.636   0.82 13.28 ?  54  ASN   A HD22 1 
ATOM   1310 H  HD22 B ASN   A 1 54  ? 25.261 11.142  4.892   0.18 12.33 ?  54  ASN   A HD22 1 
ATOM   1311 N  N    . LYS   A 1 55  ? 23.221 10.039  7.443   1.00 10.98 ?  55  LYS   A N    1 
ATOM   1312 C  CA   . LYS   A 1 55  ? 22.642 11.196  8.117   1.00 11.44 ?  55  LYS   A CA   1 
ATOM   1313 C  C    . LYS   A 1 55  ? 22.551 10.961  9.617   1.00 11.47 ?  55  LYS   A C    1 
ATOM   1314 O  O    . LYS   A 1 55  ? 22.834 11.864  10.416  1.00 12.35 ?  55  LYS   A O    1 
ATOM   1315 C  CB   . LYS   A 1 55  ? 21.267 11.498  7.513   1.00 12.32 ?  55  LYS   A CB   1 
ATOM   1316 C  CG   . LYS   A 1 55  ? 20.512 12.641  8.171   1.00 13.39 ?  55  LYS   A CG   1 
ATOM   1317 C  CD   . LYS   A 1 55  ? 19.192 12.903  7.433   1.00 14.69 ?  55  LYS   A CD   1 
ATOM   1318 C  CE   . LYS   A 1 55  ? 18.370 14.003  8.088   1.00 16.66 ?  55  LYS   A CE   1 
ATOM   1319 N  NZ   . LYS   A 1 55  ? 17.039 14.171  7.429   1.00 17.19 ?  55  LYS   A NZ   1 
ATOM   1320 H  H    A LYS   A 1 55  ? 22.713 9.692   6.837   0.82 13.21 ?  55  LYS   A H    1 
ATOM   1321 H  H    B LYS   A 1 55  ? 22.699 9.649   6.875   0.18 13.21 ?  55  LYS   A H    1 
ATOM   1322 H  HA   . LYS   A 1 55  ? 23.210 11.964  7.966   1.00 13.77 ?  55  LYS   A HA   1 
ATOM   1323 H  HB2  . LYS   A 1 55  ? 21.380 11.731  6.579   1.00 14.82 ?  55  LYS   A HB2  1 
ATOM   1324 H  HB3  . LYS   A 1 55  ? 20.712 10.705  7.585   1.00 14.82 ?  55  LYS   A HB3  1 
ATOM   1325 H  HG2  . LYS   A 1 55  ? 20.301 12.402  9.091   1.00 16.11 ?  55  LYS   A HG2  1 
ATOM   1326 H  HG3  . LYS   A 1 55  ? 21.047 13.444  8.142   1.00 16.11 ?  55  LYS   A HG3  1 
ATOM   1327 H  HD2  . LYS   A 1 55  ? 19.389 13.173  6.522   1.00 17.67 ?  55  LYS   A HD2  1 
ATOM   1328 H  HD3  . LYS   A 1 55  ? 18.661 12.089  7.429   1.00 17.67 ?  55  LYS   A HD3  1 
ATOM   1329 H  HE2  . LYS   A 1 55  ? 18.219 13.777  9.019   1.00 20.03 ?  55  LYS   A HE2  1 
ATOM   1330 H  HE3  . LYS   A 1 55  ? 18.848 14.842  8.019   1.00 20.03 ?  55  LYS   A HE3  1 
ATOM   1331 H  HZ1  . LYS   A 1 55  ? 16.503 14.664  7.945   1.00 20.67 ?  55  LYS   A HZ1  1 
ATOM   1332 H  HZ2  . LYS   A 1 55  ? 17.132 14.578  6.644   1.00 20.67 ?  55  LYS   A HZ2  1 
ATOM   1333 H  HZ3  . LYS   A 1 55  ? 16.656 13.376  7.300   1.00 20.67 ?  55  LYS   A HZ3  1 
ATOM   1334 N  N    . ALA   A 1 56  ? 22.167 9.746   10.019  1.00 11.94 ?  56  ALA   A N    1 
ATOM   1335 C  CA   . ALA   A 1 56  ? 22.051 9.417   11.434  1.00 12.77 ?  56  ALA   A CA   1 
ATOM   1336 C  C    . ALA   A 1 56  ? 23.393 9.460   12.156  1.00 12.49 ?  56  ALA   A C    1 
ATOM   1337 O  O    . ALA   A 1 56  ? 23.417 9.663   13.371  1.00 13.80 ?  56  ALA   A O    1 
ATOM   1338 C  CB   . ALA   A 1 56  ? 21.379 8.048   11.602  1.00 13.45 ?  56  ALA   A CB   1 
ATOM   1339 H  H    . ALA   A 1 56  ? 21.968 9.099   9.488   1.00 14.36 ?  56  ALA   A H    1 
ATOM   1340 H  HA   . ALA   A 1 56  ? 21.480 10.069  11.855  1.00 15.37 ?  56  ALA   A HA   1 
ATOM   1341 H  HB1  . ALA   A 1 56  ? 21.308 7.841   12.549  1.00 16.18 ?  56  ALA   A HB1  1 
ATOM   1342 H  HB2  . ALA   A 1 56  ? 20.490 8.080   11.208  1.00 16.18 ?  56  ALA   A HB2  1 
ATOM   1343 H  HB3  . ALA   A 1 56  ? 21.909 7.369   11.157  1.00 16.18 ?  56  ALA   A HB3  1 
ATOM   1344 N  N    . THR   A 1 57  ? 24.507 9.276   11.437  1.00 11.65 ?  57  THR   A N    1 
ATOM   1345 C  CA   . THR   A 1 57  ? 25.851 9.405   12.008  1.00 11.76 ?  57  THR   A CA   1 
ATOM   1346 C  C    . THR   A 1 57  ? 26.397 10.824  11.929  1.00 12.05 ?  57  THR   A C    1 
ATOM   1347 O  O    . THR   A 1 57  ? 27.579 11.038  12.225  1.00 12.70 ?  57  THR   A O    1 
ATOM   1348 C  CB   . THR   A 1 57  ? 26.861 8.454   11.332  1.00 11.49 ?  57  THR   A CB   1 
ATOM   1349 O  OG1  . THR   A 1 57  ? 27.245 8.957   10.039  1.00 11.69 ?  57  THR   A OG1  1 
ATOM   1350 C  CG2  . THR   A 1 57  ? 26.323 7.038   11.225  1.00 11.48 ?  57  THR   A CG2  1 
ATOM   1351 H  H    . THR   A 1 57  ? 24.510 9.056   10.600  1.00 14.02 ?  57  THR   A H    1 
ATOM   1352 H  HA   . THR   A 1 57  ? 25.805 9.150   12.945  1.00 14.16 ?  57  THR   A HA   1 
ATOM   1353 H  HB   . THR   A 1 57  ? 27.657 8.411   11.892  1.00 13.82 ?  57  THR   A HB   1 
ATOM   1354 H  HG1  . THR   A 1 57  ? 26.566 9.018   9.549   1.00 14.06 ?  57  THR   A HG1  1 
ATOM   1355 H  HG21 . THR   A 1 57  ? 26.946 6.478   10.730  1.00 13.82 ?  57  THR   A HG21 1 
ATOM   1356 H  HG22 . THR   A 1 57  ? 26.201 6.655   12.110  1.00 13.82 ?  57  THR   A HG22 1 
ATOM   1357 H  HG23 . THR   A 1 57  ? 25.471 7.032   10.766  1.00 13.82 ?  57  THR   A HG23 1 
ATOM   1358 N  N    . ASN   A 1 58  ? 25.578 11.794  11.523  1.00 12.22 ?  58  ASN   A N    1 
ATOM   1359 C  CA   . ASN   A 1 58  ? 26.035 13.179  11.426  1.00 13.34 ?  58  ASN   A CA   1 
ATOM   1360 C  C    . ASN   A 1 58  ? 27.187 13.309  10.423  1.00 12.21 ?  58  ASN   A C    1 
ATOM   1361 O  O    . ASN   A 1 58  ? 28.087 14.139  10.585  1.00 13.09 ?  58  ASN   A O    1 
ATOM   1362 C  CB   . ASN   A 1 58  ? 26.394 13.724  12.821  1.00 15.68 ?  58  ASN   A CB   1 
ATOM   1363 C  CG   . ASN   A 1 58  ? 26.822 15.173  12.811  1.00 19.47 ?  58  ASN   A CG   1 
ATOM   1364 O  OD1  . ASN   A 1 58  ? 26.199 16.001  12.162  1.00 21.05 ?  58  ASN   A OD1  1 
ATOM   1365 N  ND2  . ASN   A 1 58  ? 27.885 15.490  13.552  1.00 20.77 ?  58  ASN   A ND2  1 
ATOM   1366 H  H    . ASN   A 1 58  ? 24.757 11.666  11.289  1.00 14.70 ?  58  ASN   A H    1 
ATOM   1367 H  HA   . ASN   A 1 58  ? 25.295 13.705  11.090  1.00 16.05 ?  58  ASN   A HA   1 
ATOM   1368 H  HB2  . ASN   A 1 58  ? 25.610 13.642  13.398  1.00 18.85 ?  58  ASN   A HB2  1 
ATOM   1369 H  HB3  . ASN   A 1 58  ? 27.121 13.204  13.189  1.00 18.85 ?  58  ASN   A HB3  1 
ATOM   1370 H  HD21 . ASN   A 1 58  ? 28.159 16.304  13.582  1.00 24.96 ?  58  ASN   A HD21 1 
ATOM   1371 H  HD22 . ASN   A 1 58  ? 28.289 14.879  13.998  1.00 24.96 ?  58  ASN   A HD22 1 
ATOM   1372 N  N    . ASN   A 1 59  ? 27.162 12.488  9.371   1.00 11.55 ?  59  ASN   A N    1 
ATOM   1373 C  CA   . ASN   A 1 59  ? 28.138 12.463  8.275   1.00 11.34 ?  59  ASN   A CA   1 
ATOM   1374 C  C    . ASN   A 1 59  ? 29.457 11.788  8.661   1.00 11.15 ?  59  ASN   A C    1 
ATOM   1375 O  O    . ASN   A 1 59  ? 30.378 11.749  7.829   1.00 11.25 ?  59  ASN   A O    1 
ATOM   1376 C  CB   . ASN   A 1 59  ? 28.429 13.849  7.672   1.00 11.65 ?  59  ASN   A CB   1 
ATOM   1377 C  CG   . ASN   A 1 59  ? 28.776 13.784  6.203   1.00 11.86 ?  59  ASN   A CG   1 
ATOM   1378 O  OD1  . ASN   A 1 59  ? 28.069 13.156  5.415   1.00 12.22 ?  59  ASN   A OD1  1 
ATOM   1379 N  ND2  . ASN   A 1 59  ? 29.859 14.450  5.818   1.00 12.17 ?  59  ASN   A ND2  1 
ATOM   1380 H  H    . ASN   A 1 59  ? 26.550 11.894  9.258   1.00 13.90 ?  59  ASN   A H    1 
ATOM   1381 H  HA   . ASN   A 1 59  ? 27.761 11.935  7.561   1.00 13.65 ?  59  ASN   A HA   1 
ATOM   1382 H  HB2  . ASN   A 1 59  ? 27.646 14.412  7.762   1.00 14.02 ?  59  ASN   A HB2  1 
ATOM   1383 H  HB3  . ASN   A 1 59  ? 29.183 14.253  8.133   1.00 14.02 ?  59  ASN   A HB3  1 
ATOM   1384 H  HD21 . ASN   A 1 59  ? 30.104 14.450  4.992   1.00 14.65 ?  59  ASN   A HD21 1 
ATOM   1385 H  HD22 . ASN   A 1 59  ? 30.335 14.883  6.398   1.00 14.65 ?  59  ASN   A HD22 1 
ATOM   1386 N  N    . ALA   A 1 60  ? 29.585 11.242  9.870   1.00 11.16 ?  60  ALA   A N    1 
ATOM   1387 C  CA   . ALA   A 1 60  ? 30.827 10.562  10.222  1.00 11.48 ?  60  ALA   A CA   1 
ATOM   1388 C  C    . ALA   A 1 60  ? 31.051 9.328   9.353   1.00 11.41 ?  60  ALA   A C    1 
ATOM   1389 O  O    . ALA   A 1 60  ? 32.197 9.005   9.018   1.00 11.62 ?  60  ALA   A O    1 
ATOM   1390 C  CB   . ALA   A 1 60  ? 30.828 10.191  11.704  1.00 11.89 ?  60  ALA   A CB   1 
ATOM   1391 H  H    . ALA   A 1 60  ? 28.986 11.247  10.482  1.00 13.43 ?  60  ALA   A H    1 
ATOM   1392 H  HA   . ALA   A 1 60  ? 31.570 11.169  10.069  1.00 13.81 ?  60  ALA   A HA   1 
ATOM   1393 H  HB1  . ALA   A 1 60  ? 31.659 9.746   11.921  1.00 14.31 ?  60  ALA   A HB1  1 
ATOM   1394 H  HB2  . ALA   A 1 60  ? 30.742 11.006  12.232  1.00 14.31 ?  60  ALA   A HB2  1 
ATOM   1395 H  HB3  . ALA   A 1 60  ? 30.077 9.605   11.884  1.00 14.31 ?  60  ALA   A HB3  1 
ATOM   1396 N  N    . MET   A 1 61  ? 29.979 8.628   8.974   1.00 10.85 ?  61  MET   A N    1 
ATOM   1397 C  CA   . MET   A 1 61  ? 30.124 7.493   8.067   1.00 10.89 ?  61  MET   A CA   1 
ATOM   1398 C  C    . MET   A 1 61  ? 30.751 7.921   6.743   1.00 10.50 ?  61  MET   A C    1 
ATOM   1399 O  O    . MET   A 1 61  ? 31.645 7.242   6.223   1.00 10.85 ?  61  MET   A O    1 
ATOM   1400 C  CB   . MET   A 1 61  ? 28.767 6.819   7.859   1.00 10.86 ?  61  MET   A CB   1 
ATOM   1401 C  CG   . MET   A 1 61  ? 28.779 5.667   6.869   1.00 11.38 ?  61  MET   A CG   1 
ATOM   1402 S  SD   . MET   A 1 61  ? 27.147 4.919   6.653   1.00 11.84 ?  61  MET   A SD   1 
ATOM   1403 C  CE   . MET   A 1 61  ? 27.008 4.015   8.193   1.00 13.61 ?  61  MET   A CE   1 
ATOM   1404 H  H    . MET   A 1 61  ? 29.172 8.795   9.217   1.00 13.06 ?  61  MET   A H    1 
ATOM   1405 H  HA   . MET   A 1 61  ? 30.710 6.844   8.485   1.00 13.10 ?  61  MET   A HA   1 
ATOM   1406 H  HB2  . MET   A 1 61  ? 28.462 6.470   8.710   1.00 13.07 ?  61  MET   A HB2  1 
ATOM   1407 H  HB3  . MET   A 1 61  ? 28.138 7.480   7.533   1.00 13.07 ?  61  MET   A HB3  1 
ATOM   1408 H  HG2  . MET   A 1 61  ? 29.065 5.986   6.000   1.00 13.70 ?  61  MET   A HG2  1 
ATOM   1409 H  HG3  . MET   A 1 61  ? 29.376 4.975   7.185   1.00 13.70 ?  61  MET   A HG3  1 
ATOM   1410 H  HE1  . MET   A 1 61  ? 26.173 3.522   8.198   1.00 16.38 ?  61  MET   A HE1  1 
ATOM   1411 H  HE2  . MET   A 1 61  ? 27.755 3.397   8.263   1.00 16.38 ?  61  MET   A HE2  1 
ATOM   1412 H  HE3  . MET   A 1 61  ? 27.029 4.641   8.933   1.00 16.38 ?  61  MET   A HE3  1 
ATOM   1413 N  N    . GLN   A 1 62  ? 30.301 9.050   6.186   1.00 10.51 ?  62  GLN   A N    1 
ATOM   1414 C  CA   . GLN   A 1 62  ? 30.862 9.530   4.926   1.00 10.78 ?  62  GLN   A CA   1 
ATOM   1415 C  C    . GLN   A 1 62  ? 32.332 9.905   5.068   1.00 10.92 ?  62  GLN   A C    1 
ATOM   1416 O  O    . GLN   A 1 62  ? 33.140 9.589   4.189   1.00 11.34 ?  62  GLN   A O    1 
ATOM   1417 C  CB   . GLN   A 1 62  ? 30.058 10.717  4.393   1.00 10.72 ?  62  GLN   A CB   1 
ATOM   1418 C  CG   . GLN   A 1 62  ? 30.429 11.081  2.971   1.00 10.61 ?  62  GLN   A CG   1 
ATOM   1419 C  CD   . GLN   A 1 62  ? 30.102 9.950   2.028   1.00 10.99 ?  62  GLN   A CD   1 
ATOM   1420 O  OE1  . GLN   A 1 62  ? 28.925 9.638   1.826   1.00 11.56 ?  62  GLN   A OE1  1 
ATOM   1421 N  NE2  . GLN   A 1 62  ? 31.124 9.290   1.488   1.00 11.66 ?  62  GLN   A NE2  1 
ATOM   1422 H  H    . GLN   A 1 62  ? 29.673 9.537   6.508   1.00 12.65 ?  62  GLN   A H    1 
ATOM   1423 H  HA   . GLN   A 1 62  ? 30.808 8.813   4.273   1.00 12.97 ?  62  GLN   A HA   1 
ATOM   1424 H  HB2  . GLN   A 1 62  ? 29.117 10.497  4.410   1.00 12.90 ?  62  GLN   A HB2  1 
ATOM   1425 H  HB3  . GLN   A 1 62  ? 30.232 11.491  4.952   1.00 12.90 ?  62  GLN   A HB3  1 
ATOM   1426 H  HG2  . GLN   A 1 62  ? 29.921 11.858  2.696   1.00 12.78 ?  62  GLN   A HG2  1 
ATOM   1427 H  HG3  . GLN   A 1 62  ? 31.379 11.258  2.916   1.00 12.78 ?  62  GLN   A HG3  1 
ATOM   1428 H  HE21 . GLN   A 1 62  ? 31.934 9.530   1.664   1.00 14.03 ?  62  GLN   A HE21 1 
ATOM   1429 H  HE22 . GLN   A 1 62  ? 30.981 8.633   0.952   1.00 14.03 ?  62  GLN   A HE22 1 
ATOM   1430 N  N    . VAL   A 1 63  ? 32.693 10.599  6.152   1.00 11.14 ?  63  VAL   A N    1 
ATOM   1431 C  CA   . VAL   A 1 63  ? 34.087 10.988  6.364   1.00 12.02 ?  63  VAL   A CA   1 
ATOM   1432 C  C    . VAL   A 1 63  ? 34.982 9.753   6.420   1.00 11.49 ?  63  VAL   A C    1 
ATOM   1433 O  O    . VAL   A 1 63  ? 36.030 9.688   5.763   1.00 11.93 ?  63  VAL   A O    1 
ATOM   1434 C  CB   . VAL   A 1 63  ? 34.204 11.862  7.627   1.00 13.79 ?  63  VAL   A CB   1 
ATOM   1435 C  CG1  . VAL   A 1 63  ? 35.652 12.108  7.971   1.00 15.57 ?  63  VAL   A CG1  1 
ATOM   1436 C  CG2  . VAL   A 1 63  ? 33.472 13.183  7.420   1.00 14.27 ?  63  VAL   A CG2  1 
ATOM   1437 H  H    . VAL   A 1 63  ? 32.148 10.853  6.772   1.00 13.40 ?  63  VAL   A H    1 
ATOM   1438 H  HA   . VAL   A 1 63  ? 34.370 11.525  5.610   1.00 14.47 ?  63  VAL   A HA   1 
ATOM   1439 H  HB   . VAL   A 1 63  ? 33.791 11.402  8.375   1.00 16.58 ?  63  VAL   A HB   1 
ATOM   1440 H  HG11 . VAL   A 1 63  ? 35.704 12.843  8.601   1.00 18.72 ?  63  VAL   A HG11 1 
ATOM   1441 H  HG12 . VAL   A 1 63  ? 36.027 11.307  8.364   1.00 18.72 ?  63  VAL   A HG12 1 
ATOM   1442 H  HG13 . VAL   A 1 63  ? 36.131 12.338  7.158   1.00 18.72 ?  63  VAL   A HG13 1 
ATOM   1443 H  HG21 . VAL   A 1 63  ? 33.569 13.727  8.219   1.00 17.16 ?  63  VAL   A HG21 1 
ATOM   1444 H  HG22 . VAL   A 1 63  ? 33.860 13.644  6.660   1.00 17.16 ?  63  VAL   A HG22 1 
ATOM   1445 H  HG23 . VAL   A 1 63  ? 32.533 13.004  7.256   1.00 17.16 ?  63  VAL   A HG23 1 
ATOM   1446 N  N    . GLU   A 1 64  ? 34.569 8.744   7.193   1.00 11.54 ?  64  GLU   A N    1 
ATOM   1447 C  CA   . GLU   A 1 64  ? 35.332 7.507   7.288   1.00 11.40 ?  64  GLU   A CA   1 
ATOM   1448 C  C    . GLU   A 1 64  ? 35.418 6.821   5.932   1.00 10.96 ?  64  GLU   A C    1 
ATOM   1449 O  O    . GLU   A 1 64  ? 36.472 6.282   5.552   1.00 11.58 ?  64  GLU   A O    1 
ATOM   1450 C  CB   . GLU   A 1 64  ? 34.643 6.596   8.307   1.00 12.00 ?  64  GLU   A CB   1 
ATOM   1451 C  CG   . GLU   A 1 64  ? 35.295 5.241   8.455   1.00 12.51 ?  64  GLU   A CG   1 
ATOM   1452 C  CD   . GLU   A 1 64  ? 34.420 4.245   9.186   1.00 12.96 ?  64  GLU   A CD   1 
ATOM   1453 O  OE1  . GLU   A 1 64  ? 33.180 4.333   9.051   1.00 13.36 ?  64  GLU   A OE1  1 
ATOM   1454 O  OE2  . GLU   A 1 64  ? 34.969 3.349   9.872   1.00 13.17 -1 64  GLU   A OE2  1 
ATOM   1455 H  H    . GLU   A 1 64  ? 33.843 8.753   7.659   1.00 13.89 ?  64  GLU   A H    1 
ATOM   1456 H  HA   . GLU   A 1 64  ? 36.227 7.708   7.600   1.00 13.72 ?  64  GLU   A HA   1 
ATOM   1457 H  HB2  . GLU   A 1 64  ? 34.667 7.035   9.178   1.00 14.43 ?  64  GLU   A HB2  1 
ATOM   1458 H  HB3  . GLU   A 1 64  ? 33.723 6.468   8.035   1.00 14.43 ?  64  GLU   A HB3  1 
ATOM   1459 H  HG2  . GLU   A 1 64  ? 35.488 4.874   7.576   1.00 15.05 ?  64  GLU   A HG2  1 
ATOM   1460 H  HG3  . GLU   A 1 64  ? 36.116 5.338   8.957   1.00 15.05 ?  64  GLU   A HG3  1 
ATOM   1461 N  N    . SER   A 1 65  ? 34.301 6.810   5.199   1.00 10.92 ?  65  SER   A N    1 
ATOM   1462 C  CA   . SER   A 1 65  ? 34.249 6.151   3.900   1.00 10.68 ?  65  SER   A CA   1 
ATOM   1463 C  C    . SER   A 1 65  ? 35.165 6.825   2.886   1.00 11.09 ?  65  SER   A C    1 
ATOM   1464 O  O    . SER   A 1 65  ? 35.796 6.148   2.067   1.00 11.76 ?  65  SER   A O    1 
ATOM   1465 C  CB   . SER   A 1 65  ? 32.813 6.157   3.376   1.00 10.98 ?  65  SER   A CB   1 
ATOM   1466 O  OG   . SER   A 1 65  ? 31.962 5.342   4.173   1.00 11.32 ?  65  SER   A OG   1 
ATOM   1467 H  H    . SER   A 1 65  ? 33.562 7.177   5.438   1.00 13.14 ?  65  SER   A H    1 
ATOM   1468 H  HA   . SER   A 1 65  ? 34.536 5.232   3.997   1.00 12.86 ?  65  SER   A HA   1 
ATOM   1469 H  HB2  . SER   A 1 65  ? 32.476 7.066   3.388   1.00 13.22 ?  65  SER   A HB2  1 
ATOM   1470 H  HB3  . SER   A 1 65  ? 32.813 5.816   2.469   1.00 13.22 ?  65  SER   A HB3  1 
ATOM   1471 H  HG   . SER   A 1 65  ? 31.956 5.626   4.969   1.00 13.63 ?  65  SER   A HG   1 
ATOM   1472 N  N    . ASP   A 1 66  ? 35.237 8.158   2.906   1.00 11.11 ?  66  ASP   A N    1 
ATOM   1473 C  CA   . ASP   A 1 66  ? 36.091 8.857   1.951   1.00 12.12 ?  66  ASP   A CA   1 
ATOM   1474 C  C    . ASP   A 1 66  ? 37.556 8.503   2.175   1.00 12.15 ?  66  ASP   A C    1 
ATOM   1475 O  O    . ASP   A 1 66  ? 38.321 8.338   1.217   1.00 13.03 ?  66  ASP   A O    1 
ATOM   1476 C  CB   . ASP   A 1 66  ? 35.876 10.365  2.061   1.00 13.14 ?  66  ASP   A CB   1 
ATOM   1477 C  CG   . ASP   A 1 66  ? 34.537 10.825  1.472   1.00 14.78 ?  66  ASP   A CG   1 
ATOM   1478 O  OD1  . ASP   A 1 66  ? 33.818 10.029  0.825   1.00 15.05 ?  66  ASP   A OD1  1 
ATOM   1479 O  OD2  . ASP   A 1 66  ? 34.227 12.019  1.643   1.00 17.56 -1 66  ASP   A OD2  1 
ATOM   1480 H  H    . ASP   A 1 66  ? 34.792 8.672   3.441   1.00 13.38 ?  66  ASP   A H    1 
ATOM   1481 H  HA   . ASP   A 1 66  ? 35.848 8.584   1.052   1.00 14.58 ?  66  ASP   A HA   1 
ATOM   1482 H  HB2  . ASP   A 1 66  ? 35.891 10.617  2.999   1.00 15.81 ?  66  ASP   A HB2  1 
ATOM   1483 H  HB3  . ASP   A 1 66  ? 36.589 10.818  1.586   1.00 15.81 ?  66  ASP   A HB3  1 
ATOM   1484 N  N    . ASP   A 1 67  ? 37.963 8.375   3.438   1.00 12.03 ?  67  ASP   A N    1 
ATOM   1485 C  CA   . ASP   A 1 67  ? 39.318 7.924   3.734   1.00 13.01 ?  67  ASP   A CA   1 
ATOM   1486 C  C    . ASP   A 1 67  ? 39.535 6.488   3.264   1.00 12.89 ?  67  ASP   A C    1 
ATOM   1487 O  O    . ASP   A 1 67  ? 40.595 6.159   2.719   1.00 13.53 ?  67  ASP   A O    1 
ATOM   1488 C  CB   . ASP   A 1 67  ? 39.587 8.050   5.231   1.00 14.21 ?  67  ASP   A CB   1 
ATOM   1489 C  CG   . ASP   A 1 67  ? 40.889 7.391   5.644   1.00 15.51 ?  67  ASP   A CG   1 
ATOM   1490 O  OD1  . ASP   A 1 67  ? 41.961 8.021   5.494   1.00 18.10 ?  67  ASP   A OD1  1 
ATOM   1491 O  OD2  . ASP   A 1 67  ? 40.843 6.226   6.107   1.00 15.12 -1 67  ASP   A OD2  1 
ATOM   1492 H  H    . ASP   A 1 67  ? 37.482 8.543   4.129   1.00 14.47 ?  67  ASP   A H    1 
ATOM   1493 H  HA   . ASP   A 1 67  ? 39.950 8.489   3.263   1.00 15.65 ?  67  ASP   A HA   1 
ATOM   1494 H  HB2  . ASP   A 1 67  ? 39.633 8.987   5.460   1.00 17.09 ?  67  ASP   A HB2  1 
ATOM   1495 H  HB3  . ASP   A 1 67  ? 38.862 7.620   5.715   1.00 17.09 ?  67  ASP   A HB3  1 
ATOM   1496 N  N    . TYR   A 1 68  ? 38.543 5.612   3.467   1.00 12.03 ?  68  TYR   A N    1 
ATOM   1497 C  CA   . TYR   A 1 68  ? 38.661 4.232   2.992   1.00 12.35 ?  68  TYR   A CA   1 
ATOM   1498 C  C    . TYR   A 1 68  ? 38.891 4.188   1.482   1.00 12.20 ?  68  TYR   A C    1 
ATOM   1499 O  O    . TYR   A 1 68  ? 39.760 3.449   0.995   1.00 12.67 ?  68  TYR   A O    1 
ATOM   1500 C  CB   . TYR   A 1 68  ? 37.418 3.409   3.383   1.00 12.59 ?  68  TYR   A CB   1 
ATOM   1501 C  CG   . TYR   A 1 68  ? 37.440 2.026   2.756   1.00 13.74 ?  68  TYR   A CG   1 
ATOM   1502 C  CD1  . TYR   A 1 68  ? 36.981 1.835   1.457   1.00 15.23 ?  68  TYR   A CD1  1 
ATOM   1503 C  CD2  . TYR   A 1 68  ? 37.983 0.941   3.423   1.00 15.80 ?  68  TYR   A CD2  1 
ATOM   1504 C  CE1  . TYR   A 1 68  ? 37.040 0.616   0.845   1.00 16.72 ?  68  TYR   A CE1  1 
ATOM   1505 C  CE2  . TYR   A 1 68  ? 38.036 -0.318  2.811   1.00 16.29 ?  68  TYR   A CE2  1 
ATOM   1506 C  CZ   . TYR   A 1 68  ? 37.576 -0.453  1.519   1.00 16.81 ?  68  TYR   A CZ   1 
ATOM   1507 O  OH   . TYR   A 1 68  ? 37.651 -1.664  0.889   1.00 18.03 ?  68  TYR   A OH   1 
ATOM   1508 H  H    . TYR   A 1 68  ? 37.803 5.787   3.875   1.00 14.48 ?  68  TYR   A H    1 
ATOM   1509 H  HA   . TYR   A 1 68  ? 39.426 3.823   3.417   1.00 14.86 ?  68  TYR   A HA   1 
ATOM   1510 H  HB2  . TYR   A 1 68  ? 37.395 3.303   4.347   1.00 15.14 ?  68  TYR   A HB2  1 
ATOM   1511 H  HB3  . TYR   A 1 68  ? 36.619 3.869   3.078   1.00 15.14 ?  68  TYR   A HB3  1 
ATOM   1512 H  HD1  . TYR   A 1 68  ? 36.633 2.562   0.987   1.00 18.31 ?  68  TYR   A HD1  1 
ATOM   1513 H  HD2  . TYR   A 1 68  ? 38.310 1.045   4.285   1.00 19.00 ?  68  TYR   A HD2  1 
ATOM   1514 H  HE1  . TYR   A 1 68  ? 36.728 0.515   -0.025  1.00 20.10 ?  68  TYR   A HE1  1 
ATOM   1515 H  HE2  . TYR   A 1 68  ? 38.406 -1.046  3.253   1.00 19.58 ?  68  TYR   A HE2  1 
ATOM   1516 H  HH   . TYR   A 1 68  ? 37.988 -2.234  1.410   1.00 21.67 ?  68  TYR   A HH   1 
ATOM   1517 N  N    . ILE   A 1 69  ? 38.102 4.953   0.717   1.00 11.80 ?  69  ILE   A N    1 
ATOM   1518 C  CA   . ILE   A 1 69  ? 38.234 4.937   -0.738  1.00 12.12 ?  69  ILE   A CA   1 
ATOM   1519 C  C    . ILE   A 1 69  ? 39.566 5.546   -1.173  1.00 11.90 ?  69  ILE   A C    1 
ATOM   1520 O  O    . ILE   A 1 69  ? 40.215 5.053   -2.105  1.00 12.32 ?  69  ILE   A O    1 
ATOM   1521 C  CB   . ILE   A 1 69  ? 37.034 5.646   -1.400  1.00 12.83 ?  69  ILE   A CB   1 
ATOM   1522 C  CG1  . ILE   A 1 69  ? 35.720 4.910   -1.119  1.00 13.44 ?  69  ILE   A CG1  1 
ATOM   1523 C  CG2  . ILE   A 1 69  ? 37.266 5.835   -2.906  1.00 14.17 ?  69  ILE   A CG2  1 
ATOM   1524 C  CD1  . ILE   A 1 69  ? 35.547 3.618   -1.898  1.00 13.89 ?  69  ILE   A CD1  1 
ATOM   1525 H  H    . ILE   A 1 69  ? 37.498 5.486   1.016   1.00 14.20 ?  69  ILE   A H    1 
ATOM   1526 H  HA   . ILE   A 1 69  ? 38.229 4.013   -1.034  1.00 14.58 ?  69  ILE   A HA   1 
ATOM   1527 H  HB   . ILE   A 1 69  ? 36.963 6.524   -1.007  1.00 15.44 ?  69  ILE   A HB   1 
ATOM   1528 H  HG12 . ILE   A 1 69  ? 35.682 4.693   -0.174  1.00 16.17 ?  69  ILE   A HG12 1 
ATOM   1529 H  HG13 . ILE   A 1 69  ? 34.982 5.497   -1.348  1.00 16.17 ?  69  ILE   A HG13 1 
ATOM   1530 H  HG21 . ILE   A 1 69  ? 36.419 6.047   -3.333  1.00 17.05 ?  69  ILE   A HG21 1 
ATOM   1531 H  HG22 . ILE   A 1 69  ? 37.889 6.572   -3.041  1.00 17.05 ?  69  ILE   A HG22 1 
ATOM   1532 H  HG23 . ILE   A 1 69  ? 37.631 5.022   -3.282  1.00 17.05 ?  69  ILE   A HG23 1 
ATOM   1533 H  HD11 . ILE   A 1 69  ? 34.750 3.166   -1.578  1.00 16.70 ?  69  ILE   A HD11 1 
ATOM   1534 H  HD12 . ILE   A 1 69  ? 35.448 3.828   -2.840  1.00 16.70 ?  69  ILE   A HD12 1 
ATOM   1535 H  HD13 . ILE   A 1 69  ? 36.323 3.058   -1.760  1.00 16.70 ?  69  ILE   A HD13 1 
ATOM   1536 N  N    . ALA   A 1 70  ? 39.986 6.630   -0.523  1.00 12.34 ?  70  ALA   A N    1 
ATOM   1537 C  CA   . ALA   A 1 70  ? 41.262 7.232   -0.882  1.00 13.36 ?  70  ALA   A CA   1 
ATOM   1538 C  C    . ALA   A 1 70  ? 42.407 6.240   -0.715  1.00 13.48 ?  70  ALA   A C    1 
ATOM   1539 O  O    . ALA   A 1 70  ? 43.369 6.268   -1.486  1.00 15.37 ?  70  ALA   A O    1 
ATOM   1540 C  CB   . ALA   A 1 70  ? 41.510 8.481   -0.039  1.00 13.69 ?  70  ALA   A CB   1 
ATOM   1541 H  H    . ALA   A 1 70  ? 39.558 7.025   0.107   1.00 14.85 ?  70  ALA   A H    1 
ATOM   1542 H  HA   . ALA   A 1 70  ? 41.232 7.504   -1.814  1.00 16.07 ?  70  ALA   A HA   1 
ATOM   1543 H  HB1  . ALA   A 1 70  ? 42.368 8.865   -0.291  1.00 16.47 ?  70  ALA   A HB1  1 
ATOM   1544 H  HB2  . ALA   A 1 70  ? 40.802 9.119   -0.198  1.00 16.47 ?  70  ALA   A HB2  1 
ATOM   1545 H  HB3  . ALA   A 1 70  ? 41.529 8.229   0.899   1.00 16.47 ?  70  ALA   A HB3  1 
ATOM   1546 N  N    . THR   A 1 71  ? 42.316 5.350   0.270   1.00 13.09 ?  71  THR   A N    1 
ATOM   1547 C  CA   . THR   A 1 71  ? 43.370 4.371   0.513   1.00 14.45 ?  71  THR   A CA   1 
ATOM   1548 C  C    . THR   A 1 71  ? 43.247 3.147   -0.385  1.00 14.50 ?  71  THR   A C    1 
ATOM   1549 O  O    . THR   A 1 71  ? 44.257 2.638   -0.892  1.00 16.44 ?  71  THR   A O    1 
ATOM   1550 C  CB   . THR   A 1 71  ? 43.312 3.922   1.969   1.00 16.31 ?  71  THR   A CB   1 
ATOM   1551 O  OG1  . THR   A 1 71  ? 43.561 5.046   2.817   1.00 17.66 ?  71  THR   A OG1  1 
ATOM   1552 C  CG2  . THR   A 1 71  ? 44.324 2.813   2.247   1.00 17.56 ?  71  THR   A CG2  1 
ATOM   1553 H  H    . THR   A 1 71  ? 41.649 5.287   0.808   1.00 15.75 ?  71  THR   A H    1 
ATOM   1554 H  HA   . THR   A 1 71  ? 44.233 4.778   0.350   1.00 17.38 ?  71  THR   A HA   1 
ATOM   1555 H  HB   . THR   A 1 71  ? 42.426 3.568   2.157   1.00 19.61 ?  71  THR   A HB   1 
ATOM   1556 H  HG1  . THR   A 1 71  ? 43.536 4.800   3.621   1.00 21.24 ?  71  THR   A HG1  1 
ATOM   1557 H  HG21 . THR   A 1 71  ? 44.472 2.730   3.203   1.00 21.11 ?  71  THR   A HG21 1 
ATOM   1558 H  HG22 . THR   A 1 71  ? 44.001 1.962   1.908   1.00 21.11 ?  71  THR   A HG22 1 
ATOM   1559 H  HG23 . THR   A 1 71  ? 45.172 3.020   1.819   1.00 21.11 ?  71  THR   A HG23 1 
ATOM   1560 N  N    . ASN   A 1 72  ? 42.023 2.643   -0.570  1.00 13.76 ?  72  ASN   A N    1 
ATOM   1561 C  CA   . ASN   A 1 72  ? 41.807 1.319   -1.133  1.00 13.93 ?  72  ASN   A CA   1 
ATOM   1562 C  C    . ASN   A 1 72  ? 41.180 1.309   -2.516  1.00 14.01 ?  72  ASN   A C    1 
ATOM   1563 O  O    . ASN   A 1 72  ? 41.191 0.256   -3.167  1.00 15.38 ?  72  ASN   A O    1 
ATOM   1564 C  CB   . ASN   A 1 72  ? 40.923 0.494   -0.191  1.00 14.56 ?  72  ASN   A CB   1 
ATOM   1565 C  CG   . ASN   A 1 72  ? 41.536 0.344   1.179   1.00 15.42 ?  72  ASN   A CG   1 
ATOM   1566 O  OD1  . ASN   A 1 72  ? 41.082 0.945   2.149   1.00 17.12 ?  72  ASN   A OD1  1 
ATOM   1567 N  ND2  . ASN   A 1 72  ? 42.587 -0.440  1.261   1.00 16.06 ?  72  ASN   A ND2  1 
ATOM   1568 H  H    . ASN   A 1 72  ? 41.291 3.060   -0.374  1.00 16.55 ?  72  ASN   A H    1 
ATOM   1569 H  HA   . ASN   A 1 72  ? 42.662 0.872   -1.201  1.00 16.75 ?  72  ASN   A HA   1 
ATOM   1570 H  HB2  . ASN   A 1 72  ? 40.064 0.929   -0.094  1.00 17.52 ?  72  ASN   A HB2  1 
ATOM   1571 H  HB3  . ASN   A 1 72  ? 40.806 -0.396  -0.567  1.00 17.52 ?  72  ASN   A HB3  1 
ATOM   1572 H  HD21 . ASN   A 1 72  ? 42.978 -0.552  2.021   1.00 19.31 ?  72  ASN   A HD21 1 
ATOM   1573 H  HD22 . ASN   A 1 72  ? 42.888 -0.834  0.561   1.00 19.31 ?  72  ASN   A HD22 1 
ATOM   1574 N  N    . GLY   A 1 73  ? 40.628 2.423   -2.978  1.00 13.54 ?  73  GLY   A N    1 
ATOM   1575 C  CA   . GLY   A 1 73  ? 39.895 2.428   -4.218  1.00 13.26 ?  73  GLY   A CA   1 
ATOM   1576 C  C    . GLY   A 1 73  ? 38.500 1.856   -4.049  1.00 12.91 ?  73  GLY   A C    1 
ATOM   1577 O  O    . GLY   A 1 73  ? 38.112 1.399   -2.967  1.00 13.40 ?  73  GLY   A O    1 
ATOM   1578 H  H    . GLY   A 1 73  ? 40.669 3.194   -2.592  1.00 16.29 ?  73  GLY   A H    1 
ATOM   1579 H  HA2  . GLY   A 1 73  ? 39.820 3.338   -4.545  1.00 15.95 ?  73  GLY   A HA2  1 
ATOM   1580 H  HA3  . GLY   A 1 73  ? 40.367 1.898   -4.879  1.00 15.95 ?  73  GLY   A HA3  1 
ATOM   1581 N  N    . PRO   A 1 74  ? 37.717 1.881   -5.126  1.00 13.40 ?  74  PRO   A N    1 
ATOM   1582 C  CA   . PRO   A 1 74  ? 36.319 1.446   -5.038  1.00 13.24 ?  74  PRO   A CA   1 
ATOM   1583 C  C    . PRO   A 1 74  ? 36.173 -0.038  -4.724  1.00 12.67 ?  74  PRO   A C    1 
ATOM   1584 O  O    . PRO   A 1 74  ? 37.043 -0.865  -5.012  1.00 13.70 ?  74  PRO   A O    1 
ATOM   1585 C  CB   . PRO   A 1 74  ? 35.761 1.761   -6.433  1.00 15.05 ?  74  PRO   A CB   1 
ATOM   1586 C  CG   . PRO   A 1 74  ? 36.705 2.754   -7.029  1.00 17.60 ?  74  PRO   A CG   1 
ATOM   1587 C  CD   . PRO   A 1 74  ? 38.048 2.417   -6.458  1.00 15.22 ?  74  PRO   A CD   1 
ATOM   1588 H  HA   . PRO   A 1 74  ? 35.840 1.968   -4.372  1.00 15.92 ?  74  PRO   A HA   1 
ATOM   1589 H  HB2  . PRO   A 1 74  ? 35.731 0.950   -6.962  1.00 18.10 ?  74  PRO   A HB2  1 
ATOM   1590 H  HB3  . PRO   A 1 74  ? 34.870 2.145   -6.347  1.00 18.10 ?  74  PRO   A HB3  1 
ATOM   1591 H  HG2  . PRO   A 1 74  ? 36.713 2.659   -7.994  1.00 21.16 ?  74  PRO   A HG2  1 
ATOM   1592 H  HG3  . PRO   A 1 74  ? 36.442 3.651   -6.775  1.00 21.16 ?  74  PRO   A HG3  1 
ATOM   1593 H  HD2  . PRO   A 1 74  ? 38.489 1.740   -6.995  1.00 18.30 ?  74  PRO   A HD2  1 
ATOM   1594 H  HD3  . PRO   A 1 74  ? 38.590 3.220   -6.385  1.00 18.30 ?  74  PRO   A HD3  1 
ATOM   1595 N  N    . LEU   A 1 75  ? 35.030 -0.369  -4.131  1.00 12.15 ?  75  LEU   A N    1 
ATOM   1596 C  CA   . LEU   A 1 75  ? 34.632 -1.756  -3.980  1.00 11.68 ?  75  LEU   A CA   1 
ATOM   1597 C  C    . LEU   A 1 75  ? 34.242 -2.336  -5.337  1.00 12.20 ?  75  LEU   A C    1 
ATOM   1598 O  O    . LEU   A 1 75  ? 34.118 -1.624  -6.339  1.00 13.59 ?  75  LEU   A O    1 
ATOM   1599 C  CB   . LEU   A 1 75  ? 33.445 -1.873  -3.026  1.00 11.77 ?  75  LEU   A CB   1 
ATOM   1600 C  CG   . LEU   A 1 75  ? 33.674 -1.473  -1.575  1.00 13.57 ?  75  LEU   A CG   1 
ATOM   1601 C  CD1  . LEU   A 1 75  ? 32.393 -1.679  -0.774  1.00 15.39 ?  75  LEU   A CD1  1 
ATOM   1602 C  CD2  . LEU   A 1 75  ? 34.821 -2.215  -0.944  1.00 17.02 ?  75  LEU   A CD2  1 
ATOM   1603 H  H    . LEU   A 1 75  ? 34.466 0.199   -3.814  1.00 14.61 ?  75  LEU   A H    1 
ATOM   1604 H  HA   . LEU   A 1 75  ? 35.373 -2.268  -3.632  1.00 14.06 ?  75  LEU   A HA   1 
ATOM   1605 H  HB2  . LEU   A 1 75  ? 32.729 -1.317  -3.367  1.00 14.17 ?  75  LEU   A HB2  1 
ATOM   1606 H  HB3  . LEU   A 1 75  ? 33.156 -2.799  -3.025  1.00 14.17 ?  75  LEU   A HB3  1 
ATOM   1607 H  HG   . LEU   A 1 75  ? 33.893 -0.526  -1.549  1.00 16.32 ?  75  LEU   A HG   1 
ATOM   1608 H  HD11 . LEU   A 1 75  ? 32.554 -1.416  0.146   1.00 18.50 ?  75  LEU   A HD11 1 
ATOM   1609 H  HD12 . LEU   A 1 75  ? 31.694 -1.127  -1.158  1.00 18.50 ?  75  LEU   A HD12 1 
ATOM   1610 H  HD13 . LEU   A 1 75  ? 32.144 -2.612  -0.816  1.00 18.50 ?  75  LEU   A HD13 1 
ATOM   1611 H  HD21 . LEU   A 1 75  ? 34.870 -1.984  -0.004  1.00 20.46 ?  75  LEU   A HD21 1 
ATOM   1612 H  HD22 . LEU   A 1 75  ? 34.678 -3.167  -1.046  1.00 20.46 ?  75  LEU   A HD22 1 
ATOM   1613 H  HD23 . LEU   A 1 75  ? 35.650 -1.958  -1.387  1.00 20.46 ?  75  LEU   A HD23 1 
ATOM   1614 N  N    . LYS   A 1 76  ? 34.057 -3.654  -5.355  1.00 12.72 ?  76  LYS   A N    1 
ATOM   1615 C  CA   . LYS   A 1 76  ? 33.451 -4.368  -6.473  1.00 13.32 ?  76  LYS   A CA   1 
ATOM   1616 C  C    . LYS   A 1 76  ? 31.942 -4.456  -6.270  1.00 11.99 ?  76  LYS   A C    1 
ATOM   1617 O  O    . LYS   A 1 76  ? 31.466 -4.581  -5.143  1.00 11.77 ?  76  LYS   A O    1 
ATOM   1618 C  CB   . LYS   A 1 76  ? 34.000 -5.804  -6.544  1.00 14.89 ?  76  LYS   A CB   1 
ATOM   1619 C  CG   . LYS   A 1 76  ? 35.511 -5.905  -6.718  1.00 16.43 ?  76  LYS   A CG   1 
ATOM   1620 C  CD   . LYS   A 1 76  ? 36.023 -7.317  -6.569  1.00 17.88 ?  76  LYS   A CD   1 
ATOM   1621 C  CE   . LYS   A 1 76  ? 37.526 -7.375  -6.742  1.00 20.00 ?  76  LYS   A CE   1 
ATOM   1622 N  NZ   . LYS   A 1 76  ? 38.050 -8.745  -6.593  1.00 20.94 ?  76  LYS   A NZ   1 
ATOM   1623 H  H    . LYS   A 1 76  ? 34.283 -4.173  -4.705  1.00 15.31 ?  76  LYS   A H    1 
ATOM   1624 H  HA   . LYS   A 1 76  ? 33.642 -3.913  -7.308  1.00 16.02 ?  76  LYS   A HA   1 
ATOM   1625 H  HB2  . LYS   A 1 76  ? 33.767 -6.264  -5.722  1.00 17.91 ?  76  LYS   A HB2  1 
ATOM   1626 H  HB3  . LYS   A 1 76  ? 33.586 -6.254  -7.298  1.00 17.91 ?  76  LYS   A HB3  1 
ATOM   1627 H  HG2  . LYS   A 1 76  ? 35.749 -5.590  -7.605  1.00 19.76 ?  76  LYS   A HG2  1 
ATOM   1628 H  HG3  . LYS   A 1 76  ? 35.944 -5.355  -6.045  1.00 19.76 ?  76  LYS   A HG3  1 
ATOM   1629 H  HD2  . LYS   A 1 76  ? 35.805 -7.647  -5.683  1.00 21.49 ?  76  LYS   A HD2  1 
ATOM   1630 H  HD3  . LYS   A 1 76  ? 35.617 -7.880  -7.248  1.00 21.49 ?  76  LYS   A HD3  1 
ATOM   1631 H  HE2  . LYS   A 1 76  ? 37.756 -7.054  -7.628  1.00 24.04 ?  76  LYS   A HE2  1 
ATOM   1632 H  HE3  . LYS   A 1 76  ? 37.943 -6.815  -6.066  1.00 24.04 ?  76  LYS   A HE3  1 
ATOM   1633 H  HZ1  . LYS   A 1 76  ? 38.932 -8.750  -6.699  1.00 25.17 ?  76  LYS   A HZ1  1 
ATOM   1634 H  HZ2  . LYS   A 1 76  ? 37.853 -9.062  -5.783  1.00 25.17 ?  76  LYS   A HZ2  1 
ATOM   1635 H  HZ3  . LYS   A 1 76  ? 37.682 -9.280  -7.206  1.00 25.17 ?  76  LYS   A HZ3  1 
ATOM   1636 N  N    . VAL   A 1 77  ? 31.189 -4.427  -7.372  1.00 12.08 ?  77  VAL   A N    1 
ATOM   1637 C  CA   . VAL   A 1 77  ? 29.782 -4.811  -7.282  1.00 12.04 ?  77  VAL   A CA   1 
ATOM   1638 C  C    . VAL   A 1 77  ? 29.717 -6.266  -6.843  1.00 11.90 ?  77  VAL   A C    1 
ATOM   1639 O  O    . VAL   A 1 77  ? 30.377 -7.134  -7.426  1.00 12.13 ?  77  VAL   A O    1 
ATOM   1640 C  CB   . VAL   A 1 77  ? 29.053 -4.594  -8.617  1.00 13.42 ?  77  VAL   A CB   1 
ATOM   1641 C  CG1  . VAL   A 1 77  ? 27.598 -5.033  -8.500  1.00 14.29 ?  77  VAL   A CG1  1 
ATOM   1642 C  CG2  . VAL   A 1 77  ? 29.134 -3.138  -9.040  1.00 14.79 ?  77  VAL   A CG2  1 
ATOM   1643 H  H    . VAL   A 1 77  ? 31.467 -4.193  -8.153  1.00 14.54 ?  77  VAL   A H    1 
ATOM   1644 H  HA   . VAL   A 1 77  ? 29.353 -4.267  -6.606  1.00 14.49 ?  77  VAL   A HA   1 
ATOM   1645 H  HB   . VAL   A 1 77  ? 29.484 -5.130  -9.303  1.00 16.15 ?  77  VAL   A HB   1 
ATOM   1646 H  HG11 . VAL   A 1 77  ? 27.118 -4.724  -9.280  1.00 17.18 ?  77  VAL   A HG11 1 
ATOM   1647 H  HG12 . VAL   A 1 77  ? 27.565 -6.000  -8.447  1.00 17.18 ?  77  VAL   A HG12 1 
ATOM   1648 H  HG13 . VAL   A 1 77  ? 27.220 -4.641  -7.697  1.00 17.18 ?  77  VAL   A HG13 1 
ATOM   1649 H  HG21 . VAL   A 1 77  ? 28.629 -3.023  -9.858  1.00 17.79 ?  77  VAL   A HG21 1 
ATOM   1650 H  HG22 . VAL   A 1 77  ? 28.759 -2.586  -8.336  1.00 17.79 ?  77  VAL   A HG22 1 
ATOM   1651 H  HG23 . VAL   A 1 77  ? 30.063 -2.900  -9.187  1.00 17.79 ?  77  VAL   A HG23 1 
ATOM   1652 N  N    . GLY   A 1 78  ? 28.937 -6.538  -5.794  1.00 11.64 ?  78  GLY   A N    1 
ATOM   1653 C  CA   . GLY   A 1 78  ? 28.924 -7.827  -5.142  1.00 11.58 ?  78  GLY   A CA   1 
ATOM   1654 C  C    . GLY   A 1 78  ? 29.843 -7.923  -3.945  1.00 11.28 ?  78  GLY   A C    1 
ATOM   1655 O  O    . GLY   A 1 78  ? 29.780 -8.924  -3.216  1.00 12.01 ?  78  GLY   A O    1 
ATOM   1656 H  H    . GLY   A 1 78  ? 28.391 -5.966  -5.449  1.00 14.01 ?  78  GLY   A H    1 
ATOM   1657 H  HA2  . GLY   A 1 78  ? 28.023 -8.019  -4.849  1.00 13.93 ?  78  GLY   A HA2  1 
ATOM   1658 H  HA3  . GLY   A 1 78  ? 29.186 -8.505  -5.786  1.00 13.93 ?  78  GLY   A HA3  1 
ATOM   1659 N  N    . GLY   A 1 79  ? 30.699 -6.922  -3.725  1.00 11.29 ?  79  GLY   A N    1 
ATOM   1660 C  CA   . GLY   A 1 79  ? 31.662 -6.941  -2.648  1.00 11.53 ?  79  GLY   A CA   1 
ATOM   1661 C  C    . GLY   A 1 79  ? 31.218 -6.140  -1.438  1.00 10.97 ?  79  GLY   A C    1 
ATOM   1662 O  O    . GLY   A 1 79  ? 30.098 -5.628  -1.359  1.00 11.54 ?  79  GLY   A O    1 
ATOM   1663 H  H    . GLY   A 1 79  ? 30.745 -6.211  -4.209  1.00 13.59 ?  79  GLY   A H    1 
ATOM   1664 H  HA2  . GLY   A 1 79  ? 31.811 -7.868  -2.373  1.00 13.87 ?  79  GLY   A HA2  1 
ATOM   1665 H  HA3  . GLY   A 1 79  ? 32.506 -6.588  -2.963  1.00 13.87 ?  79  GLY   A HA3  1 
ATOM   1666 N  N    . SER   A 1 80  ? 32.124 -6.046  -0.468  1.00 11.52 ?  80  SER   A N    1 
ATOM   1667 C  CA   . SER   A 1 80  ? 31.807 -5.420  0.805   1.00 10.97 ?  80  SER   A CA   1 
ATOM   1668 C  C    . SER   A 1 80  ? 33.080 -4.972  1.499   1.00 11.07 ?  80  SER   A C    1 
ATOM   1669 O  O    . SER   A 1 80  ? 34.192 -5.396  1.159   1.00 12.39 ?  80  SER   A O    1 
ATOM   1670 C  CB   . SER   A 1 80  ? 31.053 -6.388  1.728   1.00 11.87 ?  80  SER   A CB   1 
ATOM   1671 O  OG   . SER   A 1 80  ? 31.891 -7.427  2.210   1.00 13.70 ?  80  SER   A OG   1 
ATOM   1672 H  H    . SER   A 1 80  ? 32.936 -6.323  -0.533  1.00 13.87 ?  80  SER   A H    1 
ATOM   1673 H  HA   . SER   A 1 80  ? 31.253 -4.644  0.636   1.00 13.20 ?  80  SER   A HA   1 
ATOM   1674 H  HB2  . SER   A 1 80  ? 30.705 -5.889  2.482   1.00 14.29 ?  80  SER   A HB2  1 
ATOM   1675 H  HB3  . SER   A 1 80  ? 30.319 -6.783  1.229   1.00 14.29 ?  80  SER   A HB3  1 
ATOM   1676 H  HG   . SER   A 1 80  ? 32.198 -7.865  1.562   1.00 16.48 ?  80  SER   A HG   1 
ATOM   1677 N  N    . CYS   A 1 81  ? 32.894 -4.125  2.506   1.00 10.69 ?  81  CYS   A N    1 
ATOM   1678 C  CA   . CYS   A 1 81  ? 33.951 -3.840  3.464   1.00 10.85 ?  81  CYS   A CA   1 
ATOM   1679 C  C    . CYS   A 1 81  ? 33.315 -3.606  4.825   1.00 10.66 ?  81  CYS   A C    1 
ATOM   1680 O  O    . CYS   A 1 81  ? 32.149 -3.211  4.917   1.00 11.96 ?  81  CYS   A O    1 
ATOM   1681 C  CB   . CYS   A 1 81  ? 34.819 -2.644  3.045   1.00 11.75 ?  81  CYS   A CB   1 
ATOM   1682 S  SG   . CYS   A 1 81  ? 33.926 -1.068  3.061   1.00 11.68 ?  81  CYS   A SG   1 
ATOM   1683 H  H    . CYS   A 1 81  ? 32.158 -3.701  2.663   1.00 12.87 ?  81  CYS   A H    1 
ATOM   1684 H  HA   . CYS   A 1 81  ? 34.530 -4.613  3.534   1.00 13.06 ?  81  CYS   A HA   1 
ATOM   1685 H  HB2  . CYS   A 1 81  ? 35.570 -2.571  3.655   1.00 14.13 ?  81  CYS   A HB2  1 
ATOM   1686 H  HB3  . CYS   A 1 81  ? 35.145 -2.796  2.142   1.00 14.13 ?  81  CYS   A HB3  1 
ATOM   1687 H  HG   . CYS   A 1 81  ? 34.679 -0.189  2.721   1.00 14.06 ?  81  CYS   A HG   1 
ATOM   1688 N  N    . VAL   A 1 82  ? 34.088 -3.860  5.877   1.00 11.05 ?  82  VAL   A N    1 
ATOM   1689 C  CA   . VAL   A 1 82  ? 33.670 -3.621  7.250   1.00 11.39 ?  82  VAL   A CA   1 
ATOM   1690 C  C    . VAL   A 1 82  ? 34.270 -2.308  7.720   1.00 11.60 ?  82  VAL   A C    1 
ATOM   1691 O  O    . VAL   A 1 82  ? 35.493 -2.133  7.701   1.00 12.38 ?  82  VAL   A O    1 
ATOM   1692 C  CB   . VAL   A 1 82  ? 34.094 -4.764  8.185   1.00 13.05 ?  82  VAL   A CB   1 
ATOM   1693 C  CG1  . VAL   A 1 82  ? 33.644 -4.464  9.606   1.00 14.62 ?  82  VAL   A CG1  1 
ATOM   1694 C  CG2  . VAL   A 1 82  ? 33.537 -6.098  7.712   1.00 14.24 ?  82  VAL   A CG2  1 
ATOM   1695 H  H    . VAL   A 1 82  ? 34.885 -4.191  5.817   1.00 13.29 ?  82  VAL   A H    1 
ATOM   1696 H  HA   . VAL   A 1 82  ? 32.700 -3.546  7.281   1.00 13.70 ?  82  VAL   A HA   1 
ATOM   1697 H  HB   . VAL   A 1 82  ? 35.060 -4.823  8.187   1.00 15.70 ?  82  VAL   A HB   1 
ATOM   1698 H  HG11 . VAL   A 1 82  ? 33.717 -5.273  10.138  1.00 17.58 ?  82  VAL   A HG11 1 
ATOM   1699 H  HG12 . VAL   A 1 82  ? 34.208 -3.771  9.984   1.00 17.58 ?  82  VAL   A HG12 1 
ATOM   1700 H  HG13 . VAL   A 1 82  ? 32.719 -4.165  9.592   1.00 17.58 ?  82  VAL   A HG13 1 
ATOM   1701 H  HG21 . VAL   A 1 82  ? 33.795 -6.788  8.344   1.00 17.13 ?  82  VAL   A HG21 1 
ATOM   1702 H  HG22 . VAL   A 1 82  ? 32.570 -6.038  7.665   1.00 17.13 ?  82  VAL   A HG22 1 
ATOM   1703 H  HG23 . VAL   A 1 82  ? 33.901 -6.299  6.837   1.00 17.13 ?  82  VAL   A HG23 1 
ATOM   1704 N  N    . LEU   A 1 83  ? 33.416 -1.390  8.147   1.00 11.29 ?  83  LEU   A N    1 
ATOM   1705 C  CA   . LEU   A 1 83  ? 33.837 -0.123  8.726   1.00 11.33 ?  83  LEU   A CA   1 
ATOM   1706 C  C    . LEU   A 1 83  ? 33.128 0.054   10.064  1.00 11.38 ?  83  LEU   A C    1 
ATOM   1707 O  O    . LEU   A 1 83  ? 32.408 -0.837  10.530  1.00 12.13 ?  83  LEU   A O    1 
ATOM   1708 C  CB   . LEU   A 1 83  ? 33.575 1.036   7.753   1.00 11.84 ?  83  LEU   A CB   1 
ATOM   1709 C  CG   . LEU   A 1 83  ? 34.467 1.037   6.504   1.00 12.51 ?  83  LEU   A CG   1 
ATOM   1710 C  CD1  . LEU   A 1 83  ? 34.021 2.078   5.497   1.00 13.13 ?  83  LEU   A CD1  1 
ATOM   1711 C  CD2  . LEU   A 1 83  ? 35.937 1.248   6.866   1.00 13.39 ?  83  LEU   A CD2  1 
ATOM   1712 H  H    . LEU   A 1 83  ? 32.560 -1.480  8.107   1.00 13.59 ?  83  LEU   A H    1 
ATOM   1713 H  HA   . LEU   A 1 83  ? 34.788 -0.153  8.897   1.00 13.63 ?  83  LEU   A HA   1 
ATOM   1714 H  HB2  . LEU   A 1 83  ? 32.653 0.994   7.451   1.00 14.25 ?  83  LEU   A HB2  1 
ATOM   1715 H  HB3  . LEU   A 1 83  ? 33.724 1.876   8.217   1.00 14.25 ?  83  LEU   A HB3  1 
ATOM   1716 H  HG   . LEU   A 1 83  ? 34.396 0.171   6.078   1.00 15.05 ?  83  LEU   A HG   1 
ATOM   1717 H  HD11 . LEU   A 1 83  ? 34.606 2.035   4.721   1.00 15.80 ?  83  LEU   A HD11 1 
ATOM   1718 H  HD12 . LEU   A 1 83  ? 33.108 1.886   5.231   1.00 15.80 ?  83  LEU   A HD12 1 
ATOM   1719 H  HD13 . LEU   A 1 83  ? 34.073 2.955   5.902   1.00 15.80 ?  83  LEU   A HD13 1 
ATOM   1720 H  HD21 . LEU   A 1 83  ? 36.444 1.398   6.051   1.00 16.11 ?  83  LEU   A HD21 1 
ATOM   1721 H  HD22 . LEU   A 1 83  ? 36.012 2.022   7.447   1.00 16.11 ?  83  LEU   A HD22 1 
ATOM   1722 H  HD23 . LEU   A 1 83  ? 36.269 0.459   7.320   1.00 16.11 ?  83  LEU   A HD23 1 
ATOM   1723 N  N    . SER   A 1 84  ? 33.337 1.205   10.695  1.00 11.99 ?  84  SER   A N    1 
ATOM   1724 C  CA   . SER   A 1 84  ? 32.696 1.460   11.973  1.00 12.08 ?  84  SER   A CA   1 
ATOM   1725 C  C    . SER   A 1 84  ? 31.179 1.539   11.829  1.00 11.84 ?  84  SER   A C    1 
ATOM   1726 O  O    . SER   A 1 84  ? 30.649 2.001   10.817  1.00 12.29 ?  84  SER   A O    1 
ATOM   1727 C  CB   . SER   A 1 84  ? 33.181 2.789   12.543  1.00 13.17 ?  84  SER   A CB   1 
ATOM   1728 O  OG   . SER   A 1 84  ? 32.556 3.062   13.783  1.00 13.92 ?  84  SER   A OG   1 
ATOM   1729 H  H    . SER   A 1 84  ? 33.833 1.849   10.398  1.00 14.43 ?  84  SER   A H    1 
ATOM   1730 H  HA   . SER   A 1 84  ? 32.921 0.750   12.591  1.00 14.54 ?  84  SER   A HA   1 
ATOM   1731 H  HB2  . SER   A 1 84  ? 34.142 2.748   12.667  1.00 15.84 ?  84  SER   A HB2  1 
ATOM   1732 H  HB3  . SER   A 1 84  ? 32.959 3.499   11.918  1.00 15.84 ?  84  SER   A HB3  1 
ATOM   1733 H  HG   . SER   A 1 84  ? 32.837 3.793   14.090  1.00 16.74 ?  84  SER   A HG   1 
ATOM   1734 N  N    . GLY   A 1 85  ? 30.479 1.114   12.876  1.00 12.59 ?  85  GLY   A N    1 
ATOM   1735 C  CA   . GLY   A 1 85  ? 29.055 1.343   12.972  1.00 13.44 ?  85  GLY   A CA   1 
ATOM   1736 C  C    . GLY   A 1 85  ? 28.682 2.654   13.621  1.00 13.23 ?  85  GLY   A C    1 
ATOM   1737 O  O    . GLY   A 1 85  ? 27.492 2.963   13.741  1.00 13.75 ?  85  GLY   A O    1 
ATOM   1738 H  H    . GLY   A 1 85  ? 30.818 0.682   13.542  1.00 15.15 ?  85  GLY   A H    1 
ATOM   1739 H  HA2  . GLY   A 1 85  ? 28.674 1.320   12.080  1.00 16.17 ?  85  GLY   A HA2  1 
ATOM   1740 H  HA3  . GLY   A 1 85  ? 28.657 0.630   13.489  1.00 16.17 ?  85  GLY   A HA3  1 
ATOM   1741 N  N    . HIS   A 1 86  ? 29.664 3.433   14.062  1.00 12.55 ?  86  HIS   A N    1 
ATOM   1742 C  CA   . HIS   A 1 86  ? 29.430 4.772   14.619  1.00 13.39 ?  86  HIS   A CA   1 
ATOM   1743 C  C    . HIS   A 1 86  ? 28.451 4.645   15.779  1.00 14.06 ?  86  HIS   A C    1 
ATOM   1744 O  O    . HIS   A 1 86  ? 28.643 3.769   16.639  1.00 15.13 ?  86  HIS   A O    1 
ATOM   1745 C  CB   . HIS   A 1 86  ? 29.044 5.751   13.513  1.00 13.26 ?  86  HIS   A CB   1 
ATOM   1746 C  CG   . HIS   A 1 86  ? 30.100 5.865   12.474  1.00 12.95 ?  86  HIS   A CG   1 
ATOM   1747 N  ND1  . HIS   A 1 86  ? 31.178 6.715   12.602  1.00 13.99 ?  86  HIS   A ND1  1 
ATOM   1748 C  CD2  . HIS   A 1 86  ? 30.299 5.166   11.335  1.00 12.72 ?  86  HIS   A CD2  1 
ATOM   1749 C  CE1  . HIS   A 1 86  ? 31.976 6.553   11.564  1.00 13.56 ?  86  HIS   A CE1  1 
ATOM   1750 N  NE2  . HIS   A 1 86  ? 31.473 5.611   10.787  1.00 13.03 ?  86  HIS   A NE2  1 
ATOM   1751 H  H    . HIS   A 1 86  ? 30.491 3.209   14.061  1.00 15.10 ?  86  HIS   A H    1 
ATOM   1752 H  HA   . HIS   A 1 86  ? 30.265 5.093   14.991  1.00 16.10 ?  86  HIS   A HA   1 
ATOM   1753 H  HB2  . HIS   A 1 86  ? 28.227 5.451   13.083  1.00 15.95 ?  86  HIS   A HB2  1 
ATOM   1754 H  HB3  . HIS   A 1 86  ? 28.906 6.637   13.897  1.00 15.95 ?  86  HIS   A HB3  1 
ATOM   1755 H  HD2  . HIS   A 1 86  ? 29.751 4.494   10.992  1.00 15.30 ?  86  HIS   A HD2  1 
ATOM   1756 H  HE1  . HIS   A 1 86  ? 32.762 7.025   11.395  1.00 16.31 ?  86  HIS   A HE1  1 
ATOM   1757 H  HE2  . HIS   A 1 86  ? 31.817 5.335   10.042  1.00 15.67 ?  86  HIS   A HE2  1 
ATOM   1758 N  N    . ASN   A 1 87  ? 27.432 5.491   15.856  1.00 15.01 ?  87  ASN   A N    1 
ATOM   1759 C  CA   . ASN   A 1 87  ? 26.446 5.469   16.922  1.00 16.21 ?  87  ASN   A CA   1 
ATOM   1760 C  C    . ASN   A 1 87  ? 25.322 4.474   16.673  1.00 17.25 ?  87  ASN   A C    1 
ATOM   1761 O  O    . ASN   A 1 87  ? 24.386 4.415   17.475  1.00 19.71 ?  87  ASN   A O    1 
ATOM   1762 C  CB   . ASN   A 1 87  ? 25.849 6.872   17.093  1.00 17.24 ?  87  ASN   A CB   1 
ATOM   1763 C  CG   . ASN   A 1 87  ? 25.332 7.456   15.782  1.00 17.94 ?  87  ASN   A CG   1 
ATOM   1764 O  OD1  . ASN   A 1 87  ? 25.960 7.334   14.733  1.00 18.47 ?  87  ASN   A OD1  1 
ATOM   1765 N  ND2  . ASN   A 1 87  ? 24.185 8.106   15.847  1.00 18.85 ?  87  ASN   A ND2  1 
ATOM   1766 H  H    . ASN   A 1 87  ? 27.287 6.110   15.282  1.00 18.04 ?  87  ASN   A H    1 
ATOM   1767 H  HA   . ASN   A 1 87  ? 26.877 5.222   17.757  1.00 19.49 ?  87  ASN   A HA   1 
ATOM   1768 H  HB2  . ASN   A 1 87  ? 25.105 6.823   17.723  1.00 20.72 ?  87  ASN   A HB2  1 
ATOM   1769 H  HB3  . ASN   A 1 87  ? 26.533 7.463   17.443  1.00 20.72 ?  87  ASN   A HB3  1 
ATOM   1770 H  HD21 . ASN   A 1 87  ? 23.853 8.454   15.137  1.00 22.66 ?  87  ASN   A HD21 1 
ATOM   1771 H  HD22 . ASN   A 1 87  ? 23.771 8.182   16.600  1.00 22.66 ?  87  ASN   A HD22 1 
ATOM   1772 N  N    . LEU   A 1 88  ? 25.395 3.686   15.604  1.00 16.33 ?  88  LEU   A N    1 
ATOM   1773 C  CA   . LEU   A 1 88  ? 24.296 2.818   15.204  1.00 16.25 ?  88  LEU   A CA   1 
ATOM   1774 C  C    . LEU   A 1 88  ? 24.516 1.345   15.508  1.00 15.83 ?  88  LEU   A C    1 
ATOM   1775 O  O    . LEU   A 1 88  ? 23.540 0.617   15.685  1.00 16.76 ?  88  LEU   A O    1 
ATOM   1776 C  CB   . LEU   A 1 88  ? 24.046 2.967   13.701  1.00 17.02 ?  88  LEU   A CB   1 
ATOM   1777 C  CG   . LEU   A 1 88  ? 23.757 4.388   13.215  1.00 18.80 ?  88  LEU   A CG   1 
ATOM   1778 C  CD1  . LEU   A 1 88  ? 23.583 4.396   11.710  1.00 19.08 ?  88  LEU   A CD1  1 
ATOM   1779 C  CD2  . LEU   A 1 88  ? 22.527 4.971   13.904  1.00 20.59 ?  88  LEU   A CD2  1 
ATOM   1780 H  H    . LEU   A 1 88  ? 26.086 3.636   15.093  1.00 19.63 ?  88  LEU   A H    1 
ATOM   1781 H  HA   . LEU   A 1 88  ? 23.494 3.101   15.667  1.00 19.54 ?  88  LEU   A HA   1 
ATOM   1782 H  HB2  . LEU   A 1 88  ? 24.825 2.654   13.223  1.00 20.46 ?  88  LEU   A HB2  1 
ATOM   1783 H  HB3  . LEU   A 1 88  ? 23.277 2.425   13.465  1.00 20.46 ?  88  LEU   A HB3  1 
ATOM   1784 H  HG   . LEU   A 1 88  ? 24.514 4.955   13.427  1.00 22.60 ?  88  LEU   A HG   1 
ATOM   1785 H  HD11 . LEU   A 1 88  ? 23.450 5.310   11.411  1.00 22.94 ?  88  LEU   A HD11 1 
ATOM   1786 H  HD12 . LEU   A 1 88  ? 24.380 4.027   11.298  1.00 22.94 ?  88  LEU   A HD12 1 
ATOM   1787 H  HD13 . LEU   A 1 88  ? 22.811 3.857   11.479  1.00 22.94 ?  88  LEU   A HD13 1 
ATOM   1788 H  HD21 . LEU   A 1 88  ? 22.306 5.820   13.491  1.00 24.75 ?  88  LEU   A HD21 1 
ATOM   1789 H  HD22 . LEU   A 1 88  ? 21.788 4.352   13.805  1.00 24.75 ?  88  LEU   A HD22 1 
ATOM   1790 H  HD23 . LEU   A 1 88  ? 22.727 5.102   14.844  1.00 24.75 ?  88  LEU   A HD23 1 
ATOM   1791 N  N    . ALA   A 1 89  ? 25.765 0.898   15.565  1.00 14.82 ?  89  ALA   A N    1 
ATOM   1792 C  CA   . ALA   A 1 89  ? 26.110 -0.514  15.653  1.00 14.74 ?  89  ALA   A CA   1 
ATOM   1793 C  C    . ALA   A 1 89  ? 27.593 -0.572  15.972  1.00 15.22 ?  89  ALA   A C    1 
ATOM   1794 O  O    . ALA   A 1 89  ? 28.298 0.430   15.863  1.00 15.94 ?  89  ALA   A O    1 
ATOM   1795 C  CB   . ALA   A 1 89  ? 25.847 -1.218  14.323  1.00 14.01 ?  89  ALA   A CB   1 
ATOM   1796 H  H    . ALA   A 1 89  ? 26.450 1.416   15.548  1.00 17.82 ?  89  ALA   A H    1 
ATOM   1797 H  HA   . ALA   A 1 89  ? 25.603 -0.943  16.360  1.00 17.72 ?  89  ALA   A HA   1 
ATOM   1798 H  HB1  . ALA   A 1 89  ? 26.104 -2.151  14.405  1.00 16.85 ?  89  ALA   A HB1  1 
ATOM   1799 H  HB2  . ALA   A 1 89  ? 24.900 -1.156  14.112  1.00 16.85 ?  89  ALA   A HB2  1 
ATOM   1800 H  HB3  . ALA   A 1 89  ? 26.370 -0.791  13.629  1.00 16.85 ?  89  ALA   A HB3  1 
ATOM   1801 N  N    . LYS   A 1 90  ? 28.081 -1.752  16.345  1.00 15.53 ?  90  LYS   A N    1 
ATOM   1802 C  CA   . LYS   A 1 90  ? 29.525 -1.896  16.494  1.00 16.18 ?  90  LYS   A CA   1 
ATOM   1803 C  C    . LYS   A 1 90  ? 30.222 -1.700  15.149  1.00 15.02 ?  90  LYS   A C    1 
ATOM   1804 O  O    . LYS   A 1 90  ? 31.155 -0.890  15.023  1.00 16.71 ?  90  LYS   A O    1 
ATOM   1805 C  CB   . LYS   A 1 90  ? 29.868 -3.255  17.107  1.00 18.73 ?  90  LYS   A CB   1 
ATOM   1806 C  CG   . LYS   A 1 90  ? 31.344 -3.401  17.444  1.00 23.02 ?  90  LYS   A CG   1 
ATOM   1807 C  CD   . LYS   A 1 90  ? 31.596 -4.641  18.287  1.00 27.13 ?  90  LYS   A CD   1 
ATOM   1808 C  CE   . LYS   A 1 90  ? 32.997 -4.647  18.880  1.00 30.15 ?  90  LYS   A CE   1 
ATOM   1809 N  NZ   . LYS   A 1 90  ? 34.044 -4.953  17.870  1.00 32.21 ?  90  LYS   A NZ   1 
ATOM   1810 H  H    . LYS   A 1 90  ? 27.616 -2.453  16.510  1.00 18.68 ?  90  LYS   A H    1 
ATOM   1811 H  HA   . LYS   A 1 90  ? 29.848 -1.209  17.094  1.00 19.45 ?  90  LYS   A HA   1 
ATOM   1812 H  HB2  . LYS   A 1 90  ? 29.359 -3.366  17.928  1.00 22.52 ?  90  LYS   A HB2  1 
ATOM   1813 H  HB3  . LYS   A 1 90  ? 29.632 -3.954  16.478  1.00 22.52 ?  90  LYS   A HB3  1 
ATOM   1814 H  HG2  . LYS   A 1 90  ? 31.854 -3.482  16.624  1.00 27.66 ?  90  LYS   A HG2  1 
ATOM   1815 H  HG3  . LYS   A 1 90  ? 31.636 -2.625  17.949  1.00 27.66 ?  90  LYS   A HG3  1 
ATOM   1816 H  HD2  . LYS   A 1 90  ? 30.957 -4.667  19.018  1.00 32.60 ?  90  LYS   A HD2  1 
ATOM   1817 H  HD3  . LYS   A 1 90  ? 31.498 -5.431  17.732  1.00 32.60 ?  90  LYS   A HD3  1 
ATOM   1818 H  HE2  . LYS   A 1 90  ? 33.187 -3.772  19.254  1.00 36.22 ?  90  LYS   A HE2  1 
ATOM   1819 H  HE3  . LYS   A 1 90  ? 33.044 -5.322  19.576  1.00 36.22 ?  90  LYS   A HE3  1 
ATOM   1820 H  HZ1  . LYS   A 1 90  ? 34.847 -4.951  18.254  1.00 38.69 ?  90  LYS   A HZ1  1 
ATOM   1821 H  HZ2  . LYS   A 1 90  ? 33.897 -5.756  17.514  1.00 38.69 ?  90  LYS   A HZ2  1 
ATOM   1822 H  HZ3  . LYS   A 1 90  ? 34.030 -4.343  17.223  1.00 38.69 ?  90  LYS   A HZ3  1 
ATOM   1823 N  N    . HIS   A 1 91  ? 29.750 -2.411  14.125  1.00 13.24 ?  91  HIS   A N    1 
ATOM   1824 C  CA   . HIS   A 1 91  ? 30.322 -2.383  12.794  1.00 12.95 ?  91  HIS   A CA   1 
ATOM   1825 C  C    . HIS   A 1 91  ? 29.230 -2.103  11.779  1.00 11.60 ?  91  HIS   A C    1 
ATOM   1826 O  O    . HIS   A 1 91  ? 28.064 -2.462  11.981  1.00 12.36 ?  91  HIS   A O    1 
ATOM   1827 C  CB   . HIS   A 1 91  ? 30.926 -3.747  12.418  1.00 15.31 ?  91  HIS   A CB   1 
ATOM   1828 C  CG   . HIS   A 1 91  ? 31.907 -4.278  13.416  1.00 19.49 ?  91  HIS   A CG   1 
ATOM   1829 N  ND1  . HIS   A 1 91  ? 33.185 -3.777  13.542  1.00 21.62 ?  91  HIS   A ND1  1 
ATOM   1830 C  CD2  . HIS   A 1 91  ? 31.804 -5.276  14.326  1.00 21.22 ?  91  HIS   A CD2  1 
ATOM   1831 C  CE1  . HIS   A 1 91  ? 33.825 -4.441  14.488  1.00 22.39 ?  91  HIS   A CE1  1 
ATOM   1832 N  NE2  . HIS   A 1 91  ? 33.009 -5.355  14.981  1.00 22.57 ?  91  HIS   A NE2  1 
ATOM   1833 H  H    . HIS   A 1 91  ? 29.074 -2.953  14.191  1.00 15.92 ?  91  HIS   A H    1 
ATOM   1834 H  HA   . HIS   A 1 91  ? 31.005 -1.705  12.733  1.00 15.57 ?  91  HIS   A HA   1 
ATOM   1835 H  HB2  . HIS   A 1 91  ? 30.211 -4.399  12.337  1.00 18.41 ?  91  HIS   A HB2  1 
ATOM   1836 H  HB3  . HIS   A 1 91  ? 31.387 -3.662  11.568  1.00 18.41 ?  91  HIS   A HB3  1 
ATOM   1837 H  HD1  . HIS   A 1 91  ? 33.516 -3.134  13.074  1.00 25.98 ?  91  HIS   A HD1  1 
ATOM   1838 H  HD2  . HIS   A 1 91  ? 31.060 -5.808  14.480  1.00 25.51 ?  91  HIS   A HD2  1 
ATOM   1839 H  HE1  . HIS   A 1 91  ? 34.703 -4.285  14.763  1.00 26.90 ?  91  HIS   A HE1  1 
ATOM   1840 N  N    . CYS   A 1 92  ? 29.629 -1.507  10.662  1.00 11.19 ?  92  CYS   A N    1 
ATOM   1841 C  CA   . CYS   A 1 92  ? 28.788 -1.427  9.478   1.00 11.11 ?  92  CYS   A CA   1 
ATOM   1842 C  C    . CYS   A 1 92  ? 29.429 -2.245  8.368   1.00 10.57 ?  92  CYS   A C    1 
ATOM   1843 O  O    . CYS   A 1 92  ? 30.586 -1.998  7.999   1.00 11.51 ?  92  CYS   A O    1 
ATOM   1844 C  CB   . CYS   A 1 92  ? 28.573 0.015   9.019   1.00 11.84 ?  92  CYS   A CB   1 
ATOM   1845 S  SG   . CYS   A 1 92  ? 27.550 0.124   7.519   1.00 11.11 ?  92  CYS   A SG   1 
ATOM   1846 H  H    . CYS   A 1 92  ? 30.397 -1.129  10.570  1.00 13.47 ?  92  CYS   A H    1 
ATOM   1847 H  HA   . CYS   A 1 92  ? 27.922 -1.809  9.678   1.00 13.37 ?  92  CYS   A HA   1 
ATOM   1848 H  HB2  . CYS   A 1 92  ? 28.129 0.512   9.723   1.00 14.25 ?  92  CYS   A HB2  1 
ATOM   1849 H  HB3  . CYS   A 1 92  ? 29.435 0.417   8.822   1.00 14.25 ?  92  CYS   A HB3  1 
ATOM   1850 H  HG   . CYS   A 1 92  ? 27.410 1.275   7.223   1.00 13.37 ?  92  CYS   A HG   1 
ATOM   1851 N  N    . LEU   A 1 93  ? 28.691 -3.229  7.866   1.00 10.40 ?  93  LEU   A N    1 
ATOM   1852 C  CA   . LEU   A 1 93  ? 29.087 -3.984  6.685   1.00 10.13 ?  93  LEU   A CA   1 
ATOM   1853 C  C    . LEU   A 1 93  ? 28.489 -3.290  5.468   1.00 9.80  ?  93  LEU   A C    1 
ATOM   1854 O  O    . LEU   A 1 93  ? 27.275 -3.353  5.245   1.00 10.19 ?  93  LEU   A O    1 
ATOM   1855 C  CB   . LEU   A 1 93  ? 28.601 -5.430  6.789   1.00 10.58 ?  93  LEU   A CB   1 
ATOM   1856 C  CG   . LEU   A 1 93  ? 28.990 -6.325  5.615   1.00 10.85 ?  93  LEU   A CG   1 
ATOM   1857 C  CD1  . LEU   A 1 93  ? 30.496 -6.574  5.601   1.00 12.11 ?  93  LEU   A CD1  1 
ATOM   1858 C  CD2  . LEU   A 1 93  ? 28.226 -7.641  5.658   1.00 11.87 ?  93  LEU   A CD2  1 
ATOM   1859 H  H    . LEU   A 1 93  ? 27.936 -3.481  8.202   1.00 12.51 ?  93  LEU   A H    1 
ATOM   1860 H  HA   . LEU   A 1 93  ? 30.049 -3.983  6.609   1.00 12.19 ?  93  LEU   A HA   1 
ATOM   1861 H  HB2  . LEU   A 1 93  ? 28.971 -5.823  7.597   1.00 12.74 ?  93  LEU   A HB2  1 
ATOM   1862 H  HB3  . LEU   A 1 93  ? 27.632 -5.430  6.847   1.00 12.74 ?  93  LEU   A HB3  1 
ATOM   1863 H  HG   . LEU   A 1 93  ? 28.762 -5.881  4.792   1.00 13.05 ?  93  LEU   A HG   1 
ATOM   1864 H  HD11 . LEU   A 1 93  ? 30.714 -7.197  4.889   1.00 14.57 ?  93  LEU   A HD11 1 
ATOM   1865 H  HD12 . LEU   A 1 93  ? 30.962 -5.735  5.458   1.00 14.57 ?  93  LEU   A HD12 1 
ATOM   1866 H  HD13 . LEU   A 1 93  ? 30.770 -6.954  6.458   1.00 14.57 ?  93  LEU   A HD13 1 
ATOM   1867 H  HD21 . LEU   A 1 93  ? 28.502 -8.189  4.903   1.00 14.28 ?  93  LEU   A HD21 1 
ATOM   1868 H  HD22 . LEU   A 1 93  ? 28.430 -8.103  6.487   1.00 14.28 ?  93  LEU   A HD22 1 
ATOM   1869 H  HD23 . LEU   A 1 93  ? 27.277 -7.458  5.604   1.00 14.28 ?  93  LEU   A HD23 1 
ATOM   1870 N  N    . HIS   A 1 94  ? 29.334 -2.591  4.711   1.00 9.91  ?  94  HIS   A N    1 
ATOM   1871 C  CA   . HIS   A 1 94  ? 28.910 -1.917  3.486   1.00 9.93  ?  94  HIS   A CA   1 
ATOM   1872 C  C    . HIS   A 1 94  ? 28.912 -2.945  2.370   1.00 9.99  ?  94  HIS   A C    1 
ATOM   1873 O  O    . HIS   A 1 94  ? 29.976 -3.457  2.016   1.00 11.27 ?  94  HIS   A O    1 
ATOM   1874 C  CB   . HIS   A 1 94  ? 29.863 -0.770  3.152   1.00 10.26 ?  94  HIS   A CB   1 
ATOM   1875 C  CG   . HIS   A 1 94  ? 29.858 0.323   4.167   1.00 10.10 ?  94  HIS   A CG   1 
ATOM   1876 N  ND1  . HIS   A 1 94  ? 28.977 1.381   4.114   1.00 10.16 ?  94  HIS   A ND1  1 
ATOM   1877 C  CD2  . HIS   A 1 94  ? 30.592 0.488   5.289   1.00 10.63 ?  94  HIS   A CD2  1 
ATOM   1878 C  CE1  . HIS   A 1 94  ? 29.191 2.163   5.158   1.00 10.46 ?  94  HIS   A CE1  1 
ATOM   1879 N  NE2  . HIS   A 1 94  ? 30.166 1.645   5.884   1.00 10.57 ?  94  HIS   A NE2  1 
ATOM   1880 H  H    . HIS   A 1 94  ? 30.170 -2.492  4.890   1.00 11.93 ?  94  HIS   A H    1 
ATOM   1881 H  HA   . HIS   A 1 94  ? 28.010 -1.570  3.595   1.00 11.96 ?  94  HIS   A HA   1 
ATOM   1882 H  HB2  . HIS   A 1 94  ? 30.762 -1.117  3.097   1.00 12.35 ?  94  HIS   A HB2  1 
ATOM   1883 H  HB3  . HIS   A 1 94  ? 29.598 -0.384  2.303   1.00 12.35 ?  94  HIS   A HB3  1 
ATOM   1884 H  HD2  . HIS   A 1 94  ? 31.266 -0.070  5.597   1.00 12.80 ?  94  HIS   A HD2  1 
ATOM   1885 H  HE1  . HIS   A 1 94  ? 28.726 2.948   5.348   1.00 12.59 ?  94  HIS   A HE1  1 
ATOM   1886 H  HE2  . HIS   A 1 94  ? 30.478 1.985   6.611   1.00 12.72 ?  94  HIS   A HE2  1 
ATOM   1887 N  N    . VAL   A 1 95  ? 27.739 -3.273  1.831   1.00 9.39  ?  95  VAL   A N    1 
ATOM   1888 C  CA   . VAL   A 1 95  ? 27.596 -4.308  0.807   1.00 9.69  ?  95  VAL   A CA   1 
ATOM   1889 C  C    . VAL   A 1 95  ? 27.049 -3.669  -0.456  1.00 9.51  ?  95  VAL   A C    1 
ATOM   1890 O  O    . VAL   A 1 95  ? 26.046 -2.950  -0.401  1.00 10.42 ?  95  VAL   A O    1 
ATOM   1891 C  CB   . VAL   A 1 95  ? 26.672 -5.456  1.263   1.00 10.25 ?  95  VAL   A CB   1 
ATOM   1892 C  CG1  . VAL   A 1 95  ? 26.572 -6.494  0.165   1.00 11.33 ?  95  VAL   A CG1  1 
ATOM   1893 C  CG2  . VAL   A 1 95  ? 27.183 -6.069  2.548   1.00 10.48 ?  95  VAL   A CG2  1 
ATOM   1894 H  H    . VAL   A 1 95  ? 26.990 -2.905  2.051   1.00 11.31 ?  95  VAL   A H    1 
ATOM   1895 H  HA   . VAL   A 1 95  ? 28.465 -4.680  0.605   1.00 11.66 ?  95  VAL   A HA   1 
ATOM   1896 H  HB   . VAL   A 1 95  ? 25.787 -5.107  1.429   1.00 12.34 ?  95  VAL   A HB   1 
ATOM   1897 H  HG11 . VAL   A 1 95  ? 26.186 -7.309  0.529   1.00 13.64 ?  95  VAL   A HG11 1 
ATOM   1898 H  HG12 . VAL   A 1 95  ? 26.009 -6.157  -0.550  1.00 13.64 ?  95  VAL   A HG12 1 
ATOM   1899 H  HG13 . VAL   A 1 95  ? 27.463 -6.685  -0.180  1.00 13.64 ?  95  VAL   A HG13 1 
ATOM   1900 H  HG21 . VAL   A 1 95  ? 26.633 -6.836  2.773   1.00 12.61 ?  95  VAL   A HG21 1 
ATOM   1901 H  HG22 . VAL   A 1 95  ? 28.104 -6.347  2.424   1.00 12.61 ?  95  VAL   A HG22 1 
ATOM   1902 H  HG23 . VAL   A 1 95  ? 27.130 -5.406  3.255   1.00 12.61 ?  95  VAL   A HG23 1 
ATOM   1903 N  N    . VAL   A 1 96  ? 27.681 -3.950  -1.593  1.00 9.65  ?  96  VAL   A N    1 
ATOM   1904 C  CA   . VAL   A 1 96  ? 27.271 -3.393  -2.877  1.00 10.37 ?  96  VAL   A CA   1 
ATOM   1905 C  C    . VAL   A 1 96  ? 26.457 -4.438  -3.632  1.00 10.66 ?  96  VAL   A C    1 
ATOM   1906 O  O    . VAL   A 1 96  ? 27.013 -5.375  -4.213  1.00 11.43 ?  96  VAL   A O    1 
ATOM   1907 C  CB   . VAL   A 1 96  ? 28.464 -2.920  -3.706  1.00 10.57 ?  96  VAL   A CB   1 
ATOM   1908 C  CG1  . VAL   A 1 96  ? 27.956 -2.291  -4.982  1.00 11.00 ?  96  VAL   A CG1  1 
ATOM   1909 C  CG2  . VAL   A 1 96  ? 29.322 -1.948  -2.912  1.00 11.22 ?  96  VAL   A CG2  1 
ATOM   1910 H  H    . VAL   A 1 96  ? 28.367 -4.471  -1.644  1.00 11.61 ?  96  VAL   A H    1 
ATOM   1911 H  HA   . VAL   A 1 96  ? 26.701 -2.627  -2.716  1.00 12.48 ?  96  VAL   A HA   1 
ATOM   1912 H  HB   . VAL   A 1 96  ? 29.014 -3.681  -3.941  1.00 12.73 ?  96  VAL   A HB   1 
ATOM   1913 H  HG11 . VAL   A 1 96  ? 28.690 -1.812  -5.406  1.00 13.24 ?  96  VAL   A HG11 1 
ATOM   1914 H  HG12 . VAL   A 1 96  ? 27.634 -2.984  -5.573  1.00 13.24 ?  96  VAL   A HG12 1 
ATOM   1915 H  HG13 . VAL   A 1 96  ? 27.244 -1.670  -4.768  1.00 13.24 ?  96  VAL   A HG13 1 
ATOM   1916 H  HG21 . VAL   A 1 96  ? 30.025 -1.604  -3.482  1.00 13.50 ?  96  VAL   A HG21 1 
ATOM   1917 H  HG22 . VAL   A 1 96  ? 28.763 -1.216  -2.598  1.00 13.50 ?  96  VAL   A HG22 1 
ATOM   1918 H  HG23 . VAL   A 1 96  ? 29.708 -2.412  -2.152  1.00 13.50 ?  96  VAL   A HG23 1 
ATOM   1919 N  N    . GLY   A 1 97  ? 25.137 -4.274  -3.648  1.00 10.61 ?  97  GLY   A N    1 
ATOM   1920 C  CA   . GLY   A 1 97  ? 24.313 -5.040  -4.546  1.00 11.31 ?  97  GLY   A CA   1 
ATOM   1921 C  C    . GLY   A 1 97  ? 24.314 -4.400  -5.919  1.00 11.23 ?  97  GLY   A C    1 
ATOM   1922 O  O    . GLY   A 1 97  ? 24.598 -3.204  -6.064  1.00 12.33 ?  97  GLY   A O    1 
ATOM   1923 H  H    . GLY   A 1 97  ? 24.697 -3.722  -3.144  1.00 12.76 ?  97  GLY   A H    1 
ATOM   1924 H  HA2  . GLY   A 1 97  ? 24.664 -5.940  -4.601  1.00 13.61 ?  97  GLY   A HA2  1 
ATOM   1925 H  HA3  . GLY   A 1 97  ? 23.402 -5.076  -4.214  1.00 13.61 ?  97  GLY   A HA3  1 
ATOM   1926 N  N    A PRO   A 1 98  ? 23.967 -5.151  -6.960  0.82 11.24 ?  98  PRO   A N    1 
ATOM   1927 N  N    B PRO   A 1 98  ? 24.037 -5.196  -6.952  0.18 11.75 ?  98  PRO   A N    1 
ATOM   1928 C  CA   A PRO   A 1 98  ? 23.844 -4.535  -8.287  0.82 12.27 ?  98  PRO   A CA   1 
ATOM   1929 C  CA   B PRO   A 1 98  ? 24.006 -4.654  -8.314  0.18 12.40 ?  98  PRO   A CA   1 
ATOM   1930 C  C    A PRO   A 1 98  ? 22.735 -3.490  -8.313  0.82 12.76 ?  98  PRO   A C    1 
ATOM   1931 C  C    B PRO   A 1 98  ? 22.869 -3.662  -8.494  0.18 12.77 ?  98  PRO   A C    1 
ATOM   1932 O  O    A PRO   A 1 98  ? 21.664 -3.672  -7.729  0.82 12.79 ?  98  PRO   A O    1 
ATOM   1933 O  O    B PRO   A 1 98  ? 21.780 -3.820  -7.938  0.18 12.90 ?  98  PRO   A O    1 
ATOM   1934 C  CB   A PRO   A 1 98  ? 23.521 -5.726  -9.199  0.82 12.45 ?  98  PRO   A CB   1 
ATOM   1935 C  CB   B PRO   A 1 98  ? 23.800 -5.900  -9.185  0.18 12.37 ?  98  PRO   A CB   1 
ATOM   1936 C  CG   A PRO   A 1 98  ? 22.878 -6.729  -8.290  0.82 12.67 ?  98  PRO   A CG   1 
ATOM   1937 C  CG   B PRO   A 1 98  ? 23.189 -6.912  -8.267  0.18 12.42 ?  98  PRO   A CG   1 
ATOM   1938 C  CD   A PRO   A 1 98  ? 23.631 -6.588  -6.986  0.82 11.82 ?  98  PRO   A CD   1 
ATOM   1939 C  CD   B PRO   A 1 98  ? 23.824 -6.654  -6.935  0.18 11.90 ?  98  PRO   A CD   1 
ATOM   1940 H  HA   A PRO   A 1 98  ? 24.688 -4.136  -8.556  0.82 14.76 ?  98  PRO   A HA   1 
ATOM   1941 H  HA   B PRO   A 1 98  ? 24.852 -4.233  -8.535  0.18 14.92 ?  98  PRO   A HA   1 
ATOM   1942 H  HB2  A PRO   A 1 98  ? 22.906 -5.446  -9.893  0.82 14.97 ?  98  PRO   A HB2  1 
ATOM   1943 H  HB2  B PRO   A 1 98  ? 23.199 -5.691  -9.917  0.18 14.89 ?  98  PRO   A HB2  1 
ATOM   1944 H  HB3  A PRO   A 1 98  ? 24.338 -6.081  -9.581  0.82 14.97 ?  98  PRO   A HB3  1 
ATOM   1945 H  HB3  B PRO   A 1 98  ? 24.655 -6.212  -9.519  0.18 14.89 ?  98  PRO   A HB3  1 
ATOM   1946 H  HG2  A PRO   A 1 98  ? 21.940 -6.512  -8.174  0.82 15.24 ?  98  PRO   A HG2  1 
ATOM   1947 H  HG2  B PRO   A 1 98  ? 22.228 -6.773  -8.221  0.18 14.94 ?  98  PRO   A HG2  1 
ATOM   1948 H  HG3  A PRO   A 1 98  ? 22.986 -7.620  -8.657  0.82 15.24 ?  98  PRO   A HG3  1 
ATOM   1949 H  HG3  B PRO   A 1 98  ? 23.392 -7.806  -8.581  0.18 14.94 ?  98  PRO   A HG3  1 
ATOM   1950 H  HD2  A PRO   A 1 98  ? 23.054 -6.818  -6.236  0.82 14.22 ?  98  PRO   A HD2  1 
ATOM   1951 H  HD2  B PRO   A 1 98  ? 23.223 -6.907  -6.216  0.18 14.32 ?  98  PRO   A HD2  1 
ATOM   1952 H  HD3  A PRO   A 1 98  ? 24.434 -7.131  -6.994  0.82 14.22 ?  98  PRO   A HD3  1 
ATOM   1953 H  HD3  B PRO   A 1 98  ? 24.674 -7.120  -6.869  0.18 14.32 ?  98  PRO   A HD3  1 
ATOM   1954 N  N    A ASN   A 1 99  ? 23.003 -2.383  -9.000  0.82 13.48 ?  99  ASN   A N    1 
ATOM   1955 N  N    B ASN   A 1 99  ? 23.136 -2.632  -9.288  0.18 13.16 ?  99  ASN   A N    1 
ATOM   1956 C  CA   A ASN   A 1 99  ? 22.025 -1.319  -9.211  0.82 14.54 ?  99  ASN   A CA   1 
ATOM   1957 C  CA   B ASN   A 1 99  ? 22.161 -1.594  -9.593  0.18 13.66 ?  99  ASN   A CA   1 
ATOM   1958 C  C    A ASN   A 1 99  ? 21.459 -1.479  -10.618 0.82 15.63 ?  99  ASN   A C    1 
ATOM   1959 C  C    B ASN   A 1 99  ? 21.509 -1.935  -10.927 0.18 14.06 ?  99  ASN   A C    1 
ATOM   1960 O  O    A ASN   A 1 99  ? 22.152 -1.226  -11.610 0.82 16.76 ?  99  ASN   A O    1 
ATOM   1961 O  O    B ASN   A 1 99  ? 22.166 -1.908  -11.974 0.18 13.32 ?  99  ASN   A O    1 
ATOM   1962 C  CB   A ASN   A 1 99  ? 22.675 0.052   -9.028  0.82 14.60 ?  99  ASN   A CB   1 
ATOM   1963 C  CB   B ASN   A 1 99  ? 22.851 -0.234  -9.655  0.18 13.92 ?  99  ASN   A CB   1 
ATOM   1964 C  CG   A ASN   A 1 99  ? 21.660 1.202   -9.022  0.82 15.09 ?  99  ASN   A CG   1 
ATOM   1965 C  CG   B ASN   A 1 99  ? 21.871 0.913   -9.780  0.18 14.24 ?  99  ASN   A CG   1 
ATOM   1966 O  OD1  A ASN   A 1 99  ? 20.648 1.163   -9.719  0.82 16.16 ?  99  ASN   A OD1  1 
ATOM   1967 O  OD1  B ASN   A 1 99  ? 20.795 0.766   -10.358 0.18 14.42 ?  99  ASN   A OD1  1 
ATOM   1968 N  ND2  A ASN   A 1 99  ? 21.945 2.233   -8.239  0.82 15.30 ?  99  ASN   A ND2  1 
ATOM   1969 N  ND2  B ASN   A 1 99  ? 22.242 2.068   -9.236  0.18 14.29 ?  99  ASN   A ND2  1 
ATOM   1970 H  H    A ASN   A 1 99  ? 23.772 -2.222  -9.351  0.82 16.21 ?  99  ASN   A H    1 
ATOM   1971 H  H    B ASN   A 1 99  ? 23.898 -2.508  -9.664  0.18 15.83 ?  99  ASN   A H    1 
ATOM   1972 H  HA   A ASN   A 1 99  ? 21.305 -1.416  -8.563  0.82 17.49 ?  99  ASN   A HA   1 
ATOM   1973 H  HA   B ASN   A 1 99  ? 21.476 -1.573  -8.903  0.18 16.43 ?  99  ASN   A HA   1 
ATOM   1974 H  HB2  A ASN   A 1 99  ? 23.156 0.064   -8.186  0.82 17.55 ?  99  ASN   A HB2  1 
ATOM   1975 H  HB2  B ASN   A 1 99  ? 23.364 -0.106  -8.844  0.18 16.74 ?  99  ASN   A HB2  1 
ATOM   1976 H  HB3  A ASN   A 1 99  ? 23.295 0.197   -9.763  0.82 17.55 ?  99  ASN   A HB3  1 
ATOM   1977 H  HB3  B ASN   A 1 99  ? 23.436 -0.215  -10.423 0.18 16.74 ?  99  ASN   A HB3  1 
ATOM   1978 H  HD21 A ASN   A 1 99  ? 21.408 2.903   -8.206  0.82 18.39 ?  99  ASN   A HD21 1 
ATOM   1979 H  HD21 B ASN   A 1 99  ? 21.721 2.751   -9.271  0.18 17.19 ?  99  ASN   A HD21 1 
ATOM   1980 H  HD22 A ASN   A 1 99  ? 22.665 2.232   -7.771  0.82 18.39 ?  99  ASN   A HD22 1 
ATOM   1981 H  HD22 B ASN   A 1 99  ? 23.006 2.132   -8.843  0.18 17.19 ?  99  ASN   A HD22 1 
ATOM   1982 N  N    A VAL   A 1 100 ? 20.198 -1.912  -10.696 0.82 16.63 ?  100 VAL   A N    1 
ATOM   1983 N  N    B VAL   A 1 100 ? 20.214 -2.254  -10.887 0.18 15.47 ?  100 VAL   A N    1 
ATOM   1984 C  CA   A VAL   A 1 100 ? 19.558 -2.132  -11.989 0.82 18.77 ?  100 VAL   A CA   1 
ATOM   1985 C  CA   B VAL   A 1 100 ? 19.495 -2.599  -12.110 0.18 17.01 ?  100 VAL   A CA   1 
ATOM   1986 C  C    A VAL   A 1 100 ? 19.459 -0.830  -12.771 0.82 19.50 ?  100 VAL   A C    1 
ATOM   1987 C  C    B VAL   A 1 100 ? 19.483 -1.418  -13.067 0.18 17.76 ?  100 VAL   A C    1 
ATOM   1988 O  O    A VAL   A 1 100 ? 19.529 -0.827  -14.005 0.82 20.60 ?  100 VAL   A O    1 
ATOM   1989 O  O    B VAL   A 1 100 ? 19.578 -1.588  -14.289 0.18 17.76 ?  100 VAL   A O    1 
ATOM   1990 C  CB   A VAL   A 1 100 ? 18.186 -2.812  -11.788 0.82 20.46 ?  100 VAL   A CB   1 
ATOM   1991 C  CB   B VAL   A 1 100 ? 18.071 -3.079  -11.779 0.18 17.89 ?  100 VAL   A CB   1 
ATOM   1992 C  CG1  A VAL   A 1 100 ? 17.447 -2.960  -13.112 0.82 21.03 ?  100 VAL   A CG1  1 
ATOM   1993 C  CG1  B VAL   A 1 100 ? 17.373 -3.577  -13.037 0.18 18.19 ?  100 VAL   A CG1  1 
ATOM   1994 C  CG2  A VAL   A 1 100 ? 18.370 -4.171  -11.131 0.82 20.99 ?  100 VAL   A CG2  1 
ATOM   1995 C  CG2  B VAL   A 1 100 ? 18.114 -4.161  -10.717 0.18 18.25 ?  100 VAL   A CG2  1 
ATOM   1996 H  H    A VAL   A 1 100 ? 19.692 -2.086  -10.013 0.82 20.00 ?  100 VAL   A H    1 
ATOM   1997 H  H    B VAL   A 1 100 ? 19.737 -2.275  -10.173 0.18 18.60 ?  100 VAL   A H    1 
ATOM   1998 H  HA   A VAL   A 1 100 ? 20.105 -2.742  -12.504 0.82 22.56 ?  100 VAL   A HA   1 
ATOM   1999 H  HA   B VAL   A 1 100 ? 19.957 -3.324  -12.555 0.18 20.45 ?  100 VAL   A HA   1 
ATOM   2000 H  HB   A VAL   A 1 100 ? 17.641 -2.268  -11.200 0.82 24.58 ?  100 VAL   A HB   1 
ATOM   2001 H  HB   B VAL   A 1 100 ? 17.559 -2.332  -11.431 0.18 21.51 ?  100 VAL   A HB   1 
ATOM   2002 H  HG11 A VAL   A 1 100 ? 16.686 -3.552  -12.984 0.82 25.28 ?  100 VAL   A HG11 1 
ATOM   2003 H  HG11 B VAL   A 1 100 ? 16.522 -3.968  -12.789 0.18 21.87 ?  100 VAL   A HG11 1 
ATOM   2004 H  HG12 A VAL   A 1 100 ? 17.140 -2.089  -13.405 0.82 25.28 ?  100 VAL   A HG12 1 
ATOM   2005 H  HG12 B VAL   A 1 100 ? 17.230 -2.829  -13.639 0.18 21.87 ?  100 VAL   A HG12 1 
ATOM   2006 H  HG13 A VAL   A 1 100 ? 18.050 -3.341  -13.770 0.82 25.28 ?  100 VAL   A HG13 1 
ATOM   2007 H  HG13 B VAL   A 1 100 ? 17.933 -4.244  -13.464 0.18 21.87 ?  100 VAL   A HG13 1 
ATOM   2008 H  HG21 A VAL   A 1 100 ? 17.508 -4.612  -11.066 0.82 25.23 ?  100 VAL   A HG21 1 
ATOM   2009 H  HG21 B VAL   A 1 100 ? 17.249 -4.594  -10.675 0.18 21.94 ?  100 VAL   A HG21 1 
ATOM   2010 H  HG22 A VAL   A 1 100 ? 18.973 -4.705  -11.673 0.82 25.23 ?  100 VAL   A HG22 1 
ATOM   2011 H  HG22 B VAL   A 1 100 ? 18.798 -4.805  -10.955 0.18 21.94 ?  100 VAL   A HG22 1 
ATOM   2012 H  HG23 A VAL   A 1 100 ? 18.745 -4.046  -10.245 0.82 25.23 ?  100 VAL   A HG23 1 
ATOM   2013 H  HG23 B VAL   A 1 100 ? 18.325 -3.755  -9.862  0.18 21.94 ?  100 VAL   A HG23 1 
ATOM   2014 N  N    A ASN   A 1 101 ? 19.310 0.295   -12.078 0.82 20.85 ?  101 ASN   A N    1 
ATOM   2015 N  N    B ASN   A 1 101 ? 19.361 -0.201  -12.528 0.18 18.46 ?  101 ASN   A N    1 
ATOM   2016 C  CA   A ASN   A 1 101 ? 19.271 1.576   -12.773 0.82 22.65 ?  101 ASN   A CA   1 
ATOM   2017 C  CA   B ASN   A 1 101 ? 19.340 0.989   -13.372 0.18 19.14 ?  101 ASN   A CA   1 
ATOM   2018 C  C    A ASN   A 1 101 ? 20.636 1.998   -13.323 0.82 24.66 ?  101 ASN   A C    1 
ATOM   2019 C  C    B ASN   A 1 101 ? 20.680 1.205   -14.061 0.18 20.03 ?  101 ASN   A C    1 
ATOM   2020 O  O    A ASN   A 1 101 ? 20.730 3.063   -13.948 0.82 26.38 ?  101 ASN   A O    1 
ATOM   2021 O  O    B ASN   A 1 101 ? 20.722 1.727   -15.182 0.18 19.85 ?  101 ASN   A O    1 
ATOM   2022 C  CB   A ASN   A 1 101 ? 18.652 2.630   -11.854 0.82 22.42 ?  101 ASN   A CB   1 
ATOM   2023 C  CB   B ASN   A 1 101 ? 18.949 2.210   -12.537 0.18 18.96 ?  101 ASN   A CB   1 
ATOM   2024 C  CG   A ASN   A 1 101 ? 17.283 2.204   -11.330 0.82 21.86 ?  101 ASN   A CG   1 
ATOM   2025 C  CG   B ASN   A 1 101 ? 17.742 1.947   -11.653 0.18 18.93 ?  101 ASN   A CG   1 
ATOM   2026 O  OD1  A ASN   A 1 101 ? 16.441 1.712   -12.086 0.82 22.65 ?  101 ASN   A OD1  1 
ATOM   2027 O  OD1  B ASN   A 1 101 ? 16.770 1.318   -12.075 0.18 19.17 ?  101 ASN   A OD1  1 
ATOM   2028 N  ND2  A ASN   A 1 101 ? 17.063 2.376   -10.033 0.82 21.26 ?  101 ASN   A ND2  1 
ATOM   2029 N  ND2  B ASN   A 1 101 ? 17.805 2.414   -10.412 0.18 18.81 ?  101 ASN   A ND2  1 
ATOM   2030 H  H    A ASN   A 1 101 ? 19.222 0.342   -11.224 0.82 25.05 ?  101 ASN   A H    1 
ATOM   2031 H  H    B ASN   A 1 101 ? 19.293 -0.038  -11.685 0.18 22.19 ?  101 ASN   A H    1 
ATOM   2032 H  HA   A ASN   A 1 101 ? 18.679 1.482   -13.533 0.82 27.21 ?  101 ASN   A HA   1 
ATOM   2033 H  HA   B ASN   A 1 101 ? 18.670 0.880   -14.061 0.18 23.00 ?  101 ASN   A HA   1 
ATOM   2034 H  HB2  A ASN   A 1 101 ? 19.235 2.777   -11.096 0.82 26.94 ?  101 ASN   A HB2  1 
ATOM   2035 H  HB2  B ASN   A 1 101 ? 19.690 2.460   -11.963 0.18 22.80 ?  101 ASN   A HB2  1 
ATOM   2036 H  HB3  A ASN   A 1 101 ? 18.540 3.457   -12.355 0.82 26.94 ?  101 ASN   A HB3  1 
ATOM   2037 H  HB3  B ASN   A 1 101 ? 18.726 2.948   -13.130 0.18 22.80 ?  101 ASN   A HB3  1 
ATOM   2038 H  HD21 A ASN   A 1 101 ? 16.306 2.150   -9.695  0.82 25.55 ?  101 ASN   A HD21 1 
ATOM   2039 H  HD21 B ASN   A 1 101 ? 17.148 2.288   -9.872  0.18 22.61 ?  101 ASN   A HD21 1 
ATOM   2040 H  HD22 A ASN   A 1 101 ? 17.672 2.721   -9.536  0.82 25.55 ?  101 ASN   A HD22 1 
ATOM   2041 H  HD22 B ASN   A 1 101 ? 18.500 2.847   -10.149 0.18 22.61 ?  101 ASN   A HD22 1 
ATOM   2042 N  N    A LYS   A 1 102 ? 21.677 1.180   -13.126 0.82 26.60 ?  102 LYS   A N    1 
ATOM   2043 N  N    B LYS   A 1 102 ? 21.778 0.809   -13.417 0.18 21.26 ?  102 LYS   A N    1 
ATOM   2044 C  CA   A LYS   A 1 102 ? 22.966 1.345   -13.786 0.82 27.84 ?  102 LYS   A CA   1 
ATOM   2045 C  CA   B LYS   A 1 102 ? 23.094 0.851   -14.040 0.18 22.26 ?  102 LYS   A CA   1 
ATOM   2046 C  C    A LYS   A 1 102 ? 23.265 0.229   -14.780 0.82 28.08 ?  102 LYS   A C    1 
ATOM   2047 C  C    B LYS   A 1 102 ? 23.334 -0.329  -14.973 0.18 22.58 ?  102 LYS   A C    1 
ATOM   2048 O  O    A LYS   A 1 102 ? 24.342 0.230   -15.384 0.82 28.77 ?  102 LYS   A O    1 
ATOM   2049 O  O    B LYS   A 1 102 ? 24.430 -0.443  -15.532 0.18 22.58 ?  102 LYS   A O    1 
ATOM   2050 C  CB   A LYS   A 1 102 ? 24.098 1.406   -12.751 0.82 29.21 ?  102 LYS   A CB   1 
ATOM   2051 C  CB   B LYS   A 1 102 ? 24.191 0.864   -12.971 0.18 22.95 ?  102 LYS   A CB   1 
ATOM   2052 C  CG   A LYS   A 1 102 ? 23.993 2.554   -11.764 0.82 30.48 ?  102 LYS   A CG   1 
ATOM   2053 C  CG   B LYS   A 1 102 ? 24.262 2.136   -12.139 0.18 23.57 ?  102 LYS   A CG   1 
ATOM   2054 C  CD   A LYS   A 1 102 ? 25.142 2.525   -10.763 0.82 31.80 ?  102 LYS   A CD   1 
ATOM   2055 C  CD   B LYS   A 1 102 ? 25.382 2.047   -11.107 0.18 24.23 ?  102 LYS   A CD   1 
ATOM   2056 C  CE   A LYS   A 1 102 ? 25.056 3.687   -9.784  0.82 32.91 ?  102 LYS   A CE   1 
ATOM   2057 C  CE   B LYS   A 1 102 ? 25.534 3.341   -10.323 0.18 24.80 ?  102 LYS   A CE   1 
ATOM   2058 N  NZ   A LYS   A 1 102 ? 26.140 3.645   -8.760  0.82 33.46 ?  102 LYS   A NZ   1 
ATOM   2059 N  NZ   B LYS   A 1 102 ? 26.613 3.246   -9.298  0.18 25.13 ?  102 LYS   A NZ   1 
ATOM   2060 H  H    A LYS   A 1 102 ? 21.657 0.497   -12.601 0.82 31.96 ?  102 LYS   A H    1 
ATOM   2061 H  H    B LYS   A 1 102 ? 21.781 0.503   -12.614 0.18 25.55 ?  102 LYS   A H    1 
ATOM   2062 H  HA   A LYS   A 1 102 ? 22.965 2.183   -14.270 0.82 33.45 ?  102 LYS   A HA   1 
ATOM   2063 H  HA   B LYS   A 1 102 ? 23.171 1.671   -14.552 0.18 26.75 ?  102 LYS   A HA   1 
ATOM   2064 H  HB2  A LYS   A 1 102 ? 24.097 0.581   -12.242 0.82 35.09 ?  102 LYS   A HB2  1 
ATOM   2065 H  HB2  B LYS   A 1 102 ? 24.045 0.118   -12.370 0.18 27.58 ?  102 LYS   A HB2  1 
ATOM   2066 H  HB3  A LYS   A 1 102 ? 24.942 1.499   -13.220 0.82 35.09 ?  102 LYS   A HB3  1 
ATOM   2067 H  HB3  B LYS   A 1 102 ? 25.047 0.759   -13.410 0.18 27.58 ?  102 LYS   A HB3  1 
ATOM   2068 H  HG2  A LYS   A 1 102 ? 24.029 3.395   -12.246 0.82 36.62 ?  102 LYS   A HG2  1 
ATOM   2069 H  HG2  B LYS   A 1 102 ? 24.443 2.892   -12.720 0.18 28.32 ?  102 LYS   A HG2  1 
ATOM   2070 H  HG3  A LYS   A 1 102 ? 23.159 2.480   -11.275 0.82 36.62 ?  102 LYS   A HG3  1 
ATOM   2071 H  HG3  B LYS   A 1 102 ? 23.424 2.265   -11.669 0.18 28.32 ?  102 LYS   A HG3  1 
ATOM   2072 H  HD2  A LYS   A 1 102 ? 25.106 1.697   -10.258 0.82 38.20 ?  102 LYS   A HD2  1 
ATOM   2073 H  HD2  B LYS   A 1 102 ? 25.183 1.334   -10.480 0.18 29.11 ?  102 LYS   A HD2  1 
ATOM   2074 H  HD3  A LYS   A 1 102 ? 25.984 2.590   -11.241 0.82 38.20 ?  102 LYS   A HD3  1 
ATOM   2075 H  HD3  B LYS   A 1 102 ? 26.221 1.868   -11.561 0.18 29.11 ?  102 LYS   A HD3  1 
ATOM   2076 H  HE2  A LYS   A 1 102 ? 25.134 4.521   -10.274 0.82 39.53 ?  102 LYS   A HE2  1 
ATOM   2077 H  HE2  B LYS   A 1 102 ? 25.759 4.060   -10.934 0.18 29.79 ?  102 LYS   A HE2  1 
ATOM   2078 H  HE3  A LYS   A 1 102 ? 24.203 3.651   -9.324  0.82 39.53 ?  102 LYS   A HE3  1 
ATOM   2079 H  HE3  B LYS   A 1 102 ? 24.700 3.537   -9.868  0.18 29.79 ?  102 LYS   A HE3  1 
ATOM   2080 H  HZ1  A LYS   A 1 102 ? 26.061 4.336   -8.205  0.82 40.19 ?  102 LYS   A HZ1  1 
ATOM   2081 H  HZ1  B LYS   A 1 102 ? 26.680 4.015   -8.855  0.18 30.20 ?  102 LYS   A HZ1  1 
ATOM   2082 H  HZ2  A LYS   A 1 102 ? 26.086 2.890   -8.291  0.82 40.19 ?  102 LYS   A HZ2  1 
ATOM   2083 H  HZ2  B LYS   A 1 102 ? 26.427 2.595   -8.721  0.18 30.20 ?  102 LYS   A HZ2  1 
ATOM   2084 H  HZ3  A LYS   A 1 102 ? 26.935 3.683   -9.158  0.82 40.19 ?  102 LYS   A HZ3  1 
ATOM   2085 H  HZ3  B LYS   A 1 102 ? 27.392 3.070   -9.692  0.18 30.20 ?  102 LYS   A HZ3  1 
ATOM   2086 N  N    A GLY   A 1 103 ? 22.356 -0.730  -14.951 0.82 28.08 ?  103 GLY   A N    1 
ATOM   2087 N  N    B GLY   A 1 103 ? 22.350 -1.208  -15.145 0.18 22.85 ?  103 GLY   A N    1 
ATOM   2088 C  CA   A GLY   A 1 103 ? 22.561 -1.826  -15.880 0.82 27.89 ?  103 GLY   A CA   1 
ATOM   2089 C  CA   B GLY   A 1 103 ? 22.538 -2.388  -15.964 0.18 23.04 ?  103 GLY   A CA   1 
ATOM   2090 C  C    A GLY   A 1 103 ? 23.373 -2.986  -15.349 0.82 27.74 ?  103 GLY   A C    1 
ATOM   2091 C  C    B GLY   A 1 103 ? 23.422 -3.444  -15.345 0.18 23.10 ?  103 GLY   A C    1 
ATOM   2092 O  O    A GLY   A 1 103 ? 23.866 -3.793  -16.142 0.82 28.97 ?  103 GLY   A O    1 
ATOM   2093 O  O    B GLY   A 1 103 ? 23.937 -4.306  -16.062 0.18 23.21 ?  103 GLY   A O    1 
ATOM   2094 H  H    A GLY   A 1 103 ? 21.609 -0.764  -14.537 0.82 33.74 ?  103 GLY   A H    1 
ATOM   2095 H  H    B GLY   A 1 103 ? 21.567 -1.140  -14.797 0.18 27.46 ?  103 GLY   A H    1 
ATOM   2096 H  HA2  A GLY   A 1 103 ? 21.693 -2.164  -16.160 0.82 33.51 ?  103 GLY   A HA2  1 
ATOM   2097 H  HA2  B GLY   A 1 103 ? 21.675 -2.787  -16.145 0.18 27.68 ?  103 GLY   A HA2  1 
ATOM   2098 H  HA3  A GLY   A 1 103 ? 23.013 -1.490  -16.671 0.82 33.51 ?  103 GLY   A HA3  1 
ATOM   2099 H  HA3  B GLY   A 1 103 ? 22.933 -2.125  -16.810 0.18 27.68 ?  103 GLY   A HA3  1 
ATOM   2100 N  N    A GLU   A 1 104 ? 23.520 -3.107  -14.033 0.82 25.51 ?  104 GLU   A N    1 
ATOM   2101 N  N    B GLU   A 1 104 ? 23.603 -3.413  -14.028 0.18 22.92 ?  104 GLU   A N    1 
ATOM   2102 C  CA   A GLU   A 1 104 ? 24.402 -4.111  -13.455 0.82 23.56 ?  104 GLU   A CA   1 
ATOM   2103 C  CA   B GLU   A 1 104 ? 24.524 -4.327  -13.370 0.18 22.75 ?  104 GLU   A CA   1 
ATOM   2104 C  C    A GLU   A 1 104 ? 23.717 -5.473  -13.351 0.82 23.67 ?  104 GLU   A C    1 
ATOM   2105 C  C    B GLU   A 1 104 ? 23.872 -5.693  -13.177 0.18 23.19 ?  104 GLU   A C    1 
ATOM   2106 O  O    A GLU   A 1 104 ? 22.494 -5.576  -13.212 0.82 24.11 ?  104 GLU   A O    1 
ATOM   2107 O  O    B GLU   A 1 104 ? 22.709 -5.796  -12.774 0.18 22.90 ?  104 GLU   A O    1 
ATOM   2108 C  CB   A GLU   A 1 104 ? 24.926 -3.627  -12.098 0.82 21.58 ?  104 GLU   A CB   1 
ATOM   2109 C  CB   B GLU   A 1 104 ? 24.985 -3.734  -12.038 0.18 22.32 ?  104 GLU   A CB   1 
ATOM   2110 C  CG   A GLU   A 1 104 ? 25.875 -2.434  -12.264 0.82 21.18 ?  104 GLU   A CG   1 
ATOM   2111 C  CG   B GLU   A 1 104 ? 25.783 -2.444  -12.218 0.18 22.12 ?  104 GLU   A CG   1 
ATOM   2112 C  CD   A GLU   A 1 104 ? 26.198 -1.662  -10.991 0.82 20.16 ?  104 GLU   A CD   1 
ATOM   2113 C  CD   B GLU   A 1 104 ? 26.137 -1.769  -10.906 0.18 21.95 ?  104 GLU   A CD   1 
ATOM   2114 O  OE1  A GLU   A 1 104 ? 25.608 -1.927  -9.924  0.82 18.63 ?  104 GLU   A OE1  1 
ATOM   2115 O  OE1  B GLU   A 1 104 ? 25.630 -2.199  -9.849  0.18 21.80 ?  104 GLU   A OE1  1 
ATOM   2116 O  OE2  A GLU   A 1 104 ? 27.058 -0.757  -11.083 0.82 20.95 -1 104 GLU   A OE2  1 
ATOM   2117 O  OE2  B GLU   A 1 104 ? 26.924 -0.800  -10.934 0.18 22.15 -1 104 GLU   A OE2  1 
ATOM   2118 H  H    A GLU   A 1 104 ? 23.124 -2.611  -13.455 0.82 30.65 ?  104 GLU   A H    1 
ATOM   2119 H  H    B GLU   A 1 104 ? 23.199 -2.875  -13.492 0.18 27.54 ?  104 GLU   A H    1 
ATOM   2120 H  HA   A GLU   A 1 104 ? 25.166 -4.216  -14.041 0.82 28.31 ?  104 GLU   A HA   1 
ATOM   2121 H  HA   B GLU   A 1 104 ? 25.309 -4.443  -13.927 0.18 27.34 ?  104 GLU   A HA   1 
ATOM   2122 H  HB2  A GLU   A 1 104 ? 24.177 -3.353  -11.549 0.82 25.94 ?  104 GLU   A HB2  1 
ATOM   2123 H  HB2  B GLU   A 1 104 ? 24.211 -3.529  -11.491 0.18 26.82 ?  104 GLU   A HB2  1 
ATOM   2124 H  HB3  A GLU   A 1 104 ? 25.412 -4.350  -11.672 0.82 25.94 ?  104 GLU   A HB3  1 
ATOM   2125 H  HB3  B GLU   A 1 104 ? 25.556 -4.372  -11.579 0.18 26.82 ?  104 GLU   A HB3  1 
ATOM   2126 H  HG2  A GLU   A 1 104 ? 26.712 -2.759  -12.626 0.82 25.45 ?  104 GLU   A HG2  1 
ATOM   2127 H  HG2  B GLU   A 1 104 ? 26.610 -2.646  -12.686 0.18 26.59 ?  104 GLU   A HG2  1 
ATOM   2128 H  HG3  A GLU   A 1 104 ? 25.471 -1.807  -12.883 0.82 25.45 ?  104 GLU   A HG3  1 
ATOM   2129 H  HG3  B GLU   A 1 104 ? 25.257 -1.818  -12.743 0.18 26.59 ?  104 GLU   A HG3  1 
ATOM   2130 N  N    A ASP   A 1 105 ? 24.533 -6.524  -13.416 0.82 24.44 ?  105 ASP   A N    1 
ATOM   2131 N  N    B ASP   A 1 105 ? 24.636 -6.739  -13.484 0.18 24.01 ?  105 ASP   A N    1 
ATOM   2132 C  CA   A ASP   A 1 105 ? 24.046 -7.892  -13.552 0.82 25.57 ?  105 ASP   A CA   1 
ATOM   2133 C  CA   B ASP   A 1 105 ? 24.142 -8.111  -13.502 0.18 24.85 ?  105 ASP   A CA   1 
ATOM   2134 C  C    A ASP   A 1 105 ? 23.366 -8.346  -12.265 0.82 23.41 ?  105 ASP   A C    1 
ATOM   2135 C  C    B ASP   A 1 105 ? 23.431 -8.459  -12.201 0.18 24.57 ?  105 ASP   A C    1 
ATOM   2136 O  O    A ASP   A 1 105 ? 24.000 -8.410  -11.209 0.82 21.23 ?  105 ASP   A O    1 
ATOM   2137 O  O    B ASP   A 1 105 ? 24.038 -8.447  -11.126 0.18 24.29 ?  105 ASP   A O    1 
ATOM   2138 C  CB   A ASP   A 1 105 ? 25.228 -8.801  -13.879 0.82 28.75 ?  105 ASP   A CB   1 
ATOM   2139 C  CB   B ASP   A 1 105 ? 25.340 -9.041  -13.716 0.18 25.94 ?  105 ASP   A CB   1 
ATOM   2140 C  CG   A ASP   A 1 105 ? 24.813 -10.227 -14.147 0.82 31.75 ?  105 ASP   A CG   1 
ATOM   2141 C  CG   B ASP   A 1 105 ? 24.937 -10.494 -13.872 0.18 26.90 ?  105 ASP   A CG   1 
ATOM   2142 O  OD1  A ASP   A 1 105 ? 23.597 -10.474 -14.278 0.82 32.43 ?  105 ASP   A OD1  1 
ATOM   2143 O  OD1  B ASP   A 1 105 ? 23.723 -10.779 -13.945 0.18 27.09 ?  105 ASP   A OD1  1 
ATOM   2144 O  OD2  A ASP   A 1 105 ? 25.709 -11.096 -14.230 0.82 33.47 -1 105 ASP   A OD2  1 
ATOM   2145 O  OD2  B ASP   A 1 105 ? 25.842 -11.355 -13.916 0.18 27.45 -1 105 ASP   A OD2  1 
ATOM   2146 H  H    A ASP   A 1 105 ? 25.391 -6.468  -13.377 0.82 29.36 ?  105 ASP   A H    1 
ATOM   2147 H  H    B ASP   A 1 105 ? 25.465 -6.676  -13.691 0.18 28.85 ?  105 ASP   A H    1 
ATOM   2148 H  HA   A ASP   A 1 105 ? 23.405 -7.945  -14.276 0.82 30.72 ?  105 ASP   A HA   1 
ATOM   2149 H  HA   B ASP   A 1 105 ? 23.519 -8.229  -14.237 0.18 29.86 ?  105 ASP   A HA   1 
ATOM   2150 H  HB2  A ASP   A 1 105 ? 25.676 -8.466  -14.673 0.82 34.53 ?  105 ASP   A HB2  1 
ATOM   2151 H  HB2  B ASP   A 1 105 ? 25.813 -8.762  -14.519 0.18 31.16 ?  105 ASP   A HB2  1 
ATOM   2152 H  HB3  A ASP   A 1 105 ? 25.845 -8.805  -13.130 0.82 34.53 ?  105 ASP   A HB3  1 
ATOM   2153 H  HB3  B ASP   A 1 105 ? 25.931 -8.978  -12.949 0.18 31.16 ?  105 ASP   A HB3  1 
ATOM   2154 N  N    A ILE   A 1 106 ? 22.077 -8.684  -12.358 0.82 23.36 ?  106 ILE   A N    1 
ATOM   2155 N  N    B ILE   A 1 106 ? 22.136 -8.775  -12.303 0.18 24.54 ?  106 ILE   A N    1 
ATOM   2156 C  CA   A ILE   A 1 106 ? 21.320 -9.088  -11.178 0.82 22.77 ?  106 ILE   A CA   1 
ATOM   2157 C  CA   B ILE   A 1 106 ? 21.370 -9.157  -11.122 0.18 24.47 ?  106 ILE   A CA   1 
ATOM   2158 C  C    A ILE   A 1 106 ? 21.867 -10.366 -10.567 0.82 21.84 ?  106 ILE   A C    1 
ATOM   2159 C  C    B ILE   A 1 106 ? 21.881 -10.461 -10.525 0.18 24.04 ?  106 ILE   A C    1 
ATOM   2160 O  O    A ILE   A 1 106 ? 21.657 -10.612 -9.375  0.82 21.18 ?  106 ILE   A O    1 
ATOM   2161 O  O    B ILE   A 1 106 ? 21.660 -10.721 -9.337  0.18 23.96 ?  106 ILE   A O    1 
ATOM   2162 C  CB   A ILE   A 1 106 ? 19.812 -9.201  -11.504 0.82 24.15 ?  106 ILE   A CB   1 
ATOM   2163 C  CB   B ILE   A 1 106 ? 19.856 -9.210  -11.426 0.18 24.98 ?  106 ILE   A CB   1 
ATOM   2164 C  CG1  A ILE   A 1 106 ? 18.979 -9.283  -10.222 0.82 24.85 ?  106 ILE   A CG1  1 
ATOM   2165 C  CG1  B ILE   A 1 106 ? 19.040 -9.229  -10.128 0.18 25.25 ?  106 ILE   A CG1  1 
ATOM   2166 C  CG2  A ILE   A 1 106 ? 19.539 -10.414 -12.377 0.82 24.62 ?  106 ILE   A CG2  1 
ATOM   2167 C  CG2  B ILE   A 1 106 ? 19.515 -10.431 -12.268 0.18 25.17 ?  106 ILE   A CG2  1 
ATOM   2168 C  CD1  A ILE   A 1 106 ? 19.077 -8.056  -9.342  0.82 25.16 ?  106 ILE   A CD1  1 
ATOM   2169 C  CD1  B ILE   A 1 106 ? 19.287 -8.033  -9.230  0.18 25.32 ?  106 ILE   A CD1  1 
ATOM   2170 H  H    A ILE   A 1 106 ? 21.626 -8.684  -13.085 0.82 28.07 ?  106 ILE   A H    1 
ATOM   2171 H  H    B ILE   A 1 106 ? 21.687 -8.771  -13.032 0.18 29.48 ?  106 ILE   A H    1 
ATOM   2172 H  HA   A ILE   A 1 106 ? 21.424 -8.402  -10.508 0.82 27.36 ?  106 ILE   A HA   1 
ATOM   2173 H  HA   B ILE   A 1 106 ? 21.510 -8.476  -10.452 0.18 29.40 ?  106 ILE   A HA   1 
ATOM   2174 H  HB   A ILE   A 1 106 ? 19.546 -8.407  -11.991 0.82 29.02 ?  106 ILE   A HB   1 
ATOM   2175 H  HB   B ILE   A 1 106 ? 19.612 -8.417  -11.927 0.18 30.02 ?  106 ILE   A HB   1 
ATOM   2176 H  HG12 A ILE   A 1 106 ? 18.047 -9.396  -10.463 0.82 29.86 ?  106 ILE   A HG12 1 
ATOM   2177 H  HG12 B ILE   A 1 106 ? 18.094 -9.237  -10.349 0.18 30.34 ?  106 ILE   A HG12 1 
ATOM   2178 H  HG13 A ILE   A 1 106 ? 19.276 -10.045 -9.701  0.82 29.86 ?  106 ILE   A HG13 1 
ATOM   2179 H  HG13 B ILE   A 1 106 ? 19.264 -10.027 -9.625  0.18 30.34 ?  106 ILE   A HG13 1 
ATOM   2180 H  HG21 A ILE   A 1 106 ? 18.642 -10.345 -12.737 0.82 29.58 ?  106 ILE   A HG21 1 
ATOM   2181 H  HG21 B ILE   A 1 106 ? 18.617 -10.329 -12.623 0.18 30.24 ?  106 ILE   A HG21 1 
ATOM   2182 H  HG22 A ILE   A 1 106 ? 20.187 -10.433 -13.097 0.82 29.58 ?  106 ILE   A HG22 1 
ATOM   2183 H  HG22 B ILE   A 1 106 ? 20.152 -10.499 -12.994 0.18 30.24 ?  106 ILE   A HG22 1 
ATOM   2184 H  HG23 A ILE   A 1 106 ? 19.618 -11.216 -11.837 0.82 29.58 ?  106 ILE   A HG23 1 
ATOM   2185 H  HG23 B ILE   A 1 106 ? 19.559 -11.224 -11.711 0.18 30.24 ?  106 ILE   A HG23 1 
ATOM   2186 H  HD11 A ILE   A 1 106 ? 18.358 -8.075  -8.694  0.82 30.24 ?  106 ILE   A HD11 1 
ATOM   2187 H  HD11 B ILE   A 1 106 ? 18.549 -7.949  -8.608  0.18 30.42 ?  106 ILE   A HD11 1 
ATOM   2188 H  HD12 A ILE   A 1 106 ? 19.934 -8.062  -8.884  0.82 30.24 ?  106 ILE   A HD12 1 
ATOM   2189 H  HD12 B ILE   A 1 106 ? 20.116 -8.169  -8.744  0.18 30.42 ?  106 ILE   A HD12 1 
ATOM   2190 H  HD13 A ILE   A 1 106 ? 19.003 -7.264  -9.896  0.82 30.24 ?  106 ILE   A HD13 1 
ATOM   2191 H  HD13 B ILE   A 1 106 ? 19.350 -7.236  -9.779  0.18 30.42 ?  106 ILE   A HD13 1 
ATOM   2192 N  N    A GLN   A 1 107 ? 22.580 -11.185 -11.354 0.82 22.41 ?  107 GLN   A N    1 
ATOM   2193 N  N    B GLN   A 1 107 ? 22.566 -11.288 -11.319 0.18 23.79 ?  107 GLN   A N    1 
ATOM   2194 C  CA   A GLN   A 1 107 ? 23.193 -12.395 -10.813 0.82 24.38 ?  107 GLN   A CA   1 
ATOM   2195 C  CA   B GLN   A 1 107 ? 23.219 -12.470 -10.769 0.18 23.70 ?  107 GLN   A CA   1 
ATOM   2196 C  C    A GLN   A 1 107 ? 24.166 -12.065 -9.691  0.82 21.95 ?  107 GLN   A C    1 
ATOM   2197 C  C    B GLN   A 1 107 ? 24.256 -12.104 -9.716  0.18 21.24 ?  107 GLN   A C    1 
ATOM   2198 O  O    A GLN   A 1 107 ? 24.395 -12.891 -8.800  0.82 23.24 ?  107 GLN   A O    1 
ATOM   2199 O  O    B GLN   A 1 107 ? 24.629 -12.960 -8.906  0.18 21.70 ?  107 GLN   A O    1 
ATOM   2200 C  CB   A GLN   A 1 107 ? 23.902 -13.169 -11.930 0.82 28.73 ?  107 GLN   A CB   1 
ATOM   2201 C  CB   B GLN   A 1 107 ? 23.870 -13.285 -11.889 0.18 25.95 ?  107 GLN   A CB   1 
ATOM   2202 C  CG   A GLN   A 1 107 ? 23.051 -13.374 -13.179 0.82 33.31 ?  107 GLN   A CG   1 
ATOM   2203 C  CG   B GLN   A 1 107 ? 22.877 -13.922 -12.847 0.18 28.06 ?  107 GLN   A CG   1 
ATOM   2204 C  CD   A GLN   A 1 107 ? 21.758 -14.111 -12.891 0.82 36.86 ?  107 GLN   A CD   1 
ATOM   2205 C  CD   B GLN   A 1 107 ? 22.010 -14.968 -12.174 0.18 29.86 ?  107 GLN   A CD   1 
ATOM   2206 O  OE1  A GLN   A 1 107 ? 21.756 -15.151 -12.231 0.82 38.31 ?  107 GLN   A OE1  1 
ATOM   2207 O  OE1  B GLN   A 1 107 ? 22.468 -15.697 -11.294 0.18 30.39 ?  107 GLN   A OE1  1 
ATOM   2208 N  NE2  A GLN   A 1 107 ? 20.647 -13.571 -13.379 0.82 38.03 ?  107 GLN   A NE2  1 
ATOM   2209 N  NE2  B GLN   A 1 107 ? 20.748 -15.041 -12.580 0.18 30.43 ?  107 GLN   A NE2  1 
ATOM   2210 H  H    A GLN   A 1 107 ? 22.727 -11.057 -12.190 0.82 26.92 ?  107 GLN   A H    1 
ATOM   2211 H  H    B GLN   A 1 107 ? 22.662 -11.187 -12.168 0.18 28.59 ?  107 GLN   A H    1 
ATOM   2212 H  HA   A GLN   A 1 107 ? 22.507 -12.971 -10.451 0.82 29.29 ?  107 GLN   A HA   1 
ATOM   2213 H  HA   B GLN   A 1 107 ? 22.549 -13.029 -10.346 0.18 28.48 ?  107 GLN   A HA   1 
ATOM   2214 H  HB2  A GLN   A 1 107 ? 24.702 -12.686 -12.193 0.82 34.52 ?  107 GLN   A HB2  1 
ATOM   2215 H  HB2  B GLN   A 1 107 ? 24.449 -12.705 -12.407 0.18 31.18 ?  107 GLN   A HB2  1 
ATOM   2216 H  HB3  A GLN   A 1 107 ? 24.148 -14.050 -11.599 0.82 34.52 ?  107 GLN   A HB3  1 
ATOM   2217 H  HB3  B GLN   A 1 107 ? 24.393 -14.000 -11.493 0.18 31.18 ?  107 GLN   A HB3  1 
ATOM   2218 H  HG2  A GLN   A 1 107 ? 22.826 -12.510 -13.558 0.82 40.01 ?  107 GLN   A HG2  1 
ATOM   2219 H  HG2  B GLN   A 1 107 ? 22.295 -13.233 -13.204 0.18 33.70 ?  107 GLN   A HG2  1 
ATOM   2220 H  HG3  A GLN   A 1 107 ? 23.559 -13.891 -13.822 0.82 40.01 ?  107 GLN   A HG3  1 
ATOM   2221 H  HG3  B GLN   A 1 107 ? 23.363 -14.352 -13.569 0.18 33.70 ?  107 GLN   A HG3  1 
ATOM   2222 H  HE21 A GLN   A 1 107 ? 20.685 -12.843 -13.834 0.82 45.67 ?  107 GLN   A HE21 1 
ATOM   2223 H  HE21 B GLN   A 1 107 ? 20.463 -14.513 -13.196 0.18 36.55 ?  107 GLN   A HE21 1 
ATOM   2224 H  HE22 A GLN   A 1 107 ? 19.889 -13.954 -13.243 0.82 45.67 ?  107 GLN   A HE22 1 
ATOM   2225 H  HE22 B GLN   A 1 107 ? 20.216 -15.618 -12.228 0.18 36.55 ?  107 GLN   A HE22 1 
ATOM   2226 N  N    . LEU   A 1 108 ? 24.729 -10.855 -9.703  1.00 18.55 ?  108 LEU   A N    1 
ATOM   2227 C  CA   . LEU   A 1 108 ? 25.647 -10.422 -8.661  1.00 15.65 ?  108 LEU   A CA   1 
ATOM   2228 C  C    . LEU   A 1 108 ? 24.952 -10.256 -7.321  1.00 13.83 ?  108 LEU   A C    1 
ATOM   2229 O  O    . LEU   A 1 108 ? 25.634 -10.098 -6.307  1.00 14.08 ?  108 LEU   A O    1 
ATOM   2230 C  CB   . LEU   A 1 108 ? 26.355 -9.126  -9.072  1.00 15.28 ?  108 LEU   A CB   1 
ATOM   2231 C  CG   . LEU   A 1 108 ? 27.366 -9.333  -10.201 1.00 16.90 ?  108 LEU   A CG   1 
ATOM   2232 C  CD1  . LEU   A 1 108 ? 27.861 -8.007  -10.755 1.00 17.78 ?  108 LEU   A CD1  1 
ATOM   2233 C  CD2  . LEU   A 1 108 ? 28.545 -10.171 -9.722  1.00 18.68 ?  108 LEU   A CD2  1 
ATOM   2234 H  H    A LEU   A 1 108 ? 24.591 -10.267 -10.309 0.82 22.30 ?  108 LEU   A H    1 
ATOM   2235 H  H    B LEU   A 1 108 ? 24.538 -10.254 -10.281 0.18 22.30 ?  108 LEU   A H    1 
ATOM   2236 H  HA   . LEU   A 1 108 ? 26.322 -11.103 -8.540  1.00 18.82 ?  108 LEU   A HA   1 
ATOM   2237 H  HB2  . LEU   A 1 108 ? 25.693 -8.486  -9.375  1.00 18.38 ?  108 LEU   A HB2  1 
ATOM   2238 H  HB3  . LEU   A 1 108 ? 26.831 -8.771  -8.307  1.00 18.38 ?  108 LEU   A HB3  1 
ATOM   2239 H  HG   . LEU   A 1 108 ? 26.935 -9.815  -10.925 1.00 20.32 ?  108 LEU   A HG   1 
ATOM   2240 H  HD11 . LEU   A 1 108 ? 28.474 -8.179  -11.489 1.00 21.37 ?  108 LEU   A HD11 1 
ATOM   2241 H  HD12 . LEU   A 1 108 ? 27.103 -7.492  -11.072 1.00 21.37 ?  108 LEU   A HD12 1 
ATOM   2242 H  HD13 . LEU   A 1 108 ? 28.320 -7.522  -10.051 1.00 21.37 ?  108 LEU   A HD13 1 
ATOM   2243 H  HD21 . LEU   A 1 108 ? 29.261 -10.104 -10.369 1.00 22.45 ?  108 LEU   A HD21 1 
ATOM   2244 H  HD22 . LEU   A 1 108 ? 28.839 -9.831  -8.862  1.00 22.45 ?  108 LEU   A HD22 1 
ATOM   2245 H  HD23 . LEU   A 1 108 ? 28.260 -11.094 -9.633  1.00 22.45 ?  108 LEU   A HD23 1 
ATOM   2246 N  N    . LEU   A 1 109 ? 23.618 -10.308 -7.283  1.00 13.17 ?  109 LEU   A N    1 
ATOM   2247 C  CA   . LEU   A 1 109 ? 22.923 -10.186 -6.007  1.00 12.66 ?  109 LEU   A CA   1 
ATOM   2248 C  C    . LEU   A 1 109 ? 23.274 -11.341 -5.076  1.00 11.70 ?  109 LEU   A C    1 
ATOM   2249 O  O    . LEU   A 1 109 ? 23.418 -11.147 -3.864  1.00 12.29 ?  109 LEU   A O    1 
ATOM   2250 C  CB   . LEU   A 1 109 ? 21.416 -10.103 -6.246  1.00 13.57 ?  109 LEU   A CB   1 
ATOM   2251 C  CG   . LEU   A 1 109 ? 20.531 -9.817  -5.035  1.00 13.98 ?  109 LEU   A CG   1 
ATOM   2252 C  CD1  . LEU   A 1 109 ? 20.981 -8.548  -4.325  1.00 14.24 ?  109 LEU   A CD1  1 
ATOM   2253 C  CD2  . LEU   A 1 109 ? 19.072 -9.704  -5.456  1.00 14.99 ?  109 LEU   A CD2  1 
ATOM   2254 H  H    . LEU   A 1 109 ? 23.102 -10.415 -7.962  1.00 15.85 ?  109 LEU   A H    1 
ATOM   2255 H  HA   . LEU   A 1 109 ? 23.205 -9.365  -5.575  1.00 15.23 ?  109 LEU   A HA   1 
ATOM   2256 H  HB2  . LEU   A 1 109 ? 21.253 -9.392  -6.885  1.00 16.33 ?  109 LEU   A HB2  1 
ATOM   2257 H  HB3  . LEU   A 1 109 ? 21.120 -10.944 -6.616  1.00 16.33 ?  109 LEU   A HB3  1 
ATOM   2258 H  HG   . LEU   A 1 109 ? 20.601 -10.550 -4.408  1.00 16.82 ?  109 LEU   A HG   1 
ATOM   2259 H  HD11 . LEU   A 1 109 ? 20.284 -8.249  -3.723  1.00 17.13 ?  109 LEU   A HD11 1 
ATOM   2260 H  HD12 . LEU   A 1 109 ? 21.793 -8.736  -3.826  1.00 17.13 ?  109 LEU   A HD12 1 
ATOM   2261 H  HD13 . LEU   A 1 109 ? 21.158 -7.863  -4.990  1.00 17.13 ?  109 LEU   A HD13 1 
ATOM   2262 H  HD21 . LEU   A 1 109 ? 18.543 -9.401  -4.698  1.00 18.03 ?  109 LEU   A HD21 1 
ATOM   2263 H  HD22 . LEU   A 1 109 ? 18.996 -9.066  -6.182  1.00 18.03 ?  109 LEU   A HD22 1 
ATOM   2264 H  HD23 . LEU   A 1 109 ? 18.756 -10.575 -5.747  1.00 18.03 ?  109 LEU   A HD23 1 
ATOM   2265 N  N    . LYS   A 1 110 ? 23.426 -12.551 -5.618  1.00 11.82 ?  110 LYS   A N    1 
ATOM   2266 C  CA   . LYS   A 1 110 ? 23.806 -13.675 -4.765  1.00 11.70 ?  110 LYS   A CA   1 
ATOM   2267 C  C    . LYS   A 1 110 ? 25.191 -13.456 -4.162  1.00 11.25 ?  110 LYS   A C    1 
ATOM   2268 O  O    . LYS   A 1 110 ? 25.394 -13.656 -2.961  1.00 11.52 ?  110 LYS   A O    1 
ATOM   2269 C  CB   . LYS   A 1 110 ? 23.729 -14.997 -5.532  1.00 12.64 ?  110 LYS   A CB   1 
ATOM   2270 C  CG   . LYS   A 1 110 ? 23.933 -16.211 -4.626  1.00 12.66 ?  110 LYS   A CG   1 
ATOM   2271 C  CD   . LYS   A 1 110 ? 23.703 -17.532 -5.338  1.00 13.32 ?  110 LYS   A CD   1 
ATOM   2272 C  CE   . LYS   A 1 110 ? 23.807 -18.709 -4.383  1.00 14.40 ?  110 LYS   A CE   1 
ATOM   2273 N  NZ   . LYS   A 1 110 ? 22.616 -18.846 -3.512  1.00 14.70 ?  110 LYS   A NZ   1 
ATOM   2274 H  H    . LYS   A 1 110 ? 23.315 -12.748 -6.447  1.00 14.23 ?  110 LYS   A H    1 
ATOM   2275 H  HA   . LYS   A 1 110 ? 23.170 -13.729 -4.028  1.00 14.08 ?  110 LYS   A HA   1 
ATOM   2276 H  HB2  . LYS   A 1 110 ? 22.853 -15.074 -5.944  1.00 15.21 ?  110 LYS   A HB2  1 
ATOM   2277 H  HB3  . LYS   A 1 110 ? 24.419 -15.008 -6.209  1.00 15.21 ?  110 LYS   A HB3  1 
ATOM   2278 H  HG2  . LYS   A 1 110 ? 24.842 -16.208 -4.288  1.00 15.23 ?  110 LYS   A HG2  1 
ATOM   2279 H  HG3  . LYS   A 1 110 ? 23.307 -16.162 -3.884  1.00 15.23 ?  110 LYS   A HG3  1 
ATOM   2280 H  HD2  . LYS   A 1 110 ? 22.818 -17.534 -5.728  1.00 16.03 ?  110 LYS   A HD2  1 
ATOM   2281 H  HD3  . LYS   A 1 110 ? 24.378 -17.639 -6.028  1.00 16.03 ?  110 LYS   A HD3  1 
ATOM   2282 H  HE2  . LYS   A 1 110 ? 23.905 -19.522 -4.897  1.00 17.32 ?  110 LYS   A HE2  1 
ATOM   2283 H  HE3  . LYS   A 1 110 ? 24.583 -18.580 -3.811  1.00 17.32 ?  110 LYS   A HE3  1 
ATOM   2284 H  HZ1  . LYS   A 1 110 ? 22.712 -19.543 -2.971  1.00 17.67 ?  110 LYS   A HZ1  1 
ATOM   2285 H  HZ2  . LYS   A 1 110 ? 22.505 -18.110 -3.024  1.00 17.67 ?  110 LYS   A HZ2  1 
ATOM   2286 H  HZ3  . LYS   A 1 110 ? 21.887 -18.968 -4.014  1.00 17.67 ?  110 LYS   A HZ3  1 
ATOM   2287 N  N    . SER   A 1 111 ? 26.150 -13.019 -4.983  1.00 11.37 ?  111 SER   A N    1 
ATOM   2288 C  CA   . SER   A 1 111 ? 27.482 -12.709 -4.467  1.00 11.75 ?  111 SER   A CA   1 
ATOM   2289 C  C    . SER   A 1 111 ? 27.418 -11.664 -3.357  1.00 11.08 ?  111 SER   A C    1 
ATOM   2290 O  O    . SER   A 1 111 ? 28.122 -11.766 -2.346  1.00 11.84 ?  111 SER   A O    1 
ATOM   2291 C  CB   . SER   A 1 111 ? 28.377 -12.221 -5.605  1.00 13.08 ?  111 SER   A CB   1 
ATOM   2292 O  OG   . SER   A 1 111 ? 28.469 -13.202 -6.626  1.00 15.28 ?  111 SER   A OG   1 
ATOM   2293 H  H    . SER   A 1 111 ? 26.052 -12.903 -5.829  1.00 13.69 ?  111 SER   A H    1 
ATOM   2294 H  HA   . SER   A 1 111 ? 27.874 -13.516 -4.101  1.00 14.13 ?  111 SER   A HA   1 
ATOM   2295 H  HB2  . SER   A 1 111 ? 27.994 -11.415 -5.987  1.00 15.74 ?  111 SER   A HB2  1 
ATOM   2296 H  HB3  . SER   A 1 111 ? 29.261 -12.030 -5.251  1.00 15.74 ?  111 SER   A HB3  1 
ATOM   2297 H  HG   . SER   A 1 111 ? 28.986 -12.923 -7.241  1.00 18.37 ?  111 SER   A HG   1 
ATOM   2298 N  N    . ALA   A 1 112 ? 26.578 -10.642 -3.536  1.00 11.25 ?  112 ALA   A N    1 
ATOM   2299 C  CA   . ALA   A 1 112 ? 26.431 -9.609  -2.514  1.00 11.23 ?  112 ALA   A CA   1 
ATOM   2300 C  C    . ALA   A 1 112 ? 25.954 -10.209 -1.195  1.00 11.01 ?  112 ALA   A C    1 
ATOM   2301 O  O    . ALA   A 1 112 ? 26.502 -9.915  -0.127  1.00 11.24 ?  112 ALA   A O    1 
ATOM   2302 C  CB   . ALA   A 1 112 ? 25.476 -8.519  -3.004  1.00 11.70 ?  112 ALA   A CB   1 
ATOM   2303 H  H    . ALA   A 1 112 ? 26.092 -10.523 -4.235  1.00 13.54 ?  112 ALA   A H    1 
ATOM   2304 H  HA   . ALA   A 1 112 ? 27.294 -9.193  -2.358  1.00 13.51 ?  112 ALA   A HA   1 
ATOM   2305 H  HB1  . ALA   A 1 112 ? 25.400 -7.831  -2.317  1.00 14.08 ?  112 ALA   A HB1  1 
ATOM   2306 H  HB2  . ALA   A 1 112 ? 25.825 -8.128  -3.818  1.00 14.08 ?  112 ALA   A HB2  1 
ATOM   2307 H  HB3  . ALA   A 1 112 ? 24.603 -8.909  -3.170  1.00 14.08 ?  112 ALA   A HB3  1 
ATOM   2308 N  N    . TYR   A 1 113 ? 24.924 -11.057 -1.246  1.00 11.11 ?  113 TYR   A N    1 
ATOM   2309 C  CA   . TYR   A 1 113 ? 24.416 -11.661 -0.016  1.00 10.70 ?  113 TYR   A CA   1 
ATOM   2310 C  C    . TYR   A 1 113 ? 25.420 -12.615 0.627   1.00 10.30 ?  113 TYR   A C    1 
ATOM   2311 O  O    . TYR   A 1 113 ? 25.390 -12.808 1.846   1.00 11.07 ?  113 TYR   A O    1 
ATOM   2312 C  CB   . TYR   A 1 113 ? 23.103 -12.394 -0.288  1.00 11.23 ?  113 TYR   A CB   1 
ATOM   2313 C  CG   . TYR   A 1 113 ? 21.883 -11.507 -0.175  1.00 11.44 ?  113 TYR   A CG   1 
ATOM   2314 C  CD1  . TYR   A 1 113 ? 21.531 -10.922 1.039   1.00 11.57 ?  113 TYR   A CD1  1 
ATOM   2315 C  CD2  . TYR   A 1 113 ? 21.066 -11.267 -1.273  1.00 11.50 ?  113 TYR   A CD2  1 
ATOM   2316 C  CE1  . TYR   A 1 113 ? 20.402 -10.126 1.155   1.00 11.92 ?  113 TYR   A CE1  1 
ATOM   2317 C  CE2  . TYR   A 1 113 ? 19.914 -10.478 -1.163  1.00 11.86 ?  113 TYR   A CE2  1 
ATOM   2318 C  CZ   . TYR   A 1 113 ? 19.597 -9.912  0.050   1.00 11.69 ?  113 TYR   A CZ   1 
ATOM   2319 O  OH   . TYR   A 1 113 ? 18.471 -9.128  0.179   1.00 12.41 ?  113 TYR   A OH   1 
ATOM   2320 H  H    . TYR   A 1 113 ? 24.515 -11.294 -1.965  1.00 13.37 ?  113 TYR   A H    1 
ATOM   2321 H  HA   . TYR   A 1 113 ? 24.239 -10.955 0.621   1.00 12.88 ?  113 TYR   A HA   1 
ATOM   2322 H  HB2  . TYR   A 1 113 ? 23.123 -12.751 -1.187  1.00 13.52 ?  113 TYR   A HB2  1 
ATOM   2323 H  HB3  . TYR   A 1 113 ? 23.009 -13.112 0.354   1.00 13.52 ?  113 TYR   A HB3  1 
ATOM   2324 H  HD1  . TYR   A 1 113 ? 22.070 -11.073 1.787   1.00 13.92 ?  113 TYR   A HD1  1 
ATOM   2325 H  HD2  . TYR   A 1 113 ? 21.269 -11.657 -2.087  1.00 13.84 ?  113 TYR   A HD2  1 
ATOM   2326 H  HE1  . TYR   A 1 113 ? 20.184 -9.747  1.976   1.00 14.34 ?  113 TYR   A HE1  1 
ATOM   2327 H  HE2  . TYR   A 1 113 ? 19.370 -10.324 -1.902  1.00 14.27 ?  113 TYR   A HE2  1 
ATOM   2328 H  HH   . TYR   A 1 113 ? 18.075 -9.082  -0.566  1.00 14.93 ?  113 TYR   A HH   1 
ATOM   2329 N  N    . GLU   A 1 114 ? 26.319 -13.224 -0.162  1.00 10.65 ?  114 GLU   A N    1 
ATOM   2330 C  CA   . GLU   A 1 114 ? 27.317 -14.118 0.427   1.00 10.85 ?  114 GLU   A CA   1 
ATOM   2331 C  C    . GLU   A 1 114 ? 28.172 -13.413 1.476   1.00 10.70 ?  114 GLU   A C    1 
ATOM   2332 O  O    . GLU   A 1 114 ? 28.652 -14.052 2.423   1.00 11.30 ?  114 GLU   A O    1 
ATOM   2333 C  CB   . GLU   A 1 114 ? 28.182 -14.759 -0.667  1.00 11.13 ?  114 GLU   A CB   1 
ATOM   2334 C  CG   . GLU   A 1 114 ? 27.413 -15.811 -1.438  1.00 11.44 ?  114 GLU   A CG   1 
ATOM   2335 C  CD   . GLU   A 1 114 ? 28.114 -16.339 -2.683  1.00 12.07 ?  114 GLU   A CD   1 
ATOM   2336 O  OE1  . GLU   A 1 114 ? 29.071 -15.708 -3.175  1.00 11.92 ?  114 GLU   A OE1  1 
ATOM   2337 O  OE2  . GLU   A 1 114 ? 27.669 -17.400 -3.182  1.00 12.92 -1 114 GLU   A OE2  1 
ATOM   2338 H  H    . GLU   A 1 114 ? 26.372 -13.132 -1.023  1.00 12.82 ?  114 GLU   A H    1 
ATOM   2339 H  HA   . GLU   A 1 114 ? 26.848 -14.834 0.870   1.00 13.06 ?  114 GLU   A HA   1 
ATOM   2340 H  HB2  . GLU   A 1 114 ? 28.471 -14.077 -1.296  1.00 13.40 ?  114 GLU   A HB2  1 
ATOM   2341 H  HB3  . GLU   A 1 114 ? 28.951 -15.185 -0.260  1.00 13.40 ?  114 GLU   A HB3  1 
ATOM   2342 H  HG2  . GLU   A 1 114 ? 27.256 -16.568 -0.854  1.00 13.76 ?  114 GLU   A HG2  1 
ATOM   2343 H  HG3  . GLU   A 1 114 ? 26.565 -15.433 -1.718  1.00 13.76 ?  114 GLU   A HG3  1 
ATOM   2344 N  N    . ASN   A 1 115 ? 28.349 -12.092 1.353   1.00 10.63 ?  115 ASN   A N    1 
ATOM   2345 C  CA   . ASN   A 1 115 ? 29.112 -11.365 2.363   1.00 10.92 ?  115 ASN   A CA   1 
ATOM   2346 C  C    . ASN   A 1 115 ? 28.492 -11.506 3.749   1.00 10.59 ?  115 ASN   A C    1 
ATOM   2347 O  O    . ASN   A 1 115 ? 29.200 -11.433 4.760   1.00 11.18 ?  115 ASN   A O    1 
ATOM   2348 C  CB   . ASN   A 1 115 ? 29.213 -9.887  1.991   1.00 11.13 ?  115 ASN   A CB   1 
ATOM   2349 C  CG   . ASN   A 1 115 ? 30.003 -9.658  0.729   1.00 11.88 ?  115 ASN   A CG   1 
ATOM   2350 O  OD1  . ASN   A 1 115 ? 31.219 -9.757  0.742   1.00 15.55 ?  115 ASN   A OD1  1 
ATOM   2351 N  ND2  . ASN   A 1 115 ? 29.327 -9.355  -0.365  1.00 11.63 ?  115 ASN   A ND2  1 
ATOM   2352 H  H    . ASN   A 1 115 ? 28.041 -11.602 0.713   1.00 12.79 ?  115 ASN   A H    1 
ATOM   2353 H  HA   . ASN   A 1 115 ? 30.009 -11.729 2.400   1.00 13.14 ?  115 ASN   A HA   1 
ATOM   2354 H  HB2  . ASN   A 1 115 ? 28.318 -9.533  1.865   1.00 13.40 ?  115 ASN   A HB2  1 
ATOM   2355 H  HB3  . ASN   A 1 115 ? 29.653 -9.412  2.718   1.00 13.40 ?  115 ASN   A HB3  1 
ATOM   2356 H  HD21 . ASN   A 1 115 ? 29.742 -9.213  -1.101  1.00 13.99 ?  115 ASN   A HD21 1 
ATOM   2357 H  HD22 . ASN   A 1 115 ? 28.466 -9.313  -0.339  1.00 13.99 ?  115 ASN   A HD22 1 
ATOM   2358 N  N    . PHE   A 1 116 ? 27.165 -11.674 3.825   1.00 10.91 ?  116 PHE   A N    1 
ATOM   2359 C  CA   . PHE   A 1 116 ? 26.521 -11.781 5.129   1.00 11.09 ?  116 PHE   A CA   1 
ATOM   2360 C  C    . PHE   A 1 116 ? 27.004 -13.012 5.894   1.00 11.10 ?  116 PHE   A C    1 
ATOM   2361 O  O    . PHE   A 1 116 ? 26.932 -13.032 7.122   1.00 11.49 ?  116 PHE   A O    1 
ATOM   2362 C  CB   . PHE   A 1 116 ? 24.993 -11.905 4.995   1.00 11.44 ?  116 PHE   A CB   1 
ATOM   2363 C  CG   . PHE   A 1 116 ? 24.240 -10.655 4.546   1.00 10.88 ?  116 PHE   A CG   1 
ATOM   2364 C  CD1  . PHE   A 1 116 ? 24.811 -9.630  3.806   1.00 11.31 ?  116 PHE   A CD1  1 
ATOM   2365 C  CD2  . PHE   A 1 116 ? 22.887 -10.555 4.864   1.00 11.68 ?  116 PHE   A CD2  1 
ATOM   2366 C  CE1  . PHE   A 1 116 ? 24.047 -8.539  3.403   1.00 11.32 ?  116 PHE   A CE1  1 
ATOM   2367 C  CE2  . PHE   A 1 116 ? 22.120 -9.479  4.468   1.00 11.70 ?  116 PHE   A CE2  1 
ATOM   2368 C  CZ   . PHE   A 1 116 ? 22.690 -8.465  3.739   1.00 11.41 ?  116 PHE   A CZ   1 
ATOM   2369 H  H    . PHE   A 1 116 ? 26.632 -11.715 3.148   1.00 13.13 ?  116 PHE   A H    1 
ATOM   2370 H  HA   . PHE   A 1 116 ? 26.717 -10.991 5.653   1.00 13.35 ?  116 PHE   A HA   1 
ATOM   2371 H  HB2  . PHE   A 1 116 ? 24.801 -12.603 4.347   1.00 13.77 ?  116 PHE   A HB2  1 
ATOM   2372 H  HB3  . PHE   A 1 116 ? 24.635 -12.164 5.858   1.00 13.77 ?  116 PHE   A HB3  1 
ATOM   2373 H  HD1  . PHE   A 1 116 ? 25.709 -9.682  3.575   1.00 13.62 ?  116 PHE   A HD1  1 
ATOM   2374 H  HD2  . PHE   A 1 116 ? 22.486 -11.247 5.351   1.00 14.05 ?  116 PHE   A HD2  1 
ATOM   2375 H  HE1  . PHE   A 1 116 ? 24.442 -7.858  2.914   1.00 13.63 ?  116 PHE   A HE1  1 
ATOM   2376 H  HE2  . PHE   A 1 116 ? 21.219 -9.444  4.702   1.00 14.08 ?  116 PHE   A HE2  1 
ATOM   2377 H  HZ   . PHE   A 1 116 ? 22.183 -7.732  3.480   1.00 13.73 ?  116 PHE   A HZ   1 
ATOM   2378 N  N    . ASN   A 1 117 ? 27.446 -14.056 5.187   1.00 11.10 ?  117 ASN   A N    1 
ATOM   2379 C  CA   . ASN   A 1 117 ? 27.817 -15.301 5.848   1.00 11.58 ?  117 ASN   A CA   1 
ATOM   2380 C  C    . ASN   A 1 117 ? 29.077 -15.180 6.683   1.00 12.04 ?  117 ASN   A C    1 
ATOM   2381 O  O    . ASN   A 1 117 ? 29.380 -16.101 7.451   1.00 12.83 ?  117 ASN   A O    1 
ATOM   2382 C  CB   . ASN   A 1 117 ? 27.932 -16.424 4.822   1.00 11.81 ?  117 ASN   A CB   1 
ATOM   2383 C  CG   . ASN   A 1 117 ? 26.577 -16.811 4.287   1.00 11.71 ?  117 ASN   A CG   1 
ATOM   2384 O  OD1  . ASN   A 1 117 ? 25.608 -16.854 5.046   1.00 12.48 ?  117 ASN   A OD1  1 
ATOM   2385 N  ND2  . ASN   A 1 117 ? 26.485 -17.054 2.993   1.00 11.87 ?  117 ASN   A ND2  1 
ATOM   2386 H  H    . ASN   A 1 117 ? 27.524 -14.067 4.328   1.00 13.36 ?  117 ASN   A H    1 
ATOM   2387 H  HA   . ASN   A 1 117 ? 27.098 -15.541 6.453   1.00 13.93 ?  117 ASN   A HA   1 
ATOM   2388 H  HB2  . ASN   A 1 117 ? 28.483 -16.127 4.080   1.00 14.21 ?  117 ASN   A HB2  1 
ATOM   2389 H  HB3  . ASN   A 1 117 ? 28.324 -17.202 5.243   1.00 14.21 ?  117 ASN   A HB3  1 
ATOM   2390 H  HD21 . ASN   A 1 117 ? 25.730 -17.269 2.648   1.00 14.29 ?  117 ASN   A HD21 1 
ATOM   2391 H  HD22 . ASN   A 1 117 ? 27.186 -16.997 2.493   1.00 14.29 ?  117 ASN   A HD22 1 
ATOM   2392 N  N    . GLN   A 1 118 ? 29.808 -14.074 6.555   1.00 11.99 ?  118 GLN   A N    1 
ATOM   2393 C  CA   . GLN   A 1 118 ? 30.987 -13.836 7.374   1.00 12.55 ?  118 GLN   A CA   1 
ATOM   2394 C  C    . GLN   A 1 118 ? 30.645 -13.261 8.742   1.00 12.39 ?  118 GLN   A C    1 
ATOM   2395 O  O    . GLN   A 1 118 ? 31.560 -12.969 9.519   1.00 13.91 ?  118 GLN   A O    1 
ATOM   2396 C  CB   . GLN   A 1 118 ? 31.966 -12.925 6.630   1.00 12.57 ?  118 GLN   A CB   1 
ATOM   2397 C  CG   . GLN   A 1 118 ? 32.451 -13.507 5.312   1.00 12.60 ?  118 GLN   A CG   1 
ATOM   2398 C  CD   . GLN   A 1 118 ? 33.270 -14.773 5.497   1.00 12.82 ?  118 GLN   A CD   1 
ATOM   2399 O  OE1  . GLN   A 1 118 ? 34.132 -14.842 6.384   1.00 13.65 ?  118 GLN   A OE1  1 
ATOM   2400 N  NE2  . GLN   A 1 118 ? 33.025 -15.772 4.651   1.00 13.18 ?  118 GLN   A NE2  1 
ATOM   2401 H  H    . GLN   A 1 118 ? 29.632 -13.437 5.996   1.00 14.42 ?  118 GLN   A H    1 
ATOM   2402 H  HA   . GLN   A 1 118 ? 31.425 -14.688 7.517   1.00 15.10 ?  118 GLN   A HA   1 
ATOM   2403 H  HB2  . GLN   A 1 118 ? 31.528 -12.080 6.444   1.00 15.12 ?  118 GLN   A HB2  1 
ATOM   2404 H  HB3  . GLN   A 1 118 ? 32.741 -12.778 7.196   1.00 15.12 ?  118 GLN   A HB3  1 
ATOM   2405 H  HG2  . GLN   A 1 118 ? 31.685 -13.719 4.753   1.00 15.16 ?  118 GLN   A HG2  1 
ATOM   2406 H  HG3  . GLN   A 1 118 ? 33.013 -12.851 4.863   1.00 15.16 ?  118 GLN   A HG3  1 
ATOM   2407 H  HE21 . GLN   A 1 118 ? 32.414 -15.687 4.045   1.00 15.86 ?  118 GLN   A HE21 1 
ATOM   2408 H  HE22 . GLN   A 1 118 ? 33.457 -16.511 4.718   1.00 15.86 ?  118 GLN   A HE22 1 
ATOM   2409 N  N    . HIS   A 1 119 ? 29.357 -13.112 9.060   1.00 11.94 ?  119 HIS   A N    1 
ATOM   2410 C  CA   . HIS   A 1 119 ? 28.903 -12.503 10.306  1.00 12.60 ?  119 HIS   A CA   1 
ATOM   2411 C  C    . HIS   A 1 119 ? 27.768 -13.328 10.883  1.00 12.86 ?  119 HIS   A C    1 
ATOM   2412 O  O    . HIS   A 1 119 ? 26.818 -13.656 10.171  1.00 13.38 ?  119 HIS   A O    1 
ATOM   2413 C  CB   . HIS   A 1 119 ? 28.447 -11.067 10.041  1.00 13.48 ?  119 HIS   A CB   1 
ATOM   2414 C  CG   . HIS   A 1 119 ? 29.526 -10.257 9.422   1.00 14.62 ?  119 HIS   A CG   1 
ATOM   2415 N  ND1  . HIS   A 1 119 ? 30.511 -9.656  10.169  1.00 16.79 ?  119 HIS   A ND1  1 
ATOM   2416 C  CD2  . HIS   A 1 119 ? 29.856 -10.068 8.125   1.00 15.80 ?  119 HIS   A CD2  1 
ATOM   2417 C  CE1  . HIS   A 1 119 ? 31.374 -9.077  9.354   1.00 16.85 ?  119 HIS   A CE1  1 
ATOM   2418 N  NE2  . HIS   A 1 119 ? 31.006 -9.320  8.109   1.00 17.08 ?  119 HIS   A NE2  1 
ATOM   2419 H  H    . HIS   A 1 119 ? 28.704 -13.371 8.556   1.00 14.36 ?  119 HIS   A H    1 
ATOM   2420 H  HA   . HIS   A 1 119 ? 29.636 -12.488 10.945  1.00 15.16 ?  119 HIS   A HA   1 
ATOM   2421 H  HB2  . HIS   A 1 119 ? 27.689 -11.086 9.436   1.00 16.21 ?  119 HIS   A HB2  1 
ATOM   2422 H  HB3  . HIS   A 1 119 ? 28.200 -10.656 10.881  1.00 16.21 ?  119 HIS   A HB3  1 
ATOM   2423 H  HD2  . HIS   A 1 119 ? 29.389 -10.380 7.379   1.00 19.00 ?  119 HIS   A HD2  1 
ATOM   2424 H  HE1  . HIS   A 1 119 ? 32.114 -8.578  9.610   1.00 20.26 ?  119 HIS   A HE1  1 
ATOM   2425 H  HE2  . HIS   A 1 119 ? 31.406 -9.032  7.402   1.00 20.53 ?  119 HIS   A HE2  1 
ATOM   2426 N  N    . GLU   A 1 120 ? 27.860 -13.642 12.175  1.00 13.64 ?  120 GLU   A N    1 
ATOM   2427 C  CA   . GLU   A 1 120 ? 26.914 -14.581 12.775  1.00 15.23 ?  120 GLU   A CA   1 
ATOM   2428 C  C    . GLU   A 1 120 ? 25.498 -14.017 12.844  1.00 13.86 ?  120 GLU   A C    1 
ATOM   2429 O  O    . GLU   A 1 120 ? 24.524 -14.776 12.725  1.00 14.23 ?  120 GLU   A O    1 
ATOM   2430 C  CB   . GLU   A 1 120 ? 27.395 -14.987 14.171  1.00 19.67 ?  120 GLU   A CB   1 
ATOM   2431 C  CG   . GLU   A 1 120 ? 28.596 -15.917 14.163  1.00 25.58 ?  120 GLU   A CG   1 
ATOM   2432 C  CD   . GLU   A 1 120 ? 28.759 -16.665 15.471  1.00 31.22 ?  120 GLU   A CD   1 
ATOM   2433 O  OE1  . GLU   A 1 120 ? 28.421 -16.096 16.532  1.00 33.11 ?  120 GLU   A OE1  1 
ATOM   2434 O  OE2  . GLU   A 1 120 ? 29.216 -17.827 15.437  1.00 33.65 -1 120 GLU   A OE2  1 
ATOM   2435 H  H    . GLU   A 1 120 ? 28.457 -13.331 12.720  1.00 16.41 ?  120 GLU   A H    1 
ATOM   2436 H  HA   . GLU   A 1 120 ? 26.888 -15.381 12.236  1.00 18.31 ?  120 GLU   A HA   1 
ATOM   2437 H  HB2  . GLU   A 1 120 ? 27.647 -14.190 14.666  1.00 23.64 ?  120 GLU   A HB2  1 
ATOM   2438 H  HB3  . GLU   A 1 120 ? 26.674 -15.443 14.633  1.00 23.64 ?  120 GLU   A HB3  1 
ATOM   2439 H  HG2  . GLU   A 1 120 ? 28.491 -16.568 13.452  1.00 30.73 ?  120 GLU   A HG2  1 
ATOM   2440 H  HG3  . GLU   A 1 120 ? 29.403 -15.399 14.026  1.00 30.73 ?  120 GLU   A HG3  1 
ATOM   2441 N  N    . VAL   A 1 121 ? 25.365 -12.708 13.068  1.00 13.29 ?  121 VAL   A N    1 
ATOM   2442 C  CA   . VAL   A 1 121 ? 24.073 -12.041 13.194  1.00 13.56 ?  121 VAL   A CA   1 
ATOM   2443 C  C    . VAL   A 1 121 ? 24.183 -10.658 12.564  1.00 12.48 ?  121 VAL   A C    1 
ATOM   2444 O  O    . VAL   A 1 121 ? 25.159 -9.939  12.803  1.00 13.29 ?  121 VAL   A O    1 
ATOM   2445 C  CB   . VAL   A 1 121 ? 23.645 -11.897 14.672  1.00 16.43 ?  121 VAL   A CB   1 
ATOM   2446 C  CG1  . VAL   A 1 121 ? 22.265 -11.257 14.774  1.00 17.21 ?  121 VAL   A CG1  1 
ATOM   2447 C  CG2  . VAL   A 1 121 ? 23.655 -13.231 15.395  1.00 18.36 ?  121 VAL   A CG2  1 
ATOM   2448 H  H    . VAL   A 1 121 ? 26.032 -12.169 13.160  1.00 15.99 ?  121 VAL   A H    1 
ATOM   2449 H  HA   . VAL   A 1 121 ? 23.396 -12.551 12.726  1.00 16.30 ?  121 VAL   A HA   1 
ATOM   2450 H  HB   . VAL   A 1 121 ? 24.270 -11.315 15.127  1.00 19.75 ?  121 VAL   A HB   1 
ATOM   2451 H  HG11 . VAL   A 1 121 ? 21.947 -11.328 15.688  1.00 20.70 ?  121 VAL   A HG11 1 
ATOM   2452 H  HG12 . VAL   A 1 121 ? 22.328 -10.323 14.520  1.00 20.70 ?  121 VAL   A HG12 1 
ATOM   2453 H  HG13 . VAL   A 1 121 ? 21.655 -11.722 14.178  1.00 20.70 ?  121 VAL   A HG13 1 
ATOM   2454 H  HG21 . VAL   A 1 121 ? 23.310 -13.109 16.299  1.00 22.06 ?  121 VAL   A HG21 1 
ATOM   2455 H  HG22 . VAL   A 1 121 ? 23.086 -13.859 14.916  1.00 22.06 ?  121 VAL   A HG22 1 
ATOM   2456 H  HG23 . VAL   A 1 121 ? 24.560 -13.569 15.433  1.00 22.06 ?  121 VAL   A HG23 1 
ATOM   2457 N  N    . LEU   A 1 122 ? 23.164 -10.261 11.794  1.00 12.37 ?  122 LEU   A N    1 
ATOM   2458 C  CA   . LEU   A 1 122 ? 23.169 -8.962  11.127  1.00 12.26 ?  122 LEU   A CA   1 
ATOM   2459 C  C    . LEU   A 1 122 ? 21.772 -8.369  11.076  1.00 12.01 ?  122 LEU   A C    1 
ATOM   2460 O  O    . LEU   A 1 122 ? 20.779 -9.090  10.946  1.00 13.11 ?  122 LEU   A O    1 
ATOM   2461 C  CB   . LEU   A 1 122 ? 23.578 -9.059  9.654   1.00 13.71 ?  122 LEU   A CB   1 
ATOM   2462 C  CG   . LEU   A 1 122 ? 24.789 -9.902  9.278   1.00 13.56 ?  122 LEU   A CG   1 
ATOM   2463 C  CD1  . LEU   A 1 122 ? 24.390 -11.361 9.068   1.00 14.26 ?  122 LEU   A CD1  1 
ATOM   2464 C  CD2  . LEU   A 1 122 ? 25.454 -9.337  8.033   1.00 13.05 ?  122 LEU   A CD2  1 
ATOM   2465 H  H    . LEU   A 1 122 ? 22.456 -10.729 11.639  1.00 14.88 ?  122 LEU   A H    1 
ATOM   2466 H  HA   . LEU   A 1 122 ? 23.765 -8.347  11.587  1.00 14.76 ?  122 LEU   A HA   1 
ATOM   2467 H  HB2  . LEU   A 1 122 ? 22.833 -9.421  9.160   1.00 16.49 ?  122 LEU   A HB2  1 
ATOM   2468 H  HB3  . LEU   A 1 122 ? 23.765 -8.161  9.338   1.00 16.49 ?  122 LEU   A HB3  1 
ATOM   2469 H  HG   . LEU   A 1 122 ? 25.445 -9.870  9.995   1.00 16.32 ?  122 LEU   A HG   1 
ATOM   2470 H  HD11 . LEU   A 1 122 ? 25.164 -11.867 8.777   1.00 17.15 ?  122 LEU   A HD11 1 
ATOM   2471 H  HD12 . LEU   A 1 122 ? 24.059 -11.721 9.907   1.00 17.15 ?  122 LEU   A HD12 1 
ATOM   2472 H  HD13 . LEU   A 1 122 ? 23.694 -11.404 8.394   1.00 17.15 ?  122 LEU   A HD13 1 
ATOM   2473 H  HD21 . LEU   A 1 122 ? 26.200 -9.907  7.780   1.00 15.70 ?  122 LEU   A HD21 1 
ATOM   2474 H  HD22 . LEU   A 1 122 ? 24.804 -9.311  7.311   1.00 15.70 ?  122 LEU   A HD22 1 
ATOM   2475 H  HD23 . LEU   A 1 122 ? 25.774 -8.441  8.219   1.00 15.70 ?  122 LEU   A HD23 1 
ATOM   2476 N  N    A LEU   A 1 123 ? 21.711 -7.042  11.185  0.82 11.62 ?  123 LEU   A N    1 
ATOM   2477 N  N    B LEU   A 1 123 ? 21.721 -7.040  11.137  0.18 11.87 ?  123 LEU   A N    1 
ATOM   2478 C  CA   A LEU   A 1 123 ? 20.541 -6.248  10.828  0.82 11.45 ?  123 LEU   A CA   1 
ATOM   2479 C  CA   B LEU   A 1 123 ? 20.528 -6.253  10.850  0.18 11.94 ?  123 LEU   A CA   1 
ATOM   2480 C  C    A LEU   A 1 123 ? 20.769 -5.718  9.421   0.82 10.80 ?  123 LEU   A C    1 
ATOM   2481 C  C    B LEU   A 1 123 ? 20.740 -5.613  9.484   0.18 11.54 ?  123 LEU   A C    1 
ATOM   2482 O  O    A LEU   A 1 123 ? 21.829 -5.155  9.149   0.82 11.14 ?  123 LEU   A O    1 
ATOM   2483 O  O    B LEU   A 1 123 ? 21.645 -4.789  9.323   0.18 11.37 ?  123 LEU   A O    1 
ATOM   2484 C  CB   A LEU   A 1 123 ? 20.409 -5.064  11.788  0.82 12.11 ?  123 LEU   A CB   1 
ATOM   2485 C  CB   B LEU   A 1 123 ? 20.351 -5.173  11.918  0.18 12.50 ?  123 LEU   A CB   1 
ATOM   2486 C  CG   A LEU   A 1 123 ? 19.355 -4.006  11.456  0.82 13.06 ?  123 LEU   A CG   1 
ATOM   2487 C  CG   B LEU   A 1 123 ? 19.335 -4.067  11.623  0.18 12.92 ?  123 LEU   A CG   1 
ATOM   2488 C  CD1  A LEU   A 1 123 ? 17.960 -4.604  11.472  0.82 13.75 ?  123 LEU   A CD1  1 
ATOM   2489 C  CD1  B LEU   A 1 123 ? 17.922 -4.624  11.630  0.18 13.30 ?  123 LEU   A CD1  1 
ATOM   2490 C  CD2  A LEU   A 1 123 ? 19.456 -2.833  12.432  0.82 13.91 ?  123 LEU   A CD2  1 
ATOM   2491 C  CD2  B LEU   A 1 123 ? 19.474 -2.919  12.613  0.18 13.14 ?  123 LEU   A CD2  1 
ATOM   2492 H  H    A LEU   A 1 123 ? 22.368 -6.558  11.464  0.82 13.98 ?  123 LEU   A H    1 
ATOM   2493 H  H    B LEU   A 1 123 ? 22.399 -6.546  11.343  0.18 14.28 ?  123 LEU   A H    1 
ATOM   2494 H  HA   A LEU   A 1 123 ? 19.735 -6.786  10.850  0.82 13.78 ?  123 LEU   A HA   1 
ATOM   2495 H  HA   B LEU   A 1 123 ? 19.741 -6.819  10.826  0.18 14.37 ?  123 LEU   A HA   1 
ATOM   2496 H  HB2  A LEU   A 1 123 ? 20.188 -5.412  12.665  0.82 14.58 ?  123 LEU   A HB2  1 
ATOM   2497 H  HB2  B LEU   A 1 123 ? 20.072 -5.607  12.741  0.18 15.04 ?  123 LEU   A HB2  1 
ATOM   2498 H  HB3  A LEU   A 1 123 ? 21.261 -4.608  11.827  0.82 14.58 ?  123 LEU   A HB3  1 
ATOM   2499 H  HB3  B LEU   A 1 123 ? 21.209 -4.745  12.060  0.18 15.04 ?  123 LEU   A HB3  1 
ATOM   2500 H  HG   A LEU   A 1 123 ? 19.515 -3.657  10.562  0.82 15.71 ?  123 LEU   A HG   1 
ATOM   2501 H  HG   B LEU   A 1 123 ? 19.504 -3.706  10.740  0.18 15.54 ?  123 LEU   A HG   1 
ATOM   2502 H  HD11 A LEU   A 1 123 ? 17.310 -3.907  11.296  0.82 16.54 ?  123 LEU   A HD11 1 
ATOM   2503 H  HD11 B LEU   A 1 123 ? 17.300 -3.903  11.448  0.18 15.99 ?  123 LEU   A HD11 1 
ATOM   2504 H  HD12 A LEU   A 1 123 ? 17.902 -5.292  10.789  0.82 16.54 ?  123 LEU   A HD12 1 
ATOM   2505 H  HD12 B LEU   A 1 123 ? 17.849 -5.307  10.945  0.18 15.99 ?  123 LEU   A HD12 1 
ATOM   2506 H  HD13 A LEU   A 1 123 ? 17.796 -4.995  12.347  0.82 16.54 ?  123 LEU   A HD13 1 
ATOM   2507 H  HD13 B LEU   A 1 123 ? 17.739 -5.008  12.502  0.18 15.99 ?  123 LEU   A HD13 1 
ATOM   2508 H  HD21 A LEU   A 1 123 ? 18.782 -2.175  12.209  0.82 16.73 ?  123 LEU   A HD21 1 
ATOM   2509 H  HD21 B LEU   A 1 123 ? 18.817 -2.238  12.397  0.18 15.81 ?  123 LEU   A HD21 1 
ATOM   2510 H  HD22 A LEU   A 1 123 ? 19.308 -3.166  13.333  0.82 16.73 ?  123 LEU   A HD22 1 
ATOM   2511 H  HD22 B LEU   A 1 123 ? 19.322 -3.255  13.509  0.18 15.81 ?  123 LEU   A HD22 1 
ATOM   2512 H  HD23 A LEU   A 1 123 ? 20.340 -2.444  12.364  0.82 16.73 ?  123 LEU   A HD23 1 
ATOM   2513 H  HD23 B LEU   A 1 123 ? 20.368 -2.550  12.544  0.18 15.81 ?  123 LEU   A HD23 1 
ATOM   2514 N  N    A ALA   A 1 124 ? 19.785 -5.869  8.534   0.82 10.72 ?  124 ALA   A N    1 
ATOM   2515 N  N    B ALA   A 1 124 ? 19.919 -5.985  8.509   0.18 11.48 ?  124 ALA   A N    1 
ATOM   2516 C  CA   A ALA   A 1 124 ? 20.052 -5.582  7.133   0.82 11.07 ?  124 ALA   A CA   1 
ATOM   2517 C  CA   B ALA   A 1 124 ? 20.184 -5.650  7.119   0.18 11.65 ?  124 ALA   A CA   1 
ATOM   2518 C  C    A ALA   A 1 124 ? 18.813 -5.117  6.387   0.82 11.09 ?  124 ALA   A C    1 
ATOM   2519 C  C    B ALA   A 1 124 ? 18.915 -5.200  6.415   0.18 11.63 ?  124 ALA   A C    1 
ATOM   2520 O  O    A ALA   A 1 124 ? 17.685 -5.494  6.739   0.82 11.85 ?  124 ALA   A O    1 
ATOM   2521 O  O    B ALA   A 1 124 ? 17.804 -5.509  6.860   0.18 11.53 ?  124 ALA   A O    1 
ATOM   2522 C  CB   A ALA   A 1 124 ? 20.625 -6.808  6.413   0.82 11.53 ?  124 ALA   A CB   1 
ATOM   2523 C  CB   B ALA   A 1 124 ? 20.753 -6.860  6.367   0.18 11.91 ?  124 ALA   A CB   1 
ATOM   2524 H  H    A ALA   A 1 124 ? 18.981 -6.128  8.708   0.82 12.91 ?  124 ALA   A H    1 
ATOM   2525 H  H    B ALA   A 1 124 ? 19.194 -6.437  8.626   0.18 13.81 ?  124 ALA   A H    1 
ATOM   2526 H  HA   A ALA   A 1 124 ? 20.719 -4.881  7.089   0.82 13.32 ?  124 ALA   A HA   1 
ATOM   2527 H  HA   B ALA   A 1 124 ? 20.832 -4.932  7.085   0.18 14.02 ?  124 ALA   A HA   1 
ATOM   2528 H  HB1  A ALA   A 1 124 ? 20.799 -6.587  5.484   0.82 13.87 ?  124 ALA   A HB1  1 
ATOM   2529 H  HB1  B ALA   A 1 124 ? 20.920 -6.608  5.446   0.18 14.34 ?  124 ALA   A HB1  1 
ATOM   2530 H  HB2  A ALA   A 1 124 ? 21.461 -7.069  6.845   0.82 13.87 ?  124 ALA   A HB2  1 
ATOM   2531 H  HB2  B ALA   A 1 124 ? 21.578 -7.133  6.794   0.18 14.34 ?  124 ALA   A HB2  1 
ATOM   2532 H  HB3  A ALA   A 1 124 ? 19.991 -7.538  6.466   0.82 13.87 ?  124 ALA   A HB3  1 
ATOM   2533 H  HB3  B ALA   A 1 124 ? 20.106 -7.583  6.402   0.18 14.34 ?  124 ALA   A HB3  1 
ATOM   2534 N  N    A PRO   A 1 125 ? 19.002 -4.350  5.317   0.82 11.00 ?  125 PRO   A N    1 
ATOM   2535 N  N    B PRO   A 1 125 ? 19.052 -4.459  5.300   0.18 11.69 ?  125 PRO   A N    1 
ATOM   2536 C  CA   A PRO   A 1 125 ? 17.944 -4.108  4.339   0.82 11.19 ?  125 PRO   A CA   1 
ATOM   2537 C  CA   B PRO   A 1 125 ? 17.907 -4.222  4.414   0.18 11.66 ?  125 PRO   A CA   1 
ATOM   2538 C  C    A PRO   A 1 125 ? 18.011 -5.189  3.264   0.82 11.37 ?  125 PRO   A C    1 
ATOM   2539 C  C    B PRO   A 1 125 ? 17.924 -5.181  3.235   0.18 11.42 ?  125 PRO   A C    1 
ATOM   2540 O  O    A PRO   A 1 125 ? 18.994 -5.926  3.148   0.82 11.61 ?  125 PRO   A O    1 
ATOM   2541 O  O    B PRO   A 1 125 ? 18.828 -6.016  3.126   0.18 11.60 ?  125 PRO   A O    1 
ATOM   2542 C  CB   A PRO   A 1 125 ? 18.377 -2.763  3.741   0.82 11.23 ?  125 PRO   A CB   1 
ATOM   2543 C  CB   B PRO   A 1 125 ? 18.141 -2.783  3.947   0.18 11.89 ?  125 PRO   A CB   1 
ATOM   2544 C  CG   A PRO   A 1 125 ? 19.892 -2.924  3.658   0.82 11.35 ?  125 PRO   A CG   1 
ATOM   2545 C  CG   B PRO   A 1 125 ? 19.634 -2.703  3.840   0.18 12.14 ?  125 PRO   A CG   1 
ATOM   2546 C  CD   A PRO   A 1 125 ? 20.273 -3.719  4.901   0.82 11.36 ?  125 PRO   A CD   1 
ATOM   2547 C  CD   B PRO   A 1 125 ? 20.201 -3.613  4.924   0.18 12.01 ?  125 PRO   A CD   1 
ATOM   2548 H  HA   A PRO   A 1 125 ? 17.060 -4.054  4.747   0.82 13.46 ?  125 PRO   A HA   1 
ATOM   2549 H  HA   B PRO   A 1 125 ? 17.067 -4.288  4.891   0.18 14.04 ?  125 PRO   A HA   1 
ATOM   2550 H  HB2  A PRO   A 1 125 ? 17.978 -2.647  2.861   0.82 13.52 ?  125 PRO   A HB2  1 
ATOM   2551 H  HB2  B PRO   A 1 125 ? 17.721 -2.636  3.083   0.18 14.31 ?  125 PRO   A HB2  1 
ATOM   2552 H  HB3  A PRO   A 1 125 ? 18.124 -2.037  4.336   0.82 13.52 ?  125 PRO   A HB3  1 
ATOM   2553 H  HB3  B PRO   A 1 125 ? 17.804 -2.158  4.608   0.18 14.31 ?  125 PRO   A HB3  1 
ATOM   2554 H  HG2  A PRO   A 1 125 ? 20.122 -3.412  2.851   0.82 13.66 ?  125 PRO   A HG2  1 
ATOM   2555 H  HG2  B PRO   A 1 125 ? 19.910 -3.008  2.961   0.18 14.61 ?  125 PRO   A HG2  1 
ATOM   2556 H  HG3  A PRO   A 1 125 ? 20.309 -2.049  3.661   0.82 13.66 ?  125 PRO   A HG3  1 
ATOM   2557 H  HG3  B PRO   A 1 125 ? 19.917 -1.787  3.983   0.18 14.61 ?  125 PRO   A HG3  1 
ATOM   2558 H  HD2  A PRO   A 1 125 ? 20.934 -4.391  4.680   0.82 13.67 ?  125 PRO   A HD2  1 
ATOM   2559 H  HD2  B PRO   A 1 125 ? 20.924 -4.152  4.565   0.18 14.45 ?  125 PRO   A HD2  1 
ATOM   2560 H  HD3  A PRO   A 1 125 ? 20.595 -3.118  5.595   0.82 13.67 ?  125 PRO   A HD3  1 
ATOM   2561 H  HD3  B PRO   A 1 125 ? 20.494 -3.087  5.684   0.18 14.45 ?  125 PRO   A HD3  1 
ATOM   2562 N  N    A LEU   A 1 126 ? 16.955 -5.256  2.460   0.82 11.74 ?  126 LEU   A N    1 
ATOM   2563 N  N    B LEU   A 1 126 ? 16.944 -5.067  2.342   0.18 11.13 ?  126 LEU   A N    1 
ATOM   2564 C  CA   A LEU   A 1 126 ? 16.990 -6.087  1.263   0.82 12.02 ?  126 LEU   A CA   1 
ATOM   2565 C  CA   B LEU   A 1 126 ? 16.901 -5.897  1.141   0.18 10.48 ?  126 LEU   A CA   1 
ATOM   2566 C  C    A LEU   A 1 126 ? 17.928 -5.470  0.231   0.82 11.89 ?  126 LEU   A C    1 
ATOM   2567 C  C    B LEU   A 1 126 ? 17.819 -5.298  0.080   0.18 10.25 ?  126 LEU   A C    1 
ATOM   2568 O  O    A LEU   A 1 126 ? 17.733 -4.328  -0.200  0.82 12.29 ?  126 LEU   A O    1 
ATOM   2569 O  O    B LEU   A 1 126 ? 17.489 -4.281  -0.539  0.18 10.14 ?  126 LEU   A O    1 
ATOM   2570 C  CB   A LEU   A 1 126 ? 15.592 -6.252  0.681   0.82 12.82 ?  126 LEU   A CB   1 
ATOM   2571 C  CB   B LEU   A 1 126 ? 15.469 -5.992  0.627   0.18 10.23 ?  126 LEU   A CB   1 
ATOM   2572 C  CG   A LEU   A 1 126 ? 14.677 -7.221  1.432   0.82 13.60 ?  126 LEU   A CG   1 
ATOM   2573 C  CG   B LEU   A 1 126 ? 14.506 -6.747  1.542   0.18 9.89  ?  126 LEU   A CG   1 
ATOM   2574 C  CD1  A LEU   A 1 126 ? 13.257 -7.085  0.921   0.82 14.90 ?  126 LEU   A CD1  1 
ATOM   2575 C  CD1  B LEU   A 1 126 ? 13.089 -6.613  1.020   0.18 10.08 ?  126 LEU   A CD1  1 
ATOM   2576 C  CD2  A LEU   A 1 126 ? 15.153 -8.665  1.285   0.82 13.00 ?  126 LEU   A CD2  1 
ATOM   2577 C  CD2  B LEU   A 1 126 ? 14.903 -8.212  1.649   0.18 9.62  ?  126 LEU   A CD2  1 
ATOM   2578 H  H    A LEU   A 1 126 ? 16.215 -4.831  2.580   0.82 14.13 ?  126 LEU   A H    1 
ATOM   2579 H  H    B LEU   A 1 126 ? 16.281 -4.520  2.416   0.18 13.39 ?  126 LEU   A H    1 
ATOM   2580 H  HA   A LEU   A 1 126 ? 17.333 -6.959  1.494   0.82 14.47 ?  126 LEU   A HA   1 
ATOM   2581 H  HA   B LEU   A 1 126 ? 17.210 -6.792  1.359   0.18 12.61 ?  126 LEU   A HA   1 
ATOM   2582 H  HB2  A LEU   A 1 126 ? 15.154 -5.388  0.679   0.82 15.42 ?  126 LEU   A HB2  1 
ATOM   2583 H  HB2  B LEU   A 1 126 ? 15.120 -5.094  0.514   0.18 12.31 ?  126 LEU   A HB2  1 
ATOM   2584 H  HB3  A LEU   A 1 126 ? 15.674 -6.578  -0.227  0.82 15.42 ?  126 LEU   A HB3  1 
ATOM   2585 H  HB3  B LEU   A 1 126 ? 15.478 -6.450  -0.228  0.18 12.31 ?  126 LEU   A HB3  1 
ATOM   2586 H  HG   A LEU   A 1 126 ? 14.681 -7.001  2.377   0.82 16.36 ?  126 LEU   A HG   1 
ATOM   2587 H  HG   B LEU   A 1 126 ? 14.537 -6.359  2.431   0.18 11.90 ?  126 LEU   A HG   1 
ATOM   2588 H  HD11 A LEU   A 1 126 ? 12.687 -7.709  1.398   0.82 17.92 ?  126 LEU   A HD11 1 
ATOM   2589 H  HD11 B LEU   A 1 126 ? 12.504 -7.182  1.544   0.18 12.13 ?  126 LEU   A HD11 1 
ATOM   2590 H  HD12 A LEU   A 1 126 ? 12.954 -6.177  1.071   0.82 17.92 ?  126 LEU   A HD12 1 
ATOM   2591 H  HD12 B LEU   A 1 126 ? 12.809 -5.689  1.098   0.18 12.13 ?  126 LEU   A HD12 1 
ATOM   2592 H  HD13 A LEU   A 1 126 ? 13.244 -7.286  -0.029  0.82 17.92 ?  126 LEU   A HD13 1 
ATOM   2593 H  HD13 B LEU   A 1 126 ? 13.070 -6.889  0.089   0.18 12.13 ?  126 LEU   A HD13 1 
ATOM   2594 H  HD21 A LEU   A 1 126 ? 14.495 -9.258  1.675   0.82 15.64 ?  126 LEU   A HD21 1 
ATOM   2595 H  HD21 B LEU   A 1 126 ? 14.196 -8.700  2.097   0.18 11.58 ?  126 LEU   A HD21 1 
ATOM   2596 H  HD22 A LEU   A 1 126 ? 15.265 -8.864  0.342   0.82 15.64 ?  126 LEU   A HD22 1 
ATOM   2597 H  HD22 B LEU   A 1 126 ? 15.037 -8.566  0.755   0.18 11.58 ?  126 LEU   A HD22 1 
ATOM   2598 H  HD23 A LEU   A 1 126 ? 16.004 -8.765  1.745   0.82 15.64 ?  126 LEU   A HD23 1 
ATOM   2599 H  HD23 B LEU   A 1 126 ? 15.727 -8.279  2.157   0.18 11.58 ?  126 LEU   A HD23 1 
ATOM   2600 N  N    A LEU   A 1 127 ? 18.945 -6.226  -0.165  0.82 11.83 ?  127 LEU   A N    1 
ATOM   2601 N  N    B LEU   A 1 127 ? 18.973 -5.927  -0.131  0.18 10.02 ?  127 LEU   A N    1 
ATOM   2602 C  CA   A LEU   A 1 127 ? 19.934 -5.719  -1.102  0.82 11.59 ?  127 LEU   A CA   1 
ATOM   2603 C  CA   B LEU   A 1 127 ? 19.930 -5.433  -1.114  0.18 10.02 ?  127 LEU   A CA   1 
ATOM   2604 C  C    A LEU   A 1 127 ? 19.316 -5.500  -2.471  0.82 11.33 ?  127 LEU   A C    1 
ATOM   2605 C  C    B LEU   A 1 127 ? 19.342 -5.440  -2.532  0.18 10.42 ?  127 LEU   A C    1 
ATOM   2606 O  O    A LEU   A 1 127 ? 18.492 -6.289  -2.947  0.82 11.85 ?  127 LEU   A O    1 
ATOM   2607 O  O    B LEU   A 1 127 ? 18.450 -6.225  -2.866  0.18 10.60 ?  127 LEU   A O    1 
ATOM   2608 C  CB   A LEU   A 1 127 ? 21.104 -6.692  -1.221  0.82 11.87 ?  127 LEU   A CB   1 
ATOM   2609 C  CB   B LEU   A 1 127 ? 21.205 -6.275  -1.046  0.18 9.81  ?  127 LEU   A CB   1 
ATOM   2610 C  CG   A LEU   A 1 127 ? 21.914 -6.932  0.051   0.82 11.98 ?  127 LEU   A CG   1 
ATOM   2611 C  CG   B LEU   A 1 127 ? 21.946 -6.279  0.290   0.18 9.74  ?  127 LEU   A CG   1 
ATOM   2612 C  CD1  A LEU   A 1 127 ? 23.017 -7.922  -0.223  0.82 12.37 ?  127 LEU   A CD1  1 
ATOM   2613 C  CD1  B LEU   A 1 127 ? 23.113 -7.241  0.195   0.18 9.86  ?  127 LEU   A CD1  1 
ATOM   2614 C  CD2  A LEU   A 1 127 ? 22.507 -5.642  0.576   0.82 12.82 ?  127 LEU   A CD2  1 
ATOM   2615 C  CD2  B LEU   A 1 127 ? 22.421 -4.876  0.631   0.18 10.04 ?  127 LEU   A CD2  1 
ATOM   2616 H  H    A LEU   A 1 127 ? 19.086 -7.030  0.101   0.82 14.23 ?  127 LEU   A H    1 
ATOM   2617 H  H    B LEU   A 1 127 ? 19.243 -6.621  0.315   0.18 12.06 ?  127 LEU   A H    1 
ATOM   2618 H  HA   A LEU   A 1 127 ? 20.270 -4.870  -0.782  0.82 13.95 ?  127 LEU   A HA   1 
ATOM   2619 H  HA   B LEU   A 1 127 ? 20.177 -4.514  -0.893  0.18 12.06 ?  127 LEU   A HA   1 
ATOM   2620 H  HB2  A LEU   A 1 127 ? 20.760 -7.549  -1.513  0.82 14.29 ?  127 LEU   A HB2  1 
ATOM   2621 H  HB2  B LEU   A 1 127 ? 20.981 -7.195  -1.238  0.18 11.81 ?  127 LEU   A HB2  1 
ATOM   2622 H  HB3  A LEU   A 1 127 ? 21.717 -6.346  -1.890  0.82 14.29 ?  127 LEU   A HB3  1 
ATOM   2623 H  HB3  B LEU   A 1 127 ? 21.834 -5.945  -1.702  0.18 11.81 ?  127 LEU   A HB3  1 
ATOM   2624 H  HG   A LEU   A 1 127 ? 21.331 -7.301  0.737   0.82 14.42 ?  127 LEU   A HG   1 
ATOM   2625 H  HG   B LEU   A 1 127 ? 21.355 -6.588  1.003   0.18 11.73 ?  127 LEU   A HG   1 
ATOM   2626 H  HD11 A LEU   A 1 127 ? 23.505 -8.087  0.601   0.82 14.88 ?  127 LEU   A HD11 1 
ATOM   2627 H  HD11 B LEU   A 1 127 ? 23.650 -7.174  0.997   0.18 11.87 ?  127 LEU   A HD11 1 
ATOM   2628 H  HD12 A LEU   A 1 127 ? 22.627 -8.751  -0.544  0.82 14.88 ?  127 LEU   A HD12 1 
ATOM   2629 H  HD12 B LEU   A 1 127 ? 22.768 -8.144  0.100   0.18 11.87 ?  127 LEU   A HD12 1 
ATOM   2630 H  HD13 A LEU   A 1 127 ? 23.612 -7.554  -0.892  0.82 14.88 ?  127 LEU   A HD13 1 
ATOM   2631 H  HD13 B LEU   A 1 127 ? 23.644 -7.007  -0.582  0.18 11.87 ?  127 LEU   A HD13 1 
ATOM   2632 H  HD21 A LEU   A 1 127 ? 23.120 -5.847  1.299   0.82 15.42 ?  127 LEU   A HD21 1 
ATOM   2633 H  HD21 B LEU   A 1 127 ? 23.006 -4.916  1.403   0.18 12.08 ?  127 LEU   A HD21 1 
ATOM   2634 H  HD22 A LEU   A 1 127 ? 22.987 -5.201  -0.147  0.82 15.42 ?  127 LEU   A HD22 1 
ATOM   2635 H  HD22 B LEU   A 1 127 ? 22.900 -4.518  -0.132  0.18 12.08 ?  127 LEU   A HD22 1 
ATOM   2636 H  HD23 A LEU   A 1 127 ? 21.795 -5.069  0.895   0.82 15.42 ?  127 LEU   A HD23 1 
ATOM   2637 H  HD23 B LEU   A 1 127 ? 21.649 -4.324  0.828   0.18 12.08 ?  127 LEU   A HD23 1 
ATOM   2638 N  N    A SER   A 1 128 ? 19.736 -4.414  -3.108  0.82 10.87 ?  128 SER   A N    1 
ATOM   2639 N  N    B SER   A 1 128 ? 19.879 -4.540  -3.363  0.18 10.46 ?  128 SER   A N    1 
ATOM   2640 C  CA   A SER   A 1 128 ? 19.324 -4.015  -4.446  0.82 11.32 ?  128 SER   A CA   1 
ATOM   2641 C  CA   B SER   A 1 128 ? 19.465 -4.202  -4.730  0.18 10.32 ?  128 SER   A CA   1 
ATOM   2642 C  C    A SER   A 1 128 ? 17.870 -3.564  -4.518  0.82 11.64 ?  128 SER   A C    1 
ATOM   2643 C  C    B SER   A 1 128 ? 18.031 -3.696  -4.887  0.18 10.15 ?  128 SER   A C    1 
ATOM   2644 O  O    A SER   A 1 128 ? 17.386 -3.276  -5.614  0.82 12.94 ?  128 SER   A O    1 
ATOM   2645 O  O    B SER   A 1 128 ? 17.665 -3.241  -5.976  0.18 10.05 ?  128 SER   A O    1 
ATOM   2646 C  CB   A SER   A 1 128 ? 19.647 -5.062  -5.520  0.82 11.21 ?  128 SER   A CB   1 
ATOM   2647 C  CB   B SER   A 1 128 ? 19.758 -5.299  -5.768  0.18 10.63 ?  128 SER   A CB   1 
ATOM   2648 O  OG   A SER   A 1 128 ? 21.058 -5.249  -5.629  0.82 11.72 ?  128 SER   A OG   1 
ATOM   2649 O  OG   B SER   A 1 128 ? 21.134 -5.657  -5.766  0.18 10.75 ?  128 SER   A OG   1 
ATOM   2650 H  H    A SER   A 1 128 ? 20.312 -3.863  -2.769  0.82 13.08 ?  128 SER   A H    1 
ATOM   2651 H  H    B SER   A 1 128 ? 20.552 -4.077  -3.125  0.18 12.60 ?  128 SER   A H    1 
ATOM   2652 H  HA   A SER   A 1 128 ? 19.849 -3.238  -4.676  0.82 13.62 ?  128 SER   A HA   1 
ATOM   2653 H  HA   B SER   A 1 128 ? 20.038 -3.468  -4.978  0.18 12.42 ?  128 SER   A HA   1 
ATOM   2654 H  HB2  A SER   A 1 128 ? 19.224 -5.901  -5.288  0.82 13.49 ?  128 SER   A HB2  1 
ATOM   2655 H  HB2  B SER   A 1 128 ? 19.224 -6.080  -5.587  0.18 12.79 ?  128 SER   A HB2  1 
ATOM   2656 H  HB3  A SER   A 1 128 ? 19.304 -4.747  -6.379  0.82 13.49 ?  128 SER   A HB3  1 
ATOM   2657 H  HB3  B SER   A 1 128 ? 19.517 -4.948  -6.659  0.18 12.79 ?  128 SER   A HB3  1 
ATOM   2658 H  HG   A SER   A 1 128 ? 21.429 -4.527  -5.830  0.82 14.10 ?  128 SER   A HG   1 
ATOM   2659 H  HG   B SER   A 1 128 ? 21.616 -5.006  -5.985  0.18 12.94 ?  128 SER   A HG   1 
ATOM   2660 N  N    A ALA   A 1 129 ? 17.171 -3.471  -3.385  0.82 11.88 ?  129 ALA   A N    1 
ATOM   2661 N  N    B ALA   A 1 129 ? 17.214 -3.755  -3.836  0.18 10.41 ?  129 ALA   A N    1 
ATOM   2662 C  CA   A ALA   A 1 129 ? 15.807 -2.964  -3.372  0.82 12.20 ?  129 ALA   A CA   1 
ATOM   2663 C  CA   B ALA   A 1 129 ? 15.862 -3.218  -3.897  0.18 10.67 ?  129 ALA   A CA   1 
ATOM   2664 C  C    A ALA   A 1 129 ? 15.817 -1.433  -3.392  0.82 11.90 ?  129 ALA   A C    1 
ATOM   2665 C  C    B ALA   A 1 129 ? 15.898 -1.720  -3.587  0.18 11.35 ?  129 ALA   A C    1 
ATOM   2666 O  O    A ALA   A 1 129 ? 16.864 -0.783  -3.494  0.82 12.00 ?  129 ALA   A O    1 
ATOM   2667 O  O    B ALA   A 1 129 ? 16.958 -1.088  -3.591  0.18 11.80 ?  129 ALA   A O    1 
ATOM   2668 C  CB   A ALA   A 1 129 ? 15.035 -3.531  -2.178  0.82 13.33 ?  129 ALA   A CB   1 
ATOM   2669 C  CB   B ALA   A 1 129 ? 14.931 -3.993  -2.962  0.18 10.04 ?  129 ALA   A CB   1 
ATOM   2670 H  H    A ALA   A 1 129 ? 17.470 -3.698  -2.606  0.82 14.30 ?  129 ALA   A H    1 
ATOM   2671 H  H    B ALA   A 1 129 ? 17.413 -4.104  -3.077  0.18 12.54 ?  129 ALA   A H    1 
ATOM   2672 H  HA   A ALA   A 1 129 ? 15.361 -3.265  -4.176  0.82 14.68 ?  129 ALA   A HA   1 
ATOM   2673 H  HA   B ALA   A 1 129 ? 15.526 -3.330  -4.800  0.18 12.84 ?  129 ALA   A HA   1 
ATOM   2674 H  HB1  A ALA   A 1 129 ? 14.127 -3.186  -2.197  0.82 16.03 ?  129 ALA   A HB1  1 
ATOM   2675 H  HB1  B ALA   A 1 129 ? 14.031 -3.636  -3.048  0.18 12.09 ?  129 ALA   A HB1  1 
ATOM   2676 H  HB2  A ALA   A 1 129 ? 15.020 -4.500  -2.241  0.82 16.03 ?  129 ALA   A HB2  1 
ATOM   2677 H  HB2  B ALA   A 1 129 ? 14.939 -4.929  -3.211  0.18 12.09 ?  129 ALA   A HB2  1 
ATOM   2678 H  HB3  A ALA   A 1 129 ? 15.473 -3.261  -1.357  0.82 16.03 ?  129 ALA   A HB3  1 
ATOM   2679 H  HB3  B ALA   A 1 129 ? 15.241 -3.888  -2.049  0.18 12.09 ?  129 ALA   A HB3  1 
ATOM   2680 N  N    A GLY   A 1 130 ? 14.628 -0.845  -3.316  0.82 13.15 ?  130 GLY   A N    1 
ATOM   2681 N  N    B GLY   A 1 130 ? 14.734 -1.131  -3.326  0.18 11.97 ?  130 GLY   A N    1 
ATOM   2682 C  CA   A GLY   A 1 130 ? 14.545 0.604   -3.305  0.82 13.53 ?  130 GLY   A CA   1 
ATOM   2683 C  CA   B GLY   A 1 130 ? 14.707 0.286   -2.999  0.18 12.08 ?  130 GLY   A CA   1 
ATOM   2684 C  C    A GLY   A 1 130 ? 15.165 1.202   -4.551  0.82 13.14 ?  130 GLY   A C    1 
ATOM   2685 C  C    B GLY   A 1 130 ? 15.113 1.115   -4.203  0.18 12.13 ?  130 GLY   A C    1 
ATOM   2686 O  O    A GLY   A 1 130 ? 14.936 0.734   -5.673  0.82 13.08 ?  130 GLY   A O    1 
ATOM   2687 O  O    B GLY   A 1 130 ? 14.681 0.863   -5.333  0.18 12.05 ?  130 GLY   A O    1 
ATOM   2688 H  H    A GLY   A 1 130 ? 13.874 -1.258  -3.278  0.82 15.81 ?  130 GLY   A H    1 
ATOM   2689 H  H    B GLY   A 1 130 ? 13.964 -1.519  -3.352  0.18 14.40 ?  130 GLY   A H    1 
ATOM   2690 H  HA2  A GLY   A 1 130 ? 13.612 0.872   -3.254  0.82 16.27 ?  130 GLY   A HA2  1 
ATOM   2691 H  HA2  B GLY   A 1 130 ? 13.813 0.543   -2.716  0.18 14.53 ?  130 GLY   A HA2  1 
ATOM   2692 H  HA3  A GLY   A 1 130 ? 15.010 0.949   -2.530  0.82 16.27 ?  130 GLY   A HA3  1 
ATOM   2693 H  HA3  B GLY   A 1 130 ? 15.326 0.464   -2.271  0.18 14.53 ?  130 GLY   A HA3  1 
ATOM   2694 N  N    A ILE   A 1 131 ? 15.969 2.254   -4.356  0.82 12.73 ?  131 ILE   A N    1 
ATOM   2695 N  N    B ILE   A 1 131 ? 15.967 2.115   -3.968  0.18 12.35 ?  131 ILE   A N    1 
ATOM   2696 C  CA   A ILE   A 1 131 ? 16.537 2.997   -5.478  0.82 12.60 ?  131 ILE   A CA   1 
ATOM   2697 C  CA   B ILE   A 1 131 ? 16.436 2.969   -5.054  0.18 12.30 ?  131 ILE   A CA   1 
ATOM   2698 C  C    A ILE   A 1 131 ? 17.548 2.199   -6.288  0.82 12.32 ?  131 ILE   A C    1 
ATOM   2699 C  C    B ILE   A 1 131 ? 17.409 2.265   -5.989  0.18 12.01 ?  131 ILE   A C    1 
ATOM   2700 O  O    A ILE   A 1 131 ? 17.967 2.669   -7.355  0.82 13.30 ?  131 ILE   A O    1 
ATOM   2701 O  O    B ILE   A 1 131 ? 17.782 2.839   -7.018  0.18 12.17 ?  131 ILE   A O    1 
ATOM   2702 C  CB   A ILE   A 1 131 ? 17.115 4.367   -5.059  0.82 13.72 ?  131 ILE   A CB   1 
ATOM   2703 C  CB   B ILE   A 1 131 ? 17.061 4.274   -4.516  0.18 12.73 ?  131 ILE   A CB   1 
ATOM   2704 C  CG1  A ILE   A 1 131 ? 18.385 4.210   -4.209  0.82 14.74 ?  131 ILE   A CG1  1 
ATOM   2705 C  CG1  B ILE   A 1 131 ? 18.292 3.971   -3.659  0.18 13.09 ?  131 ILE   A CG1  1 
ATOM   2706 C  CG2  A ILE   A 1 131 ? 16.054 5.193   -4.329  0.82 14.22 ?  131 ILE   A CG2  1 
ATOM   2707 C  CG2  B ILE   A 1 131 ? 16.033 5.063   -3.714  0.18 12.88 ?  131 ILE   A CG2  1 
ATOM   2708 C  CD1  A ILE   A 1 131 ? 19.020 5.544   -3.814  0.82 16.13 ?  131 ILE   A CD1  1 
ATOM   2709 C  CD1  B ILE   A 1 131 ? 19.041 5.208   -3.213  0.18 13.28 ?  131 ILE   A CD1  1 
ATOM   2710 H  H    A ILE   A 1 131 ? 16.184 2.556   -3.580  0.82 15.32 ?  131 ILE   A H    1 
ATOM   2711 H  H    B ILE   A 1 131 ? 16.281 2.321   -3.194  0.18 14.86 ?  131 ILE   A H    1 
ATOM   2712 H  HA   A ILE   A 1 131 ? 15.812 3.191   -6.081  0.82 15.15 ?  131 ILE   A HA   1 
ATOM   2713 H  HA   B ILE   A 1 131 ? 15.668 3.225   -5.586  0.18 14.79 ?  131 ILE   A HA   1 
ATOM   2714 H  HB   A ILE   A 1 131 ? 17.356 4.844   -5.866  0.82 16.51 ?  131 ILE   A HB   1 
ATOM   2715 H  HB   B ILE   A 1 131 ? 17.338 4.817   -5.273  0.18 15.32 ?  131 ILE   A HB   1 
ATOM   2716 H  HG12 A ILE   A 1 131 ? 18.163 3.733   -3.396  0.82 17.73 ?  131 ILE   A HG12 1 
ATOM   2717 H  HG12 B ILE   A 1 131 ? 18.007 3.494   -2.864  0.18 15.75 ?  131 ILE   A HG12 1 
ATOM   2718 H  HG13 A ILE   A 1 131 ? 19.046 3.711   -4.715  0.82 17.73 ?  131 ILE   A HG13 1 
ATOM   2719 H  HG13 B ILE   A 1 131 ? 18.907 3.424   -4.170  0.18 15.75 ?  131 ILE   A HG13 1 
ATOM   2720 H  HG21 A ILE   A 1 131 ? 16.371 6.103   -4.231  0.82 17.10 ?  131 ILE   A HG21 1 
ATOM   2721 H  HG21 B ILE   A 1 131 ? 16.397 5.937   -3.503  0.18 15.50 ?  131 ILE   A HG21 1 
ATOM   2722 H  HG22 A ILE   A 1 131 ? 15.236 5.182   -4.850  0.82 17.10 ?  131 ILE   A HG22 1 
ATOM   2723 H  HG22 B ILE   A 1 131 ? 15.227 5.161   -4.246  0.18 15.50 ?  131 ILE   A HG22 1 
ATOM   2724 H  HG23 A ILE   A 1 131 ? 15.894 4.800   -3.456  0.82 17.10 ?  131 ILE   A HG23 1 
ATOM   2725 H  HG23 B ILE   A 1 131 ? 15.833 4.579   -2.898  0.18 15.50 ?  131 ILE   A HG23 1 
ATOM   2726 H  HD11 A ILE   A 1 131 ? 19.879 5.374   -3.393  0.82 19.40 ?  131 ILE   A HD11 1 
ATOM   2727 H  HD11 B ILE   A 1 131 ? 19.866 4.937   -2.783  0.18 15.97 ?  131 ILE   A HD11 1 
ATOM   2728 H  HD12 A ILE   A 1 131 ? 19.146 6.085   -4.610  0.82 19.40 ?  131 ILE   A HD12 1 
ATOM   2729 H  HD12 B ILE   A 1 131 ? 19.238 5.754   -3.991  0.18 15.97 ?  131 ILE   A HD12 1 
ATOM   2730 H  HD13 A ILE   A 1 131 ? 18.435 6.004   -3.191  0.82 19.40 ?  131 ILE   A HD13 1 
ATOM   2731 H  HD13 B ILE   A 1 131 ? 18.490 5.706   -2.590  0.18 15.97 ?  131 ILE   A HD13 1 
ATOM   2732 N  N    A PHE   A 1 132 ? 17.952 1.008   -5.825  0.82 11.98 ?  132 PHE   A N    1 
ATOM   2733 N  N    B PHE   A 1 132 ? 17.830 1.040   -5.666  0.18 12.02 ?  132 PHE   A N    1 
ATOM   2734 C  CA   A PHE   A 1 132 ? 18.791 0.141   -6.647  0.82 12.35 ?  132 PHE   A CA   1 
ATOM   2735 C  CA   B PHE   A 1 132 ? 18.769 0.320   -6.519  0.18 12.20 ?  132 PHE   A CA   1 
ATOM   2736 C  C    A PHE   A 1 132 ? 17.994 -0.616  -7.709  0.82 13.16 ?  132 PHE   A C    1 
ATOM   2737 C  C    B PHE   A 1 132 ? 18.098 -0.375  -7.699  0.18 12.51 ?  132 PHE   A C    1 
ATOM   2738 O  O    A PHE   A 1 132 ? 18.603 -1.267  -8.563  0.82 13.39 ?  132 PHE   A O    1 
ATOM   2739 O  O    B PHE   A 1 132 ? 18.799 -0.781  -8.632  0.18 12.54 ?  132 PHE   A O    1 
ATOM   2740 C  CB   A PHE   A 1 132 ? 19.599 -0.838  -5.785  0.82 12.07 ?  132 PHE   A CB   1 
ATOM   2741 C  CB   B PHE   A 1 132 ? 19.598 -0.677  -5.702  0.18 11.99 ?  132 PHE   A CB   1 
ATOM   2742 C  CG   A PHE   A 1 132 ? 20.818 -0.232  -5.119  0.82 12.03 ?  132 PHE   A CG   1 
ATOM   2743 C  CG   B PHE   A 1 132 ? 20.836 -0.079  -5.082  0.18 11.96 ?  132 PHE   A CG   1 
ATOM   2744 C  CD1  A PHE   A 1 132 ? 20.696 0.806   -4.212  0.82 12.82 ?  132 PHE   A CD1  1 
ATOM   2745 C  CD1  B PHE   A 1 132 ? 20.740 0.866   -4.074  0.18 12.25 ?  132 PHE   A CD1  1 
ATOM   2746 C  CD2  A PHE   A 1 132 ? 22.084 -0.738  -5.374  0.82 12.46 ?  132 PHE   A CD2  1 
ATOM   2747 C  CD2  B PHE   A 1 132 ? 22.096 -0.474  -5.502  0.18 11.92 ?  132 PHE   A CD2  1 
ATOM   2748 C  CE1  A PHE   A 1 132 ? 21.817 1.343   -3.594  0.82 13.29 ?  132 PHE   A CE1  1 
ATOM   2749 C  CE1  B PHE   A 1 132 ? 21.878 1.413   -3.503  0.18 12.47 ?  132 PHE   A CE1  1 
ATOM   2750 C  CE2  A PHE   A 1 132 ? 23.204 -0.210  -4.756  0.82 12.91 ?  132 PHE   A CE2  1 
ATOM   2751 C  CE2  B PHE   A 1 132 ? 23.238 0.068   -4.933  0.18 12.33 ?  132 PHE   A CE2  1 
ATOM   2752 C  CZ   A PHE   A 1 132 ? 23.067 0.831   -3.863  0.82 12.99 ?  132 PHE   A CZ   1 
ATOM   2753 C  CZ   B PHE   A 1 132 ? 23.127 1.011   -3.932  0.18 12.47 ?  132 PHE   A CZ   1 
ATOM   2754 H  H    A PHE   A 1 132 ? 17.755 0.684   -5.046  0.82 14.41 ?  132 PHE   A H    1 
ATOM   2755 H  H    B PHE   A 1 132 ? 17.584 0.611   -4.963  0.18 14.46 ?  132 PHE   A H    1 
ATOM   2756 H  HA   A PHE   A 1 132 ? 19.430 0.700   -7.108  0.82 14.86 ?  132 PHE   A HA   1 
ATOM   2757 H  HA   B PHE   A 1 132 ? 19.390 0.967   -6.885  0.18 14.68 ?  132 PHE   A HA   1 
ATOM   2758 H  HB2  A PHE   A 1 132 ? 19.026 -1.183  -5.083  0.82 14.52 ?  132 PHE   A HB2  1 
ATOM   2759 H  HB2  B PHE   A 1 132 ? 19.050 -1.029  -4.985  0.18 14.43 ?  132 PHE   A HB2  1 
ATOM   2760 H  HB3  A PHE   A 1 132 ? 19.905 -1.572  -6.346  0.82 14.52 ?  132 PHE   A HB3  1 
ATOM   2761 H  HB3  B PHE   A 1 132 ? 19.880 -1.399  -6.286  0.18 14.43 ?  132 PHE   A HB3  1 
ATOM   2762 H  HD1  A PHE   A 1 132 ? 19.857 1.155   -4.019  0.82 15.42 ?  132 PHE   A HD1  1 
ATOM   2763 H  HD1  B PHE   A 1 132 ? 19.901 1.142   -3.782  0.18 14.74 ?  132 PHE   A HD1  1 
ATOM   2764 H  HD2  A PHE   A 1 132 ? 22.186 -1.444  -5.976  0.82 14.99 ?  132 PHE   A HD2  1 
ATOM   2765 H  HD2  B PHE   A 1 132 ? 22.179 -1.110  -6.177  0.18 14.34 ?  132 PHE   A HD2  1 
ATOM   2766 H  HE1  A PHE   A 1 132 ? 21.725 2.046   -2.991  0.82 15.98 ?  132 PHE   A HE1  1 
ATOM   2767 H  HE1  B PHE   A 1 132 ? 21.802 2.049   -2.828  0.18 15.00 ?  132 PHE   A HE1  1 
ATOM   2768 H  HE2  A PHE   A 1 132 ? 24.047 -0.555  -4.949  0.82 15.53 ?  132 PHE   A HE2  1 
ATOM   2769 H  HE2  B PHE   A 1 132 ? 24.079 -0.205  -5.226  0.18 14.83 ?  132 PHE   A HE2  1 
ATOM   2770 H  HZ   A PHE   A 1 132 ? 23.819 1.195   -3.454  0.82 15.62 ?  132 PHE   A HZ   1 
ATOM   2771 H  HZ   B PHE   A 1 132 ? 23.894 1.376   -3.550  0.18 15.00 ?  132 PHE   A HZ   1 
ATOM   2772 N  N    A GLY   A 1 133 ? 16.660 -0.570  -7.667  0.82 13.27 ?  133 GLY   A N    1 
ATOM   2773 N  N    B GLY   A 1 133 ? 16.773 -0.531  -7.689  0.18 12.66 ?  133 GLY   A N    1 
ATOM   2774 C  CA   A GLY   A 1 133 ? 15.846 -0.941  -8.808  0.82 14.09 ?  133 GLY   A CA   1 
ATOM   2775 C  CA   B GLY   A 1 133 ? 16.023 -0.883  -8.879  0.18 12.89 ?  133 GLY   A CA   1 
ATOM   2776 C  C    A GLY   A 1 133 ? 15.532 -2.411  -9.000  0.82 14.26 ?  133 GLY   A C    1 
ATOM   2777 C  C    B GLY   A 1 133 ? 15.414 -2.272  -8.903  0.18 12.82 ?  133 GLY   A C    1 
ATOM   2778 O  O    A GLY   A 1 133 ? 14.876 -2.746  -9.995  0.82 15.58 ?  133 GLY   A O    1 
ATOM   2779 O  O    B GLY   A 1 133 ? 14.523 -2.518  -9.727  0.18 12.96 ?  133 GLY   A O    1 
ATOM   2780 H  H    A GLY   A 1 133 ? 16.205 -0.329  -6.975  0.82 15.96 ?  133 GLY   A H    1 
ATOM   2781 H  H    B GLY   A 1 133 ? 16.284 -0.424  -6.987  0.18 15.23 ?  133 GLY   A H    1 
ATOM   2782 H  HA2  A GLY   A 1 133 ? 15.001 -0.475  -8.744  0.82 16.94 ?  133 GLY   A HA2  1 
ATOM   2783 H  HA2  B GLY   A 1 133 ? 15.294 -0.258  -8.979  0.18 15.51 ?  133 GLY   A HA2  1 
ATOM   2784 H  HA3  A GLY   A 1 133 ? 16.293 -0.635  -9.612  0.82 16.94 ?  133 GLY   A HA3  1 
ATOM   2785 H  HA3  B GLY   A 1 133 ? 16.602 -0.788  -9.654  0.18 15.51 ?  133 GLY   A HA3  1 
ATOM   2786 N  N    A ALA   A 1 134 ? 15.969 -3.301  -8.111  0.82 13.78 ?  134 ALA   A N    1 
ATOM   2787 N  N    B ALA   A 1 134 ? 15.848 -3.186  -8.042  0.18 12.67 ?  134 ALA   A N    1 
ATOM   2788 C  CA   A ALA   A 1 134 ? 15.624 -4.703  -8.277  0.82 14.15 ?  134 ALA   A CA   1 
ATOM   2789 C  CA   B ALA   A 1 134 ? 15.389 -4.564  -8.146  0.18 12.64 ?  134 ALA   A CA   1 
ATOM   2790 C  C    A ALA   A 1 134 ? 14.249 -4.992  -7.673  0.82 14.28 ?  134 ALA   A C    1 
ATOM   2791 C  C    B ALA   A 1 134 ? 14.107 -4.787  -7.349  0.18 12.34 ?  134 ALA   A C    1 
ATOM   2792 O  O    A ALA   A 1 134 ? 13.693 -4.203  -6.903  0.82 15.54 ?  134 ALA   A O    1 
ATOM   2793 O  O    B ALA   A 1 134 ? 13.748 -4.012  -6.460  0.18 12.30 ?  134 ALA   A O    1 
ATOM   2794 C  CB   A ALA   A 1 134 ? 16.690 -5.603  -7.654  0.82 15.45 ?  134 ALA   A CB   1 
ATOM   2795 C  CB   B ALA   A 1 134 ? 16.463 -5.542  -7.672  0.18 13.09 ?  134 ALA   A CB   1 
ATOM   2796 H  H    A ALA   A 1 134 ? 16.471 -3.119  -7.428  0.82 16.57 ?  134 ALA   A H    1 
ATOM   2797 H  H    B ALA   A 1 134 ? 16.398 -3.035  -7.398  0.18 15.24 ?  134 ALA   A H    1 
ATOM   2798 H  HA   A ALA   A 1 134 ? 15.587 -4.902  -9.227  0.82 17.02 ?  134 ALA   A HA   1 
ATOM   2799 H  HA   B ALA   A 1 134 ? 15.198 -4.757  -9.076  0.18 15.21 ?  134 ALA   A HA   1 
ATOM   2800 H  HB1  A ALA   A 1 134 ? 16.438 -6.528  -7.796  0.82 18.58 ?  134 ALA   A HB1  1 
ATOM   2801 H  HB1  B ALA   A 1 134 ? 16.123 -6.446  -7.768  0.18 15.74 ?  134 ALA   A HB1  1 
ATOM   2802 H  HB2  A ALA   A 1 134 ? 17.545 -5.424  -8.080  0.82 18.58 ?  134 ALA   A HB2  1 
ATOM   2803 H  HB2  B ALA   A 1 134 ? 17.254 -5.424  -8.217  0.18 15.74 ?  134 ALA   A HB2  1 
ATOM   2804 H  HB3  A ALA   A 1 134 ? 16.747 -5.414  -6.706  0.82 18.58 ?  134 ALA   A HB3  1 
ATOM   2805 H  HB3  B ALA   A 1 134 ? 16.665 -5.361  -6.743  0.18 15.74 ?  134 ALA   A HB3  1 
ATOM   2806 N  N    A ASP   A 1 135 ? 13.706 -6.148  -8.034  0.82 14.92 ?  135 ASP   A N    1 
ATOM   2807 N  N    B ASP   A 1 135 ? 13.424 -5.873  -7.687  0.18 12.33 ?  135 ASP   A N    1 
ATOM   2808 C  CA   A ASP   A 1 135 ? 12.446 -6.622  -7.467  0.82 15.88 ?  135 ASP   A CA   1 
ATOM   2809 C  CA   B ASP   A 1 135 ? 12.189 -6.262  -7.020  0.18 12.01 ?  135 ASP   A CA   1 
ATOM   2810 C  C    A ASP   A 1 135 ? 12.694 -7.080  -6.035  0.82 15.23 ?  135 ASP   A C    1 
ATOM   2811 C  C    B ASP   A 1 135 ? 12.504 -6.751  -5.611  0.18 11.57 ?  135 ASP   A C    1 
ATOM   2812 O  O    A ASP   A 1 135 ? 13.477 -8.015  -5.826  0.82 15.00 ?  135 ASP   A O    1 
ATOM   2813 O  O    B ASP   A 1 135 ? 13.235 -7.739  -5.460  0.18 11.63 ?  135 ASP   A O    1 
ATOM   2814 C  CB   A ASP   A 1 135 ? 11.949 -7.794  -8.314  0.82 18.28 ?  135 ASP   A CB   1 
ATOM   2815 C  CB   B ASP   A 1 135 ? 11.549 -7.389  -7.822  0.18 11.98 ?  135 ASP   A CB   1 
ATOM   2816 C  CG   A ASP   A 1 135 ? 10.660 -8.421  -7.784  0.82 20.65 ?  135 ASP   A CG   1 
ATOM   2817 C  CG   B ASP   A 1 135 ? 10.141 -7.711  -7.362  0.18 12.31 ?  135 ASP   A CG   1 
ATOM   2818 O  OD1  A ASP   A 1 135 ? 10.134 -7.976  -6.744  0.82 20.84 ?  135 ASP   A OD1  1 
ATOM   2819 O  OD1  B ASP   A 1 135 ? 9.795  -7.364  -6.213  0.18 12.15 ?  135 ASP   A OD1  1 
ATOM   2820 O  OD2  A ASP   A 1 135 ? 10.168 -9.371  -8.431  0.82 23.40 -1 135 ASP   A OD2  1 
ATOM   2821 O  OD2  B ASP   A 1 135 ? 9.387  -8.321  -8.149  0.18 12.50 -1 135 ASP   A OD2  1 
ATOM   2822 H  H    A ASP   A 1 135 ? 14.049 -6.682  -8.611  0.82 17.94 ?  135 ASP   A H    1 
ATOM   2823 H  H    B ASP   A 1 135 ? 13.656 -6.410  -8.313  0.18 14.84 ?  135 ASP   A H    1 
ATOM   2824 H  HA   A ASP   A 1 135 ? 11.782 -5.911  -7.489  0.82 19.09 ?  135 ASP   A HA   1 
ATOM   2825 H  HA   B ASP   A 1 135 ? 11.572 -5.509  -6.995  0.18 14.46 ?  135 ASP   A HA   1 
ATOM   2826 H  HB2  A ASP   A 1 135 ? 11.775 -7.481  -9.213  0.82 21.97 ?  135 ASP   A HB2  1 
ATOM   2827 H  HB2  B ASP   A 1 135 ? 11.520 -7.134  -8.758  0.18 14.42 ?  135 ASP   A HB2  1 
ATOM   2828 H  HB3  A ASP   A 1 135 ? 12.633 -8.481  -8.326  0.82 21.97 ?  135 ASP   A HB3  1 
ATOM   2829 H  HB3  B ASP   A 1 135 ? 12.083 -8.192  -7.715  0.18 14.42 ?  135 ASP   A HB3  1 
ATOM   2830 N  N    A PRO   A 1 136 ? 12.072 -6.460  -5.028  0.82 15.29 ?  136 PRO   A N    1 
ATOM   2831 N  N    B PRO   A 1 136 ? 11.988 -6.106  -4.561  0.18 11.15 ?  136 PRO   A N    1 
ATOM   2832 C  CA   A PRO   A 1 136 ? 12.335 -6.879  -3.639  0.82 15.43 ?  136 PRO   A CA   1 
ATOM   2833 C  CA   B PRO   A 1 136 ? 12.264 -6.594  -3.199  0.18 11.50 ?  136 PRO   A CA   1 
ATOM   2834 C  C    A PRO   A 1 136 ? 11.900 -8.302  -3.329  0.82 14.88 ?  136 PRO   A C    1 
ATOM   2835 C  C    B PRO   A 1 136 ? 11.852 -8.041  -2.976  0.18 11.77 ?  136 PRO   A C    1 
ATOM   2836 O  O    A PRO   A 1 136 ? 12.498 -8.944  -2.458  0.82 14.66 ?  136 PRO   A O    1 
ATOM   2837 O  O    B PRO   A 1 136 ? 12.429 -8.715  -2.113  0.18 11.30 ?  136 PRO   A O    1 
ATOM   2838 C  CB   A PRO   A 1 136 ? 11.560 -5.847  -2.810  0.82 16.70 ?  136 PRO   A CB   1 
ATOM   2839 C  CB   B PRO   A 1 136 ? 11.476 -5.618  -2.308  0.18 11.77 ?  136 PRO   A CB   1 
ATOM   2840 C  CG   A PRO   A 1 136 ? 10.503 -5.332  -3.737  0.82 17.95 ?  136 PRO   A CG   1 
ATOM   2841 C  CG   B PRO   A 1 136 ? 10.445 -5.011  -3.214  0.18 11.90 ?  136 PRO   A CG   1 
ATOM   2842 C  CD   A PRO   A 1 136 ? 11.109 -5.348  -5.102  0.82 16.58 ?  136 PRO   A CD   1 
ATOM   2843 C  CD   B PRO   A 1 136 ? 11.110 -4.923  -4.552  0.18 11.17 ?  136 PRO   A CD   1 
ATOM   2844 H  HA   A PRO   A 1 136 ? 13.284 -6.790  -3.440  0.82 18.55 ?  136 PRO   A HA   1 
ATOM   2845 H  HA   B PRO   A 1 136 ? 13.209 -6.501  -2.999  0.18 13.84 ?  136 PRO   A HA   1 
ATOM   2846 H  HB2  A PRO   A 1 136 ? 11.162 -6.281  -2.040  0.82 20.08 ?  136 PRO   A HB2  1 
ATOM   2847 H  HB2  B PRO   A 1 136 ? 11.054 -6.096  -1.579  0.18 14.16 ?  136 PRO   A HB2  1 
ATOM   2848 H  HB3  A PRO   A 1 136 ? 12.157 -5.133  -2.534  0.82 20.08 ?  136 PRO   A HB3  1 
ATOM   2849 H  HB3  B PRO   A 1 136 ? 12.072 -4.929  -1.969  0.18 14.16 ?  136 PRO   A HB3  1 
ATOM   2850 H  HG2  A PRO   A 1 136 ? 9.731  -5.914  -3.702  0.82 21.58 ?  136 PRO   A HG2  1 
ATOM   2851 H  HG2  B PRO   A 1 136 ? 9.666  -5.589  -3.257  0.18 14.32 ?  136 PRO   A HG2  1 
ATOM   2852 H  HG3  A PRO   A 1 136 ? 10.265 -4.427  -3.484  0.82 21.58 ?  136 PRO   A HG3  1 
ATOM   2853 H  HG3  B PRO   A 1 136 ? 10.200 -4.129  -2.895  0.18 14.32 ?  136 PRO   A HG3  1 
ATOM   2854 H  HD2  A PRO   A 1 136 ? 10.428 -5.539  -5.770  0.82 19.93 ?  136 PRO   A HD2  1 
ATOM   2855 H  HD2  B PRO   A 1 136 ? 10.445 -4.983  -5.260  0.18 13.44 ?  136 PRO   A HD2  1 
ATOM   2856 H  HD3  A PRO   A 1 136 ? 11.563 -4.511  -5.288  0.82 19.93 ?  136 PRO   A HD3  1 
ATOM   2857 H  HD3  B PRO   A 1 136 ? 11.633 -4.108  -4.625  0.18 13.44 ?  136 PRO   A HD3  1 
ATOM   2858 N  N    A ILE   A 1 137 ? 10.852 -8.804  -3.984  0.82 14.90 ?  137 ILE   A N    1 
ATOM   2859 N  N    B ILE   A 1 137 ? 10.868 -8.538  -3.727  0.18 12.42 ?  137 ILE   A N    1 
ATOM   2860 C  CA   A ILE   A 1 137 ? 10.474 -10.203 -3.799  0.82 15.56 ?  137 ILE   A CA   1 
ATOM   2861 C  CA   B ILE   A 1 137 ? 10.457 -9.934  -3.593  0.18 13.35 ?  137 ILE   A CA   1 
ATOM   2862 C  C    A ILE   A 1 137 ? 11.621 -11.110 -4.212  0.82 14.85 ?  137 ILE   A C    1 
ATOM   2863 C  C    B ILE   A 1 137 ? 11.595 -10.862 -4.002  0.18 13.53 ?  137 ILE   A C    1 
ATOM   2864 O  O    A ILE   A 1 137 ? 11.927 -12.106 -3.543  0.82 15.30 ?  137 ILE   A O    1 
ATOM   2865 O  O    B ILE   A 1 137 ? 11.931 -11.817 -3.291  0.18 13.70 ?  137 ILE   A O    1 
ATOM   2866 C  CB   A ILE   A 1 137 ? 9.184  -10.524 -4.578  0.82 17.14 ?  137 ILE   A CB   1 
ATOM   2867 C  CB   B ILE   A 1 137 ? 9.184  -10.200 -4.418  0.18 14.04 ?  137 ILE   A CB   1 
ATOM   2868 C  CG1  A ILE   A 1 137 ? 8.000  -9.714  -4.034  0.82 19.29 ?  137 ILE   A CG1  1 
ATOM   2869 C  CG1  B ILE   A 1 137 ? 8.038  -9.291  -3.960  0.18 14.64 ?  137 ILE   A CG1  1 
ATOM   2870 C  CG2  A ILE   A 1 137 ? 8.892  -12.024 -4.529  0.82 17.74 ?  137 ILE   A CG2  1 
ATOM   2871 C  CG2  B ILE   A 1 137 ? 8.784  -11.669 -4.322  0.18 14.34 ?  137 ILE   A CG2  1 
ATOM   2872 C  CD1  A ILE   A 1 137 ? 6.724  -9.886  -4.823  0.82 21.16 ?  137 ILE   A CD1  1 
ATOM   2873 C  CD1  B ILE   A 1 137 ? 6.797  -9.409  -4.815  0.18 15.01 ?  137 ILE   A CD1  1 
ATOM   2874 H  H    A ILE   A 1 137 ? 10.357 -8.366  -4.530  0.82 17.92 ?  137 ILE   A H    1 
ATOM   2875 H  H    B ILE   A 1 137 ? 10.425 -8.086  -4.310  0.18 14.94 ?  137 ILE   A H    1 
ATOM   2876 H  HA   A ILE   A 1 137 ? 10.306 -10.362 -2.861  0.82 18.71 ?  137 ILE   A HA   1 
ATOM   2877 H  HA   B ILE   A 1 137 ? 10.247 -10.108 -2.662  0.18 16.06 ?  137 ILE   A HA   1 
ATOM   2878 H  HB   A ILE   A 1 137 ? 9.319  -10.273 -5.504  0.82 20.61 ?  137 ILE   A HB   1 
ATOM   2879 H  HB   B ILE   A 1 137 ? 9.376  -9.995  -5.345  0.18 16.88 ?  137 ILE   A HB   1 
ATOM   2880 H  HG12 A ILE   A 1 137 ? 7.831  -9.985  -3.119  0.82 23.19 ?  137 ILE   A HG12 1 
ATOM   2881 H  HG12 B ILE   A 1 137 ? 7.795  -9.524  -3.050  0.18 17.61 ?  137 ILE   A HG12 1 
ATOM   2882 H  HG13 A ILE   A 1 137 ? 8.238  -8.769  -4.055  0.82 23.19 ?  137 ILE   A HG13 1 
ATOM   2883 H  HG13 B ILE   A 1 137 ? 8.330  -8.366  -3.996  0.18 17.61 ?  137 ILE   A HG13 1 
ATOM   2884 H  HG21 A ILE   A 1 137 ? 7.978  -12.191 -4.808  0.82 21.32 ?  137 ILE   A HG21 1 
ATOM   2885 H  HG21 B ILE   A 1 137 ? 7.916  -11.795 -4.734  0.18 17.25 ?  137 ILE   A HG21 1 
ATOM   2886 H  HG22 A ILE   A 1 137 ? 9.501  -12.481 -5.128  0.82 21.32 ?  137 ILE   A HG22 1 
ATOM   2887 H  HG22 B ILE   A 1 137 ? 9.445  -12.204 -4.786  0.18 17.25 ?  137 ILE   A HG22 1 
ATOM   2888 H  HG23 A ILE   A 1 137 ? 9.019  -12.336 -3.623  0.82 21.32 ?  137 ILE   A HG23 1 
ATOM   2889 H  HG23 B ILE   A 1 137 ? 8.745  -11.922 -3.388  0.18 17.25 ?  137 ILE   A HG23 1 
ATOM   2890 H  HD11 A ILE   A 1 137 ? 6.025  -10.191 -4.226  0.82 25.43 ?  137 ILE   A HD11 1 
ATOM   2891 H  HD11 B ILE   A 1 137 ? 6.542  -8.527  -5.118  0.18 18.05 ?  137 ILE   A HD11 1 
ATOM   2892 H  HD12 A ILE   A 1 137 ? 6.492  -9.032  -5.210  0.82 25.43 ?  137 ILE   A HD12 1 
ATOM   2893 H  HD12 B ILE   A 1 137 ? 6.990  -9.976  -5.580  0.18 18.05 ?  137 ILE   A HD12 1 
ATOM   2894 H  HD13 A ILE   A 1 137 ? 6.868  -10.534 -5.530  0.82 25.43 ?  137 ILE   A HD13 1 
ATOM   2895 H  HD13 B ILE   A 1 137 ? 6.083  -9.802  -4.286  0.18 18.05 ?  137 ILE   A HD13 1 
ATOM   2896 N  N    A HIS   A 1 138 ? 12.275 -10.773 -5.324  0.82 15.08 ?  138 HIS   A N    1 
ATOM   2897 N  N    B HIS   A 1 138 ? 12.200 -10.595 -5.162  0.18 13.77 ?  138 HIS   A N    1 
ATOM   2898 C  CA   A HIS   A 1 138 ? 13.449 -11.521 -5.748  0.82 15.00 ?  138 HIS   A CA   1 
ATOM   2899 C  CA   B HIS   A 1 138 ? 13.295 -11.432 -5.647  0.18 13.90 ?  138 HIS   A CA   1 
ATOM   2900 C  C    A HIS   A 1 138 ? 14.590 -11.373 -4.749  0.82 14.24 ?  138 HIS   A C    1 
ATOM   2901 C  C    B HIS   A 1 138 ? 14.494 -11.362 -4.711  0.18 13.71 ?  138 HIS   A C    1 
ATOM   2902 O  O    A HIS   A 1 138 ? 15.261 -12.359 -4.419  0.82 14.50 ?  138 HIS   A O    1 
ATOM   2903 O  O    B HIS   A 1 138 ? 15.121 -12.385 -4.409  0.18 13.69 ?  138 HIS   A O    1 
ATOM   2904 C  CB   A HIS   A 1 138 ? 13.869 -11.084 -7.148  0.82 15.68 ?  138 HIS   A CB   1 
ATOM   2905 C  CB   B HIS   A 1 138 ? 13.683 -10.993 -7.060  0.18 14.14 ?  138 HIS   A CB   1 
ATOM   2906 C  CG   A HIS   A 1 138 ? 15.127 -11.736 -7.616  0.82 16.92 ?  138 HIS   A CG   1 
ATOM   2907 C  CG   B HIS   A 1 138 ? 14.975 -11.575 -7.542  0.18 14.47 ?  138 HIS   A CG   1 
ATOM   2908 N  ND1  A HIS   A 1 138 ? 15.218 -13.090 -7.859  0.82 18.26 ?  138 HIS   A ND1  1 
ATOM   2909 N  ND1  B HIS   A 1 138 ? 15.121 -12.910 -7.849  0.18 14.90 ?  138 HIS   A ND1  1 
ATOM   2910 C  CD2  A HIS   A 1 138 ? 16.356 -11.225 -7.858  0.82 17.04 ?  138 HIS   A CD2  1 
ATOM   2911 C  CD2  B HIS   A 1 138 ? 16.180 -11.001 -7.772  0.18 14.46 ?  138 HIS   A CD2  1 
ATOM   2912 C  CE1  A HIS   A 1 138 ? 16.446 -13.382 -8.245  0.82 18.53 ?  138 HIS   A CE1  1 
ATOM   2913 C  CE1  B HIS   A 1 138 ? 16.361 -13.134 -8.247  0.18 14.95 ?  138 HIS   A CE1  1 
ATOM   2914 N  NE2  A HIS   A 1 138 ? 17.157 -12.269 -8.252  0.82 17.84 ?  138 HIS   A NE2  1 
ATOM   2915 N  NE2  B HIS   A 1 138 ? 17.024 -11.993 -8.209  0.18 14.74 ?  138 HIS   A NE2  1 
ATOM   2916 H  H    A HIS   A 1 138 ? 12.056 -10.121 -5.850  0.82 18.14 ?  138 HIS   A H    1 
ATOM   2917 H  H    B HIS   A 1 138 ? 11.999 -9.937  -5.679  0.18 16.56 ?  138 HIS   A H    1 
ATOM   2918 H  HA   A HIS   A 1 138 ? 13.214 -12.459 -5.797  0.82 18.04 ?  138 HIS   A HA   1 
ATOM   2919 H  HA   B HIS   A 1 138 ? 12.997 -12.351 -5.686  0.18 16.72 ?  138 HIS   A HA   1 
ATOM   2920 H  HB2  A HIS   A 1 138 ? 13.160 -11.314 -7.778  0.82 18.85 ?  138 HIS   A HB2  1 
ATOM   2921 H  HB2  B HIS   A 1 138 ? 12.985 -11.271 -7.675  0.18 17.00 ?  138 HIS   A HB2  1 
ATOM   2922 H  HB3  A HIS   A 1 138 ? 14.008 -10.125 -7.155  0.82 18.85 ?  138 HIS   A HB3  1 
ATOM   2923 H  HB3  B HIS   A 1 138 ? 13.768 -10.027 -7.077  0.18 17.00 ?  138 HIS   A HB3  1 
ATOM   2924 H  HD1  B HIS   A 1 138 ? 14.503 -13.505 -7.791  0.18 17.91 ?  138 HIS   A HD1  1 
ATOM   2925 H  HD2  A HIS   A 1 138 ? 16.603 -10.333 -7.777  0.82 20.49 ?  138 HIS   A HD2  1 
ATOM   2926 H  HD2  B HIS   A 1 138 ? 16.394 -10.104 -7.656  0.18 17.40 ?  138 HIS   A HD2  1 
ATOM   2927 H  HE1  A HIS   A 1 138 ? 16.756 -14.227 -8.472  0.82 22.27 ?  138 HIS   A HE1  1 
ATOM   2928 H  HE1  B HIS   A 1 138 ? 16.708 -13.956 -8.508  0.18 17.98 ?  138 HIS   A HE1  1 
ATOM   2929 H  HE2  A HIS   A 1 138 ? 17.983 -12.204 -8.466  0.82 21.44 ?  138 HIS   A HE2  1 
ATOM   2930 N  N    . SER   A 1 139 ? 14.824 -10.160 -4.243  1.00 13.89 ?  139 SER   A N    1 
ATOM   2931 C  CA   . SER   A 1 139 ? 15.911 -9.993  -3.290  1.00 13.50 ?  139 SER   A CA   1 
ATOM   2932 C  C    . SER   A 1 139 ? 15.693 -10.844 -2.044  1.00 12.88 ?  139 SER   A C    1 
ATOM   2933 O  O    . SER   A 1 139 ? 16.643 -11.439 -1.521  1.00 12.83 ?  139 SER   A O    1 
ATOM   2934 C  CB   . SER   A 1 139 ? 16.053 -8.518  -2.926  1.00 13.49 ?  139 SER   A CB   1 
ATOM   2935 O  OG   . SER   A 1 139 ? 17.140 -8.355  -2.035  1.00 13.38 ?  139 SER   A OG   1 
ATOM   2936 H  H    A SER   A 1 139 ? 14.381 -9.445  -4.427  0.82 16.71 ?  139 SER   A H    1 
ATOM   2937 H  H    B SER   A 1 139 ? 14.425 -9.428  -4.457  0.18 16.71 ?  139 SER   A H    1 
ATOM   2938 H  HA   . SER   A 1 139 ? 16.740 -10.274 -3.700  1.00 16.23 ?  139 SER   A HA   1 
ATOM   2939 H  HB2  . SER   A 1 139 ? 16.223 -7.997  -3.731  1.00 16.23 ?  139 SER   A HB2  1 
ATOM   2940 H  HB3  . SER   A 1 139 ? 15.241 -8.206  -2.494  1.00 16.23 ?  139 SER   A HB3  1 
ATOM   2941 H  HG   . SER   A 1 139 ? 17.234 -7.546  -1.827  1.00 16.10 ?  139 SER   A HG   1 
ATOM   2942 N  N    . LEU   A 1 140 ? 14.458 -10.900 -1.545  1.00 13.03 ?  140 LEU   A N    1 
ATOM   2943 C  CA   . LEU   A 1 140 ? 14.188 -11.721 -0.370  1.00 13.12 ?  140 LEU   A CA   1 
ATOM   2944 C  C    . LEU   A 1 140 ? 14.449 -13.196 -0.662  1.00 12.89 ?  140 LEU   A C    1 
ATOM   2945 O  O    . LEU   A 1 140 ? 14.999 -13.917 0.179   1.00 13.35 ?  140 LEU   A O    1 
ATOM   2946 C  CB   . LEU   A 1 140 ? 12.749 -11.499 0.101   1.00 13.48 ?  140 LEU   A CB   1 
ATOM   2947 C  CG   . LEU   A 1 140 ? 12.288 -12.371 1.268   1.00 14.08 ?  140 LEU   A CG   1 
ATOM   2948 C  CD1  . LEU   A 1 140 ? 13.198 -12.198 2.477   1.00 14.29 ?  140 LEU   A CD1  1 
ATOM   2949 C  CD2  . LEU   A 1 140 ? 10.831 -12.059 1.635   1.00 14.89 ?  140 LEU   A CD2  1 
ATOM   2950 H  H    . LEU   A 1 140 ? 13.775 -10.478 -1.857  1.00 15.68 ?  140 LEU   A H    1 
ATOM   2951 H  HA   . LEU   A 1 140 ? 14.779 -11.453 0.350   1.00 15.78 ?  140 LEU   A HA   1 
ATOM   2952 H  HB2  . LEU   A 1 140 ? 12.656 -10.577 0.379   1.00 16.22 ?  140 LEU   A HB2  1 
ATOM   2953 H  HB3  . LEU   A 1 140 ? 12.153 -11.676 -0.643  1.00 16.22 ?  140 LEU   A HB3  1 
ATOM   2954 H  HG   . LEU   A 1 140 ? 12.321 -13.304 0.999   1.00 16.93 ?  140 LEU   A HG   1 
ATOM   2955 H  HD11 . LEU   A 1 140 ? 12.819 -12.681 3.229   1.00 17.18 ?  140 LEU   A HD11 1 
ATOM   2956 H  HD12 . LEU   A 1 140 ? 14.074 -12.564 2.263   1.00 17.18 ?  140 LEU   A HD12 1 
ATOM   2957 H  HD13 . LEU   A 1 140 ? 13.271 -11.259 2.687   1.00 17.18 ?  140 LEU   A HD13 1 
ATOM   2958 H  HD21 . LEU   A 1 140 ? 10.551 -12.654 2.353   1.00 17.91 ?  140 LEU   A HD21 1 
ATOM   2959 H  HD22 . LEU   A 1 140 ? 10.769 -11.138 1.929   1.00 17.91 ?  140 LEU   A HD22 1 
ATOM   2960 H  HD23 . LEU   A 1 140 ? 10.270 -12.199 0.857   1.00 17.91 ?  140 LEU   A HD23 1 
ATOM   2961 N  N    . ARG   A 1 141 ? 14.054 -13.660 -1.849  1.00 13.39 ?  141 ARG   A N    1 
ATOM   2962 C  CA   . ARG   A 1 141 ? 14.289 -15.049 -2.229  1.00 14.59 ?  141 ARG   A CA   1 
ATOM   2963 C  C    . ARG   A 1 141 ? 15.783 -15.360 -2.246  1.00 13.53 ?  141 ARG   A C    1 
ATOM   2964 O  O    . ARG   A 1 141 ? 16.233 -16.375 -1.699  1.00 13.55 ?  141 ARG   A O    1 
ATOM   2965 C  CB   . ARG   A 1 141 ? 13.669 -15.284 -3.608  1.00 16.48 ?  141 ARG   A CB   1 
ATOM   2966 C  CG   . ARG   A 1 141 ? 13.658 -16.717 -4.080  1.00 19.79 ?  141 ARG   A CG   1 
ATOM   2967 C  CD   . ARG   A 1 141 ? 12.623 -17.496 -3.338  1.00 21.82 ?  141 ARG   A CD   1 
ATOM   2968 N  NE   . ARG   A 1 141 ? 13.230 -18.274 -2.273  1.00 21.72 ?  141 ARG   A NE   1 
ATOM   2969 C  CZ   . ARG   A 1 141 ? 12.543 -18.860 -1.302  1.00 22.41 ?  141 ARG   A CZ   1 
ATOM   2970 N  NH1  . ARG   A 1 141 ? 11.246 -18.649 -1.148  1.00 22.07 ?  141 ARG   A NH1  1 
ATOM   2971 N  NH2  . ARG   A 1 141 ? 13.176 -19.669 -0.457  1.00 23.10 ?  141 ARG   A NH2  1 
ATOM   2972 H  H    . ARG   A 1 141 ? 13.646 -13.192 -2.447  1.00 16.11 ?  141 ARG   A H    1 
ATOM   2973 H  HA   . ARG   A 1 141 ? 13.861 -15.638 -1.593  1.00 17.55 ?  141 ARG   A HA   1 
ATOM   2974 H  HB2  . ARG   A 1 141 ? 12.750 -14.969 -3.592  1.00 19.82 ?  141 ARG   A HB2  1 
ATOM   2975 H  HB3  . ARG   A 1 141 ? 14.170 -14.767 -4.259  1.00 19.82 ?  141 ARG   A HB3  1 
ATOM   2976 H  HG2  . ARG   A 1 141 ? 13.449 -16.745 -5.028  1.00 23.78 ?  141 ARG   A HG2  1 
ATOM   2977 H  HG3  . ARG   A 1 141 ? 14.528 -17.120 -3.917  1.00 23.78 ?  141 ARG   A HG3  1 
ATOM   2978 H  HD2  . ARG   A 1 141 ? 11.983 -16.887 -2.935  1.00 26.22 ?  141 ARG   A HD2  1 
ATOM   2979 H  HD3  . ARG   A 1 141 ? 12.171 -18.097 -3.952  1.00 26.22 ?  141 ARG   A HD3  1 
ATOM   2980 H  HE   . ARG   A 1 141 ? 14.063 -18.470 -2.345  1.00 26.11 ?  141 ARG   A HE   1 
ATOM   2981 H  HH11 . ARG   A 1 141 ? 10.820 -18.142 -1.697  1.00 26.52 ?  141 ARG   A HH11 1 
ATOM   2982 H  HH12 . ARG   A 1 141 ? 10.819 -19.039 -0.509  1.00 26.52 ?  141 ARG   A HH12 1 
ATOM   2983 H  HH21 . ARG   A 1 141 ? 14.020 -19.809 -0.546  1.00 27.75 ?  141 ARG   A HH21 1 
ATOM   2984 H  HH22 . ARG   A 1 141 ? 12.745 -20.044 0.187   1.00 27.75 ?  141 ARG   A HH22 1 
ATOM   2985 N  N    . VAL   A 1 142 ? 16.574 -14.490 -2.875  1.00 12.83 ?  142 VAL   A N    1 
ATOM   2986 C  CA   . VAL   A 1 142 ? 18.017 -14.704 -2.907  1.00 12.95 ?  142 VAL   A CA   1 
ATOM   2987 C  C    . VAL   A 1 142 ? 18.592 -14.688 -1.498  1.00 12.25 ?  142 VAL   A C    1 
ATOM   2988 O  O    . VAL   A 1 142 ? 19.462 -15.498 -1.159  1.00 12.68 ?  142 VAL   A O    1 
ATOM   2989 C  CB   . VAL   A 1 142 ? 18.709 -13.680 -3.823  1.00 13.36 ?  142 VAL   A CB   1 
ATOM   2990 C  CG1  . VAL   A 1 142 ? 20.217 -13.892 -3.787  1.00 13.23 ?  142 VAL   A CG1  1 
ATOM   2991 C  CG2  . VAL   A 1 142 ? 18.205 -13.803 -5.248  1.00 14.72 ?  142 VAL   A CG2  1 
ATOM   2992 H  H    . VAL   A 1 142 ? 16.308 -13.770 -3.281  1.00 15.44 ?  142 VAL   A H    1 
ATOM   2993 H  HA   . VAL   A 1 142 ? 18.188 -15.574 -3.282  1.00 15.58 ?  142 VAL   A HA   1 
ATOM   2994 H  HB   . VAL   A 1 142 ? 18.525 -12.774 -3.508  1.00 16.08 ?  142 VAL   A HB   1 
ATOM   2995 H  HG11 . VAL   A 1 142 ? 20.624 -13.405 -4.522  1.00 15.92 ?  142 VAL   A HG11 1 
ATOM   2996 H  HG12 . VAL   A 1 142 ? 20.568 -13.556 -2.943  1.00 15.92 ?  142 VAL   A HG12 1 
ATOM   2997 H  HG13 . VAL   A 1 142 ? 20.403 -14.836 -3.872  1.00 15.92 ?  142 VAL   A HG13 1 
ATOM   2998 H  HG21 . VAL   A 1 142 ? 18.680 -13.167 -5.807  1.00 17.71 ?  142 VAL   A HG21 1 
ATOM   2999 H  HG22 . VAL   A 1 142 ? 18.377 -14.706 -5.557  1.00 17.71 ?  142 VAL   A HG22 1 
ATOM   3000 H  HG23 . VAL   A 1 142 ? 17.258 -13.618 -5.261  1.00 17.71 ?  142 VAL   A HG23 1 
ATOM   3001 N  N    . CYS   A 1 143 ? 18.121 -13.768 -0.655  1.00 12.19 ?  143 CYS   A N    1 
ATOM   3002 C  CA   . CYS   A 1 143 ? 18.586 -13.721 0.725   1.00 12.22 ?  143 CYS   A CA   1 
ATOM   3003 C  C    . CYS   A 1 143 ? 18.365 -15.062 1.414   1.00 11.93 ?  143 CYS   A C    1 
ATOM   3004 O  O    . CYS   A 1 143 ? 19.291 -15.650 1.981   1.00 12.08 ?  143 CYS   A O    1 
ATOM   3005 C  CB   . CYS   A 1 143 ? 17.854 -12.610 1.472   1.00 12.78 ?  143 CYS   A CB   1 
ATOM   3006 S  SG   . CYS   A 1 143 ? 18.347 -12.442 3.192   1.00 13.07 ?  143 CYS   A SG   1 
ATOM   3007 H  H    . CYS   A 1 143 ? 17.537 -13.174 -0.857  1.00 14.66 ?  143 CYS   A H    1 
ATOM   3008 H  HA   . CYS   A 1 143 ? 19.536 -13.531 0.736   1.00 14.70 ?  143 CYS   A HA   1 
ATOM   3009 H  HB2  . CYS   A 1 143 ? 18.026 -11.767 1.025   1.00 15.37 ?  143 CYS   A HB2  1 
ATOM   3010 H  HB3  . CYS   A 1 143 ? 16.907 -12.799 1.455   1.00 15.37 ?  143 CYS   A HB3  1 
ATOM   3011 H  HG   . CYS   A 1 143 ? 17.759 -11.512 3.672   1.00 15.72 ?  143 CYS   A HG   1 
ATOM   3012 N  N    . VAL   A 1 144 ? 17.137 -15.572 1.357   1.00 12.82 ?  144 VAL   A N    1 
ATOM   3013 C  CA   . VAL   A 1 144 ? 16.805 -16.805 2.060   1.00 13.95 ?  144 VAL   A CA   1 
ATOM   3014 C  C    . VAL   A 1 144 ? 17.614 -17.976 1.521   1.00 13.64 ?  144 VAL   A C    1 
ATOM   3015 O  O    . VAL   A 1 144 ? 17.998 -18.880 2.274   1.00 14.05 ?  144 VAL   A O    1 
ATOM   3016 C  CB   . VAL   A 1 144 ? 15.287 -17.047 1.964   1.00 16.86 ?  144 VAL   A CB   1 
ATOM   3017 C  CG1  . VAL   A 1 144 ? 14.932 -18.476 2.315   1.00 18.59 ?  144 VAL   A CG1  1 
ATOM   3018 C  CG2  . VAL   A 1 144 ? 14.553 -16.042 2.853   1.00 16.65 ?  144 VAL   A CG2  1 
ATOM   3019 H  H    . VAL   A 1 144 ? 16.482 -15.217 0.919   1.00 15.42 ?  144 VAL   A H    1 
ATOM   3020 H  HA   . VAL   A 1 144 ? 17.023 -16.693 2.996   1.00 16.78 ?  144 VAL   A HA   1 
ATOM   3021 H  HB   . VAL   A 1 144 ? 14.999 -16.885 1.049   1.00 20.27 ?  144 VAL   A HB   1 
ATOM   3022 H  HG11 . VAL   A 1 144 ? 13.979 -18.525 2.504   1.00 22.35 ?  144 VAL   A HG11 1 
ATOM   3023 H  HG12 . VAL   A 1 144 ? 15.147 -19.050 1.566   1.00 22.35 ?  144 VAL   A HG12 1 
ATOM   3024 H  HG13 . VAL   A 1 144 ? 15.435 -18.740 3.099   1.00 22.35 ?  144 VAL   A HG13 1 
ATOM   3025 H  HG21 . VAL   A 1 144 ? 13.594 -16.194 2.793   1.00 20.02 ?  144 VAL   A HG21 1 
ATOM   3026 H  HG22 . VAL   A 1 144 ? 14.845 -16.150 3.771   1.00 20.02 ?  144 VAL   A HG22 1 
ATOM   3027 H  HG23 . VAL   A 1 144 ? 14.754 -15.136 2.551   1.00 20.02 ?  144 VAL   A HG23 1 
ATOM   3028 N  N    . ASP   A 1 145 ? 17.873 -17.991 0.215   1.00 13.80 ?  145 ASP   A N    1 
ATOM   3029 C  CA   . ASP   A 1 145 ? 18.583 -19.093 -0.424  1.00 14.32 ?  145 ASP   A CA   1 
ATOM   3030 C  C    . ASP   A 1 145 ? 20.103 -18.938 -0.396  1.00 14.04 ?  145 ASP   A C    1 
ATOM   3031 O  O    . ASP   A 1 145 ? 20.807 -19.826 -0.892  1.00 15.85 ?  145 ASP   A O    1 
ATOM   3032 C  CB   . ASP   A 1 145 ? 18.128 -19.239 -1.878  1.00 15.69 ?  145 ASP   A CB   1 
ATOM   3033 C  CG   . ASP   A 1 145 ? 16.674 -19.662 -2.001  1.00 17.73 ?  145 ASP   A CG   1 
ATOM   3034 O  OD1  . ASP   A 1 145 ? 16.113 -20.204 -1.026  1.00 18.07 ?  145 ASP   A OD1  1 
ATOM   3035 O  OD2  . ASP   A 1 145 ? 16.093 -19.453 -3.084  1.00 18.91 -1 145 ASP   A OD2  1 
ATOM   3036 H  H    . ASP   A 1 145 ? 17.631 -17.369 -0.332  1.00 16.59 ?  145 ASP   A H    1 
ATOM   3037 H  HA   . ASP   A 1 145 ? 18.357 -19.914 0.041   1.00 17.23 ?  145 ASP   A HA   1 
ATOM   3038 H  HB2  . ASP   A 1 145 ? 18.244 -18.392 -2.333  1.00 18.87 ?  145 ASP   A HB2  1 
ATOM   3039 H  HB3  . ASP   A 1 145 ? 18.665 -19.924 -2.306  1.00 18.87 ?  145 ASP   A HB3  1 
ATOM   3040 N  N    . THR   A 1 146 ? 20.629 -17.849 0.159   1.00 12.84 ?  146 THR   A N    1 
ATOM   3041 C  CA   . THR   A 1 146 ? 22.069 -17.607 0.174   1.00 12.07 ?  146 THR   A CA   1 
ATOM   3042 C  C    . THR   A 1 146 ? 22.633 -17.424 1.570   1.00 11.96 ?  146 THR   A C    1 
ATOM   3043 O  O    . THR   A 1 146 ? 23.706 -17.959 1.876   1.00 13.09 ?  146 THR   A O    1 
ATOM   3044 C  CB   . THR   A 1 146 ? 22.395 -16.358 -0.665  1.00 12.04 ?  146 THR   A CB   1 
ATOM   3045 O  OG1  . THR   A 1 146 ? 21.857 -16.513 -1.982  1.00 12.68 ?  146 THR   A OG1  1 
ATOM   3046 C  CG2  . THR   A 1 146 ? 23.894 -16.126 -0.757  1.00 12.60 ?  146 THR   A CG2  1 
ATOM   3047 H  H    . THR   A 1 146 ? 20.169 -17.223 0.534   1.00 15.44 ?  146 THR   A H    1 
ATOM   3048 H  HA   . THR   A 1 146 ? 22.521 -18.358 -0.232  1.00 14.52 ?  146 THR   A HA   1 
ATOM   3049 H  HB   . THR   A 1 146 ? 21.998 -15.576 -0.247  1.00 14.49 ?  146 THR   A HB   1 
ATOM   3050 H  HG1  . THR   A 1 146 ? 21.020 -16.580 -1.943  1.00 15.25 ?  146 THR   A HG1  1 
ATOM   3051 H  HG21 . THR   A 1 146 ? 24.086 -15.460 -1.435  1.00 15.16 ?  146 THR   A HG21 1 
ATOM   3052 H  HG22 . THR   A 1 146 ? 24.237 -15.813 0.096   1.00 15.16 ?  146 THR   A HG22 1 
ATOM   3053 H  HG23 . THR   A 1 146 ? 24.343 -16.953 -0.993  1.00 15.16 ?  146 THR   A HG23 1 
ATOM   3054 N  N    . VAL   A 1 147 ? 21.961 -16.642 2.409   1.00 11.79 ?  147 VAL   A N    1 
ATOM   3055 C  CA   . VAL   A 1 147 ? 22.450 -16.348 3.748   1.00 12.00 ?  147 VAL   A CA   1 
ATOM   3056 C  C    . VAL   A 1 147 ? 22.132 -17.519 4.665   1.00 12.10 ?  147 VAL   A C    1 
ATOM   3057 O  O    . VAL   A 1 147 ? 20.985 -17.983 4.732   1.00 12.71 ?  147 VAL   A O    1 
ATOM   3058 C  CB   . VAL   A 1 147 ? 21.829 -15.045 4.276   1.00 12.13 ?  147 VAL   A CB   1 
ATOM   3059 C  CG1  . VAL   A 1 147 ? 22.378 -14.736 5.649   1.00 13.50 ?  147 VAL   A CG1  1 
ATOM   3060 C  CG2  . VAL   A 1 147 ? 22.084 -13.896 3.310   1.00 12.36 ?  147 VAL   A CG2  1 
ATOM   3061 H  H    . VAL   A 1 147 ? 21.204 -16.271 2.228   1.00 14.19 ?  147 VAL   A H    1 
ATOM   3062 H  HA   . VAL   A 1 147 ? 23.412 -16.237 3.717   1.00 14.44 ?  147 VAL   A HA   1 
ATOM   3063 H  HB   . VAL   A 1 147 ? 20.872 -15.163 4.358   1.00 14.60 ?  147 VAL   A HB   1 
ATOM   3064 H  HG11 . VAL   A 1 147 ? 22.131 -13.833 5.892   1.00 16.24 ?  147 VAL   A HG11 1 
ATOM   3065 H  HG12 . VAL   A 1 147 ? 21.997 -15.364 6.291   1.00 16.24 ?  147 VAL   A HG12 1 
ATOM   3066 H  HG13 . VAL   A 1 147 ? 23.342 -14.827 5.635   1.00 16.24 ?  147 VAL   A HG13 1 
ATOM   3067 H  HG21 . VAL   A 1 147 ? 21.755 -13.074 3.709   1.00 14.87 ?  147 VAL   A HG21 1 
ATOM   3068 H  HG22 . VAL   A 1 147 ? 23.034 -13.829 3.144   1.00 14.87 ?  147 VAL   A HG22 1 
ATOM   3069 H  HG23 . VAL   A 1 147 ? 21.610 -14.073 2.482   1.00 14.87 ?  147 VAL   A HG23 1 
ATOM   3070 N  N    . ARG   A 1 148 ? 23.159 -18.001 5.366   1.00 12.69 ?  148 ARG   A N    1 
ATOM   3071 C  CA   . ARG   A 1 148 ? 23.027 -19.079 6.332   1.00 12.64 ?  148 ARG   A CA   1 
ATOM   3072 C  C    . ARG   A 1 148 ? 23.158 -18.603 7.768   1.00 12.95 ?  148 ARG   A C    1 
ATOM   3073 O  O    . ARG   A 1 148 ? 22.759 -19.327 8.688   1.00 14.54 ?  148 ARG   A O    1 
ATOM   3074 C  CB   . ARG   A 1 148 ? 24.065 -20.174 6.054   1.00 12.99 ?  148 ARG   A CB   1 
ATOM   3075 C  CG   . ARG   A 1 148 ? 23.894 -20.807 4.687   1.00 14.16 ?  148 ARG   A CG   1 
ATOM   3076 C  CD   . ARG   A 1 148 ? 24.976 -21.837 4.386   1.00 15.36 ?  148 ARG   A CD   1 
ATOM   3077 N  NE   . ARG   A 1 148 ? 26.314 -21.258 4.401   1.00 15.23 ?  148 ARG   A NE   1 
ATOM   3078 C  CZ   . ARG   A 1 148 ? 26.818 -20.522 3.420   1.00 14.41 ?  148 ARG   A CZ   1 
ATOM   3079 N  NH1  . ARG   A 1 148 ? 26.131 -20.281 2.316   1.00 14.73 ?  148 ARG   A NH1  1 
ATOM   3080 N  NH2  . ARG   A 1 148 ? 28.039 -20.001 3.555   1.00 14.85 ?  148 ARG   A NH2  1 
ATOM   3081 H  H    . ARG   A 1 148 ? 23.969 -17.706 5.288   1.00 15.26 ?  148 ARG   A H    1 
ATOM   3082 H  HA   . ARG   A 1 148 ? 22.151 -19.475 6.232   1.00 15.21 ?  148 ARG   A HA   1 
ATOM   3083 H  HB2  . ARG   A 1 148 ? 24.952 -19.798 6.102   1.00 15.62 ?  148 ARG   A HB2  1 
ATOM   3084 H  HB3  . ARG   A 1 148 ? 23.964 -20.880 6.718   1.00 15.62 ?  148 ARG   A HB3  1 
ATOM   3085 H  HG2  . ARG   A 1 148 ? 23.031 -21.247 4.649   1.00 17.03 ?  148 ARG   A HG2  1 
ATOM   3086 H  HG3  . ARG   A 1 148 ? 23.943 -20.109 4.014   1.00 17.03 ?  148 ARG   A HG3  1 
ATOM   3087 H  HD2  . ARG   A 1 148 ? 24.943 -22.535 5.059   1.00 18.47 ?  148 ARG   A HD2  1 
ATOM   3088 H  HD3  . ARG   A 1 148 ? 24.816 -22.215 3.507   1.00 18.47 ?  148 ARG   A HD3  1 
ATOM   3089 H  HE   . ARG   A 1 148 ? 26.808 -21.405 5.086   1.00 18.31 ?  148 ARG   A HE   1 
ATOM   3090 H  HH11 . ARG   A 1 148 ? 25.342 -20.601 2.217   1.00 17.72 ?  148 ARG   A HH11 1 
ATOM   3091 H  HH12 . ARG   A 1 148 ? 26.476 -19.791 1.694   1.00 17.72 ?  148 ARG   A HH12 1 
ATOM   3092 H  HH21 . ARG   A 1 148 ? 28.489 -20.147 4.269   1.00 17.85 ?  148 ARG   A HH21 1 
ATOM   3093 H  HH22 . ARG   A 1 148 ? 28.372 -19.516 2.926   1.00 17.85 ?  148 ARG   A HH22 1 
ATOM   3094 N  N    . THR   A 1 149 ? 23.706 -17.413 7.978   1.00 12.90 ?  149 THR   A N    1 
ATOM   3095 C  CA   . THR   A 1 149 ? 23.780 -16.821 9.299   1.00 12.99 ?  149 THR   A CA   1 
ATOM   3096 C  C    . THR   A 1 149 ? 22.453 -16.124 9.610   1.00 12.72 ?  149 THR   A C    1 
ATOM   3097 O  O    . THR   A 1 149 ? 21.510 -16.127 8.807   1.00 13.34 ?  149 THR   A O    1 
ATOM   3098 C  CB   . THR   A 1 149 ? 24.981 -15.884 9.365   1.00 13.68 ?  149 THR   A CB   1 
ATOM   3099 O  OG1  . THR   A 1 149 ? 24.855 -14.941 8.300   1.00 13.91 ?  149 THR   A OG1  1 
ATOM   3100 C  CG2  . THR   A 1 149 ? 26.293 -16.674 9.227   1.00 14.11 ?  149 THR   A CG2  1 
ATOM   3101 H  H    . THR   A 1 149 ? 24.048 -16.922 7.357   1.00 15.52 ?  149 THR   A H    1 
ATOM   3102 H  HA   . THR   A 1 149 ? 23.905 -17.527 9.950   1.00 15.62 ?  149 THR   A HA   1 
ATOM   3103 H  HB   . THR   A 1 149 ? 24.979 -15.423 10.214  1.00 16.45 ?  149 THR   A HB   1 
ATOM   3104 H  HG1  . THR   A 1 149 ? 25.505 -14.410 8.309   1.00 16.74 ?  149 THR   A HG1  1 
ATOM   3105 H  HG21 . THR   A 1 149 ? 27.051 -16.073 9.288   1.00 16.97 ?  149 THR   A HG21 1 
ATOM   3106 H  HG22 . THR   A 1 149 ? 26.361 -17.339 9.932   1.00 16.97 ?  149 THR   A HG22 1 
ATOM   3107 H  HG23 . THR   A 1 149 ? 26.323 -17.130 8.367   1.00 16.97 ?  149 THR   A HG23 1 
ATOM   3108 N  N    . ASN   A 1 150 ? 22.348 -15.564 10.807  1.00 12.72 ?  150 ASN   A N    1 
ATOM   3109 C  CA   . ASN   A 1 150 ? 21.070 -15.061 11.312  1.00 13.65 ?  150 ASN   A CA   1 
ATOM   3110 C  C    . ASN   A 1 150 ? 20.878 -13.621 10.862  1.00 12.91 ?  150 ASN   A C    1 
ATOM   3111 O  O    . ASN   A 1 150 ? 21.617 -12.723 11.287  1.00 14.55 ?  150 ASN   A O    1 
ATOM   3112 C  CB   . ASN   A 1 150 ? 21.034 -15.185 12.830  1.00 16.05 ?  150 ASN   A CB   1 
ATOM   3113 C  CG   . ASN   A 1 150 ? 20.877 -16.615 13.284  1.00 20.34 ?  150 ASN   A CG   1 
ATOM   3114 O  OD1  . ASN   A 1 150 ? 20.257 -17.425 12.596  1.00 21.79 ?  150 ASN   A OD1  1 
ATOM   3115 N  ND2  . ASN   A 1 150 ? 21.450 -16.942 14.437  1.00 22.78 ?  150 ASN   A ND2  1 
ATOM   3116 H  H    . ASN   A 1 150 ? 23.007 -15.459 11.348  1.00 15.30 ?  150 ASN   A H    1 
ATOM   3117 H  HA   . ASN   A 1 150 ? 20.348 -15.600 10.945  1.00 16.42 ?  150 ASN   A HA   1 
ATOM   3118 H  HB2  . ASN   A 1 150 ? 21.865 -14.844 13.198  1.00 19.30 ?  150 ASN   A HB2  1 
ATOM   3119 H  HB3  . ASN   A 1 150 ? 20.283 -14.680 13.174  1.00 19.30 ?  150 ASN   A HB3  1 
ATOM   3120 H  HD21 . ASN   A 1 150 ? 21.390 -17.749 14.740  1.00 27.38 ?  150 ASN   A HD21 1 
ATOM   3121 H  HD22 . ASN   A 1 150 ? 21.878 -16.350 14.892  1.00 27.38 ?  150 ASN   A HD22 1 
ATOM   3122 N  N    . VAL   A 1 151 ? 19.892 -13.394 10.002  1.00 12.58 ?  151 VAL   A N    1 
ATOM   3123 C  CA   . VAL   A 1 151 ? 19.673 -12.083 9.413   1.00 12.65 ?  151 VAL   A CA   1 
ATOM   3124 C  C    . VAL   A 1 151 ? 18.289 -11.568 9.787   1.00 12.65 ?  151 VAL   A C    1 
ATOM   3125 O  O    . VAL   A 1 151 ? 17.280 -12.279 9.653   1.00 13.97 ?  151 VAL   A O    1 
ATOM   3126 C  CB   . VAL   A 1 151 ? 19.952 -12.064 7.895   1.00 14.08 ?  151 VAL   A CB   1 
ATOM   3127 C  CG1  . VAL   A 1 151 ? 19.125 -13.086 7.150   1.00 14.88 ?  151 VAL   A CG1  1 
ATOM   3128 C  CG2  . VAL   A 1 151 ? 19.749 -10.657 7.325   1.00 14.38 ?  151 VAL   A CG2  1 
ATOM   3129 H  H    . VAL   A 1 151 ? 19.338 -13.992 9.736   1.00 15.13 ?  151 VAL   A H    1 
ATOM   3130 H  HA   . VAL   A 1 151 ? 20.315 -11.470 9.808   1.00 15.22 ?  151 VAL   A HA   1 
ATOM   3131 H  HB   . VAL   A 1 151 ? 20.886 -12.293 7.751   1.00 16.94 ?  151 VAL   A HB   1 
ATOM   3132 H  HG11 . VAL   A 1 151 ? 19.316 -13.025 6.199   1.00 17.89 ?  151 VAL   A HG11 1 
ATOM   3133 H  HG12 . VAL   A 1 151 ? 19.351 -13.975 7.471   1.00 17.89 ?  151 VAL   A HG12 1 
ATOM   3134 H  HG13 . VAL   A 1 151 ? 18.183 -12.911 7.306   1.00 17.89 ?  151 VAL   A HG13 1 
ATOM   3135 H  HG21 . VAL   A 1 151 ? 20.064 -10.638 6.405   1.00 17.29 ?  151 VAL   A HG21 1 
ATOM   3136 H  HG22 . VAL   A 1 151 ? 18.806 -10.435 7.353   1.00 17.29 ?  151 VAL   A HG22 1 
ATOM   3137 H  HG23 . VAL   A 1 151 ? 20.256 -10.023 7.857   1.00 17.29 ?  151 VAL   A HG23 1 
ATOM   3138 N  N    . TYR   A 1 152 ? 18.274 -10.324 10.270  1.00 12.51 ?  152 TYR   A N    1 
ATOM   3139 C  CA   . TYR   A 1 152 ? 17.082 -9.592  10.662  1.00 12.31 ?  152 TYR   A CA   1 
ATOM   3140 C  C    . TYR   A 1 152 ? 16.887 -8.484  9.637   1.00 12.06 ?  152 TYR   A C    1 
ATOM   3141 O  O    . TYR   A 1 152 ? 17.672 -7.529  9.584   1.00 12.61 ?  152 TYR   A O    1 
ATOM   3142 C  CB   . TYR   A 1 152 ? 17.261 -9.049  12.078  1.00 12.83 ?  152 TYR   A CB   1 
ATOM   3143 C  CG   . TYR   A 1 152 ? 17.230 -10.180 13.071  1.00 13.73 ?  152 TYR   A CG   1 
ATOM   3144 C  CD1  . TYR   A 1 152 ? 18.360 -10.940 13.333  1.00 15.29 ?  152 TYR   A CD1  1 
ATOM   3145 C  CD2  . TYR   A 1 152 ? 16.048 -10.538 13.700  1.00 13.84 ?  152 TYR   A CD2  1 
ATOM   3146 C  CE1  . TYR   A 1 152 ? 18.327 -12.008 14.209  1.00 16.23 ?  152 TYR   A CE1  1 
ATOM   3147 C  CE2  . TYR   A 1 152 ? 15.997 -11.617 14.583  1.00 15.34 ?  152 TYR   A CE2  1 
ATOM   3148 C  CZ   . TYR   A 1 152 ? 17.144 -12.346 14.831  1.00 16.17 ?  152 TYR   A CZ   1 
ATOM   3149 O  OH   . TYR   A 1 152 ? 17.115 -13.420 15.703  1.00 18.05 ?  152 TYR   A OH   1 
ATOM   3150 H  H    . TYR   A 1 152 ? 18.993 -9.854  10.367  1.00 15.06 ?  152 TYR   A H    1 
ATOM   3151 H  HA   . TYR   A 1 152 ? 16.312 -10.184 10.644  1.00 14.81 ?  152 TYR   A HA   1 
ATOM   3152 H  HB2  . TYR   A 1 152 ? 18.119 -8.608  12.150  1.00 15.43 ?  152 TYR   A HB2  1 
ATOM   3153 H  HB3  . TYR   A 1 152 ? 16.541 -8.435  12.285  1.00 15.43 ?  152 TYR   A HB3  1 
ATOM   3154 H  HD1  . TYR   A 1 152 ? 19.157 -10.723 12.909  1.00 18.39 ?  152 TYR   A HD1  1 
ATOM   3155 H  HD2  . TYR   A 1 152 ? 15.268 -10.053 13.530  1.00 16.65 ?  152 TYR   A HD2  1 
ATOM   3156 H  HE1  . TYR   A 1 152 ? 19.096 -12.498 14.379  1.00 19.51 ?  152 TYR   A HE1  1 
ATOM   3157 H  HE2  . TYR   A 1 152 ? 15.197 -11.834 15.008  1.00 18.44 ?  152 TYR   A HE2  1 
ATOM   3158 H  HH   . TYR   A 1 152 ? 16.338 -13.504 16.022  1.00 21.69 ?  152 TYR   A HH   1 
ATOM   3159 N  N    . LEU   A 1 153 ? 15.862 -8.635  8.803   1.00 12.25 ?  153 LEU   A N    1 
ATOM   3160 C  CA   . LEU   A 1 153 ? 15.602 -7.727  7.696   1.00 12.57 ?  153 LEU   A CA   1 
ATOM   3161 C  C    . LEU   A 1 153 ? 14.607 -6.653  8.104   1.00 12.97 ?  153 LEU   A C    1 
ATOM   3162 O  O    . LEU   A 1 153 ? 13.523 -6.959  8.616   1.00 14.49 ?  153 LEU   A O    1 
ATOM   3163 C  CB   . LEU   A 1 153 ? 15.034 -8.493  6.501   1.00 12.51 ?  153 LEU   A CB   1 
ATOM   3164 C  CG   . LEU   A 1 153 ? 15.963 -9.512  5.842   1.00 12.81 ?  153 LEU   A CG   1 
ATOM   3165 C  CD1  . LEU   A 1 153 ? 15.170 -10.405 4.905   1.00 13.18 ?  153 LEU   A CD1  1 
ATOM   3166 C  CD2  . LEU   A 1 153 ? 17.079 -8.810  5.087   1.00 13.32 ?  153 LEU   A CD2  1 
ATOM   3167 H  H    . LEU   A 1 153 ? 15.285 -9.280  8.864   1.00 14.74 ?  153 LEU   A H    1 
ATOM   3168 H  HA   . LEU   A 1 153 ? 16.430 -7.307  7.435   1.00 15.12 ?  153 LEU   A HA   1 
ATOM   3169 H  HB2  . LEU   A 1 153 ? 14.240 -8.965  6.794   1.00 15.05 ?  153 LEU   A HB2  1 
ATOM   3170 H  HB3  . LEU   A 1 153 ? 14.786 -7.840  5.823   1.00 15.05 ?  153 LEU   A HB3  1 
ATOM   3171 H  HG   . LEU   A 1 153 ? 16.367 -10.062 6.533   1.00 15.41 ?  153 LEU   A HG   1 
ATOM   3172 H  HD11 . LEU   A 1 153 ? 15.756 -11.096 4.565   1.00 15.85 ?  153 LEU   A HD11 1 
ATOM   3173 H  HD12 . LEU   A 1 153 ? 14.438 -10.800 5.399   1.00 15.85 ?  153 LEU   A HD12 1 
ATOM   3174 H  HD13 . LEU   A 1 153 ? 14.829 -9.865  4.176   1.00 15.85 ?  153 LEU   A HD13 1 
ATOM   3175 H  HD21 . LEU   A 1 153 ? 17.651 -9.485  4.688   1.00 16.02 ?  153 LEU   A HD21 1 
ATOM   3176 H  HD22 . LEU   A 1 153 ? 16.687 -8.256  4.398   1.00 16.02 ?  153 LEU   A HD22 1 
ATOM   3177 H  HD23 . LEU   A 1 153 ? 17.589 -8.268  5.706   1.00 16.02 ?  153 LEU   A HD23 1 
ATOM   3178 N  N    A ALA   A 1 154 ? 14.985 -5.400  7.876   0.82 13.00 ?  154 ALA   A N    1 
ATOM   3179 N  N    B ALA   A 1 154 ? 14.958 -5.397  7.842   0.18 12.97 ?  154 ALA   A N    1 
ATOM   3180 C  CA   A ALA   A 1 154 ? 14.135 -4.246  8.119   0.82 14.46 ?  154 ALA   A CA   1 
ATOM   3181 C  CA   B ALA   A 1 154 ? 14.090 -4.254  8.101   0.18 13.41 ?  154 ALA   A CA   1 
ATOM   3182 C  C    A ALA   A 1 154 ? 13.622 -3.739  6.779   0.82 14.59 ?  154 ALA   A C    1 
ATOM   3183 C  C    B ALA   A 1 154 ? 13.644 -3.667  6.768   0.18 13.70 ?  154 ALA   A C    1 
ATOM   3184 O  O    A ALA   A 1 154 ? 14.417 -3.397  5.895   0.82 15.24 ?  154 ALA   A O    1 
ATOM   3185 O  O    B ALA   A 1 154 ? 14.479 -3.219  5.974   0.18 13.64 ?  154 ALA   A O    1 
ATOM   3186 C  CB   A ALA   A 1 154 ? 14.917 -3.139  8.823   0.82 15.15 ?  154 ALA   A CB   1 
ATOM   3187 C  CB   B ALA   A 1 154 ? 14.821 -3.195  8.924   0.18 13.45 ?  154 ALA   A CB   1 
ATOM   3188 H  H    A ALA   A 1 154 ? 15.761 -5.189  7.564   0.82 15.64 ?  154 ALA   A H    1 
ATOM   3189 H  H    B ALA   A 1 154 ? 15.719 -5.179  7.503   0.18 15.60 ?  154 ALA   A H    1 
ATOM   3190 H  HA   A ALA   A 1 154 ? 13.381 -4.497  8.675   0.82 17.39 ?  154 ALA   A HA   1 
ATOM   3191 H  HA   B ALA   A 1 154 ? 13.306 -4.543  8.594   0.18 16.13 ?  154 ALA   A HA   1 
ATOM   3192 H  HB1  A ALA   A 1 154 ? 14.332 -2.381  8.972   0.82 18.21 ?  154 ALA   A HB1  1 
ATOM   3193 H  HB1  B ALA   A 1 154 ? 14.222 -2.448  9.080   0.18 16.18 ?  154 ALA   A HB1  1 
ATOM   3194 H  HB2  A ALA   A 1 154 ? 15.251 -3.473  9.670   0.82 18.21 ?  154 ALA   A HB2  1 
ATOM   3195 H  HB2  B ALA   A 1 154 ? 15.094 -3.582  9.770   0.18 16.18 ?  154 ALA   A HB2  1 
ATOM   3196 H  HB3  A ALA   A 1 154 ? 15.663 -2.871  8.258   0.82 18.21 ?  154 ALA   A HB3  1 
ATOM   3197 H  HB3  B ALA   A 1 154 ? 15.602 -2.895  8.431   0.18 16.18 ?  154 ALA   A HB3  1 
ATOM   3198 N  N    A VAL   A 1 155 ? 12.302 -3.687  6.637   0.82 14.96 ?  155 VAL   A N    1 
ATOM   3199 N  N    B VAL   A 1 155 ? 12.333 -3.661  6.531   0.18 14.25 ?  155 VAL   A N    1 
ATOM   3200 C  CA   A VAL   A 1 155 ? 11.638 -3.218  5.426   0.82 15.80 ?  155 VAL   A CA   1 
ATOM   3201 C  CA   B VAL   A 1 155 ? 11.745 -3.191  5.280   0.18 15.05 ?  155 VAL   A CA   1 
ATOM   3202 C  C    A VAL   A 1 155 ? 10.895 -1.939  5.787   0.82 17.30 ?  155 VAL   A C    1 
ATOM   3203 C  C    B VAL   A 1 155 ? 11.115 -1.824  5.522   0.18 16.07 ?  155 VAL   A C    1 
ATOM   3204 O  O    A VAL   A 1 155 ? 9.955  -1.968  6.589   0.82 17.34 ?  155 VAL   A O    1 
ATOM   3205 O  O    B VAL   A 1 155 ? 10.412 -1.626  6.521   0.18 15.99 ?  155 VAL   A O    1 
ATOM   3206 C  CB   A VAL   A 1 155 ? 10.698 -4.284  4.844   0.82 15.39 ?  155 VAL   A CB   1 
ATOM   3207 C  CB   B VAL   A 1 155 ? 10.710 -4.195  4.741   0.18 14.70 ?  155 VAL   A CB   1 
ATOM   3208 C  CG1  A VAL   A 1 155 ? 9.942  -3.728  3.654   0.82 16.63 ?  155 VAL   A CG1  1 
ATOM   3209 C  CG1  B VAL   A 1 155 ? 10.127 -3.708  3.422   0.18 14.86 ?  155 VAL   A CG1  1 
ATOM   3210 C  CG2  A VAL   A 1 155 ? 11.498 -5.520  4.435   0.82 16.15 ?  155 VAL   A CG2  1 
ATOM   3211 C  CG2  B VAL   A 1 155 ? 11.347 -5.568  4.570   0.18 14.74 ?  155 VAL   A CG2  1 
ATOM   3212 H  H    A VAL   A 1 155 ? 11.750 -3.934  7.254   0.82 18.00 ?  155 VAL   A H    1 
ATOM   3213 H  H    B VAL   A 1 155 ? 11.749 -3.938  7.099   0.18 17.13 ?  155 VAL   A H    1 
ATOM   3214 H  HA   A VAL   A 1 155 ? 12.305 -3.005  4.758   0.82 18.99 ?  155 VAL   A HA   1 
ATOM   3215 H  HA   B VAL   A 1 155 ? 12.444 -3.093  4.615   0.18 18.10 ?  155 VAL   A HA   1 
ATOM   3216 H  HB   A VAL   A 1 155 ? 10.054 -4.552  5.522   0.82 18.51 ?  155 VAL   A HB   1 
ATOM   3217 H  HB   B VAL   A 1 155 ? 9.985  -4.278  5.380   0.18 17.68 ?  155 VAL   A HB   1 
ATOM   3218 H  HG11 A VAL   A 1 155 ? 9.521  -4.460  3.177   0.82 20.00 ?  155 VAL   A HG11 1 
ATOM   3219 H  HG11 B VAL   A 1 155 ? 9.598  -4.420  3.029   0.18 17.87 ?  155 VAL   A HG11 1 
ATOM   3220 H  HG12 A VAL   A 1 155 ? 9.264  -3.108  3.968   0.82 20.00 ?  155 VAL   A HG12 1 
ATOM   3221 H  HG12 B VAL   A 1 155 ? 9.566  -2.935  3.589   0.18 17.87 ?  155 VAL   A HG12 1 
ATOM   3222 H  HG13 A VAL   A 1 155 ? 10.566 -3.269  3.071   0.82 20.00 ?  155 VAL   A HG13 1 
ATOM   3223 H  HG13 B VAL   A 1 155 ? 10.853 -3.469  2.826   0.18 17.87 ?  155 VAL   A HG13 1 
ATOM   3224 H  HG21 A VAL   A 1 155 ? 10.898 -6.173  4.046   0.82 19.42 ?  155 VAL   A HG21 1 
ATOM   3225 H  HG21 B VAL   A 1 155 ? 10.760 -6.122  4.033   0.18 17.72 ?  155 VAL   A HG21 1 
ATOM   3226 H  HG22 A VAL   A 1 155 ? 12.170 -5.257  3.783   0.82 19.42 ?  155 VAL   A HG22 1 
ATOM   3227 H  HG22 B VAL   A 1 155 ? 12.203 -5.466  4.125   0.18 17.72 ?  155 VAL   A HG22 1 
ATOM   3228 H  HG23 A VAL   A 1 155 ? 11.932 -5.893  5.220   0.82 19.42 ?  155 VAL   A HG23 1 
ATOM   3229 H  HG23 B VAL   A 1 155 ? 11.476 -5.969  5.444   0.18 17.72 ?  155 VAL   A HG23 1 
ATOM   3230 N  N    A PHE   A 1 156 ? 11.327 -0.812  5.208   0.82 18.75 ?  156 PHE   A N    1 
ATOM   3231 N  N    B PHE   A 1 156 ? 11.362 -0.891  4.607   0.18 17.25 ?  156 PHE   A N    1 
ATOM   3232 C  CA   A PHE   A 1 156 ? 10.780 0.493   5.578   0.82 20.47 ?  156 PHE   A CA   1 
ATOM   3233 C  CA   B PHE   A 1 156 ? 10.909 0.500   4.732   0.18 18.32 ?  156 PHE   A CA   1 
ATOM   3234 C  C    A PHE   A 1 156 ? 9.314  0.636   5.184   0.82 20.86 ?  156 PHE   A C    1 
ATOM   3235 C  C    B PHE   A 1 156 ? 9.663  0.760   3.893   0.18 19.42 ?  156 PHE   A C    1 
ATOM   3236 O  O    A PHE   A 1 156 ? 8.514  1.184   5.952   0.82 22.05 ?  156 PHE   A O    1 
ATOM   3237 O  O    B PHE   A 1 156 ? 9.611  1.692   3.091   0.18 19.88 ?  156 PHE   A O    1 
ATOM   3238 C  CB   A PHE   A 1 156 ? 11.606 1.595   4.914   0.82 21.59 ?  156 PHE   A CB   1 
ATOM   3239 C  CB   B PHE   A 1 156 ? 12.041 1.450   4.349   0.18 18.26 ?  156 PHE   A CB   1 
ATOM   3240 C  CG   A PHE   A 1 156 ? 11.127 2.983   5.225   0.82 22.84 ?  156 PHE   A CG   1 
ATOM   3241 C  CG   B PHE   A 1 156 ? 11.812 2.886   4.754   0.18 18.29 ?  156 PHE   A CG   1 
ATOM   3242 C  CD1  A PHE   A 1 156 ? 11.084 3.426   6.534   0.82 23.81 ?  156 PHE   A CD1  1 
ATOM   3243 C  CD1  B PHE   A 1 156 ? 11.982 3.285   6.070   0.18 18.39 ?  156 PHE   A CD1  1 
ATOM   3244 C  CD2  A PHE   A 1 156 ? 10.732 3.845   4.212   0.82 23.43 ?  156 PHE   A CD2  1 
ATOM   3245 C  CD2  B PHE   A 1 156 ? 11.460 3.843   3.813   0.18 18.47 ?  156 PHE   A CD2  1 
ATOM   3246 C  CE1  A PHE   A 1 156 ? 10.649 4.701   6.833   0.82 24.65 ?  156 PHE   A CE1  1 
ATOM   3247 C  CE1  B PHE   A 1 156 ? 11.784 4.604   6.444   0.18 18.41 ?  156 PHE   A CE1  1 
ATOM   3248 C  CE2  A PHE   A 1 156 ? 10.298 5.126   4.501   0.82 24.53 ?  156 PHE   A CE2  1 
ATOM   3249 C  CE2  B PHE   A 1 156 ? 11.261 5.163   4.182   0.18 18.50 ?  156 PHE   A CE2  1 
ATOM   3250 C  CZ   A PHE   A 1 156 ? 10.260 5.556   5.816   0.82 25.03 ?  156 PHE   A CZ   1 
ATOM   3251 C  CZ   B PHE   A 1 156 ? 11.423 5.543   5.498   0.18 18.32 ?  156 PHE   A CZ   1 
ATOM   3252 H  H    A PHE   A 1 156 ? 11.947 -0.778  4.614   0.82 22.54 ?  156 PHE   A H    1 
ATOM   3253 H  H    B PHE   A 1 156 ? 11.801 -1.044  3.884   0.18 20.74 ?  156 PHE   A H    1 
ATOM   3254 H  HA   A PHE   A 1 156 ? 10.848 0.606   6.538   0.82 24.60 ?  156 PHE   A HA   1 
ATOM   3255 H  HA   B PHE   A 1 156 ? 10.681 0.672   5.656   0.18 22.02 ?  156 PHE   A HA   1 
ATOM   3256 H  HB2  A PHE   A 1 156 ? 12.524 1.524   5.219   0.82 25.94 ?  156 PHE   A HB2  1 
ATOM   3257 H  HB2  B PHE   A 1 156 ? 12.847 1.150   4.789   0.18 21.95 ?  156 PHE   A HB2  1 
ATOM   3258 H  HB3  A PHE   A 1 156 ? 11.569 1.478   3.953   0.82 25.94 ?  156 PHE   A HB3  1 
ATOM   3259 H  HB3  B PHE   A 1 156 ? 12.161 1.428   3.387   0.18 21.95 ?  156 PHE   A HB3  1 
ATOM   3260 H  HD1  A PHE   A 1 156 ? 11.349 2.855   7.221   0.82 28.61 ?  156 PHE   A HD1  1 
ATOM   3261 H  HD1  B PHE   A 1 156 ? 12.222 2.656   6.713   0.18 22.11 ?  156 PHE   A HD1  1 
ATOM   3262 H  HD2  A PHE   A 1 156 ? 10.758 3.554   3.328   0.82 28.15 ?  156 PHE   A HD2  1 
ATOM   3263 H  HD2  B PHE   A 1 156 ? 11.349 3.595   2.925   0.18 22.21 ?  156 PHE   A HD2  1 
ATOM   3264 H  HE1  A PHE   A 1 156 ? 10.624 4.988   7.717   0.82 29.62 ?  156 PHE   A HE1  1 
ATOM   3265 H  HE1  B PHE   A 1 156 ? 11.895 4.857   7.333   0.18 22.13 ?  156 PHE   A HE1  1 
ATOM   3266 H  HE2  A PHE   A 1 156 ? 10.031 5.692   3.816   0.82 29.47 ?  156 PHE   A HE2  1 
ATOM   3267 H  HE2  B PHE   A 1 156 ? 11.021 5.794   3.542   0.18 22.23 ?  156 PHE   A HE2  1 
ATOM   3268 H  HZ   A PHE   A 1 156 ? 9.963  6.413   6.017   0.82 30.07 ?  156 PHE   A HZ   1 
ATOM   3269 H  HZ   B PHE   A 1 156 ? 11.292 6.430   5.747   0.18 22.02 ?  156 PHE   A HZ   1 
ATOM   3270 N  N    A ASP   A 1 157 ? 8.951  0.178   3.991   0.82 20.60 ?  157 ASP   A N    1 
ATOM   3271 N  N    B ASP   A 1 157 ? 8.640  -0.072  4.077   0.18 19.98 ?  157 ASP   A N    1 
ATOM   3272 C  CA   A ASP   A 1 157 ? 7.626  0.414   3.430   0.82 21.49 ?  157 ASP   A CA   1 
ATOM   3273 C  CA   B ASP   A 1 157 ? 7.382  0.073   3.355   0.18 20.35 ?  157 ASP   A CA   1 
ATOM   3274 C  C    A ASP   A 1 157 ? 6.647  -0.648  3.927   0.82 21.38 ?  157 ASP   A C    1 
ATOM   3275 C  C    B ASP   A 1 157 ? 6.358  -0.901  3.919   0.18 20.58 ?  157 ASP   A C    1 
ATOM   3276 O  O    A ASP   A 1 157 ? 6.825  -1.842  3.653   0.82 20.35 ?  157 ASP   A O    1 
ATOM   3277 O  O    B ASP   A 1 157 ? 6.568  -2.117  3.883   0.18 20.46 ?  157 ASP   A O    1 
ATOM   3278 C  CB   A ASP   A 1 157 ? 7.711  0.379   1.907   0.82 22.55 ?  157 ASP   A CB   1 
ATOM   3279 C  CB   B ASP   A 1 157 ? 7.586  -0.204  1.867   0.18 20.53 ?  157 ASP   A CB   1 
ATOM   3280 C  CG   A ASP   A 1 157 ? 6.443  0.871   1.247   0.82 24.28 ?  157 ASP   A CG   1 
ATOM   3281 C  CG   B ASP   A 1 157 ? 6.367  0.138   1.036   0.18 20.70 ?  157 ASP   A CG   1 
ATOM   3282 O  OD1  A ASP   A 1 157 ? 6.221  2.095   1.246   0.82 26.40 ?  157 ASP   A OD1  1 
ATOM   3283 O  OD1  B ASP   A 1 157 ? 5.304  0.420   1.625   0.18 20.63 ?  157 ASP   A OD1  1 
ATOM   3284 O  OD2  A ASP   A 1 157 ? 5.658  0.034   0.746   0.82 23.94 -1 157 ASP   A OD2  1 
ATOM   3285 O  OD2  B ASP   A 1 157 ? 6.476  0.127   -0.209  0.18 20.78 -1 157 ASP   A OD2  1 
ATOM   3286 H  H    A ASP   A 1 157 ? 9.470  -0.273  3.475   0.82 24.76 ?  157 ASP   A H    1 
ATOM   3287 H  H    B ASP   A 1 157 ? 8.651  -0.738  4.618   0.18 24.01 ?  157 ASP   A H    1 
ATOM   3288 H  HA   A ASP   A 1 157 ? 7.307  1.291   3.702   0.82 25.82 ?  157 ASP   A HA   1 
ATOM   3289 H  HA   B ASP   A 1 157 ? 7.045  0.976   3.457   0.18 24.46 ?  157 ASP   A HA   1 
ATOM   3290 H  HB2  A ASP   A 1 157 ? 8.458  0.934   1.619   0.82 27.10 ?  157 ASP   A HB2  1 
ATOM   3291 H  HB2  B ASP   A 1 157 ? 8.329  0.311   1.538   0.18 24.67 ?  157 ASP   A HB2  1 
ATOM   3292 H  HB3  A ASP   A 1 157 ? 7.860  -0.535  1.621   0.82 27.10 ?  157 ASP   A HB3  1 
ATOM   3293 H  HB3  B ASP   A 1 157 ? 7.766  -1.144  1.756   0.18 24.67 ?  157 ASP   A HB3  1 
ATOM   3294 N  N    A LYS   A 1 158 ? 5.609  -0.215  4.650   0.82 22.70 ?  158 LYS   A N    1 
ATOM   3295 N  N    B LYS   A 1 158 ? 5.246  -0.380  4.438   0.18 20.84 ?  158 LYS   A N    1 
ATOM   3296 C  CA   A LYS   A 1 158 ? 4.646  -1.163  5.208   0.82 23.62 ?  158 LYS   A CA   1 
ATOM   3297 C  CA   B LYS   A 1 158 ? 4.247  -1.255  5.041   0.18 21.20 ?  158 LYS   A CA   1 
ATOM   3298 C  C    A LYS   A 1 158 ? 3.920  -1.928  4.107   0.82 22.91 ?  158 LYS   A C    1 
ATOM   3299 C  C    B LYS   A 1 158 ? 3.592  -2.148  3.993   0.18 20.83 ?  158 LYS   A C    1 
ATOM   3300 O  O    A LYS   A 1 158 ? 3.735  -3.150  4.201   0.82 22.72 ?  158 LYS   A O    1 
ATOM   3301 O  O    B LYS   A 1 158 ? 3.398  -3.347  4.224   0.18 20.62 ?  158 LYS   A O    1 
ATOM   3302 C  CB   A LYS   A 1 158 ? 3.651  -0.425  6.108   0.82 24.93 ?  158 LYS   A CB   1 
ATOM   3303 C  CB   B LYS   A 1 158 ? 3.203  -0.424  5.789   0.18 21.98 ?  158 LYS   A CB   1 
ATOM   3304 C  CG   A LYS   A 1 158 ? 2.440  -1.253  6.540   0.82 26.74 ?  158 LYS   A CG   1 
ATOM   3305 C  CG   B LYS   A 1 158 ? 2.191  -1.253  6.568   0.18 22.78 ?  158 LYS   A CG   1 
ATOM   3306 C  CD   A LYS   A 1 158 ? 2.828  -2.509  7.320   0.82 28.01 ?  158 LYS   A CD   1 
ATOM   3307 C  CD   B LYS   A 1 158 ? 2.880  -2.214  7.528   0.18 23.45 ?  158 LYS   A CD   1 
ATOM   3308 C  CE   A LYS   A 1 158 ? 1.587  -3.199  7.876   0.82 29.03 ?  158 LYS   A CE   1 
ATOM   3309 C  CE   B LYS   A 1 158 ? 1.882  -2.906  8.440   0.18 23.95 ?  158 LYS   A CE   1 
ATOM   3310 N  NZ   A LYS   A 1 158 ? 1.870  -4.543  8.455   0.82 29.67 ?  158 LYS   A NZ   1 
ATOM   3311 N  NZ   B LYS   A 1 158 ? 1.721  -4.356  8.145   0.18 24.28 ?  158 LYS   A NZ   1 
ATOM   3312 H  H    A LYS   A 1 158 ? 5.455  0.610   4.835   0.82 27.28 ?  158 LYS   A H    1 
ATOM   3313 H  H    B LYS   A 1 158 ? 5.050  0.457   4.454   0.18 25.05 ?  158 LYS   A H    1 
ATOM   3314 H  HA   A LYS   A 1 158 ? 5.124  -1.804  5.761   0.82 28.39 ?  158 LYS   A HA   1 
ATOM   3315 H  HA   B LYS   A 1 158 ? 4.693  -1.827  5.682   0.18 25.48 ?  158 LYS   A HA   1 
ATOM   3316 H  HB2  A LYS   A 1 158 ? 4.113  -0.139  6.914   0.82 29.96 ?  158 LYS   A HB2  1 
ATOM   3317 H  HB2  B LYS   A 1 158 ? 3.658  0.156   6.422   0.18 26.41 ?  158 LYS   A HB2  1 
ATOM   3318 H  HB3  A LYS   A 1 158 ? 3.323  0.354   5.631   0.82 29.96 ?  158 LYS   A HB3  1 
ATOM   3319 H  HB3  B LYS   A 1 158 ? 2.713  0.115   5.149   0.18 26.41 ?  158 LYS   A HB3  1 
ATOM   3320 H  HG2  A LYS   A 1 158 ? 1.881  -0.707  7.113   0.82 32.13 ?  158 LYS   A HG2  1 
ATOM   3321 H  HG2  B LYS   A 1 158 ? 1.624  -0.659  7.087   0.18 27.38 ?  158 LYS   A HG2  1 
ATOM   3322 H  HG3  A LYS   A 1 158 ? 1.937  -1.523  5.755   0.82 32.13 ?  158 LYS   A HG3  1 
ATOM   3323 H  HG3  B LYS   A 1 158 ? 1.656  -1.771  5.948   0.18 27.38 ?  158 LYS   A HG3  1 
ATOM   3324 H  HD2  A LYS   A 1 158 ? 3.288  -3.126  6.730   0.82 33.65 ?  158 LYS   A HD2  1 
ATOM   3325 H  HD2  B LYS   A 1 158 ? 3.344  -2.898  7.019   0.18 28.18 ?  158 LYS   A HD2  1 
ATOM   3326 H  HD3  A LYS   A 1 158 ? 3.402  -2.260  8.062   0.82 33.65 ?  158 LYS   A HD3  1 
ATOM   3327 H  HD3  B LYS   A 1 158 ? 3.511  -1.720  8.078   0.18 28.18 ?  158 LYS   A HD3  1 
ATOM   3328 H  HE2  A LYS   A 1 158 ? 1.207  -2.644  8.575   0.82 34.87 ?  158 LYS   A HE2  1 
ATOM   3329 H  HE2  B LYS   A 1 158 ? 2.198  -2.830  9.351   0.18 28.77 ?  158 LYS   A HE2  1 
ATOM   3330 H  HE3  A LYS   A 1 158 ? 0.945  -3.309  7.159   0.82 34.87 ?  158 LYS   A HE3  1 
ATOM   3331 H  HE3  B LYS   A 1 158 ? 1.013  -2.478  8.348   0.18 28.77 ?  158 LYS   A HE3  1 
ATOM   3332 H  HZ1  A LYS   A 1 158 ? 1.118  -4.904  8.765   0.82 35.65 ?  158 LYS   A HZ1  1 
ATOM   3333 H  HZ1  B LYS   A 1 158 ? 1.131  -4.468  7.491   0.18 29.18 ?  158 LYS   A HZ1  1 
ATOM   3334 H  HZ2  A LYS   A 1 158 ? 2.210  -5.077  7.829   0.82 35.65 ?  158 LYS   A HZ2  1 
ATOM   3335 H  HZ2  B LYS   A 1 158 ? 2.502  -4.705  7.898   0.18 29.18 ?  158 LYS   A HZ2  1 
ATOM   3336 H  HZ3  A LYS   A 1 158 ? 2.454  -4.471  9.122   0.82 35.65 ?  158 LYS   A HZ3  1 
ATOM   3337 H  HZ3  B LYS   A 1 158 ? 1.430  -4.782  8.871   0.18 29.18 ?  158 LYS   A HZ3  1 
ATOM   3338 N  N    A ASN   A 1 159 ? 3.499  -1.228  3.054   0.82 23.61 ?  159 ASN   A N    1 
ATOM   3339 N  N    B ASN   A 1 159 ? 3.256  -1.586  2.830   0.18 20.92 ?  159 ASN   A N    1 
ATOM   3340 C  CA   A ASN   A 1 159 ? 2.841  -1.914  1.950   0.82 23.98 ?  159 ASN   A CA   1 
ATOM   3341 C  CA   B ASN   A 1 159 ? 2.612  -2.379  1.787   0.18 20.98 ?  159 ASN   A CA   1 
ATOM   3342 C  C    A ASN   A 1 159 ? 3.743  -2.991  1.356   0.82 22.69 ?  159 ASN   A C    1 
ATOM   3343 C  C    B ASN   A 1 159 ? 3.564  -3.426  1.215   0.18 19.76 ?  159 ASN   A C    1 
ATOM   3344 O  O    A ASN   A 1 159 ? 3.296  -4.115  1.098   0.82 22.23 ?  159 ASN   A O    1 
ATOM   3345 O  O    B ASN   A 1 159 ? 3.161  -4.567  0.964   0.18 19.55 ?  159 ASN   A O    1 
ATOM   3346 C  CB   A ASN   A 1 159 ? 2.395  -0.898  0.897   0.82 26.30 ?  159 ASN   A CB   1 
ATOM   3347 C  CB   B ASN   A 1 159 ? 2.067  -1.458  0.694   0.18 22.32 ?  159 ASN   A CB   1 
ATOM   3348 C  CG   A ASN   A 1 159 ? 1.186  -0.096  1.343   0.82 28.97 ?  159 ASN   A CG   1 
ATOM   3349 C  CG   B ASN   A 1 159 ? 0.929  -0.581  1.189   0.18 23.63 ?  159 ASN   A CG   1 
ATOM   3350 O  OD1  A ASN   A 1 159 ? 0.298  -0.627  2.003   0.82 30.14 ?  159 ASN   A OD1  1 
ATOM   3351 O  OD1  B ASN   A 1 159 ? -0.006 -1.062  1.829   0.18 24.14 ?  159 ASN   A OD1  1 
ATOM   3352 N  ND2  A ASN   A 1 159 ? 1.145  1.184   0.984   0.82 30.18 ?  159 ASN   A ND2  1 
ATOM   3353 N  ND2  B ASN   A 1 159 ? 1.010  0.717   0.904   0.18 24.07 ?  159 ASN   A ND2  1 
ATOM   3354 H  H    A ASN   A 1 159 ? 3.588  -0.377  2.960   0.82 28.36 ?  159 ASN   A H    1 
ATOM   3355 H  H    B ASN   A 1 159 ? 3.387  -0.760  2.628   0.18 25.14 ?  159 ASN   A H    1 
ATOM   3356 H  HA   A ASN   A 1 159 ? 2.049  -2.352  2.291   0.82 28.82 ?  159 ASN   A HA   1 
ATOM   3357 H  HA   B ASN   A 1 159 ? 1.858  -2.845  2.176   0.18 25.22 ?  159 ASN   A HA   1 
ATOM   3358 H  HB2  A ASN   A 1 159 ? 3.115  -0.273  0.727   0.82 31.60 ?  159 ASN   A HB2  1 
ATOM   3359 H  HB2  B ASN   A 1 159 ? 2.778  -0.878  0.379   0.18 26.83 ?  159 ASN   A HB2  1 
ATOM   3360 H  HB3  A ASN   A 1 159 ? 2.158  -1.367  0.083   0.82 31.60 ?  159 ASN   A HB3  1 
ATOM   3361 H  HB3  B ASN   A 1 159 ? 1.728  -1.997  -0.037  0.18 26.83 ?  159 ASN   A HB3  1 
ATOM   3362 H  HD21 A ASN   A 1 159 ? 0.478  1.677   1.215   0.82 36.25 ?  159 ASN   A HD21 1 
ATOM   3363 H  HD21 B ASN   A 1 159 ? 0.396  1.262   1.162   0.18 28.92 ?  159 ASN   A HD21 1 
ATOM   3364 H  HD22 A ASN   A 1 159 ? 1.790  1.520   0.528   0.82 36.25 ?  159 ASN   A HD22 1 
ATOM   3365 H  HD22 B ASN   A 1 159 ? 1.680  1.014   0.458   0.18 28.92 ?  159 ASN   A HD22 1 
ATOM   3366 N  N    A LEU   A 1 160 ? 5.026  -2.680  1.167   0.82 21.18 ?  160 LEU   A N    1 
ATOM   3367 N  N    B LEU   A 1 160 ? 4.833  -3.061  1.009   0.18 18.92 ?  160 LEU   A N    1 
ATOM   3368 C  CA   A LEU   A 1 160 ? 5.946  -3.673  0.620   0.82 20.21 ?  160 LEU   A CA   1 
ATOM   3369 C  CA   B LEU   A 1 160 ? 5.811  -4.045  0.550   0.18 18.38 ?  160 LEU   A CA   1 
ATOM   3370 C  C    A LEU   A 1 160 ? 6.148  -4.829  1.587   0.82 19.26 ?  160 LEU   A C    1 
ATOM   3371 C  C    B LEU   A 1 160 ? 6.078  -5.099  1.618   0.18 17.85 ?  160 LEU   A C    1 
ATOM   3372 O  O    A LEU   A 1 160 ? 6.185  -5.996  1.174   0.82 20.10 ?  160 LEU   A O    1 
ATOM   3373 O  O    B LEU   A 1 160 ? 6.191  -6.291  1.307   0.18 17.80 ?  160 LEU   A O    1 
ATOM   3374 C  CB   A LEU   A 1 160 ? 7.285  -3.025  0.277   0.82 19.91 ?  160 LEU   A CB   1 
ATOM   3375 C  CB   B LEU   A 1 160 ? 7.111  -3.354  0.137   0.18 18.35 ?  160 LEU   A CB   1 
ATOM   3376 C  CG   A LEU   A 1 160 ? 8.344  -4.039  -0.154  0.82 20.19 ?  160 LEU   A CG   1 
ATOM   3377 C  CG   B LEU   A 1 160 ? 7.116  -2.632  -1.213  0.18 18.51 ?  160 LEU   A CG   1 
ATOM   3378 C  CD1  A LEU   A 1 160 ? 7.892  -4.774  -1.395  0.82 20.94 ?  160 LEU   A CD1  1 
ATOM   3379 C  CD1  B LEU   A 1 160 ? 8.425  -1.895  -1.440  0.18 18.48 ?  160 LEU   A CD1  1 
ATOM   3380 C  CD2  A LEU   A 1 160 ? 9.670  -3.357  -0.397  0.82 20.20 ?  160 LEU   A CD2  1 
ATOM   3381 C  CD2  B LEU   A 1 160 ? 6.854  -3.619  -2.342  0.18 18.56 ?  160 LEU   A CD2  1 
ATOM   3382 H  H    A LEU   A 1 160 ? 5.385  -1.914  1.357   0.82 25.46 ?  160 LEU   A H    1 
ATOM   3383 H  H    B LEU   A 1 160 ? 5.143  -2.267  1.122   0.18 22.74 ?  160 LEU   A H    1 
ATOM   3384 H  HA   A LEU   A 1 160 ? 5.566  -4.023  -0.195  0.82 24.29 ?  160 LEU   A HA   1 
ATOM   3385 H  HA   B LEU   A 1 160 ? 5.457  -4.495  -0.228  0.18 22.09 ?  160 LEU   A HA   1 
ATOM   3386 H  HB2  A LEU   A 1 160 ? 7.159  -2.388  -0.449  0.82 23.93 ?  160 LEU   A HB2  1 
ATOM   3387 H  HB2  B LEU   A 1 160 ? 7.332  -2.707  0.815   0.18 22.06 ?  160 LEU   A HB2  1 
ATOM   3388 H  HB3  A LEU   A 1 160 ? 7.623  -2.566  1.062   0.82 23.93 ?  160 LEU   A HB3  1 
ATOM   3389 H  HB3  B LEU   A 1 160 ? 7.811  -4.018  0.103   0.18 22.06 ?  160 LEU   A HB3  1 
ATOM   3390 H  HG   A LEU   A 1 160 ? 8.478  -4.690  0.550   0.82 24.26 ?  160 LEU   A HG   1 
ATOM   3391 H  HG   B LEU   A 1 160 ? 6.409  -1.974  -1.214  0.18 22.25 ?  160 LEU   A HG   1 
ATOM   3392 H  HD11 A LEU   A 1 160 ? 8.627  -5.309  -1.725  0.82 25.17 ?  160 LEU   A HD11 1 
ATOM   3393 H  HD11 B LEU   A 1 160 ? 8.391  -1.449  -2.302  0.18 22.21 ?  160 LEU   A HD11 1 
ATOM   3394 H  HD12 A LEU   A 1 160 ? 7.141  -5.345  -1.170  0.82 25.17 ?  160 LEU   A HD12 1 
ATOM   3395 H  HD12 B LEU   A 1 160 ? 8.544  -1.240  -0.735  0.18 22.21 ?  160 LEU   A HD12 1 
ATOM   3396 H  HD13 A LEU   A 1 160 ? 7.626  -4.124  -2.066  0.82 25.17 ?  160 LEU   A HD13 1 
ATOM   3397 H  HD13 B LEU   A 1 160 ? 9.154  -2.533  -1.427  0.18 22.21 ?  160 LEU   A HD13 1 
ATOM   3398 H  HD21 A LEU   A 1 160 ? 10.322 -4.025  -0.664  0.82 24.28 ?  160 LEU   A HD21 1 
ATOM   3399 H  HD21 B LEU   A 1 160 ? 7.066  -3.196  -3.188  0.18 22.31 ?  160 LEU   A HD21 1 
ATOM   3400 H  HD22 A LEU   A 1 160 ? 9.563  -2.699  -1.101  0.82 24.28 ?  160 LEU   A HD22 1 
ATOM   3401 H  HD22 B LEU   A 1 160 ? 7.415  -4.401  -2.213  0.18 22.31 ?  160 LEU   A HD22 1 
ATOM   3402 H  HD23 A LEU   A 1 160 ? 9.956  -2.924  0.422   0.82 24.28 ?  160 LEU   A HD23 1 
ATOM   3403 H  HD23 B LEU   A 1 160 ? 5.919  -3.878  -2.326  0.18 22.31 ?  160 LEU   A HD23 1 
ATOM   3404 N  N    A TYR   A 1 161 ? 6.302  -4.526  2.875   0.82 18.32 ?  161 TYR   A N    1 
ATOM   3405 N  N    B TYR   A 1 161 ? 6.186  -4.682  2.882   0.18 17.61 ?  161 TYR   A N    1 
ATOM   3406 C  CA   A TYR   A 1 161 ? 6.445  -5.583  3.868   0.82 18.18 ?  161 TYR   A CA   1 
ATOM   3407 C  CA   B TYR   A 1 161 ? 6.382  -5.645  3.962   0.18 17.41 ?  161 TYR   A CA   1 
ATOM   3408 C  C    A TYR   A 1 161 ? 5.302  -6.591  3.771   0.82 18.55 ?  161 TYR   A C    1 
ATOM   3409 C  C    B TYR   A 1 161 ? 5.244  -6.657  4.001   0.18 17.76 ?  161 TYR   A C    1 
ATOM   3410 O  O    A TYR   A 1 161 ? 5.524  -7.806  3.766   0.82 18.42 ?  161 TYR   A O    1 
ATOM   3411 O  O    B TYR   A 1 161 ? 5.476  -7.868  4.095   0.18 17.72 ?  161 TYR   A O    1 
ATOM   3412 C  CB   A TYR   A 1 161 ? 6.524  -4.972  5.268   0.82 18.38 ?  161 TYR   A CB   1 
ATOM   3413 C  CB   B TYR   A 1 161 ? 6.502  -4.919  5.302   0.18 17.02 ?  161 TYR   A CB   1 
ATOM   3414 C  CG   A TYR   A 1 161 ? 6.433  -6.000  6.355   0.82 17.81 ?  161 TYR   A CG   1 
ATOM   3415 C  CG   B TYR   A 1 161 ? 6.358  -5.832  6.500   0.18 16.40 ?  161 TYR   A CG   1 
ATOM   3416 C  CD1  A TYR   A 1 161 ? 7.564  -6.671  6.792   0.82 17.41 ?  161 TYR   A CD1  1 
ATOM   3417 C  CD1  B TYR   A 1 161 ? 7.413  -6.633  6.919   0.18 16.29 ?  161 TYR   A CD1  1 
ATOM   3418 C  CD2  A TYR   A 1 161 ? 5.211  -6.316  6.936   0.82 17.84 ?  161 TYR   A CD2  1 
ATOM   3419 C  CD2  B TYR   A 1 161 ? 5.169  -5.890  7.216   0.18 16.05 ?  161 TYR   A CD2  1 
ATOM   3420 C  CE1  A TYR   A 1 161 ? 7.483  -7.631  7.775   0.82 17.45 ?  161 TYR   A CE1  1 
ATOM   3421 C  CE1  B TYR   A 1 161 ? 7.284  -7.470  8.012   0.18 16.25 ?  161 TYR   A CE1  1 
ATOM   3422 C  CE2  A TYR   A 1 161 ? 5.119  -7.268  7.922   0.82 17.56 ?  161 TYR   A CE2  1 
ATOM   3423 C  CE2  B TYR   A 1 161 ? 5.032  -6.724  8.311   0.18 16.06 ?  161 TYR   A CE2  1 
ATOM   3424 C  CZ   A TYR   A 1 161 ? 6.258  -7.926  8.337   0.82 17.76 ?  161 TYR   A CZ   1 
ATOM   3425 C  CZ   B TYR   A 1 161 ? 6.093  -7.511  8.705   0.18 16.33 ?  161 TYR   A CZ   1 
ATOM   3426 O  OH   A TYR   A 1 161 ? 6.178  -8.881  9.322   0.82 18.58 ?  161 TYR   A OH   1 
ATOM   3427 O  OH   B TYR   A 1 161 ? 5.960  -8.339  9.795   0.18 16.71 ?  161 TYR   A OH   1 
ATOM   3428 H  H    A TYR   A 1 161 ? 6.322  -3.727  3.195   0.82 22.02 ?  161 TYR   A H    1 
ATOM   3429 H  H    B TYR   A 1 161 ? 6.147  -3.861  3.132   0.18 21.17 ?  161 TYR   A H    1 
ATOM   3430 H  HA   A TYR   A 1 161 ? 7.271  -6.057  3.705   0.82 21.86 ?  161 TYR   A HA   1 
ATOM   3431 H  HA   B TYR   A 1 161 ? 7.209  -6.126  3.808   0.18 20.93 ?  161 TYR   A HA   1 
ATOM   3432 H  HB2  A TYR   A 1 161 ? 7.371  -4.512  5.362   0.82 22.10 ?  161 TYR   A HB2  1 
ATOM   3433 H  HB2  B TYR   A 1 161 ? 7.375  -4.498  5.354   0.18 20.46 ?  161 TYR   A HB2  1 
ATOM   3434 H  HB3  A TYR   A 1 161 ? 5.790  -4.349  5.384   0.82 22.10 ?  161 TYR   A HB3  1 
ATOM   3435 H  HB3  B TYR   A 1 161 ? 5.808  -4.244  5.358   0.18 20.46 ?  161 TYR   A HB3  1 
ATOM   3436 H  HD1  A TYR   A 1 161 ? 8.389  -6.479  6.412   0.82 20.92 ?  161 TYR   A HD1  1 
ATOM   3437 H  HD1  B TYR   A 1 161 ? 8.217  -6.609  6.454   0.18 19.59 ?  161 TYR   A HD1  1 
ATOM   3438 H  HD2  A TYR   A 1 161 ? 4.439  -5.882  6.655   0.82 21.44 ?  161 TYR   A HD2  1 
ATOM   3439 H  HD2  B TYR   A 1 161 ? 4.450  -5.362  6.954   0.18 19.30 ?  161 TYR   A HD2  1 
ATOM   3440 H  HE1  A TYR   A 1 161 ? 8.249  -8.078  8.065   0.82 20.98 ?  161 TYR   A HE1  1 
ATOM   3441 H  HE1  B TYR   A 1 161 ? 7.998  -8.002  8.280   0.18 19.54 ?  161 TYR   A HE1  1 
ATOM   3442 H  HE2  A TYR   A 1 161 ? 4.291  -7.476  8.305   0.82 21.11 ?  161 TYR   A HE2  1 
ATOM   3443 H  HE2  B TYR   A 1 161 ? 4.228  -6.754  8.781   0.18 19.31 ?  161 TYR   A HE2  1 
ATOM   3444 H  HH   A TYR   A 1 161 ? 6.927  -9.210  9.488   0.82 22.34 ?  161 TYR   A HH   1 
ATOM   3445 H  HH   B TYR   A 1 161 ? 6.672  -8.764  9.927   0.18 20.09 ?  161 TYR   A HH   1 
ATOM   3446 N  N    A ASP   A 1 162 ? 4.064  -6.103  3.683   0.82 19.32 ?  162 ASP   A N    1 
ATOM   3447 N  N    B ASP   A 1 162 ? 4.001  -6.176  3.932   0.18 18.34 ?  162 ASP   A N    1 
ATOM   3448 C  CA   A ASP   A 1 162 ? 2.921  -7.014  3.632   0.82 20.13 ?  162 ASP   A CA   1 
ATOM   3449 C  CA   B ASP   A 1 162 ? 2.862  -7.089  3.905   0.18 18.89 ?  162 ASP   A CA   1 
ATOM   3450 C  C    A ASP   A 1 162 ? 2.961  -7.880  2.377   0.82 20.37 ?  162 ASP   A C    1 
ATOM   3451 C  C    B ASP   A 1 162 ? 2.904  -7.977  2.668   0.18 19.37 ?  162 ASP   A C    1 
ATOM   3452 O  O    A ASP   A 1 162 ? 2.605  -9.064  2.418   0.82 20.99 ?  162 ASP   A O    1 
ATOM   3453 O  O    B ASP   A 1 162 ? 2.529  -9.154  2.724   0.18 19.47 ?  162 ASP   A O    1 
ATOM   3454 C  CB   A ASP   A 1 162 ? 1.602  -6.233  3.697   0.82 21.13 ?  162 ASP   A CB   1 
ATOM   3455 C  CB   B ASP   A 1 162 ? 1.554  -6.298  3.949   0.18 19.14 ?  162 ASP   A CB   1 
ATOM   3456 C  CG   A ASP   A 1 162 ? 1.308  -5.661  5.073   0.82 22.85 ?  162 ASP   A CG   1 
ATOM   3457 C  CG   B ASP   A 1 162 ? 1.319  -5.629  5.287   0.18 19.51 ?  162 ASP   A CG   1 
ATOM   3458 O  OD1  A ASP   A 1 162 ? 1.922  -6.100  6.062   0.82 23.74 ?  162 ASP   A OD1  1 
ATOM   3459 O  OD1  B ASP   A 1 162 ? 2.133  -5.833  6.212   0.18 19.81 ?  162 ASP   A OD1  1 
ATOM   3460 O  OD2  A ASP   A 1 162 ? 0.423  -4.777  5.163   0.82 24.15 -1 162 ASP   A OD2  1 
ATOM   3461 O  OD2  B ASP   A 1 162 ? 0.315  -4.896  5.415   0.18 19.70 -1 162 ASP   A OD2  1 
ATOM   3462 H  H    A ASP   A 1 162 ? 3.858  -5.273  3.648   0.82 23.23 ?  162 ASP   A H    1 
ATOM   3463 H  H    B ASP   A 1 162 ? 3.797  -5.341  3.897   0.18 22.04 ?  162 ASP   A H    1 
ATOM   3464 H  HA   A ASP   A 1 162 ? 2.951  -7.611  4.393   0.82 24.19 ?  162 ASP   A HA   1 
ATOM   3465 H  HA   B ASP   A 1 162 ? 2.897  -7.659  4.687   0.18 22.70 ?  162 ASP   A HA   1 
ATOM   3466 H  HB2  A ASP   A 1 162 ? 1.643  -5.488  3.086   0.82 25.39 ?  162 ASP   A HB2  1 
ATOM   3467 H  HB2  B ASP   A 1 162 ? 1.578  -5.605  3.272   0.18 23.00 ?  162 ASP   A HB2  1 
ATOM   3468 H  HB3  A ASP   A 1 162 ? 0.869  -6.824  3.465   0.82 25.39 ?  162 ASP   A HB3  1 
ATOM   3469 H  HB3  B ASP   A 1 162 ? 0.814  -6.902  3.781   0.18 23.00 ?  162 ASP   A HB3  1 
ATOM   3470 N  N    A LYS   A 1 163 ? 3.376  -7.304  1.247   0.82 21.22 ?  163 LYS   A N    1 
ATOM   3471 N  N    B LYS   A 1 163 ? 3.359  -7.428  1.540   0.18 19.93 ?  163 LYS   A N    1 
ATOM   3472 C  CA   A LYS   A 1 163 ? 3.471  -8.082  0.015   0.82 21.67 ?  163 LYS   A CA   1 
ATOM   3473 C  CA   B LYS   A 1 163 ? 3.419  -8.200  0.305   0.18 20.48 ?  163 LYS   A CA   1 
ATOM   3474 C  C    A LYS   A 1 163 ? 4.560  -9.143  0.116   0.82 21.13 ?  163 LYS   A C    1 
ATOM   3475 C  C    B LYS   A 1 163 ? 4.554  -9.219  0.344   0.18 19.78 ?  163 LYS   A C    1 
ATOM   3476 O  O    A LYS   A 1 163 ? 4.404  -10.253 -0.404  0.82 21.92 ?  163 LYS   A O    1 
ATOM   3477 O  O    B LYS   A 1 163 ? 4.376  -10.371 -0.069  0.18 19.96 ?  163 LYS   A O    1 
ATOM   3478 C  CB   A LYS   A 1 163 ? 3.738  -7.153  -1.167  0.82 23.99 ?  163 LYS   A CB   1 
ATOM   3479 C  CB   B LYS   A 1 163 ? 3.577  -7.246  -0.879  0.18 21.88 ?  163 LYS   A CB   1 
ATOM   3480 C  CG   A LYS   A 1 163 ? 3.810  -7.861  -2.506  0.82 26.75 ?  163 LYS   A CG   1 
ATOM   3481 C  CG   B LYS   A 1 163 ? 3.574  -7.910  -2.240  0.18 23.20 ?  163 LYS   A CG   1 
ATOM   3482 C  CD   A LYS   A 1 163 ? 4.168  -6.894  -3.617  0.82 29.49 ?  163 LYS   A CD   1 
ATOM   3483 C  CD   B LYS   A 1 163 ? 3.710  -6.866  -3.334  0.18 24.34 ?  163 LYS   A CD   1 
ATOM   3484 C  CE   A LYS   A 1 163 ? 4.052  -7.553  -4.979  0.82 31.41 ?  163 LYS   A CE   1 
ATOM   3485 C  CE   B LYS   A 1 163 ? 3.760  -7.494  -4.714  0.18 25.20 ?  163 LYS   A CE   1 
ATOM   3486 N  NZ   A LYS   A 1 163 ? 4.679  -6.730  -6.050  0.82 32.50 ?  163 LYS   A NZ   1 
ATOM   3487 N  NZ   B LYS   A 1 163 ? 4.084  -6.484  -5.760  0.18 25.62 ?  163 LYS   A NZ   1 
ATOM   3488 H  H    A LYS   A 1 163 ? 3.599  -6.476  1.167   0.82 25.51 ?  163 LYS   A H    1 
ATOM   3489 H  H    B LYS   A 1 163 ? 3.634  -6.617  1.465   0.18 23.96 ?  163 LYS   A H    1 
ATOM   3490 H  HA   A LYS   A 1 163 ? 2.624  -8.530  -0.144  0.82 26.05 ?  163 LYS   A HA   1 
ATOM   3491 H  HA   B LYS   A 1 163 ? 2.586  -8.682  0.191   0.18 24.61 ?  163 LYS   A HA   1 
ATOM   3492 H  HB2  A LYS   A 1 163 ? 3.023  -6.497  -1.220  0.82 28.82 ?  163 LYS   A HB2  1 
ATOM   3493 H  HB2  B LYS   A 1 163 ? 2.843  -6.610  -0.864  0.18 26.29 ?  163 LYS   A HB2  1 
ATOM   3494 H  HB3  A LYS   A 1 163 ? 4.585  -6.703  -1.027  0.82 28.82 ?  163 LYS   A HB3  1 
ATOM   3495 H  HB3  B LYS   A 1 163 ? 4.418  -6.772  -0.787  0.18 26.29 ?  163 LYS   A HB3  1 
ATOM   3496 H  HG2  A LYS   A 1 163 ? 4.492  -8.549  -2.474  0.82 32.14 ?  163 LYS   A HG2  1 
ATOM   3497 H  HG2  B LYS   A 1 163 ? 4.324  -8.522  -2.305  0.18 27.88 ?  163 LYS   A HG2  1 
ATOM   3498 H  HG3  A LYS   A 1 163 ? 2.945  -8.254  -2.708  0.82 32.14 ?  163 LYS   A HG3  1 
ATOM   3499 H  HG3  B LYS   A 1 163 ? 2.737  -8.384  -2.368  0.18 27.88 ?  163 LYS   A HG3  1 
ATOM   3500 H  HD2  A LYS   A 1 163 ? 3.559  -6.138  -3.592  0.82 35.42 ?  163 LYS   A HD2  1 
ATOM   3501 H  HD2  B LYS   A 1 163 ? 2.946  -6.269  -3.301  0.18 29.25 ?  163 LYS   A HD2  1 
ATOM   3502 H  HD3  A LYS   A 1 163 ? 5.082  -6.593  -3.498  0.82 35.42 ?  163 LYS   A HD3  1 
ATOM   3503 H  HD3  B LYS   A 1 163 ? 4.530  -6.366  -3.197  0.18 29.25 ?  163 LYS   A HD3  1 
ATOM   3504 H  HE2  A LYS   A 1 163 ? 4.486  -8.418  -4.956  0.82 37.73 ?  163 LYS   A HE2  1 
ATOM   3505 H  HE2  B LYS   A 1 163 ? 4.440  -8.184  -4.729  0.18 30.28 ?  163 LYS   A HE2  1 
ATOM   3506 H  HE3  A LYS   A 1 163 ? 3.115  -7.661  -5.197  0.82 37.73 ?  163 LYS   A HE3  1 
ATOM   3507 H  HE3  B LYS   A 1 163 ? 2.895  -7.876  -4.922  0.18 30.28 ?  163 LYS   A HE3  1 
ATOM   3508 H  HZ1  A LYS   A 1 163 ? 4.597  -7.140  -6.835  0.82 39.04 ?  163 LYS   A HZ1  1 
ATOM   3509 H  HZ1  B LYS   A 1 163 ? 4.111  -6.871  -6.561  0.18 30.79 ?  163 LYS   A HZ1  1 
ATOM   3510 H  HZ2  A LYS   A 1 163 ? 4.277  -5.936  -6.095  0.82 39.04 ?  163 LYS   A HZ2  1 
ATOM   3511 H  HZ2  B LYS   A 1 163 ? 3.465  -5.845  -5.768  0.18 30.79 ?  163 LYS   A HZ2  1 
ATOM   3512 H  HZ3  A LYS   A 1 163 ? 5.542  -6.607  -5.875  0.82 39.04 ?  163 LYS   A HZ3  1 
ATOM   3513 H  HZ3  B LYS   A 1 163 ? 4.877  -6.114  -5.592  0.18 30.79 ?  163 LYS   A HZ3  1 
ATOM   3514 N  N    A LEU   A 1 164 ? 5.674  -8.812  0.775   0.82 19.41 ?  164 LEU   A N    1 
ATOM   3515 N  N    B LEU   A 1 164 ? 5.726  -8.813  0.840   0.18 18.76 ?  164 LEU   A N    1 
ATOM   3516 C  CA   A LEU   A 1 164 ? 6.770  -9.766  0.928   0.82 18.38 ?  164 LEU   A CA   1 
ATOM   3517 C  CA   B LEU   A 1 164 ? 6.838  -9.749  0.983   0.18 17.90 ?  164 LEU   A CA   1 
ATOM   3518 C  C    A LEU   A 1 164 ? 6.354  -10.950 1.790   0.82 18.45 ?  164 LEU   A C    1 
ATOM   3519 C  C    B LEU   A 1 164 ? 6.442  -10.936 1.848   0.18 17.83 ?  164 LEU   A C    1 
ATOM   3520 O  O    A LEU   A 1 164 ? 6.663  -12.102 1.464   0.82 19.23 ?  164 LEU   A O    1 
ATOM   3521 O  O    B LEU   A 1 164 ? 6.832  -12.077 1.573   0.18 17.84 ?  164 LEU   A O    1 
ATOM   3522 C  CB   A LEU   A 1 164 ? 7.972  -9.066  1.554   0.82 17.67 ?  164 LEU   A CB   1 
ATOM   3523 C  CB   B LEU   A 1 164 ? 8.038  -9.030  1.596   0.18 17.30 ?  164 LEU   A CB   1 
ATOM   3524 C  CG   A LEU   A 1 164 ? 8.710  -8.060  0.667   0.82 17.98 ?  164 LEU   A CG   1 
ATOM   3525 C  CG   B LEU   A 1 164 ? 8.834  -8.107  0.674   0.18 16.84 ?  164 LEU   A CG   1 
ATOM   3526 C  CD1  A LEU   A 1 164 ? 9.666  -7.203  1.489   0.82 17.55 ?  164 LEU   A CD1  1 
ATOM   3527 C  CD1  B LEU   A 1 164 ? 9.476  -6.979  1.466   0.18 16.57 ?  164 LEU   A CD1  1 
ATOM   3528 C  CD2  A LEU   A 1 164 ? 9.464  -8.763  -0.454  0.82 18.36 ?  164 LEU   A CD2  1 
ATOM   3529 C  CD2  B LEU   A 1 164 ? 9.891  -8.903  -0.067  0.18 16.64 ?  164 LEU   A CD2  1 
ATOM   3530 H  H    A LEU   A 1 164 ? 5.816  -8.046  1.140   0.82 23.34 ?  164 LEU   A H    1 
ATOM   3531 H  H    B LEU   A 1 164 ? 5.897  -8.015  1.104   0.18 22.55 ?  164 LEU   A H    1 
ATOM   3532 H  HA   A LEU   A 1 164 ? 7.026  -10.102 0.058   0.82 22.10 ?  164 LEU   A HA   1 
ATOM   3533 H  HA   B LEU   A 1 164 ? 7.093  -10.085 0.112   0.18 21.52 ?  164 LEU   A HA   1 
ATOM   3534 H  HB2  A LEU   A 1 164 ? 7.671  -8.583  2.338   0.82 21.24 ?  164 LEU   A HB2  1 
ATOM   3535 H  HB2  B LEU   A 1 164 ? 7.722  -8.490  2.336   0.18 20.80 ?  164 LEU   A HB2  1 
ATOM   3536 H  HB3  A LEU   A 1 164 ? 8.616  -9.739  1.816   0.82 21.24 ?  164 LEU   A HB3  1 
ATOM   3537 H  HB3  B LEU   A 1 164 ? 8.655  -9.700  1.929   0.18 20.80 ?  164 LEU   A HB3  1 
ATOM   3538 H  HG   A LEU   A 1 164 ? 8.065  -7.462  0.260   0.82 21.62 ?  164 LEU   A HG   1 
ATOM   3539 H  HG   B LEU   A 1 164 ? 8.236  -7.716  0.018   0.18 20.25 ?  164 LEU   A HG   1 
ATOM   3540 H  HD11 A LEU   A 1 164 ? 10.122 -6.579  0.901   0.82 21.10 ?  164 LEU   A HD11 1 
ATOM   3541 H  HD11 B LEU   A 1 164 ? 9.989  -6.420  0.861   0.18 19.92 ?  164 LEU   A HD11 1 
ATOM   3542 H  HD12 A LEU   A 1 164 ? 9.161  -6.716  2.158   0.82 21.10 ?  164 LEU   A HD12 1 
ATOM   3543 H  HD12 B LEU   A 1 164 ? 8.778  -6.454  1.889   0.18 19.92 ?  164 LEU   A HD12 1 
ATOM   3544 H  HD13 A LEU   A 1 164 ? 10.317 -7.780  1.922   0.82 21.10 ?  164 LEU   A HD13 1 
ATOM   3545 H  HD13 B LEU   A 1 164 ? 10.060 -7.359  2.141   0.18 19.92 ?  164 LEU   A HD13 1 
ATOM   3546 H  HD21 A LEU   A 1 164 ? 9.969  -8.103  -0.959  0.82 22.07 ?  164 LEU   A HD21 1 
ATOM   3547 H  HD21 B LEU   A 1 164 ? 10.349 -8.316  -0.687  0.18 20.01 ?  164 LEU   A HD21 1 
ATOM   3548 H  HD22 A LEU   A 1 164 ? 10.066 -9.416  -0.069  0.82 22.07 ?  164 LEU   A HD22 1 
ATOM   3549 H  HD22 B LEU   A 1 164 ? 10.522 -9.263  0.576   0.18 20.01 ?  164 LEU   A HD22 1 
ATOM   3550 H  HD23 A LEU   A 1 164 ? 8.823  -9.202  -1.035  0.82 22.07 ?  164 LEU   A HD23 1 
ATOM   3551 H  HD23 B LEU   A 1 164 ? 9.460  -9.626  -0.549  0.18 20.01 ?  164 LEU   A HD23 1 
ATOM   3552 N  N    . VAL   A 1 165 ? 5.671  -10.682 2.904   1.00 18.04 ?  165 VAL   A N    1 
ATOM   3553 C  CA   . VAL   A 1 165 ? 5.204  -11.759 3.769   1.00 17.90 ?  165 VAL   A CA   1 
ATOM   3554 C  C    . VAL   A 1 165 ? 4.164  -12.606 3.048   1.00 17.98 ?  165 VAL   A C    1 
ATOM   3555 O  O    . VAL   A 1 165 ? 4.257  -13.839 3.008   1.00 17.79 ?  165 VAL   A O    1 
ATOM   3556 C  CB   . VAL   A 1 165 ? 4.647  -11.162 5.075   1.00 18.68 ?  165 VAL   A CB   1 
ATOM   3557 C  CG1  . VAL   A 1 165 ? 3.877  -12.210 5.868   1.00 19.13 ?  165 VAL   A CG1  1 
ATOM   3558 C  CG2  . VAL   A 1 165 ? 5.772  -10.548 5.906   1.00 19.34 ?  165 VAL   A CG2  1 
ATOM   3559 H  H    A VAL   A 1 165 ? 5.473  -9.894  3.183   0.82 21.69 ?  165 VAL   A H    1 
ATOM   3560 H  H    B VAL   A 1 165 ? 5.407  -9.900  3.142   0.18 21.69 ?  165 VAL   A H    1 
ATOM   3561 H  HA   . VAL   A 1 165 ? 5.952  -12.333 4.002   1.00 21.52 ?  165 VAL   A HA   1 
ATOM   3562 H  HB   . VAL   A 1 165 ? 4.031  -10.449 4.852   1.00 22.46 ?  165 VAL   A HB   1 
ATOM   3563 H  HG11 . VAL   A 1 165 ? 3.780  -11.900 6.783   1.00 22.99 ?  165 VAL   A HG11 1 
ATOM   3564 H  HG12 . VAL   A 1 165 ? 2.998  -12.321 5.468   1.00 22.99 ?  165 VAL   A HG12 1 
ATOM   3565 H  HG13 . VAL   A 1 165 ? 4.363  -13.042 5.848   1.00 22.99 ?  165 VAL   A HG13 1 
ATOM   3566 H  HG21 . VAL   A 1 165 ? 5.396  -10.150 6.707   1.00 23.25 ?  165 VAL   A HG21 1 
ATOM   3567 H  HG22 . VAL   A 1 165 ? 6.404  -11.243 6.149   1.00 23.25 ?  165 VAL   A HG22 1 
ATOM   3568 H  HG23 . VAL   A 1 165 ? 6.219  -9.865  5.379   1.00 23.25 ?  165 VAL   A HG23 1 
ATOM   3569 N  N    . SER   A 1 166 ? 3.158  -11.951 2.462   1.00 18.76 ?  166 SER   A N    1 
ATOM   3570 C  CA   . SER   A 1 166 ? 2.029  -12.682 1.900   1.00 20.01 ?  166 SER   A CA   1 
ATOM   3571 C  C    . SER   A 1 166 ? 2.430  -13.534 0.706   1.00 20.93 ?  166 SER   A C    1 
ATOM   3572 O  O    . SER   A 1 166 ? 1.768  -14.539 0.420   1.00 23.05 ?  166 SER   A O    1 
ATOM   3573 C  CB   . SER   A 1 166 ? 0.920  -11.712 1.487   1.00 21.75 ?  166 SER   A CB   1 
ATOM   3574 O  OG   . SER   A 1 166 ? 0.323  -11.098 2.614   1.00 24.32 ?  166 SER   A OG   1 
ATOM   3575 H  H    . SER   A 1 166 ? 3.102  -11.100 2.389   1.00 22.55 ?  166 SER   A H    1 
ATOM   3576 H  HA   . SER   A 1 166 ? 1.661  -13.278 2.573   1.00 24.06 ?  166 SER   A HA   1 
ATOM   3577 H  HB2  . SER   A 1 166 ? 1.293  -11.025 0.916   1.00 26.14 ?  166 SER   A HB2  1 
ATOM   3578 H  HB3  . SER   A 1 166 ? 0.230  -12.201 1.005   1.00 26.14 ?  166 SER   A HB3  1 
ATOM   3579 H  HG   . SER   A 1 166 ? 0.906  -10.663 3.042   1.00 29.22 ?  166 SER   A HG   1 
ATOM   3580 N  N    . SER   A 1 167 ? 3.485  -13.151 -0.009  1.00 20.46 ?  167 SER   A N    1 
ATOM   3581 C  CA   . SER   A 1 167 ? 3.910  -13.876 -1.196  1.00 21.25 ?  167 SER   A CA   1 
ATOM   3582 C  C    . SER   A 1 167 ? 5.068  -14.824 -0.926  1.00 21.12 ?  167 SER   A C    1 
ATOM   3583 O  O    . SER   A 1 167 ? 5.577  -15.439 -1.866  1.00 22.01 ?  167 SER   A O    1 
ATOM   3584 C  CB   . SER   A 1 167 ? 4.288  -12.894 -2.315  1.00 22.22 ?  167 SER   A CB   1 
ATOM   3585 O  OG   . SER   A 1 167 ? 5.384  -12.077 -1.932  1.00 22.56 ?  167 SER   A OG   1 
ATOM   3586 H  H    . SER   A 1 167 ? 3.977  -12.468 0.180   1.00 24.59 ?  167 SER   A H    1 
ATOM   3587 H  HA   . SER   A 1 167 ? 3.165  -14.400 -1.519  1.00 25.53 ?  167 SER   A HA   1 
ATOM   3588 H  HB2  . SER   A 1 167 ? 4.531  -13.400 -3.107  1.00 26.71 ?  167 SER   A HB2  1 
ATOM   3589 H  HB3  . SER   A 1 167 ? 3.513  -12.335 -2.516  1.00 26.71 ?  167 SER   A HB3  1 
ATOM   3590 H  HG   . SER   A 1 167 ? 5.168  -11.615 -1.261  1.00 27.10 ?  167 SER   A HG   1 
ATOM   3591 N  N    . PHE   A 1 168 ? 5.493  -14.962 0.327   1.00 20.51 ?  168 PHE   A N    1 
ATOM   3592 C  CA   . PHE   A 1 168 ? 6.685  -15.741 0.629   1.00 20.61 ?  168 PHE   A CA   1 
ATOM   3593 C  C    . PHE   A 1 168 ? 6.388  -17.230 0.547   1.00 22.91 ?  168 PHE   A C    1 
ATOM   3594 O  O    . PHE   A 1 168 ? 5.443  -17.725 1.172   1.00 24.09 ?  168 PHE   A O    1 
ATOM   3595 C  CB   . PHE   A 1 168 ? 7.221  -15.417 2.020   1.00 19.36 ?  168 PHE   A CB   1 
ATOM   3596 C  CG   . PHE   A 1 168 ? 8.492  -16.149 2.342   1.00 18.23 ?  168 PHE   A CG   1 
ATOM   3597 C  CD1  . PHE   A 1 168 ? 9.669  -15.782 1.727   1.00 18.53 ?  168 PHE   A CD1  1 
ATOM   3598 C  CD2  . PHE   A 1 168 ? 8.510  -17.224 3.217   1.00 17.58 ?  168 PHE   A CD2  1 
ATOM   3599 C  CE1  . PHE   A 1 168 ? 10.843 -16.445 1.991   1.00 17.95 ?  168 PHE   A CE1  1 
ATOM   3600 C  CE2  . PHE   A 1 168 ? 9.697  -17.890 3.487   1.00 17.65 ?  168 PHE   A CE2  1 
ATOM   3601 C  CZ   . PHE   A 1 168 ? 10.859 -17.497 2.870   1.00 17.82 ?  168 PHE   A CZ   1 
ATOM   3602 H  H    . PHE   A 1 168 ? 5.116  -14.612 1.013   1.00 24.65 ?  168 PHE   A H    1 
ATOM   3603 H  HA   . PHE   A 1 168 ? 7.380  -15.529 -0.022  1.00 24.78 ?  168 PHE   A HA   1 
ATOM   3604 H  HB2  . PHE   A 1 168 ? 7.400  -14.464 2.072   1.00 23.27 ?  168 PHE   A HB2  1 
ATOM   3605 H  HB3  . PHE   A 1 168 ? 6.552  -15.665 2.676   1.00 23.27 ?  168 PHE   A HB3  1 
ATOM   3606 H  HD1  . PHE   A 1 168 ? 9.674  -15.066 1.132   1.00 22.28 ?  168 PHE   A HD1  1 
ATOM   3607 H  HD2  . PHE   A 1 168 ? 7.722  -17.489 3.636   1.00 21.14 ?  168 PHE   A HD2  1 
ATOM   3608 H  HE1  . PHE   A 1 168 ? 11.637 -16.178 1.578   1.00 21.57 ?  168 PHE   A HE1  1 
ATOM   3609 H  HE2  . PHE   A 1 168 ? 9.699  -18.605 4.083   1.00 21.22 ?  168 PHE   A HE2  1 
ATOM   3610 H  HZ   . PHE   A 1 168 ? 11.657 -17.945 3.052   1.00 21.43 ?  168 PHE   A HZ   1 
ATOM   3611 N  N    . LEU   A 1 169 ? 7.232  -17.946 -0.192  1.00 26.84 ?  169 LEU   A N    1 
ATOM   3612 C  CA   . LEU   A 1 169 ? 7.060  -19.374 -0.355  1.00 33.24 ?  169 LEU   A CA   1 
ATOM   3613 C  C    . LEU   A 1 169 ? 7.977  -20.089 0.622   1.00 35.25 ?  169 LEU   A C    1 
ATOM   3614 O  O    . LEU   A 1 169 ? 7.543  -20.503 1.698   1.00 35.97 ?  169 LEU   A O    1 
ATOM   3615 C  CB   . LEU   A 1 169 ? 7.372  -19.791 -1.795  1.00 36.82 ?  169 LEU   A CB   1 
ATOM   3616 C  CG   . LEU   A 1 169 ? 7.034  -21.235 -2.171  1.00 39.46 ?  169 LEU   A CG   1 
ATOM   3617 C  CD1  . LEU   A 1 169 ? 5.634  -21.599 -1.703  1.00 40.44 ?  169 LEU   A CD1  1 
ATOM   3618 C  CD2  . LEU   A 1 169 ? 7.160  -21.431 -3.675  1.00 40.35 ?  169 LEU   A CD2  1 
ATOM   3619 O  OXT  . LEU   A 1 169 ? 9.171  -20.247 0.367   1.00 35.22 -1 169 LEU   A OXT  1 
ATOM   3620 H  H    . LEU   A 1 169 ? 7.917  -17.626 -0.608  1.00 32.25 ?  169 LEU   A H    1 
ATOM   3621 H  HA   . LEU   A 1 169 ? 6.139  -19.604 -0.155  1.00 39.93 ?  169 LEU   A HA   1 
ATOM   3622 H  HB2  . LEU   A 1 169 ? 6.873  -19.215 -2.392  1.00 44.23 ?  169 LEU   A HB2  1 
ATOM   3623 H  HB3  . LEU   A 1 169 ? 8.322  -19.669 -1.948  1.00 44.23 ?  169 LEU   A HB3  1 
ATOM   3624 H  HG   . LEU   A 1 169 ? 7.663  -21.833 -1.738  1.00 47.39 ?  169 LEU   A HG   1 
ATOM   3625 H  HD11 . LEU   A 1 169 ? 5.354  -22.412 -2.149  1.00 48.57 ?  169 LEU   A HD11 1 
ATOM   3626 H  HD12 . LEU   A 1 169 ? 5.649  -21.737 -0.742  1.00 48.57 ?  169 LEU   A HD12 1 
ATOM   3627 H  HD13 . LEU   A 1 169 ? 5.030  -20.873 -1.925  1.00 48.57 ?  169 LEU   A HD13 1 
ATOM   3628 H  HD21 . LEU   A 1 169 ? 6.951  -22.353 -3.892  1.00 48.45 ?  169 LEU   A HD21 1 
ATOM   3629 H  HD22 . LEU   A 1 169 ? 6.538  -20.837 -4.123  1.00 48.45 ?  169 LEU   A HD22 1 
ATOM   3630 H  HD23 . LEU   A 1 169 ? 8.068  -21.225 -3.945  1.00 48.45 ?  169 LEU   A HD23 1 
ATOM   3631 N  N    A SER   B 1 1   ? 50.841 -9.260  -23.783 0.82 27.16 ?  1   SER   B N    1 
ATOM   3632 N  N    B SER   B 1 1   ? 50.788 -9.220  -23.730 0.18 27.16 ?  1   SER   B N    1 
ATOM   3633 C  CA   A SER   B 1 1   ? 51.303 -10.299 -22.842 0.82 26.91 ?  1   SER   B CA   1 
ATOM   3634 C  CA   B SER   B 1 1   ? 51.281 -10.236 -22.776 0.18 27.05 ?  1   SER   B CA   1 
ATOM   3635 C  C    A SER   B 1 1   ? 50.210 -11.330 -22.585 0.82 25.79 ?  1   SER   B C    1 
ATOM   3636 C  C    B SER   B 1 1   ? 50.222 -11.306 -22.557 0.18 26.72 ?  1   SER   B C    1 
ATOM   3637 O  O    A SER   B 1 1   ? 49.013 -11.116 -22.860 0.82 25.45 ?  1   SER   B O    1 
ATOM   3638 O  O    B SER   B 1 1   ? 49.067 -11.149 -22.958 0.18 26.56 ?  1   SER   B O    1 
ATOM   3639 C  CB   A SER   B 1 1   ? 51.740 -9.682  -21.516 0.82 27.57 ?  1   SER   B CB   1 
ATOM   3640 C  CB   B SER   B 1 1   ? 51.645 -9.587  -21.445 0.18 27.18 ?  1   SER   B CB   1 
ATOM   3641 O  OG   A SER   B 1 1   ? 50.623 -9.462  -20.676 0.82 29.53 ?  1   SER   B OG   1 
ATOM   3642 O  OG   B SER   B 1 1   ? 50.507 -9.491  -20.608 0.18 27.64 ?  1   SER   B OG   1 
ATOM   3643 H  H1   A SER   B 1 1   ? 50.733 -9.623  -24.586 0.82 32.63 ?  1   SER   B H1   1 
ATOM   3644 H  H1   B SER   B 1 1   ? 51.480 -8.761  -24.044 0.18 32.64 ?  1   SER   B H1   1 
ATOM   3645 H  H2   A SER   B 1 1   ? 50.072 -8.931  -23.492 0.82 32.63 ?  1   SER   B H2   1 
ATOM   3646 H  H2   B SER   B 1 1   ? 50.369 -9.629  -24.398 0.18 32.64 ?  1   SER   B H2   1 
ATOM   3647 H  H3   A SER   B 1 1   ? 51.452 -8.616  -23.822 0.82 32.63 ?  1   SER   B H3   1 
ATOM   3648 H  H3   B SER   B 1 1   ? 50.229 -8.676  -23.310 0.18 32.64 ?  1   SER   B H3   1 
ATOM   3649 H  HA   A SER   B 1 1   ? 52.067 -10.744 -23.239 0.82 32.34 ?  1   SER   B HA   1 
ATOM   3650 H  HA   B SER   B 1 1   ? 52.070 -10.649 -23.150 0.18 32.50 ?  1   SER   B HA   1 
ATOM   3651 H  HB2  A SER   B 1 1   ? 52.348 -10.295 -21.077 0.82 33.13 ?  1   SER   B HB2  1 
ATOM   3652 H  HB2  B SER   B 1 1   ? 52.324 -10.128 -21.015 0.18 32.65 ?  1   SER   B HB2  1 
ATOM   3653 H  HB3  A SER   B 1 1   ? 52.184 -8.838  -21.690 0.82 33.13 ?  1   SER   B HB3  1 
ATOM   3654 H  HB3  B SER   B 1 1   ? 51.987 -8.694  -21.610 0.18 32.65 ?  1   SER   B HB3  1 
ATOM   3655 H  HG   A SER   B 1 1   ? 50.852 -8.984  -20.022 0.82 35.48 ?  1   SER   B HG   1 
ATOM   3656 H  HG   B SER   B 1 1   ? 50.625 -8.888  -20.038 0.18 33.21 ?  1   SER   B HG   1 
ATOM   3657 N  N    A MET   B 1 2   ? 50.649 -12.454 -22.038 0.82 25.43 ?  2   MET   B N    1 
ATOM   3658 N  N    B MET   B 1 2   ? 50.626 -12.390 -21.904 0.18 26.49 ?  2   MET   B N    1 
ATOM   3659 C  CA   A MET   B 1 2   ? 49.825 -13.641 -21.869 0.82 25.83 ?  2   MET   B CA   1 
ATOM   3660 C  CA   B MET   B 1 2   ? 49.798 -13.580 -21.745 0.18 26.21 ?  2   MET   B CA   1 
ATOM   3661 C  C    A MET   B 1 2   ? 49.578 -13.836 -20.380 0.82 23.98 ?  2   MET   B C    1 
ATOM   3662 C  C    B MET   B 1 2   ? 49.524 -13.787 -20.263 0.18 24.48 ?  2   MET   B C    1 
ATOM   3663 O  O    A MET   B 1 2   ? 50.511 -14.121 -19.622 0.82 24.24 ?  2   MET   B O    1 
ATOM   3664 O  O    B MET   B 1 2   ? 50.422 -14.178 -19.509 0.18 24.66 ?  2   MET   B O    1 
ATOM   3665 C  CB   A MET   B 1 2   ? 50.559 -14.838 -22.462 0.82 29.58 ?  2   MET   B CB   1 
ATOM   3666 C  CB   B MET   B 1 2   ? 50.523 -14.782 -22.335 0.18 27.78 ?  2   MET   B CB   1 
ATOM   3667 C  CG   A MET   B 1 2   ? 49.711 -16.080 -22.667 0.82 33.01 ?  2   MET   B CG   1 
ATOM   3668 C  CG   B MET   B 1 2   ? 49.627 -15.947 -22.717 0.18 29.20 ?  2   MET   B CG   1 
ATOM   3669 S  SD   A MET   B 1 2   ? 50.568 -17.283 -23.701 0.82 36.42 ?  2   MET   B SD   1 
ATOM   3670 S  SD   B MET   B 1 2   ? 50.500 -17.118 -23.765 0.18 30.49 ?  2   MET   B SD   1 
ATOM   3671 C  CE   A MET   B 1 2   ? 51.134 -16.213 -25.013 0.82 36.38 ?  2   MET   B CE   1 
ATOM   3672 C  CE   B MET   B 1 2   ? 51.335 -15.986 -24.867 0.18 30.64 ?  2   MET   B CE   1 
ATOM   3673 H  H    A MET   B 1 2   ? 51.453 -12.566 -21.747 0.82 30.56 ?  2   MET   B H    1 
ATOM   3674 H  H    B MET   B 1 2   ? 51.403 -12.465 -21.543 0.18 31.82 ?  2   MET   B H    1 
ATOM   3675 H  HA   A MET   B 1 2   ? 48.983 -13.537 -22.336 0.82 31.04 ?  2   MET   B HA   1 
ATOM   3676 H  HA   B MET   B 1 2   ? 48.965 -13.467 -22.228 0.18 31.50 ?  2   MET   B HA   1 
ATOM   3677 H  HB2  A MET   B 1 2   ? 50.910 -14.549 -23.312 0.82 35.54 ?  2   MET   B HB2  1 
ATOM   3678 H  HB2  B MET   B 1 2   ? 50.989 -14.456 -23.115 0.18 33.38 ?  2   MET   B HB2  1 
ATOM   3679 H  HB3  A MET   B 1 2   ? 51.287 -15.093 -21.879 0.82 35.54 ?  2   MET   B HB3  1 
ATOM   3680 H  HB3  B MET   B 1 2   ? 51.163 -15.124 -21.698 0.18 33.38 ?  2   MET   B HB3  1 
ATOM   3681 H  HG2  A MET   B 1 2   ? 49.526 -16.488 -21.802 0.82 39.65 ?  2   MET   B HG2  1 
ATOM   3682 H  HG2  B MET   B 1 2   ? 49.346 -16.411 -21.911 0.18 35.07 ?  2   MET   B HG2  1 
ATOM   3683 H  HG3  A MET   B 1 2   ? 48.882 -15.845 -23.111 0.82 39.65 ?  2   MET   B HG3  1 
ATOM   3684 H  HG3  B MET   B 1 2   ? 48.855 -15.627 -23.203 0.18 35.07 ?  2   MET   B HG3  1 
ATOM   3685 H  HE1  A MET   B 1 2   ? 51.284 -16.748 -25.794 0.82 43.70 ?  2   MET   B HE1  1 
ATOM   3686 H  HE1  B MET   B 1 2   ? 51.546 -16.458 -25.671 0.18 36.81 ?  2   MET   B HE1  1 
ATOM   3687 H  HE2  A MET   B 1 2   ? 50.445 -15.548 -25.184 0.82 43.70 ?  2   MET   B HE2  1 
ATOM   3688 H  HE2  B MET   B 1 2   ? 50.744 -15.237 -25.066 0.18 36.81 ?  2   MET   B HE2  1 
ATOM   3689 H  HE3  A MET   B 1 2   ? 51.958 -15.771 -24.741 0.82 43.70 ?  2   MET   B HE3  1 
ATOM   3690 H  HE3  B MET   B 1 2   ? 52.149 -15.663 -24.438 0.18 36.81 ?  2   MET   B HE3  1 
ATOM   3691 N  N    A VAL   B 1 3   ? 48.327 -13.661 -19.962 0.82 21.67 ?  3   VAL   B N    1 
ATOM   3692 N  N    B VAL   B 1 3   ? 48.289 -13.522 -19.848 0.18 22.53 ?  3   VAL   B N    1 
ATOM   3693 C  CA   A VAL   B 1 3   ? 47.910 -13.902 -18.588 0.82 20.60 ?  3   VAL   B CA   1 
ATOM   3694 C  CA   B VAL   B 1 3   ? 47.849 -13.782 -18.484 0.18 20.71 ?  3   VAL   B CA   1 
ATOM   3695 C  C    A VAL   B 1 3   ? 46.676 -14.795 -18.613 0.82 18.84 ?  3   VAL   B C    1 
ATOM   3696 C  C    B VAL   B 1 3   ? 46.599 -14.648 -18.526 0.18 18.76 ?  3   VAL   B C    1 
ATOM   3697 O  O    A VAL   B 1 3   ? 45.954 -14.875 -19.608 0.82 19.39 ?  3   VAL   B O    1 
ATOM   3698 O  O    B VAL   B 1 3   ? 45.786 -14.560 -19.451 0.18 18.67 ?  3   VAL   B O    1 
ATOM   3699 C  CB   A VAL   B 1 3   ? 47.625 -12.589 -17.819 0.82 22.29 ?  3   VAL   B CB   1 
ATOM   3700 C  CB   B VAL   B 1 3   ? 47.585 -12.486 -17.686 0.18 21.03 ?  3   VAL   B CB   1 
ATOM   3701 C  CG1  A VAL   B 1 3   ? 48.894 -11.738 -17.716 0.82 22.95 ?  3   VAL   B CG1  1 
ATOM   3702 C  CG1  B VAL   B 1 3   ? 48.853 -11.650 -17.586 0.18 21.20 ?  3   VAL   B CG1  1 
ATOM   3703 C  CG2  A VAL   B 1 3   ? 46.499 -11.812 -18.485 0.82 22.96 ?  3   VAL   B CG2  1 
ATOM   3704 C  CG2  B VAL   B 1 3   ? 46.453 -11.690 -18.316 0.18 21.17 ?  3   VAL   B CG2  1 
ATOM   3705 H  H    A VAL   B 1 3   ? 47.685 -13.407 -20.473 0.82 26.04 ?  3   VAL   B H    1 
ATOM   3706 H  H    B VAL   B 1 3   ? 47.684 -13.180 -20.354 0.18 27.08 ?  3   VAL   B H    1 
ATOM   3707 H  HA   A VAL   B 1 3   ? 48.612 -14.377 -18.118 0.82 24.76 ?  3   VAL   B HA   1 
ATOM   3708 H  HA   B VAL   B 1 3   ? 48.542 -14.278 -18.025 0.18 24.90 ?  3   VAL   B HA   1 
ATOM   3709 H  HB   A VAL   B 1 3   ? 47.346 -12.809 -16.917 0.82 26.78 ?  3   VAL   B HB   1 
ATOM   3710 H  HB   B VAL   B 1 3   ? 47.315 -12.728 -16.786 0.18 25.27 ?  3   VAL   B HB   1 
ATOM   3711 H  HG11 A VAL   B 1 3   ? 48.691 -10.929 -17.221 0.82 27.58 ?  3   VAL   B HG11 1 
ATOM   3712 H  HG11 B VAL   B 1 3   ? 48.665 -10.855 -17.062 0.18 25.47 ?  3   VAL   B HG11 1 
ATOM   3713 H  HG12 A VAL   B 1 3   ? 49.578 -12.247 -17.251 0.82 27.58 ?  3   VAL   B HG12 1 
ATOM   3714 H  HG12 B VAL   B 1 3   ? 49.544 -12.175 -17.152 0.18 25.47 ?  3   VAL   B HG12 1 
ATOM   3715 H  HG13 A VAL   B 1 3   ? 49.197 -11.515 -18.609 0.82 27.58 ?  3   VAL   B HG13 1 
ATOM   3716 H  HG13 B VAL   B 1 3   ? 49.138 -11.399 -18.478 0.18 25.47 ?  3   VAL   B HG13 1 
ATOM   3717 H  HG21 A VAL   B 1 3   ? 46.445 -10.933 -18.083 0.82 27.59 ?  3   VAL   B HG21 1 
ATOM   3718 H  HG21 B VAL   B 1 3   ? 46.409 -10.820 -17.893 0.18 25.44 ?  3   VAL   B HG21 1 
ATOM   3719 H  HG22 A VAL   B 1 3   ? 46.687 -11.733 -19.432 0.82 27.59 ?  3   VAL   B HG22 1 
ATOM   3720 H  HG22 B VAL   B 1 3   ? 46.628 -11.591 -19.265 0.18 25.44 ?  3   VAL   B HG22 1 
ATOM   3721 H  HG23 A VAL   B 1 3   ? 45.665 -12.290 -18.351 0.82 27.59 ?  3   VAL   B HG23 1 
ATOM   3722 H  HG23 B VAL   B 1 3   ? 45.617 -12.166 -18.182 0.18 25.44 ?  3   VAL   B HG23 1 
ATOM   3723 N  N    . ASN   B 1 4   ? 46.445 -15.484 -17.500 1.00 17.11 ?  4   ASN   B N    1 
ATOM   3724 C  CA   . ASN   B 1 4   ? 45.308 -16.396 -17.392 1.00 15.82 ?  4   ASN   B CA   1 
ATOM   3725 C  C    . ASN   B 1 4   ? 45.252 -17.354 -18.582 1.00 16.12 ?  4   ASN   B C    1 
ATOM   3726 O  O    . ASN   B 1 4   ? 44.193 -17.603 -19.154 1.00 17.00 ?  4   ASN   B O    1 
ATOM   3727 C  CB   . ASN   B 1 4   ? 43.987 -15.638 -17.226 1.00 15.33 ?  4   ASN   B CB   1 
ATOM   3728 C  CG   . ASN   B 1 4   ? 43.940 -14.832 -15.942 1.00 14.77 ?  4   ASN   B CG   1 
ATOM   3729 O  OD1  . ASN   B 1 4   ? 44.236 -15.344 -14.866 1.00 14.15 ?  4   ASN   B OD1  1 
ATOM   3730 N  ND2  . ASN   B 1 4   ? 43.595 -13.556 -16.055 1.00 15.71 ?  4   ASN   B ND2  1 
ATOM   3731 H  H    A ASN   B 1 4   ? 46.941 -15.451 -16.801 0.82 20.56 ?  4   ASN   B H    1 
ATOM   3732 H  H    B ASN   B 1 4   ? 46.994 -15.533 -16.842 0.18 20.56 ?  4   ASN   B H    1 
ATOM   3733 H  HA   . ASN   B 1 4   ? 45.433 -16.934 -16.597 1.00 19.03 ?  4   ASN   B HA   1 
ATOM   3734 H  HB2  . ASN   B 1 4   ? 43.875 -15.026 -17.968 1.00 18.44 ?  4   ASN   B HB2  1 
ATOM   3735 H  HB3  . ASN   B 1 4   ? 43.258 -16.278 -17.206 1.00 18.44 ?  4   ASN   B HB3  1 
ATOM   3736 H  HD21 . ASN   B 1 4   ? 43.558 -13.058 -15.352 1.00 18.89 ?  4   ASN   B HD21 1 
ATOM   3737 H  HD22 . ASN   B 1 4   ? 43.399 -13.227 -16.823 1.00 18.89 ?  4   ASN   B HD22 1 
ATOM   3738 N  N    . SER   B 1 5   ? 46.412 -17.888 -18.965 1.00 17.21 ?  5   SER   B N    1 
ATOM   3739 C  CA   . SER   B 1 5   ? 46.503 -18.815 -20.094 1.00 19.63 ?  5   SER   B CA   1 
ATOM   3740 C  C    . SER   B 1 5   ? 46.491 -20.245 -19.566 1.00 21.15 ?  5   SER   B C    1 
ATOM   3741 O  O    . SER   B 1 5   ? 47.505 -20.934 -19.517 1.00 23.01 ?  5   SER   B O    1 
ATOM   3742 C  CB   . SER   B 1 5   ? 47.760 -18.532 -20.917 1.00 21.12 ?  5   SER   B CB   1 
ATOM   3743 O  OG   . SER   B 1 5   ? 48.936 -18.793 -20.168 1.00 23.99 ?  5   SER   B OG   1 
ATOM   3744 H  H    . SER   B 1 5   ? 47.167 -17.731 -18.582 1.00 20.69 ?  5   SER   B H    1 
ATOM   3745 H  HA   . SER   B 1 5   ? 45.736 -18.697 -20.673 1.00 23.59 ?  5   SER   B HA   1 
ATOM   3746 H  HB2  . SER   B 1 5   ? 47.755 -19.094 -21.709 1.00 25.38 ?  5   SER   B HB2  1 
ATOM   3747 H  HB3  . SER   B 1 5   ? 47.750 -17.598 -21.179 1.00 25.38 ?  5   SER   B HB3  1 
ATOM   3748 H  HG   . SER   B 1 5   ? 48.978 -19.612 -19.980 1.00 28.82 ?  5   SER   B HG   1 
ATOM   3749 N  N    . PHE   B 1 6   ? 45.306 -20.675 -19.148 1.00 21.45 ?  6   PHE   B N    1 
ATOM   3750 C  CA   . PHE   B 1 6   ? 45.133 -22.021 -18.624 1.00 21.07 ?  6   PHE   B CA   1 
ATOM   3751 C  C    . PHE   B 1 6   ? 45.058 -23.010 -19.777 1.00 24.38 ?  6   PHE   B C    1 
ATOM   3752 O  O    . PHE   B 1 6   ? 44.385 -22.759 -20.780 1.00 26.40 ?  6   PHE   B O    1 
ATOM   3753 C  CB   . PHE   B 1 6   ? 43.854 -22.098 -17.792 1.00 18.93 ?  6   PHE   B CB   1 
ATOM   3754 C  CG   . PHE   B 1 6   ? 43.870 -21.223 -16.568 1.00 16.91 ?  6   PHE   B CG   1 
ATOM   3755 C  CD1  . PHE   B 1 6   ? 44.387 -21.691 -15.374 1.00 15.86 ?  6   PHE   B CD1  1 
ATOM   3756 C  CD2  . PHE   B 1 6   ? 43.365 -19.931 -16.614 1.00 16.14 ?  6   PHE   B CD2  1 
ATOM   3757 C  CE1  . PHE   B 1 6   ? 44.394 -20.890 -14.242 1.00 15.49 ?  6   PHE   B CE1  1 
ATOM   3758 C  CE2  . PHE   B 1 6   ? 43.377 -19.119 -15.493 1.00 16.56 ?  6   PHE   B CE2  1 
ATOM   3759 C  CZ   . PHE   B 1 6   ? 43.897 -19.592 -14.308 1.00 15.75 ?  6   PHE   B CZ   1 
ATOM   3760 H  H    . PHE   B 1 6   ? 44.583 -20.211 -19.167 1.00 25.78 ?  6   PHE   B H    1 
ATOM   3761 H  HA   . PHE   B 1 6   ? 45.885 -22.258 -18.062 1.00 25.32 ?  6   PHE   B HA   1 
ATOM   3762 H  HB2  . PHE   B 1 6   ? 43.102 -21.827 -18.341 1.00 22.75 ?  6   PHE   B HB2  1 
ATOM   3763 H  HB3  . PHE   B 1 6   ? 43.726 -23.016 -17.495 1.00 22.75 ?  6   PHE   B HB3  1 
ATOM   3764 H  HD1  . PHE   B 1 6   ? 44.731 -22.555 -15.326 1.00 19.07 ?  6   PHE   B HD1  1 
ATOM   3765 H  HD2  . PHE   B 1 6   ? 43.014 -19.608 -17.411 1.00 19.41 ?  6   PHE   B HD2  1 
ATOM   3766 H  HE1  . PHE   B 1 6   ? 44.756 -21.207 -13.444 1.00 18.63 ?  6   PHE   B HE1  1 
ATOM   3767 H  HE2  . PHE   B 1 6   ? 43.035 -18.255 -15.540 1.00 19.91 ?  6   PHE   B HE2  1 
ATOM   3768 H  HZ   . PHE   B 1 6   ? 43.906 -19.052 -13.551 1.00 18.94 ?  6   PHE   B HZ   1 
ATOM   3769 N  N    . SER   B 1 7   ? 45.766 -24.129 -19.636 1.00 25.47 ?  7   SER   B N    1 
ATOM   3770 C  CA   . SER   B 1 7   ? 45.863 -25.119 -20.699 1.00 27.78 ?  7   SER   B CA   1 
ATOM   3771 C  C    . SER   B 1 7   ? 45.799 -26.523 -20.117 1.00 27.05 ?  7   SER   B C    1 
ATOM   3772 O  O    . SER   B 1 7   ? 46.390 -26.802 -19.070 1.00 27.68 ?  7   SER   B O    1 
ATOM   3773 C  CB   . SER   B 1 7   ? 47.168 -24.949 -21.488 1.00 30.40 ?  7   SER   B CB   1 
ATOM   3774 O  OG   . SER   B 1 7   ? 47.191 -25.799 -22.621 1.00 32.29 ?  7   SER   B OG   1 
ATOM   3775 H  H    . SER   B 1 7   ? 46.207 -24.337 -18.923 1.00 30.60 ?  7   SER   B H    1 
ATOM   3776 H  HA   . SER   B 1 7   ? 45.120 -25.012 -21.309 1.00 33.37 ?  7   SER   B HA   1 
ATOM   3777 H  HB2  . SER   B 1 7   ? 47.239 -24.025 -21.781 1.00 36.52 ?  7   SER   B HB2  1 
ATOM   3778 H  HB3  . SER   B 1 7   ? 47.917 -25.170 -20.912 1.00 36.52 ?  7   SER   B HB3  1 
ATOM   3779 H  HG   . SER   B 1 7   ? 47.908 -25.692 -23.045 1.00 38.79 ?  7   SER   B HG   1 
ATOM   3780 N  N    . GLY   B 1 8   ? 45.080 -27.405 -20.810 1.00 26.58 ?  8   GLY   B N    1 
ATOM   3781 C  CA   . GLY   B 1 8   ? 45.037 -28.802 -20.437 1.00 25.78 ?  8   GLY   B CA   1 
ATOM   3782 C  C    . GLY   B 1 8   ? 44.095 -29.135 -19.308 1.00 24.11 ?  8   GLY   B C    1 
ATOM   3783 O  O    . GLY   B 1 8   ? 44.233 -30.202 -18.695 1.00 25.38 ?  8   GLY   B O    1 
ATOM   3784 H  H    . GLY   B 1 8   ? 44.611 -27.208 -21.501 1.00 31.93 ?  8   GLY   B H    1 
ATOM   3785 H  HA2  . GLY   B 1 8   ? 44.770 -29.324 -21.210 1.00 30.97 ?  8   GLY   B HA2  1 
ATOM   3786 H  HA3  . GLY   B 1 8   ? 45.923 -29.086 -20.173 1.00 30.97 ?  8   GLY   B HA3  1 
ATOM   3787 N  N    . TYR   B 1 9   ? 43.122 -28.274 -19.021 1.00 22.25 ?  9   TYR   B N    1 
ATOM   3788 C  CA   . TYR   B 1 9   ? 42.170 -28.548 -17.958 1.00 20.00 ?  9   TYR   B CA   1 
ATOM   3789 C  C    . TYR   B 1 9   ? 40.984 -29.337 -18.481 1.00 19.35 ?  9   TYR   B C    1 
ATOM   3790 O  O    . TYR   B 1 9   ? 40.565 -29.193 -19.633 1.00 21.28 ?  9   TYR   B O    1 
ATOM   3791 C  CB   . TYR   B 1 9   ? 41.665 -27.260 -17.316 1.00 19.40 ?  9   TYR   B CB   1 
ATOM   3792 C  CG   . TYR   B 1 9   ? 42.685 -26.634 -16.397 1.00 18.71 ?  9   TYR   B CG   1 
ATOM   3793 C  CD1  . TYR   B 1 9   ? 43.789 -25.970 -16.914 1.00 19.09 ?  9   TYR   B CD1  1 
ATOM   3794 C  CD2  . TYR   B 1 9   ? 42.564 -26.725 -15.018 1.00 17.93 ?  9   TYR   B CD2  1 
ATOM   3795 C  CE1  . TYR   B 1 9   ? 44.739 -25.412 -16.086 1.00 19.34 ?  9   TYR   B CE1  1 
ATOM   3796 C  CE2  . TYR   B 1 9   ? 43.509 -26.164 -14.180 1.00 18.21 ?  9   TYR   B CE2  1 
ATOM   3797 C  CZ   . TYR   B 1 9   ? 44.598 -25.510 -14.722 1.00 19.15 ?  9   TYR   B CZ   1 
ATOM   3798 O  OH   . TYR   B 1 9   ? 45.543 -24.951 -13.896 1.00 20.17 ?  9   TYR   B OH   1 
ATOM   3799 H  H    . TYR   B 1 9   ? 42.977 -27.539 -19.441 1.00 26.73 ?  9   TYR   B H    1 
ATOM   3800 H  HA   . TYR   B 1 9   ? 42.599 -29.077 -17.271 1.00 24.03 ?  9   TYR   B HA   1 
ATOM   3801 H  HB2  . TYR   B 1 9   ? 41.441 -26.617 -18.007 1.00 23.31 ?  9   TYR   B HB2  1 
ATOM   3802 H  HB3  . TYR   B 1 9   ? 40.882 -27.470 -16.788 1.00 23.31 ?  9   TYR   B HB3  1 
ATOM   3803 H  HD1  . TYR   B 1 9   ? 43.890 -25.908 -17.837 1.00 22.94 ?  9   TYR   B HD1  1 
ATOM   3804 H  HD2  . TYR   B 1 9   ? 41.830 -27.169 -14.651 1.00 21.56 ?  9   TYR   B HD2  1 
ATOM   3805 H  HE1  . TYR   B 1 9   ? 45.468 -24.973 -16.450 1.00 23.24 ?  9   TYR   B HE1  1 
ATOM   3806 H  HE2  . TYR   B 1 9   ? 43.408 -26.233 -13.257 1.00 21.89 ?  9   TYR   B HE2  1 
ATOM   3807 H  HH   . TYR   B 1 9   ? 46.138 -24.588 -14.359 1.00 24.24 ?  9   TYR   B HH   1 
ATOM   3808 N  N    . LEU   B 1 10  ? 40.453 -30.187 -17.612 1.00 17.41 ?  10  LEU   B N    1 
ATOM   3809 C  CA   . LEU   B 1 10  ? 39.246 -30.941 -17.887 1.00 17.39 ?  10  LEU   B CA   1 
ATOM   3810 C  C    . LEU   B 1 10  ? 38.056 -30.173 -17.327 1.00 16.77 ?  10  LEU   B C    1 
ATOM   3811 O  O    . LEU   B 1 10  ? 38.068 -29.759 -16.165 1.00 16.45 ?  10  LEU   B O    1 
ATOM   3812 C  CB   . LEU   B 1 10  ? 39.351 -32.310 -17.217 1.00 18.25 ?  10  LEU   B CB   1 
ATOM   3813 C  CG   . LEU   B 1 10  ? 38.213 -33.268 -17.550 1.00 19.78 ?  10  LEU   B CG   1 
ATOM   3814 C  CD1  . LEU   B 1 10  ? 38.345 -33.768 -18.982 1.00 20.98 ?  10  LEU   B CD1  1 
ATOM   3815 C  CD2  . LEU   B 1 10  ? 38.165 -34.420 -16.564 1.00 21.00 ?  10  LEU   B CD2  1 
ATOM   3816 H  H    . LEU   B 1 10  ? 40.781 -30.345 -16.828 1.00 20.93 ?  10  LEU   B H    1 
ATOM   3817 H  HA   . LEU   B 1 10  ? 39.129 -31.064 -18.838 1.00 20.91 ?  10  LEU   B HA   1 
ATOM   3818 H  HB2  . LEU   B 1 10  ? 40.181 -32.734 -17.494 1.00 21.93 ?  10  LEU   B HB2  1 
ATOM   3819 H  HB3  . LEU   B 1 10  ? 39.358 -32.191 -16.251 1.00 21.93 ?  10  LEU   B HB3  1 
ATOM   3820 H  HG   . LEU   B 1 10  ? 37.372 -32.791 -17.481 1.00 23.77 ?  10  LEU   B HG   1 
ATOM   3821 H  HD11 . LEU   B 1 10  ? 37.654 -34.427 -19.149 1.00 25.21 ?  10  LEU   B HD11 1 
ATOM   3822 H  HD12 . LEU   B 1 10  ? 38.238 -33.016 -19.587 1.00 25.21 ?  10  LEU   B HD12 1 
ATOM   3823 H  HD13 . LEU   B 1 10  ? 39.220 -34.166 -19.097 1.00 25.21 ?  10  LEU   B HD13 1 
ATOM   3824 H  HD21 . LEU   B 1 10  ? 37.435 -35.010 -16.806 1.00 25.23 ?  10  LEU   B HD21 1 
ATOM   3825 H  HD22 . LEU   B 1 10  ? 39.006 -34.898 -16.598 1.00 25.23 ?  10  LEU   B HD22 1 
ATOM   3826 H  HD23 . LEU   B 1 10  ? 38.021 -34.063 -15.673 1.00 25.23 ?  10  LEU   B HD23 1 
ATOM   3827 N  N    . LYS   B 1 11  ? 37.035 -29.988 -18.151 1.00 17.86 ?  11  LYS   B N    1 
ATOM   3828 C  CA   . LYS   B 1 11  ? 35.841 -29.269 -17.736 1.00 19.64 ?  11  LYS   B CA   1 
ATOM   3829 C  C    . LYS   B 1 11  ? 34.953 -30.196 -16.913 1.00 19.06 ?  11  LYS   B C    1 
ATOM   3830 O  O    . LYS   B 1 11  ? 34.561 -31.270 -17.386 1.00 21.07 ?  11  LYS   B O    1 
ATOM   3831 C  CB   . LYS   B 1 11  ? 35.106 -28.776 -18.981 1.00 23.09 ?  11  LYS   B CB   1 
ATOM   3832 C  CG   . LYS   B 1 11  ? 33.934 -27.850 -18.721 1.00 26.38 ?  11  LYS   B CG   1 
ATOM   3833 C  CD   . LYS   B 1 11  ? 33.189 -27.559 -20.019 1.00 29.16 ?  11  LYS   B CD   1 
ATOM   3834 C  CE   . LYS   B 1 11  ? 32.148 -26.470 -19.840 1.00 31.25 ?  11  LYS   B CE   1 
ATOM   3835 N  NZ   . LYS   B 1 11  ? 32.776 -25.139 -19.629 1.00 32.42 ?  11  LYS   B NZ   1 
ATOM   3836 H  H    . LYS   B 1 11  ? 37.006 -30.279 -18.959 1.00 21.47 ?  11  LYS   B H    1 
ATOM   3837 H  HA   . LYS   B 1 11  ? 36.090 -28.505 -17.192 1.00 23.61 ?  11  LYS   B HA   1 
ATOM   3838 H  HB2  . LYS   B 1 11  ? 35.737 -28.295 -19.540 1.00 27.74 ?  11  LYS   B HB2  1 
ATOM   3839 H  HB3  . LYS   B 1 11  ? 34.768 -29.545 -19.464 1.00 27.74 ?  11  LYS   B HB3  1 
ATOM   3840 H  HG2  . LYS   B 1 11  ? 33.317 -28.273 -18.104 1.00 31.70 ?  11  LYS   B HG2  1 
ATOM   3841 H  HG3  . LYS   B 1 11  ? 34.257 -27.011 -18.358 1.00 31.70 ?  11  LYS   B HG3  1 
ATOM   3842 H  HD2  . LYS   B 1 11  ? 33.824 -27.263 -20.691 1.00 35.03 ?  11  LYS   B HD2  1 
ATOM   3843 H  HD3  . LYS   B 1 11  ? 32.739 -28.365 -20.317 1.00 35.03 ?  11  LYS   B HD3  1 
ATOM   3844 H  HE2  . LYS   B 1 11  ? 31.594 -26.424 -20.635 1.00 37.54 ?  11  LYS   B HE2  1 
ATOM   3845 H  HE3  . LYS   B 1 11  ? 31.603 -26.678 -19.065 1.00 37.54 ?  11  LYS   B HE3  1 
ATOM   3846 H  HZ1  . LYS   B 1 11  ? 32.147 -24.515 -19.549 1.00 38.94 ?  11  LYS   B HZ1  1 
ATOM   3847 H  HZ2  . LYS   B 1 11  ? 33.270 -25.149 -18.890 1.00 38.94 ?  11  LYS   B HZ2  1 
ATOM   3848 H  HZ3  . LYS   B 1 11  ? 33.296 -24.936 -20.323 1.00 38.94 ?  11  LYS   B HZ3  1 
ATOM   3849 N  N    . LEU   B 1 12  ? 34.637 -29.788 -15.684 1.00 17.29 ?  12  LEU   B N    1 
ATOM   3850 C  CA   . LEU   B 1 12  ? 33.673 -30.494 -14.845 1.00 16.98 ?  12  LEU   B CA   1 
ATOM   3851 C  C    . LEU   B 1 12  ? 32.279 -29.893 -14.935 1.00 17.00 ?  12  LEU   B C    1 
ATOM   3852 O  O    . LEU   B 1 12  ? 31.296 -30.615 -15.108 1.00 17.83 ?  12  LEU   B O    1 
ATOM   3853 C  CB   . LEU   B 1 12  ? 34.134 -30.510 -13.383 1.00 16.51 ?  12  LEU   B CB   1 
ATOM   3854 C  CG   . LEU   B 1 12  ? 35.471 -31.191 -13.104 1.00 16.57 ?  12  LEU   B CG   1 
ATOM   3855 C  CD1  . LEU   B 1 12  ? 35.800 -31.136 -11.623 1.00 16.62 ?  12  LEU   B CD1  1 
ATOM   3856 C  CD2  . LEU   B 1 12  ? 35.467 -32.630 -13.609 1.00 17.66 ?  12  LEU   B CD2  1 
ATOM   3857 H  H    . LEU   B 1 12  ? 34.972 -29.089 -15.310 1.00 20.79 ?  12  LEU   B H    1 
ATOM   3858 H  HA   . LEU   B 1 12  ? 33.609 -31.410 -15.150 1.00 20.42 ?  12  LEU   B HA   1 
ATOM   3859 H  HB2  . LEU   B 1 12  ? 34.204 -29.595 -13.075 1.00 19.85 ?  12  LEU   B HB2  1 
ATOM   3860 H  HB3  . LEU   B 1 12  ? 33.460 -30.975 -12.860 1.00 19.85 ?  12  LEU   B HB3  1 
ATOM   3861 H  HG   . LEU   B 1 12  ? 36.168 -30.713 -13.580 1.00 19.92 ?  12  LEU   B HG   1 
ATOM   3862 H  HD11 . LEU   B 1 12  ? 36.656 -31.574 -11.473 1.00 19.99 ?  12  LEU   B HD11 1 
ATOM   3863 H  HD12 . LEU   B 1 12  ? 35.850 -30.210 -11.342 1.00 19.99 ?  12  LEU   B HD12 1 
ATOM   3864 H  HD13 . LEU   B 1 12  ? 35.106 -31.597 -11.126 1.00 19.99 ?  12  LEU   B HD13 1 
ATOM   3865 H  HD21 . LEU   B 1 12  ? 36.265 -33.077 -13.291 1.00 21.23 ?  12  LEU   B HD21 1 
ATOM   3866 H  HD22 . LEU   B 1 12  ? 34.677 -33.079 -13.270 1.00 21.23 ?  12  LEU   B HD22 1 
ATOM   3867 H  HD23 . LEU   B 1 12  ? 35.453 -32.624 -14.579 1.00 21.23 ?  12  LEU   B HD23 1 
ATOM   3868 N  N    . THR   B 1 13  ? 32.180 -28.575 -14.808 1.00 16.80 ?  13  THR   B N    1 
ATOM   3869 C  CA   . THR   B 1 13  ? 30.951 -27.827 -15.009 1.00 17.12 ?  13  THR   B CA   1 
ATOM   3870 C  C    . THR   B 1 13  ? 31.283 -26.622 -15.883 1.00 18.80 ?  13  THR   B C    1 
ATOM   3871 O  O    . THR   B 1 13  ? 32.427 -26.430 -16.310 1.00 19.32 ?  13  THR   B O    1 
ATOM   3872 C  CB   . THR   B 1 13  ? 30.360 -27.357 -13.676 1.00 16.91 ?  13  THR   B CB   1 
ATOM   3873 O  OG1  . THR   B 1 13  ? 31.205 -26.330 -13.137 1.00 16.47 ?  13  THR   B OG1  1 
ATOM   3874 C  CG2  . THR   B 1 13  ? 30.265 -28.511 -12.683 1.00 17.35 ?  13  THR   B CG2  1 
ATOM   3875 H  H    . THR   B 1 13  ? 32.843 -28.070 -14.590 1.00 20.20 ?  13  THR   B H    1 
ATOM   3876 H  HA   . THR   B 1 13  ? 30.296 -28.381 -15.458 1.00 20.58 ?  13  THR   B HA   1 
ATOM   3877 H  HB   . THR   B 1 13  ? 29.462 -27.004 -13.818 1.00 20.32 ?  13  THR   B HB   1 
ATOM   3878 H  HG1  . THR   B 1 13  ? 30.885 -25.572 -13.320 1.00 19.80 ?  13  THR   B HG1  1 
ATOM   3879 H  HG21 . THR   B 1 13  ? 29.732 -28.251 -11.915 1.00 20.86 ?  13  THR   B HG21 1 
ATOM   3880 H  HG22 . THR   B 1 13  ? 29.851 -29.280 -13.106 1.00 20.86 ?  13  THR   B HG22 1 
ATOM   3881 H  HG23 . THR   B 1 13  ? 31.153 -28.761 -12.379 1.00 20.86 ?  13  THR   B HG23 1 
ATOM   3882 N  N    A ASP   B 1 14  ? 30.270 -25.796 -16.145 0.82 20.01 ?  14  ASP   B N    1 
ATOM   3883 N  N    B ASP   B 1 14  ? 30.272 -25.786 -16.137 0.18 19.48 ?  14  ASP   B N    1 
ATOM   3884 C  CA   A ASP   B 1 14  ? 30.480 -24.632 -16.998 0.82 21.59 ?  14  ASP   B CA   1 
ATOM   3885 C  CA   B ASP   B 1 14  ? 30.471 -24.627 -17.001 0.18 20.21 ?  14  ASP   B CA   1 
ATOM   3886 C  C    A ASP   B 1 14  ? 31.574 -23.717 -16.462 0.82 19.91 ?  14  ASP   B C    1 
ATOM   3887 C  C    B ASP   B 1 14  ? 31.491 -23.645 -16.443 0.18 18.88 ?  14  ASP   B C    1 
ATOM   3888 O  O    A ASP   B 1 14  ? 32.217 -23.006 -17.243 0.82 21.35 ?  14  ASP   B O    1 
ATOM   3889 O  O    B ASP   B 1 14  ? 31.987 -22.798 -17.195 0.18 19.11 ?  14  ASP   B O    1 
ATOM   3890 C  CB   A ASP   B 1 14  ? 29.173 -23.857 -17.161 0.82 25.15 ?  14  ASP   B CB   1 
ATOM   3891 C  CB   B ASP   B 1 14  ? 29.146 -23.900 -17.238 0.18 22.30 ?  14  ASP   B CB   1 
ATOM   3892 C  CG   A ASP   B 1 14  ? 28.208 -24.530 -18.114 0.82 28.95 ?  14  ASP   B CG   1 
ATOM   3893 C  CG   B ASP   B 1 14  ? 28.253 -24.623 -18.228 0.18 24.19 ?  14  ASP   B CG   1 
ATOM   3894 O  OD1  A ASP   B 1 14  ? 28.610 -25.484 -18.819 0.82 30.39 ?  14  ASP   B OD1  1 
ATOM   3895 O  OD1  B ASP   B 1 14  ? 28.788 -25.326 -19.112 0.18 24.90 ?  14  ASP   B OD1  1 
ATOM   3896 O  OD2  A ASP   B 1 14  ? 27.036 -24.107 -18.151 0.82 30.39 -1 14  ASP   B OD2  1 
ATOM   3897 O  OD2  B ASP   B 1 14  ? 27.016 -24.490 -18.125 0.18 24.80 -1 14  ASP   B OD2  1 
ATOM   3898 H  H    A ASP   B 1 14  ? 29.471 -25.882 -15.839 0.82 24.05 ?  14  ASP   B H    1 
ATOM   3899 H  H    B ASP   B 1 14  ? 29.475 -25.868 -15.825 0.18 23.42 ?  14  ASP   B H    1 
ATOM   3900 H  HA   A ASP   B 1 14  ? 30.759 -24.933 -17.873 0.82 25.94 ?  14  ASP   B HA   1 
ATOM   3901 H  HA   B ASP   B 1 14  ? 30.799 -24.934 -17.859 0.18 24.30 ?  14  ASP   B HA   1 
ATOM   3902 H  HB2  A ASP   B 1 14  ? 28.728 -23.793 -16.303 0.82 30.22 ?  14  ASP   B HB2  1 
ATOM   3903 H  HB2  B ASP   B 1 14  ? 28.666 -23.836 -16.398 0.18 26.80 ?  14  ASP   B HB2  1 
ATOM   3904 H  HB3  A ASP   B 1 14  ? 29.370 -22.970 -17.502 0.82 30.22 ?  14  ASP   B HB3  1 
ATOM   3905 H  HB3  B ASP   B 1 14  ? 29.334 -23.008 -17.579 0.18 26.80 ?  14  ASP   B HB3  1 
ATOM   3906 N  N    . ASN   B 1 15  ? 31.803 -23.718 -15.146 1.00 17.46 ?  15  ASN   B N    1 
ATOM   3907 C  CA   . ASN   B 1 15  ? 32.766 -22.799 -14.544 1.00 15.15 ?  15  ASN   B CA   1 
ATOM   3908 C  C    . ASN   B 1 15  ? 33.859 -23.453 -13.707 1.00 14.27 ?  15  ASN   B C    1 
ATOM   3909 O  O    . ASN   B 1 15  ? 34.703 -22.724 -13.175 1.00 14.48 ?  15  ASN   B O    1 
ATOM   3910 C  CB   . ASN   B 1 15  ? 32.053 -21.745 -13.684 1.00 15.26 ?  15  ASN   B CB   1 
ATOM   3911 C  CG   . ASN   B 1 15  ? 31.434 -22.342 -12.443 1.00 14.90 ?  15  ASN   B CG   1 
ATOM   3912 O  OD1  . ASN   B 1 15  ? 30.491 -23.136 -12.533 1.00 16.76 ?  15  ASN   B OD1  1 
ATOM   3913 N  ND2  . ASN   B 1 15  ? 31.958 -21.992 -11.284 1.00 14.62 ?  15  ASN   B ND2  1 
ATOM   3914 H  H    A ASN   B 1 15  ? 31.407 -24.236 -14.582 0.82 20.99 ?  15  ASN   B H    1 
ATOM   3915 H  H    B ASN   B 1 15  ? 31.450 -24.275 -14.591 0.18 20.99 ?  15  ASN   B H    1 
ATOM   3916 H  HA   . ASN   B 1 15  ? 33.211 -22.318 -15.250 1.00 18.21 ?  15  ASN   B HA   1 
ATOM   3917 H  HB2  . ASN   B 1 15  ? 32.698 -21.067 -13.409 1.00 18.35 ?  15  ASN   B HB2  1 
ATOM   3918 H  HB3  . ASN   B 1 15  ? 31.346 -21.325 -14.204 1.00 18.35 ?  15  ASN   B HB3  1 
ATOM   3919 H  HD21 . ASN   B 1 15  ? 31.635 -22.300 -10.550 1.00 17.59 ?  15  ASN   B HD21 1 
ATOM   3920 H  HD22 . ASN   B 1 15  ? 32.621 -21.435 -11.256 1.00 17.59 ?  15  ASN   B HD22 1 
ATOM   3921 N  N    . VAL   B 1 16  ? 33.876 -24.777 -13.565 1.00 14.07 ?  16  VAL   B N    1 
ATOM   3922 C  CA   . VAL   B 1 16  ? 34.875 -25.468 -12.751 1.00 13.87 ?  16  VAL   B CA   1 
ATOM   3923 C  C    . VAL   B 1 16  ? 35.671 -26.400 -13.650 1.00 13.67 ?  16  VAL   B C    1 
ATOM   3924 O  O    . VAL   B 1 16  ? 35.094 -27.273 -14.317 1.00 14.83 ?  16  VAL   B O    1 
ATOM   3925 C  CB   . VAL   B 1 16  ? 34.247 -26.232 -11.576 1.00 14.21 ?  16  VAL   B CB   1 
ATOM   3926 C  CG1  . VAL   B 1 16  ? 35.327 -26.963 -10.783 1.00 14.42 ?  16  VAL   B CG1  1 
ATOM   3927 C  CG2  . VAL   B 1 16  ? 33.458 -25.283 -10.682 1.00 14.89 ?  16  VAL   B CG2  1 
ATOM   3928 H  H    . VAL   B 1 16  ? 33.305 -25.308 -13.932 1.00 16.92 ?  16  VAL   B H    1 
ATOM   3929 H  HA   . VAL   B 1 16  ? 35.489 -24.812 -12.383 1.00 16.69 ?  16  VAL   B HA   1 
ATOM   3930 H  HB   . VAL   B 1 16  ? 33.633 -26.896 -11.925 1.00 17.09 ?  16  VAL   B HB   1 
ATOM   3931 H  HG11 . VAL   B 1 16  ? 34.949 -27.261 -9.941  1.00 17.34 ?  16  VAL   B HG11 1 
ATOM   3932 H  HG12 . VAL   B 1 16  ? 35.639 -27.724 -11.294 1.00 17.34 ?  16  VAL   B HG12 1 
ATOM   3933 H  HG13 . VAL   B 1 16  ? 36.061 -26.350 -10.614 1.00 17.34 ?  16  VAL   B HG13 1 
ATOM   3934 H  HG21 . VAL   B 1 16  ? 33.116 -25.779 -9.922  1.00 17.91 ?  16  VAL   B HG21 1 
ATOM   3935 H  HG22 . VAL   B 1 16  ? 34.043 -24.573 -10.380 1.00 17.91 ?  16  VAL   B HG22 1 
ATOM   3936 H  HG23 . VAL   B 1 16  ? 32.720 -24.911 -11.192 1.00 17.91 ?  16  VAL   B HG23 1 
ATOM   3937 N  N    . TYR   B 1 17  ? 36.996 -26.230 -13.632 1.00 14.35 ?  17  TYR   B N    1 
ATOM   3938 C  CA   . TYR   B 1 17  ? 37.942 -26.978 -14.446 1.00 14.28 ?  17  TYR   B CA   1 
ATOM   3939 C  C    . TYR   B 1 17  ? 38.993 -27.591 -13.532 1.00 13.77 ?  17  TYR   B C    1 
ATOM   3940 O  O    . TYR   B 1 17  ? 39.268 -27.066 -12.450 1.00 13.95 ?  17  TYR   B O    1 
ATOM   3941 C  CB   . TYR   B 1 17  ? 38.655 -26.048 -15.432 1.00 16.53 ?  17  TYR   B CB   1 
ATOM   3942 C  CG   . TYR   B 1 17  ? 37.733 -25.281 -16.344 1.00 19.38 ?  17  TYR   B CG   1 
ATOM   3943 C  CD1  . TYR   B 1 17  ? 37.146 -24.089 -15.935 1.00 20.57 ?  17  TYR   B CD1  1 
ATOM   3944 C  CD2  . TYR   B 1 17  ? 37.446 -25.750 -17.618 1.00 21.28 ?  17  TYR   B CD2  1 
ATOM   3945 C  CE1  . TYR   B 1 17  ? 36.298 -23.384 -16.772 1.00 22.01 ?  17  TYR   B CE1  1 
ATOM   3946 C  CE2  . TYR   B 1 17  ? 36.605 -25.053 -18.462 1.00 22.60 ?  17  TYR   B CE2  1 
ATOM   3947 C  CZ   . TYR   B 1 17  ? 36.031 -23.875 -18.032 1.00 22.94 ?  17  TYR   B CZ   1 
ATOM   3948 O  OH   . TYR   B 1 17  ? 35.193 -23.177 -18.870 1.00 24.24 ?  17  TYR   B OH   1 
ATOM   3949 H  H    . TYR   B 1 17  ? 37.391 -25.651 -13.126 1.00 17.26 ?  17  TYR   B H    1 
ATOM   3950 H  HA   . TYR   B 1 17  ? 37.484 -27.683 -14.936 1.00 17.18 ?  17  TYR   B HA   1 
ATOM   3951 H  HB2  . TYR   B 1 17  ? 39.182 -25.407 -14.933 1.00 19.87 ?  17  TYR   B HB2  1 
ATOM   3952 H  HB3  . TYR   B 1 17  ? 39.230 -26.583 -15.994 1.00 19.87 ?  17  TYR   B HB3  1 
ATOM   3953 H  HD1  . TYR   B 1 17  ? 37.324 -23.758 -15.086 1.00 24.72 ?  17  TYR   B HD1  1 
ATOM   3954 H  HD2  . TYR   B 1 17  ? 37.826 -26.544 -17.911 1.00 25.57 ?  17  TYR   B HD2  1 
ATOM   3955 H  HE1  . TYR   B 1 17  ? 35.910 -22.586 -16.487 1.00 26.45 ?  17  TYR   B HE1  1 
ATOM   3956 H  HE2  . TYR   B 1 17  ? 36.416 -25.379 -19.315 1.00 27.16 ?  17  TYR   B HE2  1 
ATOM   3957 H  HH   . TYR   B 1 17  ? 35.108 -23.576 -19.604 1.00 29.13 ?  17  TYR   B HH   1 
ATOM   3958 N  N    . ILE   B 1 18  ? 39.607 -28.693 -13.970 1.00 13.63 ?  18  ILE   B N    1 
ATOM   3959 C  CA   . ILE   B 1 18  ? 40.540 -29.419 -13.113 1.00 13.55 ?  18  ILE   B CA   1 
ATOM   3960 C  C    . ILE   B 1 18  ? 41.704 -29.967 -13.931 1.00 13.89 ?  18  ILE   B C    1 
ATOM   3961 O  O    . ILE   B 1 18  ? 41.544 -30.366 -15.088 1.00 15.01 ?  18  ILE   B O    1 
ATOM   3962 C  CB   . ILE   B 1 18  ? 39.793 -30.519 -12.308 1.00 13.88 ?  18  ILE   B CB   1 
ATOM   3963 C  CG1  . ILE   B 1 18  ? 40.646 -31.058 -11.158 1.00 14.50 ?  18  ILE   B CG1  1 
ATOM   3964 C  CG2  . ILE   B 1 18  ? 39.280 -31.634 -13.230 1.00 14.01 ?  18  ILE   B CG2  1 
ATOM   3965 C  CD1  . ILE   B 1 18  ? 39.830 -31.857 -10.146 1.00 16.05 ?  18  ILE   B CD1  1 
ATOM   3966 H  H    . ILE   B 1 18  ? 39.507 -29.034 -14.753 1.00 16.39 ?  18  ILE   B H    1 
ATOM   3967 H  HA   . ILE   B 1 18  ? 40.908 -28.801 -12.464 1.00 16.30 ?  18  ILE   B HA   1 
ATOM   3968 H  HB   . ILE   B 1 18  ? 39.012 -30.107 -11.909 1.00 16.70 ?  18  ILE   B HB   1 
ATOM   3969 H  HG12 . ILE   B 1 18  ? 41.331 -31.638 -11.513 1.00 17.44 ?  18  ILE   B HG12 1 
ATOM   3970 H  HG13 . ILE   B 1 18  ? 41.047 -30.309 -10.688 1.00 17.44 ?  18  ILE   B HG13 1 
ATOM   3971 H  HG21 . ILE   B 1 18  ? 38.701 -32.224 -12.720 1.00 16.85 ?  18  ILE   B HG21 1 
ATOM   3972 H  HG22 . ILE   B 1 18  ? 38.782 -31.232 -13.958 1.00 16.85 ?  18  ILE   B HG22 1 
ATOM   3973 H  HG23 . ILE   B 1 18  ? 40.035 -32.131 -13.577 1.00 16.85 ?  18  ILE   B HG23 1 
ATOM   3974 H  HD11 . ILE   B 1 18  ? 40.406 -32.125 -9.414  1.00 19.30 ?  18  ILE   B HD11 1 
ATOM   3975 H  HD12 . ILE   B 1 18  ? 39.106 -31.302 -9.810  1.00 19.30 ?  18  ILE   B HD12 1 
ATOM   3976 H  HD13 . ILE   B 1 18  ? 39.464 -32.643 -10.583 1.00 19.30 ?  18  ILE   B HD13 1 
ATOM   3977 N  N    . LYS   B 1 19  ? 42.884 -29.997 -13.308 1.00 14.47 ?  19  LYS   B N    1 
ATOM   3978 C  CA   . LYS   B 1 19  ? 44.098 -30.471 -13.957 1.00 14.95 ?  19  LYS   B CA   1 
ATOM   3979 C  C    . LYS   B 1 19  ? 44.994 -31.146 -12.929 1.00 14.78 ?  19  LYS   B C    1 
ATOM   3980 O  O    . LYS   B 1 19  ? 45.072 -30.712 -11.778 1.00 14.64 ?  19  LYS   B O    1 
ATOM   3981 C  CB   . LYS   B 1 19  ? 44.872 -29.309 -14.596 1.00 16.19 ?  19  LYS   B CB   1 
ATOM   3982 C  CG   . LYS   B 1 19  ? 46.077 -29.720 -15.426 1.00 18.02 ?  19  LYS   B CG   1 
ATOM   3983 C  CD   . LYS   B 1 19  ? 46.810 -28.494 -15.952 1.00 19.77 ?  19  LYS   B CD   1 
ATOM   3984 C  CE   . LYS   B 1 19  ? 47.976 -28.882 -16.841 1.00 21.52 ?  19  LYS   B CE   1 
ATOM   3985 N  NZ   . LYS   B 1 19  ? 48.744 -27.700 -17.305 1.00 22.66 ?  19  LYS   B NZ   1 
ATOM   3986 H  H    . LYS   B 1 19  ? 42.999 -29.743 -12.493 1.00 17.40 ?  19  LYS   B H    1 
ATOM   3987 H  HA   . LYS   B 1 19  ? 43.867 -31.115 -14.647 1.00 17.98 ?  19  LYS   B HA   1 
ATOM   3988 H  HB2  . LYS   B 1 19  ? 44.266 -28.824 -15.177 1.00 19.47 ?  19  LYS   B HB2  1 
ATOM   3989 H  HB3  . LYS   B 1 19  ? 45.183 -28.723 -13.887 1.00 19.47 ?  19  LYS   B HB3  1 
ATOM   3990 H  HG2  . LYS   B 1 19  ? 46.685 -30.235 -14.875 1.00 21.66 ?  19  LYS   B HG2  1 
ATOM   3991 H  HG3  . LYS   B 1 19  ? 45.774 -30.251 -16.182 1.00 21.66 ?  19  LYS   B HG3  1 
ATOM   3992 H  HD2  . LYS   B 1 19  ? 46.194 -27.953 -16.471 1.00 23.76 ?  19  LYS   B HD2  1 
ATOM   3993 H  HD3  . LYS   B 1 19  ? 47.154 -27.984 -15.202 1.00 23.76 ?  19  LYS   B HD3  1 
ATOM   3994 H  HE2  . LYS   B 1 19  ? 48.573 -29.461 -16.342 1.00 25.86 ?  19  LYS   B HE2  1 
ATOM   3995 H  HE3  . LYS   B 1 19  ? 47.634 -29.351 -17.621 1.00 25.86 ?  19  LYS   B HE3  1 
ATOM   3996 H  HZ1  . LYS   B 1 19  ? 49.400 -27.961 -17.849 1.00 27.23 ?  19  LYS   B HZ1  1 
ATOM   3997 H  HZ2  . LYS   B 1 19  ? 48.209 -27.142 -17.745 1.00 27.23 ?  19  LYS   B HZ2  1 
ATOM   3998 H  HZ3  . LYS   B 1 19  ? 49.098 -27.275 -16.609 1.00 27.23 ?  19  LYS   B HZ3  1 
ATOM   3999 N  N    . ASN   B 1 20  ? 45.683 -32.198 -13.358 1.00 15.91 ?  20  ASN   B N    1 
ATOM   4000 C  CA   . ASN   B 1 20  ? 46.714 -32.829 -12.539 1.00 16.82 ?  20  ASN   B CA   1 
ATOM   4001 C  C    . ASN   B 1 20  ? 47.985 -32.012 -12.736 1.00 17.35 ?  20  ASN   B C    1 
ATOM   4002 O  O    . ASN   B 1 20  ? 48.630 -32.099 -13.785 1.00 19.44 ?  20  ASN   B O    1 
ATOM   4003 C  CB   . ASN   B 1 20  ? 46.888 -34.282 -12.974 1.00 18.59 ?  20  ASN   B CB   1 
ATOM   4004 C  CG   . ASN   B 1 20  ? 48.060 -34.981 -12.303 1.00 19.93 ?  20  ASN   B CG   1 
ATOM   4005 O  OD1  . ASN   B 1 20  ? 48.739 -35.802 -12.929 1.00 22.03 ?  20  ASN   B OD1  1 
ATOM   4006 N  ND2  . ASN   B 1 20  ? 48.293 -34.686 -11.033 1.00 19.49 ?  20  ASN   B ND2  1 
ATOM   4007 H  H    . ASN   B 1 20  ? 45.575 -32.564 -14.129 1.00 19.13 ?  20  ASN   B H    1 
ATOM   4008 H  HA   . ASN   B 1 20  ? 46.448 -32.806 -11.608 1.00 20.22 ?  20  ASN   B HA   1 
ATOM   4009 H  HB2  . ASN   B 1 20  ? 46.085 -34.776 -12.748 1.00 22.35 ?  20  ASN   B HB2  1 
ATOM   4010 H  HB3  . ASN   B 1 20  ? 47.034 -34.306 -13.932 1.00 22.35 ?  20  ASN   B HB3  1 
ATOM   4011 H  HD21 . ASN   B 1 20  ? 48.952 -35.054 -10.620 1.00 23.42 ?  20  ASN   B HD21 1 
ATOM   4012 H  HD22 . ASN   B 1 20  ? 47.795 -34.116 -10.621 1.00 23.42 ?  20  ASN   B HD22 1 
ATOM   4013 N  N    . ALA   B 1 21  ? 48.340 -31.202 -11.734 1.00 16.99 ?  21  ALA   B N    1 
ATOM   4014 C  CA   . ALA   B 1 21  ? 49.442 -30.264 -11.885 1.00 17.85 ?  21  ALA   B CA   1 
ATOM   4015 C  C    . ALA   B 1 21  ? 49.909 -29.781 -10.520 1.00 17.04 ?  21  ALA   B C    1 
ATOM   4016 O  O    . ALA   B 1 21  ? 49.166 -29.816 -9.534  1.00 16.83 ?  21  ALA   B O    1 
ATOM   4017 C  CB   . ALA   B 1 21  ? 49.034 -29.075 -12.757 1.00 19.06 ?  21  ALA   B CB   1 
ATOM   4018 H  H    . ALA   B 1 21  ? 47.956 -31.181 -10.959 1.00 20.43 ?  21  ALA   B H    1 
ATOM   4019 H  HA   . ALA   B 1 21  ? 50.182 -30.717 -12.313 1.00 21.45 ?  21  ALA   B HA   1 
ATOM   4020 H  HB1  . ALA   B 1 21  ? 49.812 -28.524 -12.905 1.00 22.91 ?  21  ALA   B HB1  1 
ATOM   4021 H  HB2  . ALA   B 1 21  ? 48.696 -29.413 -13.600 1.00 22.91 ?  21  ALA   B HB2  1 
ATOM   4022 H  HB3  . ALA   B 1 21  ? 48.342 -28.572 -12.299 1.00 22.91 ?  21  ALA   B HB3  1 
ATOM   4023 N  N    . ASP   B 1 22  ? 51.167 -29.340 -10.495 1.00 16.08 ?  22  ASP   B N    1 
ATOM   4024 C  CA   . ASP   B 1 22  ? 51.776 -28.646 -9.366  1.00 15.46 ?  22  ASP   B CA   1 
ATOM   4025 C  C    . ASP   B 1 22  ? 51.366 -27.178 -9.449  1.00 14.15 ?  22  ASP   B C    1 
ATOM   4026 O  O    . ASP   B 1 22  ? 51.674 -26.506 -10.435 1.00 14.25 ?  22  ASP   B O    1 
ATOM   4027 C  CB   . ASP   B 1 22  ? 53.293 -28.821 -9.518  1.00 16.55 ?  22  ASP   B CB   1 
ATOM   4028 C  CG   . ASP   B 1 22  ? 54.116 -28.056 -8.487  1.00 18.01 ?  22  ASP   B CG   1 
ATOM   4029 O  OD1  . ASP   B 1 22  ? 53.742 -26.942 -8.081  1.00 18.39 ?  22  ASP   B OD1  1 
ATOM   4030 O  OD2  . ASP   B 1 22  ? 55.193 -28.568 -8.111  1.00 20.28 -1 22  ASP   B OD2  1 
ATOM   4031 H  H    . ASP   B 1 22  ? 51.715 -29.445 -11.156 1.00 19.34 ?  22  ASP   B H    1 
ATOM   4032 H  HA   . ASP   B 1 22  ? 51.484 -29.036 -8.523  1.00 18.59 ?  22  ASP   B HA   1 
ATOM   4033 H  HB2  . ASP   B 1 22  ? 53.518 -29.756 -9.435  1.00 19.90 ?  22  ASP   B HB2  1 
ATOM   4034 H  HB3  . ASP   B 1 22  ? 53.557 -28.491 -10.392 1.00 19.90 ?  22  ASP   B HB3  1 
ATOM   4035 N  N    . ILE   B 1 23  ? 50.658 -26.686 -8.427  1.00 13.75 ?  23  ILE   B N    1 
ATOM   4036 C  CA   . ILE   B 1 23  ? 50.063 -25.351 -8.497  1.00 13.01 ?  23  ILE   B CA   1 
ATOM   4037 C  C    . ILE   B 1 23  ? 51.116 -24.257 -8.638  1.00 12.91 ?  23  ILE   B C    1 
ATOM   4038 O  O    . ILE   B 1 23  ? 50.846 -23.214 -9.242  1.00 12.41 ?  23  ILE   B O    1 
ATOM   4039 C  CB   . ILE   B 1 23  ? 49.123 -25.113 -7.298  1.00 13.38 ?  23  ILE   B CB   1 
ATOM   4040 C  CG1  . ILE   B 1 23  ? 48.292 -23.844 -7.496  1.00 14.27 ?  23  ILE   B CG1  1 
ATOM   4041 C  CG2  . ILE   B 1 23  ? 49.894 -25.079 -5.991  1.00 14.36 ?  23  ILE   B CG2  1 
ATOM   4042 C  CD1  . ILE   B 1 23  ? 47.165 -23.682 -6.482  1.00 15.10 ?  23  ILE   B CD1  1 
ATOM   4043 H  H    . ILE   B 1 23  ? 50.512 -27.104 -7.691  1.00 16.54 ?  23  ILE   B H    1 
ATOM   4044 H  HA   . ILE   B 1 23  ? 49.514 -25.314 -9.294  1.00 15.65 ?  23  ILE   B HA   1 
ATOM   4045 H  HB   . ILE   B 1 23  ? 48.507 -25.861 -7.257  1.00 16.10 ?  23  ILE   B HB   1 
ATOM   4046 H  HG12 . ILE   B 1 23  ? 48.877 -23.071 -7.417  1.00 17.16 ?  23  ILE   B HG12 1 
ATOM   4047 H  HG13 . ILE   B 1 23  ? 47.897 -23.862 -8.384  1.00 17.16 ?  23  ILE   B HG13 1 
ATOM   4048 H  HG21 . ILE   B 1 23  ? 49.267 -25.067 -5.253  1.00 17.27 ?  23  ILE   B HG21 1 
ATOM   4049 H  HG22 . ILE   B 1 23  ? 50.455 -25.871 -5.934  1.00 17.27 ?  23  ILE   B HG22 1 
ATOM   4050 H  HG23 . ILE   B 1 23  ? 50.448 -24.283 -5.970  1.00 17.27 ?  23  ILE   B HG23 1 
ATOM   4051 H  HD11 . ILE   B 1 23  ? 46.641 -22.902 -6.716  1.00 18.16 ?  23  ILE   B HD11 1 
ATOM   4052 H  HD12 . ILE   B 1 23  ? 46.607 -24.477 -6.510  1.00 18.16 ?  23  ILE   B HD12 1 
ATOM   4053 H  HD13 . ILE   B 1 23  ? 47.549 -23.578 -5.600  1.00 18.16 ?  23  ILE   B HD13 1 
ATOM   4054 N  N    . VAL   B 1 24  ? 52.308 -24.453 -8.071  1.00 13.39 ?  24  VAL   B N    1 
ATOM   4055 C  CA   . VAL   B 1 24  ? 53.386 -23.477 -8.240  1.00 13.71 ?  24  VAL   B CA   1 
ATOM   4056 C  C    . VAL   B 1 24  ? 53.834 -23.429 -9.694  1.00 14.09 ?  24  VAL   B C    1 
ATOM   4057 O  O    . VAL   B 1 24  ? 53.968 -22.352 -10.289 1.00 14.37 ?  24  VAL   B O    1 
ATOM   4058 C  CB   . VAL   B 1 24  ? 54.564 -23.801 -7.297  1.00 14.48 ?  24  VAL   B CB   1 
ATOM   4059 C  CG1  . VAL   B 1 24  ? 55.775 -22.920 -7.619  1.00 15.16 ?  24  VAL   B CG1  1 
ATOM   4060 C  CG2  . VAL   B 1 24  ? 54.151 -23.622 -5.854  1.00 15.53 ?  24  VAL   B CG2  1 
ATOM   4061 H  H    . VAL   B 1 24  ? 52.517 -25.135 -7.591  1.00 16.11 ?  24  VAL   B H    1 
ATOM   4062 H  HA   . VAL   B 1 24  ? 53.055 -22.600 -8.002  1.00 16.49 ?  24  VAL   B HA   1 
ATOM   4063 H  HB   . VAL   B 1 24  ? 54.826 -24.727 -7.417  1.00 17.41 ?  24  VAL   B HB   1 
ATOM   4064 H  HG11 . VAL   B 1 24  ? 56.375 -22.916 -6.854  1.00 18.23 ?  24  VAL   B HG11 1 
ATOM   4065 H  HG12 . VAL   B 1 24  ? 56.234 -23.286 -8.391  1.00 18.23 ?  24  VAL   B HG12 1 
ATOM   4066 H  HG13 . VAL   B 1 24  ? 55.472 -22.019 -7.804  1.00 18.23 ?  24  VAL   B HG13 1 
ATOM   4067 H  HG21 . VAL   B 1 24  ? 54.873 -23.910 -5.278  1.00 18.68 ?  24  VAL   B HG21 1 
ATOM   4068 H  HG22 . VAL   B 1 24  ? 53.954 -22.685 -5.698  1.00 18.68 ?  24  VAL   B HG22 1 
ATOM   4069 H  HG23 . VAL   B 1 24  ? 53.358 -24.158 -5.684  1.00 18.68 ?  24  VAL   B HG23 1 
ATOM   4070 N  N    . GLU   B 1 25  ? 54.099 -24.599 -10.281 1.00 14.91 ?  25  GLU   B N    1 
ATOM   4071 C  CA   . GLU   B 1 25  ? 54.493 -24.636 -11.684 1.00 16.20 ?  25  GLU   B CA   1 
ATOM   4072 C  C    . GLU   B 1 25  ? 53.384 -24.092 -12.571 1.00 15.04 ?  25  GLU   B C    1 
ATOM   4073 O  O    . GLU   B 1 25  ? 53.647 -23.384 -13.550 1.00 16.06 ?  25  GLU   B O    1 
ATOM   4074 C  CB   . GLU   B 1 25  ? 54.883 -26.059 -12.079 1.00 19.70 ?  25  GLU   B CB   1 
ATOM   4075 C  CG   . GLU   B 1 25  ? 56.181 -26.510 -11.431 1.00 24.77 ?  25  GLU   B CG   1 
ATOM   4076 C  CD   . GLU   B 1 25  ? 57.289 -25.469 -11.524 1.00 29.57 ?  25  GLU   B CD   1 
ATOM   4077 O  OE1  . GLU   B 1 25  ? 57.669 -25.096 -12.655 1.00 31.18 ?  25  GLU   B OE1  1 
ATOM   4078 O  OE2  . GLU   B 1 25  ? 57.767 -25.003 -10.462 1.00 31.00 -1 25  GLU   B OE2  1 
ATOM   4079 H  H    . GLU   B 1 25  ? 54.052 -25.368 -9.896  1.00 17.92 ?  25  GLU   B H    1 
ATOM   4080 H  HA   . GLU   B 1 25  ? 55.251 -24.054 -11.809 1.00 19.47 ?  25  GLU   B HA   1 
ATOM   4081 H  HB2  . GLU   B 1 25  ? 54.183 -26.673 -11.798 1.00 23.68 ?  25  GLU   B HB2  1 
ATOM   4082 H  HB3  . GLU   B 1 25  ? 54.993 -26.104 -13.042 1.00 23.68 ?  25  GLU   B HB3  1 
ATOM   4083 H  HG2  . GLU   B 1 25  ? 56.032 -26.665 -10.491 1.00 29.76 ?  25  GLU   B HG2  1 
ATOM   4084 H  HG3  . GLU   B 1 25  ? 56.487 -27.321 -11.866 1.00 29.76 ?  25  GLU   B HG3  1 
ATOM   4085 N  N    . GLU   B 1 26  ? 52.134 -24.401 -12.234 1.00 14.01 ?  26  GLU   B N    1 
ATOM   4086 C  CA   . GLU   B 1 26  ? 51.013 -23.877 -13.005 1.00 14.61 ?  26  GLU   B CA   1 
ATOM   4087 C  C    . GLU   B 1 26  ? 50.959 -22.360 -12.925 1.00 14.03 ?  26  GLU   B C    1 
ATOM   4088 O  O    . GLU   B 1 26  ? 50.762 -21.683 -13.937 1.00 15.18 ?  26  GLU   B O    1 
ATOM   4089 C  CB   . GLU   B 1 26  ? 49.695 -24.460 -12.492 1.00 16.46 ?  26  GLU   B CB   1 
ATOM   4090 C  CG   . GLU   B 1 26  ? 49.246 -25.727 -13.181 1.00 19.90 ?  26  GLU   B CG   1 
ATOM   4091 C  CD   . GLU   B 1 26  ? 48.972 -25.549 -14.672 1.00 21.46 ?  26  GLU   B CD   1 
ATOM   4092 O  OE1  . GLU   B 1 26  ? 47.975 -24.907 -15.067 1.00 22.12 ?  26  GLU   B OE1  1 
ATOM   4093 O  OE2  . GLU   B 1 26  ? 49.761 -26.085 -15.456 1.00 23.61 -1 26  GLU   B OE2  1 
ATOM   4094 H  H    . GLU   B 1 26  ? 51.906 -24.908 -11.572 1.00 16.85 ?  26  GLU   B H    1 
ATOM   4095 H  HA   . GLU   B 1 26  ? 51.117 -24.130 -13.934 1.00 17.58 ?  26  GLU   B HA   1 
ATOM   4096 H  HB2  . GLU   B 1 26  ? 49.790 -24.660 -11.547 1.00 19.79 ?  26  GLU   B HB2  1 
ATOM   4097 H  HB3  . GLU   B 1 26  ? 48.995 -23.797 -12.612 1.00 19.79 ?  26  GLU   B HB3  1 
ATOM   4098 H  HG2  . GLU   B 1 26  ? 49.944 -26.387 -13.089 1.00 23.92 ?  26  GLU   B HG2  1 
ATOM   4099 H  HG3  . GLU   B 1 26  ? 48.428 -26.040 -12.765 1.00 23.92 ?  26  GLU   B HG3  1 
ATOM   4100 N  N    . ALA   B 1 27  ? 51.094 -21.811 -11.718 1.00 13.29 ?  27  ALA   B N    1 
ATOM   4101 C  CA   . ALA   B 1 27  ? 51.059 -20.361 -11.567 1.00 13.96 ?  27  ALA   B CA   1 
ATOM   4102 C  C    . ALA   B 1 27  ? 52.130 -19.694 -12.421 1.00 14.63 ?  27  ALA   B C    1 
ATOM   4103 O  O    . ALA   B 1 27  ? 51.868 -18.683 -13.091 1.00 15.39 ?  27  ALA   B O    1 
ATOM   4104 C  CB   . ALA   B 1 27  ? 51.209 -19.987 -10.093 1.00 14.07 ?  27  ALA   B CB   1 
ATOM   4105 H  H    . ALA   B 1 27  ? 51.192 -22.250 -10.983 1.00 15.99 ?  27  ALA   B H    1 
ATOM   4106 H  HA   . ALA   B 1 27  ? 50.200 -20.034 -11.866 1.00 16.79 ?  27  ALA   B HA   1 
ATOM   4107 H  HB1  . ALA   B 1 27  ? 51.182 -19.022 -10.005 1.00 16.92 ?  27  ALA   B HB1  1 
ATOM   4108 H  HB2  . ALA   B 1 27  ? 50.474 -20.383 -9.591  1.00 16.92 ?  27  ALA   B HB2  1 
ATOM   4109 H  HB3  . ALA   B 1 27  ? 52.052 -20.329 -9.760  1.00 16.92 ?  27  ALA   B HB3  1 
ATOM   4110 N  N    . LYS   B 1 28  ? 53.343 -20.246 -12.420 1.00 16.21 ?  28  LYS   B N    1 
ATOM   4111 C  CA   . LYS   B 1 28  ? 54.417 -19.618 -13.181 1.00 18.12 ?  28  LYS   B CA   1 
ATOM   4112 C  C    . LYS   B 1 28  ? 54.167 -19.694 -14.683 1.00 18.92 ?  28  LYS   B C    1 
ATOM   4113 O  O    . LYS   B 1 28  ? 54.572 -18.789 -15.423 1.00 20.21 ?  28  LYS   B O    1 
ATOM   4114 C  CB   . LYS   B 1 28  ? 55.773 -20.216 -12.790 1.00 21.02 ?  28  LYS   B CB   1 
ATOM   4115 C  CG   . LYS   B 1 28  ? 56.167 -19.901 -11.347 1.00 24.00 ?  28  LYS   B CG   1 
ATOM   4116 C  CD   . LYS   B 1 28  ? 57.602 -20.290 -11.023 1.00 27.67 ?  28  LYS   B CD   1 
ATOM   4117 C  CE   . LYS   B 1 28  ? 57.720 -21.757 -10.686 1.00 30.84 ?  28  LYS   B CE   1 
ATOM   4118 N  NZ   . LYS   B 1 28  ? 59.075 -22.080 -10.160 1.00 32.03 ?  28  LYS   B NZ   1 
ATOM   4119 H  H    . LYS   B 1 28  ? 53.566 -20.961 -11.999 1.00 19.49 ?  28  LYS   B H    1 
ATOM   4120 H  HA   . LYS   B 1 28  ? 54.444 -18.678 -12.951 1.00 21.78 ?  28  LYS   B HA   1 
ATOM   4121 H  HB2  . LYS   B 1 28  ? 55.736 -21.177 -12.884 1.00 25.26 ?  28  LYS   B HB2  1 
ATOM   4122 H  HB3  . LYS   B 1 28  ? 56.459 -19.849 -13.370 1.00 25.26 ?  28  LYS   B HB3  1 
ATOM   4123 H  HG2  . LYS   B 1 28  ? 56.070 -18.945 -11.198 1.00 28.84 ?  28  LYS   B HG2  1 
ATOM   4124 H  HG3  . LYS   B 1 28  ? 55.578 -20.388 -10.750 1.00 28.84 ?  28  LYS   B HG3  1 
ATOM   4125 H  HD2  . LYS   B 1 28  ? 58.161 -20.105 -11.793 1.00 33.24 ?  28  LYS   B HD2  1 
ATOM   4126 H  HD3  . LYS   B 1 28  ? 57.903 -19.773 -10.259 1.00 33.24 ?  28  LYS   B HD3  1 
ATOM   4127 H  HE2  . LYS   B 1 28  ? 57.065 -21.983 -10.006 1.00 37.04 ?  28  LYS   B HE2  1 
ATOM   4128 H  HE3  . LYS   B 1 28  ? 57.568 -22.284 -11.487 1.00 37.04 ?  28  LYS   B HE3  1 
ATOM   4129 H  HZ1  . LYS   B 1 28  ? 59.128 -22.947 -9.966  1.00 38.47 ?  28  LYS   B HZ1  1 
ATOM   4130 H  HZ2  . LYS   B 1 28  ? 59.693 -21.881 -10.768 1.00 38.47 ?  28  LYS   B HZ2  1 
ATOM   4131 H  HZ3  . LYS   B 1 28  ? 59.234 -21.609 -9.421  1.00 38.47 ?  28  LYS   B HZ3  1 
ATOM   4132 N  N    . LYS   B 1 29  ? 53.471 -20.731 -15.147 1.00 20.15 ?  29  LYS   B N    1 
ATOM   4133 C  CA   . LYS   B 1 29  ? 53.175 -20.872 -16.569 1.00 22.44 ?  29  LYS   B CA   1 
ATOM   4134 C  C    . LYS   B 1 29  ? 51.926 -20.106 -16.992 1.00 21.50 ?  29  LYS   B C    1 
ATOM   4135 O  O    . LYS   B 1 29  ? 51.924 -19.468 -18.049 1.00 22.87 ?  29  LYS   B O    1 
ATOM   4136 C  CB   . LYS   B 1 29  ? 53.009 -22.351 -16.923 1.00 26.51 ?  29  LYS   B CB   1 
ATOM   4137 C  CG   . LYS   B 1 29  ? 52.898 -22.623 -18.415 1.00 30.58 ?  29  LYS   B CG   1 
ATOM   4138 C  CD   . LYS   B 1 29  ? 53.176 -24.086 -18.742 1.00 33.65 ?  29  LYS   B CD   1 
ATOM   4139 C  CE   . LYS   B 1 29  ? 52.109 -25.008 -18.174 1.00 35.75 ?  29  LYS   B CE   1 
ATOM   4140 N  NZ   . LYS   B 1 29  ? 52.383 -26.436 -18.505 1.00 37.05 ?  29  LYS   B NZ   1 
ATOM   4141 H  H    . LYS   B 1 29  ? 53.156 -21.365 -14.654 1.00 24.21 ?  29  LYS   B H    1 
ATOM   4142 H  HA   . LYS   B 1 29  ? 53.922 -20.526 -17.077 1.00 26.96 ?  29  LYS   B HA   1 
ATOM   4143 H  HB2  . LYS   B 1 29  ? 53.780 -22.836 -16.590 1.00 31.85 ?  29  LYS   B HB2  1 
ATOM   4144 H  HB3  . LYS   B 1 29  ? 52.203 -22.683 -16.501 1.00 31.85 ?  29  LYS   B HB3  1 
ATOM   4145 H  HG2  . LYS   B 1 29  ? 52.000 -22.411 -18.713 1.00 36.73 ?  29  LYS   B HG2  1 
ATOM   4146 H  HG3  . LYS   B 1 29  ? 53.546 -22.078 -18.889 1.00 36.73 ?  29  LYS   B HG3  1 
ATOM   4147 H  HD2  . LYS   B 1 29  ? 53.193 -24.200 -19.705 1.00 40.42 ?  29  LYS   B HD2  1 
ATOM   4148 H  HD3  . LYS   B 1 29  ? 54.032 -24.341 -18.361 1.00 40.42 ?  29  LYS   B HD3  1 
ATOM   4149 H  HE2  . LYS   B 1 29  ? 52.089 -24.920 -17.208 1.00 42.93 ?  29  LYS   B HE2  1 
ATOM   4150 H  HE3  . LYS   B 1 29  ? 51.247 -24.769 -18.550 1.00 42.93 ?  29  LYS   B HE3  1 
ATOM   4151 H  HZ1  . LYS   B 1 29  ? 51.746 -26.955 -18.163 1.00 44.49 ?  29  LYS   B HZ1  1 
ATOM   4152 H  HZ2  . LYS   B 1 29  ? 52.402 -26.545 -19.388 1.00 44.49 ?  29  LYS   B HZ2  1 
ATOM   4153 H  HZ3  . LYS   B 1 29  ? 53.169 -26.681 -18.166 1.00 44.49 ?  29  LYS   B HZ3  1 
ATOM   4154 N  N    . VAL   B 1 30  ? 50.862 -20.174 -16.188 1.00 19.91 ?  30  VAL   B N    1 
ATOM   4155 C  CA   . VAL   B 1 30  ? 49.568 -19.590 -16.549 1.00 20.10 ?  30  VAL   B CA   1 
ATOM   4156 C  C    . VAL   B 1 30  ? 49.565 -18.074 -16.401 1.00 18.80 ?  30  VAL   B C    1 
ATOM   4157 O  O    . VAL   B 1 30  ? 48.830 -17.372 -17.114 1.00 19.87 ?  30  VAL   B O    1 
ATOM   4158 C  CB   . VAL   B 1 30  ? 48.471 -20.215 -15.665 1.00 21.08 ?  30  VAL   B CB   1 
ATOM   4159 C  CG1  . VAL   B 1 30  ? 47.186 -19.401 -15.730 1.00 21.43 ?  30  VAL   B CG1  1 
ATOM   4160 C  CG2  . VAL   B 1 30  ? 48.222 -21.670 -16.057 1.00 21.88 ?  30  VAL   B CG2  1 
ATOM   4161 H  H    . VAL   B 1 30  ? 50.858 -20.582 -15.421 1.00 23.93 ?  30  VAL   B H    1 
ATOM   4162 H  HA   . VAL   B 1 30  ? 49.369 -19.825 -17.469 1.00 24.16 ?  30  VAL   B HA   1 
ATOM   4163 H  HB   . VAL   B 1 30  ? 48.770 -20.219 -14.742 1.00 25.34 ?  30  VAL   B HB   1 
ATOM   4164 H  HG11 . VAL   B 1 30  ? 46.443 -19.980 -15.500 1.00 25.75 ?  30  VAL   B HG11 1 
ATOM   4165 H  HG12 . VAL   B 1 30  ? 47.239 -18.670 -15.097 1.00 25.75 ?  30  VAL   B HG12 1 
ATOM   4166 H  HG13 . VAL   B 1 30  ? 47.065 -19.068 -16.629 1.00 25.75 ?  30  VAL   B HG13 1 
ATOM   4167 H  HG21 . VAL   B 1 30  ? 47.532 -22.045 -15.479 1.00 26.30 ?  30  VAL   B HG21 1 
ATOM   4168 H  HG22 . VAL   B 1 30  ? 47.923 -21.704 -16.981 1.00 26.30 ?  30  VAL   B HG22 1 
ATOM   4169 H  HG23 . VAL   B 1 30  ? 49.042 -22.174 -15.955 1.00 26.30 ?  30  VAL   B HG23 1 
ATOM   4170 N  N    . LYS   B 1 31  ? 50.346 -17.559 -15.464 1.00 18.17 ?  31  LYS   B N    1 
ATOM   4171 C  CA   . LYS   B 1 31  ? 50.376 -16.148 -15.108 1.00 18.42 ?  31  LYS   B CA   1 
ATOM   4172 C  C    . LYS   B 1 31  ? 48.976 -15.678 -14.714 1.00 16.37 ?  31  LYS   B C    1 
ATOM   4173 O  O    . LYS   B 1 31  ? 48.426 -14.765 -15.339 1.00 17.71 ?  31  LYS   B O    1 
ATOM   4174 C  CB   . LYS   B 1 31  ? 51.000 -15.327 -16.242 1.00 21.43 ?  31  LYS   B CB   1 
ATOM   4175 C  CG   . LYS   B 1 31  ? 52.428 -15.767 -16.580 1.00 24.47 ?  31  LYS   B CG   1 
ATOM   4176 C  CD   . LYS   B 1 31  ? 53.018 -14.970 -17.725 1.00 27.18 ?  31  LYS   B CD   1 
ATOM   4177 C  CE   . LYS   B 1 31  ? 54.500 -15.244 -17.874 1.00 29.42 ?  31  LYS   B CE   1 
ATOM   4178 N  NZ   . LYS   B 1 31  ? 55.240 -14.874 -16.635 1.00 30.59 ?  31  LYS   B NZ   1 
ATOM   4179 H  H    . LYS   B 1 31  ? 50.892 -18.040 -15.011 1.00 21.85 ?  31  LYS   B H    1 
ATOM   4180 H  HA   . LYS   B 1 31  ? 50.937 -16.060 -14.336 1.00 22.15 ?  31  LYS   B HA   1 
ATOM   4181 H  HB2  . LYS   B 1 31  ? 50.461 -15.422 -17.043 1.00 25.76 ?  31  LYS   B HB2  1 
ATOM   4182 H  HB3  . LYS   B 1 31  ? 51.030 -14.399 -15.968 1.00 25.76 ?  31  LYS   B HB3  1 
ATOM   4183 H  HG2  . LYS   B 1 31  ? 52.987 -15.645 -15.797 1.00 29.40 ?  31  LYS   B HG2  1 
ATOM   4184 H  HG3  . LYS   B 1 31  ? 52.420 -16.705 -16.837 1.00 29.40 ?  31  LYS   B HG3  1 
ATOM   4185 H  HD2  . LYS   B 1 31  ? 52.574 -15.222 -18.550 1.00 32.66 ?  31  LYS   B HD2  1 
ATOM   4186 H  HD3  . LYS   B 1 31  ? 52.896 -14.025 -17.550 1.00 32.66 ?  31  LYS   B HD3  1 
ATOM   4187 H  HE2  . LYS   B 1 31  ? 54.639 -16.191 -18.041 1.00 35.34 ?  31  LYS   B HE2  1 
ATOM   4188 H  HE3  . LYS   B 1 31  ? 54.852 -14.718 -18.609 1.00 35.34 ?  31  LYS   B HE3  1 
ATOM   4189 H  HZ1  . LYS   B 1 31  ? 56.117 -14.898 -16.785 1.00 36.74 ?  31  LYS   B HZ1  1 
ATOM   4190 H  HZ2  . LYS   B 1 31  ? 55.012 -14.052 -16.379 1.00 36.74 ?  31  LYS   B HZ2  1 
ATOM   4191 H  HZ3  . LYS   B 1 31  ? 55.044 -15.444 -15.979 1.00 36.74 ?  31  LYS   B HZ3  1 
ATOM   4192 N  N    . PRO   B 1 32  ? 48.370 -16.278 -13.683 1.00 14.55 ?  32  PRO   B N    1 
ATOM   4193 C  CA   . PRO   B 1 32  ? 46.991 -15.925 -13.324 1.00 13.60 ?  32  PRO   B CA   1 
ATOM   4194 C  C    . PRO   B 1 32  ? 46.903 -14.584 -12.614 1.00 13.58 ?  32  PRO   B C    1 
ATOM   4195 O  O    . PRO   B 1 32  ? 47.824 -14.157 -11.914 1.00 14.87 ?  32  PRO   B O    1 
ATOM   4196 C  CB   . PRO   B 1 32  ? 46.597 -17.047 -12.356 1.00 13.92 ?  32  PRO   B CB   1 
ATOM   4197 C  CG   . PRO   B 1 32  ? 47.900 -17.390 -11.680 1.00 14.31 ?  32  PRO   B CG   1 
ATOM   4198 C  CD   . PRO   B 1 32  ? 48.947 -17.265 -12.747 1.00 14.63 ?  32  PRO   B CD   1 
ATOM   4199 H  HA   . PRO   B 1 32  ? 46.408 -15.942 -14.104 1.00 16.36 ?  32  PRO   B HA   1 
ATOM   4200 H  HB2  . PRO   B 1 32  ? 45.946 -16.720 -11.713 1.00 16.74 ?  32  PRO   B HB2  1 
ATOM   4201 H  HB3  . PRO   B 1 32  ? 46.248 -17.810 -12.845 1.00 16.74 ?  32  PRO   B HB3  1 
ATOM   4202 H  HG2  . PRO   B 1 32  ? 48.072 -16.761 -10.959 1.00 17.22 ?  32  PRO   B HG2  1 
ATOM   4203 H  HG3  . PRO   B 1 32  ? 47.868 -18.298 -11.337 1.00 17.22 ?  32  PRO   B HG3  1 
ATOM   4204 H  HD2  . PRO   B 1 32  ? 49.772 -16.927 -12.371 1.00 17.59 ?  32  PRO   B HD2  1 
ATOM   4205 H  HD3  . PRO   B 1 32  ? 49.075 -18.118 -13.188 1.00 17.59 ?  32  PRO   B HD3  1 
ATOM   4206 N  N    . THR   B 1 33  ? 45.749 -13.933 -12.784 1.00 13.39 ?  33  THR   B N    1 
ATOM   4207 C  CA   . THR   B 1 33  ? 45.450 -12.755 -11.975 1.00 13.52 ?  33  THR   B CA   1 
ATOM   4208 C  C    . THR   B 1 33  ? 45.406 -13.109 -10.494 1.00 13.14 ?  33  THR   B C    1 
ATOM   4209 O  O    . THR   B 1 33  ? 45.872 -12.329 -9.650  1.00 14.21 ?  33  THR   B O    1 
ATOM   4210 C  CB   . THR   B 1 33  ? 44.132 -12.119 -12.424 1.00 14.00 ?  33  THR   B CB   1 
ATOM   4211 O  OG1  . THR   B 1 33  ? 44.184 -11.853 -13.828 1.00 14.10 ?  33  THR   B OG1  1 
ATOM   4212 C  CG2  . THR   B 1 33  ? 43.878 -10.822 -11.671 1.00 15.44 ?  33  THR   B CG2  1 
ATOM   4213 H  H    . THR   B 1 33  ? 45.129 -14.154 -13.345 1.00 16.11 ?  33  THR   B H    1 
ATOM   4214 H  HA   . THR   B 1 33  ? 46.148 -12.103 -12.107 1.00 16.27 ?  33  THR   B HA   1 
ATOM   4215 H  HB   . THR   B 1 33  ? 43.394 -12.731 -12.237 1.00 16.84 ?  33  THR   B HB   1 
ATOM   4216 H  HG1  . THR   B 1 33  ? 43.457 -11.496 -14.082 1.00 16.96 ?  33  THR   B HG1  1 
ATOM   4217 H  HG21 . THR   B 1 33  ? 43.126 -10.355 -12.062 1.00 18.57 ?  33  THR   B HG21 1 
ATOM   4218 H  HG22 . THR   B 1 33  ? 43.684 -11.012 -10.739 1.00 18.57 ?  33  THR   B HG22 1 
ATOM   4219 H  HG23 . THR   B 1 33  ? 44.664 -10.258 -11.722 1.00 18.57 ?  33  THR   B HG23 1 
ATOM   4220 N  N    . VAL   B 1 34  ? 44.862 -14.282 -10.156 1.00 12.31 ?  34  VAL   B N    1 
ATOM   4221 C  CA   . VAL   B 1 34  ? 44.669 -14.677 -8.765  1.00 11.85 ?  34  VAL   B CA   1 
ATOM   4222 C  C    . VAL   B 1 34  ? 45.094 -16.126 -8.600  1.00 11.05 ?  34  VAL   B C    1 
ATOM   4223 O  O    . VAL   B 1 34  ? 44.573 -17.012 -9.288  1.00 11.87 ?  34  VAL   B O    1 
ATOM   4224 C  CB   . VAL   B 1 34  ? 43.198 -14.535 -8.323  1.00 13.08 ?  34  VAL   B CB   1 
ATOM   4225 C  CG1  . VAL   B 1 34  ? 43.032 -14.981 -6.879  1.00 13.69 ?  34  VAL   B CG1  1 
ATOM   4226 C  CG2  . VAL   B 1 34  ? 42.694 -13.112 -8.516  1.00 14.17 ?  34  VAL   B CG2  1 
ATOM   4227 H  H    . VAL   B 1 34  ? 44.609 -14.884 -10.722 1.00 14.81 ?  34  VAL   B H    1 
ATOM   4228 H  HA   . VAL   B 1 34  ? 45.214 -14.122 -8.186  1.00 14.26 ?  34  VAL   B HA   1 
ATOM   4229 H  HB   . VAL   B 1 34  ? 42.649 -15.115 -8.873  1.00 15.73 ?  34  VAL   B HB   1 
ATOM   4230 H  HG11 . VAL   B 1 34  ? 42.176 -14.662 -6.545  1.00 16.47 ?  34  VAL   B HG11 1 
ATOM   4231 H  HG12 . VAL   B 1 34  ? 43.057 -15.950 -6.838  1.00 16.47 ?  34  VAL   B HG12 1 
ATOM   4232 H  HG13 . VAL   B 1 34  ? 43.750 -14.606 -6.346  1.00 16.47 ?  34  VAL   B HG13 1 
ATOM   4233 H  HG21 . VAL   B 1 34  ? 41.775 -13.055 -8.208  1.00 17.04 ?  34  VAL   B HG21 1 
ATOM   4234 H  HG22 . VAL   B 1 34  ? 43.252 -12.505 -8.007  1.00 17.04 ?  34  VAL   B HG22 1 
ATOM   4235 H  HG23 . VAL   B 1 34  ? 42.736 -12.887 -9.461  1.00 17.04 ?  34  VAL   B HG23 1 
ATOM   4236 N  N    . VAL   B 1 35  ? 46.003 -16.376 -7.661  1.00 10.73 ?  35  VAL   B N    1 
ATOM   4237 C  CA   . VAL   B 1 35  ? 46.241 -17.714 -7.142  1.00 10.77 ?  35  VAL   B CA   1 
ATOM   4238 C  C    . VAL   B 1 35  ? 45.697 -17.768 -5.724  1.00 10.41 ?  35  VAL   B C    1 
ATOM   4239 O  O    . VAL   B 1 35  ? 45.920 -16.848 -4.930  1.00 10.72 ?  35  VAL   B O    1 
ATOM   4240 C  CB   . VAL   B 1 35  ? 47.725 -18.136 -7.220  1.00 11.32 ?  35  VAL   B CB   1 
ATOM   4241 C  CG1  . VAL   B 1 35  ? 48.616 -17.304 -6.296  1.00 12.07 ?  35  VAL   B CG1  1 
ATOM   4242 C  CG2  . VAL   B 1 35  ? 47.857 -19.635 -6.909  1.00 12.16 ?  35  VAL   B CG2  1 
ATOM   4243 H  H    . VAL   B 1 35  ? 46.511 -15.774 -7.305  1.00 12.92 ?  35  VAL   B H    1 
ATOM   4244 H  HA   . VAL   B 1 35  ? 45.729 -18.346 -7.667  1.00 12.96 ?  35  VAL   B HA   1 
ATOM   4245 H  HB   . VAL   B 1 35  ? 48.034 -17.998 -8.131  1.00 13.63 ?  35  VAL   B HB   1 
ATOM   4246 H  HG11 . VAL   B 1 35  ? 49.541 -17.520 -6.481  1.00 14.52 ?  35  VAL   B HG11 1 
ATOM   4247 H  HG12 . VAL   B 1 35  ? 48.447 -16.368 -6.459  1.00 14.52 ?  35  VAL   B HG12 1 
ATOM   4248 H  HG13 . VAL   B 1 35  ? 48.401 -17.529 -5.375  1.00 14.52 ?  35  VAL   B HG13 1 
ATOM   4249 H  HG21 . VAL   B 1 35  ? 48.778 -19.907 -7.016  1.00 14.63 ?  35  VAL   B HG21 1 
ATOM   4250 H  HG22 . VAL   B 1 35  ? 47.566 -19.799 -5.994  1.00 14.63 ?  35  VAL   B HG22 1 
ATOM   4251 H  HG23 . VAL   B 1 35  ? 47.290 -20.141 -7.521  1.00 14.63 ?  35  VAL   B HG23 1 
ATOM   4252 N  N    . VAL   B 1 36  ? 44.980 -18.847 -5.409  1.00 10.54 ?  36  VAL   B N    1 
ATOM   4253 C  CA   . VAL   B 1 36  ? 44.438 -19.060 -4.077  1.00 10.22 ?  36  VAL   B CA   1 
ATOM   4254 C  C    . VAL   B 1 36  ? 45.446 -19.823 -3.226  1.00 9.97  ?  36  VAL   B C    1 
ATOM   4255 O  O    . VAL   B 1 36  ? 45.997 -20.845 -3.656  1.00 11.02 ?  36  VAL   B O    1 
ATOM   4256 C  CB   . VAL   B 1 36  ? 43.104 -19.818 -4.156  1.00 10.58 ?  36  VAL   B CB   1 
ATOM   4257 C  CG1  . VAL   B 1 36  ? 42.599 -20.174 -2.765  1.00 11.26 ?  36  VAL   B CG1  1 
ATOM   4258 C  CG2  . VAL   B 1 36  ? 42.078 -18.984 -4.905  1.00 11.03 ?  36  VAL   B CG2  1 
ATOM   4259 H  H    . VAL   B 1 36  ? 44.802 -19.480 -5.960  1.00 12.68 ?  36  VAL   B H    1 
ATOM   4260 H  HA   . VAL   B 1 36  ? 44.274 -18.201 -3.656  1.00 12.30 ?  36  VAL   B HA   1 
ATOM   4261 H  HB   . VAL   B 1 36  ? 43.239 -20.642 -4.650  1.00 12.73 ?  36  VAL   B HB   1 
ATOM   4262 H  HG11 . VAL   B 1 36  ? 41.660 -20.409 -2.823  1.00 13.55 ?  36  VAL   B HG11 1 
ATOM   4263 H  HG12 . VAL   B 1 36  ? 43.107 -20.924 -2.423  1.00 13.55 ?  36  VAL   B HG12 1 
ATOM   4264 H  HG13 . VAL   B 1 36  ? 42.709 -19.403 -2.184  1.00 13.55 ?  36  VAL   B HG13 1 
ATOM   4265 H  HG21 . VAL   B 1 36  ? 41.234 -19.459 -4.925  1.00 13.27 ?  36  VAL   B HG21 1 
ATOM   4266 H  HG22 . VAL   B 1 36  ? 41.968 -18.133 -4.451  1.00 13.27 ?  36  VAL   B HG22 1 
ATOM   4267 H  HG23 . VAL   B 1 36  ? 42.392 -18.831 -5.813  1.00 13.27 ?  36  VAL   B HG23 1 
ATOM   4268 N  N    . ASN   B 1 37  ? 45.665 -19.334 -2.007  1.00 10.10 ?  37  ASN   B N    1 
ATOM   4269 C  CA   . ASN   B 1 37  ? 46.425 -20.056 -1.003  1.00 10.56 ?  37  ASN   B CA   1 
ATOM   4270 C  C    . ASN   B 1 37  ? 45.484 -20.732 -0.013  1.00 10.38 ?  37  ASN   B C    1 
ATOM   4271 O  O    . ASN   B 1 37  ? 44.474 -20.158 0.406   1.00 10.91 ?  37  ASN   B O    1 
ATOM   4272 C  CB   . ASN   B 1 37  ? 47.354 -19.111 -0.240  1.00 10.50 ?  37  ASN   B CB   1 
ATOM   4273 C  CG   . ASN   B 1 37  ? 48.211 -19.827 0.768   1.00 10.58 ?  37  ASN   B CG   1 
ATOM   4274 O  OD1  . ASN   B 1 37  ? 48.558 -20.995 0.583   1.00 11.49 ?  37  ASN   B OD1  1 
ATOM   4275 N  ND2  . ASN   B 1 37  ? 48.561 -19.138 1.840   1.00 11.08 ?  37  ASN   B ND2  1 
ATOM   4276 H  H    . ASN   B 1 37  ? 45.377 -18.571 -1.731  1.00 12.16 ?  37  ASN   B H    1 
ATOM   4277 H  HA   . ASN   B 1 37  ? 46.963 -20.746 -1.427  1.00 12.71 ?  37  ASN   B HA   1 
ATOM   4278 H  HB2  . ASN   B 1 37  ? 47.941 -18.677 -0.874  1.00 12.64 ?  37  ASN   B HB2  1 
ATOM   4279 H  HB3  . ASN   B 1 37  ? 46.820 -18.457 0.231   1.00 12.64 ?  37  ASN   B HB3  1 
ATOM   4280 H  HD21 . ASN   B 1 37  ? 49.045 -19.508 2.450   1.00 13.33 ?  37  ASN   B HD21 1 
ATOM   4281 H  HD22 . ASN   B 1 37  ? 48.291 -18.335 1.942   1.00 13.33 ?  37  ASN   B HD22 1 
ATOM   4282 N  N    . ALA   B 1 38  ? 45.835 -21.963 0.361   1.00 10.40 ?  38  ALA   B N    1 
ATOM   4283 C  CA   . ALA   B 1 38  ? 45.185 -22.707 1.441   1.00 11.00 ?  38  ALA   B CA   1 
ATOM   4284 C  C    . ALA   B 1 38  ? 45.774 -22.221 2.762   1.00 10.75 ?  38  ALA   B C    1 
ATOM   4285 O  O    . ALA   B 1 38  ? 46.676 -22.832 3.349   1.00 11.79 ?  38  ALA   B O    1 
ATOM   4286 C  CB   . ALA   B 1 38  ? 45.397 -24.203 1.251   1.00 12.17 ?  38  ALA   B CB   1 
ATOM   4287 H  H    . ALA   B 1 38  ? 46.483 -22.401 0.005   1.00 12.52 ?  38  ALA   B H    1 
ATOM   4288 H  HA   . ALA   B 1 38  ? 44.231 -22.521 1.442   1.00 13.24 ?  38  ALA   B HA   1 
ATOM   4289 H  HB1  . ALA   B 1 38  ? 44.950 -24.680 1.978   1.00 14.65 ?  38  ALA   B HB1  1 
ATOM   4290 H  HB2  . ALA   B 1 38  ? 45.005 -24.471 0.404   1.00 14.65 ?  38  ALA   B HB2  1 
ATOM   4291 H  HB3  . ALA   B 1 38  ? 46.340 -24.397 1.263   1.00 14.65 ?  38  ALA   B HB3  1 
ATOM   4292 N  N    . ALA   B 1 39  ? 45.253 -21.083 3.221   1.00 10.58 ?  39  ALA   B N    1 
ATOM   4293 C  CA   . ALA   B 1 39  ? 45.796 -20.346 4.351   1.00 11.16 ?  39  ALA   B CA   1 
ATOM   4294 C  C    . ALA   B 1 39  ? 45.183 -20.799 5.674   1.00 11.22 ?  39  ALA   B C    1 
ATOM   4295 O  O    . ALA   B 1 39  ? 44.159 -21.477 5.719   1.00 12.09 ?  39  ALA   B O    1 
ATOM   4296 C  CB   . ALA   B 1 39  ? 45.543 -18.847 4.164   1.00 11.82 ?  39  ALA   B CB   1 
ATOM   4297 H  H    . ALA   B 1 39  ? 44.557 -20.712 2.883   1.00 12.73 ?  39  ALA   B H    1 
ATOM   4298 H  HA   . ALA   B 1 39  ? 46.752 -20.490 4.400   1.00 13.43 ?  39  ALA   B HA   1 
ATOM   4299 H  HB1  . ALA   B 1 39  ? 45.912 -18.368 4.923   1.00 14.22 ?  39  ALA   B HB1  1 
ATOM   4300 H  HB2  . ALA   B 1 39  ? 45.980 -18.556 3.347   1.00 14.22 ?  39  ALA   B HB2  1 
ATOM   4301 H  HB3  . ALA   B 1 39  ? 44.589 -18.691 4.104   1.00 14.22 ?  39  ALA   B HB3  1 
ATOM   4302 N  N    . ASN   B 1 40  ? 45.820 -20.372 6.763   1.00 12.11 ?  40  ASN   B N    1 
ATOM   4303 C  CA   . ASN   B 1 40  ? 45.260 -20.430 8.105   1.00 12.57 ?  40  ASN   B CA   1 
ATOM   4304 C  C    . ASN   B 1 40  ? 45.080 -19.004 8.632   1.00 12.17 ?  40  ASN   B C    1 
ATOM   4305 O  O    . ASN   B 1 40  ? 45.494 -18.021 8.005   1.00 12.16 ?  40  ASN   B O    1 
ATOM   4306 C  CB   . ASN   B 1 40  ? 46.116 -21.300 9.044   1.00 13.62 ?  40  ASN   B CB   1 
ATOM   4307 C  CG   . ASN   B 1 40  ? 47.574 -20.908 9.046   1.00 14.51 ?  40  ASN   B CG   1 
ATOM   4308 O  OD1  . ASN   B 1 40  ? 47.900 -19.729 9.087   1.00 15.76 ?  40  ASN   B OD1  1 
ATOM   4309 N  ND2  . ASN   B 1 40  ? 48.460 -21.892 9.012   1.00 14.56 ?  40  ASN   B ND2  1 
ATOM   4310 H  H    . ASN   B 1 40  ? 46.613 -20.039 6.742   1.00 14.57 ?  40  ASN   B H    1 
ATOM   4311 H  HA   . ASN   B 1 40  ? 44.381 -20.830 8.061   1.00 15.12 ?  40  ASN   B HA   1 
ATOM   4312 H  HB2  . ASN   B 1 40  ? 45.780 -21.208 9.951   1.00 16.38 ?  40  ASN   B HB2  1 
ATOM   4313 H  HB3  . ASN   B 1 40  ? 46.055 -22.222 8.758   1.00 16.38 ?  40  ASN   B HB3  1 
ATOM   4314 H  HD21 . ASN   B 1 40  ? 49.304 -21.719 9.012   1.00 17.51 ?  40  ASN   B HD21 1 
ATOM   4315 H  HD22 . ASN   B 1 40  ? 48.193 -22.710 8.982   1.00 17.51 ?  40  ASN   B HD22 1 
ATOM   4316 N  N    . VAL   B 1 41  ? 44.424 -18.884 9.789   1.00 12.47 ?  41  VAL   B N    1 
ATOM   4317 C  CA   . VAL   B 1 41  ? 43.969 -17.564 10.237  1.00 13.20 ?  41  VAL   B CA   1 
ATOM   4318 C  C    . VAL   B 1 41  ? 45.123 -16.613 10.536  1.00 13.13 ?  41  VAL   B C    1 
ATOM   4319 O  O    . VAL   B 1 41  ? 44.946 -15.391 10.452  1.00 13.45 ?  41  VAL   B O    1 
ATOM   4320 C  CB   . VAL   B 1 41  ? 42.991 -17.647 11.425  1.00 14.73 ?  41  VAL   B CB   1 
ATOM   4321 C  CG1  . VAL   B 1 41  ? 41.703 -18.343 11.018  1.00 15.15 ?  41  VAL   B CG1  1 
ATOM   4322 C  CG2  . VAL   B 1 41  ? 43.639 -18.328 12.617  1.00 15.76 ?  41  VAL   B CG2  1 
ATOM   4323 H  H    . VAL   B 1 41  ? 44.240 -19.527 10.320  1.00 15.00 ?  41  VAL   B H    1 
ATOM   4324 H  HA   . VAL   B 1 41  ? 43.476 -17.163 9.508   1.00 15.87 ?  41  VAL   B HA   1 
ATOM   4325 H  HB   . VAL   B 1 41  ? 42.760 -16.746 11.700  1.00 17.71 ?  41  VAL   B HB   1 
ATOM   4326 H  HG11 . VAL   B 1 41  ? 41.099 -18.356 11.777  1.00 18.22 ?  41  VAL   B HG11 1 
ATOM   4327 H  HG12 . VAL   B 1 41  ? 41.302 -17.856 10.283  1.00 18.22 ?  41  VAL   B HG12 1 
ATOM   4328 H  HG13 . VAL   B 1 41  ? 41.909 -19.250 10.743  1.00 18.22 ?  41  VAL   B HG13 1 
ATOM   4329 H  HG21 . VAL   B 1 41  ? 43.000 -18.367 13.344  1.00 18.95 ?  41  VAL   B HG21 1 
ATOM   4330 H  HG22 . VAL   B 1 41  ? 43.903 -19.228 12.362  1.00 18.95 ?  41  VAL   B HG22 1 
ATOM   4331 H  HG23 . VAL   B 1 41  ? 44.420 -17.821 12.887  1.00 18.95 ?  41  VAL   B HG23 1 
ATOM   4332 N  N    . TYR   B 1 42  ? 46.294 -17.127 10.914  1.00 13.32 ?  42  TYR   B N    1 
ATOM   4333 C  CA   . TYR   B 1 42  ? 47.445 -16.275 11.184  1.00 13.88 ?  42  TYR   B CA   1 
ATOM   4334 C  C    . TYR   B 1 42  ? 48.412 -16.204 10.007  1.00 13.02 ?  42  TYR   B C    1 
ATOM   4335 O  O    . TYR   B 1 42  ? 49.501 -15.635 10.147  1.00 14.02 ?  42  TYR   B O    1 
ATOM   4336 C  CB   . TYR   B 1 42  ? 48.144 -16.675 12.491  1.00 15.58 ?  42  TYR   B CB   1 
ATOM   4337 C  CG   . TYR   B 1 42  ? 47.541 -15.993 13.712  1.00 16.20 ?  42  TYR   B CG   1 
ATOM   4338 C  CD1  . TYR   B 1 42  ? 47.767 -14.642 13.951  1.00 15.69 ?  42  TYR   B CD1  1 
ATOM   4339 C  CD2  . TYR   B 1 42  ? 46.749 -16.690 14.613  1.00 17.66 ?  42  TYR   B CD2  1 
ATOM   4340 C  CE1  . TYR   B 1 42  ? 47.225 -14.006 15.048  1.00 16.39 ?  42  TYR   B CE1  1 
ATOM   4341 C  CE2  . TYR   B 1 42  ? 46.201 -16.058 15.718  1.00 17.93 ?  42  TYR   B CE2  1 
ATOM   4342 C  CZ   . TYR   B 1 42  ? 46.442 -14.713 15.931  1.00 18.00 ?  42  TYR   B CZ   1 
ATOM   4343 O  OH   . TYR   B 1 42  ? 45.908 -14.068 17.027  1.00 20.96 ?  42  TYR   B OH   1 
ATOM   4344 H  H    . TYR   B 1 42  ? 46.444 -17.972 11.008  1.00 16.02 ?  42  TYR   B H    1 
ATOM   4345 H  HA   . TYR   B 1 42  ? 47.117 -15.377 11.316  1.00 16.70 ?  42  TYR   B HA   1 
ATOM   4346 H  HB2  . TYR   B 1 42  ? 48.065 -17.635 12.610  1.00 18.74 ?  42  TYR   B HB2  1 
ATOM   4347 H  HB3  . TYR   B 1 42  ? 49.080 -16.425 12.435  1.00 18.74 ?  42  TYR   B HB3  1 
ATOM   4348 H  HD1  . TYR   B 1 42  ? 48.297 -14.157 13.352  1.00 18.87 ?  42  TYR   B HD1  1 
ATOM   4349 H  HD2  . TYR   B 1 42  ? 46.583 -17.596 14.467  1.00 21.23 ?  42  TYR   B HD2  1 
ATOM   4350 H  HE1  . TYR   B 1 42  ? 47.391 -13.101 15.186  1.00 19.70 ?  42  TYR   B HE1  1 
ATOM   4351 H  HE2  . TYR   B 1 42  ? 45.671 -16.541 16.310  1.00 21.56 ?  42  TYR   B HE2  1 
ATOM   4352 H  HH   . TYR   B 1 42  ? 46.139 -13.265 17.020  1.00 25.19 ?  42  TYR   B HH   1 
ATOM   4353 N  N    . LEU   B 1 43  ? 48.013 -16.710 8.842   1.00 12.11 ?  43  LEU   B N    1 
ATOM   4354 C  CA   . LEU   B 1 43  ? 48.828 -16.643 7.632   1.00 11.93 ?  43  LEU   B CA   1 
ATOM   4355 C  C    . LEU   B 1 43  ? 50.241 -17.146 7.894   1.00 12.47 ?  43  LEU   B C    1 
ATOM   4356 O  O    . LEU   B 1 43  ? 51.222 -16.549 7.452   1.00 13.20 ?  43  LEU   B O    1 
ATOM   4357 C  CB   . LEU   B 1 43  ? 48.846 -15.239 7.027   1.00 12.11 ?  43  LEU   B CB   1 
ATOM   4358 C  CG   . LEU   B 1 43  ? 47.485 -14.625 6.670   1.00 12.55 ?  43  LEU   B CG   1 
ATOM   4359 C  CD1  . LEU   B 1 43  ? 47.692 -13.221 6.109   1.00 13.99 ?  43  LEU   B CD1  1 
ATOM   4360 C  CD2  . LEU   B 1 43  ? 46.726 -15.512 5.691   1.00 12.87 ?  43  LEU   B CD2  1 
ATOM   4361 H  H    . LEU   B 1 43  ? 47.266 -17.119 8.725   1.00 14.56 ?  43  LEU   B H    1 
ATOM   4362 H  HA   . LEU   B 1 43  ? 48.433 -17.234 6.968   1.00 14.36 ?  43  LEU   B HA   1 
ATOM   4363 H  HB2  . LEU   B 1 43  ? 49.276 -14.642 7.660   1.00 14.57 ?  43  LEU   B HB2  1 
ATOM   4364 H  HB3  . LEU   B 1 43  ? 49.370 -15.269 6.210   1.00 14.57 ?  43  LEU   B HB3  1 
ATOM   4365 H  HG   . LEU   B 1 43  ? 46.957 -14.547 7.476   1.00 15.10 ?  43  LEU   B HG   1 
ATOM   4366 H  HD11 . LEU   B 1 43  ? 46.829 -12.836 5.887   1.00 16.83 ?  43  LEU   B HD11 1 
ATOM   4367 H  HD12 . LEU   B 1 43  ? 48.131 -12.671 6.782   1.00 16.83 ?  43  LEU   B HD12 1 
ATOM   4368 H  HD13 . LEU   B 1 43  ? 48.246 -13.270 5.315   1.00 16.83 ?  43  LEU   B HD13 1 
ATOM   4369 H  HD21 . LEU   B 1 43  ? 45.923 -15.050 5.401   1.00 15.48 ?  43  LEU   B HD21 1 
ATOM   4370 H  HD22 . LEU   B 1 43  ? 47.291 -15.702 4.926   1.00 15.48 ?  43  LEU   B HD22 1 
ATOM   4371 H  HD23 . LEU   B 1 43  ? 46.485 -16.341 6.136   1.00 15.48 ?  43  LEU   B HD23 1 
ATOM   4372 N  N    . LYS   B 1 44  ? 50.343 -18.271 8.602   1.00 12.39 ?  44  LYS   B N    1 
ATOM   4373 C  CA   . LYS   B 1 44  ? 51.613 -18.945 8.838   1.00 13.07 ?  44  LYS   B CA   1 
ATOM   4374 C  C    . LYS   B 1 44  ? 51.727 -20.064 7.810   1.00 12.47 ?  44  LYS   B C    1 
ATOM   4375 O  O    . LYS   B 1 44  ? 51.025 -21.077 7.895   1.00 13.98 ?  44  LYS   B O    1 
ATOM   4376 C  CB   . LYS   B 1 44  ? 51.676 -19.463 10.274  1.00 14.97 ?  44  LYS   B CB   1 
ATOM   4377 C  CG   . LYS   B 1 44  ? 51.864 -18.359 11.303  1.00 17.36 ?  44  LYS   B CG   1 
ATOM   4378 C  CD   . LYS   B 1 44  ? 53.065 -17.492 10.924  1.00 20.08 ?  44  LYS   B CD   1 
ATOM   4379 C  CE   . LYS   B 1 44  ? 53.557 -16.634 12.061  1.00 22.49 ?  44  LYS   B CE   1 
ATOM   4380 N  NZ   . LYS   B 1 44  ? 54.703 -15.780 11.661  1.00 23.68 ?  44  LYS   B NZ   1 
ATOM   4381 H  H    . LYS   B 1 44  ? 49.673 -18.665 8.972   1.00 14.91 ?  44  LYS   B H    1 
ATOM   4382 H  HA   . LYS   B 1 44  ? 52.343 -18.328 8.677   1.00 15.72 ?  44  LYS   B HA   1 
ATOM   4383 H  HB2  . LYS   B 1 44  ? 50.842 -19.921 10.479  1.00 18.00 ?  44  LYS   B HB2  1 
ATOM   4384 H  HB3  . LYS   B 1 44  ? 52.418 -20.079 10.355  1.00 18.00 ?  44  LYS   B HB3  1 
ATOM   4385 H  HG2  . LYS   B 1 44  ? 51.073 -17.804 11.332  1.00 20.87 ?  44  LYS   B HG2  1 
ATOM   4386 H  HG3  . LYS   B 1 44  ? 52.035 -18.759 12.174  1.00 20.87 ?  44  LYS   B HG3  1 
ATOM   4387 H  HD2  . LYS   B 1 44  ? 53.789 -18.075 10.630  1.00 24.14 ?  44  LYS   B HD2  1 
ATOM   4388 H  HD3  . LYS   B 1 44  ? 52.803 -16.903 10.198  1.00 24.14 ?  44  LYS   B HD3  1 
ATOM   4389 H  HE2  . LYS   B 1 44  ? 52.842 -16.047 12.328  1.00 27.03 ?  44  LYS   B HE2  1 
ATOM   4390 H  HE3  . LYS   B 1 44  ? 53.832 -17.204 12.798  1.00 27.03 ?  44  LYS   B HE3  1 
ATOM   4391 H  HZ1  . LYS   B 1 44  ? 54.965 -15.283 12.350  1.00 28.45 ?  44  LYS   B HZ1  1 
ATOM   4392 H  HZ2  . LYS   B 1 44  ? 55.383 -16.283 11.389  1.00 28.45 ?  44  LYS   B HZ2  1 
ATOM   4393 H  HZ3  . LYS   B 1 44  ? 54.459 -15.240 10.993  1.00 28.45 ?  44  LYS   B HZ3  1 
ATOM   4394 N  N    . HIS   B 1 45  ? 52.577 -19.848 6.809   1.00 12.09 ?  45  HIS   B N    1 
ATOM   4395 C  CA   . HIS   B 1 45  ? 52.597 -20.677 5.605   1.00 12.57 ?  45  HIS   B CA   1 
ATOM   4396 C  C    . HIS   B 1 45  ? 53.611 -21.805 5.766   1.00 14.47 ?  45  HIS   B C    1 
ATOM   4397 O  O    . HIS   B 1 45  ? 54.670 -21.824 5.146   1.00 16.75 ?  45  HIS   B O    1 
ATOM   4398 C  CB   . HIS   B 1 45  ? 52.913 -19.824 4.389   1.00 12.32 ?  45  HIS   B CB   1 
ATOM   4399 C  CG   . HIS   B 1 45  ? 52.041 -18.622 4.274   1.00 12.29 ?  45  HIS   B CG   1 
ATOM   4400 N  ND1  . HIS   B 1 45  ? 50.664 -18.702 4.228   1.00 12.70 ?  45  HIS   B ND1  1 
ATOM   4401 C  CD2  . HIS   B 1 45  ? 52.355 -17.307 4.217   1.00 12.91 ?  45  HIS   B CD2  1 
ATOM   4402 C  CE1  . HIS   B 1 45  ? 50.175 -17.480 4.124   1.00 12.41 ?  45  HIS   B CE1  1 
ATOM   4403 N  NE2  . HIS   B 1 45  ? 51.176 -16.617 4.122   1.00 12.74 ?  45  HIS   B NE2  1 
ATOM   4404 H  H    . HIS   B 1 45  ? 53.156 -19.209 6.801   1.00 14.54 ?  45  HIS   B H    1 
ATOM   4405 H  HA   . HIS   B 1 45  ? 51.718 -21.070 5.478   1.00 15.12 ?  45  HIS   B HA   1 
ATOM   4406 H  HB2  . HIS   B 1 45  ? 53.831 -19.526 4.443   1.00 14.83 ?  45  HIS   B HB2  1 
ATOM   4407 H  HB3  . HIS   B 1 45  ? 52.788 -20.365 3.588   1.00 14.83 ?  45  HIS   B HB3  1 
ATOM   4408 H  HD2  . HIS   B 1 45  ? 53.209 -16.942 4.236   1.00 15.53 ?  45  HIS   B HD2  1 
ATOM   4409 H  HE1  . HIS   B 1 45  ? 49.272 -17.263 4.060   1.00 14.93 ?  45  HIS   B HE1  1 
ATOM   4410 H  HE2  . HIS   B 1 45  ? 51.097 -15.763 4.066   1.00 15.33 ?  45  HIS   B HE2  1 
ATOM   4411 N  N    . GLY   B 1 46  ? 53.248 -22.768 6.605   1.00 15.48 ?  46  GLY   B N    1 
ATOM   4412 C  CA   . GLY   B 1 46  ? 54.167 -23.829 6.961   1.00 17.20 ?  46  GLY   B CA   1 
ATOM   4413 C  C    . GLY   B 1 46  ? 54.211 -25.017 6.021   1.00 18.95 ?  46  GLY   B C    1 
ATOM   4414 O  O    . GLY   B 1 46  ? 55.283 -25.414 5.557   1.00 22.36 ?  46  GLY   B O    1 
ATOM   4415 H  H    . GLY   B 1 46  ? 52.482 -22.810 7.003   1.00 18.62 ?  46  GLY   B H    1 
ATOM   4416 H  HA2  . GLY   B 1 46  ? 55.061 -23.460 7.018   1.00 20.68 ?  46  GLY   B HA2  1 
ATOM   4417 H  HA3  . GLY   B 1 46  ? 53.928 -24.168 7.838   1.00 20.68 ?  46  GLY   B HA3  1 
ATOM   4418 N  N    . GLY   B 1 47  ? 53.057 -25.609 5.731   1.00 18.01 ?  47  GLY   B N    1 
ATOM   4419 C  CA   . GLY   B 1 47  ? 53.004 -26.899 5.071   1.00 16.12 ?  47  GLY   B CA   1 
ATOM   4420 C  C    . GLY   B 1 47  ? 52.096 -26.882 3.856   1.00 14.25 ?  47  GLY   B C    1 
ATOM   4421 O  O    . GLY   B 1 47  ? 51.453 -25.878 3.558   1.00 14.09 ?  47  GLY   B O    1 
ATOM   4422 H  H    . GLY   B 1 47  ? 52.283 -25.285 5.927   1.00 21.65 ?  47  GLY   B H    1 
ATOM   4423 H  HA2  . GLY   B 1 47  ? 53.893 -27.157 4.784   1.00 19.39 ?  47  GLY   B HA2  1 
ATOM   4424 H  HA3  . GLY   B 1 47  ? 52.675 -27.567 5.694   1.00 19.39 ?  47  GLY   B HA3  1 
ATOM   4425 N  N    . GLY   B 1 48  ? 52.052 -28.023 3.172   1.00 13.24 ?  48  GLY   B N    1 
ATOM   4426 C  CA   . GLY   B 1 48  ? 51.126 -28.170 2.062   1.00 12.92 ?  48  GLY   B CA   1 
ATOM   4427 C  C    . GLY   B 1 48  ? 51.265 -27.059 1.044   1.00 12.51 ?  48  GLY   B C    1 
ATOM   4428 O  O    . GLY   B 1 48  ? 52.370 -26.590 0.734   1.00 12.83 ?  48  GLY   B O    1 
ATOM   4429 H  H    . GLY   B 1 48  ? 52.544 -28.706 3.324   1.00 15.93 ?  48  GLY   B H    1 
ATOM   4430 H  HA2  . GLY   B 1 48  ? 51.286 -29.017 1.619   1.00 15.54 ?  48  GLY   B HA2  1 
ATOM   4431 H  HA3  . GLY   B 1 48  ? 50.216 -28.164 2.397   1.00 15.54 ?  48  GLY   B HA3  1 
ATOM   4432 N  N    . VAL   B 1 49  ? 50.116 -26.623 0.520   1.00 12.45 ?  49  VAL   B N    1 
ATOM   4433 C  CA   . VAL   B 1 49  ? 50.091 -25.592 -0.515  1.00 12.38 ?  49  VAL   B CA   1 
ATOM   4434 C  C    . VAL   B 1 49  ? 50.751 -24.306 -0.024  1.00 11.59 ?  49  VAL   B C    1 
ATOM   4435 O  O    . VAL   B 1 49  ? 51.542 -23.685 -0.745  1.00 12.35 ?  49  VAL   B O    1 
ATOM   4436 C  CB   . VAL   B 1 49  ? 48.649 -25.345 -0.996  1.00 13.77 ?  49  VAL   B CB   1 
ATOM   4437 C  CG1  . VAL   B 1 49  ? 48.580 -24.093 -1.855  1.00 13.95 ?  49  VAL   B CG1  1 
ATOM   4438 C  CG2  . VAL   B 1 49  ? 48.128 -26.554 -1.766  1.00 15.45 ?  49  VAL   B CG2  1 
ATOM   4439 H  H    . VAL   B 1 49  ? 49.332 -26.911 0.746   1.00 14.97 ?  49  VAL   B H    1 
ATOM   4440 H  HA   . VAL   B 1 49  ? 50.599 -25.907 -1.278  1.00 14.89 ?  49  VAL   B HA   1 
ATOM   4441 H  HB   . VAL   B 1 49  ? 48.075 -25.210 -0.228  1.00 16.56 ?  49  VAL   B HB   1 
ATOM   4442 H  HG11 . VAL   B 1 49  ? 47.756 -24.107 -2.368  1.00 16.78 ?  49  VAL   B HG11 1 
ATOM   4443 H  HG12 . VAL   B 1 49  ? 48.596 -23.310 -1.282  1.00 16.78 ?  49  VAL   B HG12 1 
ATOM   4444 H  HG13 . VAL   B 1 49  ? 49.341 -24.080 -2.457  1.00 16.78 ?  49  VAL   B HG13 1 
ATOM   4445 H  HG21 . VAL   B 1 49  ? 47.220 -26.379 -2.058  1.00 18.57 ?  49  VAL   B HG21 1 
ATOM   4446 H  HG22 . VAL   B 1 49  ? 48.699 -26.707 -2.538  1.00 18.57 ?  49  VAL   B HG22 1 
ATOM   4447 H  HG23 . VAL   B 1 49  ? 48.146 -27.330 -1.185  1.00 18.57 ?  49  VAL   B HG23 1 
ATOM   4448 N  N    . ALA   B 1 50  ? 50.409 -23.866 1.191   1.00 11.49 ?  50  ALA   B N    1 
ATOM   4449 C  CA   . ALA   B 1 50  ? 50.925 -22.587 1.669   1.00 11.28 ?  50  ALA   B CA   1 
ATOM   4450 C  C    . ALA   B 1 50  ? 52.446 -22.615 1.776   1.00 11.81 ?  50  ALA   B C    1 
ATOM   4451 O  O    . ALA   B 1 50  ? 53.126 -21.646 1.413   1.00 11.67 ?  50  ALA   B O    1 
ATOM   4452 C  CB   . ALA   B 1 50  ? 50.301 -22.228 3.016   1.00 11.66 ?  50  ALA   B CB   1 
ATOM   4453 H  H    . ALA   B 1 50  ? 49.893 -24.280 1.743   1.00 13.82 ?  50  ALA   B H    1 
ATOM   4454 H  HA   . ALA   B 1 50  ? 50.692 -21.895 1.038   1.00 13.58 ?  50  ALA   B HA   1 
ATOM   4455 H  HB1  . ALA   B 1 50  ? 50.659 -21.375 3.315   1.00 14.03 ?  50  ALA   B HB1  1 
ATOM   4456 H  HB2  . ALA   B 1 50  ? 49.339 -22.163 2.912   1.00 14.03 ?  50  ALA   B HB2  1 
ATOM   4457 H  HB3  . ALA   B 1 50  ? 50.517 -22.919 3.663   1.00 14.03 ?  50  ALA   B HB3  1 
ATOM   4458 N  N    . GLY   B 1 51  ? 52.997 -23.709 2.294   1.00 12.17 ?  51  GLY   B N    1 
ATOM   4459 C  CA   . GLY   B 1 51  ? 54.443 -23.819 2.362   1.00 12.80 ?  51  GLY   B CA   1 
ATOM   4460 C  C    . GLY   B 1 51  ? 55.090 -23.760 0.993   1.00 12.61 ?  51  GLY   B C    1 
ATOM   4461 O  O    . GLY   B 1 51  ? 56.131 -23.122 0.813   1.00 13.57 ?  51  GLY   B O    1 
ATOM   4462 H  H    . GLY   B 1 51  ? 52.569 -24.389 2.604   1.00 14.64 ?  51  GLY   B H    1 
ATOM   4463 H  HA2  . GLY   B 1 51  ? 54.800 -23.093 2.902   1.00 15.40 ?  51  GLY   B HA2  1 
ATOM   4464 H  HA3  . GLY   B 1 51  ? 54.689 -24.659 2.782   1.00 15.40 ?  51  GLY   B HA3  1 
ATOM   4465 N  N    . ALA   B 1 52  ? 54.483 -24.419 0.007   1.00 12.39 ?  52  ALA   B N    1 
ATOM   4466 C  CA   . ALA   B 1 52  ? 55.050 -24.423 -1.336  1.00 12.60 ?  52  ALA   B CA   1 
ATOM   4467 C  C    . ALA   B 1 52  ? 54.965 -23.045 -1.986  1.00 12.40 ?  52  ALA   B C    1 
ATOM   4468 O  O    . ALA   B 1 52  ? 55.932 -22.592 -2.617  1.00 13.09 ?  52  ALA   B O    1 
ATOM   4469 C  CB   . ALA   B 1 52  ? 54.356 -25.474 -2.196  1.00 13.75 ?  52  ALA   B CB   1 
ATOM   4470 H  H    . ALA   B 1 52  ? 53.746 -24.856 0.090   1.00 14.91 ?  52  ALA   B H    1 
ATOM   4471 H  HA   . ALA   B 1 52  ? 55.986 -24.662 -1.272  1.00 15.16 ?  52  ALA   B HA   1 
ATOM   4472 H  HB1  . ALA   B 1 52  ? 54.751 -25.463 -3.082  1.00 16.54 ?  52  ALA   B HB1  1 
ATOM   4473 H  HB2  . ALA   B 1 52  ? 54.483 -26.346 -1.788  1.00 16.54 ?  52  ALA   B HB2  1 
ATOM   4474 H  HB3  . ALA   B 1 52  ? 53.412 -25.266 -2.249  1.00 16.54 ?  52  ALA   B HB3  1 
ATOM   4475 N  N    . LEU   B 1 53  ? 53.816 -22.371 -1.870  1.00 11.76 ?  53  LEU   B N    1 
ATOM   4476 C  CA   . LEU   B 1 53  ? 53.701 -21.031 -2.436  1.00 11.84 ?  53  LEU   B CA   1 
ATOM   4477 C  C    . LEU   B 1 53  ? 54.705 -20.092 -1.786  1.00 11.86 ?  53  LEU   B C    1 
ATOM   4478 O  O    . LEU   B 1 53  ? 55.407 -19.341 -2.471  1.00 12.64 ?  53  LEU   B O    1 
ATOM   4479 C  CB   . LEU   B 1 53  ? 52.279 -20.496 -2.256  1.00 12.57 ?  53  LEU   B CB   1 
ATOM   4480 C  CG   . LEU   B 1 53  ? 51.153 -21.220 -2.996  1.00 12.85 ?  53  LEU   B CG   1 
ATOM   4481 C  CD1  . LEU   B 1 53  ? 49.819 -20.587 -2.658  1.00 14.24 ?  53  LEU   B CD1  1 
ATOM   4482 C  CD2  . LEU   B 1 53  ? 51.380 -21.210 -4.499  1.00 14.69 ?  53  LEU   B CD2  1 
ATOM   4483 H  H    . LEU   B 1 53  ? 53.109 -22.664 -1.476  1.00 14.15 ?  53  LEU   B H    1 
ATOM   4484 H  HA   . LEU   B 1 53  ? 53.893 -21.073 -3.388  1.00 14.25 ?  53  LEU   B HA   1 
ATOM   4485 H  HB2  . LEU   B 1 53  ? 52.063 -20.530 -1.313  1.00 15.12 ?  53  LEU   B HB2  1 
ATOM   4486 H  HB3  . LEU   B 1 53  ? 52.264 -19.577 -2.557  1.00 15.12 ?  53  LEU   B HB3  1 
ATOM   4487 H  HG   . LEU   B 1 53  ? 51.121 -22.145 -2.701  1.00 15.46 ?  53  LEU   B HG   1 
ATOM   4488 H  HD11 . LEU   B 1 53  ? 49.114 -21.060 -3.131  1.00 17.13 ?  53  LEU   B HD11 1 
ATOM   4489 H  HD12 . LEU   B 1 53  ? 49.670 -20.651 -1.700  1.00 17.13 ?  53  LEU   B HD12 1 
ATOM   4490 H  HD13 . LEU   B 1 53  ? 49.831 -19.657 -2.929  1.00 17.13 ?  53  LEU   B HD13 1 
ATOM   4491 H  HD21 . LEU   B 1 53  ? 50.616 -21.614 -4.941  1.00 17.66 ?  53  LEU   B HD21 1 
ATOM   4492 H  HD22 . LEU   B 1 53  ? 51.486 -20.293 -4.797  1.00 17.66 ?  53  LEU   B HD22 1 
ATOM   4493 H  HD23 . LEU   B 1 53  ? 52.182 -21.717 -4.701  1.00 17.66 ?  53  LEU   B HD23 1 
ATOM   4494 N  N    . ASN   B 1 54  ? 54.798 -20.125 -0.460  1.00 11.46 ?  54  ASN   B N    1 
ATOM   4495 C  CA   . ASN   B 1 54  ? 55.715 -19.214 0.211   1.00 12.28 ?  54  ASN   B CA   1 
ATOM   4496 C  C    . ASN   B 1 54  ? 57.160 -19.490 -0.184  1.00 12.61 ?  54  ASN   B C    1 
ATOM   4497 O  O    . ASN   B 1 54  ? 57.937 -18.554 -0.409  1.00 13.06 ?  54  ASN   B O    1 
ATOM   4498 C  CB   . ASN   B 1 54  ? 55.549 -19.294 1.721   1.00 13.21 ?  54  ASN   B CB   1 
ATOM   4499 C  CG   . ASN   B 1 54  ? 56.531 -18.386 2.442   1.00 13.06 ?  54  ASN   B CG   1 
ATOM   4500 O  OD1  . ASN   B 1 54  ? 56.549 -17.171 2.210   1.00 13.38 ?  54  ASN   B OD1  1 
ATOM   4501 N  ND2  . ASN   B 1 54  ? 57.371 -18.967 3.295   1.00 14.66 ?  54  ASN   B ND2  1 
ATOM   4502 H  H    . ASN   B 1 54  ? 54.355 -20.650 0.058   1.00 13.78 ?  54  ASN   B H    1 
ATOM   4503 H  HA   . ASN   B 1 54  ? 55.500 -18.308 -0.062  1.00 14.77 ?  54  ASN   B HA   1 
ATOM   4504 H  HB2  . ASN   B 1 54  ? 54.647 -19.013 1.958   1.00 15.89 ?  54  ASN   B HB2  1 
ATOM   4505 H  HB3  . ASN   B 1 54  ? 55.703 -20.202 2.014   1.00 15.89 ?  54  ASN   B HB3  1 
ATOM   4506 H  HD21 . ASN   B 1 54  ? 57.947 -18.491 3.719   1.00 17.63 ?  54  ASN   B HD21 1 
ATOM   4507 H  HD22 . ASN   B 1 54  ? 57.336 -19.816 3.421   1.00 17.63 ?  54  ASN   B HD22 1 
ATOM   4508 N  N    . LYS   B 1 55  ? 57.542 -20.767 -0.258  1.00 13.32 ?  55  LYS   B N    1 
ATOM   4509 C  CA   . LYS   B 1 55  ? 58.896 -21.106 -0.679  1.00 14.08 ?  55  LYS   B CA   1 
ATOM   4510 C  C    . LYS   B 1 55  ? 59.192 -20.557 -2.069  1.00 13.87 ?  55  LYS   B C    1 
ATOM   4511 O  O    . LYS   B 1 55  ? 60.288 -20.044 -2.321  1.00 14.63 ?  55  LYS   B O    1 
ATOM   4512 C  CB   . LYS   B 1 55  ? 59.087 -22.621 -0.638  1.00 15.54 ?  55  LYS   B CB   1 
ATOM   4513 C  CG   . LYS   B 1 55  ? 60.486 -23.068 -1.005  1.00 19.23 ?  55  LYS   B CG   1 
ATOM   4514 C  CD   . LYS   B 1 55  ? 60.662 -24.570 -0.851  1.00 22.62 ?  55  LYS   B CD   1 
ATOM   4515 C  CE   . LYS   B 1 55  ? 60.664 -25.003 0.614   1.00 25.36 ?  55  LYS   B CE   1 
ATOM   4516 N  NZ   . LYS   B 1 55  ? 61.037 -26.430 0.780   1.00 26.73 ?  55  LYS   B NZ   1 
ATOM   4517 H  H    . LYS   B 1 55  ? 57.039 -21.439 -0.074  1.00 16.02 ?  55  LYS   B H    1 
ATOM   4518 H  HA   . LYS   B 1 55  ? 59.527 -20.708 -0.061  1.00 16.93 ?  55  LYS   B HA   1 
ATOM   4519 H  HB2  . LYS   B 1 55  ? 58.900 -22.933 0.262   1.00 18.69 ?  55  LYS   B HB2  1 
ATOM   4520 H  HB3  . LYS   B 1 55  ? 58.472 -23.033 -1.263  1.00 18.69 ?  55  LYS   B HB3  1 
ATOM   4521 H  HG2  . LYS   B 1 55  ? 60.663 -22.836 -1.929  1.00 23.11 ?  55  LYS   B HG2  1 
ATOM   4522 H  HG3  . LYS   B 1 55  ? 61.124 -22.625 -0.422  1.00 23.11 ?  55  LYS   B HG3  1 
ATOM   4523 H  HD2  . LYS   B 1 55  ? 59.932 -25.026 -1.298  1.00 27.18 ?  55  LYS   B HD2  1 
ATOM   4524 H  HD3  . LYS   B 1 55  ? 61.511 -24.834 -1.241  1.00 27.18 ?  55  LYS   B HD3  1 
ATOM   4525 H  HE2  . LYS   B 1 55  ? 61.304 -24.458 1.102   1.00 30.47 ?  55  LYS   B HE2  1 
ATOM   4526 H  HE3  . LYS   B 1 55  ? 59.773 -24.872 0.982   1.00 30.47 ?  55  LYS   B HE3  1 
ATOM   4527 H  HZ1  . LYS   B 1 55  ? 60.995 -26.654 1.641   1.00 32.11 ?  55  LYS   B HZ1  1 
ATOM   4528 H  HZ2  . LYS   B 1 55  ? 60.473 -26.943 0.321   1.00 32.11 ?  55  LYS   B HZ2  1 
ATOM   4529 H  HZ3  . LYS   B 1 55  ? 61.861 -26.564 0.483   1.00 32.11 ?  55  LYS   B HZ3  1 
ATOM   4530 N  N    . ALA   B 1 56  ? 58.222 -20.641 -2.984  1.00 13.47 ?  56  ALA   B N    1 
ATOM   4531 C  CA   . ALA   B 1 56  ? 58.442 -20.135 -4.333  1.00 14.46 ?  56  ALA   B CA   1 
ATOM   4532 C  C    . ALA   B 1 56  ? 58.721 -18.639 -4.327  1.00 14.21 ?  56  ALA   B C    1 
ATOM   4533 O  O    . ALA   B 1 56  ? 59.455 -18.141 -5.192  1.00 15.14 ?  56  ALA   B O    1 
ATOM   4534 C  CB   . ALA   B 1 56  ? 57.243 -20.459 -5.223  1.00 15.44 ?  56  ALA   B CB   1 
ATOM   4535 H  H    . ALA   B 1 56  ? 57.440 -20.980 -2.850  1.00 16.20 ?  56  ALA   B H    1 
ATOM   4536 H  HA   . ALA   B 1 56  ? 59.215 -20.574 -4.710  1.00 17.39 ?  56  ALA   B HA   1 
ATOM   4537 H  HB1  . ALA   B 1 56  ? 57.411 -20.118 -6.117  1.00 18.57 ?  56  ALA   B HB1  1 
ATOM   4538 H  HB2  . ALA   B 1 56  ? 57.125 -21.421 -5.255  1.00 18.57 ?  56  ALA   B HB2  1 
ATOM   4539 H  HB3  . ALA   B 1 56  ? 56.449 -20.041 -4.855  1.00 18.57 ?  56  ALA   B HB3  1 
ATOM   4540 N  N    . THR   B 1 57  ? 58.156 -17.908 -3.363  1.00 13.80 ?  57  THR   B N    1 
ATOM   4541 C  CA   . THR   B 1 57  ? 58.397 -16.474 -3.237  1.00 13.83 ?  57  THR   B CA   1 
ATOM   4542 C  C    . THR   B 1 57  ? 59.644 -16.150 -2.424  1.00 14.77 ?  57  THR   B C    1 
ATOM   4543 O  O    . THR   B 1 57  ? 59.874 -14.975 -2.113  1.00 14.97 ?  57  THR   B O    1 
ATOM   4544 C  CB   . THR   B 1 57  ? 57.194 -15.746 -2.609  1.00 13.21 ?  57  THR   B CB   1 
ATOM   4545 O  OG1  . THR   B 1 57  ? 57.167 -15.961 -1.191  1.00 13.56 ?  57  THR   B OG1  1 
ATOM   4546 C  CG2  . THR   B 1 57  ? 55.879 -16.167 -3.251  1.00 13.33 ?  57  THR   B CG2  1 
ATOM   4547 H  H    . THR   B 1 57  ? 57.611 -18.220 -2.773  1.00 16.60 ?  57  THR   B H    1 
ATOM   4548 H  HA   . THR   B 1 57  ? 58.523 -16.107 -4.126  1.00 16.64 ?  57  THR   B HA   1 
ATOM   4549 H  HB   . THR   B 1 57  ? 57.299 -14.792 -2.774  1.00 15.89 ?  57  THR   B HB   1 
ATOM   4550 H  HG1  . THR   B 1 57  ? 57.098 -16.778 -1.028  1.00 16.31 ?  57  THR   B HG1  1 
ATOM   4551 H  HG21 . THR   B 1 57  ? 55.154 -15.621 -2.914  1.00 16.03 ?  57  THR   B HG21 1 
ATOM   4552 H  HG22 . THR   B 1 57  ? 55.931 -16.061 -4.216  1.00 16.03 ?  57  THR   B HG22 1 
ATOM   4553 H  HG23 . THR   B 1 57  ? 55.694 -17.096 -3.049  1.00 16.03 ?  57  THR   B HG23 1 
ATOM   4554 N  N    . ASN   B 1 58  ? 60.437 -17.156 -2.058  1.00 15.37 ?  58  ASN   B N    1 
ATOM   4555 C  CA   . ASN   B 1 58  ? 61.636 -16.936 -1.254  1.00 18.18 ?  58  ASN   B CA   1 
ATOM   4556 C  C    . ASN   B 1 58  ? 61.296 -16.226 0.055   1.00 15.96 ?  58  ASN   B C    1 
ATOM   4557 O  O    . ASN   B 1 58  ? 62.026 -15.346 0.520   1.00 16.52 ?  58  ASN   B O    1 
ATOM   4558 C  CB   . ASN   B 1 58  ? 62.711 -16.176 -2.037  1.00 25.80 ?  58  ASN   B CB   1 
ATOM   4559 C  CG   . ASN   B 1 58  ? 64.085 -16.301 -1.409  1.00 34.17 ?  58  ASN   B CG   1 
ATOM   4560 O  OD1  . ASN   B 1 58  ? 64.382 -17.283 -0.729  1.00 37.42 ?  58  ASN   B OD1  1 
ATOM   4561 N  ND2  . ASN   B 1 58  ? 64.931 -15.301 -1.633  1.00 38.81 ?  58  ASN   B ND2  1 
ATOM   4562 H  H    . ASN   B 1 58  ? 60.296 -17.986 -2.254  1.00 18.49 ?  58  ASN   B H    1 
ATOM   4563 H  HA   . ASN   B 1 58  ? 62.011 -17.804 -1.030  1.00 21.86 ?  58  ASN   B HA   1 
ATOM   4564 H  HB2  . ASN   B 1 58  ? 62.760 -16.531 -2.940  1.00 31.00 ?  58  ASN   B HB2  1 
ATOM   4565 H  HB3  . ASN   B 1 58  ? 62.479 -15.235 -2.063  1.00 31.00 ?  58  ASN   B HB3  1 
ATOM   4566 H  HD21 . ASN   B 1 58  ? 65.723 -15.325 -1.299  1.00 46.62 ?  58  ASN   B HD21 1 
ATOM   4567 H  HD22 . ASN   B 1 58  ? 64.686 -14.630 -2.112  1.00 46.62 ?  58  ASN   B HD22 1 
ATOM   4568 N  N    . ASN   B 1 59  ? 60.176 -16.619 0.658   1.00 15.01 ?  59  ASN   B N    1 
ATOM   4569 C  CA   . ASN   B 1 59  ? 59.695 -16.153 1.959   1.00 14.91 ?  59  ASN   B CA   1 
ATOM   4570 C  C    . ASN   B 1 59  ? 59.101 -14.746 1.908   1.00 14.11 ?  59  ASN   B C    1 
ATOM   4571 O  O    . ASN   B 1 59  ? 58.674 -14.243 2.951   1.00 14.39 ?  59  ASN   B O    1 
ATOM   4572 C  CB   . ASN   B 1 59  ? 60.765 -16.213 3.063   1.00 16.01 ?  59  ASN   B CB   1 
ATOM   4573 C  CG   . ASN   B 1 59  ? 60.175 -16.399 4.441   1.00 17.48 ?  59  ASN   B CG   1 
ATOM   4574 O  OD1  . ASN   B 1 59  ? 59.346 -17.284 4.661   1.00 17.66 ?  59  ASN   B OD1  1 
ATOM   4575 N  ND2  . ASN   B 1 59  ? 60.601 -15.564 5.384   1.00 18.19 ?  59  ASN   B ND2  1 
ATOM   4576 H  H    . ASN   B 1 59  ? 59.642 -17.201 0.310   1.00 18.06 ?  59  ASN   B H    1 
ATOM   4577 H  HA   . ASN   B 1 59  ? 58.985 -16.752 2.238   1.00 17.93 ?  59  ASN   B HA   1 
ATOM   4578 H  HB2  . ASN   B 1 59  ? 61.360 -16.962 2.897   1.00 19.25 ?  59  ASN   B HB2  1 
ATOM   4579 H  HB3  . ASN   B 1 59  ? 61.267 -15.386 3.070   1.00 19.25 ?  59  ASN   B HB3  1 
ATOM   4580 H  HD21 . ASN   B 1 59  ? 60.296 -15.627 6.188   1.00 21.87 ?  59  ASN   B HD21 1 
ATOM   4581 H  HD22 . ASN   B 1 59  ? 61.178 -14.957 5.192   1.00 21.87 ?  59  ASN   B HD22 1 
ATOM   4582 N  N    . ALA   B 1 60  ? 59.042 -14.099 0.742   1.00 14.10 ?  60  ALA   B N    1 
ATOM   4583 C  CA   . ALA   B 1 60  ? 58.452 -12.765 0.679   1.00 13.69 ?  60  ALA   B CA   1 
ATOM   4584 C  C    . ALA   B 1 60  ? 56.979 -12.789 1.070   1.00 13.10 ?  60  ALA   B C    1 
ATOM   4585 O  O    . ALA   B 1 60  ? 56.478 -11.835 1.680   1.00 13.44 ?  60  ALA   B O    1 
ATOM   4586 C  CB   . ALA   B 1 60  ? 58.620 -12.184 -0.725  1.00 14.98 ?  60  ALA   B CB   1 
ATOM   4587 H  H    . ALA   B 1 60  ? 59.330 -14.409 -0.005  1.00 16.96 ?  60  ALA   B H    1 
ATOM   4588 H  HA   . ALA   B 1 60  ? 58.917 -12.188 1.302   1.00 16.47 ?  60  ALA   B HA   1 
ATOM   4589 H  HB1  . ALA   B 1 60  ? 58.229 -11.300 -0.749  1.00 18.01 ?  60  ALA   B HB1  1 
ATOM   4590 H  HB2  . ALA   B 1 60  ? 59.570 -12.131 -0.931  1.00 18.01 ?  60  ALA   B HB2  1 
ATOM   4591 H  HB3  . ALA   B 1 60  ? 58.178 -12.764 -1.363  1.00 18.01 ?  60  ALA   B HB3  1 
ATOM   4592 N  N    . MET   B 1 61  ? 56.270 -13.862 0.723   1.00 12.69 ?  61  MET   B N    1 
ATOM   4593 C  CA   . MET   B 1 61  ? 54.875 -13.983 1.119   1.00 12.27 ?  61  MET   B CA   1 
ATOM   4594 C  C    . MET   B 1 61  ? 54.744 -14.002 2.641   1.00 12.49 ?  61  MET   B C    1 
ATOM   4595 O  O    . MET   B 1 61  ? 53.847 -13.358 3.203   1.00 12.40 ?  61  MET   B O    1 
ATOM   4596 C  CB   . MET   B 1 61  ? 54.292 -15.245 0.481   1.00 12.22 ?  61  MET   B CB   1 
ATOM   4597 C  CG   . MET   B 1 61  ? 52.854 -15.548 0.906   1.00 11.98 ?  61  MET   B CG   1 
ATOM   4598 S  SD   . MET   B 1 61  ? 52.212 -17.050 0.132   1.00 12.69 ?  61  MET   B SD   1 
ATOM   4599 C  CE   . MET   B 1 61  ? 51.965 -16.456 -1.537  1.00 13.76 ?  61  MET   B CE   1 
ATOM   4600 H  H    . MET   B 1 61  ? 56.574 -14.528 0.264   1.00 15.26 ?  61  MET   B H    1 
ATOM   4601 H  HA   . MET   B 1 61  ? 54.385 -13.224 0.763   1.00 14.76 ?  61  MET   B HA   1 
ATOM   4602 H  HB2  . MET   B 1 61  ? 54.297 -15.142 -0.486  1.00 14.70 ?  61  MET   B HB2  1 
ATOM   4603 H  HB3  . MET   B 1 61  ? 54.842 -16.004 0.729   1.00 14.70 ?  61  MET   B HB3  1 
ATOM   4604 H  HG2  . MET   B 1 61  ? 52.825 -15.673 1.869   1.00 14.41 ?  61  MET   B HG2  1 
ATOM   4605 H  HG3  . MET   B 1 61  ? 52.284 -14.807 0.650   1.00 14.41 ?  61  MET   B HG3  1 
ATOM   4606 H  HE1  . MET   B 1 61  ? 51.573 -17.167 -2.067  1.00 16.55 ?  61  MET   B HE1  1 
ATOM   4607 H  HE2  . MET   B 1 61  ? 51.371 -15.690 -1.518  1.00 16.55 ?  61  MET   B HE2  1 
ATOM   4608 H  HE3  . MET   B 1 61  ? 52.824 -16.200 -1.910  1.00 16.55 ?  61  MET   B HE3  1 
ATOM   4609 N  N    . GLN   B 1 62  ? 55.631 -14.723 3.332   1.00 12.41 ?  62  GLN   B N    1 
ATOM   4610 C  CA   . GLN   B 1 62  ? 55.529 -14.787 4.787   1.00 12.79 ?  62  GLN   B CA   1 
ATOM   4611 C  C    . GLN   B 1 62  ? 55.808 -13.433 5.425   1.00 13.11 ?  62  GLN   B C    1 
ATOM   4612 O  O    . GLN   B 1 62  ? 55.126 -13.037 6.377   1.00 13.51 ?  62  GLN   B O    1 
ATOM   4613 C  CB   . GLN   B 1 62  ? 56.478 -15.842 5.350   1.00 12.82 ?  62  GLN   B CB   1 
ATOM   4614 C  CG   . GLN   B 1 62  ? 56.252 -16.115 6.829   1.00 13.28 ?  62  GLN   B CG   1 
ATOM   4615 C  CD   . GLN   B 1 62  ? 54.878 -16.706 7.074   1.00 13.05 ?  62  GLN   B CD   1 
ATOM   4616 O  OE1  . GLN   B 1 62  ? 54.623 -17.855 6.715   1.00 13.40 ?  62  GLN   B OE1  1 
ATOM   4617 N  NE2  . GLN   B 1 62  ? 53.970 -15.915 7.640   1.00 13.58 ?  62  GLN   B NE2  1 
ATOM   4618 H  H    . GLN   B 1 62  ? 56.274 -15.180 2.986   1.00 14.93 ?  62  GLN   B H    1 
ATOM   4619 H  HA   . GLN   B 1 62  ? 54.624 -15.042 5.020   1.00 15.39 ?  62  GLN   B HA   1 
ATOM   4620 H  HB2  . GLN   B 1 62  ? 56.350 -16.673 4.867   1.00 15.42 ?  62  GLN   B HB2  1 
ATOM   4621 H  HB3  . GLN   B 1 62  ? 57.392 -15.533 5.238   1.00 15.42 ?  62  GLN   B HB3  1 
ATOM   4622 H  HG2  . GLN   B 1 62  ? 56.916 -16.752 7.139   1.00 15.97 ?  62  GLN   B HG2  1 
ATOM   4623 H  HG3  . GLN   B 1 62  ? 56.323 -15.288 7.327   1.00 15.97 ?  62  GLN   B HG3  1 
ATOM   4624 H  HE21 . GLN   B 1 62  ? 54.184 -15.115 7.869   1.00 16.33 ?  62  GLN   B HE21 1 
ATOM   4625 H  HE22 . GLN   B 1 62  ? 53.180 -16.212 7.789   1.00 16.33 ?  62  GLN   B HE22 1 
ATOM   4626 N  N    . VAL   B 1 63  ? 56.820 -12.717 4.934   1.00 13.59 ?  63  VAL   B N    1 
ATOM   4627 C  CA   . VAL   B 1 63  ? 57.128 -11.402 5.491   1.00 14.40 ?  63  VAL   B CA   1 
ATOM   4628 C  C    . VAL   B 1 63  ? 55.935 -10.469 5.316   1.00 13.66 ?  63  VAL   B C    1 
ATOM   4629 O  O    . VAL   B 1 63  ? 55.524 -9.765  6.249   1.00 14.35 ?  63  VAL   B O    1 
ATOM   4630 C  CB   . VAL   B 1 63  ? 58.415 -10.840 4.863   1.00 15.78 ?  63  VAL   B CB   1 
ATOM   4631 C  CG1  . VAL   B 1 63  ? 58.647 -9.403  5.320   1.00 16.52 ?  63  VAL   B CG1  1 
ATOM   4632 C  CG2  . VAL   B 1 63  ? 59.602 -11.720 5.235   1.00 16.63 ?  63  VAL   B CG2  1 
ATOM   4633 H  H    . VAL   B 1 63  ? 57.335 -12.964 4.289   1.00 16.34 ?  63  VAL   B H    1 
ATOM   4634 H  HA   . VAL   B 1 63  ? 57.287 -11.500 6.440   1.00 17.32 ?  63  VAL   B HA   1 
ATOM   4635 H  HB   . VAL   B 1 63  ? 58.333 -10.842 3.897   1.00 18.97 ?  63  VAL   B HB   1 
ATOM   4636 H  HG11 . VAL   B 1 63  ? 59.562 -9.151  5.118   1.00 19.86 ?  63  VAL   B HG11 1 
ATOM   4637 H  HG12 . VAL   B 1 63  ? 58.033 -8.817  4.854   1.00 19.86 ?  63  VAL   B HG12 1 
ATOM   4638 H  HG13 . VAL   B 1 63  ? 58.497 -9.349  6.279   1.00 19.86 ?  63  VAL   B HG13 1 
ATOM   4639 H  HG21 . VAL   B 1 63  ? 60.410 -11.338 4.857   1.00 19.99 ?  63  VAL   B HG21 1 
ATOM   4640 H  HG22 . VAL   B 1 63  ? 59.676 -11.754 6.204   1.00 19.99 ?  63  VAL   B HG22 1 
ATOM   4641 H  HG23 . VAL   B 1 63  ? 59.459 -12.611 4.883   1.00 19.99 ?  63  VAL   B HG23 1 
ATOM   4642 N  N    . GLU   B 1 64  ? 55.362 -10.452 4.110   1.00 13.39 ?  64  GLU   B N    1 
ATOM   4643 C  CA   . GLU   B 1 64  ? 54.196 -9.614  3.840   1.00 13.14 ?  64  GLU   B CA   1 
ATOM   4644 C  C    . GLU   B 1 64  ? 53.017 -10.016 4.723   1.00 12.72 ?  64  GLU   B C    1 
ATOM   4645 O  O    . GLU   B 1 64  ? 52.272 -9.156  5.223   1.00 13.41 ?  64  GLU   B O    1 
ATOM   4646 C  CB   . GLU   B 1 64  ? 53.830 -9.762  2.363   1.00 13.23 ?  64  GLU   B CB   1 
ATOM   4647 C  CG   . GLU   B 1 64  ? 52.560 -9.027  1.934   1.00 13.45 ?  64  GLU   B CG   1 
ATOM   4648 C  CD   . GLU   B 1 64  ? 52.016 -9.528  0.595   1.00 13.85 ?  64  GLU   B CD   1 
ATOM   4649 O  OE1  . GLU   B 1 64  ? 52.194 -10.735 0.278   1.00 14.45 ?  64  GLU   B OE1  1 
ATOM   4650 O  OE2  . GLU   B 1 64  ? 51.400 -8.711  -0.134  1.00 14.58 -1 64  GLU   B OE2  1 
ATOM   4651 H  H    . GLU   B 1 64  ? 55.636 -10.911 3.429   1.00 16.10 ?  64  GLU   B H    1 
ATOM   4652 H  HA   . GLU   B 1 64  ? 54.414 -8.687  4.015   1.00 15.80 ?  64  GLU   B HA   1 
ATOM   4653 H  HB2  . GLU   B 1 64  ? 54.557 -9.406  1.824   1.00 15.92 ?  64  GLU   B HB2  1 
ATOM   4654 H  HB3  . GLU   B 1 64  ? 53.705 -10.698 2.164   1.00 15.92 ?  64  GLU   B HB3  1 
ATOM   4655 H  HG2  . GLU   B 1 64  ? 51.864 -9.154  2.603   1.00 16.18 ?  64  GLU   B HG2  1 
ATOM   4656 H  HG3  . GLU   B 1 64  ? 52.754 -8.080  1.844   1.00 16.18 ?  64  GLU   B HG3  1 
ATOM   4657 N  N    . SER   B 1 65  ? 52.834 -11.325 4.913   1.00 12.38 ?  65  SER   B N    1 
ATOM   4658 C  CA   . SER   B 1 65  ? 51.728 -11.834 5.714   1.00 12.53 ?  65  SER   B CA   1 
ATOM   4659 C  C    . SER   B 1 65  ? 51.864 -11.435 7.177   1.00 12.55 ?  65  SER   B C    1 
ATOM   4660 O  O    . SER   B 1 65  ? 50.867 -11.063 7.816   1.00 13.07 ?  65  SER   B O    1 
ATOM   4661 C  CB   . SER   B 1 65  ? 51.642 -13.356 5.581   1.00 12.58 ?  65  SER   B CB   1 
ATOM   4662 O  OG   . SER   B 1 65  ? 51.300 -13.752 4.259   1.00 12.79 ?  65  SER   B OG   1 
ATOM   4663 H  H    . SER   B 1 65  ? 53.344 -11.946 4.591   1.00 14.90 ?  65  SER   B H    1 
ATOM   4664 H  HA   . SER   B 1 65  ? 50.898 -11.458 5.378   1.00 15.07 ?  65  SER   B HA   1 
ATOM   4665 H  HB2  . SER   B 1 65  ? 52.501 -13.739 5.812   1.00 15.13 ?  65  SER   B HB2  1 
ATOM   4666 H  HB3  . SER   B 1 65  ? 50.960 -13.683 6.191   1.00 15.13 ?  65  SER   B HB3  1 
ATOM   4667 H  HG   . SER   B 1 65  ? 51.883 -13.466 3.716   1.00 15.39 ?  65  SER   B HG   1 
ATOM   4668 N  N    . ASP   B 1 66  ? 53.074 -11.536 7.739   1.00 12.74 ?  66  ASP   B N    1 
ATOM   4669 C  CA   . ASP   B 1 66  ? 53.265 -11.146 9.133   1.00 13.11 ?  66  ASP   B CA   1 
ATOM   4670 C  C    . ASP   B 1 66  ? 52.950 -9.668  9.335   1.00 13.72 ?  66  ASP   B C    1 
ATOM   4671 O  O    . ASP   B 1 66  ? 52.372 -9.279  10.356  1.00 14.10 ?  66  ASP   B O    1 
ATOM   4672 C  CB   . ASP   B 1 66  ? 54.696 -11.456 9.579   1.00 14.36 ?  66  ASP   B CB   1 
ATOM   4673 C  CG   . ASP   B 1 66  ? 54.963 -12.943 9.736   1.00 16.22 ?  66  ASP   B CG   1 
ATOM   4674 O  OD1  . ASP   B 1 66  ? 54.015 -13.758 9.644   1.00 16.91 ?  66  ASP   B OD1  1 
ATOM   4675 O  OD2  . ASP   B 1 66  ? 56.140 -13.301 9.963   1.00 18.73 -1 66  ASP   B OD2  1 
ATOM   4676 H  H    . ASP   B 1 66  ? 53.779 -11.829 7.344   1.00 15.33 ?  66  ASP   B H    1 
ATOM   4677 H  HA   . ASP   B 1 66  ? 52.661 -11.656 9.693   1.00 15.77 ?  66  ASP   B HA   1 
ATOM   4678 H  HB2  . ASP   B 1 66  ? 55.315 -11.115 8.918   1.00 17.26 ?  66  ASP   B HB2  1 
ATOM   4679 H  HB3  . ASP   B 1 66  ? 54.858 -11.030 10.437  1.00 17.26 ?  66  ASP   B HB3  1 
ATOM   4680 N  N    . ASP   B 1 67  ? 53.323 -8.824  8.372   1.00 13.13 ?  67  ASP   B N    1 
ATOM   4681 C  CA   . ASP   B 1 67  ? 52.982 -7.411  8.467   1.00 13.56 ?  67  ASP   B CA   1 
ATOM   4682 C  C    . ASP   B 1 67  ? 51.470 -7.204  8.386   1.00 13.94 ?  67  ASP   B C    1 
ATOM   4683 O  O    . ASP   B 1 67  ? 50.906 -6.404  9.140   1.00 14.25 ?  67  ASP   B O    1 
ATOM   4684 C  CB   . ASP   B 1 67  ? 53.697 -6.640  7.367   1.00 14.75 ?  67  ASP   B CB   1 
ATOM   4685 C  CG   . ASP   B 1 67  ? 53.277 -5.198  7.327   1.00 16.04 ?  67  ASP   B CG   1 
ATOM   4686 O  OD1  . ASP   B 1 67  ? 53.772 -4.395  8.154   1.00 17.28 ?  67  ASP   B OD1  1 
ATOM   4687 O  OD2  . ASP   B 1 67  ? 52.419 -4.889  6.484   1.00 16.94 -1 67  ASP   B OD2  1 
ATOM   4688 H  H    . ASP   B 1 67  ? 53.773 -9.043  7.671   1.00 15.80 ?  67  ASP   B H    1 
ATOM   4689 H  HA   . ASP   B 1 67  ? 53.289 -7.068  9.319   1.00 16.30 ?  67  ASP   B HA   1 
ATOM   4690 H  HB2  . ASP   B 1 67  ? 54.656 -6.671  7.524   1.00 17.74 ?  67  ASP   B HB2  1 
ATOM   4691 H  HB3  . ASP   B 1 67  ? 53.495 -7.050  6.506   1.00 17.74 ?  67  ASP   B HB3  1 
ATOM   4692 N  N    . TYR   B 1 68  ? 50.793 -7.933  7.493   1.00 13.48 ?  68  TYR   B N    1 
ATOM   4693 C  CA   . TYR   B 1 68  ? 49.334 -7.857  7.422   1.00 14.13 ?  68  TYR   B CA   1 
ATOM   4694 C  C    . TYR   B 1 68  ? 48.702 -8.200  8.767   1.00 13.51 ?  68  TYR   B C    1 
ATOM   4695 O  O    . TYR   B 1 68  ? 47.769 -7.527  9.224   1.00 14.12 ?  68  TYR   B O    1 
ATOM   4696 C  CB   . TYR   B 1 68  ? 48.803 -8.794  6.330   1.00 14.90 ?  68  TYR   B CB   1 
ATOM   4697 C  CG   . TYR   B 1 68  ? 47.294 -8.946  6.384   1.00 15.81 ?  68  TYR   B CG   1 
ATOM   4698 C  CD1  . TYR   B 1 68  ? 46.697 -9.897  7.208   1.00 16.44 ?  68  TYR   B CD1  1 
ATOM   4699 C  CD2  . TYR   B 1 68  ? 46.470 -8.113  5.650   1.00 16.50 ?  68  TYR   B CD2  1 
ATOM   4700 C  CE1  . TYR   B 1 68  ? 45.329 -10.018 7.287   1.00 17.60 ?  68  TYR   B CE1  1 
ATOM   4701 C  CE2  . TYR   B 1 68  ? 45.087 -8.236  5.717   1.00 16.92 ?  68  TYR   B CE2  1 
ATOM   4702 C  CZ   . TYR   B 1 68  ? 44.536 -9.184  6.541   1.00 17.37 ?  68  TYR   B CZ   1 
ATOM   4703 O  OH   . TYR   B 1 68  ? 43.167 -9.297  6.623   1.00 18.34 ?  68  TYR   B OH   1 
ATOM   4704 H  H    . TYR   B 1 68  ? 51.151 -8.476  6.927   1.00 16.21 ?  68  TYR   B H    1 
ATOM   4705 H  HA   . TYR   B 1 68  ? 49.081 -6.950  7.196   1.00 16.99 ?  68  TYR   B HA   1 
ATOM   4706 H  HB2  . TYR   B 1 68  ? 49.036 -8.431  5.465   1.00 17.92 ?  68  TYR   B HB2  1 
ATOM   4707 H  HB3  . TYR   B 1 68  ? 49.200 -9.670  6.448   1.00 17.92 ?  68  TYR   B HB3  1 
ATOM   4708 H  HD1  . TYR   B 1 68  ? 47.232 -10.466 7.718   1.00 19.77 ?  68  TYR   B HD1  1 
ATOM   4709 H  HD2  . TYR   B 1 68  ? 46.854 -7.464  5.109   1.00 19.84 ?  68  TYR   B HD2  1 
ATOM   4710 H  HE1  . TYR   B 1 68  ? 44.941 -10.669 7.831   1.00 21.16 ?  68  TYR   B HE1  1 
ATOM   4711 H  HE2  . TYR   B 1 68  ? 44.544 -7.669  5.221   1.00 20.34 ?  68  TYR   B HE2  1 
ATOM   4712 H  HH   . TYR   B 1 68  ? 42.787 -8.741  6.107   1.00 22.04 ?  68  TYR   B HH   1 
ATOM   4713 N  N    . ILE   B 1 69  ? 49.182 -9.269  9.406   1.00 13.52 ?  69  ILE   B N    1 
ATOM   4714 C  CA   . ILE   B 1 69  ? 48.627 -9.698  10.688  1.00 14.05 ?  69  ILE   B CA   1 
ATOM   4715 C  C    . ILE   B 1 69  ? 48.878 -8.652  11.768  1.00 13.81 ?  69  ILE   B C    1 
ATOM   4716 O  O    . ILE   B 1 69  ? 48.004 -8.376  12.598  1.00 14.17 ?  69  ILE   B O    1 
ATOM   4717 C  CB   . ILE   B 1 69  ? 49.205 -11.074 11.074  1.00 14.80 ?  69  ILE   B CB   1 
ATOM   4718 C  CG1  . ILE   B 1 69  ? 48.670 -12.179 10.152  1.00 15.19 ?  69  ILE   B CG1  1 
ATOM   4719 C  CG2  . ILE   B 1 69  ? 48.941 -11.387 12.538  1.00 15.92 ?  69  ILE   B CG2  1 
ATOM   4720 C  CD1  . ILE   B 1 69  ? 47.198 -12.499 10.322  1.00 15.36 ?  69  ILE   B CD1  1 
ATOM   4721 H  H    . ILE   B 1 69  ? 49.832 -9.756  9.126   1.00 16.26 ?  69  ILE   B H    1 
ATOM   4722 H  HA   . ILE   B 1 69  ? 47.669 -9.796  10.592  1.00 16.90 ?  69  ILE   B HA   1 
ATOM   4723 H  HB   . ILE   B 1 69  ? 50.168 -11.030 10.954  1.00 17.80 ?  69  ILE   B HB   1 
ATOM   4724 H  HG12 . ILE   B 1 69  ? 48.807 -11.902 9.232   1.00 18.27 ?  69  ILE   B HG12 1 
ATOM   4725 H  HG13 . ILE   B 1 69  ? 49.172 -12.991 10.324  1.00 18.27 ?  69  ILE   B HG13 1 
ATOM   4726 H  HG21 . ILE   B 1 69  ? 49.080 -12.337 12.682  1.00 19.14 ?  69  ILE   B HG21 1 
ATOM   4727 H  HG22 . ILE   B 1 69  ? 49.560 -10.881 13.090  1.00 19.14 ?  69  ILE   B HG22 1 
ATOM   4728 H  HG23 . ILE   B 1 69  ? 48.029 -11.150 12.753  1.00 19.14 ?  69  ILE   B HG23 1 
ATOM   4729 H  HD11 . ILE   B 1 69  ? 46.962 -13.214 9.710   1.00 18.47 ?  69  ILE   B HD11 1 
ATOM   4730 H  HD12 . ILE   B 1 69  ? 47.039 -12.784 11.236  1.00 18.47 ?  69  ILE   B HD12 1 
ATOM   4731 H  HD13 . ILE   B 1 69  ? 46.674 -11.709 10.125  1.00 18.47 ?  69  ILE   B HD13 1 
ATOM   4732 N  N    . ALA   B 1 70  ? 50.074 -8.065  11.794  1.00 13.82 ?  70  ALA   B N    1 
ATOM   4733 C  CA   . ALA   B 1 70  ? 50.356 -7.028  12.780  1.00 13.89 ?  70  ALA   B CA   1 
ATOM   4734 C  C    . ALA   B 1 70  ? 49.356 -5.885  12.671  1.00 14.15 ?  70  ALA   B C    1 
ATOM   4735 O  O    . ALA   B 1 70  ? 48.912 -5.339  13.688  1.00 14.58 ?  70  ALA   B O    1 
ATOM   4736 C  CB   . ALA   B 1 70  ? 51.788 -6.519  12.607  1.00 14.50 ?  70  ALA   B CB   1 
ATOM   4737 H  H    . ALA   B 1 70  ? 50.722 -8.250  11.267  1.00 16.62 ?  70  ALA   B H    1 
ATOM   4738 H  HA   . ALA   B 1 70  ? 50.284 -7.405  13.672  1.00 16.70 ?  70  ALA   B HA   1 
ATOM   4739 H  HB1  . ALA   B 1 70  ? 51.976 -5.856  13.291  1.00 17.44 ?  70  ALA   B HB1  1 
ATOM   4740 H  HB2  . ALA   B 1 70  ? 52.404 -7.265  12.696  1.00 17.44 ?  70  ALA   B HB2  1 
ATOM   4741 H  HB3  . ALA   B 1 70  ? 51.879 -6.121  11.727  1.00 17.44 ?  70  ALA   B HB3  1 
ATOM   4742 N  N    . THR   B 1 71  ? 48.981 -5.518  11.446  1.00 14.68 ?  71  THR   B N    1 
ATOM   4743 C  CA   . THR   B 1 71  ? 48.082 -4.387  11.238  1.00 15.45 ?  71  THR   B CA   1 
ATOM   4744 C  C    . THR   B 1 71  ? 46.616 -4.761  11.443  1.00 16.10 ?  71  THR   B C    1 
ATOM   4745 O  O    . THR   B 1 71  ? 45.835 -3.949  11.955  1.00 17.47 ?  71  THR   B O    1 
ATOM   4746 C  CB   . THR   B 1 71  ? 48.294 -3.820  9.833   1.00 17.19 ?  71  THR   B CB   1 
ATOM   4747 O  OG1  . THR   B 1 71  ? 49.609 -3.263  9.743   1.00 18.85 ?  71  THR   B OG1  1 
ATOM   4748 C  CG2  . THR   B 1 71  ? 47.258 -2.744  9.501   1.00 18.15 ?  71  THR   B CG2  1 
ATOM   4749 H  H    . THR   B 1 71  ? 49.237 -5.903  10.724  1.00 17.65 ?  71  THR   B H    1 
ATOM   4750 H  HA   . THR   B 1 71  ? 48.305 -3.686  11.873  1.00 18.57 ?  71  THR   B HA   1 
ATOM   4751 H  HB   . THR   B 1 71  ? 48.216 -4.528  9.179   1.00 20.66 ?  71  THR   B HB   1 
ATOM   4752 H  HG1  . THR   B 1 71  ? 49.739 -2.931  8.976   1.00 22.66 ?  71  THR   B HG1  1 
ATOM   4753 H  HG21 . THR   B 1 71  ? 47.560 -2.214  8.744   1.00 21.82 ?  71  THR   B HG21 1 
ATOM   4754 H  HG22 . THR   B 1 71  ? 46.411 -3.155  9.278   1.00 21.82 ?  71  THR   B HG22 1 
ATOM   4755 H  HG23 . THR   B 1 71  ? 47.137 -2.155  10.263  1.00 21.82 ?  71  THR   B HG23 1 
ATOM   4756 N  N    . ASN   B 1 72  ? 46.223 -5.974  11.045  1.00 15.71 ?  72  ASN   B N    1 
ATOM   4757 C  CA   . ASN   B 1 72  ? 44.819 -6.336  10.914  1.00 15.90 ?  72  ASN   B CA   1 
ATOM   4758 C  C    . ASN   B 1 72  ? 44.342 -7.434  11.853  1.00 16.29 ?  72  ASN   B C    1 
ATOM   4759 O  O    . ASN   B 1 72  ? 43.125 -7.593  12.011  1.00 17.10 ?  72  ASN   B O    1 
ATOM   4760 C  CB   . ASN   B 1 72  ? 44.517 -6.764  9.469   1.00 16.89 ?  72  ASN   B CB   1 
ATOM   4761 C  CG   . ASN   B 1 72  ? 44.785 -5.657  8.476   1.00 17.83 ?  72  ASN   B CG   1 
ATOM   4762 O  OD1  . ASN   B 1 72  ? 45.805 -5.653  7.785   1.00 18.94 ?  72  ASN   B OD1  1 
ATOM   4763 N  ND2  . ASN   B 1 72  ? 43.898 -4.683  8.436   1.00 19.31 ?  72  ASN   B ND2  1 
ATOM   4764 H  H    . ASN   B 1 72  ? 46.768 -6.613  10.840  1.00 18.89 ?  72  ASN   B H    1 
ATOM   4765 H  HA   . ASN   B 1 72  ? 44.288 -5.549  11.097  1.00 19.12 ?  72  ASN   B HA   1 
ATOM   4766 H  HB2  . ASN   B 1 72  ? 45.079 -7.522  9.237   1.00 20.31 ?  72  ASN   B HB2  1 
ATOM   4767 H  HB3  . ASN   B 1 72  ? 43.583 -7.010  9.401   1.00 20.31 ?  72  ASN   B HB3  1 
ATOM   4768 H  HD21 . ASN   B 1 72  ? 44.004 -4.028  7.888   1.00 23.21 ?  72  ASN   B HD21 1 
ATOM   4769 H  HD22 . ASN   B 1 72  ? 43.202 -4.713  8.940   1.00 23.21 ?  72  ASN   B HD22 1 
ATOM   4770 N  N    . GLY   B 1 73  ? 45.241 -8.191  12.475  1.00 15.62 ?  73  GLY   B N    1 
ATOM   4771 C  CA   . GLY   B 1 73  ? 44.837 -9.329  13.263  1.00 15.03 ?  73  GLY   B CA   1 
ATOM   4772 C  C    . GLY   B 1 73  ? 44.480 -10.511 12.388  1.00 13.90 ?  73  GLY   B C    1 
ATOM   4773 O  O    . GLY   B 1 73  ? 44.480 -10.428 11.158  1.00 13.92 ?  73  GLY   B O    1 
ATOM   4774 H  H    . GLY   B 1 73  ? 46.093 -8.062  12.450  1.00 18.78 ?  73  GLY   B H    1 
ATOM   4775 H  HA2  . GLY   B 1 73  ? 45.558 -9.583  13.860  1.00 18.08 ?  73  GLY   B HA2  1 
ATOM   4776 H  HA3  . GLY   B 1 73  ? 44.062 -9.092  13.801  1.00 18.08 ?  73  GLY   B HA3  1 
ATOM   4777 N  N    . PRO   B 1 74  ? 44.177 -11.639 13.020  1.00 14.27 ?  74  PRO   B N    1 
ATOM   4778 C  CA   . PRO   B 1 74  ? 43.933 -12.871 12.268  1.00 13.97 ?  74  PRO   B CA   1 
ATOM   4779 C  C    . PRO   B 1 74  ? 42.631 -12.819 11.481  1.00 13.41 ?  74  PRO   B C    1 
ATOM   4780 O  O    . PRO   B 1 74  ? 41.693 -12.078 11.796  1.00 14.56 ?  74  PRO   B O    1 
ATOM   4781 C  CB   . PRO   B 1 74  ? 43.870 -13.940 13.364  1.00 15.21 ?  74  PRO   B CB   1 
ATOM   4782 C  CG   . PRO   B 1 74  ? 43.422 -13.198 14.578  1.00 16.59 ?  74  PRO   B CG   1 
ATOM   4783 C  CD   . PRO   B 1 74  ? 44.073 -11.846 14.472  1.00 15.86 ?  74  PRO   B CD   1 
ATOM   4784 H  HA   . PRO   B 1 74  ? 44.678 -13.054 11.669  1.00 16.80 ?  74  PRO   B HA   1 
ATOM   4785 H  HB2  . PRO   B 1 74  ? 43.227 -14.623 13.116  1.00 18.30 ?  74  PRO   B HB2  1 
ATOM   4786 H  HB3  . PRO   B 1 74  ? 44.750 -14.326 13.498  1.00 18.30 ?  74  PRO   B HB3  1 
ATOM   4787 H  HG2  . PRO   B 1 74  ? 42.456 -13.120 14.571  1.00 19.94 ?  74  PRO   B HG2  1 
ATOM   4788 H  HG3  . PRO   B 1 74  ? 43.724 -13.667 15.372  1.00 19.94 ?  74  PRO   B HG3  1 
ATOM   4789 H  HD2  . PRO   B 1 74  ? 43.504 -11.170 14.880  1.00 19.07 ?  74  PRO   B HD2  1 
ATOM   4790 H  HD3  . PRO   B 1 74  ? 44.953 -11.861 14.878  1.00 19.07 ?  74  PRO   B HD3  1 
ATOM   4791 N  N    . LEU   B 1 75  ? 42.595 -13.635 10.431  1.00 13.03 ?  75  LEU   B N    1 
ATOM   4792 C  CA   . LEU   B 1 75  ? 41.383 -13.856 9.665   1.00 13.29 ?  75  LEU   B CA   1 
ATOM   4793 C  C    . LEU   B 1 75  ? 40.411 -14.719 10.468  1.00 13.49 ?  75  LEU   B C    1 
ATOM   4794 O  O    . LEU   B 1 75  ? 40.751 -15.274 11.516  1.00 14.33 ?  75  LEU   B O    1 
ATOM   4795 C  CB   . LEU   B 1 75  ? 41.713 -14.564 8.348   1.00 13.21 ?  75  LEU   B CB   1 
ATOM   4796 C  CG   . LEU   B 1 75  ? 42.552 -13.801 7.320   1.00 14.86 ?  75  LEU   B CG   1 
ATOM   4797 C  CD1  . LEU   B 1 75  ? 42.719 -14.627 6.049   1.00 16.35 ?  75  LEU   B CD1  1 
ATOM   4798 C  CD2  . LEU   B 1 75  ? 41.964 -12.453 6.997   1.00 17.92 ?  75  LEU   B CD2  1 
ATOM   4799 H  H    . LEU   B 1 75  ? 43.273 -14.077 10.136  1.00 15.67 ?  75  LEU   B H    1 
ATOM   4800 H  HA   . LEU   B 1 75  ? 40.955 -13.010 9.466   1.00 15.98 ?  75  LEU   B HA   1 
ATOM   4801 H  HB2  . LEU   B 1 75  ? 42.198 -15.379 8.558   1.00 15.89 ?  75  LEU   B HB2  1 
ATOM   4802 H  HB3  . LEU   B 1 75  ? 40.879 -14.797 7.911   1.00 15.89 ?  75  LEU   B HB3  1 
ATOM   4803 H  HG   . LEU   B 1 75  ? 43.439 -13.658 7.686   1.00 17.87 ?  75  LEU   B HG   1 
ATOM   4804 H  HD11 . LEU   B 1 75  ? 43.260 -14.126 5.412   1.00 19.66 ?  75  LEU   B HD11 1 
ATOM   4805 H  HD12 . LEU   B 1 75  ? 43.163 -15.463 6.265   1.00 19.66 ?  75  LEU   B HD12 1 
ATOM   4806 H  HD13 . LEU   B 1 75  ? 41.846 -14.806 5.666   1.00 19.66 ?  75  LEU   B HD13 1 
ATOM   4807 H  HD21 . LEU   B 1 75  ? 42.462 -12.056 6.269   1.00 21.55 ?  75  LEU   B HD21 1 
ATOM   4808 H  HD22 . LEU   B 1 75  ? 41.036 -12.571 6.743   1.00 21.55 ?  75  LEU   B HD22 1 
ATOM   4809 H  HD23 . LEU   B 1 75  ? 42.022 -11.892 7.786   1.00 21.55 ?  75  LEU   B HD23 1 
ATOM   4810 N  N    . LYS   B 1 76  ? 39.182 -14.818 9.963   1.00 14.61 ?  76  LYS   B N    1 
ATOM   4811 C  CA   . LYS   B 1 76  ? 38.200 -15.786 10.438  1.00 15.96 ?  76  LYS   B CA   1 
ATOM   4812 C  C    . LYS   B 1 76  ? 38.287 -17.051 9.587   1.00 14.27 ?  76  LYS   B C    1 
ATOM   4813 O  O    . LYS   B 1 76  ? 38.550 -16.983 8.386   1.00 13.86 ?  76  LYS   B O    1 
ATOM   4814 C  CB   . LYS   B 1 76  ? 36.779 -15.223 10.273  1.00 18.44 ?  76  LYS   B CB   1 
ATOM   4815 C  CG   . LYS   B 1 76  ? 36.516 -13.827 10.861  1.00 20.75 ?  76  LYS   B CG   1 
ATOM   4816 C  CD   . LYS   B 1 76  ? 35.097 -13.319 10.536  1.00 22.20 ?  76  LYS   B CD   1 
ATOM   4817 C  CE   . LYS   B 1 76  ? 34.837 -11.938 11.125  1.00 24.08 ?  76  LYS   B CE   1 
ATOM   4818 N  NZ   . LYS   B 1 76  ? 33.537 -11.359 10.676  1.00 24.51 ?  76  LYS   B NZ   1 
ATOM   4819 H  H    . LYS   B 1 76  ? 38.890 -14.326 9.326   1.00 17.57 ?  76  LYS   B H    1 
ATOM   4820 H  HA   . LYS   B 1 76  ? 38.356 -16.012 11.369  1.00 19.19 ?  76  LYS   B HA   1 
ATOM   4821 H  HB2  . LYS   B 1 76  ? 36.580 -15.175 9.324   1.00 22.17 ?  76  LYS   B HB2  1 
ATOM   4822 H  HB3  . LYS   B 1 76  ? 36.157 -15.834 10.698  1.00 22.17 ?  76  LYS   B HB3  1 
ATOM   4823 H  HG2  . LYS   B 1 76  ? 36.613 -13.867 11.826  1.00 24.94 ?  76  LYS   B HG2  1 
ATOM   4824 H  HG3  . LYS   B 1 76  ? 37.158 -13.200 10.488  1.00 24.94 ?  76  LYS   B HG3  1 
ATOM   4825 H  HD2  . LYS   B 1 76  ? 34.994 -13.262 9.572   1.00 26.68 ?  76  LYS   B HD2  1 
ATOM   4826 H  HD3  . LYS   B 1 76  ? 34.447 -13.935 10.906  1.00 26.68 ?  76  LYS   B HD3  1 
ATOM   4827 H  HE2  . LYS   B 1 76  ? 34.819 -12.007 12.093  1.00 28.93 ?  76  LYS   B HE2  1 
ATOM   4828 H  HE3  . LYS   B 1 76  ? 35.548 -11.338 10.849  1.00 28.93 ?  76  LYS   B HE3  1 
ATOM   4829 H  HZ1  . LYS   B 1 76  ? 33.421 -10.554 11.040  1.00 29.45 ?  76  LYS   B HZ1  1 
ATOM   4830 H  HZ2  . LYS   B 1 76  ? 33.530 -11.277 9.790   1.00 29.45 ?  76  LYS   B HZ2  1 
ATOM   4831 H  HZ3  . LYS   B 1 76  ? 32.866 -11.888 10.924  1.00 29.45 ?  76  LYS   B HZ3  1 
ATOM   4832 N  N    . VAL   B 1 77  ? 38.045 -18.212 10.210  1.00 14.68 ?  77  VAL   B N    1 
ATOM   4833 C  CA   . VAL   B 1 77  ? 37.830 -19.419 9.419   1.00 14.56 ?  77  VAL   B CA   1 
ATOM   4834 C  C    . VAL   B 1 77  ? 36.635 -19.175 8.510   1.00 13.63 ?  77  VAL   B C    1 
ATOM   4835 O  O    . VAL   B 1 77  ? 35.574 -18.722 8.961   1.00 13.56 ?  77  VAL   B O    1 
ATOM   4836 C  CB   . VAL   B 1 77  ? 37.628 -20.647 10.319  1.00 15.75 ?  77  VAL   B CB   1 
ATOM   4837 C  CG1  . VAL   B 1 77  ? 37.336 -21.869 9.459   1.00 16.45 ?  77  VAL   B CG1  1 
ATOM   4838 C  CG2  . VAL   B 1 77  ? 38.859 -20.891 11.185  1.00 17.59 ?  77  VAL   B CG2  1 
ATOM   4839 H  H    . VAL   B 1 77  ? 38.006 -18.320 11.060  1.00 17.65 ?  77  VAL   B H    1 
ATOM   4840 H  HA   . VAL   B 1 77  ? 38.601 -19.577 8.858   1.00 17.52 ?  77  VAL   B HA   1 
ATOM   4841 H  HB   . VAL   B 1 77  ? 36.865 -20.496 10.903  1.00 18.94 ?  77  VAL   B HB   1 
ATOM   4842 H  HG11 . VAL   B 1 77  ? 37.396 -22.663 10.014  1.00 19.78 ?  77  VAL   B HG11 1 
ATOM   4843 H  HG12 . VAL   B 1 77  ? 36.439 -21.795 9.091   1.00 19.78 ?  77  VAL   B HG12 1 
ATOM   4844 H  HG13 . VAL   B 1 77  ? 37.986 -21.914 8.744   1.00 19.78 ?  77  VAL   B HG13 1 
ATOM   4845 H  HG21 . VAL   B 1 77  ? 38.715 -21.689 11.714  1.00 21.15 ?  77  VAL   B HG21 1 
ATOM   4846 H  HG22 . VAL   B 1 77  ? 39.627 -21.007 10.607  1.00 21.15 ?  77  VAL   B HG22 1 
ATOM   4847 H  HG23 . VAL   B 1 77  ? 38.990 -20.126 11.765  1.00 21.15 ?  77  VAL   B HG23 1 
ATOM   4848 N  N    . GLY   B 1 78  ? 36.808 -19.455 7.220   1.00 13.12 ?  78  GLY   B N    1 
ATOM   4849 C  CA   . GLY   B 1 78  ? 35.834 -19.123 6.206   1.00 12.83 ?  78  GLY   B CA   1 
ATOM   4850 C  C    . GLY   B 1 78  ? 36.080 -17.803 5.508   1.00 12.29 ?  78  GLY   B C    1 
ATOM   4851 O  O    . GLY   B 1 78  ? 35.399 -17.512 4.519   1.00 12.88 ?  78  GLY   B O    1 
ATOM   4852 H  H    . GLY   B 1 78  ? 37.503 -19.849 6.909   1.00 15.78 ?  78  GLY   B H    1 
ATOM   4853 H  HA2  . GLY   B 1 78  ? 35.823 -19.819 5.537   1.00 15.43 ?  78  GLY   B HA2  1 
ATOM   4854 H  HA3  . GLY   B 1 78  ? 34.953 -19.080 6.614   1.00 15.43 ?  78  GLY   B HA3  1 
ATOM   4855 N  N    . GLY   B 1 79  ? 37.027 -16.998 5.993   1.00 12.55 ?  79  GLY   B N    1 
ATOM   4856 C  CA   . GLY   B 1 79  ? 37.326 -15.703 5.418   1.00 12.31 ?  79  GLY   B CA   1 
ATOM   4857 C  C    . GLY   B 1 79  ? 38.564 -15.716 4.532   1.00 11.80 ?  79  GLY   B C    1 
ATOM   4858 O  O    . GLY   B 1 79  ? 39.178 -16.751 4.280   1.00 12.27 ?  79  GLY   B O    1 
ATOM   4859 H  H    . GLY   B 1 79  ? 37.527 -17.194 6.661   1.00 15.10 ?  79  GLY   B H    1 
ATOM   4860 H  HA2  . GLY   B 1 79  ? 36.574 -15.405 4.878   1.00 14.81 ?  79  GLY   B HA2  1 
ATOM   4861 H  HA3  . GLY   B 1 79  ? 37.464 -15.059 6.128   1.00 14.81 ?  79  GLY   B HA3  1 
ATOM   4862 N  N    . SER   B 1 80  ? 38.932 -14.518 4.064   1.00 11.82 ?  80  SER   B N    1 
ATOM   4863 C  CA   . SER   B 1 80  ? 40.036 -14.384 3.124   1.00 11.69 ?  80  SER   B CA   1 
ATOM   4864 C  C    . SER   B 1 80  ? 40.614 -12.977 3.189   1.00 11.78 ?  80  SER   B C    1 
ATOM   4865 O  O    . SER   B 1 80  ? 39.998 -12.047 3.719   1.00 12.69 ?  80  SER   B O    1 
ATOM   4866 C  CB   . SER   B 1 80  ? 39.584 -14.672 1.688   1.00 12.18 ?  80  SER   B CB   1 
ATOM   4867 O  OG   . SER   B 1 80  ? 38.754 -13.639 1.186   1.00 12.95 ?  80  SER   B OG   1 
ATOM   4868 H  H    . SER   B 1 80  ? 38.564 -13.773 4.279   1.00 14.22 ?  80  SER   B H    1 
ATOM   4869 H  HA   . SER   B 1 80  ? 40.730 -15.013 3.363   1.00 14.07 ?  80  SER   B HA   1 
ATOM   4870 H  HB2  . SER   B 1 80  ? 40.363 -14.748 1.118   1.00 14.66 ?  80  SER   B HB2  1 
ATOM   4871 H  HB3  . SER   B 1 80  ? 39.085 -15.506 1.678   1.00 14.66 ?  80  SER   B HB3  1 
ATOM   4872 H  HG   . SER   B 1 80  ? 38.066 -13.563 1.670   1.00 15.58 ?  80  SER   B HG   1 
ATOM   4873 N  N    . CYS   B 1 81  ? 41.801 -12.827 2.605   1.00 11.37 ?  81  CYS   B N    1 
ATOM   4874 C  CA   . CYS   B 1 81  ? 42.342 -11.513 2.293   1.00 11.39 ?  81  CYS   B CA   1 
ATOM   4875 C  C    . CYS   B 1 81  ? 43.114 -11.593 0.986   1.00 10.86 ?  81  CYS   B C    1 
ATOM   4876 O  O    . CYS   B 1 81  ? 43.630 -12.656 0.613   1.00 12.03 ?  81  CYS   B O    1 
ATOM   4877 C  CB   . CYS   B 1 81  ? 43.237 -10.963 3.413   1.00 12.68 ?  81  CYS   B CB   1 
ATOM   4878 S  SG   . CYS   B 1 81  ? 44.752 -11.897 3.682   1.00 12.63 ?  81  CYS   B SG   1 
ATOM   4879 H  H    . CYS   B 1 81  ? 42.319 -13.478 2.371   1.00 13.68 ?  81  CYS   B H    1 
ATOM   4880 H  HA   . CYS   B 1 81  ? 41.606 -10.891 2.167   1.00 13.71 ?  81  CYS   B HA   1 
ATOM   4881 H  HB2  . CYS   B 1 81  ? 43.489 -10.053 3.194   1.00 15.25 ?  81  CYS   B HB2  1 
ATOM   4882 H  HB3  . CYS   B 1 81  ? 42.732 -10.969 4.245   1.00 15.25 ?  81  CYS   B HB3  1 
ATOM   4883 H  HG   . CYS   B 1 81  ? 45.371 -11.389 4.583   1.00 15.20 ?  81  CYS   B HG   1 
ATOM   4884 N  N    . VAL   B 1 82  ? 43.216 -10.451 0.312   1.00 11.22 ?  82  VAL   B N    1 
ATOM   4885 C  CA   . VAL   B 1 82  ? 43.981 -10.321 -0.922  1.00 11.43 ?  82  VAL   B CA   1 
ATOM   4886 C  C    . VAL   B 1 82  ? 45.324 -9.685  -0.595  1.00 11.78 ?  82  VAL   B C    1 
ATOM   4887 O  O    . VAL   B 1 82  ? 45.374 -8.569  -0.059  1.00 12.56 ?  82  VAL   B O    1 
ATOM   4888 C  CB   . VAL   B 1 82  ? 43.230 -9.480  -1.965  1.00 12.67 ?  82  VAL   B CB   1 
ATOM   4889 C  CG1  . VAL   B 1 82  ? 44.072 -9.328  -3.228  1.00 13.96 ?  82  VAL   B CG1  1 
ATOM   4890 C  CG2  . VAL   B 1 82  ? 41.867 -10.080 -2.275  1.00 14.03 ?  82  VAL   B CG2  1 
ATOM   4891 H  H    . VAL   B 1 82  ? 42.833 -9.715  0.553   1.00 13.50 ?  82  VAL   B H    1 
ATOM   4892 H  HA   . VAL   B 1 82  ? 44.142 -11.196 -1.298  1.00 13.76 ?  82  VAL   B HA   1 
ATOM   4893 H  HB   . VAL   B 1 82  ? 43.082 -8.593  -1.606  1.00 15.24 ?  82  VAL   B HB   1 
ATOM   4894 H  HG11 . VAL   B 1 82  ? 43.510 -9.003  -3.949  1.00 16.79 ?  82  VAL   B HG11 1 
ATOM   4895 H  HG12 . VAL   B 1 82  ? 44.788 -8.691  -3.060  1.00 16.79 ?  82  VAL   B HG12 1 
ATOM   4896 H  HG13 . VAL   B 1 82  ? 44.447 -10.190 -3.467  1.00 16.79 ?  82  VAL   B HG13 1 
ATOM   4897 H  HG21 . VAL   B 1 82  ? 41.432 -9.552  -2.966  1.00 16.88 ?  82  VAL   B HG21 1 
ATOM   4898 H  HG22 . VAL   B 1 82  ? 41.982 -10.993 -2.587  1.00 16.88 ?  82  VAL   B HG22 1 
ATOM   4899 H  HG23 . VAL   B 1 82  ? 41.324 -10.075 -1.470  1.00 16.88 ?  82  VAL   B HG23 1 
ATOM   4900 N  N    . LEU   B 1 83  ? 46.406 -10.368 -0.961  1.00 11.28 ?  83  LEU   B N    1 
ATOM   4901 C  CA   . LEU   B 1 83  ? 47.759 -9.848  -0.839  1.00 11.34 ?  83  LEU   B CA   1 
ATOM   4902 C  C    . LEU   B 1 83  ? 48.460 -9.991  -2.190  1.00 11.37 ?  83  LEU   B C    1 
ATOM   4903 O  O    . LEU   B 1 83  ? 47.854 -10.398 -3.186  1.00 11.29 ?  83  LEU   B O    1 
ATOM   4904 C  CB   . LEU   B 1 83  ? 48.507 -10.524 0.317   1.00 12.19 ?  83  LEU   B CB   1 
ATOM   4905 C  CG   . LEU   B 1 83  ? 47.998 -10.166 1.716   1.00 13.23 ?  83  LEU   B CG   1 
ATOM   4906 C  CD1  . LEU   B 1 83  ? 48.615 -11.046 2.786   1.00 13.69 ?  83  LEU   B CD1  1 
ATOM   4907 C  CD2  . LEU   B 1 83  ? 48.223 -8.687  2.042   1.00 14.08 ?  83  LEU   B CD2  1 
ATOM   4908 H  H    . LEU   B 1 83  ? 46.374 -11.161 -1.295  1.00 13.58 ?  83  LEU   B H    1 
ATOM   4909 H  HA   . LEU   B 1 83  ? 47.708 -8.904  -0.642  1.00 13.65 ?  83  LEU   B HA   1 
ATOM   4910 H  HB2  . LEU   B 1 83  ? 48.434 -11.483 0.216   1.00 14.66 ?  83  LEU   B HB2  1 
ATOM   4911 H  HB3  . LEU   B 1 83  ? 49.442 -10.262 0.271   1.00 14.66 ?  83  LEU   B HB3  1 
ATOM   4912 H  HG   . LEU   B 1 83  ? 47.044 -10.318 1.736   1.00 15.91 ?  83  LEU   B HG   1 
ATOM   4913 H  HD11 . LEU   B 1 83  ? 48.259 -10.790 3.652   1.00 16.47 ?  83  LEU   B HD11 1 
ATOM   4914 H  HD12 . LEU   B 1 83  ? 48.388 -11.973 2.599   1.00 16.47 ?  83  LEU   B HD12 1 
ATOM   4915 H  HD13 . LEU   B 1 83  ? 49.577 -10.935 2.777   1.00 16.47 ?  83  LEU   B HD13 1 
ATOM   4916 H  HD21 . LEU   B 1 83  ? 48.012 -8.535  2.977   1.00 16.94 ?  83  LEU   B HD21 1 
ATOM   4917 H  HD22 . LEU   B 1 83  ? 49.150 -8.462  1.871   1.00 16.94 ?  83  LEU   B HD22 1 
ATOM   4918 H  HD23 . LEU   B 1 83  ? 47.642 -8.149  1.481   1.00 16.94 ?  83  LEU   B HD23 1 
ATOM   4919 N  N    . SER   B 1 84  ? 49.737 -9.623  -2.243  1.00 12.25 ?  84  SER   B N    1 
ATOM   4920 C  CA   . SER   B 1 84  ? 50.469 -9.734  -3.494  1.00 12.62 ?  84  SER   B CA   1 
ATOM   4921 C  C    . SER   B 1 84  ? 50.620 -11.193 -3.914  1.00 11.86 ?  84  SER   B C    1 
ATOM   4922 O  O    . SER   B 1 84  ? 50.735 -12.097 -3.084  1.00 11.75 ?  84  SER   B O    1 
ATOM   4923 C  CB   . SER   B 1 84  ? 51.864 -9.128  -3.350  1.00 14.36 ?  84  SER   B CB   1 
ATOM   4924 O  OG   . SER   B 1 84  ? 52.597 -9.333  -4.542  1.00 16.04 ?  84  SER   B OG   1 
ATOM   4925 H  H    . SER   B 1 84  ? 50.190 -9.298  -1.584  1.00 14.73 ?  84  SER   B H    1 
ATOM   4926 H  HA   . SER   B 1 84  ? 49.996 -9.261  -4.194  1.00 15.18 ?  84  SER   B HA   1 
ATOM   4927 H  HB2  . SER   B 1 84  ? 51.780 -8.171  -3.185  1.00 17.28 ?  84  SER   B HB2  1 
ATOM   4928 H  HB3  . SER   B 1 84  ? 52.328 -9.553  -2.616  1.00 17.28 ?  84  SER   B HB3  1 
ATOM   4929 H  HG   . SER   B 1 84  ? 53.367 -8.988  -4.472  1.00 19.29 ?  84  SER   B HG   1 
ATOM   4930 N  N    . GLY   B 1 85  ? 50.686 -11.405 -5.221  1.00 12.98 ?  85  GLY   B N    1 
ATOM   4931 C  CA   . GLY   B 1 85  ? 51.034 -12.693 -5.773  1.00 13.47 ?  85  GLY   B CA   1 
ATOM   4932 C  C    . GLY   B 1 85  ? 52.506 -12.891 -6.067  1.00 12.78 ?  85  GLY   B C    1 
ATOM   4933 O  O    . GLY   B 1 85  ? 52.885 -13.968 -6.531  1.00 13.20 ?  85  GLY   B O    1 
ATOM   4934 H  H    . GLY   B 1 85  ? 50.541 -10.807 -5.813  1.00 15.61 ?  85  GLY   B H    1 
ATOM   4935 H  HA2  . GLY   B 1 85  ? 50.762 -13.388 -5.151  1.00 16.20 ?  85  GLY   B HA2  1 
ATOM   4936 H  HA3  . GLY   B 1 85  ? 50.549 -12.825 -6.597  1.00 16.20 ?  85  GLY   B HA3  1 
ATOM   4937 N  N    . HIS   B 1 86  ? 53.358 -11.893 -5.836  1.00 12.90 ?  86  HIS   B N    1 
ATOM   4938 C  CA   . HIS   B 1 86  ? 54.821 -12.059 -5.916  1.00 12.70 ?  86  HIS   B CA   1 
ATOM   4939 C  C    . HIS   B 1 86  ? 55.191 -12.570 -7.306  1.00 13.04 ?  86  HIS   B C    1 
ATOM   4940 O  O    . HIS   B 1 86  ? 54.799 -11.949 -8.307  1.00 13.63 ?  86  HIS   B O    1 
ATOM   4941 C  CB   . HIS   B 1 86  ? 55.309 -12.903 -4.741  1.00 13.14 ?  86  HIS   B CB   1 
ATOM   4942 C  CG   . HIS   B 1 86  ? 54.994 -12.297 -3.415  1.00 12.98 ?  86  HIS   B CG   1 
ATOM   4943 N  ND1  . HIS   B 1 86  ? 55.817 -11.377 -2.801  1.00 14.23 ?  86  HIS   B ND1  1 
ATOM   4944 C  CD2  . HIS   B 1 86  ? 53.921 -12.449 -2.603  1.00 13.24 ?  86  HIS   B CD2  1 
ATOM   4945 C  CE1  . HIS   B 1 86  ? 55.261 -10.989 -1.668  1.00 14.26 ?  86  HIS   B CE1  1 
ATOM   4946 N  NE2  . HIS   B 1 86  ? 54.110 -11.623 -1.525  1.00 13.53 ?  86  HIS   B NE2  1 
ATOM   4947 H  H    . HIS   B 1 86  ? 53.117 -11.097 -5.628  1.00 15.51 ?  86  HIS   B H    1 
ATOM   4948 H  HA   . HIS   B 1 86  ? 55.229 -11.187 -5.819  1.00 15.28 ?  86  HIS   B HA   1 
ATOM   4949 H  HB2  . HIS   B 1 86  ? 54.893 -13.777 -4.781  1.00 15.81 ?  86  HIS   B HB2  1 
ATOM   4950 H  HB3  . HIS   B 1 86  ? 56.277 -12.998 -4.801  1.00 15.81 ?  86  HIS   B HB3  1 
ATOM   4951 H  HD2  . HIS   B 1 86  ? 53.186 -13.000 -2.756  1.00 15.93 ?  86  HIS   B HD2  1 
ATOM   4952 H  HE1  . HIS   B 1 86  ? 55.629 -10.386 -1.062  1.00 17.15 ?  86  HIS   B HE1  1 
ATOM   4953 H  HE2  . HIS   B 1 86  ? 53.576 -11.544 -0.856  1.00 16.27 ?  86  HIS   B HE2  1 
ATOM   4954 N  N    . ASN   B 1 87  ? 55.956 -13.653 -7.418  1.00 12.99 ?  87  ASN   B N    1 
ATOM   4955 C  CA   . ASN   B 1 87  ? 56.355 -14.223 -8.696  1.00 14.13 ?  87  ASN   B CA   1 
ATOM   4956 C  C    . ASN   B 1 87  ? 55.374 -15.263 -9.201  1.00 13.54 ?  87  ASN   B C    1 
ATOM   4957 O  O    . ASN   B 1 87  ? 55.695 -15.984 -10.151 1.00 15.33 ?  87  ASN   B O    1 
ATOM   4958 C  CB   . ASN   B 1 87  ? 57.750 -14.853 -8.576  1.00 15.69 ?  87  ASN   B CB   1 
ATOM   4959 C  CG   . ASN   B 1 87  ? 57.806 -15.965 -7.534  1.00 16.76 ?  87  ASN   B CG   1 
ATOM   4960 O  OD1  . ASN   B 1 87  ? 57.169 -15.882 -6.480  1.00 15.84 ?  87  ASN   B OD1  1 
ATOM   4961 N  ND2  . ASN   B 1 87  ? 58.551 -17.029 -7.843  1.00 19.09 ?  87  ASN   B ND2  1 
ATOM   4962 H  H    . ASN   B 1 87  ? 56.259 -14.093 -6.744  1.00 15.62 ?  87  ASN   B H    1 
ATOM   4963 H  HA   . ASN   B 1 87  ? 56.404 -13.518 -9.353  1.00 16.99 ?  87  ASN   B HA   1 
ATOM   4964 H  HB2  . ASN   B 1 87  ? 58.002 -15.231 -9.435  1.00 18.86 ?  87  ASN   B HB2  1 
ATOM   4965 H  HB3  . ASN   B 1 87  ? 58.385 -14.169 -8.317  1.00 18.86 ?  87  ASN   B HB3  1 
ATOM   4966 H  HD21 . ASN   B 1 87  ? 58.616 -17.682 -7.290  1.00 22.94 ?  87  ASN   B HD21 1 
ATOM   4967 H  HD22 . ASN   B 1 87  ? 58.978 -17.056 -8.592  1.00 22.94 ?  87  ASN   B HD22 1 
ATOM   4968 N  N    . LEU   B 1 88  ? 54.193 -15.356 -8.591  1.00 12.74 ?  88  LEU   B N    1 
ATOM   4969 C  CA   . LEU   B 1 88  ? 53.215 -16.386 -8.919  1.00 12.92 ?  88  LEU   B CA   1 
ATOM   4970 C  C    . LEU   B 1 88  ? 51.983 -15.870 -9.643  1.00 12.65 ?  88  LEU   B C    1 
ATOM   4971 O  O    . LEU   B 1 88  ? 51.387 -16.618 -10.431 1.00 14.35 ?  88  LEU   B O    1 
ATOM   4972 C  CB   . LEU   B 1 88  ? 52.737 -17.068 -7.634  1.00 13.81 ?  88  LEU   B CB   1 
ATOM   4973 C  CG   . LEU   B 1 88  ? 53.844 -17.726 -6.824  1.00 16.10 ?  88  LEU   B CG   1 
ATOM   4974 C  CD1  . LEU   B 1 88  ? 53.340 -18.010 -5.419  1.00 17.40 ?  88  LEU   B CD1  1 
ATOM   4975 C  CD2  . LEU   B 1 88  ? 54.293 -19.002 -7.509  1.00 19.10 ?  88  LEU   B CD2  1 
ATOM   4976 H  H    . LEU   B 1 88  ? 53.933 -14.829 -7.959  1.00 15.32 ?  88  LEU   B H    1 
ATOM   4977 H  HA   . LEU   B 1 88  ? 53.629 -17.054 -9.475  1.00 15.55 ?  88  LEU   B HA   1 
ATOM   4978 H  HB2  . LEU   B 1 88  ? 52.308 -16.411 -7.065  1.00 16.61 ?  88  LEU   B HB2  1 
ATOM   4979 H  HB3  . LEU   B 1 88  ? 52.097 -17.762 -7.869  1.00 16.61 ?  88  LEU   B HB3  1 
ATOM   4980 H  HG   . LEU   B 1 88  ? 54.604 -17.126 -6.761  1.00 19.36 ?  88  LEU   B HG   1 
ATOM   4981 H  HD11 . LEU   B 1 88  ? 53.962 -18.605 -4.974  1.00 20.92 ?  88  LEU   B HD11 1 
ATOM   4982 H  HD12 . LEU   B 1 88  ? 53.276 -17.172 -4.933  1.00 20.92 ?  88  LEU   B HD12 1 
ATOM   4983 H  HD13 . LEU   B 1 88  ? 52.467 -18.426 -5.479  1.00 20.92 ?  88  LEU   B HD13 1 
ATOM   4984 H  HD21 . LEU   B 1 88  ? 54.973 -19.431 -6.965  1.00 22.96 ?  88  LEU   B HD21 1 
ATOM   4985 H  HD22 . LEU   B 1 88  ? 53.530 -19.593 -7.610  1.00 22.96 ?  88  LEU   B HD22 1 
ATOM   4986 H  HD23 . LEU   B 1 88  ? 54.659 -18.782 -8.380  1.00 22.96 ?  88  LEU   B HD23 1 
ATOM   4987 N  N    . ALA   B 1 89  ? 51.572 -14.634 -9.373  1.00 12.25 ?  89  ALA   B N    1 
ATOM   4988 C  CA   . ALA   B 1 89  ? 50.277 -14.144 -9.819  1.00 11.72 ?  89  ALA   B CA   1 
ATOM   4989 C  C    . ALA   B 1 89  ? 50.245 -12.654 -9.534  1.00 12.36 ?  89  ALA   B C    1 
ATOM   4990 O  O    . ALA   B 1 89  ? 51.089 -12.136 -8.801  1.00 12.94 ?  89  ALA   B O    1 
ATOM   4991 C  CB   . ALA   B 1 89  ? 49.139 -14.826 -9.066  1.00 11.94 ?  89  ALA   B CB   1 
ATOM   4992 H  H    . ALA   B 1 89  ? 52.018 -14.054 -8.914  1.00 14.73 ?  89  ALA   B H    1 
ATOM   4993 H  HA   . ALA   B 1 89  ? 50.168 -14.289 -10.772 1.00 14.10 ?  89  ALA   B HA   1 
ATOM   4994 H  HB1  . ALA   B 1 89  ? 48.290 -14.494 -9.408  1.00 14.37 ?  89  ALA   B HB1  1 
ATOM   4995 H  HB2  . ALA   B 1 89  ? 49.196 -15.784 -9.214  1.00 14.37 ?  89  ALA   B HB2  1 
ATOM   4996 H  HB3  . ALA   B 1 89  ? 49.217 -14.629 -8.125  1.00 14.37 ?  89  ALA   B HB3  1 
ATOM   4997 N  N    . LYS   B 1 90  ? 49.256 -11.962 -10.096 1.00 13.23 ?  90  LYS   B N    1 
ATOM   4998 C  CA   . LYS   B 1 90  ? 49.065 -10.576 -9.690  1.00 13.41 ?  90  LYS   B CA   1 
ATOM   4999 C  C    . LYS   B 1 90  ? 48.746 -10.502 -8.202  1.00 13.21 ?  90  LYS   B C    1 
ATOM   5000 O  O    . LYS   B 1 90  ? 49.381 -9.746  -7.451  1.00 14.33 ?  90  LYS   B O    1 
ATOM   5001 C  CB   . LYS   B 1 90  ? 47.981 -9.919  -10.541 1.00 14.69 ?  90  LYS   B CB   1 
ATOM   5002 C  CG   . LYS   B 1 90  ? 47.677 -8.481  -10.148 1.00 15.32 ?  90  LYS   B CG   1 
ATOM   5003 C  CD   . LYS   B 1 90  ? 48.878 -7.575  -10.256 1.00 17.78 ?  90  LYS   B CD   1 
ATOM   5004 C  CE   . LYS   B 1 90  ? 48.447 -6.147  -10.005 1.00 19.73 ?  90  LYS   B CE   1 
ATOM   5005 N  NZ   . LYS   B 1 90  ? 49.606 -5.223  -9.916  1.00 19.30 ?  90  LYS   B NZ   1 
ATOM   5006 H  H    . LYS   B 1 90  ? 48.704 -12.261 -10.686 1.00 15.91 ?  90  LYS   B H    1 
ATOM   5007 H  HA   . LYS   B 1 90  ? 49.890 -10.097 -9.838  1.00 16.13 ?  90  LYS   B HA   1 
ATOM   5008 H  HB2  . LYS   B 1 90  ? 48.277 -9.912  -11.469 1.00 17.67 ?  90  LYS   B HB2  1 
ATOM   5009 H  HB3  . LYS   B 1 90  ? 47.163 -10.430 -10.465 1.00 17.67 ?  90  LYS   B HB3  1 
ATOM   5010 H  HG2  . LYS   B 1 90  ? 46.985 -8.135  -10.734 1.00 18.42 ?  90  LYS   B HG2  1 
ATOM   5011 H  HG3  . LYS   B 1 90  ? 47.363 -8.462  -9.228  1.00 18.42 ?  90  LYS   B HG3  1 
ATOM   5012 H  HD2  . LYS   B 1 90  ? 49.537 -7.819  -9.588  1.00 21.38 ?  90  LYS   B HD2  1 
ATOM   5013 H  HD3  . LYS   B 1 90  ? 49.254 -7.634  -11.148 1.00 21.38 ?  90  LYS   B HD3  1 
ATOM   5014 H  HE2  . LYS   B 1 90  ? 47.882 -5.845  -10.737 1.00 23.72 ?  90  LYS   B HE2  1 
ATOM   5015 H  HE3  . LYS   B 1 90  ? 47.960 -6.095  -9.168  1.00 23.72 ?  90  LYS   B HE3  1 
ATOM   5016 H  HZ1  . LYS   B 1 90  ? 49.327 -4.388  -9.770  1.00 23.20 ?  90  LYS   B HZ1  1 
ATOM   5017 H  HZ2  . LYS   B 1 90  ? 50.142 -5.466  -9.248  1.00 23.20 ?  90  LYS   B HZ2  1 
ATOM   5018 H  HZ3  . LYS   B 1 90  ? 50.071 -5.238  -10.678 1.00 23.20 ?  90  LYS   B HZ3  1 
ATOM   5019 N  N    . HIS   B 1 91  ? 47.786 -11.318 -7.758  1.00 11.67 ?  91  HIS   B N    1 
ATOM   5020 C  CA   . HIS   B 1 91  ? 47.329 -11.343 -6.383  1.00 11.67 ?  91  HIS   B CA   1 
ATOM   5021 C  C    . HIS   B 1 91  ? 47.332 -12.771 -5.862  1.00 11.05 ?  91  HIS   B C    1 
ATOM   5022 O  O    . HIS   B 1 91  ? 47.103 -13.727 -6.613  1.00 11.65 ?  91  HIS   B O    1 
ATOM   5023 C  CB   . HIS   B 1 91  ? 45.877 -10.867 -6.261  1.00 13.21 ?  91  HIS   B CB   1 
ATOM   5024 C  CG   . HIS   B 1 91  ? 45.657 -9.466  -6.710  1.00 16.23 ?  91  HIS   B CG   1 
ATOM   5025 N  ND1  . HIS   B 1 91  ? 46.246 -8.383  -6.094  1.00 18.86 ?  91  HIS   B ND1  1 
ATOM   5026 C  CD2  . HIS   B 1 91  ? 44.884 -8.965  -7.697  1.00 18.42 ?  91  HIS   B CD2  1 
ATOM   5027 C  CE1  . HIS   B 1 91  ? 45.858 -7.271  -6.695  1.00 19.67 ?  91  HIS   B CE1  1 
ATOM   5028 N  NE2  . HIS   B 1 91  ? 45.026 -7.598  -7.669  1.00 19.68 ?  91  HIS   B NE2  1 
ATOM   5029 H  H    . HIS   B 1 91  ? 47.370 -11.881 -8.259  1.00 14.04 ?  91  HIS   B H    1 
ATOM   5030 H  HA   . HIS   B 1 91  ? 47.899 -10.789 -5.820  1.00 14.04 ?  91  HIS   B HA   1 
ATOM   5031 H  HB2  . HIS   B 1 91  ? 45.314 -11.442 -6.800  1.00 15.89 ?  91  HIS   B HB2  1 
ATOM   5032 H  HB3  . HIS   B 1 91  ? 45.606 -10.926 -5.328  1.00 15.89 ?  91  HIS   B HB3  1 
ATOM   5033 H  HD1  . HIS   B 1 91  ? 46.785 -8.422  -5.422  1.00 22.67 ?  91  HIS   B HD1  1 
ATOM   5034 H  HD2  . HIS   B 1 91  ? 44.361 -9.445  -8.291  1.00 22.14 ?  91  HIS   B HD2  1 
ATOM   5035 H  HE1  . HIS   B 1 91  ? 46.123 -6.406  -6.465  1.00 23.64 ?  91  HIS   B HE1  1 
ATOM   5036 N  N    . CYS   B 1 92  ? 47.522 -12.904 -4.560  1.00 10.91 ?  92  CYS   B N    1 
ATOM   5037 C  CA   . CYS   B 1 92  ? 47.222 -14.143 -3.853  1.00 10.61 ?  92  CYS   B CA   1 
ATOM   5038 C  C    . CYS   B 1 92  ? 46.004 -13.911 -2.968  1.00 10.17 ?  92  CYS   B C    1 
ATOM   5039 O  O    . CYS   B 1 92  ? 46.006 -13.013 -2.114  1.00 11.26 ?  92  CYS   B O    1 
ATOM   5040 C  CB   . CYS   B 1 92  ? 48.403 -14.604 -3.002  1.00 10.88 ?  92  CYS   B CB   1 
ATOM   5041 S  SG   . CYS   B 1 92  ? 48.050 -16.143 -2.110  1.00 11.09 ?  92  CYS   B SG   1 
ATOM   5042 H  H    . CYS   B 1 92  ? 47.836 -12.283 -4.050  1.00 13.13 ?  92  CYS   B H    1 
ATOM   5043 H  HA   . CYS   B 1 92  ? 47.018 -14.837 -4.497  1.00 12.77 ?  92  CYS   B HA   1 
ATOM   5044 H  HB2  . CYS   B 1 92  ? 49.166 -14.754 -3.574  1.00 13.10 ?  92  CYS   B HB2  1 
ATOM   5045 H  HB3  . CYS   B 1 92  ? 48.602 -13.917 -2.346  1.00 13.10 ?  92  CYS   B HB3  1 
ATOM   5046 H  HG   . CYS   B 1 92  ? 49.022 -16.455 -1.487  1.00 13.34 ?  92  CYS   B HG   1 
ATOM   5047 N  N    . LEU   B 1 93  ? 44.967 -14.716 -3.184  1.00 10.25 ?  93  LEU   B N    1 
ATOM   5048 C  CA   . LEU   B 1 93  ? 43.793 -14.738 -2.321  1.00 10.49 ?  93  LEU   B CA   1 
ATOM   5049 C  C    . LEU   B 1 93  ? 44.021 -15.805 -1.256  1.00 9.98  ?  93  LEU   B C    1 
ATOM   5050 O  O    . LEU   B 1 93  ? 43.973 -17.006 -1.551  1.00 10.73 ?  93  LEU   B O    1 
ATOM   5051 C  CB   . LEU   B 1 93  ? 42.536 -15.031 -3.135  1.00 10.79 ?  93  LEU   B CB   1 
ATOM   5052 C  CG   . LEU   B 1 93  ? 41.238 -15.045 -2.329  1.00 11.53 ?  93  LEU   B CG   1 
ATOM   5053 C  CD1  . LEU   B 1 93  ? 40.889 -13.655 -1.834  1.00 12.10 ?  93  LEU   B CD1  1 
ATOM   5054 C  CD2  . LEU   B 1 93  ? 40.113 -15.633 -3.167  1.00 11.80 ?  93  LEU   B CD2  1 
ATOM   5055 H  H    . LEU   B 1 93  ? 44.922 -15.285 -3.840  1.00 12.34 ?  93  LEU   B H    1 
ATOM   5056 H  HA   . LEU   B 1 93  ? 43.697 -13.878 -1.887  1.00 12.62 ?  93  LEU   B HA   1 
ATOM   5057 H  HB2  . LEU   B 1 93  ? 42.446 -14.344 -3.817  1.00 12.99 ?  93  LEU   B HB2  1 
ATOM   5058 H  HB3  . LEU   B 1 93  ? 42.630 -15.895 -3.552  1.00 12.99 ?  93  LEU   B HB3  1 
ATOM   5059 H  HG   . LEU   B 1 93  ? 41.353 -15.611 -1.552  1.00 13.87 ?  93  LEU   B HG   1 
ATOM   5060 H  HD11 . LEU   B 1 93  ? 40.032 -13.683 -1.388  1.00 14.56 ?  93  LEU   B HD11 1 
ATOM   5061 H  HD12 . LEU   B 1 93  ? 41.577 -13.360 -1.215  1.00 14.56 ?  93  LEU   B HD12 1 
ATOM   5062 H  HD13 . LEU   B 1 93  ? 40.850 -13.051 -2.594  1.00 14.56 ?  93  LEU   B HD13 1 
ATOM   5063 H  HD21 . LEU   B 1 93  ? 39.293 -15.631 -2.646  1.00 14.20 ?  93  LEU   B HD21 1 
ATOM   5064 H  HD22 . LEU   B 1 93  ? 39.995 -15.095 -3.966  1.00 14.20 ?  93  LEU   B HD22 1 
ATOM   5065 H  HD23 . LEU   B 1 93  ? 40.343 -16.543 -3.413  1.00 14.20 ?  93  LEU   B HD23 1 
ATOM   5066 N  N    . HIS   B 1 94  ? 44.304 -15.372 -0.033  1.00 10.00 ?  94  HIS   B N    1 
ATOM   5067 C  CA   . HIS   B 1 94  ? 44.522 -16.279 1.087   1.00 10.30 ?  94  HIS   B CA   1 
ATOM   5068 C  C    . HIS   B 1 94  ? 43.162 -16.635 1.669   1.00 10.55 ?  94  HIS   B C    1 
ATOM   5069 O  O    . HIS   B 1 94  ? 42.493 -15.765 2.228   1.00 11.81 ?  94  HIS   B O    1 
ATOM   5070 C  CB   . HIS   B 1 94  ? 45.395 -15.604 2.142   1.00 10.57 ?  94  HIS   B CB   1 
ATOM   5071 C  CG   . HIS   B 1 94  ? 46.774 -15.302 1.669   1.00 10.84 ?  94  HIS   B CG   1 
ATOM   5072 N  ND1  . HIS   B 1 94  ? 47.804 -16.214 1.748   1.00 10.93 ?  94  HIS   B ND1  1 
ATOM   5073 C  CD2  . HIS   B 1 94  ? 47.278 -14.192 1.080   1.00 10.85 ?  94  HIS   B CD2  1 
ATOM   5074 C  CE1  . HIS   B 1 94  ? 48.890 -15.662 1.238   1.00 10.82 ?  94  HIS   B CE1  1 
ATOM   5075 N  NE2  . HIS   B 1 94  ? 48.601 -14.436 0.832   1.00 10.85 ?  94  HIS   B NE2  1 
ATOM   5076 H  H    . HIS   B 1 94  ? 44.373 -14.538 0.174   1.00 12.04 ?  94  HIS   B H    1 
ATOM   5077 H  HA   . HIS   B 1 94  ? 44.956 -17.088 0.777   1.00 12.40 ?  94  HIS   B HA   1 
ATOM   5078 H  HB2  . HIS   B 1 94  ? 44.981 -14.770 2.404   1.00 12.72 ?  94  HIS   B HB2  1 
ATOM   5079 H  HB3  . HIS   B 1 94  ? 45.468 -16.196 2.906   1.00 12.72 ?  94  HIS   B HB3  1 
ATOM   5080 H  HD2  . HIS   B 1 94  ? 46.820 -13.407 0.888   1.00 13.05 ?  94  HIS   B HD2  1 
ATOM   5081 H  HE1  . HIS   B 1 94  ? 49.727 -16.073 1.177   1.00 13.02 ?  94  HIS   B HE1  1 
ATOM   5082 H  HE2  . HIS   B 1 94  ? 49.156 -13.893 0.462   1.00 13.05 ?  94  HIS   B HE2  1 
ATOM   5083 N  N    . VAL   B 1 95  ? 42.730 -17.889 1.514   1.00 10.53 ?  95  VAL   B N    1 
ATOM   5084 C  CA   . VAL   B 1 95  ? 41.405 -18.333 1.944   1.00 10.43 ?  95  VAL   B CA   1 
ATOM   5085 C  C    . VAL   B 1 95  ? 41.574 -19.373 3.038   1.00 10.72 ?  95  VAL   B C    1 
ATOM   5086 O  O    . VAL   B 1 95  ? 42.351 -20.321 2.878   1.00 11.33 ?  95  VAL   B O    1 
ATOM   5087 C  CB   . VAL   B 1 95  ? 40.586 -18.931 0.784   1.00 10.94 ?  95  VAL   B CB   1 
ATOM   5088 C  CG1  . VAL   B 1 95  ? 39.209 -19.391 1.272   1.00 12.21 ?  95  VAL   B CG1  1 
ATOM   5089 C  CG2  . VAL   B 1 95  ? 40.460 -17.947 -0.348  1.00 11.19 ?  95  VAL   B CG2  1 
ATOM   5090 H  H    . VAL   B 1 95  ? 43.198 -18.514 1.152   1.00 12.68 ?  95  VAL   B H    1 
ATOM   5091 H  HA   . VAL   B 1 95  ? 40.912 -17.583 2.309   1.00 12.56 ?  95  VAL   B HA   1 
ATOM   5092 H  HB   . VAL   B 1 95  ? 41.048 -19.712 0.444   1.00 13.17 ?  95  VAL   B HB   1 
ATOM   5093 H  HG11 . VAL   B 1 95  ? 38.646 -19.587 0.501   1.00 14.69 ?  95  VAL   B HG11 1 
ATOM   5094 H  HG12 . VAL   B 1 95  ? 39.307 -20.195 1.810   1.00 14.69 ?  95  VAL   B HG12 1 
ATOM   5095 H  HG13 . VAL   B 1 95  ? 38.802 -18.687 1.799   1.00 14.69 ?  95  VAL   B HG13 1 
ATOM   5096 H  HG21 . VAL   B 1 95  ? 39.884 -18.322 -1.030  1.00 13.46 ?  95  VAL   B HG21 1 
ATOM   5097 H  HG22 . VAL   B 1 95  ? 40.075 -17.124 -0.004  1.00 13.46 ?  95  VAL   B HG22 1 
ATOM   5098 H  HG23 . VAL   B 1 95  ? 41.341 -17.775 -0.711  1.00 13.46 ?  95  VAL   B HG23 1 
ATOM   5099 N  N    . VAL   B 1 96  ? 40.847 -19.205 4.138   1.00 11.03 ?  96  VAL   B N    1 
ATOM   5100 C  CA   . VAL   B 1 96  ? 40.933 -20.123 5.273   1.00 11.49 ?  96  VAL   B CA   1 
ATOM   5101 C  C    . VAL   B 1 96  ? 39.745 -21.083 5.220   1.00 11.83 ?  96  VAL   B C    1 
ATOM   5102 O  O    . VAL   B 1 96  ? 38.626 -20.728 5.596   1.00 12.61 ?  96  VAL   B O    1 
ATOM   5103 C  CB   . VAL   B 1 96  ? 40.979 -19.377 6.609   1.00 12.23 ?  96  VAL   B CB   1 
ATOM   5104 C  CG1  . VAL   B 1 96  ? 41.153 -20.365 7.749   1.00 12.86 ?  96  VAL   B CG1  1 
ATOM   5105 C  CG2  . VAL   B 1 96  ? 42.092 -18.333 6.621   1.00 13.00 ?  96  VAL   B CG2  1 
ATOM   5106 H  H    . VAL   B 1 96  ? 40.290 -18.563 4.252   1.00 13.27 ?  96  VAL   B H    1 
ATOM   5107 H  HA   . VAL   B 1 96  ? 41.747 -20.649 5.196   1.00 13.82 ?  96  VAL   B HA   1 
ATOM   5108 H  HB   . VAL   B 1 96  ? 40.135 -18.917 6.740   1.00 14.71 ?  96  VAL   B HB   1 
ATOM   5109 H  HG11 . VAL   B 1 96  ? 41.337 -19.873 8.567   1.00 15.47 ?  96  VAL   B HG11 1 
ATOM   5110 H  HG12 . VAL   B 1 96  ? 40.341 -20.882 7.853   1.00 15.47 ?  96  VAL   B HG12 1 
ATOM   5111 H  HG13 . VAL   B 1 96  ? 41.899 -20.953 7.547   1.00 15.47 ?  96  VAL   B HG13 1 
ATOM   5112 H  HG21 . VAL   B 1 96  ? 42.134 -17.921 7.501   1.00 15.64 ?  96  VAL   B HG21 1 
ATOM   5113 H  HG22 . VAL   B 1 96  ? 42.937 -18.760 6.417   1.00 15.64 ?  96  VAL   B HG22 1 
ATOM   5114 H  HG23 . VAL   B 1 96  ? 41.898 -17.651 5.953   1.00 15.64 ?  96  VAL   B HG23 1 
ATOM   5115 N  N    . GLY   B 1 97  ? 39.979 -22.316 4.782   1.00 11.98 ?  97  GLY   B N    1 
ATOM   5116 C  CA   . GLY   B 1 97  ? 39.001 -23.368 4.942   1.00 12.51 ?  97  GLY   B CA   1 
ATOM   5117 C  C    . GLY   B 1 97  ? 39.122 -23.978 6.320   1.00 13.36 ?  97  GLY   B C    1 
ATOM   5118 O  O    . GLY   B 1 97  ? 40.159 -23.851 6.984   1.00 14.00 ?  97  GLY   B O    1 
ATOM   5119 H  H    . GLY   B 1 97  ? 40.707 -22.563 4.389   1.00 14.42 ?  97  GLY   B H    1 
ATOM   5120 H  HA2  . GLY   B 1 97  ? 38.109 -22.996 4.827   1.00 15.05 ?  97  GLY   B HA2  1 
ATOM   5121 H  HA3  . GLY   B 1 97  ? 39.142 -24.052 4.269   1.00 15.05 ?  97  GLY   B HA3  1 
ATOM   5122 N  N    . PRO   B 1 98  ? 38.075 -24.664 6.776   1.00 14.23 ?  98  PRO   B N    1 
ATOM   5123 C  CA   . PRO   B 1 98  ? 38.165 -25.364 8.061   1.00 14.82 ?  98  PRO   B CA   1 
ATOM   5124 C  C    . PRO   B 1 98  ? 39.191 -26.485 8.015   1.00 14.68 ?  98  PRO   B C    1 
ATOM   5125 O  O    . PRO   B 1 98  ? 39.293 -27.222 7.034   1.00 14.50 ?  98  PRO   B O    1 
ATOM   5126 C  CB   . PRO   B 1 98  ? 36.750 -25.915 8.261   1.00 14.87 ?  98  PRO   B CB   1 
ATOM   5127 C  CG   . PRO   B 1 98  ? 36.197 -26.043 6.884   1.00 14.45 ?  98  PRO   B CG   1 
ATOM   5128 C  CD   . PRO   B 1 98  ? 36.761 -24.858 6.137   1.00 14.01 ?  98  PRO   B CD   1 
ATOM   5129 H  HA   . PRO   B 1 98  ? 38.384 -24.748 8.771   1.00 17.83 ?  98  PRO   B HA   1 
ATOM   5130 H  HB2  . PRO   B 1 98  ? 36.793 -26.784 8.696   1.00 17.88 ?  98  PRO   B HB2  1 
ATOM   5131 H  HB3  . PRO   B 1 98  ? 36.226 -25.293 8.785   1.00 17.88 ?  98  PRO   B HB3  1 
ATOM   5132 H  HG2  . PRO   B 1 98  ? 36.498 -26.878 6.487   1.00 17.38 ?  98  PRO   B HG2  1 
ATOM   5133 H  HG3  . PRO   B 1 98  ? 35.230 -26.005 6.914   1.00 17.38 ?  98  PRO   B HG3  1 
ATOM   5134 H  HD2  . PRO   B 1 98  ? 36.864 -25.074 5.192   1.00 16.85 ?  98  PRO   B HD2  1 
ATOM   5135 H  HD3  . PRO   B 1 98  ? 36.205 -24.078 6.265   1.00 16.85 ?  98  PRO   B HD3  1 
ATOM   5136 N  N    . ASN   B 1 99  ? 39.946 -26.612 9.101   1.00 15.84 ?  99  ASN   B N    1 
ATOM   5137 C  CA   . ASN   B 1 99  ? 40.920 -27.685 9.265   1.00 16.67 ?  99  ASN   B CA   1 
ATOM   5138 C  C    . ASN   B 1 99  ? 40.286 -28.771 10.135  1.00 18.60 ?  99  ASN   B C    1 
ATOM   5139 O  O    . ASN   B 1 99  ? 40.199 -28.630 11.356  1.00 19.26 ?  99  ASN   B O    1 
ATOM   5140 C  CB   . ASN   B 1 99  ? 42.191 -27.130 9.895   1.00 16.77 ?  99  ASN   B CB   1 
ATOM   5141 C  CG   . ASN   B 1 99  ? 43.326 -28.129 9.892   1.00 17.57 ?  99  ASN   B CG   1 
ATOM   5142 O  OD1  . ASN   B 1 99  ? 43.108 -29.324 10.048  1.00 18.52 ?  99  ASN   B OD1  1 
ATOM   5143 N  ND2  . ASN   B 1 99  ? 44.544 -27.645 9.709   1.00 17.66 ?  99  ASN   B ND2  1 
ATOM   5144 H  H    . ASN   B 1 99  ? 39.909 -26.075 9.770   1.00 19.05 ?  99  ASN   B H    1 
ATOM   5145 H  HA   . ASN   B 1 99  ? 41.136 -28.071 8.406   1.00 20.04 ?  99  ASN   B HA   1 
ATOM   5146 H  HB2  . ASN   B 1 99  ? 42.470 -26.352 9.399   1.00 20.16 ?  99  ASN   B HB2  1 
ATOM   5147 H  HB3  . ASN   B 1 99  ? 42.002 -26.890 10.819  1.00 20.16 ?  99  ASN   B HB3  1 
ATOM   5148 H  HD21 . ASN   B 1 99  ? 45.218 -28.174 9.700   1.00 21.23 ?  99  ASN   B HD21 1 
ATOM   5149 H  HD22 . ASN   B 1 99  ? 44.653 -26.799 9.608   1.00 21.23 ?  99  ASN   B HD22 1 
ATOM   5150 N  N    A VAL   B 1 100 ? 39.832 -29.853 9.495   0.82 20.47 ?  100 VAL   B N    1 
ATOM   5151 N  N    B VAL   B 1 100 ? 39.840 -29.857 9.494   0.18 20.45 ?  100 VAL   B N    1 
ATOM   5152 C  CA   A VAL   B 1 100 ? 39.216 -30.956 10.231  0.82 22.99 ?  100 VAL   B CA   1 
ATOM   5153 C  CA   B VAL   B 1 100 ? 39.222 -30.961 10.226  0.18 22.41 ?  100 VAL   B CA   1 
ATOM   5154 C  C    A VAL   B 1 100 ? 40.220 -31.617 11.169  0.82 23.37 ?  100 VAL   B C    1 
ATOM   5155 C  C    B VAL   B 1 100 ? 40.222 -31.612 11.170  0.18 23.16 ?  100 VAL   B C    1 
ATOM   5156 O  O    A VAL   B 1 100 ? 39.845 -32.124 12.233  0.82 24.20 ?  100 VAL   B O    1 
ATOM   5157 O  O    B VAL   B 1 100 ? 39.848 -32.097 12.245  0.18 23.41 ?  100 VAL   B O    1 
ATOM   5158 C  CB   A VAL   B 1 100 ? 38.579 -31.963 9.250   0.82 25.40 ?  100 VAL   B CB   1 
ATOM   5159 C  CB   B VAL   B 1 100 ? 38.605 -31.976 9.241   0.18 23.59 ?  100 VAL   B CB   1 
ATOM   5160 C  CG1  A VAL   B 1 100 ? 38.100 -33.206 9.985   0.82 26.27 ?  100 VAL   B CG1  1 
ATOM   5161 C  CG1  B VAL   B 1 100 ? 38.068 -33.194 9.982   0.18 23.98 ?  100 VAL   B CG1  1 
ATOM   5162 C  CG2  A VAL   B 1 100 ? 37.424 -31.313 8.498   0.82 25.85 ?  100 VAL   B CG2  1 
ATOM   5163 C  CG2  B VAL   B 1 100 ? 37.500 -31.316 8.432   0.18 23.94 ?  100 VAL   B CG2  1 
ATOM   5164 H  H    A VAL   B 1 100 ? 39.859 -29.964 8.641   0.82 24.60 ?  100 VAL   B H    1 
ATOM   5165 H  H    B VAL   B 1 100 ? 39.883 -29.975 8.646   0.18 24.58 ?  100 VAL   B H    1 
ATOM   5166 H  HA   A VAL   B 1 100 ? 38.498 -30.599 10.776  0.82 27.62 ?  100 VAL   B HA   1 
ATOM   5167 H  HA   B VAL   B 1 100 ? 38.499 -30.610 10.766  0.18 26.93 ?  100 VAL   B HA   1 
ATOM   5168 H  HB   A VAL   B 1 100 ? 39.243 -32.241 8.601   0.82 30.52 ?  100 VAL   B HB   1 
ATOM   5169 H  HB   B VAL   B 1 100 ? 39.288 -32.281 8.625   0.18 28.34 ?  100 VAL   B HB   1 
ATOM   5170 H  HG11 A VAL   B 1 100 ? 37.513 -33.713 9.399   0.82 31.56 ?  100 VAL   B HG11 1 
ATOM   5171 H  HG11 B VAL   B 1 100 ? 37.505 -33.707 9.379   0.18 28.81 ?  100 VAL   B HG11 1 
ATOM   5172 H  HG12 A VAL   B 1 100 ? 38.866 -33.749 10.229  0.82 31.56 ?  100 VAL   B HG12 1 
ATOM   5173 H  HG12 B VAL   B 1 100 ? 38.812 -33.740 10.280  0.18 28.81 ?  100 VAL   B HG12 1 
ATOM   5174 H  HG13 A VAL   B 1 100 ? 37.615 -32.937 10.781  0.82 31.56 ?  100 VAL   B HG13 1 
ATOM   5175 H  HG13 B VAL   B 1 100 ? 37.546 -32.896 10.744  0.18 28.81 ?  100 VAL   B HG13 1 
ATOM   5176 H  HG21 A VAL   B 1 100 ? 37.038 -31.963 7.887   0.82 31.06 ?  100 VAL   B HG21 1 
ATOM   5177 H  HG21 B VAL   B 1 100 ? 37.104 -31.976 7.842   0.18 28.77 ?  100 VAL   B HG21 1 
ATOM   5178 H  HG22 A VAL   B 1 100 ? 36.752 -31.025 9.137   0.82 31.06 ?  100 VAL   B HG22 1 
ATOM   5179 H  HG22 B VAL   B 1 100 ? 36.828 -30.971 9.041   0.18 28.77 ?  100 VAL   B HG22 1 
ATOM   5180 H  HG23 A VAL   B 1 100 ? 37.759 -30.552 8.002   0.82 31.06 ?  100 VAL   B HG23 1 
ATOM   5181 H  HG23 B VAL   B 1 100 ? 37.881 -30.592 7.913   0.18 28.77 ?  100 VAL   B HG23 1 
ATOM   5182 N  N    . ASN   B 1 101 ? 41.502 -31.640 10.792  1.00 23.71 ?  101 ASN   B N    1 
ATOM   5183 C  CA   . ASN   B 1 101 ? 42.536 -32.172 11.677  1.00 25.78 ?  101 ASN   B CA   1 
ATOM   5184 C  C    . ASN   B 1 101 ? 42.717 -31.335 12.937  1.00 27.88 ?  101 ASN   B C    1 
ATOM   5185 O  O    . ASN   B 1 101 ? 43.370 -31.800 13.880  1.00 29.01 ?  101 ASN   B O    1 
ATOM   5186 C  CB   . ASN   B 1 101 ? 43.868 -32.296 10.932  1.00 25.96 ?  101 ASN   B CB   1 
ATOM   5187 C  CG   . ASN   B 1 101 ? 43.871 -33.439 9.937   1.00 25.69 ?  101 ASN   B CG   1 
ATOM   5188 O  OD1  . ASN   B 1 101 ? 43.220 -34.455 10.151  1.00 26.53 ?  101 ASN   B OD1  1 
ATOM   5189 N  ND2  . ASN   B 1 101 ? 44.595 -33.270 8.836   1.00 25.24 ?  101 ASN   B ND2  1 
ATOM   5190 H  H    A ASN   B 1 101 ? 41.789 -31.368 10.029  0.82 28.49 ?  101 ASN   B H    1 
ATOM   5191 H  H    B ASN   B 1 101 ? 41.789 -31.365 10.030  0.18 28.49 ?  101 ASN   B H    1 
ATOM   5192 H  HA   . ASN   B 1 101 ? 42.274 -33.059 11.957  1.00 30.97 ?  101 ASN   B HA   1 
ATOM   5193 H  HB2  . ASN   B 1 101 ? 44.046 -31.477 10.444  1.00 31.19 ?  101 ASN   B HB2  1 
ATOM   5194 H  HB3  . ASN   B 1 101 ? 44.578 -32.457 11.575  1.00 31.19 ?  101 ASN   B HB3  1 
ATOM   5195 H  HD21 . ASN   B 1 101 ? 44.629 -33.893 8.243   1.00 30.33 ?  101 ASN   B HD21 1 
ATOM   5196 H  HD22 . ASN   B 1 101 ? 45.032 -32.540 8.716   1.00 30.33 ?  101 ASN   B HD22 1 
ATOM   5197 N  N    . LYS   B 1 102 ? 42.165 -30.120 12.970  1.00 30.05 ?  102 LYS   B N    1 
ATOM   5198 C  CA   . LYS   B 1 102 ? 42.135 -29.286 14.165  1.00 32.53 ?  102 LYS   B CA   1 
ATOM   5199 C  C    . LYS   B 1 102 ? 40.751 -29.238 14.799  1.00 32.01 ?  102 LYS   B C    1 
ATOM   5200 O  O    . LYS   B 1 102 ? 40.522 -28.428 15.704  1.00 32.83 ?  102 LYS   B O    1 
ATOM   5201 C  CB   . LYS   B 1 102 ? 42.583 -27.860 13.836  1.00 35.86 ?  102 LYS   B CB   1 
ATOM   5202 C  CG   . LYS   B 1 102 ? 44.047 -27.713 13.465  1.00 38.96 ?  102 LYS   B CG   1 
ATOM   5203 C  CD   . LYS   B 1 102 ? 44.331 -26.287 13.014  1.00 41.80 ?  102 LYS   B CD   1 
ATOM   5204 C  CE   . LYS   B 1 102 ? 45.815 -26.036 12.807  1.00 43.97 ?  102 LYS   B CE   1 
ATOM   5205 N  NZ   . LYS   B 1 102 ? 46.067 -24.641 12.339  1.00 45.20 ?  102 LYS   B NZ   1 
ATOM   5206 H  H    . LYS   B 1 102 ? 41.784 -29.750 12.292  1.00 36.10 ?  102 LYS   B H    1 
ATOM   5207 H  HA   . LYS   B 1 102 ? 42.757 -29.648 14.814  1.00 39.07 ?  102 LYS   B HA   1 
ATOM   5208 H  HB2  . LYS   B 1 102 ? 42.057 -27.536 13.089  1.00 43.07 ?  102 LYS   B HB2  1 
ATOM   5209 H  HB3  . LYS   B 1 102 ? 42.421 -27.300 14.613  1.00 43.07 ?  102 LYS   B HB3  1 
ATOM   5210 H  HG2  . LYS   B 1 102 ? 44.600 -27.908 14.238  1.00 46.79 ?  102 LYS   B HG2  1 
ATOM   5211 H  HG3  . LYS   B 1 102 ? 44.259 -28.315 12.735  1.00 46.79 ?  102 LYS   B HG3  1 
ATOM   5212 H  HD2  . LYS   B 1 102 ? 43.876 -26.123 12.173  1.00 50.20 ?  102 LYS   B HD2  1 
ATOM   5213 H  HD3  . LYS   B 1 102 ? 44.011 -25.670 13.691  1.00 50.20 ?  102 LYS   B HD3  1 
ATOM   5214 H  HE2  . LYS   B 1 102 ? 46.283 -26.165 13.647  1.00 52.81 ?  102 LYS   B HE2  1 
ATOM   5215 H  HE3  . LYS   B 1 102 ? 46.154 -26.649 12.136  1.00 52.81 ?  102 LYS   B HE3  1 
ATOM   5216 H  HZ1  . LYS   B 1 102 ? 46.939 -24.512 12.223  1.00 54.28 ?  102 LYS   B HZ1  1 
ATOM   5217 H  HZ2  . LYS   B 1 102 ? 45.648 -24.500 11.566  1.00 54.28 ?  102 LYS   B HZ2  1 
ATOM   5218 H  HZ3  . LYS   B 1 102 ? 45.765 -24.059 12.942  1.00 54.28 ?  102 LYS   B HZ3  1 
ATOM   5219 N  N    . GLY   B 1 103 ? 39.817 -30.066 14.336  1.00 30.93 ?  103 GLY   B N    1 
ATOM   5220 C  CA   . GLY   B 1 103 ? 38.486 -30.110 14.906  1.00 30.21 ?  103 GLY   B CA   1 
ATOM   5221 C  C    . GLY   B 1 103 ? 37.552 -29.017 14.444  1.00 28.88 ?  103 GLY   B C    1 
ATOM   5222 O  O    . GLY   B 1 103 ? 36.460 -28.879 15.008  1.00 29.45 ?  103 GLY   B O    1 
ATOM   5223 H  H    . GLY   B 1 103 ? 39.933 -30.611 13.684  1.00 37.15 ?  103 GLY   B H    1 
ATOM   5224 H  HA2  . GLY   B 1 103 ? 38.076 -30.959 14.682  1.00 36.29 ?  103 GLY   B HA2  1 
ATOM   5225 H  HA3  . GLY   B 1 103 ? 38.556 -30.059 15.874  1.00 36.29 ?  103 GLY   B HA3  1 
ATOM   5226 N  N    A GLU   B 1 104 ? 37.937 -28.241 13.435  0.82 27.09 ?  104 GLU   B N    1 
ATOM   5227 N  N    B GLU   B 1 104 ? 37.933 -28.240 13.437  0.18 28.59 ?  104 GLU   B N    1 
ATOM   5228 C  CA   A GLU   B 1 104 ? 37.112 -27.137 12.975  0.82 25.32 ?  104 GLU   B CA   1 
ATOM   5229 C  CA   B GLU   B 1 104 ? 37.092 -27.151 12.966  0.18 28.09 ?  104 GLU   B CA   1 
ATOM   5230 C  C    A GLU   B 1 104 ? 35.937 -27.653 12.150  0.82 26.15 ?  104 GLU   B C    1 
ATOM   5231 C  C    B GLU   B 1 104 ? 35.940 -27.689 12.125  0.18 28.14 ?  104 GLU   B C    1 
ATOM   5232 O  O    A GLU   B 1 104 ? 35.987 -28.737 11.560  0.82 26.95 ?  104 GLU   B O    1 
ATOM   5233 O  O    B GLU   B 1 104 ? 36.038 -28.746 11.494  0.18 28.31 ?  104 GLU   B O    1 
ATOM   5234 C  CB   A GLU   B 1 104 ? 37.960 -26.144 12.180  0.82 23.53 ?  104 GLU   B CB   1 
ATOM   5235 C  CB   B GLU   B 1 104 ? 37.927 -26.149 12.171  0.18 27.55 ?  104 GLU   B CB   1 
ATOM   5236 C  CG   A GLU   B 1 104 ? 39.073 -25.548 13.026  0.82 22.16 ?  104 GLU   B CG   1 
ATOM   5237 C  CG   B GLU   B 1 104 ? 39.023 -25.505 13.009  0.18 27.09 ?  104 GLU   B CG   1 
ATOM   5238 C  CD   A GLU   B 1 104 ? 40.003 -24.633 12.262  0.82 21.00 ?  104 GLU   B CD   1 
ATOM   5239 C  CD   B GLU   B 1 104 ? 39.953 -24.626 12.197  0.18 26.71 ?  104 GLU   B CD   1 
ATOM   5240 O  OE1  A GLU   B 1 104 ? 40.011 -24.654 11.013  0.82 19.25 ?  104 GLU   B OE1  1 
ATOM   5241 O  OE1  B GLU   B 1 104 ? 39.867 -24.649 10.951  0.18 26.42 ?  104 GLU   B OE1  1 
ATOM   5242 O  OE2  A GLU   B 1 104 ? 40.734 -23.882 12.934  0.82 21.88 -1 104 GLU   B OE2  1 
ATOM   5243 O  OE2  B GLU   B 1 104 ? 40.773 -23.911 12.809  0.18 26.77 -1 104 GLU   B OE2  1 
ATOM   5244 H  H    A GLU   B 1 104 ? 38.676 -28.333 13.005  0.82 32.55 ?  104 GLU   B H    1 
ATOM   5245 H  H    B GLU   B 1 104 ? 38.676 -28.322 13.012  0.18 34.34 ?  104 GLU   B H    1 
ATOM   5246 H  HA   A GLU   B 1 104 ? 36.757 -26.670 13.748  0.82 30.42 ?  104 GLU   B HA   1 
ATOM   5247 H  HA   B GLU   B 1 104 ? 36.717 -26.686 13.730  0.18 33.74 ?  104 GLU   B HA   1 
ATOM   5248 H  HB2  A GLU   B 1 104 ? 38.364 -26.599 11.426  0.82 28.27 ?  104 GLU   B HB2  1 
ATOM   5249 H  HB2  B GLU   B 1 104 ? 38.349 -26.607 11.427  0.18 33.10 ?  104 GLU   B HB2  1 
ATOM   5250 H  HB3  A GLU   B 1 104 ? 37.395 -25.418 11.871  0.82 28.27 ?  104 GLU   B HB3  1 
ATOM   5251 H  HB3  B GLU   B 1 104 ? 37.348 -25.443 11.842  0.18 33.10 ?  104 GLU   B HB3  1 
ATOM   5252 H  HG2  A GLU   B 1 104 ? 38.682 -25.024 13.744  0.82 26.63 ?  104 GLU   B HG2  1 
ATOM   5253 H  HG2  B GLU   B 1 104 ? 38.612 -24.954 13.695  0.18 32.55 ?  104 GLU   B HG2  1 
ATOM   5254 H  HG3  A GLU   B 1 104 ? 39.610 -26.264 13.400  0.82 26.63 ?  104 GLU   B HG3  1 
ATOM   5255 H  HG3  B GLU   B 1 104 ? 39.554 -26.203 13.426  0.18 32.55 ?  104 GLU   B HG3  1 
ATOM   5256 N  N    A ASP   B 1 105 ? 34.866 -26.863 12.129  0.82 26.37 ?  105 ASP   B N    1 
ATOM   5257 N  N    B ASP   B 1 105 ? 34.836 -26.944 12.126  0.18 27.97 ?  105 ASP   B N    1 
ATOM   5258 C  CA   A ASP   B 1 105 ? 33.592 -27.320 11.590  0.82 27.24 ?  105 ASP   B CA   1 
ATOM   5259 C  CA   B ASP   B 1 105 ? 33.588 -27.429 11.550  0.18 27.91 ?  105 ASP   B CA   1 
ATOM   5260 C  C    A ASP   B 1 105 ? 33.646 -27.369 10.067  0.82 25.57 ?  105 ASP   B C    1 
ATOM   5261 C  C    B ASP   B 1 105 ? 33.676 -27.443 10.028  0.18 27.13 ?  105 ASP   B C    1 
ATOM   5262 O  O    A ASP   B 1 105 ? 33.795 -26.336 9.406   0.82 24.56 ?  105 ASP   B O    1 
ATOM   5263 O  O    B ASP   B 1 105 ? 33.923 -26.408 9.400   0.18 26.88 ?  105 ASP   B O    1 
ATOM   5264 C  CB   A ASP   B 1 105 ? 32.474 -26.389 12.057  0.82 30.11 ?  105 ASP   B CB   1 
ATOM   5265 C  CB   B ASP   B 1 105 ? 32.432 -26.544 12.011  0.18 28.53 ?  105 ASP   B CB   1 
ATOM   5266 C  CG   A ASP   B 1 105 ? 31.097 -26.880 11.651  0.82 32.49 ?  105 ASP   B CG   1 
ATOM   5267 C  CG   B ASP   B 1 105 ? 31.076 -27.142 11.686  0.18 29.11 ?  105 ASP   B CG   1 
ATOM   5268 O  OD1  A ASP   B 1 105 ? 31.007 -27.939 10.992  0.82 32.64 ?  105 ASP   B OD1  1 
ATOM   5269 O  OD1  B ASP   B 1 105 ? 31.032 -28.167 10.972  0.18 29.26 ?  105 ASP   B OD1  1 
ATOM   5270 O  OD2  A ASP   B 1 105 ? 30.100 -26.209 11.995  0.82 33.98 -1 105 ASP   B OD2  1 
ATOM   5271 O  OD2  B ASP   B 1 105 ? 30.054 -26.595 12.150  0.18 29.32 -1 105 ASP   B OD2  1 
ATOM   5272 H  H    A ASP   B 1 105 ? 34.856 -26.053 12.418  0.82 31.68 ?  105 ASP   B H    1 
ATOM   5273 H  H    B ASP   B 1 105 ? 34.786 -26.152 12.452  0.18 33.61 ?  105 ASP   B H    1 
ATOM   5274 H  HA   A ASP   B 1 105 ? 33.401 -28.212 11.920  0.82 32.72 ?  105 ASP   B HA   1 
ATOM   5275 H  HA   B ASP   B 1 105 ? 33.418 -28.334 11.855  0.18 33.53 ?  105 ASP   B HA   1 
ATOM   5276 H  HB2  A ASP   B 1 105 ? 32.507 -26.315 13.027  0.82 36.17 ?  105 ASP   B HB2  1 
ATOM   5277 H  HB2  B ASP   B 1 105 ? 32.487 -26.427 12.974  0.18 34.27 ?  105 ASP   B HB2  1 
ATOM   5278 H  HB3  A ASP   B 1 105 ? 32.604 -25.513 11.658  0.82 36.17 ?  105 ASP   B HB3  1 
ATOM   5279 H  HB3  B ASP   B 1 105 ? 32.497 -25.681 11.571  0.18 34.27 ?  105 ASP   B HB3  1 
ATOM   5280 N  N    A ILE   B 1 106 ? 33.508 -28.576 9.510   0.82 25.03 ?  106 ILE   B N    1 
ATOM   5281 N  N    B ILE   B 1 106 ? 33.468 -28.623 9.437   0.18 26.49 ?  106 ILE   B N    1 
ATOM   5282 C  CA   A ILE   B 1 106 ? 33.499 -28.754 8.063   0.82 23.85 ?  106 ILE   B CA   1 
ATOM   5283 C  CA   B ILE   B 1 106 ? 33.484 -28.766 7.986   0.18 25.87 ?  106 ILE   B CA   1 
ATOM   5284 C  C    A ILE   B 1 106 ? 32.399 -27.931 7.397   0.82 22.74 ?  106 ILE   B C    1 
ATOM   5285 C  C    B ILE   B 1 106 ? 32.387 -27.941 7.323   0.18 25.24 ?  106 ILE   B C    1 
ATOM   5286 O  O    A ILE   B 1 106 ? 32.502 -27.608 6.209   0.82 21.97 ?  106 ILE   B O    1 
ATOM   5287 O  O    B ILE   B 1 106 ? 32.474 -27.645 6.126   0.18 25.11 ?  106 ILE   B O    1 
ATOM   5288 C  CB   A ILE   B 1 106 ? 33.399 -30.263 7.737   0.82 24.81 ?  106 ILE   B CB   1 
ATOM   5289 C  CB   B ILE   B 1 106 ? 33.390 -30.263 7.611   0.18 25.99 ?  106 ILE   B CB   1 
ATOM   5290 C  CG1  A ILE   B 1 106 ? 33.632 -30.519 6.247   0.82 25.38 ?  106 ILE   B CG1  1 
ATOM   5291 C  CG1  B ILE   B 1 106 ? 33.648 -30.473 6.116   0.18 26.03 ?  106 ILE   B CG1  1 
ATOM   5292 C  CG2  A ILE   B 1 106 ? 32.049 -30.822 8.176   0.82 25.70 ?  106 ILE   B CG2  1 
ATOM   5293 C  CG2  B ILE   B 1 106 ? 32.034 -30.832 8.004   0.18 26.18 ?  106 ILE   B CG2  1 
ATOM   5294 C  CD1  A ILE   B 1 106 ? 34.990 -30.063 5.765   0.82 25.54 ?  106 ILE   B CD1  1 
ATOM   5295 C  CD1  B ILE   B 1 106 ? 35.009 -29.993 5.660   0.18 26.05 ?  106 ILE   B CD1  1 
ATOM   5296 H  H    A ILE   B 1 106 ? 33.424 -29.304 9.957   0.82 30.07 ?  106 ILE   B H    1 
ATOM   5297 H  H    B ILE   B 1 106 ? 33.328 -29.357 9.859   0.18 31.83 ?  106 ILE   B H    1 
ATOM   5298 H  HA   A ILE   B 1 106 ? 34.343 -28.436 7.719   0.82 28.65 ?  106 ILE   B HA   1 
ATOM   5299 H  HA   B ILE   B 1 106 ? 34.332 -28.434 7.662   0.18 31.08 ?  106 ILE   B HA   1 
ATOM   5300 H  HB   A ILE   B 1 106 ? 34.090 -30.729 8.235   0.82 29.81 ?  106 ILE   B HB   1 
ATOM   5301 H  HB   B ILE   B 1 106 ? 34.072 -30.742 8.104   0.18 31.23 ?  106 ILE   B HB   1 
ATOM   5302 H  HG12 A ILE   B 1 106 ? 33.566 -31.475 6.080   0.82 30.49 ?  106 ILE   B HG12 1 
ATOM   5303 H  HG12 B ILE   B 1 106 ? 33.592 -31.423 5.920   0.18 31.27 ?  106 ILE   B HG12 1 
ATOM   5304 H  HG13 A ILE   B 1 106 ? 32.959 -30.050 5.735   0.82 30.49 ?  106 ILE   B HG13 1 
ATOM   5305 H  HG13 B ILE   B 1 106 ? 32.977 -29.995 5.607   0.18 31.27 ?  106 ILE   B HG13 1 
ATOM   5306 H  HG21 A ILE   B 1 106 ? 32.058 -31.787 8.075   0.82 30.88 ?  106 ILE   B HG21 1 
ATOM   5307 H  HG21 B ILE   B 1 106 ? 32.048 -31.794 7.880   0.18 31.46 ?  106 ILE   B HG21 1 
ATOM   5308 H  HG22 A ILE   B 1 106 ? 31.899 -30.590 9.107   0.82 30.88 ?  106 ILE   B HG22 1 
ATOM   5309 H  HG22 B ILE   B 1 106 ? 31.862 -30.623 8.936   0.18 31.46 ?  106 ILE   B HG22 1 
ATOM   5310 H  HG23 A ILE   B 1 106 ? 31.351 -30.438 7.624   0.82 30.88 ?  106 ILE   B HG23 1 
ATOM   5311 H  HG23 B ILE   B 1 106 ? 31.348 -30.437 7.445   0.18 31.46 ?  106 ILE   B HG23 1 
ATOM   5312 H  HD11 A ILE   B 1 106 ? 35.172 -30.469 4.904   0.82 30.69 ?  106 ILE   B HD11 1 
ATOM   5313 H  HD11 B ILE   B 1 106 ? 35.199 -30.369 4.788   0.18 31.30 ?  106 ILE   B HD11 1 
ATOM   5314 H  HD12 A ILE   B 1 106 ? 34.988 -29.097 5.681   0.82 30.69 ?  106 ILE   B HD12 1 
ATOM   5315 H  HD12 B ILE   B 1 106 ? 35.000 -29.024 5.608   0.18 31.30 ?  106 ILE   B HD12 1 
ATOM   5316 H  HD13 A ILE   B 1 106 ? 35.664 -30.339 6.408   0.82 30.69 ?  106 ILE   B HD13 1 
ATOM   5317 H  HD13 B ILE   B 1 106 ? 35.677 -30.285 6.300   0.18 31.30 ?  106 ILE   B HD13 1 
ATOM   5318 N  N    A GLN   B 1 107 ? 31.353 -27.566 8.140   0.82 23.43 ?  107 GLN   B N    1 
ATOM   5319 N  N    B GLN   B 1 107 ? 31.352 -27.557 8.074   0.18 24.91 ?  107 GLN   B N    1 
ATOM   5320 C  CA   A GLN   B 1 107 ? 30.275 -26.761 7.571   0.82 23.87 ?  107 GLN   B CA   1 
ATOM   5321 C  CA   B GLN   B 1 107 ? 30.273 -26.754 7.510   0.18 24.53 ?  107 GLN   B CA   1 
ATOM   5322 C  C    A GLN   B 1 107 ? 30.763 -25.411 7.055   0.82 21.91 ?  107 GLN   B C    1 
ATOM   5323 C  C    B GLN   B 1 107 ? 30.756 -25.385 7.046   0.18 22.23 ?  107 GLN   B C    1 
ATOM   5324 O  O    A GLN   B 1 107 ? 30.124 -24.832 6.173   0.82 22.62 ?  107 GLN   B O    1 
ATOM   5325 O  O    B GLN   B 1 107 ? 30.096 -24.760 6.209   0.18 22.35 ?  107 GLN   B O    1 
ATOM   5326 C  CB   A GLN   B 1 107 ? 29.173 -26.567 8.618   0.82 27.35 ?  107 GLN   B CB   1 
ATOM   5327 C  CB   B GLN   B 1 107 ? 29.152 -26.600 8.543   0.18 26.54 ?  107 GLN   B CB   1 
ATOM   5328 C  CG   A GLN   B 1 107 ? 27.838 -26.094 8.057   0.82 31.16 ?  107 GLN   B CG   1 
ATOM   5329 C  CG   B GLN   B 1 107 ? 27.824 -26.114 7.978   0.18 28.41 ?  107 GLN   B CG   1 
ATOM   5330 C  CD   A GLN   B 1 107 ? 27.751 -24.583 7.927   0.82 34.05 ?  107 GLN   B CD   1 
ATOM   5331 C  CD   B GLN   B 1 107 ? 27.707 -24.602 7.963   0.18 29.89 ?  107 GLN   B CD   1 
ATOM   5332 O  OE1  A GLN   B 1 107 ? 28.579 -23.851 8.475   0.82 35.18 ?  107 GLN   B OE1  1 
ATOM   5333 O  OE1  B GLN   B 1 107 ? 28.526 -23.895 8.553   0.18 30.44 ?  107 GLN   B OE1  1 
ATOM   5334 N  NE2  A GLN   B 1 107 ? 26.742 -24.108 7.201   0.82 35.07 ?  107 GLN   B NE2  1 
ATOM   5335 N  NE2  B GLN   B 1 107 ? 26.680 -24.096 7.289   0.18 30.39 ?  107 GLN   B NE2  1 
ATOM   5336 H  H    A GLN   B 1 107 ? 31.246 -27.767 8.966   0.82 28.15 ?  107 GLN   B H    1 
ATOM   5337 H  H    B GLN   B 1 107 ? 31.250 -27.751 8.903   0.18 29.93 ?  107 GLN   B H    1 
ATOM   5338 H  HA   A GLN   B 1 107 ? 29.888 -27.245 6.822   0.82 28.68 ?  107 GLN   B HA   1 
ATOM   5339 H  HA   B GLN   B 1 107 ? 29.905 -27.219 6.743   0.18 29.47 ?  107 GLN   B HA   1 
ATOM   5340 H  HB2  A GLN   B 1 107 ? 29.018 -27.414 9.062   0.82 32.85 ?  107 GLN   B HB2  1 
ATOM   5341 H  HB2  B GLN   B 1 107 ? 28.993 -27.462 8.954   0.18 31.89 ?  107 GLN   B HB2  1 
ATOM   5342 H  HB3  A GLN   B 1 107 ? 29.473 -25.910 9.265   0.82 32.85 ?  107 GLN   B HB3  1 
ATOM   5343 H  HB3  B GLN   B 1 107 ? 29.436 -25.966 9.220   0.18 31.89 ?  107 GLN   B HB3  1 
ATOM   5344 H  HG2  A GLN   B 1 107 ? 27.709 -26.475 7.175   0.82 37.43 ?  107 GLN   B HG2  1 
ATOM   5345 H  HG2  B GLN   B 1 107 ? 27.732 -26.429 7.066   0.18 34.13 ?  107 GLN   B HG2  1 
ATOM   5346 H  HG3  A GLN   B 1 107 ? 27.124 -26.389 8.649   0.82 37.43 ?  107 GLN   B HG3  1 
ATOM   5347 H  HG3  B GLN   B 1 107 ? 27.100 -26.468 8.523   0.18 34.13 ?  107 GLN   B HG3  1 
ATOM   5348 H  HE21 A GLN   B 1 107 ? 26.184 -24.650 6.830   0.82 42.12 ?  107 GLN   B HE21 1 
ATOM   5349 H  HE21 B GLN   B 1 107 ? 26.128 -24.621 6.888   0.18 36.51 ?  107 GLN   B HE21 1 
ATOM   5350 H  HE22 A GLN   B 1 107 ? 26.644 -23.259 7.101   0.82 42.12 ?  107 GLN   B HE22 1 
ATOM   5351 H  HE22 B GLN   B 1 107 ? 26.567 -23.245 7.253   0.18 36.51 ?  107 GLN   B HE22 1 
ATOM   5352 N  N    . LEU   B 1 108 ? 31.890 -24.908 7.564   1.00 19.98 ?  108 LEU   B N    1 
ATOM   5353 C  CA   . LEU   B 1 108 ? 32.437 -23.612 7.155   1.00 18.21 ?  108 LEU   B CA   1 
ATOM   5354 C  C    . LEU   B 1 108 ? 33.078 -23.631 5.774   1.00 15.71 ?  108 LEU   B C    1 
ATOM   5355 O  O    . LEU   B 1 108 ? 33.508 -22.573 5.286   1.00 15.52 ?  108 LEU   B O    1 
ATOM   5356 C  CB   . LEU   B 1 108 ? 33.449 -23.140 8.197   1.00 18.92 ?  108 LEU   B CB   1 
ATOM   5357 C  CG   . LEU   B 1 108 ? 32.832 -22.659 9.509   1.00 19.99 ?  108 LEU   B CG   1 
ATOM   5358 C  CD1  . LEU   B 1 108 ? 33.857 -22.642 10.629  1.00 20.33 ?  108 LEU   B CD1  1 
ATOM   5359 C  CD2  . LEU   B 1 108 ? 32.241 -21.274 9.317   1.00 21.12 ?  108 LEU   B CD2  1 
ATOM   5360 H  H    A LEU   B 1 108 ? 32.354 -25.305 8.164   0.82 24.01 ?  108 LEU   B H    1 
ATOM   5361 H  H    B LEU   B 1 108 ? 32.352 -25.315 8.159   0.18 24.01 ?  108 LEU   B H    1 
ATOM   5362 H  HA   . LEU   B 1 108 ? 31.715 -22.970 7.132   1.00 21.90 ?  108 LEU   B HA   1 
ATOM   5363 H  HB2  . LEU   B 1 108 ? 34.044 -23.876 8.409   1.00 22.75 ?  108 LEU   B HB2  1 
ATOM   5364 H  HB3  . LEU   B 1 108 ? 33.954 -22.404 7.826   1.00 22.75 ?  108 LEU   B HB3  1 
ATOM   5365 H  HG   . LEU   B 1 108 ? 32.113 -23.260 9.768   1.00 24.03 ?  108 LEU   B HG   1 
ATOM   5366 H  HD11 . LEU   B 1 108 ? 33.421 -22.367 11.453  1.00 24.44 ?  108 LEU   B HD11 1 
ATOM   5367 H  HD12 . LEU   B 1 108 ? 34.227 -23.531 10.732  1.00 24.44 ?  108 LEU   B HD12 1 
ATOM   5368 H  HD13 . LEU   B 1 108 ? 34.559 -22.013 10.403  1.00 24.44 ?  108 LEU   B HD13 1 
ATOM   5369 H  HD21 . LEU   B 1 108 ? 31.898 -20.956 10.167  1.00 25.38 ?  108 LEU   B HD21 1 
ATOM   5370 H  HD22 . LEU   B 1 108 ? 32.936 -20.679 8.996   1.00 25.38 ?  108 LEU   B HD22 1 
ATOM   5371 H  HD23 . LEU   B 1 108 ? 31.522 -21.325 8.668   1.00 25.38 ?  108 LEU   B HD23 1 
ATOM   5372 N  N    . LEU   B 1 109 ? 33.141 -24.798 5.136   1.00 14.73 ?  109 LEU   B N    1 
ATOM   5373 C  CA   . LEU   B 1 109 ? 33.767 -24.899 3.827   1.00 13.98 ?  109 LEU   B CA   1 
ATOM   5374 C  C    . LEU   B 1 109 ? 33.001 -24.112 2.770   1.00 13.33 ?  109 LEU   B C    1 
ATOM   5375 O  O    . LEU   B 1 109 ? 33.614 -23.521 1.874   1.00 13.11 ?  109 LEU   B O    1 
ATOM   5376 C  CB   . LEU   B 1 109 ? 33.884 -26.371 3.439   1.00 14.15 ?  109 LEU   B CB   1 
ATOM   5377 C  CG   . LEU   B 1 109 ? 34.660 -26.707 2.169   1.00 14.06 ?  109 LEU   B CG   1 
ATOM   5378 C  CD1  . LEU   B 1 109 ? 36.046 -26.063 2.184   1.00 14.16 ?  109 LEU   B CD1  1 
ATOM   5379 C  CD2  . LEU   B 1 109 ? 34.770 -28.215 2.016   1.00 14.83 ?  109 LEU   B CD2  1 
ATOM   5380 H  H    . LEU   B 1 109 ? 32.833 -25.542 5.436   1.00 17.72 ?  109 LEU   B H    1 
ATOM   5381 H  HA   . LEU   B 1 109 ? 34.664 -24.535 3.874   1.00 16.81 ?  109 LEU   B HA   1 
ATOM   5382 H  HB2  . LEU   B 1 109 ? 34.320 -26.843 4.164   1.00 17.01 ?  109 LEU   B HB2  1 
ATOM   5383 H  HB3  . LEU   B 1 109 ? 32.988 -26.728 3.322   1.00 17.01 ?  109 LEU   B HB3  1 
ATOM   5384 H  HG   . LEU   B 1 109 ? 34.177 -26.368 1.397   1.00 16.91 ?  109 LEU   B HG   1 
ATOM   5385 H  HD11 . LEU   B 1 109 ? 36.572 -26.423 1.453   1.00 17.03 ?  109 LEU   B HD11 1 
ATOM   5386 H  HD12 . LEU   B 1 109 ? 35.949 -25.106 2.085   1.00 17.03 ?  109 LEU   B HD12 1 
ATOM   5387 H  HD13 . LEU   B 1 109 ? 36.476 -26.270 3.031   1.00 17.03 ?  109 LEU   B HD13 1 
ATOM   5388 H  HD21 . LEU   B 1 109 ? 35.346 -28.417 1.262   1.00 17.84 ?  109 LEU   B HD21 1 
ATOM   5389 H  HD22 . LEU   B 1 109 ? 35.144 -28.588 2.827   1.00 17.84 ?  109 LEU   B HD22 1 
ATOM   5390 H  HD23 . LEU   B 1 109 ? 33.883 -28.584 1.860   1.00 17.84 ?  109 LEU   B HD23 1 
ATOM   5391 N  N    . LYS   B 1 110 ? 31.668 -24.079 2.853   1.00 13.10 ?  110 LYS   B N    1 
ATOM   5392 C  CA   . LYS   B 1 110 ? 30.911 -23.320 1.864   1.00 13.04 ?  110 LYS   B CA   1 
ATOM   5393 C  C    . LYS   B 1 110 ? 31.246 -21.832 1.953   1.00 12.50 ?  110 LYS   B C    1 
ATOM   5394 O  O    . LYS   B 1 110 ? 31.498 -21.181 0.934   1.00 12.42 ?  110 LYS   B O    1 
ATOM   5395 C  CB   . LYS   B 1 110 ? 29.404 -23.564 2.011   1.00 13.59 ?  110 LYS   B CB   1 
ATOM   5396 C  CG   . LYS   B 1 110 ? 28.602 -22.944 0.870   1.00 13.87 ?  110 LYS   B CG   1 
ATOM   5397 C  CD   . LYS   B 1 110 ? 27.137 -23.367 0.899   1.00 14.08 ?  110 LYS   B CD   1 
ATOM   5398 C  CE   . LYS   B 1 110 ? 26.374 -22.823 -0.306  1.00 14.54 ?  110 LYS   B CE   1 
ATOM   5399 N  NZ   . LYS   B 1 110 ? 26.696 -23.538 -1.567  1.00 14.96 ?  110 LYS   B NZ   1 
ATOM   5400 H  H    . LYS   B 1 110 ? 31.199 -24.480 3.448   1.00 15.76 ?  110 LYS   B H    1 
ATOM   5401 H  HA   . LYS   B 1 110 ? 31.169 -23.622 0.977   1.00 15.68 ?  110 LYS   B HA   1 
ATOM   5402 H  HB2  . LYS   B 1 110 ? 29.237 -24.524 2.007   1.00 16.35 ?  110 LYS   B HB2  1 
ATOM   5403 H  HB3  . LYS   B 1 110 ? 29.097 -23.177 2.841   1.00 16.35 ?  110 LYS   B HB3  1 
ATOM   5404 H  HG2  . LYS   B 1 110 ? 28.633 -21.980 0.943   1.00 16.68 ?  110 LYS   B HG2  1 
ATOM   5405 H  HG3  . LYS   B 1 110 ? 28.974 -23.229 0.021   1.00 16.68 ?  110 LYS   B HG3  1 
ATOM   5406 H  HD2  . LYS   B 1 110 ? 27.078 -24.338 0.884   1.00 16.93 ?  110 LYS   B HD2  1 
ATOM   5407 H  HD3  . LYS   B 1 110 ? 26.716 -23.023 1.705   1.00 16.93 ?  110 LYS   B HD3  1 
ATOM   5408 H  HE2  . LYS   B 1 110 ? 25.423 -22.913 -0.146  1.00 17.49 ?  110 LYS   B HE2  1 
ATOM   5409 H  HE3  . LYS   B 1 110 ? 26.606 -21.890 -0.426  1.00 17.49 ?  110 LYS   B HE3  1 
ATOM   5410 H  HZ1  . LYS   B 1 110 ? 26.232 -23.188 -2.240  1.00 17.99 ?  110 LYS   B HZ1  1 
ATOM   5411 H  HZ2  . LYS   B 1 110 ? 27.564 -23.468 -1.744  1.00 17.99 ?  110 LYS   B HZ2  1 
ATOM   5412 H  HZ3  . LYS   B 1 110 ? 26.485 -24.400 -1.489  1.00 17.99 ?  110 LYS   B HZ3  1 
ATOM   5413 N  N    . SER   B 1 111 ? 31.263 -21.279 3.171   1.00 12.99 ?  111 SER   B N    1 
ATOM   5414 C  CA   . SER   B 1 111 ? 31.656 -19.881 3.349   1.00 12.93 ?  111 SER   B CA   1 
ATOM   5415 C  C    . SER   B 1 111 ? 33.038 -19.622 2.763   1.00 12.53 ?  111 SER   B C    1 
ATOM   5416 O  O    . SER   B 1 111 ? 33.265 -18.589 2.116   1.00 12.57 ?  111 SER   B O    1 
ATOM   5417 C  CB   . SER   B 1 111 ? 31.649 -19.526 4.833   1.00 14.09 ?  111 SER   B CB   1 
ATOM   5418 O  OG   . SER   B 1 111 ? 30.339 -19.521 5.362   1.00 15.72 ?  111 SER   B OG   1 
ATOM   5419 H  H    . SER   B 1 111 ? 31.058 -21.694 3.898   1.00 15.63 ?  111 SER   B H    1 
ATOM   5420 H  HA   . SER   B 1 111 ? 31.020 -19.312 2.893   1.00 15.55 ?  111 SER   B HA   1 
ATOM   5421 H  HB2  . SER   B 1 111 ? 32.177 -20.178 5.317   1.00 16.95 ?  111 SER   B HB2  1 
ATOM   5422 H  HB3  . SER   B 1 111 ? 32.027 -18.643 4.946   1.00 16.95 ?  111 SER   B HB3  1 
ATOM   5423 H  HG   . SER   B 1 111 ? 30.355 -19.327 6.185   1.00 18.91 ?  111 SER   B HG   1 
ATOM   5424 N  N    . ALA   B 1 112 ? 33.977 -20.542 2.983   1.00 12.32 ?  112 ALA   B N    1 
ATOM   5425 C  CA   . ALA   B 1 112 ? 35.321 -20.370 2.440   1.00 12.38 ?  112 ALA   B CA   1 
ATOM   5426 C  C    . ALA   B 1 112 ? 35.286 -20.268 0.917   1.00 11.82 ?  112 ALA   B C    1 
ATOM   5427 O  O    . ALA   B 1 112 ? 35.917 -19.385 0.325   1.00 12.03 ?  112 ALA   B O    1 
ATOM   5428 C  CB   . ALA   B 1 112 ? 36.231 -21.512 2.902   1.00 12.73 ?  112 ALA   B CB   1 
ATOM   5429 H  H    . ALA   B 1 112 ? 33.863 -21.265 3.445   1.00 14.83 ?  112 ALA   B H    1 
ATOM   5430 H  HA   . ALA   B 1 112 ? 35.689 -19.543 2.788   1.00 14.90 ?  112 ALA   B HA   1 
ATOM   5431 H  HB1  . ALA   B 1 112 ? 37.121 -21.372 2.537   1.00 15.32 ?  112 ALA   B HB1  1 
ATOM   5432 H  HB2  . ALA   B 1 112 ? 36.274 -21.511 3.874   1.00 15.32 ?  112 ALA   B HB2  1 
ATOM   5433 H  HB3  . ALA   B 1 112 ? 35.872 -22.353 2.588   1.00 15.32 ?  112 ALA   B HB3  1 
ATOM   5434 N  N    . TYR   B 1 113 ? 34.558 -21.172 0.261   1.00 11.78 ?  113 TYR   B N    1 
ATOM   5435 C  CA   . TYR   B 1 113 ? 34.481 -21.122 -1.194  1.00 11.40 ?  113 TYR   B CA   1 
ATOM   5436 C  C    . TYR   B 1 113 ? 33.771 -19.871 -1.707  1.00 11.23 ?  113 TYR   B C    1 
ATOM   5437 O  O    . TYR   B 1 113 ? 34.048 -19.432 -2.829  1.00 11.35 ?  113 TYR   B O    1 
ATOM   5438 C  CB   . TYR   B 1 113 ? 33.813 -22.383 -1.744  1.00 11.68 ?  113 TYR   B CB   1 
ATOM   5439 C  CG   . TYR   B 1 113 ? 34.776 -23.528 -2.012  1.00 12.11 ?  113 TYR   B CG   1 
ATOM   5440 C  CD1  . TYR   B 1 113 ? 35.764 -23.419 -2.984  1.00 12.66 ?  113 TYR   B CD1  1 
ATOM   5441 C  CD2  . TYR   B 1 113 ? 34.683 -24.722 -1.308  1.00 12.34 ?  113 TYR   B CD2  1 
ATOM   5442 C  CE1  . TYR   B 1 113 ? 36.645 -24.451 -3.235  1.00 12.73 ?  113 TYR   B CE1  1 
ATOM   5443 C  CE2  . TYR   B 1 113 ? 35.549 -25.773 -1.560  1.00 12.48 ?  113 TYR   B CE2  1 
ATOM   5444 C  CZ   . TYR   B 1 113 ? 36.526 -25.631 -2.527  1.00 12.55 ?  113 TYR   B CZ   1 
ATOM   5445 O  OH   . TYR   B 1 113 ? 37.402 -26.648 -2.804  1.00 13.43 ?  113 TYR   B OH   1 
ATOM   5446 H  H    . TYR   B 1 113 ? 34.100 -21.801 0.632   1.00 14.18 ?  113 TYR   B H    1 
ATOM   5447 H  HA   . TYR   B 1 113 ? 35.382 -21.098 -1.535  1.00 13.72 ?  113 TYR   B HA   1 
ATOM   5448 H  HB2  . TYR   B 1 113 ? 33.158 -22.700 -1.102  1.00 14.06 ?  113 TYR   B HB2  1 
ATOM   5449 H  HB3  . TYR   B 1 113 ? 33.374 -22.165 -2.580  1.00 14.06 ?  113 TYR   B HB3  1 
ATOM   5450 H  HD1  . TYR   B 1 113 ? 35.842 -22.623 -3.469  1.00 15.23 ?  113 TYR   B HD1  1 
ATOM   5451 H  HD2  . TYR   B 1 113 ? 34.025 -24.820 -0.665  1.00 14.85 ?  113 TYR   B HD2  1 
ATOM   5452 H  HE1  . TYR   B 1 113 ? 37.295 -24.357 -3.899  1.00 15.32 ?  113 TYR   B HE1  1 
ATOM   5453 H  HE2  . TYR   B 1 113 ? 35.475 -26.567 -1.087  1.00 15.02 ?  113 TYR   B HE2  1 
ATOM   5454 H  HH   . TYR   B 1 113 ? 37.229 -27.311 -2.321  1.00 16.16 ?  113 TYR   B HH   1 
ATOM   5455 N  N    . GLU   B 1 114 ? 32.844 -19.296 -0.930  1.00 11.21 ?  114 GLU   B N    1 
ATOM   5456 C  CA   . GLU   B 1 114 ? 32.162 -18.086 -1.382  1.00 11.25 ?  114 GLU   B CA   1 
ATOM   5457 C  C    . GLU   B 1 114 ? 33.145 -16.962 -1.677  1.00 11.15 ?  114 GLU   B C    1 
ATOM   5458 O  O    . GLU   B 1 114 ? 32.868 -16.104 -2.521  1.00 11.68 ?  114 GLU   B O    1 
ATOM   5459 C  CB   . GLU   B 1 114 ? 31.099 -17.660 -0.368  1.00 11.61 ?  114 GLU   B CB   1 
ATOM   5460 C  CG   . GLU   B 1 114 ? 29.902 -18.594 -0.425  1.00 12.01 ?  114 GLU   B CG   1 
ATOM   5461 C  CD   . GLU   B 1 114 ? 28.881 -18.403 0.682   1.00 12.23 ?  114 GLU   B CD   1 
ATOM   5462 O  OE1  . GLU   B 1 114 ? 29.173 -17.783 1.727   1.00 12.42 ?  114 GLU   B OE1  1 
ATOM   5463 O  OE2  . GLU   B 1 114 ? 27.758 -18.939 0.518   1.00 12.83 -1 114 GLU   B OE2  1 
ATOM   5464 H  H    . GLU   B 1 114 ? 32.587 -19.593 -0.160  1.00 13.49 ?  114 GLU   B H    1 
ATOM   5465 H  HA   . GLU   B 1 114 ? 31.706 -18.285 -2.208  1.00 13.54 ?  114 GLU   B HA   1 
ATOM   5466 H  HB2  . GLU   B 1 114 ? 31.472 -17.693 0.529   1.00 13.97 ?  114 GLU   B HB2  1 
ATOM   5467 H  HB3  . GLU   B 1 114 ? 30.795 -16.764 -0.575  1.00 13.97 ?  114 GLU   B HB3  1 
ATOM   5468 H  HG2  . GLU   B 1 114 ? 29.450 -18.465 -1.269  1.00 14.45 ?  114 GLU   B HG2  1 
ATOM   5469 H  HG3  . GLU   B 1 114 ? 30.228 -19.512 -0.370  1.00 14.45 ?  114 GLU   B HG3  1 
ATOM   5470 N  N    . ASN   B 1 115 ? 34.308 -16.959 -1.025  1.00 11.08 ?  115 ASN   B N    1 
ATOM   5471 C  CA   . ASN   B 1 115 ? 35.302 -15.932 -1.324  1.00 11.05 ?  115 ASN   B CA   1 
ATOM   5472 C  C    . ASN   B 1 115 ? 35.704 -15.944 -2.791  1.00 10.77 ?  115 ASN   B C    1 
ATOM   5473 O  O    . ASN   B 1 115 ? 36.094 -14.900 -3.340  1.00 11.54 ?  115 ASN   B O    1 
ATOM   5474 C  CB   . ASN   B 1 115 ? 36.541 -16.117 -0.445  1.00 11.58 ?  115 ASN   B CB   1 
ATOM   5475 C  CG   . ASN   B 1 115 ? 36.280 -15.849 1.016   1.00 12.11 ?  115 ASN   B CG   1 
ATOM   5476 O  OD1  . ASN   B 1 115 ? 36.287 -14.705 1.453   1.00 14.09 ?  115 ASN   B OD1  1 
ATOM   5477 N  ND2  . ASN   B 1 115 ? 36.114 -16.910 1.798   1.00 12.40 ?  115 ASN   B ND2  1 
ATOM   5478 H  H    . ASN   B 1 115 ? 34.538 -17.517 -0.405  1.00 13.34 ?  115 ASN   B H    1 
ATOM   5479 H  HA   . ASN   B 1 115 ? 34.929 -15.059 -1.121  1.00 13.30 ?  115 ASN   B HA   1 
ATOM   5480 H  HB2  . ASN   B 1 115 ? 36.856 -17.031 -0.530  1.00 13.93 ?  115 ASN   B HB2  1 
ATOM   5481 H  HB3  . ASN   B 1 115 ? 37.232 -15.502 -0.738  1.00 13.93 ?  115 ASN   B HB3  1 
ATOM   5482 H  HD21 . ASN   B 1 115 ? 35.974 -16.803 2.642   1.00 14.92 ?  115 ASN   B HD21 1 
ATOM   5483 H  HD22 . ASN   B 1 115 ? 36.134 -17.699 1.463   1.00 14.92 ?  115 ASN   B HD22 1 
ATOM   5484 N  N    . PHE   B 1 116 ? 35.681 -17.120 -3.428  1.00 10.60 ?  116 PHE   B N    1 
ATOM   5485 C  CA   . PHE   B 1 116 ? 36.114 -17.212 -4.817  1.00 11.00 ?  116 PHE   B CA   1 
ATOM   5486 C  C    . PHE   B 1 116 ? 35.216 -16.384 -5.727  1.00 10.75 ?  116 PHE   B C    1 
ATOM   5487 O  O    . PHE   B 1 116 ? 35.653 -15.956 -6.798  1.00 11.14 ?  116 PHE   B O    1 
ATOM   5488 C  CB   . PHE   B 1 116 ? 36.077 -18.656 -5.337  1.00 10.94 ?  116 PHE   B CB   1 
ATOM   5489 C  CG   . PHE   B 1 116 ? 37.155 -19.610 -4.797  1.00 10.94 ?  116 PHE   B CG   1 
ATOM   5490 C  CD1  . PHE   B 1 116 ? 37.811 -19.426 -3.593  1.00 11.64 ?  116 PHE   B CD1  1 
ATOM   5491 C  CD2  . PHE   B 1 116 ? 37.460 -20.745 -5.535  1.00 11.25 ?  116 PHE   B CD2  1 
ATOM   5492 C  CE1  . PHE   B 1 116 ? 38.749 -20.358 -3.142  1.00 11.87 ?  116 PHE   B CE1  1 
ATOM   5493 C  CE2  . PHE   B 1 116 ? 38.391 -21.678 -5.089  1.00 11.45 ?  116 PHE   B CE2  1 
ATOM   5494 C  CZ   . PHE   B 1 116 ? 39.036 -21.480 -3.898  1.00 11.42 ?  116 PHE   B CZ   1 
ATOM   5495 H  H    . PHE   B 1 116 ? 35.424 -17.867 -3.080  1.00 12.75 ?  116 PHE   B H    1 
ATOM   5496 H  HA   . PHE   B 1 116 ? 37.020 -16.883 -4.899  1.00 13.24 ?  116 PHE   B HA   1 
ATOM   5497 H  HB2  . PHE   B 1 116 ? 35.206 -19.036 -5.111  1.00 13.16 ?  116 PHE   B HB2  1 
ATOM   5498 H  HB3  . PHE   B 1 116 ? 36.164 -18.634 -6.304  1.00 13.16 ?  116 PHE   B HB3  1 
ATOM   5499 H  HD1  . PHE   B 1 116 ? 37.612 -18.678 -3.076  1.00 14.01 ?  116 PHE   B HD1  1 
ATOM   5500 H  HD2  . PHE   B 1 116 ? 37.015 -20.897 -6.341  1.00 13.53 ?  116 PHE   B HD2  1 
ATOM   5501 H  HE1  . PHE   B 1 116 ? 39.189 -20.215 -2.336  1.00 14.28 ?  116 PHE   B HE1  1 
ATOM   5502 H  HE2  . PHE   B 1 116 ? 38.585 -22.427 -5.605  1.00 13.78 ?  116 PHE   B HE2  1 
ATOM   5503 H  HZ   . PHE   B 1 116 ? 39.673 -22.087 -3.602  1.00 13.74 ?  116 PHE   B HZ   1 
ATOM   5504 N  N    . ASN   B 1 117 ? 33.945 -16.189 -5.345  1.00 10.92 ?  117 ASN   B N    1 
ATOM   5505 C  CA   . ASN   B 1 117 ? 32.996 -15.482 -6.207  1.00 11.31 ?  117 ASN   B CA   1 
ATOM   5506 C  C    . ASN   B 1 117 ? 33.309 -14.002 -6.353  1.00 11.69 ?  117 ASN   B C    1 
ATOM   5507 O  O    . ASN   B 1 117 ? 32.709 -13.344 -7.206  1.00 13.03 ?  117 ASN   B O    1 
ATOM   5508 C  CB   . ASN   B 1 117 ? 31.572 -15.707 -5.719  1.00 11.89 ?  117 ASN   B CB   1 
ATOM   5509 C  CG   . ASN   B 1 117 ? 31.123 -17.119 -5.971  1.00 11.72 ?  117 ASN   B CG   1 
ATOM   5510 O  OD1  . ASN   B 1 117 ? 31.481 -17.710 -6.992  1.00 12.84 ?  117 ASN   B OD1  1 
ATOM   5511 N  ND2  . ASN   B 1 117 ? 30.381 -17.690 -5.032  1.00 11.59 ?  117 ASN   B ND2  1 
ATOM   5512 H  H    . ASN   B 1 117 ? 33.616 -16.451 -4.591  1.00 13.14 ?  117 ASN   B H    1 
ATOM   5513 H  HA   . ASN   B 1 117 ? 33.056 -15.873 -7.087  1.00 13.61 ?  117 ASN   B HA   1 
ATOM   5514 H  HB2  . ASN   B 1 117 ? 31.525 -15.539 -4.760  1.00 14.31 ?  117 ASN   B HB2  1 
ATOM   5515 H  HB3  . ASN   B 1 117 ? 30.972 -15.104 -6.188  1.00 14.31 ?  117 ASN   B HB3  1 
ATOM   5516 H  HD21 . ASN   B 1 117 ? 30.103 -18.497 -5.135  1.00 13.95 ?  117 ASN   B HD21 1 
ATOM   5517 H  HD22 . ASN   B 1 117 ? 30.154 -17.245 -4.329  1.00 13.95 ?  117 ASN   B HD22 1 
ATOM   5518 N  N    . GLN   B 1 118 ? 34.249 -13.475 -5.576  1.00 11.53 ?  118 GLN   B N    1 
ATOM   5519 C  CA   . GLN   B 1 118 ? 34.677 -12.088 -5.713  1.00 11.91 ?  118 GLN   B CA   1 
ATOM   5520 C  C    . GLN   B 1 118 ? 35.743 -11.897 -6.786  1.00 12.30 ?  118 GLN   B C    1 
ATOM   5521 O  O    . GLN   B 1 118 ? 36.213 -10.769 -6.968  1.00 13.48 ?  118 GLN   B O    1 
ATOM   5522 C  CB   . GLN   B 1 118 ? 35.154 -11.559 -4.358  1.00 12.71 ?  118 GLN   B CB   1 
ATOM   5523 C  CG   . GLN   B 1 118 ? 34.067 -11.594 -3.286  1.00 12.78 ?  118 GLN   B CG   1 
ATOM   5524 C  CD   . GLN   B 1 118 ? 32.895 -10.686 -3.618  1.00 12.67 ?  118 GLN   B CD   1 
ATOM   5525 O  OE1  . GLN   B 1 118 ? 33.085 -9.548  -4.060  1.00 13.43 ?  118 GLN   B OE1  1 
ATOM   5526 N  NE2  . GLN   B 1 118 ? 31.681 -11.179 -3.415  1.00 13.06 ?  118 GLN   B NE2  1 
ATOM   5527 H  H    . GLN   B 1 118 ? 34.669 -13.904 -4.954  1.00 13.88 ?  118 GLN   B H    1 
ATOM   5528 H  HA   . GLN   B 1 118 ? 33.909 -11.559 -5.980  1.00 14.33 ?  118 GLN   B HA   1 
ATOM   5529 H  HB2  . GLN   B 1 118 ? 35.899 -12.092 -4.052  1.00 15.29 ?  118 GLN   B HB2  1 
ATOM   5530 H  HB3  . GLN   B 1 118 ? 35.433 -10.630 -4.464  1.00 15.29 ?  118 GLN   B HB3  1 
ATOM   5531 H  HG2  . GLN   B 1 118 ? 33.733 -12.503 -3.206  1.00 15.37 ?  118 GLN   B HG2  1 
ATOM   5532 H  HG3  . GLN   B 1 118 ? 34.446 -11.305 -2.441  1.00 15.37 ?  118 GLN   B HG3  1 
ATOM   5533 H  HE21 . GLN   B 1 118 ? 31.588 -11.977 -3.105  1.00 15.71 ?  118 GLN   B HE21 1 
ATOM   5534 H  HE22 . GLN   B 1 118 ? 30.994 -10.699 -3.588  1.00 15.71 ?  118 GLN   B HE22 1 
ATOM   5535 N  N    . HIS   B 1 119 ? 36.103 -12.952 -7.516  1.00 11.56 ?  119 HIS   B N    1 
ATOM   5536 C  CA   . HIS   B 1 119 ? 37.139 -12.899 -8.539  1.00 11.93 ?  119 HIS   B CA   1 
ATOM   5537 C  C    . HIS   B 1 119 ? 36.661 -13.634 -9.776  1.00 12.00 ?  119 HIS   B C    1 
ATOM   5538 O  O    . HIS   B 1 119 ? 36.160 -14.754 -9.671  1.00 12.75 ?  119 HIS   B O    1 
ATOM   5539 C  CB   . HIS   B 1 119 ? 38.419 -13.528 -7.994  1.00 12.44 ?  119 HIS   B CB   1 
ATOM   5540 C  CG   . HIS   B 1 119 ? 38.906 -12.825 -6.773  1.00 13.81 ?  119 HIS   B CG   1 
ATOM   5541 N  ND1  . HIS   B 1 119 ? 39.702 -11.702 -6.836  1.00 15.33 ?  119 HIS   B ND1  1 
ATOM   5542 C  CD2  . HIS   B 1 119 ? 38.618 -13.017 -5.466  1.00 14.60 ?  119 HIS   B CD2  1 
ATOM   5543 C  CE1  . HIS   B 1 119 ? 39.917 -11.257 -5.611  1.00 16.26 ?  119 HIS   B CE1  1 
ATOM   5544 N  NE2  . HIS   B 1 119 ? 39.269 -12.034 -4.763  1.00 16.23 ?  119 HIS   B NE2  1 
ATOM   5545 H  H    . HIS   B 1 119 ? 35.743 -13.734 -7.438  1.00 13.91 ?  119 HIS   B H    1 
ATOM   5546 H  HA   . HIS   B 1 119 ? 37.315 -11.976 -8.777  1.00 14.35 ?  119 HIS   B HA   1 
ATOM   5547 H  HB2  . HIS   B 1 119 ? 38.247 -14.455 -7.771  1.00 14.97 ?  119 HIS   B HB2  1 
ATOM   5548 H  HB3  . HIS   B 1 119 ? 39.110 -13.473 -8.676  1.00 14.97 ?  119 HIS   B HB3  1 
ATOM   5549 H  HD2  . HIS   B 1 119 ? 38.089 -13.699 -5.111  1.00 17.56 ?  119 HIS   B HD2  1 
ATOM   5550 H  HE1  . HIS   B 1 119 ? 40.449 -10.532 -5.382  1.00 19.55 ?  119 HIS   B HE1  1 
ATOM   5551 H  HE2  . HIS   B 1 119 ? 39.275 -11.957 -3.905  1.00 19.52 ?  119 HIS   B HE2  1 
ATOM   5552 N  N    . GLU   B 1 120 ? 36.819 -13.021 -10.949 1.00 12.27 ?  120 GLU   B N    1 
ATOM   5553 C  CA   . GLU   B 1 120 ? 36.227 -13.600 -12.150 1.00 13.89 ?  120 GLU   B CA   1 
ATOM   5554 C  C    . GLU   B 1 120 ? 36.898 -14.903 -12.562 1.00 12.76 ?  120 GLU   B C    1 
ATOM   5555 O  O    . GLU   B 1 120 ? 36.234 -15.775 -13.135 1.00 12.95 ?  120 GLU   B O    1 
ATOM   5556 C  CB   . GLU   B 1 120 ? 36.234 -12.591 -13.296 1.00 17.79 ?  120 GLU   B CB   1 
ATOM   5557 C  CG   . GLU   B 1 120 ? 35.298 -11.423 -13.054 1.00 23.44 ?  120 GLU   B CG   1 
ATOM   5558 C  CD   . GLU   B 1 120 ? 35.101 -10.553 -14.275 1.00 28.84 ?  120 GLU   B CD   1 
ATOM   5559 O  OE1  . GLU   B 1 120 ? 36.092 -10.305 -14.995 1.00 30.92 ?  120 GLU   B OE1  1 
ATOM   5560 O  OE2  . GLU   B 1 120 ? 33.954 -10.115 -14.505 1.00 31.54 -1 120 GLU   B OE2  1 
ATOM   5561 H  H    . GLU   B 1 120 ? 37.254 -12.285 -11.076 1.00 14.76 ?  120 GLU   B H    1 
ATOM   5562 H  HA   . GLU   B 1 120 ? 35.304 -13.811 -11.960 1.00 16.71 ?  120 GLU   B HA   1 
ATOM   5563 H  HB2  . GLU   B 1 120 ? 37.127 -12.238 -13.408 1.00 21.39 ?  120 GLU   B HB2  1 
ATOM   5564 H  HB3  . GLU   B 1 120 ? 35.947 -13.036 -14.112 1.00 21.39 ?  120 GLU   B HB3  1 
ATOM   5565 H  HG2  . GLU   B 1 120 ? 34.426 -11.760 -12.791 1.00 28.17 ?  120 GLU   B HG2  1 
ATOM   5566 H  HG3  . GLU   B 1 120 ? 35.662 -10.863 -12.353 1.00 28.17 ?  120 GLU   B HG3  1 
ATOM   5567 N  N    . VAL   B 1 121 ? 38.198 -15.047 -12.296 1.00 12.46 ?  121 VAL   B N    1 
ATOM   5568 C  CA   . VAL   B 1 121 ? 38.943 -16.257 -12.643 1.00 12.35 ?  121 VAL   B CA   1 
ATOM   5569 C  C    . VAL   B 1 121 ? 40.058 -16.456 -11.625 1.00 11.97 ?  121 VAL   B C    1 
ATOM   5570 O  O    . VAL   B 1 121 ? 40.732 -15.498 -11.236 1.00 12.52 ?  121 VAL   B O    1 
ATOM   5571 C  CB   . VAL   B 1 121 ? 39.456 -16.214 -14.102 1.00 14.13 ?  121 VAL   B CB   1 
ATOM   5572 C  CG1  . VAL   B 1 121 ? 40.332 -14.988 -14.354 1.00 15.42 ?  121 VAL   B CG1  1 
ATOM   5573 C  CG2  . VAL   B 1 121 ? 40.189 -17.501 -14.457 1.00 15.66 ?  121 VAL   B CG2  1 
ATOM   5574 H  H    . VAL   B 1 121 ? 38.683 -14.447 -11.913 1.00 14.99 ?  121 VAL   B H    1 
ATOM   5575 H  HA   . VAL   B 1 121 ? 38.338 -17.011 -12.575 1.00 14.86 ?  121 VAL   B HA   1 
ATOM   5576 H  HB   . VAL   B 1 121 ? 38.689 -16.146 -14.696 1.00 17.00 ?  121 VAL   B HB   1 
ATOM   5577 H  HG11 . VAL   B 1 121 ? 40.632 -14.999 -15.277 1.00 18.54 ?  121 VAL   B HG11 1 
ATOM   5578 H  HG12 . VAL   B 1 121 ? 39.810 -14.187 -14.187 1.00 18.54 ?  121 VAL   B HG12 1 
ATOM   5579 H  HG13 . VAL   B 1 121 ? 41.095 -15.018 -13.758 1.00 18.54 ?  121 VAL   B HG13 1 
ATOM   5580 H  HG21 . VAL   B 1 121 ? 40.391 -17.497 -15.408 1.00 18.83 ?  121 VAL   B HG21 1 
ATOM   5581 H  HG22 . VAL   B 1 121 ? 41.014 -17.546 -13.948 1.00 18.83 ?  121 VAL   B HG22 1 
ATOM   5582 H  HG23 . VAL   B 1 121 ? 39.624 -18.257 -14.244 1.00 18.83 ?  121 VAL   B HG23 1 
ATOM   5583 N  N    . LEU   B 1 122 ? 40.251 -17.706 -11.195 1.00 11.41 ?  122 LEU   B N    1 
ATOM   5584 C  CA   . LEU   B 1 122 ? 41.233 -18.055 -10.173 1.00 11.13 ?  122 LEU   B CA   1 
ATOM   5585 C  C    . LEU   B 1 122 ? 41.888 -19.388 -10.500 1.00 10.98 ?  122 LEU   B C    1 
ATOM   5586 O  O    . LEU   B 1 122 ? 41.226 -20.310 -10.997 1.00 12.21 ?  122 LEU   B O    1 
ATOM   5587 C  CB   . LEU   B 1 122 ? 40.581 -18.273 -8.794  1.00 12.85 ?  122 LEU   B CB   1 
ATOM   5588 C  CG   . LEU   B 1 122 ? 39.538 -17.260 -8.307  1.00 13.13 ?  122 LEU   B CG   1 
ATOM   5589 C  CD1  . LEU   B 1 122 ? 38.136 -17.606 -8.794  1.00 14.26 ?  122 LEU   B CD1  1 
ATOM   5590 C  CD2  . LEU   B 1 122 ? 39.584 -17.165 -6.792  1.00 12.90 ?  122 LEU   B CD2  1 
ATOM   5591 H  H    . LEU   B 1 122 ? 39.817 -18.388 -11.492 1.00 13.73 ?  122 LEU   B H    1 
ATOM   5592 H  HA   . LEU   B 1 122 ? 41.911 -17.360 -10.102 1.00 13.40 ?  122 LEU   B HA   1 
ATOM   5593 H  HB2  . LEU   B 1 122 ? 40.143 -19.134 -8.810  1.00 15.46 ?  122 LEU   B HB2  1 
ATOM   5594 H  HB3  . LEU   B 1 122 ? 41.287 -18.284 -8.132  1.00 15.46 ?  122 LEU   B HB3  1 
ATOM   5595 H  HG   . LEU   B 1 122 ? 39.764 -16.383 -8.659  1.00 15.79 ?  122 LEU   B HG   1 
ATOM   5596 H  HD11 . LEU   B 1 122 ? 37.507 -16.968 -8.420  1.00 17.15 ?  122 LEU   B HD11 1 
ATOM   5597 H  HD12 . LEU   B 1 122 ? 38.118 -17.551 -9.764  1.00 17.15 ?  122 LEU   B HD12 1 
ATOM   5598 H  HD13 . LEU   B 1 122 ? 37.914 -18.501 -8.507  1.00 17.15 ?  122 LEU   B HD13 1 
ATOM   5599 H  HD21 . LEU   B 1 122 ? 38.897 -16.552 -6.488  1.00 15.52 ?  122 LEU   B HD21 1 
ATOM   5600 H  HD22 . LEU   B 1 122 ? 39.432 -18.046 -6.415  1.00 15.52 ?  122 LEU   B HD22 1 
ATOM   5601 H  HD23 . LEU   B 1 122 ? 40.459 -16.839 -6.520  1.00 15.52 ?  122 LEU   B HD23 1 
ATOM   5602 N  N    . LEU   B 1 123 ? 43.177 -19.492 -10.150 1.00 10.76 ?  123 LEU   B N    1 
ATOM   5603 C  CA   . LEU   B 1 123 ? 43.889 -20.763 -10.028 1.00 11.20 ?  123 LEU   B CA   1 
ATOM   5604 C  C    . LEU   B 1 123 ? 43.859 -21.155 -8.557  1.00 10.82 ?  123 LEU   B C    1 
ATOM   5605 O  O    . LEU   B 1 123 ? 44.206 -20.325 -7.704  1.00 11.41 ?  123 LEU   B O    1 
ATOM   5606 C  CB   . LEU   B 1 123 ? 45.336 -20.590 -10.497 1.00 11.54 ?  123 LEU   B CB   1 
ATOM   5607 C  CG   . LEU   B 1 123 ? 46.280 -21.767 -10.244 1.00 11.98 ?  123 LEU   B CG   1 
ATOM   5608 C  CD1  . LEU   B 1 123 ? 45.846 -22.999 -11.029 1.00 12.62 ?  123 LEU   B CD1  1 
ATOM   5609 C  CD2  . LEU   B 1 123 ? 47.700 -21.369 -10.608 1.00 12.93 ?  123 LEU   B CD2  1 
ATOM   5610 H  H    . LEU   B 1 123 ? 43.676 -18.810 -9.963  1.00 12.95 ?  123 LEU   B H    1 
ATOM   5611 H  HA   . LEU   B 1 123 ? 43.449 -21.447 -10.556 1.00 13.48 ?  123 LEU   B HA   1 
ATOM   5612 H  HB2  . LEU   B 1 123 ? 45.327 -20.435 -11.455 1.00 13.88 ?  123 LEU   B HB2  1 
ATOM   5613 H  HB3  . LEU   B 1 123 ? 45.713 -19.822 -10.048 1.00 13.88 ?  123 LEU   B HB3  1 
ATOM   5614 H  HG   . LEU   B 1 123 ? 46.266 -21.996 -9.301  1.00 14.41 ?  123 LEU   B HG   1 
ATOM   5615 H  HD11 . LEU   B 1 123 ? 46.478 -23.716 -10.865 1.00 15.18 ?  123 LEU   B HD11 1 
ATOM   5616 H  HD12 . LEU   B 1 123 ? 44.960 -23.265 -10.734 1.00 15.18 ?  123 LEU   B HD12 1 
ATOM   5617 H  HD13 . LEU   B 1 123 ? 45.829 -22.780 -11.973 1.00 15.18 ?  123 LEU   B HD13 1 
ATOM   5618 H  HD21 . LEU   B 1 123 ? 48.291 -22.121 -10.447 1.00 15.55 ?  123 LEU   B HD21 1 
ATOM   5619 H  HD22 . LEU   B 1 123 ? 47.727 -21.121 -11.545 1.00 15.55 ?  123 LEU   B HD22 1 
ATOM   5620 H  HD23 . LEU   B 1 123 ? 47.965 -20.615 -10.058 1.00 15.55 ?  123 LEU   B HD23 1 
ATOM   5621 N  N    . ALA   B 1 124 ? 43.423 -22.386 -8.248  1.00 10.80 ?  124 ALA   B N    1 
ATOM   5622 C  CA   . ALA   B 1 124 ? 43.170 -22.710 -6.852  1.00 11.03 ?  124 ALA   B CA   1 
ATOM   5623 C  C    . ALA   B 1 124 ? 43.438 -24.170 -6.523  1.00 10.92 ?  124 ALA   B C    1 
ATOM   5624 O  O    . ALA   B 1 124 ? 43.315 -25.043 -7.393  1.00 11.17 ?  124 ALA   B O    1 
ATOM   5625 C  CB   . ALA   B 1 124 ? 41.716 -22.390 -6.481  1.00 11.60 ?  124 ALA   B CB   1 
ATOM   5626 H  H    . ALA   B 1 124 ? 43.261 -23.023 -8.809  1.00 12.99 ?  124 ALA   B H    1 
ATOM   5627 H  HA   . ALA   B 1 124 ? 43.746 -22.158 -6.304  1.00 13.27 ?  124 ALA   B HA   1 
ATOM   5628 H  HB1  . ALA   B 1 124 ? 41.565 -22.607 -5.548  1.00 13.96 ?  124 ALA   B HB1  1 
ATOM   5629 H  HB2  . ALA   B 1 124 ? 41.555 -21.440 -6.626  1.00 13.96 ?  124 ALA   B HB2  1 
ATOM   5630 H  HB3  . ALA   B 1 124 ? 41.120 -22.910 -7.043  1.00 13.96 ?  124 ALA   B HB3  1 
ATOM   5631 N  N    . PRO   B 1 125 ? 43.739 -24.462 -5.262  1.00 10.94 ?  125 PRO   B N    1 
ATOM   5632 C  CA   . PRO   B 1 125 ? 43.684 -25.827 -4.745  1.00 11.68 ?  125 PRO   B CA   1 
ATOM   5633 C  C    . PRO   B 1 125 ? 42.284 -26.101 -4.199  1.00 11.73 ?  125 PRO   B C    1 
ATOM   5634 O  O    . PRO   B 1 125 ? 41.486 -25.187 -3.985  1.00 12.19 ?  125 PRO   B O    1 
ATOM   5635 C  CB   . PRO   B 1 125 ? 44.670 -25.752 -3.577  1.00 12.59 ?  125 PRO   B CB   1 
ATOM   5636 C  CG   . PRO   B 1 125 ? 44.423 -24.369 -3.003  1.00 12.78 ?  125 PRO   B CG   1 
ATOM   5637 C  CD   . PRO   B 1 125 ? 44.069 -23.494 -4.198  1.00 11.43 ?  125 PRO   B CD   1 
ATOM   5638 H  HA   . PRO   B 1 125 ? 43.955 -26.490 -5.399  1.00 14.06 ?  125 PRO   B HA   1 
ATOM   5639 H  HB2  . PRO   B 1 125 ? 44.466 -26.439 -2.921  1.00 15.15 ?  125 PRO   B HB2  1 
ATOM   5640 H  HB3  . PRO   B 1 125 ? 45.578 -25.837 -3.900  1.00 15.15 ?  125 PRO   B HB3  1 
ATOM   5641 H  HG2  . PRO   B 1 125 ? 43.685 -24.397 -2.371  1.00 15.37 ?  125 PRO   B HG2  1 
ATOM   5642 H  HG3  . PRO   B 1 125 ? 45.230 -24.044 -2.564  1.00 15.37 ?  125 PRO   B HG3  1 
ATOM   5643 H  HD2  . PRO   B 1 125 ? 43.308 -22.929 -3.995  1.00 13.75 ?  125 PRO   B HD2  1 
ATOM   5644 H  HD3  . PRO   B 1 125 ? 44.842 -22.957 -4.462  1.00 13.75 ?  125 PRO   B HD3  1 
ATOM   5645 N  N    . LEU   B 1 126 ? 42.010 -27.382 -3.935  1.00 12.23 ?  126 LEU   B N    1 
ATOM   5646 C  CA   . LEU   B 1 126 ? 40.788 -27.748 -3.224  1.00 12.88 ?  126 LEU   B CA   1 
ATOM   5647 C  C    . LEU   B 1 126 ? 40.902 -27.347 -1.760  1.00 13.03 ?  126 LEU   B C    1 
ATOM   5648 O  O    . LEU   B 1 126 ? 41.797 -27.801 -1.042  1.00 14.53 ?  126 LEU   B O    1 
ATOM   5649 C  CB   . LEU   B 1 126 ? 40.531 -29.247 -3.340  1.00 14.05 ?  126 LEU   B CB   1 
ATOM   5650 C  CG   . LEU   B 1 126 ? 39.997 -29.726 -4.692  1.00 14.67 ?  126 LEU   B CG   1 
ATOM   5651 C  CD1  . LEU   B 1 126 ? 40.049 -31.239 -4.790  1.00 16.14 ?  126 LEU   B CD1  1 
ATOM   5652 C  CD2  . LEU   B 1 126 ? 38.576 -29.227 -4.928  1.00 14.96 ?  126 LEU   B CD2  1 
ATOM   5653 H  H    . LEU   B 1 126 ? 42.514 -28.048 -4.143  1.00 14.72 ?  126 LEU   B H    1 
ATOM   5654 H  HA   . LEU   B 1 126 ? 40.040 -27.271 -3.613  1.00 15.50 ?  126 LEU   B HA   1 
ATOM   5655 H  HB2  . LEU   B 1 126 ? 41.362 -29.712 -3.175  1.00 16.89 ?  126 LEU   B HB2  1 
ATOM   5656 H  HB3  . LEU   B 1 126 ? 39.878 -29.494 -2.667  1.00 16.89 ?  126 LEU   B HB3  1 
ATOM   5657 H  HG   . LEU   B 1 126 ? 40.558 -29.363 -5.395  1.00 17.64 ?  126 LEU   B HG   1 
ATOM   5658 H  HD11 . LEU   B 1 126 ? 39.703 -31.512 -5.655  1.00 19.41 ?  126 LEU   B HD11 1 
ATOM   5659 H  HD12 . LEU   B 1 126 ? 40.966 -31.532 -4.690  1.00 19.41 ?  126 LEU   B HD12 1 
ATOM   5660 H  HD13 . LEU   B 1 126 ? 39.500 -31.620 -4.083  1.00 19.41 ?  126 LEU   B HD13 1 
ATOM   5661 H  HD21 . LEU   B 1 126 ? 38.226 -29.637 -5.733  1.00 18.00 ?  126 LEU   B HD21 1 
ATOM   5662 H  HD22 . LEU   B 1 126 ? 38.025 -29.466 -4.167  1.00 18.00 ?  126 LEU   B HD22 1 
ATOM   5663 H  HD23 . LEU   B 1 126 ? 38.591 -28.260 -5.031  1.00 18.00 ?  126 LEU   B HD23 1 
ATOM   5664 N  N    . LEU   B 1 127 ? 39.975 -26.515 -1.303  1.00 12.74 ?  127 LEU   B N    1 
ATOM   5665 C  CA   . LEU   B 1 127 ? 40.027 -26.030 0.067   1.00 12.71 ?  127 LEU   B CA   1 
ATOM   5666 C  C    . LEU   B 1 127 ? 39.755 -27.152 1.061   1.00 12.55 ?  127 LEU   B C    1 
ATOM   5667 O  O    . LEU   B 1 127 ? 38.933 -28.050 0.830   1.00 12.84 ?  127 LEU   B O    1 
ATOM   5668 C  CB   . LEU   B 1 127 ? 39.010 -24.907 0.277   1.00 13.46 ?  127 LEU   B CB   1 
ATOM   5669 C  CG   . LEU   B 1 127 ? 39.192 -23.638 -0.557  1.00 14.01 ?  127 LEU   B CG   1 
ATOM   5670 C  CD1  . LEU   B 1 127 ? 38.066 -22.673 -0.239  1.00 14.22 ?  127 LEU   B CD1  1 
ATOM   5671 C  CD2  . LEU   B 1 127 ? 40.546 -22.990 -0.313  1.00 14.96 ?  127 LEU   B CD2  1 
ATOM   5672 H  H    . LEU   B 1 127 ? 39.305 -26.214 -1.761  1.00 15.33 ?  127 LEU   B H    1 
ATOM   5673 H  HA   . LEU   B 1 127 ? 40.912 -25.668 0.242   1.00 15.29 ?  127 LEU   B HA   1 
ATOM   5674 H  HB2  . LEU   B 1 127 ? 38.127 -25.255 0.077   1.00 16.19 ?  127 LEU   B HB2  1 
ATOM   5675 H  HB3  . LEU   B 1 127 ? 39.041 -24.638 1.210   1.00 16.19 ?  127 LEU   B HB3  1 
ATOM   5676 H  HG   . LEU   B 1 127 ? 39.121 -23.858 -1.497  1.00 16.85 ?  127 LEU   B HG   1 
ATOM   5677 H  HD11 . LEU   B 1 127 ? 38.181 -21.862 -0.764  1.00 17.11 ?  127 LEU   B HD11 1 
ATOM   5678 H  HD12 . LEU   B 1 127 ? 37.215 -23.086 -0.456  1.00 17.11 ?  127 LEU   B HD12 1 
ATOM   5679 H  HD13 . LEU   B 1 127 ? 38.092 -22.453 0.708   1.00 17.11 ?  127 LEU   B HD13 1 
ATOM   5680 H  HD21 . LEU   B 1 127 ? 40.580 -22.139 -0.779  1.00 17.99 ?  127 LEU   B HD21 1 
ATOM   5681 H  HD22 . LEU   B 1 127 ? 40.660 -22.847 0.641   1.00 17.99 ?  127 LEU   B HD22 1 
ATOM   5682 H  HD23 . LEU   B 1 127 ? 41.237 -23.579 -0.646  1.00 17.99 ?  127 LEU   B HD23 1 
ATOM   5683 N  N    . SER   B 1 128 ? 40.444 -27.072 2.192   1.00 12.67 ?  128 SER   B N    1 
ATOM   5684 C  CA   . SER   B 1 128 ? 40.338 -27.990 3.314   1.00 13.01 ?  128 SER   B CA   1 
ATOM   5685 C  C    . SER   B 1 128 ? 40.830 -29.396 2.992   1.00 14.01 ?  128 SER   B C    1 
ATOM   5686 O  O    . SER   B 1 128 ? 40.736 -30.279 3.847   1.00 15.21 ?  128 SER   B O    1 
ATOM   5687 C  CB   . SER   B 1 128 ? 38.939 -28.008 3.942   1.00 13.43 ?  128 SER   B CB   1 
ATOM   5688 O  OG   . SER   B 1 128 ? 38.625 -26.736 4.495   1.00 14.17 ?  128 SER   B OG   1 
ATOM   5689 H  H    . SER   B 1 128 ? 41.018 -26.446 2.340   1.00 15.24 ?  128 SER   B H    1 
ATOM   5690 H  HA   . SER   B 1 128 ? 40.928 -27.657 4.002   1.00 15.66 ?  128 SER   B HA   1 
ATOM   5691 H  HB2  . SER   B 1 128 ? 38.285 -28.237 3.261   1.00 16.16 ?  128 SER   B HB2  1 
ATOM   5692 H  HB3  . SER   B 1 128 ? 38.920 -28.684 4.649   1.00 16.16 ?  128 SER   B HB3  1 
ATOM   5693 H  HG   . SER   B 1 128 ? 39.185 -26.544 5.090   1.00 17.04 ?  128 SER   B HG   1 
ATOM   5694 N  N    . ALA   B 1 129 ? 41.405 -29.612 1.807   1.00 14.92 ?  129 ALA   B N    1 
ATOM   5695 C  CA   . ALA   B 1 129 ? 41.949 -30.910 1.442   1.00 16.16 ?  129 ALA   B CA   1 
ATOM   5696 C  C    . ALA   B 1 129 ? 43.342 -31.093 2.036   1.00 15.42 ?  129 ALA   B C    1 
ATOM   5697 O  O    . ALA   B 1 129 ? 43.901 -30.197 2.682   1.00 15.05 ?  129 ALA   B O    1 
ATOM   5698 C  CB   . ALA   B 1 129 ? 41.990 -31.065 -0.076  1.00 18.10 ?  129 ALA   B CB   1 
ATOM   5699 H  H    . ALA   B 1 129 ? 41.489 -29.013 1.192   1.00 17.95 ?  129 ALA   B H    1 
ATOM   5700 H  HA   . ALA   B 1 129 ? 41.376 -31.603 1.799   1.00 19.43 ?  129 ALA   B HA   1 
ATOM   5701 H  HB1  . ALA   B 1 129 ? 42.347 -31.941 -0.293  1.00 21.76 ?  129 ALA   B HB1  1 
ATOM   5702 H  HB2  . ALA   B 1 129 ? 41.089 -30.980 -0.425  1.00 21.76 ?  129 ALA   B HB2  1 
ATOM   5703 H  HB3  . ALA   B 1 129 ? 42.558 -30.374 -0.450  1.00 21.76 ?  129 ALA   B HB3  1 
ATOM   5704 N  N    . GLY   B 1 130 ? 43.900 -32.282 1.811   1.00 15.30 ?  130 GLY   B N    1 
ATOM   5705 C  CA   . GLY   B 1 130 ? 45.286 -32.527 2.165   1.00 15.89 ?  130 GLY   B CA   1 
ATOM   5706 C  C    . GLY   B 1 130 ? 45.498 -32.430 3.658   1.00 15.83 ?  130 GLY   B C    1 
ATOM   5707 O  O    . GLY   B 1 130 ? 44.796 -33.069 4.456   1.00 16.65 ?  130 GLY   B O    1 
ATOM   5708 H  H    . GLY   B 1 130 ? 43.498 -32.955 1.453   1.00 18.40 ?  130 GLY   B H    1 
ATOM   5709 H  HA2  . GLY   B 1 130 ? 45.545 -33.417 1.871   1.00 19.11 ?  130 GLY   B HA2  1 
ATOM   5710 H  HA3  . GLY   B 1 130 ? 45.856 -31.878 1.725   1.00 19.11 ?  130 GLY   B HA3  1 
ATOM   5711 N  N    . ILE   B 1 131 ? 46.472 -31.600 4.046   1.00 16.07 ?  131 ILE   B N    1 
ATOM   5712 C  CA   . ILE   B 1 131 ? 46.832 -31.463 5.450   1.00 16.75 ?  131 ILE   B CA   1 
ATOM   5713 C  C    . ILE   B 1 131 ? 45.717 -30.862 6.287   1.00 16.26 ?  131 ILE   B C    1 
ATOM   5714 O  O    . ILE   B 1 131 ? 45.796 -30.922 7.518   1.00 17.97 ?  131 ILE   B O    1 
ATOM   5715 C  CB   . ILE   B 1 131 ? 48.153 -30.686 5.644   1.00 18.60 ?  131 ILE   B CB   1 
ATOM   5716 C  CG1  . ILE   B 1 131 ? 47.985 -29.207 5.260   1.00 19.08 ?  131 ILE   B CG1  1 
ATOM   5717 C  CG2  . ILE   B 1 131 ? 49.277 -31.343 4.844   1.00 19.55 ?  131 ILE   B CG2  1 
ATOM   5718 C  CD1  . ILE   B 1 131 ? 49.200 -28.346 5.578   1.00 20.12 ?  131 ILE   B CD1  1 
ATOM   5719 H  H    . ILE   B 1 131 ? 46.936 -31.111 3.514   1.00 19.32 ?  131 ILE   B H    1 
ATOM   5720 H  HA   . ILE   B 1 131 ? 46.977 -32.354 5.801   1.00 20.14 ?  131 ILE   B HA   1 
ATOM   5721 H  HB   . ILE   B 1 131 ? 48.384 -30.728 6.585   1.00 22.36 ?  131 ILE   B HB   1 
ATOM   5722 H  HG12 . ILE   B 1 131 ? 47.819 -29.153 4.306   1.00 22.94 ?  131 ILE   B HG12 1 
ATOM   5723 H  HG13 . ILE   B 1 131 ? 47.229 -28.835 5.744   1.00 22.94 ?  131 ILE   B HG13 1 
ATOM   5724 H  HG21 . ILE   B 1 131 ? 50.118 -30.938 5.099   1.00 23.50 ?  131 ILE   B HG21 1 
ATOM   5725 H  HG22 . ILE   B 1 131 ? 49.288 -32.291 5.042   1.00 23.50 ?  131 ILE   B HG22 1 
ATOM   5726 H  HG23 . ILE   B 1 131 ? 49.110 -31.202 3.899   1.00 23.50 ?  131 ILE   B HG23 1 
ATOM   5727 H  HD11 . ILE   B 1 131 ? 48.986 -27.420 5.385   1.00 24.19 ?  131 ILE   B HD11 1 
ATOM   5728 H  HD12 . ILE   B 1 131 ? 49.418 -28.446 6.518   1.00 24.19 ?  131 ILE   B HD12 1 
ATOM   5729 H  HD13 . ILE   B 1 131 ? 49.944 -28.636 5.032   1.00 24.19 ?  131 ILE   B HD13 1 
ATOM   5730 N  N    . PHE   B 1 132 ? 44.684 -30.289 5.656   1.00 15.06 ?  132 PHE   B N    1 
ATOM   5731 C  CA   . PHE   B 1 132 ? 43.523 -29.783 6.380   1.00 15.45 ?  132 PHE   B CA   1 
ATOM   5732 C  C    . PHE   B 1 132 ? 42.502 -30.873 6.707   1.00 16.99 ?  132 PHE   B C    1 
ATOM   5733 O  O    . PHE   B 1 132 ? 41.596 -30.622 7.508   1.00 18.57 ?  132 PHE   B O    1 
ATOM   5734 C  CB   . PHE   B 1 132 ? 42.855 -28.650 5.589   1.00 14.50 ?  132 PHE   B CB   1 
ATOM   5735 C  CG   . PHE   B 1 132 ? 43.547 -27.307 5.716   1.00 14.43 ?  132 PHE   B CG   1 
ATOM   5736 C  CD1  . PHE   B 1 132 ? 44.842 -27.111 5.256   1.00 15.55 ?  132 PHE   B CD1  1 
ATOM   5737 C  CD2  . PHE   B 1 132 ? 42.865 -26.218 6.245   1.00 14.02 ?  132 PHE   B CD2  1 
ATOM   5738 C  CE1  . PHE   B 1 132 ? 45.457 -25.873 5.364   1.00 15.80 ?  132 PHE   B CE1  1 
ATOM   5739 C  CE2  . PHE   B 1 132 ? 43.474 -24.971 6.347   1.00 14.69 ?  132 PHE   B CE2  1 
ATOM   5740 C  CZ   . PHE   B 1 132 ? 44.766 -24.802 5.904   1.00 15.46 ?  132 PHE   B CZ   1 
ATOM   5741 H  H    . PHE   B 1 132 ? 44.633 -30.182 4.801   1.00 18.12 ?  132 PHE   B H    1 
ATOM   5742 H  HA   . PHE   B 1 132 ? 43.826 -29.404 7.217   1.00 18.58 ?  132 PHE   B HA   1 
ATOM   5743 H  HB2  . PHE   B 1 132 ? 42.857 -28.887 4.649   1.00 17.44 ?  132 PHE   B HB2  1 
ATOM   5744 H  HB3  . PHE   B 1 132 ? 41.945 -28.543 5.901   1.00 17.44 ?  132 PHE   B HB3  1 
ATOM   5745 H  HD1  . PHE   B 1 132 ? 45.315 -27.829 4.895   1.00 18.70 ?  132 PHE   B HD1  1 
ATOM   5746 H  HD2  . PHE   B 1 132 ? 41.990 -26.328 6.544   1.00 16.86 ?  132 PHE   B HD2  1 
ATOM   5747 H  HE1  . PHE   B 1 132 ? 46.332 -25.760 5.065   1.00 19.00 ?  132 PHE   B HE1  1 
ATOM   5748 H  HE2  . PHE   B 1 132 ? 43.010 -24.252 6.715   1.00 17.66 ?  132 PHE   B HE2  1 
ATOM   5749 H  HZ   . PHE   B 1 132 ? 45.180 -23.967 5.978   1.00 18.59 ?  132 PHE   B HZ   1 
ATOM   5750 N  N    . GLY   B 1 133 ? 42.606 -32.065 6.107   1.00 16.60 ?  133 GLY   B N    1 
ATOM   5751 C  CA   . GLY   B 1 133 ? 41.895 -33.233 6.601   1.00 17.20 ?  133 GLY   B CA   1 
ATOM   5752 C  C    . GLY   B 1 133 ? 40.497 -33.490 6.073   1.00 17.32 ?  133 GLY   B C    1 
ATOM   5753 O  O    . GLY   B 1 133 ? 39.905 -34.509 6.447   1.00 19.24 ?  133 GLY   B O    1 
ATOM   5754 H  H    . GLY   B 1 133 ? 43.091 -32.214 5.411   1.00 19.96 ?  133 GLY   B H    1 
ATOM   5755 H  HA2  . GLY   B 1 133 ? 42.427 -34.015 6.401   1.00 20.67 ?  133 GLY   B HA2  1 
ATOM   5756 H  HA3  . GLY   B 1 133 ? 41.829 -33.158 7.564   1.00 20.67 ?  133 GLY   B HA3  1 
ATOM   5757 N  N    . ALA   B 1 134 ? 39.938 -32.622 5.236   1.00 16.64 ?  134 ALA   B N    1 
ATOM   5758 C  CA   . ALA   B 1 134 ? 38.614 -32.898 4.697   1.00 16.71 ?  134 ALA   B CA   1 
ATOM   5759 C  C    . ALA   B 1 134 ? 38.697 -33.898 3.547   1.00 16.52 ?  134 ALA   B C    1 
ATOM   5760 O  O    . ALA   B 1 134 ? 39.747 -34.086 2.925   1.00 17.80 ?  134 ALA   B O    1 
ATOM   5761 C  CB   . ALA   B 1 134 ? 37.945 -31.611 4.215   1.00 17.30 ?  134 ALA   B CB   1 
ATOM   5762 H  H    . ALA   B 1 134 ? 40.292 -31.879 4.972   1.00 20.01 ?  134 ALA   B H    1 
ATOM   5763 H  HA   . ALA   B 1 134 ? 38.061 -33.280 5.397   1.00 20.09 ?  134 ALA   B HA   1 
ATOM   5764 H  HB1  . ALA   B 1 134 ? 37.059 -31.823 3.882   1.00 20.80 ?  134 ALA   B HB1  1 
ATOM   5765 H  HB2  . ALA   B 1 134 ? 37.880 -30.991 4.958   1.00 20.80 ?  134 ALA   B HB2  1 
ATOM   5766 H  HB3  . ALA   B 1 134 ? 38.481 -31.223 3.506   1.00 20.80 ?  134 ALA   B HB3  1 
ATOM   5767 N  N    . ASP   B 1 135 ? 37.564 -34.531 3.264   1.00 16.61 ?  135 ASP   B N    1 
ATOM   5768 C  CA   . ASP   B 1 135 ? 37.461 -35.424 2.120   1.00 17.19 ?  135 ASP   B CA   1 
ATOM   5769 C  C    . ASP   B 1 135 ? 37.556 -34.590 0.848   1.00 16.30 ?  135 ASP   B C    1 
ATOM   5770 O  O    . ASP   B 1 135 ? 36.706 -33.714 0.631   1.00 16.60 ?  135 ASP   B O    1 
ATOM   5771 C  CB   . ASP   B 1 135 ? 36.120 -36.152 2.182   1.00 19.03 ?  135 ASP   B CB   1 
ATOM   5772 C  CG   . ASP   B 1 135 ? 35.921 -37.125 1.036   1.00 20.78 ?  135 ASP   B CG   1 
ATOM   5773 O  OD1  . ASP   B 1 135 ? 36.788 -37.191 0.140   1.00 20.58 ?  135 ASP   B OD1  1 
ATOM   5774 O  OD2  . ASP   B 1 135 ? 34.898 -37.849 1.047   1.00 23.90 -1 135 ASP   B OD2  1 
ATOM   5775 H  H    . ASP   B 1 135 ? 36.838 -34.457 3.719   1.00 19.97 ?  135 ASP   B H    1 
ATOM   5776 H  HA   . ASP   B 1 135 ? 38.177 -36.079 2.147   1.00 20.66 ?  135 ASP   B HA   1 
ATOM   5777 H  HB2  . ASP   B 1 135 ? 36.076 -36.655 3.010   1.00 22.88 ?  135 ASP   B HB2  1 
ATOM   5778 H  HB3  . ASP   B 1 135 ? 35.407 -35.497 2.152   1.00 22.88 ?  135 ASP   B HB3  1 
ATOM   5779 N  N    . PRO   B 1 136 ? 38.560 -34.802 -0.005  1.00 16.37 ?  136 PRO   B N    1 
ATOM   5780 C  CA   . PRO   B 1 136 ? 38.665 -33.967 -1.214  1.00 15.73 ?  136 PRO   B CA   1 
ATOM   5781 C  C    . PRO   B 1 136 ? 37.482 -34.118 -2.150  1.00 15.22 ?  136 PRO   B C    1 
ATOM   5782 O  O    . PRO   B 1 136 ? 37.156 -33.170 -2.872  1.00 14.53 ?  136 PRO   B O    1 
ATOM   5783 C  CB   . PRO   B 1 136 ? 39.982 -34.433 -1.853  1.00 17.02 ?  136 PRO   B CB   1 
ATOM   5784 C  CG   . PRO   B 1 136 ? 40.179 -35.829 -1.328  1.00 18.12 ?  136 PRO   B CG   1 
ATOM   5785 C  CD   . PRO   B 1 136 ? 39.626 -35.813 0.067   1.00 17.52 ?  136 PRO   B CD   1 
ATOM   5786 H  HA   . PRO   B 1 136 ? 38.751 -33.033 -0.969  1.00 18.92 ?  136 PRO   B HA   1 
ATOM   5787 H  HB2  . PRO   B 1 136 ? 39.896 -34.440 -2.821  1.00 20.47 ?  136 PRO   B HB2  1 
ATOM   5788 H  HB3  . PRO   B 1 136 ? 40.707 -33.855 -1.575  1.00 20.47 ?  136 PRO   B HB3  1 
ATOM   5789 H  HG2  . PRO   B 1 136 ? 39.691 -36.463 -1.879  1.00 21.78 ?  136 PRO   B HG2  1 
ATOM   5790 H  HG3  . PRO   B 1 136 ? 41.125 -36.047 -1.315  1.00 21.78 ?  136 PRO   B HG3  1 
ATOM   5791 H  HD2  . PRO   B 1 136 ? 39.251 -36.679 0.297   1.00 21.06 ?  136 PRO   B HD2  1 
ATOM   5792 H  HD3  . PRO   B 1 136 ? 40.306 -35.541 0.705   1.00 21.06 ?  136 PRO   B HD3  1 
ATOM   5793 N  N    . ILE   B 1 137 ? 36.825 -35.283 -2.156  1.00 15.28 ?  137 ILE   B N    1 
ATOM   5794 C  CA   . ILE   B 1 137 ? 35.606 -35.449 -2.946  1.00 15.96 ?  137 ILE   B CA   1 
ATOM   5795 C  C    . ILE   B 1 137 ? 34.532 -34.480 -2.467  1.00 15.44 ?  137 ILE   B C    1 
ATOM   5796 O  O    . ILE   B 1 137 ? 33.813 -33.872 -3.270  1.00 15.14 ?  137 ILE   B O    1 
ATOM   5797 C  CB   . ILE   B 1 137 ? 35.135 -36.917 -2.889  1.00 17.74 ?  137 ILE   B CB   1 
ATOM   5798 C  CG1  . ILE   B 1 137 ? 36.134 -37.821 -3.616  1.00 19.95 ?  137 ILE   B CG1  1 
ATOM   5799 C  CG2  . ILE   B 1 137 ? 33.743 -37.070 -3.487  1.00 18.39 ?  137 ILE   B CG2  1 
ATOM   5800 C  CD1  . ILE   B 1 137 ? 35.843 -39.307 -3.471  1.00 22.25 ?  137 ILE   B CD1  1 
ATOM   5801 H  H    . ILE   B 1 137 ? 37.059 -35.985 -1.718  1.00 18.38 ?  137 ILE   B H    1 
ATOM   5802 H  HA   . ILE   B 1 137 ? 35.801 -35.241 -3.875  1.00 19.19 ?  137 ILE   B HA   1 
ATOM   5803 H  HB   . ILE   B 1 137 ? 35.096 -37.191 -1.963  1.00 21.33 ?  137 ILE   B HB   1 
ATOM   5804 H  HG12 . ILE   B 1 137 ? 36.118 -37.612 -4.563  1.00 23.98 ?  137 ILE   B HG12 1 
ATOM   5805 H  HG13 . ILE   B 1 137 ? 37.019 -37.660 -3.258  1.00 23.98 ?  137 ILE   B HG13 1 
ATOM   5806 H  HG21 . ILE   B 1 137 ? 33.536 -38.015 -3.584  1.00 22.10 ?  137 ILE   B HG21 1 
ATOM   5807 H  HG22 . ILE   B 1 137 ? 33.095 -36.661 -2.894  1.00 22.10 ?  137 ILE   B HG22 1 
ATOM   5808 H  HG23 . ILE   B 1 137 ? 33.720 -36.640 -4.355  1.00 22.10 ?  137 ILE   B HG23 1 
ATOM   5809 H  HD11 . ILE   B 1 137 ? 36.629 -39.810 -3.738  1.00 26.74 ?  137 ILE   B HD11 1 
ATOM   5810 H  HD12 . ILE   B 1 137 ? 35.629 -39.497 -2.544  1.00 26.74 ?  137 ILE   B HD12 1 
ATOM   5811 H  HD13 . ILE   B 1 137 ? 35.092 -39.543 -4.039  1.00 26.74 ?  137 ILE   B HD13 1 
ATOM   5812 N  N    . HIS   B 1 138 ? 34.402 -34.329 -1.151  1.00 15.72 ?  138 HIS   B N    1 
ATOM   5813 C  CA   . HIS   B 1 138 ? 33.453 -33.365 -0.615  1.00 16.08 ?  138 HIS   B CA   1 
ATOM   5814 C  C    . HIS   B 1 138 ? 33.874 -31.937 -0.932  1.00 15.25 ?  138 HIS   B C    1 
ATOM   5815 O  O    . HIS   B 1 138 ? 33.028 -31.093 -1.236  1.00 15.52 ?  138 HIS   B O    1 
ATOM   5816 C  CB   . HIS   B 1 138 ? 33.325 -33.546 0.890   1.00 17.43 ?  138 HIS   B CB   1 
ATOM   5817 C  CG   . HIS   B 1 138 ? 32.383 -32.571 1.517   1.00 18.23 ?  138 HIS   B CG   1 
ATOM   5818 N  ND1  . HIS   B 1 138 ? 31.045 -32.522 1.192   1.00 19.58 ?  138 HIS   B ND1  1 
ATOM   5819 C  CD2  . HIS   B 1 138 ? 32.589 -31.584 2.420   1.00 18.71 ?  138 HIS   B CD2  1 
ATOM   5820 C  CE1  . HIS   B 1 138 ? 30.462 -31.558 1.882   1.00 19.54 ?  138 HIS   B CE1  1 
ATOM   5821 N  NE2  . HIS   B 1 138 ? 31.377 -30.977 2.638   1.00 18.82 ?  138 HIS   B NE2  1 
ATOM   5822 H  H    . HIS   B 1 138 ? 34.848 -34.767 -0.562  1.00 18.90 ?  138 HIS   B H    1 
ATOM   5823 H  HA   . HIS   B 1 138 ? 32.582 -33.523 -1.015  1.00 19.34 ?  138 HIS   B HA   1 
ATOM   5824 H  HB2  . HIS   B 1 138 ? 32.991 -34.439 1.071   1.00 20.95 ?  138 HIS   B HB2  1 
ATOM   5825 H  HB3  . HIS   B 1 138 ? 34.194 -33.426 1.297   1.00 20.95 ?  138 HIS   B HB3  1 
ATOM   5826 H  HD1  . HIS   B 1 138 ? 30.649 -33.045 0.631   1.00 23.53 ?  138 HIS   B HD1  1 
ATOM   5827 H  HD2  . HIS   B 1 138 ? 33.389 -31.365 2.830   1.00 22.49 ?  138 HIS   B HD2  1 
ATOM   5828 H  HE1  . HIS   B 1 138 ? 29.554 -31.338 1.844   1.00 23.49 ?  138 HIS   B HE1  1 
ATOM   5829 N  N    . SER   B 1 139 ? 35.169 -31.638 -0.856  1.00 14.73 ?  139 SER   B N    1 
ATOM   5830 C  CA   . SER   B 1 139 ? 35.605 -30.286 -1.175  1.00 14.12 ?  139 SER   B CA   1 
ATOM   5831 C  C    . SER   B 1 139 ? 35.272 -29.933 -2.615  1.00 13.30 ?  139 SER   B C    1 
ATOM   5832 O  O    . SER   B 1 139 ? 34.824 -28.817 -2.898  1.00 13.46 ?  139 SER   B O    1 
ATOM   5833 C  CB   . SER   B 1 139 ? 37.098 -30.150 -0.907  1.00 14.34 ?  139 SER   B CB   1 
ATOM   5834 O  OG   . SER   B 1 139 ? 37.512 -28.815 -1.158  1.00 14.64 ?  139 SER   B OG   1 
ATOM   5835 H  H    . SER   B 1 139 ? 35.790 -32.185 -0.636  1.00 17.71 ?  139 SER   B H    1 
ATOM   5836 H  HA   . SER   B 1 139 ? 35.137 -29.665 -0.601  1.00 16.98 ?  139 SER   B HA   1 
ATOM   5837 H  HB2  . SER   B 1 139 ? 37.277 -30.371 0.022   1.00 17.25 ?  139 SER   B HB2  1 
ATOM   5838 H  HB3  . SER   B 1 139 ? 37.587 -30.752 -1.491  1.00 17.25 ?  139 SER   B HB3  1 
ATOM   5839 H  HG   . SER   B 1 139 ? 38.340 -28.739 -1.008  1.00 17.61 ?  139 SER   B HG   1 
ATOM   5840 N  N    . LEU   B 1 140 ? 35.462 -30.876 -3.538  1.00 13.10 ?  140 LEU   B N    1 
ATOM   5841 C  CA   . LEU   B 1 140 ? 35.096 -30.625 -4.927  1.00 13.36 ?  140 LEU   B CA   1 
ATOM   5842 C  C    . LEU   B 1 140 ? 33.592 -30.399 -5.058  1.00 13.30 ?  140 LEU   B C    1 
ATOM   5843 O  O    . LEU   B 1 140 ? 33.154 -29.511 -5.796  1.00 13.48 ?  140 LEU   B O    1 
ATOM   5844 C  CB   . LEU   B 1 140 ? 35.564 -31.788 -5.806  1.00 13.53 ?  140 LEU   B CB   1 
ATOM   5845 C  CG   . LEU   B 1 140 ? 35.197 -31.679 -7.278  1.00 13.98 ?  140 LEU   B CG   1 
ATOM   5846 C  CD1  . LEU   B 1 140 ? 35.764 -30.409 -7.868  1.00 14.82 ?  140 LEU   B CD1  1 
ATOM   5847 C  CD2  . LEU   B 1 140 ? 35.678 -32.903 -8.035  1.00 14.76 ?  140 LEU   B CD2  1 
ATOM   5848 H  H    . LEU   B 1 140 ? 35.797 -31.651 -3.391  1.00 15.75 ?  140 LEU   B H    1 
ATOM   5849 H  HA   . LEU   B 1 140 ? 35.550 -29.822 -5.230  1.00 16.07 ?  140 LEU   B HA   1 
ATOM   5850 H  HB2  . LEU   B 1 140 ? 36.536 -31.844 -5.756  1.00 16.27 ?  140 LEU   B HB2  1 
ATOM   5851 H  HB3  . LEU   B 1 140 ? 35.177 -32.608 -5.471  1.00 16.27 ?  140 LEU   B HB3  1 
ATOM   5852 H  HG   . LEU   B 1 140 ? 34.231 -31.635 -7.358  1.00 16.82 ?  140 LEU   B HG   1 
ATOM   5853 H  HD11 . LEU   B 1 140 ? 35.657 -30.433 -8.830  1.00 17.82 ?  140 LEU   B HD11 1 
ATOM   5854 H  HD12 . LEU   B 1 140 ? 35.281 -29.646 -7.503  1.00 17.82 ?  140 LEU   B HD12 1 
ATOM   5855 H  HD13 . LEU   B 1 140 ? 36.703 -30.344 -7.638  1.00 17.82 ?  140 LEU   B HD13 1 
ATOM   5856 H  HD21 . LEU   B 1 140 ? 35.425 -32.808 -8.967  1.00 17.75 ?  140 LEU   B HD21 1 
ATOM   5857 H  HD22 . LEU   B 1 140 ? 36.637 -32.964 -7.953  1.00 17.75 ?  140 LEU   B HD22 1 
ATOM   5858 H  HD23 . LEU   B 1 140 ? 35.254 -33.686 -7.654  1.00 17.75 ?  140 LEU   B HD23 1 
ATOM   5859 N  N    . ARG   B 1 141 ? 32.790 -31.190 -4.342  1.00 13.79 ?  141 ARG   B N    1 
ATOM   5860 C  CA   . ARG   B 1 141 ? 31.339 -31.016 -4.332  1.00 14.66 ?  141 ARG   B CA   1 
ATOM   5861 C  C    . ARG   B 1 141 ? 30.959 -29.607 -3.901  1.00 14.19 ?  141 ARG   B C    1 
ATOM   5862 O  O    . ARG   B 1 141 ? 30.152 -28.930 -4.558  1.00 14.21 ?  141 ARG   B O    1 
ATOM   5863 C  CB   . ARG   B 1 141 ? 30.753 -32.046 -3.358  1.00 16.31 ?  141 ARG   B CB   1 
ATOM   5864 C  CG   . ARG   B 1 141 ? 29.287 -31.930 -3.030  1.00 18.47 ?  141 ARG   B CG   1 
ATOM   5865 C  CD   . ARG   B 1 141 ? 28.484 -32.569 -4.095  1.00 20.12 ?  141 ARG   B CD   1 
ATOM   5866 N  NE   . ARG   B 1 141 ? 28.228 -31.662 -5.203  1.00 20.69 ?  141 ARG   B NE   1 
ATOM   5867 C  CZ   . ARG   B 1 141 ? 28.244 -32.011 -6.481  1.00 20.40 ?  141 ARG   B CZ   1 
ATOM   5868 N  NH1  . ARG   B 1 141 ? 28.681 -33.200 -6.872  1.00 20.31 ?  141 ARG   B NH1  1 
ATOM   5869 N  NH2  . ARG   B 1 141 ? 27.802 -31.147 -7.391  1.00 21.11 ?  141 ARG   B NH2  1 
ATOM   5870 H  H    . ARG   B 1 141 ? 33.073 -31.835 -3.848  1.00 16.59 ?  141 ARG   B H    1 
ATOM   5871 H  HA   . ARG   B 1 141 ? 30.985 -31.181 -5.217  1.00 17.62 ?  141 ARG   B HA   1 
ATOM   5872 H  HB2  . ARG   B 1 141 ? 30.906 -32.934 -3.730  1.00 19.61 ?  141 ARG   B HB2  1 
ATOM   5873 H  HB3  . ARG   B 1 141 ? 31.238 -31.979 -2.521  1.00 19.61 ?  141 ARG   B HB3  1 
ATOM   5874 H  HG2  . ARG   B 1 141 ? 29.112 -32.382 -2.193  1.00 22.20 ?  141 ARG   B HG2  1 
ATOM   5875 H  HG3  . ARG   B 1 141 ? 29.032 -30.995 -2.967  1.00 22.20 ?  141 ARG   B HG3  1 
ATOM   5876 H  HD2  . ARG   B 1 141 ? 28.960 -33.350 -4.428  1.00 24.19 ?  141 ARG   B HD2  1 
ATOM   5877 H  HD3  . ARG   B 1 141 ? 27.635 -32.844 -3.723  1.00 24.19 ?  141 ARG   B HD3  1 
ATOM   5878 H  HE   . ARG   B 1 141 ? 28.031 -30.847 -5.011  1.00 24.87 ?  141 ARG   B HE   1 
ATOM   5879 H  HH11 . ARG   B 1 141 ? 28.956 -33.775 -6.296  1.00 24.41 ?  141 ARG   B HH11 1 
ATOM   5880 H  HH12 . ARG   B 1 141 ? 28.687 -33.397 -7.707  1.00 24.41 ?  141 ARG   B HH12 1 
ATOM   5881 H  HH21 . ARG   B 1 141 ? 27.524 -30.368 -7.149  1.00 25.37 ?  141 ARG   B HH21 1 
ATOM   5882 H  HH22 . ARG   B 1 141 ? 27.826 -31.350 -8.227  1.00 25.37 ?  141 ARG   B HH22 1 
ATOM   5883 N  N    . VAL   B 1 142 ? 31.505 -29.160 -2.772  1.00 13.92 ?  142 VAL   B N    1 
ATOM   5884 C  CA   . VAL   B 1 142 ? 31.174 -27.829 -2.282  1.00 13.62 ?  142 VAL   B CA   1 
ATOM   5885 C  C    . VAL   B 1 142 ? 31.646 -26.766 -3.267  1.00 13.58 ?  142 VAL   B C    1 
ATOM   5886 O  O    . VAL   B 1 142 ? 30.945 -25.779 -3.521  1.00 13.89 ?  142 VAL   B O    1 
ATOM   5887 C  CB   . VAL   B 1 142 ? 31.717 -27.608 -0.856  1.00 14.43 ?  142 VAL   B CB   1 
ATOM   5888 C  CG1  . VAL   B 1 142 ? 31.402 -26.178 -0.379  1.00 14.35 ?  142 VAL   B CG1  1 
ATOM   5889 C  CG2  . VAL   B 1 142 ? 31.124 -28.630 0.104   1.00 15.09 ?  142 VAL   B CG2  1 
ATOM   5890 H  H    . VAL   B 1 142 ? 32.061 -29.601 -2.280  1.00 16.75 ?  142 VAL   B H    1 
ATOM   5891 H  HA   . VAL   B 1 142 ? 30.214 -27.758 -2.230  1.00 16.38 ?  142 VAL   B HA   1 
ATOM   5892 H  HB   . VAL   B 1 142 ? 32.680 -27.721 -0.856  1.00 17.35 ?  142 VAL   B HB   1 
ATOM   5893 H  HG11 . VAL   B 1 142 ? 31.582 -26.120 0.571   1.00 17.26 ?  142 VAL   B HG11 1 
ATOM   5894 H  HG12 . VAL   B 1 142 ? 31.965 -25.554 -0.862  1.00 17.26 ?  142 VAL   B HG12 1 
ATOM   5895 H  HG13 . VAL   B 1 142 ? 30.468 -25.990 -0.553  1.00 17.26 ?  142 VAL   B HG13 1 
ATOM   5896 H  HG21 . VAL   B 1 142 ? 31.445 -28.447 1.000   1.00 18.15 ?  142 VAL   B HG21 1 
ATOM   5897 H  HG22 . VAL   B 1 142 ? 30.155 -28.559 0.079   1.00 18.15 ?  142 VAL   B HG22 1 
ATOM   5898 H  HG23 . VAL   B 1 142 ? 31.396 -29.519 -0.171  1.00 18.15 ?  142 VAL   B HG23 1 
ATOM   5899 N  N    . CYS   B 1 143 ? 32.824 -26.967 -3.860  1.00 12.95 ?  143 CYS   B N    1 
ATOM   5900 C  CA   . CYS   B 1 143 ? 33.320 -26.025 -4.859  1.00 12.94 ?  143 CYS   B CA   1 
ATOM   5901 C  C    . CYS   B 1 143 ? 32.323 -25.874 -6.002  1.00 12.75 ?  143 CYS   B C    1 
ATOM   5902 O  O    . CYS   B 1 143 ? 31.912 -24.764 -6.352  1.00 13.17 ?  143 CYS   B O    1 
ATOM   5903 C  CB   . CYS   B 1 143 ? 34.676 -26.510 -5.384  1.00 13.26 ?  143 CYS   B CB   1 
ATOM   5904 S  SG   . CYS   B 1 143 ? 35.423 -25.409 -6.604  1.00 13.50 ?  143 CYS   B SG   1 
ATOM   5905 H  H    . CYS   B 1 143 ? 33.353 -27.629 -3.702  1.00 15.57 ?  143 CYS   B H    1 
ATOM   5906 H  HA   . CYS   B 1 143 ? 33.448 -25.156 -4.448  1.00 15.57 ?  143 CYS   B HA   1 
ATOM   5907 H  HB2  . CYS   B 1 143 ? 35.298 -26.588 -4.643  1.00 15.94 ?  143 CYS   B HB2  1 
ATOM   5908 H  HB3  . CYS   B 1 143 ? 34.561 -27.373 -5.802  1.00 15.94 ?  143 CYS   B HB3  1 
ATOM   5909 H  HG   . CYS   B 1 143 ? 36.499 -25.840 -6.924  1.00 16.24 ?  143 CYS   B HG   1 
ATOM   5910 N  N    . VAL   B 1 144 ? 31.914 -26.994 -6.595  1.00 13.26 ?  144 VAL   B N    1 
ATOM   5911 C  CA   . VAL   B 1 144 ? 31.009 -26.932 -7.739  1.00 14.15 ?  144 VAL   B CA   1 
ATOM   5912 C  C    . VAL   B 1 144 ? 29.665 -26.325 -7.364  1.00 14.31 ?  144 VAL   B C    1 
ATOM   5913 O  O    . VAL   B 1 144 ? 29.048 -25.620 -8.171  1.00 15.45 ?  144 VAL   B O    1 
ATOM   5914 C  CB   . VAL   B 1 144 ? 30.859 -28.339 -8.335  1.00 16.88 ?  144 VAL   B CB   1 
ATOM   5915 C  CG1  . VAL   B 1 144 ? 29.598 -28.451 -9.183  1.00 19.56 ?  144 VAL   B CG1  1 
ATOM   5916 C  CG2  . VAL   B 1 144 ? 32.118 -28.726 -9.116  1.00 17.06 ?  144 VAL   B CG2  1 
ATOM   5917 H  H    . VAL   B 1 144 ? 32.144 -27.789 -6.359  1.00 15.95 ?  144 VAL   B H    1 
ATOM   5918 H  HA   . VAL   B 1 144 ? 31.406 -26.366 -8.418  1.00 17.02 ?  144 VAL   B HA   1 
ATOM   5919 H  HB   . VAL   B 1 144 ? 30.776 -28.973 -7.606  1.00 20.30 ?  144 VAL   B HB   1 
ATOM   5920 H  HG11 . VAL   B 1 144 ? 29.682 -29.227 -9.763  1.00 23.51 ?  144 VAL   B HG11 1 
ATOM   5921 H  HG12 . VAL   B 1 144 ? 28.836 -28.562 -8.597  1.00 23.51 ?  144 VAL   B HG12 1 
ATOM   5922 H  HG13 . VAL   B 1 144 ? 29.503 -27.651 -9.718  1.00 23.51 ?  144 VAL   B HG13 1 
ATOM   5923 H  HG21 . VAL   B 1 144 ? 32.006 -29.616 -9.479  1.00 20.50 ?  144 VAL   B HG21 1 
ATOM   5924 H  HG22 . VAL   B 1 144 ? 32.248 -28.087 -9.838  1.00 20.50 ?  144 VAL   B HG22 1 
ATOM   5925 H  HG23 . VAL   B 1 144 ? 32.881 -28.703 -8.517  1.00 20.50 ?  144 VAL   B HG23 1 
ATOM   5926 N  N    . ASP   B 1 145 ? 29.199 -26.567 -6.143  1.00 14.46 ?  145 ASP   B N    1 
ATOM   5927 C  CA   . ASP   B 1 145 ? 27.889 -26.105 -5.713  1.00 14.86 ?  145 ASP   B CA   1 
ATOM   5928 C  C    . ASP   B 1 145 ? 27.919 -24.691 -5.152  1.00 14.59 ?  145 ASP   B C    1 
ATOM   5929 O  O    . ASP   B 1 145 ? 26.860 -24.157 -4.810  1.00 16.41 ?  145 ASP   B O    1 
ATOM   5930 C  CB   . ASP   B 1 145 ? 27.308 -27.035 -4.639  1.00 16.57 ?  145 ASP   B CB   1 
ATOM   5931 C  CG   . ASP   B 1 145 ? 26.943 -28.409 -5.159  1.00 17.88 ?  145 ASP   B CG   1 
ATOM   5932 O  OD1  . ASP   B 1 145 ? 26.826 -28.595 -6.387  1.00 18.47 ?  145 ASP   B OD1  1 
ATOM   5933 O  OD2  . ASP   B 1 145 ? 26.760 -29.302 -4.310  1.00 20.27 -1 145 ASP   B OD2  1 
ATOM   5934 H  H    . ASP   B 1 145 ? 29.640 -26.988 -5.535  1.00 17.39 ?  145 ASP   B H    1 
ATOM   5935 H  HA   . ASP   B 1 145 ? 27.295 -26.094 -6.474  1.00 17.87 ?  145 ASP   B HA   1 
ATOM   5936 H  HB2  . ASP   B 1 145 ? 27.958 -27.152 -3.941  1.00 19.92 ?  145 ASP   B HB2  1 
ATOM   5937 H  HB3  . ASP   B 1 145 ? 26.500 -26.626 -4.287  1.00 19.92 ?  145 ASP   B HB3  1 
ATOM   5938 N  N    . THR   B 1 146 ? 29.095 -24.073 -5.038  1.00 13.30 ?  146 THR   B N    1 
ATOM   5939 C  CA   . THR   B 1 146 ? 29.232 -22.753 -4.431  1.00 13.05 ?  146 THR   B CA   1 
ATOM   5940 C  C    . THR   B 1 146 ? 29.864 -21.721 -5.350  1.00 12.58 ?  146 THR   B C    1 
ATOM   5941 O  O    . THR   B 1 146 ? 29.405 -20.565 -5.397  1.00 12.67 ?  146 THR   B O    1 
ATOM   5942 C  CB   . THR   B 1 146 ? 30.054 -22.856 -3.139  1.00 13.42 ?  146 THR   B CB   1 
ATOM   5943 O  OG1  . THR   B 1 146 ? 29.478 -23.849 -2.280  1.00 13.46 ?  146 THR   B OG1  1 
ATOM   5944 C  CG2  . THR   B 1 146 ? 30.125 -21.514 -2.425  1.00 13.54 ?  146 THR   B CG2  1 
ATOM   5945 H  H    . THR   B 1 146 ? 29.849 -24.404 -5.305  1.00 15.99 ?  146 THR   B H    1 
ATOM   5946 H  HA   . THR   B 1 146 ? 28.357 -22.425 -4.192  1.00 15.70 ?  146 THR   B HA   1 
ATOM   5947 H  HB   . THR   B 1 146 ? 30.962 -23.120 -3.360  1.00 16.14 ?  146 THR   B HB   1 
ATOM   5948 H  HG1  . THR   B 1 146 ? 29.506 -24.605 -2.661  1.00 16.19 ?  146 THR   B HG1  1 
ATOM   5949 H  HG21 . THR   B 1 146 ? 30.466 -21.637 -1.527  1.00 16.29 ?  146 THR   B HG21 1 
ATOM   5950 H  HG22 . THR   B 1 146 ? 30.718 -20.914 -2.907  1.00 16.29 ?  146 THR   B HG22 1 
ATOM   5951 H  HG23 . THR   B 1 146 ? 29.243 -21.119 -2.379  1.00 16.29 ?  146 THR   B HG23 1 
ATOM   5952 N  N    . VAL   B 1 147 ? 30.927 -22.092 -6.056  1.00 12.50 ?  147 VAL   B N    1 
ATOM   5953 C  CA   . VAL   B 1 147 ? 31.650 -21.144 -6.889  1.00 12.37 ?  147 VAL   B CA   1 
ATOM   5954 C  C    . VAL   B 1 147 ? 30.921 -21.008 -8.212  1.00 12.77 ?  147 VAL   B C    1 
ATOM   5955 O  O    . VAL   B 1 147 ? 30.554 -22.011 -8.841  1.00 13.46 ?  147 VAL   B O    1 
ATOM   5956 C  CB   . VAL   B 1 147 ? 33.105 -21.597 -7.095  1.00 12.72 ?  147 VAL   B CB   1 
ATOM   5957 C  CG1  . VAL   B 1 147 ? 33.867 -20.570 -7.915  1.00 12.84 ?  147 VAL   B CG1  1 
ATOM   5958 C  CG2  . VAL   B 1 147 ? 33.781 -21.811 -5.751  1.00 12.86 ?  147 VAL   B CG2  1 
ATOM   5959 H  H    . VAL   B 1 147 ? 31.249 -22.894 -6.074  1.00 15.04 ?  147 VAL   B H    1 
ATOM   5960 H  HA   . VAL   B 1 147 ? 31.664 -20.281 -6.457  1.00 14.88 ?  147 VAL   B HA   1 
ATOM   5961 H  HB   . VAL   B 1 147 ? 33.119 -22.442 -7.577  1.00 15.30 ?  147 VAL   B HB   1 
ATOM   5962 H  HG11 . VAL   B 1 147 ? 34.813 -20.793 -7.903  1.00 15.44 ?  147 VAL   B HG11 1 
ATOM   5963 H  HG12 . VAL   B 1 147 ? 33.539 -20.582 -8.827  1.00 15.44 ?  147 VAL   B HG12 1 
ATOM   5964 H  HG13 . VAL   B 1 147 ? 33.733 -19.693 -7.524  1.00 15.44 ?  147 VAL   B HG13 1 
ATOM   5965 H  HG21 . VAL   B 1 147 ? 34.723 -22.000 -5.895  1.00 15.47 ?  147 VAL   B HG21 1 
ATOM   5966 H  HG22 . VAL   B 1 147 ? 33.685 -21.007 -5.218  1.00 15.47 ?  147 VAL   B HG22 1 
ATOM   5967 H  HG23 . VAL   B 1 147 ? 33.362 -22.560 -5.299  1.00 15.47 ?  147 VAL   B HG23 1 
ATOM   5968 N  N    . ARG   B 1 148 ? 30.706 -19.761 -8.629  1.00 12.74 ?  148 ARG   B N    1 
ATOM   5969 C  CA   . ARG   B 1 148 ? 30.079 -19.447 -9.902  1.00 12.80 ?  148 ARG   B CA   1 
ATOM   5970 C  C    . ARG   B 1 148 ? 31.028 -18.769 -10.877 1.00 12.87 ?  148 ARG   B C    1 
ATOM   5971 O  O    . ARG   B 1 148 ? 30.739 -18.748 -12.076 1.00 14.08 ?  148 ARG   B O    1 
ATOM   5972 C  CB   . ARG   B 1 148 ? 28.840 -18.565 -9.683  1.00 13.34 ?  148 ARG   B CB   1 
ATOM   5973 C  CG   . ARG   B 1 148 ? 27.776 -19.273 -8.855  1.00 13.97 ?  148 ARG   B CG   1 
ATOM   5974 C  CD   . ARG   B 1 148 ? 26.563 -18.392 -8.552  1.00 14.63 ?  148 ARG   B CD   1 
ATOM   5975 N  NE   . ARG   B 1 148 ? 26.943 -17.187 -7.826  1.00 14.09 ?  148 ARG   B NE   1 
ATOM   5976 C  CZ   . ARG   B 1 148 ? 27.244 -17.149 -6.535  1.00 13.40 ?  148 ARG   B CZ   1 
ATOM   5977 N  NH1  . ARG   B 1 148 ? 27.178 -18.231 -5.774  1.00 13.54 ?  148 ARG   B NH1  1 
ATOM   5978 N  NH2  . ARG   B 1 148 ? 27.640 -15.999 -5.996  1.00 13.74 ?  148 ARG   B NH2  1 
ATOM   5979 H  H    . ARG   B 1 148 ? 30.928 -19.063 -8.173  1.00 15.33 ?  148 ARG   B H    1 
ATOM   5980 H  HA   . ARG   B 1 148 ? 29.784 -20.273 -10.311 1.00 15.39 ?  148 ARG   B HA   1 
ATOM   5981 H  HB2  . ARG   B 1 148 ? 29.102 -17.758 -9.214  1.00 16.05 ?  148 ARG   B HB2  1 
ATOM   5982 H  HB3  . ARG   B 1 148 ? 28.454 -18.343 -10.543 1.00 16.05 ?  148 ARG   B HB3  1 
ATOM   5983 H  HG2  . ARG   B 1 148 ? 27.465 -20.050 -9.341  1.00 16.80 ?  148 ARG   B HG2  1 
ATOM   5984 H  HG3  . ARG   B 1 148 ? 28.165 -19.544 -8.008  1.00 16.80 ?  148 ARG   B HG3  1 
ATOM   5985 H  HD2  . ARG   B 1 148 ? 26.145 -18.125 -9.384  1.00 17.59 ?  148 ARG   B HD2  1 
ATOM   5986 H  HD3  . ARG   B 1 148 ? 25.934 -18.892 -8.005  1.00 17.59 ?  148 ARG   B HD3  1 
ATOM   5987 H  HE   . ARG   B 1 148 ? 26.980 -16.451 -8.265  1.00 16.95 ?  148 ARG   B HE   1 
ATOM   5988 H  HH11 . ARG   B 1 148 ? 26.922 -18.984 -6.106  1.00 16.29 ?  148 ARG   B HH11 1 
ATOM   5989 H  HH12 . ARG   B 1 148 ? 27.374 -18.184 -4.935  1.00 16.29 ?  148 ARG   B HH12 1 
ATOM   5990 H  HH21 . ARG   B 1 148 ? 27.692 -15.292 -6.482  1.00 16.52 ?  148 ARG   B HH21 1 
ATOM   5991 H  HH22 . ARG   B 1 148 ? 27.839 -15.959 -5.160  1.00 16.52 ?  148 ARG   B HH22 1 
ATOM   5992 N  N    . THR   B 1 149 ? 32.133 -18.205 -10.392 1.00 12.91 ?  149 THR   B N    1 
ATOM   5993 C  CA   . THR   B 1 149 ? 33.174 -17.648 -11.241 1.00 12.83 ?  149 THR   B CA   1 
ATOM   5994 C  C    . THR   B 1 149 ? 34.064 -18.788 -11.742 1.00 12.69 ?  149 THR   B C    1 
ATOM   5995 O  O    . THR   B 1 149 ? 33.868 -19.959 -11.401 1.00 13.21 ?  149 THR   B O    1 
ATOM   5996 C  CB   . THR   B 1 149 ? 33.946 -16.596 -10.459 1.00 12.86 ?  149 THR   B CB   1 
ATOM   5997 O  OG1  . THR   B 1 149 ? 34.407 -17.198 -9.248  1.00 12.89 ?  149 THR   B OG1  1 
ATOM   5998 C  CG2  . THR   B 1 149 ? 33.053 -15.396 -10.157 1.00 13.38 ?  149 THR   B CG2  1 
ATOM   5999 H  H    . THR   B 1 149 ? 32.294 -18.122 -9.552  1.00 15.53 ?  149 THR   B H    1 
ATOM   6000 H  HA   . THR   B 1 149 ? 32.765 -17.218 -12.009 1.00 15.44 ?  149 THR   B HA   1 
ATOM   6001 H  HB   . THR   B 1 149 ? 34.705 -16.298 -10.979 1.00 15.47 ?  149 THR   B HB   1 
ATOM   6002 H  HG1  . THR   B 1 149 ? 34.826 -16.628 -8.786  1.00 15.51 ?  149 THR   B HG1  1 
ATOM   6003 H  HG21 . THR   B 1 149 ? 33.558 -14.720 -9.679  1.00 16.10 ?  149 THR   B HG21 1 
ATOM   6004 H  HG22 . THR   B 1 149 ? 32.721 -15.013 -10.986 1.00 16.10 ?  149 THR   B HG22 1 
ATOM   6005 H  HG23 . THR   B 1 149 ? 32.298 -15.669 -9.613  1.00 16.10 ?  149 THR   B HG23 1 
ATOM   6006 N  N    . ASN   B 1 150 ? 35.035 -18.466 -12.586 1.00 12.65 ?  150 ASN   B N    1 
ATOM   6007 C  CA   . ASN   B 1 150 ? 35.795 -19.493 -13.290 1.00 12.92 ?  150 ASN   B CA   1 
ATOM   6008 C  C    . ASN   B 1 150 ? 36.961 -19.945 -12.423 1.00 12.62 ?  150 ASN   B C    1 
ATOM   6009 O  O    . ASN   B 1 150 ? 37.892 -19.176 -12.174 1.00 13.41 ?  150 ASN   B O    1 
ATOM   6010 C  CB   . ASN   B 1 150 ? 36.268 -18.955 -14.633 1.00 14.88 ?  150 ASN   B CB   1 
ATOM   6011 C  CG   . ASN   B 1 150 ? 35.127 -18.739 -15.580 1.00 17.46 ?  150 ASN   B CG   1 
ATOM   6012 O  OD1  . ASN   B 1 150 ? 34.241 -19.578 -15.675 1.00 18.60 ?  150 ASN   B OD1  1 
ATOM   6013 N  ND2  . ASN   B 1 150 ? 35.117 -17.606 -16.261 1.00 19.12 ?  150 ASN   B ND2  1 
ATOM   6014 H  H    . ASN   B 1 150 ? 35.281 -17.658 -12.764 1.00 15.22 ?  150 ASN   B H    1 
ATOM   6015 H  HA   . ASN   B 1 150 ? 35.216 -20.257 -13.454 1.00 15.54 ?  150 ASN   B HA   1 
ATOM   6016 H  HB2  . ASN   B 1 150 ? 36.710 -18.102 -14.494 1.00 17.90 ?  150 ASN   B HB2  1 
ATOM   6017 H  HB3  . ASN   B 1 150 ? 36.877 -19.590 -15.033 1.00 17.90 ?  150 ASN   B HB3  1 
ATOM   6018 H  HD21 . ASN   B 1 150 ? 34.481 -17.438 -16.817 1.00 22.98 ?  150 ASN   B HD21 1 
ATOM   6019 H  HD22 . ASN   B 1 150 ? 35.755 -17.036 -16.159 1.00 22.98 ?  150 ASN   B HD22 1 
ATOM   6020 N  N    . VAL   B 1 151 ? 36.921 -21.192 -11.969 1.00 12.41 ?  151 VAL   B N    1 
ATOM   6021 C  CA   . VAL   B 1 151 ? 37.946 -21.720 -11.084 1.00 12.53 ?  151 VAL   B CA   1 
ATOM   6022 C  C    . VAL   B 1 151 ? 38.654 -22.887 -11.760 1.00 12.26 ?  151 VAL   B C    1 
ATOM   6023 O  O    . VAL   B 1 151 ? 38.013 -23.823 -12.263 1.00 13.14 ?  151 VAL   B O    1 
ATOM   6024 C  CB   . VAL   B 1 151 ? 37.391 -22.062 -9.688  1.00 13.64 ?  151 VAL   B CB   1 
ATOM   6025 C  CG1  . VAL   B 1 151 ? 36.217 -23.046 -9.768  1.00 14.57 ?  151 VAL   B CG1  1 
ATOM   6026 C  CG2  . VAL   B 1 151 ? 38.498 -22.578 -8.790  1.00 13.88 ?  151 VAL   B CG2  1 
ATOM   6027 H  H    . VAL   B 1 151 ? 36.297 -21.755 -12.165 1.00 14.93 ?  151 VAL   B H    1 
ATOM   6028 H  HA   . VAL   B 1 151 ? 38.609 -21.024 -10.955 1.00 15.07 ?  151 VAL   B HA   1 
ATOM   6029 H  HB   . VAL   B 1 151 ? 37.054 -21.244 -9.286  1.00 16.40 ?  151 VAL   B HB   1 
ATOM   6030 H  HG11 . VAL   B 1 151 ? 35.909 -23.248 -8.869  1.00 17.52 ?  151 VAL   B HG11 1 
ATOM   6031 H  HG12 . VAL   B 1 151 ? 35.496 -22.643 -10.279 1.00 17.52 ?  151 VAL   B HG12 1 
ATOM   6032 H  HG13 . VAL   B 1 151 ? 36.513 -23.861 -10.204 1.00 17.52 ?  151 VAL   B HG13 1 
ATOM   6033 H  HG21 . VAL   B 1 151 ? 38.162 -22.643 -7.881  1.00 16.70 ?  151 VAL   B HG21 1 
ATOM   6034 H  HG22 . VAL   B 1 151 ? 38.779 -23.453 -9.100  1.00 16.70 ?  151 VAL   B HG22 1 
ATOM   6035 H  HG23 . VAL   B 1 151 ? 39.246 -21.959 -8.819  1.00 16.70 ?  151 VAL   B HG23 1 
ATOM   6036 N  N    . TYR   B 1 152 ? 39.982 -22.796 -11.781 1.00 11.89 ?  152 TYR   B N    1 
ATOM   6037 C  CA   . TYR   B 1 152 ? 40.888 -23.775 -12.364 1.00 12.43 ?  152 TYR   B CA   1 
ATOM   6038 C  C    . TYR   B 1 152 ? 41.606 -24.450 -11.201 1.00 11.44 ?  152 TYR   B C    1 
ATOM   6039 O  O    . TYR   B 1 152 ? 42.445 -23.831 -10.539 1.00 12.15 ?  152 TYR   B O    1 
ATOM   6040 C  CB   . TYR   B 1 152 ? 41.860 -23.066 -13.310 1.00 13.06 ?  152 TYR   B CB   1 
ATOM   6041 C  CG   . TYR   B 1 152 ? 41.179 -22.605 -14.575 1.00 13.45 ?  152 TYR   B CG   1 
ATOM   6042 C  CD1  . TYR   B 1 152 ? 40.505 -21.386 -14.637 1.00 13.52 ?  152 TYR   B CD1  1 
ATOM   6043 C  CD2  . TYR   B 1 152 ? 41.185 -23.404 -15.703 1.00 14.50 ?  152 TYR   B CD2  1 
ATOM   6044 C  CE1  . TYR   B 1 152 ? 39.860 -20.987 -15.793 1.00 14.92 ?  152 TYR   B CE1  1 
ATOM   6045 C  CE2  . TYR   B 1 152 ? 40.547 -23.017 -16.858 1.00 15.16 ?  152 TYR   B CE2  1 
ATOM   6046 C  CZ   . TYR   B 1 152 ? 39.892 -21.805 -16.902 1.00 15.36 ?  152 TYR   B CZ   1 
ATOM   6047 O  OH   . TYR   B 1 152 ? 39.258 -21.442 -18.065 1.00 17.71 ?  152 TYR   B OH   1 
ATOM   6048 H  H    . TYR   B 1 152 ? 40.410 -22.129 -11.434 1.00 14.31 ?  152 TYR   B H    1 
ATOM   6049 H  HA   . TYR   B 1 152 ? 40.381 -24.439 -12.863 1.00 14.95 ?  152 TYR   B HA   1 
ATOM   6050 H  HB2  . TYR   B 1 152 ? 42.225 -22.287 -12.859 1.00 15.71 ?  152 TYR   B HB2  1 
ATOM   6051 H  HB3  . TYR   B 1 152 ? 42.573 -23.676 -13.551 1.00 15.71 ?  152 TYR   B HB3  1 
ATOM   6052 H  HD1  . TYR   B 1 152 ? 40.484 -20.837 -13.885 1.00 16.26 ?  152 TYR   B HD1  1 
ATOM   6053 H  HD2  . TYR   B 1 152 ? 41.624 -24.227 -15.676 1.00 17.43 ?  152 TYR   B HD2  1 
ATOM   6054 H  HE1  . TYR   B 1 152 ? 39.417 -20.172 -15.828 1.00 17.94 ?  152 TYR   B HE1  1 
ATOM   6055 H  HE2  . TYR   B 1 152 ? 40.566 -23.569 -17.608 1.00 18.23 ?  152 TYR   B HE2  1 
ATOM   6056 H  HH   . TYR   B 1 152 ? 38.895 -20.690 -17.970 1.00 21.29 ?  152 TYR   B HH   1 
ATOM   6057 N  N    . LEU   B 1 153 ? 41.254 -25.712 -10.941 1.00 11.87 ?  153 LEU   B N    1 
ATOM   6058 C  CA   . LEU   B 1 153 ? 41.754 -26.458 -9.796  1.00 11.66 ?  153 LEU   B CA   1 
ATOM   6059 C  C    . LEU   B 1 153 ? 42.988 -27.257 -10.188 1.00 11.94 ?  153 LEU   B C    1 
ATOM   6060 O  O    . LEU   B 1 153 ? 42.970 -27.986 -11.184 1.00 13.25 ?  153 LEU   B O    1 
ATOM   6061 C  CB   . LEU   B 1 153 ? 40.671 -27.414 -9.286  1.00 11.98 ?  153 LEU   B CB   1 
ATOM   6062 C  CG   . LEU   B 1 153 ? 39.414 -26.764 -8.708  1.00 12.86 ?  153 LEU   B CG   1 
ATOM   6063 C  CD1  . LEU   B 1 153 ? 38.320 -27.812 -8.540  1.00 13.60 ?  153 LEU   B CD1  1 
ATOM   6064 C  CD2  . LEU   B 1 153 ? 39.726 -26.110 -7.374  1.00 13.59 ?  153 LEU   B CD2  1 
ATOM   6065 H  H    . LEU   B 1 153 ? 40.693 -26.162 -11.426 1.00 14.28 ?  153 LEU   B H    1 
ATOM   6066 H  HA   . LEU   B 1 153 ? 41.981 -25.842 -9.088  1.00 14.03 ?  153 LEU   B HA   1 
ATOM   6067 H  HB2  . LEU   B 1 153 ? 40.386 -27.981 -10.019 1.00 14.42 ?  153 LEU   B HB2  1 
ATOM   6068 H  HB3  . LEU   B 1 153 ? 41.055 -27.964 -8.584  1.00 14.42 ?  153 LEU   B HB3  1 
ATOM   6069 H  HG   . LEU   B 1 153 ? 39.093 -26.074 -9.314  1.00 15.47 ?  153 LEU   B HG   1 
ATOM   6070 H  HD11 . LEU   B 1 153 ? 37.518 -27.374 -8.214  1.00 16.36 ?  153 LEU   B HD11 1 
ATOM   6071 H  HD12 . LEU   B 1 153 ? 38.153 -28.223 -9.396  1.00 16.36 ?  153 LEU   B HD12 1 
ATOM   6072 H  HD13 . LEU   B 1 153 ? 38.623 -28.471 -7.898  1.00 16.36 ?  153 LEU   B HD13 1 
ATOM   6073 H  HD21 . LEU   B 1 153 ? 38.915 -25.742 -6.997  1.00 16.35 ?  153 LEU   B HD21 1 
ATOM   6074 H  HD22 . LEU   B 1 153 ? 40.099 -26.778 -6.774  1.00 16.35 ?  153 LEU   B HD22 1 
ATOM   6075 H  HD23 . LEU   B 1 153 ? 40.377 -25.399 -7.512  1.00 16.35 ?  153 LEU   B HD23 1 
ATOM   6076 N  N    . ALA   B 1 154 ? 44.036 -27.148 -9.379  1.00 12.03 ?  154 ALA   B N    1 
ATOM   6077 C  CA   . ALA   B 1 154 ? 45.267 -27.905 -9.561  1.00 13.03 ?  154 ALA   B CA   1 
ATOM   6078 C  C    . ALA   B 1 154 ? 45.330 -28.990 -8.495  1.00 13.43 ?  154 ALA   B C    1 
ATOM   6079 O  O    . ALA   B 1 154 ? 45.248 -28.700 -7.295  1.00 14.54 ?  154 ALA   B O    1 
ATOM   6080 C  CB   . ALA   B 1 154 ? 46.486 -26.993 -9.474  1.00 14.02 ?  154 ALA   B CB   1 
ATOM   6081 H  H    . ALA   B 1 154 ? 44.054 -26.619 -8.697  1.00 14.48 ?  154 ALA   B H    1 
ATOM   6082 H  HA   . ALA   B 1 154 ? 45.262 -28.327 -10.430 1.00 15.68 ?  154 ALA   B HA   1 
ATOM   6083 H  HB1  . ALA   B 1 154 ? 47.289 -27.522 -9.594  1.00 16.87 ?  154 ALA   B HB1  1 
ATOM   6084 H  HB2  . ALA   B 1 154 ? 46.428 -26.316 -10.168 1.00 16.87 ?  154 ALA   B HB2  1 
ATOM   6085 H  HB3  . ALA   B 1 154 ? 46.503 -26.564 -8.600  1.00 16.87 ?  154 ALA   B HB3  1 
ATOM   6086 N  N    . VAL   B 1 155 ? 45.457 -30.234 -8.934  1.00 12.70 ?  155 VAL   B N    1 
ATOM   6087 C  CA   . VAL   B 1 155 ? 45.567 -31.380 -8.043  1.00 13.03 ?  155 VAL   B CA   1 
ATOM   6088 C  C    . VAL   B 1 155 ? 46.908 -32.047 -8.319  1.00 12.83 ?  155 VAL   B C    1 
ATOM   6089 O  O    . VAL   B 1 155 ? 47.148 -32.542 -9.429  1.00 14.71 ?  155 VAL   B O    1 
ATOM   6090 C  CB   . VAL   B 1 155 ? 44.413 -32.379 -8.238  1.00 14.50 ?  155 VAL   B CB   1 
ATOM   6091 C  CG1  . VAL   B 1 155 ? 44.597 -33.576 -7.322  1.00 14.51 ?  155 VAL   B CG1  1 
ATOM   6092 C  CG2  . VAL   B 1 155 ? 43.072 -31.696 -7.982  1.00 15.30 ?  155 VAL   B CG2  1 
ATOM   6093 H  H    . VAL   B 1 155 ? 45.485 -30.446 -9.769  1.00 15.28 ?  155 VAL   B H    1 
ATOM   6094 H  HA   . VAL   B 1 155 ? 45.553 -31.084 -7.123  1.00 15.67 ?  155 VAL   B HA   1 
ATOM   6095 H  HB   . VAL   B 1 155 ? 44.413 -32.698 -9.156  1.00 17.44 ?  155 VAL   B HB   1 
ATOM   6096 H  HG11 . VAL   B 1 155 ? 43.769 -34.082 -7.287  1.00 17.45 ?  155 VAL   B HG11 1 
ATOM   6097 H  HG12 . VAL   B 1 155 ? 45.309 -34.138 -7.667  1.00 17.45 ?  155 VAL   B HG12 1 
ATOM   6098 H  HG13 . VAL   B 1 155 ? 44.825 -33.261 -6.432  1.00 17.45 ?  155 VAL   B HG13 1 
ATOM   6099 H  HG21 . VAL   B 1 155 ? 42.361 -32.350 -8.070  1.00 18.40 ?  155 VAL   B HG21 1 
ATOM   6100 H  HG22 . VAL   B 1 155 ? 43.074 -31.328 -7.084  1.00 18.40 ?  155 VAL   B HG22 1 
ATOM   6101 H  HG23 . VAL   B 1 155 ? 42.950 -30.985 -8.631  1.00 18.40 ?  155 VAL   B HG23 1 
ATOM   6102 N  N    . PHE   B 1 156 ? 47.768 -32.095 -7.301  1.00 13.27 ?  156 PHE   B N    1 
ATOM   6103 C  CA   . PHE   B 1 156 ? 49.149 -32.549 -7.495  1.00 14.62 ?  156 PHE   B CA   1 
ATOM   6104 C  C    . PHE   B 1 156 ? 49.254 -34.050 -7.779  1.00 15.43 ?  156 PHE   B C    1 
ATOM   6105 O  O    . PHE   B 1 156 ? 49.989 -34.472 -8.683  1.00 17.13 ?  156 PHE   B O    1 
ATOM   6106 C  CB   . PHE   B 1 156 ? 49.970 -32.179 -6.264  1.00 15.15 ?  156 PHE   B CB   1 
ATOM   6107 C  CG   . PHE   B 1 156 ? 51.393 -32.640 -6.320  1.00 15.70 ?  156 PHE   B CG   1 
ATOM   6108 C  CD1  . PHE   B 1 156 ? 52.274 -32.095 -7.227  1.00 17.32 ?  156 PHE   B CD1  1 
ATOM   6109 C  CD2  . PHE   B 1 156 ? 51.849 -33.605 -5.451  1.00 16.05 ?  156 PHE   B CD2  1 
ATOM   6110 C  CE1  . PHE   B 1 156 ? 53.595 -32.504 -7.273  1.00 18.11 ?  156 PHE   B CE1  1 
ATOM   6111 C  CE2  . PHE   B 1 156 ? 53.167 -34.024 -5.491  1.00 17.16 ?  156 PHE   B CE2  1 
ATOM   6112 C  CZ   . PHE   B 1 156 ? 54.035 -33.474 -6.407  1.00 17.76 ?  156 PHE   B CZ   1 
ATOM   6113 H  H    . PHE   B 1 156 ? 47.575 -31.872 -6.492  1.00 15.96 ?  156 PHE   B H    1 
ATOM   6114 H  HA   . PHE   B 1 156 ? 49.521 -32.077 -8.251  1.00 17.59 ?  156 PHE   B HA   1 
ATOM   6115 H  HB2  . PHE   B 1 156 ? 49.976 -31.214 -6.173  1.00 18.22 ?  156 PHE   B HB2  1 
ATOM   6116 H  HB3  . PHE   B 1 156 ? 49.561 -32.580 -5.480  1.00 18.22 ?  156 PHE   B HB3  1 
ATOM   6117 H  HD1  . PHE   B 1 156 ? 51.981 -31.432 -7.815  1.00 20.82 ?  156 PHE   B HD1  1 
ATOM   6118 H  HD2  . PHE   B 1 156 ? 51.260 -33.983 -4.836  1.00 19.30 ?  156 PHE   B HD2  1 
ATOM   6119 H  HE1  . PHE   B 1 156 ? 54.180 -32.125 -7.893  1.00 21.77 ?  156 PHE   B HE1  1 
ATOM   6120 H  HE2  . PHE   B 1 156 ? 53.460 -34.685 -4.906  1.00 20.63 ?  156 PHE   B HE2  1 
ATOM   6121 H  HZ   . PHE   B 1 156 ? 54.920 -33.755 -6.436  1.00 21.36 ?  156 PHE   B HZ   1 
ATOM   6122 N  N    . ASP   B 1 157 ? 48.582 -34.874 -6.987  1.00 15.94 ?  157 ASP   B N    1 
ATOM   6123 C  CA   . ASP   B 1 157 ? 48.732 -36.320 -7.086  1.00 16.95 ?  157 ASP   B CA   1 
ATOM   6124 C  C    . ASP   B 1 157 ? 47.817 -36.861 -8.179  1.00 17.01 ?  157 ASP   B C    1 
ATOM   6125 O  O    . ASP   B 1 157 ? 46.590 -36.751 -8.075  1.00 16.18 ?  157 ASP   B O    1 
ATOM   6126 C  CB   . ASP   B 1 157 ? 48.369 -36.936 -5.742  1.00 18.40 ?  157 ASP   B CB   1 
ATOM   6127 C  CG   . ASP   B 1 157 ? 48.508 -38.444 -5.731  1.00 19.94 ?  157 ASP   B CG   1 
ATOM   6128 O  OD1  . ASP   B 1 157 ? 48.846 -39.042 -6.779  1.00 20.43 ?  157 ASP   B OD1  1 
ATOM   6129 O  OD2  . ASP   B 1 157 ? 48.299 -39.034 -4.654  1.00 22.23 -1 157 ASP   B OD2  1 
ATOM   6130 H  H    . ASP   B 1 157 ? 48.036 -34.622 -6.376  1.00 19.16 ?  157 ASP   B H    1 
ATOM   6131 H  HA   . ASP   B 1 157 ? 49.655 -36.549 -7.301  1.00 20.37 ?  157 ASP   B HA   1 
ATOM   6132 H  HB2  . ASP   B 1 157 ? 48.949 -36.565 -5.060  1.00 22.11 ?  157 ASP   B HB2  1 
ATOM   6133 H  HB3  . ASP   B 1 157 ? 47.444 -36.719 -5.541  1.00 22.11 ?  157 ASP   B HB3  1 
ATOM   6134 N  N    . LYS   B 1 158 ? 48.410 -37.472 -9.211  1.00 18.02 ?  158 LYS   B N    1 
ATOM   6135 C  CA   . LYS   B 1 158 ? 47.630 -38.088 -10.287 1.00 18.83 ?  158 LYS   B CA   1 
ATOM   6136 C  C    . LYS   B 1 158 ? 46.579 -39.058 -9.752  1.00 18.76 ?  158 LYS   B C    1 
ATOM   6137 O  O    . LYS   B 1 158 ? 45.475 -39.153 -10.300 1.00 19.14 ?  158 LYS   B O    1 
ATOM   6138 C  CB   . LYS   B 1 158 ? 48.572 -38.799 -11.268 1.00 20.73 ?  158 LYS   B CB   1 
ATOM   6139 C  CG   . LYS   B 1 158 ? 47.886 -39.703 -12.285 1.00 22.72 ?  158 LYS   B CG   1 
ATOM   6140 C  CD   . LYS   B 1 158 ? 47.050 -38.922 -13.277 1.00 24.79 ?  158 LYS   B CD   1 
ATOM   6141 C  CE   . LYS   B 1 158 ? 46.442 -39.845 -14.321 1.00 26.41 ?  158 LYS   B CE   1 
ATOM   6142 N  NZ   . LYS   B 1 158 ? 45.387 -39.161 -15.124 1.00 26.66 ?  158 LYS   B NZ   1 
ATOM   6143 H  H    . LYS   B 1 158 ? 49.264 -37.548 -9.311  1.00 21.66 ?  158 LYS   B H    1 
ATOM   6144 H  HA   . LYS   B 1 158 ? 47.170 -37.392 -10.779 1.00 22.63 ?  158 LYS   B HA   1 
ATOM   6145 H  HB2  . LYS   B 1 158 ? 49.063 -38.126 -11.770 1.00 24.91 ?  158 LYS   B HB2  1 
ATOM   6146 H  HB3  . LYS   B 1 158 ? 49.194 -39.345 -10.766 1.00 24.91 ?  158 LYS   B HB3  1 
ATOM   6147 H  HG2  . LYS   B 1 158 ? 48.566 -40.181 -12.785 1.00 27.30 ?  158 LYS   B HG2  1 
ATOM   6148 H  HG3  . LYS   B 1 158 ? 47.311 -40.343 -11.833 1.00 27.30 ?  158 LYS   B HG3  1 
ATOM   6149 H  HD2  . LYS   B 1 158 ? 46.329 -38.472 -12.809 1.00 29.78 ?  158 LYS   B HD2  1 
ATOM   6150 H  HD3  . LYS   B 1 158 ? 47.611 -38.276 -13.733 1.00 29.78 ?  158 LYS   B HD3  1 
ATOM   6151 H  HE2  . LYS   B 1 158 ? 47.135 -40.143 -14.929 1.00 31.73 ?  158 LYS   B HE2  1 
ATOM   6152 H  HE3  . LYS   B 1 158 ? 46.036 -40.608 -13.879 1.00 31.73 ?  158 LYS   B HE3  1 
ATOM   6153 H  HZ1  . LYS   B 1 158 ? 45.047 -39.721 -15.725 1.00 32.03 ?  158 LYS   B HZ1  1 
ATOM   6154 H  HZ2  . LYS   B 1 158 ? 44.732 -38.878 -14.590 1.00 32.03 ?  158 LYS   B HZ2  1 
ATOM   6155 H  HZ3  . LYS   B 1 158 ? 45.735 -38.458 -15.547 1.00 32.03 ?  158 LYS   B HZ3  1 
ATOM   6156 N  N    . ASN   B 1 159 ? 46.908 -39.814 -8.703  1.00 19.02 ?  159 ASN   B N    1 
ATOM   6157 C  CA   . ASN   B 1 159 ? 45.951 -40.791 -8.191  1.00 19.63 ?  159 ASN   B CA   1 
ATOM   6158 C  C    . ASN   B 1 159 ? 44.756 -40.118 -7.515  1.00 18.49 ?  159 ASN   B C    1 
ATOM   6159 O  O    . ASN   B 1 159 ? 43.627 -40.614 -7.627  1.00 18.78 ?  159 ASN   B O    1 
ATOM   6160 C  CB   . ASN   B 1 159 ? 46.655 -41.777 -7.264  1.00 21.33 ?  159 ASN   B CB   1 
ATOM   6161 C  CG   . ASN   B 1 159 ? 47.690 -42.612 -7.994  1.00 23.33 ?  159 ASN   B CG   1 
ATOM   6162 O  OD1  . ASN   B 1 159 ? 47.440 -43.112 -9.097  1.00 24.10 ?  159 ASN   B OD1  1 
ATOM   6163 N  ND2  . ASN   B 1 159 ? 48.860 -42.769 -7.387  1.00 23.84 ?  159 ASN   B ND2  1 
ATOM   6164 H  H    . ASN   B 1 159 ? 47.649 -39.766 -8.277  1.00 22.86 ?  159 ASN   B H    1 
ATOM   6165 H  HA   . ASN   B 1 159 ? 45.609 -41.297 -8.945  1.00 23.60 ?  159 ASN   B HA   1 
ATOM   6166 H  HB2  . ASN   B 1 159 ? 47.105 -41.293 -6.559  1.00 25.64 ?  159 ASN   B HB2  1 
ATOM   6167 H  HB3  . ASN   B 1 159 ? 45.998 -42.386 -6.890  1.00 25.64 ?  159 ASN   B HB3  1 
ATOM   6168 H  HD21 . ASN   B 1 159 ? 49.484 -43.237 -7.761  1.00 28.65 ?  159 ASN   B HD21 1 
ATOM   6169 H  HD22 . ASN   B 1 159 ? 48.997 -42.423 -6.613  1.00 28.65 ?  159 ASN   B HD22 1 
ATOM   6170 N  N    . LEU   B 1 160 ? 44.966 -38.984 -6.837  1.00 17.47 ?  160 LEU   B N    1 
ATOM   6171 C  CA   . LEU   B 1 160 ? 43.829 -38.251 -6.296  1.00 16.74 ?  160 LEU   B CA   1 
ATOM   6172 C  C    . LEU   B 1 160 ? 43.039 -37.588 -7.412  1.00 16.09 ?  160 LEU   B C    1 
ATOM   6173 O  O    . LEU   B 1 160 ? 41.803 -37.591 -7.392  1.00 15.81 ?  160 LEU   B O    1 
ATOM   6174 C  CB   . LEU   B 1 160 ? 44.288 -37.219 -5.267  1.00 16.01 ?  160 LEU   B CB   1 
ATOM   6175 C  CG   . LEU   B 1 160 ? 43.158 -36.339 -4.719  1.00 15.72 ?  160 LEU   B CG   1 
ATOM   6176 C  CD1  . LEU   B 1 160 ? 42.043 -37.175 -4.099  1.00 16.54 ?  160 LEU   B CD1  1 
ATOM   6177 C  CD2  . LEU   B 1 160 ? 43.700 -35.343 -3.706  1.00 15.81 ?  160 LEU   B CD2  1 
ATOM   6178 H  H    . LEU   B 1 160 ? 45.738 -38.628 -6.693  1.00 21.00 ?  160 LEU   B H    1 
ATOM   6179 H  HA   . LEU   B 1 160 ? 43.244 -38.878 -5.851  1.00 20.12 ?  160 LEU   B HA   1 
ATOM   6180 H  HB2  . LEU   B 1 160 ? 44.697 -37.688 -4.519  1.00 19.25 ?  160 LEU   B HB2  1 
ATOM   6181 H  HB3  . LEU   B 1 160 ? 44.950 -36.637 -5.681  1.00 19.25 ?  160 LEU   B HB3  1 
ATOM   6182 H  HG   . LEU   B 1 160 ? 42.777 -35.832 -5.450  1.00 18.90 ?  160 LEU   B HG   1 
ATOM   6183 H  HD11 . LEU   B 1 160 ? 41.410 -36.583 -3.669  1.00 19.89 ?  160 LEU   B HD11 1 
ATOM   6184 H  HD12 . LEU   B 1 160 ? 41.600 -37.684 -4.797  1.00 19.89 ?  160 LEU   B HD12 1 
ATOM   6185 H  HD13 . LEU   B 1 160 ? 42.428 -37.782 -3.444  1.00 19.89 ?  160 LEU   B HD13 1 
ATOM   6186 H  HD21 . LEU   B 1 160 ? 42.973 -34.782 -3.401  1.00 19.01 ?  160 LEU   B HD21 1 
ATOM   6187 H  HD22 . LEU   B 1 160 ? 44.083 -35.829 -2.960  1.00 19.01 ?  160 LEU   B HD22 1 
ATOM   6188 H  HD23 . LEU   B 1 160 ? 44.382 -34.800 -4.133  1.00 19.01 ?  160 LEU   B HD23 1 
ATOM   6189 N  N    . TYR   B 1 161 ? 43.736 -37.018 -8.397  1.00 16.19 ?  161 TYR   B N    1 
ATOM   6190 C  CA   . TYR   B 1 161 ? 43.059 -36.451 -9.558  1.00 16.04 ?  161 TYR   B CA   1 
ATOM   6191 C  C    . TYR   B 1 161 ? 42.116 -37.470 -10.182 1.00 15.95 ?  161 TYR   B C    1 
ATOM   6192 O  O    . TYR   B 1 161 ? 40.948 -37.170 -10.452 1.00 15.84 ?  161 TYR   B O    1 
ATOM   6193 C  CB   . TYR   B 1 161 ? 44.100 -35.962 -10.575 1.00 16.71 ?  161 TYR   B CB   1 
ATOM   6194 C  CG   . TYR   B 1 161 ? 43.522 -35.492 -11.889 1.00 16.99 ?  161 TYR   B CG   1 
ATOM   6195 C  CD1  . TYR   B 1 161 ? 43.125 -34.172 -12.058 1.00 17.05 ?  161 TYR   B CD1  1 
ATOM   6196 C  CD2  . TYR   B 1 161 ? 43.359 -36.370 -12.958 1.00 17.32 ?  161 TYR   B CD2  1 
ATOM   6197 C  CE1  . TYR   B 1 161 ? 42.591 -33.739 -13.244 1.00 18.15 ?  161 TYR   B CE1  1 
ATOM   6198 C  CE2  . TYR   B 1 161 ? 42.820 -35.946 -14.150 1.00 18.66 ?  161 TYR   B CE2  1 
ATOM   6199 C  CZ   . TYR   B 1 161 ? 42.440 -34.628 -14.290 1.00 18.73 ?  161 TYR   B CZ   1 
ATOM   6200 O  OH   . TYR   B 1 161 ? 41.902 -34.185 -15.475 1.00 20.83 ?  161 TYR   B OH   1 
ATOM   6201 H  H    . TYR   B 1 161 ? 44.592 -36.957 -8.422  1.00 19.47 ?  161 TYR   B H    1 
ATOM   6202 H  HA   . TYR   B 1 161 ? 42.532 -35.687 -9.280  1.00 19.29 ?  161 TYR   B HA   1 
ATOM   6203 H  HB2  . TYR   B 1 161 ? 44.586 -35.213 -10.189 1.00 20.10 ?  161 TYR   B HB2  1 
ATOM   6204 H  HB3  . TYR   B 1 161 ? 44.715 -36.683 -10.771 1.00 20.10 ?  161 TYR   B HB3  1 
ATOM   6205 H  HD1  . TYR   B 1 161 ? 43.229 -33.565 -11.358 1.00 20.49 ?  161 TYR   B HD1  1 
ATOM   6206 H  HD2  . TYR   B 1 161 ? 43.610 -37.258 -12.865 1.00 20.82 ?  161 TYR   B HD2  1 
ATOM   6207 H  HE1  . TYR   B 1 161 ? 42.336 -32.847 -13.342 1.00 21.81 ?  161 TYR   B HE1  1 
ATOM   6208 H  HE2  . TYR   B 1 161 ? 42.713 -36.537 -14.859 1.00 22.44 ?  161 TYR   B HE2  1 
ATOM   6209 H  HH   . TYR   B 1 161 ? 41.716 -33.365 -15.421 1.00 25.03 ?  161 TYR   B HH   1 
ATOM   6210 N  N    . ASP   B 1 162 ? 42.611 -38.691 -10.408 1.00 16.24 ?  162 ASP   B N    1 
ATOM   6211 C  CA   . ASP   B 1 162 ? 41.785 -39.725 -11.025 1.00 16.84 ?  162 ASP   B CA   1 
ATOM   6212 C  C    . ASP   B 1 162 ? 40.580 -40.067 -10.155 1.00 16.24 ?  162 ASP   B C    1 
ATOM   6213 O  O    . ASP   B 1 162 ? 39.477 -40.292 -10.670 1.00 16.60 ?  162 ASP   B O    1 
ATOM   6214 C  CB   . ASP   B 1 162 ? 42.615 -40.987 -11.286 1.00 18.38 ?  162 ASP   B CB   1 
ATOM   6215 C  CG   . ASP   B 1 162 ? 43.617 -40.819 -12.417 1.00 19.64 ?  162 ASP   B CG   1 
ATOM   6216 O  OD1  . ASP   B 1 162 ? 43.490 -39.869 -13.213 1.00 19.88 ?  162 ASP   B OD1  1 
ATOM   6217 O  OD2  . ASP   B 1 162 ? 44.521 -41.676 -12.526 1.00 21.26 -1 162 ASP   B OD2  1 
ATOM   6218 H  H    . ASP   B 1 162 ? 43.410 -38.944 -10.212 1.00 19.53 ?  162 ASP   B H    1 
ATOM   6219 H  HA   . ASP   B 1 162 ? 41.453 -39.401 -11.873 1.00 20.24 ?  162 ASP   B HA   1 
ATOM   6220 H  HB2  . ASP   B 1 162 ? 43.109 -41.211 -10.484 1.00 22.09 ?  162 ASP   B HB2  1 
ATOM   6221 H  HB3  . ASP   B 1 162 ? 42.016 -41.712 -11.524 1.00 22.09 ?  162 ASP   B HB3  1 
ATOM   6222 N  N    . LYS   B 1 163 ? 40.772 -40.131 -8.835  1.00 15.97 ?  163 LYS   B N    1 
ATOM   6223 C  CA   . LYS   B 1 163 ? 39.651 -40.415 -7.946  1.00 16.62 ?  163 LYS   B CA   1 
ATOM   6224 C  C    . LYS   B 1 163 ? 38.606 -39.308 -8.004  1.00 15.49 ?  163 LYS   B C    1 
ATOM   6225 O  O    . LYS   B 1 163 ? 37.397 -39.580 -8.002  1.00 16.23 ?  163 LYS   B O    1 
ATOM   6226 C  CB   . LYS   B 1 163 ? 40.140 -40.601 -6.512  1.00 19.66 ?  163 LYS   B CB   1 
ATOM   6227 C  CG   . LYS   B 1 163 ? 39.051 -41.094 -5.584  1.00 25.28 ?  163 LYS   B CG   1 
ATOM   6228 C  CD   . LYS   B 1 163 ? 39.549 -41.356 -4.177  1.00 30.52 ?  163 LYS   B CD   1 
ATOM   6229 C  CE   . LYS   B 1 163 ? 38.477 -42.072 -3.365  1.00 34.23 ?  163 LYS   B CE   1 
ATOM   6230 N  NZ   . LYS   B 1 163 ? 38.410 -41.588 -1.958  1.00 36.77 ?  163 LYS   B NZ   1 
ATOM   6231 H  H    . LYS   B 1 163 ? 41.527 -40.012 -8.437  1.00 19.20 ?  163 LYS   B H    1 
ATOM   6232 H  HA   . LYS   B 1 163 ? 39.228 -41.238 -8.227  1.00 19.98 ?  163 LYS   B HA   1 
ATOM   6233 H  HB2  . LYS   B 1 163 ? 40.857 -41.256 -6.505  1.00 23.63 ?  163 LYS   B HB2  1 
ATOM   6234 H  HB3  . LYS   B 1 163 ? 40.462 -39.753 -6.171  1.00 23.63 ?  163 LYS   B HB3  1 
ATOM   6235 H  HG2  . LYS   B 1 163 ? 38.350 -40.426 -5.531  1.00 30.37 ?  163 LYS   B HG2  1 
ATOM   6236 H  HG3  . LYS   B 1 163 ? 38.689 -41.926 -5.932  1.00 30.37 ?  163 LYS   B HG3  1 
ATOM   6237 H  HD2  . LYS   B 1 163 ? 40.337 -41.923 -4.211  1.00 36.66 ?  163 LYS   B HD2  1 
ATOM   6238 H  HD3  . LYS   B 1 163 ? 39.753 -40.515 -3.742  1.00 36.66 ?  163 LYS   B HD3  1 
ATOM   6239 H  HE2  . LYS   B 1 163 ? 37.612 -41.920 -3.779  1.00 41.11 ?  163 LYS   B HE2  1 
ATOM   6240 H  HE3  . LYS   B 1 163 ? 38.673 -43.023 -3.348  1.00 41.11 ?  163 LYS   B HE3  1 
ATOM   6241 H  HZ1  . LYS   B 1 163 ? 37.773 -42.026 -1.516  1.00 44.16 ?  163 LYS   B HZ1  1 
ATOM   6242 H  HZ2  . LYS   B 1 163 ? 39.190 -41.723 -1.553  1.00 44.16 ?  163 LYS   B HZ2  1 
ATOM   6243 H  HZ3  . LYS   B 1 163 ? 38.223 -40.718 -1.946  1.00 44.16 ?  163 LYS   B HZ3  1 
ATOM   6244 N  N    . LEU   B 1 164 ? 39.057 -38.053 -8.057  1.00 14.47 ?  164 LEU   B N    1 
ATOM   6245 C  CA   . LEU   B 1 164 ? 38.141 -36.919 -8.113  1.00 14.35 ?  164 LEU   B CA   1 
ATOM   6246 C  C    . LEU   B 1 164 ? 37.356 -36.905 -9.421  1.00 14.37 ?  164 LEU   B C    1 
ATOM   6247 O  O    . LEU   B 1 164 ? 36.135 -36.703 -9.422  1.00 15.23 ?  164 LEU   B O    1 
ATOM   6248 C  CB   . LEU   B 1 164 ? 38.931 -35.622 -7.945  1.00 13.82 ?  164 LEU   B CB   1 
ATOM   6249 C  CG   . LEU   B 1 164 ? 39.472 -35.347 -6.547  1.00 14.44 ?  164 LEU   B CG   1 
ATOM   6250 C  CD1  . LEU   B 1 164 ? 40.569 -34.295 -6.601  1.00 14.29 ?  164 LEU   B CD1  1 
ATOM   6251 C  CD2  . LEU   B 1 164 ? 38.362 -34.895 -5.626  1.00 16.26 ?  164 LEU   B CD2  1 
ATOM   6252 H  H    . LEU   B 1 164 ? 39.891 -37.832 -8.063  1.00 17.40 ?  164 LEU   B H    1 
ATOM   6253 H  HA   . LEU   B 1 164 ? 37.511 -36.982 -7.384  1.00 17.26 ?  164 LEU   B HA   1 
ATOM   6254 H  HB2  . LEU   B 1 164 ? 39.692 -35.641 -8.549  1.00 16.63 ?  164 LEU   B HB2  1 
ATOM   6255 H  HB3  . LEU   B 1 164 ? 38.356 -34.876 -8.182  1.00 16.63 ?  164 LEU   B HB3  1 
ATOM   6256 H  HG   . LEU   B 1 164 ? 39.856 -36.157 -6.189  1.00 17.37 ?  164 LEU   B HG   1 
ATOM   6257 H  HD11 . LEU   B 1 164 ? 40.895 -34.126 -5.701  1.00 17.18 ?  164 LEU   B HD11 1 
ATOM   6258 H  HD12 . LEU   B 1 164 ? 41.299 -34.621 -7.155  1.00 17.18 ?  164 LEU   B HD12 1 
ATOM   6259 H  HD13 . LEU   B 1 164 ? 40.212 -33.475 -6.979  1.00 17.18 ?  164 LEU   B HD13 1 
ATOM   6260 H  HD21 . LEU   B 1 164 ? 38.735 -34.690 -4.755  1.00 19.55 ?  164 LEU   B HD21 1 
ATOM   6261 H  HD22 . LEU   B 1 164 ? 37.941 -34.103 -5.999  1.00 19.55 ?  164 LEU   B HD22 1 
ATOM   6262 H  HD23 . LEU   B 1 164 ? 37.710 -35.609 -5.547  1.00 19.55 ?  164 LEU   B HD23 1 
ATOM   6263 N  N    . VAL   B 1 165 ? 38.046 -37.071 -10.549 1.00 15.72 ?  165 VAL   B N    1 
ATOM   6264 C  CA   . VAL   B 1 165 ? 37.390 -37.007 -11.852 1.00 16.53 ?  165 VAL   B CA   1 
ATOM   6265 C  C    . VAL   B 1 165 ? 36.473 -38.207 -12.040 1.00 18.19 ?  165 VAL   B C    1 
ATOM   6266 O  O    . VAL   B 1 165 ? 35.314 -38.073 -12.450 1.00 19.20 ?  165 VAL   B O    1 
ATOM   6267 C  CB   . VAL   B 1 165 ? 38.439 -36.919 -12.976 1.00 17.51 ?  165 VAL   B CB   1 
ATOM   6268 C  CG1  . VAL   B 1 165 ? 37.777 -37.020 -14.330 1.00 18.76 ?  165 VAL   B CG1  1 
ATOM   6269 C  CG2  . VAL   B 1 165 ? 39.235 -35.633 -12.862 1.00 17.29 ?  165 VAL   B CG2  1 
ATOM   6270 H  H    . VAL   B 1 165 ? 38.896 -37.212 -10.585 1.00 18.90 ?  165 VAL   B H    1 
ATOM   6271 H  HA   . VAL   B 1 165 ? 36.846 -36.208 -11.894 1.00 19.87 ?  165 VAL   B HA   1 
ATOM   6272 H  HB   . VAL   B 1 165 ? 39.063 -37.656 -12.888 1.00 21.05 ?  165 VAL   B HB   1 
ATOM   6273 H  HG11 . VAL   B 1 165 ? 38.398 -36.716 -15.008 1.00 22.55 ?  165 VAL   B HG11 1 
ATOM   6274 H  HG12 . VAL   B 1 165 ? 37.543 -37.949 -14.493 1.00 22.55 ?  165 VAL   B HG12 1 
ATOM   6275 H  HG13 . VAL   B 1 165 ? 36.981 -36.471 -14.334 1.00 22.55 ?  165 VAL   B HG13 1 
ATOM   6276 H  HG21 . VAL   B 1 165 ? 39.872 -35.585 -13.594 1.00 20.79 ?  165 VAL   B HG21 1 
ATOM   6277 H  HG22 . VAL   B 1 165 ? 38.626 -34.877 -12.908 1.00 20.79 ?  165 VAL   B HG22 1 
ATOM   6278 H  HG23 . VAL   B 1 165 ? 39.708 -35.622 -12.014 1.00 20.79 ?  165 VAL   B HG23 1 
ATOM   6279 N  N    . SER   B 1 166 ? 36.988 -39.403 -11.741 1.00 18.93 ?  166 SER   B N    1 
ATOM   6280 C  CA   . SER   B 1 166 ? 36.241 -40.621 -12.018 1.00 20.04 ?  166 SER   B CA   1 
ATOM   6281 C  C    . SER   B 1 166 ? 34.981 -40.709 -11.171 1.00 20.27 ?  166 SER   B C    1 
ATOM   6282 O  O    . SER   B 1 166 ? 34.012 -41.336 -11.596 1.00 21.71 ?  166 SER   B O    1 
ATOM   6283 C  CB   . SER   B 1 166 ? 37.114 -41.869 -11.838 1.00 20.96 ?  166 SER   B CB   1 
ATOM   6284 O  OG   . SER   B 1 166 ? 37.463 -42.079 -10.479 1.00 21.08 ?  166 SER   B OG   1 
ATOM   6285 H  H    . SER   B 1 166 ? 37.765 -39.532 -11.389 1.00 22.75 ?  166 SER   B H    1 
ATOM   6286 H  HA   . SER   B 1 166 ? 35.965 -40.605 -12.947 1.00 24.09 ?  166 SER   B HA   1 
ATOM   6287 H  HB2  . SER   B 1 166 ? 36.622 -42.644 -12.157 1.00 25.19 ?  166 SER   B HB2  1 
ATOM   6288 H  HB3  . SER   B 1 166 ? 37.926 -41.764 -12.363 1.00 25.19 ?  166 SER   B HB3  1 
ATOM   6289 H  HG   . SER   B 1 166 ? 37.906 -41.425 -10.197 1.00 25.33 ?  166 SER   B HG   1 
ATOM   6290 N  N    . SER   B 1 167 ? 34.957 -40.086 -9.993  1.00 19.16 ?  167 SER   B N    1 
ATOM   6291 C  CA   . SER   B 1 167 ? 33.803 -40.156 -9.104  1.00 18.86 ?  167 SER   B CA   1 
ATOM   6292 C  C    . SER   B 1 167 ? 32.881 -38.943 -9.203  1.00 18.38 ?  167 SER   B C    1 
ATOM   6293 O  O    . SER   B 1 167 ? 31.809 -38.942 -8.585  1.00 18.48 ?  167 SER   B O    1 
ATOM   6294 C  CB   . SER   B 1 167 ? 34.250 -40.338 -7.647  1.00 18.64 ?  167 SER   B CB   1 
ATOM   6295 O  OG   . SER   B 1 167 ? 34.920 -39.181 -7.168  1.00 18.55 ?  167 SER   B OG   1 
ATOM   6296 H  H    . SER   B 1 167 ? 35.605 -39.617 -9.687  1.00 23.03 ?  167 SER   B H    1 
ATOM   6297 H  HA   . SER   B 1 167 ? 33.278 -40.935 -9.345  1.00 22.66 ?  167 SER   B HA   1 
ATOM   6298 H  HB2  . SER   B 1 167 ? 33.468 -40.502 -7.097  1.00 22.41 ?  167 SER   B HB2  1 
ATOM   6299 H  HB3  . SER   B 1 167 ? 34.852 -41.101 -7.597  1.00 22.41 ?  167 SER   B HB3  1 
ATOM   6300 H  HG   . SER   B 1 167 ? 35.603 -39.038 -7.638  1.00 22.30 ?  167 SER   B HG   1 
ATOM   6301 N  N    . PHE   B 1 168 ? 33.258 -37.913 -9.964  1.00 18.01 ?  168 PHE   B N    1 
ATOM   6302 C  CA   . PHE   B 1 168 ? 32.427 -36.712 -10.029 1.00 17.54 ?  168 PHE   B CA   1 
ATOM   6303 C  C    . PHE   B 1 168 ? 31.112 -36.975 -10.756 1.00 15.59 ?  168 PHE   B C    1 
ATOM   6304 O  O    . PHE   B 1 168 ? 30.076 -36.368 -10.424 1.00 16.39 ?  168 PHE   B O    1 
ATOM   6305 C  CB   . PHE   B 1 168 ? 33.185 -35.575 -10.712 1.00 18.09 ?  168 PHE   B CB   1 
ATOM   6306 C  CG   . PHE   B 1 168 ? 32.382 -34.321 -10.830 1.00 18.26 ?  168 PHE   B CG   1 
ATOM   6307 C  CD1  . PHE   B 1 168 ? 32.078 -33.581 -9.698  1.00 19.36 ?  168 PHE   B CD1  1 
ATOM   6308 C  CD2  . PHE   B 1 168 ? 31.903 -33.896 -12.053 1.00 17.54 ?  168 PHE   B CD2  1 
ATOM   6309 C  CE1  . PHE   B 1 168 ? 31.320 -32.427 -9.784  1.00 19.85 ?  168 PHE   B CE1  1 
ATOM   6310 C  CE2  . PHE   B 1 168 ? 31.149 -32.732 -12.153 1.00 18.94 ?  168 PHE   B CE2  1 
ATOM   6311 C  CZ   . PHE   B 1 168 ? 30.854 -31.997 -11.014 1.00 19.25 ?  168 PHE   B CZ   1 
ATOM   6312 H  H    . PHE   B 1 168 ? 33.977 -37.881 -10.436 1.00 21.66 ?  168 PHE   B H    1 
ATOM   6313 H  HA   . PHE   B 1 168 ? 32.213 -36.427 -9.130  1.00 21.09 ?  168 PHE   B HA   1 
ATOM   6314 H  HB2  . PHE   B 1 168 ? 33.980 -35.367 -10.195 1.00 21.74 ?  168 PHE   B HB2  1 
ATOM   6315 H  HB3  . PHE   B 1 168 ? 33.436 -35.849 -11.607 1.00 21.74 ?  168 PHE   B HB3  1 
ATOM   6316 H  HD1  . PHE   B 1 168 ? 32.389 -33.869 -8.869  1.00 23.27 ?  168 PHE   B HD1  1 
ATOM   6317 H  HD2  . PHE   B 1 168 ? 32.098 -34.380 -12.821 1.00 21.08 ?  168 PHE   B HD2  1 
ATOM   6318 H  HE1  . PHE   B 1 168 ? 31.125 -31.941 -9.015  1.00 23.86 ?  168 PHE   B HE1  1 
ATOM   6319 H  HE2  . PHE   B 1 168 ? 30.832 -32.450 -12.984 1.00 22.76 ?  168 PHE   B HE2  1 
ATOM   6320 H  HZ   . PHE   B 1 168 ? 30.341 -31.222 -11.077 1.00 23.14 ?  168 PHE   B HZ   1 
ATOM   6321 N  N    . LEU   B 1 169 ? 31.139 -37.857 -11.751 1.00 15.76 ?  169 LEU   B N    1 
ATOM   6322 C  CA   . LEU   B 1 169 ? 29.958 -38.155 -12.545 1.00 17.82 ?  169 LEU   B CA   1 
ATOM   6323 C  C    . LEU   B 1 169 ? 29.945 -39.590 -13.048 1.00 20.27 ?  169 LEU   B C    1 
ATOM   6324 O  O    . LEU   B 1 169 ? 29.033 -39.998 -13.766 1.00 22.79 ?  169 LEU   B O    1 
ATOM   6325 C  CB   . LEU   B 1 169 ? 29.875 -37.204 -13.737 1.00 19.98 ?  169 LEU   B CB   1 
ATOM   6326 C  CG   . LEU   B 1 169 ? 28.606 -36.356 -13.827 1.00 23.02 ?  169 LEU   B CG   1 
ATOM   6327 C  CD1  . LEU   B 1 169 ? 28.533 -35.688 -15.186 1.00 24.08 ?  169 LEU   B CD1  1 
ATOM   6328 C  CD2  . LEU   B 1 169 ? 27.356 -37.177 -13.564 1.00 23.31 ?  169 LEU   B CD2  1 
ATOM   6329 O  OXT  . LEU   B 1 169 ? 30.857 -40.353 -12.752 1.00 20.78 -1 169 LEU   B OXT  1 
ATOM   6330 H  H    . LEU   B 1 169 ? 31.845 -38.292 -11.997 1.00 18.95 ?  169 LEU   B H    1 
ATOM   6331 H  HA   . LEU   B 1 169 ? 29.180 -38.022 -11.992 1.00 21.42 ?  169 LEU   B HA   1 
ATOM   6332 H  HB2  . LEU   B 1 169 ? 30.628 -36.589 -13.697 1.00 24.01 ?  169 LEU   B HB2  1 
ATOM   6333 H  HB3  . LEU   B 1 169 ? 29.930 -37.722 -14.556 1.00 24.01 ?  169 LEU   B HB3  1 
ATOM   6334 H  HG   . LEU   B 1 169 ? 28.650 -35.654 -13.157 1.00 27.67 ?  169 LEU   B HG   1 
ATOM   6335 H  HD11 . LEU   B 1 169 ? 27.740 -35.130 -15.220 1.00 28.93 ?  169 LEU   B HD11 1 
ATOM   6336 H  HD12 . LEU   B 1 169 ? 29.326 -35.144 -15.313 1.00 28.93 ?  169 LEU   B HD12 1 
ATOM   6337 H  HD13 . LEU   B 1 169 ? 28.487 -36.373 -15.870 1.00 28.93 ?  169 LEU   B HD13 1 
ATOM   6338 H  HD21 . LEU   B 1 169 ? 26.599 -36.747 -13.985 1.00 28.02 ?  169 LEU   B HD21 1 
ATOM   6339 H  HD22 . LEU   B 1 169 ? 27.481 -38.067 -13.933 1.00 28.02 ?  169 LEU   B HD22 1 
ATOM   6340 H  HD23 . LEU   B 1 169 ? 27.217 -37.235 -12.606 1.00 28.02 ?  169 LEU   B HD23 1 
HETATM 6341 N  N2   B A1BAV C 2 .   ? 15.316 1.262   6.332   0.18 12.27 ?  201 A1BAV A N2   1 
HETATM 6342 C  C3   B A1BAV C 2 .   ? 15.610 4.532   4.938   0.18 10.98 ?  201 A1BAV A C3   1 
HETATM 6343 C  C6   B A1BAV C 2 .   ? 15.204 1.143   3.488   0.18 12.40 ?  201 A1BAV A C6   1 
HETATM 6344 C  C9   B A1BAV C 2 .   ? 12.765 -0.027  0.616   0.18 13.90 ?  201 A1BAV A C9   1 
HETATM 6345 C  C12  B A1BAV C 2 .   ? 13.991 -2.094  0.193   0.18 13.63 ?  201 A1BAV A C12  1 
HETATM 6346 C  C1   B A1BAV C 2 .   ? 15.485 4.314   2.419   0.18 12.16 ?  201 A1BAV A C1   1 
HETATM 6347 C  C10  B A1BAV C 2 .   ? 11.497 -0.740  0.058   0.18 14.50 ?  201 A1BAV A C10  1 
HETATM 6348 C  C11  B A1BAV C 2 .   ? 12.699 -2.863  0.230   0.18 13.80 ?  201 A1BAV A C11  1 
HETATM 6349 C  C13  B A1BAV C 2 .   ? 15.359 2.411   4.127   0.18 11.99 ?  201 A1BAV A C13  1 
HETATM 6350 C  C2   B A1BAV C 2 .   ? 15.496 3.767   3.775   0.18 11.91 ?  201 A1BAV A C2   1 
HETATM 6351 C  C4   B A1BAV C 2 .   ? 15.407 2.380   5.550   0.18 11.83 ?  201 A1BAV A C4   1 
HETATM 6352 C  C5   B A1BAV C 2 .   ? 15.179 0.138   5.613   0.18 12.35 ?  201 A1BAV A C5   1 
HETATM 6353 C  C7   B A1BAV C 2 .   ? 15.204 -0.253  1.389   0.18 12.24 ?  201 A1BAV A C7   1 
HETATM 6354 C  C8   B A1BAV C 2 .   ? 13.852 -0.964  1.192   0.18 13.17 ?  201 A1BAV A C8   1 
HETATM 6355 N  N1   B A1BAV C 2 .   ? 15.565 3.667   6.041   0.18 11.70 ?  201 A1BAV A N1   1 
HETATM 6356 N  N3   B A1BAV C 2 .   ? 15.118 0.004   4.246   0.18 12.33 ?  201 A1BAV A N3   1 
HETATM 6357 N  N4   B A1BAV C 2 .   ? 15.146 1.013   2.114   0.18 12.47 ?  201 A1BAV A N4   1 
HETATM 6358 O  O1   B A1BAV C 2 .   ? 13.374 -1.415  2.428   0.18 13.32 ?  201 A1BAV A O1   1 
HETATM 6359 O  O2   B A1BAV C 2 .   ? 11.656 -2.105  -0.353  0.18 14.46 ?  201 A1BAV A O2   1 
HETATM 6360 H  H4   B A1BAV C 2 .   ? 15.719 5.596   5.087   0.18 13.21 ?  201 A1BAV A H4   1 
HETATM 6361 H  H11  B A1BAV C 2 .   ? 12.445 0.701   1.379   0.18 16.72 ?  201 A1BAV A H11  1 
HETATM 6362 H  H12  B A1BAV C 2 .   ? 13.201 0.582   -0.195  0.18 16.72 ?  201 A1BAV A H12  1 
HETATM 6363 H  H17  B A1BAV C 2 .   ? 14.168 -1.721  -0.849  0.18 16.40 ?  201 A1BAV A H17  1 
HETATM 6364 H  H18  B A1BAV C 2 .   ? 14.842 -2.756  0.417   0.18 16.40 ?  201 A1BAV A H18  1 
HETATM 6365 H  H3   B A1BAV C 2 .   ? 14.898 3.732   1.705   0.18 14.63 ?  201 A1BAV A H3   1 
HETATM 6366 H  H1   B A1BAV C 2 .   ? 16.481 4.367   1.999   0.18 14.63 ?  201 A1BAV A H1   1 
HETATM 6367 H  H2   B A1BAV C 2 .   ? 15.087 5.295   2.407   0.18 14.63 ?  201 A1BAV A H2   1 
HETATM 6368 H  H13  B A1BAV C 2 .   ? 10.622 -0.591  0.725   0.18 17.44 ?  201 A1BAV A H13  1 
HETATM 6369 H  H14  B A1BAV C 2 .   ? 11.176 -0.259  -0.902  0.18 17.44 ?  201 A1BAV A H14  1 
HETATM 6370 H  H16  B A1BAV C 2 .   ? 12.799 -3.862  -0.237  0.18 16.60 ?  201 A1BAV A H16  1 
HETATM 6371 H  H15  B A1BAV C 2 .   ? 12.360 -3.091  1.265   0.18 16.60 ?  201 A1BAV A H15  1 
HETATM 6372 H  H6   B A1BAV C 2 .   ? 15.099 -0.766  6.245   0.18 14.86 ?  201 A1BAV A H6   1 
HETATM 6373 H  H8   B A1BAV C 2 .   ? 15.624 -0.043  0.378   0.18 14.72 ?  201 A1BAV A H8   1 
HETATM 6374 H  H9   B A1BAV C 2 .   ? 15.909 -0.956  1.858   0.18 14.72 ?  201 A1BAV A H9   1 
HETATM 6375 H  H5   B A1BAV C 2 .   ? 15.613 3.915   7.025   0.18 14.08 ?  201 A1BAV A H5   1 
HETATM 6376 H  H7   B A1BAV C 2 .   ? 15.052 1.839   1.570   0.18 15.00 ?  201 A1BAV A H7   1 
HETATM 6377 H  H10  B A1BAV C 2 .   ? 13.932 -2.148  2.706   0.18 16.02 ?  201 A1BAV A H10  1 
HETATM 6378 CL CL   B CL    D 3 .   ? 15.929 2.705   -0.769  0.18 14.86 ?  202 CL    A CL   1 
HETATM 6379 O  O    . HOH   E 4 .   ? 26.850 11.392  1.687   1.00 16.23 ?  301 HOH   A O    1 
HETATM 6380 O  O    . HOH   E 4 .   ? 6.963  -8.198  11.906  1.00 21.84 ?  302 HOH   A O    1 
HETATM 6381 O  O    . HOH   E 4 .   ? 14.842 -4.721  20.559  1.00 42.50 ?  303 HOH   A O    1 
HETATM 6382 O  O    . HOH   E 4 .   ? 22.777 12.513  1.679   1.00 15.02 ?  304 HOH   A O    1 
HETATM 6383 O  O    . HOH   E 4 .   ? 4.720  3.904   0.702   1.00 25.37 ?  305 HOH   A O    1 
HETATM 6384 O  O    . HOH   E 4 .   ? 18.612 -2.430  -16.353 1.00 41.55 ?  306 HOH   A O    1 
HETATM 6385 O  O    . HOH   E 4 .   ? 7.627  -6.258  -6.487  1.00 40.53 ?  307 HOH   A O    1 
HETATM 6386 O  O    . HOH   E 4 .   ? 34.378 -1.882  12.500  1.00 36.18 ?  308 HOH   A O    1 
HETATM 6387 O  O    . HOH   E 4 .   ? -0.437 -3.097  3.186   1.00 37.96 ?  309 HOH   A O    1 
HETATM 6388 O  O    . HOH   E 4 .   ? 12.168 0.296   14.937  1.00 35.76 ?  310 HOH   A O    1 
HETATM 6389 O  O    . HOH   E 4 .   ? 0.703  -4.633  0.340   1.00 31.96 ?  311 HOH   A O    1 
HETATM 6390 O  O    . HOH   E 4 .   ? 8.034  -21.562 3.977   1.00 40.44 ?  312 HOH   A O    1 
HETATM 6391 O  O    . HOH   E 4 .   ? 9.159  -10.262 19.450  1.00 39.28 ?  313 HOH   A O    1 
HETATM 6392 O  O    . HOH   E 4 .   ? 3.583  -9.290  10.007  1.00 35.66 ?  314 HOH   A O    1 
HETATM 6393 O  O    . HOH   E 4 .   ? 28.887 0.442   -9.710  1.00 21.29 ?  315 HOH   A O    1 
HETATM 6394 O  O    . HOH   E 4 .   ? 15.137 -12.266 18.717  1.00 34.11 ?  316 HOH   A O    1 
HETATM 6395 O  O    . HOH   E 4 .   ? 23.971 -15.712 -9.176  1.00 31.79 ?  317 HOH   A O    1 
HETATM 6396 O  O    . HOH   E 4 .   ? 42.474 10.546  5.164   1.00 19.88 ?  318 HOH   A O    1 
HETATM 6397 O  O    . HOH   E 4 .   ? 17.139 -18.081 15.092  1.00 23.72 ?  319 HOH   A O    1 
HETATM 6398 O  O    . HOH   E 4 .   ? 28.314 -6.387  19.589  1.00 43.18 ?  320 HOH   A O    1 
HETATM 6399 O  O    . HOH   E 4 .   ? 19.854 -12.550 -8.887  1.00 26.41 ?  321 HOH   A O    1 
HETATM 6400 O  O    . HOH   E 4 .   ? 33.991 -1.000  -8.886  1.00 27.20 ?  322 HOH   A O    1 
HETATM 6401 O  O    . HOH   E 4 .   ? 14.101 -4.499  -11.790 1.00 30.99 ?  323 HOH   A O    1 
HETATM 6402 O  O    . HOH   E 4 .   ? 13.290 -1.424  -6.519  1.00 17.44 ?  324 HOH   A O    1 
HETATM 6403 O  O    . HOH   E 4 .   ? 30.250 -13.323 -8.564  1.00 19.68 ?  325 HOH   A O    1 
HETATM 6404 O  O    . HOH   E 4 .   ? 36.163 -5.095  -0.572  1.00 26.70 ?  326 HOH   A O    1 
HETATM 6405 O  O    . HOH   E 4 .   ? 14.748 -14.033 16.706  1.00 22.00 ?  327 HOH   A O    1 
HETATM 6406 O  O    . HOH   E 4 .   ? 26.495 -19.355 -1.822  1.00 13.64 ?  328 HOH   A O    1 
HETATM 6407 O  O    . HOH   E 4 .   ? 11.632 -10.854 -10.085 1.00 39.09 ?  329 HOH   A O    1 
HETATM 6408 O  O    . HOH   E 4 .   ? 37.556 2.764   10.196  1.00 27.26 ?  330 HOH   A O    1 
HETATM 6409 O  O    . HOH   E 4 .   ? 31.042 -18.171 7.782   1.00 19.99 ?  331 HOH   A O    1 
HETATM 6410 O  O    . HOH   E 4 .   ? 28.332 -0.160  -13.370 1.00 33.62 ?  332 HOH   A O    1 
HETATM 6411 O  O    . HOH   E 4 .   ? 17.602 -1.733  0.478   1.00 18.87 ?  333 HOH   A O    1 
HETATM 6412 O  O    . HOH   E 4 .   ? 7.961  -12.710 -0.808  1.00 21.97 ?  334 HOH   A O    1 
HETATM 6413 O  O    . HOH   E 4 .   ? 38.298 10.113  7.143   1.00 37.06 ?  335 HOH   A O    1 
HETATM 6414 O  O    . HOH   E 4 .   ? 20.607 -19.706 -5.083  1.00 27.06 ?  336 HOH   A O    1 
HETATM 6415 O  O    . HOH   E 4 .   ? 38.601 4.983   6.950   1.00 15.53 ?  337 HOH   A O    1 
HETATM 6416 O  O    . HOH   E 4 .   ? 14.617 -3.708  3.134   1.00 17.02 ?  338 HOH   A O    1 
HETATM 6417 O  O    . HOH   E 4 .   ? 18.864 -22.020 6.874   1.00 30.98 ?  339 HOH   A O    1 
HETATM 6418 O  O    . HOH   E 4 .   ? 27.290 13.763  2.895   1.00 29.49 ?  340 HOH   A O    1 
HETATM 6419 O  O    . HOH   E 4 .   ? 42.570 4.283   5.349   1.00 31.04 ?  341 HOH   A O    1 
HETATM 6420 O  O    . HOH   E 4 .   ? -1.227 -4.587  7.624   1.00 48.25 ?  342 HOH   A O    1 
HETATM 6421 O  O    . HOH   E 4 .   ? 18.668 -19.417 13.579  1.00 35.65 ?  343 HOH   A O    1 
HETATM 6422 O  O    . HOH   E 4 .   ? 22.437 5.335   19.132  1.00 44.95 ?  344 HOH   A O    1 
HETATM 6423 O  O    . HOH   E 4 .   ? 21.261 -2.413  -2.075  1.00 16.19 ?  345 HOH   A O    1 
HETATM 6424 O  O    . HOH   E 4 .   ? 30.916 6.224   -12.293 1.00 28.13 ?  346 HOH   A O    1 
HETATM 6425 O  O    . HOH   E 4 .   ? 39.753 -1.030  -5.196  1.00 20.74 ?  347 HOH   A O    1 
HETATM 6426 O  O    . HOH   E 4 .   ? 27.902 0.833   -7.149  1.00 13.90 ?  348 HOH   A O    1 
HETATM 6427 O  O    . HOH   E 4 .   ? 35.787 -12.719 6.802   1.00 15.81 ?  349 HOH   A O    1 
HETATM 6428 O  O    . HOH   E 4 .   ? 17.161 -17.865 -5.023  1.00 26.96 ?  350 HOH   A O    1 
HETATM 6429 O  O    . HOH   E 4 .   ? 22.266 -19.279 11.367  1.00 33.03 ?  351 HOH   A O    1 
HETATM 6430 O  O    . HOH   E 4 .   ? 44.354 7.089   6.417   1.00 26.49 ?  352 HOH   A O    1 
HETATM 6431 O  O    . HOH   E 4 .   ? 8.837  -12.030 17.266  1.00 42.39 ?  353 HOH   A O    1 
HETATM 6432 O  O    . HOH   E 4 .   ? 43.889 8.377   -3.149  1.00 25.67 ?  354 HOH   A O    1 
HETATM 6433 O  O    . HOH   E 4 .   ? 9.813  -21.397 5.743   1.00 18.10 ?  355 HOH   A O    1 
HETATM 6434 O  O    . HOH   E 4 .   ? 11.713 -10.801 17.081  1.00 23.62 ?  356 HOH   A O    1 
HETATM 6435 O  O    . HOH   E 4 .   ? 31.078 -13.964 -2.506  1.00 13.51 ?  357 HOH   A O    1 
HETATM 6436 O  O    . HOH   E 4 .   ? 15.208 3.934   17.827  1.00 38.07 ?  358 HOH   A O    1 
HETATM 6437 O  O    . HOH   E 4 .   ? 33.672 -7.179  4.288   1.00 17.11 ?  359 HOH   A O    1 
HETATM 6438 O  O    . HOH   E 4 .   ? 24.025 -2.114  -2.065  1.00 10.95 ?  360 HOH   A O    1 
HETATM 6439 O  O    . HOH   E 4 .   ? 14.341 -21.252 -4.210  1.00 29.59 ?  361 HOH   A O    1 
HETATM 6440 O  O    . HOH   E 4 .   ? 18.614 9.438   9.047   1.00 20.46 ?  362 HOH   A O    1 
HETATM 6441 O  O    . HOH   E 4 .   ? 15.563 11.927  8.035   1.00 25.78 ?  363 HOH   A O    1 
HETATM 6442 O  O    . HOH   E 4 .   ? 21.939 -21.943 8.425   1.00 26.74 ?  364 HOH   A O    1 
HETATM 6443 O  O    . HOH   E 4 .   ? 16.501 -22.051 0.987   1.00 25.94 ?  365 HOH   A O    1 
HETATM 6444 O  O    . HOH   E 4 .   ? -0.626 -8.538  2.195   1.00 41.26 ?  366 HOH   A O    1 
HETATM 6445 O  O    . HOH   E 4 .   ? 30.829 3.068   8.274   1.00 12.13 ?  367 HOH   A O    1 
HETATM 6446 O  O    . HOH   E 4 .   ? 24.758 -17.532 12.772  1.00 24.31 ?  368 HOH   A O    1 
HETATM 6447 O  O    . HOH   E 4 .   ? 37.288 -2.828  9.690   1.00 40.77 ?  369 HOH   A O    1 
HETATM 6448 O  O    . HOH   E 4 .   ? 31.714 8.222   14.864  1.00 22.24 ?  370 HOH   A O    1 
HETATM 6449 O  O    . HOH   E 4 .   ? 27.529 -10.648 14.051  1.00 17.21 ?  371 HOH   A O    1 
HETATM 6450 O  O    . HOH   E 4 .   ? 37.443 11.922  4.932   1.00 31.21 ?  372 HOH   A O    1 
HETATM 6451 O  O    A HOH   E 4 .   ? 14.292 0.539   6.854   0.82 22.30 ?  373 HOH   A O    1 
HETATM 6452 O  O    . HOH   E 4 .   ? 13.521 -15.241 -7.431  1.00 28.01 ?  374 HOH   A O    1 
HETATM 6453 O  O    . HOH   E 4 .   ? 31.917 -9.318  -6.646  1.00 22.00 ?  375 HOH   A O    1 
HETATM 6454 O  O    . HOH   E 4 .   ? 31.743 -7.313  -9.849  1.00 21.25 ?  376 HOH   A O    1 
HETATM 6455 O  O    . HOH   E 4 .   ? 43.384 7.829   2.665   1.00 26.33 ?  377 HOH   A O    1 
HETATM 6456 O  O    . HOH   E 4 .   ? 24.429 3.571   -1.800  1.00 14.73 ?  378 HOH   A O    1 
HETATM 6457 O  O    . HOH   E 4 .   ? 25.700 -0.821  -7.360  1.00 15.02 ?  379 HOH   A O    1 
HETATM 6458 O  O    . HOH   E 4 .   ? 14.022 -5.008  17.587  1.00 24.91 ?  380 HOH   A O    1 
HETATM 6459 O  O    . HOH   E 4 .   ? 28.530 -10.591 -14.023 1.00 42.07 ?  381 HOH   A O    1 
HETATM 6460 O  O    . HOH   E 4 .   ? 17.018 -19.317 4.895   1.00 14.87 ?  382 HOH   A O    1 
HETATM 6461 O  O    . HOH   E 4 .   ? 23.491 11.355  4.125   1.00 12.45 ?  383 HOH   A O    1 
HETATM 6462 O  O    . HOH   E 4 .   ? 10.403 -22.183 -1.237  1.00 46.79 ?  384 HOH   A O    1 
HETATM 6463 O  O    . HOH   E 4 .   ? 15.845 2.091   24.832  1.00 49.23 ?  385 HOH   A O    1 
HETATM 6464 O  O    . HOH   E 4 .   ? 24.313 -7.829  14.468  1.00 17.39 ?  386 HOH   A O    1 
HETATM 6465 O  O    . HOH   E 4 .   ? 22.676 -12.007 21.850  1.00 41.27 ?  387 HOH   A O    1 
HETATM 6466 O  O    . HOH   E 4 .   ? 18.966 -0.687  -1.616  1.00 13.38 ?  388 HOH   A O    1 
HETATM 6467 O  O    . HOH   E 4 .   ? 21.256 10.314  15.063  1.00 32.70 ?  389 HOH   A O    1 
HETATM 6468 O  O    . HOH   E 4 .   ? 24.616 1.973   -7.075  1.00 20.01 ?  390 HOH   A O    1 
HETATM 6469 O  O    . HOH   E 4 .   ? 32.786 -9.281  5.910   1.00 19.96 ?  391 HOH   A O    1 
HETATM 6470 O  O    . HOH   E 4 .   ? 30.723 1.851   16.702  1.00 22.31 ?  392 HOH   A O    1 
HETATM 6471 O  O    . HOH   E 4 .   ? 27.326 -6.034  -14.029 1.00 36.28 ?  393 HOH   A O    1 
HETATM 6472 O  O    . HOH   E 4 .   ? 37.545 -2.059  5.745   1.00 26.42 ?  394 HOH   A O    1 
HETATM 6473 O  O    . HOH   E 4 .   ? 20.126 4.506   -7.485  1.00 19.62 ?  395 HOH   A O    1 
HETATM 6474 O  O    . HOH   E 4 .   ? 11.083 1.566   12.834  1.00 24.21 ?  396 HOH   A O    1 
HETATM 6475 O  O    . HOH   E 4 .   ? 6.495  -5.619  11.231  1.00 21.50 ?  397 HOH   A O    1 
HETATM 6476 O  O    . HOH   E 4 .   ? 21.379 3.114   -0.307  1.00 13.22 ?  398 HOH   A O    1 
HETATM 6477 O  O    . HOH   E 4 .   ? 27.343 2.324   18.715  1.00 30.47 ?  399 HOH   A O    1 
HETATM 6478 O  O    . HOH   E 4 .   ? 21.801 -13.843 -8.125  1.00 38.27 ?  400 HOH   A O    1 
HETATM 6479 O  O    . HOH   E 4 .   ? 15.220 -21.629 14.206  1.00 16.98 ?  401 HOH   A O    1 
HETATM 6480 O  O    . HOH   E 4 .   ? 14.443 -24.736 11.599  1.00 30.06 ?  402 HOH   A O    1 
HETATM 6481 O  O    A HOH   E 4 .   ? 15.815 -0.977  5.319   0.82 24.58 ?  403 HOH   A O    1 
HETATM 6482 O  O    . HOH   E 4 .   ? 26.956 4.134   -0.625  1.00 12.98 ?  404 HOH   A O    1 
HETATM 6483 O  O    . HOH   E 4 .   ? 15.138 -8.068  -9.606  1.00 22.41 ?  405 HOH   A O    1 
HETATM 6484 O  O    . HOH   E 4 .   ? 20.580 -20.046 2.783   1.00 17.28 ?  406 HOH   A O    1 
HETATM 6485 O  O    . HOH   E 4 .   ? 41.580 1.538   4.911   1.00 36.78 ?  407 HOH   A O    1 
HETATM 6486 O  O    . HOH   E 4 .   ? 40.894 -8.287  -6.755  1.00 35.86 ?  408 HOH   A O    1 
HETATM 6487 O  O    . HOH   E 4 .   ? 14.085 -23.117 7.428   1.00 17.85 ?  409 HOH   A O    1 
HETATM 6488 O  O    . HOH   E 4 .   ? 16.240 16.609  8.764   1.00 26.99 ?  410 HOH   A O    1 
HETATM 6489 O  O    . HOH   E 4 .   ? 30.097 -10.139 12.997  1.00 21.66 ?  411 HOH   A O    1 
HETATM 6490 O  O    . HOH   E 4 .   ? 38.096 -1.351  -1.964  1.00 19.83 ?  412 HOH   A O    1 
HETATM 6491 O  O    . HOH   E 4 .   ? 23.934 -20.304 -1.366  1.00 15.38 ?  413 HOH   A O    1 
HETATM 6492 O  O    . HOH   E 4 .   ? 35.109 -5.220  -3.130  1.00 17.82 ?  414 HOH   A O    1 
HETATM 6493 O  O    . HOH   E 4 .   ? 32.641 -4.278  -9.900  1.00 28.28 ?  415 HOH   A O    1 
HETATM 6494 O  O    . HOH   E 4 .   ? 32.577 -10.658 3.164   1.00 30.02 ?  416 HOH   A O    1 
HETATM 6495 O  O    . HOH   E 4 .   ? 14.499 -0.516  -11.979 1.00 26.15 ?  417 HOH   A O    1 
HETATM 6496 O  O    . HOH   E 4 .   ? 16.192 -14.191 20.370  1.00 42.68 ?  418 HOH   A O    1 
HETATM 6497 O  O    . HOH   E 4 .   ? 5.159  2.610   5.279   1.00 32.79 ?  419 HOH   A O    1 
HETATM 6498 O  O    . HOH   E 4 .   ? 30.408 -12.990 13.475  1.00 19.92 ?  420 HOH   A O    1 
HETATM 6499 O  O    . HOH   E 4 .   ? 6.716  -3.424  13.023  1.00 31.71 ?  421 HOH   A O    1 
HETATM 6500 O  O    . HOH   E 4 .   ? 44.985 -0.611  2.948   1.00 42.53 ?  422 HOH   A O    1 
HETATM 6501 O  O    . HOH   E 4 .   ? 36.750 -4.994  5.369   1.00 23.34 ?  423 HOH   A O    1 
HETATM 6502 O  O    . HOH   E 4 .   ? 27.145 -3.246  19.365  1.00 33.97 ?  424 HOH   A O    1 
HETATM 6503 O  O    . HOH   E 4 .   ? 10.406 -13.756 -1.644  1.00 17.81 ?  425 HOH   A O    1 
HETATM 6504 O  O    . HOH   E 4 .   ? 24.063 3.923   -4.903  1.00 25.13 ?  426 HOH   A O    1 
HETATM 6505 O  O    . HOH   E 4 .   ? 16.039 7.026   3.088   1.00 17.79 ?  427 HOH   A O    1 
HETATM 6506 O  O    A HOH   E 4 .   ? 11.076 -0.409  1.991   0.82 25.09 ?  428 HOH   A O    1 
HETATM 6507 O  O    . HOH   E 4 .   ? 22.677 8.103   18.414  1.00 41.22 ?  429 HOH   A O    1 
HETATM 6508 O  O    . HOH   E 4 .   ? 21.294 -9.287  21.360  1.00 43.63 ?  430 HOH   A O    1 
HETATM 6509 O  O    . HOH   E 4 .   ? 18.877 1.995   -0.667  1.00 13.85 ?  431 HOH   A O    1 
HETATM 6510 O  O    . HOH   E 4 .   ? 20.608 -17.757 24.828  1.00 48.89 ?  432 HOH   A O    1 
HETATM 6511 O  O    . HOH   E 4 .   ? 37.742 -8.852  -3.572  1.00 25.05 ?  433 HOH   A O    1 
HETATM 6512 O  O    . HOH   E 4 .   ? 23.606 -8.089  17.089  1.00 20.95 ?  434 HOH   A O    1 
HETATM 6513 O  O    . HOH   E 4 .   ? 19.468 -11.113 24.113  1.00 64.30 ?  435 HOH   A O    1 
HETATM 6514 O  O    A HOH   E 4 .   ? 16.260 2.927   -1.386  0.82 15.92 ?  436 HOH   A O    1 
HETATM 6515 O  O    . HOH   E 4 .   ? 23.324 -20.995 1.298   1.00 17.81 ?  437 HOH   A O    1 
HETATM 6516 O  O    . HOH   E 4 .   ? 23.243 7.632   -3.129  1.00 22.73 ?  438 HOH   A O    1 
HETATM 6517 O  O    . HOH   E 4 .   ? 34.443 -8.076  -0.606  1.00 26.14 ?  439 HOH   A O    1 
HETATM 6518 O  O    . HOH   E 4 .   ? 30.598 14.774  2.831   1.00 18.60 ?  440 HOH   A O    1 
HETATM 6519 O  O    . HOH   E 4 .   ? 18.495 4.870   -15.094 1.00 48.82 ?  441 HOH   A O    1 
HETATM 6520 O  O    . HOH   E 4 .   ? 9.417  -16.317 -2.054  1.00 46.01 ?  442 HOH   A O    1 
HETATM 6521 O  O    . HOH   E 4 .   ? 31.355 -12.783 -0.002  1.00 18.69 ?  443 HOH   A O    1 
HETATM 6522 O  O    . HOH   E 4 .   ? 18.455 -16.143 16.473  1.00 34.84 ?  444 HOH   A O    1 
HETATM 6523 O  O    . HOH   E 4 .   ? 21.618 -14.713 17.990  1.00 48.84 ?  445 HOH   A O    1 
HETATM 6524 O  O    . HOH   E 4 .   ? 27.712 7.007   -6.278  1.00 33.78 ?  446 HOH   A O    1 
HETATM 6525 O  O    . HOH   E 4 .   ? 29.799 -16.074 10.606  1.00 33.85 ?  447 HOH   A O    1 
HETATM 6526 O  O    A HOH   E 4 .   ? 14.039 -0.368  3.515   0.82 23.13 ?  448 HOH   A O    1 
HETATM 6527 O  O    . HOH   E 4 .   ? 25.440 8.245   -4.762  1.00 21.71 ?  449 HOH   A O    1 
HETATM 6528 O  O    . HOH   E 4 .   ? 32.491 -15.976 10.820  1.00 34.76 ?  450 HOH   A O    1 
HETATM 6529 O  O    . HOH   E 4 .   ? 19.926 -17.366 -5.065  1.00 23.94 ?  451 HOH   A O    1 
HETATM 6530 O  O    . HOH   E 4 .   ? 11.989 -13.437 16.407  1.00 43.30 ?  452 HOH   A O    1 
HETATM 6531 O  O    . HOH   E 4 .   ? 29.859 -1.973  -12.732 1.00 45.77 ?  453 HOH   A O    1 
HETATM 6532 O  O    . HOH   E 4 .   ? 26.929 11.627  -1.261  1.00 27.88 ?  454 HOH   A O    1 
HETATM 6533 O  O    . HOH   E 4 .   ? 24.953 5.672   20.740  1.00 50.42 ?  455 HOH   A O    1 
HETATM 6534 O  O    . HOH   E 4 .   ? 23.195 -22.347 -3.364  1.00 34.62 ?  456 HOH   A O    1 
HETATM 6535 O  O    . HOH   E 4 .   ? 24.638 14.545  7.890   1.00 35.01 ?  457 HOH   A O    1 
HETATM 6536 O  O    . HOH   E 4 .   ? 23.532 13.712  5.544   1.00 18.98 ?  458 HOH   A O    1 
HETATM 6537 O  O    . HOH   E 4 .   ? 27.488 -11.395 16.552  1.00 36.32 ?  459 HOH   A O    1 
HETATM 6538 O  O    . HOH   E 4 .   ? 15.699 -21.522 3.676   1.00 21.02 ?  460 HOH   A O    1 
HETATM 6539 O  O    . HOH   E 4 .   ? 21.955 5.205   -5.840  1.00 27.66 ?  461 HOH   A O    1 
HETATM 6540 O  O    . HOH   E 4 .   ? 18.754 10.782  11.397  1.00 31.39 ?  462 HOH   A O    1 
HETATM 6541 O  O    . HOH   E 4 .   ? 39.623 -7.027  -3.547  1.00 44.60 ?  463 HOH   A O    1 
HETATM 6542 O  O    . HOH   E 4 .   ? 25.869 10.790  -3.678  1.00 23.45 ?  464 HOH   A O    1 
HETATM 6543 O  O    . HOH   E 4 .   ? 12.347 1.574   17.394  1.00 38.82 ?  465 HOH   A O    1 
HETATM 6544 O  O    . HOH   E 4 .   ? 10.938 -15.092 -6.025  1.00 35.05 ?  466 HOH   A O    1 
HETATM 6545 O  O    . HOH   E 4 .   ? 35.205 7.407   12.243  1.00 44.56 ?  467 HOH   A O    1 
HETATM 6546 O  O    . HOH   E 4 .   ? 28.857 8.994   17.519  1.00 36.41 ?  468 HOH   A O    1 
HETATM 6547 O  O    . HOH   E 4 .   ? 17.422 -18.762 19.819  1.00 46.48 ?  469 HOH   A O    1 
HETATM 6548 O  O    . HOH   E 4 .   ? 13.998 -10.255 -10.839 1.00 31.68 ?  470 HOH   A O    1 
HETATM 6549 O  O    . HOH   E 4 .   ? 23.147 11.806  -4.031  1.00 19.18 ?  471 HOH   A O    1 
HETATM 6550 O  O    . HOH   E 4 .   ? 18.107 -16.305 -8.749  1.00 41.72 ?  472 HOH   A O    1 
HETATM 6551 O  O    . HOH   E 4 .   ? 16.780 -20.617 16.200  1.00 26.61 ?  473 HOH   A O    1 
HETATM 6552 O  O    . HOH   E 4 .   ? 30.856 0.664   19.179  1.00 38.66 ?  474 HOH   A O    1 
HETATM 6553 O  O    . HOH   E 4 .   ? 15.678 -17.157 -6.941  1.00 32.13 ?  475 HOH   A O    1 
HETATM 6554 O  O    . HOH   E 4 .   ? 40.956 -3.993  -0.358  1.00 36.03 ?  476 HOH   A O    1 
HETATM 6555 O  O    . HOH   E 4 .   ? 41.719 9.298   -4.067  1.00 32.10 ?  477 HOH   A O    1 
HETATM 6556 O  O    . HOH   E 4 .   ? 44.514 10.420  -1.640  1.00 31.03 ?  478 HOH   A O    1 
HETATM 6557 O  O    . HOH   E 4 .   ? 23.287 -12.936 19.344  1.00 44.25 ?  479 HOH   A O    1 
HETATM 6558 O  O    . HOH   E 4 .   ? 28.572 -4.679  -12.302 1.00 36.36 ?  480 HOH   A O    1 
HETATM 6559 O  O    . HOH   E 4 .   ? 18.529 -23.222 1.929   1.00 39.59 ?  481 HOH   A O    1 
HETATM 6560 O  O    . HOH   E 4 .   ? 15.940 -6.726  -11.782 1.00 43.06 ?  482 HOH   A O    1 
HETATM 6561 O  O    . HOH   E 4 .   ? 39.193 2.394   7.535   1.00 30.88 ?  483 HOH   A O    1 
HETATM 6562 O  O    . HOH   E 4 .   ? 40.486 -0.257  -7.843  1.00 34.78 ?  484 HOH   A O    1 
HETATM 6563 O  O    . HOH   E 4 .   ? 20.510 -16.078 -7.339  1.00 29.69 ?  485 HOH   A O    1 
HETATM 6564 O  O    . HOH   E 4 .   ? 31.466 -0.649  -10.563 1.00 28.66 ?  486 HOH   A O    1 
HETATM 6565 O  O    . HOH   E 4 .   ? 20.021 -22.364 4.166   1.00 26.89 ?  487 HOH   A O    1 
HETATM 6566 O  O    . HOH   E 4 .   ? 28.667 -7.894  -15.278 1.00 44.18 ?  488 HOH   A O    1 
HETATM 6567 O  O    . HOH   E 4 .   ? 30.749 5.814   -14.694 1.00 34.68 ?  489 HOH   A O    1 
HETATM 6568 O  O    . HOH   E 4 .   ? 16.141 -23.367 5.728   1.00 26.43 ?  490 HOH   A O    1 
HETATM 6569 O  O    . HOH   E 4 .   ? 14.111 -25.426 8.923   1.00 28.16 ?  491 HOH   A O    1 
HETATM 6570 O  O    . HOH   E 4 .   ? 30.747 -5.791  -11.795 1.00 45.11 ?  492 HOH   A O    1 
HETATM 6571 O  O    . HOH   E 4 .   ? 37.385 -6.687  7.484   1.00 23.16 ?  493 HOH   A O    1 
HETATM 6572 O  O    . HOH   E 4 .   ? 8.174  -3.052  -5.611  1.00 43.85 ?  494 HOH   A O    1 
HETATM 6573 O  O    . HOH   E 4 .   ? 23.137 -23.790 1.651   1.00 30.39 ?  495 HOH   A O    1 
HETATM 6574 O  O    . HOH   E 4 .   ? 39.570 -0.026  6.586   1.00 28.71 ?  496 HOH   A O    1 
HETATM 6575 O  O    . HOH   E 4 .   ? 29.007 14.445  0.943   1.00 45.05 ?  497 HOH   A O    1 
HETATM 6576 O  O    . HOH   E 4 .   ? 38.081 13.911  6.722   1.00 41.28 ?  498 HOH   A O    1 
HETATM 6577 O  O    . HOH   E 4 .   ? 14.847 8.530   5.024   1.00 40.88 ?  499 HOH   A O    1 
HETATM 6578 O  O    . HOH   E 4 .   ? 36.492 -6.537  10.140  1.00 42.19 ?  500 HOH   A O    1 
HETATM 6579 O  O    . HOH   E 4 .   ? 22.015 -24.071 4.467   1.00 24.62 ?  501 HOH   A O    1 
HETATM 6580 O  O    . HOH   E 4 .   ? 17.368 -6.675  -14.139 1.00 37.70 ?  502 HOH   A O    1 
HETATM 6581 O  O    . HOH   E 4 .   ? 24.078 8.978   -7.238  1.00 33.14 ?  503 HOH   A O    1 
HETATM 6582 O  O    . HOH   E 4 .   ? 16.425 -21.145 18.788  1.00 32.43 ?  504 HOH   A O    1 
HETATM 6583 O  O    . HOH   E 4 .   ? 15.928 -12.318 27.483  1.00 41.97 ?  505 HOH   A O    1 
HETATM 6584 O  O    . HOH   E 4 .   ? 14.640 -22.819 19.842  1.00 32.51 ?  506 HOH   A O    1 
HETATM 6585 O  O    . HOH   F 4 .   ? 29.839 -22.439 5.469   1.00 19.88 ?  201 HOH   B O    1 
HETATM 6586 O  O    . HOH   F 4 .   ? 41.831 -35.903 -17.371 1.00 27.74 ?  202 HOH   B O    1 
HETATM 6587 O  O    . HOH   F 4 .   ? 48.139 -6.905  15.564  1.00 36.24 ?  203 HOH   B O    1 
HETATM 6588 O  O    . HOH   F 4 .   ? 27.861 -41.811 -15.161 1.00 35.57 ?  204 HOH   B O    1 
HETATM 6589 O  O    . HOH   F 4 .   ? 59.212 -18.789 6.751   1.00 37.17 ?  205 HOH   B O    1 
HETATM 6590 O  O    . HOH   F 4 .   ? 47.406 -7.459  -3.980  1.00 40.08 ?  206 HOH   B O    1 
HETATM 6591 O  O    . HOH   F 4 .   ? 27.730 -29.235 -1.913  1.00 33.55 ?  207 HOH   B O    1 
HETATM 6592 O  O    . HOH   F 4 .   ? 41.409 -7.762  5.466   1.00 37.39 ?  208 HOH   B O    1 
HETATM 6593 O  O    . HOH   F 4 .   ? 37.943 -39.493 -0.262  1.00 40.75 ?  209 HOH   B O    1 
HETATM 6594 O  O    . HOH   F 4 .   ? 49.414 -22.695 -19.798 1.00 46.69 ?  210 HOH   B O    1 
HETATM 6595 O  O    . HOH   F 4 .   ? 56.350 -19.749 7.249   1.00 32.64 ?  211 HOH   B O    1 
HETATM 6596 O  O    . HOH   F 4 .   ? 54.478 -9.386  -8.764  1.00 19.20 ?  212 HOH   B O    1 
HETATM 6597 O  O    . HOH   F 4 .   ? 50.262 -3.403  7.197   1.00 33.42 ?  213 HOH   B O    1 
HETATM 6598 O  O    . HOH   F 4 .   ? 52.939 -13.413 -20.379 1.00 35.16 ?  214 HOH   B O    1 
HETATM 6599 O  O    . HOH   F 4 .   ? 30.225 -41.030 -8.181  1.00 16.32 ?  215 HOH   B O    1 
HETATM 6600 O  O    . HOH   F 4 .   ? 57.151 -26.843 -7.612  1.00 37.85 ?  216 HOH   B O    1 
HETATM 6601 O  O    . HOH   F 4 .   ? 55.372 -16.479 -14.380 1.00 34.45 ?  217 HOH   B O    1 
HETATM 6602 O  O    . HOH   F 4 .   ? 35.966 -43.240 -8.609  1.00 29.46 ?  218 HOH   B O    1 
HETATM 6603 O  O    . HOH   F 4 .   ? 29.769 -34.186 -0.449  1.00 34.05 ?  219 HOH   B O    1 
HETATM 6604 O  O    . HOH   F 4 .   ? 58.263 -12.978 8.382   1.00 32.41 ?  220 HOH   B O    1 
HETATM 6605 O  O    . HOH   F 4 .   ? 29.916 -26.354 3.989   1.00 27.81 ?  221 HOH   B O    1 
HETATM 6606 O  O    . HOH   F 4 .   ? 50.764 -6.121  0.176   1.00 26.12 ?  222 HOH   B O    1 
HETATM 6607 O  O    . HOH   F 4 .   ? 44.454 -7.269  2.106   1.00 35.24 ?  223 HOH   B O    1 
HETATM 6608 O  O    . HOH   F 4 .   ? 56.736 -30.744 -7.781  1.00 30.76 ?  224 HOH   B O    1 
HETATM 6609 O  O    . HOH   F 4 .   ? 34.562 -36.387 -7.262  1.00 17.84 ?  225 HOH   B O    1 
HETATM 6610 O  O    . HOH   F 4 .   ? 37.132 -19.773 -18.124 1.00 38.95 ?  226 HOH   B O    1 
HETATM 6611 O  O    . HOH   F 4 .   ? 57.750 -24.453 5.002   1.00 34.98 ?  227 HOH   B O    1 
HETATM 6612 O  O    . HOH   F 4 .   ? 40.606 -16.100 14.089  1.00 24.16 ?  228 HOH   B O    1 
HETATM 6613 O  O    . HOH   F 4 .   ? 45.137 -35.028 6.851   1.00 38.90 ?  229 HOH   B O    1 
HETATM 6614 O  O    . HOH   F 4 .   ? 57.405 -16.242 -12.237 1.00 19.45 ?  230 HOH   B O    1 
HETATM 6615 O  O    . HOH   F 4 .   ? 30.891 -28.820 4.267   1.00 24.43 ?  231 HOH   B O    1 
HETATM 6616 O  O    . HOH   F 4 .   ? 41.532 -39.148 -14.950 1.00 21.39 ?  232 HOH   B O    1 
HETATM 6617 O  O    . HOH   F 4 .   ? 39.335 -10.905 6.098   1.00 26.39 ?  233 HOH   B O    1 
HETATM 6618 O  O    . HOH   F 4 .   ? 41.408 -9.664  13.025  1.00 21.87 ?  234 HOH   B O    1 
HETATM 6619 O  O    . HOH   F 4 .   ? 48.544 -36.511 -15.552 1.00 42.71 ?  235 HOH   B O    1 
HETATM 6620 O  O    . HOH   F 4 .   ? 45.042 -43.508 -10.573 1.00 26.54 ?  236 HOH   B O    1 
HETATM 6621 O  O    . HOH   F 4 .   ? 28.407 -19.706 -13.120 1.00 24.49 ?  237 HOH   B O    1 
HETATM 6622 O  O    . HOH   F 4 .   ? 51.604 -13.879 10.917  1.00 28.87 ?  238 HOH   B O    1 
HETATM 6623 O  O    . HOH   F 4 .   ? 32.846 -43.801 -11.387 1.00 19.10 ?  239 HOH   B O    1 
HETATM 6624 O  O    . HOH   F 4 .   ? 51.710 -6.515  4.401   1.00 19.13 ?  240 HOH   B O    1 
HETATM 6625 O  O    . HOH   F 4 .   ? 50.746 -12.992 -0.496  1.00 12.19 ?  241 HOH   B O    1 
HETATM 6626 O  O    . HOH   F 4 .   ? 35.118 -8.008  -3.062  1.00 18.38 ?  242 HOH   B O    1 
HETATM 6627 O  O    . HOH   F 4 .   ? 34.908 -24.698 13.815  1.00 28.01 ?  243 HOH   B O    1 
HETATM 6628 O  O    . HOH   F 4 .   ? 42.584 -25.399 2.593   1.00 14.66 ?  244 HOH   B O    1 
HETATM 6629 O  O    . HOH   F 4 .   ? 43.130 -43.247 -8.247  1.00 28.57 ?  245 HOH   B O    1 
HETATM 6630 O  O    . HOH   F 4 .   ? 44.531 -27.752 -0.729  1.00 22.42 ?  246 HOH   B O    1 
HETATM 6631 O  O    . HOH   F 4 .   ? 57.621 -24.400 -3.834  1.00 21.51 ?  247 HOH   B O    1 
HETATM 6632 O  O    . HOH   F 4 .   ? 42.667 -22.895 3.816   1.00 11.85 ?  248 HOH   B O    1 
HETATM 6633 O  O    . HOH   F 4 .   ? 39.512 -11.143 0.291   1.00 16.75 ?  249 HOH   B O    1 
HETATM 6634 O  O    . HOH   F 4 .   ? 46.393 -1.591  13.279  1.00 29.26 ?  250 HOH   B O    1 
HETATM 6635 O  O    . HOH   F 4 .   ? 25.463 -26.005 -1.359  1.00 32.54 ?  251 HOH   B O    1 
HETATM 6636 O  O    . HOH   F 4 .   ? 34.204 -18.570 11.364  1.00 23.04 ?  252 HOH   B O    1 
HETATM 6637 O  O    . HOH   F 4 .   ? 27.166 -31.847 -10.002 1.00 21.83 ?  253 HOH   B O    1 
HETATM 6638 O  O    . HOH   F 4 .   ? 40.345 -12.764 -11.562 1.00 15.20 ?  254 HOH   B O    1 
HETATM 6639 O  O    . HOH   F 4 .   ? 31.799 -18.011 -14.545 1.00 31.31 ?  255 HOH   B O    1 
HETATM 6640 O  O    . HOH   F 4 .   ? 48.003 -24.470 -17.819 1.00 30.97 ?  256 HOH   B O    1 
HETATM 6641 O  O    . HOH   F 4 .   ? 30.880 -15.777 2.645   1.00 13.39 ?  257 HOH   B O    1 
HETATM 6642 O  O    . HOH   F 4 .   ? 49.774 -0.527  10.274  1.00 30.89 ?  258 HOH   B O    1 
HETATM 6643 O  O    . HOH   F 4 .   ? 29.741 -25.242 -10.853 1.00 16.02 ?  259 HOH   B O    1 
HETATM 6644 O  O    . HOH   F 4 .   ? 48.024 -22.795 5.799   1.00 16.99 ?  260 HOH   B O    1 
HETATM 6645 O  O    . HOH   F 4 .   ? 43.245 -32.387 -17.144 1.00 22.32 ?  261 HOH   B O    1 
HETATM 6646 O  O    . HOH   F 4 .   ? 33.523 -17.046 8.039   1.00 19.68 ?  262 HOH   B O    1 
HETATM 6647 O  O    . HOH   F 4 .   ? 57.163 -12.133 12.299  1.00 36.00 ?  263 HOH   B O    1 
HETATM 6648 O  O    . HOH   F 4 .   ? 38.936 -12.056 12.314  1.00 33.36 ?  264 HOH   B O    1 
HETATM 6649 O  O    . HOH   F 4 .   ? 51.016 -39.954 -8.313  1.00 29.58 ?  265 HOH   B O    1 
HETATM 6650 O  O    . HOH   F 4 .   ? 38.470 -11.075 -2.245  1.00 18.79 ?  266 HOH   B O    1 
HETATM 6651 O  O    . HOH   F 4 .   ? 57.520 -9.240  1.399   1.00 19.73 ?  267 HOH   B O    1 
HETATM 6652 O  O    . HOH   F 4 .   ? 41.905 -23.547 9.251   1.00 17.07 ?  268 HOH   B O    1 
HETATM 6653 O  O    . HOH   F 4 .   ? 58.204 -10.631 -4.097  1.00 19.98 ?  269 HOH   B O    1 
HETATM 6654 O  O    . HOH   F 4 .   ? 30.659 -42.223 -10.649 1.00 27.38 ?  270 HOH   B O    1 
HETATM 6655 O  O    . HOH   F 4 .   ? 56.964 -8.661  8.413   1.00 19.68 ?  271 HOH   B O    1 
HETATM 6656 O  O    . HOH   F 4 .   ? 28.286 -34.385 -9.506  1.00 20.47 ?  272 HOH   B O    1 
HETATM 6657 O  O    . HOH   F 4 .   ? 49.366 -28.712 -6.941  1.00 15.65 ?  273 HOH   B O    1 
HETATM 6658 O  O    . HOH   F 4 .   ? 42.396 -9.937  9.311   1.00 20.60 ?  274 HOH   B O    1 
HETATM 6659 O  O    . HOH   F 4 .   ? 34.923 -33.376 -19.241 1.00 28.45 ?  275 HOH   B O    1 
HETATM 6660 O  O    . HOH   F 4 .   ? 43.381 -15.791 -12.205 1.00 14.13 ?  276 HOH   B O    1 
HETATM 6661 O  O    . HOH   F 4 .   ? 56.198 -23.469 -14.779 1.00 26.43 ?  277 HOH   B O    1 
HETATM 6662 O  O    . HOH   F 4 .   ? 28.488 -30.881 -14.794 1.00 29.94 ?  278 HOH   B O    1 
HETATM 6663 O  O    . HOH   F 4 .   ? 46.632 -31.288 -4.824  1.00 19.84 ?  279 HOH   B O    1 
HETATM 6664 O  O    . HOH   F 4 .   ? 46.887 -29.577 9.782   1.00 30.79 ?  280 HOH   B O    1 
HETATM 6665 O  O    . HOH   F 4 .   ? 48.435 -25.064 3.085   1.00 13.26 ?  281 HOH   B O    1 
HETATM 6666 O  O    . HOH   F 4 .   ? 42.408 -34.727 3.744   1.00 25.37 ?  282 HOH   B O    1 
HETATM 6667 O  O    . HOH   F 4 .   ? 27.965 -22.911 -8.023  1.00 16.80 ?  283 HOH   B O    1 
HETATM 6668 O  O    . HOH   F 4 .   ? 42.237 -10.085 -14.962 1.00 35.77 ?  284 HOH   B O    1 
HETATM 6669 O  O    . HOH   F 4 .   ? 33.535 -15.324 -13.982 1.00 20.67 ?  285 HOH   B O    1 
HETATM 6670 O  O    . HOH   F 4 .   ? 37.398 -35.674 7.198   1.00 33.64 ?  286 HOH   B O    1 
HETATM 6671 O  O    . HOH   F 4 .   ? 45.974 -40.397 -3.678  1.00 27.72 ?  287 HOH   B O    1 
HETATM 6672 O  O    . HOH   F 4 .   ? 42.877 -20.315 -20.789 1.00 36.26 ?  288 HOH   B O    1 
HETATM 6673 O  O    . HOH   F 4 .   ? 48.740 -20.058 5.874   1.00 14.15 ?  289 HOH   B O    1 
HETATM 6674 O  O    . HOH   F 4 .   ? 27.606 -26.776 -15.685 1.00 33.15 ?  290 HOH   B O    1 
HETATM 6675 O  O    . HOH   F 4 .   ? 34.465 -12.789 2.588   1.00 23.80 ?  291 HOH   B O    1 
HETATM 6676 O  O    . HOH   F 4 .   ? 59.813 -15.354 8.144   1.00 31.76 ?  292 HOH   B O    1 
HETATM 6677 O  O    . HOH   F 4 .   ? 36.824 -12.768 -1.540  1.00 26.34 ?  293 HOH   B O    1 
HETATM 6678 O  O    . HOH   F 4 .   ? 45.396 -33.422 -15.956 1.00 23.16 ?  294 HOH   B O    1 
HETATM 6679 O  O    . HOH   F 4 .   ? 41.203 -5.498  11.507  1.00 43.56 ?  295 HOH   B O    1 
HETATM 6680 O  O    . HOH   F 4 .   ? 35.117 -33.609 4.492   1.00 26.06 ?  296 HOH   B O    1 
HETATM 6681 O  O    . HOH   F 4 .   ? 62.806 -20.212 -0.895  1.00 39.85 ?  297 HOH   B O    1 
HETATM 6682 O  O    . HOH   F 4 .   ? 40.249 -10.850 -9.556  1.00 16.60 ?  298 HOH   B O    1 
HETATM 6683 O  O    . HOH   F 4 .   ? 57.673 -22.139 3.069   1.00 25.85 ?  299 HOH   B O    1 
HETATM 6684 O  O    . HOH   F 4 .   ? 44.640 -27.480 1.964   1.00 15.20 ?  300 HOH   B O    1 
HETATM 6685 O  O    . HOH   F 4 .   ? 52.646 -35.647 -8.611  1.00 28.19 ?  301 HOH   B O    1 
HETATM 6686 O  O    . HOH   F 4 .   ? 51.279 -37.589 -9.675  1.00 24.54 ?  302 HOH   B O    1 
HETATM 6687 O  O    . HOH   F 4 .   ? 47.104 -33.997 -4.638  1.00 17.04 ?  303 HOH   B O    1 
HETATM 6688 O  O    . HOH   F 4 .   ? 52.545 -10.440 13.027  1.00 22.37 ?  304 HOH   B O    1 
HETATM 6689 O  O    . HOH   F 4 .   ? 42.753 -12.231 -18.521 1.00 29.28 ?  305 HOH   B O    1 
HETATM 6690 O  O    . HOH   F 4 .   ? 25.968 -21.514 -3.549  1.00 15.70 ?  306 HOH   B O    1 
HETATM 6691 O  O    . HOH   F 4 .   ? 44.058 -29.371 -4.702  1.00 23.66 ?  307 HOH   B O    1 
HETATM 6692 O  O    . HOH   F 4 .   ? 53.091 -16.037 -12.777 1.00 28.15 ?  308 HOH   B O    1 
HETATM 6693 O  O    . HOH   F 4 .   ? 37.569 -18.224 13.109  1.00 29.02 ?  309 HOH   B O    1 
HETATM 6694 O  O    . HOH   F 4 .   ? 32.820 -34.622 -5.933  1.00 16.72 ?  310 HOH   B O    1 
HETATM 6695 O  O    . HOH   F 4 .   ? 50.026 -24.650 5.817   1.00 34.67 ?  311 HOH   B O    1 
HETATM 6696 O  O    . HOH   F 4 .   ? 53.498 -30.223 4.491   1.00 19.03 ?  312 HOH   B O    1 
HETATM 6697 O  O    . HOH   F 4 .   ? 52.596 -29.240 -13.068 1.00 23.72 ?  313 HOH   B O    1 
HETATM 6698 O  O    . HOH   F 4 .   ? 37.838 -10.264 -10.765 1.00 16.94 ?  314 HOH   B O    1 
HETATM 6699 O  O    . HOH   F 4 .   ? 48.160 -32.639 -16.647 1.00 43.60 ?  315 HOH   B O    1 
HETATM 6700 O  O    . HOH   F 4 .   ? 41.259 -24.537 15.765  1.00 40.51 ?  316 HOH   B O    1 
HETATM 6701 O  O    . HOH   F 4 .   ? 41.740 -8.116  1.368   1.00 23.64 ?  317 HOH   B O    1 
HETATM 6702 O  O    . HOH   F 4 .   ? 43.531 -15.375 18.209  1.00 29.02 ?  318 HOH   B O    1 
HETATM 6703 O  O    . HOH   F 4 .   ? 62.692 -13.576 4.716   1.00 26.84 ?  319 HOH   B O    1 
HETATM 6704 O  O    . HOH   F 4 .   ? 43.237 -21.474 10.645  1.00 15.61 ?  320 HOH   B O    1 
HETATM 6705 O  O    . HOH   F 4 .   ? 38.357 -9.397  -13.291 1.00 28.11 ?  321 HOH   B O    1 
HETATM 6706 O  O    . HOH   F 4 .   ? 26.345 -21.059 -6.258  1.00 15.98 ?  322 HOH   B O    1 
HETATM 6707 O  O    . HOH   F 4 .   ? 38.361 -12.797 7.912   1.00 18.54 ?  323 HOH   B O    1 
HETATM 6708 O  O    . HOH   F 4 .   ? 37.205 -30.601 -21.080 1.00 30.42 ?  324 HOH   B O    1 
HETATM 6709 O  O    . HOH   F 4 .   ? 51.425 -32.932 -10.818 1.00 38.22 ?  325 HOH   B O    1 
HETATM 6710 O  O    . HOH   F 4 .   ? 44.592 -24.646 9.558   1.00 19.18 ?  326 HOH   B O    1 
HETATM 6711 O  O    . HOH   F 4 .   ? 51.748 -5.940  -7.917  1.00 46.02 ?  327 HOH   B O    1 
HETATM 6712 O  O    . HOH   F 4 .   ? 60.013 -17.159 -10.481 1.00 34.55 ?  328 HOH   B O    1 
HETATM 6713 O  O    . HOH   F 4 .   ? 36.726 -12.461 4.277   1.00 17.85 ?  329 HOH   B O    1 
HETATM 6714 O  O    . HOH   F 4 .   ? 39.491 -23.468 -20.305 1.00 34.89 ?  330 HOH   B O    1 
HETATM 6715 O  O    . HOH   F 4 .   ? 33.662 -31.170 11.078  1.00 35.81 ?  331 HOH   B O    1 
HETATM 6716 O  O    . HOH   F 4 .   ? 47.173 -24.505 8.136   1.00 26.31 ?  332 HOH   B O    1 
HETATM 6717 O  O    . HOH   F 4 .   ? 27.953 -14.819 -9.458  1.00 34.06 ?  333 HOH   B O    1 
HETATM 6718 O  O    . HOH   F 4 .   ? 53.695 -12.563 -22.307 1.00 32.83 ?  334 HOH   B O    1 
HETATM 6719 O  O    . HOH   F 4 .   ? 42.923 -43.481 -14.422 1.00 41.42 ?  335 HOH   B O    1 
HETATM 6720 O  O    . HOH   F 4 .   ? 43.144 -34.698 0.047   1.00 19.91 ?  336 HOH   B O    1 
HETATM 6721 O  O    . HOH   F 4 .   ? 45.810 -36.270 -16.119 1.00 32.53 ?  337 HOH   B O    1 
HETATM 6722 O  O    . HOH   F 4 .   ? 44.193 -1.732  7.548   1.00 44.34 ?  338 HOH   B O    1 
HETATM 6723 O  O    . HOH   F 4 .   ? 48.602 -11.918 -13.924 1.00 26.92 ?  339 HOH   B O    1 
HETATM 6724 O  O    . HOH   F 4 .   ? 47.495 -27.465 1.997   1.00 15.17 ?  340 HOH   B O    1 
HETATM 6725 O  O    . HOH   F 4 .   ? 46.864 -19.912 12.260  1.00 29.22 ?  341 HOH   B O    1 
HETATM 6726 O  O    . HOH   F 4 .   ? 37.057 -15.103 -16.531 1.00 38.73 ?  342 HOH   B O    1 
HETATM 6727 O  O    . HOH   F 4 .   ? 37.077 -45.170 -9.788  1.00 38.08 ?  343 HOH   B O    1 
HETATM 6728 O  O    . HOH   F 4 .   ? 33.022 -14.714 1.027   1.00 17.22 ?  344 HOH   B O    1 
HETATM 6729 O  O    . HOH   F 4 .   ? 28.885 -42.964 -12.337 1.00 36.09 ?  345 HOH   B O    1 
HETATM 6730 O  O    . HOH   F 4 .   ? 38.412 -12.304 -16.288 1.00 39.59 ?  346 HOH   B O    1 
HETATM 6731 O  O    . HOH   F 4 .   ? 39.840 -44.332 -11.225 1.00 37.43 ?  347 HOH   B O    1 
HETATM 6732 O  O    . HOH   F 4 .   ? 40.431 -43.461 -9.188  1.00 25.69 ?  348 HOH   B O    1 
HETATM 6733 O  O    . HOH   F 4 .   ? 27.785 -26.618 -0.635  1.00 28.84 ?  349 HOH   B O    1 
HETATM 6734 O  O    . HOH   F 4 .   ? 38.546 -22.349 15.045  1.00 39.27 ?  350 HOH   B O    1 
HETATM 6735 O  O    . HOH   F 4 .   ? 55.658 -8.281  10.797  1.00 24.34 ?  351 HOH   B O    1 
HETATM 6736 O  O    . HOH   F 4 .   ? 33.760 -9.270  -8.823  1.00 32.19 ?  352 HOH   B O    1 
HETATM 6737 O  O    . HOH   F 4 .   ? 62.551 -20.222 -4.913  1.00 43.66 ?  353 HOH   B O    1 
HETATM 6738 O  O    . HOH   F 4 .   ? 34.611 -10.362 7.516   1.00 23.91 ?  354 HOH   B O    1 
HETATM 6739 O  O    . HOH   F 4 .   ? 44.168 -37.347 -17.852 1.00 32.36 ?  355 HOH   B O    1 
HETATM 6740 O  O    . HOH   F 4 .   ? 36.113 -8.583  -9.703  1.00 34.65 ?  356 HOH   B O    1 
HETATM 6741 O  O    . HOH   F 4 .   ? 56.627 -7.332  3.132   1.00 27.63 ?  357 HOH   B O    1 
HETATM 6742 O  O    . HOH   F 4 .   ? 23.191 -23.701 6.743   1.00 32.67 ?  358 HOH   B O    1 
HETATM 6743 O  O    . HOH   F 4 .   ? 43.201 -12.693 -21.211 1.00 37.89 ?  359 HOH   B O    1 
HETATM 6744 O  O    . HOH   F 4 .   ? 61.520 -19.924 1.586   1.00 31.71 ?  360 HOH   B O    1 
HETATM 6745 O  O    . HOH   F 4 .   ? 34.150 -7.799  11.423  1.00 40.42 ?  361 HOH   B O    1 
HETATM 6746 O  O    . HOH   F 4 .   ? 40.248 -8.814  9.896   1.00 36.76 ?  362 HOH   B O    1 
HETATM 6747 O  O    . HOH   F 4 .   ? 56.969 -21.563 -16.449 1.00 39.90 ?  363 HOH   B O    1 
HETATM 6748 O  O    . HOH   F 4 .   ? 27.145 -25.974 -11.486 1.00 32.81 ?  364 HOH   B O    1 
HETATM 6749 O  O    . HOH   F 4 .   ? 54.204 -5.712  2.980   1.00 36.89 ?  365 HOH   B O    1 
HETATM 6750 O  O    . HOH   F 4 .   ? 32.527 -23.659 14.055  1.00 39.12 ?  366 HOH   B O    1 
HETATM 6751 O  O    . HOH   F 4 .   ? 36.255 -8.809  8.942   1.00 34.99 ?  367 HOH   B O    1 
HETATM 6752 O  O    . HOH   F 4 .   ? 59.016 -10.466 9.152   1.00 40.06 ?  368 HOH   B O    1 
HETATM 6753 O  O    . HOH   F 4 .   ? 39.869 -7.092  7.838   1.00 41.15 ?  369 HOH   B O    1 
HETATM 6754 O  O    . HOH   F 4 .   ? 41.824 -10.044 -17.450 1.00 54.57 ?  370 HOH   B O    1 
HETATM 6755 O  O    . HOH   F 4 .   ? 39.994 -11.408 -13.978 1.00 32.91 ?  371 HOH   B O    1 
HETATM 6756 O  O    . HOH   F 4 .   ? 48.470 -26.566 8.749   1.00 37.47 ?  372 HOH   B O    1 
HETATM 6757 O  O    . HOH   F 4 .   ? 56.090 -7.827  -0.559  1.00 34.48 ?  373 HOH   B O    1 
HETATM 6758 O  O    . HOH   F 4 .   ? 52.046 -12.968 13.340  1.00 29.94 ?  374 HOH   B O    1 
HETATM 6759 O  O    . HOH   F 4 .   ? 36.571 -22.855 13.260  1.00 24.80 ?  375 HOH   B O    1 
HETATM 6760 O  O    . HOH   F 4 .   ? 38.033 -10.599 10.074  1.00 29.04 ?  376 HOH   B O    1 
HETATM 6761 O  O    . HOH   F 4 .   ? 63.116 -12.408 6.899   1.00 37.22 ?  377 HOH   B O    1 
HETATM 6762 O  O    . HOH   F 4 .   ? 44.099 -5.625  -3.548  1.00 41.99 ?  378 HOH   B O    1 
HETATM 6763 O  O    . HOH   F 4 .   ? 41.833 -6.809  -4.832  1.00 46.87 ?  379 HOH   B O    1 
HETATM 6764 O  O    . HOH   F 4 .   ? 42.636 -17.101 -23.232 1.00 40.18 ?  380 HOH   B O    1 
HETATM 6765 O  O    . HOH   F 4 .   ? 40.106 -7.651  3.228   1.00 33.13 ?  381 HOH   B O    1 
HETATM 6766 O  O    . HOH   F 4 .   ? 39.734 -14.115 15.695  1.00 48.21 ?  382 HOH   B O    1 
HETATM 6767 O  O    . HOH   F 4 .   ? 52.850 -29.900 7.143   1.00 23.55 ?  383 HOH   B O    1 
HETATM 6768 O  O    . HOH   F 4 .   ? 60.517 -22.326 2.760   1.00 44.13 ?  384 HOH   B O    1 
HETATM 6769 O  O    . HOH   F 4 .   ? 46.845 -5.397  2.917   1.00 42.65 ?  385 HOH   B O    1 
HETATM 6770 O  O    . HOH   F 4 .   ? 35.385 -33.716 7.233   1.00 39.79 ?  386 HOH   B O    1 
HETATM 6771 O  O    . HOH   F 4 .   ? 23.921 -20.862 -7.694  1.00 26.68 ?  387 HOH   B O    1 
HETATM 6772 O  O    . HOH   F 4 .   ? 25.781 -18.916 -11.944 1.00 37.12 ?  388 HOH   B O    1 
HETATM 6773 O  O    . HOH   F 4 .   ? 40.976 -9.772  15.784  1.00 48.26 ?  389 HOH   B O    1 
HETATM 6774 O  O    . HOH   F 4 .   ? 35.351 -20.348 13.301  1.00 30.40 ?  390 HOH   B O    1 
HETATM 6775 O  O    . HOH   F 4 .   ? 40.716 -6.653  -0.874  1.00 24.66 ?  391 HOH   B O    1 
HETATM 6776 O  O    . HOH   F 4 .   ? 44.069 -31.747 -3.874  1.00 31.55 ?  392 HOH   B O    1 
HETATM 6777 O  O    . HOH   F 4 .   ? 27.910 -27.113 2.215   1.00 32.16 ?  393 HOH   B O    1 
HETATM 6778 O  O    . HOH   F 4 .   ? 26.637 -28.017 -13.544 1.00 35.01 ?  394 HOH   B O    1 
HETATM 6779 O  O    . HOH   F 4 .   ? 24.597 -20.689 -10.439 1.00 36.52 ?  395 HOH   B O    1 
HETATM 6780 O  O    . HOH   F 4 .   ? 34.450 -33.497 9.581   1.00 32.33 ?  396 HOH   B O    1 
HETATM 6781 O  O    . HOH   F 4 .   ? 50.667 -30.805 8.661   1.00 27.30 ?  397 HOH   B O    1 
HETATM 6782 O  O    . HOH   F 4 .   ? 26.876 -30.673 -12.677 1.00 28.88 ?  398 HOH   B O    1 
HETATM 6783 O  O    . HOH   F 4 .   ? 45.797 -20.235 15.186  1.00 46.34 ?  399 HOH   B O    1 
HETATM 6784 O  O    . HOH   F 4 .   ? 57.651 -6.419  -2.345  1.00 35.21 ?  400 HOH   B O    1 
HETATM 6785 O  O    . HOH   F 4 .   ? 40.853 -11.860 -22.342 1.00 41.27 ?  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   ? 0.6101 0.5956 0.6645 0.0017  -0.0200 0.0878  3   VAL   A N   
2    N  N   B VAL   A 3   ? 0.6056 0.5975 0.6271 -0.0030 -0.0155 0.0545  3   VAL   A N   
3    C  CA  A VAL   A 3   ? 0.6085 0.5938 0.6557 0.0003  -0.0186 0.0870  3   VAL   A CA  
4    C  CA  B VAL   A 3   ? 0.6037 0.5957 0.6226 -0.0038 -0.0153 0.0562  3   VAL   A CA  
5    C  C   A VAL   A 3   ? 0.5948 0.5851 0.6250 -0.0049 -0.0196 0.0859  3   VAL   A C   
6    C  C   B VAL   A 3   ? 0.5933 0.5866 0.6063 -0.0075 -0.0176 0.0680  3   VAL   A C   
7    O  O   A VAL   A 3   ? 0.5959 0.5865 0.6327 -0.0025 -0.0211 0.0887  3   VAL   A O   
8    O  O   B VAL   A 3   ? 0.5959 0.5889 0.6131 -0.0065 -0.0187 0.0678  3   VAL   A O   
9    C  CB  A VAL   A 3   ? 0.6184 0.5989 0.6695 0.0026  -0.0160 0.0880  3   VAL   A CB  
10   C  CB  B VAL   A 3   ? 0.6101 0.6010 0.6302 -0.0015 -0.0130 0.0482  3   VAL   A CB  
11   C  CG1 A VAL   A 3   ? 0.6221 0.6006 0.6728 0.0036  -0.0155 0.0875  3   VAL   A CG1 
12   C  CG1 B VAL   A 3   ? 0.6123 0.6028 0.6320 -0.0008 -0.0122 0.0452  3   VAL   A CG1 
13   C  CG2 A VAL   A 3   ? 0.6216 0.6006 0.6725 0.0031  -0.0148 0.0901  3   VAL   A CG2 
14   C  CG2 B VAL   A 3   ? 0.6121 0.6028 0.6320 -0.0008 -0.0121 0.0458  3   VAL   A CG2 
31   N  N   . ASN   A 4   ? 0.5778 0.5735 0.5775 -0.0127 -0.0186 0.0809  4   ASN   A N   
32   C  CA  . ASN   A 4   ? 0.5433 0.5459 0.4940 -0.0267 -0.0172 0.0871  4   ASN   A CA  
33   C  C   . ASN   A 4   ? 0.5011 0.5162 0.4426 -0.0398 -0.0025 0.0665  4   ASN   A C   
34   O  O   . ASN   A 4   ? 0.5012 0.5156 0.4312 -0.0422 -0.0040 0.0729  4   ASN   A O   
35   C  CB  . ASN   A 4   ? 0.5486 0.5473 0.4574 -0.0276 -0.0298 0.1115  4   ASN   A CB  
36   C  CG  . ASN   A 4   ? 0.5522 0.5462 0.4229 -0.0295 -0.0417 0.1354  4   ASN   A CG  
37   O  OD1 . ASN   A 4   ? 0.5548 0.5450 0.4121 -0.0308 -0.0481 0.1425  4   ASN   A OD1 
38   N  ND2 . ASN   A 4   ? 0.5515 0.5445 0.4101 -0.0292 -0.0444 0.1491  4   ASN   A ND2 
46   N  N   . SER   A 5   ? 0.4566 0.4830 0.3998 -0.0512 0.0131  0.0403  5   SER   A N   
47   C  CA  . SER   A 5   ? 0.4113 0.4511 0.3631 -0.0601 0.0298  0.0108  5   SER   A CA  
48   C  C   . SER   A 5   ? 0.3633 0.4104 0.3185 -0.0594 0.0404  -0.0140 5   SER   A C   
49   O  O   . SER   A 5   ? 0.3671 0.4185 0.3102 -0.0473 0.0438  -0.0322 5   SER   A O   
50   C  CB  . SER   A 5   ? 0.4149 0.4589 0.3760 -0.0688 0.0361  0.0070  5   SER   A CB  
51   O  OG  . SER   A 5   ? 0.4167 0.4630 0.3807 -0.0733 0.0418  0.0059  5   SER   A OG  
57   N  N   . PHE   A 6   ? 0.3071 0.3588 0.2790 -0.0687 0.0557  -0.0155 6   PHE   A N   
58   C  CA  . PHE   A 6   ? 0.2610 0.3089 0.2442 -0.0738 0.0628  0.0015  6   PHE   A CA  
59   C  C   . PHE   A 6   ? 0.2513 0.3010 0.2634 -0.0801 0.0745  0.0023  6   PHE   A C   
60   O  O   . PHE   A 6   ? 0.2571 0.3112 0.2940 -0.0868 0.0665  0.0161  6   PHE   A O   
61   C  CB  . PHE   A 6   ? 0.2388 0.2776 0.2240 -0.0589 0.0512  0.0082  6   PHE   A CB  
62   C  CG  . PHE   A 6   ? 0.2238 0.2544 0.2085 -0.0511 0.0402  0.0150  6   PHE   A CG  
63   C  CD1 . PHE   A 6   ? 0.2157 0.2458 0.2108 -0.0465 0.0327  0.0201  6   PHE   A CD1 
64   C  CD2 . PHE   A 6   ? 0.2300 0.2469 0.2142 -0.0360 0.0366  0.0137  6   PHE   A CD2 
65   C  CE1 . PHE   A 6   ? 0.2172 0.2405 0.2169 -0.0415 0.0354  0.0240  6   PHE   A CE1 
66   C  CE2 . PHE   A 6   ? 0.2293 0.2441 0.2271 -0.0282 0.0333  0.0073  6   PHE   A CE2 
67   C  CZ  . PHE   A 6   ? 0.2256 0.2411 0.2199 -0.0348 0.0292  0.0097  6   PHE   A CZ  
77   N  N   A SER   A 7   ? 0.2463 0.2893 0.2658 -0.0786 0.0874  -0.0041 7   SER   A N   
78   N  N   B SER   A 7   ? 0.2445 0.2906 0.2568 -0.0762 0.0695  -0.0035 7   SER   A N   
79   C  CA  A SER   A 7   ? 0.2549 0.2913 0.2862 -0.0680 0.0855  -0.0162 7   SER   A CA  
80   C  CA  B SER   A 7   ? 0.2410 0.2815 0.2535 -0.0702 0.0631  -0.0077 7   SER   A CA  
81   C  C   A SER   A 7   ? 0.2362 0.2603 0.2823 -0.0650 0.0965  -0.0162 7   SER   A C   
82   C  C   B SER   A 7   ? 0.2318 0.2660 0.2407 -0.0634 0.0644  -0.0033 7   SER   A C   
83   O  O   A SER   A 7   ? 0.2482 0.2488 0.2834 -0.0636 0.1014  -0.0180 7   SER   A O   
84   O  O   B SER   A 7   ? 0.2333 0.2652 0.2387 -0.0645 0.0701  0.0005  7   SER   A O   
85   C  CB  A SER   A 7   ? 0.2793 0.3187 0.3121 -0.0549 0.0811  -0.0163 7   SER   A CB  
86   C  CB  B SER   A 7   ? 0.2452 0.2858 0.2568 -0.0708 0.0604  -0.0113 7   SER   A CB  
87   O  OG  A SER   A 7   ? 0.2967 0.3309 0.3451 -0.0485 0.0763  -0.0155 7   SER   A OG  
88   O  OG  B SER   A 7   ? 0.2464 0.2862 0.2605 -0.0725 0.0595  -0.0129 7   SER   A OG  
99   N  N   A GLY   A 8   ? 0.2165 0.2434 0.2841 -0.0607 0.0858  -0.0203 8   GLY   A N   
100  N  N   B GLY   A 8   ? 0.2216 0.2523 0.2289 -0.0552 0.0611  -0.0033 8   GLY   A N   
101  C  CA  A GLY   A 8   ? 0.2049 0.2283 0.2935 -0.0414 0.0759  -0.0147 8   GLY   A CA  
102  C  CA  B GLY   A 8   ? 0.2120 0.2380 0.2194 -0.0461 0.0518  -0.0006 8   GLY   A CA  
103  C  C   A GLY   A 8   ? 0.1863 0.2143 0.2791 -0.0330 0.0588  -0.0104 8   GLY   A C   
104  C  C   B GLY   A 8   ? 0.1994 0.2237 0.2052 -0.0402 0.0428  0.0043  8   GLY   A C   
105  O  O   A GLY   A 8   ? 0.1907 0.2146 0.2959 -0.0149 0.0522  -0.0219 8   GLY   A O   
106  O  O   B GLY   A 8   ? 0.2015 0.2233 0.2096 -0.0384 0.0451  0.0044  8   GLY   A O   
113  N  N   A TYR   A 9   ? 0.1699 0.1988 0.2581 -0.0284 0.0490  0.0024  9   TYR   A N   
114  N  N   B TYR   A 9   ? 0.1852 0.2096 0.1971 -0.0341 0.0295  0.0110  9   TYR   A N   
115  C  CA  A TYR   A 9   ? 0.1573 0.1831 0.2272 -0.0307 0.0376  0.0055  9   TYR   A CA  
116  C  CA  B TYR   A 9   ? 0.1720 0.1942 0.1897 -0.0286 0.0188  0.0182  9   TYR   A CA  
117  C  C   A TYR   A 9   ? 0.1551 0.1721 0.2264 -0.0220 0.0382  0.0276  9   TYR   A C   
118  C  C   B TYR   A 9   ? 0.1630 0.1831 0.1845 -0.0244 0.0108  0.0281  9   TYR   A C   
119  O  O   A TYR   A 9   ? 0.1728 0.1944 0.2506 -0.0299 0.0304  0.0337  9   TYR   A O   
120  O  O   B TYR   A 9   ? 0.1610 0.1872 0.1864 -0.0225 0.0028  0.0350  9   TYR   A O   
121  C  CB  A TYR   A 9   ? 0.1530 0.1887 0.2284 -0.0237 0.0331  -0.0049 9   TYR   A CB  
122  C  CB  B TYR   A 9   ? 0.1653 0.1914 0.1889 -0.0261 0.0146  0.0134  9   TYR   A CB  
123  C  CG  A TYR   A 9   ? 0.1516 0.1875 0.2239 -0.0121 0.0393  -0.0124 9   TYR   A CG  
124  C  CG  B TYR   A 9   ? 0.1578 0.1876 0.1816 -0.0236 0.0169  0.0126  9   TYR   A CG  
125  C  CD1 A TYR   A 9   ? 0.1542 0.1916 0.2358 -0.0193 0.0414  -0.0144 9   TYR   A CD1 
126  C  CD1 B TYR   A 9   ? 0.1542 0.1864 0.1817 -0.0260 0.0198  0.0124  9   TYR   A CD1 
127  C  CD2 A TYR   A 9   ? 0.1501 0.1787 0.2248 -0.0052 0.0342  0.0044  9   TYR   A CD2 
128  C  CD2 B TYR   A 9   ? 0.1541 0.1845 0.1747 -0.0196 0.0170  0.0163  9   TYR   A CD2 
129  C  CE1 A TYR   A 9   ? 0.1589 0.1938 0.2454 -0.0174 0.0492  -0.0186 9   TYR   A CE1 
130  C  CE1 B TYR   A 9   ? 0.1514 0.1822 0.1819 -0.0242 0.0237  0.0116  9   TYR   A CE1 
131  C  CE2 A TYR   A 9   ? 0.1524 0.1847 0.2353 -0.0063 0.0468  -0.0019 9   TYR   A CE2 
132  C  CE2 B TYR   A 9   ? 0.1503 0.1836 0.1756 -0.0176 0.0243  0.0166  9   TYR   A CE2 
133  C  CZ  A TYR   A 9   ? 0.1563 0.1910 0.2499 -0.0215 0.0562  -0.0057 9   TYR   A CZ  
134  C  CZ  B TYR   A 9   ? 0.1456 0.1803 0.1789 -0.0177 0.0308  0.0164  9   TYR   A CZ  
135  O  OH  A TYR   A 9   ? 0.1695 0.1980 0.2641 -0.0281 0.0547  -0.0058 9   TYR   A OH  
136  O  OH  B TYR   A 9   ? 0.1354 0.1785 0.1771 -0.0146 0.0400  0.0222  9   TYR   A OH  
155  N  N   A LEU   A 10  ? 0.1456 0.1576 0.2309 -0.0166 0.0277  0.0286  10  LEU   A N   
156  N  N   B LEU   A 10  ? 0.1564 0.1705 0.1740 -0.0212 0.0061  0.0316  10  LEU   A N   
157  C  CA  A LEU   A 10  ? 0.1480 0.1584 0.2281 -0.0197 0.0221  0.0344  10  LEU   A CA  
158  C  CA  B LEU   A 10  ? 0.1492 0.1629 0.1653 -0.0236 0.0028  0.0342  10  LEU   A CA  
159  C  C   A LEU   A 10  ? 0.1461 0.1516 0.2193 -0.0166 0.0197  0.0435  10  LEU   A C   
160  C  C   B LEU   A 10  ? 0.1485 0.1587 0.1612 -0.0253 -0.0026 0.0291  10  LEU   A C   
161  O  O   A LEU   A 10  ? 0.1443 0.1447 0.2407 -0.0134 0.0407  0.0481  10  LEU   A O   
162  O  O   B LEU   A 10  ? 0.1503 0.1578 0.1700 -0.0270 -0.0016 0.0334  10  LEU   A O   
163  C  CB  A LEU   A 10  ? 0.1636 0.1669 0.2475 -0.0166 0.0133  0.0479  10  LEU   A CB  
164  C  CB  B LEU   A 10  ? 0.1422 0.1551 0.1558 -0.0286 -0.0056 0.0517  10  LEU   A CB  
165  C  CG  A LEU   A 10  ? 0.1891 0.1918 0.2885 -0.0117 -0.0136 0.0470  10  LEU   A CG  
166  C  CG  B LEU   A 10  ? 0.1360 0.1530 0.1417 -0.0323 -0.0226 0.0663  10  LEU   A CG  
167  C  CD1 A LEU   A 10  ? 0.2053 0.2057 0.3163 -0.0215 -0.0109 0.0478  10  LEU   A CD1 
168  C  CD1 B LEU   A 10  ? 0.1338 0.1617 0.1405 -0.0324 -0.0276 0.0673  10  LEU   A CD1 
169  C  CD2 A LEU   A 10  ? 0.2119 0.2099 0.3163 -0.0056 -0.0135 0.0341  10  LEU   A CD2 
170  C  CD2 B LEU   A 10  ? 0.1377 0.1478 0.1313 -0.0339 -0.0346 0.0787  10  LEU   A CD2 
193  N  N   A LYS   A 11  ? 0.1491 0.1528 0.1940 -0.0213 0.0147  0.0372  11  LYS   A N   
194  N  N   B LYS   A 11  ? 0.1463 0.1550 0.1500 -0.0278 -0.0043 0.0214  11  LYS   A N   
195  C  CA  A LYS   A 11  ? 0.1489 0.1548 0.1981 -0.0190 0.0130  0.0371  11  LYS   A CA  
196  C  CA  B LYS   A 11  ? 0.1455 0.1494 0.1472 -0.0253 -0.0006 0.0175  11  LYS   A CA  
197  C  C   A LYS   A 11  ? 0.1415 0.1539 0.1983 -0.0208 0.0176  0.0344  11  LYS   A C   
198  C  C   B LYS   A 11  ? 0.1368 0.1406 0.1407 -0.0211 0.0055  0.0094  11  LYS   A C   
199  O  O   A LYS   A 11  ? 0.1482 0.1838 0.2320 -0.0507 0.0285  0.0170  11  LYS   A O   
200  O  O   B LYS   A 11  ? 0.1286 0.1308 0.1396 -0.0181 0.0087  -0.0079 11  LYS   A O   
201  C  CB  A LYS   A 11  ? 0.1533 0.1492 0.1891 -0.0209 0.0155  0.0310  11  LYS   A CB  
202  C  CB  B LYS   A 11  ? 0.1549 0.1465 0.1499 -0.0274 -0.0036 0.0160  11  LYS   A CB  
203  C  CG  A LYS   A 11  ? 0.1623 0.1463 0.1915 -0.0166 0.0227  0.0266  11  LYS   A CG  
204  C  CG  B LYS   A 11  ? 0.1627 0.1458 0.1522 -0.0247 -0.0018 0.0161  11  LYS   A CG  
205  C  CD  A LYS   A 11  ? 0.1744 0.1501 0.1949 -0.0153 0.0120  0.0312  11  LYS   A CD  
206  C  CD  B LYS   A 11  ? 0.1682 0.1472 0.1543 -0.0213 -0.0021 0.0190  11  LYS   A CD  
207  C  CE  A LYS   A 11  ? 0.1853 0.1477 0.1963 -0.0115 0.0010  0.0384  11  LYS   A CE  
208  C  CE  B LYS   A 11  ? 0.1712 0.1460 0.1527 -0.0198 -0.0024 0.0205  11  LYS   A CE  
209  N  NZ  A LYS   A 11  ? 0.1814 0.1432 0.1992 -0.0026 -0.0069 0.0336  11  LYS   A NZ  
210  N  NZ  B LYS   A 11  ? 0.1696 0.1443 0.1456 -0.0170 -0.0038 0.0209  11  LYS   A NZ  
237  N  N   A LEU   A 12  ? 0.1327 0.1444 0.1906 -0.0217 0.0155  0.0305  12  LEU   A N   
238  N  N   B LEU   A 12  ? 0.1344 0.1512 0.1469 -0.0126 0.0098  0.0091  12  LEU   A N   
239  C  CA  A LEU   A 12  ? 0.1297 0.1547 0.2009 -0.0220 0.0067  0.0387  12  LEU   A CA  
240  C  CA  B LEU   A 12  ? 0.1350 0.1613 0.1512 -0.0049 0.0195  0.0104  12  LEU   A CA  
241  C  C   A LEU   A 12  ? 0.1365 0.1488 0.1973 -0.0266 0.0150  0.0387  12  LEU   A C   
242  C  C   B LEU   A 12  ? 0.1379 0.1614 0.1513 -0.0009 0.0231  0.0084  12  LEU   A C   
243  O  O   A LEU   A 12  ? 0.1384 0.1526 0.1975 -0.0209 0.0163  0.0273  12  LEU   A O   
244  O  O   B LEU   A 12  ? 0.1401 0.1587 0.1479 0.0033  0.0223  0.0047  12  LEU   A O   
245  C  CB  A LEU   A 12  ? 0.1409 0.1557 0.2154 -0.0161 -0.0055 0.0522  12  LEU   A CB  
246  C  CB  B LEU   A 12  ? 0.1367 0.1699 0.1582 -0.0014 0.0278  0.0142  12  LEU   A CB  
247  C  CG  A LEU   A 12  ? 0.1476 0.1653 0.2383 -0.0120 0.0022  0.0544  12  LEU   A CG  
248  C  CG  B LEU   A 12  ? 0.1386 0.1752 0.1702 0.0007  0.0385  0.0158  12  LEU   A CG  
249  C  CD1 A LEU   A 12  ? 0.1656 0.1752 0.2484 -0.0012 0.0169  0.0646  12  LEU   A CD1 
250  C  CD1 B LEU   A 12  ? 0.1391 0.1785 0.1695 0.0039  0.0487  0.0142  12  LEU   A CD1 
251  C  CD2 A LEU   A 12  ? 0.1494 0.1774 0.2566 -0.0072 -0.0114 0.0428  12  LEU   A CD2 
252  C  CD2 B LEU   A 12  ? 0.1412 0.1798 0.1836 0.0007  0.0326  0.0162  12  LEU   A CD2 
275  N  N   A THR   A 13  ? 0.1323 0.1413 0.2030 -0.0241 0.0108  0.0305  13  THR   A N   
276  N  N   B THR   A 13  ? 0.1393 0.1598 0.1592 0.0016  0.0226  0.0091  13  THR   A N   
277  C  CA  A THR   A 13  ? 0.1375 0.1438 0.2099 -0.0198 0.0070  0.0265  13  THR   A CA  
278  C  CA  B THR   A 13  ? 0.1410 0.1625 0.1627 -0.0003 0.0242  0.0155  13  THR   A CA  
279  C  C   A THR   A 13  ? 0.1359 0.1407 0.2132 -0.0252 0.0114  0.0318  13  THR   A C   
280  C  C   B THR   A 13  ? 0.1443 0.1634 0.1722 -0.0077 0.0201  0.0139  13  THR   A C   
281  O  O   A THR   A 13  ? 0.1413 0.1370 0.2167 -0.0190 0.0120  0.0338  13  THR   A O   
282  O  O   B THR   A 13  ? 0.1470 0.1640 0.1771 -0.0101 0.0187  0.0142  13  THR   A O   
283  C  CB  A THR   A 13  ? 0.1442 0.1565 0.2216 -0.0211 0.0101  0.0336  13  THR   A CB  
284  C  CB  B THR   A 13  ? 0.1386 0.1715 0.1659 0.0063  0.0306  0.0212  13  THR   A CB  
285  O  OG1 A THR   A 13  ? 0.1345 0.1486 0.2230 -0.0197 -0.0019 0.0456  13  THR   A OG1 
286  O  OG1 B THR   A 13  ? 0.1312 0.1749 0.1704 0.0068  0.0443  0.0290  13  THR   A OG1 
287  C  CG2 A THR   A 13  ? 0.1512 0.1811 0.2428 -0.0204 0.0160  0.0220  13  THR   A CG2 
288  C  CG2 B THR   A 13  ? 0.1414 0.1778 0.1681 0.0114  0.0290  0.0212  13  THR   A CG2 
303  N  N   A ASP   A 14  ? 0.1412 0.1480 0.2199 -0.0215 0.0049  0.0409  14  ASP   A N   
304  N  N   B ASP   A 14  ? 0.1464 0.1619 0.1817 -0.0106 0.0124  0.0164  14  ASP   A N   
305  C  CA  A ASP   A 14  ? 0.1393 0.1516 0.2234 -0.0142 0.0033  0.0477  14  ASP   A CA  
306  C  CA  B ASP   A 14  ? 0.1504 0.1604 0.1896 -0.0122 0.0067  0.0231  14  ASP   A CA  
307  C  C   A ASP   A 14  ? 0.1441 0.1536 0.2057 -0.0178 -0.0019 0.0432  14  ASP   A C   
308  C  C   B ASP   A 14  ? 0.1450 0.1537 0.1889 -0.0211 0.0052  0.0336  14  ASP   A C   
309  O  O   A ASP   A 14  ? 0.1632 0.1670 0.2206 -0.0260 -0.0108 0.0463  14  ASP   A O   
310  O  O   B ASP   A 14  ? 0.1473 0.1575 0.1918 -0.0306 0.0005  0.0385  14  ASP   A O   
311  C  CB  A ASP   A 14  ? 0.1634 0.1787 0.2800 -0.0167 0.0060  0.0700  14  ASP   A CB  
312  C  CB  B ASP   A 14  ? 0.1639 0.1680 0.2082 -0.0028 -0.0010 0.0236  14  ASP   A CB  
313  C  CG  A ASP   A 14  ? 0.1882 0.2269 0.3558 -0.0208 0.0077  0.0686  14  ASP   A CG  
314  C  CG  B ASP   A 14  ? 0.1706 0.1818 0.2267 0.0044  -0.0104 0.0258  14  ASP   A CG  
315  O  OD1 A ASP   A 14  ? 0.2097 0.2444 0.3806 -0.0104 -0.0012 0.0689  14  ASP   A OD1 
316  O  OD1 B ASP   A 14  ? 0.1765 0.1860 0.2271 0.0143  -0.0206 0.0322  14  ASP   A OD1 
317  O  OD2 A ASP   A 14  ? 0.2113 0.2715 0.3957 -0.0083 -0.0041 0.0522  14  ASP   A OD2 
318  O  OD2 B ASP   A 14  ? 0.1752 0.1941 0.2361 0.0060  -0.0202 0.0239  14  ASP   A OD2 
327  N  N   . ASN   A 15  ? 0.1414 0.1453 0.1979 -0.0237 0.0113  0.0408  15  ASN   A N   
328  C  CA  . ASN   A 15  ? 0.1411 0.1477 0.2218 -0.0226 -0.0013 0.0323  15  ASN   A CA  
329  C  C   . ASN   A 15  ? 0.1382 0.1461 0.2323 -0.0218 0.0037  0.0327  15  ASN   A C   
330  O  O   . ASN   A 15  ? 0.1437 0.1473 0.2853 -0.0225 -0.0116 0.0312  15  ASN   A O   
331  C  CB  . ASN   A 15  ? 0.1373 0.1454 0.2219 -0.0175 -0.0038 0.0297  15  ASN   A CB  
332  C  CG  . ASN   A 15  ? 0.1388 0.1562 0.2204 -0.0105 0.0013  0.0200  15  ASN   A CG  
333  O  OD1 . ASN   A 15  ? 0.1496 0.1612 0.2366 -0.0201 0.0098  0.0210  15  ASN   A OD1 
334  N  ND2 . ASN   A 15  ? 0.1404 0.1695 0.2110 -0.0184 0.0066  0.0217  15  ASN   A ND2 
342  N  N   A VAL   A 16  ? 0.1384 0.1398 0.2159 -0.0181 0.0054  0.0406  16  VAL   A N   
343  N  N   B VAL   A 16  ? 0.1435 0.1491 0.2038 -0.0190 0.0033  0.0335  16  VAL   A N   
344  C  CA  A VAL   A 16  ? 0.1359 0.1446 0.2155 -0.0162 0.0113  0.0352  16  VAL   A CA  
345  C  CA  B VAL   A 16  ? 0.1487 0.1536 0.1768 -0.0174 0.0060  0.0295  16  VAL   A CA  
346  C  C   A VAL   A 16  ? 0.1284 0.1431 0.2030 -0.0153 0.0079  0.0397  16  VAL   A C   
347  C  C   B VAL   A 16  ? 0.1510 0.1584 0.1560 -0.0205 0.0042  0.0297  16  VAL   A C   
348  O  O   A VAL   A 16  ? 0.1201 0.1393 0.1945 -0.0149 0.0114  0.0282  16  VAL   A O   
349  O  O   B VAL   A 16  ? 0.1543 0.1614 0.1451 -0.0177 0.0053  0.0293  16  VAL   A O   
350  C  CB  A VAL   A 16  ? 0.1471 0.1605 0.2118 -0.0010 0.0289  0.0514  16  VAL   A CB  
351  C  CB  B VAL   A 16  ? 0.1525 0.1544 0.1679 -0.0105 0.0118  0.0276  16  VAL   A CB  
352  C  CG1 A VAL   A 16  ? 0.1610 0.1704 0.2191 0.0085  0.0311  0.0431  16  VAL   A CG1 
353  C  CG1 B VAL   A 16  ? 0.1567 0.1540 0.1670 -0.0064 0.0107  0.0233  16  VAL   A CG1 
354  C  CG2 A VAL   A 16  ? 0.1545 0.1784 0.2354 0.0045  0.0432  0.0489  16  VAL   A CG2 
355  C  CG2 B VAL   A 16  ? 0.1542 0.1595 0.1749 -0.0095 0.0161  0.0273  16  VAL   A CG2 
374  N  N   A TYR   A 17  ? 0.1239 0.1351 0.2169 -0.0083 0.0170  0.0360  17  TYR   A N   
375  N  N   B TYR   A 17  ? 0.1485 0.1578 0.1570 -0.0259 0.0040  0.0230  17  TYR   A N   
376  C  CA  A TYR   A 17  ? 0.1317 0.1393 0.2157 -0.0108 0.0165  0.0376  17  TYR   A CA  
377  C  CA  B TYR   A 17  ? 0.1468 0.1572 0.1575 -0.0312 0.0040  0.0204  17  TYR   A CA  
378  C  C   A TYR   A 17  ? 0.1331 0.1344 0.2307 -0.0110 0.0184  0.0323  17  TYR   A C   
379  C  C   B TYR   A 17  ? 0.1476 0.1609 0.1623 -0.0289 0.0103  0.0204  17  TYR   A C   
380  O  O   A TYR   A 17  ? 0.1243 0.1303 0.2246 -0.0116 0.0246  0.0325  17  TYR   A O   
381  O  O   B TYR   A 17  ? 0.1424 0.1601 0.1553 -0.0340 0.0084  0.0209  17  TYR   A O   
382  C  CB  A TYR   A 17  ? 0.1462 0.1452 0.2157 -0.0130 0.0124  0.0339  17  TYR   A CB  
383  C  CB  B TYR   A 17  ? 0.1482 0.1526 0.1559 -0.0356 -0.0019 0.0172  17  TYR   A CB  
384  C  CG  A TYR   A 17  ? 0.1578 0.1550 0.2129 -0.0160 0.0072  0.0278  17  TYR   A CG  
385  C  CG  B TYR   A 17  ? 0.1481 0.1491 0.1509 -0.0359 -0.0086 0.0134  17  TYR   A CG  
386  C  CD1 A TYR   A 17  ? 0.1690 0.1651 0.2235 -0.0077 0.0079  0.0254  17  TYR   A CD1 
387  C  CD1 B TYR   A 17  ? 0.1470 0.1486 0.1521 -0.0351 -0.0024 0.0169  17  TYR   A CD1 
388  C  CD2 A TYR   A 17  ? 0.1657 0.1607 0.2057 -0.0186 0.0058  0.0268  17  TYR   A CD2 
389  C  CD2 B TYR   A 17  ? 0.1494 0.1474 0.1444 -0.0383 -0.0126 0.0119  17  TYR   A CD2 
390  C  CE1 A TYR   A 17  ? 0.1801 0.1661 0.2239 -0.0110 -0.0035 0.0245  17  TYR   A CE1 
391  C  CE1 B TYR   A 17  ? 0.1436 0.1447 0.1534 -0.0360 -0.0094 0.0174  17  TYR   A CE1 
392  C  CE2 A TYR   A 17  ? 0.1802 0.1579 0.2016 -0.0170 0.0027  0.0235  17  TYR   A CE2 
393  C  CE2 B TYR   A 17  ? 0.1465 0.1422 0.1400 -0.0397 -0.0161 0.0122  17  TYR   A CE2 
394  C  CZ  A TYR   A 17  ? 0.1846 0.1581 0.2082 -0.0120 -0.0096 0.0325  17  TYR   A CZ  
395  C  CZ  B TYR   A 17  ? 0.1464 0.1403 0.1463 -0.0374 -0.0125 0.0185  17  TYR   A CZ  
396  O  OH  A TYR   A 17  ? 0.1936 0.1628 0.2183 -0.0090 0.0018  0.0339  17  TYR   A OH  
397  O  OH  B TYR   A 17  ? 0.1510 0.1368 0.1527 -0.0310 -0.0208 0.0207  17  TYR   A OH  
416  N  N   A ILE   A 18  ? 0.1351 0.1419 0.2303 -0.0124 0.0230  0.0452  18  ILE   A N   
417  N  N   B ILE   A 18  ? 0.1509 0.1640 0.1687 -0.0208 0.0193  0.0242  18  ILE   A N   
418  C  CA  A ILE   A 18  ? 0.1393 0.1465 0.2432 -0.0098 0.0270  0.0460  18  ILE   A CA  
419  C  CA  B ILE   A 18  ? 0.1560 0.1676 0.1803 -0.0150 0.0277  0.0211  18  ILE   A CA  
420  C  C   A ILE   A 18  ? 0.1400 0.1554 0.2587 -0.0155 0.0303  0.0410  18  ILE   A C   
421  C  C   B ILE   A 18  ? 0.1669 0.1737 0.1893 -0.0124 0.0278  0.0166  18  ILE   A C   
422  O  O   A ILE   A 18  ? 0.1395 0.1681 0.2683 -0.0208 0.0419  0.0496  18  ILE   A O   
423  O  O   B ILE   A 18  ? 0.1687 0.1762 0.1892 -0.0141 0.0285  0.0186  18  ILE   A O   
424  C  CB  A ILE   A 18  ? 0.1493 0.1568 0.2297 -0.0033 0.0154  0.0697  18  ILE   A CB  
425  C  CB  B ILE   A 18  ? 0.1518 0.1701 0.1816 -0.0127 0.0325  0.0245  18  ILE   A CB  
426  C  CG1 A ILE   A 18  ? 0.1597 0.1636 0.2360 0.0033  0.0070  0.0801  18  ILE   A CG1 
427  C  CG1 B ILE   A 18  ? 0.1511 0.1756 0.1862 -0.0144 0.0337  0.0239  18  ILE   A CG1 
428  C  CG2 A ILE   A 18  ? 0.1553 0.1658 0.2439 -0.0082 0.0070  0.0664  18  ILE   A CG2 
429  C  CG2 B ILE   A 18  ? 0.1531 0.1713 0.1874 -0.0150 0.0314  0.0266  18  ILE   A CG2 
430  C  CD1 A ILE   A 18  ? 0.1722 0.1769 0.2553 0.0099  0.0054  0.0791  18  ILE   A CD1 
431  C  CD1 B ILE   A 18  ? 0.1527 0.1825 0.1953 -0.0098 0.0355  0.0164  18  ILE   A CD1 
454  N  N   A LYS   A 19  ? 0.1447 0.1537 0.2774 -0.0105 0.0472  0.0384  19  LYS   A N   
455  N  N   B LYS   A 19  ? 0.1749 0.1774 0.2032 -0.0069 0.0304  0.0122  19  LYS   A N   
456  C  CA  A LYS   A 19  ? 0.1521 0.1609 0.2937 -0.0042 0.0561  0.0479  19  LYS   A CA  
457  C  CA  B LYS   A 19  ? 0.1825 0.1825 0.2129 -0.0019 0.0266  0.0105  19  LYS   A CA  
458  C  C   A LYS   A 19  ? 0.1435 0.1538 0.3194 0.0045  0.0517  0.0422  19  LYS   A C   
459  C  C   B LYS   A 19  ? 0.1852 0.1810 0.2221 -0.0044 0.0238  0.0167  19  LYS   A C   
460  O  O   A LYS   A 19  ? 0.1341 0.1480 0.3145 0.0003  0.0319  0.0480  19  LYS   A O   
461  O  O   B LYS   A 19  ? 0.1874 0.1816 0.2264 -0.0053 0.0180  0.0168  19  LYS   A O   
462  C  CB  A LYS   A 19  ? 0.1592 0.1833 0.2949 -0.0035 0.0654  0.0336  19  LYS   A CB  
463  C  CB  B LYS   A 19  ? 0.1855 0.1895 0.2151 0.0033  0.0254  0.0003  19  LYS   A CB  
464  C  CG  A LYS   A 19  ? 0.1947 0.2073 0.3008 0.0021  0.0582  0.0239  19  LYS   A CG  
465  C  CG  B LYS   A 19  ? 0.1867 0.1963 0.2153 0.0055  0.0192  -0.0071 19  LYS   A CG  
466  C  CD  A LYS   A 19  ? 0.2226 0.2276 0.3011 0.0061  0.0559  0.0232  19  LYS   A CD  
467  C  CD  B LYS   A 19  ? 0.1870 0.2025 0.2130 0.0077  0.0129  -0.0117 19  LYS   A CD  
468  C  CE  A LYS   A 19  ? 0.2399 0.2330 0.3039 0.0060  0.0490  0.0168  19  LYS   A CE  
469  C  CE  B LYS   A 19  ? 0.1882 0.2061 0.2114 0.0074  0.0082  -0.0119 19  LYS   A CE  
470  N  NZ  A LYS   A 19  ? 0.2481 0.2357 0.2972 -0.0033 0.0599  0.0075  19  LYS   A NZ  
471  N  NZ  B LYS   A 19  ? 0.1849 0.2071 0.2028 0.0086  0.0058  -0.0142 19  LYS   A NZ  
498  N  N   A ASN   A 20  ? 0.1535 0.1593 0.3516 0.0035  0.0518  0.0409  20  ASN   A N   
499  N  N   B ASN   A 20  ? 0.1866 0.1790 0.2266 -0.0085 0.0235  0.0238  20  ASN   A N   
500  C  CA  A ASN   A 20  ? 0.1639 0.1839 0.3702 0.0272  0.0587  0.0347  20  ASN   A CA  
501  C  CA  B ASN   A 20  ? 0.1881 0.1806 0.2306 -0.0046 0.0252  0.0228  20  ASN   A CA  
502  C  C   A ASN   A 20  ? 0.1894 0.1831 0.3660 0.0196  0.0645  0.0229  20  ASN   A C   
503  C  C   B ASN   A 20  ? 0.1945 0.1835 0.2337 -0.0065 0.0328  0.0198  20  ASN   A C   
504  O  O   A ASN   A 20  ? 0.2148 0.1970 0.3752 -0.0056 0.0653  0.0125  20  ASN   A O   
505  O  O   B ASN   A 20  ? 0.2004 0.1856 0.2384 -0.0096 0.0345  0.0191  20  ASN   A O   
506  C  CB  A ASN   A 20  ? 0.1698 0.2025 0.3947 0.0372  0.0600  0.0498  20  ASN   A CB  
507  C  CB  B ASN   A 20  ? 0.1847 0.1791 0.2308 -0.0046 0.0203  0.0260  20  ASN   A CB  
508  C  CG  A ASN   A 20  ? 0.1856 0.2149 0.4276 0.0504  0.0563  0.0560  20  ASN   A CG  
509  C  CG  B ASN   A 20  ? 0.1811 0.1774 0.2356 -0.0056 0.0118  0.0238  20  ASN   A CG  
510  O  OD1 A ASN   A 20  ? 0.2044 0.2224 0.4526 0.0595  0.0600  0.0549  20  ASN   A OD1 
511  O  OD1 B ASN   A 20  ? 0.1807 0.1814 0.2411 -0.0084 -0.0022 0.0184  20  ASN   A OD1 
512  N  ND2 A ASN   A 20  ? 0.1995 0.2159 0.4382 0.0495  0.0438  0.0640  20  ASN   A ND2 
513  N  ND2 B ASN   A 20  ? 0.1805 0.1730 0.2356 -0.0023 0.0129  0.0298  20  ASN   A ND2 
526  N  N   A ALA   A 21  ? 0.1895 0.1762 0.3619 0.0168  0.0544  0.0230  21  ALA   A N   
527  N  N   B ALA   A 21  ? 0.1928 0.1840 0.2301 -0.0089 0.0362  0.0176  21  ALA   A N   
528  C  CA  A ALA   A 21  ? 0.1919 0.1778 0.3473 0.0072  0.0512  0.0325  21  ALA   A CA  
529  C  CA  B ALA   A 21  ? 0.1910 0.1835 0.2216 -0.0133 0.0420  0.0208  21  ALA   A CA  
530  C  C   A ALA   A 21  ? 0.1868 0.1775 0.3343 0.0025  0.0498  0.0294  21  ALA   A C   
531  C  C   B ALA   A 21  ? 0.1854 0.1847 0.2156 -0.0127 0.0511  0.0188  21  ALA   A C   
532  O  O   A ALA   A 21  ? 0.1897 0.1899 0.3407 0.0054  0.0445  0.0269  21  ALA   A O   
533  O  O   B ALA   A 21  ? 0.1859 0.1880 0.2227 -0.0083 0.0509  0.0130  21  ALA   A O   
534  C  CB  A ALA   A 21  ? 0.2117 0.1888 0.3562 -0.0015 0.0401  0.0482  21  ALA   A CB  
535  C  CB  B ALA   A 21  ? 0.1965 0.1852 0.2288 -0.0164 0.0345  0.0229  21  ALA   A CB  
546  N  N   A ASP   A 22  ? 0.1892 0.1727 0.3251 -0.0052 0.0499  0.0253  22  ASP   A N   
547  N  N   B ASP   A 22  ? 0.1820 0.1835 0.2077 -0.0166 0.0578  0.0244  22  ASP   A N   
548  C  CA  A ASP   A 22  ? 0.1886 0.1835 0.3116 -0.0074 0.0429  0.0231  22  ASP   A CA  
549  C  CA  B ASP   A 22  ? 0.1792 0.1874 0.2045 -0.0158 0.0569  0.0246  22  ASP   A CA  
550  C  C   A ASP   A 22  ? 0.1754 0.1910 0.2688 -0.0131 0.0478  0.0252  22  ASP   A C   
551  C  C   B ASP   A 22  ? 0.1721 0.1933 0.1926 -0.0213 0.0536  0.0187  22  ASP   A C   
552  O  O   A ASP   A 22  ? 0.1900 0.2051 0.2751 -0.0131 0.0613  0.0303  22  ASP   A O   
553  O  O   B ASP   A 22  ? 0.1734 0.1965 0.1939 -0.0241 0.0542  0.0143  22  ASP   A O   
554  C  CB  A ASP   A 22  ? 0.2072 0.1883 0.3496 -0.0083 0.0383  0.0140  22  ASP   A CB  
555  C  CB  B ASP   A 22  ? 0.1838 0.1882 0.2153 -0.0089 0.0625  0.0235  22  ASP   A CB  
556  C  CG  A ASP   A 22  ? 0.2231 0.1932 0.3765 -0.0106 0.0303  0.0171  22  ASP   A CG  
557  C  CG  B ASP   A 22  ? 0.1856 0.1870 0.2207 -0.0027 0.0674  0.0281  22  ASP   A CG  
558  O  OD1 A ASP   A 22  ? 0.2160 0.1920 0.3906 -0.0189 0.0199  0.0354  22  ASP   A OD1 
559  O  OD1 B ASP   A 22  ? 0.1840 0.1861 0.2217 -0.0034 0.0664  0.0351  22  ASP   A OD1 
560  O  OD2 A ASP   A 22  ? 0.2449 0.2052 0.3979 -0.0025 0.0400  0.0018  22  ASP   A OD2 
561  O  OD2 B ASP   A 22  ? 0.1877 0.1895 0.2293 -0.0004 0.0694  0.0294  22  ASP   A OD2 
570  N  N   A ILE   A 23  ? 0.1745 0.1955 0.2445 -0.0120 0.0428  0.0225  23  ILE   A N   
571  N  N   B ILE   A 23  ? 0.1692 0.1981 0.1873 -0.0208 0.0473  0.0168  23  ILE   A N   
572  C  CA  A ILE   A 23  ? 0.1711 0.1907 0.2146 -0.0127 0.0302  0.0264  23  ILE   A CA  
573  C  CA  B ILE   A 23  ? 0.1667 0.2003 0.1804 -0.0212 0.0373  0.0175  23  ILE   A CA  
574  C  C   A ILE   A 23  ? 0.1685 0.2038 0.2081 -0.0154 0.0482  0.0135  23  ILE   A C   
575  C  C   B ILE   A 23  ? 0.1726 0.2078 0.1920 -0.0210 0.0446  0.0161  23  ILE   A C   
576  O  O   A ILE   A 23  ? 0.1712 0.2098 0.1973 -0.0115 0.0539  0.0129  23  ILE   A O   
577  O  O   B ILE   A 23  ? 0.1761 0.2106 0.1795 -0.0172 0.0455  0.0185  23  ILE   A O   
578  C  CB  A ILE   A 23  ? 0.1857 0.1829 0.1818 -0.0098 0.0226  0.0250  23  ILE   A CB  
579  C  CB  B ILE   A 23  ? 0.1604 0.1957 0.1640 -0.0225 0.0255  0.0163  23  ILE   A CB  
580  C  CG1 A ILE   A 23  ? 0.1890 0.1896 0.1828 -0.0053 0.0244  0.0220  23  ILE   A CG1 
581  C  CG1 B ILE   A 23  ? 0.1594 0.1973 0.1617 -0.0225 0.0167  0.0159  23  ILE   A CG1 
582  C  CG2 A ILE   A 23  ? 0.1890 0.1830 0.1853 -0.0082 0.0182  0.0254  23  ILE   A CG2 
583  C  CG2 B ILE   A 23  ? 0.1585 0.1923 0.1616 -0.0213 0.0213  0.0143  23  ILE   A CG2 
584  C  CD1 A ILE   A 23  ? 0.1922 0.1923 0.1921 -0.0076 0.0100  0.0061  23  ILE   A CD1 
585  C  CD1 B ILE   A 23  ? 0.1575 0.1977 0.1643 -0.0228 0.0066  0.0116  23  ILE   A CD1 
608  N  N   . VAL   A 24  ? 0.1781 0.2129 0.2216 -0.0239 0.0463  0.0126  24  VAL   A N   
609  C  CA  . VAL   A 24  ? 0.1983 0.2191 0.2420 -0.0317 0.0441  0.0027  24  VAL   A CA  
610  C  C   . VAL   A 24  ? 0.2158 0.2383 0.2428 -0.0381 0.0612  -0.0025 24  VAL   A C   
611  O  O   . VAL   A 24  ? 0.2253 0.2261 0.2492 -0.0289 0.0625  -0.0066 24  VAL   A O   
612  C  CB  . VAL   A 24  ? 0.2072 0.2245 0.2684 -0.0375 0.0432  0.0179  24  VAL   A CB  
613  C  CG1 . VAL   A 24  ? 0.2209 0.2300 0.2849 -0.0378 0.0404  0.0146  24  VAL   A CG1 
614  C  CG2 . VAL   A 24  ? 0.2157 0.2360 0.2836 -0.0286 0.0546  0.0341  24  VAL   A CG2 
625  N  N   A GLU   A 25  ? 0.2239 0.2710 0.2486 -0.0381 0.0818  -0.0077 25  GLU   A N   
626  N  N   B GLU   A 25  ? 0.2234 0.2533 0.2427 -0.0382 0.0577  -0.0036 25  GLU   A N   
627  C  CA  A GLU   A 25  ? 0.2430 0.3024 0.2628 -0.0325 0.0997  -0.0101 25  GLU   A CA  
628  C  CA  B GLU   A 25  ? 0.2327 0.2675 0.2507 -0.0385 0.0549  -0.0025 25  GLU   A CA  
629  C  C   A GLU   A 25  ? 0.2315 0.3021 0.2413 -0.0443 0.1045  -0.0103 25  GLU   A C   
630  C  C   B GLU   A 25  ? 0.2295 0.2702 0.2336 -0.0436 0.0561  -0.0035 25  GLU   A C   
631  O  O   A GLU   A 25  ? 0.2373 0.3132 0.2447 -0.0435 0.1059  -0.0159 25  GLU   A O   
632  O  O   B GLU   A 25  ? 0.2315 0.2744 0.2323 -0.0429 0.0581  -0.0059 25  GLU   A O   
633  C  CB  A GLU   A 25  ? 0.2668 0.3280 0.3016 -0.0223 0.1114  -0.0071 25  GLU   A CB  
634  C  CB  B GLU   A 25  ? 0.2438 0.2773 0.2771 -0.0342 0.0521  0.0009  25  GLU   A CB  
635  C  CG  A GLU   A 25  ? 0.2977 0.3539 0.3510 -0.0143 0.0983  -0.0098 25  GLU   A CG  
636  C  CG  B GLU   A 25  ? 0.2556 0.2873 0.3063 -0.0305 0.0444  0.0024  25  GLU   A CG  
637  C  CD  A GLU   A 25  ? 0.3232 0.3776 0.3946 -0.0080 0.0857  -0.0088 25  GLU   A CD  
638  C  CD  B GLU   A 25  ? 0.2640 0.2961 0.3301 -0.0279 0.0363  0.0027  25  GLU   A CD  
639  O  OE1 A GLU   A 25  ? 0.3351 0.3882 0.4051 -0.0020 0.0716  -0.0140 25  GLU   A OE1 
640  O  OE1 B GLU   A 25  ? 0.2672 0.3003 0.3370 -0.0250 0.0342  0.0029  25  GLU   A OE1 
641  O  OE2 A GLU   A 25  ? 0.3303 0.3843 0.4198 -0.0068 0.0818  -0.0165 25  GLU   A OE2 
642  O  OE2 B GLU   A 25  ? 0.2678 0.2976 0.3403 -0.0293 0.0335  0.0013  25  GLU   A OE2 
655  N  N   A GLU   A 26  ? 0.2210 0.2865 0.2433 -0.0578 0.1058  -0.0121 26  GLU   A N   
656  N  N   B GLU   A 26  ? 0.2256 0.2666 0.2233 -0.0501 0.0560  -0.0047 26  GLU   A N   
657  C  CA  A GLU   A 26  ? 0.2315 0.2710 0.2372 -0.0737 0.0910  -0.0037 26  GLU   A CA  
658  C  CA  B GLU   A 26  ? 0.2242 0.2611 0.2129 -0.0567 0.0523  -0.0044 26  GLU   A CA  
659  C  C   A GLU   A 26  ? 0.2261 0.2549 0.2110 -0.0720 0.0725  -0.0032 26  GLU   A C   
660  C  C   B GLU   A 26  ? 0.2192 0.2498 0.1994 -0.0606 0.0621  -0.0043 26  GLU   A C   
661  O  O   A GLU   A 26  ? 0.2332 0.2521 0.1952 -0.0786 0.0605  -0.0087 26  GLU   A O   
662  O  O   B GLU   A 26  ? 0.2219 0.2492 0.1927 -0.0599 0.0663  -0.0034 26  GLU   A O   
663  C  CB  A GLU   A 26  ? 0.2584 0.2622 0.2743 -0.0857 0.0804  0.0062  26  GLU   A CB  
664  C  CB  B GLU   A 26  ? 0.2294 0.2639 0.2201 -0.0595 0.0341  -0.0042 26  GLU   A CB  
665  C  CG  A GLU   A 26  ? 0.2831 0.2607 0.3212 -0.0867 0.0863  -0.0051 26  GLU   A CG  
666  C  CG  B GLU   A 26  ? 0.2339 0.2639 0.2318 -0.0611 0.0199  -0.0080 26  GLU   A CG  
667  C  CD  A GLU   A 26  ? 0.2900 0.2515 0.3374 -0.0968 0.1159  -0.0112 26  GLU   A CD  
668  C  CD  B GLU   A 26  ? 0.2342 0.2609 0.2345 -0.0645 0.0109  -0.0111 26  GLU   A CD  
669  O  OE1 A GLU   A 26  ? 0.2783 0.2681 0.3428 -0.0842 0.1437  -0.0627 26  GLU   A OE1 
670  O  OE1 B GLU   A 26  ? 0.2374 0.2628 0.2361 -0.0621 0.0100  -0.0147 26  GLU   A OE1 
671  O  OE2 A GLU   A 26  ? 0.3058 0.2559 0.3386 -0.0866 0.1230  -0.0007 26  GLU   A OE2 
672  O  OE2 B GLU   A 26  ? 0.2317 0.2585 0.2329 -0.0687 0.0050  -0.0145 26  GLU   A OE2 
685  N  N   . ALA   A 27  ? 0.2108 0.2377 0.1957 -0.0657 0.0681  -0.0046 27  ALA   A N   
686  C  CA  . ALA   A 27  ? 0.2175 0.2339 0.1712 -0.0584 0.0614  -0.0070 27  ALA   A CA  
687  C  C   . ALA   A 27  ? 0.2492 0.2443 0.1751 -0.0625 0.0656  -0.0216 27  ALA   A C   
688  O  O   . ALA   A 27  ? 0.2595 0.2401 0.1834 -0.0659 0.0483  -0.0188 27  ALA   A O   
689  C  CB  . ALA   A 27  ? 0.2023 0.2279 0.1785 -0.0579 0.0479  -0.0103 27  ALA   A CB  
696  N  N   . LYS   A 28  ? 0.2868 0.2688 0.2034 -0.0562 0.0642  -0.0528 28  LYS   A N   
697  C  CA  . LYS   A 28  ? 0.3261 0.3066 0.2516 -0.0541 0.0614  -0.0666 28  LYS   A CA  
698  C  C   . LYS   A 28  ? 0.3443 0.3393 0.2451 -0.0644 0.0741  -0.0515 28  LYS   A C   
699  O  O   . LYS   A 28  ? 0.3514 0.3519 0.2875 -0.0649 0.0616  -0.0455 28  LYS   A O   
700  C  CB  . LYS   A 28  ? 0.3444 0.3193 0.3020 -0.0401 0.0546  -0.0874 28  LYS   A CB  
701  C  CG  . LYS   A 28  ? 0.3616 0.3324 0.3523 -0.0294 0.0492  -0.0958 28  LYS   A CG  
702  C  CD  . LYS   A 28  ? 0.3774 0.3526 0.4128 -0.0205 0.0437  -0.0929 28  LYS   A CD  
703  C  CE  . LYS   A 28  ? 0.3885 0.3667 0.4553 -0.0180 0.0380  -0.0928 28  LYS   A CE  
704  N  NZ  . LYS   A 28  ? 0.3962 0.3751 0.4837 -0.0131 0.0386  -0.0940 28  LYS   A NZ  
718  N  N   . LYS   A 29  ? 0.3502 0.3615 0.2315 -0.0748 0.1012  -0.0303 29  LYS   A N   
719  C  CA  . LYS   A 29  ? 0.3671 0.3897 0.2483 -0.0785 0.1119  -0.0138 29  LYS   A CA  
720  C  C   . LYS   A 29  ? 0.3651 0.3885 0.2158 -0.0881 0.1028  -0.0084 29  LYS   A C   
721  O  O   . LYS   A 29  ? 0.3771 0.3998 0.2206 -0.0792 0.0964  -0.0130 29  LYS   A O   
722  C  CB  . LYS   A 29  ? 0.3833 0.4191 0.3117 -0.0699 0.1221  -0.0049 29  LYS   A CB  
723  C  CG  . LYS   A 29  ? 0.4004 0.4426 0.3810 -0.0618 0.1232  -0.0007 29  LYS   A CG  
724  C  CD  . LYS   A 29  ? 0.4160 0.4641 0.4493 -0.0551 0.1207  -0.0002 29  LYS   A CD  
725  C  CE  . LYS   A 29  ? 0.4271 0.4791 0.4948 -0.0503 0.1216  -0.0024 29  LYS   A CE  
726  N  NZ  . LYS   A 29  ? 0.4321 0.4871 0.5235 -0.0477 0.1209  -0.0044 29  LYS   A NZ  
740  N  N   . VAL   A 30  ? 0.3474 0.3714 0.2018 -0.1041 0.0965  -0.0081 30  VAL   A N   
741  C  CA  . VAL   A 30  ? 0.3430 0.3546 0.1900 -0.1149 0.0733  0.0081  30  VAL   A CA  
742  C  C   . VAL   A 30  ? 0.3424 0.3389 0.1528 -0.1118 0.0581  0.0095  30  VAL   A C   
743  O  O   . VAL   A 30  ? 0.3514 0.3418 0.1550 -0.1113 0.0509  0.0099  30  VAL   A O   
744  C  CB  . VAL   A 30  ? 0.3396 0.3514 0.2250 -0.1278 0.0486  0.0120  30  VAL   A CB  
745  C  CG1 . VAL   A 30  ? 0.3445 0.3526 0.2343 -0.1259 0.0289  0.0135  30  VAL   A CG1 
746  C  CG2 . VAL   A 30  ? 0.3372 0.3518 0.2514 -0.1346 0.0505  0.0130  30  VAL   A CG2 
756  N  N   . LYS   A 31  ? 0.3258 0.3151 0.1377 -0.1174 0.0390  0.0018  31  LYS   A N   
757  C  CA  . LYS   A 31  ? 0.3346 0.3102 0.1552 -0.1053 0.0126  0.0023  31  LYS   A CA  
758  C  C   . LYS   A 31  ? 0.3085 0.2855 0.1349 -0.0839 0.0043  0.0353  31  LYS   A C   
759  O  O   . LYS   A 31  ? 0.3129 0.2948 0.1441 -0.0778 -0.0124 0.0467  31  LYS   A O   
760  C  CB  . LYS   A 31  ? 0.3794 0.3407 0.2549 -0.1050 -0.0043 -0.0231 31  LYS   A CB  
761  C  CG  . LYS   A 31  ? 0.4261 0.3770 0.3879 -0.0952 -0.0233 -0.0341 31  LYS   A CG  
762  C  CD  . LYS   A 31  ? 0.4627 0.4051 0.4910 -0.0879 -0.0394 -0.0427 31  LYS   A CD  
763  C  CE  . LYS   A 31  ? 0.4896 0.4256 0.5559 -0.0821 -0.0534 -0.0532 31  LYS   A CE  
764  N  NZ  . LYS   A 31  ? 0.5051 0.4372 0.5929 -0.0800 -0.0619 -0.0603 31  LYS   A NZ  
778  N  N   . PRO   A 32  ? 0.2717 0.2532 0.1243 -0.0724 0.0058  0.0302  32  PRO   A N   
779  C  CA  . PRO   A 32  ? 0.2622 0.2343 0.1508 -0.0666 -0.0063 0.0371  32  PRO   A CA  
780  C  C   . PRO   A 32  ? 0.2569 0.2289 0.1563 -0.0525 -0.0175 0.0438  32  PRO   A C   
781  O  O   . PRO   A 32  ? 0.2478 0.2227 0.1619 -0.0550 -0.0260 0.0485  32  PRO   A O   
782  C  CB  . PRO   A 32  ? 0.2571 0.2393 0.1632 -0.0673 -0.0050 0.0297  32  PRO   A CB  
783  C  CG  . PRO   A 32  ? 0.2554 0.2440 0.1359 -0.0622 -0.0153 0.0195  32  PRO   A CG  
784  C  CD  . PRO   A 32  ? 0.2599 0.2429 0.1243 -0.0666 -0.0088 0.0215  32  PRO   A CD  
792  N  N   . THR   A 33  ? 0.2665 0.2244 0.1519 -0.0477 -0.0103 0.0514  33  THR   A N   
793  C  CA  . THR   A 33  ? 0.2660 0.2268 0.1518 -0.0318 -0.0215 0.0441  33  THR   A CA  
794  C  C   . THR   A 33  ? 0.2303 0.2056 0.1439 -0.0345 -0.0243 0.0344  33  THR   A C   
795  O  O   . THR   A 33  ? 0.2203 0.2086 0.1671 -0.0339 -0.0312 0.0377  33  THR   A O   
796  C  CB  . THR   A 33  ? 0.2949 0.2455 0.1747 -0.0216 -0.0318 0.0581  33  THR   A CB  
797  O  OG1 . THR   A 33  ? 0.3181 0.2574 0.2040 -0.0103 -0.0255 0.0706  33  THR   A OG1 
798  C  CG2 . THR   A 33  ? 0.2999 0.2571 0.1873 -0.0152 -0.0409 0.0575  33  THR   A CG2 
806  N  N   . VAL   A 34  ? 0.2024 0.1910 0.1301 -0.0342 -0.0149 0.0282  34  VAL   A N   
807  C  CA  . VAL   A 34  ? 0.1831 0.1782 0.1314 -0.0302 -0.0105 0.0307  34  VAL   A CA  
808  C  C   . VAL   A 34  ? 0.1695 0.1701 0.1366 -0.0224 -0.0005 0.0223  34  VAL   A C   
809  O  O   . VAL   A 34  ? 0.1710 0.1698 0.1581 -0.0346 -0.0006 0.0338  34  VAL   A O   
810  C  CB  . VAL   A 34  ? 0.1844 0.1707 0.1521 -0.0289 0.0001  0.0201  34  VAL   A CB  
811  C  CG1 . VAL   A 34  ? 0.1901 0.1731 0.1575 -0.0211 0.0060  0.0109  34  VAL   A CG1 
812  C  CG2 . VAL   A 34  ? 0.1898 0.1858 0.1786 -0.0220 -0.0182 0.0163  34  VAL   A CG2 
822  N  N   . VAL   A 35  ? 0.1579 0.1553 0.1258 -0.0262 -0.0067 0.0185  35  VAL   A N   
823  C  CA  . VAL   A 35  ? 0.1511 0.1555 0.1189 -0.0239 -0.0017 0.0159  35  VAL   A CA  
824  C  C   . VAL   A 35  ? 0.1417 0.1437 0.1274 -0.0168 0.0015  0.0190  35  VAL   A C   
825  O  O   . VAL   A 35  ? 0.1380 0.1516 0.1437 -0.0243 0.0104  0.0108  35  VAL   A O   
826  C  CB  . VAL   A 35  ? 0.1564 0.1645 0.1287 -0.0188 0.0083  0.0059  35  VAL   A CB  
827  C  CG1 . VAL   A 35  ? 0.1672 0.1629 0.1387 -0.0072 0.0053  0.0004  35  VAL   A CG1 
828  C  CG2 . VAL   A 35  ? 0.1554 0.1678 0.1478 -0.0142 0.0162  -0.0059 35  VAL   A CG2 
838  N  N   . VAL   A 36  ? 0.1274 0.1407 0.1188 -0.0170 0.0081  0.0169  36  VAL   A N   
839  C  CA  . VAL   A 36  ? 0.1238 0.1309 0.1303 -0.0118 0.0054  0.0101  36  VAL   A CA  
840  C  C   . VAL   A 36  ? 0.1178 0.1323 0.1432 -0.0155 0.0067  0.0147  36  VAL   A C   
841  O  O   . VAL   A 36  ? 0.1283 0.1300 0.1579 -0.0067 0.0241  0.0103  36  VAL   A O   
842  C  CB  . VAL   A 36  ? 0.1281 0.1239 0.1351 -0.0104 0.0031  0.0095  36  VAL   A CB  
843  C  CG1 . VAL   A 36  ? 0.1401 0.1271 0.1517 -0.0157 0.0059  0.0050  36  VAL   A CG1 
844  C  CG2 . VAL   A 36  ? 0.1374 0.1277 0.1538 -0.0112 -0.0043 0.0138  36  VAL   A CG2 
854  N  N   . ASN   A 37  ? 0.1155 0.1265 0.1357 -0.0034 -0.0001 0.0171  37  ASN   A N   
855  C  CA  . ASN   A 37  ? 0.1153 0.1191 0.1326 0.0002  -0.0017 0.0166  37  ASN   A CA  
856  C  C   . ASN   A 37  ? 0.1172 0.1175 0.1349 -0.0037 0.0080  0.0222  37  ASN   A C   
857  O  O   . ASN   A 37  ? 0.1275 0.1292 0.1267 0.0061  0.0085  0.0115  37  ASN   A O   
858  C  CB  . ASN   A 37  ? 0.1210 0.1199 0.1411 0.0006  -0.0001 0.0109  37  ASN   A CB  
859  C  CG  . ASN   A 37  ? 0.1214 0.1209 0.1517 0.0006  0.0029  0.0081  37  ASN   A CG  
860  O  OD1 . ASN   A 37  ? 0.1222 0.1212 0.1704 -0.0002 0.0023  0.0127  37  ASN   A OD1 
861  N  ND2 . ASN   A 37  ? 0.1186 0.1219 0.1580 -0.0018 0.0019  0.0217  37  ASN   A ND2 
868  N  N   A ALA   A 38  ? 0.1175 0.1241 0.1489 0.0036  0.0096  0.0105  38  ALA   A N   
869  N  N   B ALA   A 38  ? 0.1200 0.1246 0.1320 -0.0020 0.0030  0.0173  38  ALA   A N   
870  C  CA  A ALA   A 38  ? 0.1249 0.1334 0.1431 -0.0005 -0.0016 0.0052  38  ALA   A CA  
871  C  CA  B ALA   A 38  ? 0.1245 0.1318 0.1327 -0.0033 -0.0039 0.0144  38  ALA   A CA  
872  C  C   A ALA   A 38  ? 0.1264 0.1325 0.1385 0.0015  -0.0089 0.0033  38  ALA   A C   
873  C  C   B ALA   A 38  ? 0.1232 0.1302 0.1320 -0.0022 -0.0088 0.0116  38  ALA   A C   
874  O  O   A ALA   A 38  ? 0.1232 0.1287 0.1452 0.0067  -0.0085 0.0064  38  ALA   A O   
875  O  O   B ALA   A 38  ? 0.1196 0.1290 0.1283 -0.0045 -0.0160 0.0167  38  ALA   A O   
876  C  CB  A ALA   A 38  ? 0.1264 0.1597 0.1636 -0.0117 -0.0106 0.0114  38  ALA   A CB  
877  C  CB  B ALA   A 38  ? 0.1291 0.1407 0.1412 -0.0064 -0.0082 0.0112  38  ALA   A CB  
888  N  N   . ALA   A 39  ? 0.1241 0.1304 0.1442 -0.0006 -0.0003 0.0067  39  ALA   A N   
889  C  CA  . ALA   A 39  ? 0.1294 0.1282 0.1442 0.0052  0.0054  0.0110  39  ALA   A CA  
890  C  C   . ALA   A 39  ? 0.1278 0.1211 0.1446 0.0036  0.0055  0.0104  39  ALA   A C   
891  O  O   . ALA   A 39  ? 0.1353 0.1266 0.1472 -0.0054 0.0097  0.0074  39  ALA   A O   
892  C  CB  . ALA   A 39  ? 0.1279 0.1456 0.1606 0.0037  -0.0112 -0.0019 39  ALA   A CB  
899  N  N   A ASN   A 40  ? 0.1365 0.1279 0.1411 -0.0054 0.0168  0.0062  40  ASN   A N   
900  N  N   B ASN   A 40  ? 0.1376 0.1222 0.1357 0.0009  0.0104  0.0104  40  ASN   A N   
901  C  CA  A ASN   A 40  ? 0.1438 0.1271 0.1450 -0.0016 0.0078  0.0053  40  ASN   A CA  
902  C  CA  B ASN   A 40  ? 0.1475 0.1212 0.1367 0.0008  0.0125  0.0120  40  ASN   A CA  
903  C  C   A ASN   A 40  ? 0.1472 0.1158 0.1287 -0.0042 0.0168  0.0069  40  ASN   A C   
904  C  C   B ASN   A 40  ? 0.1523 0.1194 0.1289 0.0022  0.0132  0.0198  40  ASN   A C   
905  O  O   A ASN   A 40  ? 0.1400 0.1184 0.1325 -0.0074 0.0253  0.0114  40  ASN   A O   
906  O  O   B ASN   A 40  ? 0.1506 0.1207 0.1345 0.0012  0.0122  0.0229  40  ASN   A O   
907  C  CB  A ASN   A 40  ? 0.1583 0.1303 0.1617 0.0073  -0.0034 0.0094  40  ASN   A CB  
908  C  CB  B ASN   A 40  ? 0.1542 0.1212 0.1488 -0.0026 0.0163  0.0081  40  ASN   A CB  
909  C  CG  A ASN   A 40  ? 0.1640 0.1305 0.1807 0.0087  -0.0111 0.0153  40  ASN   A CG  
910  C  CG  B ASN   A 40  ? 0.1586 0.1238 0.1639 -0.0092 0.0233  0.0073  40  ASN   A CG  
911  O  OD1 A ASN   A 40  ? 0.1772 0.1330 0.2277 0.0077  -0.0136 0.0048  40  ASN   A OD1 
912  O  OD1 B ASN   A 40  ? 0.1655 0.1286 0.1806 -0.0086 0.0227  -0.0037 40  ASN   A OD1 
913  N  ND2 A ASN   A 40  ? 0.1658 0.1406 0.1795 0.0033  -0.0003 0.0040  40  ASN   A ND2 
914  N  ND2 B ASN   A 40  ? 0.1579 0.1283 0.1613 -0.0177 0.0325  0.0109  40  ASN   A ND2 
927  N  N   A VAL   A 41  ? 0.1563 0.1152 0.1404 -0.0013 0.0172  0.0116  41  VAL   A N   
928  N  N   B VAL   A 41  ? 0.1588 0.1191 0.1231 0.0062  0.0147  0.0269  41  VAL   A N   
929  C  CA  A VAL   A 41  ? 0.1566 0.1280 0.1489 -0.0016 0.0222  0.0120  41  VAL   A CA  
930  C  CA  B VAL   A 41  ? 0.1636 0.1248 0.1186 0.0046  0.0184  0.0289  41  VAL   A CA  
931  C  C   A VAL   A 41  ? 0.1487 0.1287 0.1544 -0.0002 0.0255  0.0088  41  VAL   A C   
932  C  C   B VAL   A 41  ? 0.1649 0.1331 0.1249 0.0013  0.0178  0.0225  41  VAL   A C   
933  O  O   A VAL   A 41  ? 0.1472 0.1237 0.1794 0.0034  0.0244  0.0003  41  VAL   A O   
934  O  O   B VAL   A 41  ? 0.1675 0.1305 0.1248 -0.0016 0.0132  0.0180  41  VAL   A O   
935  C  CB  A VAL   A 41  ? 0.1697 0.1386 0.1449 -0.0038 0.0302  0.0075  41  VAL   A CB  
936  C  CB  B VAL   A 41  ? 0.1661 0.1237 0.1159 0.0063  0.0246  0.0305  41  VAL   A CB  
937  C  CG1 A VAL   A 41  ? 0.1817 0.1518 0.1564 -0.0000 0.0240  0.0057  41  VAL   A CG1 
938  C  CG1 B VAL   A 41  ? 0.1723 0.1272 0.1254 0.0021  0.0372  0.0273  41  VAL   A CG1 
939  C  CG2 A VAL   A 41  ? 0.1804 0.1480 0.1323 -0.0111 0.0386  0.0099  41  VAL   A CG2 
940  C  CG2 B VAL   A 41  ? 0.1646 0.1266 0.1158 0.0087  0.0174  0.0314  41  VAL   A CG2 
959  N  N   A TYR   A 42  ? 0.1362 0.1224 0.1622 0.0028  0.0329  0.0186  42  TYR   A N   
960  N  N   B TYR   A 42  ? 0.1631 0.1402 0.1305 0.0016  0.0192  0.0263  42  TYR   A N   
961  C  CA  A TYR   A 42  ? 0.1440 0.1153 0.1705 -0.0020 0.0294  0.0222  42  TYR   A CA  
962  C  CA  B TYR   A 42  ? 0.1646 0.1479 0.1408 -0.0002 0.0133  0.0222  42  TYR   A CA  
963  C  C   A TYR   A 42  ? 0.1290 0.1171 0.1743 0.0011  0.0224  0.0249  42  TYR   A C   
964  C  C   B TYR   A 42  ? 0.1637 0.1522 0.1351 -0.0005 0.0054  0.0239  42  TYR   A C   
965  O  O   A TYR   A 42  ? 0.1321 0.1191 0.1908 -0.0110 0.0222  0.0073  42  TYR   A O   
966  O  O   B TYR   A 42  ? 0.1648 0.1537 0.1380 -0.0047 0.0096  0.0203  42  TYR   A O   
967  C  CB  A TYR   A 42  ? 0.1719 0.1280 0.1657 -0.0010 0.0361  0.0297  42  TYR   A CB  
968  C  CB  B TYR   A 42  ? 0.1682 0.1545 0.1544 -0.0026 0.0122  0.0177  42  TYR   A CB  
969  C  CG  A TYR   A 42  ? 0.1932 0.1430 0.1630 -0.0045 0.0265  0.0350  42  TYR   A CG  
970  C  CG  B TYR   A 42  ? 0.1714 0.1612 0.1655 -0.0063 0.0089  0.0129  42  TYR   A CG  
971  C  CD1 A TYR   A 42  ? 0.2021 0.1563 0.1723 -0.0120 0.0280  0.0298  42  TYR   A CD1 
972  C  CD1 B TYR   A 42  ? 0.1731 0.1644 0.1723 -0.0084 0.0077  0.0112  42  TYR   A CD1 
973  C  CD2 A TYR   A 42  ? 0.2067 0.1612 0.1775 -0.0011 0.0227  0.0235  42  TYR   A CD2 
974  C  CD2 B TYR   A 42  ? 0.1745 0.1672 0.1727 -0.0074 0.0088  0.0082  42  TYR   A CD2 
975  C  CE1 A TYR   A 42  ? 0.2133 0.1695 0.1711 -0.0164 0.0343  0.0301  42  TYR   A CE1 
976  C  CE1 B TYR   A 42  ? 0.1763 0.1685 0.1776 -0.0107 0.0087  0.0099  42  TYR   A CE1 
977  C  CE2 A TYR   A 42  ? 0.2206 0.1752 0.1876 -0.0177 0.0225  0.0315  42  TYR   A CE2 
978  C  CE2 B TYR   A 42  ? 0.1782 0.1718 0.1785 -0.0130 0.0075  0.0100  42  TYR   A CE2 
979  C  CZ  A TYR   A 42  ? 0.2280 0.1804 0.1770 -0.0179 0.0307  0.0286  42  TYR   A CZ  
980  C  CZ  B TYR   A 42  ? 0.1804 0.1735 0.1798 -0.0134 0.0101  0.0085  42  TYR   A CZ  
981  O  OH  A TYR   A 42  ? 0.2403 0.2010 0.2015 -0.0310 0.0332  0.0214  42  TYR   A OH  
982  O  OH  B TYR   A 42  ? 0.1839 0.1811 0.1875 -0.0191 0.0110  0.0057  42  TYR   A OH  
1001 N  N   A LEU   A 43  ? 0.1234 0.1151 0.1661 -0.0021 0.0121  0.0119  43  LEU   A N   
1002 N  N   B LEU   A 43  ? 0.1627 0.1548 0.1369 0.0014  -0.0044 0.0217  43  LEU   A N   
1003 C  CA  A LEU   A 43  ? 0.1190 0.1157 0.1683 -0.0040 0.0165  0.0067  43  LEU   A CA  
1004 C  CA  B LEU   A 43  ? 0.1640 0.1579 0.1384 0.0040  -0.0073 0.0185  43  LEU   A CA  
1005 C  C   A LEU   A 43  ? 0.1163 0.1183 0.1625 -0.0001 0.0162  0.0072  43  LEU   A C   
1006 C  C   B LEU   A 43  ? 0.1686 0.1647 0.1436 0.0027  -0.0056 0.0127  43  LEU   A C   
1007 O  O   A LEU   A 43  ? 0.1419 0.1246 0.1853 0.0033  0.0003  0.0063  43  LEU   A O   
1008 O  O   B LEU   A 43  ? 0.1708 0.1663 0.1434 0.0005  -0.0095 0.0098  43  LEU   A O   
1009 C  CB  A LEU   A 43  ? 0.1307 0.1145 0.1714 -0.0087 0.0185  0.0031  43  LEU   A CB  
1010 C  CB  B LEU   A 43  ? 0.1624 0.1530 0.1334 0.0073  -0.0097 0.0222  43  LEU   A CB  
1011 C  CG  A LEU   A 43  ? 0.1343 0.1164 0.1798 -0.0043 0.0152  0.0019  43  LEU   A CG  
1012 C  CG  B LEU   A 43  ? 0.1598 0.1501 0.1356 0.0111  -0.0104 0.0227  43  LEU   A CG  
1013 C  CD1 A LEU   A 43  ? 0.1389 0.1279 0.1963 -0.0013 0.0032  0.0053  43  LEU   A CD1 
1014 C  CD1 B LEU   A 43  ? 0.1600 0.1502 0.1345 0.0113  -0.0105 0.0261  43  LEU   A CD1 
1015 C  CD2 A LEU   A 43  ? 0.1511 0.1204 0.1900 -0.0044 0.0179  0.0177  43  LEU   A CD2 
1016 C  CD2 B LEU   A 43  ? 0.1620 0.1481 0.1393 0.0139  -0.0126 0.0273  43  LEU   A CD2 
1039 N  N   A LYS   A 44  ? 0.1238 0.1196 0.1532 -0.0024 0.0135  0.0114  44  LYS   A N   
1040 N  N   B LYS   A 44  ? 0.1742 0.1715 0.1526 0.0036  -0.0029 0.0106  44  LYS   A N   
1041 C  CA  A LYS   A 44  ? 0.1380 0.1176 0.1713 -0.0067 0.0117  0.0192  44  LYS   A CA  
1042 C  CA  B LYS   A 44  ? 0.1834 0.1782 0.1687 0.0050  0.0002  0.0089  44  LYS   A CA  
1043 C  C   A LYS   A 44  ? 0.1275 0.1171 0.1509 -0.0007 0.0038  0.0067  44  LYS   A C   
1044 C  C   B LYS   A 44  ? 0.1783 0.1709 0.1462 0.0089  0.0011  0.0052  44  LYS   A C   
1045 O  O   A LYS   A 44  ? 0.1354 0.1288 0.1676 0.0030  0.0031  -0.0049 44  LYS   A O   
1046 O  O   B LYS   A 44  ? 0.1801 0.1712 0.1383 0.0126  0.0069  0.0035  44  LYS   A O   
1047 C  CB  A LYS   A 44  ? 0.1684 0.1345 0.2187 -0.0033 0.0272  0.0278  44  LYS   A CB  
1048 C  CB  B LYS   A 44  ? 0.1978 0.1942 0.2091 0.0034  0.0045  0.0080  44  LYS   A CB  
1049 C  CG  A LYS   A 44  ? 0.2004 0.1632 0.2866 -0.0126 0.0480  0.0361  44  LYS   A CG  
1050 C  CG  B LYS   A 44  ? 0.2121 0.2089 0.2496 0.0014  0.0094  0.0070  44  LYS   A CG  
1051 C  CD  A LYS   A 44  ? 0.2435 0.2226 0.3937 -0.0156 0.0349  0.0285  44  LYS   A CD  
1052 C  CD  B LYS   A 44  ? 0.2273 0.2268 0.2924 -0.0020 0.0082  0.0055  44  LYS   A CD  
1053 C  CE  A LYS   A 44  ? 0.2607 0.2583 0.4602 -0.0155 0.0297  0.0281  44  LYS   A CE  
1054 C  CE  B LYS   A 44  ? 0.2344 0.2379 0.3193 -0.0037 0.0073  0.0056  44  LYS   A CE  
1055 N  NZ  A LYS   A 44  ? 0.2652 0.2795 0.4911 -0.0170 0.0296  0.0284  44  LYS   A NZ  
1056 N  NZ  B LYS   A 44  ? 0.2366 0.2434 0.3309 -0.0060 0.0078  0.0040  44  LYS   A NZ  
1083 N  N   A HIS   A 45  ? 0.1196 0.1147 0.1554 0.0010  0.0034  0.0165  45  HIS   A N   
1084 N  N   B HIS   A 45  ? 0.1732 0.1646 0.1450 0.0093  -0.0040 0.0028  45  HIS   A N   
1085 C  CA  A HIS   A 45  ? 0.1173 0.1208 0.1530 0.0015  -0.0013 0.0131  45  HIS   A CA  
1086 C  CA  B HIS   A 45  ? 0.1693 0.1584 0.1467 0.0093  -0.0092 -0.0023 45  HIS   A CA  
1087 C  C   A HIS   A 45  ? 0.1220 0.1264 0.1634 -0.0002 0.0040  0.0100  45  HIS   A C   
1088 C  C   B HIS   A 45  ? 0.1713 0.1565 0.1526 0.0115  -0.0076 -0.0057 45  HIS   A C   
1089 O  O   A HIS   A 45  ? 0.1319 0.1303 0.1895 0.0105  -0.0037 -0.0074 45  HIS   A O   
1090 O  O   B HIS   A 45  ? 0.1745 0.1577 0.1591 0.0083  -0.0130 -0.0118 45  HIS   A O   
1091 C  CB  A HIS   A 45  ? 0.1226 0.1189 0.1452 0.0032  0.0032  0.0054  45  HIS   A CB  
1092 C  CB  B HIS   A 45  ? 0.1633 0.1553 0.1424 0.0101  -0.0128 -0.0031 45  HIS   A CB  
1093 C  CG  A HIS   A 45  ? 0.1179 0.1187 0.1283 -0.0064 0.0146  0.0095  45  HIS   A CG  
1094 C  CG  B HIS   A 45  ? 0.1550 0.1516 0.1319 0.0093  -0.0062 -0.0016 45  HIS   A CG  
1095 N  ND1 A HIS   A 45  ? 0.1125 0.1246 0.1512 -0.0024 0.0047  0.0130  45  HIS   A ND1 
1096 N  ND1 B HIS   A 45  ? 0.1499 0.1505 0.1386 0.0114  -0.0103 0.0030  45  HIS   A ND1 
1097 C  CD2 A HIS   A 45  ? 0.1202 0.1223 0.1504 -0.0123 0.0026  0.0213  45  HIS   A CD2 
1098 C  CD2 B HIS   A 45  ? 0.1513 0.1468 0.1282 0.0104  -0.0040 -0.0045 45  HIS   A CD2 
1099 C  CE1 A HIS   A 45  ? 0.1171 0.1257 0.1452 -0.0096 0.0040  0.0238  45  HIS   A CE1 
1100 C  CE1 B HIS   A 45  ? 0.1476 0.1435 0.1277 0.0105  -0.0087 -0.0026 45  HIS   A CE1 
1101 N  NE2 A HIS   A 45  ? 0.1218 0.1280 0.1465 -0.0061 -0.0019 0.0258  45  HIS   A NE2 
1102 N  NE2 B HIS   A 45  ? 0.1479 0.1438 0.1206 0.0101  -0.0050 -0.0068 45  HIS   A NE2 
1117 N  N   A GLY   A 46  ? 0.1385 0.1344 0.1796 0.0078  -0.0147 0.0149  46  GLY   A N   
1118 N  N   B GLY   A 46  ? 0.1706 0.1538 0.1506 0.0185  -0.0074 -0.0032 46  GLY   A N   
1119 C  CA  A GLY   A 46  ? 0.1419 0.1405 0.1938 0.0103  -0.0156 0.0121  46  GLY   A CA  
1120 C  CA  B GLY   A 46  ? 0.1674 0.1495 0.1454 0.0212  -0.0073 -0.0033 46  GLY   A CA  
1121 C  C   A GLY   A 46  ? 0.1494 0.1394 0.1988 0.0184  -0.0276 0.0242  46  GLY   A C   
1122 C  C   B GLY   A 46  ? 0.1632 0.1423 0.1295 0.0251  -0.0086 -0.0110 46  GLY   A C   
1123 O  O   A GLY   A 46  ? 0.1489 0.1471 0.2146 0.0214  -0.0382 0.0070  46  GLY   A O   
1124 O  O   B GLY   A 46  ? 0.1631 0.1427 0.1271 0.0311  -0.0017 -0.0139 46  GLY   A O   
1131 N  N   A GLY   A 47  ? 0.1494 0.1342 0.1950 0.0204  -0.0239 0.0203  47  GLY   A N   
1132 N  N   B GLY   A 47  ? 0.1586 0.1400 0.1383 0.0210  -0.0123 -0.0086 47  GLY   A N   
1133 C  CA  A GLY   A 47  ? 0.1532 0.1407 0.1962 0.0158  -0.0391 0.0051  47  GLY   A CA  
1134 C  CA  B GLY   A 47  ? 0.1564 0.1441 0.1470 0.0182  -0.0172 -0.0061 47  GLY   A CA  
1135 C  C   A GLY   A 47  ? 0.1483 0.1330 0.1823 0.0128  -0.0448 -0.0067 47  GLY   A C   
1136 C  C   B GLY   A 47  ? 0.1509 0.1444 0.1435 0.0165  -0.0185 -0.0130 47  GLY   A C   
1137 O  O   A GLY   A 47  ? 0.1454 0.1349 0.1912 0.0203  -0.0378 0.0116  47  GLY   A O   
1138 O  O   B GLY   A 47  ? 0.1528 0.1412 0.1498 0.0182  -0.0138 -0.0179 47  GLY   A O   
1145 N  N   A GLY   A 48  ? 0.1483 0.1377 0.1853 0.0158  -0.0536 -0.0032 48  GLY   A N   
1146 N  N   B GLY   A 48  ? 0.1452 0.1499 0.1434 0.0131  -0.0213 -0.0150 48  GLY   A N   
1147 C  CA  A GLY   A 48  ? 0.1425 0.1361 0.2003 0.0103  -0.0434 -0.0114 48  GLY   A CA  
1148 C  CA  B GLY   A 48  ? 0.1391 0.1523 0.1489 0.0096  -0.0163 -0.0157 48  GLY   A CA  
1149 C  C   A GLY   A 48  ? 0.1312 0.1351 0.1787 0.0051  -0.0203 -0.0082 48  GLY   A C   
1150 C  C   B GLY   A 48  ? 0.1313 0.1516 0.1412 0.0101  -0.0095 -0.0110 48  GLY   A C   
1151 O  O   A GLY   A 48  ? 0.1443 0.1326 0.1787 0.0077  -0.0210 -0.0103 48  GLY   A O   
1152 O  O   B GLY   A 48  ? 0.1336 0.1535 0.1405 0.0050  -0.0148 -0.0109 48  GLY   A O   
1159 N  N   A VAL   A 49  ? 0.1162 0.1300 0.1814 -0.0016 -0.0227 -0.0027 49  VAL   A N   
1160 N  N   B VAL   A 49  ? 0.1229 0.1472 0.1406 0.0085  -0.0042 -0.0111 49  VAL   A N   
1161 C  CA  A VAL   A 49  ? 0.1286 0.1248 0.1808 -0.0064 0.0054  -0.0034 49  VAL   A CA  
1162 C  CA  B VAL   A 49  ? 0.1095 0.1437 0.1365 0.0135  0.0022  -0.0044 49  VAL   A CA  
1163 C  C   A VAL   A 49  ? 0.1240 0.1113 0.1580 -0.0002 0.0028  0.0033  49  VAL   A C   
1164 C  C   B VAL   A 49  ? 0.1113 0.1357 0.1235 0.0173  0.0043  -0.0087 49  VAL   A C   
1165 O  O   A VAL   A 49  ? 0.1170 0.1208 0.1578 -0.0005 0.0136  0.0011  49  VAL   A O   
1166 O  O   B VAL   A 49  ? 0.1110 0.1333 0.1215 0.0294  0.0102  -0.0072 49  VAL   A O   
1167 C  CB  A VAL   A 49  ? 0.1507 0.1286 0.2039 -0.0113 0.0064  -0.0036 49  VAL   A CB  
1168 C  CB  B VAL   A 49  ? 0.0977 0.1400 0.1349 0.0198  0.0029  0.0046  49  VAL   A CB  
1169 C  CG1 A VAL   A 49  ? 0.1635 0.1261 0.2204 -0.0036 0.0110  0.0010  49  VAL   A CG1 
1170 C  CG1 B VAL   A 49  ? 0.0901 0.1367 0.1245 0.0306  -0.0017 0.0122  49  VAL   A CG1 
1171 C  CG2 A VAL   A 49  ? 0.1649 0.1484 0.2437 -0.0287 0.0019  -0.0047 49  VAL   A CG2 
1172 C  CG2 B VAL   A 49  ? 0.0975 0.1412 0.1353 0.0198  0.0123  0.0068  49  VAL   A CG2 
1191 N  N   A ALA   A 50  ? 0.1226 0.1159 0.1457 -0.0055 -0.0132 0.0134  50  ALA   A N   
1192 N  N   B ALA   A 50  ? 0.1169 0.1316 0.1144 0.0135  0.0026  -0.0147 50  ALA   A N   
1193 C  CA  A ALA   A 50  ? 0.1176 0.1168 0.1513 -0.0101 -0.0024 0.0178  50  ALA   A CA  
1194 C  CA  B ALA   A 50  ? 0.1220 0.1262 0.1148 0.0061  -0.0032 -0.0160 50  ALA   A CA  
1195 C  C   A ALA   A 50  ? 0.1147 0.1226 0.1499 -0.0098 -0.0047 0.0141  50  ALA   A C   
1196 C  C   B ALA   A 50  ? 0.1243 0.1249 0.1090 0.0047  -0.0062 -0.0228 50  ALA   A C   
1197 O  O   A ALA   A 50  ? 0.1197 0.1223 0.1637 -0.0027 -0.0082 0.0161  50  ALA   A O   
1198 O  O   B ALA   A 50  ? 0.1213 0.1238 0.1068 0.0069  -0.0074 -0.0192 50  ALA   A O   
1199 C  CB  A ALA   A 50  ? 0.1180 0.1142 0.1531 -0.0074 -0.0023 0.0072  50  ALA   A CB  
1200 C  CB  B ALA   A 50  ? 0.1253 0.1215 0.1192 0.0056  0.0040  -0.0219 50  ALA   A CB  
1211 N  N   A GLY   A 51  ? 0.1148 0.1140 0.1601 0.0031  -0.0132 0.0126  51  GLY   A N   
1212 N  N   B GLY   A 51  ? 0.1259 0.1212 0.1149 0.0054  -0.0086 -0.0353 51  GLY   A N   
1213 C  CA  A GLY   A 51  ? 0.1330 0.1127 0.1689 0.0021  -0.0167 0.0105  51  GLY   A CA  
1214 C  CA  B GLY   A 51  ? 0.1286 0.1212 0.1125 0.0075  -0.0091 -0.0399 51  GLY   A CA  
1215 C  C   A GLY   A 51  ? 0.1237 0.1239 0.1671 0.0077  -0.0094 -0.0065 51  GLY   A C   
1216 C  C   B GLY   A 51  ? 0.1268 0.1266 0.1233 0.0097  -0.0013 -0.0351 51  GLY   A C   
1217 O  O   A GLY   A 51  ? 0.1314 0.1301 0.1747 0.0003  -0.0074 -0.0081 51  GLY   A O   
1218 O  O   B GLY   A 51  ? 0.1323 0.1273 0.1243 0.0098  -0.0004 -0.0368 51  GLY   A O   
1225 N  N   A ALA   A 52  ? 0.1234 0.1326 0.1626 0.0049  -0.0029 -0.0072 52  ALA   A N   
1226 N  N   B ALA   A 52  ? 0.1260 0.1317 0.1339 0.0052  0.0079  -0.0271 52  ALA   A N   
1227 C  CA  A ALA   A 52  ? 0.1229 0.1404 0.1756 -0.0010 0.0013  -0.0067 52  ALA   A CA  
1228 C  CA  B ALA   A 52  ? 0.1205 0.1336 0.1447 0.0018  0.0108  -0.0231 52  ALA   A CA  
1229 C  C   A ALA   A 52  ? 0.1236 0.1410 0.1433 -0.0085 0.0029  -0.0101 52  ALA   A C   
1230 C  C   B ALA   A 52  ? 0.1187 0.1336 0.1397 -0.0039 0.0115  -0.0167 52  ALA   A C   
1231 O  O   A ALA   A 52  ? 0.1359 0.1456 0.1733 -0.0024 0.0066  -0.0174 52  ALA   A O   
1232 O  O   B ALA   A 52  ? 0.1220 0.1317 0.1519 -0.0045 0.0160  -0.0182 52  ALA   A O   
1233 C  CB  A ALA   A 52  ? 0.1326 0.1583 0.2054 -0.0003 -0.0031 -0.0095 52  ALA   A CB  
1234 C  CB  B ALA   A 52  ? 0.1187 0.1389 0.1564 0.0027  0.0076  -0.0239 52  ALA   A CB  
1245 N  N   A LEU   A 53  ? 0.1222 0.1367 0.1452 -0.0061 -0.0033 -0.0079 53  LEU   A N   
1246 N  N   B LEU   A 53  ? 0.1155 0.1326 0.1340 -0.0023 0.0074  -0.0119 53  LEU   A N   
1247 C  CA  A LEU   A 53  ? 0.1310 0.1434 0.1380 -0.0099 0.0028  0.0016  53  LEU   A CA  
1248 C  CA  B LEU   A 53  ? 0.1116 0.1328 0.1239 -0.0036 0.0048  -0.0067 53  LEU   A CA  
1249 C  C   A LEU   A 53  ? 0.1310 0.1421 0.1192 -0.0008 0.0032  0.0044  53  LEU   A C   
1250 C  C   B LEU   A 53  ? 0.1155 0.1342 0.1193 -0.0031 0.0111  -0.0039 53  LEU   A C   
1251 O  O   A LEU   A 53  ? 0.1469 0.1543 0.1389 -0.0105 0.0022  0.0011  53  LEU   A O   
1252 O  O   B LEU   A 53  ? 0.1170 0.1383 0.1250 -0.0082 0.0101  -0.0025 53  LEU   A O   
1253 C  CB  A LEU   A 53  ? 0.1361 0.1474 0.1422 -0.0091 0.0062  0.0167  53  LEU   A CB  
1254 C  CB  B LEU   A 53  ? 0.1055 0.1300 0.1197 -0.0049 -0.0029 -0.0095 53  LEU   A CB  
1255 C  CG  A LEU   A 53  ? 0.1446 0.1447 0.1495 -0.0088 0.0077  0.0127  53  LEU   A CG  
1256 C  CG  B LEU   A 53  ? 0.1004 0.1271 0.1180 -0.0068 -0.0117 -0.0160 53  LEU   A CG  
1257 C  CD1 A LEU   A 53  ? 0.1451 0.1461 0.1581 -0.0016 0.0018  0.0180  53  LEU   A CD1 
1258 C  CD1 B LEU   A 53  ? 0.0988 0.1315 0.1175 -0.0043 -0.0045 -0.0204 53  LEU   A CD1 
1259 C  CD2 A LEU   A 53  ? 0.1699 0.1576 0.1743 -0.0226 0.0063  0.0190  53  LEU   A CD2 
1260 C  CD2 B LEU   A 53  ? 0.0969 0.1213 0.1202 -0.0115 -0.0081 -0.0185 53  LEU   A CD2 
1283 N  N   A ASN   A 54  ? 0.1255 0.1344 0.1211 -0.0037 -0.0023 0.0048  54  ASN   A N   
1284 N  N   B ASN   A 54  ? 0.1169 0.1346 0.1232 -0.0034 0.0083  -0.0014 54  ASN   A N   
1285 C  CA  A ASN   A 54  ? 0.1137 0.1281 0.1367 -0.0040 -0.0052 -0.0009 54  ASN   A CA  
1286 C  CA  B ASN   A 54  ? 0.1168 0.1344 0.1278 -0.0034 0.0032  -0.0009 54  ASN   A CA  
1287 C  C   A ASN   A 54  ? 0.1239 0.1369 0.1497 -0.0089 -0.0072 0.0001  54  ASN   A C   
1288 C  C   B ASN   A 54  ? 0.1215 0.1346 0.1383 -0.0057 -0.0015 -0.0023 54  ASN   A C   
1289 O  O   A ASN   A 54  ? 0.1280 0.1409 0.1509 -0.0065 -0.0080 -0.0033 54  ASN   A O   
1290 O  O   B ASN   A 54  ? 0.1222 0.1333 0.1357 -0.0038 -0.0045 -0.0014 54  ASN   A O   
1291 C  CB  A ASN   A 54  ? 0.1124 0.1250 0.1622 -0.0036 -0.0074 -0.0053 54  ASN   A CB  
1292 C  CB  B ASN   A 54  ? 0.1188 0.1356 0.1321 0.0009  0.0026  0.0030  54  ASN   A CB  
1293 C  CG  A ASN   A 54  ? 0.1152 0.1251 0.1624 -0.0059 -0.0034 -0.0013 54  ASN   A CG  
1294 C  CG  B ASN   A 54  ? 0.1213 0.1371 0.1335 0.0034  0.0015  0.0068  54  ASN   A CG  
1295 O  OD1 A ASN   A 54  ? 0.1155 0.1260 0.1478 -0.0031 -0.0037 0.0099  54  ASN   A OD1 
1296 O  OD1 B ASN   A 54  ? 0.1219 0.1421 0.1450 0.0013  0.0009  0.0070  54  ASN   A OD1 
1297 N  ND2 A ASN   A 54  ? 0.1141 0.1314 0.1737 -0.0066 -0.0096 0.0055  54  ASN   A ND2 
1298 N  ND2 B ASN   A 54  ? 0.1247 0.1343 0.1301 0.0050  -0.0011 0.0100  54  ASN   A ND2 
1311 N  N   . LYS   A 55  ? 0.1254 0.1335 0.1582 -0.0057 -0.0026 -0.0123 55  LYS   A N   
1312 C  CA  . LYS   A 55  ? 0.1315 0.1394 0.1638 -0.0000 -0.0114 -0.0202 55  LYS   A CA  
1313 C  C   . LYS   A 55  ? 0.1303 0.1480 0.1574 -0.0011 0.0001  -0.0196 55  LYS   A C   
1314 O  O   . LYS   A 55  ? 0.1445 0.1589 0.1658 0.0012  -0.0029 -0.0274 55  LYS   A O   
1315 C  CB  . LYS   A 55  ? 0.1418 0.1451 0.1812 0.0138  -0.0038 -0.0229 55  LYS   A CB  
1316 C  CG  . LYS   A 55  ? 0.1525 0.1682 0.1880 0.0205  -0.0091 -0.0273 55  LYS   A CG  
1317 C  CD  . LYS   A 55  ? 0.1621 0.1878 0.2084 0.0314  -0.0011 -0.0249 55  LYS   A CD  
1318 C  CE  . LYS   A 55  ? 0.1834 0.2145 0.2351 0.0363  -0.0182 -0.0241 55  LYS   A CE  
1319 N  NZ  . LYS   A 55  ? 0.1871 0.2234 0.2426 0.0425  -0.0168 -0.0262 55  LYS   A NZ  
1334 N  N   . ALA   A 56  ? 0.1378 0.1586 0.1573 -0.0086 0.0086  -0.0229 56  ALA   A N   
1335 C  CA  . ALA   A 56  ? 0.1534 0.1765 0.1554 -0.0124 0.0083  -0.0154 56  ALA   A CA  
1336 C  C   . ALA   A 56  ? 0.1563 0.1862 0.1319 -0.0139 0.0160  -0.0221 56  ALA   A C   
1337 O  O   . ALA   A 56  ? 0.1618 0.2147 0.1478 0.0007  0.0172  -0.0165 56  ALA   A O   
1338 C  CB  . ALA   A 56  ? 0.1569 0.1920 0.1620 -0.0157 0.0131  -0.0052 56  ALA   A CB  
1344 N  N   . THR   A 57  ? 0.1397 0.1664 0.1367 -0.0075 0.0070  -0.0188 57  THR   A N   
1345 C  CA  . THR   A 57  ? 0.1446 0.1604 0.1420 -0.0079 -0.0046 -0.0115 57  THR   A CA  
1346 C  C   . THR   A 57  ? 0.1419 0.1638 0.1522 -0.0036 -0.0052 -0.0178 57  THR   A C   
1347 O  O   . THR   A 57  ? 0.1402 0.1706 0.1719 -0.0073 -0.0061 -0.0334 57  THR   A O   
1348 C  CB  . THR   A 57  ? 0.1394 0.1590 0.1380 -0.0079 0.0060  -0.0113 57  THR   A CB  
1349 O  OG1 . THR   A 57  ? 0.1356 0.1567 0.1518 -0.0035 0.0047  -0.0124 57  THR   A OG1 
1350 C  CG2 . THR   A 57  ? 0.1501 0.1601 0.1261 -0.0025 -0.0030 -0.0070 57  THR   A CG2 
1358 N  N   . ASN   A 58  ? 0.1449 0.1583 0.1612 -0.0064 0.0031  -0.0313 58  ASN   A N   
1359 C  CA  . ASN   A 58  ? 0.1669 0.1541 0.1860 -0.0105 0.0090  -0.0351 58  ASN   A CA  
1360 C  C   . ASN   A 58  ? 0.1416 0.1420 0.1803 0.0033  0.0007  -0.0223 58  ASN   A C   
1361 O  O   . ASN   A 58  ? 0.1416 0.1584 0.1974 -0.0142 -0.0043 -0.0284 58  ASN   A O   
1362 C  CB  . ASN   A 58  ? 0.2129 0.1718 0.2111 -0.0219 0.0359  -0.0472 58  ASN   A CB  
1363 C  CG  . ASN   A 58  ? 0.2579 0.1989 0.2829 -0.0174 0.0358  -0.0372 58  ASN   A CG  
1364 O  OD1 . ASN   A 58  ? 0.2842 0.1943 0.3211 0.0202  0.0654  -0.0352 58  ASN   A OD1 
1365 N  ND2 . ASN   A 58  ? 0.2708 0.2099 0.3083 -0.0202 0.0184  -0.0444 58  ASN   A ND2 
1372 N  N   . ASN   A 59  ? 0.1321 0.1402 0.1667 -0.0034 -0.0065 -0.0094 59  ASN   A N   
1373 C  CA  . ASN   A 59  ? 0.1292 0.1307 0.1711 -0.0065 -0.0046 -0.0093 59  ASN   A CA  
1374 C  C   . ASN   A 59  ? 0.1304 0.1352 0.1579 -0.0053 -0.0071 -0.0043 59  ASN   A C   
1375 O  O   . ASN   A 59  ? 0.1267 0.1358 0.1651 -0.0034 -0.0019 0.0006  59  ASN   A O   
1376 C  CB  . ASN   A 59  ? 0.1335 0.1317 0.1774 0.0032  -0.0116 -0.0132 59  ASN   A CB  
1377 C  CG  . ASN   A 59  ? 0.1372 0.1361 0.1775 -0.0021 -0.0251 -0.0023 59  ASN   A CG  
1378 O  OD1 . ASN   A 59  ? 0.1481 0.1429 0.1733 -0.0114 -0.0296 0.0050  59  ASN   A OD1 
1379 N  ND2 . ASN   A 59  ? 0.1438 0.1388 0.1799 -0.0098 -0.0181 0.0072  59  ASN   A ND2 
1386 N  N   . ALA   A 60  ? 0.1279 0.1390 0.1572 -0.0011 -0.0081 -0.0062 60  ALA   A N   
1387 C  CA  . ALA   A 60  ? 0.1298 0.1365 0.1699 -0.0038 -0.0069 -0.0077 60  ALA   A CA  
1388 C  C   . ALA   A 60  ? 0.1272 0.1320 0.1742 -0.0039 -0.0034 -0.0075 60  ALA   A C   
1389 O  O   . ALA   A 60  ? 0.1196 0.1358 0.1862 -0.0023 -0.0074 -0.0048 60  ALA   A O   
1390 C  CB  . ALA   A 60  ? 0.1426 0.1500 0.1592 -0.0042 -0.0098 -0.0211 60  ALA   A CB  
1396 N  N   . MET   A 61  ? 0.1234 0.1270 0.1619 -0.0072 -0.0042 -0.0090 61  MET   A N   
1397 C  CA  . MET   A 61  ? 0.1264 0.1245 0.1627 -0.0085 0.0042  -0.0004 61  MET   A CA  
1398 C  C   . MET   A 61  ? 0.1184 0.1175 0.1631 -0.0071 -0.0035 -0.0034 61  MET   A C   
1399 O  O   . MET   A 61  ? 0.1274 0.1218 0.1632 -0.0039 0.0059  0.0012  61  MET   A O   
1400 C  CB  . MET   A 61  ? 0.1322 0.1281 0.1523 -0.0036 0.0017  -0.0017 61  MET   A CB  
1401 C  CG  . MET   A 61  ? 0.1301 0.1364 0.1660 -0.0005 0.0028  -0.0053 61  MET   A CG  
1402 S  SD  . MET   A 61  ? 0.1311 0.1359 0.1828 -0.0129 0.0032  -0.0176 61  MET   A SD  
1403 C  CE  . MET   A 61  ? 0.1509 0.1558 0.2106 -0.0121 0.0181  -0.0180 61  MET   A CE  
1413 N  N   . GLN   A 62  ? 0.1199 0.1181 0.1611 -0.0091 -0.0036 -0.0039 62  GLN   A N   
1414 C  CA  . GLN   A 62  ? 0.1273 0.1197 0.1625 -0.0043 0.0064  -0.0013 62  GLN   A CA  
1415 C  C   . GLN   A 62  ? 0.1293 0.1154 0.1701 -0.0024 0.0063  0.0024  62  GLN   A C   
1416 O  O   . GLN   A 62  ? 0.1293 0.1286 0.1728 -0.0018 0.0054  0.0075  62  GLN   A O   
1417 C  CB  . GLN   A 62  ? 0.1251 0.1176 0.1646 -0.0032 0.0055  -0.0003 62  GLN   A CB  
1418 C  CG  . GLN   A 62  ? 0.1329 0.1125 0.1578 -0.0012 -0.0033 0.0118  62  GLN   A CG  
1419 C  CD  . GLN   A 62  ? 0.1368 0.1213 0.1596 -0.0006 0.0039  0.0133  62  GLN   A CD  
1420 O  OE1 . GLN   A 62  ? 0.1385 0.1350 0.1659 -0.0063 0.0024  0.0019  62  GLN   A OE1 
1421 N  NE2 . GLN   A 62  ? 0.1417 0.1255 0.1756 0.0047  0.0018  -0.0059 62  GLN   A NE2 
1430 N  N   . VAL   A 63  ? 0.1246 0.1210 0.1776 -0.0057 0.0080  -0.0147 63  VAL   A N   
1431 C  CA  . VAL   A 63  ? 0.1260 0.1289 0.2020 -0.0125 -0.0014 -0.0212 63  VAL   A CA  
1432 C  C   . VAL   A 63  ? 0.1124 0.1260 0.1983 -0.0150 -0.0119 -0.0128 63  VAL   A C   
1433 O  O   . VAL   A 63  ? 0.1190 0.1279 0.2065 -0.0153 -0.0040 -0.0066 63  VAL   A O   
1434 C  CB  . VAL   A 63  ? 0.1427 0.1493 0.2319 -0.0133 -0.0033 -0.0393 63  VAL   A CB  
1435 C  CG1 . VAL   A 63  ? 0.1550 0.1681 0.2685 -0.0129 -0.0087 -0.0597 63  VAL   A CG1 
1436 C  CG2 . VAL   A 63  ? 0.1535 0.1430 0.2458 -0.0154 0.0119  -0.0427 63  VAL   A CG2 
1446 N  N   . GLU   A 64  ? 0.1223 0.1325 0.1837 -0.0035 -0.0047 -0.0068 64  GLU   A N   
1447 C  CA  . GLU   A 64  ? 0.1198 0.1322 0.1812 -0.0107 -0.0034 -0.0063 64  GLU   A CA  
1448 C  C   . GLU   A 64  ? 0.1151 0.1257 0.1757 -0.0134 0.0032  -0.0032 64  GLU   A C   
1449 O  O   . GLU   A 64  ? 0.1256 0.1339 0.1805 -0.0053 0.0079  -0.0065 64  GLU   A O   
1450 C  CB  . GLU   A 64  ? 0.1301 0.1427 0.1831 -0.0091 0.0016  -0.0032 64  GLU   A CB  
1451 C  CG  . GLU   A 64  ? 0.1414 0.1458 0.1881 -0.0126 -0.0002 -0.0032 64  GLU   A CG  
1452 C  CD  . GLU   A 64  ? 0.1463 0.1515 0.1944 -0.0169 0.0053  -0.0019 64  GLU   A CD  
1453 O  OE1 . GLU   A 64  ? 0.1409 0.1609 0.2060 -0.0224 0.0126  -0.0060 64  GLU   A OE1 
1454 O  OE2 . GLU   A 64  ? 0.1614 0.1557 0.1834 -0.0233 -0.0027 -0.0002 64  GLU   A OE2 
1461 N  N   . SER   A 65  ? 0.1153 0.1284 0.1712 -0.0052 0.0046  -0.0044 65  SER   A N   
1462 C  CA  . SER   A 65  ? 0.1225 0.1221 0.1612 -0.0065 -0.0031 -0.0051 65  SER   A CA  
1463 C  C   . SER   A 65  ? 0.1241 0.1288 0.1683 -0.0027 -0.0041 -0.0013 65  SER   A C   
1464 O  O   . SER   A 65  ? 0.1312 0.1345 0.1811 0.0005  0.0134  -0.0027 65  SER   A O   
1465 C  CB  . SER   A 65  ? 0.1278 0.1247 0.1649 -0.0120 0.0070  0.0047  65  SER   A CB  
1466 O  OG  . SER   A 65  ? 0.1249 0.1361 0.1692 -0.0100 -0.0054 0.0086  65  SER   A OG  
1472 N  N   . ASP   A 66  ? 0.1236 0.1208 0.1779 -0.0058 0.0150  0.0055  66  ASP   A N   
1473 C  CA  . ASP   A 66  ? 0.1350 0.1361 0.1893 -0.0013 0.0093  0.0148  66  ASP   A CA  
1474 C  C   . ASP   A 66  ? 0.1298 0.1348 0.1970 -0.0059 0.0156  0.0173  66  ASP   A C   
1475 O  O   . ASP   A 66  ? 0.1368 0.1451 0.2132 -0.0050 0.0245  0.0198  66  ASP   A O   
1476 C  CB  . ASP   A 66  ? 0.1398 0.1465 0.2130 0.0046  0.0117  0.0328  66  ASP   A CB  
1477 C  CG  . ASP   A 66  ? 0.1636 0.1596 0.2385 0.0048  -0.0004 0.0440  66  ASP   A CG  
1478 O  OD1 . ASP   A 66  ? 0.1631 0.1845 0.2241 -0.0057 -0.0075 0.0540  66  ASP   A OD1 
1479 O  OD2 . ASP   A 66  ? 0.1802 0.1734 0.3134 0.0256  -0.0171 0.0240  66  ASP   A OD2 
1484 N  N   . ASP   A 67  ? 0.1180 0.1356 0.2033 -0.0046 0.0131  0.0164  67  ASP   A N   
1485 C  CA  . ASP   A 67  ? 0.1260 0.1580 0.2105 -0.0042 0.0076  0.0210  67  ASP   A CA  
1486 C  C   . ASP   A 67  ? 0.1263 0.1575 0.2058 -0.0027 0.0083  0.0237  67  ASP   A C   
1487 O  O   . ASP   A 67  ? 0.1258 0.1636 0.2247 -0.0003 0.0243  0.0294  67  ASP   A O   
1488 C  CB  . ASP   A 67  ? 0.1345 0.1638 0.2417 -0.0074 -0.0143 0.0312  67  ASP   A CB  
1489 C  CG  . ASP   A 67  ? 0.1372 0.1779 0.2742 -0.0093 -0.0272 0.0350  67  ASP   A CG  
1490 O  OD1 . ASP   A 67  ? 0.1402 0.1928 0.3548 -0.0141 -0.0355 0.0466  67  ASP   A OD1 
1491 O  OD2 . ASP   A 67  ? 0.1345 0.1786 0.2613 0.0036  -0.0179 0.0302  67  ASP   A OD2 
1496 N  N   . TYR   A 68  ? 0.1284 0.1407 0.1882 -0.0028 0.0225  0.0240  68  TYR   A N   
1497 C  CA  . TYR   A 68  ? 0.1413 0.1391 0.1890 -0.0006 0.0227  0.0224  68  TYR   A CA  
1498 C  C   . TYR   A 68  ? 0.1353 0.1383 0.1898 0.0035  0.0217  0.0178  68  TYR   A C   
1499 O  O   . TYR   A 68  ? 0.1415 0.1359 0.2040 0.0088  0.0305  0.0153  68  TYR   A O   
1500 C  CB  . TYR   A 68  ? 0.1437 0.1363 0.1982 0.0080  0.0393  0.0276  68  TYR   A CB  
1501 C  CG  . TYR   A 68  ? 0.1439 0.1547 0.2236 0.0064  0.0553  0.0288  68  TYR   A CG  
1502 C  CD1 . TYR   A 68  ? 0.1597 0.1643 0.2546 -0.0195 0.0414  -0.0051 68  TYR   A CD1 
1503 C  CD2 . TYR   A 68  ? 0.1679 0.1569 0.2754 0.0115  0.0574  0.0337  68  TYR   A CD2 
1504 C  CE1 . TYR   A 68  ? 0.1640 0.1741 0.2972 -0.0179 0.0429  -0.0172 68  TYR   A CE1 
1505 C  CE2 . TYR   A 68  ? 0.1627 0.1597 0.2965 0.0026  0.0695  0.0129  68  TYR   A CE2 
1506 C  CZ  . TYR   A 68  ? 0.1657 0.1639 0.3091 -0.0169 0.0553  -0.0145 68  TYR   A CZ  
1507 O  OH  . TYR   A 68  ? 0.1957 0.1618 0.3274 -0.0115 0.0301  -0.0379 68  TYR   A OH  
1517 N  N   . ILE   A 69  ? 0.1305 0.1299 0.1878 0.0008  0.0181  0.0168  69  ILE   A N   
1518 C  CA  . ILE   A 69  ? 0.1374 0.1362 0.1869 0.0042  0.0097  0.0032  69  ILE   A CA  
1519 C  C   . ILE   A 69  ? 0.1340 0.1376 0.1804 0.0042  0.0202  0.0185  69  ILE   A C   
1520 O  O   . ILE   A 69  ? 0.1456 0.1480 0.1745 -0.0008 0.0221  0.0234  69  ILE   A O   
1521 C  CB  . ILE   A 69  ? 0.1428 0.1590 0.1858 0.0102  0.0101  -0.0064 69  ILE   A CB  
1522 C  CG1 . ILE   A 69  ? 0.1443 0.1724 0.1940 0.0060  0.0142  -0.0114 69  ILE   A CG1 
1523 C  CG2 . ILE   A 69  ? 0.1617 0.1748 0.2021 0.0167  -0.0001 -0.0165 69  ILE   A CG2 
1524 C  CD1 . ILE   A 69  ? 0.1429 0.1827 0.2020 -0.0027 0.0187  -0.0124 69  ILE   A CD1 
1536 N  N   . ALA   A 70  ? 0.1385 0.1366 0.1937 -0.0035 0.0219  0.0141  70  ALA   A N   
1537 C  CA  . ALA   A 70  ? 0.1456 0.1508 0.2112 -0.0117 0.0252  0.0238  70  ALA   A CA  
1538 C  C   . ALA   A 70  ? 0.1440 0.1698 0.1985 -0.0119 0.0279  0.0264  70  ALA   A C   
1539 O  O   . ALA   A 70  ? 0.1620 0.2011 0.2211 0.0059  0.0466  0.0360  70  ALA   A O   
1540 C  CB  . ALA   A 70  ? 0.1433 0.1489 0.2280 -0.0167 0.0232  0.0148  70  ALA   A CB  
1546 N  N   . THR   A 71  ? 0.1377 0.1636 0.1962 -0.0029 0.0203  0.0234  71  THR   A N   
1547 C  CA  . THR   A 71  ? 0.1503 0.1784 0.2203 0.0066  0.0257  0.0226  71  THR   A CA  
1548 C  C   . THR   A 71  ? 0.1403 0.1696 0.2411 0.0122  0.0343  0.0228  71  THR   A C   
1549 O  O   . THR   A 71  ? 0.1444 0.1976 0.2825 0.0090  0.0464  -0.0030 71  THR   A O   
1550 C  CB  . THR   A 71  ? 0.1793 0.2038 0.2366 0.0174  -0.0085 0.0263  71  THR   A CB  
1551 O  OG1 . THR   A 71  ? 0.1991 0.2233 0.2487 0.0080  -0.0265 0.0234  71  THR   A OG1 
1552 C  CG2 . THR   A 71  ? 0.1919 0.2185 0.2569 0.0238  -0.0183 0.0344  71  THR   A CG2 
1560 N  N   . ASN   A 72  ? 0.1425 0.1527 0.2276 0.0146  0.0248  0.0238  72  ASN   A N   
1561 C  CA  . ASN   A 72  ? 0.1499 0.1564 0.2229 0.0159  0.0338  0.0242  72  ASN   A CA  
1562 C  C   . ASN   A 72  ? 0.1620 0.1564 0.2141 0.0140  0.0439  0.0154  72  ASN   A C   
1563 O  O   . ASN   A 72  ? 0.1775 0.1600 0.2467 0.0213  0.0413  0.0014  72  ASN   A O   
1564 C  CB  . ASN   A 72  ? 0.1727 0.1587 0.2220 0.0151  0.0416  0.0176  72  ASN   A CB  
1565 C  CG  . ASN   A 72  ? 0.1929 0.1723 0.2206 0.0245  0.0423  0.0249  72  ASN   A CG  
1566 O  OD1 . ASN   A 72  ? 0.2117 0.2060 0.2328 0.0248  0.0401  0.0269  72  ASN   A OD1 
1567 N  ND2 . ASN   A 72  ? 0.2084 0.1755 0.2262 0.0426  0.0280  0.0109  72  ASN   A ND2 
1574 N  N   . GLY   A 73  ? 0.1619 0.1503 0.2022 0.0059  0.0413  0.0106  73  GLY   A N   
1575 C  CA  . GLY   A 73  ? 0.1652 0.1479 0.1909 -0.0068 0.0440  0.0098  73  GLY   A CA  
1576 C  C   . GLY   A 73  ? 0.1706 0.1401 0.1797 -0.0006 0.0492  0.0206  73  GLY   A C   
1577 O  O   . GLY   A 73  ? 0.1677 0.1466 0.1947 0.0131  0.0368  0.0241  73  GLY   A O   
1581 N  N   . PRO   A 74  ? 0.1766 0.1457 0.1867 -0.0153 0.0490  0.0095  74  PRO   A N   
1582 C  CA  . PRO   A 74  ? 0.1727 0.1411 0.1892 -0.0026 0.0463  0.0160  74  PRO   A CA  
1583 C  C   . PRO   A 74  ? 0.1675 0.1258 0.1883 0.0048  0.0290  0.0024  74  PRO   A C   
1584 O  O   . PRO   A 74  ? 0.1753 0.1327 0.2124 0.0060  0.0319  -0.0104 74  PRO   A O   
1585 C  CB  . PRO   A 74  ? 0.1851 0.1714 0.2154 0.0001  0.0472  0.0238  74  PRO   A CB  
1586 C  CG  . PRO   A 74  ? 0.2083 0.2041 0.2564 -0.0139 0.0350  0.0133  74  PRO   A CG  
1587 C  CD  . PRO   A 74  ? 0.1925 0.1804 0.2054 -0.0215 0.0390  0.0070  74  PRO   A CD  
1595 N  N   . LEU   A 75  ? 0.1605 0.1224 0.1786 0.0020  0.0284  0.0046  75  LEU   A N   
1596 C  CA  . LEU   A 75  ? 0.1636 0.1256 0.1546 0.0009  0.0106  0.0083  75  LEU   A CA  
1597 C  C   . LEU   A 75  ? 0.1719 0.1395 0.1523 0.0063  0.0122  0.0149  75  LEU   A C   
1598 O  O   . LEU   A 75  ? 0.2070 0.1566 0.1527 0.0121  0.0066  0.0040  75  LEU   A O   
1599 C  CB  . LEU   A 75  ? 0.1700 0.1310 0.1464 -0.0108 0.0131  0.0182  75  LEU   A CB  
1600 C  CG  . LEU   A 75  ? 0.1892 0.1639 0.1624 -0.0399 0.0084  0.0129  75  LEU   A CG  
1601 C  CD1 . LEU   A 75  ? 0.2006 0.2130 0.1711 -0.0363 0.0031  -0.0016 75  LEU   A CD1 
1602 C  CD2 . LEU   A 75  ? 0.2172 0.2112 0.2182 -0.0176 0.0101  0.0130  75  LEU   A CD2 
1614 N  N   . LYS   A 76  ? 0.1733 0.1367 0.1735 -0.0057 0.0141  0.0006  76  LYS   A N   
1615 C  CA  . LYS   A 76  ? 0.1706 0.1578 0.1778 -0.0058 0.0110  -0.0137 76  LYS   A CA  
1616 C  C   . LYS   A 76  ? 0.1640 0.1408 0.1507 -0.0028 0.0137  0.0038  76  LYS   A C   
1617 O  O   . LYS   A 76  ? 0.1621 0.1331 0.1521 -0.0011 0.0139  0.0063  76  LYS   A O   
1618 C  CB  . LYS   A 76  ? 0.1712 0.1819 0.2127 0.0068  0.0113  -0.0398 76  LYS   A CB  
1619 C  CG  . LYS   A 76  ? 0.1817 0.1743 0.2685 0.0092  0.0095  -0.0345 76  LYS   A CG  
1620 C  CD  . LYS   A 76  ? 0.1915 0.1751 0.3128 0.0110  0.0071  -0.0376 76  LYS   A CD  
1621 C  CE  . LYS   A 76  ? 0.2033 0.1918 0.3650 -0.0005 0.0150  -0.0431 76  LYS   A CE  
1622 N  NZ  . LYS   A 76  ? 0.2015 0.1903 0.4040 -0.0133 0.0113  -0.0508 76  LYS   A NZ  
1636 N  N   . VAL   A 77  ? 0.1772 0.1389 0.1430 -0.0025 0.0251  0.0104  77  VAL   A N   
1637 C  CA  . VAL   A 77  ? 0.1714 0.1443 0.1418 0.0056  0.0195  0.0094  77  VAL   A CA  
1638 C  C   . VAL   A 77  ? 0.1636 0.1390 0.1494 0.0099  0.0085  0.0052  77  VAL   A C   
1639 O  O   . VAL   A 77  ? 0.1691 0.1427 0.1490 0.0142  0.0194  -0.0034 77  VAL   A O   
1640 C  CB  . VAL   A 77  ? 0.1893 0.1624 0.1584 0.0080  0.0164  0.0175  77  VAL   A CB  
1641 C  CG1 . VAL   A 77  ? 0.1831 0.1742 0.1856 0.0169  0.0015  0.0083  77  VAL   A CG1 
1642 C  CG2 . VAL   A 77  ? 0.2151 0.1727 0.1743 -0.0002 0.0032  0.0226  77  VAL   A CG2 
1652 N  N   . GLY   A 78  ? 0.1586 0.1352 0.1484 0.0044  0.0201  0.0076  78  GLY   A N   
1653 C  CA  . GLY   A 78  ? 0.1540 0.1311 0.1549 0.0016  0.0248  0.0083  78  GLY   A CA  
1654 C  C   . GLY   A 78  ? 0.1441 0.1285 0.1559 0.0034  0.0200  0.0027  78  GLY   A C   
1655 O  O   . GLY   A 78  ? 0.1444 0.1320 0.1797 0.0026  0.0182  0.0263  78  GLY   A O   
1659 N  N   . GLY   A 79  ? 0.1510 0.1255 0.1524 0.0042  0.0161  0.0171  79  GLY   A N   
1660 C  CA  . GLY   A 79  ? 0.1493 0.1268 0.1618 -0.0007 0.0152  0.0130  79  GLY   A CA  
1661 C  C   . GLY   A 79  ? 0.1344 0.1222 0.1601 0.0026  0.0097  0.0037  79  GLY   A C   
1662 O  O   . GLY   A 79  ? 0.1395 0.1339 0.1650 0.0197  0.0104  0.0039  79  GLY   A O   
1666 N  N   . SER   A 80  ? 0.1276 0.1309 0.1794 -0.0014 0.0159  -0.0008 80  SER   A N   
1667 C  CA  . SER   A 80  ? 0.1248 0.1274 0.1646 0.0028  0.0055  -0.0018 80  SER   A CA  
1668 C  C   . SER   A 80  ? 0.1245 0.1332 0.1630 -0.0051 0.0135  0.0062  80  SER   A C   
1669 O  O   . SER   A 80  ? 0.1229 0.1549 0.1928 0.0077  0.0133  -0.0032 80  SER   A O   
1670 C  CB  . SER   A 80  ? 0.1397 0.1282 0.1832 -0.0034 0.0107  0.0101  80  SER   A CB  
1671 O  OG  . SER   A 80  ? 0.1627 0.1314 0.2264 0.0028  -0.0075 0.0201  80  SER   A OG  
1677 N  N   . CYS   A 81  ? 0.1186 0.1257 0.1620 0.0021  0.0001  0.0067  81  CYS   A N   
1678 C  CA  . CYS   A 81  ? 0.1187 0.1372 0.1566 -0.0055 -0.0051 0.0159  81  CYS   A CA  
1679 C  C   . CYS   A 81  ? 0.1206 0.1307 0.1536 -0.0116 -0.0006 0.0236  81  CYS   A C   
1680 O  O   . CYS   A 81  ? 0.1241 0.1608 0.1696 -0.0026 0.0035  0.0357  81  CYS   A O   
1681 C  CB  . CYS   A 81  ? 0.1298 0.1425 0.1741 -0.0115 -0.0027 0.0200  81  CYS   A CB  
1682 S  SG  . CYS   A 81  ? 0.1439 0.1317 0.1683 -0.0143 0.0009  0.0115  81  CYS   A SG  
1688 N  N   . VAL   A 82  ? 0.1276 0.1421 0.1500 -0.0007 -0.0127 0.0154  82  VAL   A N   
1689 C  CA  . VAL   A 82  ? 0.1361 0.1426 0.1541 0.0004  -0.0067 0.0211  82  VAL   A CA  
1690 C  C   . VAL   A 82  ? 0.1367 0.1438 0.1600 -0.0046 -0.0106 0.0232  82  VAL   A C   
1691 O  O   . VAL   A 82  ? 0.1303 0.1580 0.1821 -0.0034 -0.0031 0.0024  82  VAL   A O   
1692 C  CB  . VAL   A 82  ? 0.1655 0.1552 0.1750 0.0051  0.0013  0.0254  82  VAL   A CB  
1693 C  CG1 . VAL   A 82  ? 0.1925 0.1721 0.1909 0.0142  0.0017  0.0320  82  VAL   A CG1 
1694 C  CG2 . VAL   A 82  ? 0.1727 0.1610 0.2075 -0.0012 0.0037  0.0231  82  VAL   A CG2 
1704 N  N   . LEU   A 83  ? 0.1297 0.1383 0.1610 -0.0110 -0.0094 0.0105  83  LEU   A N   
1705 C  CA  . LEU   A 83  ? 0.1328 0.1449 0.1529 -0.0097 -0.0080 0.0082  83  LEU   A CA  
1706 C  C   . LEU   A 83  ? 0.1358 0.1489 0.1479 -0.0092 -0.0114 0.0048  83  LEU   A C   
1707 O  O   . LEU   A 83  ? 0.1459 0.1474 0.1677 -0.0128 -0.0070 0.0152  83  LEU   A O   
1708 C  CB  . LEU   A 83  ? 0.1379 0.1487 0.1634 -0.0118 -0.0065 0.0133  83  LEU   A CB  
1709 C  CG  . LEU   A 83  ? 0.1504 0.1624 0.1625 -0.0109 -0.0030 0.0017  83  LEU   A CG  
1710 C  CD1 . LEU   A 83  ? 0.1636 0.1648 0.1705 -0.0224 -0.0013 0.0139  83  LEU   A CD1 
1711 C  CD2 . LEU   A 83  ? 0.1504 0.1767 0.1819 -0.0125 0.0176  0.0168  83  LEU   A CD2 
1723 N  N   . SER   A 84  ? 0.1474 0.1538 0.1544 -0.0144 -0.0106 0.0086  84  SER   A N   
1724 C  CA  . SER   A 84  ? 0.1602 0.1558 0.1430 -0.0143 -0.0130 0.0016  84  SER   A CA  
1725 C  C   . SER   A 84  ? 0.1636 0.1525 0.1339 -0.0205 -0.0008 0.0039  84  SER   A C   
1726 O  O   . SER   A 84  ? 0.1597 0.1689 0.1384 -0.0113 -0.0098 0.0038  84  SER   A O   
1727 C  CB  . SER   A 84  ? 0.1678 0.1816 0.1509 -0.0137 -0.0070 0.0006  84  SER   A CB  
1728 O  OG  . SER   A 84  ? 0.1724 0.2004 0.1560 -0.0119 -0.0158 -0.0069 84  SER   A OG  
1734 N  N   . GLY   A 85  ? 0.1777 0.1624 0.1384 -0.0224 0.0099  0.0028  85  GLY   A N   
1735 C  CA  . GLY   A 85  ? 0.1817 0.1725 0.1564 -0.0288 0.0127  -0.0057 85  GLY   A CA  
1736 C  C   . GLY   A 85  ? 0.1753 0.1809 0.1463 -0.0200 0.0020  -0.0006 85  GLY   A C   
1737 O  O   . GLY   A 85  ? 0.1714 0.1953 0.1559 -0.0250 0.0167  -0.0146 85  GLY   A O   
1741 N  N   . HIS   A 86  ? 0.1783 0.1691 0.1293 -0.0192 -0.0026 0.0063  86  HIS   A N   
1742 C  CA  . HIS   A 86  ? 0.1948 0.1832 0.1307 -0.0217 -0.0018 0.0022  86  HIS   A CA  
1743 C  C   . HIS   A 86  ? 0.2161 0.1944 0.1239 -0.0220 -0.0044 -0.0022 86  HIS   A C   
1744 O  O   . HIS   A 86  ? 0.2265 0.2111 0.1373 -0.0165 0.0041  0.0013  86  HIS   A O   
1745 C  CB  . HIS   A 86  ? 0.1898 0.1777 0.1362 -0.0139 0.0015  0.0048  86  HIS   A CB  
1746 C  CG  . HIS   A 86  ? 0.1787 0.1712 0.1421 -0.0091 0.0074  0.0053  86  HIS   A CG  
1747 N  ND1 . HIS   A 86  ? 0.1844 0.1731 0.1740 -0.0202 0.0015  0.0086  86  HIS   A ND1 
1748 C  CD2 . HIS   A 86  ? 0.1784 0.1679 0.1368 0.0004  0.0104  0.0045  86  HIS   A CD2 
1749 C  CE1 . HIS   A 86  ? 0.1809 0.1697 0.1645 -0.0167 0.0193  0.0096  86  HIS   A CE1 
1750 N  NE2 . HIS   A 86  ? 0.1782 0.1616 0.1552 0.0003  0.0096  0.0195  86  HIS   A NE2 
1758 N  N   . ASN   A 87  ? 0.2249 0.2056 0.1397 -0.0178 0.0172  -0.0143 87  ASN   A N   
1759 C  CA  . ASN   A 87  ? 0.2430 0.2186 0.1543 -0.0138 0.0437  -0.0132 87  ASN   A CA  
1760 C  C   . ASN   A 87  ? 0.2433 0.2298 0.1821 -0.0224 0.0577  -0.0004 87  ASN   A C   
1761 O  O   . ASN   A 87  ? 0.2660 0.2477 0.2354 -0.0343 0.0871  -0.0056 87  ASN   A O   
1762 C  CB  . ASN   A 87  ? 0.2620 0.2275 0.1655 -0.0026 0.0469  -0.0119 87  ASN   A CB  
1763 C  CG  . ASN   A 87  ? 0.2758 0.2328 0.1729 0.0076  0.0591  -0.0052 87  ASN   A CG  
1764 O  OD1 . ASN   A 87  ? 0.2915 0.2288 0.1817 0.0250  0.0542  0.0083  87  ASN   A OD1 
1765 N  ND2 . ASN   A 87  ? 0.2811 0.2541 0.1811 0.0061  0.0579  -0.0019 87  ASN   A ND2 
1772 N  N   . LEU   A 88  ? 0.2158 0.2247 0.1799 -0.0269 0.0304  0.0102  88  LEU   A N   
1773 C  CA  . LEU   A 88  ? 0.2024 0.2246 0.1906 -0.0344 0.0234  0.0222  88  LEU   A CA  
1774 C  C   . LEU   A 88  ? 0.1944 0.2227 0.1845 -0.0346 0.0216  0.0354  88  LEU   A C   
1775 O  O   . LEU   A 88  ? 0.1970 0.2276 0.2121 -0.0326 0.0312  0.0509  88  LEU   A O   
1776 C  CB  . LEU   A 88  ? 0.2035 0.2374 0.2056 -0.0452 -0.0071 0.0339  88  LEU   A CB  
1777 C  CG  . LEU   A 88  ? 0.2227 0.2534 0.2383 -0.0418 -0.0168 0.0314  88  LEU   A CG  
1778 C  CD1 . LEU   A 88  ? 0.2349 0.2620 0.2282 -0.0407 -0.0170 0.0091  88  LEU   A CD1 
1779 C  CD2 . LEU   A 88  ? 0.2364 0.2642 0.2817 -0.0358 -0.0159 0.0246  88  LEU   A CD2 
1791 N  N   . ALA   A 89  ? 0.1954 0.2062 0.1614 -0.0328 0.0189  0.0129  89  ALA   A N   
1792 C  CA  . ALA   A 89  ? 0.2034 0.2044 0.1521 -0.0285 0.0110  0.0143  89  ALA   A CA  
1793 C  C   . ALA   A 89  ? 0.2083 0.2099 0.1602 -0.0202 -0.0110 0.0054  89  ALA   A C   
1794 O  O   . ALA   A 89  ? 0.2075 0.2045 0.1939 -0.0295 -0.0149 -0.0157 89  ALA   A O   
1795 C  CB  . ALA   A 89  ? 0.1944 0.2040 0.1339 -0.0238 0.0073  0.0170  89  ALA   A CB  
1801 N  N   . LYS   A 90  ? 0.2181 0.2236 0.1484 -0.0258 -0.0270 0.0218  90  LYS   A N   
1802 C  CA  . LYS   A 90  ? 0.2271 0.2346 0.1530 -0.0257 -0.0331 0.0226  90  LYS   A CA  
1803 C  C   . LYS   A 90  ? 0.2026 0.2209 0.1472 -0.0253 -0.0335 0.0134  90  LYS   A C   
1804 O  O   . LYS   A 90  ? 0.2087 0.2383 0.1879 -0.0298 -0.0324 0.0013  90  LYS   A O   
1805 C  CB  . LYS   A 90  ? 0.2535 0.2640 0.1944 -0.0207 -0.0365 0.0422  90  LYS   A CB  
1806 C  CG  . LYS   A 90  ? 0.2892 0.2969 0.2885 -0.0204 -0.0303 0.0496  90  LYS   A CG  
1807 C  CD  . LYS   A 90  ? 0.3238 0.3281 0.3790 -0.0225 -0.0170 0.0576  90  LYS   A CD  
1808 C  CE  . LYS   A 90  ? 0.3503 0.3529 0.4425 -0.0229 -0.0080 0.0557  90  LYS   A CE  
1809 N  NZ  . LYS   A 90  ? 0.3662 0.3682 0.4894 -0.0231 -0.0035 0.0508  90  LYS   A NZ  
1823 N  N   . HIS   A 91  ? 0.1893 0.1918 0.1219 -0.0222 -0.0310 0.0116  91  HIS   A N   
1824 C  CA  . HIS   A 91  ? 0.1760 0.1786 0.1373 -0.0210 -0.0268 0.0181  91  HIS   A CA  
1825 C  C   . HIS   A 91  ? 0.1558 0.1663 0.1188 -0.0198 -0.0159 0.0213  91  HIS   A C   
1826 O  O   . HIS   A 91  ? 0.1539 0.1779 0.1379 -0.0181 -0.0055 0.0199  91  HIS   A O   
1827 C  CB  . HIS   A 91  ? 0.1904 0.2038 0.1876 0.0043  -0.0471 0.0155  91  HIS   A CB  
1828 C  CG  . HIS   A 91  ? 0.2321 0.2491 0.2595 0.0122  -0.0717 0.0059  91  HIS   A CG  
1829 N  ND1 . HIS   A 91  ? 0.2447 0.2762 0.3006 0.0159  -0.0767 -0.0135 91  HIS   A ND1 
1830 C  CD2 . HIS   A 91  ? 0.2560 0.2687 0.2817 0.0194  -0.0815 0.0124  91  HIS   A CD2 
1831 C  CE1 . HIS   A 91  ? 0.2584 0.2831 0.3092 0.0211  -0.0742 -0.0007 91  HIS   A CE1 
1832 N  NE2 . HIS   A 91  ? 0.2684 0.2825 0.3065 0.0238  -0.0813 0.0036  91  HIS   A NE2 
1840 N  N   . CYS   A 92  ? 0.1497 0.1598 0.1157 -0.0162 -0.0115 0.0159  92  CYS   A N   
1841 C  CA  . CYS   A 92  ? 0.1392 0.1484 0.1346 -0.0154 -0.0006 0.0163  92  CYS   A CA  
1842 C  C   . CYS   A 92  ? 0.1278 0.1452 0.1285 -0.0126 0.0017  0.0080  92  CYS   A C   
1843 O  O   . CYS   A 92  ? 0.1336 0.1520 0.1517 -0.0182 -0.0075 0.0122  92  CYS   A O   
1844 C  CB  . CYS   A 92  ? 0.1426 0.1481 0.1594 -0.0050 0.0000  0.0175  92  CYS   A CB  
1845 S  SG  . CYS   A 92  ? 0.1383 0.1380 0.1457 -0.0131 -0.0035 0.0097  92  CYS   A SG  
1851 N  N   . LEU   A 93  ? 0.1263 0.1349 0.1338 -0.0066 0.0098  0.0122  93  LEU   A N   
1852 C  CA  . LEU   A 93  ? 0.1241 0.1288 0.1319 -0.0052 -0.0008 0.0118  93  LEU   A CA  
1853 C  C   . LEU   A 93  ? 0.1220 0.1204 0.1300 -0.0042 0.0002  0.0035  93  LEU   A C   
1854 O  O   . LEU   A 93  ? 0.1171 0.1328 0.1371 -0.0040 -0.0011 0.0103  93  LEU   A O   
1855 C  CB  . LEU   A 93  ? 0.1294 0.1259 0.1468 -0.0035 -0.0055 0.0196  93  LEU   A CB  
1856 C  CG  . LEU   A 93  ? 0.1329 0.1255 0.1537 -0.0058 0.0019  0.0168  93  LEU   A CG  
1857 C  CD1 . LEU   A 93  ? 0.1439 0.1358 0.1804 -0.0025 0.0117  0.0116  93  LEU   A CD1 
1858 C  CD2 . LEU   A 93  ? 0.1509 0.1279 0.1720 -0.0085 0.0018  0.0094  93  LEU   A CD2 
1870 N  N   . HIS   A 94  ? 0.1140 0.1193 0.1431 -0.0012 0.0054  0.0141  94  HIS   A N   
1871 C  CA  . HIS   A 94  ? 0.1153 0.1193 0.1429 -0.0028 -0.0006 0.0196  94  HIS   A CA  
1872 C  C   . HIS   A 94  ? 0.1142 0.1135 0.1519 -0.0044 0.0001  0.0095  94  HIS   A C   
1873 O  O   . HIS   A 94  ? 0.1179 0.1340 0.1765 -0.0005 0.0004  -0.0100 94  HIS   A O   
1874 C  CB  . HIS   A 94  ? 0.1160 0.1185 0.1553 -0.0005 -0.0013 0.0184  94  HIS   A CB  
1875 C  CG  . HIS   A 94  ? 0.1180 0.1227 0.1429 -0.0045 -0.0019 0.0161  94  HIS   A CG  
1876 N  ND1 . HIS   A 94  ? 0.1194 0.1186 0.1479 -0.0031 -0.0000 0.0117  94  HIS   A ND1 
1877 C  CD2 . HIS   A 94  ? 0.1284 0.1303 0.1453 -0.0046 -0.0055 0.0084  94  HIS   A CD2 
1878 C  CE1 . HIS   A 94  ? 0.1255 0.1183 0.1537 -0.0099 -0.0094 0.0061  94  HIS   A CE1 
1879 N  NE2 . HIS   A 94  ? 0.1309 0.1222 0.1484 -0.0114 -0.0017 0.0065  94  HIS   A NE2 
1887 N  N   . VAL   A 95  ? 0.1134 0.1139 0.1297 -0.0020 0.0092  0.0042  95  VAL   A N   
1888 C  CA  . VAL   A 95  ? 0.1215 0.1191 0.1275 -0.0017 0.0108  0.0093  95  VAL   A CA  
1889 C  C   . VAL   A 95  ? 0.1208 0.1175 0.1228 -0.0129 0.0055  0.0067  95  VAL   A C   
1890 O  O   . VAL   A 95  ? 0.1292 0.1299 0.1368 0.0086  0.0076  0.0055  95  VAL   A O   
1891 C  CB  . VAL   A 95  ? 0.1248 0.1232 0.1415 -0.0113 0.0050  0.0055  95  VAL   A CB  
1892 C  CG1 . VAL   A 95  ? 0.1391 0.1286 0.1629 -0.0171 0.0056  -0.0088 95  VAL   A CG1 
1893 C  CG2 . VAL   A 95  ? 0.1278 0.1277 0.1425 -0.0105 0.0102  0.0202  95  VAL   A CG2 
1903 N  N   . VAL   A 96  ? 0.1275 0.1173 0.1217 -0.0007 0.0068  0.0094  96  VAL   A N   
1904 C  CA  . VAL   A 96  ? 0.1386 0.1220 0.1334 -0.0012 0.0051  0.0162  96  VAL   A CA  
1905 C  C   . VAL   A 96  ? 0.1370 0.1282 0.1397 -0.0011 0.0068  0.0158  96  VAL   A C   
1906 O  O   . VAL   A 96  ? 0.1461 0.1342 0.1539 -0.0004 0.0162  -0.0050 96  VAL   A O   
1907 C  CB  . VAL   A 96  ? 0.1403 0.1262 0.1353 -0.0023 0.0176  0.0139  96  VAL   A CB  
1908 C  CG1 . VAL   A 96  ? 0.1406 0.1422 0.1352 -0.0017 0.0125  0.0139  96  VAL   A CG1 
1909 C  CG2 . VAL   A 96  ? 0.1374 0.1346 0.1542 -0.0101 0.0110  0.0096  96  VAL   A CG2 
1919 N  N   . GLY   A 97  ? 0.1334 0.1308 0.1387 -0.0039 0.0042  0.0122  97  GLY   A N   
1920 C  CA  . GLY   A 97  ? 0.1418 0.1462 0.1418 0.0004  -0.0043 0.0106  97  GLY   A CA  
1921 C  C   . GLY   A 97  ? 0.1421 0.1580 0.1267 -0.0025 0.0033  0.0085  97  GLY   A C   
1922 O  O   . GLY   A 97  ? 0.1525 0.1602 0.1558 -0.0054 -0.0018 0.0164  97  GLY   A O   
1926 N  N   A PRO   A 98  ? 0.1527 0.1608 0.1134 0.0057  -0.0032 0.0165  98  PRO   A N   
1927 N  N   B PRO   A 98  ? 0.1527 0.1579 0.1358 -0.0010 0.0028  0.0144  98  PRO   A N   
1928 C  CA  A PRO   A 98  ? 0.1637 0.1814 0.1209 0.0038  0.0007  0.0050  98  PRO   A CA  
1929 C  CA  B PRO   A 98  ? 0.1637 0.1609 0.1465 -0.0043 -0.0000 0.0146  98  PRO   A CA  
1930 C  C   A PRO   A 98  ? 0.1657 0.1880 0.1310 -0.0046 0.0033  0.0206  98  PRO   A C   
1931 C  C   B PRO   A 98  ? 0.1791 0.1544 0.1517 -0.0073 -0.0055 0.0234  98  PRO   A C   
1932 O  O   A PRO   A 98  ? 0.1596 0.1711 0.1551 -0.0034 -0.0001 0.0174  98  PRO   A O   
1933 O  O   B PRO   A 98  ? 0.1771 0.1524 0.1606 -0.0092 -0.0024 0.0219  98  PRO   A O   
1934 C  CB  A PRO   A 98  ? 0.1719 0.1926 0.1084 0.0132  -0.0115 -0.0099 98  PRO   A CB  
1935 C  CB  B PRO   A 98  ? 0.1613 0.1644 0.1445 0.0005  0.0023  0.0118  98  PRO   A CB  
1936 C  CG  A PRO   A 98  ? 0.1735 0.1813 0.1267 0.0131  -0.0111 -0.0117 98  PRO   A CG  
1937 C  CG  B PRO   A 98  ? 0.1614 0.1642 0.1464 0.0015  0.0031  0.0118  98  PRO   A CG  
1938 C  CD  A PRO   A 98  ? 0.1615 0.1633 0.1242 0.0102  -0.0077 0.0058  98  PRO   A CD  
1939 C  CD  B PRO   A 98  ? 0.1547 0.1590 0.1385 0.0018  0.0036  0.0133  98  PRO   A CD  
1954 N  N   A ASN   A 99  ? 0.1742 0.2116 0.1263 -0.0048 0.0090  0.0355  99  ASN   A N   
1955 N  N   B ASN   A 99  ? 0.1984 0.1487 0.1529 -0.0063 -0.0134 0.0309  99  ASN   A N   
1956 C  CA  A ASN   A 99  ? 0.2001 0.2304 0.1219 -0.0070 0.0058  0.0456  99  ASN   A CA  
1957 C  CA  B ASN   A 99  ? 0.2177 0.1455 0.1557 -0.0004 -0.0184 0.0393  99  ASN   A CA  
1958 C  C   A ASN   A 99  ? 0.2178 0.2653 0.1107 -0.0212 0.0073  0.0509  99  ASN   A C   
1959 C  C   B ASN   A 99  ? 0.2257 0.1484 0.1600 0.0037  -0.0237 0.0377  99  ASN   A C   
1960 O  O   A ASN   A 99  ? 0.2247 0.2878 0.1240 -0.0131 0.0001  0.0418  99  ASN   A O   
1961 O  O   B ASN   A 99  ? 0.2250 0.1298 0.1514 0.0089  -0.0303 0.0342  99  ASN   A O   
1962 C  CB  A ASN   A 99  ? 0.1991 0.2211 0.1344 -0.0076 -0.0035 0.0549  99  ASN   A CB  
1963 C  CB  B ASN   A 99  ? 0.2258 0.1404 0.1625 -0.0001 -0.0197 0.0441  99  ASN   A CB  
1964 C  CG  A ASN   A 99  ? 0.1982 0.2166 0.1585 -0.0036 -0.0089 0.0411  99  ASN   A CG  
1965 C  CG  B ASN   A 99  ? 0.2329 0.1391 0.1691 -0.0018 -0.0201 0.0503  99  ASN   A CG  
1966 O  OD1 A ASN   A 99  ? 0.2136 0.2247 0.1757 0.0070  -0.0185 0.0252  99  ASN   A OD1 
1967 O  OD1 B ASN   A 99  ? 0.2396 0.1416 0.1666 -0.0037 -0.0228 0.0536  99  ASN   A OD1 
1968 N  ND2 A ASN   A 99  ? 0.1932 0.2106 0.1773 -0.0002 -0.0120 0.0504  99  ASN   A ND2 
1969 N  ND2 B ASN   A 99  ? 0.2321 0.1374 0.1737 0.0007  -0.0239 0.0457  99  ASN   A ND2 
1982 N  N   A VAL   A 100 ? 0.2346 0.2796 0.1179 -0.0427 -0.0174 0.0461  100 VAL   A N   
1983 N  N   B VAL   A 100 ? 0.2340 0.1735 0.1802 0.0038  -0.0206 0.0342  100 VAL   A N   
1984 C  CA  A VAL   A 100 ? 0.2598 0.3052 0.1482 -0.0537 -0.0227 0.0468  100 VAL   A CA  
1985 C  CA  B VAL   A 100 ? 0.2433 0.1980 0.2051 0.0029  -0.0174 0.0264  100 VAL   A CA  
1986 C  C   A VAL   A 100 ? 0.2718 0.3217 0.1474 -0.0563 -0.0361 0.0720  100 VAL   A C   
1987 C  C   B VAL   A 100 ? 0.2492 0.2126 0.2130 0.0044  -0.0207 0.0252  100 VAL   A C   
1988 O  O   A VAL   A 100 ? 0.2786 0.3323 0.1718 -0.0506 -0.0156 0.0732  100 VAL   A O   
1989 O  O   B VAL   A 100 ? 0.2501 0.2115 0.2133 0.0038  -0.0188 0.0155  100 VAL   A O   
1990 C  CB  A VAL   A 100 ? 0.2770 0.3107 0.1895 -0.0659 -0.0265 0.0383  100 VAL   A CB  
1991 C  CB  B VAL   A 100 ? 0.2471 0.2061 0.2266 0.0030  -0.0138 0.0194  100 VAL   A CB  
1992 C  CG1 A VAL   A 100 ? 0.2770 0.3120 0.2101 -0.0746 -0.0261 0.0391  100 VAL   A CG1 
1993 C  CG1 B VAL   A 100 ? 0.2475 0.2071 0.2366 0.0022  -0.0132 0.0195  100 VAL   A CG1 
1994 C  CG2 A VAL   A 100 ? 0.2875 0.3162 0.1938 -0.0685 -0.0222 0.0314  100 VAL   A CG2 
1995 C  CG2 B VAL   A 100 ? 0.2497 0.2089 0.2347 0.0018  -0.0101 0.0131  100 VAL   A CG2 
2014 N  N   A ASN   A 101 ? 0.2839 0.3302 0.1780 -0.0569 -0.0428 0.1036  101 ASN   A N   
2015 N  N   B ASN   A 101 ? 0.2541 0.2249 0.2223 0.0068  -0.0263 0.0307  101 ASN   A N   
2016 C  CA  A ASN   A 101 ? 0.3106 0.3405 0.2093 -0.0581 -0.0435 0.1264  101 ASN   A CA  
2017 C  CA  B ASN   A 101 ? 0.2616 0.2346 0.2309 0.0090  -0.0268 0.0310  101 ASN   A CA  
2018 C  C   A ASN   A 101 ? 0.3362 0.3712 0.2296 -0.0646 -0.0109 0.1556  101 ASN   A C   
2019 C  C   B ASN   A 101 ? 0.2715 0.2473 0.2423 0.0089  -0.0189 0.0353  101 ASN   A C   
2020 O  O   A ASN   A 101 ? 0.3504 0.3777 0.2741 -0.0597 -0.0156 0.1471  101 ASN   A O   
2021 O  O   B ASN   A 101 ? 0.2736 0.2459 0.2347 0.0076  -0.0199 0.0420  101 ASN   A O   
2022 C  CB  A ASN   A 101 ? 0.3120 0.3230 0.2166 -0.0523 -0.0753 0.1079  101 ASN   A CB  
2023 C  CB  B ASN   A 101 ? 0.2598 0.2313 0.2294 0.0095  -0.0297 0.0283  101 ASN   A CB  
2024 C  CG  A ASN   A 101 ? 0.3107 0.3078 0.2123 -0.0496 -0.0971 0.0749  101 ASN   A CG  
2025 C  CG  B ASN   A 101 ? 0.2581 0.2296 0.2317 0.0102  -0.0326 0.0253  101 ASN   A CG  
2026 O  OD1 A ASN   A 101 ? 0.3078 0.3150 0.2376 -0.0340 -0.0970 0.0357  101 ASN   A OD1 
2027 O  OD1 B ASN   A 101 ? 0.2622 0.2307 0.2355 0.0061  -0.0313 0.0265  101 ASN   A OD1 
2028 N  ND2 A ASN   A 101 ? 0.3116 0.2908 0.2053 -0.0611 -0.0980 0.0779  101 ASN   A ND2 
2029 N  ND2 B ASN   A 101 ? 0.2552 0.2260 0.2333 0.0141  -0.0323 0.0195  101 ASN   A ND2 
2042 N  N   A LYS   A 102 ? 0.3448 0.4006 0.2654 -0.0731 0.0089  0.1470  102 LYS   A N   
2043 N  N   B LYS   A 102 ? 0.2792 0.2617 0.2669 0.0087  -0.0075 0.0319  102 LYS   A N   
2044 C  CA  A LYS   A 102 ? 0.3581 0.4255 0.2742 -0.0750 0.0129  0.1336  102 LYS   A CA  
2045 C  CA  B LYS   A 102 ? 0.2883 0.2742 0.2834 0.0054  -0.0006 0.0286  102 LYS   A CA  
2046 C  C   A LYS   A 102 ? 0.3662 0.4456 0.2550 -0.0647 0.0075  0.1247  102 LYS   A C   
2047 C  C   B LYS   A 102 ? 0.2954 0.2817 0.2809 0.0046  0.0014  0.0319  102 LYS   A C   
2048 O  O   A LYS   A 102 ? 0.3709 0.4587 0.2638 -0.0618 0.0120  0.1126  102 LYS   A O   
2049 O  O   B LYS   A 102 ? 0.2964 0.2810 0.2806 0.0028  0.0042  0.0354  102 LYS   A O   
2050 C  CB  A LYS   A 102 ? 0.3667 0.4317 0.3115 -0.0847 0.0096  0.1161  102 LYS   A CB  
2051 C  CB  B LYS   A 102 ? 0.2907 0.2789 0.3023 0.0040  -0.0010 0.0222  102 LYS   A CB  
2052 C  CG  A LYS   A 102 ? 0.3758 0.4376 0.3449 -0.0900 0.0005  0.0930  102 LYS   A CG  
2053 C  CG  B LYS   A 102 ? 0.2929 0.2836 0.3189 0.0020  -0.0015 0.0166  102 LYS   A CG  
2054 C  CD  A LYS   A 102 ? 0.3871 0.4444 0.3768 -0.0914 -0.0070 0.0679  102 LYS   A CD  
2055 C  CD  B LYS   A 102 ? 0.2962 0.2885 0.3357 0.0003  -0.0017 0.0116  102 LYS   A CD  
2056 C  CE  A LYS   A 102 ? 0.3970 0.4497 0.4039 -0.0902 -0.0126 0.0509  102 LYS   A CE  
2057 C  CE  B LYS   A 102 ? 0.2995 0.2928 0.3499 -0.0009 -0.0020 0.0088  102 LYS   A CE  
2058 N  NZ  A LYS   A 102 ? 0.4037 0.4516 0.4160 -0.0915 -0.0131 0.0404  102 LYS   A NZ  
2059 N  NZ  B LYS   A 102 ? 0.3015 0.2957 0.3577 -0.0024 -0.0011 0.0079  102 LYS   A NZ  
2086 N  N   A GLY   A 103 ? 0.3665 0.4560 0.2445 -0.0513 -0.0075 0.1036  103 GLY   A N   
2087 N  N   B GLY   A 103 ? 0.3010 0.2909 0.2762 0.0055  -0.0012 0.0320  103 GLY   A N   
2088 C  CA  A GLY   A 103 ? 0.3682 0.4601 0.2313 -0.0393 -0.0085 0.0847  103 GLY   A CA  
2089 C  CA  B GLY   A 103 ? 0.3063 0.2977 0.2712 0.0060  -0.0013 0.0321  103 GLY   A CA  
2090 C  C   A GLY   A 103 ? 0.3630 0.4632 0.2277 -0.0318 -0.0007 0.0583  103 GLY   A C   
2091 C  C   B GLY   A 103 ? 0.3099 0.3026 0.2653 0.0056  -0.0004 0.0298  103 GLY   A C   
2092 O  O   A GLY   A 103 ? 0.3751 0.4736 0.2521 -0.0248 -0.0008 0.0445  103 GLY   A O   
2093 O  O   B GLY   A 103 ? 0.3132 0.3044 0.2645 0.0063  -0.0006 0.0342  103 GLY   A O   
2100 N  N   A GLU   A 104 ? 0.3398 0.4498 0.1798 -0.0363 0.0055  0.0457  104 GLU   A N   
2101 N  N   B GLU   A 104 ? 0.3090 0.3043 0.2577 0.0044  -0.0018 0.0239  104 GLU   A N   
2102 C  CA  A GLU   A 104 ? 0.3093 0.4308 0.1549 -0.0473 0.0112  0.0360  104 GLU   A CA  
2103 C  CA  B GLU   A 104 ? 0.3072 0.3041 0.2533 0.0012  -0.0038 0.0188  104 GLU   A CA  
2104 C  C   A GLU   A 104 ? 0.3053 0.4354 0.1587 -0.0521 0.0114  0.0159  104 GLU   A C   
2105 C  C   B GLU   A 104 ? 0.3104 0.3079 0.2626 0.0001  -0.0014 0.0123  104 GLU   A C   
2106 O  O   A GLU   A 104 ? 0.2983 0.4339 0.1839 -0.0550 -0.0041 0.0116  104 GLU   A O   
2107 O  O   B GLU   A 104 ? 0.3084 0.3040 0.2578 0.0004  -0.0020 0.0145  104 GLU   A O   
2108 C  CB  A GLU   A 104 ? 0.2797 0.4076 0.1327 -0.0535 0.0201  0.0518  104 GLU   A CB  
2109 C  CB  B GLU   A 104 ? 0.3023 0.3015 0.2443 0.0001  -0.0064 0.0189  104 GLU   A CB  
2110 C  CG  A GLU   A 104 ? 0.2612 0.3893 0.1541 -0.0526 0.0124  0.0585  104 GLU   A CG  
2111 C  CG  B GLU   A 104 ? 0.2996 0.3001 0.2410 0.0003  -0.0090 0.0179  104 GLU   A CG  
2112 C  CD  A GLU   A 104 ? 0.2415 0.3724 0.1522 -0.0536 0.0100  0.0669  104 GLU   A CD  
2113 C  CD  B GLU   A 104 ? 0.2973 0.2990 0.2379 0.0005  -0.0104 0.0160  104 GLU   A CD  
2114 O  OE1 A GLU   A 104 ? 0.2234 0.3602 0.1242 -0.0524 -0.0027 0.0627  104 GLU   A OE1 
2115 O  OE1 B GLU   A 104 ? 0.2956 0.2979 0.2347 0.0007  -0.0119 0.0152  104 GLU   A OE1 
2116 O  OE2 A GLU   A 104 ? 0.2526 0.3688 0.1745 -0.0556 0.0166  0.0838  104 GLU   A OE2 
2117 O  OE2 B GLU   A 104 ? 0.2990 0.2993 0.2432 0.0003  -0.0103 0.0145  104 GLU   A OE2 
2130 N  N   A ASP   A 105 ? 0.3081 0.4411 0.1792 -0.0528 0.0229  -0.0079 105 ASP   A N   
2131 N  N   B ASP   A 105 ? 0.3167 0.3161 0.2795 -0.0020 0.0016  0.0028  105 ASP   A N   
2132 C  CA  A ASP   A 105 ? 0.3093 0.4456 0.2167 -0.0479 0.0323  -0.0360 105 ASP   A CA  
2133 C  CA  B ASP   A 105 ? 0.3218 0.3244 0.2979 -0.0024 0.0055  -0.0074 105 ASP   A CA  
2134 C  C   A ASP   A 105 ? 0.2748 0.4300 0.1847 -0.0529 0.0210  -0.0523 105 ASP   A C   
2135 C  C   B ASP   A 105 ? 0.3195 0.3259 0.2880 -0.0072 0.0053  -0.0091 105 ASP   A C   
2136 O  O   A ASP   A 105 ? 0.2524 0.4229 0.1315 -0.0525 0.0233  -0.0713 105 ASP   A O   
2137 O  O   B ASP   A 105 ? 0.3175 0.3259 0.2795 -0.0064 0.0049  -0.0089 105 ASP   A O   
2138 C  CB  A ASP   A 105 ? 0.3400 0.4654 0.2867 -0.0392 0.0463  -0.0494 105 ASP   A CB  
2139 C  CB  B ASP   A 105 ? 0.3290 0.3306 0.3259 0.0014  0.0090  -0.0150 105 ASP   A CB  
2140 C  CG  A ASP   A 105 ? 0.3658 0.4821 0.3584 -0.0295 0.0483  -0.0637 105 ASP   A CG  
2141 C  CG  B ASP   A 105 ? 0.3349 0.3354 0.3517 0.0057  0.0103  -0.0213 105 ASP   A CG  
2142 O  OD1 A ASP   A 105 ? 0.3735 0.4887 0.3700 -0.0299 0.0468  -0.0767 105 ASP   A OD1 
2143 O  OD1 B ASP   A 105 ? 0.3370 0.3362 0.3562 0.0059  0.0094  -0.0243 105 ASP   A OD1 
2144 O  OD2 A ASP   A 105 ? 0.3791 0.4893 0.4031 -0.0268 0.0520  -0.0599 105 ASP   A OD2 
2145 O  OD2 B ASP   A 105 ? 0.3379 0.3385 0.3665 0.0071  0.0108  -0.0216 105 ASP   A OD2 
2154 N  N   A ILE   A 106 ? 0.2582 0.4164 0.2130 -0.0576 -0.0047 -0.0554 106 ILE   A N   
2155 N  N   B ILE   A 106 ? 0.3178 0.3263 0.2881 -0.0125 0.0037  -0.0106 106 ILE   A N   
2156 C  CA  A ILE   A 106 ? 0.2303 0.3982 0.2366 -0.0697 -0.0278 -0.0687 106 ILE   A CA  
2157 C  CA  B ILE   A 106 ? 0.3142 0.3258 0.2897 -0.0198 0.0029  -0.0130 106 ILE   A CA  
2158 C  C   A ILE   A 106 ? 0.2164 0.3677 0.2458 -0.0843 -0.0269 -0.0812 106 ILE   A C   
2159 C  C   B ILE   A 106 ? 0.3066 0.3171 0.2899 -0.0268 0.0073  -0.0151 106 ILE   A C   
2160 O  O   A ILE   A 106 ? 0.1973 0.3565 0.2509 -0.0855 -0.0107 -0.0863 106 ILE   A O   
2161 O  O   B ILE   A 106 ? 0.3062 0.3168 0.2873 -0.0263 0.0088  -0.0150 106 ILE   A O   
2162 C  CB  A ILE   A 106 ? 0.2293 0.4124 0.2760 -0.0569 -0.0439 -0.0468 106 ILE   A CB  
2163 C  CB  B ILE   A 106 ? 0.3182 0.3332 0.2979 -0.0193 -0.0018 -0.0100 106 ILE   A CB  
2164 C  CG1 A ILE   A 106 ? 0.2190 0.4155 0.3098 -0.0409 -0.0443 -0.0241 106 ILE   A CG1 
2165 C  CG1 B ILE   A 106 ? 0.3188 0.3360 0.3046 -0.0179 -0.0039 -0.0063 106 ILE   A CG1 
2166 C  CG2 A ILE   A 106 ? 0.2329 0.4183 0.2842 -0.0568 -0.0554 -0.0460 106 ILE   A CG2 
2167 C  CG2 B ILE   A 106 ? 0.3201 0.3360 0.3002 -0.0195 -0.0038 -0.0095 106 ILE   A CG2 
2168 C  CD1 A ILE   A 106 ? 0.2174 0.4129 0.3257 -0.0268 -0.0345 -0.0102 106 ILE   A CD1 
2169 C  CD1 B ILE   A 106 ? 0.3193 0.3362 0.3066 -0.0163 -0.0038 -0.0038 106 ILE   A CD1 
2192 N  N   A GLN   A 107 ? 0.2372 0.3480 0.2661 -0.0828 -0.0153 -0.0898 107 GLN   A N   
2193 N  N   B GLN   A 107 ? 0.2992 0.3070 0.2977 -0.0332 0.0115  -0.0187 107 GLN   A N   
2194 C  CA  A GLN   A 107 ? 0.2649 0.3287 0.3326 -0.0651 0.0083  -0.0912 107 GLN   A CA  
2195 C  CA  B GLN   A 107 ? 0.2905 0.2965 0.3136 -0.0382 0.0166  -0.0256 107 GLN   A CA  
2196 C  C   A GLN   A 107 ? 0.2415 0.2770 0.3154 -0.0574 0.0308  -0.0616 107 GLN   A C   
2197 C  C   B GLN   A 107 ? 0.2565 0.2670 0.2835 -0.0460 0.0264  -0.0350 107 GLN   A C   
2198 O  O   A GLN   A 107 ? 0.2455 0.2689 0.3685 -0.0443 0.0457  -0.0603 107 GLN   A O   
2199 O  O   B GLN   A 107 ? 0.2601 0.2681 0.2964 -0.0435 0.0278  -0.0332 107 GLN   A O   
2200 C  CB  A GLN   A 107 ? 0.3081 0.3585 0.4252 -0.0680 0.0025  -0.1006 107 GLN   A CB  
2201 C  CB  B GLN   A 107 ? 0.3121 0.3134 0.3606 -0.0379 0.0107  -0.0195 107 GLN   A CB  
2202 C  CG  A GLN   A 107 ? 0.3514 0.3885 0.5258 -0.0667 -0.0023 -0.0978 107 GLN   A CG  
2203 C  CG  B GLN   A 107 ? 0.3303 0.3277 0.4081 -0.0376 0.0050  -0.0125 107 GLN   A CG  
2204 C  CD  A GLN   A 107 ? 0.3826 0.4098 0.6080 -0.0671 -0.0034 -0.0915 107 GLN   A CD  
2205 C  CD  B GLN   A 107 ? 0.3456 0.3403 0.4487 -0.0361 0.0004  -0.0056 107 GLN   A CD  
2206 O  OE1 A GLN   A 107 ? 0.3959 0.4176 0.6422 -0.0678 -0.0035 -0.0901 107 GLN   A OE1 
2207 O  OE1 B GLN   A 107 ? 0.3502 0.3440 0.4604 -0.0355 -0.0016 -0.0006 107 GLN   A OE1 
2208 N  NE2 A GLN   A 107 ? 0.3935 0.4177 0.6337 -0.0687 -0.0048 -0.0924 107 GLN   A NE2 
2209 N  NE2 B GLN   A 107 ? 0.3504 0.3445 0.4613 -0.0354 -0.0016 -0.0039 107 GLN   A NE2 
2226 N  N   . LEU   A 108 ? 0.2177 0.2361 0.2512 -0.0556 0.0323  -0.0498 108 LEU   A N   
2227 C  CA  . LEU   A 108 ? 0.1895 0.1881 0.2170 -0.0249 0.0271  -0.0134 108 LEU   A CA  
2228 C  C   . LEU   A 108 ? 0.1608 0.1506 0.2139 -0.0126 0.0203  0.0108  108 LEU   A C   
2229 O  O   . LEU   A 108 ? 0.1582 0.1524 0.2244 -0.0039 0.0298  0.0113  108 LEU   A O   
2230 C  CB  . LEU   A 108 ? 0.1962 0.1963 0.1883 -0.0262 0.0299  -0.0091 108 LEU   A CB  
2231 C  CG  . LEU   A 108 ? 0.2082 0.2171 0.2169 -0.0216 0.0343  -0.0181 108 LEU   A CG  
2232 C  CD1 . LEU   A 108 ? 0.2288 0.2237 0.2230 -0.0307 0.0428  -0.0162 108 LEU   A CD1 
2233 C  CD2 . LEU   A 108 ? 0.2091 0.2399 0.2606 -0.0123 0.0301  -0.0132 108 LEU   A CD2 
2246 N  N   . LEU   A 109 ? 0.1496 0.1470 0.2039 0.0006  0.0121  0.0238  109 LEU   A N   
2247 C  CA  . LEU   A 109 ? 0.1479 0.1439 0.1893 0.0016  0.0041  0.0214  109 LEU   A CA  
2248 C  C   . LEU   A 109 ? 0.1369 0.1347 0.1728 -0.0081 0.0064  0.0063  109 LEU   A C   
2249 O  O   . LEU   A 109 ? 0.1521 0.1292 0.1858 -0.0055 -0.0021 0.0059  109 LEU   A O   
2250 C  CB  . LEU   A 109 ? 0.1567 0.1503 0.2088 0.0142  -0.0053 0.0354  109 LEU   A CB  
2251 C  CG  . LEU   A 109 ? 0.1487 0.1578 0.2248 0.0036  -0.0024 0.0357  109 LEU   A CG  
2252 C  CD1 . LEU   A 109 ? 0.1526 0.1506 0.2380 -0.0006 0.0024  0.0114  109 LEU   A CD1 
2253 C  CD2 . LEU   A 109 ? 0.1506 0.1764 0.2425 0.0038  -0.0057 0.0417  109 LEU   A CD2 
2265 N  N   . LYS   A 110 ? 0.1343 0.1337 0.1812 -0.0068 -0.0013 0.0088  110 LYS   A N   
2266 C  CA  . LYS   A 110 ? 0.1350 0.1290 0.1805 -0.0080 -0.0019 0.0117  110 LYS   A CA  
2267 C  C   . LYS   A 110 ? 0.1377 0.1224 0.1672 -0.0069 0.0041  -0.0019 110 LYS   A C   
2268 O  O   . LYS   A 110 ? 0.1337 0.1225 0.1815 -0.0057 0.0025  -0.0019 110 LYS   A O   
2269 C  CB  . LYS   A 110 ? 0.1426 0.1363 0.2014 -0.0056 -0.0138 -0.0068 110 LYS   A CB  
2270 C  CG  . LYS   A 110 ? 0.1435 0.1299 0.2075 -0.0030 -0.0116 -0.0049 110 LYS   A CG  
2271 C  CD  . LYS   A 110 ? 0.1490 0.1372 0.2199 -0.0081 -0.0082 -0.0056 110 LYS   A CD  
2272 C  CE  . LYS   A 110 ? 0.1572 0.1483 0.2418 -0.0064 0.0072  -0.0070 110 LYS   A CE  
2273 N  NZ  . LYS   A 110 ? 0.1560 0.1447 0.2577 -0.0124 0.0155  -0.0025 110 LYS   A NZ  
2287 N  N   . SER   A 111 ? 0.1386 0.1242 0.1694 -0.0053 -0.0012 0.0077  111 SER   A N   
2288 C  CA  . SER   A 111 ? 0.1346 0.1286 0.1830 0.0018  0.0089  0.0050  111 SER   A CA  
2289 C  C   . SER   A 111 ? 0.1284 0.1248 0.1680 -0.0035 0.0110  0.0116  111 SER   A C   
2290 O  O   . SER   A 111 ? 0.1395 0.1212 0.1889 -0.0013 0.0087  0.0120  111 SER   A O   
2291 C  CB  . SER   A 111 ? 0.1563 0.1448 0.1960 -0.0054 0.0218  -0.0092 111 SER   A CB  
2292 O  OG  . SER   A 111 ? 0.2040 0.1651 0.2115 -0.0008 0.0261  -0.0123 111 SER   A OG  
2298 N  N   . ALA   A 112 ? 0.1329 0.1180 0.1767 -0.0014 0.0126  0.0083  112 ALA   A N   
2299 C  CA  . ALA   A 112 ? 0.1340 0.1185 0.1742 -0.0024 0.0161  0.0018  112 ALA   A CA  
2300 C  C   . ALA   A 112 ? 0.1268 0.1144 0.1770 0.0008  0.0101  -0.0010 112 ALA   A C   
2301 O  O   . ALA   A 112 ? 0.1288 0.1137 0.1845 -0.0123 0.0108  0.0074  112 ALA   A O   
2302 C  CB  . ALA   A 112 ? 0.1463 0.1144 0.1839 -0.0051 0.0116  0.0020  112 ALA   A CB  
2308 N  N   . TYR   A 113 ? 0.1178 0.1176 0.1866 -0.0051 0.0042  0.0090  113 TYR   A N   
2309 C  CA  . TYR   A 113 ? 0.1164 0.1190 0.1712 -0.0013 0.0072  0.0121  113 TYR   A CA  
2310 C  C   . TYR   A 113 ? 0.1184 0.1176 0.1553 -0.0107 0.0019  0.0068  113 TYR   A C   
2311 O  O   . TYR   A 113 ? 0.1246 0.1232 0.1726 -0.0025 0.0137  0.0006  113 TYR   A O   
2312 C  CB  . TYR   A 113 ? 0.1160 0.1301 0.1807 -0.0023 -0.0056 0.0142  113 TYR   A CB  
2313 C  CG  . TYR   A 113 ? 0.1174 0.1363 0.1810 -0.0098 0.0053  0.0203  113 TYR   A CG  
2314 C  CD1 . TYR   A 113 ? 0.1227 0.1372 0.1797 -0.0047 0.0082  0.0195  113 TYR   A CD1 
2315 C  CD2 . TYR   A 113 ? 0.1250 0.1380 0.1741 -0.0136 -0.0012 0.0194  113 TYR   A CD2 
2316 C  CE1 . TYR   A 113 ? 0.1283 0.1444 0.1801 -0.0028 0.0077  0.0266  113 TYR   A CE1 
2317 C  CE2 . TYR   A 113 ? 0.1249 0.1456 0.1801 -0.0079 -0.0014 0.0292  113 TYR   A CE2 
2318 C  CZ  . TYR   A 113 ? 0.1236 0.1443 0.1762 0.0013  0.0119  0.0313  113 TYR   A CZ  
2319 O  OH  . TYR   A 113 ? 0.1235 0.1522 0.1958 0.0107  0.0074  0.0361  113 TYR   A OH  
2329 N  N   . GLU   A 114 ? 0.1215 0.1183 0.1650 -0.0023 0.0072  0.0095  114 GLU   A N   
2330 C  CA  . GLU   A 114 ? 0.1238 0.1118 0.1766 0.0013  0.0094  0.0133  114 GLU   A CA  
2331 C  C   . GLU   A 114 ? 0.1185 0.1174 0.1705 0.0031  0.0106  0.0074  114 GLU   A C   
2332 O  O   . GLU   A 114 ? 0.1310 0.1220 0.1765 -0.0006 0.0059  0.0122  114 GLU   A O   
2333 C  CB  . GLU   A 114 ? 0.1239 0.1199 0.1792 -0.0035 0.0092  0.0115  114 GLU   A CB  
2334 C  CG  . GLU   A 114 ? 0.1285 0.1218 0.1843 -0.0013 0.0074  0.0022  114 GLU   A CG  
2335 C  CD  . GLU   A 114 ? 0.1395 0.1227 0.1965 -0.0063 0.0052  0.0032  114 GLU   A CD  
2336 O  OE1 . GLU   A 114 ? 0.1419 0.1179 0.1931 -0.0093 0.0137  -0.0059 114 GLU   A OE1 
2337 O  OE2 . GLU   A 114 ? 0.1562 0.1236 0.2110 -0.0124 0.0082  -0.0123 114 GLU   A OE2 
2344 N  N   . ASN   A 115 ? 0.1196 0.1162 0.1681 0.0009  0.0020  0.0019  115 ASN   A N   
2345 C  CA  . ASN   A 115 ? 0.1236 0.1231 0.1682 -0.0087 0.0042  0.0077  115 ASN   A CA  
2346 C  C   . ASN   A 115 ? 0.1269 0.1221 0.1534 -0.0126 0.0012  0.0042  115 ASN   A C   
2347 O  O   . ASN   A 115 ? 0.1252 0.1344 0.1650 -0.0099 0.0063  0.0128  115 ASN   A O   
2348 C  CB  . ASN   A 115 ? 0.1312 0.1269 0.1649 -0.0123 0.0083  0.0053  115 ASN   A CB  
2349 C  CG  . ASN   A 115 ? 0.1289 0.1471 0.1755 -0.0126 0.0172  0.0163  115 ASN   A CG  
2350 O  OD1 . ASN   A 115 ? 0.1371 0.2433 0.2103 -0.0157 0.0260  0.0276  115 ASN   A OD1 
2351 N  ND2 . ASN   A 115 ? 0.1320 0.1348 0.1750 -0.0098 0.0212  0.0207  115 ASN   A ND2 
2358 N  N   . PHE   A 116 ? 0.1189 0.1220 0.1737 -0.0047 0.0103  0.0142  116 PHE   A N   
2359 C  CA  . PHE   A 116 ? 0.1202 0.1341 0.1670 -0.0022 0.0126  0.0187  116 PHE   A CA  
2360 C  C   . PHE   A 116 ? 0.1203 0.1333 0.1681 -0.0076 0.0106  0.0193  116 PHE   A C   
2361 O  O   . PHE   A 116 ? 0.1279 0.1415 0.1673 -0.0020 0.0072  0.0244  116 PHE   A O   
2362 C  CB  . PHE   A 116 ? 0.1246 0.1252 0.1849 -0.0024 0.0174  0.0172  116 PHE   A CB  
2363 C  CG  . PHE   A 116 ? 0.1228 0.1242 0.1665 -0.0065 0.0136  0.0117  116 PHE   A CG  
2364 C  CD1 . PHE   A 116 ? 0.1291 0.1261 0.1747 -0.0050 0.0096  0.0097  116 PHE   A CD1 
2365 C  CD2 . PHE   A 116 ? 0.1318 0.1347 0.1773 -0.0045 0.0151  0.0129  116 PHE   A CD2 
2366 C  CE1 . PHE   A 116 ? 0.1310 0.1236 0.1756 -0.0135 0.0022  0.0071  116 PHE   A CE1 
2367 C  CE2 . PHE   A 116 ? 0.1318 0.1292 0.1835 -0.0079 0.0110  0.0103  116 PHE   A CE2 
2368 C  CZ  . PHE   A 116 ? 0.1337 0.1179 0.1819 -0.0064 0.0038  0.0114  116 PHE   A CZ  
2378 N  N   . ASN   A 117 ? 0.1253 0.1276 0.1691 0.0001  0.0119  0.0163  117 ASN   A N   
2379 C  CA  . ASN   A 117 ? 0.1276 0.1260 0.1863 -0.0025 0.0153  0.0232  117 ASN   A CA  
2380 C  C   . ASN   A 117 ? 0.1285 0.1308 0.1980 0.0008  0.0119  0.0240  117 ASN   A C   
2381 O  O   . ASN   A 117 ? 0.1336 0.1349 0.2189 -0.0061 -0.0035 0.0330  117 ASN   A O   
2382 C  CB  . ASN   A 117 ? 0.1222 0.1292 0.1973 -0.0020 0.0143  0.0312  117 ASN   A CB  
2383 C  CG  . ASN   A 117 ? 0.1198 0.1338 0.1912 -0.0009 0.0141  0.0283  117 ASN   A CG  
2384 O  OD1 . ASN   A 117 ? 0.1291 0.1510 0.1942 -0.0104 0.0104  0.0125  117 ASN   A OD1 
2385 N  ND2 . ASN   A 117 ? 0.1202 0.1318 0.1991 -0.0009 0.0078  0.0276  117 ASN   A ND2 
2392 N  N   . GLN   A 118 ? 0.1239 0.1323 0.1993 -0.0059 -0.0015 0.0264  118 GLN   A N   
2393 C  CA  . GLN   A 118 ? 0.1349 0.1464 0.1956 -0.0060 -0.0059 0.0133  118 GLN   A CA  
2394 C  C   . GLN   A 118 ? 0.1360 0.1500 0.1848 -0.0068 -0.0099 0.0154  118 GLN   A C   
2395 O  O   . GLN   A 118 ? 0.1370 0.1824 0.2092 -0.0020 -0.0123 0.0091  118 GLN   A O   
2396 C  CB  . GLN   A 118 ? 0.1306 0.1479 0.1990 -0.0056 0.0071  0.0150  118 GLN   A CB  
2397 C  CG  . GLN   A 118 ? 0.1237 0.1526 0.2025 -0.0024 0.0041  0.0180  118 GLN   A CG  
2398 C  CD  . GLN   A 118 ? 0.1213 0.1542 0.2117 -0.0005 0.0101  0.0163  118 GLN   A CD  
2399 O  OE1 . GLN   A 118 ? 0.1263 0.1678 0.2244 0.0120  -0.0019 0.0079  118 GLN   A OE1 
2400 N  NE2 . GLN   A 118 ? 0.1329 0.1514 0.2166 0.0041  0.0034  0.0188  118 GLN   A NE2 
2409 N  N   . HIS   A 119 ? 0.1347 0.1435 0.1754 -0.0002 -0.0028 0.0214  119 HIS   A N   
2410 C  CA  . HIS   A 119 ? 0.1429 0.1532 0.1827 -0.0001 0.0017  0.0255  119 HIS   A CA  
2411 C  C   . HIS   A 119 ? 0.1543 0.1603 0.1742 -0.0081 0.0081  0.0229  119 HIS   A C   
2412 O  O   . HIS   A 119 ? 0.1554 0.1727 0.1803 -0.0296 0.0005  0.0295  119 HIS   A O   
2413 C  CB  . HIS   A 119 ? 0.1497 0.1549 0.2075 -0.0009 0.0221  0.0311  119 HIS   A CB  
2414 C  CG  . HIS   A 119 ? 0.1492 0.1584 0.2481 0.0046  0.0156  0.0374  119 HIS   A CG  
2415 N  ND1 . HIS   A 119 ? 0.1621 0.1783 0.2977 -0.0066 0.0145  0.0265  119 HIS   A ND1 
2416 C  CD2 . HIS   A 119 ? 0.1631 0.1667 0.2707 0.0155  0.0315  0.0523  119 HIS   A CD2 
2417 C  CE1 . HIS   A 119 ? 0.1589 0.1758 0.3054 -0.0156 0.0302  0.0442  119 HIS   A CE1 
2418 N  NE2 . HIS   A 119 ? 0.1730 0.1706 0.3052 0.0023  0.0441  0.0638  119 HIS   A NE2 
2426 N  N   . GLU   A 120 ? 0.1620 0.1770 0.1794 -0.0024 -0.0009 0.0400  120 GLU   A N   
2427 C  CA  . GLU   A 120 ? 0.1767 0.1995 0.2024 0.0075  -0.0015 0.0691  120 GLU   A CA  
2428 C  C   . GLU   A 120 ? 0.1617 0.1854 0.1796 -0.0100 -0.0024 0.0588  120 GLU   A C   
2429 O  O   . GLU   A 120 ? 0.1633 0.1791 0.1985 -0.0066 -0.0019 0.0617  120 GLU   A O   
2430 C  CB  . GLU   A 120 ? 0.2287 0.2611 0.2575 0.0256  0.0051  0.1089  120 GLU   A CB  
2431 C  CG  . GLU   A 120 ? 0.3007 0.3182 0.3530 0.0364  0.0077  0.1135  120 GLU   A CG  
2432 C  CD  . GLU   A 120 ? 0.3651 0.3683 0.4527 0.0474  0.0135  0.1080  120 GLU   A CD  
2433 O  OE1 . GLU   A 120 ? 0.3889 0.3908 0.4784 0.0476  0.0139  0.1009  120 GLU   A OE1 
2434 O  OE2 . GLU   A 120 ? 0.3905 0.3905 0.4976 0.0509  0.0143  0.1118  120 GLU   A OE2 
2441 N  N   . VAL   A 121 ? 0.1569 0.1857 0.1623 -0.0108 0.0042  0.0453  121 VAL   A N   
2442 C  CA  . VAL   A 121 ? 0.1659 0.1954 0.1537 -0.0120 0.0175  0.0504  121 VAL   A CA  
2443 C  C   . VAL   A 121 ? 0.1544 0.1775 0.1424 -0.0162 0.0059  0.0361  121 VAL   A C   
2444 O  O   . VAL   A 121 ? 0.1589 0.1865 0.1597 -0.0245 -0.0110 0.0319  121 VAL   A O   
2445 C  CB  . VAL   A 121 ? 0.2074 0.2344 0.1824 0.0004  0.0248  0.0562  121 VAL   A CB  
2446 C  CG1 . VAL   A 121 ? 0.2134 0.2499 0.1908 0.0085  0.0308  0.0572  121 VAL   A CG1 
2447 C  CG2 . VAL   A 121 ? 0.2302 0.2519 0.2152 -0.0075 0.0215  0.0418  121 VAL   A CG2 
2457 N  N   . LEU   A 122 ? 0.1481 0.1598 0.1621 -0.0173 0.0109  0.0331  122 LEU   A N   
2458 C  CA  . LEU   A 122 ? 0.1539 0.1502 0.1619 -0.0196 0.0295  0.0319  122 LEU   A CA  
2459 C  C   . LEU   A 122 ? 0.1483 0.1503 0.1578 -0.0206 0.0097  0.0209  122 LEU   A C   
2460 O  O   . LEU   A 122 ? 0.1490 0.1595 0.1897 -0.0243 0.0105  0.0232  122 LEU   A O   
2461 C  CB  . LEU   A 122 ? 0.1748 0.1540 0.1921 -0.0101 0.0116  0.0370  122 LEU   A CB  
2462 C  CG  . LEU   A 122 ? 0.1748 0.1632 0.1773 -0.0102 0.0129  0.0283  122 LEU   A CG  
2463 C  CD1 . LEU   A 122 ? 0.1918 0.1667 0.1832 -0.0159 0.0122  0.0323  122 LEU   A CD1 
2464 C  CD2 . LEU   A 122 ? 0.1654 0.1569 0.1738 -0.0089 0.0314  0.0246  122 LEU   A CD2 
2476 N  N   A LEU   A 123 ? 0.1436 0.1465 0.1512 -0.0178 0.0058  0.0284  123 LEU   A N   
2477 N  N   B LEU   A 123 ? 0.1494 0.1513 0.1503 -0.0149 0.0031  0.0193  123 LEU   A N   
2478 C  CA  A LEU   A 123 ? 0.1397 0.1457 0.1498 -0.0168 0.0098  0.0254  123 LEU   A CA  
2479 C  CA  B LEU   A 123 ? 0.1504 0.1548 0.1485 -0.0105 0.0000  0.0164  123 LEU   A CA  
2480 C  C   A LEU   A 123 ? 0.1338 0.1370 0.1397 -0.0120 0.0087  0.0274  123 LEU   A C   
2481 C  C   B LEU   A 123 ? 0.1495 0.1517 0.1374 -0.0073 -0.0024 0.0145  123 LEU   A C   
2482 O  O   A LEU   A 123 ? 0.1265 0.1419 0.1549 -0.0151 0.0065  0.0233  123 LEU   A O   
2483 O  O   B LEU   A 123 ? 0.1463 0.1489 0.1368 -0.0022 -0.0036 0.0058  123 LEU   A O   
2484 C  CB  A LEU   A 123 ? 0.1527 0.1524 0.1552 -0.0196 0.0205  0.0252  123 LEU   A CB  
2485 C  CB  B LEU   A 123 ? 0.1546 0.1610 0.1594 -0.0090 0.0003  0.0156  123 LEU   A CB  
2486 C  CG  A LEU   A 123 ? 0.1595 0.1631 0.1736 -0.0184 0.0292  0.0155  123 LEU   A CG  
2487 C  CG  B LEU   A 123 ? 0.1576 0.1665 0.1667 -0.0085 0.0029  0.0150  123 LEU   A CG  
2488 C  CD1 A LEU   A 123 ? 0.1632 0.1730 0.1864 -0.0078 0.0274  0.0083  123 LEU   A CD1 
2489 C  CD1 B LEU   A 123 ? 0.1586 0.1696 0.1770 -0.0056 0.0019  0.0121  123 LEU   A CD1 
2490 C  CD2 A LEU   A 123 ? 0.1752 0.1748 0.1784 -0.0150 0.0197  0.0104  123 LEU   A CD2 
2491 C  CD2 B LEU   A 123 ? 0.1617 0.1708 0.1669 -0.0068 -0.0005 0.0122  123 LEU   A CD2 
2514 N  N   A ALA   A 124 ? 0.1348 0.1330 0.1396 -0.0139 0.0037  0.0196  124 ALA   A N   
2515 N  N   B ALA   A 124 ? 0.1516 0.1508 0.1339 -0.0089 -0.0046 0.0159  124 ALA   A N   
2516 C  CA  A ALA   A 124 ? 0.1250 0.1350 0.1606 -0.0121 -0.0019 0.0246  124 ALA   A CA  
2517 C  CA  B ALA   A 124 ? 0.1536 0.1527 0.1364 -0.0103 -0.0074 0.0193  124 ALA   A CA  
2518 C  C   A ALA   A 124 ? 0.1195 0.1334 0.1682 -0.0129 0.0127  0.0236  124 ALA   A C   
2519 C  C   B ALA   A 124 ? 0.1533 0.1515 0.1370 -0.0061 -0.0097 0.0192  124 ALA   A C   
2520 O  O   A ALA   A 124 ? 0.1228 0.1379 0.1896 -0.0153 0.0192  0.0343  124 ALA   A O   
2521 O  O   B ALA   A 124 ? 0.1532 0.1511 0.1336 -0.0023 -0.0139 0.0215  124 ALA   A O   
2522 C  CB  A ALA   A 124 ? 0.1237 0.1312 0.1832 -0.0067 0.0002  0.0261  124 ALA   A CB  
2523 C  CB  B ALA   A 124 ? 0.1576 0.1536 0.1415 -0.0152 -0.0027 0.0203  124 ALA   A CB  
2534 N  N   A PRO   A 125 ? 0.1190 0.1310 0.1680 -0.0099 0.0069  0.0339  125 PRO   A N   
2535 N  N   B PRO   A 125 ? 0.1524 0.1505 0.1414 -0.0030 -0.0121 0.0180  125 PRO   A N   
2536 C  CA  A PRO   A 125 ? 0.1255 0.1363 0.1632 -0.0059 0.0099  0.0301  125 PRO   A CA  
2537 C  CA  B PRO   A 125 ? 0.1507 0.1504 0.1421 -0.0005 -0.0103 0.0143  125 PRO   A CA  
2538 C  C   A PRO   A 125 ? 0.1236 0.1410 0.1674 -0.0095 0.0101  0.0279  125 PRO   A C   
2539 C  C   B PRO   A 125 ? 0.1436 0.1462 0.1441 -0.0036 -0.0050 0.0115  125 PRO   A C   
2540 O  O   A PRO   A 125 ? 0.1302 0.1372 0.1737 -0.0032 0.0022  0.0227  125 PRO   A O   
2541 O  O   B PRO   A 125 ? 0.1465 0.1449 0.1493 -0.0033 -0.0037 0.0091  125 PRO   A O   
2542 C  CB  A PRO   A 125 ? 0.1356 0.1321 0.1590 -0.0108 0.0224  0.0330  125 PRO   A CB  
2543 C  CB  B PRO   A 125 ? 0.1553 0.1535 0.1431 0.0005  -0.0082 0.0114  125 PRO   A CB  
2544 C  CG  A PRO   A 125 ? 0.1358 0.1241 0.1714 -0.0091 0.0185  0.0226  125 PRO   A CG  
2545 C  CG  B PRO   A 125 ? 0.1591 0.1534 0.1489 -0.0027 -0.0101 0.0113  125 PRO   A CG  
2546 C  CD  A PRO   A 125 ? 0.1268 0.1346 0.1704 -0.0152 0.0180  0.0281  125 PRO   A CD  
2547 C  CD  B PRO   A 125 ? 0.1559 0.1538 0.1466 -0.0045 -0.0097 0.0148  125 PRO   A CD  
2562 N  N   A LEU   A 126 ? 0.1209 0.1490 0.1762 -0.0043 0.0037  0.0290  126 LEU   A N   
2563 N  N   B LEU   A 126 ? 0.1360 0.1432 0.1437 -0.0051 -0.0044 0.0102  126 LEU   A N   
2564 C  CA  A LEU   A 126 ? 0.1270 0.1470 0.1828 -0.0073 0.0031  0.0339  126 LEU   A CA  
2565 C  CA  B LEU   A 126 ? 0.1274 0.1361 0.1347 -0.0052 -0.0043 0.0120  126 LEU   A CA  
2566 C  C   A LEU   A 126 ? 0.1323 0.1401 0.1793 0.0028  0.0014  0.0279  126 LEU   A C   
2567 C  C   B LEU   A 126 ? 0.1236 0.1342 0.1315 -0.0076 -0.0047 0.0158  126 LEU   A C   
2568 O  O   A LEU   A 126 ? 0.1394 0.1377 0.1900 0.0095  0.0134  0.0295  126 LEU   A O   
2569 O  O   B LEU   A 126 ? 0.1231 0.1322 0.1298 -0.0100 -0.0091 0.0234  126 LEU   A O   
2570 C  CB  A LEU   A 126 ? 0.1343 0.1572 0.1954 -0.0090 -0.0007 0.0288  126 LEU   A CB  
2571 C  CB  B LEU   A 126 ? 0.1227 0.1322 0.1338 -0.0078 -0.0008 0.0021  126 LEU   A CB  
2572 C  CG  A LEU   A 126 ? 0.1347 0.1685 0.2137 -0.0091 0.0071  0.0200  126 LEU   A CG  
2573 C  CG  B LEU   A 126 ? 0.1151 0.1277 0.1328 -0.0054 0.0036  -0.0145 126 LEU   A CG  
2574 C  CD1 A LEU   A 126 ? 0.1415 0.1827 0.2420 -0.0035 0.0047  0.0150  126 LEU   A CD1 
2575 C  CD1 B LEU   A 126 ? 0.1137 0.1265 0.1426 -0.0079 0.0006  -0.0247 126 LEU   A CD1 
2576 C  CD2 A LEU   A 126 ? 0.1405 0.1589 0.1947 -0.0157 0.0140  0.0193  126 LEU   A CD2 
2577 C  CD2 B LEU   A 126 ? 0.1102 0.1309 0.1244 -0.0038 0.0048  -0.0135 126 LEU   A CD2 
2600 N  N   A LEU   A 127 ? 0.1353 0.1372 0.1770 0.0031  -0.0004 0.0248  127 LEU   A N   
2601 N  N   B LEU   A 127 ? 0.1202 0.1324 0.1282 -0.0103 -0.0010 0.0181  127 LEU   A N   
2602 C  CA  A LEU   A 127 ? 0.1303 0.1413 0.1688 0.0006  -0.0024 0.0252  127 LEU   A CA  
2603 C  CA  B LEU   A 127 ? 0.1167 0.1373 0.1268 -0.0107 -0.0026 0.0218  127 LEU   A CA  
2604 C  C   A LEU   A 127 ? 0.1305 0.1360 0.1640 0.0004  -0.0007 0.0177  127 LEU   A C   
2605 C  C   B LEU   A 127 ? 0.1204 0.1359 0.1395 -0.0159 -0.0031 0.0149  127 LEU   A C   
2606 O  O   A LEU   A 127 ? 0.1434 0.1405 0.1665 -0.0079 -0.0060 0.0298  127 LEU   A O   
2607 O  O   B LEU   A 127 ? 0.1239 0.1373 0.1415 -0.0181 -0.0017 0.0152  127 LEU   A O   
2608 C  CB  A LEU   A 127 ? 0.1372 0.1539 0.1600 0.0056  -0.0054 0.0289  127 LEU   A CB  
2609 C  CB  B LEU   A 127 ? 0.1135 0.1432 0.1162 -0.0084 -0.0131 0.0191  127 LEU   A CB  
2610 C  CG  A LEU   A 127 ? 0.1417 0.1537 0.1599 0.0091  -0.0058 0.0245  127 LEU   A CG  
2611 C  CG  B LEU   A 127 ? 0.1121 0.1498 0.1081 -0.0028 -0.0181 0.0234  127 LEU   A CG  
2612 C  CD1 A LEU   A 127 ? 0.1487 0.1500 0.1712 0.0061  -0.0063 0.0144  127 LEU   A CD1 
2613 C  CD1 B LEU   A 127 ? 0.1133 0.1534 0.1078 0.0014  -0.0083 0.0260  127 LEU   A CD1 
2614 C  CD2 A LEU   A 127 ? 0.1574 0.1510 0.1787 0.0080  -0.0198 0.0185  127 LEU   A CD2 
2615 C  CD2 B LEU   A 127 ? 0.1172 0.1554 0.1088 0.0006  -0.0320 0.0147  127 LEU   A CD2 
2638 N  N   A SER   A 128 ? 0.1358 0.1310 0.1462 -0.0004 0.0003  0.0104  128 SER   A N   
2639 N  N   B SER   A 128 ? 0.1241 0.1300 0.1435 -0.0216 -0.0064 0.0144  128 SER   A N   
2640 C  CA  A SER   A 128 ? 0.1489 0.1394 0.1417 0.0010  -0.0051 0.0166  128 SER   A CA  
2641 C  CA  B SER   A 128 ? 0.1268 0.1264 0.1389 -0.0225 -0.0058 0.0105  128 SER   A CA  
2642 C  C   A SER   A 128 ? 0.1535 0.1388 0.1500 0.0041  -0.0032 0.0248  128 SER   A C   
2643 C  C   B SER   A 128 ? 0.1221 0.1242 0.1396 -0.0221 -0.0166 0.0094  128 SER   A C   
2644 O  O   A SER   A 128 ? 0.1713 0.1588 0.1618 0.0039  -0.0079 0.0161  128 SER   A O   
2645 O  O   B SER   A 128 ? 0.1178 0.1255 0.1388 -0.0248 -0.0257 0.0073  128 SER   A O   
2646 C  CB  A SER   A 128 ? 0.1430 0.1450 0.1379 -0.0040 0.0001  0.0109  128 SER   A CB  
2647 C  CB  B SER   A 128 ? 0.1348 0.1288 0.1403 -0.0263 0.0032  0.0146  128 SER   A CB  
2648 O  OG  A SER   A 128 ? 0.1451 0.1450 0.1553 -0.0032 0.0011  0.0109  128 SER   A OG  
2649 O  OG  B SER   A 128 ? 0.1402 0.1303 0.1379 -0.0256 0.0143  0.0198  128 SER   A OG  
2660 N  N   A ALA   A 129 ? 0.1465 0.1427 0.1623 -0.0014 -0.0060 0.0290  129 ALA   A N   
2661 N  N   B ALA   A 129 ? 0.1235 0.1258 0.1464 -0.0146 -0.0158 0.0078  129 ALA   A N   
2662 C  CA  A ALA   A 129 ? 0.1400 0.1475 0.1762 0.0026  -0.0084 0.0224  129 ALA   A CA  
2663 C  CA  B ALA   A 129 ? 0.1249 0.1272 0.1533 -0.0076 -0.0106 0.0036  129 ALA   A CA  
2664 C  C   A ALA   A 129 ? 0.1435 0.1410 0.1676 -0.0010 -0.0144 0.0180  129 ALA   A C   
2665 C  C   B ALA   A 129 ? 0.1335 0.1355 0.1623 0.0026  -0.0036 0.0028  129 ALA   A C   
2666 O  O   A ALA   A 129 ? 0.1443 0.1393 0.1725 -0.0082 -0.0090 0.0245  129 ALA   A O   
2667 O  O   B ALA   A 129 ? 0.1368 0.1406 0.1709 0.0037  -0.0004 0.0105  129 ALA   A O   
2668 C  CB  A ALA   A 129 ? 0.1412 0.1705 0.1948 0.0140  -0.0070 0.0310  129 ALA   A CB  
2669 C  CB  B ALA   A 129 ? 0.1177 0.1201 0.1436 -0.0093 -0.0144 0.0055  129 ALA   A CB  
2680 N  N   A GLY   A 130 ? 0.1491 0.1409 0.2094 0.0029  -0.0058 0.0053  130 GLY   A N   
2681 N  N   B GLY   A 130 ? 0.1395 0.1410 0.1743 0.0062  0.0030  0.0058  130 GLY   A N   
2682 C  CA  A GLY   A 130 ? 0.1625 0.1449 0.2066 0.0100  -0.0051 0.0116  130 GLY   A CA  
2683 C  CA  B GLY   A 130 ? 0.1447 0.1432 0.1709 0.0122  0.0072  0.0063  130 GLY   A CA  
2684 C  C   A GLY   A 130 ? 0.1664 0.1463 0.1866 0.0077  -0.0087 0.0078  130 GLY   A C   
2685 C  C   B GLY   A 130 ? 0.1483 0.1459 0.1666 0.0119  0.0131  -0.0011 130 GLY   A C   
2686 O  O   A GLY   A 130 ? 0.1674 0.1425 0.1869 0.0106  -0.0135 0.0017  130 GLY   A O   
2687 O  O   B GLY   A 130 ? 0.1479 0.1459 0.1640 0.0119  0.0179  -0.0102 130 GLY   A O   
2694 N  N   A ILE   A 131 ? 0.1747 0.1420 0.1670 0.0002  -0.0135 0.0163  131 ILE   A N   
2695 N  N   B ILE   A 131 ? 0.1540 0.1482 0.1672 0.0090  0.0079  -0.0036 131 ILE   A N   
2696 C  CA  A ILE   A 131 ? 0.1871 0.1404 0.1512 -0.0112 -0.0227 0.0135  131 ILE   A CA  
2697 C  CA  B ILE   A 131 ? 0.1573 0.1487 0.1612 0.0021  0.0026  -0.0041 131 ILE   A CA  
2698 C  C   A ILE   A 131 ? 0.1765 0.1409 0.1506 -0.0116 -0.0175 0.0215  131 ILE   A C   
2699 C  C   B ILE   A 131 ? 0.1566 0.1461 0.1536 -0.0018 -0.0003 -0.0040 131 ILE   A C   
2700 O  O   A ILE   A 131 ? 0.1831 0.1496 0.1728 -0.0030 -0.0166 0.0254  131 ILE   A O   
2701 O  O   B ILE   A 131 ? 0.1562 0.1453 0.1610 0.0013  -0.0048 -0.0044 131 ILE   A O   
2702 C  CB  A ILE   A 131 ? 0.2145 0.1536 0.1534 -0.0203 -0.0317 0.0083  131 ILE   A CB  
2703 C  CB  B ILE   A 131 ? 0.1619 0.1543 0.1675 -0.0021 0.0024  -0.0008 131 ILE   A CB  
2704 C  CG1 A ILE   A 131 ? 0.2264 0.1846 0.1490 -0.0317 -0.0312 0.0122  131 ILE   A CG1 
2705 C  CG1 B ILE   A 131 ? 0.1647 0.1613 0.1714 -0.0029 -0.0057 0.0098  131 ILE   A CG1 
2706 C  CG2 A ILE   A 131 ? 0.2317 0.1461 0.1624 -0.0104 -0.0291 -0.0024 131 ILE   A CG2 
2707 C  CG2 B ILE   A 131 ? 0.1646 0.1551 0.1697 -0.0019 0.0048  -0.0029 131 ILE   A CG2 
2708 C  CD1 A ILE   A 131 ? 0.2321 0.1989 0.1820 -0.0380 -0.0343 0.0032  131 ILE   A CD1 
2709 C  CD1 B ILE   A 131 ? 0.1673 0.1632 0.1739 -0.0046 -0.0104 0.0182  131 ILE   A CD1 
2732 N  N   A PHE   A 132 ? 0.1685 0.1404 0.1463 -0.0018 -0.0161 0.0192  132 PHE   A N   
2733 N  N   B PHE   A 132 ? 0.1588 0.1467 0.1512 -0.0042 -0.0010 0.0030  132 PHE   A N   
2734 C  CA  A PHE   A 132 ? 0.1743 0.1478 0.1473 -0.0025 -0.0085 0.0121  132 PHE   A CA  
2735 C  CA  B PHE   A 132 ? 0.1635 0.1490 0.1511 -0.0054 -0.0016 0.0047  132 PHE   A CA  
2736 C  C   A PHE   A 132 ? 0.1803 0.1613 0.1583 -0.0049 -0.0127 0.0150  132 PHE   A C   
2737 C  C   B PHE   A 132 ? 0.1681 0.1529 0.1544 -0.0057 -0.0074 0.0089  132 PHE   A C   
2738 O  O   A PHE   A 132 ? 0.1883 0.1681 0.1522 -0.0109 -0.0143 0.0122  132 PHE   A O   
2739 O  O   B PHE   A 132 ? 0.1717 0.1550 0.1496 -0.0081 -0.0105 0.0077  132 PHE   A O   
2740 C  CB  A PHE   A 132 ? 0.1649 0.1406 0.1529 -0.0015 -0.0145 0.0181  132 PHE   A CB  
2741 C  CB  B PHE   A 132 ? 0.1611 0.1462 0.1483 -0.0049 -0.0000 0.0018  132 PHE   A CB  
2742 C  CG  A PHE   A 132 ? 0.1667 0.1403 0.1500 0.0013  -0.0209 0.0161  132 PHE   A CG  
2743 C  CG  B PHE   A 132 ? 0.1606 0.1474 0.1462 -0.0030 -0.0031 -0.0046 132 PHE   A CG  
2744 C  CD1 A PHE   A 132 ? 0.1645 0.1531 0.1694 0.0041  -0.0182 -0.0042 132 PHE   A CD1 
2745 C  CD1 B PHE   A 132 ? 0.1606 0.1521 0.1528 -0.0018 -0.0036 -0.0107 132 PHE   A CD1 
2746 C  CD2 A PHE   A 132 ? 0.1689 0.1513 0.1532 0.0019  -0.0138 0.0076  132 PHE   A CD2 
2747 C  CD2 B PHE   A 132 ? 0.1616 0.1475 0.1439 -0.0029 -0.0028 -0.0138 132 PHE   A CD2 
2748 C  CE1 A PHE   A 132 ? 0.1662 0.1635 0.1752 0.0094  -0.0218 -0.0088 132 PHE   A CE1 
2749 C  CE1 B PHE   A 132 ? 0.1614 0.1557 0.1566 -0.0006 -0.0052 -0.0128 132 PHE   A CE1 
2750 C  CE2 A PHE   A 132 ? 0.1635 0.1598 0.1674 0.0105  -0.0165 0.0062  132 PHE   A CE2 
2751 C  CE2 B PHE   A 132 ? 0.1610 0.1530 0.1544 -0.0001 -0.0048 -0.0148 132 PHE   A CE2 
2752 C  CZ  A PHE   A 132 ? 0.1634 0.1629 0.1672 0.0031  -0.0235 0.0019  132 PHE   A CZ  
2753 C  CZ  B PHE   A 132 ? 0.1612 0.1559 0.1566 -0.0022 -0.0061 -0.0154 132 PHE   A CZ  
2772 N  N   A GLY   A 133 ? 0.1835 0.1680 0.1526 0.0002  -0.0358 0.0097  133 GLY   A N   
2773 N  N   B GLY   A 133 ? 0.1695 0.1541 0.1573 -0.0048 -0.0135 0.0070  133 GLY   A N   
2774 C  CA  A GLY   A 133 ? 0.1898 0.1769 0.1686 -0.0021 -0.0417 0.0043  133 GLY   A CA  
2775 C  CA  B GLY   A 133 ? 0.1706 0.1562 0.1629 -0.0033 -0.0126 0.0025  133 GLY   A CA  
2776 C  C   A GLY   A 133 ? 0.1902 0.1808 0.1709 -0.0054 -0.0483 -0.0046 133 GLY   A C   
2777 C  C   B GLY   A 133 ? 0.1692 0.1565 0.1613 -0.0010 -0.0120 -0.0048 133 GLY   A C   
2778 O  O   A GLY   A 133 ? 0.2062 0.1919 0.1940 -0.0026 -0.0476 -0.0230 133 GLY   A O   
2779 O  O   B GLY   A 133 ? 0.1710 0.1568 0.1647 0.0040  -0.0138 -0.0138 133 GLY   A O   
2786 N  N   A ALA   A 134 ? 0.1827 0.1679 0.1729 -0.0102 -0.0402 -0.0021 134 ALA   A N   
2787 N  N   B ALA   A 134 ? 0.1676 0.1522 0.1616 -0.0023 -0.0093 -0.0084 134 ALA   A N   
2788 C  CA  A ALA   A 134 ? 0.1769 0.1706 0.1903 -0.0084 -0.0360 -0.0087 134 ALA   A CA  
2789 C  CA  B ALA   A 134 ? 0.1663 0.1493 0.1647 -0.0007 -0.0101 -0.0126 134 ALA   A CA  
2790 C  C   A ALA   A 134 ? 0.1812 0.1796 0.1818 -0.0062 -0.0305 0.0007  134 ALA   A C   
2791 C  C   B ALA   A 134 ? 0.1645 0.1478 0.1565 0.0019  -0.0126 -0.0130 134 ALA   A C   
2792 O  O   A ALA   A 134 ? 0.1972 0.1948 0.1983 -0.0026 -0.0080 -0.0010 134 ALA   A O   
2793 O  O   B ALA   A 134 ? 0.1652 0.1505 0.1518 -0.0001 -0.0033 -0.0223 134 ALA   A O   
2794 C  CB  A ALA   A 134 ? 0.1870 0.1695 0.2307 -0.0065 -0.0379 -0.0079 134 ALA   A CB  
2795 C  CB  B ALA   A 134 ? 0.1682 0.1496 0.1795 -0.0007 -0.0096 -0.0107 134 ALA   A CB  
2806 N  N   A ASP   A 135 ? 0.1870 0.1805 0.1994 -0.0111 -0.0350 0.0092  135 ASP   A N   
2807 N  N   B ASP   A 135 ? 0.1650 0.1490 0.1545 0.0006  -0.0209 -0.0051 135 ASP   A N   
2808 C  CA  A ASP   A 135 ? 0.1863 0.1901 0.2269 -0.0180 -0.0436 0.0193  135 ASP   A CA  
2809 C  CA  B ASP   A 135 ? 0.1592 0.1503 0.1470 -0.0019 -0.0270 -0.0016 135 ASP   A CA  
2810 C  C   A ASP   A 135 ? 0.1721 0.1788 0.2278 -0.0156 -0.0295 0.0313  135 ASP   A C   
2811 C  C   B ASP   A 135 ? 0.1515 0.1452 0.1430 0.0027  -0.0211 0.0012  135 ASP   A C   
2812 O  O   A ASP   A 135 ? 0.1690 0.1718 0.2294 -0.0128 -0.0257 0.0374  135 ASP   A O   
2813 O  O   B ASP   A 135 ? 0.1496 0.1453 0.1468 0.0017  -0.0250 0.0036  135 ASP   A O   
2814 C  CB  A ASP   A 135 ? 0.2103 0.2201 0.2641 -0.0363 -0.0592 0.0125  135 ASP   A CB  
2815 C  CB  B ASP   A 135 ? 0.1604 0.1554 0.1396 -0.0038 -0.0364 -0.0050 135 ASP   A CB  
2816 C  CG  A ASP   A 135 ? 0.2305 0.2480 0.3063 -0.0532 -0.0617 0.0097  135 ASP   A CG  
2817 C  CG  B ASP   A 135 ? 0.1616 0.1627 0.1434 -0.0060 -0.0411 -0.0096 135 ASP   A CG  
2818 O  OD1 A ASP   A 135 ? 0.2267 0.2589 0.3063 -0.0577 -0.0663 0.0274  135 ASP   A OD1 
2819 O  OD1 B ASP   A 135 ? 0.1616 0.1609 0.1391 -0.0047 -0.0401 -0.0107 135 ASP   A OD1 
2820 O  OD2 A ASP   A 135 ? 0.2621 0.2693 0.3576 -0.0562 -0.0424 0.0051  135 ASP   A OD2 
2821 O  OD2 B ASP   A 135 ? 0.1599 0.1670 0.1479 -0.0087 -0.0500 -0.0144 135 ASP   A OD2 
2830 N  N   A PRO   A 136 ? 0.1594 0.1893 0.2325 -0.0007 -0.0145 0.0476  136 PRO   A N   
2831 N  N   B PRO   A 136 ? 0.1487 0.1400 0.1351 0.0082  -0.0122 0.0018  136 PRO   A N   
2832 C  CA  A PRO   A 136 ? 0.1532 0.1891 0.2439 -0.0018 0.0004  0.0400  136 PRO   A CA  
2833 C  CA  B PRO   A 136 ? 0.1481 0.1467 0.1421 0.0027  -0.0120 -0.0009 136 PRO   A CA  
2834 C  C   A PRO   A 136 ? 0.1340 0.1837 0.2478 0.0034  0.0005  0.0424  136 PRO   A C   
2835 C  C   B PRO   A 136 ? 0.1468 0.1541 0.1462 -0.0029 -0.0161 0.0012  136 PRO   A C   
2836 O  O   A PRO   A 136 ? 0.1309 0.1855 0.2408 -0.0052 0.0032  0.0400  136 PRO   A O   
2837 O  O   B PRO   A 136 ? 0.1450 0.1517 0.1325 -0.0026 -0.0121 -0.0017 136 PRO   A O   
2838 C  CB  A PRO   A 136 ? 0.1775 0.1941 0.2629 0.0010  -0.0011 0.0333  136 PRO   A CB  
2839 C  CB  B PRO   A 136 ? 0.1539 0.1442 0.1490 0.0067  -0.0093 -0.0040 136 PRO   A CB  
2840 C  CG  A PRO   A 136 ? 0.1934 0.2083 0.2803 0.0110  -0.0031 0.0323  136 PRO   A CG  
2841 C  CG  B PRO   A 136 ? 0.1574 0.1442 0.1507 0.0121  -0.0010 -0.0046 136 PRO   A CG  
2842 C  CD  A PRO   A 136 ? 0.1765 0.1989 0.2544 0.0132  -0.0029 0.0486  136 PRO   A CD  
2843 C  CD  B PRO   A 136 ? 0.1511 0.1377 0.1355 0.0139  -0.0020 0.0073  136 PRO   A CD  
2858 N  N   A ILE   A 137 ? 0.1305 0.1827 0.2528 0.0018  -0.0140 0.0485  137 ILE   A N   
2859 N  N   B ILE   A 137 ? 0.1482 0.1605 0.1631 -0.0074 -0.0188 0.0035  137 ILE   A N   
2860 C  CA  A ILE   A 137 ? 0.1341 0.1887 0.2685 -0.0142 -0.0274 0.0410  137 ILE   A CA  
2861 C  CA  B ILE   A 137 ? 0.1516 0.1707 0.1849 -0.0094 -0.0167 0.0060  137 ILE   A CA  
2862 C  C   A ILE   A 137 ? 0.1329 0.1813 0.2502 -0.0200 -0.0316 0.0378  137 ILE   A C   
2863 C  C   B ILE   A 137 ? 0.1519 0.1762 0.1861 -0.0122 -0.0111 0.0106  137 ILE   A C   
2864 O  O   A ILE   A 137 ? 0.1454 0.1800 0.2560 -0.0158 -0.0209 0.0356  137 ILE   A O   
2865 O  O   B ILE   A 137 ? 0.1521 0.1784 0.1899 -0.0139 -0.0067 0.0124  137 ILE   A O   
2866 C  CB  A ILE   A 137 ? 0.1466 0.2043 0.3003 -0.0183 -0.0452 0.0398  137 ILE   A CB  
2867 C  CB  B ILE   A 137 ? 0.1557 0.1742 0.2034 -0.0085 -0.0258 0.0049  137 ILE   A CB  
2868 C  CG1 A ILE   A 137 ? 0.1605 0.2307 0.3418 -0.0119 -0.0430 0.0454  137 ILE   A CG1 
2869 C  CG1 B ILE   A 137 ? 0.1587 0.1791 0.2185 -0.0046 -0.0326 0.0091  137 ILE   A CG1 
2870 C  CG2 A ILE   A 137 ? 0.1560 0.2059 0.3121 -0.0236 -0.0547 0.0275  137 ILE   A CG2 
2871 C  CG2 B ILE   A 137 ? 0.1594 0.1749 0.2107 -0.0082 -0.0296 0.0007  137 ILE   A CG2 
2872 C  CD1 A ILE   A 137 ? 0.1820 0.2485 0.3733 -0.0069 -0.0358 0.0467  137 ILE   A CD1 
2873 C  CD1 B ILE   A 137 ? 0.1616 0.1801 0.2285 -0.0039 -0.0340 0.0112  137 ILE   A CD1 
2896 N  N   A HIS   A 138 ? 0.1330 0.1940 0.2461 -0.0185 -0.0226 0.0351  138 HIS   A N   
2897 N  N   B HIS   A 138 ? 0.1522 0.1809 0.1901 -0.0128 -0.0051 0.0121  138 HIS   A N   
2898 C  CA  A HIS   A 138 ? 0.1457 0.1981 0.2262 -0.0162 -0.0187 0.0281  138 HIS   A CA  
2899 C  CA  B HIS   A 138 ? 0.1535 0.1809 0.1938 -0.0119 -0.0055 0.0147  138 HIS   A CA  
2900 C  C   A HIS   A 138 ? 0.1375 0.1869 0.2167 -0.0089 -0.0149 0.0319  138 HIS   A C   
2901 C  C   B HIS   A 138 ? 0.1430 0.1774 0.2006 -0.0106 -0.0070 0.0294  138 HIS   A C   
2902 O  O   A HIS   A 138 ? 0.1476 0.1868 0.2165 -0.0127 -0.0097 0.0221  138 HIS   A O   
2903 O  O   B HIS   A 138 ? 0.1457 0.1767 0.1977 -0.0119 -0.0064 0.0281  138 HIS   A O   
2904 C  CB  A HIS   A 138 ? 0.1642 0.2164 0.2151 -0.0134 -0.0248 0.0189  138 HIS   A CB  
2905 C  CB  B HIS   A 138 ? 0.1607 0.1844 0.1921 -0.0081 -0.0045 0.0017  138 HIS   A CB  
2906 C  CG  A HIS   A 138 ? 0.1854 0.2325 0.2249 -0.0145 -0.0255 0.0131  138 HIS   A CG  
2907 C  CG  B HIS   A 138 ? 0.1674 0.1867 0.1957 -0.0063 -0.0053 -0.0094 138 HIS   A CG  
2908 N  ND1 A HIS   A 138 ? 0.2020 0.2463 0.2456 -0.0207 -0.0284 0.0022  138 HIS   A ND1 
2909 N  ND1 B HIS   A 138 ? 0.1724 0.1895 0.2041 -0.0059 -0.0081 -0.0158 138 HIS   A ND1 
2910 C  CD2 A HIS   A 138 ? 0.1846 0.2394 0.2235 -0.0057 -0.0272 0.0195  138 HIS   A CD2 
2911 C  CD2 B HIS   A 138 ? 0.1679 0.1855 0.1961 -0.0026 -0.0034 -0.0118 138 HIS   A CD2 
2912 C  CE1 A HIS   A 138 ? 0.2057 0.2509 0.2473 -0.0114 -0.0288 0.0025  138 HIS   A CE1 
2913 C  CE1 B HIS   A 138 ? 0.1738 0.1891 0.2052 -0.0015 -0.0076 -0.0162 138 HIS   A CE1 
2914 N  NE2 A HIS   A 138 ? 0.1931 0.2498 0.2348 -0.0062 -0.0173 0.0088  138 HIS   A NE2 
2915 N  NE2 B HIS   A 138 ? 0.1714 0.1878 0.2007 0.0003  -0.0023 -0.0161 138 HIS   A NE2 
2930 N  N   . SER   A 139 ? 0.1332 0.1752 0.2195 -0.0128 -0.0120 0.0431  139 SER   A N   
2931 C  CA  . SER   A 139 ? 0.1350 0.1647 0.2131 -0.0127 -0.0091 0.0405  139 SER   A CA  
2932 C  C   . SER   A 139 ? 0.1282 0.1572 0.2041 -0.0128 -0.0038 0.0341  139 SER   A C   
2933 O  O   . SER   A 139 ? 0.1247 0.1531 0.2096 -0.0122 0.0004  0.0404  139 SER   A O   
2934 C  CB  . SER   A 139 ? 0.1330 0.1648 0.2147 -0.0134 -0.0111 0.0398  139 SER   A CB  
2935 O  OG  . SER   A 139 ? 0.1321 0.1610 0.2154 -0.0191 -0.0156 0.0443  139 SER   A OG  
2942 N  N   . LEU   A 140 ? 0.1262 0.1595 0.2095 -0.0096 -0.0002 0.0442  140 LEU   A N   
2943 C  CA  . LEU   A 140 ? 0.1232 0.1565 0.2188 -0.0051 -0.0049 0.0423  140 LEU   A CA  
2944 C  C   . LEU   A 140 ? 0.1179 0.1634 0.2085 -0.0125 -0.0045 0.0363  140 LEU   A C   
2945 O  O   . LEU   A 140 ? 0.1257 0.1650 0.2166 -0.0093 -0.0069 0.0366  140 LEU   A O   
2946 C  CB  . LEU   A 140 ? 0.1263 0.1626 0.2235 -0.0114 0.0024  0.0417  140 LEU   A CB  
2947 C  CG  . LEU   A 140 ? 0.1281 0.1773 0.2295 -0.0192 0.0079  0.0478  140 LEU   A CG  
2948 C  CD1 . LEU   A 140 ? 0.1309 0.1846 0.2274 -0.0097 0.0096  0.0440  140 LEU   A CD1 
2949 C  CD2 . LEU   A 140 ? 0.1328 0.1902 0.2429 -0.0157 0.0134  0.0579  140 LEU   A CD2 
2961 N  N   . ARG   A 141 ? 0.1274 0.1635 0.2179 -0.0120 -0.0040 0.0368  141 ARG   A N   
2962 C  CA  . ARG   A 141 ? 0.1408 0.1800 0.2336 -0.0240 -0.0149 0.0183  141 ARG   A CA  
2963 C  C   . ARG   A 141 ? 0.1410 0.1609 0.2123 -0.0189 -0.0073 0.0209  141 ARG   A C   
2964 O  O   . ARG   A 141 ? 0.1391 0.1574 0.2183 -0.0180 0.0009  0.0118  141 ARG   A O   
2965 C  CB  . ARG   A 141 ? 0.1551 0.2048 0.2663 -0.0278 -0.0306 -0.0016 141 ARG   A CB  
2966 C  CG  . ARG   A 141 ? 0.1955 0.2438 0.3125 -0.0248 -0.0223 -0.0109 141 ARG   A CG  
2967 C  CD  . ARG   A 141 ? 0.2222 0.2685 0.3383 -0.0322 -0.0173 -0.0129 141 ARG   A CD  
2968 N  NE  . ARG   A 141 ? 0.2035 0.2831 0.3387 -0.0373 -0.0251 -0.0140 141 ARG   A NE  
2969 C  CZ  . ARG   A 141 ? 0.2045 0.3006 0.3462 -0.0483 -0.0133 -0.0089 141 ARG   A CZ  
2970 N  NH1 . ARG   A 141 ? 0.1967 0.3037 0.3380 -0.0602 0.0110  -0.0256 141 ARG   A NH1 
2971 N  NH2 . ARG   A 141 ? 0.2027 0.3089 0.3659 -0.0404 -0.0269 0.0036  141 ARG   A NH2 
2985 N  N   . VAL   A 142 ? 0.1327 0.1595 0.1954 -0.0135 -0.0050 0.0146  142 VAL   A N   
2986 C  CA  . VAL   A 142 ? 0.1343 0.1549 0.2029 -0.0116 0.0088  0.0136  142 VAL   A CA  
2987 C  C   . VAL   A 142 ? 0.1209 0.1469 0.1976 -0.0161 0.0019  0.0208  142 VAL   A C   
2988 O  O   . VAL   A 142 ? 0.1274 0.1521 0.2022 -0.0036 0.0015  0.0201  142 VAL   A O   
2989 C  CB  . VAL   A 142 ? 0.1450 0.1677 0.1950 -0.0124 0.0044  0.0210  142 VAL   A CB  
2990 C  CG1 . VAL   A 142 ? 0.1455 0.1655 0.1918 -0.0113 0.0053  0.0149  142 VAL   A CG1 
2991 C  CG2 . VAL   A 142 ? 0.1562 0.1841 0.2192 -0.0070 0.0038  0.0220  142 VAL   A CG2 
3001 N  N   . CYS   A 143 ? 0.1225 0.1488 0.1917 -0.0143 -0.0025 0.0161  143 CYS   A N   
3002 C  CA  . CYS   A 143 ? 0.1254 0.1444 0.1944 -0.0127 0.0057  0.0221  143 CYS   A CA  
3003 C  C   . CYS   A 143 ? 0.1232 0.1376 0.1925 -0.0112 0.0005  0.0307  143 CYS   A C   
3004 O  O   . CYS   A 143 ? 0.1224 0.1409 0.1955 -0.0049 0.0035  0.0261  143 CYS   A O   
3005 C  CB  . CYS   A 143 ? 0.1371 0.1492 0.1991 -0.0088 0.0106  0.0270  143 CYS   A CB  
3006 S  SG  . CYS   A 143 ? 0.1535 0.1546 0.1886 0.0041  0.0094  0.0203  143 CYS   A SG  
3012 N  N   . VAL   A 144 ? 0.1254 0.1482 0.2134 -0.0083 0.0060  0.0313  144 VAL   A N   
3013 C  CA  . VAL   A 144 ? 0.1302 0.1526 0.2472 -0.0112 0.0146  0.0344  144 VAL   A CA  
3014 C  C   . VAL   A 144 ? 0.1333 0.1453 0.2397 -0.0207 -0.0086 0.0230  144 VAL   A C   
3015 O  O   . VAL   A 144 ? 0.1464 0.1493 0.2380 -0.0039 -0.0066 0.0275  144 VAL   A O   
3016 C  CB  . VAL   A 144 ? 0.1530 0.1778 0.3099 -0.0017 0.0357  0.0368  144 VAL   A CB  
3017 C  CG1 . VAL   A 144 ? 0.1591 0.1961 0.3512 -0.0089 0.0257  0.0338  144 VAL   A CG1 
3018 C  CG2 . VAL   A 144 ? 0.1369 0.1801 0.3157 -0.0054 0.0433  0.0460  144 VAL   A CG2 
3028 N  N   . ASP   A 145 ? 0.1375 0.1451 0.2416 -0.0191 -0.0010 0.0133  145 ASP   A N   
3029 C  CA  . ASP   A 145 ? 0.1483 0.1532 0.2427 -0.0184 -0.0033 0.0057  145 ASP   A CA  
3030 C  C   . ASP   A 145 ? 0.1495 0.1443 0.2395 -0.0140 0.0014  -0.0045 145 ASP   A C   
3031 O  O   . ASP   A 145 ? 0.1641 0.1521 0.2862 -0.0180 0.0023  -0.0349 145 ASP   A O   
3032 C  CB  . ASP   A 145 ? 0.1622 0.1745 0.2596 -0.0305 -0.0193 0.0114  145 ASP   A CB  
3033 C  CG  . ASP   A 145 ? 0.1824 0.2099 0.2815 -0.0426 -0.0281 0.0176  145 ASP   A CG  
3034 O  OD1 . ASP   A 145 ? 0.1716 0.2232 0.2920 -0.0514 -0.0202 0.0164  145 ASP   A OD1 
3035 O  OD2 . ASP   A 145 ? 0.2062 0.2305 0.2819 -0.0496 -0.0434 0.0138  145 ASP   A OD2 
3040 N  N   . THR   A 146 ? 0.1345 0.1374 0.2159 -0.0125 0.0107  0.0052  146 THR   A N   
3041 C  CA  . THR   A 146 ? 0.1310 0.1338 0.1937 -0.0049 0.0060  0.0084  146 THR   A CA  
3042 C  C   . THR   A 146 ? 0.1264 0.1311 0.1971 0.0043  0.0044  0.0168  146 THR   A C   
3043 O  O   . THR   A 146 ? 0.1394 0.1444 0.2135 0.0049  0.0041  0.0104  146 THR   A O   
3044 C  CB  . THR   A 146 ? 0.1279 0.1354 0.1943 -0.0014 0.0082  0.0129  146 THR   A CB  
3045 O  OG1 . THR   A 146 ? 0.1274 0.1503 0.2039 -0.0009 -0.0003 0.0125  146 THR   A OG1 
3046 C  CG2 . THR   A 146 ? 0.1306 0.1384 0.2097 -0.0073 0.0120  0.0096  146 THR   A CG2 
3054 N  N   . VAL   A 147 ? 0.1248 0.1340 0.1892 0.0021  0.0064  0.0121  147 VAL   A N   
3055 C  CA  . VAL   A 147 ? 0.1252 0.1378 0.1930 -0.0069 0.0215  0.0150  147 VAL   A CA  
3056 C  C   . VAL   A 147 ? 0.1289 0.1335 0.1975 -0.0125 0.0176  0.0209  147 VAL   A C   
3057 O  O   . VAL   A 147 ? 0.1305 0.1390 0.2134 -0.0101 0.0103  0.0219  147 VAL   A O   
3058 C  CB  . VAL   A 147 ? 0.1385 0.1371 0.1853 -0.0076 0.0193  0.0225  147 VAL   A CB  
3059 C  CG1 . VAL   A 147 ? 0.1753 0.1493 0.1883 -0.0060 0.0193  0.0299  147 VAL   A CG1 
3060 C  CG2 . VAL   A 147 ? 0.1469 0.1353 0.1873 -0.0122 0.0071  0.0181  147 VAL   A CG2 
3070 N  N   . ARG   A 148 ? 0.1316 0.1406 0.2099 -0.0124 0.0174  0.0379  148 ARG   A N   
3071 C  CA  . ARG   A 148 ? 0.1359 0.1393 0.2053 -0.0111 0.0126  0.0392  148 ARG   A CA  
3072 C  C   . ARG   A 148 ? 0.1477 0.1400 0.2044 -0.0180 0.0131  0.0500  148 ARG   A C   
3073 O  O   . ARG   A 148 ? 0.1778 0.1472 0.2274 -0.0195 0.0225  0.0400  148 ARG   A O   
3074 C  CB  . ARG   A 148 ? 0.1391 0.1403 0.2141 -0.0060 0.0176  0.0348  148 ARG   A CB  
3075 C  CG  . ARG   A 148 ? 0.1507 0.1423 0.2448 -0.0072 0.0268  0.0212  148 ARG   A CG  
3076 C  CD  . ARG   A 148 ? 0.1687 0.1412 0.2738 -0.0008 0.0408  0.0369  148 ARG   A CD  
3077 N  NE  . ARG   A 148 ? 0.1632 0.1467 0.2687 0.0067  0.0425  0.0472  148 ARG   A NE  
3078 C  CZ  . ARG   A 148 ? 0.1642 0.1307 0.2524 0.0040  0.0387  0.0392  148 ARG   A CZ  
3079 N  NH1 . ARG   A 148 ? 0.1702 0.1367 0.2529 -0.0062 0.0411  0.0146  148 ARG   A NH1 
3080 N  NH2 . ARG   A 148 ? 0.1585 0.1523 0.2532 0.0136  0.0381  0.0421  148 ARG   A NH2 
3094 N  N   . THR   A 149 ? 0.1492 0.1488 0.1923 -0.0177 0.0045  0.0437  149 THR   A N   
3095 C  CA  . THR   A 149 ? 0.1470 0.1544 0.1920 -0.0154 0.0081  0.0418  149 THR   A CA  
3096 C  C   . THR   A 149 ? 0.1428 0.1524 0.1880 -0.0205 0.0152  0.0438  149 THR   A C   
3097 O  O   . THR   A 149 ? 0.1424 0.1576 0.2067 -0.0197 0.0106  0.0420  149 THR   A O   
3098 C  CB  . THR   A 149 ? 0.1492 0.1674 0.2030 -0.0121 0.0050  0.0392  149 THR   A CB  
3099 O  OG1 . THR   A 149 ? 0.1537 0.1549 0.2200 -0.0265 0.0021  0.0293  149 THR   A OG1 
3100 C  CG2 . THR   A 149 ? 0.1462 0.1822 0.2078 -0.0045 -0.0068 0.0264  149 THR   A CG2 
3108 N  N   . ASN   A 150 ? 0.1458 0.1498 0.1879 -0.0099 0.0040  0.0448  150 ASN   A N   
3109 C  CA  . ASN   A 150 ? 0.1614 0.1624 0.1948 -0.0120 0.0098  0.0341  150 ASN   A CA  
3110 C  C   . ASN   A 150 ? 0.1421 0.1531 0.1955 -0.0177 0.0053  0.0396  150 ASN   A C   
3111 O  O   . ASN   A 150 ? 0.1532 0.1651 0.2347 -0.0144 -0.0089 0.0350  150 ASN   A O   
3112 C  CB  . ASN   A 150 ? 0.2049 0.1900 0.2150 -0.0211 0.0259  0.0522  150 ASN   A CB  
3113 C  CG  . ASN   A 150 ? 0.2599 0.2278 0.2852 -0.0148 0.0045  0.0644  150 ASN   A CG  
3114 O  OD1 . ASN   A 150 ? 0.2805 0.2390 0.3084 -0.0189 0.0065  0.0760  150 ASN   A OD1 
3115 N  ND2 . ASN   A 150 ? 0.2915 0.2491 0.3250 -0.0094 -0.0042 0.0669  150 ASN   A ND2 
3122 N  N   . VAL   A 151 ? 0.1434 0.1419 0.1926 -0.0189 0.0051  0.0380  151 VAL   A N   
3123 C  CA  . VAL   A 151 ? 0.1469 0.1453 0.1886 -0.0180 0.0137  0.0322  151 VAL   A CA  
3124 C  C   . VAL   A 151 ? 0.1390 0.1438 0.1978 -0.0256 0.0126  0.0356  151 VAL   A C   
3125 O  O   . VAL   A 151 ? 0.1496 0.1502 0.2311 -0.0190 0.0120  0.0344  151 VAL   A O   
3126 C  CB  . VAL   A 151 ? 0.1793 0.1665 0.1894 -0.0014 0.0151  0.0350  151 VAL   A CB  
3127 C  CG1 . VAL   A 151 ? 0.1655 0.1955 0.2044 -0.0050 0.0015  0.0314  151 VAL   A CG1 
3128 C  CG2 . VAL   A 151 ? 0.1930 0.1651 0.1882 0.0018  0.0237  0.0278  151 VAL   A CG2 
3138 N  N   . TYR   A 152 ? 0.1391 0.1459 0.1905 -0.0167 0.0111  0.0348  152 TYR   A N   
3139 C  CA  . TYR   A 152 ? 0.1411 0.1490 0.1776 -0.0164 0.0154  0.0332  152 TYR   A CA  
3140 C  C   . TYR   A 152 ? 0.1352 0.1475 0.1757 -0.0195 0.0196  0.0318  152 TYR   A C   
3141 O  O   . TYR   A 152 ? 0.1450 0.1427 0.1916 -0.0248 0.0142  0.0276  152 TYR   A O   
3142 C  CB  . TYR   A 152 ? 0.1542 0.1505 0.1826 -0.0077 0.0209  0.0372  152 TYR   A CB  
3143 C  CG  . TYR   A 152 ? 0.1666 0.1670 0.1882 -0.0174 0.0332  0.0393  152 TYR   A CG  
3144 C  CD1 . TYR   A 152 ? 0.1817 0.1892 0.2101 -0.0053 0.0344  0.0472  152 TYR   A CD1 
3145 C  CD2 . TYR   A 152 ? 0.1702 0.1737 0.1819 -0.0315 0.0273  0.0279  152 TYR   A CD2 
3146 C  CE1 . TYR   A 152 ? 0.2075 0.1973 0.2117 -0.0045 0.0212  0.0524  152 TYR   A CE1 
3147 C  CE2 . TYR   A 152 ? 0.1955 0.1886 0.1986 -0.0332 0.0229  0.0377  152 TYR   A CE2 
3148 C  CZ  . TYR   A 152 ? 0.2208 0.1953 0.1981 -0.0229 0.0220  0.0551  152 TYR   A CZ  
3149 O  OH  . TYR   A 152 ? 0.2507 0.2155 0.2195 -0.0150 0.0278  0.0693  152 TYR   A OH  
3159 N  N   . LEU   A 153 ? 0.1336 0.1441 0.1877 -0.0229 0.0193  0.0364  153 LEU   A N   
3160 C  CA  . LEU   A 153 ? 0.1318 0.1436 0.2022 -0.0115 0.0166  0.0372  153 LEU   A CA  
3161 C  C   . LEU   A 153 ? 0.1318 0.1453 0.2156 -0.0122 0.0213  0.0351  153 LEU   A C   
3162 O  O   . LEU   A 153 ? 0.1389 0.1578 0.2538 -0.0118 0.0299  0.0358  153 LEU   A O   
3163 C  CB  . LEU   A 153 ? 0.1248 0.1521 0.1983 -0.0098 0.0170  0.0354  153 LEU   A CB  
3164 C  CG  . LEU   A 153 ? 0.1357 0.1544 0.1965 -0.0129 0.0242  0.0306  153 LEU   A CG  
3165 C  CD1 . LEU   A 153 ? 0.1432 0.1584 0.1992 -0.0109 0.0035  0.0274  153 LEU   A CD1 
3166 C  CD2 . LEU   A 153 ? 0.1440 0.1586 0.2033 -0.0073 0.0263  0.0078  153 LEU   A CD2 
3178 N  N   A ALA   A 154 ? 0.1312 0.1403 0.2225 -0.0052 0.0278  0.0376  154 ALA   A N   
3179 N  N   B ALA   A 154 ? 0.1385 0.1528 0.2014 -0.0087 0.0208  0.0305  154 ALA   A N   
3180 C  CA  A ALA   A 154 ? 0.1471 0.1490 0.2533 -0.0038 0.0336  0.0383  154 ALA   A CA  
3181 C  CA  B ALA   A 154 ? 0.1495 0.1638 0.1961 -0.0052 0.0212  0.0259  154 ALA   A CA  
3182 C  C   A ALA   A 154 ? 0.1428 0.1478 0.2637 0.0026  0.0234  0.0496  154 ALA   A C   
3183 C  C   B ALA   A 154 ? 0.1586 0.1722 0.1896 -0.0008 0.0204  0.0245  154 ALA   A C   
3184 O  O   A ALA   A 154 ? 0.1502 0.1651 0.2635 -0.0068 0.0245  0.0524  154 ALA   A O   
3185 O  O   B ALA   A 154 ? 0.1602 0.1745 0.1836 -0.0027 0.0216  0.0236  154 ALA   A O   
3186 C  CB  A ALA   A 154 ? 0.1606 0.1491 0.2658 0.0026  0.0214  0.0310  154 ALA   A CB  
3187 C  CB  B ALA   A 154 ? 0.1498 0.1644 0.1968 -0.0038 0.0165  0.0241  154 ALA   A CB  
3198 N  N   A VAL   A 155 ? 0.1500 0.1448 0.2737 0.0084  0.0256  0.0626  155 VAL   A N   
3199 N  N   B VAL   A 155 ? 0.1692 0.1805 0.1916 0.0033  0.0231  0.0257  155 VAL   A N   
3200 C  CA  A VAL   A 155 ? 0.1546 0.1578 0.2878 0.0081  0.0171  0.0724  155 VAL   A CA  
3201 C  CA  B VAL   A 155 ? 0.1811 0.1919 0.1989 0.0087  0.0191  0.0259  155 VAL   A CA  
3202 C  C   A VAL   A 155 ? 0.1669 0.1558 0.3345 0.0164  0.0123  0.0739  155 VAL   A C   
3203 C  C   B VAL   A 155 ? 0.1962 0.2028 0.2118 0.0120  0.0174  0.0238  155 VAL   A C   
3204 O  O   A VAL   A 155 ? 0.1564 0.1558 0.3465 0.0183  0.0250  0.0662  155 VAL   A O   
3205 O  O   B VAL   A 155 ? 0.1949 0.2059 0.2067 0.0123  0.0191  0.0223  155 VAL   A O   
3206 C  CB  A VAL   A 155 ? 0.1508 0.1690 0.2650 0.0077  0.0034  0.0686  155 VAL   A CB  
3207 C  CB  B VAL   A 155 ? 0.1765 0.1919 0.1904 0.0109  0.0167  0.0270  155 VAL   A CB  
3208 C  CG1 A VAL   A 155 ? 0.1682 0.1867 0.2771 0.0125  -0.0040 0.0686  155 VAL   A CG1 
3209 C  CG1 B VAL   A 155 ? 0.1781 0.1941 0.1924 0.0126  0.0152  0.0273  155 VAL   A CG1 
3210 C  CG2 A VAL   A 155 ? 0.1596 0.1809 0.2732 0.0169  -0.0047 0.0644  155 VAL   A CG2 
3211 C  CG2 B VAL   A 155 ? 0.1762 0.1938 0.1899 0.0119  0.0151  0.0264  155 VAL   A CG2 
3230 N  N   A PHE   A 156 ? 0.1891 0.1660 0.3575 0.0118  0.0065  0.0909  156 PHE   A N   
3231 N  N   B PHE   A 156 ? 0.2135 0.2122 0.2298 0.0122  0.0136  0.0241  156 PHE   A N   
3232 C  CA  A PHE   A 156 ? 0.2115 0.1761 0.3902 0.0176  0.0102  0.0943  156 PHE   A CA  
3233 C  CA  B PHE   A 156 ? 0.2311 0.2208 0.2440 0.0131  0.0058  0.0233  156 PHE   A CA  
3234 C  C   A PHE   A 156 ? 0.2110 0.1867 0.3949 0.0315  0.0142  0.0994  156 PHE   A C   
3235 C  C   B PHE   A 156 ? 0.2439 0.2305 0.2634 0.0121  -0.0010 0.0231  156 PHE   A C   
3236 O  O   A PHE   A 156 ? 0.2196 0.2036 0.4146 0.0358  0.0131  0.0720  156 PHE   A O   
3237 O  O   B PHE   A 156 ? 0.2479 0.2340 0.2734 0.0130  -0.0031 0.0243  156 PHE   A O   
3238 C  CB  A PHE   A 156 ? 0.2365 0.1777 0.4061 0.0123  0.0053  0.1041  156 PHE   A CB  
3239 C  CB  B PHE   A 156 ? 0.2339 0.2202 0.2399 0.0144  0.0103  0.0203  156 PHE   A CB  
3240 C  CG  A PHE   A 156 ? 0.2633 0.1885 0.4162 0.0226  -0.0032 0.1020  156 PHE   A CG  
3241 C  CG  B PHE   A 156 ? 0.2356 0.2223 0.2371 0.0149  0.0130  0.0168  156 PHE   A CG  
3242 C  CD1 A PHE   A 156 ? 0.2762 0.2026 0.4259 0.0284  0.0038  0.0859  156 PHE   A CD1 
3243 C  CD1 B PHE   A 156 ? 0.2354 0.2245 0.2390 0.0130  0.0118  0.0126  156 PHE   A CD1 
3244 C  CD2 A PHE   A 156 ? 0.2732 0.1987 0.4183 0.0337  -0.0039 0.1121  156 PHE   A CD2 
3245 C  CD2 B PHE   A 156 ? 0.2392 0.2239 0.2387 0.0131  0.0132  0.0158  156 PHE   A CD2 
3246 C  CE1 A PHE   A 156 ? 0.2881 0.2104 0.4381 0.0300  0.0084  0.0783  156 PHE   A CE1 
3247 C  CE1 B PHE   A 156 ? 0.2366 0.2254 0.2373 0.0092  0.0104  0.0096  156 PHE   A CE1 
3248 C  CE2 A PHE   A 156 ? 0.2902 0.2128 0.4290 0.0378  0.0014  0.0904  156 PHE   A CE2 
3249 C  CE2 B PHE   A 156 ? 0.2399 0.2249 0.2380 0.0092  0.0130  0.0153  156 PHE   A CE2 
3250 C  CZ  A PHE   A 156 ? 0.2948 0.2146 0.4416 0.0403  0.0040  0.0700  156 PHE   A CZ  
3251 C  CZ  B PHE   A 156 ? 0.2384 0.2241 0.2334 0.0056  0.0134  0.0113  156 PHE   A CZ  
3270 N  N   A ASP   A 157 ? 0.2110 0.1874 0.3843 0.0254  0.0202  0.1222  157 ASP   A N   
3271 N  N   B ASP   A 157 ? 0.2515 0.2376 0.2699 0.0081  -0.0043 0.0259  157 ASP   A N   
3272 C  CA  A ASP   A 157 ? 0.2219 0.2037 0.3907 0.0271  0.0205  0.1273  157 ASP   A CA  
3273 C  CA  B ASP   A 157 ? 0.2578 0.2443 0.2712 0.0041  -0.0071 0.0274  157 ASP   A CA  
3274 C  C   A ASP   A 157 ? 0.2008 0.2136 0.3979 0.0310  0.0414  0.1320  157 ASP   A C   
3275 C  C   B ASP   A 157 ? 0.2560 0.2490 0.2770 0.0004  -0.0061 0.0249  157 ASP   A C   
3276 O  O   A ASP   A 157 ? 0.1848 0.2005 0.3878 0.0298  0.0449  0.1457  157 ASP   A O   
3277 O  O   B ASP   A 157 ? 0.2558 0.2492 0.2725 -0.0009 -0.0081 0.0255  157 ASP   A O   
3278 C  CB  A ASP   A 157 ? 0.2467 0.2137 0.3964 0.0296  0.0018  0.1311  157 ASP   A CB  
3279 C  CB  B ASP   A 157 ? 0.2647 0.2457 0.2696 0.0045  -0.0072 0.0338  157 ASP   A CB  
3280 C  CG  A ASP   A 157 ? 0.2706 0.2272 0.4247 0.0374  -0.0183 0.1240  157 ASP   A CG  
3281 C  CG  B ASP   A 157 ? 0.2707 0.2460 0.2697 0.0066  -0.0088 0.0381  157 ASP   A CG  
3282 O  OD1 A ASP   A 157 ? 0.3026 0.2393 0.4613 0.0348  -0.0482 0.1062  157 ASP   A OD1 
3283 O  OD1 B ASP   A 157 ? 0.2699 0.2448 0.2690 0.0079  -0.0098 0.0387  157 ASP   A OD1 
3284 O  OD2 A ASP   A 157 ? 0.2483 0.2289 0.4322 0.0387  -0.0024 0.1253  157 ASP   A OD2 
3285 O  OD2 B ASP   A 157 ? 0.2745 0.2465 0.2684 0.0070  -0.0090 0.0413  157 ASP   A OD2 
3294 N  N   A LYS   A 158 ? 0.2055 0.2399 0.4172 0.0386  0.0509  0.1187  158 LYS   A N   
3295 N  N   B LYS   A 158 ? 0.2544 0.2530 0.2846 -0.0020 -0.0032 0.0234  158 LYS   A N   
3296 C  CA  A LYS   A 158 ? 0.2027 0.2691 0.4259 0.0521  0.0625  0.1164  158 LYS   A CA  
3297 C  CA  B LYS   A 158 ? 0.2543 0.2584 0.2927 -0.0045 0.0014  0.0218  158 LYS   A CA  
3298 C  C   A LYS   A 158 ? 0.1809 0.2785 0.4111 0.0588  0.0515  0.1441  158 LYS   A C   
3299 C  C   B LYS   A 158 ? 0.2473 0.2567 0.2876 -0.0099 -0.0021 0.0278  158 LYS   A C   
3300 O  O   A LYS   A 158 ? 0.1712 0.2812 0.4106 0.0487  0.0592  0.1462  158 LYS   A O   
3301 O  O   B LYS   A 158 ? 0.2446 0.2540 0.2848 -0.0162 -0.0051 0.0307  158 LYS   A O   
3302 C  CB  A LYS   A 158 ? 0.2196 0.2823 0.4455 0.0585  0.0867  0.1045  158 LYS   A CB  
3303 C  CB  B LYS   A 158 ? 0.2611 0.2658 0.3082 -0.0017 0.0094  0.0144  158 LYS   A CB  
3304 C  CG  A LYS   A 158 ? 0.2407 0.3027 0.4726 0.0583  0.1045  0.0966  158 LYS   A CG  
3305 C  CG  B LYS   A 158 ? 0.2675 0.2737 0.3245 0.0003  0.0161  0.0090  158 LYS   A CG  
3306 C  CD  A LYS   A 158 ? 0.2531 0.3206 0.4904 0.0550  0.1291  0.0979  158 LYS   A CD  
3307 C  CD  B LYS   A 158 ? 0.2725 0.2804 0.3382 0.0017  0.0208  0.0054  158 LYS   A CD  
3308 C  CE  A LYS   A 158 ? 0.2630 0.3340 0.5060 0.0471  0.1434  0.1037  158 LYS   A CE  
3309 C  CE  B LYS   A 158 ? 0.2755 0.2847 0.3496 0.0020  0.0233  0.0050  158 LYS   A CE  
3310 N  NZ  A LYS   A 158 ? 0.2684 0.3417 0.5173 0.0399  0.1453  0.1137  158 LYS   A NZ  
3311 N  NZ  B LYS   A 158 ? 0.2773 0.2869 0.3585 0.0023  0.0240  0.0069  158 LYS   A NZ  
3338 N  N   A ASN   A 159 ? 0.1823 0.2935 0.4211 0.0625  0.0311  0.1491  159 ASN   A N   
3339 N  N   B ASN   A 159 ? 0.2444 0.2586 0.2919 -0.0094 0.0009  0.0290  159 ASN   A N   
3340 C  CA  A ASN   A 159 ? 0.1858 0.3039 0.4216 0.0605  0.0107  0.1606  159 ASN   A CA  
3341 C  CA  B ASN   A 159 ? 0.2411 0.2598 0.2964 -0.0085 0.0016  0.0305  159 ASN   A CA  
3342 C  C   A ASN   A 159 ? 0.1684 0.3020 0.3917 0.0413  0.0149  0.1528  159 ASN   A C   
3343 C  C   B ASN   A 159 ? 0.2286 0.2521 0.2701 -0.0116 -0.0004 0.0308  159 ASN   A C   
3344 O  O   A ASN   A 159 ? 0.1543 0.3099 0.3805 0.0395  0.0001  0.1395  159 ASN   A O   
3345 O  O   B ASN   A 159 ? 0.2252 0.2539 0.2637 -0.0145 -0.0031 0.0355  159 ASN   A O   
3346 C  CB  A ASN   A 159 ? 0.2119 0.3198 0.4676 0.0625  0.0077  0.1658  159 ASN   A CB  
3347 C  CB  B ASN   A 159 ? 0.2505 0.2682 0.3295 -0.0067 0.0038  0.0296  159 ASN   A CB  
3348 C  CG  A ASN   A 159 ? 0.2433 0.3378 0.5198 0.0548  0.0127  0.1581  159 ASN   A CG  
3349 C  CG  B ASN   A 159 ? 0.2610 0.2768 0.3598 -0.0069 0.0037  0.0257  159 ASN   A CG  
3350 O  OD1 A ASN   A 159 ? 0.2547 0.3481 0.5423 0.0454  0.0281  0.1515  159 ASN   A OD1 
3351 O  OD1 B ASN   A 159 ? 0.2663 0.2797 0.3712 -0.0071 0.0027  0.0217  159 ASN   A OD1 
3352 N  ND2 A ASN   A 159 ? 0.2555 0.3456 0.5456 0.0513  0.0127  0.1488  159 ASN   A ND2 
3353 N  ND2 B ASN   A 159 ? 0.2648 0.2794 0.3702 -0.0082 0.0028  0.0237  159 ASN   A ND2 
3366 N  N   A LEU   A 160 ? 0.1534 0.2816 0.3699 0.0338  0.0032  0.1544  160 LEU   A N   
3367 N  N   B LEU   A 160 ? 0.2189 0.2439 0.2561 -0.0117 -0.0027 0.0289  160 LEU   A N   
3368 C  CA  A LEU   A 160 ? 0.1557 0.2661 0.3461 0.0194  0.0129  0.1443  160 LEU   A CA  
3369 C  CA  B LEU   A 160 ? 0.2138 0.2392 0.2453 -0.0104 0.0013  0.0257  160 LEU   A CA  
3370 C  C   A LEU   A 160 ? 0.1420 0.2573 0.3324 0.0113  0.0258  0.1380  160 LEU   A C   
3371 C  C   B LEU   A 160 ? 0.2098 0.2358 0.2326 -0.0051 0.0032  0.0287  160 LEU   A C   
3372 O  O   A LEU   A 160 ? 0.1417 0.2691 0.3528 0.0075  0.0240  0.1292  160 LEU   A O   
3373 O  O   B LEU   A 160 ? 0.2077 0.2364 0.2321 -0.0047 0.0005  0.0333  160 LEU   A O   
3374 C  CB  A LEU   A 160 ? 0.1682 0.2649 0.3233 0.0114  0.0195  0.1394  160 LEU   A CB  
3375 C  CB  B LEU   A 160 ? 0.2133 0.2395 0.2444 -0.0133 0.0027  0.0176  160 LEU   A CB  
3376 C  CG  A LEU   A 160 ? 0.1795 0.2734 0.3141 -0.0032 0.0295  0.1184  160 LEU   A CG  
3377 C  CG  B LEU   A 160 ? 0.2135 0.2421 0.2477 -0.0154 0.0046  0.0073  160 LEU   A CG  
3378 C  CD1 A LEU   A 160 ? 0.1921 0.2805 0.3231 -0.0091 0.0298  0.1012  160 LEU   A CD1 
3379 C  CD1 B LEU   A 160 ? 0.2127 0.2412 0.2482 -0.0161 0.0061  0.0072  160 LEU   A CD1 
3380 C  CD2 A LEU   A 160 ? 0.1857 0.2732 0.3086 -0.0110 0.0445  0.1100  160 LEU   A CD2 
3381 C  CD2 B LEU   A 160 ? 0.2150 0.2426 0.2476 -0.0162 0.0064  0.0036  160 LEU   A CD2 
3404 N  N   A TYR   A 161 ? 0.1366 0.2362 0.3231 0.0136  0.0223  0.1285  161 TYR   A N   
3405 N  N   B TYR   A 161 ? 0.2089 0.2324 0.2276 -0.0003 0.0070  0.0269  161 TYR   A N   
3406 C  CA  A TYR   A 161 ? 0.1398 0.2237 0.3273 0.0137  0.0224  0.1187  161 TYR   A CA  
3407 C  CA  B TYR   A 161 ? 0.2079 0.2296 0.2241 0.0031  0.0129  0.0277  161 TYR   A CA  
3408 C  C   A TYR   A 161 ? 0.1331 0.2364 0.3354 0.0085  0.0192  0.1178  161 TYR   A C   
3409 C  C   B TYR   A 161 ? 0.2093 0.2378 0.2277 0.0028  0.0142  0.0275  161 TYR   A C   
3410 O  O   A TYR   A 161 ? 0.1248 0.2358 0.3394 -0.0007 0.0217  0.1123  161 TYR   A O   
3411 O  O   B TYR   A 161 ? 0.2078 0.2386 0.2270 0.0012  0.0175  0.0264  161 TYR   A O   
3412 C  CB  A TYR   A 161 ? 0.1523 0.2122 0.3340 0.0178  0.0217  0.0950  161 TYR   A CB  
3413 C  CB  B TYR   A 161 ? 0.2066 0.2204 0.2195 0.0068  0.0161  0.0269  161 TYR   A CB  
3414 C  CG  A TYR   A 161 ? 0.1539 0.2005 0.3223 0.0131  0.0186  0.0714  161 TYR   A CG  
3415 C  CG  B TYR   A 161 ? 0.2033 0.2111 0.2088 0.0097  0.0203  0.0264  161 TYR   A CG  
3416 C  CD1 A TYR   A 161 ? 0.1520 0.1889 0.3204 0.0093  0.0121  0.0662  161 TYR   A CD1 
3417 C  CD1 B TYR   A 161 ? 0.2019 0.2088 0.2082 0.0111  0.0207  0.0260  161 TYR   A CD1 
3418 C  CD2 A TYR   A 161 ? 0.1533 0.2080 0.3164 0.0167  0.0143  0.0559  161 TYR   A CD2 
3419 C  CD2 B TYR   A 161 ? 0.2018 0.2057 0.2022 0.0119  0.0241  0.0272  161 TYR   A CD2 
3420 C  CE1 A TYR   A 161 ? 0.1591 0.1853 0.3186 0.0043  0.0085  0.0684  161 TYR   A CE1 
3421 C  CE1 B TYR   A 161 ? 0.2028 0.2081 0.2066 0.0124  0.0209  0.0283  161 TYR   A CE1 
3422 C  CE2 A TYR   A 161 ? 0.1601 0.1934 0.3138 0.0072  0.0175  0.0602  161 TYR   A CE2 
3423 C  CE2 B TYR   A 161 ? 0.2026 0.2047 0.2030 0.0116  0.0265  0.0293  161 TYR   A CE2 
3424 C  CZ  A TYR   A 161 ? 0.1692 0.1851 0.3207 0.0014  0.0057  0.0676  161 TYR   A CZ  
3425 C  CZ  B TYR   A 161 ? 0.2051 0.2068 0.2086 0.0131  0.0241  0.0293  161 TYR   A CZ  
3426 O  OH  A TYR   A 161 ? 0.1886 0.1907 0.3267 -0.0043 -0.0013 0.0761  161 TYR   A OH  
3427 O  OH  B TYR   A 161 ? 0.2104 0.2071 0.2174 0.0157  0.0190  0.0307  161 TYR   A OH  
3446 N  N   A ASP   A 162 ? 0.1333 0.2540 0.3469 0.0086  0.0264  0.1232  162 ASP   A N   
3447 N  N   B ASP   A 162 ? 0.2126 0.2458 0.2384 0.0037  0.0139  0.0279  162 ASP   A N   
3448 C  CA  A ASP   A 162 ? 0.1334 0.2783 0.3531 0.0044  0.0339  0.1226  162 ASP   A CA  
3449 C  CA  B ASP   A 162 ? 0.2154 0.2544 0.2478 0.0017  0.0151  0.0309  162 ASP   A CA  
3450 C  C   A ASP   A 162 ? 0.1281 0.2941 0.3517 0.0002  0.0308  0.1271  162 ASP   A C   
3451 C  C   B ASP   A 162 ? 0.2175 0.2638 0.2546 -0.0009 0.0134  0.0302  162 ASP   A C   
3452 O  O   A ASP   A 162 ? 0.1348 0.2928 0.3698 -0.0070 0.0359  0.1214  162 ASP   A O   
3453 O  O   B ASP   A 162 ? 0.2177 0.2633 0.2587 -0.0027 0.0137  0.0246  162 ASP   A O   
3454 C  CB  A ASP   A 162 ? 0.1461 0.2898 0.3669 0.0089  0.0495  0.1133  162 ASP   A CB  
3455 C  CB  B ASP   A 162 ? 0.2177 0.2554 0.2539 0.0041  0.0186  0.0335  162 ASP   A CB  
3456 C  CG  A ASP   A 162 ? 0.1669 0.3090 0.3923 0.0182  0.0534  0.0948  162 ASP   A CG  
3457 C  CG  B ASP   A 162 ? 0.2210 0.2581 0.2624 0.0058  0.0216  0.0353  162 ASP   A CG  
3458 O  OD1 A ASP   A 162 ? 0.1786 0.3178 0.4056 0.0046  0.0547  0.0895  162 ASP   A OD1 
3459 O  OD1 B ASP   A 162 ? 0.2246 0.2607 0.2674 0.0030  0.0226  0.0353  162 ASP   A OD1 
3460 O  OD2 A ASP   A 162 ? 0.1865 0.3181 0.4129 0.0357  0.0560  0.0811  162 ASP   A OD2 
3461 O  OD2 B ASP   A 162 ? 0.2223 0.2586 0.2677 0.0085  0.0262  0.0358  162 ASP   A OD2 
3470 N  N   A LYS   A 163 ? 0.1346 0.3160 0.3558 -0.0029 0.0060  0.1230  163 LYS   A N   
3471 N  N   B LYS   A 163 ? 0.2204 0.2733 0.2636 -0.0029 0.0083  0.0338  163 LYS   A N   
3472 C  CA  A LYS   A 163 ? 0.1498 0.3334 0.3403 -0.0084 0.0044  0.1209  163 LYS   A CA  
3473 C  CA  B LYS   A 163 ? 0.2229 0.2821 0.2730 -0.0050 0.0057  0.0344  163 LYS   A CA  
3474 C  C   A LYS   A 163 ? 0.1468 0.3219 0.3342 -0.0136 0.0171  0.1124  163 LYS   A C   
3475 C  C   B LYS   A 163 ? 0.2107 0.2794 0.2612 -0.0065 0.0097  0.0382  163 LYS   A C   
3476 O  O   A LYS   A 163 ? 0.1419 0.3395 0.3515 -0.0202 0.0149  0.1022  163 LYS   A O   
3477 O  O   B LYS   A 163 ? 0.2125 0.2852 0.2607 -0.0073 0.0115  0.0361  163 LYS   A O   
3478 C  CB  A LYS   A 163 ? 0.1894 0.3615 0.3604 0.0027  -0.0207 0.1192  163 LYS   A CB  
3479 C  CB  B LYS   A 163 ? 0.2379 0.2924 0.3009 -0.0054 0.0011  0.0312  163 LYS   A CB  
3480 C  CG  A LYS   A 163 ? 0.2333 0.3866 0.3965 0.0022  -0.0197 0.1145  163 LYS   A CG  
3481 C  CG  B LYS   A 163 ? 0.2516 0.3017 0.3284 -0.0070 -0.0003 0.0267  163 LYS   A CG  
3482 C  CD  A LYS   A 163 ? 0.2709 0.4089 0.4405 0.0020  -0.0206 0.1054  163 LYS   A CD  
3483 C  CD  B LYS   A 163 ? 0.2620 0.3095 0.3533 -0.0074 -0.0017 0.0217  163 LYS   A CD  
3484 C  CE  A LYS   A 163 ? 0.2974 0.4217 0.4743 -0.0009 -0.0154 0.1013  163 LYS   A CE  
3485 C  CE  B LYS   A 163 ? 0.2685 0.3148 0.3743 -0.0078 -0.0031 0.0169  163 LYS   A CE  
3486 N  NZ  A LYS   A 163 ? 0.3122 0.4281 0.4945 -0.0034 -0.0120 0.1018  163 LYS   A NZ  
3487 N  NZ  B LYS   A 163 ? 0.2723 0.3174 0.3839 -0.0066 -0.0032 0.0161  163 LYS   A NZ  
3514 N  N   A LEU   A 164 ? 0.1321 0.2889 0.3167 -0.0221 0.0117  0.1026  164 LEU   A N   
3515 N  N   B LEU   A 164 ? 0.1934 0.2692 0.2501 -0.0095 0.0092  0.0442  164 LEU   A N   
3516 C  CA  A LEU   A 164 ? 0.1360 0.2604 0.3022 -0.0266 0.0183  0.0933  164 LEU   A CA  
3517 C  CA  B LEU   A 164 ? 0.1774 0.2591 0.2435 -0.0119 0.0116  0.0517  164 LEU   A CA  
3518 C  C   A LEU   A 164 ? 0.1486 0.2560 0.2966 -0.0244 0.0261  0.0805  164 LEU   A C   
3519 C  C   B LEU   A 164 ? 0.1647 0.2543 0.2584 -0.0172 0.0189  0.0628  164 LEU   A C   
3520 O  O   A LEU   A 164 ? 0.1565 0.2633 0.3107 -0.0318 0.0498  0.0552  164 LEU   A O   
3521 O  O   B LEU   A 164 ? 0.1661 0.2559 0.2560 -0.0196 0.0239  0.0571  164 LEU   A O   
3522 C  CB  A LEU   A 164 ? 0.1310 0.2443 0.2960 -0.0251 0.0237  0.0941  164 LEU   A CB  
3523 C  CB  B LEU   A 164 ? 0.1746 0.2548 0.2280 -0.0094 0.0081  0.0483  164 LEU   A CB  
3524 C  CG  A LEU   A 164 ? 0.1403 0.2386 0.3043 -0.0114 0.0137  0.0795  164 LEU   A CG  
3525 C  CG  B LEU   A 164 ? 0.1726 0.2508 0.2165 -0.0063 0.0035  0.0453  164 LEU   A CG  
3526 C  CD1 A LEU   A 164 ? 0.1271 0.2333 0.3064 -0.0024 0.0121  0.0670  164 LEU   A CD1 
3527 C  CD1 B LEU   A 164 ? 0.1707 0.2491 0.2097 -0.0062 0.0008  0.0454  164 LEU   A CD1 
3528 C  CD2 A LEU   A 164 ? 0.1536 0.2421 0.3020 -0.0129 0.0112  0.0748  164 LEU   A CD2 
3529 C  CD2 B LEU   A 164 ? 0.1704 0.2494 0.2126 -0.0052 0.0020  0.0432  164 LEU   A CD2 
3552 N  N   . VAL   A 165 ? 0.1508 0.2497 0.2849 -0.0222 0.0231  0.0769  165 VAL   A N   
3553 C  CA  . VAL   A 165 ? 0.1547 0.2432 0.2824 -0.0215 0.0283  0.0815  165 VAL   A CA  
3554 C  C   . VAL   A 165 ? 0.1442 0.2561 0.2828 -0.0099 0.0329  0.0780  165 VAL   A C   
3555 O  O   . VAL   A 165 ? 0.1476 0.2581 0.2702 -0.0110 0.0300  0.0777  165 VAL   A O   
3556 C  CB  . VAL   A 165 ? 0.1766 0.2361 0.2971 -0.0230 0.0341  0.0645  165 VAL   A CB  
3557 C  CG1 . VAL   A 165 ? 0.1859 0.2356 0.3053 -0.0206 0.0344  0.0551  165 VAL   A CG1 
3558 C  CG2 . VAL   A 165 ? 0.1903 0.2362 0.3083 -0.0205 0.0356  0.0633  165 VAL   A CG2 
3569 N  N   . SER   A 166 ? 0.1334 0.2763 0.3030 -0.0111 0.0354  0.0735  166 SER   A N   
3570 C  CA  . SER   A 166 ? 0.1392 0.3048 0.3164 -0.0144 0.0250  0.0612  166 SER   A CA  
3571 C  C   . SER   A 166 ? 0.1414 0.3331 0.3207 -0.0242 0.0089  0.0566  166 SER   A C   
3572 O  O   . SER   A 166 ? 0.1658 0.3500 0.3601 -0.0382 0.0179  0.0303  166 SER   A O   
3573 C  CB  . SER   A 166 ? 0.1642 0.3153 0.3469 -0.0037 0.0133  0.0435  166 SER   A CB  
3574 O  OG  . SER   A 166 ? 0.2141 0.3271 0.3828 -0.0084 0.0096  0.0430  166 SER   A OG  
3580 N  N   . SER   A 167 ? 0.1466 0.3419 0.2888 -0.0104 -0.0016 0.0674  167 SER   A N   
3581 C  CA  . SER   A 167 ? 0.1708 0.3572 0.2793 0.0008  -0.0108 0.0538  167 SER   A CA  
3582 C  C   . SER   A 167 ? 0.1746 0.3555 0.2724 0.0111  -0.0055 0.0410  167 SER   A C   
3583 O  O   . SER   A 167 ? 0.1943 0.3571 0.2850 0.0142  -0.0139 0.0323  167 SER   A O   
3584 C  CB  . SER   A 167 ? 0.1810 0.3742 0.2892 0.0032  -0.0040 0.0555  167 SER   A CB  
3585 O  OG  . SER   A 167 ? 0.1843 0.3819 0.2908 -0.0011 0.0120  0.0624  167 SER   A OG  
3591 N  N   . PHE   A 168 ? 0.1691 0.3528 0.2573 0.0190  -0.0007 0.0347  168 PHE   A N   
3592 C  CA  . PHE   A 168 ? 0.1691 0.3462 0.2680 0.0110  0.0143  0.0231  168 PHE   A CA  
3593 C  C   . PHE   A 168 ? 0.1881 0.3783 0.3040 -0.0068 0.0585  -0.0028 168 PHE   A C   
3594 O  O   . PHE   A 168 ? 0.1930 0.3823 0.3399 -0.0267 0.0598  0.0086  168 PHE   A O   
3595 C  CB  . PHE   A 168 ? 0.1697 0.3138 0.2519 0.0047  -0.0058 0.0300  168 PHE   A CB  
3596 C  CG  . PHE   A 168 ? 0.1644 0.2892 0.2391 -0.0055 -0.0086 0.0393  168 PHE   A CG  
3597 C  CD1 . PHE   A 168 ? 0.1633 0.2891 0.2518 -0.0090 -0.0100 0.0588  168 PHE   A CD1 
3598 C  CD2 . PHE   A 168 ? 0.1659 0.2761 0.2261 -0.0063 0.0027  0.0326  168 PHE   A CD2 
3599 C  CE1 . PHE   A 168 ? 0.1508 0.2856 0.2455 -0.0130 -0.0100 0.0612  168 PHE   A CE1 
3600 C  CE2 . PHE   A 168 ? 0.1662 0.2705 0.2341 -0.0128 0.0046  0.0477  168 PHE   A CE2 
3601 C  CZ  . PHE   A 168 ? 0.1577 0.2770 0.2425 -0.0179 -0.0024 0.0566  168 PHE   A CZ  
3611 N  N   . LEU   A 169 ? 0.2474 0.4100 0.3625 -0.0201 0.0546  -0.0311 169 LEU   A N   
3612 C  CA  . LEU   A 169 ? 0.3438 0.4476 0.4718 -0.0261 0.0058  -0.0467 169 LEU   A CA  
3613 C  C   . LEU   A 169 ? 0.3762 0.4563 0.5067 -0.0312 -0.0114 -0.0470 169 LEU   A C   
3614 O  O   . LEU   A 169 ? 0.3895 0.4600 0.5173 -0.0316 -0.0130 -0.0498 169 LEU   A O   
3615 C  CB  . LEU   A 169 ? 0.3989 0.4736 0.5267 -0.0292 -0.0184 -0.0567 169 LEU   A CB  
3616 C  CG  . LEU   A 169 ? 0.4386 0.4919 0.5687 -0.0349 -0.0351 -0.0700 169 LEU   A CG  
3617 C  CD1 . LEU   A 169 ? 0.4523 0.4978 0.5864 -0.0368 -0.0392 -0.0732 169 LEU   A CD1 
3618 C  CD2 . LEU   A 169 ? 0.4527 0.4988 0.5815 -0.0373 -0.0387 -0.0747 169 LEU   A CD2 
3619 O  OXT . LEU   A 169 ? 0.3705 0.4564 0.5111 -0.0338 -0.0136 -0.0482 169 LEU   A OXT 
3631 N  N   A SER   B 1   ? 0.3392 0.3279 0.3649 -0.1231 -0.0814 0.0427  1   SER   B N   
3632 N  N   B SER   B 1   ? 0.3440 0.3445 0.3436 -0.0399 -0.0290 0.0171  1   SER   B N   
3633 C  CA  A SER   B 1   ? 0.3249 0.3360 0.3617 -0.1280 -0.0899 0.0419  1   SER   B CA  
3634 C  CA  B SER   B 1   ? 0.3409 0.3446 0.3425 -0.0405 -0.0284 0.0172  1   SER   B CA  
3635 C  C   A SER   B 1   ? 0.3001 0.3421 0.3379 -0.1255 -0.1054 0.0662  1   SER   B C   
3636 C  C   B SER   B 1   ? 0.3335 0.3430 0.3386 -0.0396 -0.0315 0.0247  1   SER   B C   
3637 O  O   A SER   B 1   ? 0.3114 0.3432 0.3124 -0.1159 -0.1023 0.0675  1   SER   B O   
3638 O  O   B SER   B 1   ? 0.3357 0.3430 0.3306 -0.0387 -0.0329 0.0241  1   SER   B O   
3639 C  CB  A SER   B 1   ? 0.3376 0.3343 0.3758 -0.1292 -0.0713 0.0194  1   SER   B CB  
3640 C  CB  B SER   B 1   ? 0.3440 0.3454 0.3432 -0.0409 -0.0234 0.0100  1   SER   B CB  
3641 O  OG  A SER   B 1   ? 0.3549 0.3440 0.4233 -0.1246 -0.0566 0.0077  1   SER   B OG  
3642 O  OG  B SER   B 1   ? 0.3476 0.3479 0.3548 -0.0412 -0.0209 0.0059  1   SER   B OG  
3657 N  N   A MET   B 2   ? 0.2750 0.3454 0.3460 -0.1194 -0.1027 0.1089  2   MET   B N   
3658 N  N   B MET   B 2   ? 0.3244 0.3406 0.3414 -0.0383 -0.0316 0.0357  2   MET   B N   
3659 C  CA  A MET   B 2   ? 0.2616 0.3518 0.3682 -0.0933 -0.1002 0.1287  2   MET   B CA  
3660 C  CA  B MET   B 2   ? 0.3145 0.3371 0.3444 -0.0348 -0.0315 0.0442  2   MET   B CA  
3661 C  C   A MET   B 2   ? 0.2333 0.3308 0.3472 -0.0743 -0.0991 0.1505  2   MET   B C   
3662 C  C   B MET   B 2   ? 0.2944 0.3200 0.3158 -0.0356 -0.0320 0.0513  2   MET   B C   
3663 O  O   A MET   B 2   ? 0.2205 0.3451 0.3554 -0.0629 -0.1026 0.1545  2   MET   B O   
3664 O  O   B MET   B 2   ? 0.2961 0.3242 0.3168 -0.0336 -0.0286 0.0499  2   MET   B O   
3665 C  CB  A MET   B 2   ? 0.2908 0.3871 0.4461 -0.0697 -0.0820 0.1049  2   MET   B CB  
3666 C  CB  B MET   B 2   ? 0.3247 0.3502 0.3807 -0.0289 -0.0300 0.0435  2   MET   B CB  
3667 C  CG  A MET   B 2   ? 0.3160 0.4184 0.5199 -0.0493 -0.0633 0.0913  2   MET   B CG  
3668 C  CG  B MET   B 2   ? 0.3334 0.3616 0.4143 -0.0236 -0.0287 0.0452  2   MET   B CG  
3669 S  SD  A MET   B 2   ? 0.3440 0.4466 0.5934 -0.0313 -0.0449 0.0786  2   MET   B SD  
3670 S  SD  B MET   B 2   ? 0.3412 0.3723 0.4451 -0.0187 -0.0280 0.0473  2   MET   B SD  
3671 C  CE  A MET   B 2   ? 0.3446 0.4503 0.5876 -0.0307 -0.0371 0.0795  2   MET   B CE  
3672 C  CE  B MET   B 2   ? 0.3416 0.3739 0.4488 -0.0193 -0.0264 0.0455  2   MET   B CE  
3691 N  N   A VAL   B 3   ? 0.2136 0.2892 0.3206 -0.0803 -0.0927 0.1642  3   VAL   B N   
3692 N  N   B VAL   B 3   ? 0.2714 0.2971 0.2877 -0.0401 -0.0362 0.0601  3   VAL   B N   
3693 C  CA  A VAL   B 3   ? 0.2112 0.2531 0.3183 -0.0750 -0.0788 0.1426  3   VAL   B CA  
3694 C  CA  B VAL   B 3   ? 0.2488 0.2736 0.2647 -0.0434 -0.0405 0.0649  3   VAL   B CA  
3695 C  C   A VAL   B 3   ? 0.1988 0.2424 0.2746 -0.0682 -0.0741 0.1164  3   VAL   B C   
3696 C  C   B VAL   B 3   ? 0.2209 0.2505 0.2415 -0.0492 -0.0509 0.0741  3   VAL   B C   
3697 O  O   A VAL   B 3   ? 0.2011 0.2509 0.2848 -0.0695 -0.0775 0.1245  3   VAL   B O   
3698 O  O   B VAL   B 3   ? 0.2208 0.2536 0.2352 -0.0443 -0.0495 0.0754  3   VAL   B O   
3699 C  CB  A VAL   B 3   ? 0.2338 0.2450 0.3679 -0.0715 -0.0720 0.1247  3   VAL   B CB  
3700 C  CB  B VAL   B 3   ? 0.2550 0.2740 0.2699 -0.0417 -0.0349 0.0600  3   VAL   B CB  
3701 C  CG1 A VAL   B 3   ? 0.2441 0.2382 0.3897 -0.0702 -0.0688 0.1189  3   VAL   B CG1 
3702 C  CG1 B VAL   B 3   ? 0.2575 0.2735 0.2743 -0.0416 -0.0325 0.0576  3   VAL   B CG1 
3703 C  CG2 A VAL   B 3   ? 0.2400 0.2476 0.3849 -0.0673 -0.0654 0.1308  3   VAL   B CG2 
3704 C  CG2 B VAL   B 3   ? 0.2574 0.2750 0.2720 -0.0403 -0.0335 0.0609  3   VAL   B CG2 
3723 N  N   . ASN   B 4   ? 0.1939 0.2231 0.2330 -0.0590 -0.0632 0.0852  4   ASN   B N   
3724 C  CA  . ASN   B 4   ? 0.1864 0.2162 0.1986 -0.0592 -0.0496 0.0469  4   ASN   B CA  
3725 C  C   . ASN   B 4   ? 0.1912 0.2303 0.1910 -0.0536 -0.0409 0.0347  4   ASN   B C   
3726 O  O   . ASN   B 4   ? 0.1908 0.2355 0.2198 -0.0477 -0.0326 0.0164  4   ASN   B O   
3727 C  CB  . ASN   B 4   ? 0.1859 0.2078 0.1889 -0.0486 -0.0524 0.0354  4   ASN   B CB  
3728 C  CG  . ASN   B 4   ? 0.1879 0.1922 0.1812 -0.0444 -0.0470 0.0277  4   ASN   B CG  
3729 O  OD1 . ASN   B 4   ? 0.1862 0.1803 0.1712 -0.0440 -0.0474 0.0207  4   ASN   B OD1 
3730 N  ND2 . ASN   B 4   ? 0.2064 0.1952 0.1954 -0.0269 -0.0280 0.0287  4   ASN   B ND2 
3738 N  N   . SER   B 5   ? 0.2062 0.2462 0.2016 -0.0572 -0.0251 0.0316  5   SER   B N   
3739 C  CA  . SER   B 5   ? 0.2377 0.2803 0.2278 -0.0497 -0.0046 0.0300  5   SER   B CA  
3740 C  C   . SER   B 5   ? 0.2559 0.2848 0.2630 -0.0623 0.0227  0.0328  5   SER   B C   
3741 O  O   . SER   B 5   ? 0.2693 0.2808 0.3244 -0.0534 0.0540  0.0355  5   SER   B O   
3742 C  CB  . SER   B 5   ? 0.2522 0.2990 0.2511 -0.0386 -0.0005 0.0369  5   SER   B CB  
3743 O  OG  . SER   B 5   ? 0.2795 0.3229 0.3091 -0.0253 0.0043  0.0415  5   SER   B OG  
3749 N  N   . PHE   B 6   ? 0.2736 0.3044 0.2371 -0.0669 0.0366  0.0352  6   PHE   B N   
3750 C  CA  . PHE   B 6   ? 0.2822 0.3067 0.2115 -0.0855 0.0466  0.0156  6   PHE   B CA  
3751 C  C   . PHE   B 6   ? 0.3329 0.3405 0.2528 -0.0893 0.0698  -0.0117 6   PHE   B C   
3752 O  O   . PHE   B 6   ? 0.3481 0.3700 0.2851 -0.0831 0.0544  -0.0296 6   PHE   B O   
3753 C  CB  . PHE   B 6   ? 0.2505 0.2821 0.1866 -0.0814 0.0252  0.0122  6   PHE   B CB  
3754 C  CG  . PHE   B 6   ? 0.2139 0.2531 0.1754 -0.0745 0.0053  0.0047  6   PHE   B CG  
3755 C  CD1 . PHE   B 6   ? 0.2140 0.2272 0.1613 -0.0679 -0.0108 0.0086  6   PHE   B CD1 
3756 C  CD2 . PHE   B 6   ? 0.1905 0.2517 0.1713 -0.0615 0.0069  0.0277  6   PHE   B CD2 
3757 C  CE1 . PHE   B 6   ? 0.2084 0.2131 0.1671 -0.0531 -0.0135 0.0081  6   PHE   B CE1 
3758 C  CE2 . PHE   B 6   ? 0.1926 0.2394 0.1972 -0.0440 0.0111  0.0297  6   PHE   B CE2 
3759 C  CZ  . PHE   B 6   ? 0.1955 0.2212 0.1816 -0.0455 0.0012  0.0121  6   PHE   B CZ  
3769 N  N   . SER   B 7   ? 0.3686 0.3312 0.2680 -0.1061 0.1013  -0.0319 7   SER   B N   
3770 C  CA  . SER   B 7   ? 0.4009 0.3447 0.3099 -0.1043 0.1216  -0.0405 7   SER   B CA  
3771 C  C   . SER   B 7   ? 0.4019 0.3241 0.3016 -0.1071 0.1333  -0.0504 7   SER   B C   
3772 O  O   . SER   B 7   ? 0.4078 0.3236 0.3203 -0.1093 0.1328  -0.0503 7   SER   B O   
3773 C  CB  . SER   B 7   ? 0.4210 0.3666 0.3676 -0.1008 0.1323  -0.0338 7   SER   B CB  
3774 O  OG  . SER   B 7   ? 0.4321 0.3778 0.4169 -0.0987 0.1339  -0.0234 7   SER   B OG  
3780 N  N   . GLY   B 8   ? 0.3994 0.3052 0.3052 -0.0952 0.1367  -0.0563 8   GLY   B N   
3781 C  CA  . GLY   B 8   ? 0.3862 0.2852 0.3079 -0.0890 0.1350  -0.0622 8   GLY   B CA  
3782 C  C   . GLY   B 8   ? 0.3653 0.2566 0.2940 -0.0883 0.1332  -0.0563 8   GLY   B C   
3783 O  O   . GLY   B 8   ? 0.3766 0.2656 0.3222 -0.0764 0.1366  -0.0619 8   GLY   B O   
3787 N  N   . TYR   B 9   ? 0.3408 0.2379 0.2665 -0.0787 0.1088  -0.0613 9   TYR   B N   
3788 C  CA  . TYR   B 9   ? 0.3136 0.2088 0.2374 -0.0662 0.0808  -0.0517 9   TYR   B CA  
3789 C  C   . TYR   B 9   ? 0.3050 0.2092 0.2211 -0.0604 0.0456  -0.0398 9   TYR   B C   
3790 O  O   . TYR   B 9   ? 0.3181 0.2366 0.2538 -0.0657 0.0496  -0.0283 9   TYR   B O   
3791 C  CB  . TYR   B 9   ? 0.3068 0.1898 0.2403 -0.0556 0.0714  -0.0489 9   TYR   B CB  
3792 C  CG  . TYR   B 9   ? 0.2964 0.1770 0.2376 -0.0633 0.0674  -0.0497 9   TYR   B CG  
3793 C  CD1 . TYR   B 9   ? 0.2990 0.1754 0.2509 -0.0770 0.0669  -0.0437 9   TYR   B CD1 
3794 C  CD2 . TYR   B 9   ? 0.2832 0.1715 0.2266 -0.0558 0.0639  -0.0599 9   TYR   B CD2 
3795 C  CE1 . TYR   B 9   ? 0.2925 0.1865 0.2558 -0.0804 0.0707  -0.0569 9   TYR   B CE1 
3796 C  CE2 . TYR   B 9   ? 0.2823 0.1758 0.2339 -0.0591 0.0649  -0.0550 9   TYR   B CE2 
3797 C  CZ  . TYR   B 9   ? 0.2865 0.1868 0.2543 -0.0733 0.0700  -0.0654 9   TYR   B CZ  
3798 O  OH  . TYR   B 9   ? 0.2858 0.2025 0.2782 -0.0856 0.0726  -0.0765 9   TYR   B OH  
3808 N  N   . LEU   B 10  ? 0.2801 0.1836 0.1979 -0.0542 0.0184  -0.0360 10  LEU   B N   
3809 C  CA  . LEU   B 10  ? 0.2725 0.1828 0.2054 -0.0626 -0.0026 -0.0282 10  LEU   B CA  
3810 C  C   . LEU   B 10  ? 0.2552 0.1835 0.1986 -0.0590 -0.0141 -0.0294 10  LEU   B C   
3811 O  O   . LEU   B 10  ? 0.2451 0.1837 0.1964 -0.0410 -0.0083 -0.0209 10  LEU   B O   
3812 C  CB  . LEU   B 10  ? 0.2916 0.1826 0.2191 -0.0614 -0.0245 -0.0175 10  LEU   B CB  
3813 C  CG  . LEU   B 10  ? 0.3137 0.1917 0.2461 -0.0520 -0.0566 -0.0093 10  LEU   B CG  
3814 C  CD1 . LEU   B 10  ? 0.3239 0.2005 0.2725 -0.0494 -0.0612 -0.0117 10  LEU   B CD1 
3815 C  CD2 . LEU   B 10  ? 0.3271 0.1977 0.2729 -0.0482 -0.0528 0.0079  10  LEU   B CD2 
3827 N  N   . LYS   B 11  ? 0.2684 0.2106 0.1997 -0.0491 -0.0209 -0.0250 11  LYS   B N   
3828 C  CA  . LYS   B 11  ? 0.2829 0.2377 0.2257 -0.0361 -0.0341 -0.0303 11  LYS   B CA  
3829 C  C   . LYS   B 11  ? 0.2674 0.2185 0.2381 -0.0556 -0.0336 -0.0442 11  LYS   B C   
3830 O  O   . LYS   B 11  ? 0.2845 0.2389 0.2772 -0.0689 -0.0346 -0.0807 11  LYS   B O   
3831 C  CB  . LYS   B 11  ? 0.3124 0.2883 0.2766 -0.0084 -0.0362 -0.0212 11  LYS   B CB  
3832 C  CG  . LYS   B 11  ? 0.3412 0.3186 0.3426 0.0067  -0.0324 -0.0188 11  LYS   B CG  
3833 C  CD  . LYS   B 11  ? 0.3650 0.3390 0.4040 0.0131  -0.0260 -0.0212 11  LYS   B CD  
3834 C  CE  . LYS   B 11  ? 0.3814 0.3521 0.4537 0.0117  -0.0228 -0.0196 11  LYS   B CE  
3835 N  NZ  . LYS   B 11  ? 0.3912 0.3608 0.4797 0.0093  -0.0235 -0.0160 11  LYS   B NZ  
3849 N  N   . LEU   B 12  ? 0.2345 0.1893 0.2332 -0.0503 -0.0320 -0.0430 12  LEU   B N   
3850 C  CA  . LEU   B 12  ? 0.2180 0.1755 0.2518 -0.0476 -0.0302 -0.0318 12  LEU   B CA  
3851 C  C   . LEU   B 12  ? 0.2086 0.1744 0.2631 -0.0491 -0.0442 -0.0279 12  LEU   B C   
3852 O  O   . LEU   B 12  ? 0.2102 0.1799 0.2875 -0.0577 -0.0509 -0.0229 12  LEU   B O   
3853 C  CB  . LEU   B 12  ? 0.2205 0.1560 0.2507 -0.0381 -0.0173 -0.0345 12  LEU   B CB  
3854 C  CG  . LEU   B 12  ? 0.2214 0.1552 0.2528 -0.0370 -0.0100 -0.0247 12  LEU   B CG  
3855 C  CD1 . LEU   B 12  ? 0.2324 0.1552 0.2441 -0.0256 -0.0063 -0.0102 12  LEU   B CD1 
3856 C  CD2 . LEU   B 12  ? 0.2315 0.1633 0.2761 -0.0359 -0.0030 -0.0338 12  LEU   B CD2 
3868 N  N   . THR   B 13  ? 0.2054 0.1781 0.2547 -0.0431 -0.0468 -0.0357 13  THR   B N   
3869 C  CA  . THR   B 13  ? 0.2049 0.1878 0.2576 -0.0487 -0.0548 -0.0231 13  THR   B CA  
3870 C  C   . THR   B 13  ? 0.2423 0.2026 0.2695 -0.0565 -0.0664 -0.0205 13  THR   B C   
3871 O  O   . THR   B 13  ? 0.2565 0.1986 0.2791 -0.0593 -0.0309 -0.0190 13  THR   B O   
3872 C  CB  . THR   B 13  ? 0.1902 0.1913 0.2608 -0.0447 -0.0485 -0.0163 13  THR   B CB  
3873 O  OG1 . THR   B 13  ? 0.1804 0.1827 0.2627 -0.0403 -0.0374 -0.0205 13  THR   B OG1 
3874 C  CG2 . THR   B 13  ? 0.1974 0.1949 0.2668 -0.0336 -0.0324 -0.0051 13  THR   B CG2 
3882 N  N   A ASP   B 14  ? 0.2590 0.2149 0.2865 -0.0640 -0.0952 -0.0127 14  ASP   B N   
3883 N  N   B ASP   B 14  ? 0.2490 0.2107 0.2806 -0.0571 -0.0691 -0.0137 14  ASP   B N   
3884 C  CA  A ASP   B 14  ? 0.2751 0.2360 0.3090 -0.0645 -0.1016 0.0099  14  ASP   B CA  
3885 C  CA  B ASP   B 14  ? 0.2549 0.2191 0.2940 -0.0565 -0.0675 -0.0048 14  ASP   B CA  
3886 C  C   A ASP   B 14  ? 0.2627 0.2212 0.2727 -0.0712 -0.0825 0.0129  14  ASP   B C   
3887 C  C   B ASP   B 14  ? 0.2429 0.2076 0.2669 -0.0584 -0.0691 0.0002  14  ASP   B C   
3888 O  O   A ASP   B 14  ? 0.2918 0.2426 0.2766 -0.0739 -0.0784 0.0268  14  ASP   B O   
3889 O  O   B ASP   B 14  ? 0.2497 0.2114 0.2651 -0.0569 -0.0706 0.0002  14  ASP   B O   
3890 C  CB  A ASP   B 14  ? 0.2988 0.2721 0.3847 -0.0577 -0.1220 0.0124  14  ASP   B CB  
3891 C  CB  B ASP   B 14  ? 0.2713 0.2387 0.3375 -0.0537 -0.0636 -0.0041 14  ASP   B CB  
3892 C  CG  A ASP   B 14  ? 0.3274 0.3081 0.4646 -0.0435 -0.1203 0.0026  14  ASP   B CG  
3893 C  CG  B ASP   B 14  ? 0.2875 0.2559 0.3759 -0.0487 -0.0573 -0.0062 14  ASP   B CG  
3894 O  OD1 A ASP   B 14  ? 0.3451 0.3211 0.4883 -0.0451 -0.1169 -0.0091 14  ASP   B OD1 
3895 O  OD1 B ASP   B 14  ? 0.2947 0.2640 0.3876 -0.0473 -0.0535 -0.0079 14  ASP   B OD1 
3896 O  OD2 A ASP   B 14  ? 0.3308 0.3234 0.5007 -0.0382 -0.1189 0.0037  14  ASP   B OD2 
3897 O  OD2 B ASP   B 14  ? 0.2916 0.2612 0.3895 -0.0494 -0.0569 -0.0056 14  ASP   B OD2 
3906 N  N   . ASN   B 15  ? 0.2235 0.1919 0.2480 -0.0572 -0.0717 0.0064  15  ASN   B N   
3907 C  CA  . ASN   B 15  ? 0.1814 0.1652 0.2289 -0.0385 -0.0503 -0.0010 15  ASN   B CA  
3908 C  C   . ASN   B 15  ? 0.1680 0.1543 0.2201 -0.0233 -0.0459 -0.0035 15  ASN   B C   
3909 O  O   . ASN   B 15  ? 0.1664 0.1472 0.2365 -0.0231 -0.0491 -0.0143 15  ASN   B O   
3910 C  CB  . ASN   B 15  ? 0.1761 0.1608 0.2428 -0.0180 -0.0463 -0.0032 15  ASN   B CB  
3911 C  CG  . ASN   B 15  ? 0.1557 0.1574 0.2532 -0.0275 -0.0260 0.0027  15  ASN   B CG  
3912 O  OD1 . ASN   B 15  ? 0.1692 0.1852 0.2823 -0.0405 -0.0303 0.0098  15  ASN   B OD1 
3913 N  ND2 . ASN   B 15  ? 0.1619 0.1370 0.2568 -0.0167 0.0025  -0.0076 15  ASN   B ND2 
3921 N  N   . VAL   B 16  ? 0.1730 0.1453 0.2163 -0.0308 -0.0506 -0.0046 16  VAL   B N   
3922 C  CA  . VAL   B 16  ? 0.1708 0.1480 0.2083 -0.0280 -0.0356 -0.0236 16  VAL   B CA  
3923 C  C   . VAL   B 16  ? 0.1635 0.1611 0.1947 -0.0370 -0.0287 -0.0216 16  VAL   B C   
3924 O  O   . VAL   B 16  ? 0.1700 0.1737 0.2197 -0.0316 -0.0242 -0.0297 16  VAL   B O   
3925 C  CB  . VAL   B 16  ? 0.1763 0.1456 0.2179 -0.0126 -0.0275 -0.0260 16  VAL   B CB  
3926 C  CG1 . VAL   B 16  ? 0.1859 0.1414 0.2207 0.0032  -0.0234 -0.0161 16  VAL   B CG1 
3927 C  CG2 . VAL   B 16  ? 0.1811 0.1499 0.2348 -0.0083 -0.0145 -0.0238 16  VAL   B CG2 
3937 N  N   . TYR   B 17  ? 0.1754 0.1704 0.1995 -0.0290 -0.0218 -0.0243 17  TYR   B N   
3938 C  CA  . TYR   B 17  ? 0.1834 0.1731 0.1862 -0.0365 -0.0219 -0.0092 17  TYR   B CA  
3939 C  C   . TYR   B 17  ? 0.1767 0.1564 0.1901 -0.0372 -0.0158 -0.0121 17  TYR   B C   
3940 O  O   . TYR   B 17  ? 0.1730 0.1615 0.1957 -0.0311 -0.0249 -0.0270 17  TYR   B O   
3941 C  CB  . TYR   B 17  ? 0.2141 0.2078 0.2060 -0.0261 -0.0252 0.0177  17  TYR   B CB  
3942 C  CG  . TYR   B 17  ? 0.2415 0.2512 0.2437 -0.0165 -0.0381 0.0244  17  TYR   B CG  
3943 C  CD1 . TYR   B 17  ? 0.2571 0.2667 0.2577 -0.0105 -0.0496 0.0350  17  TYR   B CD1 
3944 C  CD2 . TYR   B 17  ? 0.2619 0.2810 0.2654 -0.0027 -0.0466 0.0178  17  TYR   B CD2 
3945 C  CE1 . TYR   B 17  ? 0.2755 0.2901 0.2707 -0.0001 -0.0571 0.0284  17  TYR   B CE1 
3946 C  CE2 . TYR   B 17  ? 0.2780 0.3012 0.2795 0.0072  -0.0596 0.0223  17  TYR   B CE2 
3947 C  CZ  . TYR   B 17  ? 0.2875 0.3048 0.2793 0.0091  -0.0634 0.0265  17  TYR   B CZ  
3948 O  OH  . TYR   B 17  ? 0.3035 0.3219 0.2956 0.0197  -0.0662 0.0274  17  TYR   B OH  
3958 N  N   . ILE   B 18  ? 0.1824 0.1527 0.1826 -0.0339 -0.0121 -0.0177 18  ILE   B N   
3959 C  CA  . ILE   B 18  ? 0.1833 0.1528 0.1788 -0.0305 -0.0046 -0.0182 18  ILE   B CA  
3960 C  C   . ILE   B 18  ? 0.1955 0.1548 0.1774 -0.0397 -0.0026 -0.0252 18  ILE   B C   
3961 O  O   . ILE   B 18  ? 0.2198 0.1721 0.1784 -0.0358 0.0078  -0.0335 18  ILE   B O   
3962 C  CB  . ILE   B 18  ? 0.1880 0.1496 0.1899 -0.0391 -0.0081 -0.0143 18  ILE   B CB  
3963 C  CG1 . ILE   B 18  ? 0.1920 0.1576 0.2013 -0.0375 -0.0019 -0.0009 18  ILE   B CG1 
3964 C  CG2 . ILE   B 18  ? 0.1902 0.1563 0.1858 -0.0423 -0.0138 -0.0107 18  ILE   B CG2 
3965 C  CD1 . ILE   B 18  ? 0.1983 0.1851 0.2264 -0.0355 -0.0188 0.0151  18  ILE   B CD1 
3977 N  N   . LYS   B 19  ? 0.1931 0.1566 0.2000 -0.0216 0.0259  -0.0348 19  LYS   B N   
3978 C  CA  . LYS   B 19  ? 0.1970 0.1562 0.2147 -0.0265 0.0251  -0.0373 19  LYS   B CA  
3979 C  C   . LYS   B 19  ? 0.1865 0.1527 0.2223 -0.0252 0.0328  -0.0445 19  LYS   B C   
3980 O  O   . LYS   B 19  ? 0.1860 0.1615 0.2089 -0.0132 0.0182  -0.0414 19  LYS   B O   
3981 C  CB  . LYS   B 19  ? 0.2168 0.1772 0.2212 -0.0325 0.0317  -0.0221 19  LYS   B CB  
3982 C  CG  . LYS   B 19  ? 0.2384 0.1954 0.2507 -0.0419 0.0377  -0.0299 19  LYS   B CG  
3983 C  CD  . LYS   B 19  ? 0.2624 0.2289 0.2599 -0.0459 0.0415  -0.0235 19  LYS   B CD  
3984 C  CE  . LYS   B 19  ? 0.2854 0.2550 0.2772 -0.0475 0.0449  -0.0228 19  LYS   B CE  
3985 N  NZ  . LYS   B 19  ? 0.3008 0.2718 0.2884 -0.0539 0.0512  -0.0195 19  LYS   B NZ  
3999 N  N   . ASN   B 20  ? 0.1865 0.1641 0.2540 -0.0204 0.0422  -0.0551 20  ASN   B N   
4000 C  CA  . ASN   B 20  ? 0.1907 0.1762 0.2721 -0.0100 0.0457  -0.0738 20  ASN   B CA  
4001 C  C   . ASN   B 20  ? 0.1873 0.1969 0.2749 -0.0165 0.0524  -0.0804 20  ASN   B C   
4002 O  O   . ASN   B 20  ? 0.2088 0.2340 0.2959 -0.0322 0.0508  -0.0819 20  ASN   B O   
4003 C  CB  . ASN   B 20  ? 0.2218 0.1839 0.3007 0.0101  0.0371  -0.0668 20  ASN   B CB  
4004 C  CG  . ASN   B 20  ? 0.2473 0.1930 0.3169 0.0386  0.0353  -0.0709 20  ASN   B CG  
4005 O  OD1 . ASN   B 20  ? 0.2742 0.2204 0.3426 0.0530  0.0256  -0.0758 20  ASN   B OD1 
4006 N  ND2 . ASN   B 20  ? 0.2401 0.1940 0.3063 0.0323  0.0267  -0.0662 20  ASN   B ND2 
4013 N  N   . ALA   B 21  ? 0.1893 0.1797 0.2766 -0.0220 0.0475  -0.0611 21  ALA   B N   
4014 C  CA  . ALA   B 21  ? 0.1957 0.1873 0.2951 -0.0271 0.0363  -0.0456 21  ALA   B CA  
4015 C  C   . ALA   B 21  ? 0.1914 0.1654 0.2905 -0.0159 0.0380  -0.0342 21  ALA   B C   
4016 O  O   . ALA   B 21  ? 0.1905 0.1542 0.2948 -0.0296 0.0395  -0.0333 21  ALA   B O   
4017 C  CB  . ALA   B 21  ? 0.2114 0.2129 0.2998 -0.0376 0.0344  -0.0323 21  ALA   B CB  
4023 N  N   . ASP   B 22  ? 0.1819 0.1545 0.2747 -0.0214 0.0261  -0.0307 22  ASP   B N   
4024 C  CA  . ASP   B 22  ? 0.1796 0.1518 0.2560 -0.0102 0.0228  -0.0202 22  ASP   B CA  
4025 C  C   . ASP   B 22  ? 0.1760 0.1481 0.2135 -0.0121 0.0177  -0.0141 22  ASP   B C   
4026 O  O   . ASP   B 22  ? 0.1797 0.1518 0.2099 -0.0084 0.0091  -0.0118 22  ASP   B O   
4027 C  CB  . ASP   B 22  ? 0.1848 0.1570 0.2870 -0.0087 0.0186  -0.0073 22  ASP   B CB  
4028 C  CG  . ASP   B 22  ? 0.1865 0.1728 0.3248 -0.0046 -0.0082 -0.0036 22  ASP   B CG  
4029 O  OD1 . ASP   B 22  ? 0.2052 0.1690 0.3244 -0.0002 -0.0270 0.0041  22  ASP   B OD1 
4030 O  OD2 . ASP   B 22  ? 0.1916 0.2034 0.3756 0.0049  -0.0265 -0.0216 22  ASP   B OD2 
4035 N  N   . ILE   B 23  ? 0.1794 0.1392 0.2041 -0.0059 0.0007  0.0084  23  ILE   B N   
4036 C  CA  . ILE   B 23  ? 0.1702 0.1420 0.1820 -0.0075 -0.0066 0.0076  23  ILE   B CA  
4037 C  C   . ILE   B 23  ? 0.1581 0.1419 0.1905 -0.0029 -0.0050 0.0009  23  ILE   B C   
4038 O  O   . ILE   B 23  ? 0.1508 0.1419 0.1789 -0.0092 -0.0068 0.0035  23  ILE   B O   
4039 C  CB  . ILE   B 23  ? 0.1694 0.1488 0.1902 -0.0171 0.0012  0.0148  23  ILE   B CB  
4040 C  CG1 . ILE   B 23  ? 0.1740 0.1570 0.2111 -0.0112 0.0086  0.0217  23  ILE   B CG1 
4041 C  CG2 . ILE   B 23  ? 0.1770 0.1700 0.1986 -0.0189 0.0019  0.0074  23  ILE   B CG2 
4042 C  CD1 . ILE   B 23  ? 0.1799 0.1694 0.2245 -0.0048 0.0050  0.0145  23  ILE   B CD1 
4054 N  N   . VAL   B 24  ? 0.1625 0.1472 0.1992 -0.0057 -0.0116 0.0043  24  VAL   B N   
4055 C  CA  . VAL   B 24  ? 0.1585 0.1495 0.2129 -0.0032 -0.0152 -0.0019 24  VAL   B CA  
4056 C  C   . VAL   B 24  ? 0.1559 0.1521 0.2274 -0.0049 -0.0124 0.0086  24  VAL   B C   
4057 O  O   . VAL   B 24  ? 0.1536 0.1607 0.2319 -0.0136 -0.0102 0.0148  24  VAL   B O   
4058 C  CB  . VAL   B 24  ? 0.1703 0.1649 0.2149 0.0053  -0.0243 0.0006  24  VAL   B CB  
4059 C  CG1 . VAL   B 24  ? 0.1743 0.1741 0.2278 -0.0051 -0.0223 0.0046  24  VAL   B CG1 
4060 C  CG2 . VAL   B 24  ? 0.1825 0.1912 0.2165 0.0075  -0.0233 -0.0044 24  VAL   B CG2 
4070 N  N   . GLU   B 25  ? 0.1776 0.1626 0.2261 -0.0082 -0.0086 0.0143  25  GLU   B N   
4071 C  CA  . GLU   B 25  ? 0.1877 0.1880 0.2397 -0.0007 0.0077  0.0059  25  GLU   B CA  
4072 C  C   . GLU   B 25  ? 0.1838 0.1779 0.2097 -0.0090 0.0134  0.0053  25  GLU   B C   
4073 O  O   . GLU   B 25  ? 0.1902 0.1944 0.2258 -0.0078 0.0226  0.0087  25  GLU   B O   
4074 C  CB  . GLU   B 25  ? 0.2190 0.2300 0.2996 0.0201  0.0110  0.0065  25  GLU   B CB  
4075 C  CG  . GLU   B 25  ? 0.2556 0.2871 0.3984 0.0280  0.0105  -0.0005 25  GLU   B CG  
4076 C  CD  . GLU   B 25  ? 0.3052 0.3381 0.4804 0.0238  0.0108  -0.0108 25  GLU   B CD  
4077 O  OE1 . GLU   B 25  ? 0.3151 0.3597 0.5098 0.0310  0.0181  -0.0093 25  GLU   B OE1 
4078 O  OE2 . GLU   B 25  ? 0.3119 0.3565 0.5095 0.0215  0.0031  -0.0239 25  GLU   B OE2 
4085 N  N   . GLU   B 26  ? 0.1803 0.1702 0.1817 -0.0266 0.0063  -0.0021 26  GLU   B N   
4086 C  CA  . GLU   B 26  ? 0.1781 0.1829 0.1943 -0.0363 -0.0062 0.0002  26  GLU   B CA  
4087 C  C   . GLU   B 26  ? 0.1663 0.1747 0.1923 -0.0242 0.0067  0.0169  26  GLU   B C   
4088 O  O   . GLU   B 26  ? 0.1839 0.1954 0.1974 -0.0223 -0.0006 0.0281  26  GLU   B O   
4089 C  CB  . GLU   B 26  ? 0.2067 0.2063 0.2123 -0.0481 -0.0054 0.0102  26  GLU   B CB  
4090 C  CG  . GLU   B 26  ? 0.2460 0.2417 0.2684 -0.0547 0.0070  -0.0131 26  GLU   B CG  
4091 C  CD  . GLU   B 26  ? 0.2695 0.2659 0.2797 -0.0733 0.0212  -0.0389 26  GLU   B CD  
4092 O  OE1 . GLU   B 26  ? 0.2936 0.2519 0.2949 -0.0809 0.0553  -0.0344 26  GLU   B OE1 
4093 O  OE2 . GLU   B 26  ? 0.2689 0.3052 0.3232 -0.0603 0.0107  -0.0344 26  GLU   B OE2 
4100 N  N   . ALA   B 27  ? 0.1503 0.1656 0.1893 -0.0228 0.0050  0.0195  27  ALA   B N   
4101 C  CA  . ALA   B 27  ? 0.1570 0.1640 0.2094 -0.0158 -0.0024 0.0233  27  ALA   B CA  
4102 C  C   . ALA   B 27  ? 0.1575 0.1702 0.2282 -0.0139 0.0119  0.0361  27  ALA   B C   
4103 O  O   . ALA   B 27  ? 0.1695 0.1780 0.2371 -0.0053 0.0116  0.0394  27  ALA   B O   
4104 C  CB  . ALA   B 27  ? 0.1755 0.1458 0.2132 -0.0172 0.0054  0.0199  27  ALA   B CB  
4110 N  N   . LYS   B 28  ? 0.1510 0.1929 0.2719 -0.0209 0.0185  0.0571  28  LYS   B N   
4111 C  CA  . LYS   B 28  ? 0.1699 0.2287 0.2899 -0.0083 0.0441  0.0871  28  LYS   B CA  
4112 C  C   . LYS   B 28  ? 0.1934 0.2495 0.2759 0.0015  0.0603  0.0820  28  LYS   B C   
4113 O  O   . LYS   B 28  ? 0.2173 0.2560 0.2946 -0.0013 0.0587  0.0822  28  LYS   B O   
4114 C  CB  . LYS   B 28  ? 0.1924 0.2618 0.3445 0.0039  0.0636  0.1042  28  LYS   B CB  
4115 C  CG  . LYS   B 28  ? 0.2205 0.3081 0.3833 0.0169  0.0705  0.1121  28  LYS   B CG  
4116 C  CD  . LYS   B 28  ? 0.2608 0.3634 0.4272 0.0215  0.0893  0.1161  28  LYS   B CD  
4117 C  CE  . LYS   B 28  ? 0.2974 0.4044 0.4699 0.0305  0.0902  0.1192  28  LYS   B CE  
4118 N  NZ  . LYS   B 28  ? 0.3103 0.4200 0.4865 0.0390  0.0893  0.1261  28  LYS   B NZ  
4132 N  N   . LYS   B 29  ? 0.2123 0.2713 0.2819 0.0240  0.0586  0.0689  29  LYS   B N   
4133 C  CA  . LYS   B 29  ? 0.2529 0.3000 0.2995 0.0272  0.0527  0.0719  29  LYS   B CA  
4134 C  C   . LYS   B 29  ? 0.2462 0.3030 0.2678 0.0241  0.0457  0.0795  29  LYS   B C   
4135 O  O   . LYS   B 29  ? 0.2654 0.3257 0.2778 0.0320  0.0483  0.0757  29  LYS   B O   
4136 C  CB  . LYS   B 29  ? 0.3039 0.3313 0.3721 0.0260  0.0480  0.0592  29  LYS   B CB  
4137 C  CG  . LYS   B 29  ? 0.3514 0.3573 0.4530 0.0199  0.0485  0.0581  29  LYS   B CG  
4138 C  CD  . LYS   B 29  ? 0.3901 0.3742 0.5142 0.0125  0.0567  0.0538  29  LYS   B CD  
4139 C  CE  . LYS   B 29  ? 0.4182 0.3838 0.5561 0.0062  0.0661  0.0490  29  LYS   B CE  
4140 N  NZ  . LYS   B 29  ? 0.4310 0.3899 0.5866 0.0033  0.0679  0.0459  29  LYS   B NZ  
4154 N  N   . VAL   B 30  ? 0.2188 0.2862 0.2515 0.0028  0.0325  0.0784  30  VAL   B N   
4155 C  CA  . VAL   B 30  ? 0.2088 0.2746 0.2804 -0.0057 -0.0006 0.0803  30  VAL   B CA  
4156 C  C   . VAL   B 30  ? 0.1818 0.2631 0.2695 -0.0090 0.0087  0.1006  30  VAL   B C   
4157 O  O   . VAL   B 30  ? 0.1953 0.2837 0.2760 -0.0032 0.0092  0.1139  30  VAL   B O   
4158 C  CB  . VAL   B 30  ? 0.2147 0.2700 0.3164 -0.0183 -0.0275 0.0669  30  VAL   B CB  
4159 C  CG1 . VAL   B 30  ? 0.2221 0.2770 0.3150 -0.0166 -0.0223 0.0559  30  VAL   B CG1 
4160 C  CG2 . VAL   B 30  ? 0.2240 0.2700 0.3375 -0.0249 -0.0430 0.0528  30  VAL   B CG2 
4170 N  N   . LYS   B 31  ? 0.1705 0.2259 0.2941 -0.0195 -0.0002 0.0997  31  LYS   B N   
4171 C  CA  . LYS   B 31  ? 0.1606 0.2183 0.3210 -0.0314 -0.0069 0.1019  31  LYS   B CA  
4172 C  C   . LYS   B 31  ? 0.1550 0.1833 0.2837 -0.0349 -0.0286 0.0832  31  LYS   B C   
4173 O  O   . LYS   B 31  ? 0.1678 0.2029 0.3024 -0.0230 -0.0212 0.1005  31  LYS   B O   
4174 C  CB  . LYS   B 31  ? 0.1768 0.2662 0.3713 -0.0268 0.0217  0.1125  31  LYS   B CB  
4175 C  CG  . LYS   B 31  ? 0.2070 0.3119 0.4107 -0.0258 0.0378  0.1074  31  LYS   B CG  
4176 C  CD  . LYS   B 31  ? 0.2351 0.3536 0.4440 -0.0149 0.0357  0.0937  31  LYS   B CD  
4177 C  CE  . LYS   B 31  ? 0.2560 0.3828 0.4789 -0.0094 0.0241  0.0818  31  LYS   B CE  
4178 N  NZ  . LYS   B 31  ? 0.2722 0.3986 0.4913 -0.0013 0.0089  0.0708  31  LYS   B NZ  
4192 N  N   . PRO   B 32  ? 0.1661 0.1568 0.2300 -0.0314 -0.0441 0.0446  32  PRO   B N   
4193 C  CA  . PRO   B 32  ? 0.1742 0.1507 0.1918 -0.0321 -0.0401 0.0320  32  PRO   B CA  
4194 C  C   . PRO   B 32  ? 0.1826 0.1417 0.1916 -0.0362 -0.0524 0.0305  32  PRO   B C   
4195 O  O   . PRO   B 32  ? 0.1981 0.1469 0.2200 -0.0406 -0.0716 0.0314  32  PRO   B O   
4196 C  CB  . PRO   B 32  ? 0.1928 0.1446 0.1915 -0.0324 -0.0295 0.0147  32  PRO   B CB  
4197 C  CG  . PRO   B 32  ? 0.2039 0.1404 0.1996 -0.0282 -0.0449 0.0217  32  PRO   B CG  
4198 C  CD  . PRO   B 32  ? 0.1910 0.1440 0.2208 -0.0240 -0.0589 0.0231  32  PRO   B CD  
4206 N  N   . THR   B 33  ? 0.1862 0.1379 0.1848 -0.0278 -0.0492 0.0188  33  THR   B N   
4207 C  CA  . THR   B 33  ? 0.1936 0.1443 0.1760 -0.0316 -0.0441 0.0157  33  THR   B CA  
4208 C  C   . THR   B 33  ? 0.1989 0.1337 0.1665 -0.0296 -0.0465 0.0141  33  THR   B C   
4209 O  O   . THR   B 33  ? 0.2186 0.1395 0.1819 -0.0385 -0.0555 0.0176  33  THR   B O   
4210 C  CB  . THR   B 33  ? 0.2009 0.1485 0.1826 -0.0154 -0.0496 0.0205  33  THR   B CB  
4211 O  OG1 . THR   B 33  ? 0.1873 0.1600 0.1884 -0.0189 -0.0480 0.0307  33  THR   B OG1 
4212 C  CG2 . THR   B 33  ? 0.2253 0.1555 0.2059 -0.0112 -0.0466 0.0155  33  THR   B CG2 
4220 N  N   . VAL   B 34  ? 0.1831 0.1314 0.1533 -0.0313 -0.0424 0.0132  34  VAL   B N   
4221 C  CA  . VAL   B 34  ? 0.1680 0.1291 0.1531 -0.0259 -0.0343 0.0086  34  VAL   B CA  
4222 C  C   . VAL   B 34  ? 0.1544 0.1246 0.1407 -0.0265 -0.0261 0.0098  34  VAL   B C   
4223 O  O   . VAL   B 34  ? 0.1719 0.1303 0.1487 -0.0230 -0.0346 0.0097  34  VAL   B O   
4224 C  CB  . VAL   B 34  ? 0.1765 0.1406 0.1798 -0.0054 -0.0230 0.0020  34  VAL   B CB  
4225 C  CG1 . VAL   B 34  ? 0.1728 0.1549 0.1925 -0.0065 -0.0101 -0.0064 34  VAL   B CG1 
4226 C  CG2 . VAL   B 34  ? 0.1848 0.1457 0.2077 -0.0041 -0.0224 0.0012  34  VAL   B CG2 
4236 N  N   . VAL   B 35  ? 0.1466 0.1258 0.1355 -0.0258 -0.0149 0.0039  35  VAL   B N   
4237 C  CA  . VAL   B 35  ? 0.1389 0.1228 0.1473 -0.0180 -0.0099 0.0101  35  VAL   B CA  
4238 C  C   . VAL   B 35  ? 0.1317 0.1201 0.1439 -0.0126 -0.0132 0.0042  35  VAL   B C   
4239 O  O   . VAL   B 35  ? 0.1382 0.1226 0.1465 -0.0235 -0.0021 -0.0056 35  VAL   B O   
4240 C  CB  . VAL   B 35  ? 0.1359 0.1402 0.1541 -0.0185 -0.0019 0.0080  35  VAL   B CB  
4241 C  CG1 . VAL   B 35  ? 0.1305 0.1540 0.1739 -0.0206 -0.0016 0.0050  35  VAL   B CG1 
4242 C  CG2 . VAL   B 35  ? 0.1410 0.1464 0.1747 -0.0081 0.0006  0.0011  35  VAL   B CG2 
4252 N  N   . VAL   B 36  ? 0.1324 0.1260 0.1419 -0.0163 -0.0140 0.0062  36  VAL   B N   
4253 C  CA  . VAL   B 36  ? 0.1296 0.1190 0.1395 -0.0118 -0.0087 0.0065  36  VAL   B CA  
4254 C  C   . VAL   B 36  ? 0.1241 0.1188 0.1358 -0.0104 -0.0063 0.0017  36  VAL   B C   
4255 O  O   . VAL   B 36  ? 0.1329 0.1290 0.1568 -0.0090 -0.0016 -0.0030 36  VAL   B O   
4256 C  CB  . VAL   B 36  ? 0.1262 0.1256 0.1501 -0.0182 -0.0012 -0.0007 36  VAL   B CB  
4257 C  CG1 . VAL   B 36  ? 0.1303 0.1349 0.1628 -0.0222 -0.0023 0.0012  36  VAL   B CG1 
4258 C  CG2 . VAL   B 36  ? 0.1331 0.1314 0.1545 -0.0135 -0.0167 0.0096  36  VAL   B CG2 
4268 N  N   . ASN   B 37  ? 0.1296 0.1228 0.1315 -0.0037 -0.0105 0.0085  37  ASN   B N   
4269 C  CA  . ASN   B 37  ? 0.1311 0.1244 0.1458 0.0007  -0.0162 0.0080  37  ASN   B CA  
4270 C  C   . ASN   B 37  ? 0.1263 0.1234 0.1448 0.0043  -0.0084 0.0029  37  ASN   B C   
4271 O  O   . ASN   B 37  ? 0.1393 0.1336 0.1417 0.0030  -0.0000 0.0050  37  ASN   B O   
4272 C  CB  . ASN   B 37  ? 0.1264 0.1291 0.1435 0.0033  -0.0116 0.0040  37  ASN   B CB  
4273 C  CG  . ASN   B 37  ? 0.1301 0.1265 0.1453 -0.0010 -0.0103 0.0046  37  ASN   B CG  
4274 O  OD1 . ASN   B 37  ? 0.1388 0.1356 0.1621 0.0098  -0.0143 0.0027  37  ASN   B OD1 
4275 N  ND2 . ASN   B 37  ? 0.1394 0.1257 0.1559 -0.0005 -0.0136 0.0055  37  ASN   B ND2 
4282 N  N   . ALA   B 38  ? 0.1360 0.1197 0.1395 0.0077  -0.0017 -0.0001 38  ALA   B N   
4283 C  CA  . ALA   B 38  ? 0.1508 0.1265 0.1408 0.0015  0.0024  0.0109  38  ALA   B CA  
4284 C  C   . ALA   B 38  ? 0.1454 0.1210 0.1420 -0.0003 0.0041  0.0132  38  ALA   B C   
4285 O  O   . ALA   B 38  ? 0.1549 0.1296 0.1633 0.0067  -0.0014 0.0132  38  ALA   B O   
4286 C  CB  . ALA   B 38  ? 0.1689 0.1352 0.1584 -0.0058 0.0090  0.0088  38  ALA   B CB  
4292 N  N   . ALA   B 39  ? 0.1408 0.1272 0.1339 0.0088  -0.0057 0.0028  39  ALA   B N   
4293 C  CA  . ALA   B 39  ? 0.1495 0.1337 0.1407 0.0057  -0.0070 0.0087  39  ALA   B CA  
4294 C  C   . ALA   B 39  ? 0.1510 0.1387 0.1366 0.0039  -0.0053 0.0064  39  ALA   B C   
4295 O  O   . ALA   B 39  ? 0.1526 0.1508 0.1559 0.0016  -0.0052 0.0119  39  ALA   B O   
4296 C  CB  . ALA   B 39  ? 0.1583 0.1340 0.1569 -0.0001 -0.0031 0.0042  39  ALA   B CB  
4302 N  N   . ASN   B 40  ? 0.1555 0.1623 0.1421 -0.0092 -0.0023 -0.0036 40  ASN   B N   
4303 C  CA  . ASN   B 40  ? 0.1611 0.1658 0.1507 -0.0028 -0.0046 -0.0035 40  ASN   B CA  
4304 C  C   . ASN   B 40  ? 0.1660 0.1648 0.1318 0.0041  -0.0088 -0.0003 40  ASN   B C   
4305 O  O   . ASN   B 40  ? 0.1641 0.1554 0.1424 0.0077  -0.0110 0.0020  40  ASN   B O   
4306 C  CB  . ASN   B 40  ? 0.1755 0.1673 0.1746 0.0089  -0.0091 0.0113  40  ASN   B CB  
4307 C  CG  . ASN   B 40  ? 0.1802 0.1692 0.2017 0.0044  -0.0189 0.0135  40  ASN   B CG  
4308 O  OD1 . ASN   B 40  ? 0.1770 0.1622 0.2594 0.0063  -0.0301 0.0142  40  ASN   B OD1 
4309 N  ND2 . ASN   B 40  ? 0.1833 0.1686 0.2011 0.0061  -0.0148 0.0190  40  ASN   B ND2 
4316 N  N   . VAL   B 41  ? 0.1769 0.1684 0.1286 0.0127  0.0022  0.0030  41  VAL   B N   
4317 C  CA  . VAL   B 41  ? 0.1821 0.1801 0.1392 0.0115  -0.0033 -0.0068 41  VAL   B CA  
4318 C  C   . VAL   B 41  ? 0.1787 0.1792 0.1410 0.0186  -0.0088 -0.0099 41  VAL   B C   
4319 O  O   . VAL   B 41  ? 0.1738 0.1766 0.1605 0.0143  -0.0103 -0.0157 41  VAL   B O   
4320 C  CB  . VAL   B 41  ? 0.1949 0.2030 0.1617 -0.0046 0.0189  -0.0190 41  VAL   B CB  
4321 C  CG1 . VAL   B 41  ? 0.1924 0.2112 0.1722 -0.0055 0.0336  -0.0209 41  VAL   B CG1 
4322 C  CG2 . VAL   B 41  ? 0.2068 0.2229 0.1693 -0.0105 0.0230  -0.0213 41  VAL   B CG2 
4332 N  N   . TYR   B 42  ? 0.1842 0.1754 0.1463 0.0197  -0.0216 0.0023  42  TYR   B N   
4333 C  CA  . TYR   B 42  ? 0.1934 0.1838 0.1502 0.0127  -0.0263 -0.0139 42  TYR   B CA  
4334 C  C   . TYR   B 42  ? 0.1733 0.1677 0.1536 0.0205  -0.0219 -0.0144 42  TYR   B C   
4335 O  O   . TYR   B 42  ? 0.1757 0.1734 0.1835 0.0164  -0.0263 -0.0180 42  TYR   B O   
4336 C  CB  . TYR   B 42  ? 0.2164 0.2105 0.1651 0.0105  -0.0234 -0.0036 42  TYR   B CB  
4337 C  CG  . TYR   B 42  ? 0.2212 0.2277 0.1666 0.0031  -0.0219 0.0051  42  TYR   B CG  
4338 C  CD1 . TYR   B 42  ? 0.2204 0.2283 0.1475 0.0011  -0.0123 -0.0055 42  TYR   B CD1 
4339 C  CD2 . TYR   B 42  ? 0.2346 0.2361 0.2002 0.0028  -0.0101 0.0091  42  TYR   B CD2 
4340 C  CE1 . TYR   B 42  ? 0.2326 0.2423 0.1476 0.0066  -0.0103 0.0000  42  TYR   B CE1 
4341 C  CE2 . TYR   B 42  ? 0.2391 0.2474 0.1949 0.0063  0.0054  0.0186  42  TYR   B CE2 
4342 C  CZ  . TYR   B 42  ? 0.2497 0.2562 0.1780 0.0227  0.0083  0.0064  42  TYR   B CZ  
4343 O  OH  . TYR   B 42  ? 0.2823 0.2862 0.2279 0.0392  0.0199  0.0139  42  TYR   B OH  
4353 N  N   . LEU   B 43  ? 0.1614 0.1541 0.1445 0.0115  -0.0162 -0.0105 43  LEU   B N   
4354 C  CA  . LEU   B 43  ? 0.1615 0.1523 0.1397 0.0085  -0.0127 -0.0012 43  LEU   B CA  
4355 C  C   . LEU   B 43  ? 0.1681 0.1544 0.1514 0.0066  -0.0157 -0.0056 43  LEU   B C   
4356 O  O   . LEU   B 43  ? 0.1643 0.1571 0.1802 0.0069  -0.0196 0.0100  43  LEU   B O   
4357 C  CB  . LEU   B 43  ? 0.1564 0.1468 0.1570 0.0015  -0.0235 -0.0071 43  LEU   B CB  
4358 C  CG  . LEU   B 43  ? 0.1630 0.1447 0.1694 0.0010  -0.0293 -0.0044 43  LEU   B CG  
4359 C  CD1 . LEU   B 43  ? 0.1756 0.1498 0.2064 -0.0035 -0.0370 -0.0025 43  LEU   B CD1 
4360 C  CD2 . LEU   B 43  ? 0.1607 0.1431 0.1851 -0.0042 -0.0294 -0.0023 43  LEU   B CD2 
4372 N  N   . LYS   B 44  ? 0.1627 0.1512 0.1567 0.0104  -0.0045 -0.0111 44  LYS   B N   
4373 C  CA  . LYS   B 44  ? 0.1764 0.1607 0.1594 0.0082  -0.0087 0.0080  44  LYS   B CA  
4374 C  C   . LYS   B 44  ? 0.1615 0.1548 0.1577 0.0137  -0.0145 0.0004  44  LYS   B C   
4375 O  O   . LYS   B 44  ? 0.1900 0.1527 0.1886 0.0058  -0.0063 0.0032  44  LYS   B O   
4376 C  CB  . LYS   B 44  ? 0.2043 0.1840 0.1803 0.0181  -0.0209 0.0004  44  LYS   B CB  
4377 C  CG  . LYS   B 44  ? 0.2384 0.2110 0.2102 0.0155  -0.0456 0.0011  44  LYS   B CG  
4378 C  CD  . LYS   B 44  ? 0.2727 0.2285 0.2618 0.0016  -0.0503 -0.0011 44  LYS   B CD  
4379 C  CE  . LYS   B 44  ? 0.2999 0.2523 0.3023 -0.0038 -0.0501 0.0081  44  LYS   B CE  
4380 N  NZ  . LYS   B 44  ? 0.3112 0.2619 0.3265 -0.0024 -0.0547 0.0190  44  LYS   B NZ  
4394 N  N   . HIS   B 45  ? 0.1597 0.1583 0.1414 0.0074  -0.0119 0.0123  45  HIS   B N   
4395 C  CA  . HIS   B 45  ? 0.1620 0.1536 0.1621 0.0121  -0.0060 -0.0023 45  HIS   B CA  
4396 C  C   . HIS   B 45  ? 0.1862 0.1705 0.1931 0.0167  -0.0196 -0.0063 45  HIS   B C   
4397 O  O   . HIS   B 45  ? 0.1984 0.1991 0.2390 0.0420  0.0120  -0.0028 45  HIS   B O   
4398 C  CB  . HIS   B 45  ? 0.1520 0.1569 0.1594 0.0024  -0.0016 -0.0033 45  HIS   B CB  
4399 C  CG  . HIS   B 45  ? 0.1538 0.1514 0.1619 -0.0050 -0.0040 -0.0032 45  HIS   B CG  
4400 N  ND1 . HIS   B 45  ? 0.1605 0.1497 0.1723 0.0039  -0.0147 -0.0082 45  HIS   B ND1 
4401 C  CD2 . HIS   B 45  ? 0.1620 0.1563 0.1722 -0.0103 -0.0155 0.0010  45  HIS   B CD2 
4402 C  CE1 . HIS   B 45  ? 0.1673 0.1435 0.1607 0.0006  -0.0186 -0.0091 45  HIS   B CE1 
4403 N  NE2 . HIS   B 45  ? 0.1704 0.1513 0.1625 -0.0006 -0.0154 -0.0016 45  HIS   B NE2 
4411 N  N   . GLY   B 46  ? 0.2043 0.1605 0.2234 0.0191  -0.0401 0.0027  46  GLY   B N   
4412 C  CA  . GLY   B 46  ? 0.2184 0.1745 0.2606 0.0175  -0.0469 0.0110  46  GLY   B CA  
4413 C  C   . GLY   B 46  ? 0.2225 0.1963 0.3013 0.0256  -0.0442 0.0109  46  GLY   B C   
4414 O  O   . GLY   B 46  ? 0.2386 0.2273 0.3836 0.0292  -0.0209 -0.0123 46  GLY   B O   
4418 N  N   . GLY   B 47  ? 0.2124 0.2022 0.2697 0.0078  -0.0257 0.0033  47  GLY   B N   
4419 C  CA  . GLY   B 47  ? 0.2009 0.1797 0.2320 0.0037  -0.0155 0.0050  47  GLY   B CA  
4420 C  C   . GLY   B 47  ? 0.1795 0.1571 0.2048 0.0074  0.0018  0.0047  47  GLY   B C   
4421 O  O   . GLY   B 47  ? 0.1860 0.1445 0.2048 0.0062  -0.0082 0.0055  47  GLY   B O   
4425 N  N   . GLY   B 48  ? 0.1606 0.1428 0.1998 0.0075  -0.0096 0.0183  48  GLY   B N   
4426 C  CA  . GLY   B 48  ? 0.1560 0.1424 0.1924 0.0009  0.0011  0.0112  48  GLY   B CA  
4427 C  C   . GLY   B 48  ? 0.1505 0.1404 0.1844 0.0009  0.0033  0.0056  48  GLY   B C   
4428 O  O   . GLY   B 48  ? 0.1440 0.1430 0.2004 0.0071  -0.0053 0.0025  48  GLY   B O   
4432 N  N   . VAL   B 49  ? 0.1528 0.1463 0.1738 0.0110  0.0031  0.0126  49  VAL   B N   
4433 C  CA  . VAL   B 49  ? 0.1542 0.1530 0.1632 0.0073  -0.0131 0.0000  49  VAL   B CA  
4434 C  C   . VAL   B 49  ? 0.1427 0.1477 0.1500 0.0136  -0.0091 0.0020  49  VAL   B C   
4435 O  O   . VAL   B 49  ? 0.1528 0.1504 0.1658 0.0040  -0.0085 0.0058  49  VAL   B O   
4436 C  CB  . VAL   B 49  ? 0.1530 0.1709 0.1993 0.0045  -0.0200 -0.0014 49  VAL   B CB  
4437 C  CG1 . VAL   B 49  ? 0.1504 0.1796 0.2002 0.0069  -0.0251 -0.0019 49  VAL   B CG1 
4438 C  CG2 . VAL   B 49  ? 0.1749 0.1855 0.2265 -0.0046 -0.0344 -0.0043 49  VAL   B CG2 
4448 N  N   . ALA   B 50  ? 0.1421 0.1386 0.1557 0.0064  -0.0055 0.0070  50  ALA   B N   
4449 C  CA  . ALA   B 50  ? 0.1391 0.1355 0.1541 0.0086  -0.0080 0.0057  50  ALA   B CA  
4450 C  C   . ALA   B 50  ? 0.1468 0.1407 0.1612 0.0079  -0.0084 0.0074  50  ALA   B C   
4451 O  O   . ALA   B 50  ? 0.1412 0.1383 0.1640 0.0098  -0.0047 0.0030  50  ALA   B O   
4452 C  CB  . ALA   B 50  ? 0.1452 0.1334 0.1646 0.0024  0.0028  0.0111  50  ALA   B CB  
4458 N  N   . GLY   B 51  ? 0.1427 0.1479 0.1717 0.0110  -0.0131 0.0070  51  GLY   B N   
4459 C  CA  . GLY   B 51  ? 0.1471 0.1553 0.1840 0.0168  -0.0183 0.0120  51  GLY   B CA  
4460 C  C   . GLY   B 51  ? 0.1454 0.1538 0.1798 0.0215  -0.0082 0.0082  51  GLY   B C   
4461 O  O   . GLY   B 51  ? 0.1482 0.1655 0.2018 0.0102  -0.0082 -0.0016 51  GLY   B O   
4465 N  N   . ALA   B 52  ? 0.1473 0.1471 0.1765 0.0199  -0.0076 0.0117  52  ALA   B N   
4466 C  CA  . ALA   B 52  ? 0.1492 0.1507 0.1787 0.0198  0.0034  -0.0018 52  ALA   B CA  
4467 C  C   . ALA   B 52  ? 0.1424 0.1523 0.1764 0.0158  -0.0009 -0.0041 52  ALA   B C   
4468 O  O   . ALA   B 52  ? 0.1500 0.1604 0.1872 0.0138  0.0076  -0.0004 52  ALA   B O   
4469 C  CB  . ALA   B 52  ? 0.1688 0.1595 0.1942 0.0067  0.0068  -0.0034 52  ALA   B CB  
4475 N  N   . LEU   B 53  ? 0.1388 0.1512 0.1567 0.0217  0.0030  0.0030  53  LEU   B N   
4476 C  CA  . LEU   B 53  ? 0.1356 0.1556 0.1588 0.0157  -0.0066 0.0081  53  LEU   B CA  
4477 C  C   . LEU   B 53  ? 0.1449 0.1482 0.1574 0.0138  0.0120  0.0087  53  LEU   B C   
4478 O  O   . LEU   B 53  ? 0.1513 0.1590 0.1700 0.0018  0.0049  0.0198  53  LEU   B O   
4479 C  CB  . LEU   B 53  ? 0.1385 0.1606 0.1784 0.0051  -0.0053 0.0159  53  LEU   B CB  
4480 C  CG  . LEU   B 53  ? 0.1386 0.1687 0.1810 0.0016  0.0012  0.0188  53  LEU   B CG  
4481 C  CD1 . LEU   B 53  ? 0.1477 0.1922 0.2011 0.0154  -0.0032 0.0104  53  LEU   B CD1 
4482 C  CD2 . LEU   B 53  ? 0.1552 0.1954 0.2075 -0.0085 -0.0035 -0.0160 53  LEU   B CD2 
4494 N  N   . ASN   B 54  ? 0.1414 0.1383 0.1556 0.0049  0.0034  0.0079  54  ASN   B N   
4495 C  CA  . ASN   B 54  ? 0.1438 0.1537 0.1690 0.0024  -0.0040 -0.0011 54  ASN   B CA  
4496 C  C   . ASN   B 54  ? 0.1412 0.1554 0.1826 0.0018  -0.0030 0.0063  54  ASN   B C   
4497 O  O   . ASN   B 54  ? 0.1400 0.1607 0.1957 -0.0029 -0.0003 0.0002  54  ASN   B O   
4498 C  CB  . ASN   B 54  ? 0.1489 0.1666 0.1865 0.0011  0.0054  0.0005  54  ASN   B CB  
4499 C  CG  . ASN   B 54  ? 0.1459 0.1709 0.1796 0.0056  -0.0043 -0.0002 54  ASN   B CG  
4500 O  OD1 . ASN   B 54  ? 0.1431 0.1709 0.1942 0.0018  -0.0138 -0.0101 54  ASN   B OD1 
4501 N  ND2 . ASN   B 54  ? 0.1584 0.1902 0.2084 -0.0000 -0.0278 0.0137  54  ASN   B ND2 
4508 N  N   . LYS   B 55  ? 0.1427 0.1611 0.2023 0.0124  -0.0019 0.0094  55  LYS   B N   
4509 C  CA  . LYS   B 55  ? 0.1452 0.1715 0.2183 0.0201  -0.0022 0.0068  55  LYS   B CA  
4510 C  C   . LYS   B 55  ? 0.1397 0.1689 0.2186 0.0143  0.0040  -0.0019 55  LYS   B C   
4511 O  O   . LYS   B 55  ? 0.1356 0.1851 0.2352 0.0131  0.0085  -0.0048 55  LYS   B O   
4512 C  CB  . LYS   B 55  ? 0.1575 0.1857 0.2474 0.0316  0.0068  0.0193  55  LYS   B CB  
4513 C  CG  . LYS   B 55  ? 0.2017 0.2133 0.3156 0.0354  0.0248  0.0302  55  LYS   B CG  
4514 C  CD  . LYS   B 55  ? 0.2388 0.2396 0.3809 0.0477  0.0489  0.0300  55  LYS   B CD  
4515 C  CE  . LYS   B 55  ? 0.2644 0.2606 0.4385 0.0510  0.0639  0.0237  55  LYS   B CE  
4516 N  NZ  . LYS   B 55  ? 0.2712 0.2750 0.4693 0.0508  0.0505  0.0264  55  LYS   B NZ  
4530 N  N   . ALA   B 56  ? 0.1401 0.1757 0.1958 0.0086  -0.0045 -0.0086 56  ALA   B N   
4531 C  CA  . ALA   B 56  ? 0.1566 0.1906 0.2024 0.0050  -0.0009 -0.0081 56  ALA   B CA  
4532 C  C   . ALA   B 56  ? 0.1496 0.1879 0.2026 0.0022  0.0095  0.0020  56  ALA   B C   
4533 O  O   . ALA   B 56  ? 0.1662 0.1993 0.2098 0.0036  0.0328  0.0049  56  ALA   B O   
4534 C  CB  . ALA   B 56  ? 0.1722 0.2122 0.2023 -0.0074 -0.0001 -0.0171 56  ALA   B CB  
4540 N  N   . THR   B 57  ? 0.1429 0.1804 0.2011 0.0072  0.0125  0.0082  57  THR   B N   
4541 C  CA  . THR   B 57  ? 0.1516 0.1767 0.1973 0.0006  0.0225  0.0081  57  THR   B CA  
4542 C  C   . THR   B 57  ? 0.1581 0.1893 0.2137 -0.0016 0.0171  0.0035  57  THR   B C   
4543 O  O   . THR   B 57  ? 0.1631 0.1884 0.2174 -0.0171 0.0140  0.0068  57  THR   B O   
4544 C  CB  . THR   B 57  ? 0.1618 0.1607 0.1794 0.0009  0.0178  0.0172  57  THR   B CB  
4545 O  OG1 . THR   B 57  ? 0.1571 0.1535 0.2046 0.0002  0.0183  0.0070  57  THR   B OG1 
4546 C  CG2 . THR   B 57  ? 0.1545 0.1629 0.1890 0.0011  0.0150  0.0113  57  THR   B CG2 
4554 N  N   . ASN   B 58  ? 0.1436 0.2056 0.2350 -0.0131 0.0033  -0.0109 58  ASN   B N   
4555 C  CA  . ASN   B 58  ? 0.1655 0.2507 0.2746 -0.0212 0.0278  0.0007  58  ASN   B CA  
4556 C  C   . ASN   B 58  ? 0.1450 0.2206 0.2410 -0.0133 0.0005  0.0004  58  ASN   B C   
4557 O  O   . ASN   B 58  ? 0.1526 0.2273 0.2480 -0.0169 0.0027  -0.0024 58  ASN   B O   
4558 C  CB  . ASN   B 58  ? 0.2618 0.3292 0.3894 -0.0337 0.0562  0.0105  58  ASN   B CB  
4559 C  CG  . ASN   B 58  ? 0.3651 0.4006 0.5324 -0.0380 0.0731  0.0289  58  ASN   B CG  
4560 O  OD1 . ASN   B 58  ? 0.4118 0.4243 0.5856 -0.0397 0.0780  0.0337  58  ASN   B OD1 
4561 N  ND2 . ASN   B 58  ? 0.4458 0.4458 0.5832 -0.0412 0.0797  0.0329  58  ASN   B ND2 
4568 N  N   . ASN   B 59  ? 0.1432 0.2064 0.2209 -0.0109 -0.0030 0.0072  59  ASN   B N   
4569 C  CA  . ASN   B 59  ? 0.1442 0.2091 0.2131 -0.0065 -0.0153 0.0159  59  ASN   B CA  
4570 C  C   . ASN   B 59  ? 0.1365 0.1974 0.2022 -0.0117 -0.0184 0.0032  59  ASN   B C   
4571 O  O   . ASN   B 59  ? 0.1454 0.1993 0.2020 -0.0096 -0.0089 0.0040  59  ASN   B O   
4572 C  CB  . ASN   B 59  ? 0.1570 0.2273 0.2241 0.0017  -0.0304 0.0145  59  ASN   B CB  
4573 C  CG  . ASN   B 59  ? 0.1731 0.2465 0.2445 0.0015  -0.0432 0.0113  59  ASN   B CG  
4574 O  OD1 . ASN   B 59  ? 0.1837 0.2479 0.2395 0.0010  -0.0288 0.0242  59  ASN   B OD1 
4575 N  ND2 . ASN   B 59  ? 0.1773 0.2544 0.2594 -0.0068 -0.0485 0.0033  59  ASN   B ND2 
4582 N  N   . ALA   B 60  ? 0.1482 0.1797 0.2080 -0.0103 -0.0073 0.0028  60  ALA   B N   
4583 C  CA  . ALA   B 60  ? 0.1550 0.1719 0.1934 -0.0164 -0.0101 0.0090  60  ALA   B CA  
4584 C  C   . ALA   B 60  ? 0.1532 0.1615 0.1832 -0.0143 -0.0134 0.0092  60  ALA   B C   
4585 O  O   . ALA   B 60  ? 0.1532 0.1665 0.1909 -0.0208 -0.0059 -0.0027 60  ALA   B O   
4586 C  CB  . ALA   B 60  ? 0.1670 0.1733 0.2288 -0.0168 0.0010  0.0146  60  ALA   B CB  
4592 N  N   . MET   B 61  ? 0.1435 0.1581 0.1804 -0.0063 -0.0017 0.0071  61  MET   B N   
4593 C  CA  . MET   B 61  ? 0.1393 0.1494 0.1775 -0.0079 -0.0111 0.0013  61  MET   B CA  
4594 C  C   . MET   B 61  ? 0.1492 0.1472 0.1783 -0.0094 -0.0126 0.0102  61  MET   B C   
4595 O  O   . MET   B 61  ? 0.1509 0.1464 0.1739 -0.0049 -0.0044 -0.0002 61  MET   B O   
4596 C  CB  . MET   B 61  ? 0.1378 0.1506 0.1758 0.0026  -0.0143 0.0043  61  MET   B CB  
4597 C  CG  . MET   B 61  ? 0.1391 0.1534 0.1627 -0.0064 -0.0085 0.0089  61  MET   B CG  
4598 S  SD  . MET   B 61  ? 0.1393 0.1520 0.1909 -0.0019 -0.0056 -0.0114 61  MET   B SD  
4599 C  CE  . MET   B 61  ? 0.1527 0.1721 0.1980 0.0025  0.0008  -0.0181 61  MET   B CE  
4609 N  N   . GLN   B 62  ? 0.1526 0.1523 0.1668 -0.0022 -0.0230 0.0109  62  GLN   B N   
4610 C  CA  . GLN   B 62  ? 0.1482 0.1571 0.1808 -0.0006 -0.0140 -0.0008 62  GLN   B CA  
4611 C  C   . GLN   B 62  ? 0.1464 0.1655 0.1861 -0.0051 -0.0193 -0.0058 62  GLN   B C   
4612 O  O   . GLN   B 62  ? 0.1614 0.1641 0.1876 -0.0034 -0.0273 -0.0189 62  GLN   B O   
4613 C  CB  . GLN   B 62  ? 0.1508 0.1601 0.1762 0.0020  -0.0139 0.0020  62  GLN   B CB  
4614 C  CG  . GLN   B 62  ? 0.1494 0.1717 0.1833 -0.0010 -0.0230 -0.0071 62  GLN   B CG  
4615 C  CD  . GLN   B 62  ? 0.1523 0.1662 0.1774 0.0080  -0.0258 0.0009  62  GLN   B CD  
4616 O  OE1 . GLN   B 62  ? 0.1575 0.1612 0.1903 0.0043  -0.0218 -0.0117 62  GLN   B OE1 
4617 N  NE2 . GLN   B 62  ? 0.1562 0.1675 0.1921 0.0053  -0.0221 -0.0163 62  GLN   B NE2 
4626 N  N   . VAL   B 63  ? 0.1446 0.1676 0.2041 -0.0110 -0.0239 -0.0134 63  VAL   B N   
4627 C  CA  . VAL   B 63  ? 0.1575 0.1688 0.2210 -0.0112 -0.0310 -0.0059 63  VAL   B CA  
4628 C  C   . VAL   B 63  ? 0.1588 0.1561 0.2042 -0.0171 -0.0317 -0.0097 63  VAL   B C   
4629 O  O   . VAL   B 63  ? 0.1715 0.1551 0.2185 -0.0097 -0.0449 -0.0083 63  VAL   B O   
4630 C  CB  . VAL   B 63  ? 0.1625 0.1823 0.2546 -0.0197 -0.0328 -0.0069 63  VAL   B CB  
4631 C  CG1 . VAL   B 63  ? 0.1728 0.1874 0.2676 -0.0305 -0.0272 -0.0067 63  VAL   B CG1 
4632 C  CG2 . VAL   B 63  ? 0.1560 0.2015 0.2743 -0.0122 -0.0319 -0.0069 63  VAL   B CG2 
4642 N  N   . GLU   B 64  ? 0.1599 0.1490 0.1997 -0.0120 -0.0292 -0.0195 64  GLU   B N   
4643 C  CA  . GLU   B 64  ? 0.1606 0.1434 0.1951 -0.0083 -0.0354 -0.0076 64  GLU   B CA  
4644 C  C   . GLU   B 64  ? 0.1524 0.1416 0.1891 -0.0056 -0.0306 -0.0121 64  GLU   B C   
4645 O  O   . GLU   B 64  ? 0.1622 0.1527 0.1946 -0.0089 -0.0312 -0.0122 64  GLU   B O   
4646 C  CB  . GLU   B 64  ? 0.1621 0.1530 0.1877 -0.0148 -0.0273 0.0019  64  GLU   B CB  
4647 C  CG  . GLU   B 64  ? 0.1649 0.1524 0.1938 -0.0221 -0.0298 -0.0042 64  GLU   B CG  
4648 C  CD  . GLU   B 64  ? 0.1638 0.1631 0.1995 -0.0288 -0.0257 -0.0067 64  GLU   B CD  
4649 O  OE1 . GLU   B 64  ? 0.1698 0.1801 0.1989 -0.0320 -0.0241 -0.0228 64  GLU   B OE1 
4650 O  OE2 . GLU   B 64  ? 0.1789 0.1721 0.2031 -0.0337 -0.0383 -0.0069 64  GLU   B OE2 
4657 N  N   . SER   B 65  ? 0.1545 0.1398 0.1762 -0.0076 -0.0144 -0.0183 65  SER   B N   
4658 C  CA  . SER   B 65  ? 0.1550 0.1438 0.1773 -0.0053 -0.0212 -0.0143 65  SER   B CA  
4659 C  C   . SER   B 65  ? 0.1572 0.1504 0.1692 -0.0086 -0.0229 -0.0140 65  SER   B C   
4660 O  O   . SER   B 65  ? 0.1625 0.1544 0.1796 -0.0091 -0.0240 -0.0209 65  SER   B O   
4661 C  CB  . SER   B 65  ? 0.1559 0.1479 0.1742 -0.0122 -0.0194 -0.0144 65  SER   B CB  
4662 O  OG  . SER   B 65  ? 0.1585 0.1490 0.1786 -0.0103 -0.0127 -0.0194 65  SER   B OG  
4668 N  N   . ASP   B 66  ? 0.1636 0.1547 0.1657 -0.0031 -0.0280 -0.0154 66  ASP   B N   
4669 C  CA  . ASP   B 66  ? 0.1708 0.1622 0.1650 0.0027  -0.0294 -0.0154 66  ASP   B CA  
4670 C  C   . ASP   B 66  ? 0.1767 0.1679 0.1766 -0.0061 -0.0250 -0.0197 66  ASP   B C   
4671 O  O   . ASP   B 66  ? 0.1770 0.1719 0.1868 0.0018  -0.0279 -0.0270 66  ASP   B O   
4672 C  CB  . ASP   B 66  ? 0.1861 0.1742 0.1851 0.0113  -0.0425 -0.0129 66  ASP   B CB  
4673 C  CG  . ASP   B 66  ? 0.2163 0.1879 0.2123 0.0202  -0.0602 -0.0004 66  ASP   B CG  
4674 O  OD1 . ASP   B 66  ? 0.2377 0.1827 0.2221 0.0122  -0.0570 0.0052  66  ASP   B OD1 
4675 O  OD2 . ASP   B 66  ? 0.2349 0.2108 0.2660 0.0407  -0.0618 0.0006  66  ASP   B OD2 
4680 N  N   . ASP   B 67  ? 0.1708 0.1572 0.1710 -0.0086 -0.0235 -0.0204 67  ASP   B N   
4681 C  CA  . ASP   B 67  ? 0.1835 0.1514 0.1802 -0.0118 -0.0237 -0.0122 67  ASP   B CA  
4682 C  C   . ASP   B 67  ? 0.1821 0.1517 0.1958 -0.0010 -0.0232 -0.0212 67  ASP   B C   
4683 O  O   . ASP   B 67  ? 0.1857 0.1572 0.1986 0.0002  -0.0160 -0.0232 67  ASP   B O   
4684 C  CB  . ASP   B 67  ? 0.2039 0.1629 0.1937 -0.0142 -0.0403 -0.0114 67  ASP   B CB  
4685 C  CG  . ASP   B 67  ? 0.2389 0.1702 0.2003 -0.0110 -0.0611 -0.0106 67  ASP   B CG  
4686 O  OD1 . ASP   B 67  ? 0.2571 0.1790 0.2203 -0.0113 -0.0629 -0.0068 67  ASP   B OD1 
4687 O  OD2 . ASP   B 67  ? 0.2571 0.1723 0.2144 0.0023  -0.0640 -0.0067 67  ASP   B OD2 
4692 N  N   . TYR   B 68  ? 0.1736 0.1530 0.1855 0.0045  -0.0389 -0.0243 68  TYR   B N   
4693 C  CA  . TYR   B 68  ? 0.1713 0.1689 0.1966 0.0041  -0.0368 -0.0314 68  TYR   B CA  
4694 C  C   . TYR   B 68  ? 0.1648 0.1641 0.1844 -0.0028 -0.0334 -0.0388 68  TYR   B C   
4695 O  O   . TYR   B 68  ? 0.1735 0.1730 0.1900 0.0044  -0.0303 -0.0531 68  TYR   B O   
4696 C  CB  . TYR   B 68  ? 0.1774 0.1923 0.1964 0.0049  -0.0438 -0.0414 68  TYR   B CB  
4697 C  CG  . TYR   B 68  ? 0.1917 0.2034 0.2054 0.0106  -0.0362 -0.0559 68  TYR   B CG  
4698 C  CD1 . TYR   B 68  ? 0.1916 0.2034 0.2298 -0.0095 -0.0382 -0.0702 68  TYR   B CD1 
4699 C  CD2 . TYR   B 68  ? 0.1946 0.2228 0.2095 0.0185  -0.0426 -0.0519 68  TYR   B CD2 
4700 C  CE1 . TYR   B 68  ? 0.1977 0.2229 0.2481 -0.0071 -0.0328 -0.0609 68  TYR   B CE1 
4701 C  CE2 . TYR   B 68  ? 0.1944 0.2268 0.2218 0.0135  -0.0350 -0.0580 68  TYR   B CE2 
4702 C  CZ  . TYR   B 68  ? 0.1869 0.2296 0.2436 0.0016  -0.0346 -0.0586 68  TYR   B CZ  
4703 O  OH  . TYR   B 68  ? 0.1804 0.2469 0.2695 0.0008  -0.0292 -0.0449 68  TYR   B OH  
4713 N  N   . ILE   B 69  ? 0.1633 0.1555 0.1950 -0.0016 -0.0297 -0.0311 69  ILE   B N   
4714 C  CA  . ILE   B 69  ? 0.1682 0.1614 0.2044 -0.0057 -0.0265 -0.0326 69  ILE   B CA  
4715 C  C   . ILE   B 69  ? 0.1681 0.1609 0.1956 0.0053  -0.0407 -0.0246 69  ILE   B C   
4716 O  O   . ILE   B 69  ? 0.1754 0.1682 0.1950 0.0052  -0.0268 -0.0273 69  ILE   B O   
4717 C  CB  . ILE   B 69  ? 0.1789 0.1692 0.2141 -0.0074 -0.0006 -0.0286 69  ILE   B CB  
4718 C  CG1 . ILE   B 69  ? 0.1835 0.1731 0.2205 -0.0087 0.0074  -0.0315 69  ILE   B CG1 
4719 C  CG2 . ILE   B 69  ? 0.1956 0.1806 0.2288 -0.0044 -0.0071 -0.0209 69  ILE   B CG2 
4720 C  CD1 . ILE   B 69  ? 0.1783 0.1789 0.2265 -0.0167 0.0077  -0.0324 69  ILE   B CD1 
4732 N  N   . ALA   B 70  ? 0.1684 0.1622 0.1945 0.0092  -0.0426 -0.0287 70  ALA   B N   
4733 C  CA  . ALA   B 70  ? 0.1761 0.1686 0.1830 0.0038  -0.0415 -0.0306 70  ALA   B CA  
4734 C  C   . ALA   B 70  ? 0.1817 0.1658 0.1900 0.0013  -0.0462 -0.0321 70  ALA   B C   
4735 O  O   . ALA   B 70  ? 0.1923 0.1628 0.1988 0.0022  -0.0374 -0.0296 70  ALA   B O   
4736 C  CB  . ALA   B 70  ? 0.1788 0.1845 0.1876 0.0003  -0.0478 -0.0289 70  ALA   B CB  
4742 N  N   . THR   B 71  ? 0.1894 0.1664 0.2018 0.0025  -0.0552 -0.0396 71  THR   B N   
4743 C  CA  . THR   B 71  ? 0.2009 0.1649 0.2210 0.0085  -0.0628 -0.0398 71  THR   B CA  
4744 C  C   . THR   B 71  ? 0.1980 0.1709 0.2426 0.0246  -0.0553 -0.0580 71  THR   B C   
4745 O  O   . THR   B 71  ? 0.2076 0.1815 0.2746 0.0242  -0.0521 -0.0679 71  THR   B O   
4746 C  CB  . THR   B 71  ? 0.2255 0.1880 0.2396 -0.0005 -0.0695 -0.0147 71  THR   B CB  
4747 O  OG1 . THR   B 71  ? 0.2413 0.2086 0.2664 -0.0182 -0.0740 0.0192  71  THR   B OG1 
4748 C  CG2 . THR   B 71  ? 0.2435 0.1878 0.2585 0.0035  -0.0572 -0.0099 71  THR   B CG2 
4756 N  N   . ASN   B 72  ? 0.1839 0.1765 0.2364 0.0154  -0.0616 -0.0673 72  ASN   B N   
4757 C  CA  . ASN   B 72  ? 0.1862 0.1900 0.2281 0.0195  -0.0488 -0.0679 72  ASN   B CA  
4758 C  C   . ASN   B 72  ? 0.1886 0.1997 0.2308 0.0083  -0.0230 -0.0637 72  ASN   B C   
4759 O  O   . ASN   B 72  ? 0.1911 0.2116 0.2471 0.0102  -0.0097 -0.0652 72  ASN   B O   
4760 C  CB  . ASN   B 72  ? 0.1953 0.2073 0.2393 0.0189  -0.0622 -0.0582 72  ASN   B CB  
4761 C  CG  . ASN   B 72  ? 0.2095 0.2185 0.2493 0.0351  -0.0672 -0.0373 72  ASN   B CG  
4762 O  OD1 . ASN   B 72  ? 0.2298 0.2341 0.2559 0.0202  -0.0501 -0.0491 72  ASN   B OD1 
4763 N  ND2 . ASN   B 72  ? 0.2227 0.2240 0.2870 0.0511  -0.0495 -0.0024 72  ASN   B ND2 
4770 N  N   . GLY   B 73  ? 0.1892 0.1974 0.2068 0.0041  -0.0231 -0.0584 73  GLY   B N   
4771 C  CA  . GLY   B 73  ? 0.1839 0.2042 0.1830 -0.0026 -0.0204 -0.0455 73  GLY   B CA  
4772 C  C   . GLY   B 73  ? 0.1781 0.2020 0.1481 0.0053  -0.0157 -0.0442 73  GLY   B C   
4773 O  O   . GLY   B 73  ? 0.1742 0.1892 0.1654 0.0029  -0.0160 -0.0321 73  GLY   B O   
4777 N  N   . PRO   B 74  ? 0.1776 0.2113 0.1534 0.0031  -0.0182 -0.0343 74  PRO   B N   
4778 C  CA  . PRO   B 74  ? 0.1733 0.2108 0.1466 0.0084  -0.0222 -0.0222 74  PRO   B CA  
4779 C  C   . PRO   B 74  ? 0.1584 0.2024 0.1488 0.0060  -0.0162 -0.0165 74  PRO   B C   
4780 O  O   . PRO   B 74  ? 0.1657 0.2056 0.1821 0.0070  -0.0163 -0.0335 74  PRO   B O   
4781 C  CB  . PRO   B 74  ? 0.1898 0.2275 0.1608 0.0041  -0.0234 -0.0179 74  PRO   B CB  
4782 C  CG  . PRO   B 74  ? 0.2065 0.2366 0.1871 0.0061  -0.0168 -0.0145 74  PRO   B CG  
4783 C  CD  . PRO   B 74  ? 0.2037 0.2243 0.1746 0.0087  -0.0095 -0.0302 74  PRO   B CD  
4791 N  N   . LEU   B 75  ? 0.1534 0.1920 0.1495 0.0113  -0.0160 -0.0236 75  LEU   B N   
4792 C  CA  . LEU   B 75  ? 0.1597 0.1921 0.1531 0.0044  -0.0059 -0.0065 75  LEU   B CA  
4793 C  C   . LEU   B 75  ? 0.1670 0.1979 0.1476 0.0021  -0.0048 -0.0079 75  LEU   B C   
4794 O  O   . LEU   B 75  ? 0.1837 0.2034 0.1572 -0.0023 -0.0048 -0.0035 75  LEU   B O   
4795 C  CB  . LEU   B 75  ? 0.1657 0.1933 0.1429 -0.0036 -0.0082 0.0089  75  LEU   B CB  
4796 C  CG  . LEU   B 75  ? 0.1991 0.2072 0.1583 -0.0275 -0.0027 -0.0012 75  LEU   B CG  
4797 C  CD1 . LEU   B 75  ? 0.2317 0.2213 0.1682 -0.0395 0.0100  -0.0067 75  LEU   B CD1 
4798 C  CD2 . LEU   B 75  ? 0.2365 0.2262 0.2184 -0.0236 0.0063  0.0116  75  LEU   B CD2 
4810 N  N   . LYS   B 76  ? 0.1625 0.2122 0.1804 -0.0000 0.0004  -0.0022 76  LYS   B N   
4811 C  CA  . LYS   B 76  ? 0.1773 0.2235 0.2056 -0.0053 0.0131  -0.0040 76  LYS   B CA  
4812 C  C   . LYS   B 76  ? 0.1710 0.2060 0.1650 0.0048  0.0006  0.0128  76  LYS   B C   
4813 O  O   . LYS   B 76  ? 0.1687 0.1916 0.1665 0.0045  -0.0002 0.0084  76  LYS   B O   
4814 C  CB  . LYS   B 76  ? 0.1927 0.2363 0.2716 -0.0108 0.0398  -0.0399 76  LYS   B CB  
4815 C  CG  . LYS   B 76  ? 0.2034 0.2579 0.3272 -0.0025 0.0291  -0.0466 76  LYS   B CG  
4816 C  CD  . LYS   B 76  ? 0.2046 0.2688 0.3701 0.0048  0.0159  -0.0610 76  LYS   B CD  
4817 C  CE  . LYS   B 76  ? 0.2117 0.2847 0.4184 0.0061  -0.0004 -0.0712 76  LYS   B CE  
4818 N  NZ  . LYS   B 76  ? 0.2111 0.2880 0.4321 0.0034  -0.0192 -0.0924 76  LYS   B NZ  
4832 N  N   . VAL   B 77  ? 0.1803 0.2144 0.1629 0.0180  0.0068  0.0178  77  VAL   B N   
4833 C  CA  . VAL   B 77  ? 0.1783 0.2058 0.1694 0.0221  0.0133  0.0319  77  VAL   B CA  
4834 C  C   . VAL   B 77  ? 0.1612 0.1897 0.1670 0.0191  0.0051  0.0290  77  VAL   B C   
4835 O  O   . VAL   B 77  ? 0.1620 0.1802 0.1731 0.0246  0.0174  0.0214  77  VAL   B O   
4836 C  CB  . VAL   B 77  ? 0.1869 0.2133 0.1983 0.0233  0.0336  0.0507  77  VAL   B CB  
4837 C  CG1 . VAL   B 77  ? 0.1948 0.2026 0.2277 0.0134  0.0399  0.0660  77  VAL   B CG1 
4838 C  CG2 . VAL   B 77  ? 0.2043 0.2339 0.2302 0.0217  0.0183  0.0569  77  VAL   B CG2 
4848 N  N   . GLY   B 78  ? 0.1569 0.1769 0.1648 0.0110  0.0033  0.0179  78  GLY   B N   
4849 C  CA  . GLY   B 78  ? 0.1541 0.1704 0.1629 0.0070  0.0195  0.0099  78  GLY   B CA  
4850 C  C   . GLY   B 78  ? 0.1501 0.1623 0.1548 0.0104  0.0165  0.0155  78  GLY   B C   
4851 O  O   . GLY   B 78  ? 0.1545 0.1594 0.1757 0.0151  0.0162  0.0214  78  GLY   B O   
4855 N  N   . GLY   B 79  ? 0.1456 0.1672 0.1639 0.0081  0.0148  0.0103  79  GLY   B N   
4856 C  CA  . GLY   B 79  ? 0.1482 0.1583 0.1613 0.0102  0.0054  0.0078  79  GLY   B CA  
4857 C  C   . GLY   B 79  ? 0.1376 0.1483 0.1623 0.0139  0.0124  0.0006  79  GLY   B C   
4858 O  O   . GLY   B 79  ? 0.1470 0.1488 0.1704 0.0130  0.0201  0.0132  79  GLY   B O   
4862 N  N   . SER   B 80  ? 0.1379 0.1405 0.1706 0.0100  0.0154  -0.0019 80  SER   B N   
4863 C  CA  . SER   B 80  ? 0.1344 0.1354 0.1746 0.0040  -0.0006 0.0051  80  SER   B CA  
4864 C  C   . SER   B 80  ? 0.1380 0.1386 0.1711 0.0077  -0.0094 -0.0010 80  SER   B C   
4865 O  O   . SER   B 80  ? 0.1509 0.1368 0.1944 0.0095  0.0000  -0.0060 80  SER   B O   
4866 C  CB  . SER   B 80  ? 0.1408 0.1461 0.1759 -0.0048 -0.0023 0.0058  80  SER   B CB  
4867 O  OG  . SER   B 80  ? 0.1475 0.1559 0.1885 0.0035  -0.0168 0.0124  80  SER   B OG  
4873 N  N   . CYS   B 81  ? 0.1341 0.1253 0.1726 0.0014  -0.0077 -0.0025 81  CYS   B N   
4874 C  CA  . CYS   B 81  ? 0.1405 0.1238 0.1687 0.0020  -0.0142 -0.0051 81  CYS   B CA  
4875 C  C   . CYS   B 81  ? 0.1388 0.1256 0.1483 -0.0005 -0.0152 -0.0059 81  CYS   B C   
4876 O  O   . CYS   B 81  ? 0.1628 0.1292 0.1651 0.0064  -0.0107 -0.0091 81  CYS   B O   
4877 C  CB  . CYS   B 81  ? 0.1557 0.1422 0.1837 -0.0044 -0.0104 0.0001  81  CYS   B CB  
4878 S  SG  . CYS   B 81  ? 0.1596 0.1577 0.1627 -0.0025 -0.0250 -0.0114 81  CYS   B SG  
4884 N  N   . VAL   B 82  ? 0.1452 0.1243 0.1566 -0.0005 -0.0144 -0.0022 82  VAL   B N   
4885 C  CA  . VAL   B 82  ? 0.1469 0.1270 0.1606 -0.0042 -0.0107 0.0072  82  VAL   B CA  
4886 C  C   . VAL   B 82  ? 0.1579 0.1238 0.1659 0.0003  -0.0091 -0.0028 82  VAL   B C   
4887 O  O   . VAL   B 82  ? 0.1651 0.1220 0.1901 -0.0026 -0.0101 -0.0148 82  VAL   B O   
4888 C  CB  . VAL   B 82  ? 0.1573 0.1470 0.1771 -0.0037 -0.0186 0.0134  82  VAL   B CB  
4889 C  CG1 . VAL   B 82  ? 0.1787 0.1671 0.1846 -0.0001 -0.0155 0.0142  82  VAL   B CG1 
4890 C  CG2 . VAL   B 82  ? 0.1673 0.1641 0.2018 -0.0063 -0.0322 0.0121  82  VAL   B CG2 
4900 N  N   . LEU   B 83  ? 0.1450 0.1206 0.1631 -0.0086 -0.0232 -0.0081 83  LEU   B N   
4901 C  CA  . LEU   B 83  ? 0.1471 0.1249 0.1589 -0.0123 -0.0224 0.0012  83  LEU   B CA  
4902 C  C   . LEU   B 83  ? 0.1465 0.1214 0.1641 -0.0181 -0.0168 0.0008  83  LEU   B C   
4903 O  O   . LEU   B 83  ? 0.1451 0.1313 0.1525 -0.0200 -0.0146 0.0052  83  LEU   B O   
4904 C  CB  . LEU   B 83  ? 0.1542 0.1389 0.1698 -0.0137 -0.0295 -0.0110 83  LEU   B CB  
4905 C  CG  . LEU   B 83  ? 0.1699 0.1601 0.1725 -0.0149 -0.0106 -0.0094 83  LEU   B CG  
4906 C  CD1 . LEU   B 83  ? 0.1796 0.1685 0.1721 -0.0102 -0.0152 -0.0054 83  LEU   B CD1 
4907 C  CD2 . LEU   B 83  ? 0.1840 0.1615 0.1896 -0.0100 -0.0086 -0.0218 83  LEU   B CD2 
4919 N  N   . SER   B 84  ? 0.1477 0.1337 0.1839 -0.0198 -0.0145 -0.0047 84  SER   B N   
4920 C  CA  . SER   B 84  ? 0.1523 0.1514 0.1759 -0.0242 -0.0097 0.0128  84  SER   B CA  
4921 C  C   . SER   B 84  ? 0.1420 0.1699 0.1386 -0.0184 -0.0127 0.0205  84  SER   B C   
4922 O  O   . SER   B 84  ? 0.1516 0.1553 0.1394 -0.0198 -0.0119 -0.0015 84  SER   B O   
4923 C  CB  . SER   B 84  ? 0.1684 0.1575 0.2200 -0.0213 0.0124  0.0173  84  SER   B CB  
4924 O  OG  . SER   B 84  ? 0.1667 0.1770 0.2657 -0.0301 0.0146  0.0211  84  SER   B OG  
4930 N  N   . GLY   B 85  ? 0.1501 0.1909 0.1521 -0.0243 -0.0130 0.0229  85  GLY   B N   
4931 C  CA  . GLY   B 85  ? 0.1527 0.1966 0.1624 -0.0325 -0.0042 0.0018  85  GLY   B CA  
4932 C  C   . GLY   B 85  ? 0.1464 0.1806 0.1585 -0.0397 -0.0029 0.0089  85  GLY   B C   
4933 O  O   . GLY   B 85  ? 0.1596 0.1847 0.1575 -0.0565 0.0163  -0.0065 85  GLY   B O   
4937 N  N   . HIS   B 86  ? 0.1445 0.1645 0.1810 -0.0314 -0.0178 0.0143  86  HIS   B N   
4938 C  CA  . HIS   B 86  ? 0.1472 0.1600 0.1753 -0.0261 -0.0134 0.0220  86  HIS   B CA  
4939 C  C   . HIS   B 86  ? 0.1511 0.1763 0.1682 -0.0379 -0.0116 0.0300  86  HIS   B C   
4940 O  O   . HIS   B 86  ? 0.1611 0.1829 0.1739 -0.0279 0.0038  0.0323  86  HIS   B O   
4941 C  CB  . HIS   B 86  ? 0.1594 0.1611 0.1787 -0.0174 -0.0240 0.0113  86  HIS   B CB  
4942 C  CG  . HIS   B 86  ? 0.1567 0.1670 0.1695 -0.0107 -0.0261 0.0091  86  HIS   B CG  
4943 N  ND1 . HIS   B 86  ? 0.1653 0.1914 0.1840 -0.0226 -0.0271 -0.0047 86  HIS   B ND1 
4944 C  CD2 . HIS   B 86  ? 0.1606 0.1714 0.1711 -0.0139 -0.0260 0.0123  86  HIS   B CD2 
4945 C  CE1 . HIS   B 86  ? 0.1747 0.1889 0.1782 -0.0146 -0.0135 -0.0200 86  HIS   B CE1 
4946 N  NE2 . HIS   B 86  ? 0.1698 0.1766 0.1675 -0.0041 -0.0197 -0.0017 86  HIS   B NE2 
4954 N  N   . ASN   B 87  ? 0.1497 0.1800 0.1638 -0.0329 -0.0090 0.0311  87  ASN   B N   
4955 C  CA  . ASN   B 87  ? 0.1567 0.1980 0.1822 -0.0293 0.0204  0.0166  87  ASN   B CA  
4956 C  C   . ASN   B 87  ? 0.1691 0.1773 0.1679 -0.0309 0.0265  0.0131  87  ASN   B C   
4957 O  O   . ASN   B 87  ? 0.1931 0.1872 0.2020 -0.0237 0.0442  0.0051  87  ASN   B O   
4958 C  CB  . ASN   B 87  ? 0.1562 0.2276 0.2122 -0.0251 0.0199  0.0050  87  ASN   B CB  
4959 C  CG  . ASN   B 87  ? 0.1648 0.2485 0.2235 0.0067  0.0301  0.0245  87  ASN   B CG  
4960 O  OD1 . ASN   B 87  ? 0.1550 0.2360 0.2107 0.0094  0.0432  0.0456  87  ASN   B OD1 
4961 N  ND2 . ASN   B 87  ? 0.2045 0.2628 0.2579 0.0097  0.0388  0.0201  87  ASN   B ND2 
4968 N  N   . LEU   B 88  ? 0.1574 0.1699 0.1566 -0.0346 0.0132  0.0113  88  LEU   B N   
4969 C  CA  . LEU   B 88  ? 0.1739 0.1631 0.1541 -0.0305 0.0020  0.0038  88  LEU   B CA  
4970 C  C   . LEU   B 88  ? 0.1747 0.1531 0.1530 -0.0373 -0.0040 0.0001  88  LEU   B C   
4971 O  O   . LEU   B 88  ? 0.2004 0.1620 0.1828 -0.0237 -0.0310 -0.0121 88  LEU   B O   
4972 C  CB  . LEU   B 88  ? 0.1829 0.1690 0.1728 -0.0385 -0.0074 0.0135  88  LEU   B CB  
4973 C  CG  . LEU   B 88  ? 0.2220 0.2024 0.1874 -0.0344 -0.0287 0.0366  88  LEU   B CG  
4974 C  CD1 . LEU   B 88  ? 0.2304 0.2334 0.1975 -0.0428 -0.0240 0.0437  88  LEU   B CD1 
4975 C  CD2 . LEU   B 88  ? 0.2537 0.2298 0.2423 -0.0005 -0.0504 0.0154  88  LEU   B CD2 
4987 N  N   . ALA   B 89  ? 0.1632 0.1512 0.1510 -0.0369 0.0206  0.0011  89  ALA   B N   
4988 C  CA  . ALA   B 89  ? 0.1564 0.1470 0.1417 -0.0344 0.0065  0.0131  89  ALA   B CA  
4989 C  C   . ALA   B 89  ? 0.1670 0.1539 0.1487 -0.0390 0.0139  0.0091  89  ALA   B C   
4990 O  O   . ALA   B 89  ? 0.1521 0.1618 0.1777 -0.0394 0.0128  -0.0200 89  ALA   B O   
4991 C  CB  . ALA   B 89  ? 0.1479 0.1451 0.1608 -0.0328 0.0063  0.0164  89  ALA   B CB  
4997 N  N   . LYS   B 90  ? 0.2004 0.1445 0.1577 -0.0446 -0.0056 0.0076  90  LYS   B N   
4998 C  CA  . LYS   B 90  ? 0.2117 0.1371 0.1606 -0.0400 -0.0107 0.0071  90  LYS   B CA  
4999 C  C   . LYS   B 90  ? 0.1991 0.1278 0.1750 -0.0398 -0.0104 -0.0007 90  LYS   B C   
5000 O  O   . LYS   B 90  ? 0.2097 0.1539 0.1808 -0.0580 -0.0004 0.0009  90  LYS   B O   
5001 C  CB  . LYS   B 90  ? 0.2312 0.1446 0.1824 -0.0324 -0.0045 0.0174  90  LYS   B CB  
5002 C  CG  . LYS   B 90  ? 0.2316 0.1659 0.1845 -0.0199 0.0164  0.0125  90  LYS   B CG  
5003 C  CD  . LYS   B 90  ? 0.2524 0.1921 0.2312 -0.0123 0.0332  0.0014  90  LYS   B CD  
5004 C  CE  . LYS   B 90  ? 0.2644 0.2100 0.2754 -0.0171 0.0391  -0.0059 90  LYS   B CE  
5005 N  NZ  . LYS   B 90  ? 0.2662 0.2031 0.2640 -0.0307 0.0551  -0.0029 90  LYS   B NZ  
5019 N  N   . HIS   B 91  ? 0.1699 0.1242 0.1493 -0.0284 -0.0145 0.0082  91  HIS   B N   
5020 C  CA  . HIS   B 91  ? 0.1576 0.1278 0.1578 -0.0235 -0.0106 0.0040  91  HIS   B CA  
5021 C  C   . HIS   B 91  ? 0.1514 0.1308 0.1375 -0.0234 -0.0034 -0.0001 91  HIS   B C   
5022 O  O   . HIS   B 91  ? 0.1639 0.1342 0.1446 -0.0260 -0.0168 0.0036  91  HIS   B O   
5023 C  CB  . HIS   B 91  ? 0.1771 0.1277 0.1970 -0.0068 -0.0107 0.0112  91  HIS   B CB  
5024 C  CG  . HIS   B 91  ? 0.2174 0.1430 0.2565 0.0047  0.0169  0.0200  91  HIS   B CG  
5025 N  ND1 . HIS   B 91  ? 0.2488 0.1514 0.3164 0.0013  0.0241  0.0028  91  HIS   B ND1 
5026 C  CD2 . HIS   B 91  ? 0.2323 0.1720 0.2954 0.0193  0.0082  0.0537  91  HIS   B CD2 
5027 C  CE1 . HIS   B 91  ? 0.2523 0.1658 0.3293 0.0193  0.0253  0.0146  91  HIS   B CE1 
5028 N  NE2 . HIS   B 91  ? 0.2446 0.1791 0.3242 0.0314  0.0223  0.0585  91  HIS   B NE2 
5036 N  N   . CYS   B 92  ? 0.1450 0.1307 0.1390 -0.0223 -0.0126 0.0059  92  CYS   B N   
5037 C  CA  . CYS   B 92  ? 0.1440 0.1279 0.1312 -0.0159 -0.0099 -0.0022 92  CYS   B CA  
5038 C  C   . CYS   B 92  ? 0.1380 0.1217 0.1267 -0.0087 -0.0012 -0.0025 92  CYS   B C   
5039 O  O   . CYS   B 92  ? 0.1462 0.1284 0.1531 -0.0138 0.0014  -0.0006 92  CYS   B O   
5040 C  CB  . CYS   B 92  ? 0.1392 0.1332 0.1411 -0.0142 -0.0048 0.0043  92  CYS   B CB  
5041 S  SG  . CYS   B 92  ? 0.1396 0.1355 0.1461 -0.0109 -0.0102 0.0065  92  CYS   B SG  
5047 N  N   . LEU   B 93  ? 0.1262 0.1236 0.1397 -0.0131 -0.0034 -0.0045 93  LEU   B N   
5048 C  CA  . LEU   B 93  ? 0.1327 0.1262 0.1396 -0.0043 -0.0125 0.0008  93  LEU   B CA  
5049 C  C   . LEU   B 93  ? 0.1222 0.1247 0.1322 -0.0021 -0.0091 0.0055  93  LEU   B C   
5050 O  O   . LEU   B 93  ? 0.1304 0.1263 0.1510 -0.0020 -0.0070 0.0026  93  LEU   B O   
5051 C  CB  . LEU   B 93  ? 0.1344 0.1230 0.1528 0.0047  -0.0093 0.0039  93  LEU   B CB  
5052 C  CG  . LEU   B 93  ? 0.1340 0.1358 0.1683 -0.0006 0.0002  0.0138  93  LEU   B CG  
5053 C  CD1 . LEU   B 93  ? 0.1411 0.1481 0.1706 0.0046  -0.0048 0.0001  93  LEU   B CD1 
5054 C  CD2 . LEU   B 93  ? 0.1349 0.1367 0.1767 -0.0051 -0.0105 0.0052  93  LEU   B CD2 
5066 N  N   . HIS   B 94  ? 0.1293 0.1191 0.1317 -0.0086 -0.0165 0.0045  94  HIS   B N   
5067 C  CA  . HIS   B 94  ? 0.1344 0.1214 0.1356 -0.0011 -0.0078 0.0066  94  HIS   B CA  
5068 C  C   . HIS   B 94  ? 0.1304 0.1204 0.1502 -0.0008 -0.0026 0.0074  94  HIS   B C   
5069 O  O   . HIS   B 94  ? 0.1306 0.1310 0.1874 -0.0027 0.0114  -0.0031 94  HIS   B O   
5070 C  CB  . HIS   B 94  ? 0.1324 0.1292 0.1400 0.0028  -0.0061 0.0049  94  HIS   B CB  
5071 C  CG  . HIS   B 94  ? 0.1351 0.1261 0.1505 -0.0070 -0.0204 0.0041  94  HIS   B CG  
5072 N  ND1 . HIS   B 94  ? 0.1366 0.1285 0.1500 -0.0081 -0.0252 -0.0001 94  HIS   B ND1 
5073 C  CD2 . HIS   B 94  ? 0.1375 0.1282 0.1464 0.0014  -0.0130 0.0049  94  HIS   B CD2 
5074 C  CE1 . HIS   B 94  ? 0.1356 0.1358 0.1398 -0.0102 -0.0260 0.0007  94  HIS   B CE1 
5075 N  NE2 . HIS   B 94  ? 0.1340 0.1358 0.1423 -0.0140 -0.0192 0.0081  94  HIS   B NE2 
5083 N  N   . VAL   B 95  ? 0.1203 0.1228 0.1570 0.0042  0.0006  0.0035  95  VAL   B N   
5084 C  CA  . VAL   B 95  ? 0.1244 0.1262 0.1457 0.0044  0.0034  0.0115  95  VAL   B CA  
5085 C  C   . VAL   B 95  ? 0.1352 0.1277 0.1443 -0.0008 0.0108  0.0069  95  VAL   B C   
5086 O  O   . VAL   B 95  ? 0.1419 0.1244 0.1644 0.0053  0.0126  0.0175  95  VAL   B O   
5087 C  CB  . VAL   B 95  ? 0.1359 0.1259 0.1540 -0.0016 -0.0071 -0.0008 95  VAL   B CB  
5088 C  CG1 . VAL   B 95  ? 0.1453 0.1414 0.1773 -0.0086 -0.0087 0.0051  95  VAL   B CG1 
5089 C  CG2 . VAL   B 95  ? 0.1461 0.1222 0.1567 -0.0001 -0.0084 0.0063  95  VAL   B CG2 
5099 N  N   . VAL   B 96  ? 0.1426 0.1360 0.1403 0.0109  0.0126  0.0176  96  VAL   B N   
5100 C  CA  . VAL   B 96  ? 0.1508 0.1452 0.1404 0.0084  0.0105  0.0188  96  VAL   B CA  
5101 C  C   . VAL   B 96  ? 0.1515 0.1495 0.1485 0.0085  0.0151  0.0167  96  VAL   B C   
5102 O  O   . VAL   B 96  ? 0.1521 0.1524 0.1748 0.0025  0.0182  -0.0007 96  VAL   B O   
5103 C  CB  . VAL   B 96  ? 0.1549 0.1652 0.1445 0.0100  0.0090  0.0062  96  VAL   B CB  
5104 C  CG1 . VAL   B 96  ? 0.1534 0.1808 0.1544 0.0210  0.0088  0.0064  96  VAL   B CG1 
5105 C  CG2 . VAL   B 96  ? 0.1671 0.1717 0.1551 0.0026  0.0102  -0.0014 96  VAL   B CG2 
5115 N  N   . GLY   B 97  ? 0.1601 0.1476 0.1475 0.0065  0.0099  0.0181  97  GLY   B N   
5116 C  CA  . GLY   B 97  ? 0.1725 0.1549 0.1479 -0.0016 0.0180  0.0167  97  GLY   B CA  
5117 C  C   . GLY   B 97  ? 0.1876 0.1586 0.1615 0.0087  0.0018  0.0135  97  GLY   B C   
5118 O  O   . GLY   B 97  ? 0.2003 0.1637 0.1680 0.0071  -0.0024 0.0125  97  GLY   B O   
5122 N  N   . PRO   B 98  ? 0.1966 0.1650 0.1792 0.0105  0.0218  0.0304  98  PRO   B N   
5123 C  CA  . PRO   B 98  ? 0.2061 0.1723 0.1849 0.0189  0.0365  0.0294  98  PRO   B CA  
5124 C  C   . PRO   B 98  ? 0.2192 0.1756 0.1631 0.0303  0.0337  0.0396  98  PRO   B C   
5125 O  O   . PRO   B 98  ? 0.2107 0.1687 0.1717 0.0238  0.0336  0.0362  98  PRO   B O   
5126 C  CB  . PRO   B 98  ? 0.1935 0.1785 0.1929 0.0137  0.0498  0.0242  98  PRO   B CB  
5127 C  CG  . PRO   B 98  ? 0.1878 0.1703 0.1909 0.0080  0.0382  0.0348  98  PRO   B CG  
5128 C  CD  . PRO   B 98  ? 0.1788 0.1619 0.1915 0.0135  0.0285  0.0326  98  PRO   B CD  
5136 N  N   . ASN   B 99  ? 0.2301 0.1893 0.1825 0.0442  0.0367  0.0257  99  ASN   B N   
5137 C  CA  . ASN   B 99  ? 0.2492 0.1988 0.1852 0.0532  0.0304  0.0439  99  ASN   B CA  
5138 C  C   . ASN   B 99  ? 0.2729 0.2335 0.2002 0.0473  0.0484  0.0712  99  ASN   B C   
5139 O  O   . ASN   B 99  ? 0.2846 0.2438 0.2035 0.0482  0.0375  0.0735  99  ASN   B O   
5140 C  CB  . ASN   B 99  ? 0.2540 0.1977 0.1854 0.0532  0.0258  0.0442  99  ASN   B CB  
5141 C  CG  . ASN   B 99  ? 0.2578 0.2055 0.2041 0.0449  0.0175  0.0439  99  ASN   B CG  
5142 O  OD1 . ASN   B 99  ? 0.2615 0.2087 0.2333 0.0480  0.0105  0.0510  99  ASN   B OD1 
5143 N  ND2 . ASN   B 99  ? 0.2584 0.2046 0.2081 0.0488  -0.0054 0.0343  99  ASN   B ND2 
5150 N  N   A VAL   B 100 ? 0.2849 0.2490 0.2439 0.0329  0.0515  0.0869  100 VAL   B N   
5151 N  N   B VAL   B 100 ? 0.2931 0.2483 0.2356 0.0408  0.0411  0.0807  100 VAL   B N   
5152 C  CA  A VAL   B 100 ? 0.3108 0.2646 0.2980 0.0223  0.0539  0.0971  100 VAL   B CA  
5153 C  CA  B VAL   B 100 ? 0.3163 0.2616 0.2736 0.0350  0.0331  0.0874  100 VAL   B CA  
5154 C  C   A VAL   B 100 ? 0.3318 0.2689 0.2872 0.0317  0.0515  0.1102  100 VAL   B C   
5155 C  C   B VAL   B 100 ? 0.3335 0.2676 0.2790 0.0386  0.0321  0.1037  100 VAL   B C   
5156 O  O   A VAL   B 100 ? 0.3404 0.2809 0.2980 0.0283  0.0668  0.1007  100 VAL   B O   
5157 O  O   B VAL   B 100 ? 0.3364 0.2720 0.2810 0.0366  0.0342  0.1025  100 VAL   B O   
5158 C  CB  A VAL   B 100 ? 0.3190 0.2808 0.3652 -0.0034 0.0520  0.1016  100 VAL   B CB  
5159 C  CB  B VAL   B 100 ? 0.3230 0.2695 0.3038 0.0250  0.0263  0.0800  100 VAL   B CB  
5160 C  CG1 A VAL   B 100 ? 0.3237 0.2858 0.3884 -0.0064 0.0523  0.1045  100 VAL   B CG1 
5161 C  CG1 B VAL   B 100 ? 0.3255 0.2717 0.3139 0.0231  0.0242  0.0788  100 VAL   B CG1 
5162 C  CG2 A VAL   B 100 ? 0.3189 0.2845 0.3787 -0.0142 0.0577  0.1135  100 VAL   B CG2 
5163 C  CG2 B VAL   B 100 ? 0.3247 0.2719 0.3131 0.0210  0.0252  0.0792  100 VAL   B CG2 
5182 N  N   . ASN   B 101 ? 0.3472 0.2706 0.2831 0.0446  0.0318  0.1178  101 ASN   B N   
5183 C  CA  . ASN   B 101 ? 0.3873 0.2878 0.3043 0.0537  0.0151  0.1293  101 ASN   B CA  
5184 C  C   . ASN   B 101 ? 0.4282 0.3223 0.3087 0.0570  0.0070  0.1412  101 ASN   B C   
5185 O  O   . ASN   B 101 ? 0.4337 0.3359 0.3325 0.0606  0.0132  0.1192  101 ASN   B O   
5186 C  CB  . ASN   B 101 ? 0.3866 0.2774 0.3225 0.0499  0.0209  0.1137  101 ASN   B CB  
5187 C  CG  . ASN   B 101 ? 0.3851 0.2678 0.3234 0.0474  0.0270  0.1154  101 ASN   B CG  
5188 O  OD1 . ASN   B 101 ? 0.3903 0.2685 0.3494 0.0416  0.0399  0.1080  101 ASN   B OD1 
5189 N  ND2 . ASN   B 101 ? 0.3815 0.2659 0.3117 0.0463  0.0261  0.1074  101 ASN   B ND2 
5197 N  N   . LYS   B 102 ? 0.4609 0.3518 0.3290 0.0489  0.0098  0.1364  102 LYS   B N   
5198 C  CA  . LYS   B 102 ? 0.4911 0.3902 0.3546 0.0356  0.0209  0.1122  102 LYS   B CA  
5199 C  C   . LYS   B 102 ? 0.4877 0.3903 0.3383 0.0352  0.0330  0.1090  102 LYS   B C   
5200 O  O   . LYS   B 102 ? 0.4981 0.3959 0.3533 0.0356  0.0262  0.1009  102 LYS   B O   
5201 C  CB  . LYS   B 102 ? 0.5200 0.4263 0.4162 0.0256  0.0297  0.0777  102 LYS   B CB  
5202 C  CG  . LYS   B 102 ? 0.5439 0.4592 0.4773 0.0197  0.0391  0.0440  102 LYS   B CG  
5203 C  CD  . LYS   B 102 ? 0.5645 0.4859 0.5379 0.0152  0.0482  0.0181  102 LYS   B CD  
5204 C  CE  . LYS   B 102 ? 0.5795 0.5055 0.5859 0.0114  0.0529  -0.0005 102 LYS   B CE  
5205 N  NZ  . LYS   B 102 ? 0.5876 0.5161 0.6138 0.0097  0.0536  -0.0112 102 LYS   B NZ  
5219 N  N   . GLY   B 103 ? 0.4687 0.3812 0.3253 0.0318  0.0539  0.1062  103 GLY   B N   
5220 C  CA  . GLY   B 103 ? 0.4482 0.3721 0.3274 0.0310  0.0716  0.0866  103 GLY   B CA  
5221 C  C   . GLY   B 103 ? 0.4233 0.3573 0.3168 0.0259  0.0862  0.0682  103 GLY   B C   
5222 O  O   . GLY   B 103 ? 0.4294 0.3644 0.3253 0.0261  0.0887  0.0681  103 GLY   B O   
5226 N  N   A GLU   B 104 ? 0.4038 0.3342 0.2914 0.0245  0.1072  0.0537  104 GLU   B N   
5227 N  N   B GLU   B 104 ? 0.4108 0.3550 0.3203 0.0206  0.0692  0.0539  104 GLU   B N   
5228 C  CA  A GLU   B 104 ? 0.3836 0.3154 0.2628 0.0228  0.1182  0.0421  104 GLU   B CA  
5229 C  CA  B GLU   B 104 ? 0.3970 0.3523 0.3178 0.0151  0.0533  0.0383  104 GLU   B CA  
5230 C  C   A GLU   B 104 ? 0.3919 0.3181 0.2838 0.0107  0.1424  0.0345  104 GLU   B C   
5231 C  C   B GLU   B 104 ? 0.3903 0.3515 0.3272 0.0092  0.0517  0.0297  104 GLU   B C   
5232 O  O   A GLU   B 104 ? 0.3961 0.3210 0.3070 0.0049  0.1373  0.0234  104 GLU   B O   
5233 O  O   B GLU   B 104 ? 0.3910 0.3527 0.3318 0.0075  0.0514  0.0273  104 GLU   B O   
5234 C  CB  A GLU   B 104 ? 0.3619 0.2946 0.2373 0.0336  0.0898  0.0240  104 GLU   B CB  
5235 C  CB  B GLU   B 104 ? 0.3908 0.3494 0.3066 0.0152  0.0397  0.0287  104 GLU   B CB  
5236 C  CG  A GLU   B 104 ? 0.3456 0.2791 0.2173 0.0432  0.0498  -0.0069 104 GLU   B CG  
5237 C  CG  B GLU   B 104 ? 0.3858 0.3470 0.2966 0.0158  0.0265  0.0172  104 GLU   B CG  
5238 C  CD  A GLU   B 104 ? 0.3303 0.2664 0.2014 0.0482  0.0132  -0.0098 104 GLU   B CD  
5239 C  CD  B GLU   B 104 ? 0.3820 0.3448 0.2881 0.0159  0.0158  0.0095  104 GLU   B CD  
5240 O  OE1 A GLU   B 104 ? 0.3090 0.2506 0.1717 0.0526  0.0155  -0.0039 104 GLU   B OE1 
5241 O  OE1 B GLU   B 104 ? 0.3796 0.3429 0.2813 0.0158  0.0151  0.0086  104 GLU   B OE1 
5242 O  OE2 A GLU   B 104 ? 0.3366 0.2753 0.2194 0.0427  -0.0193 -0.0256 104 GLU   B OE2 
5243 O  OE2 B GLU   B 104 ? 0.3819 0.3456 0.2898 0.0158  0.0083  0.0036  104 GLU   B OE2 
5256 N  N   A ASP   B 105 ? 0.3912 0.3225 0.2882 -0.0001 0.1688  0.0466  105 ASP   B N   
5257 N  N   B ASP   B 105 ? 0.3823 0.3499 0.3308 0.0049  0.0506  0.0242  105 ASP   B N   
5258 C  CA  A ASP   B 105 ? 0.3944 0.3260 0.3145 -0.0087 0.1889  0.0388  105 ASP   B CA  
5259 C  CA  B ASP   B 105 ? 0.3749 0.3473 0.3382 0.0012  0.0486  0.0165  105 ASP   B CA  
5260 C  C   A ASP   B 105 ? 0.3786 0.2929 0.3001 -0.0148 0.1854  0.0304  105 ASP   B C   
5261 C  C   B ASP   B 105 ? 0.3659 0.3401 0.3249 -0.0005 0.0467  0.0091  105 ASP   B C   
5262 O  O   A ASP   B 105 ? 0.3637 0.2824 0.2870 -0.0162 0.1865  0.0258  105 ASP   B O   
5263 O  O   B ASP   B 105 ? 0.3652 0.3389 0.3172 -0.0005 0.0460  0.0079  105 ASP   B O   
5264 C  CB  A ASP   B 105 ? 0.4107 0.3569 0.3765 -0.0025 0.2023  0.0225  105 ASP   B CB  
5265 C  CB  B ASP   B 105 ? 0.3755 0.3511 0.3572 0.0007  0.0490  0.0146  105 ASP   B CB  
5266 C  CG  A ASP   B 105 ? 0.4223 0.3789 0.4331 -0.0004 0.2194  0.0106  105 ASP   B CG  
5267 C  CG  B ASP   B 105 ? 0.3762 0.3533 0.3766 -0.0006 0.0501  0.0144  105 ASP   B CG  
5268 O  OD1 A ASP   B 105 ? 0.4228 0.3846 0.4327 -0.0109 0.2334  0.0226  105 ASP   B OD1 
5269 O  OD1 B ASP   B 105 ? 0.3756 0.3541 0.3821 -0.0027 0.0500  0.0154  105 ASP   B OD1 
5270 O  OD2 A ASP   B 105 ? 0.4282 0.3909 0.4722 0.0066  0.2151  -0.0049 105 ASP   B OD2 
5271 O  OD2 B ASP   B 105 ? 0.3761 0.3544 0.3835 -0.0010 0.0511  0.0150  105 ASP   B OD2 
5280 N  N   A ILE   B 106 ? 0.3715 0.2672 0.3123 -0.0144 0.1707  0.0339  106 ILE   B N   
5281 N  N   B ILE   B 106 ? 0.3565 0.3329 0.3173 -0.0011 0.0438  0.0046  106 ILE   B N   
5282 C  CA  A ILE   B 106 ? 0.3481 0.2368 0.3211 -0.0214 0.1736  0.0310  106 ILE   B CA  
5283 C  CA  B ILE   B 106 ? 0.3448 0.3252 0.3128 -0.0019 0.0436  0.0003  106 ILE   B CA  
5284 C  C   A ILE   B 106 ? 0.3092 0.2304 0.3244 -0.0163 0.1714  0.0091  106 ILE   B C   
5285 C  C   B ILE   B 106 ? 0.3290 0.3181 0.3119 -0.0019 0.0457  -0.0053 106 ILE   B C   
5286 O  O   A ILE   B 106 ? 0.2971 0.2058 0.3319 -0.0168 0.1602  -0.0007 106 ILE   B O   
5287 O  O   B ILE   B 106 ? 0.3279 0.3164 0.3096 -0.0036 0.0417  -0.0077 106 ILE   B O   
5288 C  CB  A ILE   B 106 ? 0.3696 0.2283 0.3448 -0.0294 0.1576  0.0436  106 ILE   B CB  
5289 C  CB  B ILE   B 106 ? 0.3486 0.3253 0.3137 -0.0028 0.0408  0.0014  106 ILE   B CB  
5290 C  CG1 A ILE   B 106 ? 0.3787 0.2293 0.3563 -0.0200 0.1468  0.0355  106 ILE   B CG1 
5291 C  CG1 B ILE   B 106 ? 0.3497 0.3246 0.3147 -0.0020 0.0385  0.0020  106 ILE   B CG1 
5292 C  CG2 A ILE   B 106 ? 0.3765 0.2329 0.3671 -0.0387 0.1539  0.0513  106 ILE   B CG2 
5293 C  CG2 B ILE   B 106 ? 0.3505 0.3270 0.3175 -0.0036 0.0406  0.0017  106 ILE   B CG2 
5294 C  CD1 A ILE   B 106 ? 0.3837 0.2309 0.3558 -0.0097 0.1438  0.0354  106 ILE   B CD1 
5295 C  CD1 B ILE   B 106 ? 0.3502 0.3241 0.3156 -0.0007 0.0375  0.0029  106 ILE   B CD1 
5318 N  N   A GLN   B 107 ? 0.2924 0.2567 0.3410 -0.0194 0.1624  0.0044  107 GLN   B N   
5319 N  N   B GLN   B 107 ? 0.3148 0.3130 0.3187 -0.0013 0.0508  -0.0077 107 GLN   B N   
5320 C  CA  A GLN   B 107 ? 0.2763 0.2800 0.3505 -0.0221 0.1493  0.0062  107 GLN   B CA  
5321 C  CA  B GLN   B 107 ? 0.2997 0.3060 0.3262 0.0001  0.0566  -0.0073 107 GLN   B CA  
5322 C  C   A GLN   B 107 ? 0.2507 0.2647 0.3172 -0.0100 0.1063  -0.0049 107 GLN   B C   
5323 C  C   B GLN   B 107 ? 0.2685 0.2800 0.2964 0.0030  0.0682  -0.0094 107 GLN   B C   
5324 O  O   A GLN   B 107 ? 0.2410 0.2652 0.3531 -0.0040 0.0760  -0.0170 107 GLN   B O   
5325 O  O   B GLN   B 107 ? 0.2684 0.2819 0.2988 0.0034  0.0626  -0.0138 107 GLN   B O   
5326 C  CB  A GLN   B 107 ? 0.3055 0.3234 0.4102 -0.0247 0.1456  0.0099  107 GLN   B CB  
5327 C  CB  B GLN   B 107 ? 0.3167 0.3241 0.3677 0.0001  0.0484  -0.0054 107 GLN   B CB  
5328 C  CG  A GLN   B 107 ? 0.3390 0.3668 0.4781 -0.0182 0.1148  0.0078  107 GLN   B CG  
5329 C  CG  B GLN   B 107 ? 0.3315 0.3399 0.4080 0.0012  0.0381  -0.0033 107 GLN   B CG  
5330 C  CD  A GLN   B 107 ? 0.3627 0.3978 0.5332 -0.0175 0.0903  0.0109  107 GLN   B CD  
5331 C  CD  B GLN   B 107 ? 0.3422 0.3520 0.4415 0.0013  0.0300  -0.0006 107 GLN   B CD  
5332 O  OE1 A GLN   B 107 ? 0.3724 0.4121 0.5523 -0.0162 0.0901  0.0084  107 GLN   B OE1 
5333 O  OE1 B GLN   B 107 ? 0.3465 0.3569 0.4532 0.0011  0.0295  -0.0006 107 GLN   B OE1 
5334 N  NE2 A GLN   B 107 ? 0.3717 0.4089 0.5519 -0.0127 0.0756  0.0163  107 GLN   B NE2 
5335 N  NE2 B GLN   B 107 ? 0.3460 0.3557 0.4531 0.0027  0.0263  0.0018  107 GLN   B NE2 
5352 N  N   . LEU   B 108 ? 0.2353 0.2495 0.2743 0.0071  0.0839  -0.0074 108 LEU   B N   
5353 C  CA  . LEU   B 108 ? 0.2202 0.2272 0.2447 0.0230  0.0604  0.0039  108 LEU   B CA  
5354 C  C   . LEU   B 108 ? 0.1878 0.1846 0.2247 0.0232  0.0367  0.0221  108 LEU   B C   
5355 O  O   . LEU   B 108 ? 0.1929 0.1764 0.2205 0.0217  0.0258  0.0217  108 LEU   B O   
5356 C  CB  . LEU   B 108 ? 0.2384 0.2501 0.2304 0.0242  0.0598  0.0072  108 LEU   B CB  
5357 C  CG  . LEU   B 108 ? 0.2560 0.2751 0.2285 0.0325  0.0494  -0.0099 108 LEU   B CG  
5358 C  CD1 . LEU   B 108 ? 0.2670 0.2908 0.2147 0.0204  0.0500  -0.0092 108 LEU   B CD1 
5359 C  CD2 . LEU   B 108 ? 0.2701 0.2844 0.2479 0.0425  0.0372  -0.0154 108 LEU   B CD2 
5372 N  N   . LEU   B 109 ? 0.1732 0.1680 0.2186 0.0148  0.0349  0.0193  109 LEU   B N   
5373 C  CA  . LEU   B 109 ? 0.1601 0.1434 0.2276 0.0110  0.0313  0.0272  109 LEU   B CA  
5374 C  C   . LEU   B 109 ? 0.1480 0.1356 0.2229 0.0051  0.0299  0.0161  109 LEU   B C   
5375 O  O   . LEU   B 109 ? 0.1437 0.1355 0.2189 0.0092  0.0288  0.0304  109 LEU   B O   
5376 C  CB  . LEU   B 109 ? 0.1655 0.1408 0.2311 0.0084  0.0225  0.0378  109 LEU   B CB  
5377 C  CG  . LEU   B 109 ? 0.1674 0.1395 0.2273 0.0064  0.0125  0.0198  109 LEU   B CG  
5378 C  CD1 . LEU   B 109 ? 0.1693 0.1551 0.2135 0.0131  0.0247  0.0160  109 LEU   B CD1 
5379 C  CD2 . LEU   B 109 ? 0.1783 0.1441 0.2411 0.0070  0.0091  0.0185  109 LEU   B CD2 
5391 N  N   . LYS   B 110 ? 0.1470 0.1316 0.2192 -0.0037 0.0325  0.0234  110 LYS   B N   
5392 C  CA  . LYS   B 110 ? 0.1454 0.1338 0.2161 0.0029  0.0244  0.0157  110 LYS   B CA  
5393 C  C   . LYS   B 110 ? 0.1372 0.1343 0.2035 -0.0001 0.0239  0.0102  110 LYS   B C   
5394 O  O   . LYS   B 110 ? 0.1360 0.1367 0.1991 -0.0037 0.0145  0.0046  110 LYS   B O   
5395 C  CB  . LYS   B 110 ? 0.1436 0.1404 0.2323 0.0010  0.0267  0.0077  110 LYS   B CB  
5396 C  CG  . LYS   B 110 ? 0.1458 0.1321 0.2491 -0.0080 0.0105  0.0144  110 LYS   B CG  
5397 C  CD  . LYS   B 110 ? 0.1470 0.1352 0.2526 -0.0038 0.0067  0.0123  110 LYS   B CD  
5398 C  CE  . LYS   B 110 ? 0.1470 0.1444 0.2610 -0.0041 0.0027  0.0056  110 LYS   B CE  
5399 N  NZ  . LYS   B 110 ? 0.1470 0.1601 0.2613 0.0059  -0.0015 0.0055  110 LYS   B NZ  
5413 N  N   . SER   B 111 ? 0.1453 0.1331 0.2151 -0.0045 0.0282  0.0189  111 SER   B N   
5414 C  CA  . SER   B 111 ? 0.1486 0.1345 0.2080 -0.0001 0.0161  0.0176  111 SER   B CA  
5415 C  C   . SER   B 111 ? 0.1442 0.1306 0.2013 0.0021  0.0115  0.0068  111 SER   B C   
5416 O  O   . SER   B 111 ? 0.1379 0.1336 0.2060 -0.0000 0.0051  0.0092  111 SER   B O   
5417 C  CB  . SER   B 111 ? 0.1647 0.1529 0.2177 0.0031  0.0280  0.0250  111 SER   B CB  
5418 O  OG  . SER   B 111 ? 0.1831 0.1915 0.2228 0.0047  0.0371  0.0246  111 SER   B OG  
5424 N  N   . ALA   B 112 ? 0.1371 0.1320 0.1992 0.0050  0.0151  0.0129  112 ALA   B N   
5425 C  CA  . ALA   B 112 ? 0.1344 0.1414 0.1947 0.0029  0.0069  0.0026  112 ALA   B CA  
5426 C  C   . ALA   B 112 ? 0.1287 0.1312 0.1891 -0.0010 0.0001  0.0015  112 ALA   B C   
5427 O  O   . ALA   B 112 ? 0.1306 0.1297 0.1968 -0.0048 0.0058  0.0019  112 ALA   B O   
5428 C  CB  . ALA   B 112 ? 0.1373 0.1436 0.2030 0.0059  0.0027  0.0135  112 ALA   B CB  
5434 N  N   . TYR   B 113 ? 0.1297 0.1225 0.1954 -0.0011 0.0103  0.0050  113 TYR   B N   
5435 C  CA  . TYR   B 113 ? 0.1244 0.1187 0.1901 -0.0024 0.0136  0.0001  113 TYR   B CA  
5436 C  C   . TYR   B 113 ? 0.1248 0.1142 0.1877 -0.0076 0.0094  0.0039  113 TYR   B C   
5437 O  O   . TYR   B 113 ? 0.1282 0.1193 0.1838 -0.0043 0.0064  -0.0007 113 TYR   B O   
5438 C  CB  . TYR   B 113 ? 0.1335 0.1154 0.1949 -0.0035 0.0229  0.0117  113 TYR   B CB  
5439 C  CG  . TYR   B 113 ? 0.1308 0.1222 0.2072 -0.0060 0.0131  0.0136  113 TYR   B CG  
5440 C  CD1 . TYR   B 113 ? 0.1383 0.1221 0.2206 -0.0032 0.0164  0.0180  113 TYR   B CD1 
5441 C  CD2 . TYR   B 113 ? 0.1414 0.1225 0.2052 -0.0045 0.0075  0.0058  113 TYR   B CD2 
5442 C  CE1 . TYR   B 113 ? 0.1409 0.1268 0.2160 0.0004  0.0223  0.0079  113 TYR   B CE1 
5443 C  CE2 . TYR   B 113 ? 0.1421 0.1123 0.2199 0.0027  0.0082  0.0125  113 TYR   B CE2 
5444 C  CZ  . TYR   B 113 ? 0.1361 0.1191 0.2217 0.0069  0.0093  0.0055  113 TYR   B CZ  
5445 O  OH  . TYR   B 113 ? 0.1463 0.1204 0.2436 0.0079  0.0171  0.0074  113 TYR   B OH  
5455 N  N   . GLU   B 114 ? 0.1220 0.1123 0.1917 -0.0021 0.0107  0.0031  114 GLU   B N   
5456 C  CA  . GLU   B 114 ? 0.1236 0.1119 0.1919 -0.0037 0.0065  -0.0004 114 GLU   B CA  
5457 C  C   . GLU   B 114 ? 0.1219 0.1145 0.1871 -0.0008 0.0090  -0.0037 114 GLU   B C   
5458 O  O   . GLU   B 114 ? 0.1205 0.1173 0.2062 0.0005  0.0006  0.0115  114 GLU   B O   
5459 C  CB  . GLU   B 114 ? 0.1233 0.1167 0.2011 -0.0010 0.0150  -0.0025 114 GLU   B CB  
5460 C  CG  . GLU   B 114 ? 0.1321 0.1211 0.2031 0.0001  0.0114  0.0056  114 GLU   B CG  
5461 C  CD  . GLU   B 114 ? 0.1278 0.1260 0.2108 -0.0084 0.0103  0.0038  114 GLU   B CD  
5462 O  OE1 . GLU   B 114 ? 0.1270 0.1404 0.2045 -0.0088 0.0159  0.0119  114 GLU   B OE1 
5463 O  OE2 . GLU   B 114 ? 0.1276 0.1438 0.2160 -0.0191 0.0098  0.0075  114 GLU   B OE2 
5470 N  N   . ASN   B 115 ? 0.1276 0.1119 0.1816 -0.0062 -0.0018 -0.0018 115 ASN   B N   
5471 C  CA  . ASN   B 115 ? 0.1287 0.1192 0.1718 -0.0063 -0.0015 0.0059  115 ASN   B CA  
5472 C  C   . ASN   B 115 ? 0.1233 0.1192 0.1667 -0.0084 -0.0045 0.0010  115 ASN   B C   
5473 O  O   . ASN   B 115 ? 0.1334 0.1249 0.1801 -0.0134 0.0009  -0.0010 115 ASN   B O   
5474 C  CB  . ASN   B 115 ? 0.1346 0.1343 0.1709 -0.0064 0.0073  0.0083  115 ASN   B CB  
5475 C  CG  . ASN   B 115 ? 0.1426 0.1398 0.1777 0.0061  0.0047  -0.0008 115 ASN   B CG  
5476 O  OD1 . ASN   B 115 ? 0.1890 0.1542 0.1920 -0.0010 0.0148  -0.0130 115 ASN   B OD1 
5477 N  ND2 . ASN   B 115 ? 0.1411 0.1469 0.1833 -0.0006 0.0053  0.0083  115 ASN   B ND2 
5484 N  N   . PHE   B 116 ? 0.1218 0.1170 0.1638 -0.0040 -0.0006 0.0001  116 PHE   B N   
5485 C  CA  . PHE   B 116 ? 0.1284 0.1185 0.1710 -0.0072 0.0010  0.0017  116 PHE   B CA  
5486 C  C   . PHE   B 116 ? 0.1267 0.1115 0.1704 -0.0096 0.0002  0.0060  116 PHE   B C   
5487 O  O   . PHE   B 116 ? 0.1314 0.1210 0.1707 -0.0040 -0.0034 0.0043  116 PHE   B O   
5488 C  CB  . PHE   B 116 ? 0.1267 0.1183 0.1706 -0.0049 -0.0084 0.0052  116 PHE   B CB  
5489 C  CG  . PHE   B 116 ? 0.1223 0.1226 0.1709 -0.0048 0.0037  0.0047  116 PHE   B CG  
5490 C  CD1 . PHE   B 116 ? 0.1266 0.1265 0.1892 -0.0044 0.0037  0.0064  116 PHE   B CD1 
5491 C  CD2 . PHE   B 116 ? 0.1268 0.1317 0.1688 0.0002  0.0074  -0.0035 116 PHE   B CD2 
5492 C  CE1 . PHE   B 116 ? 0.1309 0.1308 0.1893 -0.0021 -0.0118 0.0070  116 PHE   B CE1 
5493 C  CE2 . PHE   B 116 ? 0.1281 0.1289 0.1779 0.0009  0.0006  0.0005  116 PHE   B CE2 
5494 C  CZ  . PHE   B 116 ? 0.1251 0.1270 0.1816 0.0021  -0.0097 0.0027  116 PHE   B CZ  
5504 N  N   . ASN   B 117 ? 0.1232 0.1172 0.1744 -0.0060 -0.0094 0.0023  117 ASN   B N   
5505 C  CA  . ASN   B 117 ? 0.1348 0.1191 0.1759 -0.0013 -0.0031 -0.0026 117 ASN   B CA  
5506 C  C   . ASN   B 117 ? 0.1331 0.1147 0.1963 0.0000  -0.0018 0.0005  117 ASN   B C   
5507 O  O   . ASN   B 117 ? 0.1430 0.1231 0.2289 -0.0031 -0.0282 0.0047  117 ASN   B O   
5508 C  CB  . ASN   B 117 ? 0.1396 0.1237 0.1887 -0.0013 -0.0035 0.0003  117 ASN   B CB  
5509 C  CG  . ASN   B 117 ? 0.1295 0.1246 0.1913 0.0027  -0.0063 -0.0081 117 ASN   B CG  
5510 O  OD1 . ASN   B 117 ? 0.1511 0.1236 0.2131 -0.0143 0.0061  -0.0054 117 ASN   B OD1 
5511 N  ND2 . ASN   B 117 ? 0.1338 0.1272 0.1795 -0.0018 0.0019  -0.0091 117 ASN   B ND2 
5518 N  N   . GLN   B 118 ? 0.1334 0.1141 0.1906 -0.0063 -0.0140 0.0008  118 GLN   B N   
5519 C  CA  . GLN   B 118 ? 0.1347 0.1168 0.2010 0.0041  -0.0114 -0.0000 118 GLN   B CA  
5520 C  C   . GLN   B 118 ? 0.1386 0.1223 0.2065 -0.0002 -0.0090 -0.0057 118 GLN   B C   
5521 O  O   . GLN   B 118 ? 0.1593 0.1201 0.2327 -0.0119 -0.0006 0.0029  118 GLN   B O   
5522 C  CB  . GLN   B 118 ? 0.1461 0.1266 0.2103 0.0031  -0.0148 -0.0007 118 GLN   B CB  
5523 C  CG  . GLN   B 118 ? 0.1532 0.1292 0.2031 0.0057  -0.0102 -0.0104 118 GLN   B CG  
5524 C  CD  . GLN   B 118 ? 0.1573 0.1217 0.2024 0.0039  -0.0104 -0.0084 118 GLN   B CD  
5525 O  OE1 . GLN   B 118 ? 0.1669 0.1209 0.2224 0.0053  0.0087  0.0076  118 GLN   B OE1 
5526 N  NE2 . GLN   B 118 ? 0.1615 0.1214 0.2131 0.0023  -0.0167 0.0034  118 GLN   B NE2 
5535 N  N   . HIS   B 119 ? 0.1357 0.1258 0.1777 -0.0075 -0.0062 0.0069  119 HIS   B N   
5536 C  CA  . HIS   B 119 ? 0.1473 0.1354 0.1706 -0.0028 -0.0199 0.0066  119 HIS   B CA  
5537 C  C   . HIS   B 119 ? 0.1549 0.1319 0.1689 -0.0054 -0.0237 0.0081  119 HIS   B C   
5538 O  O   . HIS   B 119 ? 0.1600 0.1334 0.1909 -0.0226 -0.0146 0.0139  119 HIS   B O   
5539 C  CB  . HIS   B 119 ? 0.1552 0.1463 0.1713 -0.0021 -0.0181 0.0023  119 HIS   B CB  
5540 C  CG  . HIS   B 119 ? 0.1660 0.1691 0.1896 0.0043  -0.0272 -0.0143 119 HIS   B CG  
5541 N  ND1 . HIS   B 119 ? 0.1807 0.1824 0.2193 0.0006  -0.0399 -0.0360 119 HIS   B ND1 
5542 C  CD2 . HIS   B 119 ? 0.1762 0.1854 0.1932 0.0297  -0.0364 -0.0144 119 HIS   B CD2 
5543 C  CE1 . HIS   B 119 ? 0.1982 0.1927 0.2267 0.0171  -0.0422 -0.0407 119 HIS   B CE1 
5544 N  NE2 . HIS   B 119 ? 0.1948 0.2072 0.2147 0.0289  -0.0393 -0.0313 119 HIS   B NE2 
5552 N  N   . GLU   B 120 ? 0.1724 0.1310 0.1629 -0.0092 -0.0324 0.0086  120 GLU   B N   
5553 C  CA  . GLU   B 120 ? 0.2006 0.1506 0.1767 -0.0000 -0.0467 0.0196  120 GLU   B CA  
5554 C  C   . GLU   B 120 ? 0.1788 0.1399 0.1662 -0.0138 -0.0339 0.0246  120 GLU   B C   
5555 O  O   . GLU   B 120 ? 0.1693 0.1525 0.1702 -0.0163 -0.0273 0.0096  120 GLU   B O   
5556 C  CB  . GLU   B 120 ? 0.2586 0.1848 0.2326 0.0238  -0.0730 0.0418  120 GLU   B CB  
5557 C  CG  . GLU   B 120 ? 0.3119 0.2514 0.3275 0.0318  -0.0886 0.0578  120 GLU   B CG  
5558 C  CD  . GLU   B 120 ? 0.3521 0.3151 0.4286 0.0267  -0.0886 0.0669  120 GLU   B CD  
5559 O  OE1 . GLU   B 120 ? 0.3748 0.3370 0.4631 0.0156  -0.0815 0.0816  120 GLU   B OE1 
5560 O  OE2 . GLU   B 120 ? 0.3730 0.3408 0.4846 0.0259  -0.0870 0.0536  120 GLU   B OE2 
5567 N  N   . VAL   B 121 ? 0.1695 0.1370 0.1668 -0.0205 -0.0201 0.0170  121 VAL   B N   
5568 C  CA  . VAL   B 121 ? 0.1681 0.1452 0.1559 -0.0185 -0.0167 0.0169  121 VAL   B CA  
5569 C  C   . VAL   B 121 ? 0.1548 0.1419 0.1580 -0.0231 -0.0141 0.0133  121 VAL   B C   
5570 O  O   . VAL   B 121 ? 0.1599 0.1352 0.1806 -0.0257 -0.0250 0.0095  121 VAL   B O   
5571 C  CB  . VAL   B 121 ? 0.1878 0.1828 0.1663 -0.0099 -0.0258 0.0174  121 VAL   B CB  
5572 C  CG1 . VAL   B 121 ? 0.1931 0.1941 0.1985 -0.0139 -0.0125 0.0080  121 VAL   B CG1 
5573 C  CG2 . VAL   B 121 ? 0.2132 0.2059 0.1758 -0.0015 -0.0215 0.0114  121 VAL   B CG2 
5583 N  N   . LEU   B 122 ? 0.1455 0.1340 0.1541 -0.0170 -0.0280 0.0096  122 LEU   B N   
5584 C  CA  . LEU   B 122 ? 0.1421 0.1392 0.1416 -0.0206 -0.0189 0.0098  122 LEU   B CA  
5585 C  C   . LEU   B 122 ? 0.1412 0.1295 0.1467 -0.0250 -0.0164 0.0071  122 LEU   B C   
5586 O  O   . LEU   B 122 ? 0.1511 0.1341 0.1787 -0.0278 -0.0221 -0.0008 122 LEU   B O   
5587 C  CB  . LEU   B 122 ? 0.1649 0.1582 0.1653 -0.0005 -0.0226 0.0100  122 LEU   B CB  
5588 C  CG  . LEU   B 122 ? 0.1549 0.1627 0.1813 -0.0156 -0.0119 0.0047  122 LEU   B CG  
5589 C  CD1 . LEU   B 122 ? 0.1614 0.1799 0.2006 -0.0158 -0.0150 0.0061  122 LEU   B CD1 
5590 C  CD2 . LEU   B 122 ? 0.1574 0.1616 0.1714 -0.0109 -0.0058 -0.0059 122 LEU   B CD2 
5602 N  N   . LEU   B 123 ? 0.1440 0.1208 0.1439 -0.0243 -0.0069 0.0059  123 LEU   B N   
5603 C  CA  . LEU   B 123 ? 0.1504 0.1255 0.1495 -0.0214 -0.0145 -0.0023 123 LEU   B CA  
5604 C  C   . LEU   B 123 ? 0.1397 0.1187 0.1530 -0.0190 -0.0135 0.0023  123 LEU   B C   
5605 O  O   . LEU   B 123 ? 0.1552 0.1211 0.1570 -0.0301 -0.0130 0.0002  123 LEU   B O   
5606 C  CB  . LEU   B 123 ? 0.1554 0.1317 0.1513 -0.0206 -0.0076 0.0001  123 LEU   B CB  
5607 C  CG  . LEU   B 123 ? 0.1491 0.1355 0.1704 -0.0156 -0.0074 0.0001  123 LEU   B CG  
5608 C  CD1 . LEU   B 123 ? 0.1566 0.1400 0.1827 -0.0178 -0.0067 -0.0134 123 LEU   B CD1 
5609 C  CD2 . LEU   B 123 ? 0.1593 0.1424 0.1894 -0.0112 -0.0028 0.0138  123 LEU   B CD2 
5621 N  N   . ALA   B 124 ? 0.1403 0.1209 0.1490 -0.0183 -0.0056 -0.0027 124 ALA   B N   
5622 C  CA  . ALA   B 124 ? 0.1344 0.1231 0.1616 -0.0118 -0.0062 -0.0110 124 ALA   B CA  
5623 C  C   . ALA   B 124 ? 0.1312 0.1252 0.1585 -0.0099 -0.0046 -0.0086 124 ALA   B C   
5624 O  O   . ALA   B 124 ? 0.1432 0.1252 0.1558 -0.0149 -0.0074 -0.0022 124 ALA   B O   
5625 C  CB  . ALA   B 124 ? 0.1403 0.1284 0.1720 -0.0068 0.0035  -0.0035 124 ALA   B CB  
5631 N  N   . PRO   B 125 ? 0.1396 0.1240 0.1521 -0.0119 -0.0169 0.0081  125 PRO   B N   
5632 C  CA  . PRO   B 125 ? 0.1440 0.1274 0.1724 -0.0114 -0.0097 0.0195  125 PRO   B CA  
5633 C  C   . PRO   B 125 ? 0.1398 0.1161 0.1899 -0.0143 -0.0062 0.0088  125 PRO   B C   
5634 O  O   . PRO   B 125 ? 0.1424 0.1150 0.2056 -0.0099 0.0036  0.0223  125 PRO   B O   
5635 C  CB  . PRO   B 125 ? 0.1479 0.1486 0.1820 -0.0184 -0.0107 0.0274  125 PRO   B CB  
5636 C  CG  . PRO   B 125 ? 0.1567 0.1568 0.1721 -0.0264 -0.0134 0.0092  125 PRO   B CG  
5637 C  CD  . PRO   B 125 ? 0.1505 0.1364 0.1473 -0.0250 -0.0154 0.0046  125 PRO   B CD  
5645 N  N   . LEU   B 126 ? 0.1437 0.1186 0.2025 -0.0130 0.0111  0.0097  126 LEU   B N   
5646 C  CA  . LEU   B 126 ? 0.1546 0.1260 0.2088 -0.0093 0.0185  0.0144  126 LEU   B CA  
5647 C  C   . LEU   B 126 ? 0.1541 0.1317 0.2091 -0.0005 0.0208  0.0193  126 LEU   B C   
5648 O  O   . LEU   B 126 ? 0.1740 0.1589 0.2194 0.0158  0.0033  -0.0042 126 LEU   B O   
5649 C  CB  . LEU   B 126 ? 0.1726 0.1345 0.2267 -0.0107 0.0292  0.0081  126 LEU   B CB  
5650 C  CG  . LEU   B 126 ? 0.1902 0.1393 0.2277 -0.0208 0.0228  -0.0102 126 LEU   B CG  
5651 C  CD1 . LEU   B 126 ? 0.2005 0.1484 0.2645 -0.0202 0.0102  -0.0139 126 LEU   B CD1 
5652 C  CD2 . LEU   B 126 ? 0.1907 0.1503 0.2276 -0.0269 0.0113  -0.0089 126 LEU   B CD2 
5664 N  N   . LEU   B 127 ? 0.1445 0.1293 0.2103 0.0049  0.0223  0.0135  127 LEU   B N   
5665 C  CA  . LEU   B 127 ? 0.1423 0.1322 0.2085 -0.0029 0.0259  0.0190  127 LEU   B CA  
5666 C  C   . LEU   B 127 ? 0.1386 0.1285 0.2099 -0.0001 0.0142  0.0147  127 LEU   B C   
5667 O  O   . LEU   B 127 ? 0.1430 0.1332 0.2115 -0.0108 0.0090  0.0137  127 LEU   B O   
5668 C  CB  . LEU   B 127 ? 0.1553 0.1330 0.2231 -0.0022 0.0195  0.0264  127 LEU   B CB  
5669 C  CG  . LEU   B 127 ? 0.1668 0.1354 0.2302 0.0065  0.0186  0.0247  127 LEU   B CG  
5670 C  CD1 . LEU   B 127 ? 0.1727 0.1373 0.2304 0.0094  0.0116  0.0020  127 LEU   B CD1 
5671 C  CD2 . LEU   B 127 ? 0.1692 0.1526 0.2466 -0.0031 0.0225  0.0338  127 LEU   B CD2 
5683 N  N   . SER   B 128 ? 0.1444 0.1324 0.2045 0.0035  0.0028  0.0110  128 SER   B N   
5684 C  CA  . SER   B 128 ? 0.1569 0.1403 0.1972 0.0123  -0.0058 0.0200  128 SER   B CA  
5685 C  C   . SER   B 128 ? 0.1706 0.1433 0.2184 0.0118  -0.0202 0.0165  128 SER   B C   
5686 O  O   . SER   B 128 ? 0.1783 0.1463 0.2534 0.0081  -0.0135 0.0275  128 SER   B O   
5687 C  CB  . SER   B 128 ? 0.1686 0.1363 0.2055 0.0088  0.0008  0.0280  128 SER   B CB  
5688 O  OG  . SER   B 128 ? 0.1709 0.1541 0.2133 0.0116  0.0123  0.0324  128 SER   B OG  
5694 N  N   . ALA   B 129 ? 0.1815 0.1431 0.2425 0.0260  -0.0085 0.0010  129 ALA   B N   
5695 C  CA  . ALA   B 129 ? 0.1972 0.1553 0.2615 0.0311  -0.0063 -0.0069 129 ALA   B CA  
5696 C  C   . ALA   B 129 ? 0.1852 0.1518 0.2490 0.0250  0.0012  -0.0028 129 ALA   B C   
5697 O  O   . ALA   B 129 ? 0.1747 0.1524 0.2447 0.0184  -0.0019 0.0045  129 ALA   B O   
5698 C  CB  . ALA   B 129 ? 0.2168 0.1778 0.2933 0.0319  0.0020  -0.0170 129 ALA   B CB  
5704 N  N   . GLY   B 130 ? 0.1872 0.1459 0.2482 0.0303  0.0127  -0.0038 130 GLY   B N   
5705 C  CA  . GLY   B 130 ? 0.1873 0.1616 0.2549 0.0291  0.0368  -0.0003 130 GLY   B CA  
5706 C  C   . GLY   B 130 ? 0.1894 0.1624 0.2497 0.0218  0.0199  0.0105  130 GLY   B C   
5707 O  O   . GLY   B 130 ? 0.2051 0.1735 0.2539 0.0201  0.0103  0.0201  130 GLY   B O   
5711 N  N   . ILE   B 131 ? 0.1827 0.1682 0.2596 0.0341  0.0216  0.0085  131 ILE   B N   
5712 C  CA  . ILE   B 131 ? 0.2017 0.1813 0.2534 0.0284  0.0106  0.0175  131 ILE   B CA  
5713 C  C   . ILE   B 131 ? 0.2123 0.1724 0.2331 0.0184  0.0096  0.0109  131 ILE   B C   
5714 O  O   . ILE   B 131 ? 0.2396 0.1880 0.2551 0.0197  -0.0020 0.0101  131 ILE   B O   
5715 C  CB  . ILE   B 131 ? 0.2034 0.2190 0.2843 0.0275  0.0031  0.0212  131 ILE   B CB  
5716 C  CG1 . ILE   B 131 ? 0.2017 0.2355 0.2879 0.0043  0.0131  0.0239  131 ILE   B CG1 
5717 C  CG2 . ILE   B 131 ? 0.2011 0.2385 0.3033 0.0310  -0.0001 0.0103  131 ILE   B CG2 
5718 C  CD1 . ILE   B 131 ? 0.2123 0.2564 0.2959 -0.0105 0.0061  0.0268  131 ILE   B CD1 
5730 N  N   . PHE   B 132 ? 0.1983 0.1512 0.2228 0.0200  0.0216  0.0186  132 PHE   B N   
5731 C  CA  . PHE   B 132 ? 0.2061 0.1572 0.2238 0.0130  0.0399  0.0163  132 PHE   B CA  
5732 C  C   . PHE   B 132 ? 0.2254 0.1751 0.2449 0.0157  0.0436  0.0174  132 PHE   B C   
5733 O  O   . PHE   B 132 ? 0.2424 0.1968 0.2663 0.0085  0.0505  0.0223  132 PHE   B O   
5734 C  CB  . PHE   B 132 ? 0.1889 0.1536 0.2084 0.0157  0.0371  0.0209  132 PHE   B CB  
5735 C  CG  . PHE   B 132 ? 0.1835 0.1611 0.2038 0.0153  0.0282  0.0173  132 PHE   B CG  
5736 C  CD1 . PHE   B 132 ? 0.1918 0.1644 0.2347 0.0081  0.0262  0.0125  132 PHE   B CD1 
5737 C  CD2 . PHE   B 132 ? 0.1843 0.1643 0.1840 0.0227  0.0188  0.0279  132 PHE   B CD2 
5738 C  CE1 . PHE   B 132 ? 0.1943 0.1686 0.2376 0.0049  0.0200  0.0122  132 PHE   B CE1 
5739 C  CE2 . PHE   B 132 ? 0.1924 0.1707 0.1950 0.0200  0.0095  0.0123  132 PHE   B CE2 
5740 C  CZ  . PHE   B 132 ? 0.1945 0.1674 0.2253 0.0085  -0.0003 0.0227  132 PHE   B CZ  
5750 N  N   . GLY   B 133 ? 0.2189 0.1681 0.2437 0.0173  0.0323  0.0389  133 GLY   B N   
5751 C  CA  . GLY   B 133 ? 0.2301 0.1803 0.2429 -0.0096 0.0294  0.0460  133 GLY   B CA  
5752 C  C   . GLY   B 133 ? 0.2335 0.1800 0.2448 -0.0226 0.0338  0.0411  133 GLY   B C   
5753 O  O   . GLY   B 133 ? 0.2531 0.1914 0.2864 -0.0321 0.0319  0.0524  133 GLY   B O   
5757 N  N   . ALA   B 134 ? 0.2194 0.1786 0.2344 -0.0242 0.0277  0.0223  134 ALA   B N   
5758 C  CA  . ALA   B 134 ? 0.2146 0.1745 0.2459 -0.0209 0.0343  0.0075  134 ALA   B CA  
5759 C  C   . ALA   B 134 ? 0.2175 0.1690 0.2413 -0.0095 0.0382  0.0242  134 ALA   B C   
5760 O  O   . ALA   B 134 ? 0.2228 0.1902 0.2635 0.0015  0.0299  0.0153  134 ALA   B O   
5761 C  CB  . ALA   B 134 ? 0.2153 0.1709 0.2714 -0.0096 0.0311  -0.0053 134 ALA   B CB  
5767 N  N   . ASP   B 135 ? 0.2320 0.1638 0.2352 -0.0125 0.0251  0.0273  135 ASP   B N   
5768 C  CA  . ASP   B 135 ? 0.2470 0.1556 0.2504 -0.0094 0.0108  0.0333  135 ASP   B CA  
5769 C  C   . ASP   B 135 ? 0.2277 0.1489 0.2429 -0.0025 0.0091  0.0232  135 ASP   B C   
5770 O  O   . ASP   B 135 ? 0.2228 0.1465 0.2616 -0.0008 0.0118  0.0244  135 ASP   B O   
5771 C  CB  . ASP   B 135 ? 0.2771 0.1683 0.2778 -0.0272 0.0104  0.0354  135 ASP   B CB  
5772 C  CG  . ASP   B 135 ? 0.3057 0.1670 0.3170 -0.0480 0.0073  0.0285  135 ASP   B CG  
5773 O  OD1 . ASP   B 135 ? 0.3178 0.1531 0.3109 -0.0319 0.0029  0.0259  135 ASP   B OD1 
5774 O  OD2 . ASP   B 135 ? 0.3270 0.2086 0.3724 -0.0634 0.0008  0.0071  135 ASP   B OD2 
5779 N  N   . PRO   B 136 ? 0.2190 0.1514 0.2517 0.0168  -0.0056 0.0189  136 PRO   B N   
5780 C  CA  . PRO   B 136 ? 0.1977 0.1464 0.2538 0.0187  -0.0047 0.0091  136 PRO   B CA  
5781 C  C   . PRO   B 136 ? 0.1826 0.1368 0.2588 0.0152  -0.0006 0.0053  136 PRO   B C   
5782 O  O   . PRO   B 136 ? 0.1645 0.1335 0.2542 0.0099  -0.0010 0.0137  136 PRO   B O   
5783 C  CB  . PRO   B 136 ? 0.2063 0.1688 0.2717 0.0347  -0.0131 0.0017  136 PRO   B CB  
5784 C  CG  . PRO   B 136 ? 0.2271 0.1749 0.2864 0.0351  -0.0117 -0.0004 136 PRO   B CG  
5785 C  CD  . PRO   B 136 ? 0.2268 0.1640 0.2747 0.0417  -0.0056 0.0117  136 PRO   B CD  
5793 N  N   . ILE   B 137 ? 0.1864 0.1291 0.2651 0.0170  -0.0075 0.0084  137 ILE   B N   
5794 C  CA  . ILE   B 137 ? 0.1970 0.1268 0.2826 0.0005  -0.0031 0.0036  137 ILE   B CA  
5795 C  C   . ILE   B 137 ? 0.1896 0.1291 0.2679 -0.0075 0.0093  0.0119  137 ILE   B C   
5796 O  O   . ILE   B 137 ? 0.1789 0.1348 0.2614 -0.0111 0.0072  0.0115  137 ILE   B O   
5797 C  CB  . ILE   B 137 ? 0.2228 0.1323 0.3190 0.0003  -0.0056 0.0047  137 ILE   B CB  
5798 C  CG1 . ILE   B 137 ? 0.2504 0.1511 0.3564 0.0047  -0.0015 -0.0129 137 ILE   B CG1 
5799 C  CG2 . ILE   B 137 ? 0.2259 0.1376 0.3351 -0.0238 -0.0092 0.0134  137 ILE   B CG2 
5800 C  CD1 . ILE   B 137 ? 0.2743 0.1797 0.3912 0.0183  -0.0055 -0.0070 137 ILE   B CD1 
5812 N  N   . HIS   B 138 ? 0.1962 0.1285 0.2724 -0.0058 0.0169  0.0091  138 HIS   B N   
5813 C  CA  . HIS   B 138 ? 0.2010 0.1398 0.2702 -0.0013 0.0378  0.0095  138 HIS   B CA  
5814 C  C   . HIS   B 138 ? 0.1838 0.1395 0.2560 -0.0033 0.0339  0.0168  138 HIS   B C   
5815 O  O   . HIS   B 138 ? 0.1721 0.1440 0.2736 0.0036  0.0330  0.0313  138 HIS   B O   
5816 C  CB  . HIS   B 138 ? 0.2191 0.1586 0.2846 -0.0094 0.0466  0.0108  138 HIS   B CB  
5817 C  CG  . HIS   B 138 ? 0.2387 0.1757 0.2783 -0.0100 0.0527  0.0284  138 HIS   B CG  
5818 N  ND1 . HIS   B 138 ? 0.2481 0.1938 0.3021 -0.0077 0.0626  0.0270  138 HIS   B ND1 
5819 C  CD2 . HIS   B 138 ? 0.2544 0.1874 0.2691 -0.0135 0.0611  0.0210  138 HIS   B CD2 
5820 C  CE1 . HIS   B 138 ? 0.2537 0.1926 0.2963 -0.0069 0.0674  0.0271  138 HIS   B CE1 
5821 N  NE2 . HIS   B 138 ? 0.2610 0.1817 0.2724 0.0001  0.0672  0.0203  138 HIS   B NE2 
5829 N  N   . SER   B 139 ? 0.1799 0.1247 0.2551 0.0030  0.0281  0.0013  139 SER   B N   
5830 C  CA  . SER   B 139 ? 0.1740 0.1208 0.2417 0.0031  0.0246  0.0009  139 SER   B CA  
5831 C  C   . SER   B 139 ? 0.1511 0.1183 0.2360 0.0005  0.0180  -0.0007 139 SER   B C   
5832 O  O   . SER   B 139 ? 0.1514 0.1201 0.2400 0.0048  0.0042  0.0058  139 SER   B O   
5833 C  CB  . SER   B 139 ? 0.1839 0.1194 0.2417 0.0035  0.0106  0.0054  139 SER   B CB  
5834 O  OG  . SER   B 139 ? 0.1815 0.1254 0.2495 0.0025  -0.0078 0.0086  139 SER   B OG  
5840 N  N   . LEU   B 140 ? 0.1534 0.1163 0.2279 -0.0039 0.0161  -0.0022 140 LEU   B N   
5841 C  CA  . LEU   B 140 ? 0.1485 0.1196 0.2396 -0.0019 0.0089  0.0026  140 LEU   B CA  
5842 C  C   . LEU   B 140 ? 0.1419 0.1146 0.2489 -0.0034 0.0086  -0.0072 140 LEU   B C   
5843 O  O   . LEU   B 140 ? 0.1444 0.1249 0.2427 0.0014  0.0027  0.0015  140 LEU   B O   
5844 C  CB  . LEU   B 140 ? 0.1460 0.1207 0.2472 -0.0059 0.0156  -0.0069 140 LEU   B CB  
5845 C  CG  . LEU   B 140 ? 0.1625 0.1230 0.2457 -0.0103 0.0101  0.0041  140 LEU   B CG  
5846 C  CD1 . LEU   B 140 ? 0.1756 0.1319 0.2556 -0.0116 0.0096  0.0005  140 LEU   B CD1 
5847 C  CD2 . LEU   B 140 ? 0.1786 0.1398 0.2425 -0.0094 -0.0001 -0.0084 140 LEU   B CD2 
5859 N  N   . ARG   B 141 ? 0.1367 0.1219 0.2654 -0.0099 0.0139  -0.0077 141 ARG   B N   
5860 C  CA  . ARG   B 141 ? 0.1383 0.1220 0.2965 -0.0149 0.0213  -0.0046 141 ARG   B CA  
5861 C  C   . ARG   B 141 ? 0.1374 0.1237 0.2780 -0.0151 0.0190  0.0011  141 ARG   B C   
5862 O  O   . ARG   B 141 ? 0.1426 0.1258 0.2716 -0.0125 0.0006  -0.0065 141 ARG   B O   
5863 C  CB  . ARG   B 141 ? 0.1579 0.1344 0.3273 -0.0201 0.0307  -0.0023 141 ARG   B CB  
5864 C  CG  . ARG   B 141 ? 0.1912 0.1616 0.3490 -0.0268 0.0241  0.0037  141 ARG   B CG  
5865 C  CD  . ARG   B 141 ? 0.2355 0.1817 0.3474 -0.0171 0.0131  -0.0078 141 ARG   B CD  
5866 N  NE  . ARG   B 141 ? 0.2602 0.1834 0.3426 -0.0317 0.0267  -0.0117 141 ARG   B NE  
5867 C  CZ  . ARG   B 141 ? 0.2764 0.1694 0.3291 -0.0255 0.0401  -0.0226 141 ARG   B CZ  
5868 N  NH1 . ARG   B 141 ? 0.2859 0.1614 0.3242 -0.0199 0.0434  -0.0277 141 ARG   B NH1 
5869 N  NH2 . ARG   B 141 ? 0.2859 0.1785 0.3376 -0.0117 0.0274  -0.0160 141 ARG   B NH2 
5883 N  N   . VAL   B 142 ? 0.1406 0.1219 0.2666 -0.0123 0.0187  -0.0031 142 VAL   B N   
5884 C  CA  . VAL   B 142 ? 0.1380 0.1181 0.2613 -0.0066 0.0186  -0.0071 142 VAL   B CA  
5885 C  C   . VAL   B 142 ? 0.1391 0.1175 0.2593 -0.0092 0.0125  -0.0098 142 VAL   B C   
5886 O  O   . VAL   B 142 ? 0.1476 0.1164 0.2636 0.0017  0.0238  -0.0017 142 VAL   B O   
5887 C  CB  . VAL   B 142 ? 0.1498 0.1329 0.2655 -0.0024 0.0248  0.0085  142 VAL   B CB  
5888 C  CG1 . VAL   B 142 ? 0.1474 0.1292 0.2686 0.0089  0.0218  0.0054  142 VAL   B CG1 
5889 C  CG2 . VAL   B 142 ? 0.1723 0.1337 0.2675 -0.0013 0.0160  0.0148  142 VAL   B CG2 
5899 N  N   . CYS   B 143 ? 0.1321 0.1237 0.2361 -0.0034 0.0092  0.0043  143 CYS   B N   
5900 C  CA  . CYS   B 143 ? 0.1307 0.1233 0.2376 -0.0076 0.0042  0.0027  143 CYS   B CA  
5901 C  C   . CYS   B 143 ? 0.1262 0.1214 0.2367 -0.0075 0.0130  -0.0047 143 CYS   B C   
5902 O  O   . CYS   B 143 ? 0.1376 0.1253 0.2376 -0.0070 0.0013  -0.0042 143 CYS   B O   
5903 C  CB  . CYS   B 143 ? 0.1373 0.1319 0.2344 -0.0070 0.0057  0.0033  143 CYS   B CB  
5904 S  SG  . CYS   B 143 ? 0.1419 0.1469 0.2243 -0.0036 0.0103  0.0053  143 CYS   B SG  
5910 N  N   . VAL   B 144 ? 0.1346 0.1231 0.2460 -0.0059 0.0090  -0.0091 144 VAL   B N   
5911 C  CA  . VAL   B 144 ? 0.1414 0.1297 0.2664 -0.0102 -0.0012 -0.0205 144 VAL   B CA  
5912 C  C   . VAL   B 144 ? 0.1377 0.1316 0.2742 -0.0122 -0.0044 -0.0008 144 VAL   B C   
5913 O  O   . VAL   B 144 ? 0.1477 0.1518 0.2876 0.0015  -0.0072 0.0162  144 VAL   B O   
5914 C  CB  . VAL   B 144 ? 0.1640 0.1507 0.3268 -0.0066 -0.0160 -0.0269 144 VAL   B CB  
5915 C  CG1 . VAL   B 144 ? 0.1898 0.1876 0.3657 0.0004  -0.0199 -0.0246 144 VAL   B CG1 
5916 C  CG2 . VAL   B 144 ? 0.1749 0.1507 0.3224 0.0014  -0.0279 -0.0365 144 VAL   B CG2 
5926 N  N   . ASP   B 145 ? 0.1403 0.1263 0.2828 -0.0070 -0.0015 -0.0135 145 ASP   B N   
5927 C  CA  . ASP   B 145 ? 0.1362 0.1310 0.2973 -0.0052 0.0090  -0.0140 145 ASP   B CA  
5928 C  C   . ASP   B 145 ? 0.1344 0.1346 0.2852 -0.0049 0.0133  -0.0143 145 ASP   B C   
5929 O  O   . ASP   B 145 ? 0.1359 0.1506 0.3370 -0.0085 0.0165  -0.0283 145 ASP   B O   
5930 C  CB  . ASP   B 145 ? 0.1538 0.1408 0.3349 -0.0152 0.0183  -0.0095 145 ASP   B CB  
5931 C  CG  . ASP   B 145 ? 0.1678 0.1420 0.3696 -0.0252 0.0266  -0.0041 145 ASP   B CG  
5932 O  OD1 . ASP   B 145 ? 0.1725 0.1486 0.3805 -0.0251 0.0007  -0.0145 145 ASP   B OD1 
5933 O  OD2 . ASP   B 145 ? 0.2000 0.1565 0.4138 -0.0264 0.0497  0.0081  145 ASP   B OD2 
5938 N  N   . THR   B 146 ? 0.1300 0.1239 0.2513 -0.0083 0.0062  -0.0054 146 THR   B N   
5939 C  CA  . THR   B 146 ? 0.1401 0.1219 0.2340 -0.0067 0.0104  -0.0079 146 THR   B CA  
5940 C  C   . THR   B 146 ? 0.1359 0.1187 0.2235 -0.0042 0.0050  -0.0018 146 THR   B C   
5941 O  O   . THR   B 146 ? 0.1386 0.1204 0.2223 -0.0068 -0.0015 0.0006  146 THR   B O   
5942 C  CB  . THR   B 146 ? 0.1421 0.1245 0.2432 -0.0005 0.0188  -0.0020 146 THR   B CB  
5943 O  OG1 . THR   B 146 ? 0.1415 0.1197 0.2502 -0.0094 0.0177  0.0070  146 THR   B OG1 
5944 C  CG2 . THR   B 146 ? 0.1537 0.1300 0.2310 -0.0018 0.0180  0.0003  146 THR   B CG2 
5952 N  N   . VAL   B 147 ? 0.1388 0.1246 0.2117 -0.0016 0.0103  0.0028  147 VAL   B N   
5953 C  CA  . VAL   B 147 ? 0.1363 0.1223 0.2113 -0.0116 0.0024  0.0003  147 VAL   B CA  
5954 C  C   . VAL   B 147 ? 0.1358 0.1240 0.2253 -0.0149 -0.0089 -0.0068 147 VAL   B C   
5955 O  O   . VAL   B 147 ? 0.1492 0.1333 0.2288 -0.0187 -0.0302 -0.0087 147 VAL   B O   
5956 C  CB  . VAL   B 147 ? 0.1415 0.1400 0.2018 -0.0057 -0.0006 0.0078  147 VAL   B CB  
5957 C  CG1 . VAL   B 147 ? 0.1404 0.1525 0.1948 -0.0131 0.0007  0.0002  147 VAL   B CG1 
5958 C  CG2 . VAL   B 147 ? 0.1437 0.1370 0.2080 -0.0070 0.0040  0.0074  147 VAL   B CG2 
5968 N  N   . ARG   B 148 ? 0.1382 0.1244 0.2216 -0.0076 -0.0171 -0.0131 148 ARG   B N   
5969 C  CA  . ARG   B 148 ? 0.1400 0.1335 0.2127 -0.0068 -0.0236 -0.0134 148 ARG   B CA  
5970 C  C   . ARG   B 148 ? 0.1480 0.1420 0.1988 -0.0048 -0.0192 -0.0023 148 ARG   B C   
5971 O  O   . ARG   B 148 ? 0.1683 0.1707 0.1962 -0.0219 -0.0263 0.0049  148 ARG   B O   
5972 C  CB  . ARG   B 148 ? 0.1458 0.1447 0.2166 -0.0032 -0.0276 -0.0158 148 ARG   B CB  
5973 C  CG  . ARG   B 148 ? 0.1477 0.1560 0.2272 -0.0093 -0.0266 -0.0337 148 ARG   B CG  
5974 C  CD  . ARG   B 148 ? 0.1566 0.1695 0.2298 0.0043  -0.0198 -0.0290 148 ARG   B CD  
5975 N  NE  . ARG   B 148 ? 0.1565 0.1642 0.2149 0.0189  -0.0236 -0.0290 148 ARG   B NE  
5976 C  CZ  . ARG   B 148 ? 0.1501 0.1579 0.2009 0.0137  -0.0167 -0.0172 148 ARG   B CZ  
5977 N  NH1 . ARG   B 148 ? 0.1411 0.1586 0.2148 -0.0076 -0.0003 -0.0141 148 ARG   B NH1 
5978 N  NH2 . ARG   B 148 ? 0.1747 0.1439 0.2033 0.0119  -0.0142 -0.0021 148 ARG   B NH2 
5992 N  N   . THR   B 149 ? 0.1525 0.1386 0.1994 -0.0101 -0.0216 0.0020  149 THR   B N   
5993 C  CA  . THR   B 149 ? 0.1545 0.1411 0.1921 -0.0131 -0.0233 0.0068  149 THR   B CA  
5994 C  C   . THR   B 149 ? 0.1543 0.1346 0.1931 -0.0142 -0.0230 0.0058  149 THR   B C   
5995 O  O   . THR   B 149 ? 0.1620 0.1349 0.2051 -0.0194 -0.0105 -0.0006 149 THR   B O   
5996 C  CB  . THR   B 149 ? 0.1554 0.1356 0.1975 -0.0113 -0.0250 -0.0025 149 THR   B CB  
5997 O  OG1 . THR   B 149 ? 0.1622 0.1444 0.1832 -0.0232 -0.0284 0.0003  149 THR   B OG1 
5998 C  CG2 . THR   B 149 ? 0.1570 0.1404 0.2110 -0.0079 -0.0169 -0.0045 149 THR   B CG2 
6006 N  N   . ASN   B 150 ? 0.1612 0.1327 0.1866 -0.0139 -0.0280 0.0010  150 ASN   B N   
6007 C  CA  . ASN   B 150 ? 0.1645 0.1491 0.1774 -0.0191 -0.0264 -0.0052 150 ASN   B CA  
6008 C  C   . ASN   B 150 ? 0.1543 0.1421 0.1831 -0.0134 -0.0274 -0.0076 150 ASN   B C   
6009 O  O   . ASN   B 150 ? 0.1616 0.1389 0.2089 -0.0213 -0.0443 -0.0010 150 ASN   B O   
6010 C  CB  . ASN   B 150 ? 0.1897 0.1885 0.1873 -0.0233 -0.0378 0.0139  150 ASN   B CB  
6011 C  CG  . ASN   B 150 ? 0.2156 0.2277 0.2203 -0.0271 -0.0384 0.0271  150 ASN   B CG  
6012 O  OD1 . ASN   B 150 ? 0.2278 0.2427 0.2364 -0.0348 -0.0579 0.0230  150 ASN   B OD1 
6013 N  ND2 . ASN   B 150 ? 0.2272 0.2458 0.2533 -0.0156 -0.0424 0.0622  150 ASN   B ND2 
6020 N  N   . VAL   B 151 ? 0.1505 0.1393 0.1818 -0.0164 -0.0235 -0.0013 151 VAL   B N   
6021 C  CA  . VAL   B 151 ? 0.1483 0.1454 0.1823 -0.0224 -0.0224 -0.0022 151 VAL   B CA  
6022 C  C   . VAL   B 151 ? 0.1528 0.1350 0.1781 -0.0312 -0.0176 -0.0071 151 VAL   B C   
6023 O  O   . VAL   B 151 ? 0.1601 0.1434 0.1958 -0.0269 -0.0109 -0.0155 151 VAL   B O   
6024 C  CB  . VAL   B 151 ? 0.1684 0.1636 0.1861 -0.0094 -0.0207 0.0014  151 VAL   B CB  
6025 C  CG1 . VAL   B 151 ? 0.1775 0.1654 0.2106 -0.0196 -0.0094 -0.0121 151 VAL   B CG1 
6026 C  CG2 . VAL   B 151 ? 0.1785 0.1784 0.1707 0.0053  -0.0117 0.0125  151 VAL   B CG2 
6036 N  N   . TYR   B 152 ? 0.1473 0.1241 0.1805 -0.0254 -0.0179 -0.0067 152 TYR   B N   
6037 C  CA  . TYR   B 152 ? 0.1534 0.1470 0.1717 -0.0221 -0.0046 -0.0057 152 TYR   B CA  
6038 C  C   . TYR   B 152 ? 0.1457 0.1312 0.1579 -0.0178 -0.0031 -0.0067 152 TYR   B C   
6039 O  O   . TYR   B 152 ? 0.1503 0.1337 0.1779 -0.0251 -0.0099 0.0000  152 TYR   B O   
6040 C  CB  . TYR   B 152 ? 0.1645 0.1579 0.1739 -0.0210 -0.0084 0.0077  152 TYR   B CB  
6041 C  CG  . TYR   B 152 ? 0.1782 0.1646 0.1683 -0.0344 -0.0118 0.0065  152 TYR   B CG  
6042 C  CD1 . TYR   B 152 ? 0.1869 0.1734 0.1533 -0.0239 -0.0247 0.0043  152 TYR   B CD1 
6043 C  CD2 . TYR   B 152 ? 0.1960 0.1813 0.1735 -0.0315 -0.0083 -0.0034 152 TYR   B CD2 
6044 C  CE1 . TYR   B 152 ? 0.2031 0.1894 0.1744 -0.0198 -0.0281 0.0243  152 TYR   B CE1 
6045 C  CE2 . TYR   B 152 ? 0.2077 0.2022 0.1662 -0.0317 -0.0166 -0.0093 152 TYR   B CE2 
6046 C  CZ  . TYR   B 152 ? 0.2122 0.2113 0.1601 -0.0316 -0.0351 0.0194  152 TYR   B CZ  
6047 O  OH  . TYR   B 152 ? 0.2362 0.2455 0.1912 -0.0228 -0.0325 0.0198  152 TYR   B OH  
6057 N  N   . LEU   B 153 ? 0.1492 0.1281 0.1736 -0.0242 -0.0070 -0.0054 153 LEU   B N   
6058 C  CA  . LEU   B 153 ? 0.1522 0.1243 0.1664 -0.0193 -0.0005 -0.0097 153 LEU   B CA  
6059 C  C   . LEU   B 153 ? 0.1517 0.1245 0.1777 -0.0215 0.0003  -0.0155 153 LEU   B C   
6060 O  O   . LEU   B 153 ? 0.1599 0.1470 0.1966 -0.0165 -0.0066 -0.0360 153 LEU   B O   
6061 C  CB  . LEU   B 153 ? 0.1557 0.1199 0.1796 -0.0223 0.0030  -0.0046 153 LEU   B CB  
6062 C  CG  . LEU   B 153 ? 0.1504 0.1348 0.2035 -0.0203 0.0002  -0.0033 153 LEU   B CG  
6063 C  CD1 . LEU   B 153 ? 0.1583 0.1486 0.2100 -0.0250 0.0118  0.0025  153 LEU   B CD1 
6064 C  CD2 . LEU   B 153 ? 0.1549 0.1451 0.2164 -0.0282 0.0112  0.0000  153 LEU   B CD2 
6076 N  N   . ALA   B 154 ? 0.1480 0.1250 0.1843 -0.0066 -0.0109 -0.0115 154 ALA   B N   
6077 C  CA  . ALA   B 154 ? 0.1601 0.1367 0.1983 -0.0013 -0.0112 -0.0186 154 ALA   B CA  
6078 C  C   . ALA   B 154 ? 0.1711 0.1384 0.2007 0.0040  -0.0206 -0.0256 154 ALA   B C   
6079 O  O   . ALA   B 154 ? 0.1996 0.1388 0.2142 0.0052  -0.0083 -0.0143 154 ALA   B O   
6080 C  CB  . ALA   B 154 ? 0.1569 0.1536 0.2223 -0.0062 -0.0113 -0.0291 154 ALA   B CB  
6086 N  N   . VAL   B 155 ? 0.1454 0.1313 0.2060 -0.0035 -0.0020 -0.0155 155 VAL   B N   
6087 C  CA  . VAL   B 155 ? 0.1407 0.1319 0.2225 -0.0001 -0.0080 -0.0093 155 VAL   B CA  
6088 C  C   . VAL   B 155 ? 0.1400 0.1300 0.2173 -0.0038 -0.0050 -0.0214 155 VAL   B C   
6089 O  O   . VAL   B 155 ? 0.1609 0.1507 0.2473 -0.0007 -0.0072 -0.0396 155 VAL   B O   
6090 C  CB  . VAL   B 155 ? 0.1469 0.1451 0.2591 -0.0057 -0.0127 0.0051  155 VAL   B CB  
6091 C  CG1 . VAL   B 155 ? 0.1479 0.1434 0.2601 -0.0108 -0.0099 0.0012  155 VAL   B CG1 
6092 C  CG2 . VAL   B 155 ? 0.1427 0.1525 0.2861 -0.0034 -0.0115 0.0270  155 VAL   B CG2 
6102 N  N   . PHE   B 156 ? 0.1322 0.1396 0.2325 0.0017  -0.0021 -0.0107 156 PHE   B N   
6103 C  CA  . PHE   B 156 ? 0.1355 0.1498 0.2703 0.0037  -0.0015 -0.0175 156 PHE   B CA  
6104 C  C   . PHE   B 156 ? 0.1348 0.1575 0.2939 0.0140  -0.0104 -0.0348 156 PHE   B C   
6105 O  O   . PHE   B 156 ? 0.1623 0.1722 0.3162 0.0271  0.0025  -0.0364 156 PHE   B O   
6106 C  CB  . PHE   B 156 ? 0.1449 0.1487 0.2821 -0.0029 -0.0150 -0.0084 156 PHE   B CB  
6107 C  CG  . PHE   B 156 ? 0.1435 0.1567 0.2963 -0.0030 -0.0174 0.0081  156 PHE   B CG  
6108 C  CD1 . PHE   B 156 ? 0.1488 0.1792 0.3301 0.0027  -0.0088 0.0407  156 PHE   B CD1 
6109 C  CD2 . PHE   B 156 ? 0.1484 0.1662 0.2953 0.0084  -0.0228 0.0100  156 PHE   B CD2 
6110 C  CE1 . PHE   B 156 ? 0.1511 0.1946 0.3423 0.0017  -0.0079 0.0441  156 PHE   B CE1 
6111 C  CE2 . PHE   B 156 ? 0.1550 0.1874 0.3096 0.0077  -0.0254 0.0180  156 PHE   B CE2 
6112 C  CZ  . PHE   B 156 ? 0.1470 0.1931 0.3348 0.0134  -0.0188 0.0300  156 PHE   B CZ  
6122 N  N   . ASP   B 157 ? 0.1416 0.1483 0.3156 0.0099  -0.0208 -0.0192 157 ASP   B N   
6123 C  CA  . ASP   B 157 ? 0.1484 0.1500 0.3455 0.0043  -0.0252 -0.0249 157 ASP   B CA  
6124 C  C   . ASP   B 157 ? 0.1486 0.1493 0.3485 0.0077  -0.0235 -0.0441 157 ASP   B C   
6125 O  O   . ASP   B 157 ? 0.1367 0.1491 0.3290 0.0017  -0.0165 -0.0335 157 ASP   B O   
6126 C  CB  . ASP   B 157 ? 0.1727 0.1688 0.3575 0.0030  -0.0408 -0.0145 157 ASP   B CB  
6127 C  CG  . ASP   B 157 ? 0.1982 0.1829 0.3766 -0.0004 -0.0213 -0.0144 157 ASP   B CG  
6128 O  OD1 . ASP   B 157 ? 0.2041 0.1768 0.3952 0.0139  -0.0125 -0.0099 157 ASP   B OD1 
6129 O  OD2 . ASP   B 157 ? 0.2304 0.2051 0.4094 -0.0064 -0.0024 -0.0095 157 ASP   B OD2 
6134 N  N   . LYS   B 158 ? 0.1478 0.1753 0.3617 0.0094  -0.0120 -0.0658 158 LYS   B N   
6135 C  CA  . LYS   B 158 ? 0.1631 0.1884 0.3639 0.0051  0.0011  -0.0795 158 LYS   B CA  
6136 C  C   . LYS   B 158 ? 0.1650 0.1761 0.3718 0.0054  -0.0040 -0.0739 158 LYS   B C   
6137 O  O   . LYS   B 158 ? 0.1679 0.1732 0.3859 -0.0037 -0.0101 -0.0820 158 LYS   B O   
6138 C  CB  . LYS   B 158 ? 0.1904 0.2283 0.3689 0.0087  0.0123  -0.0943 158 LYS   B CB  
6139 C  CG  . LYS   B 158 ? 0.2248 0.2658 0.3725 0.0147  0.0198  -0.1001 158 LYS   B CG  
6140 C  CD  . LYS   B 158 ? 0.2494 0.3065 0.3858 0.0122  0.0243  -0.0922 158 LYS   B CD  
6141 C  CE  . LYS   B 158 ? 0.2681 0.3381 0.3974 0.0146  0.0253  -0.0872 158 LYS   B CE  
6142 N  NZ  . LYS   B 158 ? 0.2670 0.3499 0.3961 0.0137  0.0269  -0.0839 158 LYS   B NZ  
6156 N  N   . ASN   B 159 ? 0.1686 0.1659 0.3881 0.0062  -0.0154 -0.0592 159 ASN   B N   
6157 C  CA  . ASN   B 159 ? 0.1825 0.1613 0.4022 0.0176  -0.0313 -0.0472 159 ASN   B CA  
6158 C  C   . ASN   B 159 ? 0.1643 0.1472 0.3909 0.0155  -0.0436 -0.0394 159 ASN   B C   
6159 O  O   . ASN   B 159 ? 0.1711 0.1444 0.3982 0.0014  -0.0452 -0.0319 159 ASN   B O   
6160 C  CB  . ASN   B 159 ? 0.2060 0.1744 0.4302 0.0241  -0.0359 -0.0414 159 ASN   B CB  
6161 C  CG  . ASN   B 159 ? 0.2341 0.1959 0.4564 0.0275  -0.0463 -0.0506 159 ASN   B CG  
6162 O  OD1 . ASN   B 159 ? 0.2480 0.2080 0.4596 0.0378  -0.0472 -0.0620 159 ASN   B OD1 
6163 N  ND2 . ASN   B 159 ? 0.2371 0.2009 0.4678 0.0377  -0.0583 -0.0441 159 ASN   B ND2 
6170 N  N   . LEU   B 160 ? 0.1520 0.1416 0.3701 0.0093  -0.0391 -0.0322 160 LEU   B N   
6171 C  CA  . LEU   B 160 ? 0.1525 0.1514 0.3320 0.0084  -0.0303 -0.0170 160 LEU   B CA  
6172 C  C   . LEU   B 160 ? 0.1479 0.1395 0.3240 0.0018  -0.0244 -0.0303 160 LEU   B C   
6173 O  O   . LEU   B 160 ? 0.1398 0.1435 0.3175 -0.0018 -0.0243 -0.0248 160 LEU   B O   
6174 C  CB  . LEU   B 160 ? 0.1495 0.1571 0.3016 0.0080  -0.0325 -0.0130 160 LEU   B CB  
6175 C  CG  . LEU   B 160 ? 0.1541 0.1685 0.2747 0.0085  -0.0284 -0.0019 160 LEU   B CG  
6176 C  CD1 . LEU   B 160 ? 0.1696 0.1882 0.2708 -0.0034 -0.0158 -0.0063 160 LEU   B CD1 
6177 C  CD2 . LEU   B 160 ? 0.1586 0.1718 0.2703 0.0228  -0.0255 -0.0135 160 LEU   B CD2 
6189 N  N   . TYR   B 161 ? 0.1477 0.1408 0.3266 -0.0025 -0.0026 -0.0385 161 TYR   B N   
6190 C  CA  . TYR   B 161 ? 0.1539 0.1387 0.3168 -0.0094 0.0121  -0.0425 161 TYR   B CA  
6191 C  C   . TYR   B 161 ? 0.1572 0.1427 0.3062 -0.0086 0.0105  -0.0335 161 TYR   B C   
6192 O  O   . TYR   B 161 ? 0.1641 0.1429 0.2950 -0.0138 0.0037  -0.0336 161 TYR   B O   
6193 C  CB  . TYR   B 161 ? 0.1689 0.1489 0.3172 -0.0165 0.0297  -0.0440 161 TYR   B CB  
6194 C  CG  . TYR   B 161 ? 0.1874 0.1507 0.3075 -0.0265 0.0327  -0.0483 161 TYR   B CG  
6195 C  CD1 . TYR   B 161 ? 0.1954 0.1462 0.3061 -0.0395 0.0341  -0.0427 161 TYR   B CD1 
6196 C  CD2 . TYR   B 161 ? 0.2082 0.1577 0.2920 -0.0241 0.0293  -0.0491 161 TYR   B CD2 
6197 C  CE1 . TYR   B 161 ? 0.2116 0.1685 0.3094 -0.0409 0.0290  -0.0469 161 TYR   B CE1 
6198 C  CE2 . TYR   B 161 ? 0.2286 0.1811 0.2995 -0.0293 0.0299  -0.0481 161 TYR   B CE2 
6199 C  CZ  . TYR   B 161 ? 0.2246 0.1821 0.3048 -0.0417 0.0227  -0.0432 161 TYR   B CZ  
6200 O  OH  . TYR   B 161 ? 0.2548 0.2090 0.3276 -0.0399 0.0236  -0.0393 161 TYR   B OH  
6210 N  N   . ASP   B 162 ? 0.1595 0.1441 0.3135 -0.0086 -0.0037 -0.0414 162 ASP   B N   
6211 C  CA  . ASP   B 162 ? 0.1700 0.1544 0.3154 -0.0101 -0.0051 -0.0414 162 ASP   B CA  
6212 C  C   . ASP   B 162 ? 0.1670 0.1414 0.3085 -0.0115 -0.0086 -0.0402 162 ASP   B C   
6213 O  O   . ASP   B 162 ? 0.1754 0.1453 0.3098 -0.0169 -0.0163 -0.0345 162 ASP   B O   
6214 C  CB  . ASP   B 162 ? 0.1875 0.1725 0.3382 0.0011  -0.0087 -0.0594 162 ASP   B CB  
6215 C  CG  . ASP   B 162 ? 0.1925 0.1968 0.3567 0.0091  -0.0067 -0.0751 162 ASP   B CG  
6216 O  OD1 . ASP   B 162 ? 0.1926 0.2180 0.3448 0.0059  0.0115  -0.0743 162 ASP   B OD1 
6217 O  OD2 . ASP   B 162 ? 0.2074 0.2137 0.3869 0.0243  -0.0005 -0.0749 162 ASP   B OD2 
6222 N  N   . LYS   B 163 ? 0.1673 0.1349 0.3045 -0.0090 -0.0241 -0.0281 163 LYS   B N   
6223 C  CA  . LYS   B 163 ? 0.1778 0.1421 0.3115 -0.0158 -0.0187 -0.0096 163 LYS   B CA  
6224 C  C   . LYS   B 163 ? 0.1498 0.1397 0.2992 -0.0195 -0.0157 -0.0009 163 LYS   B C   
6225 O  O   . LYS   B 163 ? 0.1454 0.1473 0.3238 -0.0234 -0.0140 0.0005  163 LYS   B O   
6226 C  CB  . LYS   B 163 ? 0.2202 0.1797 0.3473 -0.0100 -0.0210 0.0076  163 LYS   B CB  
6227 C  CG  . LYS   B 163 ? 0.2910 0.2613 0.4082 -0.0104 -0.0148 0.0159  163 LYS   B CG  
6228 C  CD  . LYS   B 163 ? 0.3558 0.3343 0.4694 -0.0172 -0.0176 0.0111  163 LYS   B CD  
6229 C  CE  . LYS   B 163 ? 0.4049 0.3864 0.5091 -0.0239 -0.0157 0.0086  163 LYS   B CE  
6230 N  NZ  . LYS   B 163 ? 0.4337 0.4239 0.5395 -0.0272 -0.0146 0.0037  163 LYS   B NZ  
6244 N  N   . LEU   B 164 ? 0.1377 0.1338 0.2782 -0.0142 -0.0109 0.0033  164 LEU   B N   
6245 C  CA  . LEU   B 164 ? 0.1432 0.1333 0.2688 -0.0096 -0.0149 0.0032  164 LEU   B CA  
6246 C  C   . LEU   B 164 ? 0.1475 0.1354 0.2632 -0.0095 -0.0280 -0.0023 164 LEU   B C   
6247 O  O   . LEU   B 164 ? 0.1506 0.1505 0.2775 -0.0132 -0.0259 -0.0026 164 LEU   B O   
6248 C  CB  . LEU   B 164 ? 0.1397 0.1313 0.2542 -0.0077 -0.0138 0.0022  164 LEU   B CB  
6249 C  CG  . LEU   B 164 ? 0.1462 0.1479 0.2547 -0.0076 -0.0082 0.0024  164 LEU   B CG  
6250 C  CD1 . LEU   B 164 ? 0.1519 0.1475 0.2434 -0.0155 -0.0250 -0.0004 164 LEU   B CD1 
6251 C  CD2 . LEU   B 164 ? 0.1615 0.1844 0.2720 -0.0071 0.0103  -0.0167 164 LEU   B CD2 
6263 N  N   . VAL   B 165 ? 0.1744 0.1482 0.2747 -0.0152 -0.0275 -0.0121 165 VAL   B N   
6264 C  CA  . VAL   B 165 ? 0.2056 0.1521 0.2702 -0.0274 -0.0410 -0.0122 165 VAL   B CA  
6265 C  C   . VAL   B 165 ? 0.2303 0.1592 0.3016 -0.0366 -0.0709 -0.0061 165 VAL   B C   
6266 O  O   . VAL   B 165 ? 0.2470 0.1717 0.3108 -0.0401 -0.0767 0.0053  165 VAL   B O   
6267 C  CB  . VAL   B 165 ? 0.2268 0.1683 0.2703 -0.0108 -0.0143 -0.0230 165 VAL   B CB  
6268 C  CG1 . VAL   B 165 ? 0.2423 0.1727 0.2977 -0.0142 -0.0057 -0.0188 165 VAL   B CG1 
6269 C  CG2 . VAL   B 165 ? 0.2193 0.1734 0.2644 -0.0093 -0.0078 -0.0131 165 VAL   B CG2 
6279 N  N   . SER   B 166 ? 0.2384 0.1506 0.3303 -0.0350 -0.0769 -0.0248 166 SER   B N   
6280 C  CA  . SER   B 166 ? 0.2313 0.1549 0.3752 -0.0358 -0.0618 -0.0309 166 SER   B CA  
6281 C  C   . SER   B 166 ? 0.2161 0.1644 0.3897 -0.0380 -0.0640 -0.0088 166 SER   B C   
6282 O  O   . SER   B 166 ? 0.2151 0.1879 0.4218 -0.0457 -0.0799 -0.0322 166 SER   B O   
6283 C  CB  . SER   B 166 ? 0.2315 0.1659 0.3991 -0.0273 -0.0506 -0.0377 166 SER   B CB  
6284 O  OG  . SER   B 166 ? 0.2271 0.1626 0.4111 -0.0226 -0.0478 -0.0233 166 SER   B OG  
6290 N  N   . SER   B 167 ? 0.2009 0.1649 0.3623 -0.0392 -0.0690 0.0274  167 SER   B N   
6291 C  CA  . SER   B 167 ? 0.1976 0.1689 0.3499 -0.0339 -0.0425 0.0248  167 SER   B CA  
6292 C  C   . SER   B 167 ? 0.1909 0.1754 0.3319 -0.0435 -0.0355 0.0436  167 SER   B C   
6293 O  O   . SER   B 167 ? 0.1946 0.1865 0.3212 -0.0457 -0.0291 0.0398  167 SER   B O   
6294 C  CB  . SER   B 167 ? 0.1875 0.1731 0.3476 -0.0320 -0.0194 0.0163  167 SER   B CB  
6295 O  OG  . SER   B 167 ? 0.1853 0.1834 0.3360 -0.0222 -0.0070 0.0095  167 SER   B OG  
6301 N  N   . PHE   B 168 ? 0.1902 0.1701 0.3242 -0.0404 -0.0234 0.0447  168 PHE   B N   
6302 C  CA  . PHE   B 168 ? 0.2015 0.1634 0.3016 -0.0454 -0.0248 0.0263  168 PHE   B CA  
6303 C  C   . PHE   B 168 ? 0.1758 0.1529 0.2637 -0.0242 -0.0041 0.0121  168 PHE   B C   
6304 O  O   . PHE   B 168 ? 0.2092 0.1448 0.2687 0.0025  -0.0092 -0.0019 168 PHE   B O   
6305 C  CB  . PHE   B 168 ? 0.2128 0.1697 0.3048 -0.0542 -0.0449 0.0400  168 PHE   B CB  
6306 C  CG  . PHE   B 168 ? 0.2399 0.1560 0.2978 -0.0561 -0.0474 0.0230  168 PHE   B CG  
6307 C  CD1 . PHE   B 168 ? 0.2739 0.1626 0.2992 -0.0493 -0.0569 0.0173  168 PHE   B CD1 
6308 C  CD2 . PHE   B 168 ? 0.2238 0.1526 0.2899 -0.0513 -0.0435 0.0331  168 PHE   B CD2 
6309 C  CE1 . PHE   B 168 ? 0.2861 0.1713 0.2969 -0.0339 -0.0544 0.0190  168 PHE   B CE1 
6310 C  CE2 . PHE   B 168 ? 0.2539 0.1629 0.3027 -0.0320 -0.0494 0.0284  168 PHE   B CE2 
6311 C  CZ  . PHE   B 168 ? 0.2731 0.1598 0.2986 -0.0245 -0.0581 0.0292  168 PHE   B CZ  
6321 N  N   . LEU   B 169 ? 0.1691 0.1689 0.2609 -0.0074 0.0020  0.0043  169 LEU   B N   
6322 C  CA  . LEU   B 169 ? 0.1900 0.1982 0.2888 -0.0151 0.0053  -0.0202 169 LEU   B CA  
6323 C  C   . LEU   B 169 ? 0.2201 0.2208 0.3293 0.0046  -0.0030 -0.0465 169 LEU   B C   
6324 O  O   . LEU   B 169 ? 0.2448 0.2384 0.3825 -0.0005 -0.0016 -0.0699 169 LEU   B O   
6325 C  CB  . LEU   B 169 ? 0.2115 0.2424 0.3052 -0.0197 -0.0007 0.0113  169 LEU   B CB  
6326 C  CG  . LEU   B 169 ? 0.2524 0.2808 0.3416 -0.0035 -0.0037 0.0198  169 LEU   B CG  
6327 C  CD1 . LEU   B 169 ? 0.2679 0.3021 0.3447 -0.0013 -0.0121 0.0370  169 LEU   B CD1 
6328 C  CD2 . LEU   B 169 ? 0.2493 0.2890 0.3475 0.0141  0.0104  0.0083  169 LEU   B CD2 
6329 O  OXT . LEU   B 169 ? 0.2375 0.2334 0.3186 0.0337  -0.0048 -0.0424 169 LEU   B OXT 
6341 N  N2  B A1BAV C .   ? 0.1106 0.1904 0.1650 -0.0102 0.0037  -0.0005 201 A1BAV A N2  
6342 C  C3  B A1BAV C .   ? 0.0722 0.1780 0.1669 -0.0167 0.0153  0.0171  201 A1BAV A C3  
6343 C  C6  B A1BAV C .   ? 0.1086 0.1906 0.1718 -0.0044 -0.0066 -0.0063 201 A1BAV A C6  
6344 C  C9  B A1BAV C .   ? 0.1384 0.1851 0.2047 -0.0006 0.0091  0.0028  201 A1BAV A C9  
6345 C  C12 B A1BAV C .   ? 0.1319 0.1850 0.2011 -0.0036 0.0152  0.0071  201 A1BAV A C12 
6346 C  C1  B A1BAV C .   ? 0.1069 0.1858 0.1693 0.0067  0.0069  0.0138  201 A1BAV A C1  
6347 C  C10 B A1BAV C .   ? 0.1468 0.1907 0.2134 0.0010  0.0060  0.0016  201 A1BAV A C10 
6348 C  C11 B A1BAV C .   ? 0.1353 0.1888 0.2002 0.0014  0.0107  0.0123  201 A1BAV A C11 
6349 C  C13 B A1BAV C .   ? 0.1031 0.1878 0.1647 -0.0018 0.0052  0.0018  201 A1BAV A C13 
6350 C  C2  B A1BAV C .   ? 0.0972 0.1866 0.1686 -0.0026 0.0140  0.0095  201 A1BAV A C2  
6351 C  C4  B A1BAV C .   ? 0.1016 0.1880 0.1598 -0.0032 0.0019  0.0026  201 A1BAV A C4  
6352 C  C5  B A1BAV C .   ? 0.1071 0.1935 0.1687 -0.0089 -0.0067 -0.0122 201 A1BAV A C5  
6353 C  C7  B A1BAV C .   ? 0.1055 0.1772 0.1823 -0.0046 0.0126  0.0070  201 A1BAV A C7  
6354 C  C8  B A1BAV C .   ? 0.1277 0.1803 0.1925 -0.0060 0.0103  0.0041  201 A1BAV A C8  
6355 N  N1  B A1BAV C .   ? 0.0910 0.1882 0.1655 0.0001  -0.0035 0.0051  201 A1BAV A N1  
6356 N  N3  B A1BAV C .   ? 0.1028 0.1924 0.1733 -0.0095 -0.0103 -0.0154 201 A1BAV A N3  
6357 N  N4  B A1BAV C .   ? 0.1108 0.1852 0.1777 -0.0035 -0.0010 0.0050  201 A1BAV A N4  
6358 O  O1  B A1BAV C .   ? 0.1464 0.1758 0.1838 -0.0039 -0.0046 -0.0016 201 A1BAV A O1  
6359 O  O2  B A1BAV C .   ? 0.1451 0.1938 0.2106 0.0047  -0.0012 0.0050  201 A1BAV A O2  
6378 CL CL  B CL    D .   ? 0.2120 0.1513 0.2011 -0.0299 0.0460  -0.0038 202 CL    A CL  
6379 O  O   . HOH   E .   ? 0.2080 0.1751 0.2335 0.0212  -0.0203 -0.0081 301 HOH   A O   
6380 O  O   . HOH   E .   ? 0.2554 0.2226 0.3519 -0.0265 0.0798  0.0538  302 HOH   A O   
6381 O  O   . HOH   E .   ? 0.4148 0.7342 0.4658 -0.1168 0.0874  0.0141  303 HOH   A O   
6382 O  O   . HOH   E .   ? 0.1766 0.1638 0.2302 0.0128  -0.0150 0.0317  304 HOH   A O   
6383 O  O   . HOH   E .   ? 0.3732 0.2297 0.3609 -0.0056 -0.0426 0.0536  305 HOH   A O   
6384 O  O   . HOH   E .   ? 0.6674 0.5241 0.3870 -0.1059 0.0494  0.1649  306 HOH   A O   
6385 O  O   . HOH   E .   ? 0.3090 0.6864 0.5444 -0.0257 -0.0680 0.2231  307 HOH   A O   
6386 O  O   . HOH   E .   ? 0.5837 0.4642 0.3266 0.1546  -0.1032 0.0599  308 HOH   A O   
6387 O  O   . HOH   E .   ? 0.2982 0.5378 0.6063 0.0889  0.0592  0.0962  309 HOH   A O   
6388 O  O   . HOH   E .   ? 0.4395 0.3467 0.5725 -0.0235 0.1832  -0.0580 310 HOH   A O   
6389 O  O   . HOH   E .   ? 0.2347 0.5713 0.4084 -0.0340 -0.0513 0.1326  311 HOH   A O   
6390 O  O   . HOH   E .   ? 0.7544 0.2979 0.4841 -0.0238 -0.1266 0.0718  312 HOH   A O   
6391 O  O   . HOH   E .   ? 0.5927 0.4820 0.4178 -0.1043 0.1446  0.1180  313 HOH   A O   
6392 O  O   . HOH   E .   ? 0.2881 0.4694 0.5973 -0.0345 0.1031  0.2343  314 HOH   A O   
6393 O  O   . HOH   E .   ? 0.3102 0.3326 0.1661 -0.0419 0.0483  0.0393  315 HOH   A O   
6394 O  O   . HOH   E .   ? 0.5089 0.3154 0.4716 -0.0508 0.1385  0.0633  316 HOH   A O   
6395 O  O   . HOH   E .   ? 0.4805 0.3191 0.4081 0.1092  -0.0360 -0.0132 317 HOH   A O   
6396 O  O   . HOH   E .   ? 0.1966 0.1907 0.3680 -0.0374 0.0111  -0.0225 318 HOH   A O   
6397 O  O   . HOH   E .   ? 0.2597 0.2358 0.4056 -0.0197 -0.0742 0.0806  319 HOH   A O   
6398 O  O   . HOH   E .   ? 0.6654 0.5901 0.3853 -0.0511 -0.0615 0.1282  320 HOH   A O   
6399 O  O   . HOH   E .   ? 0.1927 0.3357 0.4751 -0.0270 0.0435  -0.1250 321 HOH   A O   
6400 O  O   . HOH   E .   ? 0.3263 0.4454 0.2618 -0.0202 0.0513  0.0617  322 HOH   A O   
6401 O  O   . HOH   E .   ? 0.4545 0.3590 0.3637 -0.0676 -0.1052 -0.0355 323 HOH   A O   
6402 O  O   . HOH   E .   ? 0.2061 0.1787 0.2778 -0.0008 -0.0566 -0.0108 324 HOH   A O   
6403 O  O   . HOH   E .   ? 0.1861 0.2546 0.3070 0.0156  -0.0132 -0.0267 325 HOH   A O   
6404 O  O   . HOH   E .   ? 0.3202 0.3302 0.3642 -0.0856 0.1199  -0.0215 326 HOH   A O   
6405 O  O   . HOH   E .   ? 0.2761 0.2740 0.2859 -0.0709 0.0266  0.0477  327 HOH   A O   
6406 O  O   . HOH   E .   ? 0.1530 0.1516 0.2137 -0.0160 0.0105  0.0055  328 HOH   A O   
6407 O  O   . HOH   E .   ? 0.5061 0.5735 0.4056 -0.1154 -0.0976 -0.0717 329 HOH   A O   
6408 O  O   . HOH   E .   ? 0.2123 0.4194 0.4039 -0.0160 -0.0483 0.1782  330 HOH   A O   
6409 O  O   . HOH   E .   ? 0.2497 0.2261 0.2839 0.0386  0.0391  0.0356  331 HOH   A O   
6410 O  O   . HOH   E .   ? 0.4919 0.5471 0.2385 -0.1093 0.1174  0.0670  332 HOH   A O   
6411 O  O   . HOH   E .   ? 0.3303 0.1707 0.2159 0.0171  0.0369  0.0220  333 HOH   A O   
6412 O  O   . HOH   E .   ? 0.1473 0.3871 0.3003 -0.0220 0.0111  0.0718  334 HOH   A O   
6413 O  O   . HOH   E .   ? 0.4956 0.5066 0.4059 0.0145  -0.0557 -0.0939 335 HOH   A O   
6414 O  O   . HOH   E .   ? 0.3092 0.3586 0.3605 -0.0916 -0.0657 -0.0438 336 HOH   A O   
6415 O  O   . HOH   E .   ? 0.1548 0.2135 0.2219 0.0075  -0.0015 0.0507  337 HOH   A O   
6416 O  O   . HOH   E .   ? 0.1571 0.2407 0.2490 0.0307  0.0414  0.0691  338 HOH   A O   
6417 O  O   . HOH   E .   ? 0.4971 0.1952 0.4846 0.0571  0.0260  0.0214  339 HOH   A O   
6418 O  O   . HOH   E .   ? 0.4044 0.2250 0.4912 0.0229  -0.1664 0.0777  340 HOH   A O   
6419 O  O   . HOH   E .   ? 0.3640 0.4404 0.3749 0.2030  0.0713  0.0577  341 HOH   A O   
6420 O  O   . HOH   E .   ? 0.6090 0.6755 0.5489 0.0778  -0.0603 0.1850  342 HOH   A O   
6421 O  O   . HOH   E .   ? 0.5319 0.3831 0.4395 -0.1842 -0.0502 0.1853  343 HOH   A O   
6422 O  O   . HOH   E .   ? 0.6937 0.4930 0.5210 0.1413  0.2134  -0.1052 344 HOH   A O   
6423 O  O   . HOH   E .   ? 0.1497 0.1743 0.2913 0.0030  -0.0386 -0.0501 345 HOH   A O   
6424 O  O   . HOH   E .   ? 0.4720 0.3051 0.2918 -0.1174 0.0266  0.0611  346 HOH   A O   
6425 O  O   . HOH   E .   ? 0.2017 0.1993 0.3870 0.0187  0.0903  -0.0131 347 HOH   A O   
6426 O  O   . HOH   E .   ? 0.2031 0.1646 0.1604 -0.0013 0.0152  0.0167  348 HOH   A O   
6427 O  O   . HOH   E .   ? 0.1480 0.1899 0.2626 0.0096  -0.0173 0.0128  349 HOH   A O   
6428 O  O   . HOH   E .   ? 0.2844 0.4269 0.3129 -0.0494 0.0399  0.0162  350 HOH   A O   
6429 O  O   . HOH   E .   ? 0.5619 0.4002 0.2931 0.0246  0.0623  0.1245  351 HOH   A O   
6430 O  O   . HOH   E .   ? 0.2602 0.3866 0.3597 0.1012  -0.0598 -0.0170 352 HOH   A O   
6431 O  O   . HOH   E .   ? 0.5620 0.4568 0.5919 -0.1080 0.0456  0.0942  353 HOH   A O   
6432 O  O   . HOH   E .   ? 0.2621 0.4131 0.3001 0.0468  0.0527  0.1561  354 HOH   A O   
6433 O  O   . HOH   E .   ? 0.2504 0.1963 0.2410 -0.0292 0.0089  -0.0065 355 HOH   A O   
6434 O  O   . HOH   E .   ? 0.3573 0.2708 0.2693 -0.0271 -0.0218 0.0147  356 HOH   A O   
6435 O  O   . HOH   E .   ? 0.1535 0.1287 0.2311 -0.0056 0.0152  -0.0124 357 HOH   A O   
6436 O  O   . HOH   E .   ? 0.4870 0.4592 0.5003 0.1506  0.1511  -0.0496 358 HOH   A O   
6437 O  O   . HOH   E .   ? 0.1893 0.1893 0.2715 -0.0343 0.0081  0.0333  359 HOH   A O   
6438 O  O   . HOH   E .   ? 0.1352 0.1278 0.1531 -0.0025 0.0075  0.0099  360 HOH   A O   
6439 O  O   . HOH   E .   ? 0.2768 0.3254 0.5221 -0.0519 -0.1041 -0.0979 361 HOH   A O   
6440 O  O   . HOH   E .   ? 0.1874 0.2389 0.3512 0.0240  0.0739  -0.0487 362 HOH   A O   
6441 O  O   . HOH   E .   ? 0.2506 0.3362 0.3929 0.0591  0.0529  0.0281  363 HOH   A O   
6442 O  O   . HOH   E .   ? 0.3880 0.2220 0.4059 -0.1047 0.0918  0.0110  364 HOH   A O   
6443 O  O   . HOH   E .   ? 0.2887 0.2228 0.4743 -0.0550 -0.0246 0.0285  365 HOH   A O   
6444 O  O   . HOH   E .   ? 0.6334 0.3807 0.5536 0.0759  -0.0975 0.0405  366 HOH   A O   
6445 O  O   . HOH   E .   ? 0.1388 0.1515 0.1706 -0.0049 -0.0101 -0.0051 367 HOH   A O   
6446 O  O   . HOH   E .   ? 0.3017 0.2585 0.3635 -0.0066 -0.0421 0.0882  368 HOH   A O   
6447 O  O   . HOH   E .   ? 0.4004 0.6784 0.4704 -0.0671 -0.1146 0.0395  369 HOH   A O   
6448 O  O   . HOH   E .   ? 0.2758 0.3246 0.2446 -0.0712 -0.0246 -0.0516 370 HOH   A O   
6449 O  O   . HOH   E .   ? 0.2085 0.2201 0.2252 -0.0252 -0.0453 0.0295  371 HOH   A O   
6450 O  O   . HOH   E .   ? 0.4974 0.2598 0.4286 -0.1560 0.1923  -0.0733 372 HOH   A O   
6451 O  O   A HOH   E .   ? 0.2292 0.3642 0.2538 0.0955  -0.0058 -0.0034 373 HOH   A O   
6452 O  O   . HOH   E .   ? 0.3892 0.3069 0.3683 -0.1303 -0.0279 -0.0061 374 HOH   A O   
6453 O  O   . HOH   E .   ? 0.4070 0.2187 0.2101 0.1247  0.0435  0.0170  375 HOH   A O   
6454 O  O   . HOH   E .   ? 0.2973 0.2775 0.2325 0.0443  0.0658  0.0121  376 HOH   A O   
6455 O  O   . HOH   E .   ? 0.2087 0.4225 0.3691 -0.0213 0.0037  0.1025  377 HOH   A O   
6456 O  O   . HOH   E .   ? 0.1994 0.1748 0.1855 0.0067  0.0119  0.0235  378 HOH   A O   
6457 O  O   . HOH   E .   ? 0.1697 0.2141 0.1868 -0.0086 0.0053  0.0567  379 HOH   A O   
6458 O  O   . HOH   E .   ? 0.2679 0.2533 0.4253 -0.0662 0.1292  -0.0265 380 HOH   A O   
6459 O  O   . HOH   E .   ? 0.6208 0.5964 0.3813 0.2159  -0.0699 -0.0710 381 HOH   A O   
6460 O  O   . HOH   E .   ? 0.1732 0.1690 0.2227 -0.0194 0.0129  0.0314  382 HOH   A O   
6461 O  O   . HOH   E .   ? 0.1366 0.1428 0.1938 0.0006  -0.0077 0.0075  383 HOH   A O   
6462 O  O   . HOH   E .   ? 0.6398 0.5948 0.5434 -0.0233 0.0527  -0.0110 384 HOH   A O   
6463 O  O   . HOH   E .   ? 0.5849 0.7003 0.5852 0.0994  -0.0601 0.0423  385 HOH   A O   
6464 O  O   . HOH   E .   ? 0.2583 0.1901 0.2122 -0.0505 0.0328  0.0236  386 HOH   A O   
6465 O  O   . HOH   E .   ? 0.4897 0.5142 0.5643 -0.1085 -0.0383 0.1112  387 HOH   A O   
6466 O  O   . HOH   E .   ? 0.1514 0.1698 0.1870 0.0030  -0.0256 0.0032  388 HOH   A O   
6467 O  O   . HOH   E .   ? 0.2573 0.6194 0.3658 0.0891  0.0233  -0.1052 389 HOH   A O   
6468 O  O   . HOH   E .   ? 0.2058 0.2182 0.3361 0.0141  -0.0400 0.0283  390 HOH   A O   
6469 O  O   . HOH   E .   ? 0.1880 0.1855 0.3849 0.0356  0.1052  0.0914  391 HOH   A O   
6470 O  O   . HOH   E .   ? 0.3208 0.2801 0.2468 -0.0758 -0.1067 0.0460  392 HOH   A O   
6471 O  O   . HOH   E .   ? 0.3742 0.5790 0.4254 -0.0766 0.0150  0.1311  393 HOH   A O   
6472 O  O   . HOH   E .   ? 0.2518 0.3958 0.3564 -0.0294 0.1007  -0.0580 394 HOH   A O   
6473 O  O   . HOH   E .   ? 0.2338 0.2340 0.2778 0.0262  0.0062  0.0917  395 HOH   A O   
6474 O  O   . HOH   E .   ? 0.2800 0.2819 0.3581 -0.0042 0.1022  -0.0135 396 HOH   A O   
6475 O  O   . HOH   E .   ? 0.1720 0.2631 0.3819 -0.0264 0.0611  0.0508  397 HOH   A O   
6476 O  O   . HOH   E .   ? 0.1367 0.1722 0.1933 0.0072  -0.0243 -0.0262 398 HOH   A O   
6477 O  O   . HOH   E .   ? 0.5144 0.4407 0.2026 0.0243  0.1152  0.0795  399 HOH   A O   
6478 O  O   . HOH   E .   ? 0.3440 0.5963 0.5136 0.0609  0.0088  0.1408  400 HOH   A O   
6479 O  O   . HOH   E .   ? 0.1841 0.2018 0.2593 -0.0097 -0.0040 0.0730  401 HOH   A O   
6480 O  O   . HOH   E .   ? 0.3392 0.3359 0.4669 0.1018  0.0772  -0.0570 402 HOH   A O   
6481 O  O   A HOH   E .   ? 0.3057 0.2028 0.4254 -0.0082 0.1139  -0.0056 403 HOH   A O   
6482 O  O   . HOH   E .   ? 0.1721 0.1426 0.1784 -0.0183 0.0076  0.0081  404 HOH   A O   
6483 O  O   . HOH   E .   ? 0.2532 0.2761 0.3223 -0.0041 -0.0292 -0.0457 405 HOH   A O   
6484 O  O   . HOH   E .   ? 0.2080 0.1656 0.2831 0.0028  -0.0316 0.0097  406 HOH   A O   
6485 O  O   . HOH   E .   ? 0.4365 0.6152 0.3455 -0.0906 -0.0286 0.1504  407 HOH   A O   
6486 O  O   . HOH   E .   ? 0.2660 0.3910 0.7053 -0.0260 0.1153  -0.0433 408 HOH   A O   
6487 O  O   . HOH   E .   ? 0.2357 0.1787 0.2639 -0.0030 0.0092  0.0183  409 HOH   A O   
6488 O  O   . HOH   E .   ? 0.3355 0.3746 0.3156 0.1283  -0.0610 -0.0921 410 HOH   A O   
6489 O  O   . HOH   E .   ? 0.1867 0.2502 0.3861 -0.0140 -0.0310 0.0100  411 HOH   A O   
6490 O  O   . HOH   E .   ? 0.2538 0.2163 0.2833 -0.0593 -0.0178 0.0634  412 HOH   A O   
6491 O  O   . HOH   E .   ? 0.1504 0.1612 0.2729 -0.0015 0.0088  0.0151  413 HOH   A O   
6492 O  O   . HOH   E .   ? 0.3294 0.1379 0.2096 0.0026  -0.0374 0.0083  414 HOH   A O   
6493 O  O   . HOH   E .   ? 0.2808 0.6225 0.1712 -0.0645 0.0387  -0.0133 415 HOH   A O   
6494 O  O   . HOH   E .   ? 0.4189 0.2171 0.5047 -0.0774 -0.2305 0.0917  416 HOH   A O   
6495 O  O   . HOH   E .   ? 0.3598 0.3578 0.2760 0.0039  -0.1186 0.0478  417 HOH   A O   
6496 O  O   . HOH   E .   ? 0.5745 0.4886 0.5586 -0.1080 -0.0695 -0.1426 418 HOH   A O   
6497 O  O   . HOH   E .   ? 0.3937 0.2742 0.5780 0.0777  0.0874  0.0428  419 HOH   A O   
6498 O  O   . HOH   E .   ? 0.2282 0.2684 0.2604 0.0047  -0.0569 0.0393  420 HOH   A O   
6499 O  O   . HOH   E .   ? 0.2915 0.3643 0.5490 -0.0011 0.1126  -0.0285 421 HOH   A O   
6500 O  O   . HOH   E .   ? 0.6957 0.4038 0.5163 0.1926  -0.0686 0.1363  422 HOH   A O   
6501 O  O   . HOH   E .   ? 0.2174 0.4212 0.2482 0.1376  -0.0074 0.0177  423 HOH   A O   
6502 O  O   . HOH   E .   ? 0.4916 0.4789 0.3202 -0.0090 -0.1359 0.0284  424 HOH   A O   
6503 O  O   . HOH   E .   ? 0.1658 0.2101 0.3009 -0.0184 -0.0081 0.0605  425 HOH   A O   
6504 O  O   . HOH   E .   ? 0.2307 0.2799 0.4440 0.0219  -0.0668 -0.0841 426 HOH   A O   
6505 O  O   . HOH   E .   ? 0.1842 0.1912 0.3006 0.0246  -0.0406 0.0294  427 HOH   A O   
6506 O  O   A HOH   E .   ? 0.3333 0.2408 0.3793 0.0384  0.0908  0.1079  428 HOH   A O   
6507 O  O   . HOH   E .   ? 0.5424 0.6251 0.3987 0.0808  0.2155  -0.0934 429 HOH   A O   
6508 O  O   . HOH   E .   ? 0.4774 0.5835 0.5969 -0.1651 0.0364  -0.0848 430 HOH   A O   
6509 O  O   . HOH   E .   ? 0.2050 0.1544 0.1670 0.0041  -0.0082 -0.0085 431 HOH   A O   
6510 O  O   . HOH   E .   ? 0.6429 0.6414 0.5732 0.0117  -0.1281 0.0779  432 HOH   A O   
6511 O  O   . HOH   E .   ? 0.1845 0.2163 0.5511 -0.0268 -0.0882 0.0584  433 HOH   A O   
6512 O  O   . HOH   E .   ? 0.3533 0.2565 0.1863 -0.0684 0.0332  0.0260  434 HOH   A O   
6513 O  O   . HOH   E .   ? 0.8963 0.8931 0.6536 -0.0364 0.0005  -0.0989 435 HOH   A O   
6514 O  O   A HOH   E .   ? 0.1939 0.1553 0.2555 0.0249  -0.0720 -0.0317 436 HOH   A O   
6515 O  O   . HOH   E .   ? 0.2483 0.1703 0.2579 0.0066  0.0125  0.0137  437 HOH   A O   
6516 O  O   . HOH   E .   ? 0.2506 0.2173 0.3957 0.0206  0.0287  0.0048  438 HOH   A O   
6517 O  O   . HOH   E .   ? 0.3437 0.3216 0.3276 0.1651  -0.0690 -0.0671 439 HOH   A O   
6518 O  O   . HOH   E .   ? 0.2368 0.1998 0.2703 0.0155  0.0314  0.0095  440 HOH   A O   
6519 O  O   . HOH   E .   ? 0.7229 0.7158 0.4162 0.2297  -0.1110 0.1688  441 HOH   A O   
6520 O  O   . HOH   E .   ? 0.6234 0.4300 0.6948 0.1363  -0.0453 -0.1201 442 HOH   A O   
6521 O  O   . HOH   E .   ? 0.2174 0.2587 0.2342 0.0112  -0.0038 -0.0415 443 HOH   A O   
6522 O  O   . HOH   E .   ? 0.4192 0.4109 0.4936 -0.1175 -0.0755 -0.1024 444 HOH   A O   
6523 O  O   . HOH   E .   ? 0.5843 0.5110 0.7604 0.0970  -0.1353 0.1547  445 HOH   A O   
6524 O  O   . HOH   E .   ? 0.4818 0.4062 0.3956 0.0463  -0.0599 0.1129  446 HOH   A O   
6525 O  O   . HOH   E .   ? 0.5675 0.3263 0.3925 0.0057  -0.0106 0.1355  447 HOH   A O   
6526 O  O   A HOH   E .   ? 0.2476 0.2344 0.3970 0.0527  0.1035  0.1363  448 HOH   A O   
6527 O  O   . HOH   E .   ? 0.2215 0.2730 0.3305 0.0403  -0.0043 0.0501  449 HOH   A O   
6528 O  O   . HOH   E .   ? 0.5140 0.3406 0.4663 0.0564  0.0821  0.0301  450 HOH   A O   
6529 O  O   . HOH   E .   ? 0.3172 0.2872 0.3054 -0.0688 0.0185  -0.0737 451 HOH   A O   
6530 O  O   . HOH   E .   ? 0.6776 0.4529 0.5145 0.1814  0.2704  0.1929  452 HOH   A O   
6531 O  O   . HOH   E .   ? 0.6771 0.5759 0.4859 -0.0513 0.1432  0.0640  453 HOH   A O   
6532 O  O   . HOH   E .   ? 0.2717 0.3926 0.3952 -0.0380 -0.0203 -0.0200 454 HOH   A O   
6533 O  O   . HOH   E .   ? 0.6488 0.7971 0.4699 -0.0399 -0.1110 -0.0028 455 HOH   A O   
6534 O  O   . HOH   E .   ? 0.2952 0.5107 0.5097 -0.1447 0.0695  -0.1814 456 HOH   A O   
6535 O  O   . HOH   E .   ? 0.3326 0.5254 0.4721 0.1056  -0.0464 0.1688  457 HOH   A O   
6536 O  O   . HOH   E .   ? 0.2881 0.1797 0.2535 0.0416  -0.0793 -0.0228 458 HOH   A O   
6537 O  O   . HOH   E .   ? 0.4133 0.5734 0.3932 -0.0912 -0.0748 0.1875  459 HOH   A O   
6538 O  O   . HOH   E .   ? 0.2267 0.2554 0.3166 -0.0627 0.0236  -0.0185 460 HOH   A O   
6539 O  O   . HOH   E .   ? 0.2780 0.2170 0.5558 0.0443  -0.1214 0.0022  461 HOH   A O   
6540 O  O   . HOH   E .   ? 0.2948 0.4070 0.4909 0.0686  0.0328  -0.1621 462 HOH   A O   
6541 O  O   . HOH   E .   ? 0.6232 0.3258 0.7455 0.0999  0.0892  0.2186  463 HOH   A O   
6542 O  O   . HOH   E .   ? 0.2748 0.2267 0.3894 -0.0008 0.0634  0.0122  464 HOH   A O   
6543 O  O   . HOH   E .   ? 0.5516 0.4879 0.4355 0.0275  0.0855  0.0679  465 HOH   A O   
6544 O  O   . HOH   E .   ? 0.4214 0.5444 0.3660 0.0557  -0.0637 -0.0588 466 HOH   A O   
6545 O  O   . HOH   E .   ? 0.5497 0.5854 0.5581 -0.1664 -0.0984 0.1159  467 HOH   A O   
6546 O  O   . HOH   E .   ? 0.4647 0.4175 0.5011 -0.2012 -0.0209 -0.0506 468 HOH   A O   
6547 O  O   . HOH   E .   ? 0.6682 0.4893 0.6085 -0.1230 0.0376  -0.0656 469 HOH   A O   
6548 O  O   . HOH   E .   ? 0.4576 0.3938 0.3524 -0.0629 -0.0525 -0.0264 470 HOH   A O   
6549 O  O   . HOH   E .   ? 0.2402 0.2101 0.2785 0.0193  0.0069  -0.0047 471 HOH   A O   
6550 O  O   . HOH   E .   ? 0.5370 0.5768 0.4712 0.1301  -0.1294 -0.1271 472 HOH   A O   
6551 O  O   . HOH   E .   ? 0.4042 0.2704 0.3366 -0.0576 -0.1139 0.0617  473 HOH   A O   
6552 O  O   . HOH   E .   ? 0.7661 0.3703 0.3323 -0.0443 -0.1131 -0.0161 474 HOH   A O   
6553 O  O   . HOH   E .   ? 0.4169 0.5149 0.2891 -0.0459 -0.0185 0.0418  475 HOH   A O   
6554 O  O   . HOH   E .   ? 0.5444 0.4342 0.3904 0.0278  0.0643  -0.1328 476 HOH   A O   
6555 O  O   . HOH   E .   ? 0.2857 0.5734 0.3604 0.1415  0.1062  0.2409  477 HOH   A O   
6556 O  O   . HOH   E .   ? 0.2706 0.4443 0.4639 0.0044  0.0858  0.1417  478 HOH   A O   
6557 O  O   . HOH   E .   ? 0.5580 0.6786 0.4449 -0.0384 0.1320  0.0849  479 HOH   A O   
6558 O  O   . HOH   E .   ? 0.5716 0.3955 0.4146 -0.0106 0.1412  0.0041  480 HOH   A O   
6559 O  O   . HOH   E .   ? 0.5295 0.4664 0.5083 -0.0878 -0.1308 0.0260  481 HOH   A O   
6560 O  O   . HOH   E .   ? 0.6360 0.5471 0.4529 -0.0661 -0.0761 -0.0751 482 HOH   A O   
6561 O  O   . HOH   E .   ? 0.2576 0.2558 0.6597 -0.0140 -0.1297 0.0424  483 HOH   A O   
6562 O  O   . HOH   E .   ? 0.5271 0.3312 0.4632 -0.0208 0.2742  0.0088  484 HOH   A O   
6563 O  O   . HOH   E .   ? 0.2963 0.4870 0.3448 -0.0418 -0.0263 -0.0745 485 HOH   A O   
6564 O  O   . HOH   E .   ? 0.4370 0.3733 0.2787 -0.0777 0.1187  -0.0345 486 HOH   A O   
6565 O  O   . HOH   E .   ? 0.2940 0.2036 0.5242 0.0142  0.0694  0.0807  487 HOH   A O   
6566 O  O   . HOH   E .   ? 0.5303 0.5425 0.6060 0.0481  0.1402  -0.1094 488 HOH   A O   
6567 O  O   . HOH   E .   ? 0.6294 0.2690 0.4194 -0.1005 0.0449  0.0693  489 HOH   A O   
6568 O  O   . HOH   E .   ? 0.2420 0.2912 0.4712 -0.0035 0.0949  -0.0304 490 HOH   A O   
6569 O  O   . HOH   E .   ? 0.3683 0.2805 0.4211 -0.0778 0.0468  0.0580  491 HOH   A O   
6570 O  O   . HOH   E .   ? 0.3715 0.8306 0.5118 -0.0910 0.0137  0.2631  492 HOH   A O   
6571 O  O   . HOH   E .   ? 0.2417 0.2907 0.3475 0.0434  -0.0569 0.0416  493 HOH   A O   
6572 O  O   . HOH   E .   ? 0.5953 0.5347 0.5361 0.1104  -0.1584 0.0574  494 HOH   A O   
6573 O  O   . HOH   E .   ? 0.4681 0.2311 0.4553 -0.1277 0.0076  0.0196  495 HOH   A O   
6574 O  O   . HOH   E .   ? 0.2837 0.4021 0.4050 0.0688  -0.0125 0.0472  496 HOH   A O   
6575 O  O   . HOH   E .   ? 0.5305 0.6876 0.4934 0.0701  -0.0676 0.0931  497 HOH   A O   
6576 O  O   . HOH   E .   ? 0.5832 0.4120 0.5733 -0.0695 0.0665  0.0320  498 HOH   A O   
6577 O  O   . HOH   E .   ? 0.3969 0.7825 0.3740 0.0482  0.1437  0.0685  499 HOH   A O   
6578 O  O   . HOH   E .   ? 0.4364 0.6718 0.4950 0.2717  0.0030  0.1294  500 HOH   A O   
6579 O  O   . HOH   E .   ? 0.2794 0.2293 0.4266 0.0047  0.0301  0.0399  501 HOH   A O   
6580 O  O   . HOH   E .   ? 0.4552 0.5138 0.4632 0.0031  -0.0452 -0.1288 502 HOH   A O   
6581 O  O   . HOH   E .   ? 0.2554 0.6796 0.3240 0.0485  0.0228  0.0245  503 HOH   A O   
6582 O  O   . HOH   E .   ? 0.4113 0.4978 0.3231 0.1274  -0.0534 0.0871  504 HOH   A O   
6583 O  O   . HOH   E .   ? 0.4582 0.5990 0.5373 -0.0390 -0.0843 0.0181  505 HOH   A O   
6584 O  O   . HOH   E .   ? 0.3116 0.3823 0.5413 -0.0330 -0.0738 0.2145  506 HOH   A O   
6585 O  O   . HOH   F .   ? 0.2397 0.2132 0.3022 0.0253  0.0757  0.0260  201 HOH   B O   
6586 O  O   . HOH   F .   ? 0.4012 0.3049 0.3478 -0.0894 0.0374  -0.0917 202 HOH   B O   
6587 O  O   . HOH   F .   ? 0.5619 0.5501 0.2648 0.1082  -0.0847 -0.1396 203 HOH   B O   
6588 O  O   . HOH   F .   ? 0.2948 0.5821 0.4745 -0.0119 0.1388  -0.2104 204 HOH   B O   
6589 O  O   . HOH   F .   ? 0.3583 0.6783 0.3758 0.0605  0.0095  0.2252  205 HOH   B O   
6590 O  O   . HOH   F .   ? 0.5352 0.3914 0.5963 0.0508  -0.1075 0.2477  206 HOH   B O   
6591 O  O   . HOH   F .   ? 0.3846 0.2895 0.6009 -0.0308 0.0673  -0.0053 207 HOH   B O   
6592 O  O   . HOH   F .   ? 0.4591 0.5805 0.3810 0.2848  -0.0945 -0.0192 208 HOH   B O   
6593 O  O   . HOH   F .   ? 0.6991 0.3501 0.4990 -0.0010 0.1968  0.0103  209 HOH   B O   
6594 O  O   . HOH   F .   ? 0.6119 0.6219 0.5404 0.2199  0.0394  0.0345  210 HOH   B O   
6595 O  O   . HOH   F .   ? 0.2857 0.2821 0.6722 0.0641  -0.1077 0.0424  211 HOH   B O   
6596 O  O   . HOH   F .   ? 0.1935 0.2280 0.3080 0.0049  0.0269  -0.0205 212 HOH   B O   
6597 O  O   . HOH   F .   ? 0.4177 0.4358 0.4163 0.2170  -0.0442 0.0292  213 HOH   B O   
6598 O  O   . HOH   F .   ? 0.4098 0.4197 0.5064 -0.1441 0.0277  -0.1253 214 HOH   B O   
6599 O  O   . HOH   F .   ? 0.1669 0.1887 0.2647 -0.0220 -0.0116 0.0056  215 HOH   B O   
6600 O  O   . HOH   F .   ? 0.4005 0.3766 0.6611 -0.0228 -0.1718 -0.0595 216 HOH   B O   
6601 O  O   . HOH   F .   ? 0.5764 0.3145 0.4180 -0.1725 0.0312  0.0168  217 HOH   B O   
6602 O  O   . HOH   F .   ? 0.3066 0.2495 0.5632 -0.0268 0.0747  0.0064  218 HOH   B O   
6603 O  O   . HOH   F .   ? 0.4020 0.3920 0.4997 -0.1713 0.0365  0.0677  219 HOH   B O   
6604 O  O   . HOH   F .   ? 0.4992 0.3839 0.3484 -0.0379 -0.0912 0.0517  220 HOH   B O   
6605 O  O   . HOH   F .   ? 0.3098 0.2054 0.5415 0.0155  0.1955  0.0842  221 HOH   B O   
6606 O  O   . HOH   F .   ? 0.4818 0.1910 0.3195 0.0001  -0.0966 0.0148  222 HOH   B O   
6607 O  O   . HOH   F .   ? 0.4451 0.4538 0.4400 0.0454  0.1364  -0.0811 223 HOH   B O   
6608 O  O   . HOH   F .   ? 0.3244 0.3525 0.4919 0.0486  -0.1130 -0.0166 224 HOH   B O   
6609 O  O   . HOH   F .   ? 0.1687 0.2051 0.3040 -0.0106 -0.0014 -0.0036 225 HOH   B O   
6610 O  O   . HOH   F .   ? 0.4236 0.6697 0.3865 0.2327  0.0218  -0.0676 226 HOH   B O   
6611 O  O   . HOH   F .   ? 0.3070 0.5398 0.4823 0.1954  -0.0026 -0.0764 227 HOH   B O   
6612 O  O   . HOH   F .   ? 0.3616 0.3412 0.2153 0.0462  0.0596  0.0459  228 HOH   B O   
6613 O  O   . HOH   F .   ? 0.4983 0.6487 0.3311 0.0404  -0.0213 0.0105  229 HOH   B O   
6614 O  O   . HOH   F .   ? 0.2593 0.1775 0.3021 -0.0316 0.1067  -0.0060 230 HOH   B O   
6615 O  O   . HOH   F .   ? 0.3109 0.2246 0.3927 0.0079  0.1477  0.0229  231 HOH   B O   
6616 O  O   . HOH   F .   ? 0.2186 0.2169 0.3771 -0.0260 -0.0077 -0.0600 232 HOH   B O   
6617 O  O   . HOH   F .   ? 0.2778 0.3670 0.3580 -0.0850 0.0531  -0.0244 233 HOH   B O   
6618 O  O   . HOH   F .   ? 0.2653 0.2360 0.3296 0.0318  0.0202  -0.0707 234 HOH   B O   
6619 O  O   . HOH   F .   ? 0.6849 0.4326 0.5053 0.1298  -0.0140 -0.1137 235 HOH   B O   
6620 O  O   . HOH   F .   ? 0.3730 0.2356 0.3998 0.0637  -0.0531 -0.0727 236 HOH   B O   
6621 O  O   . HOH   F .   ? 0.2265 0.3983 0.3056 -0.0476 -0.0556 -0.0581 237 HOH   B O   
6622 O  O   . HOH   F .   ? 0.2954 0.4675 0.3339 -0.1179 -0.0230 -0.0717 238 HOH   B O   
6623 O  O   . HOH   F .   ? 0.2125 0.2235 0.2896 -0.0454 0.0013  -0.0206 239 HOH   B O   
6624 O  O   . HOH   F .   ? 0.3198 0.1891 0.2178 0.0139  -0.0659 -0.0120 240 HOH   B O   
6625 O  O   . HOH   F .   ? 0.1495 0.1413 0.1724 -0.0119 -0.0076 -0.0015 241 HOH   B O   
6626 O  O   . HOH   F .   ? 0.2128 0.1358 0.3496 0.0118  -0.0629 -0.0205 242 HOH   B O   
6627 O  O   . HOH   F .   ? 0.5102 0.2756 0.2786 0.0173  0.0846  -0.0142 243 HOH   B O   
6628 O  O   . HOH   F .   ? 0.1566 0.1469 0.2537 -0.0067 -0.0022 -0.0043 244 HOH   B O   
6629 O  O   . HOH   F .   ? 0.3057 0.1755 0.6043 -0.0120 -0.1382 -0.0337 245 HOH   B O   
6630 O  O   . HOH   F .   ? 0.2119 0.4108 0.2293 -0.0669 -0.0153 0.0614  246 HOH   B O   
6631 O  O   . HOH   F .   ? 0.2887 0.2461 0.2824 0.0952  0.0721  0.0059  247 HOH   B O   
6632 O  O   . HOH   F .   ? 0.1435 0.1352 0.1714 -0.0041 -0.0064 0.0073  248 HOH   B O   
6633 O  O   . HOH   F .   ? 0.2202 0.1997 0.2164 -0.0282 -0.0445 0.0114  249 HOH   B O   
6634 O  O   . HOH   F .   ? 0.3823 0.3295 0.4000 0.0855  -0.1126 -0.1600 250 HOH   B O   
6635 O  O   . HOH   F .   ? 0.4994 0.3268 0.4099 -0.2323 0.0027  0.0034  251 HOH   B O   
6636 O  O   . HOH   F .   ? 0.3226 0.3485 0.2045 0.0396  0.0488  0.0173  252 HOH   B O   
6637 O  O   . HOH   F .   ? 0.2355 0.1904 0.4034 -0.0002 -0.0586 -0.0340 253 HOH   B O   
6638 O  O   . HOH   F .   ? 0.2145 0.1554 0.2075 -0.0334 -0.0361 0.0272  254 HOH   B O   
6639 O  O   . HOH   F .   ? 0.3384 0.4776 0.3737 -0.0376 -0.1127 0.1331  255 HOH   B O   
6640 O  O   . HOH   F .   ? 0.4297 0.3821 0.3649 -0.0879 0.0780  -0.1237 256 HOH   B O   
6641 O  O   . HOH   F .   ? 0.1331 0.1614 0.2143 -0.0068 0.0068  0.0167  257 HOH   B O   
6642 O  O   . HOH   F .   ? 0.4272 0.2969 0.4496 -0.0234 -0.1141 -0.0853 258 HOH   B O   
6643 O  O   . HOH   F .   ? 0.1641 0.1637 0.2809 -0.0159 -0.0203 0.0055  259 HOH   B O   
6644 O  O   . HOH   F .   ? 0.2307 0.2101 0.2048 0.0103  -0.0073 0.0032  260 HOH   B O   
6645 O  O   . HOH   F .   ? 0.3199 0.2387 0.2896 -0.0413 0.0384  -0.0448 261 HOH   B O   
6646 O  O   . HOH   F .   ? 0.1882 0.2703 0.2893 0.0461  0.0514  0.1034  262 HOH   B O   
6647 O  O   . HOH   F .   ? 0.3867 0.4905 0.4907 0.0046  -0.1218 0.0012  263 HOH   B O   
6648 O  O   . HOH   F .   ? 0.2854 0.4654 0.5165 0.0904  0.0356  -0.0811 264 HOH   B O   
6649 O  O   . HOH   F .   ? 0.2567 0.3759 0.4911 0.1144  -0.0645 -0.1129 265 HOH   B O   
6650 O  O   . HOH   F .   ? 0.2365 0.2187 0.2587 0.0770  -0.0724 -0.0595 266 HOH   B O   
6651 O  O   . HOH   F .   ? 0.2426 0.2043 0.3028 -0.0617 0.0122  -0.0001 267 HOH   B O   
6652 O  O   . HOH   F .   ? 0.2430 0.2208 0.1846 0.0155  0.0050  0.0008  268 HOH   B O   
6653 O  O   . HOH   F .   ? 0.2316 0.3082 0.2194 -0.0443 0.0318  0.0375  269 HOH   B O   
6654 O  O   . HOH   F .   ? 0.4466 0.3204 0.2734 0.0720  -0.0209 -0.0835 270 HOH   B O   
6655 O  O   . HOH   F .   ? 0.2508 0.2545 0.2424 -0.0470 -0.0704 -0.0267 271 HOH   B O   
6656 O  O   . HOH   F .   ? 0.1765 0.1421 0.4590 -0.0081 -0.0253 -0.0113 272 HOH   B O   
6657 O  O   . HOH   F .   ? 0.2004 0.1565 0.2379 -0.0303 -0.0230 0.0114  273 HOH   B O   
6658 O  O   . HOH   F .   ? 0.2702 0.2819 0.2305 -0.0412 -0.0766 0.0196  274 HOH   B O   
6659 O  O   . HOH   F .   ? 0.2900 0.2954 0.4954 -0.0307 0.0378  -0.1358 275 HOH   B O   
6660 O  O   . HOH   F .   ? 0.1850 0.1759 0.1759 -0.0357 -0.0388 0.0089  276 HOH   B O   
6661 O  O   . HOH   F .   ? 0.2511 0.3811 0.3721 0.0418  0.0977  0.0225  277 HOH   B O   
6662 O  O   . HOH   F .   ? 0.2263 0.4505 0.4609 -0.0691 -0.0223 -0.1634 278 HOH   B O   
6663 O  O   . HOH   F .   ? 0.2224 0.3033 0.2281 0.0906  -0.0144 -0.0020 279 HOH   B O   
6664 O  O   . HOH   F .   ? 0.3636 0.3663 0.4400 0.1177  -0.0610 -0.0772 280 HOH   B O   
6665 O  O   . HOH   F .   ? 0.1600 0.1559 0.1881 0.0040  -0.0007 0.0077  281 HOH   B O   
6666 O  O   . HOH   F .   ? 0.2817 0.2162 0.4660 0.0207  0.0556  0.0337  282 HOH   B O   
6667 O  O   . HOH   F .   ? 0.1634 0.1600 0.3148 -0.0128 0.0052  -0.0037 283 HOH   B O   
6668 O  O   . HOH   F .   ? 0.3952 0.6548 0.3091 0.2390  -0.0722 -0.0026 284 HOH   B O   
6669 O  O   . HOH   F .   ? 0.2479 0.2757 0.2615 0.0146  -0.0584 0.0196  285 HOH   B O   
6670 O  O   . HOH   F .   ? 0.4335 0.3596 0.4851 -0.0986 0.0056  0.1435  286 HOH   B O   
6671 O  O   . HOH   F .   ? 0.2758 0.2690 0.5083 -0.0132 -0.0606 0.0786  287 HOH   B O   
6672 O  O   . HOH   F .   ? 0.5244 0.5964 0.2569 0.0106  -0.0590 0.1272  288 HOH   B O   
6673 O  O   . HOH   F .   ? 0.1594 0.1997 0.1785 -0.0091 -0.0211 0.0003  289 HOH   B O   
6674 O  O   . HOH   F .   ? 0.2793 0.4699 0.5104 -0.0995 -0.1151 0.1230  290 HOH   B O   
6675 O  O   . HOH   F .   ? 0.2542 0.3332 0.3167 -0.0773 0.0497  -0.0969 291 HOH   B O   
6676 O  O   . HOH   F .   ? 0.2504 0.6832 0.2731 0.0354  -0.0297 -0.0370 292 HOH   B O   
6677 O  O   . HOH   F .   ? 0.3848 0.2151 0.4011 -0.0975 -0.2146 0.0858  293 HOH   B O   
6678 O  O   . HOH   F .   ? 0.3045 0.2896 0.2858 -0.0092 0.0006  -0.1068 294 HOH   B O   
6679 O  O   . HOH   F .   ? 0.2749 0.6593 0.7211 0.1188  -0.0804 -0.1216 295 HOH   B O   
6680 O  O   . HOH   F .   ? 0.2914 0.2838 0.4148 -0.0801 0.1125  -0.0384 296 HOH   B O   
6681 O  O   . HOH   F .   ? 0.4530 0.4240 0.6370 0.0775  0.0136  0.0773  297 HOH   B O   
6682 O  O   . HOH   F .   ? 0.2050 0.1586 0.2670 -0.0199 -0.0265 -0.0027 298 HOH   B O   
6683 O  O   . HOH   F .   ? 0.2436 0.3456 0.3929 -0.0373 -0.1080 0.0825  299 HOH   B O   
6684 O  O   . HOH   F .   ? 0.1862 0.1598 0.2316 0.0113  0.0056  0.0164  300 HOH   B O   
6685 O  O   . HOH   F .   ? 0.2010 0.2838 0.5861 0.0398  -0.0368 -0.1202 301 HOH   B O   
6686 O  O   . HOH   F .   ? 0.1730 0.3144 0.4451 0.0175  -0.0062 -0.1114 302 HOH   B O   
6687 O  O   . HOH   F .   ? 0.1680 0.1868 0.2926 0.0200  -0.0127 0.0083  303 HOH   B O   
6688 O  O   . HOH   F .   ? 0.3486 0.2717 0.2297 0.0512  -0.0686 -0.0254 304 HOH   B O   
6689 O  O   . HOH   F .   ? 0.4440 0.4018 0.2668 0.1356  -0.0869 0.0570  305 HOH   B O   
6690 O  O   . HOH   F .   ? 0.1610 0.1511 0.2844 0.0040  -0.0022 -0.0055 306 HOH   B O   
6691 O  O   . HOH   F .   ? 0.3447 0.1937 0.3604 0.0771  0.1242  0.0521  307 HOH   B O   
6692 O  O   . HOH   F .   ? 0.5256 0.3043 0.2397 -0.1777 0.0784  -0.0196 308 HOH   B O   
6693 O  O   . HOH   F .   ? 0.4339 0.4420 0.2269 -0.0317 0.0576  0.0478  309 HOH   B O   
6694 O  O   . HOH   F .   ? 0.1576 0.1939 0.2836 -0.0264 -0.0054 0.0109  310 HOH   B O   
6695 O  O   . HOH   F .   ? 0.6112 0.4009 0.3051 0.2786  0.0956  0.0727  311 HOH   B O   
6696 O  O   . HOH   F .   ? 0.2078 0.1579 0.3574 0.0275  -0.0987 -0.0042 312 HOH   B O   
6697 O  O   . HOH   F .   ? 0.2715 0.2971 0.3325 -0.0345 0.0843  -0.0793 313 HOH   B O   
6698 O  O   . HOH   F .   ? 0.2408 0.1521 0.2507 -0.0131 -0.0127 0.0268  314 HOH   B O   
6699 O  O   . HOH   F .   ? 0.6755 0.4692 0.5118 0.1539  0.0835  0.0404  315 HOH   B O   
6700 O  O   . HOH   F .   ? 0.5830 0.4679 0.4881 -0.0983 -0.0158 0.0839  316 HOH   B O   
6701 O  O   . HOH   F .   ? 0.3995 0.2161 0.2828 0.1331  0.1023  0.0347  317 HOH   B O   
6702 O  O   . HOH   F .   ? 0.4451 0.3999 0.2577 0.1308  -0.0638 -0.0208 318 HOH   B O   
6703 O  O   . HOH   F .   ? 0.2256 0.3152 0.4791 -0.0302 -0.0245 0.0125  319 HOH   B O   
6704 O  O   . HOH   F .   ? 0.2237 0.1862 0.1834 -0.0071 0.0145  0.0160  320 HOH   B O   
6705 O  O   . HOH   F .   ? 0.4856 0.2448 0.3374 0.0294  -0.0121 0.1031  321 HOH   B O   
6706 O  O   . HOH   F .   ? 0.1614 0.1644 0.2812 -0.0089 -0.0134 -0.0225 322 HOH   B O   
6707 O  O   . HOH   F .   ? 0.1657 0.2879 0.2507 -0.0161 -0.0211 0.0666  323 HOH   B O   
6708 O  O   . HOH   F .   ? 0.4585 0.4334 0.2639 0.0379  -0.0338 -0.0637 324 HOH   B O   
6709 O  O   . HOH   F .   ? 0.3105 0.3706 0.7710 -0.0438 -0.0721 0.2132  325 HOH   B O   
6710 O  O   . HOH   F .   ? 0.2713 0.2130 0.2447 0.0209  -0.0123 0.0237  326 HOH   B O   
6711 O  O   . HOH   F .   ? 0.6598 0.5956 0.4931 0.3136  0.0723  0.0173  327 HOH   B O   
6712 O  O   . HOH   F .   ? 0.4292 0.3371 0.5464 0.1195  0.2340  0.1910  328 HOH   B O   
6713 O  O   . HOH   F .   ? 0.1869 0.2093 0.2820 0.0360  0.0345  0.0234  329 HOH   B O   
6714 O  O   . HOH   F .   ? 0.4569 0.5512 0.3176 0.0176  -0.0856 0.0333  330 HOH   B O   
6715 O  O   . HOH   F .   ? 0.6624 0.3463 0.3518 -0.0176 0.1185  0.1135  331 HOH   B O   
6716 O  O   . HOH   F .   ? 0.2607 0.2022 0.5367 0.0057  0.0134  0.0316  332 HOH   B O   
6717 O  O   . HOH   F .   ? 0.8017 0.2055 0.2871 -0.0181 -0.0680 0.0149  333 HOH   B O   
6718 O  O   . HOH   F .   ? 0.2097 0.5009 0.5368 -0.0296 -0.0219 -0.0248 334 HOH   B O   
6719 O  O   . HOH   F .   ? 0.5477 0.4449 0.5811 -0.0521 -0.0496 -0.1189 335 HOH   B O   
6720 O  O   . HOH   F .   ? 0.1701 0.2789 0.3076 0.0338  -0.0093 -0.0531 336 HOH   B O   
6721 O  O   . HOH   F .   ? 0.4677 0.3472 0.4212 0.0325  0.0391  -0.1455 337 HOH   B O   
6722 O  O   . HOH   F .   ? 0.5640 0.5433 0.5773 0.0846  -0.0808 0.2192  338 HOH   B O   
6723 O  O   . HOH   F .   ? 0.2274 0.2382 0.5570 -0.0397 0.0181  0.1486  339 HOH   B O   
6724 O  O   . HOH   F .   ? 0.1684 0.1515 0.2566 0.0054  -0.0205 -0.0011 340 HOH   B O   
6725 O  O   . HOH   F .   ? 0.5007 0.3054 0.3042 0.0456  -0.1190 -0.0744 341 HOH   B O   
6726 O  O   . HOH   F .   ? 0.4445 0.6866 0.3406 0.0303  -0.0204 0.1278  342 HOH   B O   
6727 O  O   . HOH   F .   ? 0.4109 0.6568 0.3791 -0.0853 -0.0963 -0.0639 343 HOH   B O   
6728 O  O   . HOH   F .   ? 0.2008 0.1925 0.2609 -0.0085 0.0453  -0.0091 344 HOH   B O   
6729 O  O   . HOH   F .   ? 0.1660 0.5957 0.6098 -0.0121 -0.0352 0.0464  345 HOH   B O   
6730 O  O   . HOH   F .   ? 0.5881 0.6499 0.2664 -0.0173 -0.0616 0.1300  346 HOH   B O   
6731 O  O   . HOH   F .   ? 0.4438 0.4809 0.4978 0.0120  -0.0868 0.0375  347 HOH   B O   
6732 O  O   . HOH   F .   ? 0.2678 0.2130 0.4952 -0.0185 -0.0925 -0.0383 348 HOH   B O   
6733 O  O   . HOH   F .   ? 0.2120 0.3712 0.5126 0.0200  0.0336  0.0311  349 HOH   B O   
6734 O  O   . HOH   F .   ? 0.4984 0.5389 0.4550 -0.1200 0.0476  0.1019  350 HOH   B O   
6735 O  O   . HOH   F .   ? 0.3778 0.2133 0.3336 -0.0551 -0.0221 -0.0475 351 HOH   B O   
6736 O  O   . HOH   F .   ? 0.2327 0.6205 0.3700 0.1468  -0.0414 -0.1333 352 HOH   B O   
6737 O  O   . HOH   F .   ? 0.4507 0.6223 0.5858 0.0487  -0.0004 -0.0875 353 HOH   B O   
6738 O  O   . HOH   F .   ? 0.3095 0.1810 0.4181 0.0411  -0.1156 -0.0401 354 HOH   B O   
6739 O  O   . HOH   F .   ? 0.3833 0.3762 0.4700 -0.1574 0.0023  -0.0122 355 HOH   B O   
6740 O  O   . HOH   F .   ? 0.5093 0.3819 0.4252 0.0815  0.1307  -0.0218 356 HOH   B O   
6741 O  O   . HOH   F .   ? 0.3765 0.2892 0.3841 -0.0960 -0.0140 -0.0598 357 HOH   B O   
6742 O  O   . HOH   F .   ? 0.4357 0.2383 0.5672 -0.0644 0.1587  0.0329  358 HOH   B O   
6743 O  O   . HOH   F .   ? 0.4722 0.4595 0.5079 -0.0318 -0.0325 -0.0102 359 HOH   B O   
6744 O  O   . HOH   F .   ? 0.4413 0.3275 0.4362 0.0523  -0.1613 -0.0149 360 HOH   B O   
6745 O  O   . HOH   F .   ? 0.4611 0.5345 0.5402 0.1705  -0.1320 0.1530  361 HOH   B O   
6746 O  O   . HOH   F .   ? 0.3912 0.7094 0.2963 0.2203  0.0089  0.0596  362 HOH   B O   
6747 O  O   . HOH   F .   ? 0.5082 0.4008 0.6069 0.0497  0.1191  0.1255  363 HOH   B O   
6748 O  O   . HOH   F .   ? 0.2179 0.3564 0.6723 -0.0673 -0.0551 -0.0692 364 HOH   B O   
6749 O  O   . HOH   F .   ? 0.4906 0.3356 0.5753 -0.1345 -0.0548 0.0190  365 HOH   B O   
6750 O  O   . HOH   F .   ? 0.6299 0.4364 0.4200 0.1050  0.0948  0.0631  366 HOH   B O   
6751 O  O   . HOH   F .   ? 0.5195 0.3427 0.4673 0.1115  -0.1686 0.0050  367 HOH   B O   
6752 O  O   . HOH   F .   ? 0.5658 0.6139 0.3426 0.2004  -0.1462 0.0606  368 HOH   B O   
6753 O  O   . HOH   F .   ? 0.4431 0.5493 0.5710 0.2556  0.1096  0.0989  369 HOH   B O   
6754 O  O   . HOH   F .   ? 0.7522 0.8031 0.5183 0.3080  -0.1373 0.1405  370 HOH   B O   
6755 O  O   . HOH   F .   ? 0.6450 0.2061 0.3993 0.0270  0.0625  0.0414  371 HOH   B O   
6756 O  O   . HOH   F .   ? 0.4803 0.5280 0.4156 -0.0314 -0.0682 -0.1114 372 HOH   B O   
6757 O  O   . HOH   F .   ? 0.6313 0.3872 0.2916 -0.1209 -0.1022 -0.0529 373 HOH   B O   
6758 O  O   . HOH   F .   ? 0.3460 0.3372 0.4546 0.0651  -0.1335 -0.0587 374 HOH   B O   
6759 O  O   . HOH   F .   ? 0.3227 0.3950 0.2246 0.0674  0.0174  0.0135  375 HOH   B O   
6760 O  O   . HOH   F .   ? 0.2377 0.4038 0.4618 0.0247  -0.0858 -0.0582 376 HOH   B O   
6761 O  O   . HOH   F .   ? 0.4428 0.4770 0.4943 -0.0923 -0.0573 0.0480  377 HOH   B O   
6762 O  O   . HOH   F .   ? 0.7610 0.3380 0.4966 -0.0732 -0.0303 -0.0088 378 HOH   B O   
6763 O  O   . HOH   F .   ? 0.4624 0.7093 0.6090 0.1548  0.0869  0.2898  379 HOH   B O   
6764 O  O   . HOH   F .   ? 0.5071 0.6533 0.3663 -0.1302 0.0381  -0.1598 380 HOH   B O   
6765 O  O   . HOH   F .   ? 0.3569 0.4001 0.5019 0.1094  -0.0275 0.0326  381 HOH   B O   
6766 O  O   . HOH   F .   ? 0.5439 0.6936 0.5944 0.0131  0.2325  0.1313  382 HOH   B O   
6767 O  O   . HOH   F .   ? 0.3064 0.2518 0.3368 0.0003  0.0147  0.0365  383 HOH   B O   
6768 O  O   . HOH   F .   ? 0.3421 0.7487 0.5859 0.0428  0.1858  0.1334  384 HOH   B O   
6769 O  O   . HOH   F .   ? 0.7453 0.4455 0.4298 0.1081  0.1030  -0.0845 385 HOH   B O   
6770 O  O   . HOH   F .   ? 0.5775 0.4217 0.5127 -0.0647 0.0284  -0.0165 386 HOH   B O   
6771 O  O   . HOH   F .   ? 0.2449 0.4111 0.3577 -0.0686 -0.0754 -0.0337 387 HOH   B O   
6772 O  O   . HOH   F .   ? 0.5624 0.4553 0.3929 -0.0627 -0.0439 -0.0211 388 HOH   B O   
6773 O  O   . HOH   F .   ? 0.7502 0.6539 0.4296 0.2272  0.0250  0.0048  389 HOH   B O   
6774 O  O   . HOH   F .   ? 0.4897 0.3531 0.3122 0.0320  0.0553  -0.0014 390 HOH   B O   
6775 O  O   . HOH   F .   ? 0.3749 0.2285 0.3334 0.0868  -0.0088 0.0266  391 HOH   B O   
6776 O  O   . HOH   F .   ? 0.4381 0.4271 0.3335 -0.0166 0.0215  0.0478  392 HOH   B O   
6777 O  O   . HOH   F .   ? 0.4736 0.2291 0.5191 -0.0710 0.0402  0.0261  393 HOH   B O   
6778 O  O   . HOH   F .   ? 0.2518 0.4599 0.6184 -0.1438 -0.0759 0.0111  394 HOH   B O   
6779 O  O   . HOH   F .   ? 0.4407 0.5851 0.3619 0.1227  -0.0259 -0.0963 395 HOH   B O   
6780 O  O   . HOH   F .   ? 0.4229 0.3838 0.4217 0.0272  0.0936  0.0605  396 HOH   B O   
6781 O  O   . HOH   F .   ? 0.3090 0.3813 0.3469 0.0477  0.0298  -0.0736 397 HOH   B O   
6782 O  O   . HOH   F .   ? 0.2230 0.3058 0.5684 -0.0636 -0.0805 -0.0346 398 HOH   B O   
6783 O  O   . HOH   F .   ? 0.5594 0.5565 0.6448 0.0695  -0.1087 0.2052  399 HOH   B O   
6784 O  O   . HOH   F .   ? 0.5917 0.4274 0.3185 -0.2248 0.0219  0.1089  400 HOH   B O   
6785 O  O   . HOH   F .   ? 0.6017 0.6056 0.3608 0.1942  -0.0606 0.0106  401 HOH   B O   
# 
